data_9G7I
# 
_entry.id   9G7I 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9G7I         pdb_00009g7i 10.2210/pdb9g7i/pdb 
WWPDB D_1292140501 ?            ?                   
# 
_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       2025-02-12 
# 
_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                        9G7I 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-21 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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_database_related.db_name        PDB 
_pdbx_database_related.details        'Structure without Acetyl-CoA' 
_pdbx_database_related.db_id          6YTT 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              twagner@mpi-bremen.de 
_pdbx_contact_author.name_first         Tristan 
_pdbx_contact_author.name_last          Wagner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3382-8969 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lemaire, O.N.' 1 0000-0002-4389-5786 
'Yin, M.D.'     2 0000-0002-5549-9158 
'Murphy, B.J.'  3 0000-0001-6341-9368 
'Wagner, T.'    4 0000-0002-3382-8969 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Science 
_citation.journal_id_ASTM           SCIEAS 
_citation.journal_id_CSD            0038 
_citation.journal_id_ISSN           1095-9203 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            387 
_citation.language                  ? 
_citation.page_first                498 
_citation.page_last                 504 
_citation.title                     'Conformational dynamics of a multienzyme complex in anaerobic carbon fixation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1126/science.adr9672 
_citation.pdbx_database_id_PubMed   39883773 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yin, M.D.'           1 0000-0002-5549-9158 
primary 'Lemaire, O.N.'       2 0000-0002-4389-5786 
primary 'Rosas Jimenez, J.G.' 3 0009-0002-1354-6312 
primary 'Belhamri, M.'        4 0000-0001-6208-1983 
primary 'Shevchenko, A.'      5 0009-0008-6157-4442 
primary 'Hummer, G.'          6 0000-0001-7768-746X 
primary 'Wagner, T.'          7 0000-0002-3382-8969 
primary 'Murphy, B.J.'        8 0000-0001-6341-9368 
# 
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     nat 'CO-methylating acetyl-CoA synthase'                                                 76991.070 2  2.3.1.169 ? ? 
? 
2  polymer     nat 'Carbon monoxide dehydrogenase'                                                      67977.531 2  1.2.7.4   ? ? 
? 
3  non-polymer syn 'IRON/SULFUR CLUSTER'                                                                351.640   5  ?         ? ? 
? 
4  non-polymer syn 'NICKEL (II) ION'                                                                    58.693    4  ?         ? ? 
? 
5  non-polymer syn 1,2-ETHANEDIOL                                                                       62.068    34 ?         ? ? 
? 
6  non-polymer syn '2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL' 354.436   1  ?         ? ? 
? 
7  non-polymer syn GLYCEROL                                                                             92.094    6  ?         ? ? 
? 
8  non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                              106.120   3  ?         ? ? 
? 
9  non-polymer syn 'CALCIUM ION'                                                                        40.078    10 ?         ? ? 
? 
10 non-polymer syn 'CHLORIDE ION'                                                                       35.453    8  ?         ? ? 
? 
11 non-polymer syn 'FE(4)-NI(1)-S(4) CLUSTER'                                                           410.333   2  ?         ? ? 
? 
12 non-polymer syn 'ACETYL COENZYME *A'                                                                 809.571   1  ?         ? ? 
? 
13 non-polymer syn 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                                             122.143   1  ?         ? ? 
? 
14 water       nat water                                                                                18.015    14 ?         ? ? 
? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbon monoxide dehydrogenase/acetyl-CoA synthase complex, alpha subunit' 
# 
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 
;MNLFQTVFTGSKQALAAAEGIVKQAVDEKGRDYKVAFPDTAYSLPVIFAATGKKITNVGELEGALDIVRSLIVEEEMLDK
LLNSGLATAVAAEIIEAAKYVLSDAPYAEPCVGFISDPIIRSLGVPLVTGDIPGVAVILGECPDSETAAKIIKDYQSKGL
LTCLVGKVIDQAIEGKVKMGLDLRVIPLGYDVTSVIHVVTIAIRAALIFGGIKGGQLNDILKYTAERVPAFVNAFGPLSE
LVVSAGAGAIALGFPVLTDQVVPEVPTLLLTQKDYDKMVKTSLEARNIKIKITEIPIPVSFAAAFEGERIRKNDMLAEFG
GNKTKAWELVMCADQGEVEDHKIEVIGPDIDTIDKAPGRMPLGMLIKVSGTNMQKDFEPVLERRLHYFLNYIEGVMHVGQ
RNLTWVRIGKEAFEKGFRLKHFGEVIYAKMLDEFGSVVDKCEVTIITDPGKAEELEGKYAVPRYKERDARLESLVDEKVD
TFYSCNLCQSFAPAHVCIVTPERLGLCGAVSWLDAKATLELNPTGPCQAVPKEGVVDENLGIWEKVNETVSKISQGAVTS
VTLYSILQDPMTSCGCFECITGIMPEANGVVMVNREFGATTPLGMTFGELASMTGGGVQTPGFMGHGRQFIASKKFMKGE
GGLGRIVWMPKELKDFVAEKLNKTAKELYNIDNFADMICDETIATESEEVVKFLEEKGHPALKMDPIM
;
;MNLFQTVFTGSKQALAAAEGIVKQAVDEKGRDYKVAFPDTAYSLPVIFAATGKKITNVGELEGALDIVRSLIVEEEMLDK
LLNSGLATAVAAEIIEAAKYVLSDAPYAEPCVGFISDPIIRSLGVPLVTGDIPGVAVILGECPDSETAAKIIKDYQSKGL
LTCLVGKVIDQAIEGKVKMGLDLRVIPLGYDVTSVIHVVTIAIRAALIFGGIKGGQLNDILKYTAERVPAFVNAFGPLSE
LVVSAGAGAIALGFPVLTDQVVPEVPTLLLTQKDYDKMVKTSLEARNIKIKITEIPIPVSFAAAFEGERIRKNDMLAEFG
GNKTKAWELVMCADQGEVEDHKIEVIGPDIDTIDKAPGRMPLGMLIKVSGTNMQKDFEPVLERRLHYFLNYIEGVMHVGQ
RNLTWVRIGKEAFEKGFRLKHFGEVIYAKMLDEFGSVVDKCEVTIITDPGKAEELEGKYAVPRYKERDARLESLVDEKVD
TFYSCNLCQSFAPAHVCIVTPERLGLCGAVSWLDAKATLELNPTGPCQAVPKEGVVDENLGIWEKVNETVSKISQGAVTS
VTLYSILQDPMTSCGCFECITGIMPEANGVVMVNREFGATTPLGMTFGELASMTGGGVQTPGFMGHGRQFIASKKFMKGE
GGLGRIVWMPKELKDFVAEKLNKTAKELYNIDNFADMICDETIATESEEVVKFLEEKGHPALKMDPIM
;
A,D ? 
2 'polypeptide(L)' no no 
;MEEKAKSIDQATLQLLDKAKQDGVETVWDRKADMKVQCGFGSAGVCCRNCSMGPCRVSPVPGKGVERGICGATADVIVSR
NFARMVAAGTAAHSDHGRSIALSLYHTSKDGDIKVKDENKLKEVAKSFNVETEGRDIYDIAHDVAKEGLSNYGKQLGEVT
LPPSLPEKRKELWRKLGVYPRAVDREIAAVMHSTHIGCNADAEAMIKMSMRCSLTDGWMGSFMGTEFSDIMFGTPHSIDT
EANLGVLEKNSVNVVLHGHEPLLSEMVVEAASDPELVELAKSVGADGINLCGMCCTGNEVSMRHGIKIAGNFMQQELAVV
TGAVDGLIVDVQCIMPALAKLSKSYHTKFITTSPKAHITDSIYMEFDEENPLDSAKKILKEAILNFKNRDQSKVMIPELK
CKAILGYSVEEIINKLDKVVNTQIGPMQTVKPLADVLVSGVLRGAAAVVGCNNPKVVQDSAHIETIKGLIKNDVIVVVTG
CAAQAAAKYGLLQKEAAEKYAGPGLATVCKLVDIPPVLHMGSCVDISRILDLVGRVANLLGVDMSDLPVAGVAPEWMSEK
AVAIGTYVVTSGIDTWLGVAPPVTGGPEVVDILTNKMEDWVGAKFFIETDPHKAVEQIVNRMNEKRKKLGI
;
;MEEKAKSIDQATLQLLDKAKQDGVETVWDRKADMKVQCGFGSAGVCCRNCSMGPCRVSPVPGKGVERGICGATADVIVSR
NFARMVAAGTAAHSDHGRSIALSLYHTSKDGDIKVKDENKLKEVAKSFNVETEGRDIYDIAHDVAKEGLSNYGKQLGEVT
LPPSLPEKRKELWRKLGVYPRAVDREIAAVMHSTHIGCNADAEAMIKMSMRCSLTDGWMGSFMGTEFSDIMFGTPHSIDT
EANLGVLEKNSVNVVLHGHEPLLSEMVVEAASDPELVELAKSVGADGINLCGMCCTGNEVSMRHGIKIAGNFMQQELAVV
TGAVDGLIVDVQCIMPALAKLSKSYHTKFITTSPKAHITDSIYMEFDEENPLDSAKKILKEAILNFKNRDQSKVMIPELK
CKAILGYSVEEIINKLDKVVNTQIGPMQTVKPLADVLVSGVLRGAAAVVGCNNPKVVQDSAHIETIKGLIKNDVIVVVTG
CAAQAAAKYGLLQKEAAEKYAGPGLATVCKLVDIPPVLHMGSCVDISRILDLVGRVANLLGVDMSDLPVAGVAPEWMSEK
AVAIGTYVVTSGIDTWLGVAPPVTGGPEVVDILTNKMEDWVGAKFFIETDPHKAVEQIVNRMNEKRKKLGI
;
B,C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3  'IRON/SULFUR CLUSTER'                                                                SF4 
4  'NICKEL (II) ION'                                                                    NI  
5  1,2-ETHANEDIOL                                                                       EDO 
6  '2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL' PE4 
7  GLYCEROL                                                                             GOL 
8  'DI(HYDROXYETHYL)ETHER'                                                              PEG 
9  'CALCIUM ION'                                                                        CA  
10 'CHLORIDE ION'                                                                       CL  
11 'FE(4)-NI(1)-S(4) CLUSTER'                                                           XCC 
12 'ACETYL COENZYME *A'                                                                 ACO 
13 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                                             TRS 
14 water                                                                                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASN n 
1 3   LEU n 
1 4   PHE n 
1 5   GLN n 
1 6   THR n 
1 7   VAL n 
1 8   PHE n 
1 9   THR n 
1 10  GLY n 
1 11  SER n 
1 12  LYS n 
1 13  GLN n 
1 14  ALA n 
1 15  LEU n 
1 16  ALA n 
1 17  ALA n 
1 18  ALA n 
1 19  GLU n 
1 20  GLY n 
1 21  ILE n 
1 22  VAL n 
1 23  LYS n 
1 24  GLN n 
1 25  ALA n 
1 26  VAL n 
1 27  ASP n 
1 28  GLU n 
1 29  LYS n 
1 30  GLY n 
1 31  ARG n 
1 32  ASP n 
1 33  TYR n 
1 34  LYS n 
1 35  VAL n 
1 36  ALA n 
1 37  PHE n 
1 38  PRO n 
1 39  ASP n 
1 40  THR n 
1 41  ALA n 
1 42  TYR n 
1 43  SER n 
1 44  LEU n 
1 45  PRO n 
1 46  VAL n 
1 47  ILE n 
1 48  PHE n 
1 49  ALA n 
1 50  ALA n 
1 51  THR n 
1 52  GLY n 
1 53  LYS n 
1 54  LYS n 
1 55  ILE n 
1 56  THR n 
1 57  ASN n 
1 58  VAL n 
1 59  GLY n 
1 60  GLU n 
1 61  LEU n 
1 62  GLU n 
1 63  GLY n 
1 64  ALA n 
1 65  LEU n 
1 66  ASP n 
1 67  ILE n 
1 68  VAL n 
1 69  ARG n 
1 70  SER n 
1 71  LEU n 
1 72  ILE n 
1 73  VAL n 
1 74  GLU n 
1 75  GLU n 
1 76  GLU n 
1 77  MET n 
1 78  LEU n 
1 79  ASP n 
1 80  LYS n 
1 81  LEU n 
1 82  LEU n 
1 83  ASN n 
1 84  SER n 
1 85  GLY n 
1 86  LEU n 
1 87  ALA n 
1 88  THR n 
1 89  ALA n 
1 90  VAL n 
1 91  ALA n 
1 92  ALA n 
1 93  GLU n 
1 94  ILE n 
1 95  ILE n 
1 96  GLU n 
1 97  ALA n 
1 98  ALA n 
1 99  LYS n 
1 100 TYR n 
1 101 VAL n 
1 102 LEU n 
1 103 SER n 
1 104 ASP n 
1 105 ALA n 
1 106 PRO n 
1 107 TYR n 
1 108 ALA n 
1 109 GLU n 
1 110 PRO n 
1 111 CYS n 
1 112 VAL n 
1 113 GLY n 
1 114 PHE n 
1 115 ILE n 
1 116 SER n 
1 117 ASP n 
1 118 PRO n 
1 119 ILE n 
1 120 ILE n 
1 121 ARG n 
1 122 SER n 
1 123 LEU n 
1 124 GLY n 
1 125 VAL n 
1 126 PRO n 
1 127 LEU n 
1 128 VAL n 
1 129 THR n 
1 130 GLY n 
1 131 ASP n 
1 132 ILE n 
1 133 PRO n 
1 134 GLY n 
1 135 VAL n 
1 136 ALA n 
1 137 VAL n 
1 138 ILE n 
1 139 LEU n 
1 140 GLY n 
1 141 GLU n 
1 142 CYS n 
1 143 PRO n 
1 144 ASP n 
1 145 SER n 
1 146 GLU n 
1 147 THR n 
1 148 ALA n 
1 149 ALA n 
1 150 LYS n 
1 151 ILE n 
1 152 ILE n 
1 153 LYS n 
1 154 ASP n 
1 155 TYR n 
1 156 GLN n 
1 157 SER n 
1 158 LYS n 
1 159 GLY n 
1 160 LEU n 
1 161 LEU n 
1 162 THR n 
1 163 CYS n 
1 164 LEU n 
1 165 VAL n 
1 166 GLY n 
1 167 LYS n 
1 168 VAL n 
1 169 ILE n 
1 170 ASP n 
1 171 GLN n 
1 172 ALA n 
1 173 ILE n 
1 174 GLU n 
1 175 GLY n 
1 176 LYS n 
1 177 VAL n 
1 178 LYS n 
1 179 MET n 
1 180 GLY n 
1 181 LEU n 
1 182 ASP n 
1 183 LEU n 
1 184 ARG n 
1 185 VAL n 
1 186 ILE n 
1 187 PRO n 
1 188 LEU n 
1 189 GLY n 
1 190 TYR n 
1 191 ASP n 
1 192 VAL n 
1 193 THR n 
1 194 SER n 
1 195 VAL n 
1 196 ILE n 
1 197 HIS n 
1 198 VAL n 
1 199 VAL n 
1 200 THR n 
1 201 ILE n 
1 202 ALA n 
1 203 ILE n 
1 204 ARG n 
1 205 ALA n 
1 206 ALA n 
1 207 LEU n 
1 208 ILE n 
1 209 PHE n 
1 210 GLY n 
1 211 GLY n 
1 212 ILE n 
1 213 LYS n 
1 214 GLY n 
1 215 GLY n 
1 216 GLN n 
1 217 LEU n 
1 218 ASN n 
1 219 ASP n 
1 220 ILE n 
1 221 LEU n 
1 222 LYS n 
1 223 TYR n 
1 224 THR n 
1 225 ALA n 
1 226 GLU n 
1 227 ARG n 
1 228 VAL n 
1 229 PRO n 
1 230 ALA n 
1 231 PHE n 
1 232 VAL n 
1 233 ASN n 
1 234 ALA n 
1 235 PHE n 
1 236 GLY n 
1 237 PRO n 
1 238 LEU n 
1 239 SER n 
1 240 GLU n 
1 241 LEU n 
1 242 VAL n 
1 243 VAL n 
1 244 SER n 
1 245 ALA n 
1 246 GLY n 
1 247 ALA n 
1 248 GLY n 
1 249 ALA n 
1 250 ILE n 
1 251 ALA n 
1 252 LEU n 
1 253 GLY n 
1 254 PHE n 
1 255 PRO n 
1 256 VAL n 
1 257 LEU n 
1 258 THR n 
1 259 ASP n 
1 260 GLN n 
1 261 VAL n 
1 262 VAL n 
1 263 PRO n 
1 264 GLU n 
1 265 VAL n 
1 266 PRO n 
1 267 THR n 
1 268 LEU n 
1 269 LEU n 
1 270 LEU n 
1 271 THR n 
1 272 GLN n 
1 273 LYS n 
1 274 ASP n 
1 275 TYR n 
1 276 ASP n 
1 277 LYS n 
1 278 MET n 
1 279 VAL n 
1 280 LYS n 
1 281 THR n 
1 282 SER n 
1 283 LEU n 
1 284 GLU n 
1 285 ALA n 
1 286 ARG n 
1 287 ASN n 
1 288 ILE n 
1 289 LYS n 
1 290 ILE n 
1 291 LYS n 
1 292 ILE n 
1 293 THR n 
1 294 GLU n 
1 295 ILE n 
1 296 PRO n 
1 297 ILE n 
1 298 PRO n 
1 299 VAL n 
1 300 SER n 
1 301 PHE n 
1 302 ALA n 
1 303 ALA n 
1 304 ALA n 
1 305 PHE n 
1 306 GLU n 
1 307 GLY n 
1 308 GLU n 
1 309 ARG n 
1 310 ILE n 
1 311 ARG n 
1 312 LYS n 
1 313 ASN n 
1 314 ASP n 
1 315 MET n 
1 316 LEU n 
1 317 ALA n 
1 318 GLU n 
1 319 PHE n 
1 320 GLY n 
1 321 GLY n 
1 322 ASN n 
1 323 LYS n 
1 324 THR n 
1 325 LYS n 
1 326 ALA n 
1 327 TRP n 
1 328 GLU n 
1 329 LEU n 
1 330 VAL n 
1 331 MET n 
1 332 CYS n 
1 333 ALA n 
1 334 ASP n 
1 335 GLN n 
1 336 GLY n 
1 337 GLU n 
1 338 VAL n 
1 339 GLU n 
1 340 ASP n 
1 341 HIS n 
1 342 LYS n 
1 343 ILE n 
1 344 GLU n 
1 345 VAL n 
1 346 ILE n 
1 347 GLY n 
1 348 PRO n 
1 349 ASP n 
1 350 ILE n 
1 351 ASP n 
1 352 THR n 
1 353 ILE n 
1 354 ASP n 
1 355 LYS n 
1 356 ALA n 
1 357 PRO n 
1 358 GLY n 
1 359 ARG n 
1 360 MET n 
1 361 PRO n 
1 362 LEU n 
1 363 GLY n 
1 364 MET n 
1 365 LEU n 
1 366 ILE n 
1 367 LYS n 
1 368 VAL n 
1 369 SER n 
1 370 GLY n 
1 371 THR n 
1 372 ASN n 
1 373 MET n 
1 374 GLN n 
1 375 LYS n 
1 376 ASP n 
1 377 PHE n 
1 378 GLU n 
1 379 PRO n 
1 380 VAL n 
1 381 LEU n 
1 382 GLU n 
1 383 ARG n 
1 384 ARG n 
1 385 LEU n 
1 386 HIS n 
1 387 TYR n 
1 388 PHE n 
1 389 LEU n 
1 390 ASN n 
1 391 TYR n 
1 392 ILE n 
1 393 GLU n 
1 394 GLY n 
1 395 VAL n 
1 396 MET n 
1 397 HIS n 
1 398 VAL n 
1 399 GLY n 
1 400 GLN n 
1 401 ARG n 
1 402 ASN n 
1 403 LEU n 
1 404 THR n 
1 405 TRP n 
1 406 VAL n 
1 407 ARG n 
1 408 ILE n 
1 409 GLY n 
1 410 LYS n 
1 411 GLU n 
1 412 ALA n 
1 413 PHE n 
1 414 GLU n 
1 415 LYS n 
1 416 GLY n 
1 417 PHE n 
1 418 ARG n 
1 419 LEU n 
1 420 LYS n 
1 421 HIS n 
1 422 PHE n 
1 423 GLY n 
1 424 GLU n 
1 425 VAL n 
1 426 ILE n 
1 427 TYR n 
1 428 ALA n 
1 429 LYS n 
1 430 MET n 
1 431 LEU n 
1 432 ASP n 
1 433 GLU n 
1 434 PHE n 
1 435 GLY n 
1 436 SER n 
1 437 VAL n 
1 438 VAL n 
1 439 ASP n 
1 440 LYS n 
1 441 CYS n 
1 442 GLU n 
1 443 VAL n 
1 444 THR n 
1 445 ILE n 
1 446 ILE n 
1 447 THR n 
1 448 ASP n 
1 449 PRO n 
1 450 GLY n 
1 451 LYS n 
1 452 ALA n 
1 453 GLU n 
1 454 GLU n 
1 455 LEU n 
1 456 GLU n 
1 457 GLY n 
1 458 LYS n 
1 459 TYR n 
1 460 ALA n 
1 461 VAL n 
1 462 PRO n 
1 463 ARG n 
1 464 TYR n 
1 465 LYS n 
1 466 GLU n 
1 467 ARG n 
1 468 ASP n 
1 469 ALA n 
1 470 ARG n 
1 471 LEU n 
1 472 GLU n 
1 473 SER n 
1 474 LEU n 
1 475 VAL n 
1 476 ASP n 
1 477 GLU n 
1 478 LYS n 
1 479 VAL n 
1 480 ASP n 
1 481 THR n 
1 482 PHE n 
1 483 TYR n 
1 484 SER n 
1 485 CYS n 
1 486 ASN n 
1 487 LEU n 
1 488 CYS n 
1 489 GLN n 
1 490 SER n 
1 491 PHE n 
1 492 ALA n 
1 493 PRO n 
1 494 ALA n 
1 495 HIS n 
1 496 VAL n 
1 497 CYS n 
1 498 ILE n 
1 499 VAL n 
1 500 THR n 
1 501 PRO n 
1 502 GLU n 
1 503 ARG n 
1 504 LEU n 
1 505 GLY n 
1 506 LEU n 
1 507 CYS n 
1 508 GLY n 
1 509 ALA n 
1 510 VAL n 
1 511 SER n 
1 512 TRP n 
1 513 LEU n 
1 514 ASP n 
1 515 ALA n 
1 516 LYS n 
1 517 ALA n 
1 518 THR n 
1 519 LEU n 
1 520 GLU n 
1 521 LEU n 
1 522 ASN n 
1 523 PRO n 
1 524 THR n 
1 525 GLY n 
1 526 PRO n 
1 527 CYS n 
1 528 GLN n 
1 529 ALA n 
1 530 VAL n 
1 531 PRO n 
1 532 LYS n 
1 533 GLU n 
1 534 GLY n 
1 535 VAL n 
1 536 VAL n 
1 537 ASP n 
1 538 GLU n 
1 539 ASN n 
1 540 LEU n 
1 541 GLY n 
1 542 ILE n 
1 543 TRP n 
1 544 GLU n 
1 545 LYS n 
1 546 VAL n 
1 547 ASN n 
1 548 GLU n 
1 549 THR n 
1 550 VAL n 
1 551 SER n 
1 552 LYS n 
1 553 ILE n 
1 554 SER n 
1 555 GLN n 
1 556 GLY n 
1 557 ALA n 
1 558 VAL n 
1 559 THR n 
1 560 SER n 
1 561 VAL n 
1 562 THR n 
1 563 LEU n 
1 564 TYR n 
1 565 SER n 
1 566 ILE n 
1 567 LEU n 
1 568 GLN n 
1 569 ASP n 
1 570 PRO n 
1 571 MET n 
1 572 THR n 
1 573 SER n 
1 574 CYS n 
1 575 GLY n 
1 576 CYS n 
1 577 PHE n 
1 578 GLU n 
1 579 CYS n 
1 580 ILE n 
1 581 THR n 
1 582 GLY n 
1 583 ILE n 
1 584 MET n 
1 585 PRO n 
1 586 GLU n 
1 587 ALA n 
1 588 ASN n 
1 589 GLY n 
1 590 VAL n 
1 591 VAL n 
1 592 MET n 
1 593 VAL n 
1 594 ASN n 
1 595 ARG n 
1 596 GLU n 
1 597 PHE n 
1 598 GLY n 
1 599 ALA n 
1 600 THR n 
1 601 THR n 
1 602 PRO n 
1 603 LEU n 
1 604 GLY n 
1 605 MET n 
1 606 THR n 
1 607 PHE n 
1 608 GLY n 
1 609 GLU n 
1 610 LEU n 
1 611 ALA n 
1 612 SER n 
1 613 MET n 
1 614 THR n 
1 615 GLY n 
1 616 GLY n 
1 617 GLY n 
1 618 VAL n 
1 619 GLN n 
1 620 THR n 
1 621 PRO n 
1 622 GLY n 
1 623 PHE n 
1 624 MET n 
1 625 GLY n 
1 626 HIS n 
1 627 GLY n 
1 628 ARG n 
1 629 GLN n 
1 630 PHE n 
1 631 ILE n 
1 632 ALA n 
1 633 SER n 
1 634 LYS n 
1 635 LYS n 
1 636 PHE n 
1 637 MET n 
1 638 LYS n 
1 639 GLY n 
1 640 GLU n 
1 641 GLY n 
1 642 GLY n 
1 643 LEU n 
1 644 GLY n 
1 645 ARG n 
1 646 ILE n 
1 647 VAL n 
1 648 TRP n 
1 649 MET n 
1 650 PRO n 
1 651 LYS n 
1 652 GLU n 
1 653 LEU n 
1 654 LYS n 
1 655 ASP n 
1 656 PHE n 
1 657 VAL n 
1 658 ALA n 
1 659 GLU n 
1 660 LYS n 
1 661 LEU n 
1 662 ASN n 
1 663 LYS n 
1 664 THR n 
1 665 ALA n 
1 666 LYS n 
1 667 GLU n 
1 668 LEU n 
1 669 TYR n 
1 670 ASN n 
1 671 ILE n 
1 672 ASP n 
1 673 ASN n 
1 674 PHE n 
1 675 ALA n 
1 676 ASP n 
1 677 MET n 
1 678 ILE n 
1 679 CYS n 
1 680 ASP n 
1 681 GLU n 
1 682 THR n 
1 683 ILE n 
1 684 ALA n 
1 685 THR n 
1 686 GLU n 
1 687 SER n 
1 688 GLU n 
1 689 GLU n 
1 690 VAL n 
1 691 VAL n 
1 692 LYS n 
1 693 PHE n 
1 694 LEU n 
1 695 GLU n 
1 696 GLU n 
1 697 LYS n 
1 698 GLY n 
1 699 HIS n 
1 700 PRO n 
1 701 ALA n 
1 702 LEU n 
1 703 LYS n 
1 704 MET n 
1 705 ASP n 
1 706 PRO n 
1 707 ILE n 
1 708 MET n 
2 1   MET n 
2 2   GLU n 
2 3   GLU n 
2 4   LYS n 
2 5   ALA n 
2 6   LYS n 
2 7   SER n 
2 8   ILE n 
2 9   ASP n 
2 10  GLN n 
2 11  ALA n 
2 12  THR n 
2 13  LEU n 
2 14  GLN n 
2 15  LEU n 
2 16  LEU n 
2 17  ASP n 
2 18  LYS n 
2 19  ALA n 
2 20  LYS n 
2 21  GLN n 
2 22  ASP n 
2 23  GLY n 
2 24  VAL n 
2 25  GLU n 
2 26  THR n 
2 27  VAL n 
2 28  TRP n 
2 29  ASP n 
2 30  ARG n 
2 31  LYS n 
2 32  ALA n 
2 33  ASP n 
2 34  MET n 
2 35  LYS n 
2 36  VAL n 
2 37  GLN n 
2 38  CYS n 
2 39  GLY n 
2 40  PHE n 
2 41  GLY n 
2 42  SER n 
2 43  ALA n 
2 44  GLY n 
2 45  VAL n 
2 46  CYS n 
2 47  CYS n 
2 48  ARG n 
2 49  ASN n 
2 50  CYS n 
2 51  SER n 
2 52  MET n 
2 53  GLY n 
2 54  PRO n 
2 55  CYS n 
2 56  ARG n 
2 57  VAL n 
2 58  SER n 
2 59  PRO n 
2 60  VAL n 
2 61  PRO n 
2 62  GLY n 
2 63  LYS n 
2 64  GLY n 
2 65  VAL n 
2 66  GLU n 
2 67  ARG n 
2 68  GLY n 
2 69  ILE n 
2 70  CYS n 
2 71  GLY n 
2 72  ALA n 
2 73  THR n 
2 74  ALA n 
2 75  ASP n 
2 76  VAL n 
2 77  ILE n 
2 78  VAL n 
2 79  SER n 
2 80  ARG n 
2 81  ASN n 
2 82  PHE n 
2 83  ALA n 
2 84  ARG n 
2 85  MET n 
2 86  VAL n 
2 87  ALA n 
2 88  ALA n 
2 89  GLY n 
2 90  THR n 
2 91  ALA n 
2 92  ALA n 
2 93  HIS n 
2 94  SER n 
2 95  ASP n 
2 96  HIS n 
2 97  GLY n 
2 98  ARG n 
2 99  SER n 
2 100 ILE n 
2 101 ALA n 
2 102 LEU n 
2 103 SER n 
2 104 LEU n 
2 105 TYR n 
2 106 HIS n 
2 107 THR n 
2 108 SER n 
2 109 LYS n 
2 110 ASP n 
2 111 GLY n 
2 112 ASP n 
2 113 ILE n 
2 114 LYS n 
2 115 VAL n 
2 116 LYS n 
2 117 ASP n 
2 118 GLU n 
2 119 ASN n 
2 120 LYS n 
2 121 LEU n 
2 122 LYS n 
2 123 GLU n 
2 124 VAL n 
2 125 ALA n 
2 126 LYS n 
2 127 SER n 
2 128 PHE n 
2 129 ASN n 
2 130 VAL n 
2 131 GLU n 
2 132 THR n 
2 133 GLU n 
2 134 GLY n 
2 135 ARG n 
2 136 ASP n 
2 137 ILE n 
2 138 TYR n 
2 139 ASP n 
2 140 ILE n 
2 141 ALA n 
2 142 HIS n 
2 143 ASP n 
2 144 VAL n 
2 145 ALA n 
2 146 LYS n 
2 147 GLU n 
2 148 GLY n 
2 149 LEU n 
2 150 SER n 
2 151 ASN n 
2 152 TYR n 
2 153 GLY n 
2 154 LYS n 
2 155 GLN n 
2 156 LEU n 
2 157 GLY n 
2 158 GLU n 
2 159 VAL n 
2 160 THR n 
2 161 LEU n 
2 162 PRO n 
2 163 PRO n 
2 164 SER n 
2 165 LEU n 
2 166 PRO n 
2 167 GLU n 
2 168 LYS n 
2 169 ARG n 
2 170 LYS n 
2 171 GLU n 
2 172 LEU n 
2 173 TRP n 
2 174 ARG n 
2 175 LYS n 
2 176 LEU n 
2 177 GLY n 
2 178 VAL n 
2 179 TYR n 
2 180 PRO n 
2 181 ARG n 
2 182 ALA n 
2 183 VAL n 
2 184 ASP n 
2 185 ARG n 
2 186 GLU n 
2 187 ILE n 
2 188 ALA n 
2 189 ALA n 
2 190 VAL n 
2 191 MET n 
2 192 HIS n 
2 193 SER n 
2 194 THR n 
2 195 HIS n 
2 196 ILE n 
2 197 GLY n 
2 198 CYS n 
2 199 ASN n 
2 200 ALA n 
2 201 ASP n 
2 202 ALA n 
2 203 GLU n 
2 204 ALA n 
2 205 MET n 
2 206 ILE n 
2 207 LYS n 
2 208 MET n 
2 209 SER n 
2 210 MET n 
2 211 ARG n 
2 212 CYS n 
2 213 SER n 
2 214 LEU n 
2 215 THR n 
2 216 ASP n 
2 217 GLY n 
2 218 TRP n 
2 219 MET n 
2 220 GLY n 
2 221 SER n 
2 222 PHE n 
2 223 MET n 
2 224 GLY n 
2 225 THR n 
2 226 GLU n 
2 227 PHE n 
2 228 SER n 
2 229 ASP n 
2 230 ILE n 
2 231 MET n 
2 232 PHE n 
2 233 GLY n 
2 234 THR n 
2 235 PRO n 
2 236 HIS n 
2 237 SER n 
2 238 ILE n 
2 239 ASP n 
2 240 THR n 
2 241 GLU n 
2 242 ALA n 
2 243 ASN n 
2 244 LEU n 
2 245 GLY n 
2 246 VAL n 
2 247 LEU n 
2 248 GLU n 
2 249 LYS n 
2 250 ASN n 
2 251 SER n 
2 252 VAL n 
2 253 ASN n 
2 254 VAL n 
2 255 VAL n 
2 256 LEU n 
2 257 HIS n 
2 258 GLY n 
2 259 HIS n 
2 260 GLU n 
2 261 PRO n 
2 262 LEU n 
2 263 LEU n 
2 264 SER n 
2 265 GLU n 
2 266 MET n 
2 267 VAL n 
2 268 VAL n 
2 269 GLU n 
2 270 ALA n 
2 271 ALA n 
2 272 SER n 
2 273 ASP n 
2 274 PRO n 
2 275 GLU n 
2 276 LEU n 
2 277 VAL n 
2 278 GLU n 
2 279 LEU n 
2 280 ALA n 
2 281 LYS n 
2 282 SER n 
2 283 VAL n 
2 284 GLY n 
2 285 ALA n 
2 286 ASP n 
2 287 GLY n 
2 288 ILE n 
2 289 ASN n 
2 290 LEU n 
2 291 CYS n 
2 292 GLY n 
2 293 MET n 
2 294 CYS n 
2 295 CYS n 
2 296 THR n 
2 297 GLY n 
2 298 ASN n 
2 299 GLU n 
2 300 VAL n 
2 301 SER n 
2 302 MET n 
2 303 ARG n 
2 304 HIS n 
2 305 GLY n 
2 306 ILE n 
2 307 LYS n 
2 308 ILE n 
2 309 ALA n 
2 310 GLY n 
2 311 ASN n 
2 312 PHE n 
2 313 MET n 
2 314 GLN n 
2 315 GLN n 
2 316 GLU n 
2 317 LEU n 
2 318 ALA n 
2 319 VAL n 
2 320 VAL n 
2 321 THR n 
2 322 GLY n 
2 323 ALA n 
2 324 VAL n 
2 325 ASP n 
2 326 GLY n 
2 327 LEU n 
2 328 ILE n 
2 329 VAL n 
2 330 ASP n 
2 331 VAL n 
2 332 GLN n 
2 333 CYS n 
2 334 ILE n 
2 335 MET n 
2 336 PRO n 
2 337 ALA n 
2 338 LEU n 
2 339 ALA n 
2 340 LYS n 
2 341 LEU n 
2 342 SER n 
2 343 LYS n 
2 344 SER n 
2 345 TYR n 
2 346 HIS n 
2 347 THR n 
2 348 LYS n 
2 349 PHE n 
2 350 ILE n 
2 351 THR n 
2 352 THR n 
2 353 SER n 
2 354 PRO n 
2 355 LYS n 
2 356 ALA n 
2 357 HIS n 
2 358 ILE n 
2 359 THR n 
2 360 ASP n 
2 361 SER n 
2 362 ILE n 
2 363 TYR n 
2 364 MET n 
2 365 GLU n 
2 366 PHE n 
2 367 ASP n 
2 368 GLU n 
2 369 GLU n 
2 370 ASN n 
2 371 PRO n 
2 372 LEU n 
2 373 ASP n 
2 374 SER n 
2 375 ALA n 
2 376 LYS n 
2 377 LYS n 
2 378 ILE n 
2 379 LEU n 
2 380 LYS n 
2 381 GLU n 
2 382 ALA n 
2 383 ILE n 
2 384 LEU n 
2 385 ASN n 
2 386 PHE n 
2 387 LYS n 
2 388 ASN n 
2 389 ARG n 
2 390 ASP n 
2 391 GLN n 
2 392 SER n 
2 393 LYS n 
2 394 VAL n 
2 395 MET n 
2 396 ILE n 
2 397 PRO n 
2 398 GLU n 
2 399 LEU n 
2 400 LYS n 
2 401 CYS n 
2 402 LYS n 
2 403 ALA n 
2 404 ILE n 
2 405 LEU n 
2 406 GLY n 
2 407 TYR n 
2 408 SER n 
2 409 VAL n 
2 410 GLU n 
2 411 GLU n 
2 412 ILE n 
2 413 ILE n 
2 414 ASN n 
2 415 LYS n 
2 416 LEU n 
2 417 ASP n 
2 418 LYS n 
2 419 VAL n 
2 420 VAL n 
2 421 ASN n 
2 422 THR n 
2 423 GLN n 
2 424 ILE n 
2 425 GLY n 
2 426 PRO n 
2 427 MET n 
2 428 GLN n 
2 429 THR n 
2 430 VAL n 
2 431 LYS n 
2 432 PRO n 
2 433 LEU n 
2 434 ALA n 
2 435 ASP n 
2 436 VAL n 
2 437 LEU n 
2 438 VAL n 
2 439 SER n 
2 440 GLY n 
2 441 VAL n 
2 442 LEU n 
2 443 ARG n 
2 444 GLY n 
2 445 ALA n 
2 446 ALA n 
2 447 ALA n 
2 448 VAL n 
2 449 VAL n 
2 450 GLY n 
2 451 CYS n 
2 452 ASN n 
2 453 ASN n 
2 454 PRO n 
2 455 LYS n 
2 456 VAL n 
2 457 VAL n 
2 458 GLN n 
2 459 ASP n 
2 460 SER n 
2 461 ALA n 
2 462 HIS n 
2 463 ILE n 
2 464 GLU n 
2 465 THR n 
2 466 ILE n 
2 467 LYS n 
2 468 GLY n 
2 469 LEU n 
2 470 ILE n 
2 471 LYS n 
2 472 ASN n 
2 473 ASP n 
2 474 VAL n 
2 475 ILE n 
2 476 VAL n 
2 477 VAL n 
2 478 VAL n 
2 479 THR n 
2 480 GLY n 
2 481 CYS n 
2 482 ALA n 
2 483 ALA n 
2 484 GLN n 
2 485 ALA n 
2 486 ALA n 
2 487 ALA n 
2 488 LYS n 
2 489 TYR n 
2 490 GLY n 
2 491 LEU n 
2 492 LEU n 
2 493 GLN n 
2 494 LYS n 
2 495 GLU n 
2 496 ALA n 
2 497 ALA n 
2 498 GLU n 
2 499 LYS n 
2 500 TYR n 
2 501 ALA n 
2 502 GLY n 
2 503 PRO n 
2 504 GLY n 
2 505 LEU n 
2 506 ALA n 
2 507 THR n 
2 508 VAL n 
2 509 CYS n 
2 510 LYS n 
2 511 LEU n 
2 512 VAL n 
2 513 ASP n 
2 514 ILE n 
2 515 PRO n 
2 516 PRO n 
2 517 VAL n 
2 518 LEU n 
2 519 HIS n 
2 520 MET n 
2 521 GLY n 
2 522 SER n 
2 523 CYS n 
2 524 VAL n 
2 525 ASP n 
2 526 ILE n 
2 527 SER n 
2 528 ARG n 
2 529 ILE n 
2 530 LEU n 
2 531 ASP n 
2 532 LEU n 
2 533 VAL n 
2 534 GLY n 
2 535 ARG n 
2 536 VAL n 
2 537 ALA n 
2 538 ASN n 
2 539 LEU n 
2 540 LEU n 
2 541 GLY n 
2 542 VAL n 
2 543 ASP n 
2 544 MET n 
2 545 SER n 
2 546 ASP n 
2 547 LEU n 
2 548 PRO n 
2 549 VAL n 
2 550 ALA n 
2 551 GLY n 
2 552 VAL n 
2 553 ALA n 
2 554 PRO n 
2 555 GLU n 
2 556 TRP n 
2 557 MET n 
2 558 SER n 
2 559 GLU n 
2 560 LYS n 
2 561 ALA n 
2 562 VAL n 
2 563 ALA n 
2 564 ILE n 
2 565 GLY n 
2 566 THR n 
2 567 TYR n 
2 568 VAL n 
2 569 VAL n 
2 570 THR n 
2 571 SER n 
2 572 GLY n 
2 573 ILE n 
2 574 ASP n 
2 575 THR n 
2 576 TRP n 
2 577 LEU n 
2 578 GLY n 
2 579 VAL n 
2 580 ALA n 
2 581 PRO n 
2 582 PRO n 
2 583 VAL n 
2 584 THR n 
2 585 GLY n 
2 586 GLY n 
2 587 PRO n 
2 588 GLU n 
2 589 VAL n 
2 590 VAL n 
2 591 ASP n 
2 592 ILE n 
2 593 LEU n 
2 594 THR n 
2 595 ASN n 
2 596 LYS n 
2 597 MET n 
2 598 GLU n 
2 599 ASP n 
2 600 TRP n 
2 601 VAL n 
2 602 GLY n 
2 603 ALA n 
2 604 LYS n 
2 605 PHE n 
2 606 PHE n 
2 607 ILE n 
2 608 GLU n 
2 609 THR n 
2 610 ASP n 
2 611 PRO n 
2 612 HIS n 
2 613 LYS n 
2 614 ALA n 
2 615 VAL n 
2 616 GLU n 
2 617 GLN n 
2 618 ILE n 
2 619 VAL n 
2 620 ASN n 
2 621 ARG n 
2 622 MET n 
2 623 ASN n 
2 624 GLU n 
2 625 LYS n 
2 626 ARG n 
2 627 LYS n 
2 628 LYS n 
2 629 LEU n 
2 630 GLY n 
2 631 ILE n 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_entity_src_nat.genus 
_entity_src_nat.species 
_entity_src_nat.strain 
_entity_src_nat.tissue 
_entity_src_nat.tissue_fraction 
_entity_src_nat.pdbx_secretion 
_entity_src_nat.pdbx_fragment 
_entity_src_nat.pdbx_variant 
_entity_src_nat.pdbx_cell_line 
_entity_src_nat.pdbx_atcc 
_entity_src_nat.pdbx_cellular_location 
_entity_src_nat.pdbx_organ 
_entity_src_nat.pdbx_organelle 
_entity_src_nat.pdbx_cell 
_entity_src_nat.pdbx_plasmid_name 
_entity_src_nat.pdbx_plasmid_details 
_entity_src_nat.details 
1 1 sample 1 708 ? 'Clostridium autoethanogenum DSM 10061' 1341692 ? ? 'DSM 10061' / ? ? ? 'wild type' / / ? / ? ? ? / ? 
2 1 sample 1 631 ? 'Clostridium autoethanogenum DSM 10061' 1341692 ? ? 'DSM 10061' / ? ? ? 'wild type' / / ? / ? ? ? / ? 
# 
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 
ACO non-polymer         . 'ACETYL COENZYME *A'                                                                 ? 
'C23 H38 N7 O17 P3 S' 809.571 
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 
CA  non-polymer         . 'CALCIUM ION'                                                                        ? 'Ca 2' 40.078  
CL  non-polymer         . 'CHLORIDE ION'                                                                       ? 'Cl -1' 35.453  
CYS 'L-peptide linking' y CYSTEINE                                                                             ? 'C3 H7 N O2 S' 
121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                                                       'ETHYLENE GLYCOL' 
'C2 H6 O2'            62.068  
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  
GOL non-polymer         . GLYCEROL                                                                             
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'            92.094  
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 
NI  non-polymer         . 'NICKEL (II) ION'                                                                    ? 'Ni 2' 58.693  
PE4 non-polymer         . '2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL' 
'POLYETHYLENE GLYCOL PEG4000'   'C16 H34 O8'          354.436 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                                              ? 'C4 H10 O3' 
106.120 
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 
SF4 non-polymer         . 'IRON/SULFUR CLUSTER'                                                                ? 'Fe4 S4' 351.640 
THR 'L-peptide linking' y THREONINE                                                                            ? 'C4 H9 N O3' 
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                           ? 'C11 H12 N2 O2' 
204.225 
TRS non-polymer         . 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                                             'TRIS BUFFER' 
'C4 H12 N O3 1'       122.143 
TYR 'L-peptide linking' y TYROSINE                                                                             ? 'C9 H11 N O3' 
181.189 
VAL 'L-peptide linking' y VALINE                                                                               ? 'C5 H11 N O2' 
117.146 
XCC non-polymer         . 'FE(4)-NI(1)-S(4) CLUSTER'                                                           'C CLUSTER' 
'Fe4 Ni S4'           410.333 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   1   MET MET A . n 
A 1 2   ASN 2   2   2   ASN ASN A . n 
A 1 3   LEU 3   3   3   LEU LEU A . n 
A 1 4   PHE 4   4   4   PHE PHE A . n 
A 1 5   GLN 5   5   5   GLN GLN A . n 
A 1 6   THR 6   6   6   THR THR A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   THR 9   9   9   THR THR A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  GLN 13  13  13  GLN GLN A . n 
A 1 14  ALA 14  14  14  ALA ALA A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  ALA 16  16  16  ALA ALA A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  GLU 19  19  19  GLU GLU A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  ILE 21  21  21  ILE ILE A . n 
A 1 22  VAL 22  22  22  VAL VAL A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLN 24  24  24  GLN GLN A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  VAL 26  26  26  VAL VAL A . n 
A 1 27  ASP 27  27  27  ASP ASP A . n 
A 1 28  GLU 28  28  28  GLU GLU A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  TYR 33  33  33  TYR TYR A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  PRO 38  38  38  PRO PRO A . n 
A 1 39  ASP 39  39  39  ASP ASP A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  VAL 46  46  46  VAL VAL A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  ALA 49  49  49  ALA ALA A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  THR 51  51  51  THR THR A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  LYS 53  53  53  LYS LYS A . n 
A 1 54  LYS 54  54  54  LYS LYS A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  THR 56  56  56  THR THR A . n 
A 1 57  ASN 57  57  57  ASN ASN A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  GLU 60  60  60  GLU GLU A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  GLU 76  76  76  GLU GLU A . n 
A 1 77  MET 77  77  77  MET MET A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  ASP 79  79  79  ASP ASP A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ASN 83  83  83  ASN ASN A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  ILE 95  95  95  ILE ILE A . n 
A 1 96  GLU 96  96  96  GLU GLU A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 LEU 102 102 102 LEU LEU A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 TYR 107 107 107 TYR TYR A . n 
A 1 108 ALA 108 108 108 ALA ALA A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 PRO 110 110 110 PRO PRO A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 ILE 115 115 115 ILE ILE A . n 
A 1 116 SER 116 116 116 SER SER A . n 
A 1 117 ASP 117 117 117 ASP ASP A . n 
A 1 118 PRO 118 118 118 PRO PRO A . n 
A 1 119 ILE 119 119 119 ILE ILE A . n 
A 1 120 ILE 120 120 120 ILE ILE A . n 
A 1 121 ARG 121 121 121 ARG ARG A . n 
A 1 122 SER 122 122 122 SER SER A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 PRO 126 126 126 PRO PRO A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 THR 129 129 129 THR THR A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASP 131 131 131 ASP ASP A . n 
A 1 132 ILE 132 132 132 ILE ILE A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 GLY 134 134 134 GLY GLY A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 VAL 137 137 137 VAL VAL A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 CYS 142 142 142 CYS CYS A . n 
A 1 143 PRO 143 143 143 PRO PRO A . n 
A 1 144 ASP 144 144 144 ASP ASP A . n 
A 1 145 SER 145 145 145 SER SER A . n 
A 1 146 GLU 146 146 146 GLU GLU A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 ALA 148 148 148 ALA ALA A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 LYS 150 150 150 LYS LYS A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 GLN 156 156 156 GLN GLN A . n 
A 1 157 SER 157 157 157 SER SER A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 LEU 161 161 161 LEU LEU A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 CYS 163 163 163 CYS CYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 GLY 166 166 166 GLY GLY A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 ASP 170 170 170 ASP ASP A . n 
A 1 171 GLN 171 171 171 GLN GLN A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 GLU 174 174 174 GLU GLU A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 LYS 178 178 178 LYS LYS A . n 
A 1 179 MET 179 179 179 MET MET A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 ASP 182 182 182 ASP ASP A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 VAL 185 185 185 VAL VAL A . n 
A 1 186 ILE 186 186 186 ILE ILE A . n 
A 1 187 PRO 187 187 187 PRO PRO A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 GLY 189 189 189 GLY GLY A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 VAL 192 192 192 VAL VAL A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 SER 194 194 194 SER SER A . n 
A 1 195 VAL 195 195 195 VAL VAL A . n 
A 1 196 ILE 196 196 196 ILE ILE A . n 
A 1 197 HIS 197 197 197 HIS HIS A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 THR 200 200 200 THR THR A . n 
A 1 201 ILE 201 201 201 ILE ILE A . n 
A 1 202 ALA 202 202 202 ALA ALA A . n 
A 1 203 ILE 203 203 203 ILE ILE A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 ALA 205 205 205 ALA ALA A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 ILE 208 208 208 ILE ILE A . n 
A 1 209 PHE 209 209 209 PHE PHE A . n 
A 1 210 GLY 210 210 210 GLY GLY A . n 
A 1 211 GLY 211 211 211 GLY GLY A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 LYS 213 213 213 LYS LYS A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 ASP 219 219 219 ASP ASP A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 LEU 221 221 221 LEU LEU A . n 
A 1 222 LYS 222 222 222 LYS LYS A . n 
A 1 223 TYR 223 223 223 TYR TYR A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 ARG 227 227 227 ARG ARG A . n 
A 1 228 VAL 228 228 228 VAL VAL A . n 
A 1 229 PRO 229 229 229 PRO PRO A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 PHE 231 231 231 PHE PHE A . n 
A 1 232 VAL 232 232 232 VAL VAL A . n 
A 1 233 ASN 233 233 233 ASN ASN A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 PHE 235 235 235 PHE PHE A . n 
A 1 236 GLY 236 236 236 GLY GLY A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 LEU 238 238 238 LEU LEU A . n 
A 1 239 SER 239 239 239 SER SER A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 VAL 242 242 242 VAL VAL A . n 
A 1 243 VAL 243 243 243 VAL VAL A . n 
A 1 244 SER 244 244 244 SER SER A . n 
A 1 245 ALA 245 245 245 ALA ALA A . n 
A 1 246 GLY 246 246 246 GLY GLY A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 GLY 248 248 248 GLY GLY A . n 
A 1 249 ALA 249 249 249 ALA ALA A . n 
A 1 250 ILE 250 250 250 ILE ILE A . n 
A 1 251 ALA 251 251 251 ALA ALA A . n 
A 1 252 LEU 252 252 252 LEU LEU A . n 
A 1 253 GLY 253 253 253 GLY GLY A . n 
A 1 254 PHE 254 254 254 PHE PHE A . n 
A 1 255 PRO 255 255 255 PRO PRO A . n 
A 1 256 VAL 256 256 256 VAL VAL A . n 
A 1 257 LEU 257 257 257 LEU LEU A . n 
A 1 258 THR 258 258 258 THR THR A . n 
A 1 259 ASP 259 259 259 ASP ASP A . n 
A 1 260 GLN 260 260 260 GLN GLN A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 VAL 262 262 262 VAL VAL A . n 
A 1 263 PRO 263 263 263 PRO PRO A . n 
A 1 264 GLU 264 264 264 GLU GLU A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 PRO 266 266 266 PRO PRO A . n 
A 1 267 THR 267 267 267 THR THR A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 THR 271 271 271 THR THR A . n 
A 1 272 GLN 272 272 272 GLN GLN A . n 
A 1 273 LYS 273 273 273 LYS LYS A . n 
A 1 274 ASP 274 274 274 ASP ASP A . n 
A 1 275 TYR 275 275 275 TYR TYR A . n 
A 1 276 ASP 276 276 276 ASP ASP A . n 
A 1 277 LYS 277 277 277 LYS LYS A . n 
A 1 278 MET 278 278 278 MET MET A . n 
A 1 279 VAL 279 279 279 VAL VAL A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 THR 281 281 281 THR THR A . n 
A 1 282 SER 282 282 282 SER SER A . n 
A 1 283 LEU 283 283 283 LEU LEU A . n 
A 1 284 GLU 284 284 284 GLU GLU A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 ARG 286 286 286 ARG ARG A . n 
A 1 287 ASN 287 287 287 ASN ASN A . n 
A 1 288 ILE 288 288 288 ILE ILE A . n 
A 1 289 LYS 289 289 289 LYS LYS A . n 
A 1 290 ILE 290 290 290 ILE ILE A . n 
A 1 291 LYS 291 291 291 LYS LYS A . n 
A 1 292 ILE 292 292 292 ILE ILE A . n 
A 1 293 THR 293 293 293 THR THR A . n 
A 1 294 GLU 294 294 ?   ?   ?   A . n 
A 1 295 ILE 295 295 ?   ?   ?   A . n 
A 1 296 PRO 296 296 296 PRO PRO A . n 
A 1 297 ILE 297 297 297 ILE ILE A . n 
A 1 298 PRO 298 298 298 PRO PRO A . n 
A 1 299 VAL 299 299 299 VAL VAL A . n 
A 1 300 SER 300 300 300 SER SER A . n 
A 1 301 PHE 301 301 301 PHE PHE A . n 
A 1 302 ALA 302 302 302 ALA ALA A . n 
A 1 303 ALA 303 303 303 ALA ALA A . n 
A 1 304 ALA 304 304 304 ALA ALA A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 GLU 306 306 306 GLU GLU A . n 
A 1 307 GLY 307 307 307 GLY GLY A . n 
A 1 308 GLU 308 308 308 GLU GLU A . n 
A 1 309 ARG 309 309 ?   ?   ?   A . n 
A 1 310 ILE 310 310 ?   ?   ?   A . n 
A 1 311 ARG 311 311 ?   ?   ?   A . n 
A 1 312 LYS 312 312 ?   ?   ?   A . n 
A 1 313 ASN 313 313 313 ASN ASN A . n 
A 1 314 ASP 314 314 314 ASP ASP A . n 
A 1 315 MET 315 315 315 MET MET A . n 
A 1 316 LEU 316 316 316 LEU LEU A . n 
A 1 317 ALA 317 317 317 ALA ALA A . n 
A 1 318 GLU 318 318 318 GLU GLU A . n 
A 1 319 PHE 319 319 319 PHE PHE A . n 
A 1 320 GLY 320 320 320 GLY GLY A . n 
A 1 321 GLY 321 321 321 GLY GLY A . n 
A 1 322 ASN 322 322 322 ASN ASN A . n 
A 1 323 LYS 323 323 323 LYS LYS A . n 
A 1 324 THR 324 324 324 THR THR A . n 
A 1 325 LYS 325 325 325 LYS LYS A . n 
A 1 326 ALA 326 326 326 ALA ALA A . n 
A 1 327 TRP 327 327 327 TRP TRP A . n 
A 1 328 GLU 328 328 328 GLU GLU A . n 
A 1 329 LEU 329 329 329 LEU LEU A . n 
A 1 330 VAL 330 330 330 VAL VAL A . n 
A 1 331 MET 331 331 331 MET MET A . n 
A 1 332 CYS 332 332 332 CYS CYS A . n 
A 1 333 ALA 333 333 333 ALA ALA A . n 
A 1 334 ASP 334 334 334 ASP ASP A . n 
A 1 335 GLN 335 335 335 GLN GLN A . n 
A 1 336 GLY 336 336 336 GLY GLY A . n 
A 1 337 GLU 337 337 337 GLU GLU A . n 
A 1 338 VAL 338 338 338 VAL VAL A . n 
A 1 339 GLU 339 339 339 GLU GLU A . n 
A 1 340 ASP 340 340 340 ASP ASP A . n 
A 1 341 HIS 341 341 341 HIS HIS A . n 
A 1 342 LYS 342 342 342 LYS LYS A . n 
A 1 343 ILE 343 343 343 ILE ILE A . n 
A 1 344 GLU 344 344 344 GLU GLU A . n 
A 1 345 VAL 345 345 345 VAL VAL A . n 
A 1 346 ILE 346 346 346 ILE ILE A . n 
A 1 347 GLY 347 347 347 GLY GLY A . n 
A 1 348 PRO 348 348 348 PRO PRO A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 ILE 350 350 350 ILE ILE A . n 
A 1 351 ASP 351 351 351 ASP ASP A . n 
A 1 352 THR 352 352 352 THR THR A . n 
A 1 353 ILE 353 353 353 ILE ILE A . n 
A 1 354 ASP 354 354 354 ASP ASP A . n 
A 1 355 LYS 355 355 355 LYS LYS A . n 
A 1 356 ALA 356 356 356 ALA ALA A . n 
A 1 357 PRO 357 357 ?   ?   ?   A . n 
A 1 358 GLY 358 358 ?   ?   ?   A . n 
A 1 359 ARG 359 359 ?   ?   ?   A . n 
A 1 360 MET 360 360 360 MET MET A . n 
A 1 361 PRO 361 361 361 PRO PRO A . n 
A 1 362 LEU 362 362 362 LEU LEU A . n 
A 1 363 GLY 363 363 363 GLY GLY A . n 
A 1 364 MET 364 364 364 MET MET A . n 
A 1 365 LEU 365 365 365 LEU LEU A . n 
A 1 366 ILE 366 366 366 ILE ILE A . n 
A 1 367 LYS 367 367 367 LYS LYS A . n 
A 1 368 VAL 368 368 368 VAL VAL A . n 
A 1 369 SER 369 369 369 SER SER A . n 
A 1 370 GLY 370 370 370 GLY GLY A . n 
A 1 371 THR 371 371 371 THR THR A . n 
A 1 372 ASN 372 372 372 ASN ASN A . n 
A 1 373 MET 373 373 373 MET MET A . n 
A 1 374 GLN 374 374 374 GLN GLN A . n 
A 1 375 LYS 375 375 375 LYS LYS A . n 
A 1 376 ASP 376 376 376 ASP ASP A . n 
A 1 377 PHE 377 377 377 PHE PHE A . n 
A 1 378 GLU 378 378 378 GLU GLU A . n 
A 1 379 PRO 379 379 379 PRO PRO A . n 
A 1 380 VAL 380 380 380 VAL VAL A . n 
A 1 381 LEU 381 381 381 LEU LEU A . n 
A 1 382 GLU 382 382 382 GLU GLU A . n 
A 1 383 ARG 383 383 383 ARG ARG A . n 
A 1 384 ARG 384 384 384 ARG ARG A . n 
A 1 385 LEU 385 385 385 LEU LEU A . n 
A 1 386 HIS 386 386 386 HIS HIS A . n 
A 1 387 TYR 387 387 387 TYR TYR A . n 
A 1 388 PHE 388 388 388 PHE PHE A . n 
A 1 389 LEU 389 389 389 LEU LEU A . n 
A 1 390 ASN 390 390 390 ASN ASN A . n 
A 1 391 TYR 391 391 391 TYR TYR A . n 
A 1 392 ILE 392 392 392 ILE ILE A . n 
A 1 393 GLU 393 393 393 GLU GLU A . n 
A 1 394 GLY 394 394 394 GLY GLY A . n 
A 1 395 VAL 395 395 395 VAL VAL A . n 
A 1 396 MET 396 396 396 MET MET A . n 
A 1 397 HIS 397 397 397 HIS HIS A . n 
A 1 398 VAL 398 398 398 VAL VAL A . n 
A 1 399 GLY 399 399 399 GLY GLY A . n 
A 1 400 GLN 400 400 400 GLN GLN A . n 
A 1 401 ARG 401 401 401 ARG ARG A . n 
A 1 402 ASN 402 402 402 ASN ASN A . n 
A 1 403 LEU 403 403 403 LEU LEU A . n 
A 1 404 THR 404 404 404 THR THR A . n 
A 1 405 TRP 405 405 405 TRP TRP A . n 
A 1 406 VAL 406 406 406 VAL VAL A . n 
A 1 407 ARG 407 407 407 ARG ARG A . n 
A 1 408 ILE 408 408 408 ILE ILE A . n 
A 1 409 GLY 409 409 409 GLY GLY A . n 
A 1 410 LYS 410 410 410 LYS LYS A . n 
A 1 411 GLU 411 411 411 GLU GLU A . n 
A 1 412 ALA 412 412 412 ALA ALA A . n 
A 1 413 PHE 413 413 413 PHE PHE A . n 
A 1 414 GLU 414 414 414 GLU GLU A . n 
A 1 415 LYS 415 415 415 LYS LYS A . n 
A 1 416 GLY 416 416 416 GLY GLY A . n 
A 1 417 PHE 417 417 417 PHE PHE A . n 
A 1 418 ARG 418 418 418 ARG ARG A . n 
A 1 419 LEU 419 419 419 LEU LEU A . n 
A 1 420 LYS 420 420 420 LYS LYS A . n 
A 1 421 HIS 421 421 421 HIS HIS A . n 
A 1 422 PHE 422 422 422 PHE PHE A . n 
A 1 423 GLY 423 423 423 GLY GLY A . n 
A 1 424 GLU 424 424 424 GLU GLU A . n 
A 1 425 VAL 425 425 425 VAL VAL A . n 
A 1 426 ILE 426 426 426 ILE ILE A . n 
A 1 427 TYR 427 427 427 TYR TYR A . n 
A 1 428 ALA 428 428 428 ALA ALA A . n 
A 1 429 LYS 429 429 429 LYS LYS A . n 
A 1 430 MET 430 430 430 MET MET A . n 
A 1 431 LEU 431 431 431 LEU LEU A . n 
A 1 432 ASP 432 432 432 ASP ASP A . n 
A 1 433 GLU 433 433 433 GLU GLU A . n 
A 1 434 PHE 434 434 434 PHE PHE A . n 
A 1 435 GLY 435 435 435 GLY GLY A . n 
A 1 436 SER 436 436 436 SER SER A . n 
A 1 437 VAL 437 437 437 VAL VAL A . n 
A 1 438 VAL 438 438 438 VAL VAL A . n 
A 1 439 ASP 439 439 ?   ?   ?   A . n 
A 1 440 LYS 440 440 ?   ?   ?   A . n 
A 1 441 CYS 441 441 ?   ?   ?   A . n 
A 1 442 GLU 442 442 ?   ?   ?   A . n 
A 1 443 VAL 443 443 ?   ?   ?   A . n 
A 1 444 THR 444 444 444 THR THR A . n 
A 1 445 ILE 445 445 445 ILE ILE A . n 
A 1 446 ILE 446 446 446 ILE ILE A . n 
A 1 447 THR 447 447 447 THR THR A . n 
A 1 448 ASP 448 448 448 ASP ASP A . n 
A 1 449 PRO 449 449 449 PRO PRO A . n 
A 1 450 GLY 450 450 450 GLY GLY A . n 
A 1 451 LYS 451 451 451 LYS LYS A . n 
A 1 452 ALA 452 452 452 ALA ALA A . n 
A 1 453 GLU 453 453 453 GLU GLU A . n 
A 1 454 GLU 454 454 454 GLU GLU A . n 
A 1 455 LEU 455 455 455 LEU LEU A . n 
A 1 456 GLU 456 456 456 GLU GLU A . n 
A 1 457 GLY 457 457 457 GLY GLY A . n 
A 1 458 LYS 458 458 458 LYS LYS A . n 
A 1 459 TYR 459 459 459 TYR TYR A . n 
A 1 460 ALA 460 460 460 ALA ALA A . n 
A 1 461 VAL 461 461 461 VAL VAL A . n 
A 1 462 PRO 462 462 462 PRO PRO A . n 
A 1 463 ARG 463 463 463 ARG ARG A . n 
A 1 464 TYR 464 464 464 TYR TYR A . n 
A 1 465 LYS 465 465 465 LYS LYS A . n 
A 1 466 GLU 466 466 466 GLU GLU A . n 
A 1 467 ARG 467 467 467 ARG ARG A . n 
A 1 468 ASP 468 468 468 ASP ASP A . n 
A 1 469 ALA 469 469 469 ALA ALA A . n 
A 1 470 ARG 470 470 470 ARG ARG A . n 
A 1 471 LEU 471 471 471 LEU LEU A . n 
A 1 472 GLU 472 472 472 GLU GLU A . n 
A 1 473 SER 473 473 473 SER SER A . n 
A 1 474 LEU 474 474 474 LEU LEU A . n 
A 1 475 VAL 475 475 475 VAL VAL A . n 
A 1 476 ASP 476 476 476 ASP ASP A . n 
A 1 477 GLU 477 477 477 GLU GLU A . n 
A 1 478 LYS 478 478 478 LYS LYS A . n 
A 1 479 VAL 479 479 479 VAL VAL A . n 
A 1 480 ASP 480 480 480 ASP ASP A . n 
A 1 481 THR 481 481 481 THR THR A . n 
A 1 482 PHE 482 482 482 PHE PHE A . n 
A 1 483 TYR 483 483 483 TYR TYR A . n 
A 1 484 SER 484 484 484 SER SER A . n 
A 1 485 CYS 485 485 485 CYS CYS A . n 
A 1 486 ASN 486 486 486 ASN ASN A . n 
A 1 487 LEU 487 487 487 LEU LEU A . n 
A 1 488 CYS 488 488 488 CYS CYS A . n 
A 1 489 GLN 489 489 489 GLN GLN A . n 
A 1 490 SER 490 490 490 SER SER A . n 
A 1 491 PHE 491 491 491 PHE PHE A . n 
A 1 492 ALA 492 492 492 ALA ALA A . n 
A 1 493 PRO 493 493 493 PRO PRO A . n 
A 1 494 ALA 494 494 494 ALA ALA A . n 
A 1 495 HIS 495 495 495 HIS HIS A . n 
A 1 496 VAL 496 496 496 VAL VAL A . n 
A 1 497 CYS 497 497 497 CYS CYS A . n 
A 1 498 ILE 498 498 498 ILE ILE A . n 
A 1 499 VAL 499 499 499 VAL VAL A . n 
A 1 500 THR 500 500 500 THR THR A . n 
A 1 501 PRO 501 501 501 PRO PRO A . n 
A 1 502 GLU 502 502 502 GLU GLU A . n 
A 1 503 ARG 503 503 503 ARG ARG A . n 
A 1 504 LEU 504 504 504 LEU LEU A . n 
A 1 505 GLY 505 505 505 GLY GLY A . n 
A 1 506 LEU 506 506 506 LEU LEU A . n 
A 1 507 CYS 507 507 507 CYS CYS A . n 
A 1 508 GLY 508 508 508 GLY GLY A . n 
A 1 509 ALA 509 509 509 ALA ALA A . n 
A 1 510 VAL 510 510 510 VAL VAL A . n 
A 1 511 SER 511 511 511 SER SER A . n 
A 1 512 TRP 512 512 512 TRP TRP A . n 
A 1 513 LEU 513 513 513 LEU LEU A . n 
A 1 514 ASP 514 514 514 ASP ASP A . n 
A 1 515 ALA 515 515 515 ALA ALA A . n 
A 1 516 LYS 516 516 516 LYS LYS A . n 
A 1 517 ALA 517 517 517 ALA ALA A . n 
A 1 518 THR 518 518 518 THR THR A . n 
A 1 519 LEU 519 519 519 LEU LEU A . n 
A 1 520 GLU 520 520 520 GLU GLU A . n 
A 1 521 LEU 521 521 521 LEU LEU A . n 
A 1 522 ASN 522 522 522 ASN ASN A . n 
A 1 523 PRO 523 523 523 PRO PRO A . n 
A 1 524 THR 524 524 524 THR THR A . n 
A 1 525 GLY 525 525 525 GLY GLY A . n 
A 1 526 PRO 526 526 526 PRO PRO A . n 
A 1 527 CYS 527 527 527 CYS CYS A . n 
A 1 528 GLN 528 528 528 GLN GLN A . n 
A 1 529 ALA 529 529 529 ALA ALA A . n 
A 1 530 VAL 530 530 530 VAL VAL A . n 
A 1 531 PRO 531 531 531 PRO PRO A . n 
A 1 532 LYS 532 532 532 LYS LYS A . n 
A 1 533 GLU 533 533 533 GLU GLU A . n 
A 1 534 GLY 534 534 534 GLY GLY A . n 
A 1 535 VAL 535 535 535 VAL VAL A . n 
A 1 536 VAL 536 536 536 VAL VAL A . n 
A 1 537 ASP 537 537 537 ASP ASP A . n 
A 1 538 GLU 538 538 538 GLU GLU A . n 
A 1 539 ASN 539 539 539 ASN ASN A . n 
A 1 540 LEU 540 540 540 LEU LEU A . n 
A 1 541 GLY 541 541 541 GLY GLY A . n 
A 1 542 ILE 542 542 542 ILE ILE A . n 
A 1 543 TRP 543 543 543 TRP TRP A . n 
A 1 544 GLU 544 544 544 GLU GLU A . n 
A 1 545 LYS 545 545 545 LYS LYS A . n 
A 1 546 VAL 546 546 546 VAL VAL A . n 
A 1 547 ASN 547 547 547 ASN ASN A . n 
A 1 548 GLU 548 548 548 GLU GLU A . n 
A 1 549 THR 549 549 549 THR THR A . n 
A 1 550 VAL 550 550 550 VAL VAL A . n 
A 1 551 SER 551 551 551 SER SER A . n 
A 1 552 LYS 552 552 552 LYS LYS A . n 
A 1 553 ILE 553 553 553 ILE ILE A . n 
A 1 554 SER 554 554 554 SER SER A . n 
A 1 555 GLN 555 555 555 GLN GLN A . n 
A 1 556 GLY 556 556 556 GLY GLY A . n 
A 1 557 ALA 557 557 557 ALA ALA A . n 
A 1 558 VAL 558 558 558 VAL VAL A . n 
A 1 559 THR 559 559 559 THR THR A . n 
A 1 560 SER 560 560 560 SER SER A . n 
A 1 561 VAL 561 561 561 VAL VAL A . n 
A 1 562 THR 562 562 562 THR THR A . n 
A 1 563 LEU 563 563 563 LEU LEU A . n 
A 1 564 TYR 564 564 564 TYR TYR A . n 
A 1 565 SER 565 565 565 SER SER A . n 
A 1 566 ILE 566 566 566 ILE ILE A . n 
A 1 567 LEU 567 567 567 LEU LEU A . n 
A 1 568 GLN 568 568 568 GLN GLN A . n 
A 1 569 ASP 569 569 569 ASP ASP A . n 
A 1 570 PRO 570 570 570 PRO PRO A . n 
A 1 571 MET 571 571 571 MET MET A . n 
A 1 572 THR 572 572 572 THR THR A . n 
A 1 573 SER 573 573 573 SER SER A . n 
A 1 574 CYS 574 574 574 CYS CYS A . n 
A 1 575 GLY 575 575 575 GLY GLY A . n 
A 1 576 CYS 576 576 576 CYS CYS A . n 
A 1 577 PHE 577 577 577 PHE PHE A . n 
A 1 578 GLU 578 578 578 GLU GLU A . n 
A 1 579 CYS 579 579 579 CYS CYS A . n 
A 1 580 ILE 580 580 580 ILE ILE A . n 
A 1 581 THR 581 581 581 THR THR A . n 
A 1 582 GLY 582 582 582 GLY GLY A . n 
A 1 583 ILE 583 583 583 ILE ILE A . n 
A 1 584 MET 584 584 584 MET MET A . n 
A 1 585 PRO 585 585 585 PRO PRO A . n 
A 1 586 GLU 586 586 586 GLU GLU A . n 
A 1 587 ALA 587 587 587 ALA ALA A . n 
A 1 588 ASN 588 588 588 ASN ASN A . n 
A 1 589 GLY 589 589 589 GLY GLY A . n 
A 1 590 VAL 590 590 590 VAL VAL A . n 
A 1 591 VAL 591 591 591 VAL VAL A . n 
A 1 592 MET 592 592 592 MET MET A . n 
A 1 593 VAL 593 593 593 VAL VAL A . n 
A 1 594 ASN 594 594 594 ASN ASN A . n 
A 1 595 ARG 595 595 595 ARG ARG A . n 
A 1 596 GLU 596 596 596 GLU GLU A . n 
A 1 597 PHE 597 597 597 PHE PHE A . n 
A 1 598 GLY 598 598 598 GLY GLY A . n 
A 1 599 ALA 599 599 599 ALA ALA A . n 
A 1 600 THR 600 600 600 THR THR A . n 
A 1 601 THR 601 601 601 THR THR A . n 
A 1 602 PRO 602 602 602 PRO PRO A . n 
A 1 603 LEU 603 603 603 LEU LEU A . n 
A 1 604 GLY 604 604 604 GLY GLY A . n 
A 1 605 MET 605 605 605 MET MET A . n 
A 1 606 THR 606 606 606 THR THR A . n 
A 1 607 PHE 607 607 607 PHE PHE A . n 
A 1 608 GLY 608 608 608 GLY GLY A . n 
A 1 609 GLU 609 609 609 GLU GLU A . n 
A 1 610 LEU 610 610 610 LEU LEU A . n 
A 1 611 ALA 611 611 611 ALA ALA A . n 
A 1 612 SER 612 612 612 SER SER A . n 
A 1 613 MET 613 613 613 MET MET A . n 
A 1 614 THR 614 614 614 THR THR A . n 
A 1 615 GLY 615 615 615 GLY GLY A . n 
A 1 616 GLY 616 616 616 GLY GLY A . n 
A 1 617 GLY 617 617 617 GLY GLY A . n 
A 1 618 VAL 618 618 618 VAL VAL A . n 
A 1 619 GLN 619 619 619 GLN GLN A . n 
A 1 620 THR 620 620 620 THR THR A . n 
A 1 621 PRO 621 621 621 PRO PRO A . n 
A 1 622 GLY 622 622 622 GLY GLY A . n 
A 1 623 PHE 623 623 623 PHE PHE A . n 
A 1 624 MET 624 624 624 MET MET A . n 
A 1 625 GLY 625 625 625 GLY GLY A . n 
A 1 626 HIS 626 626 626 HIS HIS A . n 
A 1 627 GLY 627 627 627 GLY GLY A . n 
A 1 628 ARG 628 628 628 ARG ARG A . n 
A 1 629 GLN 629 629 629 GLN GLN A . n 
A 1 630 PHE 630 630 630 PHE PHE A . n 
A 1 631 ILE 631 631 631 ILE ILE A . n 
A 1 632 ALA 632 632 632 ALA ALA A . n 
A 1 633 SER 633 633 633 SER SER A . n 
A 1 634 LYS 634 634 634 LYS LYS A . n 
A 1 635 LYS 635 635 635 LYS LYS A . n 
A 1 636 PHE 636 636 636 PHE PHE A . n 
A 1 637 MET 637 637 637 MET MET A . n 
A 1 638 LYS 638 638 638 LYS LYS A . n 
A 1 639 GLY 639 639 639 GLY GLY A . n 
A 1 640 GLU 640 640 640 GLU GLU A . n 
A 1 641 GLY 641 641 641 GLY GLY A . n 
A 1 642 GLY 642 642 642 GLY GLY A . n 
A 1 643 LEU 643 643 643 LEU LEU A . n 
A 1 644 GLY 644 644 644 GLY GLY A . n 
A 1 645 ARG 645 645 645 ARG ARG A . n 
A 1 646 ILE 646 646 646 ILE ILE A . n 
A 1 647 VAL 647 647 647 VAL VAL A . n 
A 1 648 TRP 648 648 648 TRP TRP A . n 
A 1 649 MET 649 649 649 MET MET A . n 
A 1 650 PRO 650 650 650 PRO PRO A . n 
A 1 651 LYS 651 651 651 LYS LYS A . n 
A 1 652 GLU 652 652 652 GLU GLU A . n 
A 1 653 LEU 653 653 653 LEU LEU A . n 
A 1 654 LYS 654 654 654 LYS LYS A . n 
A 1 655 ASP 655 655 655 ASP ASP A . n 
A 1 656 PHE 656 656 656 PHE PHE A . n 
A 1 657 VAL 657 657 657 VAL VAL A . n 
A 1 658 ALA 658 658 658 ALA ALA A . n 
A 1 659 GLU 659 659 659 GLU GLU A . n 
A 1 660 LYS 660 660 660 LYS LYS A . n 
A 1 661 LEU 661 661 661 LEU LEU A . n 
A 1 662 ASN 662 662 662 ASN ASN A . n 
A 1 663 LYS 663 663 663 LYS LYS A . n 
A 1 664 THR 664 664 664 THR THR A . n 
A 1 665 ALA 665 665 665 ALA ALA A . n 
A 1 666 LYS 666 666 666 LYS LYS A . n 
A 1 667 GLU 667 667 667 GLU GLU A . n 
A 1 668 LEU 668 668 668 LEU LEU A . n 
A 1 669 TYR 669 669 669 TYR TYR A . n 
A 1 670 ASN 670 670 670 ASN ASN A . n 
A 1 671 ILE 671 671 671 ILE ILE A . n 
A 1 672 ASP 672 672 672 ASP ASP A . n 
A 1 673 ASN 673 673 673 ASN ASN A . n 
A 1 674 PHE 674 674 674 PHE PHE A . n 
A 1 675 ALA 675 675 675 ALA ALA A . n 
A 1 676 ASP 676 676 676 ASP ASP A . n 
A 1 677 MET 677 677 677 MET MET A . n 
A 1 678 ILE 678 678 678 ILE ILE A . n 
A 1 679 CYS 679 679 679 CYS CYS A . n 
A 1 680 ASP 680 680 680 ASP ASP A . n 
A 1 681 GLU 681 681 681 GLU GLU A . n 
A 1 682 THR 682 682 682 THR THR A . n 
A 1 683 ILE 683 683 683 ILE ILE A . n 
A 1 684 ALA 684 684 684 ALA ALA A . n 
A 1 685 THR 685 685 685 THR THR A . n 
A 1 686 GLU 686 686 686 GLU GLU A . n 
A 1 687 SER 687 687 687 SER SER A . n 
A 1 688 GLU 688 688 688 GLU GLU A . n 
A 1 689 GLU 689 689 689 GLU GLU A . n 
A 1 690 VAL 690 690 690 VAL VAL A . n 
A 1 691 VAL 691 691 691 VAL VAL A . n 
A 1 692 LYS 692 692 692 LYS LYS A . n 
A 1 693 PHE 693 693 693 PHE PHE A . n 
A 1 694 LEU 694 694 694 LEU LEU A . n 
A 1 695 GLU 695 695 695 GLU GLU A . n 
A 1 696 GLU 696 696 696 GLU GLU A . n 
A 1 697 LYS 697 697 697 LYS LYS A . n 
A 1 698 GLY 698 698 698 GLY GLY A . n 
A 1 699 HIS 699 699 699 HIS HIS A . n 
A 1 700 PRO 700 700 700 PRO PRO A . n 
A 1 701 ALA 701 701 701 ALA ALA A . n 
A 1 702 LEU 702 702 702 LEU LEU A . n 
A 1 703 LYS 703 703 703 LYS LYS A . n 
A 1 704 MET 704 704 704 MET MET A . n 
A 1 705 ASP 705 705 705 ASP ASP A . n 
A 1 706 PRO 706 706 706 PRO PRO A . n 
A 1 707 ILE 707 707 707 ILE ILE A . n 
A 1 708 MET 708 708 708 MET MET A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   GLU 2   2   ?   ?   ?   B . n 
B 2 3   GLU 3   3   3   GLU GLU B . n 
B 2 4   LYS 4   4   4   LYS LYS B . n 
B 2 5   ALA 5   5   5   ALA ALA B . n 
B 2 6   LYS 6   6   6   LYS LYS B . n 
B 2 7   SER 7   7   7   SER SER B . n 
B 2 8   ILE 8   8   8   ILE ILE B . n 
B 2 9   ASP 9   9   9   ASP ASP B . n 
B 2 10  GLN 10  10  10  GLN GLN B . n 
B 2 11  ALA 11  11  11  ALA ALA B . n 
B 2 12  THR 12  12  12  THR THR B . n 
B 2 13  LEU 13  13  13  LEU LEU B . n 
B 2 14  GLN 14  14  14  GLN GLN B . n 
B 2 15  LEU 15  15  15  LEU LEU B . n 
B 2 16  LEU 16  16  16  LEU LEU B . n 
B 2 17  ASP 17  17  17  ASP ASP B . n 
B 2 18  LYS 18  18  18  LYS LYS B . n 
B 2 19  ALA 19  19  19  ALA ALA B . n 
B 2 20  LYS 20  20  20  LYS LYS B . n 
B 2 21  GLN 21  21  21  GLN GLN B . n 
B 2 22  ASP 22  22  22  ASP ASP B . n 
B 2 23  GLY 23  23  23  GLY GLY B . n 
B 2 24  VAL 24  24  24  VAL VAL B . n 
B 2 25  GLU 25  25  25  GLU GLU B . n 
B 2 26  THR 26  26  26  THR THR B . n 
B 2 27  VAL 27  27  27  VAL VAL B . n 
B 2 28  TRP 28  28  28  TRP TRP B . n 
B 2 29  ASP 29  29  29  ASP ASP B . n 
B 2 30  ARG 30  30  30  ARG ARG B . n 
B 2 31  LYS 31  31  31  LYS LYS B . n 
B 2 32  ALA 32  32  32  ALA ALA B . n 
B 2 33  ASP 33  33  33  ASP ASP B . n 
B 2 34  MET 34  34  34  MET MET B . n 
B 2 35  LYS 35  35  35  LYS LYS B . n 
B 2 36  VAL 36  36  36  VAL VAL B . n 
B 2 37  GLN 37  37  37  GLN GLN B . n 
B 2 38  CYS 38  38  38  CYS CYS B . n 
B 2 39  GLY 39  39  39  GLY GLY B . n 
B 2 40  PHE 40  40  40  PHE PHE B . n 
B 2 41  GLY 41  41  41  GLY GLY B . n 
B 2 42  SER 42  42  42  SER SER B . n 
B 2 43  ALA 43  43  43  ALA ALA B . n 
B 2 44  GLY 44  44  44  GLY GLY B . n 
B 2 45  VAL 45  45  45  VAL VAL B . n 
B 2 46  CYS 46  46  46  CYS CYS B . n 
B 2 47  CYS 47  47  47  CYS CYS B . n 
B 2 48  ARG 48  48  48  ARG ARG B . n 
B 2 49  ASN 49  49  49  ASN ASN B . n 
B 2 50  CYS 50  50  50  CYS CYS B . n 
B 2 51  SER 51  51  51  SER SER B . n 
B 2 52  MET 52  52  52  MET MET B . n 
B 2 53  GLY 53  53  53  GLY GLY B . n 
B 2 54  PRO 54  54  54  PRO PRO B . n 
B 2 55  CYS 55  55  55  CYS CYS B . n 
B 2 56  ARG 56  56  56  ARG ARG B . n 
B 2 57  VAL 57  57  57  VAL VAL B . n 
B 2 58  SER 58  58  58  SER SER B . n 
B 2 59  PRO 59  59  59  PRO PRO B . n 
B 2 60  VAL 60  60  60  VAL VAL B . n 
B 2 61  PRO 61  61  61  PRO PRO B . n 
B 2 62  GLY 62  62  62  GLY GLY B . n 
B 2 63  LYS 63  63  63  LYS LYS B . n 
B 2 64  GLY 64  64  64  GLY GLY B . n 
B 2 65  VAL 65  65  65  VAL VAL B . n 
B 2 66  GLU 66  66  66  GLU GLU B . n 
B 2 67  ARG 67  67  67  ARG ARG B . n 
B 2 68  GLY 68  68  68  GLY GLY B . n 
B 2 69  ILE 69  69  69  ILE ILE B . n 
B 2 70  CYS 70  70  70  CYS CYS B . n 
B 2 71  GLY 71  71  71  GLY GLY B . n 
B 2 72  ALA 72  72  72  ALA ALA B . n 
B 2 73  THR 73  73  73  THR THR B . n 
B 2 74  ALA 74  74  74  ALA ALA B . n 
B 2 75  ASP 75  75  75  ASP ASP B . n 
B 2 76  VAL 76  76  76  VAL VAL B . n 
B 2 77  ILE 77  77  77  ILE ILE B . n 
B 2 78  VAL 78  78  78  VAL VAL B . n 
B 2 79  SER 79  79  79  SER SER B . n 
B 2 80  ARG 80  80  80  ARG ARG B . n 
B 2 81  ASN 81  81  81  ASN ASN B . n 
B 2 82  PHE 82  82  82  PHE PHE B . n 
B 2 83  ALA 83  83  83  ALA ALA B . n 
B 2 84  ARG 84  84  84  ARG ARG B . n 
B 2 85  MET 85  85  85  MET MET B . n 
B 2 86  VAL 86  86  86  VAL VAL B . n 
B 2 87  ALA 87  87  87  ALA ALA B . n 
B 2 88  ALA 88  88  88  ALA ALA B . n 
B 2 89  GLY 89  89  89  GLY GLY B . n 
B 2 90  THR 90  90  90  THR THR B . n 
B 2 91  ALA 91  91  91  ALA ALA B . n 
B 2 92  ALA 92  92  92  ALA ALA B . n 
B 2 93  HIS 93  93  93  HIS HIS B . n 
B 2 94  SER 94  94  94  SER SER B . n 
B 2 95  ASP 95  95  95  ASP ASP B . n 
B 2 96  HIS 96  96  96  HIS HIS B . n 
B 2 97  GLY 97  97  97  GLY GLY B . n 
B 2 98  ARG 98  98  98  ARG ARG B . n 
B 2 99  SER 99  99  99  SER SER B . n 
B 2 100 ILE 100 100 100 ILE ILE B . n 
B 2 101 ALA 101 101 101 ALA ALA B . n 
B 2 102 LEU 102 102 102 LEU LEU B . n 
B 2 103 SER 103 103 103 SER SER B . n 
B 2 104 LEU 104 104 104 LEU LEU B . n 
B 2 105 TYR 105 105 105 TYR TYR B . n 
B 2 106 HIS 106 106 106 HIS HIS B . n 
B 2 107 THR 107 107 107 THR THR B . n 
B 2 108 SER 108 108 108 SER SER B . n 
B 2 109 LYS 109 109 109 LYS LYS B . n 
B 2 110 ASP 110 110 110 ASP ASP B . n 
B 2 111 GLY 111 111 111 GLY GLY B . n 
B 2 112 ASP 112 112 112 ASP ASP B . n 
B 2 113 ILE 113 113 113 ILE ILE B . n 
B 2 114 LYS 114 114 114 LYS LYS B . n 
B 2 115 VAL 115 115 115 VAL VAL B . n 
B 2 116 LYS 116 116 116 LYS LYS B . n 
B 2 117 ASP 117 117 117 ASP ASP B . n 
B 2 118 GLU 118 118 118 GLU GLU B . n 
B 2 119 ASN 119 119 119 ASN ASN B . n 
B 2 120 LYS 120 120 120 LYS LYS B . n 
B 2 121 LEU 121 121 121 LEU LEU B . n 
B 2 122 LYS 122 122 122 LYS LYS B . n 
B 2 123 GLU 123 123 123 GLU GLU B . n 
B 2 124 VAL 124 124 124 VAL VAL B . n 
B 2 125 ALA 125 125 125 ALA ALA B . n 
B 2 126 LYS 126 126 126 LYS LYS B . n 
B 2 127 SER 127 127 127 SER SER B . n 
B 2 128 PHE 128 128 128 PHE PHE B . n 
B 2 129 ASN 129 129 129 ASN ASN B . n 
B 2 130 VAL 130 130 130 VAL VAL B . n 
B 2 131 GLU 131 131 131 GLU GLU B . n 
B 2 132 THR 132 132 132 THR THR B . n 
B 2 133 GLU 133 133 133 GLU GLU B . n 
B 2 134 GLY 134 134 134 GLY GLY B . n 
B 2 135 ARG 135 135 135 ARG ARG B . n 
B 2 136 ASP 136 136 136 ASP ASP B . n 
B 2 137 ILE 137 137 137 ILE ILE B . n 
B 2 138 TYR 138 138 138 TYR TYR B . n 
B 2 139 ASP 139 139 139 ASP ASP B . n 
B 2 140 ILE 140 140 140 ILE ILE B . n 
B 2 141 ALA 141 141 141 ALA ALA B . n 
B 2 142 HIS 142 142 142 HIS HIS B . n 
B 2 143 ASP 143 143 143 ASP ASP B . n 
B 2 144 VAL 144 144 144 VAL VAL B . n 
B 2 145 ALA 145 145 145 ALA ALA B . n 
B 2 146 LYS 146 146 146 LYS LYS B . n 
B 2 147 GLU 147 147 147 GLU GLU B . n 
B 2 148 GLY 148 148 148 GLY GLY B . n 
B 2 149 LEU 149 149 149 LEU LEU B . n 
B 2 150 SER 150 150 150 SER SER B . n 
B 2 151 ASN 151 151 151 ASN ASN B . n 
B 2 152 TYR 152 152 152 TYR TYR B . n 
B 2 153 GLY 153 153 153 GLY GLY B . n 
B 2 154 LYS 154 154 154 LYS LYS B . n 
B 2 155 GLN 155 155 155 GLN GLN B . n 
B 2 156 LEU 156 156 156 LEU LEU B . n 
B 2 157 GLY 157 157 157 GLY GLY B . n 
B 2 158 GLU 158 158 158 GLU GLU B . n 
B 2 159 VAL 159 159 159 VAL VAL B . n 
B 2 160 THR 160 160 160 THR THR B . n 
B 2 161 LEU 161 161 161 LEU LEU B . n 
B 2 162 PRO 162 162 162 PRO PRO B . n 
B 2 163 PRO 163 163 163 PRO PRO B . n 
B 2 164 SER 164 164 164 SER SER B . n 
B 2 165 LEU 165 165 165 LEU LEU B . n 
B 2 166 PRO 166 166 166 PRO PRO B . n 
B 2 167 GLU 167 167 167 GLU GLU B . n 
B 2 168 LYS 168 168 168 LYS LYS B . n 
B 2 169 ARG 169 169 169 ARG ARG B . n 
B 2 170 LYS 170 170 170 LYS LYS B . n 
B 2 171 GLU 171 171 171 GLU GLU B . n 
B 2 172 LEU 172 172 172 LEU LEU B . n 
B 2 173 TRP 173 173 173 TRP TRP B . n 
B 2 174 ARG 174 174 174 ARG ARG B . n 
B 2 175 LYS 175 175 175 LYS LYS B . n 
B 2 176 LEU 176 176 176 LEU LEU B . n 
B 2 177 GLY 177 177 177 GLY GLY B . n 
B 2 178 VAL 178 178 178 VAL VAL B . n 
B 2 179 TYR 179 179 179 TYR TYR B . n 
B 2 180 PRO 180 180 180 PRO PRO B . n 
B 2 181 ARG 181 181 181 ARG ARG B . n 
B 2 182 ALA 182 182 182 ALA ALA B . n 
B 2 183 VAL 183 183 183 VAL VAL B . n 
B 2 184 ASP 184 184 184 ASP ASP B . n 
B 2 185 ARG 185 185 185 ARG ARG B . n 
B 2 186 GLU 186 186 186 GLU GLU B . n 
B 2 187 ILE 187 187 187 ILE ILE B . n 
B 2 188 ALA 188 188 188 ALA ALA B . n 
B 2 189 ALA 189 189 189 ALA ALA B . n 
B 2 190 VAL 190 190 190 VAL VAL B . n 
B 2 191 MET 191 191 191 MET MET B . n 
B 2 192 HIS 192 192 192 HIS HIS B . n 
B 2 193 SER 193 193 193 SER SER B . n 
B 2 194 THR 194 194 194 THR THR B . n 
B 2 195 HIS 195 195 195 HIS HIS B . n 
B 2 196 ILE 196 196 196 ILE ILE B . n 
B 2 197 GLY 197 197 197 GLY GLY B . n 
B 2 198 CYS 198 198 198 CYS CYS B . n 
B 2 199 ASN 199 199 199 ASN ASN B . n 
B 2 200 ALA 200 200 200 ALA ALA B . n 
B 2 201 ASP 201 201 201 ASP ASP B . n 
B 2 202 ALA 202 202 202 ALA ALA B . n 
B 2 203 GLU 203 203 203 GLU GLU B . n 
B 2 204 ALA 204 204 204 ALA ALA B . n 
B 2 205 MET 205 205 205 MET MET B . n 
B 2 206 ILE 206 206 206 ILE ILE B . n 
B 2 207 LYS 207 207 207 LYS LYS B . n 
B 2 208 MET 208 208 208 MET MET B . n 
B 2 209 SER 209 209 209 SER SER B . n 
B 2 210 MET 210 210 210 MET MET B . n 
B 2 211 ARG 211 211 211 ARG ARG B . n 
B 2 212 CYS 212 212 212 CYS CYS B . n 
B 2 213 SER 213 213 213 SER SER B . n 
B 2 214 LEU 214 214 214 LEU LEU B . n 
B 2 215 THR 215 215 215 THR THR B . n 
B 2 216 ASP 216 216 216 ASP ASP B . n 
B 2 217 GLY 217 217 217 GLY GLY B . n 
B 2 218 TRP 218 218 218 TRP TRP B . n 
B 2 219 MET 219 219 219 MET MET B . n 
B 2 220 GLY 220 220 220 GLY GLY B . n 
B 2 221 SER 221 221 221 SER SER B . n 
B 2 222 PHE 222 222 222 PHE PHE B . n 
B 2 223 MET 223 223 223 MET MET B . n 
B 2 224 GLY 224 224 224 GLY GLY B . n 
B 2 225 THR 225 225 225 THR THR B . n 
B 2 226 GLU 226 226 226 GLU GLU B . n 
B 2 227 PHE 227 227 227 PHE PHE B . n 
B 2 228 SER 228 228 228 SER SER B . n 
B 2 229 ASP 229 229 229 ASP ASP B . n 
B 2 230 ILE 230 230 230 ILE ILE B . n 
B 2 231 MET 231 231 231 MET MET B . n 
B 2 232 PHE 232 232 232 PHE PHE B . n 
B 2 233 GLY 233 233 233 GLY GLY B . n 
B 2 234 THR 234 234 234 THR THR B . n 
B 2 235 PRO 235 235 235 PRO PRO B . n 
B 2 236 HIS 236 236 236 HIS HIS B . n 
B 2 237 SER 237 237 237 SER SER B . n 
B 2 238 ILE 238 238 238 ILE ILE B . n 
B 2 239 ASP 239 239 239 ASP ASP B . n 
B 2 240 THR 240 240 240 THR THR B . n 
B 2 241 GLU 241 241 241 GLU GLU B . n 
B 2 242 ALA 242 242 242 ALA ALA B . n 
B 2 243 ASN 243 243 243 ASN ASN B . n 
B 2 244 LEU 244 244 244 LEU LEU B . n 
B 2 245 GLY 245 245 245 GLY GLY B . n 
B 2 246 VAL 246 246 246 VAL VAL B . n 
B 2 247 LEU 247 247 247 LEU LEU B . n 
B 2 248 GLU 248 248 248 GLU GLU B . n 
B 2 249 LYS 249 249 249 LYS LYS B . n 
B 2 250 ASN 250 250 250 ASN ASN B . n 
B 2 251 SER 251 251 251 SER SER B . n 
B 2 252 VAL 252 252 252 VAL VAL B . n 
B 2 253 ASN 253 253 253 ASN ASN B . n 
B 2 254 VAL 254 254 254 VAL VAL B . n 
B 2 255 VAL 255 255 255 VAL VAL B . n 
B 2 256 LEU 256 256 256 LEU LEU B . n 
B 2 257 HIS 257 257 257 HIS HIS B . n 
B 2 258 GLY 258 258 258 GLY GLY B . n 
B 2 259 HIS 259 259 259 HIS HIS B . n 
B 2 260 GLU 260 260 260 GLU GLU B . n 
B 2 261 PRO 261 261 261 PRO PRO B . n 
B 2 262 LEU 262 262 262 LEU LEU B . n 
B 2 263 LEU 263 263 263 LEU LEU B . n 
B 2 264 SER 264 264 264 SER SER B . n 
B 2 265 GLU 265 265 265 GLU GLU B . n 
B 2 266 MET 266 266 266 MET MET B . n 
B 2 267 VAL 267 267 267 VAL VAL B . n 
B 2 268 VAL 268 268 268 VAL VAL B . n 
B 2 269 GLU 269 269 269 GLU GLU B . n 
B 2 270 ALA 270 270 270 ALA ALA B . n 
B 2 271 ALA 271 271 271 ALA ALA B . n 
B 2 272 SER 272 272 272 SER SER B . n 
B 2 273 ASP 273 273 273 ASP ASP B . n 
B 2 274 PRO 274 274 274 PRO PRO B . n 
B 2 275 GLU 275 275 275 GLU GLU B . n 
B 2 276 LEU 276 276 276 LEU LEU B . n 
B 2 277 VAL 277 277 277 VAL VAL B . n 
B 2 278 GLU 278 278 278 GLU GLU B . n 
B 2 279 LEU 279 279 279 LEU LEU B . n 
B 2 280 ALA 280 280 280 ALA ALA B . n 
B 2 281 LYS 281 281 281 LYS LYS B . n 
B 2 282 SER 282 282 282 SER SER B . n 
B 2 283 VAL 283 283 283 VAL VAL B . n 
B 2 284 GLY 284 284 284 GLY GLY B . n 
B 2 285 ALA 285 285 285 ALA ALA B . n 
B 2 286 ASP 286 286 286 ASP ASP B . n 
B 2 287 GLY 287 287 287 GLY GLY B . n 
B 2 288 ILE 288 288 288 ILE ILE B . n 
B 2 289 ASN 289 289 289 ASN ASN B . n 
B 2 290 LEU 290 290 290 LEU LEU B . n 
B 2 291 CYS 291 291 291 CYS CYS B . n 
B 2 292 GLY 292 292 292 GLY GLY B . n 
B 2 293 MET 293 293 293 MET MET B . n 
B 2 294 CYS 294 294 294 CYS CYS B . n 
B 2 295 CYS 295 295 295 CYS CYS B . n 
B 2 296 THR 296 296 296 THR THR B . n 
B 2 297 GLY 297 297 297 GLY GLY B . n 
B 2 298 ASN 298 298 298 ASN ASN B . n 
B 2 299 GLU 299 299 299 GLU GLU B . n 
B 2 300 VAL 300 300 300 VAL VAL B . n 
B 2 301 SER 301 301 301 SER SER B . n 
B 2 302 MET 302 302 302 MET MET B . n 
B 2 303 ARG 303 303 303 ARG ARG B . n 
B 2 304 HIS 304 304 304 HIS HIS B . n 
B 2 305 GLY 305 305 305 GLY GLY B . n 
B 2 306 ILE 306 306 306 ILE ILE B . n 
B 2 307 LYS 307 307 307 LYS LYS B . n 
B 2 308 ILE 308 308 308 ILE ILE B . n 
B 2 309 ALA 309 309 309 ALA ALA B . n 
B 2 310 GLY 310 310 310 GLY GLY B . n 
B 2 311 ASN 311 311 311 ASN ASN B . n 
B 2 312 PHE 312 312 312 PHE PHE B . n 
B 2 313 MET 313 313 313 MET MET B . n 
B 2 314 GLN 314 314 314 GLN GLN B . n 
B 2 315 GLN 315 315 315 GLN GLN B . n 
B 2 316 GLU 316 316 316 GLU GLU B . n 
B 2 317 LEU 317 317 317 LEU LEU B . n 
B 2 318 ALA 318 318 318 ALA ALA B . n 
B 2 319 VAL 319 319 319 VAL VAL B . n 
B 2 320 VAL 320 320 320 VAL VAL B . n 
B 2 321 THR 321 321 321 THR THR B . n 
B 2 322 GLY 322 322 322 GLY GLY B . n 
B 2 323 ALA 323 323 323 ALA ALA B . n 
B 2 324 VAL 324 324 324 VAL VAL B . n 
B 2 325 ASP 325 325 325 ASP ASP B . n 
B 2 326 GLY 326 326 326 GLY GLY B . n 
B 2 327 LEU 327 327 327 LEU LEU B . n 
B 2 328 ILE 328 328 328 ILE ILE B . n 
B 2 329 VAL 329 329 329 VAL VAL B . n 
B 2 330 ASP 330 330 330 ASP ASP B . n 
B 2 331 VAL 331 331 331 VAL VAL B . n 
B 2 332 GLN 332 332 332 GLN GLN B . n 
B 2 333 CYS 333 333 333 CYS CYS B . n 
B 2 334 ILE 334 334 334 ILE ILE B . n 
B 2 335 MET 335 335 335 MET MET B . n 
B 2 336 PRO 336 336 336 PRO PRO B . n 
B 2 337 ALA 337 337 337 ALA ALA B . n 
B 2 338 LEU 338 338 338 LEU LEU B . n 
B 2 339 ALA 339 339 339 ALA ALA B . n 
B 2 340 LYS 340 340 340 LYS LYS B . n 
B 2 341 LEU 341 341 341 LEU LEU B . n 
B 2 342 SER 342 342 342 SER SER B . n 
B 2 343 LYS 343 343 343 LYS LYS B . n 
B 2 344 SER 344 344 344 SER SER B . n 
B 2 345 TYR 345 345 345 TYR TYR B . n 
B 2 346 HIS 346 346 346 HIS HIS B . n 
B 2 347 THR 347 347 347 THR THR B . n 
B 2 348 LYS 348 348 348 LYS LYS B . n 
B 2 349 PHE 349 349 349 PHE PHE B . n 
B 2 350 ILE 350 350 350 ILE ILE B . n 
B 2 351 THR 351 351 351 THR THR B . n 
B 2 352 THR 352 352 352 THR THR B . n 
B 2 353 SER 353 353 353 SER SER B . n 
B 2 354 PRO 354 354 354 PRO PRO B . n 
B 2 355 LYS 355 355 355 LYS LYS B . n 
B 2 356 ALA 356 356 356 ALA ALA B . n 
B 2 357 HIS 357 357 357 HIS HIS B . n 
B 2 358 ILE 358 358 358 ILE ILE B . n 
B 2 359 THR 359 359 359 THR THR B . n 
B 2 360 ASP 360 360 360 ASP ASP B . n 
B 2 361 SER 361 361 361 SER SER B . n 
B 2 362 ILE 362 362 362 ILE ILE B . n 
B 2 363 TYR 363 363 363 TYR TYR B . n 
B 2 364 MET 364 364 364 MET MET B . n 
B 2 365 GLU 365 365 365 GLU GLU B . n 
B 2 366 PHE 366 366 366 PHE PHE B . n 
B 2 367 ASP 367 367 367 ASP ASP B . n 
B 2 368 GLU 368 368 368 GLU GLU B . n 
B 2 369 GLU 369 369 369 GLU GLU B . n 
B 2 370 ASN 370 370 370 ASN ASN B . n 
B 2 371 PRO 371 371 371 PRO PRO B . n 
B 2 372 LEU 372 372 372 LEU LEU B . n 
B 2 373 ASP 373 373 373 ASP ASP B . n 
B 2 374 SER 374 374 374 SER SER B . n 
B 2 375 ALA 375 375 375 ALA ALA B . n 
B 2 376 LYS 376 376 376 LYS LYS B . n 
B 2 377 LYS 377 377 377 LYS LYS B . n 
B 2 378 ILE 378 378 378 ILE ILE B . n 
B 2 379 LEU 379 379 379 LEU LEU B . n 
B 2 380 LYS 380 380 380 LYS LYS B . n 
B 2 381 GLU 381 381 381 GLU GLU B . n 
B 2 382 ALA 382 382 382 ALA ALA B . n 
B 2 383 ILE 383 383 383 ILE ILE B . n 
B 2 384 LEU 384 384 384 LEU LEU B . n 
B 2 385 ASN 385 385 385 ASN ASN B . n 
B 2 386 PHE 386 386 386 PHE PHE B . n 
B 2 387 LYS 387 387 387 LYS LYS B . n 
B 2 388 ASN 388 388 388 ASN ASN B . n 
B 2 389 ARG 389 389 389 ARG ARG B . n 
B 2 390 ASP 390 390 390 ASP ASP B . n 
B 2 391 GLN 391 391 391 GLN GLN B . n 
B 2 392 SER 392 392 392 SER SER B . n 
B 2 393 LYS 393 393 393 LYS LYS B . n 
B 2 394 VAL 394 394 394 VAL VAL B . n 
B 2 395 MET 395 395 395 MET MET B . n 
B 2 396 ILE 396 396 396 ILE ILE B . n 
B 2 397 PRO 397 397 397 PRO PRO B . n 
B 2 398 GLU 398 398 398 GLU GLU B . n 
B 2 399 LEU 399 399 399 LEU LEU B . n 
B 2 400 LYS 400 400 400 LYS LYS B . n 
B 2 401 CYS 401 401 401 CYS CYS B . n 
B 2 402 LYS 402 402 402 LYS LYS B . n 
B 2 403 ALA 403 403 403 ALA ALA B . n 
B 2 404 ILE 404 404 404 ILE ILE B . n 
B 2 405 LEU 405 405 405 LEU LEU B . n 
B 2 406 GLY 406 406 406 GLY GLY B . n 
B 2 407 TYR 407 407 407 TYR TYR B . n 
B 2 408 SER 408 408 408 SER SER B . n 
B 2 409 VAL 409 409 409 VAL VAL B . n 
B 2 410 GLU 410 410 410 GLU GLU B . n 
B 2 411 GLU 411 411 411 GLU GLU B . n 
B 2 412 ILE 412 412 412 ILE ILE B . n 
B 2 413 ILE 413 413 413 ILE ILE B . n 
B 2 414 ASN 414 414 414 ASN ASN B . n 
B 2 415 LYS 415 415 415 LYS LYS B . n 
B 2 416 LEU 416 416 416 LEU LEU B . n 
B 2 417 ASP 417 417 417 ASP ASP B . n 
B 2 418 LYS 418 418 418 LYS LYS B . n 
B 2 419 VAL 419 419 419 VAL VAL B . n 
B 2 420 VAL 420 420 420 VAL VAL B . n 
B 2 421 ASN 421 421 421 ASN ASN B . n 
B 2 422 THR 422 422 422 THR THR B . n 
B 2 423 GLN 423 423 423 GLN GLN B . n 
B 2 424 ILE 424 424 424 ILE ILE B . n 
B 2 425 GLY 425 425 425 GLY GLY B . n 
B 2 426 PRO 426 426 426 PRO PRO B . n 
B 2 427 MET 427 427 427 MET MET B . n 
B 2 428 GLN 428 428 428 GLN GLN B . n 
B 2 429 THR 429 429 429 THR THR B . n 
B 2 430 VAL 430 430 430 VAL VAL B . n 
B 2 431 LYS 431 431 431 LYS LYS B . n 
B 2 432 PRO 432 432 432 PRO PRO B . n 
B 2 433 LEU 433 433 433 LEU LEU B . n 
B 2 434 ALA 434 434 434 ALA ALA B . n 
B 2 435 ASP 435 435 435 ASP ASP B . n 
B 2 436 VAL 436 436 436 VAL VAL B . n 
B 2 437 LEU 437 437 437 LEU LEU B . n 
B 2 438 VAL 438 438 438 VAL VAL B . n 
B 2 439 SER 439 439 439 SER SER B . n 
B 2 440 GLY 440 440 440 GLY GLY B . n 
B 2 441 VAL 441 441 441 VAL VAL B . n 
B 2 442 LEU 442 442 442 LEU LEU B . n 
B 2 443 ARG 443 443 443 ARG ARG B . n 
B 2 444 GLY 444 444 444 GLY GLY B . n 
B 2 445 ALA 445 445 445 ALA ALA B . n 
B 2 446 ALA 446 446 446 ALA ALA B . n 
B 2 447 ALA 447 447 447 ALA ALA B . n 
B 2 448 VAL 448 448 448 VAL VAL B . n 
B 2 449 VAL 449 449 449 VAL VAL B . n 
B 2 450 GLY 450 450 450 GLY GLY B . n 
B 2 451 CYS 451 451 451 CYS CYS B . n 
B 2 452 ASN 452 452 452 ASN ASN B . n 
B 2 453 ASN 453 453 453 ASN ASN B . n 
B 2 454 PRO 454 454 454 PRO PRO B . n 
B 2 455 LYS 455 455 455 LYS LYS B . n 
B 2 456 VAL 456 456 456 VAL VAL B . n 
B 2 457 VAL 457 457 457 VAL VAL B . n 
B 2 458 GLN 458 458 458 GLN GLN B . n 
B 2 459 ASP 459 459 459 ASP ASP B . n 
B 2 460 SER 460 460 460 SER SER B . n 
B 2 461 ALA 461 461 461 ALA ALA B . n 
B 2 462 HIS 462 462 462 HIS HIS B . n 
B 2 463 ILE 463 463 463 ILE ILE B . n 
B 2 464 GLU 464 464 464 GLU GLU B . n 
B 2 465 THR 465 465 465 THR THR B . n 
B 2 466 ILE 466 466 466 ILE ILE B . n 
B 2 467 LYS 467 467 467 LYS LYS B . n 
B 2 468 GLY 468 468 468 GLY GLY B . n 
B 2 469 LEU 469 469 469 LEU LEU B . n 
B 2 470 ILE 470 470 470 ILE ILE B . n 
B 2 471 LYS 471 471 471 LYS LYS B . n 
B 2 472 ASN 472 472 472 ASN ASN B . n 
B 2 473 ASP 473 473 473 ASP ASP B . n 
B 2 474 VAL 474 474 474 VAL VAL B . n 
B 2 475 ILE 475 475 475 ILE ILE B . n 
B 2 476 VAL 476 476 476 VAL VAL B . n 
B 2 477 VAL 477 477 477 VAL VAL B . n 
B 2 478 VAL 478 478 478 VAL VAL B . n 
B 2 479 THR 479 479 479 THR THR B . n 
B 2 480 GLY 480 480 480 GLY GLY B . n 
B 2 481 CYS 481 481 481 CYS CYS B . n 
B 2 482 ALA 482 482 482 ALA ALA B . n 
B 2 483 ALA 483 483 483 ALA ALA B . n 
B 2 484 GLN 484 484 484 GLN GLN B . n 
B 2 485 ALA 485 485 485 ALA ALA B . n 
B 2 486 ALA 486 486 486 ALA ALA B . n 
B 2 487 ALA 487 487 487 ALA ALA B . n 
B 2 488 LYS 488 488 488 LYS LYS B . n 
B 2 489 TYR 489 489 489 TYR TYR B . n 
B 2 490 GLY 490 490 490 GLY GLY B . n 
B 2 491 LEU 491 491 491 LEU LEU B . n 
B 2 492 LEU 492 492 492 LEU LEU B . n 
B 2 493 GLN 493 493 493 GLN GLN B . n 
B 2 494 LYS 494 494 494 LYS LYS B . n 
B 2 495 GLU 495 495 495 GLU GLU B . n 
B 2 496 ALA 496 496 496 ALA ALA B . n 
B 2 497 ALA 497 497 497 ALA ALA B . n 
B 2 498 GLU 498 498 498 GLU GLU B . n 
B 2 499 LYS 499 499 499 LYS LYS B . n 
B 2 500 TYR 500 500 500 TYR TYR B . n 
B 2 501 ALA 501 501 501 ALA ALA B . n 
B 2 502 GLY 502 502 502 GLY GLY B . n 
B 2 503 PRO 503 503 503 PRO PRO B . n 
B 2 504 GLY 504 504 504 GLY GLY B . n 
B 2 505 LEU 505 505 505 LEU LEU B . n 
B 2 506 ALA 506 506 506 ALA ALA B . n 
B 2 507 THR 507 507 507 THR THR B . n 
B 2 508 VAL 508 508 508 VAL VAL B . n 
B 2 509 CYS 509 509 509 CYS CYS B . n 
B 2 510 LYS 510 510 510 LYS LYS B . n 
B 2 511 LEU 511 511 511 LEU LEU B . n 
B 2 512 VAL 512 512 512 VAL VAL B . n 
B 2 513 ASP 513 513 513 ASP ASP B . n 
B 2 514 ILE 514 514 514 ILE ILE B . n 
B 2 515 PRO 515 515 515 PRO PRO B . n 
B 2 516 PRO 516 516 516 PRO PRO B . n 
B 2 517 VAL 517 517 517 VAL VAL B . n 
B 2 518 LEU 518 518 518 LEU LEU B . n 
B 2 519 HIS 519 519 519 HIS HIS B . n 
B 2 520 MET 520 520 520 MET MET B . n 
B 2 521 GLY 521 521 521 GLY GLY B . n 
B 2 522 SER 522 522 522 SER SER B . n 
B 2 523 CYS 523 523 523 CYS CYS B . n 
B 2 524 VAL 524 524 524 VAL VAL B . n 
B 2 525 ASP 525 525 525 ASP ASP B . n 
B 2 526 ILE 526 526 526 ILE ILE B . n 
B 2 527 SER 527 527 527 SER SER B . n 
B 2 528 ARG 528 528 528 ARG ARG B . n 
B 2 529 ILE 529 529 529 ILE ILE B . n 
B 2 530 LEU 530 530 530 LEU LEU B . n 
B 2 531 ASP 531 531 531 ASP ASP B . n 
B 2 532 LEU 532 532 532 LEU LEU B . n 
B 2 533 VAL 533 533 533 VAL VAL B . n 
B 2 534 GLY 534 534 534 GLY GLY B . n 
B 2 535 ARG 535 535 535 ARG ARG B . n 
B 2 536 VAL 536 536 536 VAL VAL B . n 
B 2 537 ALA 537 537 537 ALA ALA B . n 
B 2 538 ASN 538 538 538 ASN ASN B . n 
B 2 539 LEU 539 539 539 LEU LEU B . n 
B 2 540 LEU 540 540 540 LEU LEU B . n 
B 2 541 GLY 541 541 541 GLY GLY B . n 
B 2 542 VAL 542 542 542 VAL VAL B . n 
B 2 543 ASP 543 543 543 ASP ASP B . n 
B 2 544 MET 544 544 544 MET MET B . n 
B 2 545 SER 545 545 545 SER SER B . n 
B 2 546 ASP 546 546 546 ASP ASP B . n 
B 2 547 LEU 547 547 547 LEU LEU B . n 
B 2 548 PRO 548 548 548 PRO PRO B . n 
B 2 549 VAL 549 549 549 VAL VAL B . n 
B 2 550 ALA 550 550 550 ALA ALA B . n 
B 2 551 GLY 551 551 551 GLY GLY B . n 
B 2 552 VAL 552 552 552 VAL VAL B . n 
B 2 553 ALA 553 553 553 ALA ALA B . n 
B 2 554 PRO 554 554 554 PRO PRO B . n 
B 2 555 GLU 555 555 555 GLU GLU B . n 
B 2 556 TRP 556 556 556 TRP TRP B . n 
B 2 557 MET 557 557 557 MET MET B . n 
B 2 558 SER 558 558 558 SER SER B . n 
B 2 559 GLU 559 559 559 GLU GLU B . n 
B 2 560 LYS 560 560 560 LYS LYS B . n 
B 2 561 ALA 561 561 561 ALA ALA B . n 
B 2 562 VAL 562 562 562 VAL VAL B . n 
B 2 563 ALA 563 563 563 ALA ALA B . n 
B 2 564 ILE 564 564 564 ILE ILE B . n 
B 2 565 GLY 565 565 565 GLY GLY B . n 
B 2 566 THR 566 566 566 THR THR B . n 
B 2 567 TYR 567 567 567 TYR TYR B . n 
B 2 568 VAL 568 568 568 VAL VAL B . n 
B 2 569 VAL 569 569 569 VAL VAL B . n 
B 2 570 THR 570 570 570 THR THR B . n 
B 2 571 SER 571 571 571 SER SER B . n 
B 2 572 GLY 572 572 572 GLY GLY B . n 
B 2 573 ILE 573 573 573 ILE ILE B . n 
B 2 574 ASP 574 574 574 ASP ASP B . n 
B 2 575 THR 575 575 575 THR THR B . n 
B 2 576 TRP 576 576 576 TRP TRP B . n 
B 2 577 LEU 577 577 577 LEU LEU B . n 
B 2 578 GLY 578 578 578 GLY GLY B . n 
B 2 579 VAL 579 579 579 VAL VAL B . n 
B 2 580 ALA 580 580 580 ALA ALA B . n 
B 2 581 PRO 581 581 581 PRO PRO B . n 
B 2 582 PRO 582 582 582 PRO PRO B . n 
B 2 583 VAL 583 583 583 VAL VAL B . n 
B 2 584 THR 584 584 584 THR THR B . n 
B 2 585 GLY 585 585 585 GLY GLY B . n 
B 2 586 GLY 586 586 586 GLY GLY B . n 
B 2 587 PRO 587 587 587 PRO PRO B . n 
B 2 588 GLU 588 588 588 GLU GLU B . n 
B 2 589 VAL 589 589 589 VAL VAL B . n 
B 2 590 VAL 590 590 590 VAL VAL B . n 
B 2 591 ASP 591 591 591 ASP ASP B . n 
B 2 592 ILE 592 592 592 ILE ILE B . n 
B 2 593 LEU 593 593 593 LEU LEU B . n 
B 2 594 THR 594 594 594 THR THR B . n 
B 2 595 ASN 595 595 595 ASN ASN B . n 
B 2 596 LYS 596 596 596 LYS LYS B . n 
B 2 597 MET 597 597 597 MET MET B . n 
B 2 598 GLU 598 598 598 GLU GLU B . n 
B 2 599 ASP 599 599 599 ASP ASP B . n 
B 2 600 TRP 600 600 600 TRP TRP B . n 
B 2 601 VAL 601 601 601 VAL VAL B . n 
B 2 602 GLY 602 602 602 GLY GLY B . n 
B 2 603 ALA 603 603 603 ALA ALA B . n 
B 2 604 LYS 604 604 604 LYS LYS B . n 
B 2 605 PHE 605 605 605 PHE PHE B . n 
B 2 606 PHE 606 606 606 PHE PHE B . n 
B 2 607 ILE 607 607 607 ILE ILE B . n 
B 2 608 GLU 608 608 608 GLU GLU B . n 
B 2 609 THR 609 609 609 THR THR B . n 
B 2 610 ASP 610 610 610 ASP ASP B . n 
B 2 611 PRO 611 611 611 PRO PRO B . n 
B 2 612 HIS 612 612 612 HIS HIS B . n 
B 2 613 LYS 613 613 613 LYS LYS B . n 
B 2 614 ALA 614 614 614 ALA ALA B . n 
B 2 615 VAL 615 615 615 VAL VAL B . n 
B 2 616 GLU 616 616 616 GLU GLU B . n 
B 2 617 GLN 617 617 617 GLN GLN B . n 
B 2 618 ILE 618 618 618 ILE ILE B . n 
B 2 619 VAL 619 619 619 VAL VAL B . n 
B 2 620 ASN 620 620 620 ASN ASN B . n 
B 2 621 ARG 621 621 621 ARG ARG B . n 
B 2 622 MET 622 622 622 MET MET B . n 
B 2 623 ASN 623 623 623 ASN ASN B . n 
B 2 624 GLU 624 624 624 GLU GLU B . n 
B 2 625 LYS 625 625 625 LYS LYS B . n 
B 2 626 ARG 626 626 626 ARG ARG B . n 
B 2 627 LYS 627 627 627 LYS LYS B . n 
B 2 628 LYS 628 628 628 LYS LYS B . n 
B 2 629 LEU 629 629 629 LEU LEU B . n 
B 2 630 GLY 630 630 630 GLY GLY B . n 
B 2 631 ILE 631 631 631 ILE ILE B . n 
C 2 1   MET 1   1   ?   ?   ?   C . n 
C 2 2   GLU 2   2   2   GLU GLU C . n 
C 2 3   GLU 3   3   3   GLU GLU C . n 
C 2 4   LYS 4   4   4   LYS LYS C . n 
C 2 5   ALA 5   5   5   ALA ALA C . n 
C 2 6   LYS 6   6   6   LYS LYS C . n 
C 2 7   SER 7   7   7   SER SER C . n 
C 2 8   ILE 8   8   8   ILE ILE C . n 
C 2 9   ASP 9   9   9   ASP ASP C . n 
C 2 10  GLN 10  10  10  GLN GLN C . n 
C 2 11  ALA 11  11  11  ALA ALA C . n 
C 2 12  THR 12  12  12  THR THR C . n 
C 2 13  LEU 13  13  13  LEU LEU C . n 
C 2 14  GLN 14  14  14  GLN GLN C . n 
C 2 15  LEU 15  15  15  LEU LEU C . n 
C 2 16  LEU 16  16  16  LEU LEU C . n 
C 2 17  ASP 17  17  17  ASP ASP C . n 
C 2 18  LYS 18  18  18  LYS LYS C . n 
C 2 19  ALA 19  19  19  ALA ALA C . n 
C 2 20  LYS 20  20  20  LYS LYS C . n 
C 2 21  GLN 21  21  21  GLN GLN C . n 
C 2 22  ASP 22  22  22  ASP ASP C . n 
C 2 23  GLY 23  23  23  GLY GLY C . n 
C 2 24  VAL 24  24  24  VAL VAL C . n 
C 2 25  GLU 25  25  25  GLU GLU C . n 
C 2 26  THR 26  26  26  THR THR C . n 
C 2 27  VAL 27  27  27  VAL VAL C . n 
C 2 28  TRP 28  28  28  TRP TRP C . n 
C 2 29  ASP 29  29  29  ASP ASP C . n 
C 2 30  ARG 30  30  30  ARG ARG C . n 
C 2 31  LYS 31  31  31  LYS LYS C . n 
C 2 32  ALA 32  32  32  ALA ALA C . n 
C 2 33  ASP 33  33  33  ASP ASP C . n 
C 2 34  MET 34  34  34  MET MET C . n 
C 2 35  LYS 35  35  35  LYS LYS C . n 
C 2 36  VAL 36  36  36  VAL VAL C . n 
C 2 37  GLN 37  37  37  GLN GLN C . n 
C 2 38  CYS 38  38  38  CYS CYS C . n 
C 2 39  GLY 39  39  39  GLY GLY C . n 
C 2 40  PHE 40  40  40  PHE PHE C . n 
C 2 41  GLY 41  41  41  GLY GLY C . n 
C 2 42  SER 42  42  42  SER SER C . n 
C 2 43  ALA 43  43  43  ALA ALA C . n 
C 2 44  GLY 44  44  44  GLY GLY C . n 
C 2 45  VAL 45  45  45  VAL VAL C . n 
C 2 46  CYS 46  46  46  CYS CYS C . n 
C 2 47  CYS 47  47  47  CYS CYS C . n 
C 2 48  ARG 48  48  48  ARG ARG C . n 
C 2 49  ASN 49  49  49  ASN ASN C . n 
C 2 50  CYS 50  50  50  CYS CYS C . n 
C 2 51  SER 51  51  51  SER SER C . n 
C 2 52  MET 52  52  52  MET MET C . n 
C 2 53  GLY 53  53  53  GLY GLY C . n 
C 2 54  PRO 54  54  54  PRO PRO C . n 
C 2 55  CYS 55  55  55  CYS CYS C . n 
C 2 56  ARG 56  56  56  ARG ARG C . n 
C 2 57  VAL 57  57  57  VAL VAL C . n 
C 2 58  SER 58  58  58  SER SER C . n 
C 2 59  PRO 59  59  59  PRO PRO C . n 
C 2 60  VAL 60  60  60  VAL VAL C . n 
C 2 61  PRO 61  61  61  PRO PRO C . n 
C 2 62  GLY 62  62  62  GLY GLY C . n 
C 2 63  LYS 63  63  63  LYS LYS C . n 
C 2 64  GLY 64  64  64  GLY GLY C . n 
C 2 65  VAL 65  65  65  VAL VAL C . n 
C 2 66  GLU 66  66  66  GLU GLU C . n 
C 2 67  ARG 67  67  67  ARG ARG C . n 
C 2 68  GLY 68  68  68  GLY GLY C . n 
C 2 69  ILE 69  69  69  ILE ILE C . n 
C 2 70  CYS 70  70  70  CYS CYS C . n 
C 2 71  GLY 71  71  71  GLY GLY C . n 
C 2 72  ALA 72  72  72  ALA ALA C . n 
C 2 73  THR 73  73  73  THR THR C . n 
C 2 74  ALA 74  74  74  ALA ALA C . n 
C 2 75  ASP 75  75  75  ASP ASP C . n 
C 2 76  VAL 76  76  76  VAL VAL C . n 
C 2 77  ILE 77  77  77  ILE ILE C . n 
C 2 78  VAL 78  78  78  VAL VAL C . n 
C 2 79  SER 79  79  79  SER SER C . n 
C 2 80  ARG 80  80  80  ARG ARG C . n 
C 2 81  ASN 81  81  81  ASN ASN C . n 
C 2 82  PHE 82  82  82  PHE PHE C . n 
C 2 83  ALA 83  83  83  ALA ALA C . n 
C 2 84  ARG 84  84  84  ARG ARG C . n 
C 2 85  MET 85  85  85  MET MET C . n 
C 2 86  VAL 86  86  86  VAL VAL C . n 
C 2 87  ALA 87  87  87  ALA ALA C . n 
C 2 88  ALA 88  88  88  ALA ALA C . n 
C 2 89  GLY 89  89  89  GLY GLY C . n 
C 2 90  THR 90  90  90  THR THR C . n 
C 2 91  ALA 91  91  91  ALA ALA C . n 
C 2 92  ALA 92  92  92  ALA ALA C . n 
C 2 93  HIS 93  93  93  HIS HIS C . n 
C 2 94  SER 94  94  94  SER SER C . n 
C 2 95  ASP 95  95  95  ASP ASP C . n 
C 2 96  HIS 96  96  96  HIS HIS C . n 
C 2 97  GLY 97  97  97  GLY GLY C . n 
C 2 98  ARG 98  98  98  ARG ARG C . n 
C 2 99  SER 99  99  99  SER SER C . n 
C 2 100 ILE 100 100 100 ILE ILE C . n 
C 2 101 ALA 101 101 101 ALA ALA C . n 
C 2 102 LEU 102 102 102 LEU LEU C . n 
C 2 103 SER 103 103 103 SER SER C . n 
C 2 104 LEU 104 104 104 LEU LEU C . n 
C 2 105 TYR 105 105 105 TYR TYR C . n 
C 2 106 HIS 106 106 106 HIS HIS C . n 
C 2 107 THR 107 107 107 THR THR C . n 
C 2 108 SER 108 108 108 SER SER C . n 
C 2 109 LYS 109 109 109 LYS LYS C . n 
C 2 110 ASP 110 110 110 ASP ASP C . n 
C 2 111 GLY 111 111 111 GLY GLY C . n 
C 2 112 ASP 112 112 112 ASP ASP C . n 
C 2 113 ILE 113 113 113 ILE ILE C . n 
C 2 114 LYS 114 114 114 LYS LYS C . n 
C 2 115 VAL 115 115 115 VAL VAL C . n 
C 2 116 LYS 116 116 116 LYS LYS C . n 
C 2 117 ASP 117 117 117 ASP ASP C . n 
C 2 118 GLU 118 118 118 GLU GLU C . n 
C 2 119 ASN 119 119 119 ASN ASN C . n 
C 2 120 LYS 120 120 120 LYS LYS C . n 
C 2 121 LEU 121 121 121 LEU LEU C . n 
C 2 122 LYS 122 122 122 LYS LYS C . n 
C 2 123 GLU 123 123 123 GLU GLU C . n 
C 2 124 VAL 124 124 124 VAL VAL C . n 
C 2 125 ALA 125 125 125 ALA ALA C . n 
C 2 126 LYS 126 126 126 LYS LYS C . n 
C 2 127 SER 127 127 127 SER SER C . n 
C 2 128 PHE 128 128 128 PHE PHE C . n 
C 2 129 ASN 129 129 129 ASN ASN C . n 
C 2 130 VAL 130 130 130 VAL VAL C . n 
C 2 131 GLU 131 131 131 GLU GLU C . n 
C 2 132 THR 132 132 132 THR THR C . n 
C 2 133 GLU 133 133 133 GLU GLU C . n 
C 2 134 GLY 134 134 134 GLY GLY C . n 
C 2 135 ARG 135 135 135 ARG ARG C . n 
C 2 136 ASP 136 136 136 ASP ASP C . n 
C 2 137 ILE 137 137 137 ILE ILE C . n 
C 2 138 TYR 138 138 138 TYR TYR C . n 
C 2 139 ASP 139 139 139 ASP ASP C . n 
C 2 140 ILE 140 140 140 ILE ILE C . n 
C 2 141 ALA 141 141 141 ALA ALA C . n 
C 2 142 HIS 142 142 142 HIS HIS C . n 
C 2 143 ASP 143 143 143 ASP ASP C . n 
C 2 144 VAL 144 144 144 VAL VAL C . n 
C 2 145 ALA 145 145 145 ALA ALA C . n 
C 2 146 LYS 146 146 146 LYS LYS C . n 
C 2 147 GLU 147 147 147 GLU GLU C . n 
C 2 148 GLY 148 148 148 GLY GLY C . n 
C 2 149 LEU 149 149 149 LEU LEU C . n 
C 2 150 SER 150 150 150 SER SER C . n 
C 2 151 ASN 151 151 151 ASN ASN C . n 
C 2 152 TYR 152 152 152 TYR TYR C . n 
C 2 153 GLY 153 153 153 GLY GLY C . n 
C 2 154 LYS 154 154 154 LYS LYS C . n 
C 2 155 GLN 155 155 155 GLN GLN C . n 
C 2 156 LEU 156 156 156 LEU LEU C . n 
C 2 157 GLY 157 157 157 GLY GLY C . n 
C 2 158 GLU 158 158 158 GLU GLU C . n 
C 2 159 VAL 159 159 159 VAL VAL C . n 
C 2 160 THR 160 160 160 THR THR C . n 
C 2 161 LEU 161 161 161 LEU LEU C . n 
C 2 162 PRO 162 162 162 PRO PRO C . n 
C 2 163 PRO 163 163 163 PRO PRO C . n 
C 2 164 SER 164 164 164 SER SER C . n 
C 2 165 LEU 165 165 165 LEU LEU C . n 
C 2 166 PRO 166 166 166 PRO PRO C . n 
C 2 167 GLU 167 167 167 GLU GLU C . n 
C 2 168 LYS 168 168 168 LYS LYS C . n 
C 2 169 ARG 169 169 169 ARG ARG C . n 
C 2 170 LYS 170 170 170 LYS LYS C . n 
C 2 171 GLU 171 171 171 GLU GLU C . n 
C 2 172 LEU 172 172 172 LEU LEU C . n 
C 2 173 TRP 173 173 173 TRP TRP C . n 
C 2 174 ARG 174 174 174 ARG ARG C . n 
C 2 175 LYS 175 175 175 LYS LYS C . n 
C 2 176 LEU 176 176 176 LEU LEU C . n 
C 2 177 GLY 177 177 177 GLY GLY C . n 
C 2 178 VAL 178 178 178 VAL VAL C . n 
C 2 179 TYR 179 179 179 TYR TYR C . n 
C 2 180 PRO 180 180 180 PRO PRO C . n 
C 2 181 ARG 181 181 181 ARG ARG C . n 
C 2 182 ALA 182 182 182 ALA ALA C . n 
C 2 183 VAL 183 183 183 VAL VAL C . n 
C 2 184 ASP 184 184 184 ASP ASP C . n 
C 2 185 ARG 185 185 185 ARG ARG C . n 
C 2 186 GLU 186 186 186 GLU GLU C . n 
C 2 187 ILE 187 187 187 ILE ILE C . n 
C 2 188 ALA 188 188 188 ALA ALA C . n 
C 2 189 ALA 189 189 189 ALA ALA C . n 
C 2 190 VAL 190 190 190 VAL VAL C . n 
C 2 191 MET 191 191 191 MET MET C . n 
C 2 192 HIS 192 192 192 HIS HIS C . n 
C 2 193 SER 193 193 193 SER SER C . n 
C 2 194 THR 194 194 194 THR THR C . n 
C 2 195 HIS 195 195 195 HIS HIS C . n 
C 2 196 ILE 196 196 196 ILE ILE C . n 
C 2 197 GLY 197 197 197 GLY GLY C . n 
C 2 198 CYS 198 198 198 CYS CYS C . n 
C 2 199 ASN 199 199 199 ASN ASN C . n 
C 2 200 ALA 200 200 200 ALA ALA C . n 
C 2 201 ASP 201 201 201 ASP ASP C . n 
C 2 202 ALA 202 202 202 ALA ALA C . n 
C 2 203 GLU 203 203 203 GLU GLU C . n 
C 2 204 ALA 204 204 204 ALA ALA C . n 
C 2 205 MET 205 205 205 MET MET C . n 
C 2 206 ILE 206 206 206 ILE ILE C . n 
C 2 207 LYS 207 207 207 LYS LYS C . n 
C 2 208 MET 208 208 208 MET MET C . n 
C 2 209 SER 209 209 209 SER SER C . n 
C 2 210 MET 210 210 210 MET MET C . n 
C 2 211 ARG 211 211 211 ARG ARG C . n 
C 2 212 CYS 212 212 212 CYS CYS C . n 
C 2 213 SER 213 213 213 SER SER C . n 
C 2 214 LEU 214 214 214 LEU LEU C . n 
C 2 215 THR 215 215 215 THR THR C . n 
C 2 216 ASP 216 216 216 ASP ASP C . n 
C 2 217 GLY 217 217 217 GLY GLY C . n 
C 2 218 TRP 218 218 218 TRP TRP C . n 
C 2 219 MET 219 219 219 MET MET C . n 
C 2 220 GLY 220 220 220 GLY GLY C . n 
C 2 221 SER 221 221 221 SER SER C . n 
C 2 222 PHE 222 222 222 PHE PHE C . n 
C 2 223 MET 223 223 223 MET MET C . n 
C 2 224 GLY 224 224 224 GLY GLY C . n 
C 2 225 THR 225 225 225 THR THR C . n 
C 2 226 GLU 226 226 226 GLU GLU C . n 
C 2 227 PHE 227 227 227 PHE PHE C . n 
C 2 228 SER 228 228 228 SER SER C . n 
C 2 229 ASP 229 229 229 ASP ASP C . n 
C 2 230 ILE 230 230 230 ILE ILE C . n 
C 2 231 MET 231 231 231 MET MET C . n 
C 2 232 PHE 232 232 232 PHE PHE C . n 
C 2 233 GLY 233 233 233 GLY GLY C . n 
C 2 234 THR 234 234 234 THR THR C . n 
C 2 235 PRO 235 235 235 PRO PRO C . n 
C 2 236 HIS 236 236 236 HIS HIS C . n 
C 2 237 SER 237 237 237 SER SER C . n 
C 2 238 ILE 238 238 238 ILE ILE C . n 
C 2 239 ASP 239 239 239 ASP ASP C . n 
C 2 240 THR 240 240 240 THR THR C . n 
C 2 241 GLU 241 241 241 GLU GLU C . n 
C 2 242 ALA 242 242 242 ALA ALA C . n 
C 2 243 ASN 243 243 243 ASN ASN C . n 
C 2 244 LEU 244 244 244 LEU LEU C . n 
C 2 245 GLY 245 245 245 GLY GLY C . n 
C 2 246 VAL 246 246 246 VAL VAL C . n 
C 2 247 LEU 247 247 247 LEU LEU C . n 
C 2 248 GLU 248 248 248 GLU GLU C . n 
C 2 249 LYS 249 249 249 LYS LYS C . n 
C 2 250 ASN 250 250 250 ASN ASN C . n 
C 2 251 SER 251 251 251 SER SER C . n 
C 2 252 VAL 252 252 252 VAL VAL C . n 
C 2 253 ASN 253 253 253 ASN ASN C . n 
C 2 254 VAL 254 254 254 VAL VAL C . n 
C 2 255 VAL 255 255 255 VAL VAL C . n 
C 2 256 LEU 256 256 256 LEU LEU C . n 
C 2 257 HIS 257 257 257 HIS HIS C . n 
C 2 258 GLY 258 258 258 GLY GLY C . n 
C 2 259 HIS 259 259 259 HIS HIS C . n 
C 2 260 GLU 260 260 260 GLU GLU C . n 
C 2 261 PRO 261 261 261 PRO PRO C . n 
C 2 262 LEU 262 262 262 LEU LEU C . n 
C 2 263 LEU 263 263 263 LEU LEU C . n 
C 2 264 SER 264 264 264 SER SER C . n 
C 2 265 GLU 265 265 265 GLU GLU C . n 
C 2 266 MET 266 266 266 MET MET C . n 
C 2 267 VAL 267 267 267 VAL VAL C . n 
C 2 268 VAL 268 268 268 VAL VAL C . n 
C 2 269 GLU 269 269 269 GLU GLU C . n 
C 2 270 ALA 270 270 270 ALA ALA C . n 
C 2 271 ALA 271 271 271 ALA ALA C . n 
C 2 272 SER 272 272 272 SER SER C . n 
C 2 273 ASP 273 273 273 ASP ASP C . n 
C 2 274 PRO 274 274 274 PRO PRO C . n 
C 2 275 GLU 275 275 275 GLU GLU C . n 
C 2 276 LEU 276 276 276 LEU LEU C . n 
C 2 277 VAL 277 277 277 VAL VAL C . n 
C 2 278 GLU 278 278 278 GLU GLU C . n 
C 2 279 LEU 279 279 279 LEU LEU C . n 
C 2 280 ALA 280 280 280 ALA ALA C . n 
C 2 281 LYS 281 281 281 LYS LYS C . n 
C 2 282 SER 282 282 282 SER SER C . n 
C 2 283 VAL 283 283 283 VAL VAL C . n 
C 2 284 GLY 284 284 284 GLY GLY C . n 
C 2 285 ALA 285 285 285 ALA ALA C . n 
C 2 286 ASP 286 286 286 ASP ASP C . n 
C 2 287 GLY 287 287 287 GLY GLY C . n 
C 2 288 ILE 288 288 288 ILE ILE C . n 
C 2 289 ASN 289 289 289 ASN ASN C . n 
C 2 290 LEU 290 290 290 LEU LEU C . n 
C 2 291 CYS 291 291 291 CYS CYS C . n 
C 2 292 GLY 292 292 292 GLY GLY C . n 
C 2 293 MET 293 293 293 MET MET C . n 
C 2 294 CYS 294 294 294 CYS CYS C . n 
C 2 295 CYS 295 295 295 CYS CYS C . n 
C 2 296 THR 296 296 296 THR THR C . n 
C 2 297 GLY 297 297 297 GLY GLY C . n 
C 2 298 ASN 298 298 298 ASN ASN C . n 
C 2 299 GLU 299 299 299 GLU GLU C . n 
C 2 300 VAL 300 300 300 VAL VAL C . n 
C 2 301 SER 301 301 301 SER SER C . n 
C 2 302 MET 302 302 302 MET MET C . n 
C 2 303 ARG 303 303 303 ARG ARG C . n 
C 2 304 HIS 304 304 304 HIS HIS C . n 
C 2 305 GLY 305 305 305 GLY GLY C . n 
C 2 306 ILE 306 306 306 ILE ILE C . n 
C 2 307 LYS 307 307 307 LYS LYS C . n 
C 2 308 ILE 308 308 308 ILE ILE C . n 
C 2 309 ALA 309 309 309 ALA ALA C . n 
C 2 310 GLY 310 310 310 GLY GLY C . n 
C 2 311 ASN 311 311 311 ASN ASN C . n 
C 2 312 PHE 312 312 312 PHE PHE C . n 
C 2 313 MET 313 313 313 MET MET C . n 
C 2 314 GLN 314 314 314 GLN GLN C . n 
C 2 315 GLN 315 315 315 GLN GLN C . n 
C 2 316 GLU 316 316 316 GLU GLU C . n 
C 2 317 LEU 317 317 317 LEU LEU C . n 
C 2 318 ALA 318 318 318 ALA ALA C . n 
C 2 319 VAL 319 319 319 VAL VAL C . n 
C 2 320 VAL 320 320 320 VAL VAL C . n 
C 2 321 THR 321 321 321 THR THR C . n 
C 2 322 GLY 322 322 322 GLY GLY C . n 
C 2 323 ALA 323 323 323 ALA ALA C . n 
C 2 324 VAL 324 324 324 VAL VAL C . n 
C 2 325 ASP 325 325 325 ASP ASP C . n 
C 2 326 GLY 326 326 326 GLY GLY C . n 
C 2 327 LEU 327 327 327 LEU LEU C . n 
C 2 328 ILE 328 328 328 ILE ILE C . n 
C 2 329 VAL 329 329 329 VAL VAL C . n 
C 2 330 ASP 330 330 330 ASP ASP C . n 
C 2 331 VAL 331 331 331 VAL VAL C . n 
C 2 332 GLN 332 332 332 GLN GLN C . n 
C 2 333 CYS 333 333 333 CYS CYS C . n 
C 2 334 ILE 334 334 334 ILE ILE C . n 
C 2 335 MET 335 335 335 MET MET C . n 
C 2 336 PRO 336 336 336 PRO PRO C . n 
C 2 337 ALA 337 337 337 ALA ALA C . n 
C 2 338 LEU 338 338 338 LEU LEU C . n 
C 2 339 ALA 339 339 339 ALA ALA C . n 
C 2 340 LYS 340 340 340 LYS LYS C . n 
C 2 341 LEU 341 341 341 LEU LEU C . n 
C 2 342 SER 342 342 342 SER SER C . n 
C 2 343 LYS 343 343 343 LYS LYS C . n 
C 2 344 SER 344 344 344 SER SER C . n 
C 2 345 TYR 345 345 345 TYR TYR C . n 
C 2 346 HIS 346 346 346 HIS HIS C . n 
C 2 347 THR 347 347 347 THR THR C . n 
C 2 348 LYS 348 348 348 LYS LYS C . n 
C 2 349 PHE 349 349 349 PHE PHE C . n 
C 2 350 ILE 350 350 350 ILE ILE C . n 
C 2 351 THR 351 351 351 THR THR C . n 
C 2 352 THR 352 352 352 THR THR C . n 
C 2 353 SER 353 353 353 SER SER C . n 
C 2 354 PRO 354 354 354 PRO PRO C . n 
C 2 355 LYS 355 355 355 LYS LYS C . n 
C 2 356 ALA 356 356 356 ALA ALA C . n 
C 2 357 HIS 357 357 357 HIS HIS C . n 
C 2 358 ILE 358 358 358 ILE ILE C . n 
C 2 359 THR 359 359 359 THR THR C . n 
C 2 360 ASP 360 360 360 ASP ASP C . n 
C 2 361 SER 361 361 361 SER SER C . n 
C 2 362 ILE 362 362 362 ILE ILE C . n 
C 2 363 TYR 363 363 363 TYR TYR C . n 
C 2 364 MET 364 364 364 MET MET C . n 
C 2 365 GLU 365 365 365 GLU GLU C . n 
C 2 366 PHE 366 366 366 PHE PHE C . n 
C 2 367 ASP 367 367 367 ASP ASP C . n 
C 2 368 GLU 368 368 368 GLU GLU C . n 
C 2 369 GLU 369 369 369 GLU GLU C . n 
C 2 370 ASN 370 370 370 ASN ASN C . n 
C 2 371 PRO 371 371 371 PRO PRO C . n 
C 2 372 LEU 372 372 372 LEU LEU C . n 
C 2 373 ASP 373 373 373 ASP ASP C . n 
C 2 374 SER 374 374 374 SER SER C . n 
C 2 375 ALA 375 375 375 ALA ALA C . n 
C 2 376 LYS 376 376 376 LYS LYS C . n 
C 2 377 LYS 377 377 377 LYS LYS C . n 
C 2 378 ILE 378 378 378 ILE ILE C . n 
C 2 379 LEU 379 379 379 LEU LEU C . n 
C 2 380 LYS 380 380 380 LYS LYS C . n 
C 2 381 GLU 381 381 381 GLU GLU C . n 
C 2 382 ALA 382 382 382 ALA ALA C . n 
C 2 383 ILE 383 383 383 ILE ILE C . n 
C 2 384 LEU 384 384 384 LEU LEU C . n 
C 2 385 ASN 385 385 385 ASN ASN C . n 
C 2 386 PHE 386 386 386 PHE PHE C . n 
C 2 387 LYS 387 387 387 LYS LYS C . n 
C 2 388 ASN 388 388 388 ASN ASN C . n 
C 2 389 ARG 389 389 389 ARG ARG C . n 
C 2 390 ASP 390 390 390 ASP ASP C . n 
C 2 391 GLN 391 391 391 GLN GLN C . n 
C 2 392 SER 392 392 392 SER SER C . n 
C 2 393 LYS 393 393 393 LYS LYS C . n 
C 2 394 VAL 394 394 394 VAL VAL C . n 
C 2 395 MET 395 395 395 MET MET C . n 
C 2 396 ILE 396 396 396 ILE ILE C . n 
C 2 397 PRO 397 397 397 PRO PRO C . n 
C 2 398 GLU 398 398 398 GLU GLU C . n 
C 2 399 LEU 399 399 399 LEU LEU C . n 
C 2 400 LYS 400 400 400 LYS LYS C . n 
C 2 401 CYS 401 401 401 CYS CYS C . n 
C 2 402 LYS 402 402 402 LYS LYS C . n 
C 2 403 ALA 403 403 403 ALA ALA C . n 
C 2 404 ILE 404 404 404 ILE ILE C . n 
C 2 405 LEU 405 405 405 LEU LEU C . n 
C 2 406 GLY 406 406 406 GLY GLY C . n 
C 2 407 TYR 407 407 407 TYR TYR C . n 
C 2 408 SER 408 408 408 SER SER C . n 
C 2 409 VAL 409 409 409 VAL VAL C . n 
C 2 410 GLU 410 410 410 GLU GLU C . n 
C 2 411 GLU 411 411 411 GLU GLU C . n 
C 2 412 ILE 412 412 412 ILE ILE C . n 
C 2 413 ILE 413 413 413 ILE ILE C . n 
C 2 414 ASN 414 414 414 ASN ASN C . n 
C 2 415 LYS 415 415 415 LYS LYS C . n 
C 2 416 LEU 416 416 416 LEU LEU C . n 
C 2 417 ASP 417 417 417 ASP ASP C . n 
C 2 418 LYS 418 418 418 LYS LYS C . n 
C 2 419 VAL 419 419 419 VAL VAL C . n 
C 2 420 VAL 420 420 420 VAL VAL C . n 
C 2 421 ASN 421 421 421 ASN ASN C . n 
C 2 422 THR 422 422 422 THR THR C . n 
C 2 423 GLN 423 423 423 GLN GLN C . n 
C 2 424 ILE 424 424 424 ILE ILE C . n 
C 2 425 GLY 425 425 425 GLY GLY C . n 
C 2 426 PRO 426 426 426 PRO PRO C . n 
C 2 427 MET 427 427 427 MET MET C . n 
C 2 428 GLN 428 428 428 GLN GLN C . n 
C 2 429 THR 429 429 429 THR THR C . n 
C 2 430 VAL 430 430 430 VAL VAL C . n 
C 2 431 LYS 431 431 431 LYS LYS C . n 
C 2 432 PRO 432 432 432 PRO PRO C . n 
C 2 433 LEU 433 433 433 LEU LEU C . n 
C 2 434 ALA 434 434 434 ALA ALA C . n 
C 2 435 ASP 435 435 435 ASP ASP C . n 
C 2 436 VAL 436 436 436 VAL VAL C . n 
C 2 437 LEU 437 437 437 LEU LEU C . n 
C 2 438 VAL 438 438 438 VAL VAL C . n 
C 2 439 SER 439 439 439 SER SER C . n 
C 2 440 GLY 440 440 440 GLY GLY C . n 
C 2 441 VAL 441 441 441 VAL VAL C . n 
C 2 442 LEU 442 442 442 LEU LEU C . n 
C 2 443 ARG 443 443 443 ARG ARG C . n 
C 2 444 GLY 444 444 444 GLY GLY C . n 
C 2 445 ALA 445 445 445 ALA ALA C . n 
C 2 446 ALA 446 446 446 ALA ALA C . n 
C 2 447 ALA 447 447 447 ALA ALA C . n 
C 2 448 VAL 448 448 448 VAL VAL C . n 
C 2 449 VAL 449 449 449 VAL VAL C . n 
C 2 450 GLY 450 450 450 GLY GLY C . n 
C 2 451 CYS 451 451 451 CYS CYS C . n 
C 2 452 ASN 452 452 452 ASN ASN C . n 
C 2 453 ASN 453 453 453 ASN ASN C . n 
C 2 454 PRO 454 454 454 PRO PRO C . n 
C 2 455 LYS 455 455 455 LYS LYS C . n 
C 2 456 VAL 456 456 456 VAL VAL C . n 
C 2 457 VAL 457 457 457 VAL VAL C . n 
C 2 458 GLN 458 458 458 GLN GLN C . n 
C 2 459 ASP 459 459 459 ASP ASP C . n 
C 2 460 SER 460 460 460 SER SER C . n 
C 2 461 ALA 461 461 461 ALA ALA C . n 
C 2 462 HIS 462 462 462 HIS HIS C . n 
C 2 463 ILE 463 463 463 ILE ILE C . n 
C 2 464 GLU 464 464 464 GLU GLU C . n 
C 2 465 THR 465 465 465 THR THR C . n 
C 2 466 ILE 466 466 466 ILE ILE C . n 
C 2 467 LYS 467 467 467 LYS LYS C . n 
C 2 468 GLY 468 468 468 GLY GLY C . n 
C 2 469 LEU 469 469 469 LEU LEU C . n 
C 2 470 ILE 470 470 470 ILE ILE C . n 
C 2 471 LYS 471 471 471 LYS LYS C . n 
C 2 472 ASN 472 472 472 ASN ASN C . n 
C 2 473 ASP 473 473 473 ASP ASP C . n 
C 2 474 VAL 474 474 474 VAL VAL C . n 
C 2 475 ILE 475 475 475 ILE ILE C . n 
C 2 476 VAL 476 476 476 VAL VAL C . n 
C 2 477 VAL 477 477 477 VAL VAL C . n 
C 2 478 VAL 478 478 478 VAL VAL C . n 
C 2 479 THR 479 479 479 THR THR C . n 
C 2 480 GLY 480 480 480 GLY GLY C . n 
C 2 481 CYS 481 481 481 CYS CYS C . n 
C 2 482 ALA 482 482 482 ALA ALA C . n 
C 2 483 ALA 483 483 483 ALA ALA C . n 
C 2 484 GLN 484 484 484 GLN GLN C . n 
C 2 485 ALA 485 485 485 ALA ALA C . n 
C 2 486 ALA 486 486 486 ALA ALA C . n 
C 2 487 ALA 487 487 487 ALA ALA C . n 
C 2 488 LYS 488 488 488 LYS LYS C . n 
C 2 489 TYR 489 489 489 TYR TYR C . n 
C 2 490 GLY 490 490 490 GLY GLY C . n 
C 2 491 LEU 491 491 491 LEU LEU C . n 
C 2 492 LEU 492 492 492 LEU LEU C . n 
C 2 493 GLN 493 493 493 GLN GLN C . n 
C 2 494 LYS 494 494 494 LYS LYS C . n 
C 2 495 GLU 495 495 495 GLU GLU C . n 
C 2 496 ALA 496 496 496 ALA ALA C . n 
C 2 497 ALA 497 497 497 ALA ALA C . n 
C 2 498 GLU 498 498 498 GLU GLU C . n 
C 2 499 LYS 499 499 499 LYS LYS C . n 
C 2 500 TYR 500 500 500 TYR TYR C . n 
C 2 501 ALA 501 501 501 ALA ALA C . n 
C 2 502 GLY 502 502 502 GLY GLY C . n 
C 2 503 PRO 503 503 503 PRO PRO C . n 
C 2 504 GLY 504 504 504 GLY GLY C . n 
C 2 505 LEU 505 505 505 LEU LEU C . n 
C 2 506 ALA 506 506 506 ALA ALA C . n 
C 2 507 THR 507 507 507 THR THR C . n 
C 2 508 VAL 508 508 508 VAL VAL C . n 
C 2 509 CYS 509 509 509 CYS CYS C . n 
C 2 510 LYS 510 510 510 LYS LYS C . n 
C 2 511 LEU 511 511 511 LEU LEU C . n 
C 2 512 VAL 512 512 512 VAL VAL C . n 
C 2 513 ASP 513 513 513 ASP ASP C . n 
C 2 514 ILE 514 514 514 ILE ILE C . n 
C 2 515 PRO 515 515 515 PRO PRO C . n 
C 2 516 PRO 516 516 516 PRO PRO C . n 
C 2 517 VAL 517 517 517 VAL VAL C . n 
C 2 518 LEU 518 518 518 LEU LEU C . n 
C 2 519 HIS 519 519 519 HIS HIS C . n 
C 2 520 MET 520 520 520 MET MET C . n 
C 2 521 GLY 521 521 521 GLY GLY C . n 
C 2 522 SER 522 522 522 SER SER C . n 
C 2 523 CYS 523 523 523 CYS CYS C . n 
C 2 524 VAL 524 524 524 VAL VAL C . n 
C 2 525 ASP 525 525 525 ASP ASP C . n 
C 2 526 ILE 526 526 526 ILE ILE C . n 
C 2 527 SER 527 527 527 SER SER C . n 
C 2 528 ARG 528 528 528 ARG ARG C . n 
C 2 529 ILE 529 529 529 ILE ILE C . n 
C 2 530 LEU 530 530 530 LEU LEU C . n 
C 2 531 ASP 531 531 531 ASP ASP C . n 
C 2 532 LEU 532 532 532 LEU LEU C . n 
C 2 533 VAL 533 533 533 VAL VAL C . n 
C 2 534 GLY 534 534 534 GLY GLY C . n 
C 2 535 ARG 535 535 535 ARG ARG C . n 
C 2 536 VAL 536 536 536 VAL VAL C . n 
C 2 537 ALA 537 537 537 ALA ALA C . n 
C 2 538 ASN 538 538 538 ASN ASN C . n 
C 2 539 LEU 539 539 539 LEU LEU C . n 
C 2 540 LEU 540 540 540 LEU LEU C . n 
C 2 541 GLY 541 541 541 GLY GLY C . n 
C 2 542 VAL 542 542 542 VAL VAL C . n 
C 2 543 ASP 543 543 543 ASP ASP C . n 
C 2 544 MET 544 544 544 MET MET C . n 
C 2 545 SER 545 545 545 SER SER C . n 
C 2 546 ASP 546 546 546 ASP ASP C . n 
C 2 547 LEU 547 547 547 LEU LEU C . n 
C 2 548 PRO 548 548 548 PRO PRO C . n 
C 2 549 VAL 549 549 549 VAL VAL C . n 
C 2 550 ALA 550 550 550 ALA ALA C . n 
C 2 551 GLY 551 551 551 GLY GLY C . n 
C 2 552 VAL 552 552 552 VAL VAL C . n 
C 2 553 ALA 553 553 553 ALA ALA C . n 
C 2 554 PRO 554 554 554 PRO PRO C . n 
C 2 555 GLU 555 555 555 GLU GLU C . n 
C 2 556 TRP 556 556 556 TRP TRP C . n 
C 2 557 MET 557 557 557 MET MET C . n 
C 2 558 SER 558 558 558 SER SER C . n 
C 2 559 GLU 559 559 559 GLU GLU C . n 
C 2 560 LYS 560 560 560 LYS LYS C . n 
C 2 561 ALA 561 561 561 ALA ALA C . n 
C 2 562 VAL 562 562 562 VAL VAL C . n 
C 2 563 ALA 563 563 563 ALA ALA C . n 
C 2 564 ILE 564 564 564 ILE ILE C . n 
C 2 565 GLY 565 565 565 GLY GLY C . n 
C 2 566 THR 566 566 566 THR THR C . n 
C 2 567 TYR 567 567 567 TYR TYR C . n 
C 2 568 VAL 568 568 568 VAL VAL C . n 
C 2 569 VAL 569 569 569 VAL VAL C . n 
C 2 570 THR 570 570 570 THR THR C . n 
C 2 571 SER 571 571 571 SER SER C . n 
C 2 572 GLY 572 572 572 GLY GLY C . n 
C 2 573 ILE 573 573 573 ILE ILE C . n 
C 2 574 ASP 574 574 574 ASP ASP C . n 
C 2 575 THR 575 575 575 THR THR C . n 
C 2 576 TRP 576 576 576 TRP TRP C . n 
C 2 577 LEU 577 577 577 LEU LEU C . n 
C 2 578 GLY 578 578 578 GLY GLY C . n 
C 2 579 VAL 579 579 579 VAL VAL C . n 
C 2 580 ALA 580 580 580 ALA ALA C . n 
C 2 581 PRO 581 581 581 PRO PRO C . n 
C 2 582 PRO 582 582 582 PRO PRO C . n 
C 2 583 VAL 583 583 583 VAL VAL C . n 
C 2 584 THR 584 584 584 THR THR C . n 
C 2 585 GLY 585 585 585 GLY GLY C . n 
C 2 586 GLY 586 586 586 GLY GLY C . n 
C 2 587 PRO 587 587 587 PRO PRO C . n 
C 2 588 GLU 588 588 588 GLU GLU C . n 
C 2 589 VAL 589 589 589 VAL VAL C . n 
C 2 590 VAL 590 590 590 VAL VAL C . n 
C 2 591 ASP 591 591 591 ASP ASP C . n 
C 2 592 ILE 592 592 592 ILE ILE C . n 
C 2 593 LEU 593 593 593 LEU LEU C . n 
C 2 594 THR 594 594 594 THR THR C . n 
C 2 595 ASN 595 595 595 ASN ASN C . n 
C 2 596 LYS 596 596 596 LYS LYS C . n 
C 2 597 MET 597 597 597 MET MET C . n 
C 2 598 GLU 598 598 598 GLU GLU C . n 
C 2 599 ASP 599 599 599 ASP ASP C . n 
C 2 600 TRP 600 600 600 TRP TRP C . n 
C 2 601 VAL 601 601 601 VAL VAL C . n 
C 2 602 GLY 602 602 602 GLY GLY C . n 
C 2 603 ALA 603 603 603 ALA ALA C . n 
C 2 604 LYS 604 604 604 LYS LYS C . n 
C 2 605 PHE 605 605 605 PHE PHE C . n 
C 2 606 PHE 606 606 606 PHE PHE C . n 
C 2 607 ILE 607 607 607 ILE ILE C . n 
C 2 608 GLU 608 608 608 GLU GLU C . n 
C 2 609 THR 609 609 609 THR THR C . n 
C 2 610 ASP 610 610 610 ASP ASP C . n 
C 2 611 PRO 611 611 611 PRO PRO C . n 
C 2 612 HIS 612 612 612 HIS HIS C . n 
C 2 613 LYS 613 613 613 LYS LYS C . n 
C 2 614 ALA 614 614 614 ALA ALA C . n 
C 2 615 VAL 615 615 615 VAL VAL C . n 
C 2 616 GLU 616 616 616 GLU GLU C . n 
C 2 617 GLN 617 617 617 GLN GLN C . n 
C 2 618 ILE 618 618 618 ILE ILE C . n 
C 2 619 VAL 619 619 619 VAL VAL C . n 
C 2 620 ASN 620 620 620 ASN ASN C . n 
C 2 621 ARG 621 621 621 ARG ARG C . n 
C 2 622 MET 622 622 622 MET MET C . n 
C 2 623 ASN 623 623 623 ASN ASN C . n 
C 2 624 GLU 624 624 624 GLU GLU C . n 
C 2 625 LYS 625 625 625 LYS LYS C . n 
C 2 626 ARG 626 626 626 ARG ARG C . n 
C 2 627 LYS 627 627 627 LYS LYS C . n 
C 2 628 LYS 628 628 628 LYS LYS C . n 
C 2 629 LEU 629 629 629 LEU LEU C . n 
C 2 630 GLY 630 630 630 GLY GLY C . n 
C 2 631 ILE 631 631 631 ILE ILE C . n 
D 1 1   MET 1   1   1   MET MET D . n 
D 1 2   ASN 2   2   2   ASN ASN D . n 
D 1 3   LEU 3   3   3   LEU LEU D . n 
D 1 4   PHE 4   4   4   PHE PHE D . n 
D 1 5   GLN 5   5   5   GLN GLN D . n 
D 1 6   THR 6   6   6   THR THR D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   PHE 8   8   8   PHE PHE D . n 
D 1 9   THR 9   9   9   THR THR D . n 
D 1 10  GLY 10  10  10  GLY GLY D . n 
D 1 11  SER 11  11  11  SER SER D . n 
D 1 12  LYS 12  12  12  LYS LYS D . n 
D 1 13  GLN 13  13  13  GLN GLN D . n 
D 1 14  ALA 14  14  14  ALA ALA D . n 
D 1 15  LEU 15  15  15  LEU LEU D . n 
D 1 16  ALA 16  16  16  ALA ALA D . n 
D 1 17  ALA 17  17  17  ALA ALA D . n 
D 1 18  ALA 18  18  18  ALA ALA D . n 
D 1 19  GLU 19  19  19  GLU GLU D . n 
D 1 20  GLY 20  20  20  GLY GLY D . n 
D 1 21  ILE 21  21  21  ILE ILE D . n 
D 1 22  VAL 22  22  22  VAL VAL D . n 
D 1 23  LYS 23  23  23  LYS LYS D . n 
D 1 24  GLN 24  24  24  GLN GLN D . n 
D 1 25  ALA 25  25  25  ALA ALA D . n 
D 1 26  VAL 26  26  26  VAL VAL D . n 
D 1 27  ASP 27  27  27  ASP ASP D . n 
D 1 28  GLU 28  28  28  GLU GLU D . n 
D 1 29  LYS 29  29  29  LYS LYS D . n 
D 1 30  GLY 30  30  30  GLY GLY D . n 
D 1 31  ARG 31  31  31  ARG ARG D . n 
D 1 32  ASP 32  32  32  ASP ASP D . n 
D 1 33  TYR 33  33  33  TYR TYR D . n 
D 1 34  LYS 34  34  34  LYS LYS D . n 
D 1 35  VAL 35  35  35  VAL VAL D . n 
D 1 36  ALA 36  36  36  ALA ALA D . n 
D 1 37  PHE 37  37  37  PHE PHE D . n 
D 1 38  PRO 38  38  38  PRO PRO D . n 
D 1 39  ASP 39  39  39  ASP ASP D . n 
D 1 40  THR 40  40  40  THR THR D . n 
D 1 41  ALA 41  41  41  ALA ALA D . n 
D 1 42  TYR 42  42  42  TYR TYR D . n 
D 1 43  SER 43  43  43  SER SER D . n 
D 1 44  LEU 44  44  44  LEU LEU D . n 
D 1 45  PRO 45  45  45  PRO PRO D . n 
D 1 46  VAL 46  46  46  VAL VAL D . n 
D 1 47  ILE 47  47  47  ILE ILE D . n 
D 1 48  PHE 48  48  48  PHE PHE D . n 
D 1 49  ALA 49  49  49  ALA ALA D . n 
D 1 50  ALA 50  50  50  ALA ALA D . n 
D 1 51  THR 51  51  51  THR THR D . n 
D 1 52  GLY 52  52  52  GLY GLY D . n 
D 1 53  LYS 53  53  53  LYS LYS D . n 
D 1 54  LYS 54  54  54  LYS LYS D . n 
D 1 55  ILE 55  55  55  ILE ILE D . n 
D 1 56  THR 56  56  56  THR THR D . n 
D 1 57  ASN 57  57  57  ASN ASN D . n 
D 1 58  VAL 58  58  58  VAL VAL D . n 
D 1 59  GLY 59  59  59  GLY GLY D . n 
D 1 60  GLU 60  60  60  GLU GLU D . n 
D 1 61  LEU 61  61  61  LEU LEU D . n 
D 1 62  GLU 62  62  62  GLU GLU D . n 
D 1 63  GLY 63  63  63  GLY GLY D . n 
D 1 64  ALA 64  64  64  ALA ALA D . n 
D 1 65  LEU 65  65  65  LEU LEU D . n 
D 1 66  ASP 66  66  66  ASP ASP D . n 
D 1 67  ILE 67  67  67  ILE ILE D . n 
D 1 68  VAL 68  68  68  VAL VAL D . n 
D 1 69  ARG 69  69  69  ARG ARG D . n 
D 1 70  SER 70  70  70  SER SER D . n 
D 1 71  LEU 71  71  71  LEU LEU D . n 
D 1 72  ILE 72  72  72  ILE ILE D . n 
D 1 73  VAL 73  73  73  VAL VAL D . n 
D 1 74  GLU 74  74  74  GLU GLU D . n 
D 1 75  GLU 75  75  75  GLU GLU D . n 
D 1 76  GLU 76  76  76  GLU GLU D . n 
D 1 77  MET 77  77  77  MET MET D . n 
D 1 78  LEU 78  78  78  LEU LEU D . n 
D 1 79  ASP 79  79  79  ASP ASP D . n 
D 1 80  LYS 80  80  80  LYS LYS D . n 
D 1 81  LEU 81  81  81  LEU LEU D . n 
D 1 82  LEU 82  82  82  LEU LEU D . n 
D 1 83  ASN 83  83  83  ASN ASN D . n 
D 1 84  SER 84  84  84  SER SER D . n 
D 1 85  GLY 85  85  85  GLY GLY D . n 
D 1 86  LEU 86  86  86  LEU LEU D . n 
D 1 87  ALA 87  87  87  ALA ALA D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  ALA 89  89  89  ALA ALA D . n 
D 1 90  VAL 90  90  90  VAL VAL D . n 
D 1 91  ALA 91  91  91  ALA ALA D . n 
D 1 92  ALA 92  92  92  ALA ALA D . n 
D 1 93  GLU 93  93  93  GLU GLU D . n 
D 1 94  ILE 94  94  94  ILE ILE D . n 
D 1 95  ILE 95  95  95  ILE ILE D . n 
D 1 96  GLU 96  96  96  GLU GLU D . n 
D 1 97  ALA 97  97  97  ALA ALA D . n 
D 1 98  ALA 98  98  98  ALA ALA D . n 
D 1 99  LYS 99  99  99  LYS LYS D . n 
D 1 100 TYR 100 100 100 TYR TYR D . n 
D 1 101 VAL 101 101 101 VAL VAL D . n 
D 1 102 LEU 102 102 102 LEU LEU D . n 
D 1 103 SER 103 103 103 SER SER D . n 
D 1 104 ASP 104 104 104 ASP ASP D . n 
D 1 105 ALA 105 105 105 ALA ALA D . n 
D 1 106 PRO 106 106 106 PRO PRO D . n 
D 1 107 TYR 107 107 107 TYR TYR D . n 
D 1 108 ALA 108 108 108 ALA ALA D . n 
D 1 109 GLU 109 109 109 GLU GLU D . n 
D 1 110 PRO 110 110 110 PRO PRO D . n 
D 1 111 CYS 111 111 111 CYS CYS D . n 
D 1 112 VAL 112 112 112 VAL VAL D . n 
D 1 113 GLY 113 113 113 GLY GLY D . n 
D 1 114 PHE 114 114 114 PHE PHE D . n 
D 1 115 ILE 115 115 115 ILE ILE D . n 
D 1 116 SER 116 116 116 SER SER D . n 
D 1 117 ASP 117 117 117 ASP ASP D . n 
D 1 118 PRO 118 118 118 PRO PRO D . n 
D 1 119 ILE 119 119 119 ILE ILE D . n 
D 1 120 ILE 120 120 120 ILE ILE D . n 
D 1 121 ARG 121 121 121 ARG ARG D . n 
D 1 122 SER 122 122 122 SER SER D . n 
D 1 123 LEU 123 123 123 LEU LEU D . n 
D 1 124 GLY 124 124 124 GLY GLY D . n 
D 1 125 VAL 125 125 125 VAL VAL D . n 
D 1 126 PRO 126 126 126 PRO PRO D . n 
D 1 127 LEU 127 127 127 LEU LEU D . n 
D 1 128 VAL 128 128 128 VAL VAL D . n 
D 1 129 THR 129 129 129 THR THR D . n 
D 1 130 GLY 130 130 130 GLY GLY D . n 
D 1 131 ASP 131 131 131 ASP ASP D . n 
D 1 132 ILE 132 132 132 ILE ILE D . n 
D 1 133 PRO 133 133 133 PRO PRO D . n 
D 1 134 GLY 134 134 134 GLY GLY D . n 
D 1 135 VAL 135 135 135 VAL VAL D . n 
D 1 136 ALA 136 136 136 ALA ALA D . n 
D 1 137 VAL 137 137 137 VAL VAL D . n 
D 1 138 ILE 138 138 138 ILE ILE D . n 
D 1 139 LEU 139 139 139 LEU LEU D . n 
D 1 140 GLY 140 140 140 GLY GLY D . n 
D 1 141 GLU 141 141 141 GLU GLU D . n 
D 1 142 CYS 142 142 142 CYS CYS D . n 
D 1 143 PRO 143 143 143 PRO PRO D . n 
D 1 144 ASP 144 144 144 ASP ASP D . n 
D 1 145 SER 145 145 145 SER SER D . n 
D 1 146 GLU 146 146 146 GLU GLU D . n 
D 1 147 THR 147 147 147 THR THR D . n 
D 1 148 ALA 148 148 148 ALA ALA D . n 
D 1 149 ALA 149 149 149 ALA ALA D . n 
D 1 150 LYS 150 150 150 LYS LYS D . n 
D 1 151 ILE 151 151 151 ILE ILE D . n 
D 1 152 ILE 152 152 152 ILE ILE D . n 
D 1 153 LYS 153 153 153 LYS LYS D . n 
D 1 154 ASP 154 154 154 ASP ASP D . n 
D 1 155 TYR 155 155 155 TYR TYR D . n 
D 1 156 GLN 156 156 156 GLN GLN D . n 
D 1 157 SER 157 157 157 SER SER D . n 
D 1 158 LYS 158 158 158 LYS LYS D . n 
D 1 159 GLY 159 159 159 GLY GLY D . n 
D 1 160 LEU 160 160 160 LEU LEU D . n 
D 1 161 LEU 161 161 161 LEU LEU D . n 
D 1 162 THR 162 162 162 THR THR D . n 
D 1 163 CYS 163 163 163 CYS CYS D . n 
D 1 164 LEU 164 164 164 LEU LEU D . n 
D 1 165 VAL 165 165 165 VAL VAL D . n 
D 1 166 GLY 166 166 166 GLY GLY D . n 
D 1 167 LYS 167 167 167 LYS LYS D . n 
D 1 168 VAL 168 168 168 VAL VAL D . n 
D 1 169 ILE 169 169 169 ILE ILE D . n 
D 1 170 ASP 170 170 170 ASP ASP D . n 
D 1 171 GLN 171 171 171 GLN GLN D . n 
D 1 172 ALA 172 172 172 ALA ALA D . n 
D 1 173 ILE 173 173 173 ILE ILE D . n 
D 1 174 GLU 174 174 174 GLU GLU D . n 
D 1 175 GLY 175 175 175 GLY GLY D . n 
D 1 176 LYS 176 176 176 LYS LYS D . n 
D 1 177 VAL 177 177 177 VAL VAL D . n 
D 1 178 LYS 178 178 178 LYS LYS D . n 
D 1 179 MET 179 179 179 MET MET D . n 
D 1 180 GLY 180 180 180 GLY GLY D . n 
D 1 181 LEU 181 181 181 LEU LEU D . n 
D 1 182 ASP 182 182 182 ASP ASP D . n 
D 1 183 LEU 183 183 183 LEU LEU D . n 
D 1 184 ARG 184 184 184 ARG ARG D . n 
D 1 185 VAL 185 185 185 VAL VAL D . n 
D 1 186 ILE 186 186 186 ILE ILE D . n 
D 1 187 PRO 187 187 187 PRO PRO D . n 
D 1 188 LEU 188 188 188 LEU LEU D . n 
D 1 189 GLY 189 189 189 GLY GLY D . n 
D 1 190 TYR 190 190 190 TYR TYR D . n 
D 1 191 ASP 191 191 191 ASP ASP D . n 
D 1 192 VAL 192 192 192 VAL VAL D . n 
D 1 193 THR 193 193 193 THR THR D . n 
D 1 194 SER 194 194 194 SER SER D . n 
D 1 195 VAL 195 195 195 VAL VAL D . n 
D 1 196 ILE 196 196 196 ILE ILE D . n 
D 1 197 HIS 197 197 197 HIS HIS D . n 
D 1 198 VAL 198 198 198 VAL VAL D . n 
D 1 199 VAL 199 199 199 VAL VAL D . n 
D 1 200 THR 200 200 200 THR THR D . n 
D 1 201 ILE 201 201 201 ILE ILE D . n 
D 1 202 ALA 202 202 202 ALA ALA D . n 
D 1 203 ILE 203 203 203 ILE ILE D . n 
D 1 204 ARG 204 204 204 ARG ARG D . n 
D 1 205 ALA 205 205 205 ALA ALA D . n 
D 1 206 ALA 206 206 206 ALA ALA D . n 
D 1 207 LEU 207 207 207 LEU LEU D . n 
D 1 208 ILE 208 208 208 ILE ILE D . n 
D 1 209 PHE 209 209 209 PHE PHE D . n 
D 1 210 GLY 210 210 210 GLY GLY D . n 
D 1 211 GLY 211 211 211 GLY GLY D . n 
D 1 212 ILE 212 212 212 ILE ILE D . n 
D 1 213 LYS 213 213 213 LYS LYS D . n 
D 1 214 GLY 214 214 214 GLY GLY D . n 
D 1 215 GLY 215 215 215 GLY GLY D . n 
D 1 216 GLN 216 216 216 GLN GLN D . n 
D 1 217 LEU 217 217 217 LEU LEU D . n 
D 1 218 ASN 218 218 218 ASN ASN D . n 
D 1 219 ASP 219 219 219 ASP ASP D . n 
D 1 220 ILE 220 220 220 ILE ILE D . n 
D 1 221 LEU 221 221 221 LEU LEU D . n 
D 1 222 LYS 222 222 222 LYS LYS D . n 
D 1 223 TYR 223 223 223 TYR TYR D . n 
D 1 224 THR 224 224 224 THR THR D . n 
D 1 225 ALA 225 225 225 ALA ALA D . n 
D 1 226 GLU 226 226 226 GLU GLU D . n 
D 1 227 ARG 227 227 227 ARG ARG D . n 
D 1 228 VAL 228 228 228 VAL VAL D . n 
D 1 229 PRO 229 229 229 PRO PRO D . n 
D 1 230 ALA 230 230 230 ALA ALA D . n 
D 1 231 PHE 231 231 231 PHE PHE D . n 
D 1 232 VAL 232 232 232 VAL VAL D . n 
D 1 233 ASN 233 233 233 ASN ASN D . n 
D 1 234 ALA 234 234 234 ALA ALA D . n 
D 1 235 PHE 235 235 235 PHE PHE D . n 
D 1 236 GLY 236 236 236 GLY GLY D . n 
D 1 237 PRO 237 237 237 PRO PRO D . n 
D 1 238 LEU 238 238 238 LEU LEU D . n 
D 1 239 SER 239 239 239 SER SER D . n 
D 1 240 GLU 240 240 240 GLU GLU D . n 
D 1 241 LEU 241 241 241 LEU LEU D . n 
D 1 242 VAL 242 242 242 VAL VAL D . n 
D 1 243 VAL 243 243 243 VAL VAL D . n 
D 1 244 SER 244 244 244 SER SER D . n 
D 1 245 ALA 245 245 245 ALA ALA D . n 
D 1 246 GLY 246 246 246 GLY GLY D . n 
D 1 247 ALA 247 247 247 ALA ALA D . n 
D 1 248 GLY 248 248 248 GLY GLY D . n 
D 1 249 ALA 249 249 249 ALA ALA D . n 
D 1 250 ILE 250 250 250 ILE ILE D . n 
D 1 251 ALA 251 251 251 ALA ALA D . n 
D 1 252 LEU 252 252 252 LEU LEU D . n 
D 1 253 GLY 253 253 253 GLY GLY D . n 
D 1 254 PHE 254 254 254 PHE PHE D . n 
D 1 255 PRO 255 255 255 PRO PRO D . n 
D 1 256 VAL 256 256 256 VAL VAL D . n 
D 1 257 LEU 257 257 257 LEU LEU D . n 
D 1 258 THR 258 258 258 THR THR D . n 
D 1 259 ASP 259 259 259 ASP ASP D . n 
D 1 260 GLN 260 260 260 GLN GLN D . n 
D 1 261 VAL 261 261 261 VAL VAL D . n 
D 1 262 VAL 262 262 262 VAL VAL D . n 
D 1 263 PRO 263 263 263 PRO PRO D . n 
D 1 264 GLU 264 264 264 GLU GLU D . n 
D 1 265 VAL 265 265 265 VAL VAL D . n 
D 1 266 PRO 266 266 266 PRO PRO D . n 
D 1 267 THR 267 267 267 THR THR D . n 
D 1 268 LEU 268 268 268 LEU LEU D . n 
D 1 269 LEU 269 269 269 LEU LEU D . n 
D 1 270 LEU 270 270 270 LEU LEU D . n 
D 1 271 THR 271 271 271 THR THR D . n 
D 1 272 GLN 272 272 272 GLN GLN D . n 
D 1 273 LYS 273 273 273 LYS LYS D . n 
D 1 274 ASP 274 274 274 ASP ASP D . n 
D 1 275 TYR 275 275 275 TYR TYR D . n 
D 1 276 ASP 276 276 276 ASP ASP D . n 
D 1 277 LYS 277 277 277 LYS LYS D . n 
D 1 278 MET 278 278 278 MET MET D . n 
D 1 279 VAL 279 279 279 VAL VAL D . n 
D 1 280 LYS 280 280 280 LYS LYS D . n 
D 1 281 THR 281 281 281 THR THR D . n 
D 1 282 SER 282 282 282 SER SER D . n 
D 1 283 LEU 283 283 283 LEU LEU D . n 
D 1 284 GLU 284 284 284 GLU GLU D . n 
D 1 285 ALA 285 285 285 ALA ALA D . n 
D 1 286 ARG 286 286 286 ARG ARG D . n 
D 1 287 ASN 287 287 287 ASN ASN D . n 
D 1 288 ILE 288 288 288 ILE ILE D . n 
D 1 289 LYS 289 289 289 LYS LYS D . n 
D 1 290 ILE 290 290 290 ILE ILE D . n 
D 1 291 LYS 291 291 291 LYS LYS D . n 
D 1 292 ILE 292 292 292 ILE ILE D . n 
D 1 293 THR 293 293 293 THR THR D . n 
D 1 294 GLU 294 294 294 GLU GLU D . n 
D 1 295 ILE 295 295 295 ILE ILE D . n 
D 1 296 PRO 296 296 296 PRO PRO D . n 
D 1 297 ILE 297 297 297 ILE ILE D . n 
D 1 298 PRO 298 298 298 PRO PRO D . n 
D 1 299 VAL 299 299 299 VAL VAL D . n 
D 1 300 SER 300 300 300 SER SER D . n 
D 1 301 PHE 301 301 301 PHE PHE D . n 
D 1 302 ALA 302 302 302 ALA ALA D . n 
D 1 303 ALA 303 303 303 ALA ALA D . n 
D 1 304 ALA 304 304 304 ALA ALA D . n 
D 1 305 PHE 305 305 305 PHE PHE D . n 
D 1 306 GLU 306 306 306 GLU GLU D . n 
D 1 307 GLY 307 307 307 GLY GLY D . n 
D 1 308 GLU 308 308 308 GLU GLU D . n 
D 1 309 ARG 309 309 309 ARG ARG D . n 
D 1 310 ILE 310 310 310 ILE ILE D . n 
D 1 311 ARG 311 311 311 ARG ARG D . n 
D 1 312 LYS 312 312 312 LYS LYS D . n 
D 1 313 ASN 313 313 313 ASN ASN D . n 
D 1 314 ASP 314 314 314 ASP ASP D . n 
D 1 315 MET 315 315 315 MET MET D . n 
D 1 316 LEU 316 316 316 LEU LEU D . n 
D 1 317 ALA 317 317 317 ALA ALA D . n 
D 1 318 GLU 318 318 318 GLU GLU D . n 
D 1 319 PHE 319 319 319 PHE PHE D . n 
D 1 320 GLY 320 320 320 GLY GLY D . n 
D 1 321 GLY 321 321 321 GLY GLY D . n 
D 1 322 ASN 322 322 322 ASN ASN D . n 
D 1 323 LYS 323 323 323 LYS LYS D . n 
D 1 324 THR 324 324 324 THR THR D . n 
D 1 325 LYS 325 325 325 LYS LYS D . n 
D 1 326 ALA 326 326 326 ALA ALA D . n 
D 1 327 TRP 327 327 327 TRP TRP D . n 
D 1 328 GLU 328 328 328 GLU GLU D . n 
D 1 329 LEU 329 329 329 LEU LEU D . n 
D 1 330 VAL 330 330 330 VAL VAL D . n 
D 1 331 MET 331 331 331 MET MET D . n 
D 1 332 CYS 332 332 332 CYS CYS D . n 
D 1 333 ALA 333 333 333 ALA ALA D . n 
D 1 334 ASP 334 334 334 ASP ASP D . n 
D 1 335 GLN 335 335 335 GLN GLN D . n 
D 1 336 GLY 336 336 336 GLY GLY D . n 
D 1 337 GLU 337 337 337 GLU GLU D . n 
D 1 338 VAL 338 338 338 VAL VAL D . n 
D 1 339 GLU 339 339 339 GLU GLU D . n 
D 1 340 ASP 340 340 340 ASP ASP D . n 
D 1 341 HIS 341 341 341 HIS HIS D . n 
D 1 342 LYS 342 342 342 LYS LYS D . n 
D 1 343 ILE 343 343 343 ILE ILE D . n 
D 1 344 GLU 344 344 344 GLU GLU D . n 
D 1 345 VAL 345 345 345 VAL VAL D . n 
D 1 346 ILE 346 346 346 ILE ILE D . n 
D 1 347 GLY 347 347 347 GLY GLY D . n 
D 1 348 PRO 348 348 348 PRO PRO D . n 
D 1 349 ASP 349 349 349 ASP ASP D . n 
D 1 350 ILE 350 350 350 ILE ILE D . n 
D 1 351 ASP 351 351 351 ASP ASP D . n 
D 1 352 THR 352 352 352 THR THR D . n 
D 1 353 ILE 353 353 353 ILE ILE D . n 
D 1 354 ASP 354 354 354 ASP ASP D . n 
D 1 355 LYS 355 355 355 LYS LYS D . n 
D 1 356 ALA 356 356 356 ALA ALA D . n 
D 1 357 PRO 357 357 357 PRO PRO D . n 
D 1 358 GLY 358 358 358 GLY GLY D . n 
D 1 359 ARG 359 359 359 ARG ARG D . n 
D 1 360 MET 360 360 360 MET MET D . n 
D 1 361 PRO 361 361 361 PRO PRO D . n 
D 1 362 LEU 362 362 362 LEU LEU D . n 
D 1 363 GLY 363 363 363 GLY GLY D . n 
D 1 364 MET 364 364 364 MET MET D . n 
D 1 365 LEU 365 365 365 LEU LEU D . n 
D 1 366 ILE 366 366 366 ILE ILE D . n 
D 1 367 LYS 367 367 367 LYS LYS D . n 
D 1 368 VAL 368 368 368 VAL VAL D . n 
D 1 369 SER 369 369 369 SER SER D . n 
D 1 370 GLY 370 370 370 GLY GLY D . n 
D 1 371 THR 371 371 371 THR THR D . n 
D 1 372 ASN 372 372 372 ASN ASN D . n 
D 1 373 MET 373 373 373 MET MET D . n 
D 1 374 GLN 374 374 374 GLN GLN D . n 
D 1 375 LYS 375 375 375 LYS LYS D . n 
D 1 376 ASP 376 376 376 ASP ASP D . n 
D 1 377 PHE 377 377 377 PHE PHE D . n 
D 1 378 GLU 378 378 378 GLU GLU D . n 
D 1 379 PRO 379 379 379 PRO PRO D . n 
D 1 380 VAL 380 380 380 VAL VAL D . n 
D 1 381 LEU 381 381 381 LEU LEU D . n 
D 1 382 GLU 382 382 382 GLU GLU D . n 
D 1 383 ARG 383 383 383 ARG ARG D . n 
D 1 384 ARG 384 384 384 ARG ARG D . n 
D 1 385 LEU 385 385 385 LEU LEU D . n 
D 1 386 HIS 386 386 386 HIS HIS D . n 
D 1 387 TYR 387 387 387 TYR TYR D . n 
D 1 388 PHE 388 388 388 PHE PHE D . n 
D 1 389 LEU 389 389 389 LEU LEU D . n 
D 1 390 ASN 390 390 390 ASN ASN D . n 
D 1 391 TYR 391 391 391 TYR TYR D . n 
D 1 392 ILE 392 392 392 ILE ILE D . n 
D 1 393 GLU 393 393 393 GLU GLU D . n 
D 1 394 GLY 394 394 394 GLY GLY D . n 
D 1 395 VAL 395 395 395 VAL VAL D . n 
D 1 396 MET 396 396 396 MET MET D . n 
D 1 397 HIS 397 397 397 HIS HIS D . n 
D 1 398 VAL 398 398 398 VAL VAL D . n 
D 1 399 GLY 399 399 399 GLY GLY D . n 
D 1 400 GLN 400 400 400 GLN GLN D . n 
D 1 401 ARG 401 401 401 ARG ARG D . n 
D 1 402 ASN 402 402 402 ASN ASN D . n 
D 1 403 LEU 403 403 403 LEU LEU D . n 
D 1 404 THR 404 404 404 THR THR D . n 
D 1 405 TRP 405 405 405 TRP TRP D . n 
D 1 406 VAL 406 406 406 VAL VAL D . n 
D 1 407 ARG 407 407 407 ARG ARG D . n 
D 1 408 ILE 408 408 408 ILE ILE D . n 
D 1 409 GLY 409 409 409 GLY GLY D . n 
D 1 410 LYS 410 410 410 LYS LYS D . n 
D 1 411 GLU 411 411 411 GLU GLU D . n 
D 1 412 ALA 412 412 412 ALA ALA D . n 
D 1 413 PHE 413 413 413 PHE PHE D . n 
D 1 414 GLU 414 414 414 GLU GLU D . n 
D 1 415 LYS 415 415 415 LYS LYS D . n 
D 1 416 GLY 416 416 416 GLY GLY D . n 
D 1 417 PHE 417 417 417 PHE PHE D . n 
D 1 418 ARG 418 418 418 ARG ARG D . n 
D 1 419 LEU 419 419 419 LEU LEU D . n 
D 1 420 LYS 420 420 420 LYS LYS D . n 
D 1 421 HIS 421 421 421 HIS HIS D . n 
D 1 422 PHE 422 422 422 PHE PHE D . n 
D 1 423 GLY 423 423 423 GLY GLY D . n 
D 1 424 GLU 424 424 424 GLU GLU D . n 
D 1 425 VAL 425 425 425 VAL VAL D . n 
D 1 426 ILE 426 426 426 ILE ILE D . n 
D 1 427 TYR 427 427 427 TYR TYR D . n 
D 1 428 ALA 428 428 428 ALA ALA D . n 
D 1 429 LYS 429 429 429 LYS LYS D . n 
D 1 430 MET 430 430 430 MET MET D . n 
D 1 431 LEU 431 431 431 LEU LEU D . n 
D 1 432 ASP 432 432 432 ASP ASP D . n 
D 1 433 GLU 433 433 433 GLU GLU D . n 
D 1 434 PHE 434 434 434 PHE PHE D . n 
D 1 435 GLY 435 435 435 GLY GLY D . n 
D 1 436 SER 436 436 436 SER SER D . n 
D 1 437 VAL 437 437 437 VAL VAL D . n 
D 1 438 VAL 438 438 438 VAL VAL D . n 
D 1 439 ASP 439 439 439 ASP ASP D . n 
D 1 440 LYS 440 440 440 LYS LYS D . n 
D 1 441 CYS 441 441 441 CYS CYS D . n 
D 1 442 GLU 442 442 442 GLU GLU D . n 
D 1 443 VAL 443 443 443 VAL VAL D . n 
D 1 444 THR 444 444 444 THR THR D . n 
D 1 445 ILE 445 445 445 ILE ILE D . n 
D 1 446 ILE 446 446 446 ILE ILE D . n 
D 1 447 THR 447 447 447 THR THR D . n 
D 1 448 ASP 448 448 448 ASP ASP D . n 
D 1 449 PRO 449 449 449 PRO PRO D . n 
D 1 450 GLY 450 450 450 GLY GLY D . n 
D 1 451 LYS 451 451 451 LYS LYS D . n 
D 1 452 ALA 452 452 452 ALA ALA D . n 
D 1 453 GLU 453 453 453 GLU GLU D . n 
D 1 454 GLU 454 454 454 GLU GLU D . n 
D 1 455 LEU 455 455 455 LEU LEU D . n 
D 1 456 GLU 456 456 456 GLU GLU D . n 
D 1 457 GLY 457 457 457 GLY GLY D . n 
D 1 458 LYS 458 458 458 LYS LYS D . n 
D 1 459 TYR 459 459 459 TYR TYR D . n 
D 1 460 ALA 460 460 460 ALA ALA D . n 
D 1 461 VAL 461 461 461 VAL VAL D . n 
D 1 462 PRO 462 462 462 PRO PRO D . n 
D 1 463 ARG 463 463 463 ARG ARG D . n 
D 1 464 TYR 464 464 464 TYR TYR D . n 
D 1 465 LYS 465 465 465 LYS LYS D . n 
D 1 466 GLU 466 466 466 GLU GLU D . n 
D 1 467 ARG 467 467 467 ARG ARG D . n 
D 1 468 ASP 468 468 468 ASP ASP D . n 
D 1 469 ALA 469 469 469 ALA ALA D . n 
D 1 470 ARG 470 470 470 ARG ARG D . n 
D 1 471 LEU 471 471 471 LEU LEU D . n 
D 1 472 GLU 472 472 472 GLU GLU D . n 
D 1 473 SER 473 473 473 SER SER D . n 
D 1 474 LEU 474 474 474 LEU LEU D . n 
D 1 475 VAL 475 475 475 VAL VAL D . n 
D 1 476 ASP 476 476 476 ASP ASP D . n 
D 1 477 GLU 477 477 477 GLU GLU D . n 
D 1 478 LYS 478 478 478 LYS LYS D . n 
D 1 479 VAL 479 479 479 VAL VAL D . n 
D 1 480 ASP 480 480 480 ASP ASP D . n 
D 1 481 THR 481 481 481 THR THR D . n 
D 1 482 PHE 482 482 482 PHE PHE D . n 
D 1 483 TYR 483 483 483 TYR TYR D . n 
D 1 484 SER 484 484 484 SER SER D . n 
D 1 485 CYS 485 485 485 CYS CYS D . n 
D 1 486 ASN 486 486 486 ASN ASN D . n 
D 1 487 LEU 487 487 487 LEU LEU D . n 
D 1 488 CYS 488 488 488 CYS CYS D . n 
D 1 489 GLN 489 489 489 GLN GLN D . n 
D 1 490 SER 490 490 490 SER SER D . n 
D 1 491 PHE 491 491 491 PHE PHE D . n 
D 1 492 ALA 492 492 492 ALA ALA D . n 
D 1 493 PRO 493 493 493 PRO PRO D . n 
D 1 494 ALA 494 494 494 ALA ALA D . n 
D 1 495 HIS 495 495 495 HIS HIS D . n 
D 1 496 VAL 496 496 496 VAL VAL D . n 
D 1 497 CYS 497 497 497 CYS CYS D . n 
D 1 498 ILE 498 498 498 ILE ILE D . n 
D 1 499 VAL 499 499 499 VAL VAL D . n 
D 1 500 THR 500 500 500 THR THR D . n 
D 1 501 PRO 501 501 501 PRO PRO D . n 
D 1 502 GLU 502 502 502 GLU GLU D . n 
D 1 503 ARG 503 503 503 ARG ARG D . n 
D 1 504 LEU 504 504 504 LEU LEU D . n 
D 1 505 GLY 505 505 505 GLY GLY D . n 
D 1 506 LEU 506 506 506 LEU LEU D . n 
D 1 507 CYS 507 507 507 CYS CYS D . n 
D 1 508 GLY 508 508 508 GLY GLY D . n 
D 1 509 ALA 509 509 509 ALA ALA D . n 
D 1 510 VAL 510 510 510 VAL VAL D . n 
D 1 511 SER 511 511 511 SER SER D . n 
D 1 512 TRP 512 512 512 TRP TRP D . n 
D 1 513 LEU 513 513 513 LEU LEU D . n 
D 1 514 ASP 514 514 514 ASP ASP D . n 
D 1 515 ALA 515 515 515 ALA ALA D . n 
D 1 516 LYS 516 516 516 LYS LYS D . n 
D 1 517 ALA 517 517 517 ALA ALA D . n 
D 1 518 THR 518 518 518 THR THR D . n 
D 1 519 LEU 519 519 519 LEU LEU D . n 
D 1 520 GLU 520 520 520 GLU GLU D . n 
D 1 521 LEU 521 521 521 LEU LEU D . n 
D 1 522 ASN 522 522 522 ASN ASN D . n 
D 1 523 PRO 523 523 523 PRO PRO D . n 
D 1 524 THR 524 524 524 THR THR D . n 
D 1 525 GLY 525 525 525 GLY GLY D . n 
D 1 526 PRO 526 526 526 PRO PRO D . n 
D 1 527 CYS 527 527 527 CYS CYS D . n 
D 1 528 GLN 528 528 528 GLN GLN D . n 
D 1 529 ALA 529 529 529 ALA ALA D . n 
D 1 530 VAL 530 530 530 VAL VAL D . n 
D 1 531 PRO 531 531 531 PRO PRO D . n 
D 1 532 LYS 532 532 532 LYS LYS D . n 
D 1 533 GLU 533 533 533 GLU GLU D . n 
D 1 534 GLY 534 534 534 GLY GLY D . n 
D 1 535 VAL 535 535 535 VAL VAL D . n 
D 1 536 VAL 536 536 536 VAL VAL D . n 
D 1 537 ASP 537 537 537 ASP ASP D . n 
D 1 538 GLU 538 538 538 GLU GLU D . n 
D 1 539 ASN 539 539 539 ASN ASN D . n 
D 1 540 LEU 540 540 540 LEU LEU D . n 
D 1 541 GLY 541 541 541 GLY GLY D . n 
D 1 542 ILE 542 542 542 ILE ILE D . n 
D 1 543 TRP 543 543 543 TRP TRP D . n 
D 1 544 GLU 544 544 544 GLU GLU D . n 
D 1 545 LYS 545 545 545 LYS LYS D . n 
D 1 546 VAL 546 546 546 VAL VAL D . n 
D 1 547 ASN 547 547 547 ASN ASN D . n 
D 1 548 GLU 548 548 548 GLU GLU D . n 
D 1 549 THR 549 549 549 THR THR D . n 
D 1 550 VAL 550 550 550 VAL VAL D . n 
D 1 551 SER 551 551 551 SER SER D . n 
D 1 552 LYS 552 552 552 LYS LYS D . n 
D 1 553 ILE 553 553 553 ILE ILE D . n 
D 1 554 SER 554 554 554 SER SER D . n 
D 1 555 GLN 555 555 555 GLN GLN D . n 
D 1 556 GLY 556 556 556 GLY GLY D . n 
D 1 557 ALA 557 557 557 ALA ALA D . n 
D 1 558 VAL 558 558 558 VAL VAL D . n 
D 1 559 THR 559 559 559 THR THR D . n 
D 1 560 SER 560 560 560 SER SER D . n 
D 1 561 VAL 561 561 561 VAL VAL D . n 
D 1 562 THR 562 562 562 THR THR D . n 
D 1 563 LEU 563 563 563 LEU LEU D . n 
D 1 564 TYR 564 564 564 TYR TYR D . n 
D 1 565 SER 565 565 565 SER SER D . n 
D 1 566 ILE 566 566 566 ILE ILE D . n 
D 1 567 LEU 567 567 567 LEU LEU D . n 
D 1 568 GLN 568 568 568 GLN GLN D . n 
D 1 569 ASP 569 569 569 ASP ASP D . n 
D 1 570 PRO 570 570 570 PRO PRO D . n 
D 1 571 MET 571 571 571 MET MET D . n 
D 1 572 THR 572 572 572 THR THR D . n 
D 1 573 SER 573 573 573 SER SER D . n 
D 1 574 CYS 574 574 574 CYS CYS D . n 
D 1 575 GLY 575 575 575 GLY GLY D . n 
D 1 576 CYS 576 576 576 CYS CYS D . n 
D 1 577 PHE 577 577 577 PHE PHE D . n 
D 1 578 GLU 578 578 578 GLU GLU D . n 
D 1 579 CYS 579 579 579 CYS CYS D . n 
D 1 580 ILE 580 580 580 ILE ILE D . n 
D 1 581 THR 581 581 581 THR THR D . n 
D 1 582 GLY 582 582 582 GLY GLY D . n 
D 1 583 ILE 583 583 583 ILE ILE D . n 
D 1 584 MET 584 584 584 MET MET D . n 
D 1 585 PRO 585 585 585 PRO PRO D . n 
D 1 586 GLU 586 586 586 GLU GLU D . n 
D 1 587 ALA 587 587 587 ALA ALA D . n 
D 1 588 ASN 588 588 588 ASN ASN D . n 
D 1 589 GLY 589 589 589 GLY GLY D . n 
D 1 590 VAL 590 590 590 VAL VAL D . n 
D 1 591 VAL 591 591 591 VAL VAL D . n 
D 1 592 MET 592 592 592 MET MET D . n 
D 1 593 VAL 593 593 593 VAL VAL D . n 
D 1 594 ASN 594 594 594 ASN ASN D . n 
D 1 595 ARG 595 595 595 ARG ARG D . n 
D 1 596 GLU 596 596 596 GLU GLU D . n 
D 1 597 PHE 597 597 597 PHE PHE D . n 
D 1 598 GLY 598 598 598 GLY GLY D . n 
D 1 599 ALA 599 599 599 ALA ALA D . n 
D 1 600 THR 600 600 600 THR THR D . n 
D 1 601 THR 601 601 601 THR THR D . n 
D 1 602 PRO 602 602 602 PRO PRO D . n 
D 1 603 LEU 603 603 603 LEU LEU D . n 
D 1 604 GLY 604 604 604 GLY GLY D . n 
D 1 605 MET 605 605 605 MET MET D . n 
D 1 606 THR 606 606 606 THR THR D . n 
D 1 607 PHE 607 607 607 PHE PHE D . n 
D 1 608 GLY 608 608 608 GLY GLY D . n 
D 1 609 GLU 609 609 609 GLU GLU D . n 
D 1 610 LEU 610 610 610 LEU LEU D . n 
D 1 611 ALA 611 611 611 ALA ALA D . n 
D 1 612 SER 612 612 612 SER SER D . n 
D 1 613 MET 613 613 613 MET MET D . n 
D 1 614 THR 614 614 614 THR THR D . n 
D 1 615 GLY 615 615 615 GLY GLY D . n 
D 1 616 GLY 616 616 616 GLY GLY D . n 
D 1 617 GLY 617 617 617 GLY GLY D . n 
D 1 618 VAL 618 618 618 VAL VAL D . n 
D 1 619 GLN 619 619 619 GLN GLN D . n 
D 1 620 THR 620 620 620 THR THR D . n 
D 1 621 PRO 621 621 621 PRO PRO D . n 
D 1 622 GLY 622 622 622 GLY GLY D . n 
D 1 623 PHE 623 623 623 PHE PHE D . n 
D 1 624 MET 624 624 624 MET MET D . n 
D 1 625 GLY 625 625 625 GLY GLY D . n 
D 1 626 HIS 626 626 626 HIS HIS D . n 
D 1 627 GLY 627 627 627 GLY GLY D . n 
D 1 628 ARG 628 628 628 ARG ARG D . n 
D 1 629 GLN 629 629 629 GLN GLN D . n 
D 1 630 PHE 630 630 630 PHE PHE D . n 
D 1 631 ILE 631 631 631 ILE ILE D . n 
D 1 632 ALA 632 632 632 ALA ALA D . n 
D 1 633 SER 633 633 633 SER SER D . n 
D 1 634 LYS 634 634 634 LYS LYS D . n 
D 1 635 LYS 635 635 635 LYS LYS D . n 
D 1 636 PHE 636 636 636 PHE PHE D . n 
D 1 637 MET 637 637 637 MET MET D . n 
D 1 638 LYS 638 638 638 LYS LYS D . n 
D 1 639 GLY 639 639 639 GLY GLY D . n 
D 1 640 GLU 640 640 640 GLU GLU D . n 
D 1 641 GLY 641 641 641 GLY GLY D . n 
D 1 642 GLY 642 642 642 GLY GLY D . n 
D 1 643 LEU 643 643 643 LEU LEU D . n 
D 1 644 GLY 644 644 644 GLY GLY D . n 
D 1 645 ARG 645 645 645 ARG ARG D . n 
D 1 646 ILE 646 646 646 ILE ILE D . n 
D 1 647 VAL 647 647 647 VAL VAL D . n 
D 1 648 TRP 648 648 648 TRP TRP D . n 
D 1 649 MET 649 649 649 MET MET D . n 
D 1 650 PRO 650 650 650 PRO PRO D . n 
D 1 651 LYS 651 651 651 LYS LYS D . n 
D 1 652 GLU 652 652 652 GLU GLU D . n 
D 1 653 LEU 653 653 653 LEU LEU D . n 
D 1 654 LYS 654 654 654 LYS LYS D . n 
D 1 655 ASP 655 655 655 ASP ASP D . n 
D 1 656 PHE 656 656 656 PHE PHE D . n 
D 1 657 VAL 657 657 657 VAL VAL D . n 
D 1 658 ALA 658 658 658 ALA ALA D . n 
D 1 659 GLU 659 659 659 GLU GLU D . n 
D 1 660 LYS 660 660 660 LYS LYS D . n 
D 1 661 LEU 661 661 661 LEU LEU D . n 
D 1 662 ASN 662 662 662 ASN ASN D . n 
D 1 663 LYS 663 663 663 LYS LYS D . n 
D 1 664 THR 664 664 664 THR THR D . n 
D 1 665 ALA 665 665 665 ALA ALA D . n 
D 1 666 LYS 666 666 666 LYS LYS D . n 
D 1 667 GLU 667 667 667 GLU GLU D . n 
D 1 668 LEU 668 668 668 LEU LEU D . n 
D 1 669 TYR 669 669 669 TYR TYR D . n 
D 1 670 ASN 670 670 670 ASN ASN D . n 
D 1 671 ILE 671 671 671 ILE ILE D . n 
D 1 672 ASP 672 672 672 ASP ASP D . n 
D 1 673 ASN 673 673 673 ASN ASN D . n 
D 1 674 PHE 674 674 674 PHE PHE D . n 
D 1 675 ALA 675 675 675 ALA ALA D . n 
D 1 676 ASP 676 676 676 ASP ASP D . n 
D 1 677 MET 677 677 677 MET MET D . n 
D 1 678 ILE 678 678 678 ILE ILE D . n 
D 1 679 CYS 679 679 679 CYS CYS D . n 
D 1 680 ASP 680 680 680 ASP ASP D . n 
D 1 681 GLU 681 681 681 GLU GLU D . n 
D 1 682 THR 682 682 682 THR THR D . n 
D 1 683 ILE 683 683 683 ILE ILE D . n 
D 1 684 ALA 684 684 684 ALA ALA D . n 
D 1 685 THR 685 685 685 THR THR D . n 
D 1 686 GLU 686 686 686 GLU GLU D . n 
D 1 687 SER 687 687 687 SER SER D . n 
D 1 688 GLU 688 688 688 GLU GLU D . n 
D 1 689 GLU 689 689 689 GLU GLU D . n 
D 1 690 VAL 690 690 690 VAL VAL D . n 
D 1 691 VAL 691 691 691 VAL VAL D . n 
D 1 692 LYS 692 692 692 LYS LYS D . n 
D 1 693 PHE 693 693 693 PHE PHE D . n 
D 1 694 LEU 694 694 694 LEU LEU D . n 
D 1 695 GLU 695 695 695 GLU GLU D . n 
D 1 696 GLU 696 696 696 GLU GLU D . n 
D 1 697 LYS 697 697 697 LYS LYS D . n 
D 1 698 GLY 698 698 698 GLY GLY D . n 
D 1 699 HIS 699 699 699 HIS HIS D . n 
D 1 700 PRO 700 700 700 PRO PRO D . n 
D 1 701 ALA 701 701 701 ALA ALA D . n 
D 1 702 LEU 702 702 702 LEU LEU D . n 
D 1 703 LYS 703 703 703 LYS LYS D . n 
D 1 704 MET 704 704 704 MET MET D . n 
D 1 705 ASP 705 705 705 ASP ASP D . n 
D 1 706 PRO 706 706 706 PRO PRO D . n 
D 1 707 ILE 707 707 707 ILE ILE D . n 
D 1 708 MET 708 708 708 MET MET D . 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 ACO ? ? ACO ? ? 'SUBJECT OF INVESTIGATION' ? 
2 XCC ? ? XCC ? ? 'SUBJECT OF INVESTIGATION' ? 
3 NI  ? ? NI  ? ? '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 
E  3  SF4 1 801 804  SF4 SF4 A . 
F  4  NI  1 802 807  NI  NI  A . 
G  4  NI  1 803 808  NI  NI  A . 
H  5  EDO 1 804 809  EDO EDO A . 
I  6  PE4 1 805 810  PE4 PE4 A . 
J  5  EDO 1 806 811  EDO EDO A . 
K  7  GOL 1 807 812  GOL GOL A . 
L  8  PEG 1 808 813  PEG PEG A . 
M  9  CA  1 809 82   CA  CA  A . 
N  9  CA  1 810 84   CA  CA  A . 
O  9  CA  1 811 85   CA  CA  A . 
P  9  CA  1 812 89   CA  CA  A . 
Q  10 CL  1 813 5    CL  CL  A . 
R  10 CL  1 814 12   CL  CL  A . 
S  5  EDO 1 815 1    EDO EDO A . 
T  5  EDO 1 816 2    EDO EDO A . 
U  5  EDO 1 817 3    EDO EDO A . 
V  5  EDO 1 818 18   EDO EDO A . 
W  5  EDO 1 819 32   EDO EDO A . 
X  5  EDO 1 820 34   EDO EDO A . 
Y  7  GOL 1 701 704  GOL GOL B . 
Z  3  SF4 1 702 708  SF4 SF4 B . 
AA 8  PEG 1 703 715  PEG PEG B . 
BA 7  GOL 1 704 716  GOL GOL B . 
CA 11 XCC 1 705 717  XCC XCC B . 
DA 7  GOL 1 706 718  GOL GOL B . 
EA 7  GOL 1 707 719  GOL GOL B . 
FA 9  CA  1 708 90   CA  CA  B . 
GA 10 CL  1 709 6    CL  CL  B . 
HA 10 CL  1 710 7    CL  CL  B . 
IA 10 CL  1 711 9    CL  CL  B . 
JA 10 CL  1 712 10   CL  CL  B . 
KA 10 CL  1 713 11   CL  CL  B . 
LA 5  EDO 1 714 6    EDO EDO B . 
MA 5  EDO 1 715 7    EDO EDO B . 
NA 5  EDO 1 716 10   EDO EDO B . 
OA 5  EDO 1 717 16   EDO EDO B . 
PA 5  EDO 1 718 20   EDO EDO B . 
QA 5  EDO 1 719 21   EDO EDO B . 
RA 5  EDO 1 720 23   EDO EDO B . 
SA 5  EDO 1 721 24   EDO EDO B . 
TA 5  EDO 1 722 25   EDO EDO B . 
UA 5  EDO 1 723 26   EDO EDO B . 
VA 5  EDO 1 724 27   EDO EDO B . 
WA 5  EDO 1 725 28   EDO EDO B . 
XA 5  EDO 1 726 30   EDO EDO B . 
YA 5  EDO 1 727 33   EDO EDO B . 
ZA 5  EDO 1 728 36   EDO EDO B . 
AB 3  SF4 1 701 707  SF4 SF4 C . 
BB 3  SF4 1 702 1004 SF4 SF4 C . 
CB 5  EDO 1 703 1016 EDO EDO C . 
DB 11 XCC 1 704 1017 XCC XCC C . 
EB 9  CA  1 705 24   CA  CA  C . 
FB 9  CA  1 706 83   CA  CA  C . 
GB 9  CA  1 707 86   CA  CA  C . 
HB 10 CL  1 708 8    CL  CL  C . 
IB 5  EDO 1 709 8    EDO EDO C . 
JB 5  EDO 1 710 9    EDO EDO C . 
KB 5  EDO 1 711 17   EDO EDO C . 
LB 5  EDO 1 712 19   EDO EDO C . 
MB 5  EDO 1 713 22   EDO EDO C . 
NB 5  EDO 1 714 31   EDO EDO C . 
OB 3  SF4 1 801 1002 SF4 SF4 D . 
PB 4  NI  1 802 1003 NI  NI  D . 
QB 4  NI  1 803 1004 NI  NI  D . 
RB 8  PEG 1 804 1006 PEG PEG D . 
SB 12 ACO 1 805 1008 ACO ACO D . 
TB 7  GOL 1 806 1009 GOL GOL D . 
UB 13 TRS 1 807 1010 TRS TRS D . 
VB 9  CA  1 808 87   CA  CA  D . 
WB 9  CA  1 809 88   CA  CA  D . 
XB 5  EDO 1 810 11   EDO EDO D . 
YB 5  EDO 1 811 13   EDO EDO D . 
ZB 5  EDO 1 812 15   EDO EDO D . 
AC 5  EDO 1 813 35   EDO EDO D . 
BC 14 HOH 1 901 4    HOH HOH A . 
BC 14 HOH 2 902 14   HOH HOH A . 
CC 14 HOH 1 801 6    HOH HOH B . 
CC 14 HOH 2 802 3    HOH HOH B . 
CC 14 HOH 3 803 13   HOH HOH B . 
CC 14 HOH 4 804 11   HOH HOH B . 
CC 14 HOH 5 805 10   HOH HOH B . 
DC 14 HOH 1 801 5    HOH HOH C . 
DC 14 HOH 2 802 1    HOH HOH C . 
DC 14 HOH 3 803 7    HOH HOH C . 
DC 14 HOH 4 804 9    HOH HOH C . 
DC 14 HOH 5 805 8    HOH HOH C . 
EC 14 HOH 1 901 2    HOH HOH D . 
EC 14 HOH 2 902 12   HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 N 1 A PE4 805 ? O1  ? I PE4 1 O1  
2  1 N 1 A PE4 805 ? C1  ? I PE4 1 C1  
3  1 N 1 A PE4 805 ? C2  ? I PE4 1 C2  
4  1 N 1 A PE4 805 ? O2  ? I PE4 1 O2  
5  1 N 1 A PE4 805 ? C3  ? I PE4 1 C3  
6  1 N 1 A PE4 805 ? C4  ? I PE4 1 C4  
7  1 N 1 A PE4 805 ? O3  ? I PE4 1 O3  
8  1 N 1 A PE4 805 ? C5  ? I PE4 1 C5  
9  1 N 1 A PE4 805 ? C6  ? I PE4 1 C6  
10 1 N 1 A PE4 805 ? O4  ? I PE4 1 O4  
11 1 N 1 A PE4 805 ? C7  ? I PE4 1 C7  
12 1 N 1 A PE4 805 ? C8  ? I PE4 1 C8  
13 1 N 1 A PE4 805 ? C15 ? I PE4 1 C15 
14 1 N 1 A PE4 805 ? C16 ? I PE4 1 C16 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9G7I 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     298.077 
_cell.length_a_esd                 ? 
_cell.length_b                     298.077 
_cell.length_b_esd                 ? 
_cell.length_c                     127.526 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9G7I 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                94 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 42 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9G7I 
_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             4.74 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          74.08 
_exptl_crystal.description                  'brown square plate' 
_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    
;Crystallization was performed anaerobically by initial screening at 20 degrees Celsius using the sitting drop method on 96 Well MRC 2 Drop polystyrene Crystallization Plates SWISSCI in a Coy tent containing an N2/H2 (97:3%) atmosphere. The reservoir contained 90 ul of 25 % (w/v) glycerol ethoxylate 1,000, 100 mM Tris/HCl pH 8.5, and 100 mM CaCl2. 0.6 ul of crystallization solution was mixed with 0.6 ul of the protein, containing a final concentration of 2 mM acetyl-CoA. The protein was concentrated at 15 mg/ml in 25 mM Tris/HCl pH 7.6, 10% (v/v) glycerol, and 2 mM dithiothreitol.
The crystals appeared in few weeks and were soaked in the crystallization solution supplemented with 15% (v/v) Ethylene glycol for a few seconds before freezing in liquid nitrogen.
;
_exptl_crystal_grow.pdbx_pH_range   / 
_exptl_crystal_grow.temp            293.15 
# 
_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 PILATUS 2M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-01-29 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00003 
_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                        'SLS BEAMLINE X06DA' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00003 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   X06DA 
_diffrn_source.pdbx_synchrotron_site       SLS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9G7I 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.93 
_reflns.d_resolution_low                               59.61 
_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                                     99666 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           96.1 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                22.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.5 
_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                                0.211 
_reflns.pdbx_Rpim_I_all                                0.045 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.207 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.045 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.93 
_reflns_shell.d_res_low                                     3.16 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.6 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4983 
_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                               23.3 
_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                               2.477 
_reflns_shell.pdbx_Rpim_I_all                               0.513 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.593 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          73 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  2.423 
_reflns_shell.pdbx_Rsym_value                               0.513 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               89.64 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  
;The structure was refined with phenix.refine considering translation libration screw. Riding hydrogens and non-crystallography symmetry were not used during the refinement.
;
_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                                 9G7I 
_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                            2.93 
_refine.ls_d_res_low                             49.68 
_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                     99636 
_refine.ls_number_reflns_R_free                  5002 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    81.39 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1917 
_refine.ls_R_factor_R_free                       0.2202 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1902 
_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                          1.33 
_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                 23.23 
_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                            0.28 
_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.pdbx_number_atoms_protein        20122 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         342 
_refine_hist.number_atoms_solvent             14 
_refine_hist.number_atoms_total               20478 
_refine_hist.d_res_high                       2.93 
_refine_hist.d_res_low                        49.68 
# 
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' ? 0.010  ? 20780 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.367  ? 28075 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 15.855 ? 7736  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.090  ? 3264  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 3566  ? 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' 2.93 2.97  . . 5   60   2.00   . . . . 0.3451 . . . . . . . . . . . 0.3362 
'X-RAY DIFFRACTION' 2.97 3.00  . . 14  304  8.00   . . . . 0.3644 . . . . . . . . . . . 0.3515 
'X-RAY DIFFRACTION' 3.00 3.04  . . 38  654  17.00  . . . . 0.3483 . . . . . . . . . . . 0.4075 
'X-RAY DIFFRACTION' 3.04 3.08  . . 51  970  25.00  . . . . 0.3270 . . . . . . . . . . . 0.3064 
'X-RAY DIFFRACTION' 3.08 3.12  . . 78  1265 33.00  . . . . 0.3102 . . . . . . . . . . . 0.3511 
'X-RAY DIFFRACTION' 3.12 3.16  . . 99  1669 44.00  . . . . 0.3029 . . . . . . . . . . . 0.3234 
'X-RAY DIFFRACTION' 3.16 3.21  . . 115 2107 55.00  . . . . 0.2888 . . . . . . . . . . . 0.3263 
'X-RAY DIFFRACTION' 3.21 3.25  . . 131 2639 69.00  . . . . 0.2914 . . . . . . . . . . . 0.3328 
'X-RAY DIFFRACTION' 3.25 3.30  . . 177 3240 85.00  . . . . 0.2836 . . . . . . . . . . . 0.3290 
'X-RAY DIFFRACTION' 3.30 3.36  . . 198 3787 98.00  . . . . 0.2673 . . . . . . . . . . . 0.3072 
'X-RAY DIFFRACTION' 3.36 3.42  . . 210 3827 100.00 . . . . 0.2498 . . . . . . . . . . . 0.3071 
'X-RAY DIFFRACTION' 3.42 3.48  . . 190 3826 100.00 . . . . 0.2423 . . . . . . . . . . . 0.2889 
'X-RAY DIFFRACTION' 3.48 3.55  . . 207 3853 100.00 . . . . 0.2364 . . . . . . . . . . . 0.2972 
'X-RAY DIFFRACTION' 3.55 3.62  . . 205 3827 100.00 . . . . 0.2236 . . . . . . . . . . . 0.2702 
'X-RAY DIFFRACTION' 3.62 3.70  . . 202 3863 100.00 . . . . 0.2108 . . . . . . . . . . . 0.2302 
'X-RAY DIFFRACTION' 3.70 3.78  . . 209 3842 100.00 . . . . 0.1989 . . . . . . . . . . . 0.2426 
'X-RAY DIFFRACTION' 3.78 3.88  . . 191 3889 100.00 . . . . 0.1907 . . . . . . . . . . . 0.2264 
'X-RAY DIFFRACTION' 3.88 3.98  . . 206 3851 100.00 . . . . 0.1780 . . . . . . . . . . . 0.1916 
'X-RAY DIFFRACTION' 3.98 4.10  . . 221 3841 100.00 . . . . 0.1635 . . . . . . . . . . . 0.1985 
'X-RAY DIFFRACTION' 4.10 4.23  . . 199 3857 100.00 . . . . 0.1604 . . . . . . . . . . . 0.1771 
'X-RAY DIFFRACTION' 4.23 4.38  . . 201 3903 100.00 . . . . 0.1492 . . . . . . . . . . . 0.1761 
'X-RAY DIFFRACTION' 4.38 4.56  . . 186 3892 100.00 . . . . 0.1470 . . . . . . . . . . . 0.1940 
'X-RAY DIFFRACTION' 4.56 4.76  . . 187 3899 100.00 . . . . 0.1425 . . . . . . . . . . . 0.1817 
'X-RAY DIFFRACTION' 4.76 5.02  . . 216 3877 100.00 . . . . 0.1481 . . . . . . . . . . . 0.1982 
'X-RAY DIFFRACTION' 5.02 5.33  . . 231 3892 100.00 . . . . 0.1680 . . . . . . . . . . . 0.2145 
'X-RAY DIFFRACTION' 5.33 5.74  . . 204 3903 100.00 . . . . 0.1829 . . . . . . . . . . . 0.1946 
'X-RAY DIFFRACTION' 5.74 6.32  . . 193 3957 100.00 . . . . 0.2003 . . . . . . . . . . . 0.2343 
'X-RAY DIFFRACTION' 6.32 7.23  . . 221 3944 100.00 . . . . 0.1969 . . . . . . . . . . . 0.2033 
'X-RAY DIFFRACTION' 7.23 9.10  . . 203 4014 100.00 . . . . 0.1733 . . . . . . . . . . . 0.1818 
'X-RAY DIFFRACTION' 9.10 49.68 . . 214 4182 100.00 . . . . 0.1935 . . . . . . . . . . . 0.2121 
# 
_struct.entry_id                     9G7I 
_struct.title                        
;Structure of carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS) in complex with acetyl-Coenyzme A from Clostridium autoethanogenum
;
_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        9G7I 
_struct_keywords.text            
'Carbon monoxide, acetyl-CoA, Wood-Ljungdahl pathway, C-cluster, A-cluster, gas channelling, acetogenic bacteria, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1  ? 
B  N N 2  ? 
C  N N 2  ? 
D  N N 1  ? 
E  N N 3  ? 
F  N N 4  ? 
G  N N 4  ? 
H  N N 5  ? 
I  N N 6  ? 
J  N N 5  ? 
K  N N 7  ? 
L  N N 8  ? 
M  N N 9  ? 
N  N N 9  ? 
O  N N 9  ? 
P  N N 9  ? 
Q  N N 10 ? 
R  N N 10 ? 
S  N N 5  ? 
T  N N 5  ? 
U  N N 5  ? 
V  N N 5  ? 
W  N N 5  ? 
X  N N 5  ? 
Y  N N 7  ? 
Z  N N 3  ? 
AA N N 8  ? 
BA N N 7  ? 
CA N N 11 ? 
DA N N 7  ? 
EA N N 7  ? 
FA N N 9  ? 
GA N N 10 ? 
HA N N 10 ? 
IA N N 10 ? 
JA N N 10 ? 
KA N N 10 ? 
LA N N 5  ? 
MA N N 5  ? 
NA N N 5  ? 
OA N N 5  ? 
PA N N 5  ? 
QA N N 5  ? 
RA N N 5  ? 
SA N N 5  ? 
TA N N 5  ? 
UA N N 5  ? 
VA N N 5  ? 
WA N N 5  ? 
XA N N 5  ? 
YA N N 5  ? 
ZA N N 5  ? 
AB N N 3  ? 
BB N N 3  ? 
CB N N 5  ? 
DB N N 11 ? 
EB N N 9  ? 
FB N N 9  ? 
GB N N 9  ? 
HB N N 10 ? 
IB N N 5  ? 
JB N N 5  ? 
KB N N 5  ? 
LB N N 5  ? 
MB N N 5  ? 
NB N N 5  ? 
OB N N 3  ? 
PB N N 4  ? 
QB N N 4  ? 
RB N N 8  ? 
SB N N 12 ? 
TB N N 7  ? 
UB N N 13 ? 
VB N N 9  ? 
WB N N 9  ? 
XB N N 5  ? 
YB N N 5  ? 
ZB N N 5  ? 
AC N N 5  ? 
BC N N 14 ? 
CC N N 14 ? 
DC N N 14 ? 
EC N N 14 ? 
# 
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 F8TEQ9_9CLOT F8TEQ9 ? 1 
;MNLFQTVFTGSKQALAAAEGIVKQAVDEKGRDYKVAFPDTAYSLPVIFAATGKKITNVGELEGALDIVRSLIVEEEMLDK
LLNSGLATAVAAEIIEAAKYVLSDAPYAEPCVGFISDPIIRSLGVPLVTGDIPGVAVILGECPDSETAAKIIKDYQSKGL
LTCLVGKVIDQAIEGKVKMGLDLRVIPLGYDVTSVIHVVTIAIRAALIFGGIKGGQLNDILKYTAERVPAFVNAFGPLSE
LVVSAGAGAIALGFPVLTDQVVPEVPTLLLTQKDYDKMVKTSLEARNIKIKITEIPIPVSFAAAFEGERIRKNDMLAEFG
GNKTKAWELVMCADQGEVEDHKIEVIGPDIDTIDKAPGRMPLGMLIKVSGTNMQKDFEPVLERRLHYFLNYIEGVMHVGQ
RNLTWVRIGKEAFEKGFRLKHFGEVIYAKMLDEFGSVVDKCEVTIITDPGKAEELEGKYAVPRYKERDARLESLVDEKVD
TFYSCNLCQSFAPAHVCIVTPERLGLCGAVSWLDAKATLELNPTGPCQAVPKEGVVDENLGIWEKVNETVSKISQGAVTS
VTLYSILQDPMTSCGCFECITGIMPEANGVVMVNREFGATTPLGMTFGELASMTGGGVQTPGFMGHGRQFIASKKFMKGE
GGLGRIVWMPKELKDFVAEKLNKTAKELYNIDNFADMICDETIATESEEVVKFLEEKGHPALKMDPIM
;
1 
2 PDB 9G7I         9G7I   ? 2 ? 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 9G7I A 1 ? 708 ? F8TEQ9 1 ? 708 ? 1 708 
2 2 9G7I B 1 ? 631 ? 9G7I   1 ? 631 ? 1 631 
3 2 9G7I C 1 ? 631 ? 9G7I   1 ? 631 ? 1 631 
4 1 9G7I D 1 ? 708 ? F8TEQ9 1 ? 708 ? 1 708 
# 
_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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      
;A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,LA,MA,NA,OA,PA,QA,RA,SA,TA,UA,VA,WA,XA,YA,ZA,AB,BB,CB,DB,EB,FB,GB,HB,IB,JB,KB,LB,MB,NB,OB,PB,QB,RB,SB,TB,UB,VB,WB,XB,YB,ZB,AC,BC,CC,DC,EC
;
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 2   ? GLY A 30  ? ASN A 2   GLY A 30  1 ? 29 
HELX_P HELX_P2   AA2 LEU A 44  ? GLY A 52  ? LEU A 44  GLY A 52  1 ? 9  
HELX_P HELX_P3   AA3 ASN A 57  ? ALA A 64  ? ASN A 57  ALA A 64  1 ? 8  
HELX_P HELX_P4   AA4 ALA A 64  ? ILE A 72  ? ALA A 64  ILE A 72  1 ? 9  
HELX_P HELX_P5   AA5 MET A 77  ? SER A 103 ? MET A 77  SER A 103 1 ? 27 
HELX_P HELX_P6   AA6 SER A 116 ? THR A 129 ? SER A 116 THR A 129 1 ? 14 
HELX_P HELX_P7   AA7 ASP A 144 ? LYS A 158 ? ASP A 144 LYS A 158 1 ? 15 
HELX_P HELX_P8   AA8 LYS A 167 ? GLY A 175 ? LYS A 167 GLY A 175 1 ? 9  
HELX_P HELX_P9   AA9 ASP A 191 ? SER A 194 ? ASP A 191 SER A 194 5 ? 4  
HELX_P HELX_P10  AB1 VAL A 195 ? PHE A 209 ? VAL A 195 PHE A 209 1 ? 15 
HELX_P HELX_P11  AB2 GLN A 216 ? VAL A 228 ? GLN A 216 VAL A 228 1 ? 13 
HELX_P HELX_P12  AB3 SER A 239 ? LEU A 252 ? SER A 239 LEU A 252 1 ? 14 
HELX_P HELX_P13  AB4 ASP A 274 ? ASP A 276 ? ASP A 274 ASP A 276 5 ? 3  
HELX_P HELX_P14  AB5 LYS A 277 ? ARG A 286 ? LYS A 277 ARG A 286 1 ? 10 
HELX_P HELX_P15  AB6 ALA A 302 ? GLY A 307 ? ALA A 302 GLY A 307 5 ? 6  
HELX_P HELX_P16  AB7 ASP A 349 ? ILE A 353 ? ASP A 349 ILE A 353 5 ? 5  
HELX_P HELX_P17  AB8 GLU A 378 ? ILE A 392 ? GLU A 378 ILE A 392 1 ? 15 
HELX_P HELX_P18  AB9 LYS A 410 ? GLY A 416 ? LYS A 410 GLY A 416 1 ? 7  
HELX_P HELX_P19  AC1 ARG A 418 ? PHE A 434 ? ARG A 418 PHE A 434 1 ? 17 
HELX_P HELX_P20  AC2 ASP A 448 ? TYR A 459 ? ASP A 448 TYR A 459 1 ? 12 
HELX_P HELX_P21  AC3 TYR A 459 ? LEU A 474 ? TYR A 459 LEU A 474 1 ? 16 
HELX_P HELX_P22  AC4 VAL A 475 ? VAL A 479 ? VAL A 475 VAL A 479 5 ? 5  
HELX_P HELX_P23  AC5 ASN A 486 ? PHE A 491 ? ASN A 486 PHE A 491 5 ? 6  
HELX_P HELX_P24  AC6 LEU A 513 ? ASN A 522 ? LEU A 513 ASN A 522 1 ? 10 
HELX_P HELX_P25  AC7 GLU A 544 ? GLN A 555 ? GLU A 544 GLN A 555 1 ? 12 
HELX_P HELX_P26  AC8 PRO A 585 ? ASN A 588 ? PRO A 585 ASN A 588 5 ? 4  
HELX_P HELX_P27  AC9 THR A 606 ? GLY A 615 ? THR A 606 GLY A 615 1 ? 10 
HELX_P HELX_P28  AD1 MET A 637 ? GLY A 644 ? MET A 637 GLY A 644 5 ? 8  
HELX_P HELX_P29  AD2 PRO A 650 ? VAL A 657 ? PRO A 650 VAL A 657 1 ? 8  
HELX_P HELX_P30  AD3 ALA A 658 ? GLU A 667 ? ALA A 658 GLU A 667 1 ? 10 
HELX_P HELX_P31  AD4 ASN A 673 ? ILE A 678 ? ASN A 673 ILE A 678 1 ? 6  
HELX_P HELX_P32  AD5 GLU A 686 ? GLY A 698 ? GLU A 686 GLY A 698 1 ? 13 
HELX_P HELX_P33  AD6 HIS A 699 ? MET A 704 ? HIS A 699 MET A 704 1 ? 6  
HELX_P HELX_P34  AD7 ASP B 9   ? GLY B 23  ? ASP B 9   GLY B 23  1 ? 15 
HELX_P HELX_P35  AD8 THR B 26  ? MET B 34  ? THR B 26  MET B 34  1 ? 9  
HELX_P HELX_P36  AD9 CYS B 38  ? GLY B 44  ? CYS B 38  GLY B 44  1 ? 7  
HELX_P HELX_P37  AE1 THR B 73  ? TYR B 105 ? THR B 73  TYR B 105 1 ? 33 
HELX_P HELX_P38  AE2 ASP B 117 ? PHE B 128 ? ASP B 117 PHE B 128 1 ? 12 
HELX_P HELX_P39  AE3 ASP B 136 ? LYS B 154 ? ASP B 136 LYS B 154 1 ? 19 
HELX_P HELX_P40  AE4 PRO B 166 ? GLY B 177 ? PRO B 166 GLY B 177 1 ? 12 
HELX_P HELX_P41  AE5 ALA B 182 ? THR B 194 ? ALA B 182 THR B 194 1 ? 13 
HELX_P HELX_P42  AE6 ASP B 201 ? TRP B 218 ? ASP B 201 TRP B 218 1 ? 18 
HELX_P HELX_P43  AE7 MET B 219 ? GLY B 233 ? MET B 219 GLY B 233 1 ? 15 
HELX_P HELX_P44  AE8 ASN B 243 ? LEU B 247 ? ASN B 243 LEU B 247 5 ? 5  
HELX_P HELX_P45  AE9 GLU B 260 ? ALA B 271 ? GLU B 260 ALA B 271 1 ? 12 
HELX_P HELX_P46  AF1 ASP B 273 ? VAL B 283 ? ASP B 273 VAL B 283 1 ? 11 
HELX_P HELX_P47  AF2 CYS B 294 ? GLY B 305 ? CYS B 294 GLY B 305 1 ? 12 
HELX_P HELX_P48  AF3 ASN B 311 ? MET B 313 ? ASN B 311 MET B 313 5 ? 3  
HELX_P HELX_P49  AF4 GLN B 314 ? THR B 321 ? GLN B 314 THR B 321 1 ? 8  
HELX_P HELX_P50  AF5 PRO B 336 ? SER B 342 ? PRO B 336 SER B 342 1 ? 7  
HELX_P HELX_P51  AF6 LYS B 343 ? TYR B 345 ? LYS B 343 TYR B 345 5 ? 3  
HELX_P HELX_P52  AF7 ASN B 370 ? ASN B 385 ? ASN B 370 ASN B 385 1 ? 16 
HELX_P HELX_P53  AF8 PHE B 386 ? ARG B 389 ? PHE B 386 ARG B 389 5 ? 4  
HELX_P HELX_P54  AF9 ASP B 390 ? VAL B 394 ? ASP B 390 VAL B 394 5 ? 5  
HELX_P HELX_P55  AG1 SER B 408 ? ASP B 417 ? SER B 408 ASP B 417 1 ? 10 
HELX_P HELX_P56  AG2 LYS B 418 ? VAL B 420 ? LYS B 418 VAL B 420 5 ? 3  
HELX_P HELX_P57  AG3 VAL B 430 ? GLY B 440 ? VAL B 430 GLY B 440 1 ? 11 
HELX_P HELX_P58  AG4 ASP B 459 ? ASN B 472 ? ASP B 459 ASN B 472 1 ? 14 
HELX_P HELX_P59  AG5 THR B 479 ? GLY B 490 ? THR B 479 GLY B 490 1 ? 12 
HELX_P HELX_P60  AG6 GLU B 495 ? ALA B 501 ? GLU B 495 ALA B 501 1 ? 7  
HELX_P HELX_P61  AG7 GLY B 502 ? ASP B 513 ? GLY B 502 ASP B 513 1 ? 12 
HELX_P HELX_P62  AG8 ASP B 525 ? LEU B 540 ? ASP B 525 LEU B 540 1 ? 16 
HELX_P HELX_P63  AG9 ASP B 543 ? LEU B 547 ? ASP B 543 LEU B 547 5 ? 5  
HELX_P HELX_P64  AH1 SER B 558 ? SER B 571 ? SER B 558 SER B 571 1 ? 14 
HELX_P HELX_P65  AH2 GLY B 586 ? ASN B 595 ? GLY B 586 ASN B 595 1 ? 10 
HELX_P HELX_P66  AH3 LYS B 596 ? GLY B 602 ? LYS B 596 GLY B 602 1 ? 7  
HELX_P HELX_P67  AH4 ASP B 610 ? GLY B 630 ? ASP B 610 GLY B 630 1 ? 21 
HELX_P HELX_P68  AH5 ASP C 9   ? GLY C 23  ? ASP C 9   GLY C 23  1 ? 15 
HELX_P HELX_P69  AH6 THR C 26  ? LYS C 35  ? THR C 26  LYS C 35  1 ? 10 
HELX_P HELX_P70  AH7 CYS C 38  ? GLY C 44  ? CYS C 38  GLY C 44  1 ? 7  
HELX_P HELX_P71  AH8 THR C 73  ? HIS C 106 ? THR C 73  HIS C 106 1 ? 34 
HELX_P HELX_P72  AH9 ASP C 117 ? PHE C 128 ? ASP C 117 PHE C 128 1 ? 12 
HELX_P HELX_P73  AI1 ASP C 136 ? LYS C 154 ? ASP C 136 LYS C 154 1 ? 19 
HELX_P HELX_P74  AI2 PRO C 166 ? GLY C 177 ? PRO C 166 GLY C 177 1 ? 12 
HELX_P HELX_P75  AI3 ALA C 182 ? HIS C 195 ? ALA C 182 HIS C 195 1 ? 14 
HELX_P HELX_P76  AI4 ASP C 201 ? TRP C 218 ? ASP C 201 TRP C 218 1 ? 18 
HELX_P HELX_P77  AI5 MET C 219 ? GLY C 233 ? MET C 219 GLY C 233 1 ? 15 
HELX_P HELX_P78  AI6 ASN C 243 ? LEU C 247 ? ASN C 243 LEU C 247 5 ? 5  
HELX_P HELX_P79  AI7 GLU C 260 ? ALA C 271 ? GLU C 260 ALA C 271 1 ? 12 
HELX_P HELX_P80  AI8 ASP C 273 ? GLY C 284 ? ASP C 273 GLY C 284 1 ? 12 
HELX_P HELX_P81  AI9 CYS C 294 ? GLY C 305 ? CYS C 294 GLY C 305 1 ? 12 
HELX_P HELX_P82  AJ1 ASN C 311 ? MET C 313 ? ASN C 311 MET C 313 5 ? 3  
HELX_P HELX_P83  AJ2 GLN C 314 ? THR C 321 ? GLN C 314 THR C 321 1 ? 8  
HELX_P HELX_P84  AJ3 PRO C 336 ? SER C 342 ? PRO C 336 SER C 342 1 ? 7  
HELX_P HELX_P85  AJ4 LYS C 343 ? TYR C 345 ? LYS C 343 TYR C 345 5 ? 3  
HELX_P HELX_P86  AJ5 ASN C 370 ? PHE C 386 ? ASN C 370 PHE C 386 1 ? 17 
HELX_P HELX_P87  AJ6 LYS C 387 ? ARG C 389 ? LYS C 387 ARG C 389 5 ? 3  
HELX_P HELX_P88  AJ7 ASP C 390 ? VAL C 394 ? ASP C 390 VAL C 394 5 ? 5  
HELX_P HELX_P89  AJ8 SER C 408 ? ASP C 417 ? SER C 408 ASP C 417 1 ? 10 
HELX_P HELX_P90  AJ9 LYS C 418 ? VAL C 420 ? LYS C 418 VAL C 420 5 ? 3  
HELX_P HELX_P91  AK1 VAL C 430 ? GLY C 440 ? VAL C 430 GLY C 440 1 ? 11 
HELX_P HELX_P92  AK2 ASP C 459 ? ASN C 472 ? ASP C 459 ASN C 472 1 ? 14 
HELX_P HELX_P93  AK3 GLY C 480 ? GLY C 490 ? GLY C 480 GLY C 490 1 ? 11 
HELX_P HELX_P94  AK4 GLU C 495 ? ALA C 501 ? GLU C 495 ALA C 501 1 ? 7  
HELX_P HELX_P95  AK5 GLY C 502 ? ASP C 513 ? GLY C 502 ASP C 513 1 ? 12 
HELX_P HELX_P96  AK6 ASP C 525 ? GLY C 541 ? ASP C 525 GLY C 541 1 ? 17 
HELX_P HELX_P97  AK7 ASP C 543 ? LEU C 547 ? ASP C 543 LEU C 547 5 ? 5  
HELX_P HELX_P98  AK8 SER C 558 ? SER C 571 ? SER C 558 SER C 571 1 ? 14 
HELX_P HELX_P99  AK9 GLY C 586 ? ASN C 595 ? GLY C 586 ASN C 595 1 ? 10 
HELX_P HELX_P100 AL1 LYS C 596 ? GLY C 602 ? LYS C 596 GLY C 602 1 ? 7  
HELX_P HELX_P101 AL2 ASP C 610 ? GLY C 630 ? ASP C 610 GLY C 630 1 ? 21 
HELX_P HELX_P102 AL3 ASN D 2   ? GLY D 30  ? ASN D 2   GLY D 30  1 ? 29 
HELX_P HELX_P103 AL4 LEU D 44  ? GLY D 52  ? LEU D 44  GLY D 52  1 ? 9  
HELX_P HELX_P104 AL5 ASN D 57  ? ALA D 64  ? ASN D 57  ALA D 64  1 ? 8  
HELX_P HELX_P105 AL6 ALA D 64  ? ILE D 72  ? ALA D 64  ILE D 72  1 ? 9  
HELX_P HELX_P106 AL7 MET D 77  ? LEU D 102 ? MET D 77  LEU D 102 1 ? 26 
HELX_P HELX_P107 AL8 SER D 116 ? THR D 129 ? SER D 116 THR D 129 1 ? 14 
HELX_P HELX_P108 AL9 ASP D 144 ? GLY D 159 ? ASP D 144 GLY D 159 1 ? 16 
HELX_P HELX_P109 AM1 LYS D 167 ? GLY D 175 ? LYS D 167 GLY D 175 1 ? 9  
HELX_P HELX_P110 AM2 ASP D 191 ? SER D 194 ? ASP D 191 SER D 194 5 ? 4  
HELX_P HELX_P111 AM3 VAL D 195 ? PHE D 209 ? VAL D 195 PHE D 209 1 ? 15 
HELX_P HELX_P112 AM4 GLN D 216 ? VAL D 228 ? GLN D 216 VAL D 228 1 ? 13 
HELX_P HELX_P113 AM5 SER D 239 ? LEU D 252 ? SER D 239 LEU D 252 1 ? 14 
HELX_P HELX_P114 AM6 ASP D 274 ? ARG D 286 ? ASP D 274 ARG D 286 1 ? 13 
HELX_P HELX_P115 AM7 ALA D 302 ? GLU D 306 ? ALA D 302 GLU D 306 5 ? 5  
HELX_P HELX_P116 AM8 ASP D 349 ? ILE D 353 ? ASP D 349 ILE D 353 5 ? 5  
HELX_P HELX_P117 AM9 GLN D 374 ? ASP D 376 ? GLN D 374 ASP D 376 5 ? 3  
HELX_P HELX_P118 AN1 PHE D 377 ? ARG D 384 ? PHE D 377 ARG D 384 1 ? 8  
HELX_P HELX_P119 AN2 ARG D 384 ? TYR D 391 ? ARG D 384 TYR D 391 1 ? 8  
HELX_P HELX_P120 AN3 LYS D 410 ? GLY D 416 ? LYS D 410 GLY D 416 1 ? 7  
HELX_P HELX_P121 AN4 ARG D 418 ? GLU D 433 ? ARG D 418 GLU D 433 1 ? 16 
HELX_P HELX_P122 AN5 ASP D 448 ? TYR D 459 ? ASP D 448 TYR D 459 1 ? 12 
HELX_P HELX_P123 AN6 TYR D 459 ? ALA D 469 ? TYR D 459 ALA D 469 1 ? 11 
HELX_P HELX_P124 AN7 VAL D 475 ? VAL D 479 ? VAL D 475 VAL D 479 5 ? 5  
HELX_P HELX_P125 AN8 LEU D 487 ? PHE D 491 ? LEU D 487 PHE D 491 5 ? 5  
HELX_P HELX_P126 AN9 SER D 511 ? ASN D 522 ? SER D 511 ASN D 522 1 ? 12 
HELX_P HELX_P127 AO1 GLU D 544 ? SER D 554 ? GLU D 544 SER D 554 1 ? 11 
HELX_P HELX_P128 AO2 PRO D 585 ? ASN D 588 ? PRO D 585 ASN D 588 5 ? 4  
HELX_P HELX_P129 AO3 THR D 606 ? GLY D 615 ? THR D 606 GLY D 615 1 ? 10 
HELX_P HELX_P130 AO4 GLY D 627 ? ILE D 631 ? GLY D 627 ILE D 631 5 ? 5  
HELX_P HELX_P131 AO5 MET D 637 ? GLY D 644 ? MET D 637 GLY D 644 5 ? 8  
HELX_P HELX_P132 AO6 PRO D 650 ? VAL D 657 ? PRO D 650 VAL D 657 1 ? 8  
HELX_P HELX_P133 AO7 VAL D 657 ? LYS D 663 ? VAL D 657 LYS D 663 1 ? 7  
HELX_P HELX_P134 AO8 ASN D 673 ? ILE D 678 ? ASN D 673 ILE D 678 5 ? 6  
HELX_P HELX_P135 AO9 GLU D 686 ? GLY D 698 ? GLU D 686 GLY D 698 1 ? 13 
# 
_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 ? ? A ASP 39  OD1 ? ? ? 1_555 M  CA  .   CA  ? ? A ASP 39  A CA  809 1_555 ? ? ? ? ? ? ? 2.952 ? ? 
metalc2  metalc ? ? A GLU 75  OE1 ? ? ? 1_555 P  CA  .   CA  ? ? A GLU 75  A CA  812 1_555 ? ? ? ? ? ? ? 3.199 ? ? 
metalc3  metalc ? ? A GLU 174 OE2 A ? ? 1_555 N  CA  .   CA  ? ? A GLU 174 A CA  810 1_555 ? ? ? ? ? ? ? 2.798 ? ? 
metalc4  metalc ? ? A CYS 485 SG  ? ? ? 1_555 E  SF4 .   FE1 ? ? A CYS 485 A SF4 801 1_555 ? ? ? ? ? ? ? 2.548 ? ? 
metalc5  metalc ? ? A CYS 488 SG  ? ? ? 1_555 E  SF4 .   FE4 ? ? A CYS 488 A SF4 801 1_555 ? ? ? ? ? ? ? 2.407 ? ? 
metalc6  metalc ? ? A CYS 488 SG  ? ? ? 1_555 G  NI  .   NI  ? ? A CYS 488 A NI  803 1_555 ? ? ? ? ? ? ? 2.377 ? ? 
metalc7  metalc ? ? A CYS 507 SG  ? ? ? 1_555 E  SF4 .   FE3 ? ? A CYS 507 A SF4 801 1_555 ? ? ? ? ? ? ? 2.464 ? ? 
metalc8  metalc ? ? A CYS 574 SG  ? ? ? 1_555 F  NI  .   NI  ? ? A CYS 574 A NI  802 1_555 ? ? ? ? ? ? ? 2.275 ? ? 
metalc9  metalc ? ? A CYS 574 SG  ? ? ? 1_555 G  NI  .   NI  ? ? A CYS 574 A NI  803 1_555 ? ? ? ? ? ? ? 2.059 ? ? 
metalc10 metalc ? ? A GLY 575 N   ? ? ? 1_555 F  NI  .   NI  ? ? A GLY 575 A NI  802 1_555 ? ? ? ? ? ? ? 1.994 ? ? 
metalc11 metalc ? ? A CYS 576 N   ? ? ? 1_555 F  NI  .   NI  ? ? A CYS 576 A NI  802 1_555 ? ? ? ? ? ? ? 1.903 ? ? 
metalc12 metalc ? ? A CYS 576 SG  ? ? ? 1_555 F  NI  .   NI  ? ? A CYS 576 A NI  802 1_555 ? ? ? ? ? ? ? 2.694 ? ? 
metalc13 metalc ? ? A CYS 576 SG  ? ? ? 1_555 G  NI  .   NI  ? ? A CYS 576 A NI  803 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
metalc14 metalc ? ? M CA  .   CA  ? ? ? 1_555 BC HOH .   O   ? ? A CA  809 A HOH 902 1_555 ? ? ? ? ? ? ? 2.961 ? ? 
metalc15 metalc ? ? M CA  .   CA  ? ? ? 5_555 D  GLY 604 O   ? ? A CA  809 D GLY 604 1_555 ? ? ? ? ? ? ? 2.785 ? ? 
metalc16 metalc ? ? N CA  .   CA  ? ? ? 5_555 D  ASP 104 OD1 ? ? A CA  810 D ASP 104 1_555 ? ? ? ? ? ? ? 2.477 ? ? 
metalc17 metalc ? ? B CYS 38  SG  ? ? ? 1_555 AB SF4 .   FE1 ? ? B CYS 38  C SF4 701 1_555 ? ? ? ? ? ? ? 2.621 ? ? 
metalc18 metalc ? ? B CYS 46  SG  ? ? ? 1_555 AB SF4 .   FE4 ? ? B CYS 46  C SF4 701 1_555 ? ? ? ? ? ? ? 2.237 ? ? 
metalc19 metalc ? ? B CYS 47  SG  ? ? ? 1_555 Z  SF4 .   FE3 ? ? B CYS 47  B SF4 702 1_555 ? ? ? ? ? ? ? 2.442 ? ? 
metalc20 metalc ? ? B CYS 50  SG  ? ? ? 1_555 Z  SF4 .   FE4 ? ? B CYS 50  B SF4 702 1_555 ? ? ? ? ? ? ? 2.355 ? ? 
metalc21 metalc ? ? B CYS 55  SG  ? ? ? 1_555 Z  SF4 .   FE1 ? ? B CYS 55  B SF4 702 1_555 ? ? ? ? ? ? ? 2.220 ? ? 
metalc22 metalc ? ? B CYS 70  SG  ? ? ? 1_555 Z  SF4 .   FE2 ? ? B CYS 70  B SF4 702 1_555 ? ? ? ? ? ? ? 2.366 ? ? 
metalc23 metalc ? ? B GLU 226 OE2 ? ? ? 1_555 FA CA  .   CA  ? ? B GLU 226 B CA  708 1_555 ? ? ? ? ? ? ? 2.589 ? ? 
metalc24 metalc ? ? B HIS 259 NE2 ? ? ? 1_555 CA XCC .   FE2 ? ? B HIS 259 B XCC 705 1_555 ? ? ? ? ? ? ? 2.401 ? ? 
metalc25 metalc ? ? B CYS 295 SG  ? ? ? 1_555 CA XCC .   FE2 ? ? B CYS 295 B XCC 705 1_555 ? ? ? ? ? ? ? 2.232 ? ? 
metalc26 metalc ? ? B CYS 333 SG  ? ? ? 1_555 CA XCC .   FE1 ? ? B CYS 333 B XCC 705 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc27 metalc ? ? B CYS 451 SG  ? ? ? 1_555 CA XCC .   FE3 ? ? B CYS 451 B XCC 705 1_555 ? ? ? ? ? ? ? 2.209 ? ? 
metalc28 metalc ? ? B CYS 481 SG  ? ? ? 1_555 CA XCC .   FE4 ? ? B CYS 481 B XCC 705 1_555 ? ? ? ? ? ? ? 2.249 ? ? 
metalc29 metalc ? ? B CYS 523 SG  ? ? ? 1_555 CA XCC .   NI  ? ? B CYS 523 B XCC 705 1_555 ? ? ? ? ? ? ? 2.253 ? ? 
metalc30 metalc ? ? C CYS 38  SG  ? ? ? 1_555 AB SF4 .   FE3 ? ? C CYS 38  C SF4 701 1_555 ? ? ? ? ? ? ? 2.368 ? ? 
metalc31 metalc ? ? C CYS 46  SG  ? ? ? 1_555 AB SF4 .   FE2 ? ? C CYS 46  C SF4 701 1_555 ? ? ? ? ? ? ? 2.467 ? ? 
metalc32 metalc ? ? C CYS 50  SG  ? ? ? 1_555 BB SF4 .   FE1 ? ? C CYS 50  C SF4 702 1_555 ? ? ? ? ? ? ? 2.402 ? ? 
metalc33 metalc ? ? C CYS 55  SG  ? ? ? 1_555 BB SF4 .   FE3 ? ? C CYS 55  C SF4 702 1_555 ? ? ? ? ? ? ? 2.217 ? ? 
metalc34 metalc ? ? C GLU 226 OE1 ? ? ? 1_555 GB CA  .   CA  ? ? C GLU 226 C CA  707 1_555 ? ? ? ? ? ? ? 2.803 ? ? 
metalc35 metalc ? ? C ASP 239 OD1 ? ? ? 1_555 FB CA  .   CA  ? ? C ASP 239 C CA  706 1_555 ? ? ? ? ? ? ? 3.049 ? ? 
metalc36 metalc ? ? C HIS 259 NE2 ? ? ? 1_555 DB XCC .   FE2 ? ? C HIS 259 C XCC 704 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc37 metalc ? ? C CYS 295 SG  ? ? ? 1_555 DB XCC .   FE2 ? ? C CYS 295 C XCC 704 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc38 metalc ? ? C CYS 333 SG  ? ? ? 1_555 DB XCC .   FE1 ? ? C CYS 333 C XCC 704 1_555 ? ? ? ? ? ? ? 2.564 ? ? 
metalc39 metalc ? ? C GLU 365 O   ? ? ? 1_555 EB CA  .   CA  ? ? C GLU 365 C CA  705 1_555 ? ? ? ? ? ? ? 3.021 ? ? 
metalc40 metalc ? ? C SER 374 OG  ? ? ? 1_555 EB CA  .   CA  ? ? C SER 374 C CA  705 1_555 ? ? ? ? ? ? ? 3.081 ? ? 
metalc41 metalc ? ? C CYS 451 SG  ? ? ? 1_555 DB XCC .   FE3 ? ? C CYS 451 C XCC 704 1_555 ? ? ? ? ? ? ? 2.377 ? ? 
metalc42 metalc ? ? C CYS 481 SG  ? ? ? 1_555 DB XCC .   FE4 ? ? C CYS 481 C XCC 704 1_555 ? ? ? ? ? ? ? 2.597 ? ? 
metalc43 metalc ? ? D CYS 485 SG  ? ? ? 1_555 OB SF4 .   FE1 ? ? D CYS 485 D SF4 801 1_555 ? ? ? ? ? ? ? 2.307 ? ? 
metalc44 metalc ? ? D CYS 488 SG  ? ? ? 1_555 OB SF4 .   FE4 ? ? D CYS 488 D SF4 801 1_555 ? ? ? ? ? ? ? 2.198 ? ? 
metalc45 metalc ? ? D CYS 488 SG  ? ? ? 1_555 PB NI  .   NI  ? ? D CYS 488 D NI  802 1_555 ? ? ? ? ? ? ? 1.939 ? ? 
metalc46 metalc ? ? D SER 490 O   ? ? ? 1_555 WB CA  .   CA  ? ? D SER 490 D CA  809 1_555 ? ? ? ? ? ? ? 2.741 ? ? 
metalc47 metalc ? ? D CYS 497 SG  ? ? ? 1_555 OB SF4 .   FE2 ? ? D CYS 497 D SF4 801 1_555 ? ? ? ? ? ? ? 2.230 ? ? 
metalc48 metalc ? ? D CYS 507 SG  ? ? ? 1_555 OB SF4 .   FE3 ? ? D CYS 507 D SF4 801 1_555 ? ? ? ? ? ? ? 2.277 ? ? 
metalc49 metalc ? ? D CYS 574 SG  ? ? ? 1_555 PB NI  .   NI  ? ? D CYS 574 D NI  802 1_555 ? ? ? ? ? ? ? 2.267 ? ? 
metalc50 metalc ? ? D CYS 574 SG  ? ? ? 1_555 QB NI  .   NI  ? ? D CYS 574 D NI  803 1_555 ? ? ? ? ? ? ? 2.123 ? ? 
metalc51 metalc ? ? D GLY 575 N   ? ? ? 1_555 QB NI  .   NI  ? ? D GLY 575 D NI  803 1_555 ? ? ? ? ? ? ? 2.205 ? ? 
metalc52 metalc ? ? D CYS 576 SG  ? ? ? 1_555 PB NI  .   NI  ? ? D CYS 576 D NI  802 1_555 ? ? ? ? ? ? ? 2.200 ? ? 
metalc53 metalc ? ? D CYS 576 N   ? ? ? 1_555 QB NI  .   NI  ? ? D CYS 576 D NI  803 1_555 ? ? ? ? ? ? ? 1.867 ? ? 
metalc54 metalc ? ? D CYS 576 SG  ? ? ? 1_555 QB NI  .   NI  ? ? D CYS 576 D NI  803 1_555 ? ? ? ? ? ? ? 2.425 ? ? 
metalc55 metalc ? ? D ASP 705 OD1 ? ? ? 1_555 VB CA  .   CA  ? ? D ASP 705 D CA  808 1_555 ? ? ? ? ? ? ? 2.728 ? ? 
# 
_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   OD1 ? A  ASP 39  ? A ASP 39  ? 1_555 CA  ? M  CA  . ? A CA  809 ? 1_555 O   ? BC HOH .   ? A HOH 902 ? 1_555 53.3  ? 
2   OD1 ? A  ASP 39  ? A ASP 39  ? 1_555 CA  ? M  CA  . ? A CA  809 ? 1_555 O   ? D  GLY 604 ? D GLY 604 ? 1_555 31.5  ? 
3   O   ? BC HOH .   ? A HOH 902 ? 1_555 CA  ? M  CA  . ? A CA  809 ? 1_555 O   ? D  GLY 604 ? D GLY 604 ? 1_555 39.7  ? 
4   OE2 A A  GLU 174 ? A GLU 174 ? 1_555 CA  ? N  CA  . ? A CA  810 ? 1_555 OD1 ? D  ASP 104 ? D ASP 104 ? 1_555 85.8  ? 
5   SG  ? A  CYS 485 ? A CYS 485 ? 1_555 FE1 ? E  SF4 . ? A SF4 801 ? 1_555 S2  ? E  SF4 .   ? A SF4 801 ? 1_555 118.2 ? 
6   SG  ? A  CYS 485 ? A CYS 485 ? 1_555 FE1 ? E  SF4 . ? A SF4 801 ? 1_555 S3  ? E  SF4 .   ? A SF4 801 ? 1_555 90.3  ? 
7   S2  ? E  SF4 .   ? A SF4 801 ? 1_555 FE1 ? E  SF4 . ? A SF4 801 ? 1_555 S3  ? E  SF4 .   ? A SF4 801 ? 1_555 107.4 ? 
8   SG  ? A  CYS 485 ? A CYS 485 ? 1_555 FE1 ? E  SF4 . ? A SF4 801 ? 1_555 S4  ? E  SF4 .   ? A SF4 801 ? 1_555 123.9 ? 
9   S2  ? E  SF4 .   ? A SF4 801 ? 1_555 FE1 ? E  SF4 . ? A SF4 801 ? 1_555 S4  ? E  SF4 .   ? A SF4 801 ? 1_555 106.5 ? 
10  S3  ? E  SF4 .   ? A SF4 801 ? 1_555 FE1 ? E  SF4 . ? A SF4 801 ? 1_555 S4  ? E  SF4 .   ? A SF4 801 ? 1_555 107.7 ? 
11  SG  ? A  CYS 488 ? A CYS 488 ? 1_555 FE4 ? E  SF4 . ? A SF4 801 ? 1_555 S1  ? E  SF4 .   ? A SF4 801 ? 1_555 110.8 ? 
12  SG  ? A  CYS 488 ? A CYS 488 ? 1_555 FE4 ? E  SF4 . ? A SF4 801 ? 1_555 S2  ? E  SF4 .   ? A SF4 801 ? 1_555 114.7 ? 
13  S1  ? E  SF4 .   ? A SF4 801 ? 1_555 FE4 ? E  SF4 . ? A SF4 801 ? 1_555 S2  ? E  SF4 .   ? A SF4 801 ? 1_555 106.4 ? 
14  SG  ? A  CYS 488 ? A CYS 488 ? 1_555 FE4 ? E  SF4 . ? A SF4 801 ? 1_555 S3  ? E  SF4 .   ? A SF4 801 ? 1_555 110.0 ? 
15  S1  ? E  SF4 .   ? A SF4 801 ? 1_555 FE4 ? E  SF4 . ? A SF4 801 ? 1_555 S3  ? E  SF4 .   ? A SF4 801 ? 1_555 106.9 ? 
16  S2  ? E  SF4 .   ? A SF4 801 ? 1_555 FE4 ? E  SF4 . ? A SF4 801 ? 1_555 S3  ? E  SF4 .   ? A SF4 801 ? 1_555 107.7 ? 
17  SG  ? A  CYS 488 ? A CYS 488 ? 1_555 NI  ? G  NI  . ? A NI  803 ? 1_555 SG  ? A  CYS 574 ? A CYS 574 ? 1_555 115.0 ? 
18  SG  ? A  CYS 488 ? A CYS 488 ? 1_555 NI  ? G  NI  . ? A NI  803 ? 1_555 SG  ? A  CYS 576 ? A CYS 576 ? 1_555 129.7 ? 
19  SG  ? A  CYS 574 ? A CYS 574 ? 1_555 NI  ? G  NI  . ? A NI  803 ? 1_555 SG  ? A  CYS 576 ? A CYS 576 ? 1_555 114.5 ? 
20  SG  ? A  CYS 507 ? A CYS 507 ? 1_555 FE3 ? E  SF4 . ? A SF4 801 ? 1_555 S1  ? E  SF4 .   ? A SF4 801 ? 1_555 101.2 ? 
21  SG  ? A  CYS 507 ? A CYS 507 ? 1_555 FE3 ? E  SF4 . ? A SF4 801 ? 1_555 S2  ? E  SF4 .   ? A SF4 801 ? 1_555 110.7 ? 
22  S1  ? E  SF4 .   ? A SF4 801 ? 1_555 FE3 ? E  SF4 . ? A SF4 801 ? 1_555 S2  ? E  SF4 .   ? A SF4 801 ? 1_555 106.6 ? 
23  SG  ? A  CYS 507 ? A CYS 507 ? 1_555 FE3 ? E  SF4 . ? A SF4 801 ? 1_555 S4  ? E  SF4 .   ? A SF4 801 ? 1_555 123.6 ? 
24  S1  ? E  SF4 .   ? A SF4 801 ? 1_555 FE3 ? E  SF4 . ? A SF4 801 ? 1_555 S4  ? E  SF4 .   ? A SF4 801 ? 1_555 106.4 ? 
25  S2  ? E  SF4 .   ? A SF4 801 ? 1_555 FE3 ? E  SF4 . ? A SF4 801 ? 1_555 S4  ? E  SF4 .   ? A SF4 801 ? 1_555 107.1 ? 
26  SG  ? A  CYS 574 ? A CYS 574 ? 1_555 NI  ? F  NI  . ? A NI  802 ? 1_555 N   ? A  GLY 575 ? A GLY 575 ? 1_555 100.9 ? 
27  SG  ? A  CYS 574 ? A CYS 574 ? 1_555 NI  ? F  NI  . ? A NI  802 ? 1_555 N   ? A  CYS 576 ? A CYS 576 ? 1_555 168.9 ? 
28  N   ? A  GLY 575 ? A GLY 575 ? 1_555 NI  ? F  NI  . ? A NI  802 ? 1_555 N   ? A  CYS 576 ? A CYS 576 ? 1_555 90.1  ? 
29  SG  ? A  CYS 574 ? A CYS 574 ? 1_555 NI  ? F  NI  . ? A NI  802 ? 1_555 SG  ? A  CYS 576 ? A CYS 576 ? 1_555 87.6  ? 
30  N   ? A  GLY 575 ? A GLY 575 ? 1_555 NI  ? F  NI  . ? A NI  802 ? 1_555 SG  ? A  CYS 576 ? A CYS 576 ? 1_555 161.1 ? 
31  N   ? A  CYS 576 ? A CYS 576 ? 1_555 NI  ? F  NI  . ? A NI  802 ? 1_555 SG  ? A  CYS 576 ? A CYS 576 ? 1_555 81.4  ? 
32  SG  ? B  CYS 38  ? B CYS 38  ? 1_555 FE1 ? AB SF4 . ? C SF4 701 ? 1_555 S2  ? AB SF4 .   ? C SF4 701 ? 1_555 104.4 ? 
33  SG  ? B  CYS 38  ? B CYS 38  ? 1_555 FE1 ? AB SF4 . ? C SF4 701 ? 1_555 S3  ? AB SF4 .   ? C SF4 701 ? 1_555 118.2 ? 
34  S2  ? AB SF4 .   ? C SF4 701 ? 1_555 FE1 ? AB SF4 . ? C SF4 701 ? 1_555 S3  ? AB SF4 .   ? C SF4 701 ? 1_555 106.7 ? 
35  SG  ? B  CYS 38  ? B CYS 38  ? 1_555 FE1 ? AB SF4 . ? C SF4 701 ? 1_555 S4  ? AB SF4 .   ? C SF4 701 ? 1_555 112.3 ? 
36  S2  ? AB SF4 .   ? C SF4 701 ? 1_555 FE1 ? AB SF4 . ? C SF4 701 ? 1_555 S4  ? AB SF4 .   ? C SF4 701 ? 1_555 106.9 ? 
37  S3  ? AB SF4 .   ? C SF4 701 ? 1_555 FE1 ? AB SF4 . ? C SF4 701 ? 1_555 S4  ? AB SF4 .   ? C SF4 701 ? 1_555 107.5 ? 
38  SG  ? B  CYS 46  ? B CYS 46  ? 1_555 FE4 ? AB SF4 . ? C SF4 701 ? 1_555 S1  ? AB SF4 .   ? C SF4 701 ? 1_555 110.5 ? 
39  SG  ? B  CYS 46  ? B CYS 46  ? 1_555 FE4 ? AB SF4 . ? C SF4 701 ? 1_555 S2  ? AB SF4 .   ? C SF4 701 ? 1_555 117.9 ? 
40  S1  ? AB SF4 .   ? C SF4 701 ? 1_555 FE4 ? AB SF4 . ? C SF4 701 ? 1_555 S2  ? AB SF4 .   ? C SF4 701 ? 1_555 107.0 ? 
41  SG  ? B  CYS 46  ? B CYS 46  ? 1_555 FE4 ? AB SF4 . ? C SF4 701 ? 1_555 S3  ? AB SF4 .   ? C SF4 701 ? 1_555 105.7 ? 
42  S1  ? AB SF4 .   ? C SF4 701 ? 1_555 FE4 ? AB SF4 . ? C SF4 701 ? 1_555 S3  ? AB SF4 .   ? C SF4 701 ? 1_555 108.2 ? 
43  S2  ? AB SF4 .   ? C SF4 701 ? 1_555 FE4 ? AB SF4 . ? C SF4 701 ? 1_555 S3  ? AB SF4 .   ? C SF4 701 ? 1_555 107.2 ? 
44  SG  ? B  CYS 47  ? B CYS 47  ? 1_555 FE3 ? Z  SF4 . ? B SF4 702 ? 1_555 S1  ? Z  SF4 .   ? B SF4 702 ? 1_555 86.7  ? 
45  SG  ? B  CYS 47  ? B CYS 47  ? 1_555 FE3 ? Z  SF4 . ? B SF4 702 ? 1_555 S2  ? Z  SF4 .   ? B SF4 702 ? 1_555 125.0 ? 
46  S1  ? Z  SF4 .   ? B SF4 702 ? 1_555 FE3 ? Z  SF4 . ? B SF4 702 ? 1_555 S2  ? Z  SF4 .   ? B SF4 702 ? 1_555 107.9 ? 
47  SG  ? B  CYS 47  ? B CYS 47  ? 1_555 FE3 ? Z  SF4 . ? B SF4 702 ? 1_555 S4  ? Z  SF4 .   ? B SF4 702 ? 1_555 119.4 ? 
48  S1  ? Z  SF4 .   ? B SF4 702 ? 1_555 FE3 ? Z  SF4 . ? B SF4 702 ? 1_555 S4  ? Z  SF4 .   ? B SF4 702 ? 1_555 105.5 ? 
49  S2  ? Z  SF4 .   ? B SF4 702 ? 1_555 FE3 ? Z  SF4 . ? B SF4 702 ? 1_555 S4  ? Z  SF4 .   ? B SF4 702 ? 1_555 107.5 ? 
50  SG  ? B  CYS 50  ? B CYS 50  ? 1_555 FE4 ? Z  SF4 . ? B SF4 702 ? 1_555 S1  ? Z  SF4 .   ? B SF4 702 ? 1_555 137.6 ? 
51  SG  ? B  CYS 50  ? B CYS 50  ? 1_555 FE4 ? Z  SF4 . ? B SF4 702 ? 1_555 S2  ? Z  SF4 .   ? B SF4 702 ? 1_555 103.0 ? 
52  S1  ? Z  SF4 .   ? B SF4 702 ? 1_555 FE4 ? Z  SF4 . ? B SF4 702 ? 1_555 S2  ? Z  SF4 .   ? B SF4 702 ? 1_555 108.0 ? 
53  SG  ? B  CYS 50  ? B CYS 50  ? 1_555 FE4 ? Z  SF4 . ? B SF4 702 ? 1_555 S3  ? Z  SF4 .   ? B SF4 702 ? 1_555 91.4  ? 
54  S1  ? Z  SF4 .   ? B SF4 702 ? 1_555 FE4 ? Z  SF4 . ? B SF4 702 ? 1_555 S3  ? Z  SF4 .   ? B SF4 702 ? 1_555 106.3 ? 
55  S2  ? Z  SF4 .   ? B SF4 702 ? 1_555 FE4 ? Z  SF4 . ? B SF4 702 ? 1_555 S3  ? Z  SF4 .   ? B SF4 702 ? 1_555 106.6 ? 
56  SG  ? B  CYS 55  ? B CYS 55  ? 1_555 FE1 ? Z  SF4 . ? B SF4 702 ? 1_555 S2  ? Z  SF4 .   ? B SF4 702 ? 1_555 100.3 ? 
57  SG  ? B  CYS 55  ? B CYS 55  ? 1_555 FE1 ? Z  SF4 . ? B SF4 702 ? 1_555 S3  ? Z  SF4 .   ? B SF4 702 ? 1_555 141.7 ? 
58  S2  ? Z  SF4 .   ? B SF4 702 ? 1_555 FE1 ? Z  SF4 . ? B SF4 702 ? 1_555 S3  ? Z  SF4 .   ? B SF4 702 ? 1_555 106.2 ? 
59  SG  ? B  CYS 55  ? B CYS 55  ? 1_555 FE1 ? Z  SF4 . ? B SF4 702 ? 1_555 S4  ? Z  SF4 .   ? B SF4 702 ? 1_555 91.2  ? 
60  S2  ? Z  SF4 .   ? B SF4 702 ? 1_555 FE1 ? Z  SF4 . ? B SF4 702 ? 1_555 S4  ? Z  SF4 .   ? B SF4 702 ? 1_555 106.6 ? 
61  S3  ? Z  SF4 .   ? B SF4 702 ? 1_555 FE1 ? Z  SF4 . ? B SF4 702 ? 1_555 S4  ? Z  SF4 .   ? B SF4 702 ? 1_555 106.6 ? 
62  SG  ? B  CYS 70  ? B CYS 70  ? 1_555 FE2 ? Z  SF4 . ? B SF4 702 ? 1_555 S1  ? Z  SF4 .   ? B SF4 702 ? 1_555 108.5 ? 
63  SG  ? B  CYS 70  ? B CYS 70  ? 1_555 FE2 ? Z  SF4 . ? B SF4 702 ? 1_555 S3  ? Z  SF4 .   ? B SF4 702 ? 1_555 93.3  ? 
64  S1  ? Z  SF4 .   ? B SF4 702 ? 1_555 FE2 ? Z  SF4 . ? B SF4 702 ? 1_555 S3  ? Z  SF4 .   ? B SF4 702 ? 1_555 105.9 ? 
65  SG  ? B  CYS 70  ? B CYS 70  ? 1_555 FE2 ? Z  SF4 . ? B SF4 702 ? 1_555 S4  ? Z  SF4 .   ? B SF4 702 ? 1_555 133.1 ? 
66  S1  ? Z  SF4 .   ? B SF4 702 ? 1_555 FE2 ? Z  SF4 . ? B SF4 702 ? 1_555 S4  ? Z  SF4 .   ? B SF4 702 ? 1_555 106.1 ? 
67  S3  ? Z  SF4 .   ? B SF4 702 ? 1_555 FE2 ? Z  SF4 . ? B SF4 702 ? 1_555 S4  ? Z  SF4 .   ? B SF4 702 ? 1_555 106.7 ? 
68  NE2 ? B  HIS 259 ? B HIS 259 ? 1_555 FE2 ? CA XCC . ? B XCC 705 ? 1_555 S3  ? CA XCC .   ? B XCC 705 ? 1_555 85.0  ? 
69  NE2 ? B  HIS 259 ? B HIS 259 ? 1_555 FE2 ? CA XCC . ? B XCC 705 ? 1_555 SG  ? B  CYS 295 ? B CYS 295 ? 1_555 103.0 ? 
70  S3  ? CA XCC .   ? B XCC 705 ? 1_555 FE2 ? CA XCC . ? B XCC 705 ? 1_555 SG  ? B  CYS 295 ? B CYS 295 ? 1_555 146.1 ? 
71  SG  ? B  CYS 333 ? B CYS 333 ? 1_555 FE1 ? CA XCC . ? B XCC 705 ? 1_555 S2  ? CA XCC .   ? B XCC 705 ? 1_555 138.8 ? 
72  SG  ? B  CYS 333 ? B CYS 333 ? 1_555 FE1 ? CA XCC . ? B XCC 705 ? 1_555 S4  ? CA XCC .   ? B XCC 705 ? 1_555 121.6 ? 
73  S2  ? CA XCC .   ? B XCC 705 ? 1_555 FE1 ? CA XCC . ? B XCC 705 ? 1_555 S4  ? CA XCC .   ? B XCC 705 ? 1_555 83.9  ? 
74  SG  ? B  CYS 333 ? B CYS 333 ? 1_555 FE1 ? CA XCC . ? B XCC 705 ? 1_555 S3  ? CA XCC .   ? B XCC 705 ? 1_555 124.7 ? 
75  S2  ? CA XCC .   ? B XCC 705 ? 1_555 FE1 ? CA XCC . ? B XCC 705 ? 1_555 S3  ? CA XCC .   ? B XCC 705 ? 1_555 78.3  ? 
76  S4  ? CA XCC .   ? B XCC 705 ? 1_555 FE1 ? CA XCC . ? B XCC 705 ? 1_555 S3  ? CA XCC .   ? B XCC 705 ? 1_555 95.6  ? 
77  SG  ? B  CYS 451 ? B CYS 451 ? 1_555 FE3 ? CA XCC . ? B XCC 705 ? 1_555 S1  ? CA XCC .   ? B XCC 705 ? 1_555 136.8 ? 
78  SG  ? B  CYS 451 ? B CYS 451 ? 1_555 FE3 ? CA XCC . ? B XCC 705 ? 1_555 S2  ? CA XCC .   ? B XCC 705 ? 1_555 125.4 ? 
79  S1  ? CA XCC .   ? B XCC 705 ? 1_555 FE3 ? CA XCC . ? B XCC 705 ? 1_555 S2  ? CA XCC .   ? B XCC 705 ? 1_555 78.8  ? 
80  SG  ? B  CYS 451 ? B CYS 451 ? 1_555 FE3 ? CA XCC . ? B XCC 705 ? 1_555 S4  ? CA XCC .   ? B XCC 705 ? 1_555 127.5 ? 
81  S1  ? CA XCC .   ? B XCC 705 ? 1_555 FE3 ? CA XCC . ? B XCC 705 ? 1_555 S4  ? CA XCC .   ? B XCC 705 ? 1_555 85.8  ? 
82  S2  ? CA XCC .   ? B XCC 705 ? 1_555 FE3 ? CA XCC . ? B XCC 705 ? 1_555 S4  ? CA XCC .   ? B XCC 705 ? 1_555 84.3  ? 
83  SG  ? B  CYS 481 ? B CYS 481 ? 1_555 FE4 ? CA XCC . ? B XCC 705 ? 1_555 S1  ? CA XCC .   ? B XCC 705 ? 1_555 117.3 ? 
84  SG  ? B  CYS 481 ? B CYS 481 ? 1_555 FE4 ? CA XCC . ? B XCC 705 ? 1_555 S2  ? CA XCC .   ? B XCC 705 ? 1_555 121.7 ? 
85  S1  ? CA XCC .   ? B XCC 705 ? 1_555 FE4 ? CA XCC . ? B XCC 705 ? 1_555 S2  ? CA XCC .   ? B XCC 705 ? 1_555 77.7  ? 
86  SG  ? B  CYS 481 ? B CYS 481 ? 1_555 FE4 ? CA XCC . ? B XCC 705 ? 1_555 S3  ? CA XCC .   ? B XCC 705 ? 1_555 144.3 ? 
87  S1  ? CA XCC .   ? B XCC 705 ? 1_555 FE4 ? CA XCC . ? B XCC 705 ? 1_555 S3  ? CA XCC .   ? B XCC 705 ? 1_555 94.7  ? 
88  S2  ? CA XCC .   ? B XCC 705 ? 1_555 FE4 ? CA XCC . ? B XCC 705 ? 1_555 S3  ? CA XCC .   ? B XCC 705 ? 1_555 78.0  ? 
89  SG  ? B  CYS 523 ? B CYS 523 ? 1_555 NI  ? CA XCC . ? B XCC 705 ? 1_555 S1  ? CA XCC .   ? B XCC 705 ? 1_555 123.4 ? 
90  SG  ? C  CYS 38  ? C CYS 38  ? 1_555 FE3 ? AB SF4 . ? C SF4 701 ? 1_555 S1  ? AB SF4 .   ? C SF4 701 ? 1_555 112.5 ? 
91  SG  ? C  CYS 38  ? C CYS 38  ? 1_555 FE3 ? AB SF4 . ? C SF4 701 ? 1_555 S2  ? AB SF4 .   ? C SF4 701 ? 1_555 115.6 ? 
92  S1  ? AB SF4 .   ? C SF4 701 ? 1_555 FE3 ? AB SF4 . ? C SF4 701 ? 1_555 S2  ? AB SF4 .   ? C SF4 701 ? 1_555 106.3 ? 
93  SG  ? C  CYS 38  ? C CYS 38  ? 1_555 FE3 ? AB SF4 . ? C SF4 701 ? 1_555 S4  ? AB SF4 .   ? C SF4 701 ? 1_555 108.6 ? 
94  S1  ? AB SF4 .   ? C SF4 701 ? 1_555 FE3 ? AB SF4 . ? C SF4 701 ? 1_555 S4  ? AB SF4 .   ? C SF4 701 ? 1_555 106.5 ? 
95  S2  ? AB SF4 .   ? C SF4 701 ? 1_555 FE3 ? AB SF4 . ? C SF4 701 ? 1_555 S4  ? AB SF4 .   ? C SF4 701 ? 1_555 106.9 ? 
96  SG  ? C  CYS 46  ? C CYS 46  ? 1_555 FE2 ? AB SF4 . ? C SF4 701 ? 1_555 S1  ? AB SF4 .   ? C SF4 701 ? 1_555 114.7 ? 
97  SG  ? C  CYS 46  ? C CYS 46  ? 1_555 FE2 ? AB SF4 . ? C SF4 701 ? 1_555 S3  ? AB SF4 .   ? C SF4 701 ? 1_555 108.4 ? 
98  S1  ? AB SF4 .   ? C SF4 701 ? 1_555 FE2 ? AB SF4 . ? C SF4 701 ? 1_555 S3  ? AB SF4 .   ? C SF4 701 ? 1_555 107.7 ? 
99  SG  ? C  CYS 46  ? C CYS 46  ? 1_555 FE2 ? AB SF4 . ? C SF4 701 ? 1_555 S4  ? AB SF4 .   ? C SF4 701 ? 1_555 112.0 ? 
100 S1  ? AB SF4 .   ? C SF4 701 ? 1_555 FE2 ? AB SF4 . ? C SF4 701 ? 1_555 S4  ? AB SF4 .   ? C SF4 701 ? 1_555 106.2 ? 
101 S3  ? AB SF4 .   ? C SF4 701 ? 1_555 FE2 ? AB SF4 . ? C SF4 701 ? 1_555 S4  ? AB SF4 .   ? C SF4 701 ? 1_555 107.4 ? 
102 SG  ? C  CYS 50  ? C CYS 50  ? 1_555 FE1 ? BB SF4 . ? C SF4 702 ? 1_555 S2  ? BB SF4 .   ? C SF4 702 ? 1_555 110.8 ? 
103 SG  ? C  CYS 50  ? C CYS 50  ? 1_555 FE1 ? BB SF4 . ? C SF4 702 ? 1_555 S3  ? BB SF4 .   ? C SF4 702 ? 1_555 107.8 ? 
104 S2  ? BB SF4 .   ? C SF4 702 ? 1_555 FE1 ? BB SF4 . ? C SF4 702 ? 1_555 S3  ? BB SF4 .   ? C SF4 702 ? 1_555 106.6 ? 
105 SG  ? C  CYS 50  ? C CYS 50  ? 1_555 FE1 ? BB SF4 . ? C SF4 702 ? 1_555 S4  ? BB SF4 .   ? C SF4 702 ? 1_555 117.2 ? 
106 S2  ? BB SF4 .   ? C SF4 702 ? 1_555 FE1 ? BB SF4 . ? C SF4 702 ? 1_555 S4  ? BB SF4 .   ? C SF4 702 ? 1_555 107.7 ? 
107 S3  ? BB SF4 .   ? C SF4 702 ? 1_555 FE1 ? BB SF4 . ? C SF4 702 ? 1_555 S4  ? BB SF4 .   ? C SF4 702 ? 1_555 106.1 ? 
108 SG  ? C  CYS 55  ? C CYS 55  ? 1_555 FE3 ? BB SF4 . ? C SF4 702 ? 1_555 S1  ? BB SF4 .   ? C SF4 702 ? 1_555 109.2 ? 
109 SG  ? C  CYS 55  ? C CYS 55  ? 1_555 FE3 ? BB SF4 . ? C SF4 702 ? 1_555 S2  ? BB SF4 .   ? C SF4 702 ? 1_555 119.4 ? 
110 S1  ? BB SF4 .   ? C SF4 702 ? 1_555 FE3 ? BB SF4 . ? C SF4 702 ? 1_555 S2  ? BB SF4 .   ? C SF4 702 ? 1_555 106.6 ? 
111 SG  ? C  CYS 55  ? C CYS 55  ? 1_555 FE3 ? BB SF4 . ? C SF4 702 ? 1_555 S4  ? BB SF4 .   ? C SF4 702 ? 1_555 108.3 ? 
112 S1  ? BB SF4 .   ? C SF4 702 ? 1_555 FE3 ? BB SF4 . ? C SF4 702 ? 1_555 S4  ? BB SF4 .   ? C SF4 702 ? 1_555 105.5 ? 
113 S2  ? BB SF4 .   ? C SF4 702 ? 1_555 FE3 ? BB SF4 . ? C SF4 702 ? 1_555 S4  ? BB SF4 .   ? C SF4 702 ? 1_555 107.1 ? 
114 NE2 ? C  HIS 259 ? C HIS 259 ? 1_555 FE2 ? DB XCC . ? C XCC 704 ? 1_555 S3  ? DB XCC .   ? C XCC 704 ? 1_555 87.2  ? 
115 NE2 ? C  HIS 259 ? C HIS 259 ? 1_555 FE2 ? DB XCC . ? C XCC 704 ? 1_555 SG  ? C  CYS 295 ? C CYS 295 ? 1_555 89.1  ? 
116 S3  ? DB XCC .   ? C XCC 704 ? 1_555 FE2 ? DB XCC . ? C XCC 704 ? 1_555 SG  ? C  CYS 295 ? C CYS 295 ? 1_555 174.3 ? 
117 SG  ? C  CYS 333 ? C CYS 333 ? 1_555 FE1 ? DB XCC . ? C XCC 704 ? 1_555 S2  ? DB XCC .   ? C XCC 704 ? 1_555 99.9  ? 
118 SG  ? C  CYS 333 ? C CYS 333 ? 1_555 FE1 ? DB XCC . ? C XCC 704 ? 1_555 S4  ? DB XCC .   ? C XCC 704 ? 1_555 178.7 ? 
119 S2  ? DB XCC .   ? C XCC 704 ? 1_555 FE1 ? DB XCC . ? C XCC 704 ? 1_555 S4  ? DB XCC .   ? C XCC 704 ? 1_555 79.3  ? 
120 SG  ? C  CYS 333 ? C CYS 333 ? 1_555 FE1 ? DB XCC . ? C XCC 704 ? 1_555 S3  ? DB XCC .   ? C XCC 704 ? 1_555 74.6  ? 
121 S2  ? DB XCC .   ? C XCC 704 ? 1_555 FE1 ? DB XCC . ? C XCC 704 ? 1_555 S3  ? DB XCC .   ? C XCC 704 ? 1_555 79.1  ? 
122 S4  ? DB XCC .   ? C XCC 704 ? 1_555 FE1 ? DB XCC . ? C XCC 704 ? 1_555 S3  ? DB XCC .   ? C XCC 704 ? 1_555 106.1 ? 
123 O   ? C  GLU 365 ? C GLU 365 ? 1_555 CA  ? EB CA  . ? C CA  705 ? 1_555 OG  ? C  SER 374 ? C SER 374 ? 1_555 68.4  ? 
124 SG  ? C  CYS 451 ? C CYS 451 ? 1_555 FE3 ? DB XCC . ? C XCC 704 ? 1_555 S1  ? DB XCC .   ? C XCC 704 ? 1_555 153.6 ? 
125 SG  ? C  CYS 451 ? C CYS 451 ? 1_555 FE3 ? DB XCC . ? C XCC 704 ? 1_555 S2  ? DB XCC .   ? C XCC 704 ? 1_555 100.2 ? 
126 S1  ? DB XCC .   ? C XCC 704 ? 1_555 FE3 ? DB XCC . ? C XCC 704 ? 1_555 S2  ? DB XCC .   ? C XCC 704 ? 1_555 69.8  ? 
127 SG  ? C  CYS 451 ? C CYS 451 ? 1_555 FE3 ? DB XCC . ? C XCC 704 ? 1_555 S4  ? DB XCC .   ? C XCC 704 ? 1_555 118.8 ? 
128 S1  ? DB XCC .   ? C XCC 704 ? 1_555 FE3 ? DB XCC . ? C XCC 704 ? 1_555 S4  ? DB XCC .   ? C XCC 704 ? 1_555 83.9  ? 
129 S2  ? DB XCC .   ? C XCC 704 ? 1_555 FE3 ? DB XCC . ? C XCC 704 ? 1_555 S4  ? DB XCC .   ? C XCC 704 ? 1_555 78.0  ? 
130 SG  ? C  CYS 481 ? C CYS 481 ? 1_555 FE4 ? DB XCC . ? C XCC 704 ? 1_555 S1  ? DB XCC .   ? C XCC 704 ? 1_555 82.4  ? 
131 SG  ? C  CYS 481 ? C CYS 481 ? 1_555 FE4 ? DB XCC . ? C XCC 704 ? 1_555 S2  ? DB XCC .   ? C XCC 704 ? 1_555 128.4 ? 
132 S1  ? DB XCC .   ? C XCC 704 ? 1_555 FE4 ? DB XCC . ? C XCC 704 ? 1_555 S2  ? DB XCC .   ? C XCC 704 ? 1_555 70.0  ? 
133 SG  ? C  CYS 481 ? C CYS 481 ? 1_555 FE4 ? DB XCC . ? C XCC 704 ? 1_555 S3  ? DB XCC .   ? C XCC 704 ? 1_555 148.6 ? 
134 S1  ? DB XCC .   ? C XCC 704 ? 1_555 FE4 ? DB XCC . ? C XCC 704 ? 1_555 S3  ? DB XCC .   ? C XCC 704 ? 1_555 96.8  ? 
135 S2  ? DB XCC .   ? C XCC 704 ? 1_555 FE4 ? DB XCC . ? C XCC 704 ? 1_555 S3  ? DB XCC .   ? C XCC 704 ? 1_555 79.3  ? 
136 SG  ? D  CYS 485 ? D CYS 485 ? 1_555 FE1 ? OB SF4 . ? D SF4 801 ? 1_555 S2  ? OB SF4 .   ? D SF4 801 ? 1_555 128.5 ? 
137 SG  ? D  CYS 485 ? D CYS 485 ? 1_555 FE1 ? OB SF4 . ? D SF4 801 ? 1_555 S3  ? OB SF4 .   ? D SF4 801 ? 1_555 98.7  ? 
138 S2  ? OB SF4 .   ? D SF4 801 ? 1_555 FE1 ? OB SF4 . ? D SF4 801 ? 1_555 S3  ? OB SF4 .   ? D SF4 801 ? 1_555 106.8 ? 
139 SG  ? D  CYS 485 ? D CYS 485 ? 1_555 FE1 ? OB SF4 . ? D SF4 801 ? 1_555 S4  ? OB SF4 .   ? D SF4 801 ? 1_555 108.3 ? 
140 S2  ? OB SF4 .   ? D SF4 801 ? 1_555 FE1 ? OB SF4 . ? D SF4 801 ? 1_555 S4  ? OB SF4 .   ? D SF4 801 ? 1_555 106.3 ? 
141 S3  ? OB SF4 .   ? D SF4 801 ? 1_555 FE1 ? OB SF4 . ? D SF4 801 ? 1_555 S4  ? OB SF4 .   ? D SF4 801 ? 1_555 106.2 ? 
142 SG  ? D  CYS 488 ? D CYS 488 ? 1_555 FE4 ? OB SF4 . ? D SF4 801 ? 1_555 S1  ? OB SF4 .   ? D SF4 801 ? 1_555 113.4 ? 
143 SG  ? D  CYS 488 ? D CYS 488 ? 1_555 FE4 ? OB SF4 . ? D SF4 801 ? 1_555 S2  ? OB SF4 .   ? D SF4 801 ? 1_555 115.0 ? 
144 S1  ? OB SF4 .   ? D SF4 801 ? 1_555 FE4 ? OB SF4 . ? D SF4 801 ? 1_555 S2  ? OB SF4 .   ? D SF4 801 ? 1_555 107.5 ? 
145 SG  ? D  CYS 488 ? D CYS 488 ? 1_555 FE4 ? OB SF4 . ? D SF4 801 ? 1_555 S3  ? OB SF4 .   ? D SF4 801 ? 1_555 106.8 ? 
146 S1  ? OB SF4 .   ? D SF4 801 ? 1_555 FE4 ? OB SF4 . ? D SF4 801 ? 1_555 S3  ? OB SF4 .   ? D SF4 801 ? 1_555 106.8 ? 
147 S2  ? OB SF4 .   ? D SF4 801 ? 1_555 FE4 ? OB SF4 . ? D SF4 801 ? 1_555 S3  ? OB SF4 .   ? D SF4 801 ? 1_555 106.8 ? 
148 SG  ? D  CYS 488 ? D CYS 488 ? 1_555 NI  ? PB NI  . ? D NI  802 ? 1_555 SG  ? D  CYS 574 ? D CYS 574 ? 1_555 127.2 ? 
149 SG  ? D  CYS 488 ? D CYS 488 ? 1_555 NI  ? PB NI  . ? D NI  802 ? 1_555 SG  ? D  CYS 576 ? D CYS 576 ? 1_555 133.9 ? 
150 SG  ? D  CYS 574 ? D CYS 574 ? 1_555 NI  ? PB NI  . ? D NI  802 ? 1_555 SG  ? D  CYS 576 ? D CYS 576 ? 1_555 96.0  ? 
151 SG  ? D  CYS 497 ? D CYS 497 ? 1_555 FE2 ? OB SF4 . ? D SF4 801 ? 1_555 S1  ? OB SF4 .   ? D SF4 801 ? 1_555 106.2 ? 
152 SG  ? D  CYS 497 ? D CYS 497 ? 1_555 FE2 ? OB SF4 . ? D SF4 801 ? 1_555 S3  ? OB SF4 .   ? D SF4 801 ? 1_555 121.0 ? 
153 S1  ? OB SF4 .   ? D SF4 801 ? 1_555 FE2 ? OB SF4 . ? D SF4 801 ? 1_555 S3  ? OB SF4 .   ? D SF4 801 ? 1_555 106.7 ? 
154 SG  ? D  CYS 497 ? D CYS 497 ? 1_555 FE2 ? OB SF4 . ? D SF4 801 ? 1_555 S4  ? OB SF4 .   ? D SF4 801 ? 1_555 109.6 ? 
155 S1  ? OB SF4 .   ? D SF4 801 ? 1_555 FE2 ? OB SF4 . ? D SF4 801 ? 1_555 S4  ? OB SF4 .   ? D SF4 801 ? 1_555 105.8 ? 
156 S3  ? OB SF4 .   ? D SF4 801 ? 1_555 FE2 ? OB SF4 . ? D SF4 801 ? 1_555 S4  ? OB SF4 .   ? D SF4 801 ? 1_555 106.6 ? 
157 SG  ? D  CYS 507 ? D CYS 507 ? 1_555 FE3 ? OB SF4 . ? D SF4 801 ? 1_555 S1  ? OB SF4 .   ? D SF4 801 ? 1_555 108.6 ? 
158 SG  ? D  CYS 507 ? D CYS 507 ? 1_555 FE3 ? OB SF4 . ? D SF4 801 ? 1_555 S2  ? OB SF4 .   ? D SF4 801 ? 1_555 102.1 ? 
159 S1  ? OB SF4 .   ? D SF4 801 ? 1_555 FE3 ? OB SF4 . ? D SF4 801 ? 1_555 S2  ? OB SF4 .   ? D SF4 801 ? 1_555 106.6 ? 
160 SG  ? D  CYS 507 ? D CYS 507 ? 1_555 FE3 ? OB SF4 . ? D SF4 801 ? 1_555 S4  ? OB SF4 .   ? D SF4 801 ? 1_555 125.6 ? 
161 S1  ? OB SF4 .   ? D SF4 801 ? 1_555 FE3 ? OB SF4 . ? D SF4 801 ? 1_555 S4  ? OB SF4 .   ? D SF4 801 ? 1_555 106.3 ? 
162 S2  ? OB SF4 .   ? D SF4 801 ? 1_555 FE3 ? OB SF4 . ? D SF4 801 ? 1_555 S4  ? OB SF4 .   ? D SF4 801 ? 1_555 106.1 ? 
163 SG  ? D  CYS 574 ? D CYS 574 ? 1_555 NI  ? QB NI  . ? D NI  803 ? 1_555 N   ? D  GLY 575 ? D GLY 575 ? 1_555 92.5  ? 
164 SG  ? D  CYS 574 ? D CYS 574 ? 1_555 NI  ? QB NI  . ? D NI  803 ? 1_555 N   ? D  CYS 576 ? D CYS 576 ? 1_555 176.0 ? 
165 N   ? D  GLY 575 ? D GLY 575 ? 1_555 NI  ? QB NI  . ? D NI  803 ? 1_555 N   ? D  CYS 576 ? D CYS 576 ? 1_555 84.7  ? 
166 SG  ? D  CYS 574 ? D CYS 574 ? 1_555 NI  ? QB NI  . ? D NI  803 ? 1_555 SG  ? D  CYS 576 ? D CYS 576 ? 1_555 93.6  ? 
167 N   ? D  GLY 575 ? D GLY 575 ? 1_555 NI  ? QB NI  . ? D NI  803 ? 1_555 SG  ? D  CYS 576 ? D CYS 576 ? 1_555 164.4 ? 
168 N   ? D  CYS 576 ? D CYS 576 ? 1_555 NI  ? QB NI  . ? D NI  803 ? 1_555 SG  ? D  CYS 576 ? D CYS 576 ? 1_555 88.5  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLU 109 A . ? GLU 109 A PRO 110 A ? PRO 110 A 1 2.61  
2 GLY 53  B . ? GLY 53  B PRO 54  B ? PRO 54  B 1 17.66 
3 GLY 53  C . ? GLY 53  C PRO 54  C ? PRO 54  C 1 25.36 
4 GLU 109 D . ? GLU 109 D PRO 110 D ? PRO 110 D 1 -0.36 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 3 ? 
AA3 ? 3 ? 
AA4 ? 3 ? 
AA5 ? 2 ? 
AA6 ? 4 ? 
AA7 ? 2 ? 
AA8 ? 2 ? 
AA9 ? 6 ? 
AB1 ? 6 ? 
AB2 ? 2 ? 
AB3 ? 2 ? 
AB4 ? 6 ? 
AB5 ? 6 ? 
AB6 ? 6 ? 
AB7 ? 4 ? 
AB8 ? 4 ? 
AB9 ? 3 ? 
AC1 ? 2 ? 
AC2 ? 4 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? parallel      
AA7 1 2 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? parallel      
AA9 3 4 ? parallel      
AA9 4 5 ? parallel      
AA9 5 6 ? parallel      
AB1 1 2 ? parallel      
AB1 2 3 ? parallel      
AB1 3 4 ? parallel      
AB1 4 5 ? parallel      
AB1 5 6 ? parallel      
AB2 1 2 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? parallel      
AB4 3 4 ? parallel      
AB4 4 5 ? parallel      
AB4 5 6 ? parallel      
AB5 1 2 ? parallel      
AB5 2 3 ? parallel      
AB5 3 4 ? parallel      
AB5 4 5 ? parallel      
AB5 5 6 ? parallel      
AB6 1 2 ? parallel      
AB6 2 3 ? parallel      
AB6 3 4 ? parallel      
AB6 4 5 ? parallel      
AB6 5 6 ? parallel      
AB7 1 2 ? parallel      
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? parallel      
AB8 2 3 ? anti-parallel 
AB8 3 4 ? parallel      
AB9 1 2 ? anti-parallel 
AB9 2 3 ? anti-parallel 
AC1 1 2 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC2 3 4 ? 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 VAL A 185 ? GLY A 189 ? VAL A 185 GLY A 189 
AA1 2 LEU A 161 ? VAL A 165 ? LEU A 161 VAL A 165 
AA1 3 VAL A 135 ? GLY A 140 ? VAL A 135 GLY A 140 
AA1 4 ALA A 230 ? PHE A 235 ? ALA A 230 PHE A 235 
AA1 5 VAL A 256 ? THR A 258 ? VAL A 256 THR A 258 
AA1 6 LEU A 269 ? THR A 271 ? LEU A 269 THR A 271 
AA2 1 MET A 315 ? GLY A 320 ? MET A 315 GLY A 320 
AA2 2 THR A 404 ? GLY A 409 ? THR A 404 GLY A 409 
AA2 3 VAL A 395 ? GLY A 399 ? VAL A 395 GLY A 399 
AA3 1 TRP A 327 ? MET A 331 ? TRP A 327 MET A 331 
AA3 2 GLY A 363 ? LYS A 367 ? GLY A 363 LYS A 367 
AA3 3 ILE A 445 ? ILE A 446 ? ILE A 445 ILE A 446 
AA4 1 CYS A 497 ? VAL A 499 ? CYS A 497 VAL A 499 
AA4 2 THR A 481 ? CYS A 485 ? THR A 481 CYS A 485 
AA4 3 GLN A 528 ? PRO A 531 ? GLN A 528 PRO A 531 
AA5 1 VAL A 535 ? ASP A 537 ? VAL A 535 ASP A 537 
AA5 2 ILE A 542 ? TRP A 543 ? ILE A 542 TRP A 543 
AA6 1 PHE A 623 ? HIS A 626 ? PHE A 623 HIS A 626 
AA6 2 CYS A 579 ? MET A 584 ? CYS A 579 MET A 584 
AA6 3 GLY A 589 ? ASN A 594 ? GLY A 589 ASN A 594 
AA6 4 ILE A 646 ? TRP A 648 ? ILE A 646 TRP A 648 
AA7 1 CYS B 46  ? CYS B 47  ? CYS B 46  CYS B 47  
AA7 2 CYS B 55  ? ARG B 56  ? CYS B 55  ARG B 56  
AA8 1 ILE B 238 ? ALA B 242 ? ILE B 238 ALA B 242 
AA8 2 CYS B 401 ? LEU B 405 ? CYS B 401 LEU B 405 
AA9 1 ILE B 308 ? GLY B 310 ? ILE B 308 GLY B 310 
AA9 2 ILE B 288 ? MET B 293 ? ILE B 288 MET B 293 
AA9 3 VAL B 252 ? LEU B 256 ? VAL B 252 LEU B 256 
AA9 4 VAL B 324 ? VAL B 329 ? VAL B 324 VAL B 329 
AA9 5 LYS B 348 ? THR B 351 ? LYS B 348 THR B 351 
AA9 6 ILE B 362 ? TYR B 363 ? ILE B 362 TYR B 363 
AB1 1 VAL B 517 ? HIS B 519 ? VAL B 517 HIS B 519 
AB1 2 VAL B 474 ? VAL B 478 ? VAL B 474 VAL B 478 
AB1 3 GLY B 444 ? VAL B 448 ? GLY B 444 VAL B 448 
AB1 4 VAL B 549 ? ALA B 553 ? VAL B 549 ALA B 553 
AB1 5 ASP B 574 ? LEU B 577 ? ASP B 574 LEU B 577 
AB1 6 PHE B 605 ? ILE B 607 ? PHE B 605 ILE B 607 
AB2 1 CYS C 46  ? CYS C 47  ? CYS C 46  CYS C 47  
AB2 2 CYS C 55  ? ARG C 56  ? CYS C 55  ARG C 56  
AB3 1 ILE C 238 ? ALA C 242 ? ILE C 238 ALA C 242 
AB3 2 CYS C 401 ? LEU C 405 ? CYS C 401 LEU C 405 
AB4 1 LYS C 307 ? GLY C 310 ? LYS C 307 GLY C 310 
AB4 2 ILE C 288 ? MET C 293 ? ILE C 288 MET C 293 
AB4 3 VAL C 252 ? HIS C 257 ? VAL C 252 HIS C 257 
AB4 4 VAL C 324 ? VAL C 329 ? VAL C 324 VAL C 329 
AB4 5 LYS C 348 ? THR C 351 ? LYS C 348 THR C 351 
AB4 6 ILE C 362 ? TYR C 363 ? ILE C 362 TYR C 363 
AB5 1 VAL C 517 ? GLY C 521 ? VAL C 517 GLY C 521 
AB5 2 VAL C 474 ? THR C 479 ? VAL C 474 THR C 479 
AB5 3 GLY C 444 ? VAL C 448 ? GLY C 444 VAL C 448 
AB5 4 VAL C 549 ? ALA C 553 ? VAL C 549 ALA C 553 
AB5 5 ASP C 574 ? LEU C 577 ? ASP C 574 LEU C 577 
AB5 6 PHE C 605 ? ILE C 607 ? PHE C 605 ILE C 607 
AB6 1 VAL D 185 ? GLY D 189 ? VAL D 185 GLY D 189 
AB6 2 LEU D 161 ? VAL D 165 ? LEU D 161 VAL D 165 
AB6 3 VAL D 135 ? GLY D 140 ? VAL D 135 GLY D 140 
AB6 4 ALA D 230 ? PHE D 235 ? ALA D 230 PHE D 235 
AB6 5 VAL D 256 ? THR D 258 ? VAL D 256 THR D 258 
AB6 6 LEU D 269 ? THR D 271 ? LEU D 269 THR D 271 
AB7 1 GLY D 358 ? ARG D 359 ? GLY D 358 ARG D 359 
AB7 2 MET D 315 ? GLY D 320 ? MET D 315 GLY D 320 
AB7 3 LEU D 403 ? GLY D 409 ? LEU D 403 GLY D 409 
AB7 4 VAL D 395 ? GLN D 400 ? VAL D 395 GLN D 400 
AB8 1 ALA D 326 ? ALA D 333 ? ALA D 326 ALA D 333 
AB8 2 LEU D 362 ? SER D 369 ? LEU D 362 SER D 369 
AB8 3 CYS D 441 ? ILE D 446 ? CYS D 441 ILE D 446 
AB8 4 ILE D 343 ? ILE D 346 ? ILE D 343 ILE D 346 
AB9 1 CYS D 497 ? VAL D 499 ? CYS D 497 VAL D 499 
AB9 2 THR D 481 ? CYS D 485 ? THR D 481 CYS D 485 
AB9 3 CYS D 527 ? PRO D 531 ? CYS D 527 PRO D 531 
AC1 1 VAL D 535 ? ASP D 537 ? VAL D 535 ASP D 537 
AC1 2 ILE D 542 ? TRP D 543 ? ILE D 542 TRP D 543 
AC2 1 PHE D 623 ? HIS D 626 ? PHE D 623 HIS D 626 
AC2 2 CYS D 579 ? MET D 584 ? CYS D 579 MET D 584 
AC2 3 GLY D 589 ? ASN D 594 ? GLY D 589 ASN D 594 
AC2 4 ILE D 646 ? TRP D 648 ? ILE D 646 TRP D 648 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ILE A 186 ? O ILE A 186 N THR A 162 ? N THR A 162 
AA1 2 3 O CYS A 163 ? O CYS A 163 N ALA A 136 ? N ALA A 136 
AA1 3 4 N VAL A 137 ? N VAL A 137 O PHE A 231 ? O PHE A 231 
AA1 4 5 N VAL A 232 ? N VAL A 232 O LEU A 257 ? O LEU A 257 
AA1 5 6 N THR A 258 ? N THR A 258 O LEU A 270 ? O LEU A 270 
AA2 1 2 N PHE A 319 ? N PHE A 319 O VAL A 406 ? O VAL A 406 
AA2 2 3 O TRP A 405 ? O TRP A 405 N VAL A 398 ? N VAL A 398 
AA3 1 2 N MET A 331 ? N MET A 331 O ILE A 366 ? O ILE A 366 
AA3 2 3 N GLY A 363 ? N GLY A 363 O ILE A 446 ? O ILE A 446 
AA4 1 2 O CYS A 497 ? O CYS A 497 N CYS A 485 ? N CYS A 485 
AA4 2 3 N PHE A 482 ? N PHE A 482 O VAL A 530 ? O VAL A 530 
AA5 1 2 N VAL A 536 ? N VAL A 536 O ILE A 542 ? O ILE A 542 
AA6 1 2 O MET A 624 ? O MET A 624 N THR A 581 ? N THR A 581 
AA6 2 3 N GLY A 582 ? N GLY A 582 O VAL A 591 ? O VAL A 591 
AA6 3 4 N VAL A 590 ? N VAL A 590 O VAL A 647 ? O VAL A 647 
AA7 1 2 N CYS B 47  ? N CYS B 47  O CYS B 55  ? O CYS B 55  
AA8 1 2 N ALA B 242 ? N ALA B 242 O CYS B 401 ? O CYS B 401 
AA9 1 2 O ALA B 309 ? O ALA B 309 N GLY B 292 ? N GLY B 292 
AA9 2 3 O ASN B 289 ? O ASN B 289 N VAL B 252 ? N VAL B 252 
AA9 3 4 N VAL B 255 ? N VAL B 255 O GLY B 326 ? O GLY B 326 
AA9 4 5 N VAL B 329 ? N VAL B 329 O ILE B 350 ? O ILE B 350 
AA9 5 6 N THR B 351 ? N THR B 351 O ILE B 362 ? O ILE B 362 
AB1 1 2 O LEU B 518 ? O LEU B 518 N VAL B 478 ? N VAL B 478 
AB1 2 3 O VAL B 477 ? O VAL B 477 N ALA B 446 ? N ALA B 446 
AB1 3 4 N ALA B 447 ? N ALA B 447 O VAL B 552 ? O VAL B 552 
AB1 4 5 N GLY B 551 ? N GLY B 551 O ASP B 574 ? O ASP B 574 
AB1 5 6 N LEU B 577 ? N LEU B 577 O PHE B 606 ? O PHE B 606 
AB2 1 2 N CYS C 47  ? N CYS C 47  O CYS C 55  ? O CYS C 55  
AB3 1 2 N ALA C 242 ? N ALA C 242 O CYS C 401 ? O CYS C 401 
AB4 1 2 O ALA C 309 ? O ALA C 309 N GLY C 292 ? N GLY C 292 
AB4 2 3 O ASN C 289 ? O ASN C 289 N VAL C 252 ? N VAL C 252 
AB4 3 4 N HIS C 257 ? N HIS C 257 O ILE C 328 ? O ILE C 328 
AB4 4 5 N LEU C 327 ? N LEU C 327 O LYS C 348 ? O LYS C 348 
AB4 5 6 N THR C 351 ? N THR C 351 O ILE C 362 ? O ILE C 362 
AB5 1 2 O MET C 520 ? O MET C 520 N VAL C 478 ? N VAL C 478 
AB5 2 3 O ILE C 475 ? O ILE C 475 N ALA C 446 ? N ALA C 446 
AB5 3 4 N ALA C 447 ? N ALA C 447 O VAL C 552 ? O VAL C 552 
AB5 4 5 N GLY C 551 ? N GLY C 551 O TRP C 576 ? O TRP C 576 
AB5 5 6 N LEU C 577 ? N LEU C 577 O PHE C 606 ? O PHE C 606 
AB6 1 2 O LEU D 188 ? O LEU D 188 N LEU D 164 ? N LEU D 164 
AB6 2 3 O LEU D 161 ? O LEU D 161 N ALA D 136 ? N ALA D 136 
AB6 3 4 N VAL D 137 ? N VAL D 137 O PHE D 231 ? O PHE D 231 
AB6 4 5 N VAL D 232 ? N VAL D 232 O LEU D 257 ? O LEU D 257 
AB6 5 6 N THR D 258 ? N THR D 258 O LEU D 270 ? O LEU D 270 
AB7 1 2 O GLY D 358 ? O GLY D 358 N GLU D 318 ? N GLU D 318 
AB7 2 3 N LEU D 316 ? N LEU D 316 O ILE D 408 ? O ILE D 408 
AB7 3 4 O LEU D 403 ? O LEU D 403 N GLN D 400 ? N GLN D 400 
AB8 1 2 N MET D 331 ? N MET D 331 O ILE D 366 ? O ILE D 366 
AB8 2 3 N GLY D 363 ? N GLY D 363 O ILE D 446 ? O ILE D 446 
AB8 3 4 O ILE D 445 ? O ILE D 445 N ILE D 346 ? N ILE D 346 
AB9 1 2 O CYS D 497 ? O CYS D 497 N CYS D 485 ? N CYS D 485 
AB9 2 3 N PHE D 482 ? N PHE D 482 O VAL D 530 ? O VAL D 530 
AC1 1 2 N ASP D 537 ? N ASP D 537 O ILE D 542 ? O ILE D 542 
AC2 1 2 O HIS D 626 ? O HIS D 626 N CYS D 579 ? N CYS D 579 
AC2 2 3 N MET D 584 ? N MET D 584 O GLY D 589 ? O GLY D 589 
AC2 3 4 N VAL D 590 ? N VAL D 590 O VAL D 647 ? O VAL D 647 
# 
_pdbx_entry_details.entry_id                   9G7I 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 ASP A 39  ? ? 46.46   77.95   
2  1 SER A 43  ? ? 44.57   -116.08 
3  1 PRO A 263 ? ? -66.68  92.76   
4  1 THR A 267 ? ? 62.58   -5.66   
5  1 GLN A 400 ? ? -98.12  -67.30  
6  1 ARG A 401 ? ? -127.33 -72.80  
7  1 GLU A 453 ? ? -62.86  -70.03  
8  1 PRO A 501 ? ? -49.80  -16.06  
9  1 ALA A 509 ? ? -96.66  -65.40  
10 1 THR A 524 ? ? -106.55 41.69   
11 1 TYR A 564 ? ? -119.38 51.32   
12 1 ASP A 569 ? ? 30.95   68.38   
13 1 CYS A 574 ? ? -103.57 -83.64  
14 1 LYS B 35  ? ? 44.28   -139.12 
15 1 ARG B 181 ? ? -107.99 -161.24 
16 1 CYS B 198 ? ? -112.88 -113.36 
17 1 MET B 219 ? ? -131.17 -85.81  
18 1 ASN B 243 ? ? 88.46   157.25  
19 1 HIS B 259 ? ? -139.26 -37.06  
20 1 CYS B 294 ? ? 59.68   -159.72 
21 1 ASP B 330 ? ? -130.79 -93.37  
22 1 GLN B 332 ? ? 68.80   116.32  
23 1 THR B 347 ? ? -38.46  135.67  
24 1 ILE B 424 ? ? -135.63 -67.31  
25 1 CYS B 451 ? ? -96.01  -157.87 
26 1 ASP B 459 ? ? 68.84   -13.75  
27 1 ASN B 472 ? ? -86.05  33.69   
28 1 LEU B 492 ? ? -85.14  44.64   
29 1 MET B 557 ? ? -159.78 -36.03  
30 1 ASN B 595 ? ? -154.02 -73.17  
31 1 LYS C 35  ? ? 54.34   -147.93 
32 1 ARG C 181 ? ? -117.48 -155.87 
33 1 CYS C 198 ? ? -114.70 -112.23 
34 1 ALA C 200 ? ? -140.88 48.76   
35 1 ASP C 216 ? ? -91.56  -68.87  
36 1 MET C 219 ? ? -128.37 -69.62  
37 1 ASN C 243 ? ? 91.85   158.12  
38 1 HIS C 259 ? ? -137.83 -30.04  
39 1 CYS C 294 ? ? 58.95   -155.79 
40 1 PHE C 312 ? ? -29.43  -69.74  
41 1 ASP C 330 ? ? -119.94 -89.14  
42 1 GLN C 332 ? ? 64.01   136.64  
43 1 ASN C 370 ? ? -118.40 76.52   
44 1 ILE C 424 ? ? -124.60 -79.38  
45 1 CYS C 451 ? ? -112.25 -153.50 
46 1 ASP C 459 ? ? 72.52   -14.64  
47 1 ASP C 513 ? ? 61.65   68.37   
48 1 MET C 557 ? ? -142.49 -57.72  
49 1 ASN C 595 ? ? -161.25 -74.55  
50 1 PRO D 38  ? ? -57.71  109.89  
51 1 ASP D 39  ? ? 56.09   81.65   
52 1 SER D 43  ? ? 47.38   -114.05 
53 1 THR D 267 ? ? 54.81   18.38   
54 1 LEU D 268 ? ? -136.19 -71.03  
55 1 ARG D 309 ? ? -100.57 73.53   
56 1 LYS D 323 ? ? -136.50 -54.12  
57 1 GLU D 339 ? ? -108.93 50.36   
58 1 ASP D 340 ? ? 40.89   -134.54 
59 1 ASP D 354 ? ? -139.62 -48.16  
60 1 PRO D 357 ? ? -95.10  52.11   
61 1 THR D 371 ? ? -154.71 85.99   
62 1 ARG D 401 ? ? 49.07   -122.76 
63 1 THR D 524 ? ? -101.27 44.87   
64 1 ASP D 569 ? ? 33.37   61.61   
65 1 CYS D 574 ? ? -87.71  -96.21  
66 1 LEU D 668 ? ? 70.49   -42.40  
67 1 LYS D 703 ? ? -99.84  57.57   
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 97.7512  51.3211  43.9543 0.6758 ? 0.1606  ? 0.0524  ? 0.3657 ? 0.0683  ? 0.5304 ? 1.9373 ? 
-0.2980 ? -0.8494 ? 0.8259 ? 0.2942  ? 1.8754 ? -0.1522 ? -0.3276 ? 0.0955  ? 0.1533  ? 0.1389  ? -0.1499 ? -0.4096 ? 0.0912  ? 
-0.0079 ? 
2  'X-RAY DIFFRACTION' ? refined 60.4855  35.1723  40.7864 0.7320 ? 0.2175  ? 0.4007  ? 1.0997 ? 0.2556  ? 1.1740 ? 5.4226 ? 
1.1416  ? 2.0974  ? 4.0180 ? 2.7755  ? 5.1382 ? -0.2943 ? 0.1273  ? -0.3691 ? 0.4509  ? -0.0277 ? 1.1736  ? 0.2935  ? -1.2335 ? 
0.3088  ? 
3  'X-RAY DIFFRACTION' ? refined 74.1349  37.8145  28.5016 0.4808 ? 0.1518  ? 0.1428  ? 0.5863 ? 0.0811  ? 0.7613 ? 1.8943 ? 
-0.4400 ? -0.2839 ? 1.5059 ? 1.1377  ? 0.8600 ? -0.0163 ? -0.0065 ? -0.3076 ? -0.0942 ? 0.0080  ? 0.6646  ? -0.0884 ? -0.7852 ? 
0.0025  ? 
4  'X-RAY DIFFRACTION' ? refined 78.2401  47.0431  49.8076 0.7631 ? 0.3034  ? 0.2700  ? 0.6576 ? 0.0771  ? 0.6907 ? 0.5201 ? 
-0.4919 ? 0.4752  ? 0.6960 ? -0.3154 ? 0.4679 ? -0.2136 ? -0.3820 ? -0.0389 ? 0.3630  ? 0.2463  ? 0.4417  ? -0.4293 ? -0.3446 ? 
-0.1066 ? 
5  'X-RAY DIFFRACTION' ? refined 83.1910  44.6390  64.6389 0.9311 ? 0.4124  ? 0.2477  ? 0.8140 ? 0.1416  ? 0.6442 ? 2.9269 ? 
-0.0550 ? 0.2171  ? 2.9319 ? -0.5184 ? 1.7727 ? -0.2985 ? -0.5763 ? -0.1880 ? 1.1629  ? 0.3625  ? 0.2217  ? -0.0238 ? -0.2113 ? 
-0.0568 ? 
6  'X-RAY DIFFRACTION' ? refined 76.6906  61.8226  35.4249 0.6825 ? 0.2124  ? 0.1352  ? 0.3531 ? 0.0125  ? 0.6344 ? 2.0476 ? 
-0.8562 ? 0.2111  ? 1.3923 ? -0.4007 ? 1.4685 ? -0.1912 ? -0.0865 ? 0.3083  ? 0.2493  ? 0.1155  ? 0.1292  ? -0.3378 ? -0.1008 ? 
0.0507  ? 
7  'X-RAY DIFFRACTION' ? refined 47.9814  86.5928  24.2458 0.7683 ? 0.3295  ? 0.0914  ? 0.5384 ? 0.0693  ? 0.8716 ? 2.5649 ? 
0.1126  ? -0.7289 ? 2.9141 ? -0.2014 ? 1.7860 ? 0.1839  ? 0.2135  ? 0.2910  ? -0.0370 ? -0.1194 ? 0.3343  ? -0.1687 ? -0.3695 ? 
-0.0661 ? 
8  'X-RAY DIFFRACTION' ? refined 11.7312  95.3194  42.3143 0.5975 ? 0.0118  ? 0.1757  ? 0.7361 ? -0.0511 ? 0.7351 ? 3.9526 ? 
-0.1090 ? -0.4773 ? 3.5722 ? 0.6456  ? 2.9162 ? 0.1365  ? -0.3785 ? -0.2612 ? 0.4089  ? -0.1064 ? 0.5577  ? 0.4362  ? 0.0027  ? 
0.0044  ? 
9  'X-RAY DIFFRACTION' ? refined 124.0156 -22.3914 45.2066 0.4875 ? 0.0337  ? -0.0338 ? 0.2778 ? 0.1361  ? 0.4253 ? 2.4936 ? 
-0.1064 ? 0.1158  ? 3.5620 ? -0.2358 ? 2.9019 ? -0.0274 ? 0.0426  ? -0.1058 ? 0.4298  ? -0.0345 ? -0.2460 ? 0.2123  ? 0.1781  ? 
0.0597  ? 
10 'X-RAY DIFFRACTION' ? refined 94.8831  -19.5076 -0.6517 1.6126 ? -0.2323 ? 0.1059  ? 0.9349 ? -0.0259 ? 0.9938 ? 2.9935 ? 
0.5135  ? -1.0947 ? 1.9659 ? -0.1204 ? 4.2312 ? 0.7751  ? -0.4761 ? 0.1313  ? 0.9024  ? -0.5399 ? 0.0344  ? -1.3378 ? 0.1839  ? 
-0.2104 ? 
11 'X-RAY DIFFRACTION' ? refined 109.1353 38.5316  36.5799 0.5333 ? 0.1109  ? 0.0750  ? 0.4015 ? 0.1146  ? 0.5046 ? 0.7900 ? 
-0.2733 ? 0.0883  ? 1.9482 ? 0.4558  ? 0.9630 ? -0.2097 ? -0.1157 ? 0.1610  ? 0.3141  ? 0.2115  ? -0.0980 ? -0.2086 ? 0.0909  ? 
-0.0184 ? 
12 'X-RAY DIFFRACTION' ? refined 85.7990  8.8385   22.0328 0.5438 ? -0.0570 ? 0.1891  ? 0.5595 ? 0.0423  ? 0.8821 ? 6.4965 ? 
0.7280  ? 0.1759  ? 6.5065 ? 1.6955  ? 9.3735 ? -0.0636 ? 0.3549  ? -0.7513 ? 0.7510  ? -0.2228 ? 0.6901  ? 1.2567  ? -0.9519 ? 
0.2613  ? 
13 'X-RAY DIFFRACTION' ? refined 86.7766  17.1953  38.6190 0.5991 ? 0.1022  ? 0.3222  ? 0.5238 ? 0.1891  ? 0.8228 ? 2.3872 ? 
0.2294  ? 0.5767  ? 1.0318 ? 0.9036  ? 1.9426 ? -0.0901 ? -0.3491 ? -0.4385 ? 0.4533  ? 0.1295  ? 0.5406  ? 0.1450  ? -0.8080 ? 
-0.0287 ? 
14 'X-RAY DIFFRACTION' ? refined 104.7012 26.0238  21.7656 0.3150 ? 0.0562  ? 0.1248  ? 0.3065 ? 0.1061  ? 0.4725 ? 1.0466 ? 
-0.3220 ? -0.1523 ? 0.9488 ? 0.3082  ? 1.3107 ? -0.0763 ? 0.1184  ? 0.0140  ? 0.1416  ? 0.1370  ? 0.0847  ? -0.0575 ? -0.0221 ? 
-0.0700 ? 
15 'X-RAY DIFFRACTION' ? refined 105.8673 31.4039  9.0219  0.3043 ? 0.0111  ? 0.0812  ? 0.3562 ? 0.1236  ? 0.4621 ? 1.4197 ? 
0.0105  ? 0.3304  ? 4.6605 ? 0.0958  ? 4.3792 ? -0.0392 ? 0.3175  ? 0.2361  ? -0.1835 ? -0.0312 ? 0.2860  ? -0.4064 ? -0.1170 ? 
0.0559  ? 
16 'X-RAY DIFFRACTION' ? refined 111.5413 13.7111  39.4234 0.3057 ? 0.0755  ? 0.0829  ? 0.3081 ? 0.1219  ? 0.4007 ? 1.4041 ? 
-0.3412 ? 0.0833  ? 3.5643 ? 0.2438  ? 1.6623 ? -0.0708 ? -0.0858 ? -0.0639 ? 0.4794  ? 0.1208  ? -0.0576 ? 0.0204  ? -0.0112 ? 
-0.0320 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 2 through 106 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 107 through 136 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 137 through 182 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 183 through 320 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 321 through 400 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 401 through 631 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 1 through 314 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'D' and (resid 315 through 708 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 1 through 302 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 303 through 708 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 3 through 106 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 107 through 136 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 137 through 182 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 183 through 351 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 352 through 400 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 401 through 631 )
;
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 294 ? A GLU 294 
2  1 Y 1 A ILE 295 ? A ILE 295 
3  1 Y 1 A ARG 309 ? A ARG 309 
4  1 Y 1 A ILE 310 ? A ILE 310 
5  1 Y 1 A ARG 311 ? A ARG 311 
6  1 Y 1 A LYS 312 ? A LYS 312 
7  1 Y 1 A PRO 357 ? A PRO 357 
8  1 Y 1 A GLY 358 ? A GLY 358 
9  1 Y 1 A ARG 359 ? A ARG 359 
10 1 Y 1 A ASP 439 ? A ASP 439 
11 1 Y 1 A LYS 440 ? A LYS 440 
12 1 Y 1 A CYS 441 ? A CYS 441 
13 1 Y 1 A GLU 442 ? A GLU 442 
14 1 Y 1 A VAL 443 ? A VAL 443 
15 1 Y 1 B MET 1   ? B MET 1   
16 1 Y 1 B GLU 2   ? B GLU 2   
17 1 Y 1 C MET 1   ? C MET 1   
# 
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 
ACO N1A  N  Y N 1   
ACO C2A  C  Y N 2   
ACO N3A  N  Y N 3   
ACO C4A  C  Y N 4   
ACO C5A  C  Y N 5   
ACO C6A  C  Y N 6   
ACO N6A  N  N N 7   
ACO N7A  N  Y N 8   
ACO C8A  C  Y N 9   
ACO N9A  N  Y N 10  
ACO C1B  C  N R 11  
ACO C2B  C  N R 12  
ACO O2B  O  N N 13  
ACO C3B  C  N S 14  
ACO O3B  O  N N 15  
ACO P3B  P  N N 16  
ACO O7A  O  N N 17  
ACO O8A  O  N N 18  
ACO O9A  O  N N 19  
ACO C4B  C  N R 20  
ACO O4B  O  N N 21  
ACO C5B  C  N N 22  
ACO O5B  O  N N 23  
ACO P1A  P  N S 24  
ACO O1A  O  N N 25  
ACO O2A  O  N N 26  
ACO O3A  O  N N 27  
ACO P2A  P  N S 28  
ACO O4A  O  N N 29  
ACO O5A  O  N N 30  
ACO O6A  O  N N 31  
ACO CBP  C  N N 32  
ACO CCP  C  N N 33  
ACO CDP  C  N N 34  
ACO CEP  C  N N 35  
ACO CAP  C  N R 36  
ACO OAP  O  N N 37  
ACO C9P  C  N N 38  
ACO O9P  O  N N 39  
ACO N8P  N  N N 40  
ACO C7P  C  N N 41  
ACO C6P  C  N N 42  
ACO C5P  C  N N 43  
ACO O5P  O  N N 44  
ACO N4P  N  N N 45  
ACO C3P  C  N N 46  
ACO C2P  C  N N 47  
ACO S1P  S  N N 48  
ACO C    C  N N 49  
ACO O    O  N N 50  
ACO CH3  C  N N 51  
ACO H2A  H  N N 52  
ACO H61A H  N N 53  
ACO H62A H  N N 54  
ACO H8A  H  N N 55  
ACO H1B  H  N N 56  
ACO H2B  H  N N 57  
ACO HO2A H  N N 58  
ACO H3B  H  N N 59  
ACO HOA8 H  N N 60  
ACO HOA9 H  N N 61  
ACO H4B  H  N N 62  
ACO H51A H  N N 63  
ACO H52A H  N N 64  
ACO HOA2 H  N N 65  
ACO HOA5 H  N N 66  
ACO H121 H  N N 67  
ACO H122 H  N N 68  
ACO H131 H  N N 69  
ACO H132 H  N N 70  
ACO H133 H  N N 71  
ACO H141 H  N N 72  
ACO H142 H  N N 73  
ACO H143 H  N N 74  
ACO H10  H  N N 75  
ACO HO1  H  N N 76  
ACO HN8  H  N N 77  
ACO H71  H  N N 78  
ACO H72  H  N N 79  
ACO H61  H  N N 80  
ACO H62  H  N N 81  
ACO HN4  H  N N 82  
ACO H31  H  N N 83  
ACO H32  H  N N 84  
ACO H21  H  N N 85  
ACO H22  H  N N 86  
ACO HH31 H  N N 87  
ACO HH32 H  N N 88  
ACO HH33 H  N N 89  
ALA N    N  N N 90  
ALA CA   C  N S 91  
ALA C    C  N N 92  
ALA O    O  N N 93  
ALA CB   C  N N 94  
ALA OXT  O  N N 95  
ALA H    H  N N 96  
ALA H2   H  N N 97  
ALA HA   H  N N 98  
ALA HB1  H  N N 99  
ALA HB2  H  N N 100 
ALA HB3  H  N N 101 
ALA HXT  H  N N 102 
ARG N    N  N N 103 
ARG CA   C  N S 104 
ARG C    C  N N 105 
ARG O    O  N N 106 
ARG CB   C  N N 107 
ARG CG   C  N N 108 
ARG CD   C  N N 109 
ARG NE   N  N N 110 
ARG CZ   C  N N 111 
ARG NH1  N  N N 112 
ARG NH2  N  N N 113 
ARG OXT  O  N N 114 
ARG H    H  N N 115 
ARG H2   H  N N 116 
ARG HA   H  N N 117 
ARG HB2  H  N N 118 
ARG HB3  H  N N 119 
ARG HG2  H  N N 120 
ARG HG3  H  N N 121 
ARG HD2  H  N N 122 
ARG HD3  H  N N 123 
ARG HE   H  N N 124 
ARG HH11 H  N N 125 
ARG HH12 H  N N 126 
ARG HH21 H  N N 127 
ARG HH22 H  N N 128 
ARG HXT  H  N N 129 
ASN N    N  N N 130 
ASN CA   C  N S 131 
ASN C    C  N N 132 
ASN O    O  N N 133 
ASN CB   C  N N 134 
ASN CG   C  N N 135 
ASN OD1  O  N N 136 
ASN ND2  N  N N 137 
ASN OXT  O  N N 138 
ASN H    H  N N 139 
ASN H2   H  N N 140 
ASN HA   H  N N 141 
ASN HB2  H  N N 142 
ASN HB3  H  N N 143 
ASN HD21 H  N N 144 
ASN HD22 H  N N 145 
ASN HXT  H  N N 146 
ASP N    N  N N 147 
ASP CA   C  N S 148 
ASP C    C  N N 149 
ASP O    O  N N 150 
ASP CB   C  N N 151 
ASP CG   C  N N 152 
ASP OD1  O  N N 153 
ASP OD2  O  N N 154 
ASP OXT  O  N N 155 
ASP H    H  N N 156 
ASP H2   H  N N 157 
ASP HA   H  N N 158 
ASP HB2  H  N N 159 
ASP HB3  H  N N 160 
ASP HD2  H  N N 161 
ASP HXT  H  N N 162 
CA  CA   CA N N 163 
CL  CL   CL N N 164 
CYS N    N  N N 165 
CYS CA   C  N R 166 
CYS C    C  N N 167 
CYS O    O  N N 168 
CYS CB   C  N N 169 
CYS SG   S  N N 170 
CYS OXT  O  N N 171 
CYS H    H  N N 172 
CYS H2   H  N N 173 
CYS HA   H  N N 174 
CYS HB2  H  N N 175 
CYS HB3  H  N N 176 
CYS HG   H  N N 177 
CYS HXT  H  N N 178 
EDO C1   C  N N 179 
EDO O1   O  N N 180 
EDO C2   C  N N 181 
EDO O2   O  N N 182 
EDO H11  H  N N 183 
EDO H12  H  N N 184 
EDO HO1  H  N N 185 
EDO H21  H  N N 186 
EDO H22  H  N N 187 
EDO HO2  H  N N 188 
GLN N    N  N N 189 
GLN CA   C  N S 190 
GLN C    C  N N 191 
GLN O    O  N N 192 
GLN CB   C  N N 193 
GLN CG   C  N N 194 
GLN CD   C  N N 195 
GLN OE1  O  N N 196 
GLN NE2  N  N N 197 
GLN OXT  O  N N 198 
GLN H    H  N N 199 
GLN H2   H  N N 200 
GLN HA   H  N N 201 
GLN HB2  H  N N 202 
GLN HB3  H  N N 203 
GLN HG2  H  N N 204 
GLN HG3  H  N N 205 
GLN HE21 H  N N 206 
GLN HE22 H  N N 207 
GLN HXT  H  N N 208 
GLU N    N  N N 209 
GLU CA   C  N S 210 
GLU C    C  N N 211 
GLU O    O  N N 212 
GLU CB   C  N N 213 
GLU CG   C  N N 214 
GLU CD   C  N N 215 
GLU OE1  O  N N 216 
GLU OE2  O  N N 217 
GLU OXT  O  N N 218 
GLU H    H  N N 219 
GLU H2   H  N N 220 
GLU HA   H  N N 221 
GLU HB2  H  N N 222 
GLU HB3  H  N N 223 
GLU HG2  H  N N 224 
GLU HG3  H  N N 225 
GLU HE2  H  N N 226 
GLU HXT  H  N N 227 
GLY N    N  N N 228 
GLY CA   C  N N 229 
GLY C    C  N N 230 
GLY O    O  N N 231 
GLY OXT  O  N N 232 
GLY H    H  N N 233 
GLY H2   H  N N 234 
GLY HA2  H  N N 235 
GLY HA3  H  N N 236 
GLY HXT  H  N N 237 
GOL C1   C  N N 238 
GOL O1   O  N N 239 
GOL C2   C  N N 240 
GOL O2   O  N N 241 
GOL C3   C  N N 242 
GOL O3   O  N N 243 
GOL H11  H  N N 244 
GOL H12  H  N N 245 
GOL HO1  H  N N 246 
GOL H2   H  N N 247 
GOL HO2  H  N N 248 
GOL H31  H  N N 249 
GOL H32  H  N N 250 
GOL HO3  H  N N 251 
HIS N    N  N N 252 
HIS CA   C  N S 253 
HIS C    C  N N 254 
HIS O    O  N N 255 
HIS CB   C  N N 256 
HIS CG   C  Y N 257 
HIS ND1  N  Y N 258 
HIS CD2  C  Y N 259 
HIS CE1  C  Y N 260 
HIS NE2  N  Y N 261 
HIS OXT  O  N N 262 
HIS H    H  N N 263 
HIS H2   H  N N 264 
HIS HA   H  N N 265 
HIS HB2  H  N N 266 
HIS HB3  H  N N 267 
HIS HD1  H  N N 268 
HIS HD2  H  N N 269 
HIS HE1  H  N N 270 
HIS HE2  H  N N 271 
HIS HXT  H  N N 272 
HOH O    O  N N 273 
HOH H1   H  N N 274 
HOH H2   H  N N 275 
ILE N    N  N N 276 
ILE CA   C  N S 277 
ILE C    C  N N 278 
ILE O    O  N N 279 
ILE CB   C  N S 280 
ILE CG1  C  N N 281 
ILE CG2  C  N N 282 
ILE CD1  C  N N 283 
ILE OXT  O  N N 284 
ILE H    H  N N 285 
ILE H2   H  N N 286 
ILE HA   H  N N 287 
ILE HB   H  N N 288 
ILE HG12 H  N N 289 
ILE HG13 H  N N 290 
ILE HG21 H  N N 291 
ILE HG22 H  N N 292 
ILE HG23 H  N N 293 
ILE HD11 H  N N 294 
ILE HD12 H  N N 295 
ILE HD13 H  N N 296 
ILE HXT  H  N N 297 
LEU N    N  N N 298 
LEU CA   C  N S 299 
LEU C    C  N N 300 
LEU O    O  N N 301 
LEU CB   C  N N 302 
LEU CG   C  N N 303 
LEU CD1  C  N N 304 
LEU CD2  C  N N 305 
LEU OXT  O  N N 306 
LEU H    H  N N 307 
LEU H2   H  N N 308 
LEU HA   H  N N 309 
LEU HB2  H  N N 310 
LEU HB3  H  N N 311 
LEU HG   H  N N 312 
LEU HD11 H  N N 313 
LEU HD12 H  N N 314 
LEU HD13 H  N N 315 
LEU HD21 H  N N 316 
LEU HD22 H  N N 317 
LEU HD23 H  N N 318 
LEU HXT  H  N N 319 
LYS N    N  N N 320 
LYS CA   C  N S 321 
LYS C    C  N N 322 
LYS O    O  N N 323 
LYS CB   C  N N 324 
LYS CG   C  N N 325 
LYS CD   C  N N 326 
LYS CE   C  N N 327 
LYS NZ   N  N N 328 
LYS OXT  O  N N 329 
LYS H    H  N N 330 
LYS H2   H  N N 331 
LYS HA   H  N N 332 
LYS HB2  H  N N 333 
LYS HB3  H  N N 334 
LYS HG2  H  N N 335 
LYS HG3  H  N N 336 
LYS HD2  H  N N 337 
LYS HD3  H  N N 338 
LYS HE2  H  N N 339 
LYS HE3  H  N N 340 
LYS HZ1  H  N N 341 
LYS HZ2  H  N N 342 
LYS HZ3  H  N N 343 
LYS HXT  H  N N 344 
MET N    N  N N 345 
MET CA   C  N S 346 
MET C    C  N N 347 
MET O    O  N N 348 
MET CB   C  N N 349 
MET CG   C  N N 350 
MET SD   S  N N 351 
MET CE   C  N N 352 
MET OXT  O  N N 353 
MET H    H  N N 354 
MET H2   H  N N 355 
MET HA   H  N N 356 
MET HB2  H  N N 357 
MET HB3  H  N N 358 
MET HG2  H  N N 359 
MET HG3  H  N N 360 
MET HE1  H  N N 361 
MET HE2  H  N N 362 
MET HE3  H  N N 363 
MET HXT  H  N N 364 
NI  NI   NI N N 365 
PE4 O1   O  N N 366 
PE4 C1   C  N N 367 
PE4 C2   C  N N 368 
PE4 O2   O  N N 369 
PE4 C3   C  N N 370 
PE4 C4   C  N N 371 
PE4 O3   O  N N 372 
PE4 C5   C  N N 373 
PE4 C6   C  N N 374 
PE4 O4   O  N N 375 
PE4 C7   C  N N 376 
PE4 C8   C  N N 377 
PE4 O5   O  N N 378 
PE4 C9   C  N N 379 
PE4 C10  C  N N 380 
PE4 O6   O  N N 381 
PE4 C11  C  N N 382 
PE4 C12  C  N N 383 
PE4 O7   O  N N 384 
PE4 C13  C  N N 385 
PE4 C14  C  N N 386 
PE4 O8   O  N N 387 
PE4 C15  C  N N 388 
PE4 C16  C  N N 389 
PE4 HO1  H  N N 390 
PE4 H11  H  N N 391 
PE4 H12  H  N N 392 
PE4 H21  H  N N 393 
PE4 H22  H  N N 394 
PE4 H31  H  N N 395 
PE4 H32  H  N N 396 
PE4 H41  H  N N 397 
PE4 H42  H  N N 398 
PE4 H51  H  N N 399 
PE4 H52  H  N N 400 
PE4 H61  H  N N 401 
PE4 H62  H  N N 402 
PE4 H71  H  N N 403 
PE4 H72  H  N N 404 
PE4 H81  H  N N 405 
PE4 H82  H  N N 406 
PE4 H91  H  N N 407 
PE4 H92  H  N N 408 
PE4 H101 H  N N 409 
PE4 H102 H  N N 410 
PE4 H111 H  N N 411 
PE4 H112 H  N N 412 
PE4 H121 H  N N 413 
PE4 H122 H  N N 414 
PE4 H131 H  N N 415 
PE4 H132 H  N N 416 
PE4 H141 H  N N 417 
PE4 H142 H  N N 418 
PE4 H151 H  N N 419 
PE4 H152 H  N N 420 
PE4 H161 H  N N 421 
PE4 H162 H  N N 422 
PE4 H163 H  N N 423 
PEG C1   C  N N 424 
PEG O1   O  N N 425 
PEG C2   C  N N 426 
PEG O2   O  N N 427 
PEG C3   C  N N 428 
PEG C4   C  N N 429 
PEG O4   O  N N 430 
PEG H11  H  N N 431 
PEG H12  H  N N 432 
PEG HO1  H  N N 433 
PEG H21  H  N N 434 
PEG H22  H  N N 435 
PEG H31  H  N N 436 
PEG H32  H  N N 437 
PEG H41  H  N N 438 
PEG H42  H  N N 439 
PEG HO4  H  N N 440 
PHE N    N  N N 441 
PHE CA   C  N S 442 
PHE C    C  N N 443 
PHE O    O  N N 444 
PHE CB   C  N N 445 
PHE CG   C  Y N 446 
PHE CD1  C  Y N 447 
PHE CD2  C  Y N 448 
PHE CE1  C  Y N 449 
PHE CE2  C  Y N 450 
PHE CZ   C  Y N 451 
PHE OXT  O  N N 452 
PHE H    H  N N 453 
PHE H2   H  N N 454 
PHE HA   H  N N 455 
PHE HB2  H  N N 456 
PHE HB3  H  N N 457 
PHE HD1  H  N N 458 
PHE HD2  H  N N 459 
PHE HE1  H  N N 460 
PHE HE2  H  N N 461 
PHE HZ   H  N N 462 
PHE HXT  H  N N 463 
PRO N    N  N N 464 
PRO CA   C  N S 465 
PRO C    C  N N 466 
PRO O    O  N N 467 
PRO CB   C  N N 468 
PRO CG   C  N N 469 
PRO CD   C  N N 470 
PRO OXT  O  N N 471 
PRO H    H  N N 472 
PRO HA   H  N N 473 
PRO HB2  H  N N 474 
PRO HB3  H  N N 475 
PRO HG2  H  N N 476 
PRO HG3  H  N N 477 
PRO HD2  H  N N 478 
PRO HD3  H  N N 479 
PRO HXT  H  N N 480 
SER N    N  N N 481 
SER CA   C  N S 482 
SER C    C  N N 483 
SER O    O  N N 484 
SER CB   C  N N 485 
SER OG   O  N N 486 
SER OXT  O  N N 487 
SER H    H  N N 488 
SER H2   H  N N 489 
SER HA   H  N N 490 
SER HB2  H  N N 491 
SER HB3  H  N N 492 
SER HG   H  N N 493 
SER HXT  H  N N 494 
SF4 FE1  FE N N 495 
SF4 FE2  FE N N 496 
SF4 FE3  FE N N 497 
SF4 FE4  FE N N 498 
SF4 S1   S  N N 499 
SF4 S2   S  N N 500 
SF4 S3   S  N N 501 
SF4 S4   S  N N 502 
THR N    N  N N 503 
THR CA   C  N S 504 
THR C    C  N N 505 
THR O    O  N N 506 
THR CB   C  N R 507 
THR OG1  O  N N 508 
THR CG2  C  N N 509 
THR OXT  O  N N 510 
THR H    H  N N 511 
THR H2   H  N N 512 
THR HA   H  N N 513 
THR HB   H  N N 514 
THR HG1  H  N N 515 
THR HG21 H  N N 516 
THR HG22 H  N N 517 
THR HG23 H  N N 518 
THR HXT  H  N N 519 
TRP N    N  N N 520 
TRP CA   C  N S 521 
TRP C    C  N N 522 
TRP O    O  N N 523 
TRP CB   C  N N 524 
TRP CG   C  Y N 525 
TRP CD1  C  Y N 526 
TRP CD2  C  Y N 527 
TRP NE1  N  Y N 528 
TRP CE2  C  Y N 529 
TRP CE3  C  Y N 530 
TRP CZ2  C  Y N 531 
TRP CZ3  C  Y N 532 
TRP CH2  C  Y N 533 
TRP OXT  O  N N 534 
TRP H    H  N N 535 
TRP H2   H  N N 536 
TRP HA   H  N N 537 
TRP HB2  H  N N 538 
TRP HB3  H  N N 539 
TRP HD1  H  N N 540 
TRP HE1  H  N N 541 
TRP HE3  H  N N 542 
TRP HZ2  H  N N 543 
TRP HZ3  H  N N 544 
TRP HH2  H  N N 545 
TRP HXT  H  N N 546 
TRS C    C  N N 547 
TRS C1   C  N N 548 
TRS C2   C  N N 549 
TRS C3   C  N N 550 
TRS N    N  N N 551 
TRS O1   O  N N 552 
TRS O2   O  N N 553 
TRS O3   O  N N 554 
TRS H11  H  N N 555 
TRS H12  H  N N 556 
TRS H21  H  N N 557 
TRS H22  H  N N 558 
TRS H31  H  N N 559 
TRS H32  H  N N 560 
TRS HN1  H  N N 561 
TRS HN2  H  N N 562 
TRS HN3  H  N N 563 
TRS HO1  H  N N 564 
TRS HO2  H  N N 565 
TRS HO3  H  N N 566 
TYR N    N  N N 567 
TYR CA   C  N S 568 
TYR C    C  N N 569 
TYR O    O  N N 570 
TYR CB   C  N N 571 
TYR CG   C  Y N 572 
TYR CD1  C  Y N 573 
TYR CD2  C  Y N 574 
TYR CE1  C  Y N 575 
TYR CE2  C  Y N 576 
TYR CZ   C  Y N 577 
TYR OH   O  N N 578 
TYR OXT  O  N N 579 
TYR H    H  N N 580 
TYR H2   H  N N 581 
TYR HA   H  N N 582 
TYR HB2  H  N N 583 
TYR HB3  H  N N 584 
TYR HD1  H  N N 585 
TYR HD2  H  N N 586 
TYR HE1  H  N N 587 
TYR HE2  H  N N 588 
TYR HH   H  N N 589 
TYR HXT  H  N N 590 
VAL N    N  N N 591 
VAL CA   C  N S 592 
VAL C    C  N N 593 
VAL O    O  N N 594 
VAL CB   C  N N 595 
VAL CG1  C  N N 596 
VAL CG2  C  N N 597 
VAL OXT  O  N N 598 
VAL H    H  N N 599 
VAL H2   H  N N 600 
VAL HA   H  N N 601 
VAL HB   H  N N 602 
VAL HG11 H  N N 603 
VAL HG12 H  N N 604 
VAL HG13 H  N N 605 
VAL HG21 H  N N 606 
VAL HG22 H  N N 607 
VAL HG23 H  N N 608 
VAL HXT  H  N N 609 
XCC FE1  FE N N 610 
XCC FE2  FE N N 611 
XCC FE3  FE N N 612 
XCC FE4  FE N N 613 
XCC S1   S  N N 614 
XCC S2   S  N N 615 
XCC S4   S  N N 616 
XCC S3   S  N N 617 
XCC NI   NI N N 618 
# 
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 
ACO N1A C2A  sing Y N 1   
ACO N1A C6A  doub Y N 2   
ACO C2A N3A  doub Y N 3   
ACO C2A H2A  sing N N 4   
ACO N3A C4A  sing Y N 5   
ACO C4A C5A  doub Y N 6   
ACO C4A N9A  sing Y N 7   
ACO C5A C6A  sing Y N 8   
ACO C5A N7A  sing Y N 9   
ACO C6A N6A  sing N N 10  
ACO N6A H61A sing N N 11  
ACO N6A H62A sing N N 12  
ACO N7A C8A  doub Y N 13  
ACO C8A N9A  sing Y N 14  
ACO C8A H8A  sing N N 15  
ACO N9A C1B  sing N N 16  
ACO C1B C2B  sing N N 17  
ACO C1B O4B  sing N N 18  
ACO C1B H1B  sing N N 19  
ACO C2B O2B  sing N N 20  
ACO C2B C3B  sing N N 21  
ACO C2B H2B  sing N N 22  
ACO O2B HO2A sing N N 23  
ACO C3B O3B  sing N N 24  
ACO C3B C4B  sing N N 25  
ACO C3B H3B  sing N N 26  
ACO O3B P3B  sing N N 27  
ACO P3B O7A  doub N N 28  
ACO P3B O8A  sing N N 29  
ACO P3B O9A  sing N N 30  
ACO O8A HOA8 sing N N 31  
ACO O9A HOA9 sing N N 32  
ACO C4B O4B  sing N N 33  
ACO C4B C5B  sing N N 34  
ACO C4B H4B  sing N N 35  
ACO C5B O5B  sing N N 36  
ACO C5B H51A sing N N 37  
ACO C5B H52A sing N N 38  
ACO O5B P1A  sing N N 39  
ACO P1A O1A  doub N N 40  
ACO P1A O2A  sing N N 41  
ACO P1A O3A  sing N N 42  
ACO O2A HOA2 sing N N 43  
ACO O3A P2A  sing N N 44  
ACO P2A O4A  doub N N 45  
ACO P2A O5A  sing N N 46  
ACO P2A O6A  sing N N 47  
ACO O5A HOA5 sing N N 48  
ACO O6A CCP  sing N N 49  
ACO CBP CCP  sing N N 50  
ACO CBP CDP  sing N N 51  
ACO CBP CEP  sing N N 52  
ACO CBP CAP  sing N N 53  
ACO CCP H121 sing N N 54  
ACO CCP H122 sing N N 55  
ACO CDP H131 sing N N 56  
ACO CDP H132 sing N N 57  
ACO CDP H133 sing N N 58  
ACO CEP H141 sing N N 59  
ACO CEP H142 sing N N 60  
ACO CEP H143 sing N N 61  
ACO CAP OAP  sing N N 62  
ACO CAP C9P  sing N N 63  
ACO CAP H10  sing N N 64  
ACO OAP HO1  sing N N 65  
ACO C9P O9P  doub N N 66  
ACO C9P N8P  sing N N 67  
ACO N8P C7P  sing N N 68  
ACO N8P HN8  sing N N 69  
ACO C7P C6P  sing N N 70  
ACO C7P H71  sing N N 71  
ACO C7P H72  sing N N 72  
ACO C6P C5P  sing N N 73  
ACO C6P H61  sing N N 74  
ACO C6P H62  sing N N 75  
ACO C5P O5P  doub N N 76  
ACO C5P N4P  sing N N 77  
ACO N4P C3P  sing N N 78  
ACO N4P HN4  sing N N 79  
ACO C3P C2P  sing N N 80  
ACO C3P H31  sing N N 81  
ACO C3P H32  sing N N 82  
ACO C2P S1P  sing N N 83  
ACO C2P H21  sing N N 84  
ACO C2P H22  sing N N 85  
ACO S1P C    sing N N 86  
ACO C   O    doub N N 87  
ACO C   CH3  sing N N 88  
ACO CH3 HH31 sing N N 89  
ACO CH3 HH32 sing N N 90  
ACO CH3 HH33 sing N N 91  
ALA N   CA   sing N N 92  
ALA N   H    sing N N 93  
ALA N   H2   sing N N 94  
ALA CA  C    sing N N 95  
ALA CA  CB   sing N N 96  
ALA CA  HA   sing N N 97  
ALA C   O    doub N N 98  
ALA C   OXT  sing N N 99  
ALA CB  HB1  sing N N 100 
ALA CB  HB2  sing N N 101 
ALA CB  HB3  sing N N 102 
ALA OXT HXT  sing N N 103 
ARG N   CA   sing N N 104 
ARG N   H    sing N N 105 
ARG N   H2   sing N N 106 
ARG CA  C    sing N N 107 
ARG CA  CB   sing N N 108 
ARG CA  HA   sing N N 109 
ARG C   O    doub N N 110 
ARG C   OXT  sing N N 111 
ARG CB  CG   sing N N 112 
ARG CB  HB2  sing N N 113 
ARG CB  HB3  sing N N 114 
ARG CG  CD   sing N N 115 
ARG CG  HG2  sing N N 116 
ARG CG  HG3  sing N N 117 
ARG CD  NE   sing N N 118 
ARG CD  HD2  sing N N 119 
ARG CD  HD3  sing N N 120 
ARG NE  CZ   sing N N 121 
ARG NE  HE   sing N N 122 
ARG CZ  NH1  sing N N 123 
ARG CZ  NH2  doub N N 124 
ARG NH1 HH11 sing N N 125 
ARG NH1 HH12 sing N N 126 
ARG NH2 HH21 sing N N 127 
ARG NH2 HH22 sing N N 128 
ARG OXT HXT  sing N N 129 
ASN N   CA   sing N N 130 
ASN N   H    sing N N 131 
ASN N   H2   sing N N 132 
ASN CA  C    sing N N 133 
ASN CA  CB   sing N N 134 
ASN CA  HA   sing N N 135 
ASN C   O    doub N N 136 
ASN C   OXT  sing N N 137 
ASN CB  CG   sing N N 138 
ASN CB  HB2  sing N N 139 
ASN CB  HB3  sing N N 140 
ASN CG  OD1  doub N N 141 
ASN CG  ND2  sing N N 142 
ASN ND2 HD21 sing N N 143 
ASN ND2 HD22 sing N N 144 
ASN OXT HXT  sing N N 145 
ASP N   CA   sing N N 146 
ASP N   H    sing N N 147 
ASP N   H2   sing N N 148 
ASP CA  C    sing N N 149 
ASP CA  CB   sing N N 150 
ASP CA  HA   sing N N 151 
ASP C   O    doub N N 152 
ASP C   OXT  sing N N 153 
ASP CB  CG   sing N N 154 
ASP CB  HB2  sing N N 155 
ASP CB  HB3  sing N N 156 
ASP CG  OD1  doub N N 157 
ASP CG  OD2  sing N N 158 
ASP OD2 HD2  sing N N 159 
ASP OXT HXT  sing N N 160 
CYS N   CA   sing N N 161 
CYS N   H    sing N N 162 
CYS N   H2   sing N N 163 
CYS CA  C    sing N N 164 
CYS CA  CB   sing N N 165 
CYS CA  HA   sing N N 166 
CYS C   O    doub N N 167 
CYS C   OXT  sing N N 168 
CYS CB  SG   sing N N 169 
CYS CB  HB2  sing N N 170 
CYS CB  HB3  sing N N 171 
CYS SG  HG   sing N N 172 
CYS OXT HXT  sing N N 173 
EDO C1  O1   sing N N 174 
EDO C1  C2   sing N N 175 
EDO C1  H11  sing N N 176 
EDO C1  H12  sing N N 177 
EDO O1  HO1  sing N N 178 
EDO C2  O2   sing N N 179 
EDO C2  H21  sing N N 180 
EDO C2  H22  sing N N 181 
EDO O2  HO2  sing N N 182 
GLN N   CA   sing N N 183 
GLN N   H    sing N N 184 
GLN N   H2   sing N N 185 
GLN CA  C    sing N N 186 
GLN CA  CB   sing N N 187 
GLN CA  HA   sing N N 188 
GLN C   O    doub N N 189 
GLN C   OXT  sing N N 190 
GLN CB  CG   sing N N 191 
GLN CB  HB2  sing N N 192 
GLN CB  HB3  sing N N 193 
GLN CG  CD   sing N N 194 
GLN CG  HG2  sing N N 195 
GLN CG  HG3  sing N N 196 
GLN CD  OE1  doub N N 197 
GLN CD  NE2  sing N N 198 
GLN NE2 HE21 sing N N 199 
GLN NE2 HE22 sing N N 200 
GLN OXT HXT  sing N N 201 
GLU N   CA   sing N N 202 
GLU N   H    sing N N 203 
GLU N   H2   sing N N 204 
GLU CA  C    sing N N 205 
GLU CA  CB   sing N N 206 
GLU CA  HA   sing N N 207 
GLU C   O    doub N N 208 
GLU C   OXT  sing N N 209 
GLU CB  CG   sing N N 210 
GLU CB  HB2  sing N N 211 
GLU CB  HB3  sing N N 212 
GLU CG  CD   sing N N 213 
GLU CG  HG2  sing N N 214 
GLU CG  HG3  sing N N 215 
GLU CD  OE1  doub N N 216 
GLU CD  OE2  sing N N 217 
GLU OE2 HE2  sing N N 218 
GLU OXT HXT  sing N N 219 
GLY N   CA   sing N N 220 
GLY N   H    sing N N 221 
GLY N   H2   sing N N 222 
GLY CA  C    sing N N 223 
GLY CA  HA2  sing N N 224 
GLY CA  HA3  sing N N 225 
GLY C   O    doub N N 226 
GLY C   OXT  sing N N 227 
GLY OXT HXT  sing N N 228 
GOL C1  O1   sing N N 229 
GOL C1  C2   sing N N 230 
GOL C1  H11  sing N N 231 
GOL C1  H12  sing N N 232 
GOL O1  HO1  sing N N 233 
GOL C2  O2   sing N N 234 
GOL C2  C3   sing N N 235 
GOL C2  H2   sing N N 236 
GOL O2  HO2  sing N N 237 
GOL C3  O3   sing N N 238 
GOL C3  H31  sing N N 239 
GOL C3  H32  sing N N 240 
GOL O3  HO3  sing N N 241 
HIS N   CA   sing N N 242 
HIS N   H    sing N N 243 
HIS N   H2   sing N N 244 
HIS CA  C    sing N N 245 
HIS CA  CB   sing N N 246 
HIS CA  HA   sing N N 247 
HIS C   O    doub N N 248 
HIS C   OXT  sing N N 249 
HIS CB  CG   sing N N 250 
HIS CB  HB2  sing N N 251 
HIS CB  HB3  sing N N 252 
HIS CG  ND1  sing Y N 253 
HIS CG  CD2  doub Y N 254 
HIS ND1 CE1  doub Y N 255 
HIS ND1 HD1  sing N N 256 
HIS CD2 NE2  sing Y N 257 
HIS CD2 HD2  sing N N 258 
HIS CE1 NE2  sing Y N 259 
HIS CE1 HE1  sing N N 260 
HIS NE2 HE2  sing N N 261 
HIS OXT HXT  sing N N 262 
HOH O   H1   sing N N 263 
HOH O   H2   sing N N 264 
ILE N   CA   sing N N 265 
ILE N   H    sing N N 266 
ILE N   H2   sing N N 267 
ILE CA  C    sing N N 268 
ILE CA  CB   sing N N 269 
ILE CA  HA   sing N N 270 
ILE C   O    doub N N 271 
ILE C   OXT  sing N N 272 
ILE CB  CG1  sing N N 273 
ILE CB  CG2  sing N N 274 
ILE CB  HB   sing N N 275 
ILE CG1 CD1  sing N N 276 
ILE CG1 HG12 sing N N 277 
ILE CG1 HG13 sing N N 278 
ILE CG2 HG21 sing N N 279 
ILE CG2 HG22 sing N N 280 
ILE CG2 HG23 sing N N 281 
ILE CD1 HD11 sing N N 282 
ILE CD1 HD12 sing N N 283 
ILE CD1 HD13 sing N N 284 
ILE OXT HXT  sing N N 285 
LEU N   CA   sing N N 286 
LEU N   H    sing N N 287 
LEU N   H2   sing N N 288 
LEU CA  C    sing N N 289 
LEU CA  CB   sing N N 290 
LEU CA  HA   sing N N 291 
LEU C   O    doub N N 292 
LEU C   OXT  sing N N 293 
LEU CB  CG   sing N N 294 
LEU CB  HB2  sing N N 295 
LEU CB  HB3  sing N N 296 
LEU CG  CD1  sing N N 297 
LEU CG  CD2  sing N N 298 
LEU CG  HG   sing N N 299 
LEU CD1 HD11 sing N N 300 
LEU CD1 HD12 sing N N 301 
LEU CD1 HD13 sing N N 302 
LEU CD2 HD21 sing N N 303 
LEU CD2 HD22 sing N N 304 
LEU CD2 HD23 sing N N 305 
LEU OXT HXT  sing N N 306 
LYS N   CA   sing N N 307 
LYS N   H    sing N N 308 
LYS N   H2   sing N N 309 
LYS CA  C    sing N N 310 
LYS CA  CB   sing N N 311 
LYS CA  HA   sing N N 312 
LYS C   O    doub N N 313 
LYS C   OXT  sing N N 314 
LYS CB  CG   sing N N 315 
LYS CB  HB2  sing N N 316 
LYS CB  HB3  sing N N 317 
LYS CG  CD   sing N N 318 
LYS CG  HG2  sing N N 319 
LYS CG  HG3  sing N N 320 
LYS CD  CE   sing N N 321 
LYS CD  HD2  sing N N 322 
LYS CD  HD3  sing N N 323 
LYS CE  NZ   sing N N 324 
LYS CE  HE2  sing N N 325 
LYS CE  HE3  sing N N 326 
LYS NZ  HZ1  sing N N 327 
LYS NZ  HZ2  sing N N 328 
LYS NZ  HZ3  sing N N 329 
LYS OXT HXT  sing N N 330 
MET N   CA   sing N N 331 
MET N   H    sing N N 332 
MET N   H2   sing N N 333 
MET CA  C    sing N N 334 
MET CA  CB   sing N N 335 
MET CA  HA   sing N N 336 
MET C   O    doub N N 337 
MET C   OXT  sing N N 338 
MET CB  CG   sing N N 339 
MET CB  HB2  sing N N 340 
MET CB  HB3  sing N N 341 
MET CG  SD   sing N N 342 
MET CG  HG2  sing N N 343 
MET CG  HG3  sing N N 344 
MET SD  CE   sing N N 345 
MET CE  HE1  sing N N 346 
MET CE  HE2  sing N N 347 
MET CE  HE3  sing N N 348 
MET OXT HXT  sing N N 349 
PE4 O1  C1   sing N N 350 
PE4 O1  HO1  sing N N 351 
PE4 C1  C2   sing N N 352 
PE4 C1  H11  sing N N 353 
PE4 C1  H12  sing N N 354 
PE4 C2  O2   sing N N 355 
PE4 C2  H21  sing N N 356 
PE4 C2  H22  sing N N 357 
PE4 O2  C3   sing N N 358 
PE4 C3  C4   sing N N 359 
PE4 C3  H31  sing N N 360 
PE4 C3  H32  sing N N 361 
PE4 C4  O3   sing N N 362 
PE4 C4  H41  sing N N 363 
PE4 C4  H42  sing N N 364 
PE4 O3  C5   sing N N 365 
PE4 C5  C6   sing N N 366 
PE4 C5  H51  sing N N 367 
PE4 C5  H52  sing N N 368 
PE4 C6  O4   sing N N 369 
PE4 C6  H61  sing N N 370 
PE4 C6  H62  sing N N 371 
PE4 O4  C7   sing N N 372 
PE4 C7  C8   sing N N 373 
PE4 C7  H71  sing N N 374 
PE4 C7  H72  sing N N 375 
PE4 C8  O5   sing N N 376 
PE4 C8  H81  sing N N 377 
PE4 C8  H82  sing N N 378 
PE4 O5  C9   sing N N 379 
PE4 C9  C10  sing N N 380 
PE4 C9  H91  sing N N 381 
PE4 C9  H92  sing N N 382 
PE4 C10 O6   sing N N 383 
PE4 C10 H101 sing N N 384 
PE4 C10 H102 sing N N 385 
PE4 O6  C11  sing N N 386 
PE4 C11 C12  sing N N 387 
PE4 C11 H111 sing N N 388 
PE4 C11 H112 sing N N 389 
PE4 C12 O7   sing N N 390 
PE4 C12 H121 sing N N 391 
PE4 C12 H122 sing N N 392 
PE4 O7  C13  sing N N 393 
PE4 C13 C14  sing N N 394 
PE4 C13 H131 sing N N 395 
PE4 C13 H132 sing N N 396 
PE4 C14 O8   sing N N 397 
PE4 C14 H141 sing N N 398 
PE4 C14 H142 sing N N 399 
PE4 O8  C15  sing N N 400 
PE4 C15 C16  sing N N 401 
PE4 C15 H151 sing N N 402 
PE4 C15 H152 sing N N 403 
PE4 C16 H161 sing N N 404 
PE4 C16 H162 sing N N 405 
PE4 C16 H163 sing N N 406 
PEG C1  O1   sing N N 407 
PEG C1  C2   sing N N 408 
PEG C1  H11  sing N N 409 
PEG C1  H12  sing N N 410 
PEG O1  HO1  sing N N 411 
PEG C2  O2   sing N N 412 
PEG C2  H21  sing N N 413 
PEG C2  H22  sing N N 414 
PEG O2  C3   sing N N 415 
PEG C3  C4   sing N N 416 
PEG C3  H31  sing N N 417 
PEG C3  H32  sing N N 418 
PEG C4  O4   sing N N 419 
PEG C4  H41  sing N N 420 
PEG C4  H42  sing N N 421 
PEG O4  HO4  sing N N 422 
PHE N   CA   sing N N 423 
PHE N   H    sing N N 424 
PHE N   H2   sing N N 425 
PHE CA  C    sing N N 426 
PHE CA  CB   sing N N 427 
PHE CA  HA   sing N N 428 
PHE C   O    doub N N 429 
PHE C   OXT  sing N N 430 
PHE CB  CG   sing N N 431 
PHE CB  HB2  sing N N 432 
PHE CB  HB3  sing N N 433 
PHE CG  CD1  doub Y N 434 
PHE CG  CD2  sing Y N 435 
PHE CD1 CE1  sing Y N 436 
PHE CD1 HD1  sing N N 437 
PHE CD2 CE2  doub Y N 438 
PHE CD2 HD2  sing N N 439 
PHE CE1 CZ   doub Y N 440 
PHE CE1 HE1  sing N N 441 
PHE CE2 CZ   sing Y N 442 
PHE CE2 HE2  sing N N 443 
PHE CZ  HZ   sing N N 444 
PHE OXT HXT  sing N N 445 
PRO N   CA   sing N N 446 
PRO N   CD   sing N N 447 
PRO N   H    sing N N 448 
PRO CA  C    sing N N 449 
PRO CA  CB   sing N N 450 
PRO CA  HA   sing N N 451 
PRO C   O    doub N N 452 
PRO C   OXT  sing N N 453 
PRO CB  CG   sing N N 454 
PRO CB  HB2  sing N N 455 
PRO CB  HB3  sing N N 456 
PRO CG  CD   sing N N 457 
PRO CG  HG2  sing N N 458 
PRO CG  HG3  sing N N 459 
PRO CD  HD2  sing N N 460 
PRO CD  HD3  sing N N 461 
PRO OXT HXT  sing N N 462 
SER N   CA   sing N N 463 
SER N   H    sing N N 464 
SER N   H2   sing N N 465 
SER CA  C    sing N N 466 
SER CA  CB   sing N N 467 
SER CA  HA   sing N N 468 
SER C   O    doub N N 469 
SER C   OXT  sing N N 470 
SER CB  OG   sing N N 471 
SER CB  HB2  sing N N 472 
SER CB  HB3  sing N N 473 
SER OG  HG   sing N N 474 
SER OXT HXT  sing N N 475 
SF4 FE1 S2   sing N N 476 
SF4 FE1 S3   sing N N 477 
SF4 FE1 S4   sing N N 478 
SF4 FE2 S1   sing N N 479 
SF4 FE2 S3   sing N N 480 
SF4 FE2 S4   sing N N 481 
SF4 FE3 S1   sing N N 482 
SF4 FE3 S2   sing N N 483 
SF4 FE3 S4   sing N N 484 
SF4 FE4 S1   sing N N 485 
SF4 FE4 S2   sing N N 486 
SF4 FE4 S3   sing N N 487 
THR N   CA   sing N N 488 
THR N   H    sing N N 489 
THR N   H2   sing N N 490 
THR CA  C    sing N N 491 
THR CA  CB   sing N N 492 
THR CA  HA   sing N N 493 
THR C   O    doub N N 494 
THR C   OXT  sing N N 495 
THR CB  OG1  sing N N 496 
THR CB  CG2  sing N N 497 
THR CB  HB   sing N N 498 
THR OG1 HG1  sing N N 499 
THR CG2 HG21 sing N N 500 
THR CG2 HG22 sing N N 501 
THR CG2 HG23 sing N N 502 
THR OXT HXT  sing N N 503 
TRP N   CA   sing N N 504 
TRP N   H    sing N N 505 
TRP N   H2   sing N N 506 
TRP CA  C    sing N N 507 
TRP CA  CB   sing N N 508 
TRP CA  HA   sing N N 509 
TRP C   O    doub N N 510 
TRP C   OXT  sing N N 511 
TRP CB  CG   sing N N 512 
TRP CB  HB2  sing N N 513 
TRP CB  HB3  sing N N 514 
TRP CG  CD1  doub Y N 515 
TRP CG  CD2  sing Y N 516 
TRP CD1 NE1  sing Y N 517 
TRP CD1 HD1  sing N N 518 
TRP CD2 CE2  doub Y N 519 
TRP CD2 CE3  sing Y N 520 
TRP NE1 CE2  sing Y N 521 
TRP NE1 HE1  sing N N 522 
TRP CE2 CZ2  sing Y N 523 
TRP CE3 CZ3  doub Y N 524 
TRP CE3 HE3  sing N N 525 
TRP CZ2 CH2  doub Y N 526 
TRP CZ2 HZ2  sing N N 527 
TRP CZ3 CH2  sing Y N 528 
TRP CZ3 HZ3  sing N N 529 
TRP CH2 HH2  sing N N 530 
TRP OXT HXT  sing N N 531 
TRS C   C1   sing N N 532 
TRS C   C2   sing N N 533 
TRS C   C3   sing N N 534 
TRS C   N    sing N N 535 
TRS C1  O1   sing N N 536 
TRS C1  H11  sing N N 537 
TRS C1  H12  sing N N 538 
TRS C2  O2   sing N N 539 
TRS C2  H21  sing N N 540 
TRS C2  H22  sing N N 541 
TRS C3  O3   sing N N 542 
TRS C3  H31  sing N N 543 
TRS C3  H32  sing N N 544 
TRS N   HN1  sing N N 545 
TRS N   HN2  sing N N 546 
TRS N   HN3  sing N N 547 
TRS O1  HO1  sing N N 548 
TRS O2  HO2  sing N N 549 
TRS O3  HO3  sing N N 550 
TYR N   CA   sing N N 551 
TYR N   H    sing N N 552 
TYR N   H2   sing N N 553 
TYR CA  C    sing N N 554 
TYR CA  CB   sing N N 555 
TYR CA  HA   sing N N 556 
TYR C   O    doub N N 557 
TYR C   OXT  sing N N 558 
TYR CB  CG   sing N N 559 
TYR CB  HB2  sing N N 560 
TYR CB  HB3  sing N N 561 
TYR CG  CD1  doub Y N 562 
TYR CG  CD2  sing Y N 563 
TYR CD1 CE1  sing Y N 564 
TYR CD1 HD1  sing N N 565 
TYR CD2 CE2  doub Y N 566 
TYR CD2 HD2  sing N N 567 
TYR CE1 CZ   doub Y N 568 
TYR CE1 HE1  sing N N 569 
TYR CE2 CZ   sing Y N 570 
TYR CE2 HE2  sing N N 571 
TYR CZ  OH   sing N N 572 
TYR OH  HH   sing N N 573 
TYR OXT HXT  sing N N 574 
VAL N   CA   sing N N 575 
VAL N   H    sing N N 576 
VAL N   H2   sing N N 577 
VAL CA  C    sing N N 578 
VAL CA  CB   sing N N 579 
VAL CA  HA   sing N N 580 
VAL C   O    doub N N 581 
VAL C   OXT  sing N N 582 
VAL CB  CG1  sing N N 583 
VAL CB  CG2  sing N N 584 
VAL CB  HB   sing N N 585 
VAL CG1 HG11 sing N N 586 
VAL CG1 HG12 sing N N 587 
VAL CG1 HG13 sing N N 588 
VAL CG2 HG21 sing N N 589 
VAL CG2 HG22 sing N N 590 
VAL CG2 HG23 sing N N 591 
VAL OXT HXT  sing N N 592 
XCC FE1 S2   sing N N 593 
XCC FE1 S4   sing N N 594 
XCC FE1 S3   sing N N 595 
XCC FE2 S3   sing N N 596 
XCC FE3 S1   sing N N 597 
XCC FE3 S2   sing N N 598 
XCC FE3 S4   sing N N 599 
XCC FE4 S1   sing N N 600 
XCC FE4 S2   sing N N 601 
XCC FE4 S3   sing N N 602 
XCC S1  NI   sing N N 603 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Max Planck Society'               Germany ?                          1 
'German Research Foundation (DFG)' Germany 'DFG-SPP 1927 WA 4053/1-1' 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6YTT 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9G7I 
_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]   0.003355 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.003355 
_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]   0.007842 
_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  
CA 
CL 
FE 
N  
NI 
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   . MET A  1  1   ? 112.245 -4.893  57.993  1.00 71.45  ?  1   MET A N   1 
ATOM   2     C  CA  . MET A  1  1   ? 113.468 -4.390  57.374  1.00 61.92  ?  1   MET A CA  1 
ATOM   3     C  C   . MET A  1  1   ? 113.321 -4.366  55.868  1.00 68.74  ?  1   MET A C   1 
ATOM   4     O  O   . MET A  1  1   ? 112.629 -5.213  55.305  1.00 85.66  ?  1   MET A O   1 
ATOM   5     C  CB  . MET A  1  1   ? 114.656 -5.307  57.684  1.00 65.31  ?  1   MET A CB  1 
ATOM   6     C  CG  . MET A  1  1   ? 114.977 -5.458  59.138  1.00 64.85  ?  1   MET A CG  1 
ATOM   7     S  SD  . MET A  1  1   ? 116.096 -6.863  59.378  1.00 88.71  ?  1   MET A SD  1 
ATOM   8     C  CE  . MET A  1  1   ? 117.609 -6.088  59.167  1.00 72.72  ?  1   MET A CE  1 
ATOM   9     N  N   . ASN A  1  2   ? 114.007 -3.437  55.206  1.00 65.96  ?  2   ASN A N   1 
ATOM   10    C  CA  . ASN A  1  2   ? 113.979 -3.366  53.746  1.00 72.83  ?  2   ASN A CA  1 
ATOM   11    C  C   . ASN A  1  2   ? 114.882 -4.485  53.180  1.00 66.94  ?  2   ASN A C   1 
ATOM   12    O  O   . ASN A  1  2   ? 115.591 -5.149  53.942  1.00 57.76  ?  2   ASN A O   1 
ATOM   13    C  CB  . ASN A  1  2   ? 114.434 -1.983  53.261  1.00 71.98  ?  2   ASN A CB  1 
ATOM   14    C  CG  . ASN A  1  2   ? 115.710 -1.504  53.906  1.00 68.10  ?  2   ASN A CG  1 
ATOM   15    O  OD1 . ASN A  1  2   ? 116.759 -2.138  53.808  1.00 61.13  ?  2   ASN A OD1 1 
ATOM   16    N  ND2 . ASN A  1  2   ? 115.651 -0.373  54.590  1.00 86.22  ?  2   ASN A ND2 1 
ATOM   17    N  N   . LEU A  1  3   ? 114.863 -4.703  51.853  1.00 63.17  ?  3   LEU A N   1 
ATOM   18    C  CA  . LEU A  1  3   ? 115.687 -5.741  51.242  1.00 52.61  ?  3   LEU A CA  1 
ATOM   19    C  C   . LEU A  1  3   ? 117.173 -5.554  51.578  1.00 66.90  ?  3   LEU A C   1 
ATOM   20    O  O   . LEU A  1  3   ? 117.862 -6.526  51.877  1.00 70.33  ?  3   LEU A O   1 
ATOM   21    C  CB  . LEU A  1  3   ? 115.491 -5.739  49.713  1.00 48.87  ?  3   LEU A CB  1 
ATOM   22    C  CG  . LEU A  1  3   ? 116.178 -6.854  48.915  1.00 50.43  ?  3   LEU A CG  1 
ATOM   23    C  CD1 . LEU A  1  3   ? 115.860 -8.235  49.476  1.00 45.17  ?  3   LEU A CD1 1 
ATOM   24    C  CD2 . LEU A  1  3   ? 115.777 -6.792  47.461  1.00 41.51  ?  3   LEU A CD2 1 
ATOM   25    N  N   . PHE A  1  4   ? 117.660 -4.310  51.546  1.00 67.54  ?  4   PHE A N   1 
ATOM   26    C  CA  . PHE A  1  4   ? 119.061 -4.020  51.832  1.00 55.51  ?  4   PHE A CA  1 
ATOM   27    C  C   . PHE A  1  4   ? 119.474 -4.452  53.231  1.00 57.30  ?  4   PHE A C   1 
ATOM   28    O  O   . PHE A  1  4   ? 120.397 -5.250  53.381  1.00 62.03  ?  4   PHE A O   1 
ATOM   29    C  CB  . PHE A  1  4   ? 119.356 -2.520  51.626  1.00 62.98  ?  4   PHE A CB  1 
ATOM   30    C  CG  . PHE A  1  4   ? 119.590 -2.165  50.182  1.00 57.20  ?  4   PHE A CG  1 
ATOM   31    C  CD1 . PHE A  1  4   ? 118.529 -2.007  49.312  1.00 64.83  ?  4   PHE A CD1 1 
ATOM   32    C  CD2 . PHE A  1  4   ? 120.871 -2.095  49.672  1.00 62.57  ?  4   PHE A CD2 1 
ATOM   33    C  CE1 . PHE A  1  4   ? 118.747 -1.739  47.969  1.00 64.90  ?  4   PHE A CE1 1 
ATOM   34    C  CE2 . PHE A  1  4   ? 121.086 -1.822  48.331  1.00 62.12  ?  4   PHE A CE2 1 
ATOM   35    C  CZ  . PHE A  1  4   ? 120.023 -1.640  47.488  1.00 66.84  ?  4   PHE A CZ  1 
ATOM   36    N  N   . GLN A  1  5   ? 118.787 -3.950  54.255  1.00 65.62  ?  5   GLN A N   1 
ATOM   37    C  CA  . GLN A  1  5   ? 119.119 -4.277  55.635  1.00 61.12  ?  5   GLN A CA  1 
ATOM   38    C  C   . GLN A  1  5   ? 118.993 -5.776  55.898  1.00 67.67  ?  5   GLN A C   1 
ATOM   39    O  O   . GLN A  1  5   ? 119.803 -6.328  56.642  1.00 79.49  ?  5   GLN A O   1 
ATOM   40    C  CB  . GLN A  1  5   ? 118.265 -3.451  56.612  1.00 59.48  ?  5   GLN A CB  1 
ATOM   41    C  CG  . GLN A  1  5   ? 118.488 -1.938  56.518  1.00 68.77  ?  5   GLN A CG  1 
ATOM   42    C  CD  . GLN A  1  5   ? 119.945 -1.534  56.627  1.00 78.21  ?  5   GLN A CD  1 
ATOM   43    O  OE1 . GLN A  1  5   ? 120.710 -2.072  57.441  1.00 76.31  ?  5   GLN A OE1 1 
ATOM   44    N  NE2 . GLN A  1  5   ? 120.367 -0.575  55.805  1.00 76.48  ?  5   GLN A NE2 1 
ATOM   45    N  N   . THR A  1  6   ? 118.021 -6.448  55.260  1.00 69.34  ?  6   THR A N   1 
ATOM   46    C  CA  . THR A  1  6   ? 117.849 -7.892  55.421  1.00 64.63  ?  6   THR A CA  1 
ATOM   47    C  C   . THR A  1  6   ? 119.103 -8.617  54.915  1.00 62.29  ?  6   THR A C   1 
ATOM   48    O  O   . THR A  1  6   ? 119.632 -9.484  55.606  1.00 70.64  ?  6   THR A O   1 
ATOM   49    C  CB  . THR A  1  6   ? 116.589 -8.360  54.678  1.00 62.88  ?  6   THR A CB  1 
ATOM   50    O  OG1 . THR A  1  6   ? 115.457 -7.658  55.196  1.00 68.40  ?  6   THR A OG1 1 
ATOM   51    C  CG2 . THR A  1  6   ? 116.362 -9.855  54.802  1.00 54.71  ?  6   THR A CG2 1 
ATOM   52    N  N   . VAL A  1  7   ? 119.593 -8.237  53.725  1.00 60.20  ?  7   VAL A N   1 
ATOM   53    C  CA  . VAL A  1  7   ? 120.787 -8.843  53.135  1.00 56.73  ?  7   VAL A CA  1 
ATOM   54    C  C   . VAL A  1  7   ? 122.016 -8.571  54.017  1.00 61.58  ?  7   VAL A C   1 
ATOM   55    O  O   . VAL A  1  7   ? 122.781 -9.494  54.296  1.00 65.01  ?  7   VAL A O   1 
ATOM   56    C  CB  . VAL A  1  7   ? 121.000 -8.350  51.680  1.00 49.67  ?  7   VAL A CB  1 
ATOM   57    C  CG1 . VAL A  1  7   ? 122.390 -8.707  51.170  1.00 58.72  ?  7   VAL A CG1 1 
ATOM   58    C  CG2 . VAL A  1  7   ? 119.934 -8.918  50.753  1.00 66.62  ?  7   VAL A CG2 1 
ATOM   59    N  N   . PHE A  1  8   ? 122.205 -7.323  54.466  1.00 55.67  ?  8   PHE A N   1 
ATOM   60    C  CA  . PHE A  1  8   ? 123.351 -6.986  55.313  1.00 63.25  ?  8   PHE A CA  1 
ATOM   61    C  C   . PHE A  1  8   ? 123.305 -7.858  56.558  1.00 63.71  ?  8   PHE A C   1 
ATOM   62    O  O   . PHE A  1  8   ? 124.298 -8.495  56.901  1.00 67.33  ?  8   PHE A O   1 
ATOM   63    C  CB  . PHE A  1  8   ? 123.378 -5.482  55.633  1.00 61.89  ?  8   PHE A CB  1 
ATOM   64    C  CG  . PHE A  1  8   ? 123.533 -4.570  54.437  1.00 61.40  ?  8   PHE A CG  1 
ATOM   65    C  CD1 . PHE A  1  8   ? 124.423 -4.876  53.419  1.00 56.26  ?  8   PHE A CD1 1 
ATOM   66    C  CD2 . PHE A  1  8   ? 122.787 -3.410  54.330  1.00 69.14  ?  8   PHE A CD2 1 
ATOM   67    C  CE1 . PHE A  1  8   ? 124.558 -4.041  52.318  1.00 67.19  ?  8   PHE A CE1 1 
ATOM   68    C  CE2 . PHE A  1  8   ? 122.916 -2.582  53.221  1.00 67.24  ?  8   PHE A CE2 1 
ATOM   69    C  CZ  . PHE A  1  8   ? 123.806 -2.899  52.226  1.00 67.31  ?  8   PHE A CZ  1 
ATOM   70    N  N   . THR A  1  9   ? 122.149 -7.899  57.224  1.00 63.58  ?  9   THR A N   1 
ATOM   71    C  CA  . THR A  1  9   ? 121.975 -8.707  58.428  1.00 70.63  ?  9   THR A CA  1 
ATOM   72    C  C   . THR A  1  9   ? 122.377 -10.173 58.241  1.00 73.39  ?  9   THR A C   1 
ATOM   73    O  O   . THR A  1  9   ? 123.124 -10.705 59.060  1.00 82.29  ?  9   THR A O   1 
ATOM   74    C  CB  . THR A  1  9   ? 120.539 -8.588  58.935  1.00 62.25  ?  9   THR A CB  1 
ATOM   75    O  OG1 . THR A  1  9   ? 120.276 -7.214  59.224  1.00 69.26  ?  9   THR A OG1 1 
ATOM   76    C  CG2 . THR A  1  9   ? 120.287 -9.445  60.165  1.00 72.66  ?  9   THR A CG2 1 
ATOM   77    N  N   . GLY A  1  10  ? 121.885 -10.806 57.177  1.00 65.29  ?  10  GLY A N   1 
ATOM   78    C  CA  . GLY A  1  10  ? 122.199 -12.198 56.883  1.00 68.25  ?  10  GLY A CA  1 
ATOM   79    C  C   . GLY A  1  10  ? 123.664 -12.406 56.557  1.00 70.99  ?  10  GLY A C   1 
ATOM   80    O  O   . GLY A  1  10  ? 124.223 -13.456 56.880  1.00 72.55  ?  10  GLY A O   1 
ATOM   81    N  N   . SER A  1  11  ? 124.306 -11.405 55.920  1.00 68.28  ?  11  SER A N   1 
ATOM   82    C  CA  . SER A  1  11  ? 125.731 -11.479 55.581  1.00 58.23  ?  11  SER A CA  1 
ATOM   83    C  C   . SER A  1  11  ? 126.553 -11.428 56.854  1.00 59.76  ?  11  SER A C   1 
ATOM   84    O  O   . SER A  1  11  ? 127.532 -12.158 56.976  1.00 61.95  ?  11  SER A O   1 
ATOM   85    C  CB  . SER A  1  11  ? 126.140 -10.330 54.664  1.00 56.52  ?  11  SER A CB  1 
ATOM   86    O  OG  . SER A  1  11  ? 125.610 -10.437 53.352  1.00 65.84  ?  11  SER A OG  1 
ATOM   87    N  N   . LYS A  1  12  ? 126.155 -10.579 57.812  1.00 59.53  ?  12  LYS A N   1 
ATOM   88    C  CA  . LYS A  1  12  ? 126.853 -10.490 59.088  1.00 68.31  ?  12  LYS A CA  1 
ATOM   89    C  C   . LYS A  1  12  ? 126.694 -11.820 59.840  1.00 65.64  ?  12  LYS A C   1 
ATOM   90    O  O   . LYS A  1  12  ? 127.658 -12.298 60.428  1.00 58.70  ?  12  LYS A O   1 
ATOM   91    C  CB  . LYS A  1  12  ? 126.322 -9.304  59.915  1.00 78.06  ?  12  LYS A CB  1 
ATOM   92    C  CG  . LYS A  1  12  ? 126.980 -7.956  59.558  1.00 70.41  ?  12  LYS A CG  1 
ATOM   93    C  CD  . LYS A  1  12  ? 125.992 -6.834  59.260  1.00 65.03  ?  12  LYS A CD  1 
ATOM   94    C  CE  . LYS A  1  12  ? 125.277 -6.322  60.489  1.00 71.26  ?  12  LYS A CE  1 
ATOM   95    N  NZ  . LYS A  1  12  ? 124.344 -5.205  60.171  1.00 78.18  ?  12  LYS A NZ  1 
ATOM   96    N  N   . GLN A  1  13  ? 125.497 -12.436 59.776  1.00 69.72  ?  13  GLN A N   1 
ATOM   97    C  CA  . GLN A  1  13  ? 125.228 -13.735 60.399  1.00 62.28  ?  13  GLN A CA  1 
ATOM   98    C  C   . GLN A  1  13  ? 126.136 -14.796 59.752  1.00 73.65  ?  13  GLN A C   1 
ATOM   99    O  O   . GLN A  1  13  ? 126.690 -15.641 60.456  1.00 69.52  ?  13  GLN A O   1 
ATOM   100   C  CB  . GLN A  1  13  ? 123.755 -14.142 60.208  1.00 62.30  ?  13  GLN A CB  1 
ATOM   101   C  CG  . GLN A  1  13  ? 122.767 -13.341 61.045  1.00 64.65  ?  13  GLN A CG  1 
ATOM   102   C  CD  . GLN A  1  13  ? 121.319 -13.642 60.710  1.00 78.69  ?  13  GLN A CD  1 
ATOM   103   O  OE1 . GLN A  1  13  ? 120.997 -14.560 59.940  1.00 70.97  ?  13  GLN A OE1 1 
ATOM   104   N  NE2 . GLN A  1  13  ? 120.402 -12.867 61.284  1.00 75.02  ?  13  GLN A NE2 1 
ATOM   105   N  N   . ALA A  1  14  ? 126.284 -14.749 58.409  1.00 72.42  ?  14  ALA A N   1 
ATOM   106   C  CA  . ALA A  1  14  ? 127.135 -15.677 57.665  1.00 56.20  ?  14  ALA A CA  1 
ATOM   107   C  C   . ALA A  1  14  ? 128.586 -15.520 58.113  1.00 67.99  ?  14  ALA A C   1 
ATOM   108   O  O   . ALA A  1  14  ? 129.268 -16.518 58.321  1.00 71.28  ?  14  ALA A O   1 
ATOM   109   C  CB  . ALA A  1  14  ? 127.015 -15.416 56.169  1.00 48.25  ?  14  ALA A CB  1 
ATOM   110   N  N   . LEU A  1  15  ? 129.054 -14.273 58.282  1.00 66.97  ?  15  LEU A N   1 
ATOM   111   C  CA  . LEU A  1  15  ? 130.413 -14.015 58.742  1.00 64.81  ?  15  LEU A CA  1 
ATOM   112   C  C   . LEU A  1  15  ? 130.575 -14.553 60.171  1.00 73.03  ?  15  LEU A C   1 
ATOM   113   O  O   . LEU A  1  15  ? 131.570 -15.212 60.465  1.00 80.48  ?  15  LEU A O   1 
ATOM   114   C  CB  . LEU A  1  15  ? 130.704 -12.503 58.694  1.00 62.55  ?  15  LEU A CB  1 
ATOM   115   C  CG  . LEU A  1  15  ? 131.992 -12.022 59.365  1.00 54.61  ?  15  LEU A CG  1 
ATOM   116   C  CD1 . LEU A  1  15  ? 133.223 -12.477 58.602  1.00 59.62  ?  15  LEU A CD1 1 
ATOM   117   C  CD2 . LEU A  1  15  ? 131.996 -10.516 59.477  1.00 69.04  ?  15  LEU A CD2 1 
ATOM   118   N  N   . ALA A  1  16  ? 129.591 -14.296 61.047  1.00 67.74  ?  16  ALA A N   1 
ATOM   119   C  CA  . ALA A  1  16  ? 129.628 -14.764 62.435  1.00 70.41  ?  16  ALA A CA  1 
ATOM   120   C  C   . ALA A  1  16  ? 129.732 -16.287 62.497  1.00 80.81  ?  16  ALA A C   1 
ATOM   121   O  O   . ALA A  1  16  ? 130.438 -16.819 63.352  1.00 82.11  ?  16  ALA A O   1 
ATOM   122   C  CB  . ALA A  1  16  ? 128.384 -14.298 63.176  1.00 61.31  ?  16  ALA A CB  1 
ATOM   123   N  N   . ALA A  1  17  ? 129.032 -16.984 61.592  1.00 81.03  ?  17  ALA A N   1 
ATOM   124   C  CA  . ALA A  1  17  ? 129.065 -18.442 61.534  1.00 70.94  ?  17  ALA A CA  1 
ATOM   125   C  C   . ALA A  1  17  ? 130.435 -18.924 61.043  1.00 71.60  ?  17  ALA A C   1 
ATOM   126   O  O   . ALA A  1  17  ? 130.929 -19.950 61.509  1.00 73.75  ?  17  ALA A O   1 
ATOM   127   C  CB  . ALA A  1  17  ? 127.974 -18.945 60.607  1.00 62.24  ?  17  ALA A CB  1 
ATOM   128   N  N   . ALA A  1  18  ? 131.045 -18.187 60.101  1.00 74.25  ?  18  ALA A N   1 
ATOM   129   C  CA  . ALA A  1  18  ? 132.357 -18.531 59.561  1.00 67.98  ?  18  ALA A CA  1 
ATOM   130   C  C   . ALA A  1  18  ? 133.481 -18.227 60.539  1.00 71.24  ?  18  ALA A C   1 
ATOM   131   O  O   . ALA A  1  18  ? 134.543 -18.832 60.447  1.00 77.62  ?  18  ALA A O   1 
ATOM   132   C  CB  . ALA A  1  18  ? 132.637 -17.713 58.313  1.00 62.70  ?  18  ALA A CB  1 
ATOM   133   N  N   . GLU A  1  19  ? 133.259 -17.298 61.474  1.00 57.74  ?  19  GLU A N   1 
ATOM   134   C  CA  . GLU A  1  19  ? 134.271 -16.960 62.467  1.00 69.09  ?  19  GLU A CA  1 
ATOM   135   C  C   . GLU A  1  19  ? 134.271 -18.081 63.520  1.00 86.30  ?  19  GLU A C   1 
ATOM   136   O  O   . GLU A  1  19  ? 135.337 -18.521 63.955  1.00 90.50  ?  19  GLU A O   1 
ATOM   137   C  CB  . GLU A  1  19  ? 133.977 -15.596 63.118  1.00 77.47  ?  19  GLU A CB  1 
ATOM   138   C  CG  . GLU A  1  19  ? 134.358 -14.415 62.240  1.00 81.02  ?  19  GLU A CG  1 
ATOM   139   C  CD  . GLU A  1  19  ? 133.773 -13.076 62.647  1.00 89.61  ?  19  GLU A CD  1 
ATOM   140   O  OE1 . GLU A  1  19  ? 132.616 -13.048 63.125  1.00 87.36  ?  19  GLU A OE1 1 
ATOM   141   O  OE2 . GLU A  1  19  ? 134.469 -12.050 62.477  1.00 98.95  ?  19  GLU A OE2 1 
ATOM   142   N  N   . GLY A  1  20  ? 133.081 -18.546 63.895  1.00 88.14  ?  20  GLY A N   1 
ATOM   143   C  CA  . GLY A  1  20  ? 132.919 -19.606 64.881  1.00 80.73  ?  20  GLY A CA  1 
ATOM   144   C  C   . GLY A  1  20  ? 133.457 -20.960 64.464  1.00 74.97  ?  20  GLY A C   1 
ATOM   145   O  O   . GLY A  1  20  ? 134.051 -21.662 65.284  1.00 84.99  ?  20  GLY A O   1 
ATOM   146   N  N   . ILE A  1  21  ? 133.262 -21.310 63.193  1.00 80.80  ?  21  ILE A N   1 
ATOM   147   C  CA  . ILE A  1  21  ? 133.741 -22.624 62.678  1.00 86.05  ?  21  ILE A CA  1 
ATOM   148   C  C   . ILE A  1  21  ? 135.259 -22.555 62.502  1.00 80.02  ?  21  ILE A C   1 
ATOM   149   O  O   . ILE A  1  21  ? 135.937 -23.549 62.822  1.00 74.18  ?  21  ILE A O   1 
ATOM   150   C  CB  . ILE A  1  21  ? 133.024 -22.963 61.359  1.00 78.11  ?  21  ILE A CB  1 
ATOM   151   C  CG1 . ILE A  1  21  ? 133.276 -24.409 60.933  1.00 65.21  ?  21  ILE A CG1 1 
ATOM   152   C  CG2 . ILE A  1  21  ? 133.400 -21.981 60.260  1.00 98.70  ?  21  ILE A CG2 1 
ATOM   153   C  CD1 . ILE A  1  21  ? 132.114 -25.003 60.199  1.00 79.84  ?  21  ILE A CD1 1 
ATOM   154   N  N   . VAL A  1  22  ? 135.764 -21.420 62.015  1.00 76.29  ?  22  VAL A N   1 
ATOM   155   C  CA  . VAL A  1  22  ? 137.203 -21.268 61.785  1.00 64.14  ?  22  VAL A CA  1 
ATOM   156   C  C   . VAL A  1  22  ? 137.924 -21.359 63.133  1.00 77.25  ?  22  VAL A C   1 
ATOM   157   O  O   . VAL A  1  22  ? 138.991 -21.963 63.202  1.00 85.56  ?  22  VAL A O   1 
ATOM   158   C  CB  . VAL A  1  22  ? 137.546 -19.955 61.017  1.00 71.05  ?  22  VAL A CB  1 
ATOM   159   C  CG1 . VAL A  1  22  ? 138.989 -19.521 61.253  1.00 79.34  ?  22  VAL A CG1 1 
ATOM   160   C  CG2 . VAL A  1  22  ? 137.286 -20.113 59.524  1.00 73.40  ?  22  VAL A CG2 1 
ATOM   161   N  N   . LYS A  1  23  ? 137.342 -20.793 64.207  1.00 74.74  ?  23  LYS A N   1 
ATOM   162   C  CA  . LYS A  1  23  ? 137.949 -20.862 65.538  1.00 78.26  ?  23  LYS A CA  1 
ATOM   163   C  C   . LYS A  1  23  ? 138.114 -22.326 65.966  1.00 88.66  ?  23  LYS A C   1 
ATOM   164   O  O   . LYS A  1  23  ? 139.154 -22.691 66.504  1.00 95.03  ?  23  LYS A O   1 
ATOM   165   C  CB  . LYS A  1  23  ? 137.093 -20.112 66.567  1.00 74.32  ?  23  LYS A CB  1 
ATOM   166   C  CG  . LYS A  1  23  ? 137.776 -19.938 67.918  1.00 78.86  ?  23  LYS A CG  1 
ATOM   167   C  CD  . LYS A  1  23  ? 136.816 -19.393 68.957  1.00 88.60  ?  23  LYS A CD  1 
ATOM   168   C  CE  . LYS A  1  23  ? 137.441 -19.302 70.323  1.00 85.27  ?  23  LYS A CE  1 
ATOM   169   N  NZ  . LYS A  1  23  ? 136.587 -18.526 71.261  1.00 97.00  ?  23  LYS A NZ  1 
ATOM   170   N  N   . GLN A  1  24  ? 137.108 -23.169 65.700  1.00 89.34  ?  24  GLN A N   1 
ATOM   171   C  CA  . GLN A  1  24  ? 137.182 -24.587 66.046  1.00 78.90  ?  24  GLN A CA  1 
ATOM   172   C  C   . GLN A  1  24  ? 138.354 -25.257 65.335  1.00 83.93  ?  24  GLN A C   1 
ATOM   173   O  O   . GLN A  1  24  ? 139.018 -26.098 65.925  1.00 87.35  ?  24  GLN A O   1 
ATOM   174   C  CB  . GLN A  1  24  ? 135.889 -25.314 65.667  1.00 74.31  ?  24  GLN A CB  1 
ATOM   175   C  CG  . GLN A  1  24  ? 134.680 -24.887 66.478  1.00 102.73 ?  24  GLN A CG  1 
ATOM   176   C  CD  . GLN A  1  24  ? 133.489 -25.768 66.192  1.00 117.88 ?  24  GLN A CD  1 
ATOM   177   O  OE1 . GLN A  1  24  ? 133.615 -26.991 66.047  1.00 107.86 ?  24  GLN A OE1 1 
ATOM   178   N  NE2 . GLN A  1  24  ? 132.302 -25.169 66.107  1.00 115.95 ?  24  GLN A NE2 1 
ATOM   179   N  N   . ALA A  1  25  ? 138.603 -24.896 64.071  1.00 80.19  ?  25  ALA A N   1 
ATOM   180   C  CA  . ALA A  1  25  ? 139.700 -25.474 63.304  1.00 78.65  ?  25  ALA A CA  1 
ATOM   181   C  C   . ALA A  1  25  ? 141.057 -25.019 63.833  1.00 89.55  ?  25  ALA A C   1 
ATOM   182   O  O   . ALA A  1  25  ? 141.999 -25.806 63.800  1.00 103.44 ?  25  ALA A O   1 
ATOM   183   C  CB  . ALA A  1  25  ? 139.565 -25.104 61.837  1.00 69.65  ?  25  ALA A CB  1 
ATOM   184   N  N   . VAL A  1  26  ? 141.176 -23.770 64.316  1.00 77.54  ?  26  VAL A N   1 
ATOM   185   C  CA  . VAL A  1  26  ? 142.461 -23.298 64.842  1.00 81.39  ?  26  VAL A CA  1 
ATOM   186   C  C   . VAL A  1  26  ? 142.715 -23.935 66.210  1.00 96.08  ?  26  VAL A C   1 
ATOM   187   O  O   . VAL A  1  26  ? 143.842 -24.338 66.499  1.00 110.26 ?  26  VAL A O   1 
ATOM   188   C  CB  . VAL A  1  26  ? 142.599 -21.752 64.895  1.00 92.33  ?  26  VAL A CB  1 
ATOM   189   C  CG1 . VAL A  1  26  ? 142.218 -21.112 63.565  1.00 89.39  ?  26  VAL A CG1 1 
ATOM   190   C  CG2 . VAL A  1  26  ? 141.805 -21.145 66.048  1.00 91.53  ?  26  VAL A CG2 1 
ATOM   191   N  N   . ASP A  1  27  ? 141.667 -24.046 67.044  1.00 91.09  ?  27  ASP A N   1 
ATOM   192   C  CA  . ASP A  1  27  ? 141.780 -24.625 68.379  1.00 98.02  ?  27  ASP A CA  1 
ATOM   193   C  C   . ASP A  1  27  ? 141.903 -26.156 68.360  1.00 96.79  ?  27  ASP A C   1 
ATOM   194   O  O   . ASP A  1  27  ? 142.454 -26.726 69.300  1.00 110.07 ?  27  ASP A O   1 
ATOM   195   C  CB  . ASP A  1  27  ? 140.557 -24.227 69.233  1.00 98.41  ?  27  ASP A CB  1 
ATOM   196   C  CG  . ASP A  1  27  ? 140.448 -22.748 69.557  1.00 114.96 ?  27  ASP A CG  1 
ATOM   197   O  OD1 . ASP A  1  27  ? 141.474 -22.039 69.458  1.00 124.90 ?  27  ASP A OD1 1 
ATOM   198   O  OD2 . ASP A  1  27  ? 139.335 -22.298 69.914  1.00 108.11 ?  27  ASP A OD2 1 
ATOM   199   N  N   . GLU A  1  28  ? 141.392 -26.820 67.315  1.00 94.18  ?  28  GLU A N   1 
ATOM   200   C  CA  . GLU A  1  28  ? 141.406 -28.279 67.227  1.00 87.00  ?  28  GLU A CA  1 
ATOM   201   C  C   . GLU A  1  28  ? 142.475 -28.861 66.295  1.00 87.54  ?  28  GLU A C   1 
ATOM   202   O  O   . GLU A  1  28  ? 142.992 -29.938 66.587  1.00 102.06 ?  28  GLU A O   1 
ATOM   203   C  CB  . GLU A  1  28  ? 140.019 -28.752 66.774  1.00 83.37  ?  28  GLU A CB  1 
ATOM   204   C  CG  . GLU A  1  28  ? 139.663 -30.174 67.160  1.00 100.25 ?  28  GLU A CG  1 
ATOM   205   C  CD  . GLU A  1  28  ? 138.307 -30.597 66.632  1.00 127.36 ?  28  GLU A CD  1 
ATOM   206   O  OE1 . GLU A  1  28  ? 137.298 -29.964 67.019  1.00 127.98 ?  28  GLU A OE1 1 
ATOM   207   O  OE2 . GLU A  1  28  ? 138.252 -31.555 65.826  1.00 131.48 ?  28  GLU A OE2 1 
ATOM   208   N  N   . LYS A  1  29  ? 142.791 -28.193 65.175  1.00 85.21  ?  29  LYS A N   1 
ATOM   209   C  CA  . LYS A  1  29  ? 143.781 -28.713 64.223  1.00 92.14  ?  29  LYS A CA  1 
ATOM   210   C  C   . LYS A  1  29  ? 145.013 -27.811 64.022  1.00 94.02  ?  29  LYS A C   1 
ATOM   211   O  O   . LYS A  1  29  ? 145.950 -28.217 63.339  1.00 102.67 ?  29  LYS A O   1 
ATOM   212   C  CB  . LYS A  1  29  ? 143.120 -28.975 62.857  1.00 81.61  ?  29  LYS A CB  1 
ATOM   213   C  CG  . LYS A  1  29  ? 141.953 -29.963 62.891  1.00 88.59  ?  29  LYS A CG  1 
ATOM   214   C  CD  . LYS A  1  29  ? 142.408 -31.417 62.828  1.00 89.89  ?  29  LYS A CD  1 
ATOM   215   C  CE  . LYS A  1  29  ? 141.281 -32.373 62.507  1.00 99.14  ?  29  LYS A CE  1 
ATOM   216   N  NZ  . LYS A  1  29  ? 140.319 -32.521 63.633  1.00 102.85 ?  29  LYS A NZ  1 
ATOM   217   N  N   . GLY A  1  30  ? 145.010 -26.612 64.593  1.00 88.29  ?  30  GLY A N   1 
ATOM   218   C  CA  . GLY A  1  30  ? 146.135 -25.694 64.451  1.00 90.41  ?  30  GLY A CA  1 
ATOM   219   C  C   . GLY A  1  30  ? 146.072 -24.879 63.176  1.00 102.52 ?  30  GLY A C   1 
ATOM   220   O  O   . GLY A  1  30  ? 145.360 -25.245 62.241  1.00 109.93 ?  30  GLY A O   1 
ATOM   221   N  N   . ARG A  1  31  ? 146.829 -23.771 63.120  1.00 107.70 ?  31  ARG A N   1 
ATOM   222   C  CA  . ARG A  1  31  ? 146.837 -22.883 61.952  1.00 106.40 ?  31  ARG A CA  1 
ATOM   223   C  C   . ARG A  1  31  ? 147.691 -23.383 60.777  1.00 100.45 ?  31  ARG A C   1 
ATOM   224   O  O   . ARG A  1  31  ? 147.777 -22.687 59.767  1.00 103.14 ?  31  ARG A O   1 
ATOM   225   C  CB  . ARG A  1  31  ? 147.282 -21.464 62.353  1.00 121.32 ?  31  ARG A CB  1 
ATOM   226   C  CG  . ARG A  1  31  ? 146.383 -20.797 63.396  1.00 104.88 ?  31  ARG A CG  1 
ATOM   227   C  CD  . ARG A  1  31  ? 146.057 -19.353 63.054  1.00 86.01  ?  31  ARG A CD  1 
ATOM   228   N  NE  . ARG A  1  31  ? 145.172 -18.747 64.049  1.00 92.01  ?  31  ARG A NE  1 
ATOM   229   C  CZ  . ARG A  1  31  ? 145.570 -18.227 65.208  1.00 111.32 ?  31  ARG A CZ  1 
ATOM   230   N  NH1 . ARG A  1  31  ? 146.857 -18.225 65.538  1.00 125.83 ?  31  ARG A NH1 1 
ATOM   231   N  NH2 . ARG A  1  31  ? 144.682 -17.702 66.046  1.00 109.73 ?  31  ARG A NH2 1 
ATOM   232   N  N   . ASP A  1  32  ? 148.311 -24.563 60.884  1.00 100.85 ?  32  ASP A N   1 
ATOM   233   C  CA  . ASP A  1  32  ? 149.128 -25.098 59.791  1.00 99.25  ?  32  ASP A CA  1 
ATOM   234   C  C   . ASP A  1  32  ? 148.479 -26.311 59.101  1.00 100.91 ?  32  ASP A C   1 
ATOM   235   O  O   . ASP A  1  32  ? 148.982 -26.759 58.069  1.00 87.97  ?  32  ASP A O   1 
ATOM   236   C  CB  . ASP A  1  32  ? 150.527 -25.469 60.304  1.00 112.72 ?  32  ASP A CB  1 
ATOM   237   C  CG  . ASP A  1  32  ? 151.433 -24.274 60.519  1.00 131.38 ?  32  ASP A CG  1 
ATOM   238   O  OD1 . ASP A  1  32  ? 151.261 -23.260 59.802  1.00 121.79 ?  32  ASP A OD1 1 
ATOM   239   O  OD2 . ASP A  1  32  ? 152.319 -24.352 61.400  1.00 130.84 ?  32  ASP A OD2 1 
ATOM   240   N  N   . TYR A  1  33  ? 147.367 -26.833 59.657  1.00 104.09 ?  33  TYR A N   1 
ATOM   241   C  CA  . TYR A  1  33  ? 146.655 -27.985 59.101  1.00 92.20  ?  33  TYR A CA  1 
ATOM   242   C  C   . TYR A  1  33  ? 146.209 -27.690 57.668  1.00 79.28  ?  33  TYR A C   1 
ATOM   243   O  O   . TYR A  1  33  ? 145.773 -26.579 57.379  1.00 89.92  ?  33  TYR A O   1 
ATOM   244   C  CB  . TYR A  1  33  ? 145.446 -28.333 59.990  1.00 94.64  ?  33  TYR A CB  1 
ATOM   245   C  CG  . TYR A  1  33  ? 144.807 -29.668 59.683  1.00 92.44  ?  33  TYR A CG  1 
ATOM   246   C  CD1 . TYR A  1  33  ? 145.256 -30.832 60.288  1.00 83.56  ?  33  TYR A CD1 1 
ATOM   247   C  CD2 . TYR A  1  33  ? 143.710 -29.758 58.839  1.00 89.70  ?  33  TYR A CD2 1 
ATOM   248   C  CE1 . TYR A  1  33  ? 144.657 -32.058 60.028  1.00 82.81  ?  33  TYR A CE1 1 
ATOM   249   C  CE2 . TYR A  1  33  ? 143.105 -30.979 58.568  1.00 93.62  ?  33  TYR A CE2 1 
ATOM   250   C  CZ  . TYR A  1  33  ? 143.579 -32.129 59.165  1.00 95.02  ?  33  TYR A CZ  1 
ATOM   251   O  OH  . TYR A  1  33  ? 142.980 -33.340 58.902  1.00 99.86  ?  33  TYR A OH  1 
ATOM   252   N  N   . LYS A  1  34  ? 146.337 -28.674 56.773  1.00 91.31  ?  34  LYS A N   1 
ATOM   253   C  CA  . LYS A  1  34  ? 145.974 -28.512 55.366  1.00 76.03  ?  34  LYS A CA  1 
ATOM   254   C  C   . LYS A  1  34  ? 144.469 -28.406 55.141  1.00 75.03  ?  34  LYS A C   1 
ATOM   255   O  O   . LYS A  1  34  ? 143.706 -29.253 55.602  1.00 81.90  ?  34  LYS A O   1 
ATOM   256   C  CB  . LYS A  1  34  ? 146.523 -29.694 54.551  1.00 87.88  ?  34  LYS A CB  1 
ATOM   257   C  CG  . LYS A  1  34  ? 146.300 -29.586 53.046  1.00 95.55  ?  34  LYS A CG  1 
ATOM   258   C  CD  . LYS A  1  34  ? 146.503 -30.931 52.362  1.00 76.13  ?  34  LYS A CD  1 
ATOM   259   C  CE  . LYS A  1  34  ? 146.501 -30.818 50.857  1.00 106.59 ?  34  LYS A CE  1 
ATOM   260   N  NZ  . LYS A  1  34  ? 146.842 -32.109 50.199  1.00 105.65 ?  34  LYS A NZ  1 
ATOM   261   N  N   . VAL A  1  35  ? 144.051 -27.379 54.395  1.00 69.16  ?  35  VAL A N   1 
ATOM   262   C  CA  . VAL A  1  35  ? 142.647 -27.172 54.050  1.00 83.66  ?  35  VAL A CA  1 
ATOM   263   C  C   . VAL A  1  35  ? 142.532 -27.356 52.542  1.00 82.75  ?  35  VAL A C   1 
ATOM   264   O  O   . VAL A  1  35  ? 143.285 -26.745 51.782  1.00 84.45  ?  35  VAL A O   1 
ATOM   265   C  CB  . VAL A  1  35  ? 142.068 -25.812 54.525  1.00 79.52  ?  35  VAL A CB  1 
ATOM   266   C  CG1 . VAL A  1  35  ? 142.899 -24.643 54.032  1.00 90.08  ?  35  VAL A CG1 1 
ATOM   267   C  CG2 . VAL A  1  35  ? 140.616 -25.650 54.087  1.00 65.66  ?  35  VAL A CG2 1 
ATOM   268   N  N   . ALA A  1  36  ? 141.623 -28.236 52.113  1.00 78.00  ?  36  ALA A N   1 
ATOM   269   C  CA  . ALA A  1  36  ? 141.416 -28.516 50.697  1.00 82.02  ?  36  ALA A CA  1 
ATOM   270   C  C   . ALA A  1  36  ? 140.084 -29.229 50.474  1.00 77.59  ?  36  ALA A C   1 
ATOM   271   O  O   . ALA A  1  36  ? 139.558 -29.875 51.383  1.00 70.32  ?  36  ALA A O   1 
ATOM   272   C  CB  . ALA A  1  36  ? 142.560 -29.370 50.157  1.00 76.78  ?  36  ALA A CB  1 
ATOM   273   N  N   . PHE A  1  37  ? 139.541 -29.109 49.260  1.00 70.90  ?  37  PHE A N   1 
ATOM   274   C  CA  . PHE A  1  37  ? 138.287 -29.765 48.917  1.00 67.58  ?  37  PHE A CA  1 
ATOM   275   C  C   . PHE A  1  37  ? 138.621 -31.043 48.123  1.00 69.66  ?  37  PHE A C   1 
ATOM   276   O  O   . PHE A  1  37  ? 139.666 -31.095 47.470  1.00 79.33  ?  37  PHE A O   1 
ATOM   277   C  CB  . PHE A  1  37  ? 137.379 -28.822 48.105  1.00 63.66  ?  37  PHE A CB  1 
ATOM   278   C  CG  . PHE A  1  37  ? 136.500 -27.898 48.922  1.00 60.58  ?  37  PHE A CG  1 
ATOM   279   C  CD1 . PHE A  1  37  ? 135.533 -28.406 49.770  1.00 70.64  ?  37  PHE A CD1 1 
ATOM   280   C  CD2 . PHE A  1  37  ? 136.605 -26.524 48.795  1.00 71.12  ?  37  PHE A CD2 1 
ATOM   281   C  CE1 . PHE A  1  37  ? 134.707 -27.557 50.495  1.00 67.78  ?  37  PHE A CE1 1 
ATOM   282   C  CE2 . PHE A  1  37  ? 135.779 -25.679 49.524  1.00 60.52  ?  37  PHE A CE2 1 
ATOM   283   C  CZ  . PHE A  1  37  ? 134.833 -26.200 50.364  1.00 50.13  ?  37  PHE A CZ  1 
ATOM   284   N  N   . PRO A  1  38  ? 137.784 -32.094 48.164  1.00 60.78  ?  38  PRO A N   1 
ATOM   285   C  CA  . PRO A  1  38  ? 138.133 -33.325 47.435  1.00 64.51  ?  38  PRO A CA  1 
ATOM   286   C  C   . PRO A  1  38  ? 138.243 -33.223 45.915  1.00 74.58  ?  38  PRO A C   1 
ATOM   287   O  O   . PRO A  1  38  ? 137.282 -32.863 45.235  1.00 66.31  ?  38  PRO A O   1 
ATOM   288   C  CB  . PRO A  1  38  ? 137.025 -34.313 47.826  1.00 68.64  ?  38  PRO A CB  1 
ATOM   289   C  CG  . PRO A  1  38  ? 136.305 -33.703 48.941  1.00 74.21  ?  38  PRO A CG  1 
ATOM   290   C  CD  . PRO A  1  38  ? 136.507 -32.237 48.887  1.00 65.60  ?  38  PRO A CD  1 
ATOM   291   N  N   . ASP A  1  39  ? 139.420 -33.584 45.382  1.00 79.40  ?  39  ASP A N   1 
ATOM   292   C  CA  . ASP A  1  39  ? 139.694 -33.615 43.945  1.00 86.52  ?  39  ASP A CA  1 
ATOM   293   C  C   . ASP A  1  39  ? 139.223 -32.361 43.196  1.00 79.88  ?  39  ASP A C   1 
ATOM   294   O  O   . ASP A  1  39  ? 138.190 -32.375 42.522  1.00 71.16  ?  39  ASP A O   1 
ATOM   295   C  CB  . ASP A  1  39  ? 139.087 -34.899 43.347  1.00 88.84  ?  39  ASP A CB  1 
ATOM   296   C  CG  . ASP A  1  39  ? 139.479 -35.213 41.915  1.00 100.31 ?  39  ASP A CG  1 
ATOM   297   O  OD1 . ASP A  1  39  ? 140.363 -34.512 41.369  1.00 105.49 ?  39  ASP A OD1 1 
ATOM   298   O  OD2 . ASP A  1  39  ? 138.910 -36.167 41.342  1.00 101.58 ?  39  ASP A OD2 1 
ATOM   299   N  N   . THR A  1  40  ? 140.005 -31.280 43.315  1.00 81.21  ?  40  THR A N   1 
ATOM   300   C  CA  . THR A  1  40  ? 139.725 -30.015 42.642  1.00 66.00  ?  40  THR A CA  1 
ATOM   301   C  C   . THR A  1  40  ? 141.039 -29.306 42.342  1.00 71.78  ?  40  THR A C   1 
ATOM   302   O  O   . THR A  1  40  ? 141.944 -29.293 43.177  1.00 78.16  ?  40  THR A O   1 
ATOM   303   C  CB  . THR A  1  40  ? 138.767 -29.132 43.458  1.00 56.89  ?  40  THR A CB  1 
ATOM   304   O  OG1 . THR A  1  40  ? 138.461 -27.965 42.695  1.00 61.93  ?  40  THR A OG1 1 
ATOM   305   C  CG2 . THR A  1  40  ? 139.337 -28.722 44.806  1.00 68.12  ?  40  THR A CG2 1 
ATOM   306   N  N   . ALA A  1  41  ? 141.152 -28.725 41.149  1.00 67.78  ?  41  ALA A N   1 
ATOM   307   C  CA  . ALA A  1  41  ? 142.365 -28.018 40.756  1.00 69.87  ?  41  ALA A CA  1 
ATOM   308   C  C   . ALA A  1  41  ? 142.273 -26.509 41.011  1.00 69.45  ?  41  ALA A C   1 
ATOM   309   O  O   . ALA A  1  41  ? 143.150 -25.775 40.560  1.00 89.62  ?  41  ALA A O   1 
ATOM   310   C  CB  . ALA A  1  41  ? 142.641 -28.268 39.284  1.00 79.56  ?  41  ALA A CB  1 
ATOM   311   N  N   . TYR A  1  42  ? 141.239 -26.070 41.733  1.00 64.51  ?  42  TYR A N   1 
ATOM   312   C  CA  . TYR A  1  42  ? 141.041 -24.613 41.955  1.00 74.60  ?  42  TYR A CA  1 
ATOM   313   C  C   . TYR A  1  42  ? 140.899 -24.316 43.452  1.00 75.88  ?  42  TYR A C   1 
ATOM   314   O  O   . TYR A  1  42  ? 140.247 -23.314 43.800  1.00 75.69  ?  42  TYR A O   1 
ATOM   315   C  CB  . TYR A  1  42  ? 139.823 -24.122 41.168  1.00 58.46  ?  42  TYR A CB  1 
ATOM   316   C  CG  . TYR A  1  42  ? 139.908 -24.362 39.682  1.00 70.80  ?  42  TYR A CG  1 
ATOM   317   C  CD1 . TYR A  1  42  ? 140.575 -23.476 38.854  1.00 64.07  ?  42  TYR A CD1 1 
ATOM   318   C  CD2 . TYR A  1  42  ? 139.332 -25.480 39.104  1.00 77.16  ?  42  TYR A CD2 1 
ATOM   319   C  CE1 . TYR A  1  42  ? 140.663 -23.688 37.489  1.00 62.43  ?  42  TYR A CE1 1 
ATOM   320   C  CE2 . TYR A  1  42  ? 139.411 -25.709 37.740  1.00 69.82  ?  42  TYR A CE2 1 
ATOM   321   C  CZ  . TYR A  1  42  ? 140.078 -24.810 36.929  1.00 69.89  ?  42  TYR A CZ  1 
ATOM   322   O  OH  . TYR A  1  42  ? 140.163 -25.026 35.576  1.00 83.35  ?  42  TYR A OH  1 
ATOM   323   N  N   . SER A  1  43  ? 141.492 -25.158 44.304  1.00 75.43  ?  43  SER A N   1 
ATOM   324   C  CA  . SER A  1  43  ? 141.448 -24.912 45.768  1.00 74.49  ?  43  SER A CA  1 
ATOM   325   C  C   . SER A  1  43  ? 140.041 -24.508 46.209  1.00 75.40  ?  43  SER A C   1 
ATOM   326   O  O   . SER A  1  43  ? 139.127 -25.343 46.084  1.00 78.19  ?  43  SER A O   1 
ATOM   327   C  CB  . SER A  1  43  ? 142.458 -23.872 46.169  1.00 78.95  ?  43  SER A CB  1 
ATOM   328   O  OG  . SER A  1  43  ? 142.417 -23.639 47.570  1.00 103.65 ?  43  SER A OG  1 
ATOM   329   N  N   . LEU A  1  44  ? 139.881 -23.283 46.714  1.00 69.04  ?  44  LEU A N   1 
ATOM   330   C  CA  . LEU A  1  44  ? 138.528 -22.782 47.069  1.00 63.72  ?  44  LEU A CA  1 
ATOM   331   C  C   . LEU A  1  44  ? 138.056 -21.980 45.854  1.00 73.75  ?  44  LEU A C   1 
ATOM   332   O  O   . LEU A  1  44  ? 138.484 -20.819 45.717  1.00 79.67  ?  44  LEU A O   1 
ATOM   333   C  CB  . LEU A  1  44  ? 138.611 -21.912 48.325  1.00 69.37  ?  44  LEU A CB  1 
ATOM   334   C  CG  . LEU A  1  44  ? 138.299 -22.630 49.637  1.00 67.59  ?  44  LEU A CG  1 
ATOM   335   C  CD1 . LEU A  1  44  ? 139.191 -23.849 49.815  1.00 54.47  ?  44  LEU A CD1 1 
ATOM   336   C  CD2 . LEU A  1  44  ? 138.446 -21.687 50.821  1.00 68.50  ?  44  LEU A CD2 1 
ATOM   337   N  N   . PRO A  1  45  ? 137.195 -22.536 44.974  1.00 61.65  ?  45  PRO A N   1 
ATOM   338   C  CA  . PRO A  1  45  ? 136.813 -21.850 43.732  1.00 64.44  ?  45  PRO A CA  1 
ATOM   339   C  C   . PRO A  1  45  ? 136.362 -20.396 43.932  1.00 65.20  ?  45  PRO A C   1 
ATOM   340   O  O   . PRO A  1  45  ? 136.867 -19.536 43.237  1.00 72.49  ?  45  PRO A O   1 
ATOM   341   C  CB  . PRO A  1  45  ? 135.632 -22.696 43.236  1.00 70.55  ?  45  PRO A CB  1 
ATOM   342   C  CG  . PRO A  1  45  ? 135.931 -24.080 43.762  1.00 63.68  ?  45  PRO A CG  1 
ATOM   343   C  CD  . PRO A  1  45  ? 136.545 -23.839 45.125  1.00 54.67  ?  45  PRO A CD  1 
ATOM   344   N  N   . VAL A  1  46  ? 135.438 -20.157 44.863  1.00 55.92  ?  46  VAL A N   1 
ATOM   345   C  CA  . VAL A  1  46  ? 134.902 -18.778 45.066  1.00 59.22  ?  46  VAL A CA  1 
ATOM   346   C  C   . VAL A  1  46  ? 136.073 -17.835 45.352  1.00 66.68  ?  46  VAL A C   1 
ATOM   347   O  O   . VAL A  1  46  ? 136.248 -16.866 44.589  1.00 68.10  ?  46  VAL A O   1 
ATOM   348   C  CB  . VAL A  1  46  ? 133.854 -18.737 46.194  1.00 64.56  ?  46  VAL A CB  1 
ATOM   349   C  CG1 . VAL A  1  46  ? 133.240 -17.354 46.344  1.00 50.68  ?  46  VAL A CG1 1 
ATOM   350   C  CG2 . VAL A  1  46  ? 132.770 -19.785 45.992  1.00 75.22  ?  46  VAL A CG2 1 
ATOM   351   N  N   . ILE A  1  47  ? 136.839 -18.107 46.409  1.00 58.12  ?  47  ILE A N   1 
ATOM   352   C  CA  . ILE A  1  47  ? 137.991 -17.232 46.775  1.00 58.06  ?  47  ILE A CA  1 
ATOM   353   C  C   . ILE A  1  47  ? 138.949 -17.162 45.583  1.00 66.69  ?  47  ILE A C   1 
ATOM   354   O  O   . ILE A  1  47  ? 139.455 -16.061 45.298  1.00 70.50  ?  47  ILE A O   1 
ATOM   355   C  CB  . ILE A  1  47  ? 138.689 -17.762 48.041  1.00 56.12  ?  47  ILE A CB  1 
ATOM   356   C  CG1 . ILE A  1  47  ? 137.695 -17.954 49.188  1.00 49.73  ?  47  ILE A CG1 1 
ATOM   357   C  CG2 . ILE A  1  47  ? 139.846 -16.859 48.438  1.00 63.14  ?  47  ILE A CG2 1 
ATOM   358   C  CD1 . ILE A  1  47  ? 138.288 -17.725 50.553  1.00 66.93  ?  47  ILE A CD1 1 
ATOM   359   N  N   . PHE A  1  48  ? 139.180 -18.293 44.913  1.00 67.82  ?  48  PHE A N   1 
ATOM   360   C  CA  . PHE A  1  48  ? 140.108 -18.324 43.792  1.00 61.41  ?  48  PHE A CA  1 
ATOM   361   C  C   . PHE A  1  48  ? 139.595 -17.449 42.648  1.00 63.15  ?  48  PHE A C   1 
ATOM   362   O  O   . PHE A  1  48  ? 140.398 -16.847 41.944  1.00 72.86  ?  48  PHE A O   1 
ATOM   363   C  CB  . PHE A  1  48  ? 140.338 -19.763 43.311  1.00 52.56  ?  48  PHE A CB  1 
ATOM   364   C  CG  . PHE A  1  48  ? 141.308 -19.844 42.158  1.00 62.94  ?  48  PHE A CG  1 
ATOM   365   C  CD1 . PHE A  1  48  ? 142.660 -19.645 42.356  1.00 64.76  ?  48  PHE A CD1 1 
ATOM   366   C  CD2 . PHE A  1  48  ? 140.860 -20.073 40.869  1.00 68.00  ?  48  PHE A CD2 1 
ATOM   367   C  CE1 . PHE A  1  48  ? 143.547 -19.694 41.291  1.00 71.80  ?  48  PHE A CE1 1 
ATOM   368   C  CE2 . PHE A  1  48  ? 141.749 -20.128 39.807  1.00 59.93  ?  48  PHE A CE2 1 
ATOM   369   C  CZ  . PHE A  1  48  ? 143.086 -19.941 40.024  1.00 62.62  ?  48  PHE A CZ  1 
ATOM   370   N  N   . ALA A  1  49  ? 138.272 -17.369 42.458  1.00 57.91  ?  49  ALA A N   1 
ATOM   371   C  CA  . ALA A  1  49  ? 137.702 -16.544 41.398  1.00 56.76  ?  49  ALA A CA  1 
ATOM   372   C  C   . ALA A  1  49  ? 137.801 -15.057 41.747  1.00 65.91  ?  49  ALA A C   1 
ATOM   373   O  O   . ALA A  1  49  ? 138.131 -14.248 40.886  1.00 68.93  ?  49  ALA A O   1 
ATOM   374   C  CB  . ALA A  1  49  ? 136.250 -16.924 41.162  1.00 57.47  ?  49  ALA A CB  1 
ATOM   375   N  N   . ALA A  1  50  ? 137.526 -14.695 43.002  1.00 68.87  ?  50  ALA A N   1 
ATOM   376   C  CA  . ALA A  1  50  ? 137.563 -13.301 43.434  1.00 68.63  ?  50  ALA A CA  1 
ATOM   377   C  C   . ALA A  1  50  ? 138.977 -12.733 43.631  1.00 73.87  ?  50  ALA A C   1 
ATOM   378   O  O   . ALA A  1  50  ? 139.246 -11.611 43.202  1.00 74.16  ?  50  ALA A O   1 
ATOM   379   C  CB  . ALA A  1  50  ? 136.761 -13.146 44.718  1.00 58.73  ?  50  ALA A CB  1 
ATOM   380   N  N   . THR A  1  51  ? 139.870 -13.492 44.282  1.00 64.70  ?  51  THR A N   1 
ATOM   381   C  CA  . THR A  1  51  ? 141.229 -13.041 44.580  1.00 67.25  ?  51  THR A CA  1 
ATOM   382   C  C   . THR A  1  51  ? 142.321 -13.643 43.699  1.00 75.21  ?  51  THR A C   1 
ATOM   383   O  O   . THR A  1  51  ? 143.412 -13.081 43.620  1.00 74.14  ?  51  THR A O   1 
ATOM   384   C  CB  . THR A  1  51  ? 141.552 -13.374 46.038  1.00 79.43  ?  51  THR A CB  1 
ATOM   385   O  OG1 . THR A  1  51  ? 141.607 -14.796 46.194  1.00 76.30  ?  51  THR A OG1 1 
ATOM   386   C  CG2 . THR A  1  51  ? 140.543 -12.774 47.010  1.00 78.94  ?  51  THR A CG2 1 
ATOM   387   N  N   . GLY A  1  52  ? 142.051 -14.783 43.081  1.00 65.23  ?  52  GLY A N   1 
ATOM   388   C  CA  . GLY A  1  52  ? 143.047 -15.457 42.258  1.00 72.54  ?  52  GLY A CA  1 
ATOM   389   C  C   . GLY A  1  52  ? 144.098 -16.183 43.084  1.00 86.38  ?  52  GLY A C   1 
ATOM   390   O  O   . GLY A  1  52  ? 145.041 -16.750 42.527  1.00 82.26  ?  52  GLY A O   1 
ATOM   391   N  N   . LYS A  1  53  ? 143.940 -16.177 44.422  1.00 82.97  ?  53  LYS A N   1 
ATOM   392   C  CA  . LYS A  1  53  ? 144.857 -16.820 45.356  1.00 76.05  ?  53  LYS A CA  1 
ATOM   393   C  C   . LYS A  1  53  ? 144.272 -18.150 45.805  1.00 75.72  ?  53  LYS A C   1 
ATOM   394   O  O   . LYS A  1  53  ? 143.053 -18.319 45.804  1.00 73.93  ?  53  LYS A O   1 
ATOM   395   C  CB  . LYS A  1  53  ? 145.068 -15.930 46.593  1.00 83.48  ?  53  LYS A CB  1 
ATOM   396   C  CG  . LYS A  1  53  ? 145.448 -14.485 46.280  1.00 101.22 ?  53  LYS A CG  1 
ATOM   397   C  CD  . LYS A  1  53  ? 145.413 -13.610 47.534  1.00 123.56 ?  53  LYS A CD  1 
ATOM   398   C  CE  . LYS A  1  53  ? 145.314 -12.133 47.220  1.00 136.07 ?  53  LYS A CE  1 
ATOM   399   N  NZ  . LYS A  1  53  ? 144.708 -11.366 48.342  1.00 131.18 ?  53  LYS A NZ  1 
ATOM   400   N  N   . LYS A  1  54  ? 145.137 -19.086 46.215  1.00 86.66  ?  54  LYS A N   1 
ATOM   401   C  CA  . LYS A  1  54  ? 144.700 -20.399 46.679  1.00 78.52  ?  54  LYS A CA  1 
ATOM   402   C  C   . LYS A  1  54  ? 144.868 -20.516 48.193  1.00 76.17  ?  54  LYS A C   1 
ATOM   403   O  O   . LYS A  1  54  ? 145.869 -20.064 48.742  1.00 79.50  ?  54  LYS A O   1 
ATOM   404   C  CB  . LYS A  1  54  ? 145.484 -21.501 45.959  1.00 74.72  ?  54  LYS A CB  1 
ATOM   405   C  CG  . LYS A  1  54  ? 145.225 -21.515 44.459  1.00 72.93  ?  54  LYS A CG  1 
ATOM   406   C  CD  . LYS A  1  54  ? 145.883 -22.703 43.749  1.00 80.63  ?  54  LYS A CD  1 
ATOM   407   C  CE  . LYS A  1  54  ? 144.956 -23.381 42.767  1.00 93.42  ?  54  LYS A CE  1 
ATOM   408   N  NZ  . LYS A  1  54  ? 145.653 -24.423 41.971  1.00 97.23  ?  54  LYS A NZ  1 
ATOM   409   N  N   . ILE A  1  55  ? 143.878 -21.111 48.863  1.00 80.22  ?  55  ILE A N   1 
ATOM   410   C  CA  . ILE A  1  55  ? 143.898 -21.303 50.310  1.00 77.50  ?  55  ILE A CA  1 
ATOM   411   C  C   . ILE A  1  55  ? 144.387 -22.728 50.569  1.00 87.32  ?  55  ILE A C   1 
ATOM   412   O  O   . ILE A  1  55  ? 143.712 -23.679 50.176  1.00 94.24  ?  55  ILE A O   1 
ATOM   413   C  CB  . ILE A  1  55  ? 142.481 -21.063 50.886  1.00 76.00  ?  55  ILE A CB  1 
ATOM   414   C  CG1 . ILE A  1  55  ? 141.968 -19.637 50.570  1.00 64.70  ?  55  ILE A CG1 1 
ATOM   415   C  CG2 . ILE A  1  55  ? 142.443 -21.351 52.377  1.00 82.87  ?  55  ILE A CG2 1 
ATOM   416   C  CD1 . ILE A  1  55  ? 142.821 -18.473 51.086  1.00 85.40  ?  55  ILE A CD1 1 
ATOM   417   N  N   . THR A  1  56  ? 145.563 -22.879 51.210  1.00 79.43  ?  56  THR A N   1 
ATOM   418   C  CA  . THR A  1  56  ? 146.154 -24.193 51.474  1.00 72.05  ?  56  THR A CA  1 
ATOM   419   C  C   . THR A  1  56  ? 146.158 -24.610 52.949  1.00 87.61  ?  56  THR A C   1 
ATOM   420   O  O   . THR A  1  56  ? 146.071 -25.806 53.217  1.00 97.67  ?  56  THR A O   1 
ATOM   421   C  CB  . THR A  1  56  ? 147.581 -24.251 50.909  1.00 86.93  ?  56  THR A CB  1 
ATOM   422   O  OG1 . THR A  1  56  ? 148.441 -23.438 51.709  1.00 101.69 ?  56  THR A OG1 1 
ATOM   423   C  CG2 . THR A  1  56  ? 147.652 -23.813 49.450  1.00 78.94  ?  56  THR A CG2 1 
ATOM   424   N  N   . ASN A  1  57  ? 146.280 -23.665 53.899  1.00 78.99  ?  57  ASN A N   1 
ATOM   425   C  CA  . ASN A  1  57  ? 146.300 -24.022 55.325  1.00 77.66  ?  57  ASN A CA  1 
ATOM   426   C  C   . ASN A  1  57  ? 145.223 -23.291 56.141  1.00 76.54  ?  57  ASN A C   1 
ATOM   427   O  O   . ASN A  1  57  ? 144.663 -22.302 55.675  1.00 84.95  ?  57  ASN A O   1 
ATOM   428   C  CB  . ASN A  1  57  ? 147.699 -23.800 55.927  1.00 87.36  ?  57  ASN A CB  1 
ATOM   429   C  CG  . ASN A  1  57  ? 148.241 -22.395 55.801  1.00 98.04  ?  57  ASN A CG  1 
ATOM   430   O  OD1 . ASN A  1  57  ? 147.871 -21.489 56.558  1.00 101.99 ?  57  ASN A OD1 1 
ATOM   431   N  ND2 . ASN A  1  57  ? 149.148 -22.185 54.852  1.00 106.67 ?  57  ASN A ND2 1 
ATOM   432   N  N   . VAL A  1  58  ? 144.931 -23.787 57.357  1.00 89.87  ?  58  VAL A N   1 
ATOM   433   C  CA  . VAL A  1  58  ? 143.925 -23.195 58.247  1.00 79.66  ?  58  VAL A CA  1 
ATOM   434   C  C   . VAL A  1  58  ? 144.235 -21.712 58.536  1.00 90.72  ?  58  VAL A C   1 
ATOM   435   O  O   . VAL A  1  58  ? 143.311 -20.913 58.686  1.00 93.07  ?  58  VAL A O   1 
ATOM   436   C  CB  . VAL A  1  58  ? 143.773 -24.021 59.555  1.00 85.20  ?  58  VAL A CB  1 
ATOM   437   C  CG1 . VAL A  1  58  ? 142.961 -23.268 60.601  1.00 73.97  ?  58  VAL A CG1 1 
ATOM   438   C  CG2 . VAL A  1  58  ? 143.140 -25.383 59.278  1.00 86.57  ?  58  VAL A CG2 1 
ATOM   439   N  N   . GLY A  1  59  ? 145.513 -21.351 58.600  1.00 86.61  ?  59  GLY A N   1 
ATOM   440   C  CA  . GLY A  1  59  ? 145.913 -19.969 58.832  1.00 77.78  ?  59  GLY A CA  1 
ATOM   441   C  C   . GLY A  1  59  ? 145.480 -19.086 57.681  1.00 87.30  ?  59  GLY A C   1 
ATOM   442   O  O   . GLY A  1  59  ? 144.980 -17.979 57.892  1.00 92.58  ?  59  GLY A O   1 
ATOM   443   N  N   . GLU A  1  60  ? 145.649 -19.591 56.444  1.00 78.02  ?  60  GLU A N   1 
ATOM   444   C  CA  . GLU A  1  60  ? 145.243 -18.877 55.233  1.00 79.85  ?  60  GLU A CA  1 
ATOM   445   C  C   . GLU A  1  60  ? 143.710 -18.790 55.180  1.00 81.11  ?  60  GLU A C   1 
ATOM   446   O  O   . GLU A  1  60  ? 143.172 -17.752 54.799  1.00 79.43  ?  60  GLU A O   1 
ATOM   447   C  CB  . GLU A  1  60  ? 145.809 -19.564 53.974  1.00 77.58  ?  60  GLU A CB  1 
ATOM   448   C  CG  . GLU A  1  60  ? 147.302 -19.337 53.789  1.00 75.38  ?  60  GLU A CG  1 
ATOM   449   C  CD  . GLU A  1  60  ? 147.914 -19.965 52.553  1.00 87.31  ?  60  GLU A CD  1 
ATOM   450   O  OE1 . GLU A  1  60  ? 147.203 -20.720 51.854  1.00 93.33  ?  60  GLU A OE1 1 
ATOM   451   O  OE2 . GLU A  1  60  ? 149.108 -19.705 52.284  1.00 87.24  ?  60  GLU A OE2 1 
ATOM   452   N  N   . LEU A  1  61  ? 143.009 -19.865 55.588  1.00 88.35  ?  61  LEU A N   1 
ATOM   453   C  CA  . LEU A  1  61  ? 141.545 -19.890 55.640  1.00 73.30  ?  61  LEU A CA  1 
ATOM   454   C  C   . LEU A  1  61  ? 141.054 -18.832 56.631  1.00 83.91  ?  61  LEU A C   1 
ATOM   455   O  O   . LEU A  1  61  ? 140.021 -18.213 56.398  1.00 98.74  ?  61  LEU A O   1 
ATOM   456   C  CB  . LEU A  1  61  ? 141.053 -21.280 56.076  1.00 75.75  ?  61  LEU A CB  1 
ATOM   457   C  CG  . LEU A  1  61  ? 139.539 -21.517 56.049  1.00 75.40  ?  61  LEU A CG  1 
ATOM   458   C  CD1 . LEU A  1  61  ? 139.034 -21.688 54.631  1.00 76.62  ?  61  LEU A CD1 1 
ATOM   459   C  CD2 . LEU A  1  61  ? 139.152 -22.736 56.890  1.00 61.67  ?  61  LEU A CD2 1 
ATOM   460   N  N   . GLU A  1  62  ? 141.790 -18.621 57.730  1.00 85.52  ?  62  GLU A N   1 
ATOM   461   C  CA  . GLU A  1  62  ? 141.437 -17.608 58.716  1.00 86.23  ?  62  GLU A CA  1 
ATOM   462   C  C   . GLU A  1  62  ? 141.556 -16.215 58.070  1.00 93.18  ?  62  GLU A C   1 
ATOM   463   O  O   . GLU A  1  62  ? 140.697 -15.360 58.283  1.00 78.95  ?  62  GLU A O   1 
ATOM   464   C  CB  . GLU A  1  62  ? 142.360 -17.724 59.940  1.00 79.57  ?  62  GLU A CB  1 
ATOM   465   C  CG  . GLU A  1  62  ? 141.890 -16.933 61.147  1.00 85.16  ?  62  GLU A CG  1 
ATOM   466   C  CD  . GLU A  1  62  ? 142.875 -16.908 62.302  1.00 101.24 ?  62  GLU A CD  1 
ATOM   467   O  OE1 . GLU A  1  62  ? 144.090 -16.738 62.047  1.00 94.80  ?  62  GLU A OE1 1 
ATOM   468   O  OE2 . GLU A  1  62  ? 142.430 -17.052 63.464  1.00 86.89  ?  62  GLU A OE2 1 
ATOM   469   N  N   . GLY A  1  63  ? 142.608 -16.010 57.277  1.00 86.92  ?  63  GLY A N   1 
ATOM   470   C  CA  . GLY A  1  63  ? 142.840 -14.752 56.580  1.00 81.18  ?  63  GLY A CA  1 
ATOM   471   C  C   . GLY A  1  63  ? 141.755 -14.434 55.570  1.00 80.84  ?  63  GLY A C   1 
ATOM   472   O  O   . GLY A  1  63  ? 141.423 -13.264 55.362  1.00 81.96  ?  63  GLY A O   1 
ATOM   473   N  N   . ALA A  1  64  ? 141.188 -15.481 54.935  1.00 80.21  ?  64  ALA A N   1 
ATOM   474   C  CA  . ALA A  1  64  ? 140.108 -15.330 53.957  1.00 77.46  ?  64  ALA A CA  1 
ATOM   475   C  C   . ALA A  1  64  ? 138.863 -14.693 54.585  1.00 82.46  ?  64  ALA A C   1 
ATOM   476   O  O   . ALA A  1  64  ? 138.020 -14.188 53.847  1.00 77.88  ?  64  ALA A O   1 
ATOM   477   C  CB  . ALA A  1  64  ? 139.745 -16.679 53.361  1.00 69.36  ?  64  ALA A CB  1 
ATOM   478   N  N   . LEU A  1  65  ? 138.735 -14.711 55.932  1.00 81.64  ?  65  LEU A N   1 
ATOM   479   C  CA  . LEU A  1  65  ? 137.590 -14.089 56.599  1.00 75.21  ?  65  LEU A CA  1 
ATOM   480   C  C   . LEU A  1  65  ? 137.569 -12.581 56.322  1.00 84.10  ?  65  LEU A C   1 
ATOM   481   O  O   . LEU A  1  65  ? 136.492 -11.994 56.298  1.00 86.99  ?  65  LEU A O   1 
ATOM   482   C  CB  . LEU A  1  65  ? 137.615 -14.338 58.120  1.00 65.99  ?  65  LEU A CB  1 
ATOM   483   C  CG  . LEU A  1  65  ? 137.015 -15.666 58.611  1.00 71.44  ?  65  LEU A CG  1 
ATOM   484   C  CD1 . LEU A  1  65  ? 137.509 -16.010 59.997  1.00 73.43  ?  65  LEU A CD1 1 
ATOM   485   C  CD2 . LEU A  1  65  ? 135.501 -15.616 58.630  1.00 61.31  ?  65  LEU A CD2 1 
ATOM   486   N  N   . ASP A  1  66  ? 138.744 -11.954 56.100  1.00 82.18  ?  66  ASP A N   1 
ATOM   487   C  CA  . ASP A  1  66  ? 138.821 -10.523 55.801  1.00 79.82  ?  66  ASP A CA  1 
ATOM   488   C  C   . ASP A  1  66  ? 138.182 -10.193 54.441  1.00 81.57  ?  66  ASP A C   1 
ATOM   489   O  O   . ASP A  1  66  ? 137.713 -9.069  54.252  1.00 73.46  ?  66  ASP A O   1 
ATOM   490   C  CB  . ASP A  1  66  ? 140.276 -10.034 55.854  1.00 85.44  ?  66  ASP A CB  1 
ATOM   491   C  CG  . ASP A  1  66  ? 140.833 -9.946  57.263  1.00 101.07 ?  66  ASP A CG  1 
ATOM   492   O  OD1 . ASP A  1  66  ? 140.097 -9.487  58.168  1.00 95.08  ?  66  ASP A OD1 1 
ATOM   493   O  OD2 . ASP A  1  66  ? 142.006 -10.331 57.461  1.00 121.19 ?  66  ASP A OD2 1 
ATOM   494   N  N   . ILE A  1  67  ? 138.141 -11.169 53.505  1.00 79.73  ?  67  ILE A N   1 
ATOM   495   C  CA  . ILE A  1  67  ? 137.504 -10.983 52.196  1.00 71.30  ?  67  ILE A CA  1 
ATOM   496   C  C   . ILE A  1  67  ? 136.004 -10.808 52.443  1.00 68.51  ?  67  ILE A C   1 
ATOM   497   O  O   . ILE A  1  67  ? 135.379 -9.927  51.859  1.00 75.92  ?  67  ILE A O   1 
ATOM   498   C  CB  . ILE A  1  67  ? 137.758 -12.193 51.256  1.00 60.93  ?  67  ILE A CB  1 
ATOM   499   C  CG1 . ILE A  1  67  ? 139.253 -12.339 50.912  1.00 74.75  ?  67  ILE A CG1 1 
ATOM   500   C  CG2 . ILE A  1  67  ? 136.933 -12.068 49.974  1.00 49.71  ?  67  ILE A CG2 1 
ATOM   501   C  CD1 . ILE A  1  67  ? 139.652 -13.742 50.425  1.00 65.57  ?  67  ILE A CD1 1 
ATOM   502   N  N   . VAL A  1  68  ? 135.432 -11.636 53.333  1.00 64.96  ?  68  VAL A N   1 
ATOM   503   C  CA  . VAL A  1  68  ? 134.014 -11.569 53.677  1.00 66.48  ?  68  VAL A CA  1 
ATOM   504   C  C   . VAL A  1  68  ? 133.707 -10.197 54.276  1.00 67.40  ?  68  VAL A C   1 
ATOM   505   O  O   . VAL A  1  68  ? 132.724 -9.564  53.898  1.00 76.50  ?  68  VAL A O   1 
ATOM   506   C  CB  . VAL A  1  68  ? 133.610 -12.694 54.662  1.00 58.55  ?  68  VAL A CB  1 
ATOM   507   C  CG1 . VAL A  1  68  ? 132.153 -12.550 55.087  1.00 54.95  ?  68  VAL A CG1 1 
ATOM   508   C  CG2 . VAL A  1  68  ? 133.848 -14.071 54.058  1.00 52.86  ?  68  VAL A CG2 1 
ATOM   509   N  N   . ARG A  1  69  ? 134.561 -9.734  55.198  1.00 67.54  ?  69  ARG A N   1 
ATOM   510   C  CA  . ARG A  1  69  ? 134.385 -8.442  55.862  1.00 70.13  ?  69  ARG A CA  1 
ATOM   511   C  C   . ARG A  1  69  ? 134.458 -7.291  54.856  1.00 64.98  ?  69  ARG A C   1 
ATOM   512   O  O   . ARG A  1  69  ? 133.655 -6.362  54.932  1.00 70.25  ?  69  ARG A O   1 
ATOM   513   C  CB  . ARG A  1  69  ? 135.443 -8.259  56.969  1.00 62.71  ?  69  ARG A CB  1 
ATOM   514   C  CG  . ARG A  1  69  ? 135.393 -9.345  58.042  1.00 64.09  ?  69  ARG A CG  1 
ATOM   515   C  CD  . ARG A  1  69  ? 136.142 -8.980  59.312  1.00 85.22  ?  69  ARG A CD  1 
ATOM   516   N  NE  . ARG A  1  69  ? 136.173 -10.099 60.260  1.00 81.40  ?  69  ARG A NE  1 
ATOM   517   C  CZ  . ARG A  1  69  ? 137.132 -11.024 60.330  1.00 82.81  ?  69  ARG A CZ  1 
ATOM   518   N  NH1 . ARG A  1  69  ? 138.174 -10.978 59.507  1.00 82.61  ?  69  ARG A NH1 1 
ATOM   519   N  NH2 . ARG A  1  69  ? 137.054 -12.001 61.222  1.00 93.03  ?  69  ARG A NH2 1 
ATOM   520   N  N   . SER A  1  70  ? 135.410 -7.360  53.912  1.00 58.69  ?  70  SER A N   1 
ATOM   521   C  CA  . SER A  1  70  ? 135.593 -6.319  52.901  1.00 71.62  ?  70  SER A CA  1 
ATOM   522   C  C   . SER A  1  70  ? 134.402 -6.196  51.944  1.00 69.38  ?  70  SER A C   1 
ATOM   523   O  O   . SER A  1  70  ? 134.108 -5.099  51.464  1.00 72.42  ?  70  SER A O   1 
ATOM   524   C  CB  . SER A  1  70  ? 136.873 -6.571  52.108  1.00 65.36  ?  70  SER A CB  1 
ATOM   525   O  OG  . SER A  1  70  ? 136.734 -7.645  51.191  1.00 82.44  ?  70  SER A OG  1 
ATOM   526   N  N   . LEU A  1  71  ? 133.723 -7.310  51.665  1.00 68.70  ?  71  LEU A N   1 
ATOM   527   C  CA  . LEU A  1  71  ? 132.574 -7.297  50.769  1.00 62.29  ?  71  LEU A CA  1 
ATOM   528   C  C   . LEU A  1  71  ? 131.296 -6.760  51.440  1.00 67.87  ?  71  LEU A C   1 
ATOM   529   O  O   . LEU A  1  71  ? 130.353 -6.401  50.730  1.00 74.73  ?  71  LEU A O   1 
ATOM   530   C  CB  . LEU A  1  71  ? 132.345 -8.704  50.199  1.00 50.98  ?  71  LEU A CB  1 
ATOM   531   C  CG  . LEU A  1  71  ? 133.319 -9.136  49.097  1.00 51.99  ?  71  LEU A CG  1 
ATOM   532   C  CD1 . LEU A  1  71  ? 133.400 -10.638 48.999  1.00 52.87  ?  71  LEU A CD1 1 
ATOM   533   C  CD2 . LEU A  1  71  ? 132.911 -8.563  47.755  1.00 68.67  ?  71  LEU A CD2 1 
ATOM   534   N  N   . ILE A  1  72  ? 131.255 -6.675  52.785  1.00 64.57  ?  72  ILE A N   1 
ATOM   535   C  CA  . ILE A  1  72  ? 130.072 -6.143  53.467  1.00 63.44  ?  72  ILE A CA  1 
ATOM   536   C  C   . ILE A  1  72  ? 130.252 -4.640  53.729  1.00 63.90  ?  72  ILE A C   1 
ATOM   537   O  O   . ILE A  1  72  ? 131.025 -4.250  54.603  1.00 69.24  ?  72  ILE A O   1 
ATOM   538   C  CB  . ILE A  1  72  ? 129.729 -6.913  54.776  1.00 53.93  ?  72  ILE A CB  1 
ATOM   539   C  CG1 . ILE A  1  72  ? 129.542 -8.414  54.503  1.00 56.98  ?  72  ILE A CG1 1 
ATOM   540   C  CG2 . ILE A  1  72  ? 128.452 -6.341  55.408  1.00 49.87  ?  72  ILE A CG2 1 
ATOM   541   C  CD1 . ILE A  1  72  ? 129.539 -9.287  55.750  1.00 48.35  ?  72  ILE A CD1 1 
ATOM   542   N  N   . VAL A  1  73  ? 129.543 -3.800  52.963  1.00 63.36  ?  73  VAL A N   1 
ATOM   543   C  CA  . VAL A  1  73  ? 129.574 -2.345  53.121  1.00 62.36  ?  73  VAL A CA  1 
ATOM   544   C  C   . VAL A  1  73  ? 128.122 -1.918  53.247  1.00 72.70  ?  73  VAL A C   1 
ATOM   545   O  O   . VAL A  1  73  ? 127.406 -1.858  52.249  1.00 68.42  ?  73  VAL A O   1 
ATOM   546   C  CB  . VAL A  1  73  ? 130.274 -1.642  51.947  1.00 53.64  ?  73  VAL A CB  1 
ATOM   547   C  CG1 . VAL A  1  73  ? 130.268 -0.130  52.142  1.00 56.27  ?  73  VAL A CG1 1 
ATOM   548   C  CG2 . VAL A  1  73  ? 131.697 -2.161  51.784  1.00 70.88  ?  73  VAL A CG2 1 
ATOM   549   N  N   . GLU A  1  74  ? 127.710 -1.612  54.488  1.00 76.29  ?  74  GLU A N   1 
ATOM   550   C  CA  . GLU A  1  74  ? 126.294 -1.254  54.785  1.00 64.05  ?  74  GLU A CA  1 
ATOM   551   C  C   . GLU A  1  74  ? 125.946 0.133   54.243  1.00 70.48  ?  74  GLU A C   1 
ATOM   552   O  O   . GLU A  1  74  ? 125.851 1.075   55.052  1.00 61.23  ?  74  GLU A O   1 
ATOM   553   C  CB  . GLU A  1  74  ? 126.037 -1.352  56.291  1.00 83.14  ?  74  GLU A CB  1 
ATOM   554   C  CG  . GLU A  1  74  ? 126.083 -2.777  56.811  1.00 65.93  ?  74  GLU A CG  1 
ATOM   555   C  CD  . GLU A  1  74  ? 125.362 -2.994  58.130  1.00 83.00  ?  74  GLU A CD  1 
ATOM   556   O  OE1 . GLU A  1  74  ? 124.124 -2.858  58.153  1.00 90.83  ?  74  GLU A OE1 1 
ATOM   557   O  OE2 . GLU A  1  74  ? 126.042 -3.296  59.129  1.00 67.13  ?  74  GLU A OE2 1 
ATOM   558   N  N   . GLU A  1  75  ? 125.757 0.242   52.933  1.00 70.58  ?  75  GLU A N   1 
ATOM   559   C  CA  . GLU A  1  75  ? 125.354 1.477   52.263  1.00 70.67  ?  75  GLU A CA  1 
ATOM   560   C  C   . GLU A  1  75  ? 124.289 1.051   51.263  1.00 60.38  ?  75  GLU A C   1 
ATOM   561   O  O   . GLU A  1  75  ? 124.509 0.103   50.515  1.00 69.11  ?  75  GLU A O   1 
ATOM   562   C  CB  . GLU A  1  75  ? 126.550 2.150   51.576  1.00 56.63  ?  75  GLU A CB  1 
ATOM   563   C  CG  . GLU A  1  75  ? 127.572 2.671   52.572  1.00 59.27  ?  75  GLU A CG  1 
ATOM   564   C  CD  . GLU A  1  75  ? 128.765 3.374   51.959  1.00 78.22  ?  75  GLU A CD  1 
ATOM   565   O  OE1 . GLU A  1  75  ? 128.690 3.748   50.766  1.00 93.21  ?  75  GLU A OE1 1 
ATOM   566   O  OE2 . GLU A  1  75  ? 129.776 3.556   52.675  1.00 76.27  ?  75  GLU A OE2 1 
ATOM   567   N  N   . GLU A  1  76  ? 123.128 1.703   51.268  1.00 61.27  ?  76  GLU A N   1 
ATOM   568   C  CA  . GLU A  1  76  ? 122.034 1.293   50.393  1.00 63.56  ?  76  GLU A CA  1 
ATOM   569   C  C   . GLU A  1  76  ? 122.196 1.707   48.923  1.00 62.74  ?  76  GLU A C   1 
ATOM   570   O  O   . GLU A  1  76  ? 121.640 2.714   48.493  1.00 68.19  ?  76  GLU A O   1 
ATOM   571   C  CB  . GLU A  1  76  ? 120.691 1.768   50.970  1.00 72.66  ?  76  GLU A CB  1 
ATOM   572   C  CG  . GLU A  1  76  ? 120.462 1.258   52.388  1.00 68.91  ?  76  GLU A CG  1 
ATOM   573   C  CD  . GLU A  1  76  ? 119.032 1.239   52.889  1.00 77.88  ?  76  GLU A CD  1 
ATOM   574   O  OE1 . GLU A  1  76  ? 118.142 1.794   52.202  1.00 79.28  ?  76  GLU A OE1 1 
ATOM   575   O  OE2 . GLU A  1  76  ? 118.803 0.665   53.979  1.00 81.65  ?  76  GLU A OE2 1 
ATOM   576   N  N   . MET A  1  77  ? 122.936 0.874   48.179  1.00 49.30  ?  77  MET A N   1 
ATOM   577   C  CA  . MET A  1  77  ? 123.134 1.071   46.719  1.00 52.01  ?  77  MET A CA  1 
ATOM   578   C  C   . MET A  1  77  ? 123.280 -0.337  46.133  1.00 51.83  ?  77  MET A C   1 
ATOM   579   O  O   . MET A  1  77  ? 123.907 -1.175  46.806  1.00 58.55  ?  77  MET A O   1 
ATOM   580   C  CB  . MET A  1  77  ? 124.397 1.884   46.429  1.00 60.81  ?  77  MET A CB  1 
ATOM   581   C  CG  . MET A  1  77  ? 124.232 3.369   46.681  1.00 61.98  ?  77  MET A CG  1 
ATOM   582   S  SD  . MET A  1  77  ? 123.240 4.186   45.406  1.00 75.21  ?  77  MET A SD  1 
ATOM   583   C  CE  . MET A  1  77  ? 124.502 4.541   44.185  1.00 72.37  ?  77  MET A CE  1 
ATOM   584   N  N   . LEU A  1  78  ? 122.735 -0.601  44.943  1.00 54.01  ?  78  LEU A N   1 
ATOM   585   C  CA  . LEU A  1  78  ? 122.734 -1.987  44.390  1.00 47.60  ?  78  LEU A CA  1 
ATOM   586   C  C   . LEU A  1  78  ? 124.096 -2.669  44.566  1.00 55.50  ?  78  LEU A C   1 
ATOM   587   O  O   . LEU A  1  78  ? 124.141 -3.709  45.248  1.00 63.96  ?  78  LEU A O   1 
ATOM   588   C  CB  . LEU A  1  78  ? 122.351 -1.929  42.908  1.00 56.13  ?  78  LEU A CB  1 
ATOM   589   C  CG  . LEU A  1  78  ? 122.115 -3.282  42.241  1.00 45.98  ?  78  LEU A CG  1 
ATOM   590   C  CD1 . LEU A  1  78  ? 121.271 -4.182  43.131  1.00 38.91  ?  78  LEU A CD1 1 
ATOM   591   C  CD2 . LEU A  1  78  ? 121.457 -3.108  40.882  1.00 47.20  ?  78  LEU A CD2 1 
ATOM   592   N  N   . ASP A  1  79  ? 125.156 -2.123  43.967  1.00 46.43  ?  79  ASP A N   1 
ATOM   593   C  CA  . ASP A  1  79  ? 126.495 -2.773  44.014  1.00 47.48  ?  79  ASP A CA  1 
ATOM   594   C  C   . ASP A  1  79  ? 126.794 -3.292  45.422  1.00 55.89  ?  79  ASP A C   1 
ATOM   595   O  O   . ASP A  1  79  ? 127.336 -4.407  45.531  1.00 61.43  ?  79  ASP A O   1 
ATOM   596   C  CB  . ASP A  1  79  ? 127.584 -1.797  43.568  1.00 45.76  ?  79  ASP A CB  1 
ATOM   597   C  CG  . ASP A  1  79  ? 127.714 -0.590  44.480  1.00 63.46  ?  79  ASP A CG  1 
ATOM   598   O  OD1 . ASP A  1  79  ? 126.672 0.013   44.804  1.00 77.06  ?  79  ASP A OD1 1 
ATOM   599   O  OD2 . ASP A  1  79  ? 128.855 -0.265  44.862  1.00 76.12  ?  79  ASP A OD2 1 
ATOM   600   N  N   . LYS A  1  80  ? 126.456 -2.518  46.453  1.00 61.93  ?  80  LYS A N   1 
ATOM   601   C  CA  . LYS A  1  80  ? 126.772 -2.882  47.839  1.00 63.57  ?  80  LYS A CA  1 
ATOM   602   C  C   . LYS A  1  80  ? 125.988 -4.134  48.221  1.00 52.06  ?  80  LYS A C   1 
ATOM   603   O  O   . LYS A  1  80  ? 126.535 -5.029  48.866  1.00 58.00  ?  80  LYS A O   1 
ATOM   604   C  CB  . LYS A  1  80  ? 126.437 -1.735  48.819  1.00 51.63  ?  80  LYS A CB  1 
ATOM   605   C  CG  . LYS A  1  80  ? 126.853 -0.328  48.372  1.00 50.78  ?  80  LYS A CG  1 
ATOM   606   C  CD  . LYS A  1  80  ? 128.306 -0.021  48.632  1.00 61.89  ?  80  LYS A CD  1 
ATOM   607   C  CE  . LYS A  1  80  ? 128.705 1.318   48.053  1.00 53.51  ?  80  LYS A CE  1 
ATOM   608   N  NZ  . LYS A  1  80  ? 129.869 1.190   47.144  1.00 84.27  ?  80  LYS A NZ  1 
ATOM   609   N  N   . LEU A  1  81  ? 124.714 -4.177  47.824  1.00 46.81  ?  81  LEU A N   1 
ATOM   610   C  CA  . LEU A  1  81  ? 123.852 -5.352  48.116  1.00 50.48  ?  81  LEU A CA  1 
ATOM   611   C  C   . LEU A  1  81  ? 124.463 -6.586  47.453  1.00 56.01  ?  81  LEU A C   1 
ATOM   612   O  O   . LEU A  1  81  ? 124.587 -7.620  48.131  1.00 62.13  ?  81  LEU A O   1 
ATOM   613   C  CB  . LEU A  1  81  ? 122.454 -5.073  47.559  1.00 46.64  ?  81  LEU A CB  1 
ATOM   614   C  CG  . LEU A  1  81  ? 121.335 -5.986  48.054  1.00 61.18  ?  81  LEU A CG  1 
ATOM   615   C  CD1 . LEU A  1  81  ? 120.052 -5.193  48.259  1.00 70.54  ?  81  LEU A CD1 1 
ATOM   616   C  CD2 . LEU A  1  81  ? 121.100 -7.125  47.076  1.00 37.13  ?  81  LEU A CD2 1 
ATOM   617   N  N   . LEU A  1  82  ? 124.824 -6.474  46.174  1.00 53.54  ?  82  LEU A N   1 
ATOM   618   C  CA  . LEU A  1  82  ? 125.364 -7.629  45.463  1.00 59.77  ?  82  LEU A CA  1 
ATOM   619   C  C   . LEU A  1  82  ? 126.687 -8.086  46.094  1.00 59.16  ?  82  LEU A C   1 
ATOM   620   O  O   . LEU A  1  82  ? 126.888 -9.288  46.259  1.00 63.38  ?  82  LEU A O   1 
ATOM   621   C  CB  . LEU A  1  82  ? 125.520 -7.326  43.962  1.00 57.76  ?  82  LEU A CB  1 
ATOM   622   C  CG  . LEU A  1  82  ? 124.245 -6.861  43.232  1.00 49.83  ?  82  LEU A CG  1 
ATOM   623   C  CD1 . LEU A  1  82  ? 124.577 -6.293  41.877  1.00 46.00  ?  82  LEU A CD1 1 
ATOM   624   C  CD2 . LEU A  1  82  ? 123.248 -7.987  43.066  1.00 35.15  ?  82  LEU A CD2 1 
ATOM   625   N  N   . ASN A  1  83  ? 127.571 -7.148  46.483  1.00 59.86  ?  83  ASN A N   1 
ATOM   626   C  CA  . ASN A  1  83  ? 128.833 -7.517  47.135  1.00 57.65  ?  83  ASN A CA  1 
ATOM   627   C  C   . ASN A  1  83  ? 128.558 -8.193  48.470  1.00 59.31  ?  83  ASN A C   1 
ATOM   628   O  O   . ASN A  1  83  ? 129.263 -9.133  48.828  1.00 63.38  ?  83  ASN A O   1 
ATOM   629   C  CB  . ASN A  1  83  ? 129.723 -6.301  47.347  1.00 51.30  ?  83  ASN A CB  1 
ATOM   630   C  CG  . ASN A  1  83  ? 130.468 -5.883  46.112  1.00 57.57  ?  83  ASN A CG  1 
ATOM   631   O  OD1 . ASN A  1  83  ? 130.517 -6.605  45.112  1.00 65.43  ?  83  ASN A OD1 1 
ATOM   632   N  ND2 . ASN A  1  83  ? 131.071 -4.705  46.150  1.00 65.39  ?  83  ASN A ND2 1 
ATOM   633   N  N   . SER A  1  84  ? 127.526 -7.739  49.202  1.00 57.60  ?  84  SER A N   1 
ATOM   634   C  CA  . SER A  1  84  ? 127.139 -8.358  50.471  1.00 52.27  ?  84  SER A CA  1 
ATOM   635   C  C   . SER A  1  84  ? 126.721 -9.816  50.207  1.00 58.36  ?  84  SER A C   1 
ATOM   636   O  O   . SER A  1  84  ? 127.001 -10.693 51.020  1.00 60.96  ?  84  SER A O   1 
ATOM   637   C  CB  . SER A  1  84  ? 125.984 -7.589  51.107  1.00 59.61  ?  84  SER A CB  1 
ATOM   638   O  OG  . SER A  1  84  ? 125.793 -7.943  52.468  1.00 63.74  ?  84  SER A OG  1 
ATOM   639   N  N   . GLY A  1  85  ? 126.070 -10.058 49.071  1.00 56.88  ?  85  GLY A N   1 
ATOM   640   C  CA  . GLY A  1  85  ? 125.667 -11.394 48.667  1.00 52.87  ?  85  GLY A CA  1 
ATOM   641   C  C   . GLY A  1  85  ? 126.890 -12.245 48.386  1.00 61.21  ?  85  GLY A C   1 
ATOM   642   O  O   . GLY A  1  85  ? 126.923 -13.418 48.763  1.00 72.31  ?  85  GLY A O   1 
ATOM   643   N  N   . LEU A  1  86  ? 127.922 -11.658 47.737  1.00 54.54  ?  86  LEU A N   1 
ATOM   644   C  CA  . LEU A  1  86  ? 129.169 -12.380 47.461  1.00 50.75  ?  86  LEU A CA  1 
ATOM   645   C  C   . LEU A  1  86  ? 129.909 -12.653 48.771  1.00 61.50  ?  86  LEU A C   1 
ATOM   646   O  O   . LEU A  1  86  ? 130.620 -13.650 48.870  1.00 58.43  ?  86  LEU A O   1 
ATOM   647   C  CB  . LEU A  1  86  ? 130.088 -11.610 46.502  1.00 45.44  ?  86  LEU A CB  1 
ATOM   648   C  CG  . LEU A  1  86  ? 129.590 -11.433 45.068  1.00 57.70  ?  86  LEU A CG  1 
ATOM   649   C  CD1 . LEU A  1  86  ? 130.520 -10.524 44.289  1.00 48.81  ?  86  LEU A CD1 1 
ATOM   650   C  CD2 . LEU A  1  86  ? 129.440 -12.768 44.350  1.00 45.40  ?  86  LEU A CD2 1 
ATOM   651   N  N   . ALA A  1  87  ? 129.736 -11.788 49.787  1.00 56.63  ?  87  ALA A N   1 
ATOM   652   C  CA  . ALA A  1  87  ? 130.352 -11.993 51.091  1.00 55.47  ?  87  ALA A CA  1 
ATOM   653   C  C   . ALA A  1  87  ? 129.747 -13.259 51.704  1.00 49.66  ?  87  ALA A C   1 
ATOM   654   O  O   . ALA A  1  87  ? 130.475 -14.076 52.251  1.00 61.98  ?  87  ALA A O   1 
ATOM   655   C  CB  . ALA A  1  87  ? 130.085 -10.798 51.996  1.00 56.59  ?  87  ALA A CB  1 
ATOM   656   N  N   . THR A  1  88  ? 128.421 -13.435 51.581  1.00 45.96  ?  88  THR A N   1 
ATOM   657   C  CA  . THR A  1  88  ? 127.735 -14.620 52.091  1.00 55.42  ?  88  THR A CA  1 
ATOM   658   C  C   . THR A  1  88  ? 128.243 -15.863 51.356  1.00 56.49  ?  88  THR A C   1 
ATOM   659   O  O   . THR A  1  88  ? 128.433 -16.906 51.979  1.00 57.78  ?  88  THR A O   1 
ATOM   660   C  CB  . THR A  1  88  ? 126.213 -14.449 51.957  1.00 60.48  ?  88  THR A CB  1 
ATOM   661   O  OG1 . THR A  1  88  ? 125.784 -13.360 52.785  1.00 62.74  ?  88  THR A OG1 1 
ATOM   662   C  CG2 . THR A  1  88  ? 125.443 -15.703 52.346  1.00 43.24  ?  88  THR A CG2 1 
ATOM   663   N  N   . ALA A  1  89  ? 128.478 -15.757 50.043  1.00 49.61  ?  89  ALA A N   1 
ATOM   664   C  CA  . ALA A  1  89  ? 128.991 -16.878 49.265  1.00 52.28  ?  89  ALA A CA  1 
ATOM   665   C  C   . ALA A  1  89  ? 130.402 -17.249 49.745  1.00 67.23  ?  89  ALA A C   1 
ATOM   666   O  O   . ALA A  1  89  ? 130.681 -18.427 49.942  1.00 70.49  ?  89  ALA A O   1 
ATOM   667   C  CB  . ALA A  1  89  ? 129.005 -16.526 47.787  1.00 44.17  ?  89  ALA A CB  1 
ATOM   668   N  N   . VAL A  1  90  ? 131.281 -16.256 49.962  1.00 60.28  ?  90  VAL A N   1 
ATOM   669   C  CA  . VAL A  1  90  ? 132.639 -16.532 50.439  1.00 63.63  ?  90  VAL A CA  1 
ATOM   670   C  C   . VAL A  1  90  ? 132.577 -17.125 51.862  1.00 65.06  ?  90  VAL A C   1 
ATOM   671   O  O   . VAL A  1  90  ? 133.325 -18.050 52.178  1.00 73.96  ?  90  VAL A O   1 
ATOM   672   C  CB  . VAL A  1  90  ? 133.541 -15.273 50.376  1.00 59.17  ?  90  VAL A CB  1 
ATOM   673   C  CG1 . VAL A  1  90  ? 134.875 -15.526 51.071  1.00 51.09  ?  90  VAL A CG1 1 
ATOM   674   C  CG2 . VAL A  1  90  ? 133.772 -14.839 48.931  1.00 49.91  ?  90  VAL A CG2 1 
ATOM   675   N  N   . ALA A  1  91  ? 131.680 -16.612 52.713  1.00 58.64  ?  91  ALA A N   1 
ATOM   676   C  CA  . ALA A  1  91  ? 131.525 -17.118 54.072  1.00 58.29  ?  91  ALA A CA  1 
ATOM   677   C  C   . ALA A  1  91  ? 131.087 -18.582 54.045  1.00 64.46  ?  91  ALA A C   1 
ATOM   678   O  O   . ALA A  1  91  ? 131.593 -19.386 54.825  1.00 70.22  ?  91  ALA A O   1 
ATOM   679   C  CB  . ALA A  1  91  ? 130.496 -16.285 54.822  1.00 53.78  ?  91  ALA A CB  1 
ATOM   680   N  N   . ALA A  1  92  ? 130.153 -18.931 53.138  1.00 54.51  ?  92  ALA A N   1 
ATOM   681   C  CA  . ALA A  1  92  ? 129.650 -20.298 53.007  1.00 56.74  ?  92  ALA A CA  1 
ATOM   682   C  C   . ALA A  1  92  ? 130.769 -21.242 52.581  1.00 66.11  ?  92  ALA A C   1 
ATOM   683   O  O   . ALA A  1  92  ? 130.824 -22.376 53.057  1.00 66.62  ?  92  ALA A O   1 
ATOM   684   C  CB  . ALA A  1  92  ? 128.515 -20.343 51.997  1.00 44.79  ?  92  ALA A CB  1 
ATOM   685   N  N   . GLU A  1  93  ? 131.662 -20.776 51.694  1.00 56.94  ?  93  GLU A N   1 
ATOM   686   C  CA  . GLU A  1  93  ? 132.786 -21.577 51.232  1.00 53.66  ?  93  GLU A CA  1 
ATOM   687   C  C   . GLU A  1  93  ? 133.725 -21.845 52.390  1.00 50.39  ?  93  GLU A C   1 
ATOM   688   O  O   . GLU A  1  93  ? 134.164 -22.975 52.568  1.00 59.49  ?  93  GLU A O   1 
ATOM   689   C  CB  . GLU A  1  93  ? 133.549 -20.862 50.114  1.00 57.43  ?  93  GLU A CB  1 
ATOM   690   C  CG  . GLU A  1  93  ? 134.715 -21.685 49.609  1.00 59.90  ?  93  GLU A CG  1 
ATOM   691   C  CD  . GLU A  1  93  ? 135.229 -21.273 48.249  1.00 82.32  ?  93  GLU A CD  1 
ATOM   692   O  OE1 . GLU A  1  93  ? 135.935 -20.241 48.166  1.00 81.67  ?  93  GLU A OE1 1 
ATOM   693   O  OE2 . GLU A  1  93  ? 134.929 -21.984 47.262  1.00 90.41  ?  93  GLU A OE2 1 
ATOM   694   N  N   . ILE A  1  94  ? 134.035 -20.812 53.182  1.00 58.84  ?  94  ILE A N   1 
ATOM   695   C  CA  . ILE A  1  94  ? 134.920 -20.956 54.339  1.00 69.65  ?  94  ILE A CA  1 
ATOM   696   C  C   . ILE A  1  94  ? 134.300 -21.958 55.330  1.00 67.87  ?  94  ILE A C   1 
ATOM   697   O  O   . ILE A  1  94  ? 134.988 -22.875 55.777  1.00 70.36  ?  94  ILE A O   1 
ATOM   698   C  CB  . ILE A  1  94  ? 135.200 -19.573 54.992  1.00 59.60  ?  94  ILE A CB  1 
ATOM   699   C  CG1 . ILE A  1  94  ? 136.102 -18.711 54.082  1.00 69.26  ?  94  ILE A CG1 1 
ATOM   700   C  CG2 . ILE A  1  94  ? 135.833 -19.742 56.368  1.00 64.97  ?  94  ILE A CG2 1 
ATOM   701   C  CD1 . ILE A  1  94  ? 135.943 -17.205 54.271  1.00 66.20  ?  94  ILE A CD1 1 
ATOM   702   N  N   . ILE A  1  95  ? 132.998 -21.811 55.632  1.00 56.86  ?  95  ILE A N   1 
ATOM   703   C  CA  . ILE A  1  95  ? 132.308 -22.727 56.547  1.00 67.74  ?  95  ILE A CA  1 
ATOM   704   C  C   . ILE A  1  95  ? 132.411 -24.186 56.047  1.00 72.02  ?  95  ILE A C   1 
ATOM   705   O  O   . ILE A  1  95  ? 132.677 -25.090 56.839  1.00 65.84  ?  95  ILE A O   1 
ATOM   706   C  CB  . ILE A  1  95  ? 130.827 -22.297 56.754  1.00 58.69  ?  95  ILE A CB  1 
ATOM   707   C  CG1 . ILE A  1  95  ? 130.749 -20.963 57.528  1.00 63.45  ?  95  ILE A CG1 1 
ATOM   708   C  CG2 . ILE A  1  95  ? 130.036 -23.391 57.491  1.00 53.63  ?  95  ILE A CG2 1 
ATOM   709   C  CD1 . ILE A  1  95  ? 129.479 -20.179 57.304  1.00 64.33  ?  95  ILE A CD1 1 
ATOM   710   N  N   . GLU A  1  96  ? 132.214 -24.409 54.738  1.00 64.44  ?  96  GLU A N   1 
ATOM   711   C  CA  . GLU A  1  96  ? 132.282 -25.748 54.147  1.00 56.12  ?  96  GLU A CA  1 
ATOM   712   C  C   . GLU A  1  96  ? 133.712 -26.283 54.085  1.00 67.56  ?  96  GLU A C   1 
ATOM   713   O  O   . GLU A  1  96  ? 133.923 -27.476 54.306  1.00 60.23  ?  96  GLU A O   1 
ATOM   714   C  CB  . GLU A  1  96  ? 131.642 -25.754 52.753  1.00 49.57  ?  96  GLU A CB  1 
ATOM   715   C  CG  . GLU A  1  96  ? 130.135 -25.558 52.781  1.00 57.00  ?  96  GLU A CG  1 
ATOM   716   C  CD  . GLU A  1  96  ? 129.376 -26.694 53.432  1.00 67.51  ?  96  GLU A CD  1 
ATOM   717   O  OE1 . GLU A  1  96  ? 129.780 -27.865 53.246  1.00 65.48  ?  96  GLU A OE1 1 
ATOM   718   O  OE2 . GLU A  1  96  ? 128.371 -26.418 54.127  1.00 65.99  ?  96  GLU A OE2 1 
ATOM   719   N  N   . ALA A  1  97  ? 134.697 -25.416 53.796  1.00 65.02  ?  97  ALA A N   1 
ATOM   720   C  CA  . ALA A  1  97  ? 136.098 -25.833 53.752  1.00 51.34  ?  97  ALA A CA  1 
ATOM   721   C  C   . ALA A  1  97  ? 136.530 -26.266 55.156  1.00 64.52  ?  97  ALA A C   1 
ATOM   722   O  O   . ALA A  1  97  ? 137.240 -27.264 55.311  1.00 64.19  ?  97  ALA A O   1 
ATOM   723   C  CB  . ALA A  1  97  ? 136.970 -24.692 53.259  1.00 51.68  ?  97  ALA A CB  1 
ATOM   724   N  N   . ALA A  1  98  ? 136.077 -25.529 56.182  1.00 60.90  ?  98  ALA A N   1 
ATOM   725   C  CA  . ALA A  1  98  ? 136.383 -25.862 57.565  1.00 69.25  ?  98  ALA A CA  1 
ATOM   726   C  C   . ALA A  1  98  ? 135.751 -27.207 57.931  1.00 64.38  ?  98  ALA A C   1 
ATOM   727   O  O   . ALA A  1  98  ? 136.367 -27.984 58.653  1.00 70.13  ?  98  ALA A O   1 
ATOM   728   C  CB  . ALA A  1  98  ? 135.874 -24.777 58.485  1.00 62.23  ?  98  ALA A CB  1 
ATOM   729   N  N   . LYS A  1  99  ? 134.542 -27.499 57.411  1.00 60.74  ?  99  LYS A N   1 
ATOM   730   C  CA  . LYS A  1  99  ? 133.848 -28.770 57.652  1.00 57.00  ?  99  LYS A CA  1 
ATOM   731   C  C   . LYS A  1  99  ? 134.743 -29.951 57.230  1.00 66.46  ?  99  LYS A C   1 
ATOM   732   O  O   . LYS A  1  99  ? 134.811 -30.955 57.932  1.00 72.38  ?  99  LYS A O   1 
ATOM   733   C  CB  . LYS A  1  99  ? 132.533 -28.829 56.850  1.00 52.25  ?  99  LYS A CB  1 
ATOM   734   C  CG  . LYS A  1  99  ? 131.378 -28.028 57.437  1.00 54.76  ?  99  LYS A CG  1 
ATOM   735   C  CD  . LYS A  1  99  ? 130.112 -28.186 56.597  1.00 56.88  ?  99  LYS A CD  1 
ATOM   736   C  CE  . LYS A  1  99  ? 128.841 -28.148 57.401  1.00 69.69  ?  99  LYS A CE  1 
ATOM   737   N  NZ  . LYS A  1  99  ? 127.665 -28.525 56.575  1.00 74.04  ?  99  LYS A NZ  1 
ATOM   738   N  N   . TYR A  1  100 ? 135.423 -29.816 56.078  1.00 72.11  ?  100 TYR A N   1 
ATOM   739   C  CA  . TYR A  1  100 ? 136.328 -30.841 55.549  1.00 62.83  ?  100 TYR A CA  1 
ATOM   740   C  C   . TYR A  1  100 ? 137.645 -30.923 56.346  1.00 73.85  ?  100 TYR A C   1 
ATOM   741   O  O   . TYR A  1  100 ? 138.357 -31.924 56.239  1.00 80.54  ?  100 TYR A O   1 
ATOM   742   C  CB  . TYR A  1  100 ? 136.604 -30.589 54.050  1.00 64.62  ?  100 TYR A CB  1 
ATOM   743   C  CG  . TYR A  1  100 ? 135.483 -31.067 53.153  1.00 59.39  ?  100 TYR A CG  1 
ATOM   744   C  CD1 . TYR A  1  100 ? 134.323 -30.324 53.000  1.00 51.09  ?  100 TYR A CD1 1 
ATOM   745   C  CD2 . TYR A  1  100 ? 135.559 -32.290 52.504  1.00 66.56  ?  100 TYR A CD2 1 
ATOM   746   C  CE1 . TYR A  1  100 ? 133.273 -30.779 52.212  1.00 60.47  ?  100 TYR A CE1 1 
ATOM   747   C  CE2 . TYR A  1  100 ? 134.515 -32.757 51.718  1.00 52.62  ?  100 TYR A CE2 1 
ATOM   748   C  CZ  . TYR A  1  100 ? 133.378 -31.993 51.563  1.00 54.12  ?  100 TYR A CZ  1 
ATOM   749   O  OH  . TYR A  1  100 ? 132.343 -32.461 50.787  1.00 67.01  ?  100 TYR A OH  1 
ATOM   750   N  N   . VAL A  1  101 ? 137.964 -29.891 57.148  1.00 69.17  ?  101 VAL A N   1 
ATOM   751   C  CA  . VAL A  1  101 ? 139.164 -29.881 57.986  1.00 80.01  ?  101 VAL A CA  1 
ATOM   752   C  C   . VAL A  1  101 ? 138.843 -30.645 59.280  1.00 80.27  ?  101 VAL A C   1 
ATOM   753   O  O   . VAL A  1  101 ? 139.559 -31.580 59.637  1.00 77.55  ?  101 VAL A O   1 
ATOM   754   C  CB  . VAL A  1  101 ? 139.639 -28.430 58.281  1.00 79.17  ?  101 VAL A CB  1 
ATOM   755   C  CG1 . VAL A  1  101 ? 140.598 -28.387 59.470  1.00 72.84  ?  101 VAL A CG1 1 
ATOM   756   C  CG2 . VAL A  1  101 ? 140.280 -27.807 57.048  1.00 82.93  ?  101 VAL A CG2 1 
ATOM   757   N  N   . LEU A  1  102 ? 137.753 -30.257 59.964  1.00 76.77  ?  102 LEU A N   1 
ATOM   758   C  CA  . LEU A  1  102 ? 137.341 -30.898 61.212  1.00 81.57  ?  102 LEU A CA  1 
ATOM   759   C  C   . LEU A  1  102 ? 136.848 -32.338 61.019  1.00 82.16  ?  102 LEU A C   1 
ATOM   760   O  O   . LEU A  1  102 ? 136.685 -33.055 62.008  1.00 89.16  ?  102 LEU A O   1 
ATOM   761   C  CB  . LEU A  1  102 ? 136.254 -30.063 61.908  1.00 71.89  ?  102 LEU A CB  1 
ATOM   762   C  CG  . LEU A  1  102 ? 136.682 -28.673 62.394  1.00 69.42  ?  102 LEU A CG  1 
ATOM   763   C  CD1 . LEU A  1  102 ? 135.477 -27.817 62.723  1.00 70.33  ?  102 LEU A CD1 1 
ATOM   764   C  CD2 . LEU A  1  102 ? 137.603 -28.765 63.607  1.00 84.51  ?  102 LEU A CD2 1 
ATOM   765   N  N   . SER A  1  103 ? 136.615 -32.766 59.769  1.00 76.28  ?  103 SER A N   1 
ATOM   766   C  CA  . SER A  1  103 ? 136.158 -34.122 59.474  1.00 70.33  ?  103 SER A CA  1 
ATOM   767   C  C   . SER A  1  103 ? 136.623 -34.500 58.068  1.00 72.47  ?  103 SER A C   1 
ATOM   768   O  O   . SER A  1  103 ? 136.373 -33.751 57.133  1.00 82.28  ?  103 SER A O   1 
ATOM   769   C  CB  . SER A  1  103 ? 134.638 -34.196 59.577  1.00 67.63  ?  103 SER A CB  1 
ATOM   770   O  OG  . SER A  1  103 ? 134.169 -35.516 59.363  1.00 91.02  ?  103 SER A OG  1 
ATOM   771   N  N   . ASP A  1  104 ? 137.313 -35.636 57.910  1.00 73.26  ?  104 ASP A N   1 
ATOM   772   C  CA  . ASP A  1  104 ? 137.826 -36.053 56.602  1.00 67.82  ?  104 ASP A CA  1 
ATOM   773   C  C   . ASP A  1  104 ? 136.706 -36.164 55.564  1.00 76.60  ?  104 ASP A C   1 
ATOM   774   O  O   . ASP A  1  104 ? 136.802 -35.572 54.487  1.00 77.16  ?  104 ASP A O   1 
ATOM   775   C  CB  . ASP A  1  104 ? 138.600 -37.381 56.719  1.00 71.33  ?  104 ASP A CB  1 
ATOM   776   C  CG  . ASP A  1  104 ? 139.888 -37.277 57.517  1.00 102.48 ?  104 ASP A CG  1 
ATOM   777   O  OD1 . ASP A  1  104 ? 140.544 -36.207 57.456  1.00 117.78 ?  104 ASP A OD1 1 
ATOM   778   O  OD2 . ASP A  1  104 ? 140.244 -38.266 58.202  1.00 106.38 ?  104 ASP A OD2 1 
ATOM   779   N  N   . ALA A  1  105 ? 135.639 -36.897 55.896  1.00 67.58  ?  105 ALA A N   1 
ATOM   780   C  CA  . ALA A  1  105 ? 134.487 -37.059 55.012  1.00 70.68  ?  105 ALA A CA  1 
ATOM   781   C  C   . ALA A  1  105 ? 133.272 -36.509 55.759  1.00 66.51  ?  105 ALA A C   1 
ATOM   782   O  O   . ALA A  1  105 ? 132.547 -37.283 56.384  1.00 65.78  ?  105 ALA A O   1 
ATOM   783   C  CB  . ALA A  1  105 ? 134.282 -38.531 54.680  1.00 85.66  ?  105 ALA A CB  1 
ATOM   784   N  N   . PRO A  1  106 ? 133.045 -35.178 55.759  1.00 59.51  ?  106 PRO A N   1 
ATOM   785   C  CA  . PRO A  1  106 ? 131.906 -34.646 56.517  1.00 57.09  ?  106 PRO A CA  1 
ATOM   786   C  C   . PRO A  1  106 ? 130.549 -35.065 55.979  1.00 63.75  ?  106 PRO A C   1 
ATOM   787   O  O   . PRO A  1  106 ? 129.605 -35.167 56.757  1.00 66.93  ?  106 PRO A O   1 
ATOM   788   C  CB  . PRO A  1  106 ? 132.106 -33.128 56.455  1.00 58.57  ?  106 PRO A CB  1 
ATOM   789   C  CG  . PRO A  1  106 ? 132.954 -32.896 55.291  1.00 59.68  ?  106 PRO A CG  1 
ATOM   790   C  CD  . PRO A  1  106 ? 133.809 -34.102 55.102  1.00 61.67  ?  106 PRO A CD  1 
ATOM   791   N  N   . TYR A  1  107 ? 130.444 -35.321 54.672  1.00 58.88  ?  107 TYR A N   1 
ATOM   792   C  CA  . TYR A  1  107 ? 129.173 -35.707 54.074  1.00 52.61  ?  107 TYR A CA  1 
ATOM   793   C  C   . TYR A  1  107 ? 129.030 -37.215 53.897  1.00 54.49  ?  107 TYR A C   1 
ATOM   794   O  O   . TYR A  1  107 ? 130.013 -37.948 53.903  1.00 70.28  ?  107 TYR A O   1 
ATOM   795   C  CB  . TYR A  1  107 ? 128.986 -34.984 52.733  1.00 55.08  ?  107 TYR A CB  1 
ATOM   796   C  CG  . TYR A  1  107 ? 128.637 -33.521 52.896  1.00 61.16  ?  107 TYR A CG  1 
ATOM   797   C  CD1 . TYR A  1  107 ? 129.630 -32.557 53.018  1.00 58.48  ?  107 TYR A CD1 1 
ATOM   798   C  CD2 . TYR A  1  107 ? 127.317 -33.103 52.944  1.00 63.12  ?  107 TYR A CD2 1 
ATOM   799   C  CE1 . TYR A  1  107 ? 129.315 -31.214 53.179  1.00 54.81  ?  107 TYR A CE1 1 
ATOM   800   C  CE2 . TYR A  1  107 ? 126.989 -31.763 53.102  1.00 65.53  ?  107 TYR A CE2 1 
ATOM   801   C  CZ  . TYR A  1  107 ? 127.990 -30.820 53.222  1.00 64.04  ?  107 TYR A CZ  1 
ATOM   802   O  OH  . TYR A  1  107 ? 127.646 -29.500 53.392  1.00 62.54  ?  107 TYR A OH  1 
ATOM   803   N  N   . ALA A  1  108 ? 127.786 -37.670 53.754  1.00 65.02  ?  108 ALA A N   1 
ATOM   804   C  CA  . ALA A  1  108 ? 127.446 -39.079 53.565  1.00 55.89  ?  108 ALA A CA  1 
ATOM   805   C  C   . ALA A  1  108 ? 126.105 -39.158 52.845  1.00 60.02  ?  108 ALA A C   1 
ATOM   806   O  O   . ALA A  1  108 ? 125.292 -38.240 52.976  1.00 75.31  ?  108 ALA A O   1 
ATOM   807   C  CB  . ALA A  1  108 ? 127.343 -39.771 54.910  1.00 58.58  ?  108 ALA A CB  1 
ATOM   808   N  N   . GLU A  1  109 ? 125.851 -40.243 52.101  1.00 60.56  ?  109 GLU A N   1 
ATOM   809   C  CA  . GLU A  1  109 ? 124.586 -40.400 51.370  1.00 71.60  ?  109 GLU A CA  1 
ATOM   810   C  C   . GLU A  1  109 ? 123.359 -40.138 52.273  1.00 67.42  ?  109 GLU A C   1 
ATOM   811   O  O   . GLU A  1  109 ? 123.404 -40.489 53.451  1.00 72.25  ?  109 GLU A O   1 
ATOM   812   C  CB  . GLU A  1  109 ? 124.490 -41.805 50.759  1.00 82.70  ?  109 GLU A CB  1 
ATOM   813   C  CG  . GLU A  1  109 ? 125.274 -41.974 49.469  1.00 101.17 ?  109 GLU A CG  1 
ATOM   814   C  CD  . GLU A  1  109 ? 125.164 -43.365 48.878  1.00 134.22 ?  109 GLU A CD  1 
ATOM   815   O  OE1 . GLU A  1  109 ? 124.185 -43.619 48.138  1.00 149.20 ?  109 GLU A OE1 1 
ATOM   816   O  OE2 . GLU A  1  109 ? 126.054 -44.203 49.155  1.00 141.70 ?  109 GLU A OE2 1 
ATOM   817   N  N   . PRO A  1  110 ? 122.276 -39.495 51.783  1.00 59.08  ?  110 PRO A N   1 
ATOM   818   C  CA  . PRO A  1  110 ? 122.039 -39.010 50.412  1.00 58.77  ?  110 PRO A CA  1 
ATOM   819   C  C   . PRO A  1  110 ? 122.882 -37.804 50.012  1.00 66.14  ?  110 PRO A C   1 
ATOM   820   O  O   . PRO A  1  110 ? 123.302 -37.722 48.861  1.00 77.61  ?  110 PRO A O   1 
ATOM   821   C  CB  . PRO A  1  110 ? 120.537 -38.703 50.414  1.00 58.28  ?  110 PRO A CB  1 
ATOM   822   C  CG  . PRO A  1  110 ? 120.235 -38.332 51.827  1.00 59.41  ?  110 PRO A CG  1 
ATOM   823   C  CD  . PRO A  1  110 ? 121.111 -39.236 52.651  1.00 52.82  ?  110 PRO A CD  1 
ATOM   824   N  N   . CYS A  1  111 ? 123.121 -36.867 50.931  1.00 60.51  ?  111 CYS A N   1 
ATOM   825   C  CA  . CYS A  1  111 ? 123.892 -35.670 50.613  1.00 56.24  ?  111 CYS A CA  1 
ATOM   826   C  C   . CYS A  1  111 ? 125.277 -35.942 50.038  1.00 50.31  ?  111 CYS A C   1 
ATOM   827   O  O   . CYS A  1  111 ? 125.943 -36.897 50.422  1.00 65.30  ?  111 CYS A O   1 
ATOM   828   C  CB  . CYS A  1  111 ? 123.945 -34.740 51.818  1.00 63.18  ?  111 CYS A CB  1 
ATOM   829   S  SG  . CYS A  1  111 ? 122.314 -34.177 52.372  1.00 71.88  ?  111 CYS A SG  1 
ATOM   830   N  N   . VAL A  1  112 ? 125.693 -35.095 49.097  1.00 62.74  ?  112 VAL A N   1 
ATOM   831   C  CA  . VAL A  1  112 ? 126.960 -35.227 48.389  1.00 58.09  ?  112 VAL A CA  1 
ATOM   832   C  C   . VAL A  1  112 ? 128.029 -34.267 48.906  1.00 55.93  ?  112 VAL A C   1 
ATOM   833   O  O   . VAL A  1  112 ? 129.185 -34.656 49.067  1.00 64.38  ?  112 VAL A O   1 
ATOM   834   C  CB  . VAL A  1  112 ? 126.701 -34.998 46.877  1.00 56.60  ?  112 VAL A CB  1 
ATOM   835   C  CG1 . VAL A  1  112 ? 128.000 -35.044 46.078  1.00 68.95  ?  112 VAL A CG1 1 
ATOM   836   C  CG2 . VAL A  1  112 ? 125.698 -36.013 46.342  1.00 55.84  ?  112 VAL A CG2 1 
ATOM   837   N  N   . GLY A  1  113 ? 127.650 -33.019 49.129  1.00 55.39  ?  113 GLY A N   1 
ATOM   838   C  CA  . GLY A  1  113 ? 128.593 -32.011 49.583  1.00 58.33  ?  113 GLY A CA  1 
ATOM   839   C  C   . GLY A  1  113 ? 129.358 -31.449 48.405  1.00 65.40  ?  113 GLY A C   1 
ATOM   840   O  O   . GLY A  1  113 ? 128.756 -31.084 47.392  1.00 66.74  ?  113 GLY A O   1 
ATOM   841   N  N   . PHE A  1  114 ? 130.689 -31.385 48.512  1.00 66.67  ?  114 PHE A N   1 
ATOM   842   C  CA  . PHE A  1  114 ? 131.514 -30.844 47.439  1.00 57.33  ?  114 PHE A CA  1 
ATOM   843   C  C   . PHE A  1  114 ? 131.414 -31.685 46.170  1.00 65.23  ?  114 PHE A C   1 
ATOM   844   O  O   . PHE A  1  114 ? 131.375 -32.913 46.242  1.00 72.80  ?  114 PHE A O   1 
ATOM   845   C  CB  . PHE A  1  114 ? 132.977 -30.738 47.890  1.00 61.53  ?  114 PHE A CB  1 
ATOM   846   C  CG  . PHE A  1  114 ? 133.862 -30.047 46.884  1.00 63.09  ?  114 PHE A CG  1 
ATOM   847   C  CD1 . PHE A  1  114 ? 133.845 -28.671 46.754  1.00 66.70  ?  114 PHE A CD1 1 
ATOM   848   C  CD2 . PHE A  1  114 ? 134.685 -30.774 46.045  1.00 58.53  ?  114 PHE A CD2 1 
ATOM   849   C  CE1 . PHE A  1  114 ? 134.657 -28.035 45.826  1.00 62.84  ?  114 PHE A CE1 1 
ATOM   850   C  CE2 . PHE A  1  114 ? 135.493 -30.136 45.117  1.00 60.16  ?  114 PHE A CE2 1 
ATOM   851   C  CZ  . PHE A  1  114 ? 135.474 -28.772 45.013  1.00 54.89  ?  114 PHE A CZ  1 
ATOM   852   N  N   . ILE A  1  115 ? 131.372 -31.014 45.007  1.00 69.22  ?  115 ILE A N   1 
ATOM   853   C  CA  . ILE A  1  115 ? 131.297 -31.675 43.704  1.00 69.37  ?  115 ILE A CA  1 
ATOM   854   C  C   . ILE A  1  115 ? 132.694 -31.631 43.078  1.00 66.44  ?  115 ILE A C   1 
ATOM   855   O  O   . ILE A  1  115 ? 133.202 -30.548 42.812  1.00 65.99  ?  115 ILE A O   1 
ATOM   856   C  CB  . ILE A  1  115 ? 130.253 -30.983 42.797  1.00 59.56  ?  115 ILE A CB  1 
ATOM   857   C  CG1 . ILE A  1  115 ? 128.871 -30.862 43.481  1.00 51.90  ?  115 ILE A CG1 1 
ATOM   858   C  CG2 . ILE A  1  115 ? 130.149 -31.716 41.476  1.00 52.83  ?  115 ILE A CG2 1 
ATOM   859   C  CD1 . ILE A  1  115 ? 128.149 -32.184 43.806  1.00 58.55  ?  115 ILE A CD1 1 
ATOM   860   N  N   . SER A  1  116 ? 133.315 -32.794 42.853  1.00 70.72  ?  116 SER A N   1 
ATOM   861   C  CA  . SER A  1  116 ? 134.667 -32.869 42.295  1.00 66.73  ?  116 SER A CA  1 
ATOM   862   C  C   . SER A  1  116 ? 134.750 -32.403 40.840  1.00 66.10  ?  116 SER A C   1 
ATOM   863   O  O   . SER A  1  116 ? 133.759 -32.471 40.114  1.00 71.62  ?  116 SER A O   1 
ATOM   864   C  CB  . SER A  1  116 ? 135.205 -34.288 42.423  1.00 87.19  ?  116 SER A CB  1 
ATOM   865   O  OG  . SER A  1  116 ? 135.120 -34.748 43.764  1.00 98.50  ?  116 SER A OG  1 
ATOM   866   N  N   . ASP A  1  117 ? 135.945 -31.930 40.419  1.00 64.22  ?  117 ASP A N   1 
ATOM   867   C  CA  . ASP A  1  117 ? 136.176 -31.430 39.056  1.00 65.67  ?  117 ASP A CA  1 
ATOM   868   C  C   . ASP A  1  117 ? 135.736 -32.414 37.954  1.00 62.99  ?  117 ASP A C   1 
ATOM   869   O  O   . ASP A  1  117 ? 135.100 -31.977 36.999  1.00 61.95  ?  117 ASP A O   1 
ATOM   870   C  CB  . ASP A  1  117 ? 137.645 -31.021 38.849  1.00 66.22  ?  117 ASP A CB  1 
ATOM   871   C  CG  . ASP A  1  117 ? 137.991 -29.663 39.423  1.00 69.13  ?  117 ASP A CG  1 
ATOM   872   O  OD1 . ASP A  1  117 ? 137.267 -29.199 40.328  1.00 63.86  ?  117 ASP A OD1 1 
ATOM   873   O  OD2 . ASP A  1  117 ? 138.987 -29.065 38.968  1.00 75.87  ?  117 ASP A OD2 1 
ATOM   874   N  N   . PRO A  1  118 ? 136.023 -33.732 38.036  1.00 56.65  ?  118 PRO A N   1 
ATOM   875   C  CA  . PRO A  1  118 ? 135.559 -34.640 36.975  1.00 58.74  ?  118 PRO A CA  1 
ATOM   876   C  C   . PRO A  1  118 ? 134.055 -34.548 36.730  1.00 60.04  ?  118 PRO A C   1 
ATOM   877   O  O   . PRO A  1  118 ? 133.625 -34.667 35.586  1.00 75.27  ?  118 PRO A O   1 
ATOM   878   C  CB  . PRO A  1  118 ? 135.965 -36.021 37.491  1.00 60.30  ?  118 PRO A CB  1 
ATOM   879   C  CG  . PRO A  1  118 ? 137.104 -35.761 38.394  1.00 72.14  ?  118 PRO A CG  1 
ATOM   880   C  CD  . PRO A  1  118 ? 136.763 -34.474 39.072  1.00 68.78  ?  118 PRO A CD  1 
ATOM   881   N  N   . ILE A  1  119 ? 133.256 -34.318 37.784  1.00 55.36  ?  119 ILE A N   1 
ATOM   882   C  CA  . ILE A  1  119 ? 131.810 -34.183 37.611  1.00 52.60  ?  119 ILE A CA  1 
ATOM   883   C  C   . ILE A  1  119 ? 131.524 -32.889 36.841  1.00 57.56  ?  119 ILE A C   1 
ATOM   884   O  O   . ILE A  1  119 ? 130.679 -32.891 35.954  1.00 67.74  ?  119 ILE A O   1 
ATOM   885   C  CB  . ILE A  1  119 ? 131.066 -34.237 38.967  1.00 55.20  ?  119 ILE A CB  1 
ATOM   886   C  CG1 . ILE A  1  119 ? 131.091 -35.668 39.535  1.00 50.77  ?  119 ILE A CG1 1 
ATOM   887   C  CG2 . ILE A  1  119 ? 129.627 -33.726 38.818  1.00 43.96  ?  119 ILE A CG2 1 
ATOM   888   C  CD1 . ILE A  1  119 ? 130.856 -35.759 41.035  1.00 86.16  ?  119 ILE A CD1 1 
ATOM   889   N  N   . ILE A  1  120 ? 132.249 -31.802 37.152  1.00 54.94  ?  120 ILE A N   1 
ATOM   890   C  CA  . ILE A  1  120 ? 132.091 -30.509 36.471  1.00 54.27  ?  120 ILE A CA  1 
ATOM   891   C  C   . ILE A  1  120 ? 132.391 -30.686 34.979  1.00 59.86  ?  120 ILE A C   1 
ATOM   892   O  O   . ILE A  1  120 ? 131.723 -30.089 34.140  1.00 45.63  ?  120 ILE A O   1 
ATOM   893   C  CB  . ILE A  1  120 ? 133.038 -29.432 37.070  1.00 55.60  ?  120 ILE A CB  1 
ATOM   894   C  CG1 . ILE A  1  120 ? 132.928 -29.317 38.615  1.00 63.48  ?  120 ILE A CG1 1 
ATOM   895   C  CG2 . ILE A  1  120 ? 132.822 -28.078 36.390  1.00 42.73  ?  120 ILE A CG2 1 
ATOM   896   C  CD1 . ILE A  1  120 ? 131.585 -29.129 39.160  1.00 59.43  ?  120 ILE A CD1 1 
ATOM   897   N  N   . ARG A  1  121 ? 133.401 -31.506 34.652  1.00 59.14  ?  121 ARG A N   1 
ATOM   898   C  CA  . ARG A  1  121 ? 133.770 -31.767 33.266  1.00 53.94  ?  121 ARG A CA  1 
ATOM   899   C  C   . ARG A  1  121 ? 132.651 -32.569 32.608  1.00 64.49  ?  121 ARG A C   1 
ATOM   900   O  O   . ARG A  1  121 ? 132.209 -32.229 31.512  1.00 76.96  ?  121 ARG A O   1 
ATOM   901   C  CB  . ARG A  1  121 ? 135.095 -32.543 33.193  1.00 52.98  ?  121 ARG A CB  1 
ATOM   902   C  CG  . ARG A  1  121 ? 136.251 -31.866 33.932  1.00 68.20  ?  121 ARG A CG  1 
ATOM   903   C  CD  . ARG A  1  121 ? 137.616 -32.363 33.473  1.00 76.26  ?  121 ARG A CD  1 
ATOM   904   N  NE  . ARG A  1  121 ? 138.292 -31.387 32.617  1.00 71.95  ?  121 ARG A NE  1 
ATOM   905   C  CZ  . ARG A  1  121 ? 139.011 -30.359 33.057  1.00 84.23  ?  121 ARG A CZ  1 
ATOM   906   N  NH1 . ARG A  1  121 ? 139.163 -30.151 34.362  1.00 83.13  ?  121 ARG A NH1 1 
ATOM   907   N  NH2 . ARG A  1  121 ? 139.585 -29.528 32.196  1.00 90.78  ?  121 ARG A NH2 1 
ATOM   908   N  N   . SER A  1  122 ? 132.182 -33.619 33.294  1.00 67.09  ?  122 SER A N   1 
ATOM   909   C  CA  . SER A  1  122 ? 131.112 -34.488 32.811  1.00 60.48  ?  122 SER A CA  1 
ATOM   910   C  C   . SER A  1  122 ? 129.810 -33.733 32.538  1.00 62.55  ?  122 SER A C   1 
ATOM   911   O  O   . SER A  1  122 ? 129.142 -34.028 31.550  1.00 74.98  ?  122 SER A O   1 
ATOM   912   C  CB  . SER A  1  122 ? 130.838 -35.595 33.823  1.00 60.56  ?  122 SER A CB  1 
ATOM   913   O  OG  . SER A  1  122 ? 129.672 -36.322 33.478  1.00 77.18  ?  122 SER A OG  1 
ATOM   914   N  N   . LEU A  1  123 ? 129.433 -32.791 33.415  1.00 60.53  ?  123 LEU A N   1 
ATOM   915   C  CA  . LEU A  1  123 ? 128.194 -32.025 33.267  1.00 66.29  ?  123 LEU A CA  1 
ATOM   916   C  C   . LEU A  1  123 ? 128.365 -30.743 32.472  1.00 67.68  ?  123 LEU A C   1 
ATOM   917   O  O   . LEU A  1  123 ? 127.379 -30.219 31.965  1.00 75.78  ?  123 LEU A O   1 
ATOM   918   C  CB  . LEU A  1  123 ? 127.621 -31.651 34.642  1.00 51.29  ?  123 LEU A CB  1 
ATOM   919   C  CG  . LEU A  1  123 ? 127.228 -32.798 35.566  1.00 75.63  ?  123 LEU A CG  1 
ATOM   920   C  CD1 . LEU A  1  123 ? 126.917 -32.277 36.967  1.00 63.81  ?  123 LEU A CD1 1 
ATOM   921   C  CD2 . LEU A  1  123 ? 126.042 -33.582 35.011  1.00 87.80  ?  123 LEU A CD2 1 
ATOM   922   N  N   . GLY A  1  124 ? 129.579 -30.224 32.392  1.00 64.09  ?  124 GLY A N   1 
ATOM   923   C  CA  . GLY A  1  124 ? 129.836 -28.983 31.678  1.00 60.37  ?  124 GLY A CA  1 
ATOM   924   C  C   . GLY A  1  124 ? 129.580 -29.054 30.190  1.00 60.70  ?  124 GLY A C   1 
ATOM   925   O  O   . GLY A  1  124 ? 129.031 -28.112 29.615  1.00 61.97  ?  124 GLY A O   1 
ATOM   926   N  N   . VAL A  1  125 ? 129.958 -30.165 29.551  1.00 52.86  ?  125 VAL A N   1 
ATOM   927   C  CA  . VAL A  1  125 ? 129.757 -30.301 28.112  1.00 58.28  ?  125 VAL A CA  1 
ATOM   928   C  C   . VAL A  1  125 ? 128.251 -30.320 27.779  1.00 67.92  ?  125 VAL A C   1 
ATOM   929   O  O   . VAL A  1  125 ? 127.812 -29.496 26.977  1.00 66.57  ?  125 VAL A O   1 
ATOM   930   C  CB  . VAL A  1  125 ? 130.514 -31.508 27.517  1.00 59.00  ?  125 VAL A CB  1 
ATOM   931   C  CG1 . VAL A  1  125 ? 130.331 -31.557 26.005  1.00 54.04  ?  125 VAL A CG1 1 
ATOM   932   C  CG2 . VAL A  1  125 ? 131.996 -31.439 27.873  1.00 60.99  ?  125 VAL A CG2 1 
ATOM   933   N  N   . PRO A  1  126 ? 127.422 -31.199 28.391  1.00 69.16  ?  126 PRO A N   1 
ATOM   934   C  CA  . PRO A  1  126 ? 125.982 -31.166 28.082  1.00 62.59  ?  126 PRO A CA  1 
ATOM   935   C  C   . PRO A  1  126 ? 125.348 -29.814 28.409  1.00 63.00  ?  126 PRO A C   1 
ATOM   936   O  O   . PRO A  1  126 ? 124.368 -29.436 27.769  1.00 70.27  ?  126 PRO A O   1 
ATOM   937   C  CB  . PRO A  1  126 ? 125.398 -32.301 28.924  1.00 53.33  ?  126 PRO A CB  1 
ATOM   938   C  CG  . PRO A  1  126 ? 126.401 -32.579 29.958  1.00 64.87  ?  126 PRO A CG  1 
ATOM   939   C  CD  . PRO A  1  126 ? 127.731 -32.248 29.378  1.00 69.02  ?  126 PRO A CD  1 
ATOM   940   N  N   . LEU A  1  127 ? 125.907 -29.073 29.383  1.00 52.55  ?  127 LEU A N   1 
ATOM   941   C  CA  . LEU A  1  127 ? 125.395 -27.748 29.718  1.00 60.67  ?  127 LEU A CA  1 
ATOM   942   C  C   . LEU A  1  127 ? 125.650 -26.821 28.537  1.00 59.76  ?  127 LEU A C   1 
ATOM   943   O  O   . LEU A  1  127 ? 124.748 -26.091 28.132  1.00 75.38  ?  127 LEU A O   1 
ATOM   944   C  CB  . LEU A  1  127 ? 126.085 -27.165 30.967  1.00 45.35  ?  127 LEU A CB  1 
ATOM   945   C  CG  . LEU A  1  127 ? 125.469 -27.519 32.319  1.00 55.32  ?  127 LEU A CG  1 
ATOM   946   C  CD1 . LEU A  1  127 ? 126.443 -27.231 33.444  1.00 42.07  ?  127 LEU A CD1 1 
ATOM   947   C  CD2 . LEU A  1  127 ? 124.180 -26.751 32.558  1.00 67.15  ?  127 LEU A CD2 1 
ATOM   948   N  N   . VAL A  1  128 ? 126.871 -26.871 27.972  1.00 56.19  ?  128 VAL A N   1 
ATOM   949   C  CA  . VAL A  1  128 ? 127.254 -26.040 26.832  1.00 58.37  ?  128 VAL A CA  1 
ATOM   950   C  C   . VAL A  1  128 ? 126.433 -26.420 25.596  1.00 58.69  ?  128 VAL A C   1 
ATOM   951   O  O   . VAL A  1  128 ? 125.931 -25.536 24.907  1.00 72.48  ?  128 VAL A O   1 
ATOM   952   C  CB  . VAL A  1  128 ? 128.775 -26.127 26.553  1.00 61.15  ?  128 VAL A CB  1 
ATOM   953   C  CG1 . VAL A  1  128 ? 129.142 -25.367 25.281  1.00 57.41  ?  128 VAL A CG1 1 
ATOM   954   C  CG2 . VAL A  1  128 ? 129.577 -25.602 27.741  1.00 47.33  ?  128 VAL A CG2 1 
ATOM   955   N  N   . THR A  1  129 ? 126.270 -27.724 25.326  1.00 60.75  ?  129 THR A N   1 
ATOM   956   C  CA  . THR A  1  129 ? 125.487 -28.170 24.170  1.00 54.85  ?  129 THR A CA  1 
ATOM   957   C  C   . THR A  1  129 ? 123.980 -27.922 24.340  1.00 58.26  ?  129 THR A C   1 
ATOM   958   O  O   . THR A  1  129 ? 123.230 -28.099 23.385  1.00 74.94  ?  129 THR A O   1 
ATOM   959   C  CB  . THR A  1  129 ? 125.724 -29.659 23.880  1.00 62.64  ?  129 THR A CB  1 
ATOM   960   O  OG1 . THR A  1  129 ? 125.183 -30.438 24.945  1.00 73.80  ?  129 THR A OG1 1 
ATOM   961   C  CG2 . THR A  1  129 ? 127.194 -29.991 23.664  1.00 59.85  ?  129 THR A CG2 1 
ATOM   962   N  N   . GLY A  1  130 ? 123.543 -27.544 25.534  1.00 54.09  ?  130 GLY A N   1 
ATOM   963   C  CA  . GLY A  1  130 ? 122.133 -27.291 25.790  1.00 63.05  ?  130 GLY A CA  1 
ATOM   964   C  C   . GLY A  1  130 ? 121.336 -28.528 26.154  1.00 66.91  ?  130 GLY A C   1 
ATOM   965   O  O   . GLY A  1  130 ? 120.132 -28.426 26.391  1.00 65.86  ?  130 GLY A O   1 
ATOM   966   N  N   . ASP A  1  131 ? 121.983 -29.709 26.202  1.00 58.09  ?  131 ASP A N   1 
ATOM   967   C  CA  . ASP A  1  131 ? 121.287 -30.950 26.560  1.00 61.91  ?  131 ASP A CA  1 
ATOM   968   C  C   . ASP A  1  131 ? 120.742 -30.869 28.001  1.00 62.03  ?  131 ASP A C   1 
ATOM   969   O  O   . ASP A  1  131 ? 119.746 -31.524 28.319  1.00 68.63  ?  131 ASP A O   1 
ATOM   970   C  CB  . ASP A  1  131 ? 122.190 -32.171 26.328  1.00 66.01  ?  131 ASP A CB  1 
ATOM   971   C  CG  . ASP A  1  131 ? 122.545 -32.368 24.860  1.00 91.30  ?  131 ASP A CG  1 
ATOM   972   O  OD1 . ASP A  1  131 ? 121.669 -32.126 23.997  1.00 98.33  ?  131 ASP A OD1 1 
ATOM   973   O  OD2 . ASP A  1  131 ? 123.702 -32.754 24.574  1.00 99.34  ?  131 ASP A OD2 1 
ATOM   974   N  N   . ILE A  1  132 ? 121.385 -30.048 28.856  1.00 55.33  ?  132 ILE A N   1 
ATOM   975   C  CA  . ILE A  1  132 ? 120.939 -29.748 30.212  1.00 63.68  ?  132 ILE A CA  1 
ATOM   976   C  C   . ILE A  1  132 ? 120.460 -28.298 30.036  1.00 68.16  ?  132 ILE A C   1 
ATOM   977   O  O   . ILE A  1  132 ? 121.290 -27.387 29.970  1.00 62.12  ?  132 ILE A O   1 
ATOM   978   C  CB  . ILE A  1  132 ? 122.054 -29.874 31.279  1.00 56.15  ?  132 ILE A CB  1 
ATOM   979   C  CG1 . ILE A  1  132 ? 122.405 -31.352 31.513  1.00 58.11  ?  132 ILE A CG1 1 
ATOM   980   C  CG2 . ILE A  1  132 ? 121.593 -29.231 32.593  1.00 61.76  ?  132 ILE A CG2 1 
ATOM   981   C  CD1 . ILE A  1  132 ? 123.680 -31.576 32.267  1.00 53.23  ?  132 ILE A CD1 1 
ATOM   982   N  N   . PRO A  1  133 ? 119.148 -28.061 29.851  1.00 57.63  ?  133 PRO A N   1 
ATOM   983   C  CA  . PRO A  1  133 ? 118.686 -26.685 29.611  1.00 42.77  ?  133 PRO A CA  1 
ATOM   984   C  C   . PRO A  1  133 ? 118.840 -25.710 30.767  1.00 54.29  ?  133 PRO A C   1 
ATOM   985   O  O   . PRO A  1  133 ? 118.970 -24.512 30.526  1.00 63.82  ?  133 PRO A O   1 
ATOM   986   C  CB  . PRO A  1  133 ? 117.205 -26.852 29.253  1.00 46.72  ?  133 PRO A CB  1 
ATOM   987   C  CG  . PRO A  1  133 ? 116.975 -28.300 29.089  1.00 62.30  ?  133 PRO A CG  1 
ATOM   988   C  CD  . PRO A  1  133 ? 118.026 -29.016 29.843  1.00 57.15  ?  133 PRO A CD  1 
ATOM   989   N  N   . GLY A  1  134 ? 118.798 -26.204 31.996  1.00 48.74  ?  134 GLY A N   1 
ATOM   990   C  CA  . GLY A  1  134 ? 118.902 -25.340 33.161  1.00 51.88  ?  134 GLY A CA  1 
ATOM   991   C  C   . GLY A  1  134 ? 119.333 -26.054 34.415  1.00 50.76  ?  134 GLY A C   1 
ATOM   992   O  O   . GLY A  1  134 ? 119.319 -27.285 34.468  1.00 54.37  ?  134 GLY A O   1 
ATOM   993   N  N   . VAL A  1  135 ? 119.721 -25.273 35.432  1.00 37.10  ?  135 VAL A N   1 
ATOM   994   C  CA  . VAL A  1  135 ? 120.144 -25.803 36.720  1.00 46.45  ?  135 VAL A CA  1 
ATOM   995   C  C   . VAL A  1  135 ? 119.210 -25.235 37.780  1.00 53.81  ?  135 VAL A C   1 
ATOM   996   O  O   . VAL A  1  135 ? 119.323 -24.070 38.155  1.00 58.76  ?  135 VAL A O   1 
ATOM   997   C  CB  . VAL A  1  135 ? 121.628 -25.503 37.039  1.00 46.71  ?  135 VAL A CB  1 
ATOM   998   C  CG1 . VAL A  1  135 ? 122.031 -26.131 38.370  1.00 47.66  ?  135 VAL A CG1 1 
ATOM   999   C  CG2 . VAL A  1  135 ? 122.540 -26.000 35.922  1.00 46.29  ?  135 VAL A CG2 1 
ATOM   1000  N  N   . ALA A  1  136 ? 118.273 -26.064 38.250  1.00 56.63  ?  136 ALA A N   1 
ATOM   1001  C  CA  . ALA A  1  136 ? 117.301 -25.672 39.262  1.00 45.70  ?  136 ALA A CA  1 
ATOM   1002  C  C   . ALA A  1  136 ? 117.867 -25.864 40.665  1.00 46.57  ?  136 ALA A C   1 
ATOM   1003  O  O   . ALA A  1  136 ? 118.003 -26.999 41.114  1.00 64.68  ?  136 ALA A O   1 
ATOM   1004  C  CB  . ALA A  1  136 ? 116.039 -26.507 39.101  1.00 54.39  ?  136 ALA A CB  1 
ATOM   1005  N  N   . VAL A  1  137 ? 118.186 -24.774 41.366  1.00 43.92  ?  137 VAL A N   1 
ATOM   1006  C  CA  . VAL A  1  137 ? 118.707 -24.874 42.727  1.00 47.79  ?  137 VAL A CA  1 
ATOM   1007  C  C   . VAL A  1  137 ? 117.515 -24.757 43.670  1.00 50.34  ?  137 VAL A C   1 
ATOM   1008  O  O   . VAL A  1  137 ? 117.103 -23.645 43.990  1.00 58.84  ?  137 VAL A O   1 
ATOM   1009  C  CB  . VAL A  1  137 ? 119.773 -23.792 43.013  1.00 46.34  ?  137 VAL A CB  1 
ATOM   1010  C  CG1 . VAL A  1  137 ? 120.287 -23.895 44.447  1.00 30.90  ?  137 VAL A CG1 1 
ATOM   1011  C  CG2 . VAL A  1  137 ? 120.924 -23.888 42.019  1.00 40.99  ?  137 VAL A CG2 1 
ATOM   1012  N  N   . ILE A  1  138 ? 116.917 -25.898 44.030  1.00 44.06  ?  138 ILE A N   1 
ATOM   1013  C  CA  . ILE A  1  138 ? 115.730 -25.895 44.937  1.00 43.99  ?  138 ILE A CA  1 
ATOM   1014  C  C   . ILE A  1  138 ? 116.246 -25.766 46.373  1.00 50.92  ?  138 ILE A C   1 
ATOM   1015  O  O   . ILE A  1  138 ? 117.121 -26.562 46.749  1.00 50.43  ?  138 ILE A O   1 
ATOM   1016  C  CB  . ILE A  1  138 ? 114.845 -27.137 44.703  1.00 49.49  ?  138 ILE A CB  1 
ATOM   1017  C  CG1 . ILE A  1  138 ? 114.203 -27.121 43.311  1.00 36.65  ?  138 ILE A CG1 1 
ATOM   1018  C  CG2 . ILE A  1  138 ? 113.805 -27.272 45.804  1.00 52.36  ?  138 ILE A CG2 1 
ATOM   1019  C  CD1 . ILE A  1  138 ? 113.530 -28.422 42.897  1.00 59.27  ?  138 ILE A CD1 1 
ATOM   1020  N  N   . LEU A  1  139 ? 115.726 -24.811 47.150  1.00 48.24  ?  139 LEU A N   1 
ATOM   1021  C  CA  . LEU A  1  139 ? 116.264 -24.582 48.520  1.00 52.69  ?  139 LEU A CA  1 
ATOM   1022  C  C   . LEU A  1  139 ? 115.118 -24.324 49.504  1.00 54.93  ?  139 LEU A C   1 
ATOM   1023  O  O   . LEU A  1  139 ? 114.223 -23.530 49.165  1.00 61.82  ?  139 LEU A O   1 
ATOM   1024  C  CB  . LEU A  1  139 ? 117.229 -23.391 48.472  1.00 47.61  ?  139 LEU A CB  1 
ATOM   1025  C  CG  . LEU A  1  139 ? 117.582 -22.754 49.816  1.00 54.69  ?  139 LEU A CG  1 
ATOM   1026  C  CD1 . LEU A  1  139 ? 119.045 -22.330 49.850  1.00 50.55  ?  139 LEU A CD1 1 
ATOM   1027  C  CD2 . LEU A  1  139 ? 116.683 -21.560 50.101  1.00 66.65  ?  139 LEU A CD2 1 
ATOM   1028  N  N   . GLY A  1  140 ? 115.146 -24.973 50.674  1.00 51.92  ?  140 GLY A N   1 
ATOM   1029  C  CA  . GLY A  1  140 ? 114.126 -24.709 51.707  1.00 60.30  ?  140 GLY A CA  1 
ATOM   1030  C  C   . GLY A  1  140 ? 113.178 -25.872 51.930  1.00 66.81  ?  140 GLY A C   1 
ATOM   1031  O  O   . GLY A  1  140 ? 113.613 -27.028 51.765  1.00 60.82  ?  140 GLY A O   1 
ATOM   1032  N  N   . GLU A  1  141 ? 111.930 -25.577 52.302  1.00 59.75  ?  141 GLU A N   1 
ATOM   1033  C  CA  . GLU A  1  141 ? 110.936 -26.610 52.574  1.00 57.74  ?  141 GLU A CA  1 
ATOM   1034  C  C   . GLU A  1  141 ? 109.621 -26.304 51.856  1.00 62.68  ?  141 GLU A C   1 
ATOM   1035  O  O   . GLU A  1  141 ? 109.170 -25.163 51.838  1.00 69.68  ?  141 GLU A O   1 
ATOM   1036  C  CB  . GLU A  1  141 ? 110.689 -26.699 54.089  1.00 62.68  ?  141 GLU A CB  1 
ATOM   1037  C  CG  . GLU A  1  141 ? 109.965 -27.956 54.534  1.00 69.91  ?  141 GLU A CG  1 
ATOM   1038  C  CD  . GLU A  1  141 ? 109.872 -28.093 56.040  1.00 94.06  ?  141 GLU A CD  1 
ATOM   1039  O  OE1 . GLU A  1  141 ? 109.784 -27.048 56.723  1.00 97.98  ?  141 GLU A OE1 1 
ATOM   1040  O  OE2 . GLU A  1  141 ? 109.890 -29.241 56.540  1.00 87.77  ?  141 GLU A OE2 1 
ATOM   1041  N  N   . CYS A  1  142 ? 108.995 -27.331 51.286  1.00 60.86  ?  142 CYS A N   1 
ATOM   1042  C  CA  . CYS A  1  142 ? 107.723 -27.201 50.573  1.00 63.48  ?  142 CYS A CA  1 
ATOM   1043  C  C   . CYS A  1  142 ? 106.562 -27.425 51.552  1.00 65.44  ?  142 CYS A C   1 
ATOM   1044  O  O   . CYS A  1  142 ? 106.785 -27.984 52.629  1.00 64.43  ?  142 CYS A O   1 
ATOM   1045  C  CB  . CYS A  1  142 ? 107.678 -28.212 49.428  1.00 58.02  ?  142 CYS A CB  1 
ATOM   1046  S  SG  . CYS A  1  142 ? 108.597 -27.709 47.952  1.00 63.09  ?  142 CYS A SG  1 
ATOM   1047  N  N   . PRO A  1  143 ? 105.308 -27.034 51.217  1.00 71.07  ?  143 PRO A N   1 
ATOM   1048  C  CA  . PRO A  1  143 ? 104.204 -27.281 52.160  1.00 64.69  ?  143 PRO A CA  1 
ATOM   1049  C  C   . PRO A  1  143 ? 104.029 -28.770 52.482  1.00 66.23  ?  143 PRO A C   1 
ATOM   1050  O  O   . PRO A  1  143 ? 103.710 -29.128 53.616  1.00 71.87  ?  143 PRO A O   1 
ATOM   1051  C  CB  . PRO A  1  143 ? 102.980 -26.700 51.442  1.00 52.53  ?  143 PRO A CB  1 
ATOM   1052  C  CG  . PRO A  1  143 ? 103.358 -26.629 50.010  1.00 62.02  ?  143 PRO A CG  1 
ATOM   1053  C  CD  . PRO A  1  143 ? 104.825 -26.359 49.995  1.00 59.30  ?  143 PRO A CD  1 
ATOM   1054  N  N   . ASP A  1  144 ? 104.258 -29.636 51.484  1.00 66.26  ?  144 ASP A N   1 
ATOM   1055  C  CA  . ASP A  1  144 ? 104.147 -31.083 51.640  1.00 63.24  ?  144 ASP A CA  1 
ATOM   1056  C  C   . ASP A  1  144 ? 105.054 -31.804 50.632  1.00 65.49  ?  144 ASP A C   1 
ATOM   1057  O  O   . ASP A  1  144 ? 105.468 -31.214 49.634  1.00 63.83  ?  144 ASP A O   1 
ATOM   1058  C  CB  . ASP A  1  144 ? 102.681 -31.532 51.477  1.00 77.90  ?  144 ASP A CB  1 
ATOM   1059  C  CG  . ASP A  1  144 ? 101.949 -30.935 50.287  1.00 88.15  ?  144 ASP A CG  1 
ATOM   1060  O  OD1 . ASP A  1  144 ? 102.545 -30.875 49.192  1.00 80.93  ?  144 ASP A OD1 1 
ATOM   1061  O  OD2 . ASP A  1  144 ? 100.771 -30.541 50.451  1.00 97.69  ?  144 ASP A OD2 1 
ATOM   1062  N  N   . SER A  1  145 ? 105.369 -33.076 50.893  1.00 76.92  ?  145 SER A N   1 
ATOM   1063  C  CA  . SER A  1  145 ? 106.216 -33.852 49.990  1.00 70.92  ?  145 SER A CA  1 
ATOM   1064  C  C   . SER A  1  145 ? 105.584 -33.991 48.605  1.00 74.27  ?  145 SER A C   1 
ATOM   1065  O  O   . SER A  1  145 ? 106.304 -34.128 47.620  1.00 83.07  ?  145 SER A O   1 
ATOM   1066  C  CB  . SER A  1  145 ? 106.501 -35.233 50.574  1.00 74.67  ?  145 SER A CB  1 
ATOM   1067  O  OG  . SER A  1  145 ? 105.366 -36.077 50.475  1.00 87.26  ?  145 SER A OG  1 
ATOM   1068  N  N   . GLU A  1  146 ? 104.249 -33.956 48.527  1.00 80.05  ?  146 GLU A N   1 
ATOM   1069  C  CA  . GLU A  1  146 ? 103.540 -34.076 47.260  1.00 67.47  ?  146 GLU A CA  1 
ATOM   1070  C  C   . GLU A  1  146 ? 103.901 -32.923 46.324  1.00 72.58  ?  146 GLU A C   1 
ATOM   1071  O  O   . GLU A  1  146 ? 104.115 -33.166 45.140  1.00 85.99  ?  146 GLU A O   1 
ATOM   1072  C  CB  . GLU A  1  146 ? 102.020 -34.130 47.486  1.00 76.05  ?  146 GLU A CB  1 
ATOM   1073  C  CG  . GLU A  1  146 ? 101.528 -35.430 48.112  1.00 98.95  ?  146 GLU A CG  1 
ATOM   1074  C  CD  . GLU A  1  146 ? 101.584 -35.536 49.626  1.00 97.80  ?  146 GLU A CD  1 
ATOM   1075  O  OE1 . GLU A  1  146 ? 101.618 -34.485 50.306  1.00 92.79  ?  146 GLU A OE1 1 
ATOM   1076  O  OE2 . GLU A  1  146 ? 101.584 -36.680 50.136  1.00 98.09  ?  146 GLU A OE2 1 
ATOM   1077  N  N   . THR A  1  147 ? 103.988 -31.678 46.839  1.00 77.94  ?  147 THR A N   1 
ATOM   1078  C  CA  . THR A  1  147 ? 104.344 -30.525 45.995  1.00 78.25  ?  147 THR A CA  1 
ATOM   1079  C  C   . THR A  1  147 ? 105.839 -30.541 45.642  1.00 66.86  ?  147 THR A C   1 
ATOM   1080  O  O   . THR A  1  147 ? 106.204 -30.135 44.539  1.00 59.91  ?  147 THR A O   1 
ATOM   1081  C  CB  . THR A  1  147 ? 103.927 -29.180 46.643  1.00 65.70  ?  147 THR A CB  1 
ATOM   1082  O  OG1 . THR A  1  147 ? 104.388 -29.128 47.994  1.00 88.18  ?  147 THR A OG1 1 
ATOM   1083  C  CG2 . THR A  1  147 ? 102.417 -28.930 46.581  1.00 68.95  ?  147 THR A CG2 1 
ATOM   1084  N  N   . ALA A  1  148 ? 106.701 -31.016 46.559  1.00 65.28  ?  148 ALA A N   1 
ATOM   1085  C  CA  . ALA A  1  148 ? 108.138 -31.075 46.297  1.00 63.91  ?  148 ALA A CA  1 
ATOM   1086  C  C   . ALA A  1  148 ? 108.349 -32.061 45.149  1.00 65.33  ?  148 ALA A C   1 
ATOM   1087  O  O   . ALA A  1  148 ? 108.847 -31.666 44.094  1.00 62.16  ?  148 ALA A O   1 
ATOM   1088  C  CB  . ALA A  1  148 ? 108.897 -31.438 47.571  1.00 69.62  ?  148 ALA A CB  1 
ATOM   1089  N  N   . ALA A  1  149 ? 107.957 -33.332 45.333  1.00 54.80  ?  149 ALA A N   1 
ATOM   1090  C  CA  . ALA A  1  149 ? 108.111 -34.335 44.287  1.00 62.21  ?  149 ALA A CA  1 
ATOM   1091  C  C   . ALA A  1  149 ? 107.516 -33.902 42.960  1.00 65.18  ?  149 ALA A C   1 
ATOM   1092  O  O   . ALA A  1  149 ? 108.137 -34.102 41.922  1.00 66.36  ?  149 ALA A O   1 
ATOM   1093  C  CB  . ALA A  1  149 ? 107.499 -35.648 44.729  1.00 81.02  ?  149 ALA A CB  1 
ATOM   1094  N  N   . LYS A  1  150 ? 106.325 -33.287 42.990  1.00 61.73  ?  150 LYS A N   1 
ATOM   1095  C  CA  . LYS A  1  150 ? 105.655 -32.805 41.783  1.00 60.63  ?  150 LYS A CA  1 
ATOM   1096  C  C   . LYS A  1  150 ? 106.580 -31.862 40.995  1.00 59.55  ?  150 LYS A C   1 
ATOM   1097  O  O   . LYS A  1  150 ? 106.746 -32.037 39.789  1.00 60.71  ?  150 LYS A O   1 
ATOM   1098  C  CB  . LYS A  1  150 ? 104.333 -32.103 42.172  1.00 54.98  ?  150 LYS A CB  1 
ATOM   1099  C  CG  . LYS A  1  150 ? 103.700 -31.199 41.103  1.00 70.13  ?  150 LYS A CG  1 
ATOM   1100  C  CD  . LYS A  1  150 ? 102.982 -29.982 41.720  1.00 86.40  ?  150 LYS A CD  1 
ATOM   1101  C  CE  . LYS A  1  150 ? 101.811 -30.349 42.607  1.00 86.40  ?  150 LYS A CE  1 
ATOM   1102  N  NZ  . LYS A  1  150 ? 101.113 -29.142 43.131  1.00 89.04  ?  150 LYS A NZ  1 
ATOM   1103  N  N   . ILE A  1  151 ? 107.198 -30.890 41.687  1.00 57.60  ?  151 ILE A N   1 
ATOM   1104  C  CA  . ILE A  1  151 ? 108.096 -29.913 41.071  1.00 52.28  ?  151 ILE A CA  1 
ATOM   1105  C  C   . ILE A  1  151 ? 109.401 -30.568 40.610  1.00 58.42  ?  151 ILE A C   1 
ATOM   1106  O  O   . ILE A  1  151 ? 109.782 -30.413 39.448  1.00 60.36  ?  151 ILE A O   1 
ATOM   1107  C  CB  . ILE A  1  151 ? 108.369 -28.723 42.044  1.00 50.06  ?  151 ILE A CB  1 
ATOM   1108  C  CG1 . ILE A  1  151 ? 107.132 -27.816 42.157  1.00 47.05  ?  151 ILE A CG1 1 
ATOM   1109  C  CG2 . ILE A  1  151 ? 109.577 -27.903 41.591  1.00 46.20  ?  151 ILE A CG2 1 
ATOM   1110  C  CD1 . ILE A  1  151 ? 107.123 -26.920 43.377  1.00 54.16  ?  151 ILE A CD1 1 
ATOM   1111  N  N   . ILE A  1  152 ? 110.096 -31.293 41.507  1.00 57.84  ?  152 ILE A N   1 
ATOM   1112  C  CA  . ILE A  1  152 ? 111.372 -31.917 41.147  1.00 50.52  ?  152 ILE A CA  1 
ATOM   1113  C  C   . ILE A  1  152 ? 111.214 -32.853 39.944  1.00 52.38  ?  152 ILE A C   1 
ATOM   1114  O  O   . ILE A  1  152 ? 111.966 -32.742 38.976  1.00 56.04  ?  152 ILE A O   1 
ATOM   1115  C  CB  . ILE A  1  152 ? 112.029 -32.619 42.355  1.00 42.20  ?  152 ILE A CB  1 
ATOM   1116  C  CG1 . ILE A  1  152 ? 112.412 -31.593 43.436  1.00 40.80  ?  152 ILE A CG1 1 
ATOM   1117  C  CG2 . ILE A  1  152 ? 113.268 -33.383 41.904  1.00 50.29  ?  152 ILE A CG2 1 
ATOM   1118  C  CD1 . ILE A  1  152 ? 112.647 -32.180 44.793  1.00 54.01  ?  152 ILE A CD1 1 
ATOM   1119  N  N   . LYS A  1  153 ? 110.215 -33.740 39.978  1.00 52.11  ?  153 LYS A N   1 
ATOM   1120  C  CA  . LYS A  1  153 ? 109.982 -34.663 38.865  1.00 54.53  ?  153 LYS A CA  1 
ATOM   1121  C  C   . LYS A  1  153 ? 109.684 -33.907 37.566  1.00 65.75  ?  153 LYS A C   1 
ATOM   1122  O  O   . LYS A  1  153 ? 110.013 -34.400 36.490  1.00 79.04  ?  153 LYS A O   1 
ATOM   1123  C  CB  . LYS A  1  153 ? 108.845 -35.640 39.189  1.00 53.48  ?  153 LYS A CB  1 
ATOM   1124  C  CG  . LYS A  1  153 ? 109.195 -36.641 40.277  1.00 50.53  ?  153 LYS A CG  1 
ATOM   1125  C  CD  . LYS A  1  153 ? 108.016 -37.540 40.611  1.00 73.18  ?  153 LYS A CD  1 
ATOM   1126  C  CE  . LYS A  1  153 ? 108.336 -38.598 41.646  1.00 95.18  ?  153 LYS A CE  1 
ATOM   1127  N  NZ  . LYS A  1  153 ? 108.188 -39.978 41.103  1.00 100.40 ?  153 LYS A NZ  1 
ATOM   1128  N  N   . ASP A  1  154 ? 109.075 -32.719 37.661  1.00 64.53  ?  154 ASP A N   1 
ATOM   1129  C  CA  . ASP A  1  154 ? 108.762 -31.910 36.491  1.00 64.52  ?  154 ASP A CA  1 
ATOM   1130  C  C   . ASP A  1  154 ? 110.042 -31.300 35.927  1.00 63.96  ?  154 ASP A C   1 
ATOM   1131  O  O   . ASP A  1  154 ? 110.233 -31.321 34.712  1.00 65.19  ?  154 ASP A O   1 
ATOM   1132  C  CB  . ASP A  1  154 ? 107.761 -30.806 36.862  1.00 59.86  ?  154 ASP A CB  1 
ATOM   1133  C  CG  . ASP A  1  154 ? 107.138 -30.088 35.678  1.00 74.56  ?  154 ASP A CG  1 
ATOM   1134  O  OD1 . ASP A  1  154 ? 107.397 -30.503 34.521  1.00 78.19  ?  154 ASP A OD1 1 
ATOM   1135  O  OD2 . ASP A  1  154 ? 106.384 -29.117 35.905  1.00 83.30  ?  154 ASP A OD2 1 
ATOM   1136  N  N   . TYR A  1  155 ? 110.928 -30.772 36.794  1.00 57.98  ?  155 TYR A N   1 
ATOM   1137  C  CA  . TYR A  1  155 ? 112.189 -30.192 36.323  1.00 51.20  ?  155 TYR A CA  1 
ATOM   1138  C  C   . TYR A  1  155 ? 113.033 -31.284 35.675  1.00 66.63  ?  155 TYR A C   1 
ATOM   1139  O  O   . TYR A  1  155 ? 113.568 -31.075 34.585  1.00 66.35  ?  155 TYR A O   1 
ATOM   1140  C  CB  . TYR A  1  155 ? 112.986 -29.552 37.473  1.00 37.99  ?  155 TYR A CB  1 
ATOM   1141  C  CG  . TYR A  1  155 ? 112.548 -28.155 37.854  1.00 55.68  ?  155 TYR A CG  1 
ATOM   1142  C  CD1 . TYR A  1  155 ? 112.442 -27.152 36.900  1.00 50.68  ?  155 TYR A CD1 1 
ATOM   1143  C  CD2 . TYR A  1  155 ? 112.315 -27.817 39.178  1.00 58.98  ?  155 TYR A CD2 1 
ATOM   1144  C  CE1 . TYR A  1  155 ? 112.053 -25.864 37.246  1.00 45.28  ?  155 TYR A CE1 1 
ATOM   1145  C  CE2 . TYR A  1  155 ? 111.940 -26.529 39.539  1.00 62.70  ?  155 TYR A CE2 1 
ATOM   1146  C  CZ  . TYR A  1  155 ? 111.809 -25.554 38.570  1.00 57.40  ?  155 TYR A CZ  1 
ATOM   1147  O  OH  . TYR A  1  155 ? 111.436 -24.281 38.923  1.00 60.66  ?  155 TYR A OH  1 
ATOM   1148  N  N   . GLN A  1  156 ? 113.128 -32.460 36.333  1.00 65.16  ?  156 GLN A N   1 
ATOM   1149  C  CA  . GLN A  1  156 ? 113.901 -33.573 35.790  1.00 60.27  ?  156 GLN A CA  1 
ATOM   1150  C  C   . GLN A  1  156 ? 113.309 -34.057 34.459  1.00 52.31  ?  156 GLN A C   1 
ATOM   1151  O  O   . GLN A  1  156 ? 114.061 -34.519 33.607  1.00 66.19  ?  156 GLN A O   1 
ATOM   1152  C  CB  . GLN A  1  156 ? 114.073 -34.715 36.818  1.00 52.10  ?  156 GLN A CB  1 
ATOM   1153  C  CG  . GLN A  1  156 ? 113.171 -35.929 36.626  1.00 60.00  ?  156 GLN A CG  1 
ATOM   1154  C  CD  . GLN A  1  156 ? 113.396 -36.970 37.698  1.00 71.68  ?  156 GLN A CD  1 
ATOM   1155  O  OE1 . GLN A  1  156 ? 114.530 -37.249 38.104  1.00 55.53  ?  156 GLN A OE1 1 
ATOM   1156  N  NE2 . GLN A  1  156 ? 112.320 -37.580 38.182  1.00 84.50  ?  156 GLN A NE2 1 
ATOM   1157  N  N   . SER A  1  157 ? 111.980 -33.930 34.268  1.00 58.90  ?  157 SER A N   1 
ATOM   1158  C  CA  . SER A  1  157 ? 111.315 -34.331 33.021  1.00 67.99  ?  157 SER A CA  1 
ATOM   1159  C  C   . SER A  1  157 ? 111.775 -33.492 31.839  1.00 65.27  ?  157 SER A C   1 
ATOM   1160  O  O   . SER A  1  157 ? 111.729 -33.968 30.705  1.00 73.60  ?  157 SER A O   1 
ATOM   1161  C  CB  . SER A  1  157 ? 109.802 -34.191 33.137  1.00 64.01  ?  157 SER A CB  1 
ATOM   1162  O  OG  . SER A  1  157 ? 109.238 -35.210 33.945  1.00 104.69 ?  157 SER A OG  1 
ATOM   1163  N  N   . LYS A  1  158 ? 112.195 -32.244 32.088  1.00 60.66  ?  158 LYS A N   1 
ATOM   1164  C  CA  . LYS A  1  158 ? 112.665 -31.366 31.023  1.00 59.15  ?  158 LYS A CA  1 
ATOM   1165  C  C   . LYS A  1  158 ? 114.201 -31.423 30.841  1.00 67.83  ?  158 LYS A C   1 
ATOM   1166  O  O   . LYS A  1  158 ? 114.762 -30.587 30.134  1.00 69.27  ?  158 LYS A O   1 
ATOM   1167  C  CB  . LYS A  1  158 ? 112.192 -29.931 31.294  1.00 71.18  ?  158 LYS A CB  1 
ATOM   1168  C  CG  . LYS A  1  158 ? 110.672 -29.760 31.200  1.00 63.19  ?  158 LYS A CG  1 
ATOM   1169  C  CD  . LYS A  1  158 ? 110.071 -29.052 32.408  1.00 63.33  ?  158 LYS A CD  1 
ATOM   1170  C  CE  . LYS A  1  158 ? 108.684 -28.519 32.136  1.00 60.33  ?  158 LYS A CE  1 
ATOM   1171  N  NZ  . LYS A  1  158 ? 107.771 -29.555 31.583  1.00 62.76  ?  158 LYS A NZ  1 
ATOM   1172  N  N   . GLY A  1  159 ? 114.858 -32.409 31.455  1.00 63.14  ?  159 GLY A N   1 
ATOM   1173  C  CA  . GLY A  1  159 ? 116.301 -32.581 31.346  1.00 59.44  ?  159 GLY A CA  1 
ATOM   1174  C  C   . GLY A  1  159 ? 117.121 -31.585 32.141  1.00 60.83  ?  159 GLY A C   1 
ATOM   1175  O  O   . GLY A  1  159 ? 118.317 -31.429 31.886  1.00 70.44  ?  159 GLY A O   1 
ATOM   1176  N  N   . LEU A  1  160 ? 116.499 -30.905 33.113  1.00 61.08  ?  160 LEU A N   1 
ATOM   1177  C  CA  . LEU A  1  160 ? 117.213 -29.924 33.922  1.00 56.35  ?  160 LEU A CA  1 
ATOM   1178  C  C   . LEU A  1  160 ? 117.975 -30.622 35.030  1.00 66.79  ?  160 LEU A C   1 
ATOM   1179  O  O   . LEU A  1  160 ? 117.580 -31.709 35.473  1.00 65.65  ?  160 LEU A O   1 
ATOM   1180  C  CB  . LEU A  1  160 ? 116.233 -28.909 34.555  1.00 40.78  ?  160 LEU A CB  1 
ATOM   1181  C  CG  . LEU A  1  160 ? 115.992 -27.606 33.787  1.00 43.17  ?  160 LEU A CG  1 
ATOM   1182  C  CD1 . LEU A  1  160 ? 115.015 -27.812 32.650  1.00 50.94  ?  160 LEU A CD1 1 
ATOM   1183  C  CD2 . LEU A  1  160 ? 115.491 -26.514 34.708  1.00 36.24  ?  160 LEU A CD2 1 
ATOM   1184  N  N   . LEU A  1  161 ? 119.068 -29.989 35.488  1.00 57.26  ?  161 LEU A N   1 
ATOM   1185  C  CA  . LEU A  1  161 ? 119.862 -30.518 36.586  1.00 48.03  ?  161 LEU A CA  1 
ATOM   1186  C  C   . LEU A  1  161 ? 119.316 -29.887 37.856  1.00 53.33  ?  161 LEU A C   1 
ATOM   1187  O  O   . LEU A  1  161 ? 119.446 -28.685 38.051  1.00 62.66  ?  161 LEU A O   1 
ATOM   1188  C  CB  . LEU A  1  161 ? 121.358 -30.207 36.414  1.00 50.74  ?  161 LEU A CB  1 
ATOM   1189  C  CG  . LEU A  1  161 ? 122.253 -30.523 37.623  1.00 54.15  ?  161 LEU A CG  1 
ATOM   1190  C  CD1 . LEU A  1  161 ? 122.171 -31.990 38.010  1.00 50.27  ?  161 LEU A CD1 1 
ATOM   1191  C  CD2 . LEU A  1  161 ? 123.689 -30.128 37.356  1.00 38.57  ?  161 LEU A CD2 1 
ATOM   1192  N  N   . THR A  1  162 ? 118.681 -30.689 38.707  1.00 57.31  ?  162 THR A N   1 
ATOM   1193  C  CA  . THR A  1  162 ? 118.105 -30.197 39.950  1.00 52.85  ?  162 THR A CA  1 
ATOM   1194  C  C   . THR A  1  162 ? 119.087 -30.440 41.094  1.00 56.58  ?  162 THR A C   1 
ATOM   1195  O  O   . THR A  1  162 ? 119.633 -31.535 41.192  1.00 60.51  ?  162 THR A O   1 
ATOM   1196  C  CB  . THR A  1  162 ? 116.769 -30.914 40.225  1.00 55.54  ?  162 THR A CB  1 
ATOM   1197  O  OG1 . THR A  1  162 ? 116.024 -31.050 39.009  1.00 67.49  ?  162 THR A OG1 1 
ATOM   1198  C  CG2 . THR A  1  162 ? 115.933 -30.196 41.263  1.00 50.32  ?  162 THR A CG2 1 
ATOM   1199  N  N   . CYS A  1  163 ? 119.306 -29.431 41.954  1.00 51.05  ?  163 CYS A N   1 
ATOM   1200  C  CA  . CYS A  1  163 ? 120.199 -29.534 43.109  1.00 49.61  ?  163 CYS A CA  1 
ATOM   1201  C  C   . CYS A  1  163 ? 119.378 -29.187 44.330  1.00 43.39  ?  163 CYS A C   1 
ATOM   1202  O  O   . CYS A  1  163 ? 118.766 -28.127 44.364  1.00 57.11  ?  163 CYS A O   1 
ATOM   1203  C  CB  . CYS A  1  163 ? 121.397 -28.605 42.960  1.00 41.57  ?  163 CYS A CB  1 
ATOM   1204  S  SG  . CYS A  1  163 ? 122.479 -29.013 41.567  1.00 61.31  ?  163 CYS A SG  1 
ATOM   1205  N  N   . LEU A  1  164 ? 119.348 -30.066 45.324  1.00 41.05  ?  164 LEU A N   1 
ATOM   1206  C  CA  . LEU A  1  164 ? 118.531 -29.847 46.509  1.00 46.10  ?  164 LEU A CA  1 
ATOM   1207  C  C   . LEU A  1  164 ? 119.333 -29.522 47.764  1.00 58.40  ?  164 LEU A C   1 
ATOM   1208  O  O   . LEU A  1  164 ? 120.356 -30.149 48.032  1.00 58.26  ?  164 LEU A O   1 
ATOM   1209  C  CB  . LEU A  1  164 ? 117.665 -31.092 46.767  1.00 46.44  ?  164 LEU A CB  1 
ATOM   1210  C  CG  . LEU A  1  164 ? 116.948 -31.714 45.568  1.00 49.40  ?  164 LEU A CG  1 
ATOM   1211  C  CD1 . LEU A  1  164 ? 116.250 -32.989 45.966  1.00 55.50  ?  164 LEU A CD1 1 
ATOM   1212  C  CD2 . LEU A  1  164 ? 115.959 -30.751 44.945  1.00 47.27  ?  164 LEU A CD2 1 
ATOM   1213  N  N   . VAL A  1  165 ? 118.862 -28.506 48.499  1.00 47.46  ?  165 VAL A N   1 
ATOM   1214  C  CA  . VAL A  1  165 ? 119.480 -28.165 49.814  1.00 60.90  ?  165 VAL A CA  1 
ATOM   1215  C  C   . VAL A  1  165 ? 118.355 -27.907 50.817  1.00 61.06  ?  165 VAL A C   1 
ATOM   1216  O  O   . VAL A  1  165 ? 117.368 -27.251 50.439  1.00 67.10  ?  165 VAL A O   1 
ATOM   1217  C  CB  . VAL A  1  165 ? 120.444 -26.964 49.786  1.00 49.63  ?  165 VAL A CB  1 
ATOM   1218  C  CG1 . VAL A  1  165 ? 119.903 -25.822 48.943  1.00 56.00  ?  165 VAL A CG1 1 
ATOM   1219  C  CG2 . VAL A  1  165 ? 120.749 -26.496 51.210  1.00 60.18  ?  165 VAL A CG2 1 
ATOM   1220  N  N   . GLY A  1  166 ? 118.507 -28.406 52.038  1.00 54.49  ?  166 GLY A N   1 
ATOM   1221  C  CA  . GLY A  1  166 ? 117.543 -28.227 53.117  1.00 65.84  ?  166 GLY A CA  1 
ATOM   1222  C  C   . GLY A  1  166 ? 116.577 -29.375 53.315  1.00 65.55  ?  166 GLY A C   1 
ATOM   1223  O  O   . GLY A  1  166 ? 116.847 -30.506 52.908  1.00 67.45  ?  166 GLY A O   1 
ATOM   1224  N  N   . LYS A  1  167 ? 115.436 -29.085 53.956  1.00 65.59  ?  167 LYS A N   1 
ATOM   1225  C  CA  . LYS A  1  167 ? 114.412 -30.095 54.225  1.00 56.59  ?  167 LYS A CA  1 
ATOM   1226  C  C   . LYS A  1  167 ? 113.763 -30.628 52.945  1.00 66.24  ?  167 LYS A C   1 
ATOM   1227  O  O   . LYS A  1  167 ? 113.142 -31.685 52.982  1.00 68.43  ?  167 LYS A O   1 
ATOM   1228  C  CB  . LYS A  1  167 ? 113.327 -29.537 55.157  1.00 69.02  ?  167 LYS A CB  1 
ATOM   1229  C  CG  . LYS A  1  167 ? 113.820 -29.185 56.563  1.00 77.71  ?  167 LYS A CG  1 
ATOM   1230  C  CD  . LYS A  1  167 ? 114.094 -30.415 57.436  1.00 67.00  ?  167 LYS A CD  1 
ATOM   1231  C  CE  . LYS A  1  167 ? 113.895 -30.125 58.905  1.00 85.16  ?  167 LYS A CE  1 
ATOM   1232  N  NZ  . LYS A  1  167 ? 114.007 -31.351 59.741  1.00 86.35  ?  167 LYS A NZ  1 
ATOM   1233  N  N   . VAL A  1  168 ? 113.891 -29.911 51.822  1.00 69.87  ?  168 VAL A N   1 
ATOM   1234  C  CA  . VAL A  1  168 ? 113.330 -30.366 50.555  1.00 54.00  ?  168 VAL A CA  1 
ATOM   1235  C  C   . VAL A  1  168 ? 113.966 -31.718 50.127  1.00 60.07  ?  168 VAL A C   1 
ATOM   1236  O  O   . VAL A  1  168 ? 113.362 -32.446 49.342  1.00 65.79  ?  168 VAL A O   1 
ATOM   1237  C  CB  . VAL A  1  168 ? 113.457 -29.270 49.465  1.00 48.89  ?  168 VAL A CB  1 
ATOM   1238  C  CG1 . VAL A  1  168 ? 114.911 -29.045 49.080  1.00 70.82  ?  168 VAL A CG1 1 
ATOM   1239  C  CG2 . VAL A  1  168 ? 112.615 -29.604 48.239  1.00 48.23  ?  168 VAL A CG2 1 
ATOM   1240  N  N   . ILE A  1  169 ? 115.162 -32.067 50.653  1.00 65.83  ?  169 ILE A N   1 
ATOM   1241  C  CA  . ILE A  1  169 ? 115.816 -33.340 50.333  1.00 64.58  ?  169 ILE A CA  1 
ATOM   1242  C  C   . ILE A  1  169 ? 114.961 -34.475 50.913  1.00 67.54  ?  169 ILE A C   1 
ATOM   1243  O  O   . ILE A  1  169 ? 114.648 -35.436 50.212  1.00 67.57  ?  169 ILE A O   1 
ATOM   1244  C  CB  . ILE A  1  169 ? 117.265 -33.389 50.895  1.00 57.19  ?  169 ILE A CB  1 
ATOM   1245  C  CG1 . ILE A  1  169 ? 118.181 -32.415 50.140  1.00 53.07  ?  169 ILE A CG1 1 
ATOM   1246  C  CG2 . ILE A  1  169 ? 117.829 -34.816 50.823  1.00 76.04  ?  169 ILE A CG2 1 
ATOM   1247  C  CD1 . ILE A  1  169 ? 119.437 -32.072 50.858  1.00 62.12  ?  169 ILE A CD1 1 
ATOM   1248  N  N   . ASP A  1  170 ? 114.583 -34.356 52.198  1.00 66.28  ?  170 ASP A N   1 
ATOM   1249  C  CA  . ASP A  1  170 ? 113.756 -35.351 52.878  1.00 66.68  ?  170 ASP A CA  1 
ATOM   1250  C  C   . ASP A  1  170 ? 112.404 -35.488 52.178  1.00 74.24  ?  170 ASP A C   1 
ATOM   1251  O  O   . ASP A  1  170 ? 111.894 -36.596 52.032  1.00 79.71  ?  170 ASP A O   1 
ATOM   1252  C  CB  . ASP A  1  170 ? 113.563 -34.960 54.352  1.00 68.19  ?  170 ASP A CB  1 
ATOM   1253  C  CG  . ASP A  1  170 ? 114.830 -35.056 55.182  1.00 89.88  ?  170 ASP A CG  1 
ATOM   1254  O  OD1 . ASP A  1  170 ? 115.764 -35.776 54.762  1.00 85.22  ?  170 ASP A OD1 1 
ATOM   1255  O  OD2 . ASP A  1  170 ? 114.887 -34.413 56.258  1.00 94.74  ?  170 ASP A OD2 1 
ATOM   1256  N  N   . GLN A  1  171 ? 111.833 -34.370 51.734  1.00 68.01  ?  171 GLN A N   1 
ATOM   1257  C  CA  . GLN A  1  171 ? 110.557 -34.377 51.034  1.00 69.31  ?  171 GLN A CA  1 
ATOM   1258  C  C   . GLN A  1  171 ? 110.666 -35.085 49.682  1.00 77.72  ?  171 GLN A C   1 
ATOM   1259  O  O   . GLN A  1  171 ? 109.742 -35.802 49.304  1.00 84.62  ?  171 GLN A O   1 
ATOM   1260  C  CB  . GLN A  1  171 ? 110.060 -32.944 50.847  1.00 63.40  ?  171 GLN A CB  1 
ATOM   1261  C  CG  . GLN A  1  171 ? 109.493 -32.349 52.124  1.00 56.26  ?  171 GLN A CG  1 
ATOM   1262  C  CD  . GLN A  1  171 ? 108.936 -30.974 51.898  1.00 63.45  ?  171 GLN A CD  1 
ATOM   1263  O  OE1 . GLN A  1  171 ? 109.455 -30.202 51.092  1.00 70.47  ?  171 GLN A OE1 1 
ATOM   1264  N  NE2 . GLN A  1  171 ? 107.869 -30.631 52.606  1.00 66.64  ?  171 GLN A NE2 1 
ATOM   1265  N  N   . ALA A  1  172 ? 111.781 -34.899 48.954  1.00 73.75  ?  172 ALA A N   1 
ATOM   1266  C  CA  . ALA A  1  172 ? 111.980 -35.567 47.665  1.00 64.77  ?  172 ALA A CA  1 
ATOM   1267  C  C   . ALA A  1  172 ? 112.036 -37.085 47.878  1.00 76.45  ?  172 ALA A C   1 
ATOM   1268  O  O   . ALA A  1  172 ? 111.478 -37.842 47.088  1.00 82.12  ?  172 ALA A O   1 
ATOM   1269  C  CB  . ALA A  1  172 ? 113.267 -35.085 47.019  1.00 53.52  ?  172 ALA A CB  1 
ATOM   1270  N  N   . ILE A  1  173 ? 112.694 -37.526 48.961  1.00 74.50  ?  173 ILE A N   1 
ATOM   1271  C  CA  . ILE A  1  173 ? 112.799 -38.947 49.291  1.00 75.70  ?  173 ILE A CA  1 
ATOM   1272  C  C   . ILE A  1  173 ? 111.398 -39.474 49.629  1.00 82.46  ?  173 ILE A C   1 
ATOM   1273  O  O   . ILE A  1  173 ? 110.968 -40.479 49.061  1.00 77.67  ?  173 ILE A O   1 
ATOM   1274  C  CB  . ILE A  1  173 ? 113.801 -39.168 50.463  1.00 65.36  ?  173 ILE A CB  1 
ATOM   1275  C  CG1 . ILE A  1  173 ? 115.248 -38.861 50.020  1.00 59.27  ?  173 ILE A CG1 1 
ATOM   1276  C  CG2 . ILE A  1  173 ? 113.693 -40.593 51.005  1.00 65.33  ?  173 ILE A CG2 1 
ATOM   1277  C  CD1 . ILE A  1  173 ? 116.191 -38.445 51.144  1.00 86.50  ?  173 ILE A CD1 1 
ATOM   1278  N  N   A GLU A  1  174 ? 110.689 -38.785 50.541  0.46 79.07  ?  174 GLU A N   1 
ATOM   1279  N  N   B GLU A  1  174 ? 110.688 -38.791 50.545  0.54 77.19  ?  174 GLU A N   1 
ATOM   1280  C  CA  A GLU A  1  174 ? 109.338 -39.157 50.962  0.46 79.44  ?  174 GLU A CA  1 
ATOM   1281  C  CA  B GLU A  1  174 ? 109.344 -39.194 50.963  0.54 78.96  ?  174 GLU A CA  1 
ATOM   1282  C  C   A GLU A  1  174 ? 108.391 -39.270 49.764  0.46 87.06  ?  174 GLU A C   1 
ATOM   1283  C  C   B GLU A  1  174 ? 108.366 -39.252 49.781  0.54 86.57  ?  174 GLU A C   1 
ATOM   1284  O  O   A GLU A  1  174 ? 107.565 -40.179 49.715  0.46 93.41  ?  174 GLU A O   1 
ATOM   1285  O  O   B GLU A  1  174 ? 107.492 -40.117 49.756  0.54 93.49  ?  174 GLU A O   1 
ATOM   1286  C  CB  A GLU A  1  174 ? 108.796 -38.119 51.966  0.46 78.93  ?  174 GLU A CB  1 
ATOM   1287  C  CB  B GLU A  1  174 ? 108.822 -38.269 52.080  0.54 78.73  ?  174 GLU A CB  1 
ATOM   1288  C  CG  A GLU A  1  174 ? 107.401 -38.426 52.482  0.46 83.83  ?  174 GLU A CG  1 
ATOM   1289  C  CG  B GLU A  1  174 ? 109.504 -38.501 53.421  0.54 82.64  ?  174 GLU A CG  1 
ATOM   1290  C  CD  A GLU A  1  174 ? 106.831 -37.415 53.458  0.46 89.04  ?  174 GLU A CD  1 
ATOM   1291  C  CD  B GLU A  1  174 ? 109.528 -37.305 54.350  0.54 77.43  ?  174 GLU A CD  1 
ATOM   1292  O  OE1 A GLU A  1  174 ? 107.619 -36.648 54.054  0.46 94.64  ?  174 GLU A OE1 1 
ATOM   1293  O  OE1 B GLU A  1  174 ? 108.488 -36.618 54.470  0.54 90.64  ?  174 GLU A OE1 1 
ATOM   1294  O  OE2 A GLU A  1  174 ? 105.590 -37.397 53.630  0.46 87.41  ?  174 GLU A OE2 1 
ATOM   1295  O  OE2 B GLU A  1  174 ? 110.590 -37.058 54.966  0.54 62.67  ?  174 GLU A OE2 1 
ATOM   1296  N  N   . GLY A  1  175 ? 108.529 -38.358 48.810  1.00 81.32  ?  175 GLY A N   1 
ATOM   1297  C  CA  . GLY A  1  175 ? 107.683 -38.340 47.624  1.00 80.73  ?  175 GLY A CA  1 
ATOM   1298  C  C   . GLY A  1  175 ? 108.136 -39.272 46.514  1.00 80.11  ?  175 GLY A C   1 
ATOM   1299  O  O   . GLY A  1  175 ? 107.640 -39.174 45.388  1.00 83.19  ?  175 GLY A O   1 
ATOM   1300  N  N   . LYS A  1  176 ? 109.078 -40.187 46.821  1.00 80.64  ?  176 LYS A N   1 
ATOM   1301  C  CA  . LYS A  1  176 ? 109.616 -41.178 45.886  1.00 75.79  ?  176 LYS A CA  1 
ATOM   1302  C  C   . LYS A  1  176 ? 110.277 -40.572 44.640  1.00 66.20  ?  176 LYS A C   1 
ATOM   1303  O  O   . LYS A  1  176 ? 109.887 -40.891 43.519  1.00 66.91  ?  176 LYS A O   1 
ATOM   1304  C  CB  . LYS A  1  176 ? 108.532 -42.203 45.490  1.00 77.01  ?  176 LYS A CB  1 
ATOM   1305  C  CG  . LYS A  1  176 ? 107.872 -42.927 46.667  1.00 87.06  ?  176 LYS A CG  1 
ATOM   1306  C  CD  . LYS A  1  176 ? 108.808 -43.933 47.354  1.00 96.78  ?  176 LYS A CD  1 
ATOM   1307  C  CE  . LYS A  1  176 ? 108.296 -45.352 47.313  1.00 113.19 ?  176 LYS A CE  1 
ATOM   1308  N  NZ  . LYS A  1  176 ? 109.184 -46.275 48.070  1.00 108.29 ?  176 LYS A NZ  1 
ATOM   1309  N  N   . VAL A  1  177 ? 111.297 -39.725 44.834  1.00 68.88  ?  177 VAL A N   1 
ATOM   1310  C  CA  . VAL A  1  177 ? 112.025 -39.109 43.721  1.00 74.75  ?  177 VAL A CA  1 
ATOM   1311  C  C   . VAL A  1  177 ? 113.308 -39.915 43.488  1.00 80.74  ?  177 VAL A C   1 
ATOM   1312  O  O   . VAL A  1  177 ? 114.004 -40.252 44.447  1.00 81.81  ?  177 VAL A O   1 
ATOM   1313  C  CB  . VAL A  1  177 ? 112.329 -37.609 43.996  1.00 67.16  ?  177 VAL A CB  1 
ATOM   1314  C  CG1 . VAL A  1  177 ? 113.387 -37.063 43.042  1.00 58.83  ?  177 VAL A CG1 1 
ATOM   1315  C  CG2 . VAL A  1  177 ? 111.061 -36.772 43.917  1.00 69.08  ?  177 VAL A CG2 1 
ATOM   1316  N  N   . LYS A  1  178 ? 113.615 -40.235 42.223  1.00 91.57  ?  178 LYS A N   1 
ATOM   1317  C  CA  . LYS A  1  178 ? 114.821 -40.990 41.884  1.00 91.97  ?  178 LYS A CA  1 
ATOM   1318  C  C   . LYS A  1  178 ? 115.997 -40.016 41.899  1.00 84.63  ?  178 LYS A C   1 
ATOM   1319  O  O   . LYS A  1  178 ? 116.084 -39.159 41.019  1.00 81.12  ?  178 LYS A O   1 
ATOM   1320  C  CB  . LYS A  1  178 ? 114.684 -41.631 40.490  1.00 110.69 ?  178 LYS A CB  1 
ATOM   1321  C  CG  . LYS A  1  178 ? 113.541 -42.631 40.369  1.00 111.77 ?  178 LYS A CG  1 
ATOM   1322  C  CD  . LYS A  1  178 ? 113.559 -43.325 39.012  1.00 104.05 ?  178 LYS A CD  1 
ATOM   1323  C  CE  . LYS A  1  178 ? 112.499 -44.392 38.896  1.00 124.44 ?  178 LYS A CE  1 
ATOM   1324  N  NZ  . LYS A  1  178 ? 112.440 -44.970 37.525  1.00 120.47 ?  178 LYS A NZ  1 
ATOM   1325  N  N   . MET A  1  179 ? 116.893 -40.127 42.894  1.00 79.20  ?  179 MET A N   1 
ATOM   1326  C  CA  . MET A  1  179 ? 118.031 -39.213 43.002  1.00 76.88  ?  179 MET A CA  1 
ATOM   1327  C  C   . MET A  1  179 ? 119.373 -39.823 42.613  1.00 77.13  ?  179 MET A C   1 
ATOM   1328  O  O   . MET A  1  179 ? 119.687 -40.951 42.988  1.00 92.27  ?  179 MET A O   1 
ATOM   1329  C  CB  . MET A  1  179 ? 118.107 -38.641 44.416  1.00 57.75  ?  179 MET A CB  1 
ATOM   1330  C  CG  . MET A  1  179 ? 116.864 -37.890 44.799  1.00 68.24  ?  179 MET A CG  1 
ATOM   1331  S  SD  . MET A  1  179 ? 117.109 -36.812 46.214  1.00 81.31  ?  179 MET A SD  1 
ATOM   1332  C  CE  . MET A  1  179 ? 117.316 -38.022 47.493  1.00 93.11  ?  179 MET A CE  1 
ATOM   1333  N  N   . GLY A  1  180 ? 120.161 -39.049 41.878  1.00 66.10  ?  180 GLY A N   1 
ATOM   1334  C  CA  . GLY A  1  180 ? 121.477 -39.464 41.418  1.00 67.65  ?  180 GLY A CA  1 
ATOM   1335  C  C   . GLY A  1  180 ? 122.006 -38.535 40.347  1.00 66.61  ?  180 GLY A C   1 
ATOM   1336  O  O   . GLY A  1  180 ? 121.258 -37.721 39.806  1.00 68.10  ?  180 GLY A O   1 
ATOM   1337  N  N   . LEU A  1  181 ? 123.294 -38.650 40.023  1.00 74.48  ?  181 LEU A N   1 
ATOM   1338  C  CA  . LEU A  1  181 ? 123.905 -37.802 39.005  1.00 59.33  ?  181 LEU A CA  1 
ATOM   1339  C  C   . LEU A  1  181 ? 123.344 -38.138 37.629  1.00 73.38  ?  181 LEU A C   1 
ATOM   1340  O  O   . LEU A  1  181 ? 123.079 -37.235 36.835  1.00 71.22  ?  181 LEU A O   1 
ATOM   1341  C  CB  . LEU A  1  181 ? 125.426 -37.975 39.022  1.00 62.39  ?  181 LEU A CB  1 
ATOM   1342  C  CG  . LEU A  1  181 ? 126.242 -36.830 38.409  1.00 64.97  ?  181 LEU A CG  1 
ATOM   1343  C  CD1 . LEU A  1  181 ? 127.528 -36.645 39.147  1.00 90.47  ?  181 LEU A CD1 1 
ATOM   1344  C  CD2 . LEU A  1  181 ? 126.530 -37.077 36.928  1.00 83.10  ?  181 LEU A CD2 1 
ATOM   1345  N  N   . ASP A  1  182 ? 123.158 -39.433 37.342  1.00 88.83  ?  182 ASP A N   1 
ATOM   1346  C  CA  . ASP A  1  182 ? 122.587 -39.858 36.060  1.00 88.93  ?  182 ASP A CA  1 
ATOM   1347  C  C   . ASP A  1  182 ? 121.113 -39.425 35.982  1.00 81.91  ?  182 ASP A C   1 
ATOM   1348  O  O   . ASP A  1  182 ? 120.632 -39.102 34.897  1.00 88.00  ?  182 ASP A O   1 
ATOM   1349  C  CB  . ASP A  1  182 ? 122.698 -41.387 35.882  1.00 100.17 ?  182 ASP A CB  1 
ATOM   1350  C  CG  . ASP A  1  182 ? 124.027 -41.867 35.326  1.00 101.79 ?  182 ASP A CG  1 
ATOM   1351  O  OD1 . ASP A  1  182 ? 124.673 -41.096 34.582  1.00 102.99 ?  182 ASP A OD1 1 
ATOM   1352  O  OD2 . ASP A  1  182 ? 124.416 -43.020 35.628  1.00 104.73 ?  182 ASP A OD2 1 
ATOM   1353  N  N   . LEU A  1  183 ? 120.406 -39.410 37.133  1.00 80.31  ?  183 LEU A N   1 
ATOM   1354  C  CA  . LEU A  1  183 ? 119.001 -39.001 37.219  1.00 66.23  ?  183 LEU A CA  1 
ATOM   1355  C  C   . LEU A  1  183 ? 118.832 -37.468 37.314  1.00 70.16  ?  183 LEU A C   1 
ATOM   1356  O  O   . LEU A  1  183 ? 117.709 -36.989 37.456  1.00 69.89  ?  183 LEU A O   1 
ATOM   1357  C  CB  . LEU A  1  183 ? 118.348 -39.678 38.427  1.00 66.48  ?  183 LEU A CB  1 
ATOM   1358  C  CG  . LEU A  1  183 ? 118.349 -41.214 38.412  1.00 62.06  ?  183 LEU A CG  1 
ATOM   1359  C  CD1 . LEU A  1  183 ? 118.386 -41.768 39.823  1.00 68.84  ?  183 LEU A CD1 1 
ATOM   1360  C  CD2 . LEU A  1  183 ? 117.155 -41.754 37.640  1.00 65.20  ?  183 LEU A CD2 1 
ATOM   1361  N  N   . ARG A  1  184 ? 119.944 -36.712 37.243  1.00 60.61  ?  184 ARG A N   1 
ATOM   1362  C  CA  . ARG A  1  184 ? 119.979 -35.250 37.268  1.00 57.31  ?  184 ARG A CA  1 
ATOM   1363  C  C   . ARG A  1  184 ? 119.320 -34.599 38.495  1.00 59.06  ?  184 ARG A C   1 
ATOM   1364  O  O   . ARG A  1  184 ? 118.761 -33.514 38.376  1.00 65.33  ?  184 ARG A O   1 
ATOM   1365  C  CB  . ARG A  1  184 ? 119.382 -34.688 35.963  1.00 69.86  ?  184 ARG A CB  1 
ATOM   1366  C  CG  . ARG A  1  184 ? 120.010 -35.252 34.689  1.00 72.33  ?  184 ARG A CG  1 
ATOM   1367  C  CD  . ARG A  1  184 ? 121.353 -34.611 34.364  1.00 85.40  ?  184 ARG A CD  1 
ATOM   1368  N  NE  . ARG A  1  184 ? 122.103 -35.364 33.356  1.00 104.55 ?  184 ARG A NE  1 
ATOM   1369  C  CZ  . ARG A  1  184 ? 121.920 -35.275 32.038  1.00 116.68 ?  184 ARG A CZ  1 
ATOM   1370  N  NH1 . ARG A  1  184 ? 120.991 -34.460 31.540  1.00 95.23  ?  184 ARG A NH1 1 
ATOM   1371  N  NH2 . ARG A  1  184 ? 122.661 -36.002 31.208  1.00 119.72 ?  184 ARG A NH2 1 
ATOM   1372  N  N   . VAL A  1  185 ? 119.389 -35.277 39.644  1.00 54.94  ?  185 VAL A N   1 
ATOM   1373  C  CA  . VAL A  1  185 ? 118.848 -34.710 40.916  1.00 65.76  ?  185 VAL A CA  1 
ATOM   1374  C  C   . VAL A  1  185 ? 119.914 -34.929 41.993  1.00 68.75  ?  185 VAL A C   1 
ATOM   1375  O  O   . VAL A  1  185 ? 120.044 -36.077 42.457  1.00 60.37  ?  185 VAL A O   1 
ATOM   1376  C  CB  . VAL A  1  185 ? 117.507 -35.357 41.308  1.00 56.15  ?  185 VAL A CB  1 
ATOM   1377  C  CG1 . VAL A  1  185 ? 116.984 -34.810 42.627  1.00 59.43  ?  185 VAL A CG1 1 
ATOM   1378  C  CG2 . VAL A  1  185 ? 116.463 -35.204 40.212  1.00 59.39  ?  185 VAL A CG2 1 
ATOM   1379  N  N   . ILE A  1  186 ? 120.651 -33.879 42.367  1.00 57.69  ?  186 ILE A N   1 
ATOM   1380  C  CA  . ILE A  1  186 ? 121.783 -34.056 43.325  1.00 46.12  ?  186 ILE A CA  1 
ATOM   1381  C  C   . ILE A  1  186 ? 121.466 -33.376 44.660  1.00 50.80  ?  186 ILE A C   1 
ATOM   1382  O  O   . ILE A  1  186 ? 121.330 -32.140 44.672  1.00 65.96  ?  186 ILE A O   1 
ATOM   1383  C  CB  . ILE A  1  186 ? 123.089 -33.507 42.717  1.00 39.14  ?  186 ILE A CB  1 
ATOM   1384  C  CG1 . ILE A  1  186 ? 123.466 -34.243 41.429  1.00 67.75  ?  186 ILE A CG1 1 
ATOM   1385  C  CG2 . ILE A  1  186 ? 124.214 -33.539 43.739  1.00 59.33  ?  186 ILE A CG2 1 
ATOM   1386  C  CD1 . ILE A  1  186 ? 124.408 -33.472 40.536  1.00 59.73  ?  186 ILE A CD1 1 
ATOM   1387  N  N   . PRO A  1  187 ? 121.351 -34.124 45.779  1.00 48.81  ?  187 PRO A N   1 
ATOM   1388  C  CA  . PRO A  1  187 ? 121.158 -33.513 47.095  1.00 44.40  ?  187 PRO A CA  1 
ATOM   1389  C  C   . PRO A  1  187 ? 122.517 -33.059 47.641  1.00 50.67  ?  187 PRO A C   1 
ATOM   1390  O  O   . PRO A  1  187 ? 123.354 -33.907 47.881  1.00 55.36  ?  187 PRO A O   1 
ATOM   1391  C  CB  . PRO A  1  187 ? 120.586 -34.666 47.926  1.00 43.06  ?  187 PRO A CB  1 
ATOM   1392  C  CG  . PRO A  1  187 ? 121.174 -35.912 47.299  1.00 53.82  ?  187 PRO A CG  1 
ATOM   1393  C  CD  . PRO A  1  187 ? 121.369 -35.586 45.832  1.00 57.67  ?  187 PRO A CD  1 
ATOM   1394  N  N   . LEU A  1  188 ? 122.711 -31.749 47.817  1.00 47.37  ?  188 LEU A N   1 
ATOM   1395  C  CA  . LEU A  1  188 ? 124.014 -31.249 48.249  1.00 38.75  ?  188 LEU A CA  1 
ATOM   1396  C  C   . LEU A  1  188 ? 124.215 -31.281 49.753  1.00 50.28  ?  188 LEU A C   1 
ATOM   1397  O  O   . LEU A  1  188 ? 125.282 -31.674 50.217  1.00 64.13  ?  188 LEU A O   1 
ATOM   1398  C  CB  . LEU A  1  188 ? 124.249 -29.831 47.717  1.00 49.44  ?  188 LEU A CB  1 
ATOM   1399  C  CG  . LEU A  1  188 ? 124.110 -29.655 46.205  1.00 50.20  ?  188 LEU A CG  1 
ATOM   1400  C  CD1 . LEU A  1  188 ? 123.869 -28.220 45.857  1.00 44.25  ?  188 LEU A CD1 1 
ATOM   1401  C  CD2 . LEU A  1  188 ? 125.335 -30.187 45.466  1.00 62.75  ?  188 LEU A CD2 1 
ATOM   1402  N  N   . GLY A  1  189 ? 123.213 -30.858 50.508  1.00 58.93  ?  189 GLY A N   1 
ATOM   1403  C  CA  . GLY A  1  189 ? 123.309 -30.852 51.961  1.00 50.99  ?  189 GLY A CA  1 
ATOM   1404  C  C   . GLY A  1  189 ? 122.085 -30.273 52.632  1.00 55.28  ?  189 GLY A C   1 
ATOM   1405  O  O   . GLY A  1  189 ? 121.225 -29.698 51.969  1.00 50.11  ?  189 GLY A O   1 
ATOM   1406  N  N   . TYR A  1  190 ? 121.997 -30.412 53.956  1.00 70.70  ?  190 TYR A N   1 
ATOM   1407  C  CA  . TYR A  1  190 ? 120.861 -29.879 54.709  1.00 66.19  ?  190 TYR A CA  1 
ATOM   1408  C  C   . TYR A  1  190 ? 121.097 -28.428 55.134  1.00 67.08  ?  190 TYR A C   1 
ATOM   1409  O  O   . TYR A  1  190 ? 120.135 -27.675 55.275  1.00 57.15  ?  190 TYR A O   1 
ATOM   1410  C  CB  . TYR A  1  190 ? 120.566 -30.757 55.928  1.00 55.02  ?  190 TYR A CB  1 
ATOM   1411  C  CG  . TYR A  1  190 ? 120.034 -32.120 55.554  1.00 48.13  ?  190 TYR A CG  1 
ATOM   1412  C  CD1 . TYR A  1  190 ? 118.748 -32.275 55.063  1.00 58.25  ?  190 TYR A CD1 1 
ATOM   1413  C  CD2 . TYR A  1  190 ? 120.824 -33.251 55.670  1.00 47.62  ?  190 TYR A CD2 1 
ATOM   1414  C  CE1 . TYR A  1  190 ? 118.254 -33.523 54.711  1.00 59.21  ?  190 TYR A CE1 1 
ATOM   1415  C  CE2 . TYR A  1  190 ? 120.341 -34.507 55.330  1.00 61.15  ?  190 TYR A CE2 1 
ATOM   1416  C  CZ  . TYR A  1  190 ? 119.052 -34.641 54.851  1.00 69.37  ?  190 TYR A CZ  1 
ATOM   1417  O  OH  . TYR A  1  190 ? 118.576 -35.890 54.520  1.00 70.54  ?  190 TYR A OH  1 
ATOM   1418  N  N   . ASP A  1  191 ? 122.368 -28.031 55.337  1.00 63.15  ?  191 ASP A N   1 
ATOM   1419  C  CA  . ASP A  1  191 ? 122.703 -26.664 55.732  1.00 58.57  ?  191 ASP A CA  1 
ATOM   1420  C  C   . ASP A  1  191 ? 122.517 -25.705 54.566  1.00 58.35  ?  191 ASP A C   1 
ATOM   1421  O  O   . ASP A  1  191 ? 122.628 -26.112 53.412  1.00 62.57  ?  191 ASP A O   1 
ATOM   1422  C  CB  . ASP A  1  191 ? 124.170 -26.573 56.188  1.00 73.28  ?  191 ASP A CB  1 
ATOM   1423  C  CG  . ASP A  1  191 ? 124.460 -27.238 57.517  1.00 93.91  ?  191 ASP A CG  1 
ATOM   1424  O  OD1 . ASP A  1  191 ? 123.612 -28.034 57.982  1.00 103.17 ?  191 ASP A OD1 1 
ATOM   1425  O  OD2 . ASP A  1  191 ? 125.536 -26.964 58.093  1.00 102.77 ?  191 ASP A OD2 1 
ATOM   1426  N  N   . VAL A  1  192 ? 122.262 -24.426 54.860  1.00 69.22  ?  192 VAL A N   1 
ATOM   1427  C  CA  . VAL A  1  192 ? 122.101 -23.421 53.805  1.00 62.33  ?  192 VAL A CA  1 
ATOM   1428  C  C   . VAL A  1  192 ? 123.439 -23.215 53.090  1.00 59.66  ?  192 VAL A C   1 
ATOM   1429  O  O   . VAL A  1  192 ? 123.461 -23.030 51.877  1.00 64.59  ?  192 VAL A O   1 
ATOM   1430  C  CB  . VAL A  1  192 ? 121.557 -22.086 54.364  1.00 50.45  ?  192 VAL A CB  1 
ATOM   1431  C  CG1 . VAL A  1  192 ? 121.389 -21.054 53.257  1.00 59.37  ?  192 VAL A CG1 1 
ATOM   1432  C  CG2 . VAL A  1  192 ? 120.238 -22.304 55.092  1.00 78.19  ?  192 VAL A CG2 1 
ATOM   1433  N  N   . THR A  1  193 ? 124.549 -23.266 53.833  1.00 57.48  ?  193 THR A N   1 
ATOM   1434  C  CA  . THR A  1  193 ? 125.883 -23.091 53.267  1.00 47.71  ?  193 THR A CA  1 
ATOM   1435  C  C   . THR A  1  193 ? 126.191 -24.102 52.160  1.00 59.89  ?  193 THR A C   1 
ATOM   1436  O  O   . THR A  1  193 ? 127.009 -23.796 51.297  1.00 64.72  ?  193 THR A O   1 
ATOM   1437  C  CB  . THR A  1  193 ? 126.939 -23.160 54.375  1.00 60.62  ?  193 THR A CB  1 
ATOM   1438  O  OG1 . THR A  1  193 ? 126.682 -24.313 55.184  1.00 73.64  ?  193 THR A OG1 1 
ATOM   1439  C  CG2 . THR A  1  193 ? 126.943 -21.917 55.249  1.00 70.29  ?  193 THR A CG2 1 
ATOM   1440  N  N   . SER A  1  194 ? 125.491 -25.239 52.124  1.00 58.45  ?  194 SER A N   1 
ATOM   1441  C  CA  . SER A  1  194 ? 125.834 -26.264 51.102  1.00 56.04  ?  194 SER A CA  1 
ATOM   1442  C  C   . SER A  1  194 ? 125.384 -25.796 49.712  1.00 57.05  ?  194 SER A C   1 
ATOM   1443  O  O   . SER A  1  194 ? 125.738 -26.469 48.728  1.00 58.92  ?  194 SER A O   1 
ATOM   1444  C  CB  . SER A  1  194 ? 125.304 -27.642 51.444  1.00 49.39  ?  194 SER A CB  1 
ATOM   1445  O  OG  . SER A  1  194 ? 123.996 -27.603 51.984  1.00 65.54  ?  194 SER A OG  1 
ATOM   1446  N  N   . VAL A  1  195 ? 124.648 -24.683 49.630  1.00 56.31  ?  195 VAL A N   1 
ATOM   1447  C  CA  . VAL A  1  195 ? 124.262 -24.135 48.329  1.00 49.26  ?  195 VAL A CA  1 
ATOM   1448  C  C   . VAL A  1  195 ? 125.553 -23.772 47.565  1.00 62.40  ?  195 VAL A C   1 
ATOM   1449  O  O   . VAL A  1  195 ? 125.591 -23.900 46.342  1.00 57.29  ?  195 VAL A O   1 
ATOM   1450  C  CB  . VAL A  1  195 ? 123.281 -22.938 48.467  1.00 43.60  ?  195 VAL A CB  1 
ATOM   1451  C  CG1 . VAL A  1  195 ? 124.002 -21.681 48.947  1.00 50.53  ?  195 VAL A CG1 1 
ATOM   1452  C  CG2 . VAL A  1  195 ? 122.560 -22.661 47.151  1.00 41.08  ?  195 VAL A CG2 1 
ATOM   1453  N  N   . ILE A  1  196 ? 126.610 -23.329 48.280  1.00 55.85  ?  196 ILE A N   1 
ATOM   1454  C  CA  . ILE A  1  196 ? 127.875 -22.962 47.648  1.00 53.49  ?  196 ILE A CA  1 
ATOM   1455  C  C   . ILE A  1  196 ? 128.431 -24.070 46.738  1.00 61.69  ?  196 ILE A C   1 
ATOM   1456  O  O   . ILE A  1  196 ? 129.165 -23.764 45.800  1.00 60.88  ?  196 ILE A O   1 
ATOM   1457  C  CB  . ILE A  1  196 ? 128.931 -22.494 48.702  1.00 46.18  ?  196 ILE A CB  1 
ATOM   1458  C  CG1 . ILE A  1  196 ? 129.983 -21.567 48.069  1.00 48.72  ?  196 ILE A CG1 1 
ATOM   1459  C  CG2 . ILE A  1  196 ? 129.617 -23.681 49.372  1.00 63.59  ?  196 ILE A CG2 1 
ATOM   1460  C  CD1 . ILE A  1  196 ? 129.464 -20.226 47.658  1.00 68.95  ?  196 ILE A CD1 1 
ATOM   1461  N  N   . HIS A  1  197 ? 128.073 -25.343 46.993  1.00 60.21  ?  197 HIS A N   1 
ATOM   1462  C  CA  . HIS A  1  197 ? 128.557 -26.466 46.192  1.00 57.61  ?  197 HIS A CA  1 
ATOM   1463  C  C   . HIS A  1  197 ? 128.010 -26.468 44.760  1.00 57.67  ?  197 HIS A C   1 
ATOM   1464  O  O   . HIS A  1  197 ? 128.600 -27.115 43.896  1.00 70.80  ?  197 HIS A O   1 
ATOM   1465  C  CB  . HIS A  1  197 ? 128.292 -27.786 46.917  1.00 55.96  ?  197 HIS A CB  1 
ATOM   1466  C  CG  . HIS A  1  197 ? 129.035 -27.881 48.215  1.00 64.40  ?  197 HIS A CG  1 
ATOM   1467  N  ND1 . HIS A  1  197 ? 130.385 -27.575 48.297  1.00 62.42  ?  197 HIS A ND1 1 
ATOM   1468  C  CD2 . HIS A  1  197 ? 128.590 -28.223 49.447  1.00 59.40  ?  197 HIS A CD2 1 
ATOM   1469  C  CE1 . HIS A  1  197 ? 130.719 -27.753 49.565  1.00 51.01  ?  197 HIS A CE1 1 
ATOM   1470  N  NE2 . HIS A  1  197 ? 129.671 -28.140 50.295  1.00 57.07  ?  197 HIS A NE2 1 
ATOM   1471  N  N   . VAL A  1  198 ? 126.931 -25.724 44.504  1.00 48.22  ?  198 VAL A N   1 
ATOM   1472  C  CA  . VAL A  1  198 ? 126.441 -25.603 43.097  1.00 48.13  ?  198 VAL A CA  1 
ATOM   1473  C  C   . VAL A  1  198 ? 126.991 -24.292 42.527  1.00 59.22  ?  198 VAL A C   1 
ATOM   1474  O  O   . VAL A  1  198 ? 127.223 -24.235 41.305  1.00 64.38  ?  198 VAL A O   1 
ATOM   1475  C  CB  . VAL A  1  198 ? 124.906 -25.686 43.000  1.00 53.43  ?  198 VAL A CB  1 
ATOM   1476  C  CG1 . VAL A  1  198 ? 124.235 -24.380 43.384  1.00 57.35  ?  198 VAL A CG1 1 
ATOM   1477  C  CG2 . VAL A  1  198 ? 124.456 -26.128 41.616  1.00 54.56  ?  198 VAL A CG2 1 
ATOM   1478  N  N   . VAL A  1  199 ? 127.202 -23.287 43.381  1.00 55.99  ?  199 VAL A N   1 
ATOM   1479  C  CA  . VAL A  1  199 ? 127.798 -22.029 42.940  1.00 44.63  ?  199 VAL A CA  1 
ATOM   1480  C  C   . VAL A  1  199 ? 129.199 -22.319 42.381  1.00 54.07  ?  199 VAL A C   1 
ATOM   1481  O  O   . VAL A  1  199 ? 129.566 -21.755 41.354  1.00 56.18  ?  199 VAL A O   1 
ATOM   1482  C  CB  . VAL A  1  199 ? 127.840 -21.008 44.104  1.00 53.78  ?  199 VAL A CB  1 
ATOM   1483  C  CG1 . VAL A  1  199 ? 128.734 -19.816 43.773  1.00 44.84  ?  199 VAL A CG1 1 
ATOM   1484  C  CG2 . VAL A  1  199 ? 126.433 -20.553 44.480  1.00 31.96  ?  199 VAL A CG2 1 
ATOM   1485  N  N   . THR A  1  200 ? 129.968 -23.224 43.026  1.00 49.31  ?  200 THR A N   1 
ATOM   1486  C  CA  . THR A  1  200 ? 131.305 -23.577 42.530  1.00 53.74  ?  200 THR A CA  1 
ATOM   1487  C  C   . THR A  1  200 ? 131.225 -24.295 41.178  1.00 59.49  ?  200 THR A C   1 
ATOM   1488  O  O   . THR A  1  200 ? 132.183 -24.228 40.418  1.00 67.04  ?  200 THR A O   1 
ATOM   1489  C  CB  . THR A  1  200 ? 132.111 -24.394 43.543  1.00 55.74  ?  200 THR A CB  1 
ATOM   1490  O  OG1 . THR A  1  200 ? 131.497 -25.671 43.752  1.00 74.83  ?  200 THR A OG1 1 
ATOM   1491  C  CG2 . THR A  1  200 ? 132.306 -23.662 44.857  1.00 69.91  ?  200 THR A CG2 1 
ATOM   1492  N  N   . ILE A  1  201 ? 130.101 -24.966 40.860  1.00 53.80  ?  201 ILE A N   1 
ATOM   1493  C  CA  . ILE A  1  201 ? 129.943 -25.627 39.559  1.00 54.35  ?  201 ILE A CA  1 
ATOM   1494  C  C   . ILE A  1  201 ? 129.903 -24.529 38.490  1.00 56.34  ?  201 ILE A C   1 
ATOM   1495  O  O   . ILE A  1  201 ? 130.551 -24.650 37.456  1.00 53.90  ?  201 ILE A O   1 
ATOM   1496  C  CB  . ILE A  1  201 ? 128.641 -26.479 39.492  1.00 54.75  ?  201 ILE A CB  1 
ATOM   1497  C  CG1 . ILE A  1  201 ? 128.668 -27.653 40.485  1.00 63.57  ?  201 ILE A CG1 1 
ATOM   1498  C  CG2 . ILE A  1  201 ? 128.360 -26.963 38.055  1.00 36.33  ?  201 ILE A CG2 1 
ATOM   1499  C  CD1 . ILE A  1  201 ? 127.324 -28.405 40.614  1.00 46.96  ?  201 ILE A CD1 1 
ATOM   1500  N  N   . ALA A  1  202 ? 129.134 -23.461 38.743  1.00 50.20  ?  202 ALA A N   1 
ATOM   1501  C  CA  . ALA A  1  202 ? 129.021 -22.356 37.810  1.00 56.11  ?  202 ALA A CA  1 
ATOM   1502  C  C   . ALA A  1  202 ? 130.354 -21.616 37.702  1.00 58.38  ?  202 ALA A C   1 
ATOM   1503  O  O   . ALA A  1  202 ? 130.782 -21.311 36.590  1.00 61.91  ?  202 ALA A O   1 
ATOM   1504  C  CB  . ALA A  1  202 ? 127.925 -21.404 38.261  1.00 33.30  ?  202 ALA A CB  1 
ATOM   1505  N  N   . ILE A  1  203 ? 131.027 -21.345 38.836  1.00 46.29  ?  203 ILE A N   1 
ATOM   1506  C  CA  . ILE A  1  203 ? 132.307 -20.634 38.798  1.00 50.61  ?  203 ILE A CA  1 
ATOM   1507  C  C   . ILE A  1  203 ? 133.358 -21.469 38.074  1.00 58.63  ?  203 ILE A C   1 
ATOM   1508  O  O   . ILE A  1  203 ? 134.102 -20.931 37.256  1.00 65.89  ?  203 ILE A O   1 
ATOM   1509  C  CB  . ILE A  1  203 ? 132.777 -20.203 40.216  1.00 44.94  ?  203 ILE A CB  1 
ATOM   1510  C  CG1 . ILE A  1  203 ? 131.933 -19.008 40.725  1.00 42.26  ?  203 ILE A CG1 1 
ATOM   1511  C  CG2 . ILE A  1  203 ? 134.263 -19.833 40.216  1.00 48.26  ?  203 ILE A CG2 1 
ATOM   1512  C  CD1 . ILE A  1  203 ? 131.849 -18.886 42.204  1.00 67.31  ?  203 ILE A CD1 1 
ATOM   1513  N  N   . ARG A  1  204 ? 133.428 -22.774 38.365  1.00 55.95  ?  204 ARG A N   1 
ATOM   1514  C  CA  . ARG A  1  204 ? 134.407 -23.642 37.712  1.00 53.72  ?  204 ARG A CA  1 
ATOM   1515  C  C   . ARG A  1  204 ? 134.111 -23.804 36.220  1.00 62.22  ?  204 ARG A C   1 
ATOM   1516  O  O   . ARG A  1  204 ? 135.043 -23.997 35.445  1.00 57.23  ?  204 ARG A O   1 
ATOM   1517  C  CB  . ARG A  1  204 ? 134.520 -24.998 38.426  1.00 55.23  ?  204 ARG A CB  1 
ATOM   1518  C  CG  . ARG A  1  204 ? 135.392 -24.942 39.679  1.00 52.13  ?  204 ARG A CG  1 
ATOM   1519  C  CD  . ARG A  1  204 ? 135.444 -26.270 40.395  1.00 52.80  ?  204 ARG A CD  1 
ATOM   1520  N  NE  . ARG A  1  204 ? 134.253 -26.500 41.213  1.00 61.73  ?  204 ARG A NE  1 
ATOM   1521  C  CZ  . ARG A  1  204 ? 133.944 -27.661 41.784  1.00 64.02  ?  204 ARG A CZ  1 
ATOM   1522  N  NH1 . ARG A  1  204 ? 134.735 -28.718 41.630  1.00 60.57  ?  204 ARG A NH1 1 
ATOM   1523  N  NH2 . ARG A  1  204 ? 132.839 -27.778 42.513  1.00 62.90  ?  204 ARG A NH2 1 
ATOM   1524  N  N   . ALA A  1  205 ? 132.838 -23.682 35.798  1.00 51.12  ?  205 ALA A N   1 
ATOM   1525  C  CA  . ALA A  1  205 ? 132.499 -23.759 34.374  1.00 52.79  ?  205 ALA A CA  1 
ATOM   1526  C  C   . ALA A  1  205 ? 133.160 -22.579 33.638  1.00 68.42  ?  205 ALA A C   1 
ATOM   1527  O  O   . ALA A  1  205 ? 133.610 -22.722 32.500  1.00 69.48  ?  205 ALA A O   1 
ATOM   1528  C  CB  . ALA A  1  205 ? 130.991 -23.704 34.190  1.00 45.34  ?  205 ALA A CB  1 
ATOM   1529  N  N   . ALA A  1  206 ? 133.217 -21.417 34.303  1.00 59.43  ?  206 ALA A N   1 
ATOM   1530  C  CA  . ALA A  1  206 ? 133.848 -20.223 33.764  1.00 51.10  ?  206 ALA A CA  1 
ATOM   1531  C  C   . ALA A  1  206 ? 135.361 -20.423 33.670  1.00 58.13  ?  206 ALA A C   1 
ATOM   1532  O  O   . ALA A  1  206 ? 135.975 -19.983 32.708  1.00 62.24  ?  206 ALA A O   1 
ATOM   1533  C  CB  . ALA A  1  206 ? 133.541 -19.033 34.660  1.00 52.59  ?  206 ALA A CB  1 
ATOM   1534  N  N   . LEU A  1  207 ? 135.964 -21.084 34.661  1.00 57.71  ?  207 LEU A N   1 
ATOM   1535  C  CA  . LEU A  1  207 ? 137.405 -21.315 34.673  1.00 53.35  ?  207 LEU A CA  1 
ATOM   1536  C  C   . LEU A  1  207 ? 137.842 -22.412 33.700  1.00 61.19  ?  207 LEU A C   1 
ATOM   1537  O  O   . LEU A  1  207 ? 138.903 -22.294 33.094  1.00 68.18  ?  207 LEU A O   1 
ATOM   1538  C  CB  . LEU A  1  207 ? 137.867 -21.691 36.088  1.00 53.82  ?  207 LEU A CB  1 
ATOM   1539  C  CG  . LEU A  1  207 ? 137.638 -20.653 37.181  1.00 55.54  ?  207 LEU A CG  1 
ATOM   1540  C  CD1 . LEU A  1  207 ? 137.836 -21.260 38.548  1.00 55.45  ?  207 LEU A CD1 1 
ATOM   1541  C  CD2 . LEU A  1  207 ? 138.571 -19.461 37.025  1.00 65.14  ?  207 LEU A CD2 1 
ATOM   1542  N  N   . ILE A  1  208 ? 137.050 -23.478 33.557  1.00 59.22  ?  208 ILE A N   1 
ATOM   1543  C  CA  . ILE A  1  208 ? 137.412 -24.592 32.681  1.00 68.91  ?  208 ILE A CA  1 
ATOM   1544  C  C   . ILE A  1  208 ? 137.010 -24.348 31.213  1.00 72.28  ?  208 ILE A C   1 
ATOM   1545  O  O   . ILE A  1  208 ? 137.875 -24.324 30.341  1.00 74.27  ?  208 ILE A O   1 
ATOM   1546  C  CB  . ILE A  1  208 ? 136.821 -25.929 33.226  1.00 61.15  ?  208 ILE A CB  1 
ATOM   1547  C  CG1 . ILE A  1  208 ? 137.412 -26.272 34.615  1.00 61.40  ?  208 ILE A CG1 1 
ATOM   1548  C  CG2 . ILE A  1  208 ? 137.064 -27.071 32.233  1.00 60.88  ?  208 ILE A CG2 1 
ATOM   1549  C  CD1 . ILE A  1  208 ? 136.542 -27.170 35.474  1.00 48.17  ?  208 ILE A CD1 1 
ATOM   1550  N  N   . PHE A  1  209 ? 135.707 -24.177 30.938  1.00 72.41  ?  209 PHE A N   1 
ATOM   1551  C  CA  . PHE A  1  209 ? 135.214 -23.988 29.576  1.00 61.63  ?  209 PHE A CA  1 
ATOM   1552  C  C   . PHE A  1  209 ? 135.375 -22.558 29.111  1.00 61.25  ?  209 PHE A C   1 
ATOM   1553  O  O   . PHE A  1  209 ? 135.759 -22.327 27.968  1.00 70.28  ?  209 PHE A O   1 
ATOM   1554  C  CB  . PHE A  1  209 ? 133.750 -24.428 29.474  1.00 65.21  ?  209 PHE A CB  1 
ATOM   1555  C  CG  . PHE A  1  209 ? 133.523 -25.792 30.074  1.00 70.21  ?  209 PHE A CG  1 
ATOM   1556  C  CD1 . PHE A  1  209 ? 133.957 -26.933 29.424  1.00 67.17  ?  209 PHE A CD1 1 
ATOM   1557  C  CD2 . PHE A  1  209 ? 132.960 -25.927 31.329  1.00 67.83  ?  209 PHE A CD2 1 
ATOM   1558  C  CE1 . PHE A  1  209 ? 133.781 -28.187 29.992  1.00 55.89  ?  209 PHE A CE1 1 
ATOM   1559  C  CE2 . PHE A  1  209 ? 132.794 -27.181 31.901  1.00 73.22  ?  209 PHE A CE2 1 
ATOM   1560  C  CZ  . PHE A  1  209 ? 133.209 -28.302 31.229  1.00 76.94  ?  209 PHE A CZ  1 
ATOM   1561  N  N   . GLY A  1  210 ? 135.089 -21.609 29.991  1.00 62.85  ?  210 GLY A N   1 
ATOM   1562  C  CA  . GLY A  1  210 ? 135.223 -20.195 29.666  1.00 63.59  ?  210 GLY A CA  1 
ATOM   1563  C  C   . GLY A  1  210 ? 136.659 -19.725 29.537  1.00 56.59  ?  210 GLY A C   1 
ATOM   1564  O  O   . GLY A  1  210 ? 136.909 -18.640 29.014  1.00 61.32  ?  210 GLY A O   1 
ATOM   1565  N  N   . GLY A  1  211 ? 137.600 -20.525 30.029  1.00 61.51  ?  211 GLY A N   1 
ATOM   1566  C  CA  . GLY A  1  211 ? 139.016 -20.201 29.964  1.00 64.40  ?  211 GLY A CA  1 
ATOM   1567  C  C   . GLY A  1  211 ? 139.393 -18.923 30.684  1.00 64.40  ?  211 GLY A C   1 
ATOM   1568  O  O   . GLY A  1  211 ? 140.404 -18.302 30.347  1.00 68.54  ?  211 GLY A O   1 
ATOM   1569  N  N   . ILE A  1  212 ? 138.597 -18.517 31.682  1.00 53.36  ?  212 ILE A N   1 
ATOM   1570  C  CA  . ILE A  1  212 ? 138.891 -17.303 32.434  1.00 60.03  ?  212 ILE A CA  1 
ATOM   1571  C  C   . ILE A  1  212 ? 139.875 -17.661 33.548  1.00 73.97  ?  212 ILE A C   1 
ATOM   1572  O  O   . ILE A  1  212 ? 139.902 -18.806 34.002  1.00 76.98  ?  212 ILE A O   1 
ATOM   1573  C  CB  . ILE A  1  212 ? 137.598 -16.632 32.969  1.00 49.03  ?  212 ILE A CB  1 
ATOM   1574  C  CG1 . ILE A  1  212 ? 136.596 -16.406 31.821  1.00 53.35  ?  212 ILE A CG1 1 
ATOM   1575  C  CG2 . ILE A  1  212 ? 137.932 -15.307 33.652  1.00 59.43  ?  212 ILE A CG2 1 
ATOM   1576  C  CD1 . ILE A  1  212 ? 135.236 -15.979 32.244  1.00 54.43  ?  212 ILE A CD1 1 
ATOM   1577  N  N   . LYS A  1  213 ? 140.704 -16.693 33.968  1.00 68.52  ?  213 LYS A N   1 
ATOM   1578  C  CA  . LYS A  1  213 ? 141.694 -16.916 35.020  1.00 65.73  ?  213 LYS A CA  1 
ATOM   1579  C  C   . LYS A  1  213 ? 141.215 -16.311 36.335  1.00 63.99  ?  213 LYS A C   1 
ATOM   1580  O  O   . LYS A  1  213 ? 140.419 -15.371 36.334  1.00 65.81  ?  213 LYS A O   1 
ATOM   1581  C  CB  . LYS A  1  213 ? 143.057 -16.314 34.630  1.00 59.36  ?  213 LYS A CB  1 
ATOM   1582  C  CG  . LYS A  1  213 ? 143.526 -16.638 33.212  1.00 76.55  ?  213 LYS A CG  1 
ATOM   1583  C  CD  . LYS A  1  213 ? 143.900 -18.116 33.011  1.00 90.85  ?  213 LYS A CD  1 
ATOM   1584  C  CE  . LYS A  1  213 ? 143.985 -18.517 31.551  1.00 91.59  ?  213 LYS A CE  1 
ATOM   1585  N  NZ  . LYS A  1  213 ? 143.011 -19.593 31.210  1.00 111.69 ?  213 LYS A NZ  1 
ATOM   1586  N  N   . GLY A  1  214 ? 141.715 -16.846 37.446  1.00 66.49  ?  214 GLY A N   1 
ATOM   1587  C  CA  . GLY A  1  214 ? 141.357 -16.373 38.778  1.00 56.41  ?  214 GLY A CA  1 
ATOM   1588  C  C   . GLY A  1  214 ? 141.610 -14.891 38.939  1.00 63.35  ?  214 GLY A C   1 
ATOM   1589  O  O   . GLY A  1  214 ? 142.527 -14.351 38.319  1.00 69.15  ?  214 GLY A O   1 
ATOM   1590  N  N   . GLY A  1  215 ? 140.791 -14.227 39.740  1.00 64.33  ?  215 GLY A N   1 
ATOM   1591  C  CA  . GLY A  1  215 ? 140.923 -12.791 39.950  1.00 74.92  ?  215 GLY A CA  1 
ATOM   1592  C  C   . GLY A  1  215 ? 140.075 -11.974 38.994  1.00 61.33  ?  215 GLY A C   1 
ATOM   1593  O  O   . GLY A  1  215 ? 139.745 -10.826 39.295  1.00 79.57  ?  215 GLY A O   1 
ATOM   1594  N  N   . GLN A  1  216 ? 139.708 -12.547 37.831  1.00 59.88  ?  216 GLN A N   1 
ATOM   1595  C  CA  . GLN A  1  216 ? 138.867 -11.845 36.861  1.00 69.71  ?  216 GLN A CA  1 
ATOM   1596  C  C   . GLN A  1  216 ? 137.417 -12.060 37.279  1.00 69.67  ?  216 GLN A C   1 
ATOM   1597  O  O   . GLN A  1  216 ? 136.624 -12.646 36.539  1.00 65.42  ?  216 GLN A O   1 
ATOM   1598  C  CB  . GLN A  1  216 ? 139.107 -12.363 35.430  1.00 68.13  ?  216 GLN A CB  1 
ATOM   1599  C  CG  . GLN A  1  216 ? 140.565 -12.396 34.995  1.00 74.05  ?  216 GLN A CG  1 
ATOM   1600  C  CD  . GLN A  1  216 ? 141.267 -11.077 35.207  1.00 83.71  ?  216 GLN A CD  1 
ATOM   1601  O  OE1 . GLN A  1  216 ? 142.020 -10.898 36.169  1.00 103.65 ?  216 GLN A OE1 1 
ATOM   1602  N  NE2 . GLN A  1  216 ? 141.036 -10.122 34.319  1.00 82.46  ?  216 GLN A NE2 1 
ATOM   1603  N  N   . LEU A  1  217 ? 137.076 -11.583 38.481  1.00 56.39  ?  217 LEU A N   1 
ATOM   1604  C  CA  . LEU A  1  217 ? 135.744 -11.742 39.042  1.00 57.25  ?  217 LEU A CA  1 
ATOM   1605  C  C   . LEU A  1  217 ? 134.653 -11.202 38.135  1.00 67.23  ?  217 LEU A C   1 
ATOM   1606  O  O   . LEU A  1  217 ? 133.663 -11.890 37.903  1.00 71.20  ?  217 LEU A O   1 
ATOM   1607  C  CB  . LEU A  1  217 ? 135.663 -11.068 40.416  1.00 56.59  ?  217 LEU A CB  1 
ATOM   1608  C  CG  . LEU A  1  217 ? 134.416 -11.357 41.243  1.00 54.32  ?  217 LEU A CG  1 
ATOM   1609  C  CD1 . LEU A  1  217 ? 134.189 -12.851 41.417  1.00 62.69  ?  217 LEU A CD1 1 
ATOM   1610  C  CD2 . LEU A  1  217 ? 134.508 -10.686 42.586  1.00 75.72  ?  217 LEU A CD2 1 
ATOM   1611  N  N   . ASN A  1  218 ? 134.824 -9.989  37.606  1.00 59.40  ?  218 ASN A N   1 
ATOM   1612  C  CA  . ASN A  1  218 ? 133.807 -9.413  36.734  1.00 70.07  ?  218 ASN A CA  1 
ATOM   1613  C  C   . ASN A  1  218 ? 133.600 -10.264 35.482  1.00 71.82  ?  218 ASN A C   1 
ATOM   1614  O  O   . ASN A  1  218 ? 132.466 -10.416 35.033  1.00 77.34  ?  218 ASN A O   1 
ATOM   1615  C  CB  . ASN A  1  218 ? 134.149 -7.969  36.386  1.00 67.11  ?  218 ASN A CB  1 
ATOM   1616  C  CG  . ASN A  1  218 ? 134.116 -7.060  37.595  1.00 94.15  ?  218 ASN A CG  1 
ATOM   1617  O  OD1 . ASN A  1  218 ? 133.512 -7.379  38.633  1.00 90.39  ?  218 ASN A OD1 1 
ATOM   1618  N  ND2 . ASN A  1  218 ? 134.771 -5.908  37.498  1.00 101.92 ?  218 ASN A ND2 1 
ATOM   1619  N  N   . ASP A  1  219 ? 134.673 -10.849 34.943  1.00 61.72  ?  219 ASP A N   1 
ATOM   1620  C  CA  . ASP A  1  219 ? 134.558 -11.692 33.755  1.00 67.12  ?  219 ASP A CA  1 
ATOM   1621  C  C   . ASP A  1  219 ? 133.870 -13.019 34.106  1.00 66.48  ?  219 ASP A C   1 
ATOM   1622  O  O   . ASP A  1  219 ? 133.109 -13.540 33.294  1.00 72.72  ?  219 ASP A O   1 
ATOM   1623  C  CB  . ASP A  1  219 ? 135.938 -11.938 33.128  1.00 78.86  ?  219 ASP A CB  1 
ATOM   1624  C  CG  . ASP A  1  219 ? 136.631 -10.674 32.641  1.00 91.14  ?  219 ASP A CG  1 
ATOM   1625  O  OD1 . ASP A  1  219 ? 136.292 -9.578  33.144  1.00 95.91  ?  219 ASP A OD1 1 
ATOM   1626  O  OD2 . ASP A  1  219 ? 137.512 -10.781 31.759  1.00 92.23  ?  219 ASP A OD2 1 
ATOM   1627  N  N   . ILE A  1  220 ? 134.126 -13.554 35.313  1.00 68.32  ?  220 ILE A N   1 
ATOM   1628  C  CA  . ILE A  1  220 ? 133.512 -14.805 35.773  1.00 56.20  ?  220 ILE A CA  1 
ATOM   1629  C  C   . ILE A  1  220 ? 132.031 -14.550 36.054  1.00 62.30  ?  220 ILE A C   1 
ATOM   1630  O  O   . ILE A  1  220 ? 131.185 -15.325 35.609  1.00 66.28  ?  220 ILE A O   1 
ATOM   1631  C  CB  . ILE A  1  220 ? 134.261 -15.377 37.017  1.00 46.57  ?  220 ILE A CB  1 
ATOM   1632  C  CG1 . ILE A  1  220 ? 135.593 -16.051 36.585  1.00 56.38  ?  220 ILE A CG1 1 
ATOM   1633  C  CG2 . ILE A  1  220 ? 133.382 -16.373 37.791  1.00 58.01  ?  220 ILE A CG2 1 
ATOM   1634  C  CD1 . ILE A  1  220 ? 136.756 -15.886 37.540  1.00 53.75  ?  220 ILE A CD1 1 
ATOM   1635  N  N   . LEU A  1  221 ? 131.714 -13.460 36.767  1.00 59.05  ?  221 LEU A N   1 
ATOM   1636  C  CA  . LEU A  1  221 ? 130.326 -13.121 37.072  1.00 49.04  ?  221 LEU A CA  1 
ATOM   1637  C  C   . LEU A  1  221 ? 129.527 -12.866 35.788  1.00 60.83  ?  221 LEU A C   1 
ATOM   1638  O  O   . LEU A  1  221 ? 128.312 -13.061 35.780  1.00 54.95  ?  221 LEU A O   1 
ATOM   1639  C  CB  . LEU A  1  221 ? 130.250 -11.897 37.990  1.00 48.74  ?  221 LEU A CB  1 
ATOM   1640  C  CG  . LEU A  1  221 ? 130.800 -12.070 39.405  1.00 44.89  ?  221 LEU A CG  1 
ATOM   1641  C  CD1 . LEU A  1  221 ? 130.891 -10.734 40.109  1.00 63.73  ?  221 LEU A CD1 1 
ATOM   1642  C  CD2 . LEU A  1  221 ? 129.959 -13.030 40.211  1.00 43.56  ?  221 LEU A CD2 1 
ATOM   1643  N  N   . LYS A  1  222 ? 130.207 -12.429 34.710  1.00 55.46  ?  222 LYS A N   1 
ATOM   1644  C  CA  . LYS A  1  222 ? 129.588 -12.186 33.411  1.00 50.00  ?  222 LYS A CA  1 
ATOM   1645  C  C   . LYS A  1  222 ? 129.348 -13.530 32.718  1.00 58.29  ?  222 LYS A C   1 
ATOM   1646  O  O   . LYS A  1  222 ? 128.318 -13.711 32.077  1.00 63.66  ?  222 LYS A O   1 
ATOM   1647  C  CB  . LYS A  1  222 ? 130.501 -11.301 32.554  1.00 41.14  ?  222 LYS A CB  1 
ATOM   1648  C  CG  . LYS A  1  222 ? 129.896 -10.920 31.211  1.00 66.16  ?  222 LYS A CG  1 
ATOM   1649  C  CD  . LYS A  1  222 ? 130.706 -9.833  30.494  1.00 76.52  ?  222 LYS A CD  1 
ATOM   1650  C  CE  . LYS A  1  222 ? 130.546 -9.858  28.987  1.00 67.47  ?  222 LYS A CE  1 
ATOM   1651  N  NZ  . LYS A  1  222 ? 129.210 -9.364  28.548  1.00 70.68  ?  222 LYS A NZ  1 
ATOM   1652  N  N   . TYR A  1  223 ? 130.295 -14.475 32.845  1.00 57.43  ?  223 TYR A N   1 
ATOM   1653  C  CA  . TYR A  1  223 ? 130.154 -15.792 32.240  1.00 51.80  ?  223 TYR A CA  1 
ATOM   1654  C  C   . TYR A  1  223 ? 128.993 -16.528 32.887  1.00 55.39  ?  223 TYR A C   1 
ATOM   1655  O  O   . TYR A  1  223 ? 128.157 -17.062 32.173  1.00 58.28  ?  223 TYR A O   1 
ATOM   1656  C  CB  . TYR A  1  223 ? 131.439 -16.611 32.408  1.00 47.34  ?  223 TYR A CB  1 
ATOM   1657  C  CG  . TYR A  1  223 ? 131.396 -17.960 31.725  1.00 42.28  ?  223 TYR A CG  1 
ATOM   1658  C  CD1 . TYR A  1  223 ? 130.846 -19.065 32.357  1.00 54.14  ?  223 TYR A CD1 1 
ATOM   1659  C  CD2 . TYR A  1  223 ? 131.937 -18.139 30.463  1.00 51.67  ?  223 TYR A CD2 1 
ATOM   1660  C  CE1 . TYR A  1  223 ? 130.822 -20.311 31.743  1.00 58.53  ?  223 TYR A CE1 1 
ATOM   1661  C  CE2 . TYR A  1  223 ? 131.907 -19.375 29.832  1.00 61.34  ?  223 TYR A CE2 1 
ATOM   1662  C  CZ  . TYR A  1  223 ? 131.358 -20.465 30.480  1.00 59.92  ?  223 TYR A CZ  1 
ATOM   1663  O  OH  . TYR A  1  223 ? 131.337 -21.697 29.868  1.00 67.87  ?  223 TYR A OH  1 
ATOM   1664  N  N   . THR A  1  224 ? 128.919 -16.559 34.232  1.00 54.98  ?  224 THR A N   1 
ATOM   1665  C  CA  . THR A  1  224 ? 127.821 -17.258 34.910  1.00 45.86  ?  224 THR A CA  1 
ATOM   1666  C  C   . THR A  1  224 ? 126.482 -16.623 34.543  1.00 50.62  ?  224 THR A C   1 
ATOM   1667  O  O   . THR A  1  224 ? 125.539 -17.329 34.197  1.00 56.95  ?  224 THR A O   1 
ATOM   1668  C  CB  . THR A  1  224 ? 128.022 -17.292 36.434  1.00 47.00  ?  224 THR A CB  1 
ATOM   1669  O  OG1 . THR A  1  224 ? 128.176 -15.962 36.932  1.00 44.11  ?  224 THR A OG1 1 
ATOM   1670  C  CG2 . THR A  1  224 ? 129.213 -18.146 36.845  1.00 51.39  ?  224 THR A CG2 1 
ATOM   1671  N  N   . ALA A  1  225 ? 126.408 -15.294 34.588  1.00 54.84  ?  225 ALA A N   1 
ATOM   1672  C  CA  . ALA A  1  225 ? 125.181 -14.579 34.266  1.00 45.40  ?  225 ALA A CA  1 
ATOM   1673  C  C   . ALA A  1  225 ? 124.718 -14.796 32.836  1.00 45.60  ?  225 ALA A C   1 
ATOM   1674  O  O   . ALA A  1  225 ? 123.515 -14.813 32.599  1.00 67.74  ?  225 ALA A O   1 
ATOM   1675  C  CB  . ALA A  1  225 ? 125.368 -13.096 34.517  1.00 46.61  ?  225 ALA A CB  1 
ATOM   1676  N  N   . GLU A  1  226 ? 125.644 -14.949 31.881  1.00 46.34  ?  226 GLU A N   1 
ATOM   1677  C  CA  . GLU A  1  226 ? 125.272 -15.124 30.477  1.00 46.63  ?  226 GLU A CA  1 
ATOM   1678  C  C   . GLU A  1  226 ? 125.355 -16.555 29.947  1.00 48.03  ?  226 GLU A C   1 
ATOM   1679  O  O   . GLU A  1  226 ? 124.729 -16.838 28.929  1.00 56.32  ?  226 GLU A O   1 
ATOM   1680  C  CB  . GLU A  1  226 ? 126.178 -14.259 29.596  1.00 48.71  ?  226 GLU A CB  1 
ATOM   1681  C  CG  . GLU A  1  226 ? 126.135 -12.778 29.914  1.00 70.45  ?  226 GLU A CG  1 
ATOM   1682  C  CD  . GLU A  1  226 ? 126.997 -11.929 28.998  1.00 83.97  ?  226 GLU A CD  1 
ATOM   1683  O  OE1 . GLU A  1  226 ? 127.948 -12.477 28.394  1.00 72.74  ?  226 GLU A OE1 1 
ATOM   1684  O  OE2 . GLU A  1  226 ? 126.723 -10.712 28.886  1.00 83.93  ?  226 GLU A OE2 1 
ATOM   1685  N  N   . ARG A  1  227 ? 126.134 -17.446 30.583  1.00 47.37  ?  227 ARG A N   1 
ATOM   1686  C  CA  . ARG A  1  227 ? 126.321 -18.804 30.070  1.00 45.59  ?  227 ARG A CA  1 
ATOM   1687  C  C   . ARG A  1  227 ? 125.864 -19.957 30.966  1.00 54.49  ?  227 ARG A C   1 
ATOM   1688  O  O   . ARG A  1  227 ? 125.680 -21.055 30.444  1.00 53.28  ?  227 ARG A O   1 
ATOM   1689  C  CB  . ARG A  1  227 ? 127.801 -19.017 29.709  1.00 47.99  ?  227 ARG A CB  1 
ATOM   1690  C  CG  . ARG A  1  227 ? 128.435 -17.895 28.874  1.00 56.05  ?  227 ARG A CG  1 
ATOM   1691  C  CD  . ARG A  1  227 ? 127.967 -17.877 27.426  1.00 78.44  ?  227 ARG A CD  1 
ATOM   1692  N  NE  . ARG A  1  227 ? 128.213 -19.152 26.747  1.00 90.37  ?  227 ARG A NE  1 
ATOM   1693  C  CZ  . ARG A  1  227 ? 129.392 -19.550 26.275  1.00 110.64 ?  227 ARG A CZ  1 
ATOM   1694  N  NH1 . ARG A  1  227 ? 130.467 -18.773 26.399  1.00 96.35  ?  227 ARG A NH1 1 
ATOM   1695  N  NH2 . ARG A  1  227 ? 129.510 -20.729 25.674  1.00 119.16 ?  227 ARG A NH2 1 
ATOM   1696  N  N   . VAL A  1  228 ? 125.707 -19.754 32.283  1.00 49.19  ?  228 VAL A N   1 
ATOM   1697  C  CA  . VAL A  1  228 ? 125.265 -20.841 33.170  1.00 42.18  ?  228 VAL A CA  1 
ATOM   1698  C  C   . VAL A  1  228 ? 123.755 -20.676 33.416  1.00 53.02  ?  228 VAL A C   1 
ATOM   1699  O  O   . VAL A  1  228 ? 123.358 -19.749 34.114  1.00 58.35  ?  228 VAL A O   1 
ATOM   1700  C  CB  . VAL A  1  228 ? 126.059 -20.856 34.487  1.00 33.75  ?  228 VAL A CB  1 
ATOM   1701  C  CG1 . VAL A  1  228 ? 125.565 -21.974 35.391  1.00 41.14  ?  228 VAL A CG1 1 
ATOM   1702  C  CG2 . VAL A  1  228 ? 127.550 -21.008 34.217  1.00 42.34  ?  228 VAL A CG2 1 
ATOM   1703  N  N   . PRO A  1  229 ? 122.887 -21.534 32.842  1.00 53.03  ?  229 PRO A N   1 
ATOM   1704  C  CA  . PRO A  1  229 ? 121.435 -21.344 33.028  1.00 50.42  ?  229 PRO A CA  1 
ATOM   1705  C  C   . PRO A  1  229 ? 120.868 -21.802 34.376  1.00 53.83  ?  229 PRO A C   1 
ATOM   1706  O  O   . PRO A  1  229 ? 119.967 -22.636 34.419  1.00 58.63  ?  229 PRO A O   1 
ATOM   1707  C  CB  . PRO A  1  229 ? 120.847 -22.135 31.861  1.00 49.64  ?  229 PRO A CB  1 
ATOM   1708  C  CG  . PRO A  1  229 ? 121.822 -23.250 31.648  1.00 43.03  ?  229 PRO A CG  1 
ATOM   1709  C  CD  . PRO A  1  229 ? 123.174 -22.681 31.955  1.00 50.89  ?  229 PRO A CD  1 
ATOM   1710  N  N   . ALA A  1  230 ? 121.365 -21.235 35.475  1.00 49.79  ?  230 ALA A N   1 
ATOM   1711  C  CA  . ALA A  1  230 ? 120.901 -21.603 36.806  1.00 50.85  ?  230 ALA A CA  1 
ATOM   1712  C  C   . ALA A  1  230 ? 119.892 -20.599 37.368  1.00 50.59  ?  230 ALA A C   1 
ATOM   1713  O  O   . ALA A  1  230 ? 119.833 -19.449 36.932  1.00 48.60  ?  230 ALA A O   1 
ATOM   1714  C  CB  . ALA A  1  230 ? 122.094 -21.726 37.747  1.00 39.28  ?  230 ALA A CB  1 
ATOM   1715  N  N   . PHE A  1  231 ? 119.090 -21.049 38.331  1.00 45.32  ?  231 PHE A N   1 
ATOM   1716  C  CA  . PHE A  1  231 ? 118.096 -20.220 39.007  1.00 43.50  ?  231 PHE A CA  1 
ATOM   1717  C  C   . PHE A  1  231 ? 117.791 -20.840 40.372  1.00 51.96  ?  231 PHE A C   1 
ATOM   1718  O  O   . PHE A  1  231 ? 117.977 -22.045 40.556  1.00 57.15  ?  231 PHE A O   1 
ATOM   1719  C  CB  . PHE A  1  231 ? 116.823 -20.076 38.164  1.00 42.31  ?  231 PHE A CB  1 
ATOM   1720  C  CG  . PHE A  1  231 ? 116.147 -21.382 37.821  1.00 53.06  ?  231 PHE A CG  1 
ATOM   1721  C  CD1 . PHE A  1  231 ? 115.307 -22.005 38.728  1.00 55.10  ?  231 PHE A CD1 1 
ATOM   1722  C  CD2 . PHE A  1  231 ? 116.308 -21.956 36.574  1.00 51.39  ?  231 PHE A CD2 1 
ATOM   1723  C  CE1 . PHE A  1  231 ? 114.688 -23.206 38.412  1.00 54.50  ?  231 PHE A CE1 1 
ATOM   1724  C  CE2 . PHE A  1  231 ? 115.678 -23.150 36.257  1.00 48.76  ?  231 PHE A CE2 1 
ATOM   1725  C  CZ  . PHE A  1  231 ? 114.871 -23.766 37.177  1.00 54.47  ?  231 PHE A CZ  1 
ATOM   1726  N  N   . VAL A  1  232 ? 117.340 -20.031 41.329  1.00 46.22  ?  232 VAL A N   1 
ATOM   1727  C  CA  . VAL A  1  232 ? 117.045 -20.531 42.669  1.00 48.37  ?  232 VAL A CA  1 
ATOM   1728  C  C   . VAL A  1  232 ? 115.542 -20.559 42.905  1.00 49.13  ?  232 VAL A C   1 
ATOM   1729  O  O   . VAL A  1  232 ? 114.828 -19.658 42.481  1.00 45.14  ?  232 VAL A O   1 
ATOM   1730  C  CB  . VAL A  1  232 ? 117.772 -19.692 43.752  1.00 46.97  ?  232 VAL A CB  1 
ATOM   1731  C  CG1 . VAL A  1  232 ? 117.426 -20.176 45.154  1.00 34.32  ?  232 VAL A CG1 1 
ATOM   1732  C  CG2 . VAL A  1  232 ? 119.281 -19.705 43.540  1.00 37.53  ?  232 VAL A CG2 1 
ATOM   1733  N  N   . ASN A  1  233 ? 115.077 -21.635 43.546  1.00 47.79  ?  233 ASN A N   1 
ATOM   1734  C  CA  . ASN A  1  233 ? 113.641 -21.760 43.906  1.00 39.10  ?  233 ASN A CA  1 
ATOM   1735  C  C   . ASN A  1  233 ? 113.584 -21.938 45.423  1.00 48.91  ?  233 ASN A C   1 
ATOM   1736  O  O   . ASN A  1  233 ? 113.677 -23.090 45.880  1.00 50.64  ?  233 ASN A O   1 
ATOM   1737  C  CB  . ASN A  1  233 ? 112.961 -22.902 43.151  1.00 39.36  ?  233 ASN A CB  1 
ATOM   1738  C  CG  . ASN A  1  233 ? 112.502 -22.508 41.764  1.00 59.66  ?  233 ASN A CG  1 
ATOM   1739  O  OD1 . ASN A  1  233 ? 112.998 -21.542 41.189  1.00 71.72  ?  233 ASN A OD1 1 
ATOM   1740  N  ND2 . ASN A  1  233 ? 111.554 -23.252 41.219  1.00 41.20  ?  233 ASN A ND2 1 
ATOM   1741  N  N   . ALA A  1  234 ? 113.462 -20.840 46.169  1.00 41.61  ?  234 ALA A N   1 
ATOM   1742  C  CA  . ALA A  1  234 ? 113.474 -20.886 47.628  1.00 54.70  ?  234 ALA A CA  1 
ATOM   1743  C  C   . ALA A  1  234 ? 112.055 -21.072 48.169  1.00 53.52  ?  234 ALA A C   1 
ATOM   1744  O  O   . ALA A  1  234 ? 111.194 -20.229 47.937  1.00 59.89  ?  234 ALA A O   1 
ATOM   1745  C  CB  . ALA A  1  234 ? 114.099 -19.617 48.184  1.00 48.99  ?  234 ALA A CB  1 
ATOM   1746  N  N   . PHE A  1  235 ? 111.805 -22.177 48.879  1.00 41.19  ?  235 PHE A N   1 
ATOM   1747  C  CA  . PHE A  1  235 ? 110.487 -22.465 49.426  1.00 48.17  ?  235 PHE A CA  1 
ATOM   1748  C  C   . PHE A  1  235 ? 110.473 -22.377 50.953  1.00 65.17  ?  235 PHE A C   1 
ATOM   1749  O  O   . PHE A  1  235 ? 111.503 -22.570 51.601  1.00 62.05  ?  235 PHE A O   1 
ATOM   1750  C  CB  . PHE A  1  235 ? 110.043 -23.864 48.988  1.00 57.30  ?  235 PHE A CB  1 
ATOM   1751  C  CG  . PHE A  1  235 ? 109.840 -24.026 47.503  1.00 46.44  ?  235 PHE A CG  1 
ATOM   1752  C  CD1 . PHE A  1  235 ? 108.769 -23.429 46.866  1.00 49.18  ?  235 PHE A CD1 1 
ATOM   1753  C  CD2 . PHE A  1  235 ? 110.688 -24.823 46.755  1.00 48.24  ?  235 PHE A CD2 1 
ATOM   1754  C  CE1 . PHE A  1  235 ? 108.568 -23.600 45.504  1.00 60.61  ?  235 PHE A CE1 1 
ATOM   1755  C  CE2 . PHE A  1  235 ? 110.482 -24.998 45.394  1.00 56.14  ?  235 PHE A CE2 1 
ATOM   1756  C  CZ  . PHE A  1  235 ? 109.428 -24.381 44.776  1.00 60.76  ?  235 PHE A CZ  1 
ATOM   1757  N  N   . GLY A  1  236 ? 109.302 -22.102 51.520  1.00 61.43  ?  236 GLY A N   1 
ATOM   1758  C  CA  . GLY A  1  236 ? 109.148 -22.007 52.965  1.00 55.98  ?  236 GLY A CA  1 
ATOM   1759  C  C   . GLY A  1  236 ? 109.757 -20.752 53.557  1.00 56.53  ?  236 GLY A C   1 
ATOM   1760  O  O   . GLY A  1  236 ? 110.406 -19.980 52.852  1.00 68.33  ?  236 GLY A O   1 
ATOM   1761  N  N   . PRO A  1  237 ? 109.568 -20.512 54.866  1.00 51.82  ?  237 PRO A N   1 
ATOM   1762  C  CA  . PRO A  1  237 ? 110.124 -19.293 55.479  1.00 53.07  ?  237 PRO A CA  1 
ATOM   1763  C  C   . PRO A  1  237 ? 111.601 -19.047 55.199  1.00 60.58  ?  237 PRO A C   1 
ATOM   1764  O  O   . PRO A  1  237 ? 112.423 -19.942 55.386  1.00 68.21  ?  237 PRO A O   1 
ATOM   1765  C  CB  . PRO A  1  237 ? 109.872 -19.505 56.971  1.00 51.25  ?  237 PRO A CB  1 
ATOM   1766  C  CG  . PRO A  1  237 ? 108.718 -20.418 57.032  1.00 67.79  ?  237 PRO A CG  1 
ATOM   1767  C  CD  . PRO A  1  237 ? 108.817 -21.318 55.846  1.00 54.65  ?  237 PRO A CD  1 
ATOM   1768  N  N   . LEU A  1  238 ? 111.940 -17.828 54.755  1.00 61.43  ?  238 LEU A N   1 
ATOM   1769  C  CA  . LEU A  1  238 ? 113.327 -17.486 54.444  1.00 64.66  ?  238 LEU A CA  1 
ATOM   1770  C  C   . LEU A  1  238 ? 113.945 -16.636 55.539  1.00 60.50  ?  238 LEU A C   1 
ATOM   1771  O  O   . LEU A  1  238 ? 113.413 -15.581 55.880  1.00 62.20  ?  238 LEU A O   1 
ATOM   1772  C  CB  . LEU A  1  238 ? 113.438 -16.739 53.099  1.00 55.42  ?  238 LEU A CB  1 
ATOM   1773  C  CG  . LEU A  1  238 ? 112.693 -17.340 51.914  1.00 64.03  ?  238 LEU A CG  1 
ATOM   1774  C  CD1 . LEU A  1  238 ? 112.697 -16.383 50.736  1.00 49.71  ?  238 LEU A CD1 1 
ATOM   1775  C  CD2 . LEU A  1  238 ? 113.276 -18.676 51.509  1.00 54.34  ?  238 LEU A CD2 1 
ATOM   1776  N  N   . SER A  1  239 ? 115.082 -17.081 56.074  1.00 56.81  ?  239 SER A N   1 
ATOM   1777  C  CA  . SER A  1  239 ? 115.784 -16.333 57.108  1.00 56.90  ?  239 SER A CA  1 
ATOM   1778  C  C   . SER A  1  239 ? 116.581 -15.205 56.454  1.00 60.38  ?  239 SER A C   1 
ATOM   1779  O  O   . SER A  1  239 ? 116.695 -15.165 55.230  1.00 65.96  ?  239 SER A O   1 
ATOM   1780  C  CB  . SER A  1  239 ? 116.733 -17.259 57.864  1.00 69.94  ?  239 SER A CB  1 
ATOM   1781  O  OG  . SER A  1  239 ? 117.814 -17.671 57.043  1.00 84.40  ?  239 SER A OG  1 
ATOM   1782  N  N   . GLU A  1  240 ? 117.156 -14.297 57.255  1.00 64.15  ?  240 GLU A N   1 
ATOM   1783  C  CA  . GLU A  1  240 ? 117.971 -13.209 56.707  1.00 60.20  ?  240 GLU A CA  1 
ATOM   1784  C  C   . GLU A  1  240 ? 119.190 -13.806 55.996  1.00 64.87  ?  240 GLU A C   1 
ATOM   1785  O  O   . GLU A  1  240 ? 119.611 -13.284 54.966  1.00 64.55  ?  240 GLU A O   1 
ATOM   1786  C  CB  . GLU A  1  240 ? 118.429 -12.243 57.813  1.00 71.18  ?  240 GLU A CB  1 
ATOM   1787  C  CG  . GLU A  1  240 ? 117.300 -11.454 58.458  1.00 71.76  ?  240 GLU A CG  1 
ATOM   1788  C  CD  . GLU A  1  240 ? 116.792 -11.987 59.783  1.00 86.72  ?  240 GLU A CD  1 
ATOM   1789  O  OE1 . GLU A  1  240 ? 117.230 -13.082 60.206  1.00 96.11  ?  240 GLU A OE1 1 
ATOM   1790  O  OE2 . GLU A  1  240 ? 115.944 -11.303 60.401  1.00 99.14  ?  240 GLU A OE2 1 
ATOM   1791  N  N   . LEU A  1  241 ? 119.741 -14.909 56.536  1.00 61.10  ?  241 LEU A N   1 
ATOM   1792  C  CA  . LEU A  1  241 ? 120.884 -15.591 55.940  1.00 59.93  ?  241 LEU A CA  1 
ATOM   1793  C  C   . LEU A  1  241 ? 120.510 -16.140 54.562  1.00 62.94  ?  241 LEU A C   1 
ATOM   1794  O  O   . LEU A  1  241 ? 121.290 -16.008 53.624  1.00 65.07  ?  241 LEU A O   1 
ATOM   1795  C  CB  . LEU A  1  241 ? 121.326 -16.748 56.842  1.00 54.82  ?  241 LEU A CB  1 
ATOM   1796  C  CG  . LEU A  1  241 ? 122.596 -17.486 56.405  1.00 50.52  ?  241 LEU A CG  1 
ATOM   1797  C  CD1 . LEU A  1  241 ? 123.816 -16.847 56.999  1.00 64.32  ?  241 LEU A CD1 1 
ATOM   1798  C  CD2 . LEU A  1  241 ? 122.543 -18.938 56.803  1.00 62.86  ?  241 LEU A CD2 1 
ATOM   1799  N  N   . VAL A  1  242 ? 119.324 -16.754 54.438  1.00 61.52  ?  242 VAL A N   1 
ATOM   1800  C  CA  . VAL A  1  242 ? 118.870 -17.310 53.164  1.00 53.59  ?  242 VAL A CA  1 
ATOM   1801  C  C   . VAL A  1  242 ? 118.670 -16.181 52.156  1.00 60.66  ?  242 VAL A C   1 
ATOM   1802  O  O   . VAL A  1  242 ? 119.041 -16.339 50.993  1.00 63.93  ?  242 VAL A O   1 
ATOM   1803  C  CB  . VAL A  1  242 ? 117.586 -18.162 53.335  1.00 58.00  ?  242 VAL A CB  1 
ATOM   1804  C  CG1 . VAL A  1  242 ? 116.933 -18.458 51.986  1.00 47.32  ?  242 VAL A CG1 1 
ATOM   1805  C  CG2 . VAL A  1  242 ? 117.888 -19.460 54.085  1.00 69.64  ?  242 VAL A CG2 1 
ATOM   1806  N  N   . VAL A  1  243 ? 118.104 -15.036 52.590  1.00 63.53  ?  243 VAL A N   1 
ATOM   1807  C  CA  . VAL A  1  243 ? 117.902 -13.887 51.693  1.00 50.37  ?  243 VAL A CA  1 
ATOM   1808  C  C   . VAL A  1  243 ? 119.270 -13.387 51.244  1.00 55.78  ?  243 VAL A C   1 
ATOM   1809  O  O   . VAL A  1  243 ? 119.477 -13.142 50.060  1.00 59.44  ?  243 VAL A O   1 
ATOM   1810  C  CB  . VAL A  1  243 ? 117.075 -12.761 52.354  1.00 44.82  ?  243 VAL A CB  1 
ATOM   1811  C  CG1 . VAL A  1  243 ? 117.064 -11.507 51.487  1.00 37.43  ?  243 VAL A CG1 1 
ATOM   1812  C  CG2 . VAL A  1  243 ? 115.650 -13.228 52.634  1.00 62.50  ?  243 VAL A CG2 1 
ATOM   1813  N  N   . SER A  1  244 ? 120.219 -13.294 52.182  1.00 55.85  ?  244 SER A N   1 
ATOM   1814  C  CA  . SER A  1  244 ? 121.585 -12.879 51.888  1.00 57.53  ?  244 SER A CA  1 
ATOM   1815  C  C   . SER A  1  244 ? 122.219 -13.836 50.863  1.00 58.64  ?  244 SER A C   1 
ATOM   1816  O  O   . SER A  1  244 ? 122.892 -13.390 49.936  1.00 64.33  ?  244 SER A O   1 
ATOM   1817  C  CB  . SER A  1  244 ? 122.406 -12.852 53.173  1.00 55.85  ?  244 SER A CB  1 
ATOM   1818  O  OG  . SER A  1  244 ? 123.718 -12.367 52.946  1.00 67.55  ?  244 SER A OG  1 
ATOM   1819  N  N   . ALA A  1  245 ? 121.982 -15.148 51.017  1.00 56.89  ?  245 ALA A N   1 
ATOM   1820  C  CA  . ALA A  1  245 ? 122.490 -16.157 50.087  1.00 62.91  ?  245 ALA A CA  1 
ATOM   1821  C  C   . ALA A  1  245 ? 121.866 -15.947 48.690  1.00 59.32  ?  245 ALA A C   1 
ATOM   1822  O  O   . ALA A  1  245 ? 122.543 -16.122 47.674  1.00 58.24  ?  245 ALA A O   1 
ATOM   1823  C  CB  . ALA A  1  245 ? 122.163 -17.549 50.606  1.00 53.22  ?  245 ALA A CB  1 
ATOM   1824  N  N   . GLY A  1  246 ? 120.587 -15.572 48.664  1.00 55.82  ?  246 GLY A N   1 
ATOM   1825  C  CA  . GLY A  1  246 ? 119.853 -15.287 47.438  1.00 56.21  ?  246 GLY A CA  1 
ATOM   1826  C  C   . GLY A  1  246 ? 120.458 -14.112 46.701  1.00 56.22  ?  246 GLY A C   1 
ATOM   1827  O  O   . GLY A  1  246 ? 120.472 -14.097 45.470  1.00 52.63  ?  246 GLY A O   1 
ATOM   1828  N  N   . ALA A  1  247 ? 120.974 -13.118 47.448  1.00 52.97  ?  247 ALA A N   1 
ATOM   1829  C  CA  . ALA A  1  247 ? 121.641 -11.964 46.852  1.00 45.91  ?  247 ALA A CA  1 
ATOM   1830  C  C   . ALA A  1  247 ? 122.922 -12.434 46.145  1.00 57.20  ?  247 ALA A C   1 
ATOM   1831  O  O   . ALA A  1  247 ? 123.265 -11.898 45.100  1.00 56.43  ?  247 ALA A O   1 
ATOM   1832  C  CB  . ALA A  1  247 ? 121.980 -10.940 47.920  1.00 43.94  ?  247 ALA A CB  1 
ATOM   1833  N  N   . GLY A  1  248 ? 123.603 -13.436 46.711  1.00 54.64  ?  248 GLY A N   1 
ATOM   1834  C  CA  . GLY A  1  248 ? 124.805 -14.014 46.124  1.00 50.46  ?  248 GLY A CA  1 
ATOM   1835  C  C   . GLY A  1  248 ? 124.477 -14.710 44.817  1.00 58.86  ?  248 GLY A C   1 
ATOM   1836  O  O   . GLY A  1  248 ? 125.239 -14.615 43.853  1.00 54.15  ?  248 GLY A O   1 
ATOM   1837  N  N   . ALA A  1  249 ? 123.323 -15.406 44.762  1.00 53.59  ?  249 ALA A N   1 
ATOM   1838  C  CA  . ALA A  1  249 ? 122.872 -16.068 43.539  1.00 39.57  ?  249 ALA A CA  1 
ATOM   1839  C  C   . ALA A  1  249 ? 122.538 -14.992 42.498  1.00 49.90  ?  249 ALA A C   1 
ATOM   1840  O  O   . ALA A  1  249 ? 122.871 -15.152 41.325  1.00 49.91  ?  249 ALA A O   1 
ATOM   1841  C  CB  . ALA A  1  249 ? 121.643 -16.915 43.825  1.00 39.89  ?  249 ALA A CB  1 
ATOM   1842  N  N   . ILE A  1  250 ? 121.896 -13.887 42.933  1.00 58.40  ?  250 ILE A N   1 
ATOM   1843  C  CA  . ILE A  1  250 ? 121.551 -12.761 42.063  1.00 45.62  ?  250 ILE A CA  1 
ATOM   1844  C  C   . ILE A  1  250 ? 122.842 -12.112 41.553  1.00 46.35  ?  250 ILE A C   1 
ATOM   1845  O  O   . ILE A  1  250 ? 122.891 -11.719 40.389  1.00 58.52  ?  250 ILE A O   1 
ATOM   1846  C  CB  . ILE A  1  250 ? 120.626 -11.742 42.796  1.00 37.88  ?  250 ILE A CB  1 
ATOM   1847  C  CG1 . ILE A  1  250 ? 119.191 -12.296 42.898  1.00 41.37  ?  250 ILE A CG1 1 
ATOM   1848  C  CG2 . ILE A  1  250 ? 120.626 -10.389 42.085  1.00 36.24  ?  250 ILE A CG2 1 
ATOM   1849  C  CD1 . ILE A  1  250 ? 118.299 -11.596 43.874  1.00 37.29  ?  250 ILE A CD1 1 
ATOM   1850  N  N   . ALA A  1  251 ? 123.889 -12.014 42.402  1.00 42.17  ?  251 ALA A N   1 
ATOM   1851  C  CA  . ALA A  1  251 ? 125.184 -11.448 42.016  1.00 45.63  ?  251 ALA A CA  1 
ATOM   1852  C  C   . ALA A  1  251 ? 125.816 -12.251 40.874  1.00 50.05  ?  251 ALA A C   1 
ATOM   1853  O  O   . ALA A  1  251 ? 126.521 -11.672 40.051  1.00 52.50  ?  251 ALA A O   1 
ATOM   1854  C  CB  . ALA A  1  251 ? 126.122 -11.409 43.210  1.00 49.99  ?  251 ALA A CB  1 
ATOM   1855  N  N   . LEU A  1  252 ? 125.555 -13.571 40.803  1.00 50.07  ?  252 LEU A N   1 
ATOM   1856  C  CA  . LEU A  1  252 ? 126.068 -14.400 39.707  1.00 52.87  ?  252 LEU A CA  1 
ATOM   1857  C  C   . LEU A  1  252 ? 125.111 -14.376 38.493  1.00 48.82  ?  252 LEU A C   1 
ATOM   1858  O  O   . LEU A  1  252 ? 125.305 -15.148 37.560  1.00 61.51  ?  252 LEU A O   1 
ATOM   1859  C  CB  . LEU A  1  252 ? 126.240 -15.861 40.145  1.00 46.28  ?  252 LEU A CB  1 
ATOM   1860  C  CG  . LEU A  1  252 ? 126.944 -16.122 41.469  1.00 53.59  ?  252 LEU A CG  1 
ATOM   1861  C  CD1 . LEU A  1  252 ? 126.799 -17.566 41.862  1.00 60.60  ?  252 LEU A CD1 1 
ATOM   1862  C  CD2 . LEU A  1  252 ? 128.413 -15.753 41.404  1.00 43.25  ?  252 LEU A CD2 1 
ATOM   1863  N  N   . GLY A  1  253 ? 124.088 -13.524 38.528  1.00 46.29  ?  253 GLY A N   1 
ATOM   1864  C  CA  . GLY A  1  253 ? 123.100 -13.402 37.467  1.00 50.48  ?  253 GLY A CA  1 
ATOM   1865  C  C   . GLY A  1  253 ? 122.005 -14.451 37.503  1.00 53.56  ?  253 GLY A C   1 
ATOM   1866  O  O   . GLY A  1  253 ? 121.314 -14.637 36.503  1.00 68.54  ?  253 GLY A O   1 
ATOM   1867  N  N   . PHE A  1  254 ? 121.813 -15.136 38.643  1.00 54.66  ?  254 PHE A N   1 
ATOM   1868  C  CA  . PHE A  1  254 ? 120.781 -16.172 38.752  1.00 50.29  ?  254 PHE A CA  1 
ATOM   1869  C  C   . PHE A  1  254 ? 119.494 -15.640 39.409  1.00 46.57  ?  254 PHE A C   1 
ATOM   1870  O  O   . PHE A  1  254 ? 119.545 -15.169 40.545  1.00 45.38  ?  254 PHE A O   1 
ATOM   1871  C  CB  . PHE A  1  254 ? 121.309 -17.369 39.554  1.00 45.03  ?  254 PHE A CB  1 
ATOM   1872  C  CG  . PHE A  1  254 ? 122.574 -18.013 39.033  1.00 48.67  ?  254 PHE A CG  1 
ATOM   1873  C  CD1 . PHE A  1  254 ? 122.861 -18.029 37.675  1.00 49.08  ?  254 PHE A CD1 1 
ATOM   1874  C  CD2 . PHE A  1  254 ? 123.446 -18.655 39.894  1.00 48.71  ?  254 PHE A CD2 1 
ATOM   1875  C  CE1 . PHE A  1  254 ? 124.014 -18.643 37.202  1.00 56.14  ?  254 PHE A CE1 1 
ATOM   1876  C  CE2 . PHE A  1  254 ? 124.597 -19.268 39.416  1.00 34.26  ?  254 PHE A CE2 1 
ATOM   1877  C  CZ  . PHE A  1  254 ? 124.871 -19.263 38.074  1.00 55.52  ?  254 PHE A CZ  1 
ATOM   1878  N  N   . PRO A  1  255 ? 118.323 -15.713 38.737  1.00 45.26  ?  255 PRO A N   1 
ATOM   1879  C  CA  . PRO A  1  255 ? 117.092 -15.216 39.376  1.00 43.81  ?  255 PRO A CA  1 
ATOM   1880  C  C   . PRO A  1  255 ? 116.609 -16.103 40.516  1.00 44.41  ?  255 PRO A C   1 
ATOM   1881  O  O   . PRO A  1  255 ? 116.645 -17.326 40.411  1.00 57.97  ?  255 PRO A O   1 
ATOM   1882  C  CB  . PRO A  1  255 ? 116.062 -15.170 38.241  1.00 50.28  ?  255 PRO A CB  1 
ATOM   1883  C  CG  . PRO A  1  255 ? 116.673 -15.814 37.082  1.00 55.27  ?  255 PRO A CG  1 
ATOM   1884  C  CD  . PRO A  1  255 ? 118.067 -16.242 37.383  1.00 58.20  ?  255 PRO A CD  1 
ATOM   1885  N  N   . VAL A  1  256 ? 116.145 -15.477 41.597  1.00 43.94  ?  256 VAL A N   1 
ATOM   1886  C  CA  . VAL A  1  256 ? 115.642 -16.174 42.770  1.00 49.96  ?  256 VAL A CA  1 
ATOM   1887  C  C   . VAL A  1  256 ? 114.126 -16.068 42.770  1.00 48.22  ?  256 VAL A C   1 
ATOM   1888  O  O   . VAL A  1  256 ? 113.602 -14.959 42.781  1.00 56.72  ?  256 VAL A O   1 
ATOM   1889  C  CB  . VAL A  1  256 ? 116.222 -15.554 44.061  1.00 44.99  ?  256 VAL A CB  1 
ATOM   1890  C  CG1 . VAL A  1  256 ? 115.676 -16.264 45.290  1.00 34.87  ?  256 VAL A CG1 1 
ATOM   1891  C  CG2 . VAL A  1  256 ? 117.749 -15.583 44.054  1.00 43.36  ?  256 VAL A CG2 1 
ATOM   1892  N  N   . LEU A  1  257 ? 113.422 -17.204 42.748  1.00 47.40  ?  257 LEU A N   1 
ATOM   1893  C  CA  . LEU A  1  257 ? 111.963 -17.229 42.763  1.00 44.57  ?  257 LEU A CA  1 
ATOM   1894  C  C   . LEU A  1  257 ? 111.530 -17.920 44.034  1.00 51.69  ?  257 LEU A C   1 
ATOM   1895  O  O   . LEU A  1  257 ? 111.944 -19.047 44.280  1.00 57.85  ?  257 LEU A O   1 
ATOM   1896  C  CB  . LEU A  1  257 ? 111.412 -17.973 41.545  1.00 40.21  ?  257 LEU A CB  1 
ATOM   1897  C  CG  . LEU A  1  257 ? 111.826 -17.399 40.183  1.00 49.10  ?  257 LEU A CG  1 
ATOM   1898  C  CD1 . LEU A  1  257 ? 113.020 -18.146 39.606  1.00 56.22  ?  257 LEU A CD1 1 
ATOM   1899  C  CD2 . LEU A  1  257 ? 110.681 -17.437 39.211  1.00 46.94  ?  257 LEU A CD2 1 
ATOM   1900  N  N   . THR A  1  258 ? 110.709 -17.255 44.844  1.00 52.90  ?  258 THR A N   1 
ATOM   1901  C  CA  . THR A  1  258 ? 110.254 -17.811 46.116  1.00 49.25  ?  258 THR A CA  1 
ATOM   1902  C  C   . THR A  1  258 ? 108.737 -17.804 46.248  1.00 57.05  ?  258 THR A C   1 
ATOM   1903  O  O   . THR A  1  258 ? 108.052 -17.028 45.590  1.00 64.57  ?  258 THR A O   1 
ATOM   1904  C  CB  . THR A  1  258 ? 110.900 -17.038 47.283  1.00 46.87  ?  258 THR A CB  1 
ATOM   1905  O  OG1 . THR A  1  258 ? 110.388 -17.540 48.517  1.00 53.65  ?  258 THR A OG1 1 
ATOM   1906  C  CG2 . THR A  1  258 ? 110.663 -15.535 47.207  1.00 37.12  ?  258 THR A CG2 1 
ATOM   1907  N  N   . ASP A  1  259 ? 108.217 -18.666 47.115  1.00 51.28  ?  259 ASP A N   1 
ATOM   1908  C  CA  . ASP A  1  259 ? 106.783 -18.729 47.383  1.00 55.06  ?  259 ASP A CA  1 
ATOM   1909  C  C   . ASP A  1  259 ? 106.402 -17.770 48.536  1.00 62.83  ?  259 ASP A C   1 
ATOM   1910  O  O   . ASP A  1  259 ? 105.228 -17.699 48.896  1.00 69.26  ?  259 ASP A O   1 
ATOM   1911  C  CB  . ASP A  1  259 ? 106.369 -20.169 47.737  1.00 54.94  ?  259 ASP A CB  1 
ATOM   1912  C  CG  . ASP A  1  259 ? 107.021 -20.739 48.989  1.00 59.48  ?  259 ASP A CG  1 
ATOM   1913  O  OD1 . ASP A  1  259 ? 107.952 -20.094 49.526  1.00 62.13  ?  259 ASP A OD1 1 
ATOM   1914  O  OD2 . ASP A  1  259 ? 106.610 -21.832 49.426  1.00 56.32  ?  259 ASP A OD2 1 
ATOM   1915  N  N   . GLN A  1  260 ? 107.394 -17.047 49.065  1.00 56.72  ?  260 GLN A N   1 
ATOM   1916  C  CA  . GLN A  1  260 ? 107.139 -16.153 50.226  1.00 62.53  ?  260 GLN A CA  1 
ATOM   1917  C  C   . GLN A  1  260 ? 107.074 -14.691 49.775  1.00 56.03  ?  260 GLN A C   1 
ATOM   1918  O  O   . GLN A  1  260 ? 107.630 -14.379 48.705  1.00 55.42  ?  260 GLN A O   1 
ATOM   1919  C  CB  . GLN A  1  260 ? 108.210 -16.367 51.300  1.00 54.32  ?  260 GLN A CB  1 
ATOM   1920  C  CG  . GLN A  1  260 ? 107.663 -16.343 52.722  1.00 75.11  ?  260 GLN A CG  1 
ATOM   1921  C  CD  . GLN A  1  260 ? 107.304 -17.716 53.236  1.00 75.93  ?  260 GLN A CD  1 
ATOM   1922  O  OE1 . GLN A  1  260 ? 107.637 -18.732 52.629  1.00 61.52  ?  260 GLN A OE1 1 
ATOM   1923  N  NE2 . GLN A  1  260 ? 106.617 -17.758 54.368  1.00 114.96 ?  260 GLN A NE2 1 
ATOM   1924  N  N   . VAL A  1  261 ? 106.424 -13.836 50.567  1.00 61.05  ?  261 VAL A N   1 
ATOM   1925  C  CA  . VAL A  1  261 ? 106.268 -12.417 50.257  1.00 54.02  ?  261 VAL A CA  1 
ATOM   1926  C  C   . VAL A  1  261 ? 107.581 -11.707 50.599  1.00 58.96  ?  261 VAL A C   1 
ATOM   1927  O  O   . VAL A  1  261 ? 107.956 -11.627 51.767  1.00 61.25  ?  261 VAL A O   1 
ATOM   1928  C  CB  . VAL A  1  261 ? 105.062 -11.806 51.013  1.00 48.11  ?  261 VAL A CB  1 
ATOM   1929  C  CG1 . VAL A  1  261 ? 105.118 -10.283 51.004  1.00 57.83  ?  261 VAL A CG1 1 
ATOM   1930  C  CG2 . VAL A  1  261 ? 103.745 -12.301 50.420  1.00 55.05  ?  261 VAL A CG2 1 
ATOM   1931  N  N   . VAL A  1  262 ? 108.283 -11.209 49.565  1.00 59.66  ?  262 VAL A N   1 
ATOM   1932  C  CA  . VAL A  1  262 ? 109.568 -10.517 49.712  1.00 61.62  ?  262 VAL A CA  1 
ATOM   1933  C  C   . VAL A  1  262 ? 109.584 -9.252  48.833  1.00 60.97  ?  262 VAL A C   1 
ATOM   1934  O  O   . VAL A  1  262 ? 108.800 -9.187  47.891  1.00 72.18  ?  262 VAL A O   1 
ATOM   1935  C  CB  . VAL A  1  262 ? 110.744 -11.449 49.307  1.00 56.98  ?  262 VAL A CB  1 
ATOM   1936  C  CG1 . VAL A  1  262 ? 110.790 -12.702 50.177  1.00 57.30  ?  262 VAL A CG1 1 
ATOM   1937  C  CG2 . VAL A  1  262 ? 110.681 -11.814 47.823  1.00 38.71  ?  262 VAL A CG2 1 
ATOM   1938  N  N   . PRO A  1  263 ? 110.472 -8.257  49.076  1.00 51.34  ?  263 PRO A N   1 
ATOM   1939  C  CA  . PRO A  1  263 ? 110.511 -7.079  48.190  1.00 56.27  ?  263 PRO A CA  1 
ATOM   1940  C  C   . PRO A  1  263 ? 110.992 -7.468  46.785  1.00 62.15  ?  263 PRO A C   1 
ATOM   1941  O  O   . PRO A  1  263 ? 112.189 -7.501  46.518  1.00 62.63  ?  263 PRO A O   1 
ATOM   1942  C  CB  . PRO A  1  263 ? 111.504 -6.136  48.892  1.00 52.39  ?  263 PRO A CB  1 
ATOM   1943  C  CG  . PRO A  1  263 ? 111.663 -6.680  50.267  1.00 57.10  ?  263 PRO A CG  1 
ATOM   1944  C  CD  . PRO A  1  263 ? 111.490 -8.147  50.136  1.00 55.75  ?  263 PRO A CD  1 
ATOM   1945  N  N   . GLU A  1  264 ? 110.050 -7.774  45.893  1.00 64.31  ?  264 GLU A N   1 
ATOM   1946  C  CA  . GLU A  1  264 ? 110.345 -8.218  44.537  1.00 44.58  ?  264 GLU A CA  1 
ATOM   1947  C  C   . GLU A  1  264 ? 111.173 -7.228  43.736  1.00 51.81  ?  264 GLU A C   1 
ATOM   1948  O  O   . GLU A  1  264 ? 110.934 -6.028  43.807  1.00 72.15  ?  264 GLU A O   1 
ATOM   1949  C  CB  . GLU A  1  264 ? 109.039 -8.483  43.775  1.00 60.03  ?  264 GLU A CB  1 
ATOM   1950  C  CG  . GLU A  1  264 ? 108.292 -9.731  44.206  1.00 61.21  ?  264 GLU A CG  1 
ATOM   1951  C  CD  . GLU A  1  264 ? 107.029 -9.986  43.403  1.00 80.51  ?  264 GLU A CD  1 
ATOM   1952  O  OE1 . GLU A  1  264 ? 107.134 -10.208 42.174  1.00 89.97  ?  264 GLU A OE1 1 
ATOM   1953  O  OE2 . GLU A  1  264 ? 105.931 -9.961  44.003  1.00 92.81  ?  264 GLU A OE2 1 
ATOM   1954  N  N   . VAL A  1  265 ? 112.126 -7.741  42.947  1.00 53.56  ?  265 VAL A N   1 
ATOM   1955  C  CA  . VAL A  1  265 ? 112.967 -6.948  42.054  1.00 59.63  ?  265 VAL A CA  1 
ATOM   1956  C  C   . VAL A  1  265 ? 112.721 -7.558  40.684  1.00 60.97  ?  265 VAL A C   1 
ATOM   1957  O  O   . VAL A  1  265 ? 113.019 -8.739  40.498  1.00 59.94  ?  265 VAL A O   1 
ATOM   1958  C  CB  . VAL A  1  265 ? 114.462 -7.020  42.420  1.00 56.56  ?  265 VAL A CB  1 
ATOM   1959  C  CG1 . VAL A  1  265 ? 115.321 -6.395  41.324  1.00 40.27  ?  265 VAL A CG1 1 
ATOM   1960  C  CG2 . VAL A  1  265 ? 114.722 -6.348  43.759  1.00 42.61  ?  265 VAL A CG2 1 
ATOM   1961  N  N   . PRO A  1  266 ? 112.155 -6.816  39.712  1.00 56.60  ?  266 PRO A N   1 
ATOM   1962  C  CA  . PRO A  1  266 ? 111.886 -7.423  38.396  1.00 48.56  ?  266 PRO A CA  1 
ATOM   1963  C  C   . PRO A  1  266 ? 113.035 -8.246  37.816  1.00 59.55  ?  266 PRO A C   1 
ATOM   1964  O  O   . PRO A  1  266 ? 114.189 -7.827  37.874  1.00 72.03  ?  266 PRO A O   1 
ATOM   1965  C  CB  . PRO A  1  266 ? 111.561 -6.219  37.513  1.00 41.88  ?  266 PRO A CB  1 
ATOM   1966  C  CG  . PRO A  1  266 ? 111.038 -5.202  38.436  1.00 56.46  ?  266 PRO A CG  1 
ATOM   1967  C  CD  . PRO A  1  266 ? 111.722 -5.407  39.756  1.00 56.04  ?  266 PRO A CD  1 
ATOM   1968  N  N   . THR A  1  267 ? 112.708 -9.427  37.259  1.00 57.19  ?  267 THR A N   1 
ATOM   1969  C  CA  . THR A  1  267 ? 113.652 -10.360 36.629  1.00 49.09  ?  267 THR A CA  1 
ATOM   1970  C  C   . THR A  1  267 ? 114.727 -10.937 37.560  1.00 48.82  ?  267 THR A C   1 
ATOM   1971  O  O   . THR A  1  267 ? 115.478 -11.792 37.098  1.00 65.87  ?  267 THR A O   1 
ATOM   1972  C  CB  . THR A  1  267 ? 114.335 -9.738  35.374  1.00 54.78  ?  267 THR A CB  1 
ATOM   1973  O  OG1 . THR A  1  267 ? 115.438 -8.922  35.777  1.00 54.05  ?  267 THR A OG1 1 
ATOM   1974  C  CG2 . THR A  1  267 ? 113.377 -8.915  34.514  1.00 45.08  ?  267 THR A CG2 1 
ATOM   1975  N  N   . LEU A  1  268 ? 114.834 -10.496 38.833  1.00 51.81  ?  268 LEU A N   1 
ATOM   1976  C  CA  . LEU A  1  268 ? 115.882 -11.013 39.724  1.00 51.32  ?  268 LEU A CA  1 
ATOM   1977  C  C   . LEU A  1  268 ? 115.350 -11.676 41.000  1.00 56.77  ?  268 LEU A C   1 
ATOM   1978  O  O   . LEU A  1  268 ? 115.873 -12.712 41.395  1.00 62.10  ?  268 LEU A O   1 
ATOM   1979  C  CB  . LEU A  1  268 ? 116.862 -9.898  40.101  1.00 48.71  ?  268 LEU A CB  1 
ATOM   1980  C  CG  . LEU A  1  268 ? 117.600 -9.222  38.943  1.00 53.08  ?  268 LEU A CG  1 
ATOM   1981  C  CD1 . LEU A  1  268 ? 118.301 -7.965  39.420  1.00 44.31  ?  268 LEU A CD1 1 
ATOM   1982  C  CD2 . LEU A  1  268 ? 118.591 -10.172 38.282  1.00 39.64  ?  268 LEU A CD2 1 
ATOM   1983  N  N   . LEU A  1  269 ? 114.350 -11.082 41.667  1.00 56.67  ?  269 LEU A N   1 
ATOM   1984  C  CA  . LEU A  1  269 ? 113.773 -11.655 42.890  1.00 47.79  ?  269 LEU A CA  1 
ATOM   1985  C  C   . LEU A  1  269 ? 112.260 -11.651 42.712  1.00 50.76  ?  269 LEU A C   1 
ATOM   1986  O  O   . LEU A  1  269 ? 111.665 -10.583 42.641  1.00 60.23  ?  269 LEU A O   1 
ATOM   1987  C  CB  . LEU A  1  269 ? 114.197 -10.836 44.118  1.00 39.72  ?  269 LEU A CB  1 
ATOM   1988  C  CG  . LEU A  1  269 ? 113.679 -11.317 45.474  1.00 52.10  ?  269 LEU A CG  1 
ATOM   1989  C  CD1 . LEU A  1  269 ? 114.129 -12.737 45.772  1.00 45.64  ?  269 LEU A CD1 1 
ATOM   1990  C  CD2 . LEU A  1  269 ? 114.149 -10.395 46.586  1.00 49.39  ?  269 LEU A CD2 1 
ATOM   1991  N  N   . LEU A  1  270 ? 111.637 -12.831 42.590  1.00 44.47  ?  270 LEU A N   1 
ATOM   1992  C  CA  . LEU A  1  270 ? 110.197 -12.914 42.338  1.00 54.83  ?  270 LEU A CA  1 
ATOM   1993  C  C   . LEU A  1  270 ? 109.435 -13.768 43.344  1.00 61.38  ?  270 LEU A C   1 
ATOM   1994  O  O   . LEU A  1  270 ? 110.019 -14.634 43.982  1.00 59.61  ?  270 LEU A O   1 
ATOM   1995  C  CB  . LEU A  1  270 ? 109.963 -13.483 40.931  1.00 49.83  ?  270 LEU A CB  1 
ATOM   1996  C  CG  . LEU A  1  270 ? 110.781 -12.862 39.800  1.00 44.99  ?  270 LEU A CG  1 
ATOM   1997  C  CD1 . LEU A  1  270 ? 110.772 -13.748 38.582  1.00 44.84  ?  270 LEU A CD1 1 
ATOM   1998  C  CD2 . LEU A  1  270 ? 110.274 -11.478 39.460  1.00 54.99  ?  270 LEU A CD2 1 
ATOM   1999  N  N   . THR A  1  271 ? 108.117 -13.534 43.461  1.00 54.93  ?  271 THR A N   1 
ATOM   2000  C  CA  . THR A  1  271 ? 107.244 -14.274 44.373  1.00 53.67  ?  271 THR A CA  1 
ATOM   2001  C  C   . THR A  1  271 ? 106.078 -14.967 43.659  1.00 65.49  ?  271 THR A C   1 
ATOM   2002  O  O   . THR A  1  271 ? 105.135 -14.298 43.240  1.00 73.51  ?  271 THR A O   1 
ATOM   2003  C  CB  . THR A  1  271 ? 106.641 -13.328 45.435  1.00 54.72  ?  271 THR A CB  1 
ATOM   2004  O  OG1 . THR A  1  271 ? 107.655 -12.918 46.358  1.00 62.70  ?  271 THR A OG1 1 
ATOM   2005  C  CG2 . THR A  1  271 ? 105.491 -13.963 46.202  1.00 61.81  ?  271 THR A CG2 1 
ATOM   2006  N  N   . GLN A  1  272 ? 106.144 -16.299 43.518  1.00 57.46  ?  272 GLN A N   1 
ATOM   2007  C  CA  . GLN A  1  272 ? 105.088 -17.094 42.889  1.00 57.02  ?  272 GLN A CA  1 
ATOM   2008  C  C   . GLN A  1  272 ? 104.514 -18.059 43.931  1.00 68.62  ?  272 GLN A C   1 
ATOM   2009  O  O   . GLN A  1  272 ? 105.236 -18.920 44.434  1.00 68.54  ?  272 GLN A O   1 
ATOM   2010  C  CB  . GLN A  1  272 ? 105.696 -17.851 41.697  1.00 40.18  ?  272 GLN A CB  1 
ATOM   2011  C  CG  . GLN A  1  272 ? 104.768 -18.883 41.059  1.00 63.13  ?  272 GLN A CG  1 
ATOM   2012  C  CD  . GLN A  1  272 ? 103.595 -18.266 40.342  1.00 65.95  ?  272 GLN A CD  1 
ATOM   2013  O  OE1 . GLN A  1  272 ? 102.513 -18.075 40.907  1.00 59.31  ?  272 GLN A OE1 1 
ATOM   2014  N  NE2 . GLN A  1  272 ? 103.780 -17.951 39.072  1.00 67.06  ?  272 GLN A NE2 1 
ATOM   2015  N  N   . LYS A  1  273 ? 103.231 -17.908 44.273  1.00 61.14  ?  273 LYS A N   1 
ATOM   2016  C  CA  . LYS A  1  273 ? 102.606 -18.754 45.290  1.00 54.00  ?  273 LYS A CA  1 
ATOM   2017  C  C   . LYS A  1  273 ? 102.017 -20.024 44.680  1.00 68.74  ?  273 LYS A C   1 
ATOM   2018  O  O   . LYS A  1  273 ? 101.949 -21.038 45.369  1.00 86.55  ?  273 LYS A O   1 
ATOM   2019  C  CB  . LYS A  1  273 ? 101.496 -18.006 46.060  1.00 68.86  ?  273 LYS A CB  1 
ATOM   2020  C  CG  . LYS A  1  273 ? 101.939 -16.847 46.955  1.00 61.29  ?  273 LYS A CG  1 
ATOM   2021  C  CD  . LYS A  1  273 ? 100.777 -16.139 47.666  1.00 116.99 ?  273 LYS A CD  1 
ATOM   2022  C  CE  . LYS A  1  273 ? 101.190 -14.999 48.580  1.00 100.62 ?  273 LYS A CE  1 
ATOM   2023  N  NZ  . LYS A  1  273 ? 100.031 -14.321 49.236  1.00 127.29 ?  273 LYS A NZ  1 
ATOM   2024  N  N   . ASP A  1  274 ? 101.562 -19.975 43.414  1.00 69.43  ?  274 ASP A N   1 
ATOM   2025  C  CA  . ASP A  1  274 ? 100.973 -21.147 42.774  1.00 54.30  ?  274 ASP A CA  1 
ATOM   2026  C  C   . ASP A  1  274 ? 102.064 -22.144 42.397  1.00 69.80  ?  274 ASP A C   1 
ATOM   2027  O  O   . ASP A  1  274 ? 102.764 -21.954 41.401  1.00 71.76  ?  274 ASP A O   1 
ATOM   2028  C  CB  . ASP A  1  274 ? 100.162 -20.737 41.535  1.00 62.99  ?  274 ASP A CB  1 
ATOM   2029  C  CG  . ASP A  1  274 ? 99.362  -21.869 40.909  1.00 85.03  ?  274 ASP A CG  1 
ATOM   2030  O  OD1 . ASP A  1  274 ? 99.219  -22.931 41.559  1.00 103.59 ?  274 ASP A OD1 1 
ATOM   2031  O  OD2 . ASP A  1  274 ? 98.868  -21.690 39.775  1.00 85.27  ?  274 ASP A OD2 1 
ATOM   2032  N  N   . TYR A  1  275 ? 102.204 -23.214 43.194  1.00 69.04  ?  275 TYR A N   1 
ATOM   2033  C  CA  . TYR A  1  275 ? 103.223 -24.232 42.954  1.00 60.13  ?  275 TYR A CA  1 
ATOM   2034  C  C   . TYR A  1  275 ? 103.037 -24.908 41.601  1.00 62.07  ?  275 TYR A C   1 
ATOM   2035  O  O   . TYR A  1  275 ? 104.022 -25.272 40.966  1.00 73.06  ?  275 TYR A O   1 
ATOM   2036  C  CB  . TYR A  1  275 ? 103.226 -25.260 44.084  1.00 56.36  ?  275 TYR A CB  1 
ATOM   2037  C  CG  . TYR A  1  275 ? 103.529 -24.652 45.434  1.00 54.88  ?  275 TYR A CG  1 
ATOM   2038  C  CD1 . TYR A  1  275 ? 104.832 -24.382 45.822  1.00 56.62  ?  275 TYR A CD1 1 
ATOM   2039  C  CD2 . TYR A  1  275 ? 102.509 -24.330 46.317  1.00 64.87  ?  275 TYR A CD2 1 
ATOM   2040  C  CE1 . TYR A  1  275 ? 105.115 -23.826 47.064  1.00 63.32  ?  275 TYR A CE1 1 
ATOM   2041  C  CE2 . TYR A  1  275 ? 102.778 -23.771 47.559  1.00 52.41  ?  275 TYR A CE2 1 
ATOM   2042  C  CZ  . TYR A  1  275 ? 104.082 -23.519 47.929  1.00 57.74  ?  275 TYR A CZ  1 
ATOM   2043  O  OH  . TYR A  1  275 ? 104.337 -22.966 49.159  1.00 65.13  ?  275 TYR A OH  1 
ATOM   2044  N  N   . ASP A  1  276 ? 101.790 -25.056 41.140  1.00 58.94  ?  276 ASP A N   1 
ATOM   2045  C  CA  . ASP A  1  276 ? 101.523 -25.671 39.840  1.00 63.91  ?  276 ASP A CA  1 
ATOM   2046  C  C   . ASP A  1  276 ? 102.029 -24.808 38.669  1.00 71.58  ?  276 ASP A C   1 
ATOM   2047  O  O   . ASP A  1  276 ? 101.967 -25.254 37.524  1.00 77.65  ?  276 ASP A O   1 
ATOM   2048  C  CB  . ASP A  1  276 ? 100.019 -25.943 39.677  1.00 65.72  ?  276 ASP A CB  1 
ATOM   2049  C  CG  . ASP A  1  276 ? 99.475  -26.973 40.646  1.00 94.81  ?  276 ASP A CG  1 
ATOM   2050  O  OD1 . ASP A  1  276 ? 100.116 -28.036 40.805  1.00 96.76  ?  276 ASP A OD1 1 
ATOM   2051  O  OD2 . ASP A  1  276 ? 98.405  -26.718 41.245  1.00 97.22  ?  276 ASP A OD2 1 
ATOM   2052  N  N   . LYS A  1  277 ? 102.523 -23.581 38.944  1.00 71.07  ?  277 LYS A N   1 
ATOM   2053  C  CA  . LYS A  1  277 ? 103.046 -22.665 37.923  1.00 66.99  ?  277 LYS A CA  1 
ATOM   2054  C  C   . LYS A  1  277 ? 104.527 -22.314 38.152  1.00 61.53  ?  277 LYS A C   1 
ATOM   2055  O  O   . LYS A  1  277 ? 105.136 -21.711 37.274  1.00 61.43  ?  277 LYS A O   1 
ATOM   2056  C  CB  . LYS A  1  277 ? 102.225 -21.364 37.923  1.00 60.54  ?  277 LYS A CB  1 
ATOM   2057  C  CG  . LYS A  1  277 ? 101.069 -21.332 36.926  1.00 55.99  ?  277 LYS A CG  1 
ATOM   2058  C  CD  . LYS A  1  277 ? 100.614 -19.904 36.575  1.00 79.51  ?  277 LYS A CD  1 
ATOM   2059  C  CE  . LYS A  1  277 ? 100.267 -19.022 37.759  1.00 93.23  ?  277 LYS A CE  1 
ATOM   2060  N  NZ  . LYS A  1  277 ? 98.950  -19.354 38.362  1.00 100.29 ?  277 LYS A NZ  1 
ATOM   2061  N  N   . MET A  1  278 ? 105.102 -22.673 39.316  1.00 55.86  ?  278 MET A N   1 
ATOM   2062  C  CA  . MET A  1  278 ? 106.497 -22.373 39.641  1.00 61.11  ?  278 MET A CA  1 
ATOM   2063  C  C   . MET A  1  278 ? 107.504 -22.865 38.590  1.00 61.85  ?  278 MET A C   1 
ATOM   2064  O  O   . MET A  1  278 ? 108.519 -22.197 38.381  1.00 56.83  ?  278 MET A O   1 
ATOM   2065  C  CB  . MET A  1  278 ? 106.851 -22.950 41.021  1.00 49.32  ?  278 MET A CB  1 
ATOM   2066  C  CG  . MET A  1  278 ? 108.275 -22.671 41.460  1.00 49.46  ?  278 MET A CG  1 
ATOM   2067  S  SD  . MET A  1  278 ? 108.676 -20.913 41.585  1.00 54.17  ?  278 MET A SD  1 
ATOM   2068  C  CE  . MET A  1  278 ? 108.543 -20.682 43.358  1.00 52.42  ?  278 MET A CE  1 
ATOM   2069  N  N   . VAL A  1  279 ? 107.249 -24.010 37.937  1.00 63.64  ?  279 VAL A N   1 
ATOM   2070  C  CA  . VAL A  1  279 ? 108.182 -24.517 36.931  1.00 52.33  ?  279 VAL A CA  1 
ATOM   2071  C  C   . VAL A  1  279 ? 108.185 -23.580 35.714  1.00 56.39  ?  279 VAL A C   1 
ATOM   2072  O  O   . VAL A  1  279 ? 109.241 -23.057 35.362  1.00 64.00  ?  279 VAL A O   1 
ATOM   2073  C  CB  . VAL A  1  279 ? 107.887 -25.983 36.540  1.00 42.65  ?  279 VAL A CB  1 
ATOM   2074  C  CG1 . VAL A  1  279 ? 108.773 -26.428 35.382  1.00 46.28  ?  279 VAL A CG1 1 
ATOM   2075  C  CG2 . VAL A  1  279 ? 108.068 -26.909 37.739  1.00 64.87  ?  279 VAL A CG2 1 
ATOM   2076  N  N   . LYS A  1  280 ? 107.009 -23.333 35.095  1.00 53.32  ?  280 LYS A N   1 
ATOM   2077  C  CA  . LYS A  1  280 ? 106.902 -22.442 33.924  1.00 48.18  ?  280 LYS A CA  1 
ATOM   2078  C  C   . LYS A  1  280 ? 107.440 -21.048 34.247  1.00 59.13  ?  280 LYS A C   1 
ATOM   2079  O  O   . LYS A  1  280 ? 108.050 -20.405 33.392  1.00 63.98  ?  280 LYS A O   1 
ATOM   2080  C  CB  . LYS A  1  280 ? 105.442 -22.316 33.446  1.00 56.46  ?  280 LYS A CB  1 
ATOM   2081  C  CG  . LYS A  1  280 ? 104.890 -23.561 32.761  1.00 69.42  ?  280 LYS A CG  1 
ATOM   2082  C  CD  . LYS A  1  280 ? 103.398 -23.425 32.450  1.00 86.46  ?  280 LYS A CD  1 
ATOM   2083  C  CE  . LYS A  1  280 ? 102.740 -24.759 32.171  1.00 105.97 ?  280 LYS A CE  1 
ATOM   2084  N  NZ  . LYS A  1  280 ? 101.274 -24.630 31.944  1.00 67.48  ?  280 LYS A NZ  1 
ATOM   2085  N  N   . THR A  1  281 ? 107.206 -20.587 35.482  1.00 57.98  ?  281 THR A N   1 
ATOM   2086  C  CA  . THR A  1  281 ? 107.664 -19.283 35.952  1.00 50.61  ?  281 THR A CA  1 
ATOM   2087  C  C   . THR A  1  281 ? 109.193 -19.231 35.956  1.00 53.20  ?  281 THR A C   1 
ATOM   2088  O  O   . THR A  1  281 ? 109.766 -18.289 35.413  1.00 60.84  ?  281 THR A O   1 
ATOM   2089  C  CB  . THR A  1  281 ? 107.123 -19.014 37.369  1.00 56.88  ?  281 THR A CB  1 
ATOM   2090  O  OG1 . THR A  1  281 ? 105.706 -19.182 37.388  1.00 63.23  ?  281 THR A OG1 1 
ATOM   2091  C  CG2 . THR A  1  281 ? 107.473 -17.653 37.865  1.00 48.93  ?  281 THR A CG2 1 
ATOM   2092  N  N   . SER A  1  282 ? 109.852 -20.236 36.564  1.00 51.74  ?  282 SER A N   1 
ATOM   2093  C  CA  . SER A  1  282 ? 111.306 -20.275 36.646  1.00 52.33  ?  282 SER A CA  1 
ATOM   2094  C  C   . SER A  1  282 ? 111.948 -20.418 35.273  1.00 59.21  ?  282 SER A C   1 
ATOM   2095  O  O   . SER A  1  282 ? 112.927 -19.727 34.994  1.00 63.48  ?  282 SER A O   1 
ATOM   2096  C  CB  . SER A  1  282 ? 111.756 -21.414 37.550  1.00 42.17  ?  282 SER A CB  1 
ATOM   2097  O  OG  . SER A  1  282 ? 111.255 -21.241 38.866  1.00 50.51  ?  282 SER A OG  1 
ATOM   2098  N  N   . LEU A  1  283 ? 111.405 -21.284 34.404  1.00 45.30  ?  283 LEU A N   1 
ATOM   2099  C  CA  . LEU A  1  283 ? 111.975 -21.459 33.068  1.00 44.74  ?  283 LEU A CA  1 
ATOM   2100  C  C   . LEU A  1  283 ? 111.909 -20.146 32.292  1.00 57.13  ?  283 LEU A C   1 
ATOM   2101  O  O   . LEU A  1  283 ? 112.862 -19.804 31.602  1.00 58.41  ?  283 LEU A O   1 
ATOM   2102  C  CB  . LEU A  1  283 ? 111.272 -22.575 32.283  1.00 46.44  ?  283 LEU A CB  1 
ATOM   2103  C  CG  . LEU A  1  283 ? 111.237 -23.964 32.937  1.00 55.97  ?  283 LEU A CG  1 
ATOM   2104  C  CD1 . LEU A  1  283 ? 110.439 -24.938 32.087  1.00 57.24  ?  283 LEU A CD1 1 
ATOM   2105  C  CD2 . LEU A  1  283 ? 112.637 -24.509 33.185  1.00 52.88  ?  283 LEU A CD2 1 
ATOM   2106  N  N   . GLU A  1  284 ? 110.811 -19.391 32.429  1.00 59.38  ?  284 GLU A N   1 
ATOM   2107  C  CA  . GLU A  1  284 ? 110.685 -18.101 31.754  1.00 55.11  ?  284 GLU A CA  1 
ATOM   2108  C  C   . GLU A  1  284 ? 111.670 -17.099 32.366  1.00 51.71  ?  284 GLU A C   1 
ATOM   2109  O  O   . GLU A  1  284 ? 112.375 -16.407 31.632  1.00 48.06  ?  284 GLU A O   1 
ATOM   2110  C  CB  . GLU A  1  284 ? 109.250 -17.565 31.881  1.00 44.46  ?  284 GLU A CB  1 
ATOM   2111  C  CG  . GLU A  1  284 ? 109.074 -16.178 31.288  1.00 52.31  ?  284 GLU A CG  1 
ATOM   2112  C  CD  . GLU A  1  284 ? 107.675 -15.618 31.411  1.00 61.22  ?  284 GLU A CD  1 
ATOM   2113  O  OE1 . GLU A  1  284 ? 106.713 -16.419 31.410  1.00 65.01  ?  284 GLU A OE1 1 
ATOM   2114  O  OE2 . GLU A  1  284 ? 107.539 -14.376 31.507  1.00 64.83  ?  284 GLU A OE2 1 
ATOM   2115  N  N   . ALA A  1  285 ? 111.720 -17.028 33.708  1.00 53.10  ?  285 ALA A N   1 
ATOM   2116  C  CA  . ALA A  1  285 ? 112.603 -16.112 34.426  1.00 52.55  ?  285 ALA A CA  1 
ATOM   2117  C  C   . ALA A  1  285 ? 114.071 -16.247 34.027  1.00 50.62  ?  285 ALA A C   1 
ATOM   2118  O  O   . ALA A  1  285 ? 114.813 -15.270 34.123  1.00 51.37  ?  285 ALA A O   1 
ATOM   2119  C  CB  . ALA A  1  285 ? 112.454 -16.317 35.924  1.00 51.49  ?  285 ALA A CB  1 
ATOM   2120  N  N   . ARG A  1  286 ? 114.498 -17.443 33.584  1.00 49.89  ?  286 ARG A N   1 
ATOM   2121  C  CA  . ARG A  1  286 ? 115.883 -17.667 33.172  1.00 51.27  ?  286 ARG A CA  1 
ATOM   2122  C  C   . ARG A  1  286 ? 115.997 -17.953 31.660  1.00 58.69  ?  286 ARG A C   1 
ATOM   2123  O  O   . ARG A  1  286 ? 116.968 -18.563 31.222  1.00 70.55  ?  286 ARG A O   1 
ATOM   2124  C  CB  . ARG A  1  286 ? 116.499 -18.812 34.009  1.00 46.26  ?  286 ARG A CB  1 
ATOM   2125  C  CG  . ARG A  1  286 ? 118.022 -18.988 33.911  1.00 51.85  ?  286 ARG A CG  1 
ATOM   2126  C  CD  . ARG A  1  286 ? 118.795 -17.684 34.002  1.00 55.22  ?  286 ARG A CD  1 
ATOM   2127  N  NE  . ARG A  1  286 ? 120.224 -17.893 34.224  1.00 52.08  ?  286 ARG A NE  1 
ATOM   2128  C  CZ  . ARG A  1  286 ? 121.148 -16.945 34.102  1.00 46.76  ?  286 ARG A CZ  1 
ATOM   2129  N  NH1 . ARG A  1  286 ? 120.804 -15.708 33.766  1.00 55.03  ?  286 ARG A NH1 1 
ATOM   2130  N  NH2 . ARG A  1  286 ? 122.425 -17.225 34.321  1.00 49.91  ?  286 ARG A NH2 1 
ATOM   2131  N  N   . ASN A  1  287 ? 115.020 -17.494 30.865  1.00 61.87  ?  287 ASN A N   1 
ATOM   2132  C  CA  . ASN A  1  287 ? 114.992 -17.668 29.413  1.00 68.70  ?  287 ASN A CA  1 
ATOM   2133  C  C   . ASN A  1  287 ? 115.275 -19.100 28.927  1.00 60.09  ?  287 ASN A C   1 
ATOM   2134  O  O   . ASN A  1  287 ? 115.806 -19.281 27.834  1.00 74.34  ?  287 ASN A O   1 
ATOM   2135  C  CB  . ASN A  1  287 ? 115.952 -16.675 28.755  1.00 57.63  ?  287 ASN A CB  1 
ATOM   2136  C  CG  . ASN A  1  287 ? 115.512 -16.232 27.381  1.00 93.32  ?  287 ASN A CG  1 
ATOM   2137  O  OD1 . ASN A  1  287 ? 114.420 -15.676 27.209  1.00 109.53 ?  287 ASN A OD1 1 
ATOM   2138  N  ND2 . ASN A  1  287 ? 116.341 -16.471 26.369  1.00 109.17 ?  287 ASN A ND2 1 
ATOM   2139  N  N   . ILE A  1  288 ? 114.900 -20.112 29.717  1.00 58.08  ?  288 ILE A N   1 
ATOM   2140  C  CA  . ILE A  1  288 ? 115.092 -21.515 29.345  1.00 62.11  ?  288 ILE A CA  1 
ATOM   2141  C  C   . ILE A  1  288 ? 113.914 -21.923 28.471  1.00 69.21  ?  288 ILE A C   1 
ATOM   2142  O  O   . ILE A  1  288 ? 112.784 -21.953 28.955  1.00 78.97  ?  288 ILE A O   1 
ATOM   2143  C  CB  . ILE A  1  288 ? 115.180 -22.429 30.600  1.00 49.85  ?  288 ILE A CB  1 
ATOM   2144  C  CG1 . ILE A  1  288 ? 116.439 -22.114 31.439  1.00 55.06  ?  288 ILE A CG1 1 
ATOM   2145  C  CG2 . ILE A  1  288 ? 115.171 -23.902 30.187  1.00 55.82  ?  288 ILE A CG2 1 
ATOM   2146  C  CD1 . ILE A  1  288 ? 116.333 -22.479 32.889  1.00 44.12  ?  288 ILE A CD1 1 
ATOM   2147  N  N   . LYS A  1  289 ? 114.159 -22.234 27.194  1.00 86.33  ?  289 LYS A N   1 
ATOM   2148  C  CA  . LYS A  1  289 ? 113.082 -22.649 26.297  1.00 101.82 ?  289 LYS A CA  1 
ATOM   2149  C  C   . LYS A  1  289 ? 113.194 -24.148 26.096  1.00 103.34 ?  289 LYS A C   1 
ATOM   2150  O  O   . LYS A  1  289 ? 114.245 -24.632 25.679  1.00 109.54 ?  289 LYS A O   1 
ATOM   2151  C  CB  . LYS A  1  289 ? 113.143 -21.904 24.945  1.00 100.62 ?  289 LYS A CB  1 
ATOM   2152  C  CG  . LYS A  1  289 ? 113.325 -20.384 25.056  1.00 105.22 ?  289 LYS A CG  1 
ATOM   2153  C  CD  . LYS A  1  289 ? 112.082 -19.647 25.591  1.00 106.29 ?  289 LYS A CD  1 
ATOM   2154  C  CE  . LYS A  1  289 ? 112.405 -18.315 26.248  1.00 114.47 ?  289 LYS A CE  1 
ATOM   2155  N  NZ  . LYS A  1  289 ? 111.794 -18.189 27.604  1.00 95.16  ?  289 LYS A NZ  1 
ATOM   2156  N  N   . ILE A  1  290 ? 112.130 -24.890 26.421  1.00 90.37  ?  290 ILE A N   1 
ATOM   2157  C  CA  . ILE A  1  290 ? 112.139 -26.339 26.266  1.00 108.80 ?  290 ILE A CA  1 
ATOM   2158  C  C   . ILE A  1  290 ? 111.578 -26.680 24.887  1.00 124.78 ?  290 ILE A C   1 
ATOM   2159  O  O   . ILE A  1  290 ? 110.609 -26.060 24.442  1.00 125.31 ?  290 ILE A O   1 
ATOM   2160  C  CB  . ILE A  1  290 ? 111.354 -27.024 27.416  1.00 100.98 ?  290 ILE A CB  1 
ATOM   2161  C  CG1 . ILE A  1  290 ? 111.952 -26.670 28.802  1.00 91.78  ?  290 ILE A CG1 1 
ATOM   2162  C  CG2 . ILE A  1  290 ? 111.291 -28.541 27.213  1.00 113.32 ?  290 ILE A CG2 1 
ATOM   2163  C  CD1 . ILE A  1  290 ? 113.435 -27.041 29.036  1.00 70.67  ?  290 ILE A CD1 1 
ATOM   2164  N  N   . LYS A  1  291 ? 112.195 -27.662 24.208  1.00 133.17 ?  291 LYS A N   1 
ATOM   2165  C  CA  . LYS A  1  291 ? 111.778 -28.082 22.867  1.00 146.16 ?  291 LYS A CA  1 
ATOM   2166  C  C   . LYS A  1  291 ? 110.383 -28.718 22.922  1.00 145.47 ?  291 LYS A C   1 
ATOM   2167  O  O   . LYS A  1  291 ? 109.525 -28.400 22.095  1.00 131.92 ?  291 LYS A O   1 
ATOM   2168  C  CB  . LYS A  1  291 ? 112.798 -29.070 22.255  1.00 154.35 ?  291 LYS A CB  1 
ATOM   2169  C  CG  . LYS A  1  291 ? 114.277 -28.625 22.290  1.00 144.92 ?  291 LYS A CG  1 
ATOM   2170  C  CD  . LYS A  1  291 ? 114.576 -27.247 21.662  1.00 120.98 ?  291 LYS A CD  1 
ATOM   2171  C  CE  . LYS A  1  291 ? 114.398 -27.188 20.159  1.00 136.99 ?  291 LYS A CE  1 
ATOM   2172  N  NZ  . LYS A  1  291 ? 115.292 -28.136 19.439  1.00 131.12 ?  291 LYS A NZ  1 
ATOM   2173  N  N   . ILE A  1  292 ? 110.158 -29.600 23.911  1.00 159.98 ?  292 ILE A N   1 
ATOM   2174  C  CA  . ILE A  1  292 ? 108.874 -30.278 24.101  1.00 158.14 ?  292 ILE A CA  1 
ATOM   2175  C  C   . ILE A  1  292 ? 107.873 -29.271 24.683  1.00 153.24 ?  292 ILE A C   1 
ATOM   2176  O  O   . ILE A  1  292 ? 108.185 -28.591 25.658  1.00 157.55 ?  292 ILE A O   1 
ATOM   2177  C  CB  . ILE A  1  292 ? 109.041 -31.513 25.038  1.00 156.84 ?  292 ILE A CB  1 
ATOM   2178  C  CG1 . ILE A  1  292 ? 110.118 -32.513 24.515  1.00 146.02 ?  292 ILE A CG1 1 
ATOM   2179  C  CG2 . ILE A  1  292 ? 107.698 -32.211 25.282  1.00 150.77 ?  292 ILE A CG2 1 
ATOM   2180  C  CD1 . ILE A  1  292 ? 109.910 -33.103 23.099  1.00 123.42 ?  292 ILE A CD1 1 
ATOM   2181  N  N   . THR A  1  293 ? 106.679 -29.170 24.086  1.00 128.73 ?  293 THR A N   1 
ATOM   2182  C  CA  . THR A  1  293 ? 105.659 -28.236 24.555  1.00 128.83 ?  293 THR A CA  1 
ATOM   2183  C  C   . THR A  1  293 ? 104.420 -29.006 25.006  1.00 123.83 ?  293 THR A C   1 
ATOM   2184  O  O   . THR A  1  293 ? 104.533 -29.954 25.780  1.00 128.19 ?  293 THR A O   1 
ATOM   2185  C  CB  . THR A  1  293 ? 105.336 -27.222 23.450  1.00 131.57 ?  293 THR A CB  1 
ATOM   2186  O  OG1 . THR A  1  293 ? 106.560 -26.665 22.959  1.00 141.14 ?  293 THR A OG1 1 
ATOM   2187  C  CG2 . THR A  1  293 ? 104.418 -26.108 23.928  1.00 130.99 ?  293 THR A CG2 1 
ATOM   2188  N  N   . PRO A  1  296 ? 99.480  -32.196 26.047  1.00 132.90 ?  296 PRO A N   1 
ATOM   2189  C  CA  . PRO A  1  296 ? 98.157  -32.182 26.678  1.00 139.67 ?  296 PRO A CA  1 
ATOM   2190  C  C   . PRO A  1  296 ? 97.141  -32.984 25.854  1.00 154.73 ?  296 PRO A C   1 
ATOM   2191  O  O   . PRO A  1  296 ? 95.976  -32.984 26.207  1.00 157.96 ?  296 PRO A O   1 
ATOM   2192  C  CB  . PRO A  1  296 ? 97.789  -30.695 26.655  1.00 143.15 ?  296 PRO A CB  1 
ATOM   2193  C  CG  . PRO A  1  296 ? 98.342  -30.226 25.336  1.00 139.63 ?  296 PRO A CG  1 
ATOM   2194  C  CD  . PRO A  1  296 ? 99.599  -31.049 25.136  1.00 132.99 ?  296 PRO A CD  1 
ATOM   2195  N  N   . ILE A  1  297 ? 97.601  -33.654 24.783  1.00 168.76 ?  297 ILE A N   1 
ATOM   2196  C  CA  . ILE A  1  297 ? 96.699  -34.416 23.860  1.00 190.66 ?  297 ILE A CA  1 
ATOM   2197  C  C   . ILE A  1  297 ? 97.260  -35.836 23.674  1.00 197.93 ?  297 ILE A C   1 
ATOM   2198  O  O   . ILE A  1  297 ? 98.438  -35.952 23.285  1.00 195.95 ?  297 ILE A O   1 
ATOM   2199  C  CB  . ILE A  1  297 ? 96.554  -33.642 22.525  1.00 195.47 ?  297 ILE A CB  1 
ATOM   2200  C  CG1 . ILE A  1  297 ? 96.122  -34.511 21.336  1.00 206.92 ?  297 ILE A CG1 1 
ATOM   2201  C  CG2 . ILE A  1  297 ? 97.833  -32.877 22.216  1.00 177.08 ?  297 ILE A CG2 1 
ATOM   2202  C  CD1 . ILE A  1  297 ? 95.986  -33.750 20.005  1.00 203.75 ?  297 ILE A CD1 1 
ATOM   2203  N  N   . PRO A  1  298 ? 96.482  -36.917 23.930  1.00 199.40 ?  298 PRO A N   1 
ATOM   2204  C  CA  . PRO A  1  298 ? 96.978  -38.296 23.832  1.00 203.81 ?  298 PRO A CA  1 
ATOM   2205  C  C   . PRO A  1  298 ? 97.644  -38.612 22.485  1.00 210.22 ?  298 PRO A C   1 
ATOM   2206  O  O   . PRO A  1  298 ? 98.625  -39.332 22.486  1.00 226.31 ?  298 PRO A O   1 
ATOM   2207  C  CB  . PRO A  1  298 ? 95.709  -39.154 23.975  1.00 176.37 ?  298 PRO A CB  1 
ATOM   2208  C  CG  . PRO A  1  298 ? 94.567  -38.192 23.728  1.00 169.68 ?  298 PRO A CG  1 
ATOM   2209  C  CD  . PRO A  1  298 ? 95.063  -36.871 24.274  1.00 178.09 ?  298 PRO A CD  1 
ATOM   2210  N  N   . VAL A  1  299 ? 97.110  -38.079 21.384  1.00 199.72 ?  299 VAL A N   1 
ATOM   2211  C  CA  . VAL A  1  299 ? 97.651  -38.429 20.035  1.00 186.35 ?  299 VAL A CA  1 
ATOM   2212  C  C   . VAL A  1  299 ? 98.958  -37.666 19.785  1.00 188.11 ?  299 VAL A C   1 
ATOM   2213  O  O   . VAL A  1  299 ? 99.091  -36.540 20.304  1.00 182.33 ?  299 VAL A O   1 
ATOM   2214  C  CB  . VAL A  1  299 ? 96.611  -38.163 18.930  1.00 174.40 ?  299 VAL A CB  1 
ATOM   2215  C  CG1 . VAL A  1  299 ? 95.274  -37.724 19.507  1.00 187.45 ?  299 VAL A CG1 1 
ATOM   2216  C  CG2 . VAL A  1  299 ? 97.114  -37.154 17.913  1.00 180.46 ?  299 VAL A CG2 1 
ATOM   2217  N  N   . SER A  1  300 ? 99.883  -38.262 19.024  1.00 172.87 ?  300 SER A N   1 
ATOM   2218  C  CA  . SER A  1  300 ? 101.167 -37.625 18.715  1.00 165.53 ?  300 SER A CA  1 
ATOM   2219  C  C   . SER A  1  300 ? 101.024 -36.280 17.989  1.00 164.50 ?  300 SER A C   1 
ATOM   2220  O  O   . SER A  1  300 ? 100.055 -36.063 17.266  1.00 162.59 ?  300 SER A O   1 
ATOM   2221  C  CB  . SER A  1  300 ? 102.036 -38.571 17.891  1.00 144.59 ?  300 SER A CB  1 
ATOM   2222  O  OG  . SER A  1  300 ? 103.382 -38.125 17.832  1.00 151.76 ?  300 SER A OG  1 
ATOM   2223  N  N   . PHE A  1  301 ? 102.006 -35.381 18.192  1.00 175.08 ?  301 PHE A N   1 
ATOM   2224  C  CA  . PHE A  1  301 ? 102.042 -34.045 17.588  1.00 172.00 ?  301 PHE A CA  1 
ATOM   2225  C  C   . PHE A  1  301 ? 103.477 -33.754 17.128  1.00 176.80 ?  301 PHE A C   1 
ATOM   2226  O  O   . PHE A  1  301 ? 104.368 -33.623 17.966  1.00 173.53 ?  301 PHE A O   1 
ATOM   2227  C  CB  . PHE A  1  301 ? 101.591 -32.995 18.622  1.00 160.15 ?  301 PHE A CB  1 
ATOM   2228  C  CG  . PHE A  1  301 ? 101.642 -31.556 18.163  1.00 151.34 ?  301 PHE A CG  1 
ATOM   2229  C  CD1 . PHE A  1  301 ? 102.797 -30.809 18.301  1.00 146.38 ?  301 PHE A CD1 1 
ATOM   2230  C  CD2 . PHE A  1  301 ? 100.516 -30.933 17.662  1.00 153.63 ?  301 PHE A CD2 1 
ATOM   2231  C  CE1 . PHE A  1  301 ? 102.839 -29.482 17.896  1.00 142.69 ?  301 PHE A CE1 1 
ATOM   2232  C  CE2 . PHE A  1  301 ? 100.557 -29.604 17.267  1.00 156.69 ?  301 PHE A CE2 1 
ATOM   2233  C  CZ  . PHE A  1  301 ? 101.717 -28.886 17.389  1.00 147.20 ?  301 PHE A CZ  1 
ATOM   2234  N  N   . ALA A  1  302 ? 103.708 -33.667 15.804  1.00 163.08 ?  302 ALA A N   1 
ATOM   2235  C  CA  . ALA A  1  302 ? 105.047 -33.410 15.260  1.00 143.62 ?  302 ALA A CA  1 
ATOM   2236  C  C   . ALA A  1  302 ? 104.981 -32.998 13.780  1.00 151.52 ?  302 ALA A C   1 
ATOM   2237  O  O   . ALA A  1  302 ? 103.972 -33.233 13.119  1.00 156.77 ?  302 ALA A O   1 
ATOM   2238  C  CB  . ALA A  1  302 ? 105.917 -34.655 15.411  1.00 125.75 ?  302 ALA A CB  1 
ATOM   2239  N  N   . ALA A  1  303 ? 106.064 -32.391 13.258  1.00 173.37 ?  303 ALA A N   1 
ATOM   2240  C  CA  . ALA A  1  303 ? 106.130 -31.968 11.859  1.00 174.01 ?  303 ALA A CA  1 
ATOM   2241  C  C   . ALA A  1  303 ? 106.006 -33.145 10.877  1.00 183.73 ?  303 ALA A C   1 
ATOM   2242  O  O   . ALA A  1  303 ? 105.733 -32.920 9.700   1.00 179.60 ?  303 ALA A O   1 
ATOM   2243  C  CB  . ALA A  1  303 ? 107.427 -31.220 11.605  1.00 162.89 ?  303 ALA A CB  1 
ATOM   2244  N  N   . ALA A  1  304 ? 106.208 -34.390 11.348  1.00 179.27 ?  304 ALA A N   1 
ATOM   2245  C  CA  . ALA A  1  304 ? 106.100 -35.580 10.503  1.00 172.25 ?  304 ALA A CA  1 
ATOM   2246  C  C   . ALA A  1  304 ? 104.662 -35.810 10.019  1.00 168.88 ?  304 ALA A C   1 
ATOM   2247  O  O   . ALA A  1  304 ? 104.465 -36.396 8.955   1.00 172.31 ?  304 ALA A O   1 
ATOM   2248  C  CB  . ALA A  1  304 ? 106.587 -36.801 11.267  1.00 162.74 ?  304 ALA A CB  1 
ATOM   2249  N  N   . PHE A  1  305 ? 103.663 -35.353 10.794  1.00 166.43 ?  305 PHE A N   1 
ATOM   2250  C  CA  . PHE A  1  305 ? 102.251 -35.501 10.438  1.00 159.98 ?  305 PHE A CA  1 
ATOM   2251  C  C   . PHE A  1  305 ? 101.745 -34.303 9.616   1.00 162.61 ?  305 PHE A C   1 
ATOM   2252  O  O   . PHE A  1  305 ? 100.539 -34.063 9.568   1.00 160.13 ?  305 PHE A O   1 
ATOM   2253  C  CB  . PHE A  1  305 ? 101.397 -35.670 11.708  1.00 158.73 ?  305 PHE A CB  1 
ATOM   2254  C  CG  . PHE A  1  305 ? 101.914 -36.736 12.645  1.00 161.61 ?  305 PHE A CG  1 
ATOM   2255  C  CD1 . PHE A  1  305 ? 102.887 -36.444 13.583  1.00 158.32 ?  305 PHE A CD1 1 
ATOM   2256  C  CD2 . PHE A  1  305 ? 101.444 -38.033 12.570  1.00 168.10 ?  305 PHE A CD2 1 
ATOM   2257  C  CE1 . PHE A  1  305 ? 103.377 -37.428 14.429  1.00 149.09 ?  305 PHE A CE1 1 
ATOM   2258  C  CE2 . PHE A  1  305 ? 101.935 -39.016 13.418  1.00 162.96 ?  305 PHE A CE2 1 
ATOM   2259  C  CZ  . PHE A  1  305 ? 102.895 -38.706 14.345  1.00 158.43 ?  305 PHE A CZ  1 
ATOM   2260  N  N   . GLU A  1  306 ? 102.657 -33.557 8.966   1.00 161.80 ?  306 GLU A N   1 
ATOM   2261  C  CA  . GLU A  1  306 ? 102.294 -32.405 8.147   1.00 159.05 ?  306 GLU A CA  1 
ATOM   2262  C  C   . GLU A  1  306 ? 101.725 -32.862 6.799   1.00 158.80 ?  306 GLU A C   1 
ATOM   2263  O  O   . GLU A  1  306 ? 100.800 -32.235 6.284   1.00 163.66 ?  306 GLU A O   1 
ATOM   2264  C  CB  . GLU A  1  306 ? 103.518 -31.497 7.937   1.00 156.71 ?  306 GLU A CB  1 
ATOM   2265  C  CG  . GLU A  1  306 ? 103.182 -30.099 7.442   1.00 157.25 ?  306 GLU A CG  1 
ATOM   2266  C  CD  . GLU A  1  306 ? 104.387 -29.233 7.129   1.00 152.23 ?  306 GLU A CD  1 
ATOM   2267  O  OE1 . GLU A  1  306 ? 105.521 -29.635 7.475   1.00 154.41 ?  306 GLU A OE1 1 
ATOM   2268  O  OE2 . GLU A  1  306 ? 104.195 -28.149 6.533   1.00 144.69 ?  306 GLU A OE2 1 
ATOM   2269  N  N   . GLY A  1  307 ? 102.276 -33.940 6.242   1.00 146.36 ?  307 GLY A N   1 
ATOM   2270  C  CA  . GLY A  1  307 ? 101.832 -34.488 4.965   1.00 133.62 ?  307 GLY A CA  1 
ATOM   2271  C  C   . GLY A  1  307 ? 100.354 -34.825 4.940   1.00 132.54 ?  307 GLY A C   1 
ATOM   2272  O  O   . GLY A  1  307 ? 99.622  -34.336 4.077   1.00 118.03 ?  307 GLY A O   1 
ATOM   2273  N  N   . GLU A  1  308 ? 99.914  -35.631 5.910   1.00 131.50 ?  308 GLU A N   1 
ATOM   2274  C  CA  . GLU A  1  308 ? 98.476  -35.997 6.007   1.00 127.40 ?  308 GLU A CA  1 
ATOM   2275  C  C   . GLU A  1  308 ? 98.215  -36.626 7.380   1.00 122.50 ?  308 GLU A C   1 
ATOM   2276  O  O   . GLU A  1  308 ? 99.101  -36.487 8.246   1.00 125.49 ?  308 GLU A O   1 
ATOM   2277  C  CB  . GLU A  1  308 ? 98.094  -36.954 4.878   1.00 131.41 ?  308 GLU A CB  1 
ATOM   2278  C  CG  . GLU A  1  308 ? 97.000  -36.414 3.976   1.00 129.51 ?  308 GLU A CG  1 
ATOM   2279  C  CD  . GLU A  1  308 ? 96.919  -37.086 2.617   1.00 128.76 ?  308 GLU A CD  1 
ATOM   2280  O  OE1 . GLU A  1  308 ? 96.728  -38.317 2.579   1.00 121.21 ?  308 GLU A OE1 1 
ATOM   2281  O  OE2 . GLU A  1  308 ? 97.050  -36.377 1.600   1.00 134.92 ?  308 GLU A OE2 1 
ATOM   2282  N  N   . ASN A  1  313 ? 92.030  -45.015 4.400   1.00 138.09 ?  313 ASN A N   1 
ATOM   2283  C  CA  . ASN A  1  313 ? 91.394  -44.646 5.662   1.00 155.01 ?  313 ASN A CA  1 
ATOM   2284  C  C   . ASN A  1  313 ? 90.279  -43.624 5.438   1.00 156.66 ?  313 ASN A C   1 
ATOM   2285  O  O   . ASN A  1  313 ? 90.388  -42.773 4.557   1.00 168.94 ?  313 ASN A O   1 
ATOM   2286  C  CB  . ASN A  1  313 ? 92.432  -44.087 6.639   1.00 169.26 ?  313 ASN A CB  1 
ATOM   2287  C  CG  . ASN A  1  313 ? 93.376  -45.129 7.193   1.00 177.19 ?  313 ASN A CG  1 
ATOM   2288  O  OD1 . ASN A  1  313 ? 93.282  -46.322 6.881   1.00 171.56 ?  313 ASN A OD1 1 
ATOM   2289  N  ND2 . ASN A  1  313 ? 94.312  -44.699 8.032   1.00 160.45 ?  313 ASN A ND2 1 
ATOM   2290  N  N   . ASP A  1  314 ? 89.208  -43.709 6.241   1.00 159.28 ?  314 ASP A N   1 
ATOM   2291  C  CA  . ASP A  1  314 ? 88.063  -42.801 6.149   1.00 163.37 ?  314 ASP A CA  1 
ATOM   2292  C  C   . ASP A  1  314 ? 88.081  -41.807 7.328   1.00 157.96 ?  314 ASP A C   1 
ATOM   2293  O  O   . ASP A  1  314 ? 88.920  -41.930 8.221   1.00 146.10 ?  314 ASP A O   1 
ATOM   2294  C  CB  . ASP A  1  314 ? 86.755  -43.615 6.128   1.00 166.64 ?  314 ASP A CB  1 
ATOM   2295  C  CG  . ASP A  1  314 ? 85.526  -42.810 5.754   1.00 163.18 ?  314 ASP A CG  1 
ATOM   2296  O  OD1 . ASP A  1  314 ? 85.589  -42.061 4.754   1.00 146.36 ?  314 ASP A OD1 1 
ATOM   2297  O  OD2 . ASP A  1  314 ? 84.503  -42.926 6.462   1.00 148.39 ?  314 ASP A OD2 1 
ATOM   2298  N  N   . MET A  1  315 ? 87.135  -40.863 7.318   1.00 163.30 ?  315 MET A N   1 
ATOM   2299  C  CA  . MET A  1  315 ? 87.090  -39.824 8.380   1.00 156.61 ?  315 MET A CA  1 
ATOM   2300  C  C   . MET A  1  315 ? 85.866  -40.031 9.274   1.00 154.85 ?  315 MET A C   1 
ATOM   2301  O  O   . MET A  1  315 ? 84.806  -40.414 8.744   1.00 162.56 ?  315 MET A O   1 
ATOM   2302  C  CB  . MET A  1  315 ? 87.023  -38.424 7.762   1.00 161.05 ?  315 MET A CB  1 
ATOM   2303  C  CG  . MET A  1  315 ? 85.959  -38.285 6.693   1.00 155.56 ?  315 MET A CG  1 
ATOM   2304  S  SD  . MET A  1  315 ? 86.548  -37.355 5.257   1.00 163.64 ?  315 MET A SD  1 
ATOM   2305  C  CE  . MET A  1  315 ? 84.996  -36.990 4.441   1.00 147.71 ?  315 MET A CE  1 
ATOM   2306  N  N   . LEU A  1  316 ? 86.015  -39.786 10.575  1.00 154.52 ?  316 LEU A N   1 
ATOM   2307  C  CA  . LEU A  1  316 ? 84.911  -39.896 11.526  1.00 155.78 ?  316 LEU A CA  1 
ATOM   2308  C  C   . LEU A  1  316 ? 83.990  -38.687 11.349  1.00 159.47 ?  316 LEU A C   1 
ATOM   2309  O  O   . LEU A  1  316 ? 82.771  -38.839 11.284  1.00 156.24 ?  316 LEU A O   1 
ATOM   2310  C  CB  . LEU A  1  316 ? 85.474  -39.936 12.965  1.00 147.85 ?  316 LEU A CB  1 
ATOM   2311  C  CG  . LEU A  1  316 ? 84.606  -40.523 14.095  1.00 157.77 ?  316 LEU A CG  1 
ATOM   2312  C  CD1 . LEU A  1  316 ? 83.504  -39.572 14.506  1.00 156.25 ?  316 LEU A CD1 1 
ATOM   2313  C  CD2 . LEU A  1  316 ? 84.046  -41.887 13.740  1.00 162.57 ?  316 LEU A CD2 1 
ATOM   2314  N  N   . ALA A  1  317 ? 84.579  -37.485 11.264  1.00 169.78 ?  317 ALA A N   1 
ATOM   2315  C  CA  . ALA A  1  317 ? 83.825  -36.251 11.094  1.00 166.88 ?  317 ALA A CA  1 
ATOM   2316  C  C   . ALA A  1  317 ? 84.560  -35.318 10.142  1.00 170.34 ?  317 ALA A C   1 
ATOM   2317  O  O   . ALA A  1  317 ? 85.769  -35.131 10.273  1.00 166.30 ?  317 ALA A O   1 
ATOM   2318  C  CB  . ALA A  1  317 ? 83.640  -35.569 12.438  1.00 164.07 ?  317 ALA A CB  1 
ATOM   2319  N  N   . GLU A  1  318 ? 83.832  -34.754 9.177   1.00 166.49 ?  318 GLU A N   1 
ATOM   2320  C  CA  . GLU A  1  318 ? 84.457  -33.757 8.271   1.00 159.48 ?  318 GLU A CA  1 
ATOM   2321  C  C   . GLU A  1  318 ? 83.744  -32.420 8.473   1.00 155.13 ?  318 GLU A C   1 
ATOM   2322  O  O   . GLU A  1  318 ? 82.512  -32.429 8.660   1.00 154.40 ?  318 GLU A O   1 
ATOM   2323  C  CB  . GLU A  1  318 ? 84.367  -34.191 6.809   1.00 154.50 ?  318 GLU A CB  1 
ATOM   2324  C  CG  . GLU A  1  318 ? 84.600  -33.046 5.842   1.00 156.45 ?  318 GLU A CG  1 
ATOM   2325  C  CD  . GLU A  1  318 ? 84.308  -33.408 4.396   1.00 158.49 ?  318 GLU A CD  1 
ATOM   2326  O  OE1 . GLU A  1  318 ? 83.256  -34.027 4.147   1.00 145.24 ?  318 GLU A OE1 1 
ATOM   2327  O  OE2 . GLU A  1  318 ? 85.135  -33.078 3.525   1.00 163.77 ?  318 GLU A OE2 1 
ATOM   2328  N  N   . PHE A  1  319 ? 84.498  -31.322 8.444   1.00 150.14 ?  319 PHE A N   1 
ATOM   2329  C  CA  . PHE A  1  319 ? 83.895  -29.983 8.668   1.00 136.95 ?  319 PHE A CA  1 
ATOM   2330  C  C   . PHE A  1  319 ? 84.436  -28.972 7.657   1.00 132.02 ?  319 PHE A C   1 
ATOM   2331  O  O   . PHE A  1  319 ? 85.664  -28.937 7.448   1.00 128.61 ?  319 PHE A O   1 
ATOM   2332  C  CB  . PHE A  1  319 ? 84.216  -29.448 10.065  1.00 152.85 ?  319 PHE A CB  1 
ATOM   2333  C  CG  . PHE A  1  319 ? 84.098  -30.431 11.201  1.00 160.13 ?  319 PHE A CG  1 
ATOM   2334  C  CD1 . PHE A  1  319 ? 85.113  -31.334 11.466  1.00 150.50 ?  319 PHE A CD1 1 
ATOM   2335  C  CD2 . PHE A  1  319 ? 82.988  -30.429 12.029  1.00 165.37 ?  319 PHE A CD2 1 
ATOM   2336  C  CE1 . PHE A  1  319 ? 85.010  -32.221 12.525  1.00 163.99 ?  319 PHE A CE1 1 
ATOM   2337  C  CE2 . PHE A  1  319 ? 82.882  -31.322 13.083  1.00 162.11 ?  319 PHE A CE2 1 
ATOM   2338  C  CZ  . PHE A  1  319 ? 83.895  -32.218 13.329  1.00 164.92 ?  319 PHE A CZ  1 
ATOM   2339  N  N   . GLY A  1  320 ? 83.550  -28.175 7.056   1.00 137.22 ?  320 GLY A N   1 
ATOM   2340  C  CA  . GLY A  1  320 ? 84.008  -27.095 6.160   1.00 145.42 ?  320 GLY A CA  1 
ATOM   2341  C  C   . GLY A  1  320 ? 83.924  -27.459 4.691   1.00 139.70 ?  320 GLY A C   1 
ATOM   2342  O  O   . GLY A  1  320 ? 82.944  -28.124 4.301   1.00 139.36 ?  320 GLY A O   1 
ATOM   2343  N  N   . GLY A  1  321 ? 84.911  -27.028 3.901   1.00 172.01 ?  321 GLY A N   1 
ATOM   2344  C  CA  . GLY A  1  321 ? 84.919  -27.280 2.470   1.00 170.17 ?  321 GLY A CA  1 
ATOM   2345  C  C   . GLY A  1  321 ? 83.589  -26.891 1.865   1.00 170.77 ?  321 GLY A C   1 
ATOM   2346  O  O   . GLY A  1  321 ? 83.073  -25.810 2.151   1.00 176.20 ?  321 GLY A O   1 
ATOM   2347  N  N   . ASN A  1  322 ? 83.014  -27.772 1.046   1.00 150.67 ?  322 ASN A N   1 
ATOM   2348  C  CA  . ASN A  1  322 ? 81.723  -27.504 0.428   1.00 153.30 ?  322 ASN A CA  1 
ATOM   2349  C  C   . ASN A  1  322 ? 80.635  -28.412 1.017   1.00 147.98 ?  322 ASN A C   1 
ATOM   2350  O  O   . ASN A  1  322 ? 79.684  -28.756 0.319   1.00 153.62 ?  322 ASN A O   1 
ATOM   2351  C  CB  . ASN A  1  322 ? 81.828  -27.706 -1.083  1.00 154.51 ?  322 ASN A CB  1 
ATOM   2352  C  CG  . ASN A  1  322 ? 80.826  -26.914 -1.882  1.00 173.18 ?  322 ASN A CG  1 
ATOM   2353  O  OD1 . ASN A  1  322 ? 80.015  -26.155 -1.339  1.00 181.69 ?  322 ASN A OD1 1 
ATOM   2354  N  ND2 . ASN A  1  322 ? 80.863  -27.071 -3.192  1.00 167.43 ?  322 ASN A ND2 1 
ATOM   2355  N  N   . LYS A  1  323 ? 80.764  -28.787 2.300   1.00 137.76 ?  323 LYS A N   1 
ATOM   2356  C  CA  . LYS A  1  323 ? 79.793  -29.653 2.967   1.00 136.26 ?  323 LYS A CA  1 
ATOM   2357  C  C   . LYS A  1  323 ? 79.153  -28.936 4.165   1.00 155.15 ?  323 LYS A C   1 
ATOM   2358  O  O   . LYS A  1  323 ? 77.930  -28.948 4.296   1.00 147.65 ?  323 LYS A O   1 
ATOM   2359  C  CB  . LYS A  1  323 ? 80.473  -30.957 3.412   1.00 132.90 ?  323 LYS A CB  1 
ATOM   2360  C  CG  . LYS A  1  323 ? 79.499  -32.082 3.729   1.00 138.97 ?  323 LYS A CG  1 
ATOM   2361  C  CD  . LYS A  1  323 ? 80.220  -33.397 3.979   1.00 125.27 ?  323 LYS A CD  1 
ATOM   2362  C  CE  . LYS A  1  323 ? 79.309  -34.435 4.579   1.00 115.35 ?  323 LYS A CE  1 
ATOM   2363  N  NZ  . LYS A  1  323 ? 80.025  -35.707 4.850   1.00 114.09 ?  323 LYS A NZ  1 
ATOM   2364  N  N   . THR A  1  324 ? 79.989  -28.295 4.979   1.00 164.91 ?  324 THR A N   1 
ATOM   2365  C  CA  . THR A  1  324 ? 79.447  -27.523 6.122   1.00 160.26 ?  324 THR A CA  1 
ATOM   2366  C  C   . THR A  1  324 ? 80.171  -26.183 6.203   1.00 159.77 ?  324 THR A C   1 
ATOM   2367  O  O   . THR A  1  324 ? 81.259  -26.053 5.613   1.00 162.34 ?  324 THR A O   1 
ATOM   2368  C  CB  . THR A  1  324 ? 79.568  -28.318 7.421   1.00 163.49 ?  324 THR A CB  1 
ATOM   2369  O  OG1 . THR A  1  324 ? 80.940  -28.656 7.622   1.00 156.61 ?  324 THR A OG1 1 
ATOM   2370  C  CG2 . THR A  1  324 ? 78.727  -29.568 7.359   1.00 157.87 ?  324 THR A CG2 1 
ATOM   2371  N  N   . LYS A  1  325 ? 79.571  -25.215 6.904   1.00 161.73 ?  325 LYS A N   1 
ATOM   2372  C  CA  . LYS A  1  325 ? 80.161  -23.853 6.999   1.00 157.23 ?  325 LYS A CA  1 
ATOM   2373  C  C   . LYS A  1  325 ? 81.086  -23.772 8.215   1.00 165.15 ?  325 LYS A C   1 
ATOM   2374  O  O   . LYS A  1  325 ? 80.581  -23.502 9.322   1.00 170.27 ?  325 LYS A O   1 
ATOM   2375  C  CB  . LYS A  1  325 ? 79.054  -22.800 7.104   1.00 153.05 ?  325 LYS A CB  1 
ATOM   2376  C  CG  . LYS A  1  325 ? 77.931  -22.929 6.083   1.00 149.42 ?  325 LYS A CG  1 
ATOM   2377  C  CD  . LYS A  1  325 ? 76.765  -22.003 6.360   1.00 149.29 ?  325 LYS A CD  1 
ATOM   2378  C  CE  . LYS A  1  325 ? 76.356  -21.985 7.818   1.00 143.88 ?  325 LYS A CE  1 
ATOM   2379  N  NZ  . LYS A  1  325 ? 75.796  -20.672 8.218   1.00 156.76 ?  325 LYS A NZ  1 
ATOM   2380  N  N   . ALA A  1  326 ? 82.386  -23.999 8.016   1.00 178.90 ?  326 ALA A N   1 
ATOM   2381  C  CA  . ALA A  1  326 ? 83.358  -23.850 9.124   1.00 183.65 ?  326 ALA A CA  1 
ATOM   2382  C  C   . ALA A  1  326 ? 84.171  -22.574 8.885   1.00 181.31 ?  326 ALA A C   1 
ATOM   2383  O  O   . ALA A  1  326 ? 84.149  -22.070 7.745   1.00 172.62 ?  326 ALA A O   1 
ATOM   2384  C  CB  . ALA A  1  326 ? 84.244  -25.067 9.207   1.00 189.78 ?  326 ALA A CB  1 
ATOM   2385  N  N   . TRP A  1  327 ? 84.853  -22.072 9.917   1.00 183.37 ?  327 TRP A N   1 
ATOM   2386  C  CA  . TRP A  1  327 ? 85.616  -20.803 9.777   1.00 179.57 ?  327 TRP A CA  1 
ATOM   2387  C  C   . TRP A  1  327 ? 86.663  -20.690 10.889  1.00 180.58 ?  327 TRP A C   1 
ATOM   2388  O  O   . TRP A  1  327 ? 86.439  -21.271 11.970  1.00 189.46 ?  327 TRP A O   1 
ATOM   2389  C  CB  . TRP A  1  327 ? 84.655  -19.610 9.789   1.00 173.92 ?  327 TRP A CB  1 
ATOM   2390  C  CG  . TRP A  1  327 ? 83.826  -19.570 11.032  1.00 181.54 ?  327 TRP A CG  1 
ATOM   2391  C  CD1 . TRP A  1  327 ? 82.709  -20.306 11.302  1.00 187.90 ?  327 TRP A CD1 1 
ATOM   2392  C  CD2 . TRP A  1  327 ? 84.095  -18.804 12.220  1.00 191.61 ?  327 TRP A CD2 1 
ATOM   2393  N  NE1 . TRP A  1  327 ? 82.243  -20.022 12.557  1.00 194.96 ?  327 TRP A NE1 1 
ATOM   2394  C  CE2 . TRP A  1  327 ? 83.074  -19.106 13.145  1.00 191.72 ?  327 TRP A CE2 1 
ATOM   2395  C  CE3 . TRP A  1  327 ? 85.084  -17.883 12.584  1.00 190.54 ?  327 TRP A CE3 1 
ATOM   2396  C  CZ2 . TRP A  1  327 ? 83.019  -18.518 14.407  1.00 189.68 ?  327 TRP A CZ2 1 
ATOM   2397  C  CZ3 . TRP A  1  327 ? 85.028  -17.303 13.831  1.00 185.42 ?  327 TRP A CZ3 1 
ATOM   2398  C  CH2 . TRP A  1  327 ? 84.008  -17.618 14.729  1.00 185.17 ?  327 TRP A CH2 1 
ATOM   2399  N  N   . GLU A  1  328 ? 87.762  -19.977 10.632  1.00 154.32 ?  328 GLU A N   1 
ATOM   2400  C  CA  . GLU A  1  328 ? 88.784  -19.765 11.691  1.00 156.71 ?  328 GLU A CA  1 
ATOM   2401  C  C   . GLU A  1  328 ? 89.064  -18.264 11.817  1.00 165.77 ?  328 GLU A C   1 
ATOM   2402  O  O   . GLU A  1  328 ? 89.003  -17.571 10.786  1.00 168.84 ?  328 GLU A O   1 
ATOM   2403  C  CB  . GLU A  1  328 ? 90.035  -20.597 11.405  1.00 156.42 ?  328 GLU A CB  1 
ATOM   2404  C  CG  . GLU A  1  328 ? 91.022  -19.943 10.461  1.00 163.73 ?  328 GLU A CG  1 
ATOM   2405  C  CD  . GLU A  1  328 ? 92.239  -20.821 10.235  1.00 155.48 ?  328 GLU A CD  1 
ATOM   2406  O  OE1 . GLU A  1  328 ? 92.207  -21.983 10.688  1.00 148.96 ?  328 GLU A OE1 1 
ATOM   2407  O  OE2 . GLU A  1  328 ? 93.211  -20.343 9.618   1.00 150.34 ?  328 GLU A OE2 1 
ATOM   2408  N  N   . LEU A  1  329 ? 89.370  -17.791 13.027  1.00 165.63 ?  329 LEU A N   1 
ATOM   2409  C  CA  . LEU A  1  329 ? 89.547  -16.332 13.260  1.00 160.76 ?  329 LEU A CA  1 
ATOM   2410  C  C   . LEU A  1  329 ? 90.412  -16.089 14.499  1.00 162.95 ?  329 LEU A C   1 
ATOM   2411  O  O   . LEU A  1  329 ? 90.092  -16.658 15.561  1.00 174.64 ?  329 LEU A O   1 
ATOM   2412  C  CB  . LEU A  1  329 ? 88.170  -15.681 13.431  1.00 157.69 ?  329 LEU A CB  1 
ATOM   2413  C  CG  . LEU A  1  329 ? 88.188  -14.265 14.007  1.00 165.87 ?  329 LEU A CG  1 
ATOM   2414  C  CD1 . LEU A  1  329 ? 89.013  -13.333 13.133  1.00 163.44 ?  329 LEU A CD1 1 
ATOM   2415  C  CD2 . LEU A  1  329 ? 86.776  -13.727 14.174  1.00 189.34 ?  329 LEU A CD2 1 
ATOM   2416  N  N   . VAL A  1  330 ? 91.463  -15.275 14.364  1.00 155.97 ?  330 VAL A N   1 
ATOM   2417  C  CA  . VAL A  1  330 ? 92.296  -14.920 15.508  1.00 163.69 ?  330 VAL A CA  1 
ATOM   2418  C  C   . VAL A  1  330 ? 92.095  -13.417 15.695  1.00 177.40 ?  330 VAL A C   1 
ATOM   2419  O  O   . VAL A  1  330 ? 92.522  -12.640 14.845  1.00 178.75 ?  330 VAL A O   1 
ATOM   2420  C  CB  . VAL A  1  330 ? 93.787  -15.266 15.268  1.00 149.74 ?  330 VAL A CB  1 
ATOM   2421  C  CG1 . VAL A  1  330 ? 94.656  -14.770 16.419  1.00 167.75 ?  330 VAL A CG1 1 
ATOM   2422  C  CG2 . VAL A  1  330 ? 93.974  -16.765 15.069  1.00 145.76 ?  330 VAL A CG2 1 
ATOM   2423  N  N   . MET A  1  331 ? 91.476  -13.035 16.815  1.00 205.26 ?  331 MET A N   1 
ATOM   2424  C  CA  . MET A  1  331 ? 91.206  -11.599 17.080  1.00 214.72 ?  331 MET A CA  1 
ATOM   2425  C  C   . MET A  1  331 ? 91.953  -11.154 18.341  1.00 222.06 ?  331 MET A C   1 
ATOM   2426  O  O   . MET A  1  331 ? 91.927  -11.903 19.338  1.00 216.17 ?  331 MET A O   1 
ATOM   2427  C  CB  . MET A  1  331 ? 89.707  -11.361 17.279  1.00 210.92 ?  331 MET A CB  1 
ATOM   2428  C  CG  . MET A  1  331 ? 89.352  -9.906  17.489  1.00 223.50 ?  331 MET A CG  1 
ATOM   2429  S  SD  . MET A  1  331 ? 87.563  -9.663  17.604  1.00 205.01 ?  331 MET A SD  1 
ATOM   2430  C  CE  . MET A  1  331 ? 87.153  -9.431  15.875  1.00 199.48 ?  331 MET A CE  1 
ATOM   2431  N  N   . CYS A  1  332 ? 92.589  -9.982  18.291  1.00 220.78 ?  332 CYS A N   1 
ATOM   2432  C  CA  . CYS A  1  332 ? 93.291  -9.429  19.478  1.00 207.25 ?  332 CYS A CA  1 
ATOM   2433  C  C   . CYS A  1  332 ? 92.366  -8.418  20.162  1.00 211.66 ?  332 CYS A C   1 
ATOM   2434  O  O   . CYS A  1  332 ? 92.072  -7.382  19.537  1.00 214.86 ?  332 CYS A O   1 
ATOM   2435  C  CB  . CYS A  1  332 ? 94.582  -8.736  19.062  1.00 190.96 ?  332 CYS A CB  1 
ATOM   2436  S  SG  . CYS A  1  332 ? 95.265  -7.652  20.344  1.00 244.95 ?  332 CYS A SG  1 
ATOM   2437  N  N   . ALA A  1  333 ? 91.920  -8.712  21.388  1.00 194.76 ?  333 ALA A N   1 
ATOM   2438  C  CA  . ALA A  1  333 ? 90.968  -7.820  22.093  1.00 171.16 ?  333 ALA A CA  1 
ATOM   2439  C  C   . ALA A  1  333 ? 91.142  -7.894  23.612  1.00 175.24 ?  333 ALA A C   1 
ATOM   2440  O  O   . ALA A  1  333 ? 91.079  -9.013  24.155  1.00 194.70 ?  333 ALA A O   1 
ATOM   2441  C  CB  . ALA A  1  333 ? 89.551  -8.203  21.750  1.00 163.75 ?  333 ALA A CB  1 
ATOM   2442  N  N   . ASP A  1  334 ? 91.342  -6.746  24.267  1.00 184.84 ?  334 ASP A N   1 
ATOM   2443  C  CA  . ASP A  1  334 ? 91.577  -6.723  25.736  1.00 207.04 ?  334 ASP A CA  1 
ATOM   2444  C  C   . ASP A  1  334 ? 90.295  -6.976  26.533  1.00 217.65 ?  334 ASP A C   1 
ATOM   2445  O  O   . ASP A  1  334 ? 90.408  -7.333  27.723  1.00 211.67 ?  334 ASP A O   1 
ATOM   2446  C  CB  . ASP A  1  334 ? 92.353  -5.461  26.120  1.00 198.96 ?  334 ASP A CB  1 
ATOM   2447  C  CG  . ASP A  1  334 ? 91.477  -4.222  26.180  1.00 189.70 ?  334 ASP A CG  1 
ATOM   2448  O  OD1 . ASP A  1  334 ? 90.993  -3.797  25.114  1.00 190.66 ?  334 ASP A OD1 1 
ATOM   2449  O  OD2 . ASP A  1  334 ? 91.283  -3.697  27.294  1.00 195.17 ?  334 ASP A OD2 1 
ATOM   2450  N  N   . GLN A  1  335 ? 89.118  -6.812  25.923  1.00 239.11 ?  335 GLN A N   1 
ATOM   2451  C  CA  . GLN A  1  335 ? 87.870  -7.157  26.659  1.00 237.13 ?  335 GLN A CA  1 
ATOM   2452  C  C   . GLN A  1  335 ? 86.776  -7.727  25.751  1.00 240.39 ?  335 GLN A C   1 
ATOM   2453  O  O   . GLN A  1  335 ? 87.109  -8.165  24.634  1.00 241.69 ?  335 GLN A O   1 
ATOM   2454  C  CB  . GLN A  1  335 ? 87.457  -5.857  27.358  1.00 237.55 ?  335 GLN A CB  1 
ATOM   2455  C  CG  . GLN A  1  335 ? 88.403  -5.402  28.458  1.00 233.32 ?  335 GLN A CG  1 
ATOM   2456  C  CD  . GLN A  1  335 ? 87.980  -4.084  29.054  1.00 240.60 ?  335 GLN A CD  1 
ATOM   2457  O  OE1 . GLN A  1  335 ? 87.303  -3.286  28.414  1.00 241.71 ?  335 GLN A OE1 1 
ATOM   2458  N  NE2 . GLN A  1  335 ? 88.384  -3.845  30.291  1.00 260.17 ?  335 GLN A NE2 1 
ATOM   2459  N  N   . GLY A  1  336 ? 85.525  -7.725  26.220  1.00 216.57 ?  336 GLY A N   1 
ATOM   2460  C  CA  . GLY A  1  336 ? 84.420  -8.327  25.448  1.00 206.45 ?  336 GLY A CA  1 
ATOM   2461  C  C   . GLY A  1  336 ? 84.167  -9.772  25.841  1.00 204.69 ?  336 GLY A C   1 
ATOM   2462  O  O   . GLY A  1  336 ? 83.072  -10.279 25.534  1.00 193.31 ?  336 GLY A O   1 
ATOM   2463  N  N   . GLU A  1  337 ? 85.141  -10.410 26.497  1.00 223.70 ?  337 GLU A N   1 
ATOM   2464  C  CA  . GLU A  1  337 ? 85.001  -11.832 26.909  1.00 227.59 ?  337 GLU A CA  1 
ATOM   2465  C  C   . GLU A  1  337 ? 86.097  -12.171 27.924  1.00 230.52 ?  337 GLU A C   1 
ATOM   2466  O  O   . GLU A  1  337 ? 87.017  -11.348 28.091  1.00 227.91 ?  337 GLU A O   1 
ATOM   2467  C  CB  . GLU A  1  337 ? 85.083  -12.745 25.684  1.00 222.15 ?  337 GLU A CB  1 
ATOM   2468  C  CG  . GLU A  1  337 ? 84.591  -14.157 25.942  1.00 215.96 ?  337 GLU A CG  1 
ATOM   2469  C  CD  . GLU A  1  337 ? 85.694  -15.161 26.228  1.00 216.47 ?  337 GLU A CD  1 
ATOM   2470  O  OE1 . GLU A  1  337 ? 86.693  -15.168 25.482  1.00 195.26 ?  337 GLU A OE1 1 
ATOM   2471  O  OE2 . GLU A  1  337 ? 85.555  -15.929 27.201  1.00 210.57 ?  337 GLU A OE2 1 
ATOM   2472  N  N   . VAL A  1  338 ? 86.000  -13.337 28.571  1.00 249.37 ?  338 VAL A N   1 
ATOM   2473  C  CA  . VAL A  1  338 ? 87.056  -13.773 29.532  1.00 244.86 ?  338 VAL A CA  1 
ATOM   2474  C  C   . VAL A  1  338 ? 88.336  -14.055 28.743  1.00 246.51 ?  338 VAL A C   1 
ATOM   2475  O  O   . VAL A  1  338 ? 88.349  -15.031 27.970  1.00 254.46 ?  338 VAL A O   1 
ATOM   2476  C  CB  . VAL A  1  338 ? 86.614  -15.015 30.328  1.00 242.09 ?  338 VAL A CB  1 
ATOM   2477  C  CG1 . VAL A  1  338 ? 87.383  -15.152 31.633  1.00 236.61 ?  338 VAL A CG1 1 
ATOM   2478  C  CG2 . VAL A  1  338 ? 85.115  -15.020 30.582  1.00 239.57 ?  338 VAL A CG2 1 
ATOM   2479  N  N   . GLU A  1  339 ? 89.367  -13.228 28.942  1.00 206.50 ?  339 GLU A N   1 
ATOM   2480  C  CA  . GLU A  1  339 ? 90.670  -13.436 28.258  1.00 188.39 ?  339 GLU A CA  1 
ATOM   2481  C  C   . GLU A  1  339 ? 91.522  -14.387 29.102  1.00 173.29 ?  339 GLU A C   1 
ATOM   2482  O  O   . GLU A  1  339 ? 92.139  -13.916 30.076  1.00 177.99 ?  339 GLU A O   1 
ATOM   2483  C  CB  . GLU A  1  339 ? 91.390  -12.100 28.073  1.00 181.75 ?  339 GLU A CB  1 
ATOM   2484  C  CG  . GLU A  1  339 ? 90.717  -11.192 27.064  1.00 173.07 ?  339 GLU A CG  1 
ATOM   2485  C  CD  . GLU A  1  339 ? 90.256  -11.910 25.809  1.00 180.25 ?  339 GLU A CD  1 
ATOM   2486  O  OE1 . GLU A  1  339 ? 91.117  -12.245 24.971  1.00 185.73 ?  339 GLU A OE1 1 
ATOM   2487  O  OE2 . GLU A  1  339 ? 89.037  -12.139 25.676  1.00 195.27 ?  339 GLU A OE2 1 
ATOM   2488  N  N   . ASP A  1  340 ? 91.548  -15.671 28.739  1.00 169.50 ?  340 ASP A N   1 
ATOM   2489  C  CA  . ASP A  1  340 ? 92.331  -16.672 29.509  1.00 170.71 ?  340 ASP A CA  1 
ATOM   2490  C  C   . ASP A  1  340 ? 92.464  -17.938 28.661  1.00 175.59 ?  340 ASP A C   1 
ATOM   2491  O  O   . ASP A  1  340 ? 92.045  -17.904 27.489  1.00 181.62 ?  340 ASP A O   1 
ATOM   2492  C  CB  . ASP A  1  340 ? 91.671  -16.970 30.855  1.00 181.02 ?  340 ASP A CB  1 
ATOM   2493  C  CG  . ASP A  1  340 ? 90.209  -17.365 30.731  1.00 198.86 ?  340 ASP A CG  1 
ATOM   2494  O  OD1 . ASP A  1  340 ? 89.529  -16.821 29.839  1.00 191.35 ?  340 ASP A OD1 1 
ATOM   2495  O  OD2 . ASP A  1  340 ? 89.764  -18.214 31.527  1.00 203.90 ?  340 ASP A OD2 1 
ATOM   2496  N  N   . HIS A  1  341 ? 93.115  -18.969 29.210  1.00 203.92 ?  341 HIS A N   1 
ATOM   2497  C  CA  . HIS A  1  341 ? 93.264  -20.262 28.489  1.00 221.41 ?  341 HIS A CA  1 
ATOM   2498  C  C   . HIS A  1  341 ? 91.922  -20.944 28.754  1.00 221.53 ?  341 HIS A C   1 
ATOM   2499  O  O   . HIS A  1  341 ? 91.873  -21.991 29.434  1.00 211.28 ?  341 HIS A O   1 
ATOM   2500  C  CB  . HIS A  1  341 ? 94.437  -21.072 29.050  1.00 220.44 ?  341 HIS A CB  1 
ATOM   2501  C  CG  . HIS A  1  341 ? 94.905  -22.171 28.153  1.00 242.51 ?  341 HIS A CG  1 
ATOM   2502  N  ND1 . HIS A  1  341 ? 94.045  -23.007 27.473  1.00 251.32 ?  341 HIS A ND1 1 
ATOM   2503  C  CD2 . HIS A  1  341 ? 96.141  -22.573 27.830  1.00 244.19 ?  341 HIS A CD2 1 
ATOM   2504  C  CE1 . HIS A  1  341 ? 94.749  -23.878 26.765  1.00 245.93 ?  341 HIS A CE1 1 
ATOM   2505  N  NE2 . HIS A  1  341 ? 96.024  -23.633 26.967  1.00 250.16 ?  341 HIS A NE2 1 
ATOM   2506  N  N   . LYS A  1  342 ? 90.850  -20.346 28.232  1.00 204.27 ?  342 LYS A N   1 
ATOM   2507  C  CA  . LYS A  1  342 ? 89.496  -20.908 28.458  1.00 181.92 ?  342 LYS A CA  1 
ATOM   2508  C  C   . LYS A  1  342 ? 89.425  -21.847 27.253  1.00 193.70 ?  342 LYS A C   1 
ATOM   2509  O  O   . LYS A  1  342 ? 89.395  -21.331 26.119  1.00 191.10 ?  342 LYS A O   1 
ATOM   2510  C  CB  . LYS A  1  342 ? 88.418  -19.821 28.490  1.00 170.10 ?  342 LYS A CB  1 
ATOM   2511  C  CG  . LYS A  1  342 ? 87.008  -20.311 28.789  1.00 180.13 ?  342 LYS A CG  1 
ATOM   2512  C  CD  . LYS A  1  342 ? 85.991  -19.193 28.856  1.00 188.29 ?  342 LYS A CD  1 
ATOM   2513  C  CE  . LYS A  1  342 ? 84.587  -19.686 29.130  1.00 190.77 ?  342 LYS A CE  1 
ATOM   2514  N  NZ  . LYS A  1  342 ? 83.617  -18.568 29.189  1.00 208.91 ?  342 LYS A NZ  1 
ATOM   2515  N  N   . ILE A  1  343 ? 89.475  -23.161 27.489  1.00 212.33 ?  343 ILE A N   1 
ATOM   2516  C  CA  . ILE A  1  343 ? 89.250  -24.137 26.383  1.00 207.03 ?  343 ILE A CA  1 
ATOM   2517  C  C   . ILE A  1  343 ? 87.750  -24.418 26.441  1.00 222.24 ?  343 ILE A C   1 
ATOM   2518  O  O   . ILE A  1  343 ? 87.318  -25.062 27.416  1.00 237.94 ?  343 ILE A O   1 
ATOM   2519  C  CB  . ILE A  1  343 ? 90.098  -25.409 26.565  1.00 213.18 ?  343 ILE A CB  1 
ATOM   2520  C  CG1 . ILE A  1  343 ? 91.567  -25.077 26.833  1.00 199.41 ?  343 ILE A CG1 1 
ATOM   2521  C  CG2 . ILE A  1  343 ? 89.938  -26.333 25.369  1.00 194.21 ?  343 ILE A CG2 1 
ATOM   2522  C  CD1 . ILE A  1  343 ? 92.078  -25.591 28.158  1.00 212.61 ?  343 ILE A CD1 1 
ATOM   2523  N  N   . GLU A  1  344 ? 87.000  -23.871 25.479  1.00 199.37 ?  344 GLU A N   1 
ATOM   2524  C  CA  . GLU A  1  344 ? 85.520  -23.992 25.515  1.00 201.86 ?  344 GLU A CA  1 
ATOM   2525  C  C   . GLU A  1  344 ? 84.994  -24.550 24.192  1.00 194.40 ?  344 GLU A C   1 
ATOM   2526  O  O   . GLU A  1  344 ? 85.432  -24.065 23.130  1.00 185.52 ?  344 GLU A O   1 
ATOM   2527  C  CB  . GLU A  1  344 ? 84.898  -22.625 25.805  1.00 185.13 ?  344 GLU A CB  1 
ATOM   2528  C  CG  . GLU A  1  344 ? 83.382  -22.631 25.775  1.00 182.52 ?  344 GLU A CG  1 
ATOM   2529  C  CD  . GLU A  1  344 ? 82.748  -21.317 26.193  1.00 176.65 ?  344 GLU A CD  1 
ATOM   2530  O  OE1 . GLU A  1  344 ? 83.358  -20.261 25.936  1.00 173.49 ?  344 GLU A OE1 1 
ATOM   2531  O  OE2 . GLU A  1  344 ? 81.646  -21.352 26.775  1.00 193.67 ?  344 GLU A OE2 1 
ATOM   2532  N  N   . VAL A  1  345 ? 84.091  -25.526 24.264  1.00 197.63 ?  345 VAL A N   1 
ATOM   2533  C  CA  . VAL A  1  345 ? 83.474  -26.122 23.081  1.00 184.21 ?  345 VAL A CA  1 
ATOM   2534  C  C   . VAL A  1  345 ? 81.966  -25.885 23.198  1.00 189.08 ?  345 VAL A C   1 
ATOM   2535  O  O   . VAL A  1  345 ? 81.346  -26.412 24.120  1.00 191.02 ?  345 VAL A O   1 
ATOM   2536  C  CB  . VAL A  1  345 ? 83.788  -27.635 22.986  1.00 168.84 ?  345 VAL A CB  1 
ATOM   2537  C  CG1 . VAL A  1  345 ? 83.012  -28.280 21.844  1.00 173.86 ?  345 VAL A CG1 1 
ATOM   2538  C  CG2 . VAL A  1  345 ? 85.286  -27.879 22.824  1.00 152.77 ?  345 VAL A CG2 1 
ATOM   2539  N  N   . ILE A  1  346 ? 81.374  -25.090 22.290  1.00 184.91 ?  346 ILE A N   1 
ATOM   2540  C  CA  . ILE A  1  346 ? 79.938  -24.810 22.340  1.00 185.75 ?  346 ILE A CA  1 
ATOM   2541  C  C   . ILE A  1  346 ? 79.233  -25.404 21.117  1.00 177.81 ?  346 ILE A C   1 
ATOM   2542  O  O   . ILE A  1  346 ? 79.119  -24.746 20.082  1.00 169.72 ?  346 ILE A O   1 
ATOM   2543  C  CB  . ILE A  1  346 ? 79.652  -23.286 22.480  1.00 184.11 ?  346 ILE A CB  1 
ATOM   2544  C  CG1 . ILE A  1  346 ? 80.496  -22.661 23.611  1.00 185.95 ?  346 ILE A CG1 1 
ATOM   2545  C  CG2 . ILE A  1  346 ? 78.155  -23.042 22.724  1.00 186.00 ?  346 ILE A CG2 1 
ATOM   2546  C  CD1 . ILE A  1  346 ? 80.621  -21.151 23.540  1.00 178.61 ?  346 ILE A CD1 1 
ATOM   2547  N  N   . GLY A  1  347 ? 78.764  -26.641 21.251  1.00 194.18 ?  347 GLY A N   1 
ATOM   2548  C  CA  . GLY A  1  347 ? 78.051  -27.330 20.184  1.00 188.74 ?  347 GLY A CA  1 
ATOM   2549  C  C   . GLY A  1  347 ? 78.105  -28.841 20.295  1.00 194.74 ?  347 GLY A C   1 
ATOM   2550  O  O   . GLY A  1  347 ? 78.834  -29.377 21.132  1.00 198.00 ?  347 GLY A O   1 
ATOM   2551  N  N   . PRO A  1  348 ? 77.341  -29.574 19.459  1.00 190.51 ?  348 PRO A N   1 
ATOM   2552  C  CA  . PRO A  1  348 ? 77.379  -31.043 19.542  1.00 182.10 ?  348 PRO A CA  1 
ATOM   2553  C  C   . PRO A  1  348 ? 78.789  -31.599 19.365  1.00 182.13 ?  348 PRO A C   1 
ATOM   2554  O  O   . PRO A  1  348 ? 79.436  -31.322 18.362  1.00 183.73 ?  348 PRO A O   1 
ATOM   2555  C  CB  . PRO A  1  348 ? 76.452  -31.495 18.408  1.00 170.70 ?  348 PRO A CB  1 
ATOM   2556  C  CG  . PRO A  1  348 ? 75.605  -30.327 18.098  1.00 168.44 ?  348 PRO A CG  1 
ATOM   2557  C  CD  . PRO A  1  348 ? 76.415  -29.112 18.407  1.00 183.50 ?  348 PRO A CD  1 
ATOM   2558  N  N   . ASP A  1  349 ? 79.269  -32.372 20.340  1.00 194.57 ?  349 ASP A N   1 
ATOM   2559  C  CA  . ASP A  1  349 ? 80.609  -32.949 20.280  1.00 190.76 ?  349 ASP A CA  1 
ATOM   2560  C  C   . ASP A  1  349 ? 80.712  -34.033 19.188  1.00 190.30 ?  349 ASP A C   1 
ATOM   2561  O  O   . ASP A  1  349 ? 79.692  -34.485 18.667  1.00 196.15 ?  349 ASP A O   1 
ATOM   2562  C  CB  . ASP A  1  349 ? 80.990  -33.514 21.658  1.00 197.86 ?  349 ASP A CB  1 
ATOM   2563  C  CG  . ASP A  1  349 ? 81.255  -32.451 22.700  1.00 204.92 ?  349 ASP A CG  1 
ATOM   2564  O  OD1 . ASP A  1  349 ? 81.427  -31.279 22.314  1.00 205.38 ?  349 ASP A OD1 1 
ATOM   2565  O  OD2 . ASP A  1  349 ? 81.290  -32.794 23.901  1.00 212.95 ?  349 ASP A OD2 1 
ATOM   2566  N  N   . ILE A  1  350 ? 81.936  -34.462 18.880  1.00 174.78 ?  350 ILE A N   1 
ATOM   2567  C  CA  . ILE A  1  350 ? 82.119  -35.458 17.783  1.00 162.21 ?  350 ILE A CA  1 
ATOM   2568  C  C   . ILE A  1  350 ? 81.581  -36.824 18.236  1.00 172.61 ?  350 ILE A C   1 
ATOM   2569  O  O   . ILE A  1  350 ? 81.058  -37.559 17.376  1.00 162.44 ?  350 ILE A O   1 
ATOM   2570  C  CB  . ILE A  1  350 ? 83.592  -35.506 17.329  1.00 150.06 ?  350 ILE A CB  1 
ATOM   2571  C  CG1 . ILE A  1  350 ? 83.916  -34.326 16.409  1.00 150.74 ?  350 ILE A CG1 1 
ATOM   2572  C  CG2 . ILE A  1  350 ? 83.923  -36.839 16.679  1.00 157.56 ?  350 ILE A CG2 1 
ATOM   2573  C  CD1 . ILE A  1  350 ? 85.341  -34.310 15.910  1.00 150.19 ?  350 ILE A CD1 1 
ATOM   2574  N  N   . ASP A  1  351 ? 81.676  -37.147 19.527  1.00 185.65 ?  351 ASP A N   1 
ATOM   2575  C  CA  . ASP A  1  351 ? 81.231  -38.484 20.006  1.00 178.20 ?  351 ASP A CA  1 
ATOM   2576  C  C   . ASP A  1  351 ? 79.789  -38.737 19.549  1.00 176.81 ?  351 ASP A C   1 
ATOM   2577  O  O   . ASP A  1  351 ? 79.443  -39.914 19.331  1.00 180.38 ?  351 ASP A O   1 
ATOM   2578  C  CB  . ASP A  1  351 ? 81.388  -38.611 21.523  1.00 165.90 ?  351 ASP A CB  1 
ATOM   2579  C  CG  . ASP A  1  351 ? 82.769  -39.087 21.938  1.00 169.15 ?  351 ASP A CG  1 
ATOM   2580  O  OD1 . ASP A  1  351 ? 83.727  -38.836 21.180  1.00 168.79 ?  351 ASP A OD1 1 
ATOM   2581  O  OD2 . ASP A  1  351 ? 82.876  -39.703 23.017  1.00 152.52 ?  351 ASP A OD2 1 
ATOM   2582  N  N   . THR A  1  352 ? 78.986  -37.679 19.401  1.00 173.74 ?  352 THR A N   1 
ATOM   2583  C  CA  . THR A  1  352 ? 77.581  -37.812 19.001  1.00 167.43 ?  352 THR A CA  1 
ATOM   2584  C  C   . THR A  1  352 ? 77.467  -38.489 17.621  1.00 170.95 ?  352 THR A C   1 
ATOM   2585  O  O   . THR A  1  352 ? 76.500  -39.207 17.368  1.00 176.56 ?  352 THR A O   1 
ATOM   2586  C  CB  . THR A  1  352 ? 76.910  -36.427 18.976  1.00 148.26 ?  352 THR A CB  1 
ATOM   2587  O  OG1 . THR A  1  352 ? 77.164  -35.763 20.216  1.00 154.76 ?  352 THR A OG1 1 
ATOM   2588  C  CG2 . THR A  1  352 ? 75.410  -36.504 18.734  1.00 143.81 ?  352 THR A CG2 1 
ATOM   2589  N  N   . ILE A  1  353 ? 78.450  -38.257 16.735  1.00 170.91 ?  353 ILE A N   1 
ATOM   2590  C  CA  . ILE A  1  353 ? 78.463  -38.830 15.386  1.00 170.12 ?  353 ILE A CA  1 
ATOM   2591  C  C   . ILE A  1  353 ? 78.567  -40.362 15.438  1.00 180.59 ?  353 ILE A C   1 
ATOM   2592  O  O   . ILE A  1  353 ? 79.405  -40.901 16.162  1.00 174.27 ?  353 ILE A O   1 
ATOM   2593  C  CB  . ILE A  1  353 ? 79.609  -38.187 14.540  1.00 161.41 ?  353 ILE A CB  1 
ATOM   2594  C  CG1 . ILE A  1  353 ? 79.257  -36.723 14.172  1.00 162.46 ?  353 ILE A CG1 1 
ATOM   2595  C  CG2 . ILE A  1  353 ? 79.893  -39.000 13.274  1.00 159.69 ?  353 ILE A CG2 1 
ATOM   2596  C  CD1 . ILE A  1  353 ? 80.438  -35.833 13.899  1.00 170.64 ?  353 ILE A CD1 1 
ATOM   2597  N  N   . ASP A  1  354 ? 77.706  -41.055 14.669  1.00 189.18 ?  354 ASP A N   1 
ATOM   2598  C  CA  . ASP A  1  354 ? 77.676  -42.518 14.598  1.00 180.44 ?  354 ASP A CA  1 
ATOM   2599  C  C   . ASP A  1  354 ? 78.190  -43.028 13.238  1.00 174.74 ?  354 ASP A C   1 
ATOM   2600  O  O   . ASP A  1  354 ? 78.743  -44.122 13.174  1.00 180.28 ?  354 ASP A O   1 
ATOM   2601  C  CB  . ASP A  1  354 ? 76.250  -43.029 14.857  1.00 175.12 ?  354 ASP A CB  1 
ATOM   2602  C  CG  . ASP A  1  354 ? 75.675  -42.567 16.181  1.00 191.19 ?  354 ASP A CG  1 
ATOM   2603  O  OD1 . ASP A  1  354 ? 76.388  -42.660 17.203  1.00 190.24 ?  354 ASP A OD1 1 
ATOM   2604  O  OD2 . ASP A  1  354 ? 74.510  -42.112 16.196  1.00 191.67 ?  354 ASP A OD2 1 
ATOM   2605  N  N   . LYS A  1  355 ? 78.007  -42.243 12.159  1.00 159.01 ?  355 LYS A N   1 
ATOM   2606  C  CA  . LYS A  1  355 ? 78.463  -42.608 10.813  1.00 136.18 ?  355 LYS A CA  1 
ATOM   2607  C  C   . LYS A  1  355 ? 79.145  -41.408 10.148  1.00 135.31 ?  355 LYS A C   1 
ATOM   2608  O  O   . LYS A  1  355 ? 78.782  -40.268 10.425  1.00 146.73 ?  355 LYS A O   1 
ATOM   2609  C  CB  . LYS A  1  355 ? 77.281  -43.080 9.952   1.00 132.99 ?  355 LYS A CB  1 
ATOM   2610  C  CG  . LYS A  1  355 ? 76.860  -44.522 10.213  1.00 149.02 ?  355 LYS A CG  1 
ATOM   2611  C  CD  . LYS A  1  355 ? 75.652  -44.921 9.370   1.00 159.24 ?  355 LYS A CD  1 
ATOM   2612  C  CE  . LYS A  1  355 ? 75.023  -46.210 9.844   1.00 166.02 ?  355 LYS A CE  1 
ATOM   2613  N  NZ  . LYS A  1  355 ? 73.796  -46.546 9.073   1.00 127.49 ?  355 LYS A NZ  1 
ATOM   2614  N  N   . ALA A  1  356 ? 80.123  -41.667 9.259   1.00 140.62 ?  356 ALA A N   1 
ATOM   2615  C  CA  . ALA A  1  356 ? 80.888  -40.630 8.548   1.00 154.21 ?  356 ALA A CA  1 
ATOM   2616  C  C   . ALA A  1  356 ? 80.044  -39.435 8.085   1.00 145.70 ?  356 ALA A C   1 
ATOM   2617  O  O   . ALA A  1  356 ? 80.277  -38.308 8.522   1.00 124.00 ?  356 ALA A O   1 
ATOM   2618  C  CB  . ALA A  1  356 ? 81.599  -41.244 7.353   1.00 129.45 ?  356 ALA A CB  1 
ATOM   2619  N  N   . MET A  1  360 ? 79.383  -31.521 9.971   1.00 163.35 ?  360 MET A N   1 
ATOM   2620  C  CA  . MET A  1  360 ? 79.175  -30.550 11.078  1.00 169.07 ?  360 MET A CA  1 
ATOM   2621  C  C   . MET A  1  360 ? 80.069  -29.330 10.850  1.00 173.08 ?  360 MET A C   1 
ATOM   2622  O  O   . MET A  1  360 ? 81.068  -29.463 10.121  1.00 172.11 ?  360 MET A O   1 
ATOM   2623  C  CB  . MET A  1  360 ? 79.532  -31.180 12.427  1.00 171.57 ?  360 MET A CB  1 
ATOM   2624  C  CG  . MET A  1  360 ? 79.318  -32.678 12.469  1.00 172.92 ?  360 MET A CG  1 
ATOM   2625  S  SD  . MET A  1  360 ? 77.708  -33.107 13.173  1.00 208.36 ?  360 MET A SD  1 
ATOM   2626  C  CE  . MET A  1  360 ? 77.569  -31.860 14.452  1.00 170.39 ?  360 MET A CE  1 
ATOM   2627  N  N   . PRO A  1  361 ? 79.754  -28.150 11.425  1.00 230.84 ?  361 PRO A N   1 
ATOM   2628  C  CA  . PRO A  1  361 ? 80.632  -26.986 11.309  1.00 229.27 ?  361 PRO A CA  1 
ATOM   2629  C  C   . PRO A  1  361 ? 81.766  -27.064 12.341  1.00 233.39 ?  361 PRO A C   1 
ATOM   2630  O  O   . PRO A  1  361 ? 81.712  -27.927 13.198  1.00 234.48 ?  361 PRO A O   1 
ATOM   2631  C  CB  . PRO A  1  361 ? 79.690  -25.823 11.641  1.00 229.55 ?  361 PRO A CB  1 
ATOM   2632  C  CG  . PRO A  1  361 ? 78.719  -26.422 12.635  1.00 231.47 ?  361 PRO A CG  1 
ATOM   2633  C  CD  . PRO A  1  361 ? 78.540  -27.860 12.193  1.00 232.23 ?  361 PRO A CD  1 
ATOM   2634  N  N   . LEU A  1  362 ? 82.757  -26.179 12.236  1.00 200.77 ?  362 LEU A N   1 
ATOM   2635  C  CA  . LEU A  1  362 ? 83.879  -26.181 13.210  1.00 197.51 ?  362 LEU A CA  1 
ATOM   2636  C  C   . LEU A  1  362 ? 84.360  -24.744 13.416  1.00 190.29 ?  362 LEU A C   1 
ATOM   2637  O  O   . LEU A  1  362 ? 85.386  -24.375 12.811  1.00 184.43 ?  362 LEU A O   1 
ATOM   2638  C  CB  . LEU A  1  362 ? 85.007  -27.064 12.669  1.00 197.12 ?  362 LEU A CB  1 
ATOM   2639  C  CG  . LEU A  1  362 ? 85.988  -27.587 13.716  1.00 191.16 ?  362 LEU A CG  1 
ATOM   2640  C  CD1 . LEU A  1  362 ? 85.274  -28.458 14.738  1.00 195.54 ?  362 LEU A CD1 1 
ATOM   2641  C  CD2 . LEU A  1  362 ? 87.120  -28.360 13.058  1.00 186.17 ?  362 LEU A CD2 1 
ATOM   2642  N  N   . GLY A  1  363 ? 83.643  -23.962 14.227  1.00 185.91 ?  363 GLY A N   1 
ATOM   2643  C  CA  . GLY A  1  363 ? 84.044  -22.549 14.368  1.00 167.43 ?  363 GLY A CA  1 
ATOM   2644  C  C   . GLY A  1  363 ? 85.247  -22.420 15.282  1.00 153.50 ?  363 GLY A C   1 
ATOM   2645  O  O   . GLY A  1  363 ? 85.280  -23.125 16.308  1.00 155.09 ?  363 GLY A O   1 
ATOM   2646  N  N   . MET A  1  364 ? 86.204  -21.558 14.934  1.00 144.79 ?  364 MET A N   1 
ATOM   2647  C  CA  . MET A  1  364 ? 87.445  -21.453 15.747  1.00 140.75 ?  364 MET A CA  1 
ATOM   2648  C  C   . MET A  1  364 ? 87.773  -19.979 16.007  1.00 150.77 ?  364 MET A C   1 
ATOM   2649  O  O   . MET A  1  364 ? 88.490  -19.384 15.180  1.00 157.30 ?  364 MET A O   1 
ATOM   2650  C  CB  . MET A  1  364 ? 88.618  -22.128 15.030  1.00 136.90 ?  364 MET A CB  1 
ATOM   2651  C  CG  . MET A  1  364 ? 88.365  -23.590 14.714  1.00 137.77 ?  364 MET A CG  1 
ATOM   2652  S  SD  . MET A  1  364 ? 89.873  -24.484 14.263  1.00 130.19 ?  364 MET A SD  1 
ATOM   2653  C  CE  . MET A  1  364 ? 90.755  -24.452 15.822  1.00 118.36 ?  364 MET A CE  1 
ATOM   2654  N  N   . LEU A  1  365 ? 87.270  -19.420 17.112  1.00 144.35 ?  365 LEU A N   1 
ATOM   2655  C  CA  . LEU A  1  365 ? 87.576  -18.035 17.463  1.00 141.71 ?  365 LEU A CA  1 
ATOM   2656  C  C   . LEU A  1  365 ? 88.615  -18.003 18.577  1.00 148.66 ?  365 LEU A C   1 
ATOM   2657  O  O   . LEU A  1  365 ? 88.342  -18.456 19.687  1.00 155.53 ?  365 LEU A O   1 
ATOM   2658  C  CB  . LEU A  1  365 ? 86.301  -17.299 17.905  1.00 133.58 ?  365 LEU A CB  1 
ATOM   2659  C  CG  . LEU A  1  365 ? 86.463  -15.881 18.465  1.00 144.22 ?  365 LEU A CG  1 
ATOM   2660  C  CD1 . LEU A  1  365 ? 87.255  -14.979 17.516  1.00 150.53 ?  365 LEU A CD1 1 
ATOM   2661  C  CD2 . LEU A  1  365 ? 85.107  -15.268 18.750  1.00 160.05 ?  365 LEU A CD2 1 
ATOM   2662  N  N   . ILE A  1  366 ? 89.803  -17.465 18.277  1.00 156.68 ?  366 ILE A N   1 
ATOM   2663  C  CA  . ILE A  1  366 ? 90.899  -17.363 19.239  1.00 176.59 ?  366 ILE A CA  1 
ATOM   2664  C  C   . ILE A  1  366 ? 91.055  -15.904 19.657  1.00 176.28 ?  366 ILE A C   1 
ATOM   2665  O  O   . ILE A  1  366 ? 91.034  -15.021 18.803  1.00 174.58 ?  366 ILE A O   1 
ATOM   2666  C  CB  . ILE A  1  366 ? 92.204  -17.928 18.615  1.00 168.81 ?  366 ILE A CB  1 
ATOM   2667  C  CG1 . ILE A  1  366 ? 92.041  -19.437 18.270  1.00 151.12 ?  366 ILE A CG1 1 
ATOM   2668  C  CG2 . ILE A  1  366 ? 93.404  -17.702 19.547  1.00 171.89 ?  366 ILE A CG2 1 
ATOM   2669  C  CD1 . ILE A  1  366 ? 91.648  -19.748 16.817  1.00 140.19 ?  366 ILE A CD1 1 
ATOM   2670  N  N   . LYS A  1  367 ? 91.233  -15.683 20.963  1.00 171.87 ?  367 LYS A N   1 
ATOM   2671  C  CA  . LYS A  1  367 ? 91.357  -14.296 21.483  1.00 178.16 ?  367 LYS A CA  1 
ATOM   2672  C  C   . LYS A  1  367 ? 92.666  -14.152 22.263  1.00 194.81 ?  367 LYS A C   1 
ATOM   2673  O  O   . LYS A  1  367 ? 92.887  -14.949 23.195  1.00 195.89 ?  367 LYS A O   1 
ATOM   2674  C  CB  . LYS A  1  367 ? 90.125  -13.938 22.319  1.00 185.16 ?  367 LYS A CB  1 
ATOM   2675  C  CG  . LYS A  1  367 ? 88.847  -13.756 21.511  1.00 178.00 ?  367 LYS A CG  1 
ATOM   2676  C  CD  . LYS A  1  367 ? 88.130  -12.456 21.804  1.00 175.71 ?  367 LYS A CD  1 
ATOM   2677  C  CE  . LYS A  1  367 ? 86.652  -12.644 22.073  1.00 168.85 ?  367 LYS A CE  1 
ATOM   2678  N  NZ  . LYS A  1  367 ? 86.373  -13.958 22.700  1.00 167.55 ?  367 LYS A NZ  1 
ATOM   2679  N  N   . VAL A  1  368 ? 93.497  -13.183 21.872  1.00 197.56 ?  368 VAL A N   1 
ATOM   2680  C  CA  . VAL A  1  368 ? 94.772  -12.929 22.605  1.00 193.68 ?  368 VAL A CA  1 
ATOM   2681  C  C   . VAL A  1  368 ? 95.001  -11.426 22.779  1.00 182.49 ?  368 VAL A C   1 
ATOM   2682  O  O   . VAL A  1  368 ? 94.998  -10.708 21.763  1.00 200.24 ?  368 VAL A O   1 
ATOM   2683  C  CB  . VAL A  1  368 ? 95.978  -13.578 21.901  1.00 187.42 ?  368 VAL A CB  1 
ATOM   2684  C  CG1 . VAL A  1  368 ? 95.804  -15.088 21.824  1.00 197.11 ?  368 VAL A CG1 1 
ATOM   2685  C  CG2 . VAL A  1  368 ? 96.206  -12.990 20.517  1.00 173.72 ?  368 VAL A CG2 1 
ATOM   2686  N  N   . SER A  1  369 ? 95.185  -10.979 24.020  1.00 175.39 ?  369 SER A N   1 
ATOM   2687  C  CA  . SER A  1  369 ? 95.347  -9.555  24.319  1.00 169.51 ?  369 SER A CA  1 
ATOM   2688  C  C   . SER A  1  369 ? 96.625  -9.220  25.092  1.00 183.47 ?  369 SER A C   1 
ATOM   2689  O  O   . SER A  1  369 ? 96.630  -8.275  25.878  1.00 220.23 ?  369 SER A O   1 
ATOM   2690  C  CB  . SER A  1  369 ? 94.124  -9.079  25.098  1.00 187.38 ?  369 SER A CB  1 
ATOM   2691  O  OG  . SER A  1  369 ? 94.205  -9.401  26.477  1.00 176.57 ?  369 SER A OG  1 
ATOM   2692  N  N   . GLY A  1  370 ? 97.695  -9.973  24.861  1.00 175.79 ?  370 GLY A N   1 
ATOM   2693  C  CA  . GLY A  1  370 ? 98.964  -9.719  25.531  1.00 205.61 ?  370 GLY A CA  1 
ATOM   2694  C  C   . GLY A  1  370 ? 99.616  -8.443  25.030  1.00 206.35 ?  370 GLY A C   1 
ATOM   2695  O  O   . GLY A  1  370 ? 99.263  -7.943  23.959  1.00 181.23 ?  370 GLY A O   1 
ATOM   2696  N  N   . THR A  1  371 ? 100.568 -7.899  25.799  1.00 194.79 ?  371 THR A N   1 
ATOM   2697  C  CA  . THR A  1  371 ? 101.258 -6.661  25.420  1.00 200.25 ?  371 THR A CA  1 
ATOM   2698  C  C   . THR A  1  371 ? 101.980 -6.786  24.076  1.00 202.07 ?  371 THR A C   1 
ATOM   2699  O  O   . THR A  1  371 ? 102.380 -7.883  23.683  1.00 191.21 ?  371 THR A O   1 
ATOM   2700  C  CB  . THR A  1  371 ? 102.246 -6.226  26.526  1.00 192.24 ?  371 THR A CB  1 
ATOM   2701  O  OG1 . THR A  1  371 ? 102.688 -4.889  26.270  1.00 195.83 ?  371 THR A OG1 1 
ATOM   2702  C  CG2 . THR A  1  371 ? 103.459 -7.150  26.633  1.00 191.60 ?  371 THR A CG2 1 
ATOM   2703  N  N   . ASN A  1  372 ? 102.141 -5.650  23.375  1.00 212.78 ?  372 ASN A N   1 
ATOM   2704  C  CA  . ASN A  1  372 ? 102.830 -5.581  22.086  1.00 221.85 ?  372 ASN A CA  1 
ATOM   2705  C  C   . ASN A  1  372 ? 102.134 -6.396  20.987  1.00 227.68 ?  372 ASN A C   1 
ATOM   2706  O  O   . ASN A  1  372 ? 102.805 -7.046  20.188  1.00 226.72 ?  372 ASN A O   1 
ATOM   2707  C  CB  . ASN A  1  372 ? 104.287 -6.034  22.259  1.00 213.57 ?  372 ASN A CB  1 
ATOM   2708  C  CG  . ASN A  1  372 ? 105.284 -5.370  21.338  1.00 230.10 ?  372 ASN A CG  1 
ATOM   2709  O  OD1 . ASN A  1  372 ? 105.053 -4.279  20.805  1.00 249.88 ?  372 ASN A OD1 1 
ATOM   2710  N  ND2 . ASN A  1  372 ? 106.429 -6.015  21.136  1.00 239.02 ?  372 ASN A ND2 1 
ATOM   2711  N  N   . MET A  1  373 ? 100.796 -6.351  20.930  1.00 204.11 ?  373 MET A N   1 
ATOM   2712  C  CA  . MET A  1  373 ? 100.048 -7.085  19.912  1.00 185.15 ?  373 MET A CA  1 
ATOM   2713  C  C   . MET A  1  373 ? 99.302  -6.104  19.004  1.00 183.01 ?  373 MET A C   1 
ATOM   2714  O  O   . MET A  1  373 ? 98.357  -5.452  19.446  1.00 189.67 ?  373 MET A O   1 
ATOM   2715  C  CB  . MET A  1  373 ? 99.070  -8.072  20.577  1.00 186.67 ?  373 MET A CB  1 
ATOM   2716  C  CG  . MET A  1  373 ? 98.561  -9.153  19.647  1.00 176.46 ?  373 MET A CG  1 
ATOM   2717  S  SD  . MET A  1  373 ? 99.888  -10.192 18.987  1.00 182.16 ?  373 MET A SD  1 
ATOM   2718  C  CE  . MET A  1  373 ? 98.988  -11.646 18.591  1.00 162.01 ?  373 MET A CE  1 
ATOM   2719  N  N   . GLN A  1  374 ? 99.731  -5.996  17.733  1.00 189.11 ?  374 GLN A N   1 
ATOM   2720  C  CA  . GLN A  1  374 ? 99.109  -5.087  16.764  1.00 181.72 ?  374 GLN A CA  1 
ATOM   2721  C  C   . GLN A  1  374 ? 97.911  -5.750  16.086  1.00 186.79 ?  374 GLN A C   1 
ATOM   2722  O  O   . GLN A  1  374 ? 97.858  -6.974  15.988  1.00 196.70 ?  374 GLN A O   1 
ATOM   2723  C  CB  . GLN A  1  374 ? 100.129 -4.638  15.701  1.00 172.95 ?  374 GLN A CB  1 
ATOM   2724  C  CG  . GLN A  1  374 ? 101.364 -3.949  16.274  1.00 174.35 ?  374 GLN A CG  1 
ATOM   2725  C  CD  . GLN A  1  374 ? 102.328 -3.485  15.206  1.00 191.98 ?  374 GLN A CD  1 
ATOM   2726  O  OE1 . GLN A  1  374 ? 102.233 -3.856  14.030  1.00 206.44 ?  374 GLN A OE1 1 
ATOM   2727  N  NE2 . GLN A  1  374 ? 103.291 -2.659  15.594  1.00 172.35 ?  374 GLN A NE2 1 
ATOM   2728  N  N   . LYS A  1  375 ? 96.952  -4.945  15.611  1.00 174.98 ?  375 LYS A N   1 
ATOM   2729  C  CA  . LYS A  1  375 ? 95.756  -5.462  14.946  1.00 168.13 ?  375 LYS A CA  1 
ATOM   2730  C  C   . LYS A  1  375 ? 96.008  -6.035  13.546  1.00 176.24 ?  375 LYS A C   1 
ATOM   2731  O  O   . LYS A  1  375 ? 95.153  -6.738  13.009  1.00 177.87 ?  375 LYS A O   1 
ATOM   2732  C  CB  . LYS A  1  375 ? 94.768  -4.315  14.677  1.00 156.25 ?  375 LYS A CB  1 
ATOM   2733  C  CG  . LYS A  1  375 ? 94.168  -3.703  15.935  1.00 163.65 ?  375 LYS A CG  1 
ATOM   2734  C  CD  . LYS A  1  375 ? 93.223  -2.563  15.601  1.00 170.55 ?  375 LYS A CD  1 
ATOM   2735  C  CE  . LYS A  1  375 ? 92.602  -1.962  16.834  1.00 182.68 ?  375 LYS A CE  1 
ATOM   2736  N  NZ  . LYS A  1  375 ? 91.698  -0.833  16.502  1.00 175.31 ?  375 LYS A NZ  1 
ATOM   2737  N  N   . ASP A  1  376 ? 97.180  -5.742  12.961  1.00 189.02 ?  376 ASP A N   1 
ATOM   2738  C  CA  . ASP A  1  376 ? 97.535  -6.231  11.628  1.00 190.25 ?  376 ASP A CA  1 
ATOM   2739  C  C   . ASP A  1  376 ? 98.570  -7.366  11.807  1.00 186.41 ?  376 ASP A C   1 
ATOM   2740  O  O   . ASP A  1  376 ? 99.157  -7.814  10.822  1.00 181.84 ?  376 ASP A O   1 
ATOM   2741  C  CB  . ASP A  1  376 ? 98.092  -5.138  10.702  1.00 207.38 ?  376 ASP A CB  1 
ATOM   2742  C  CG  . ASP A  1  376 ? 97.024  -4.211  10.158  1.00 207.41 ?  376 ASP A CG  1 
ATOM   2743  O  OD1 . ASP A  1  376 ? 95.827  -4.563  10.254  1.00 198.64 ?  376 ASP A OD1 1 
ATOM   2744  O  OD2 . ASP A  1  376 ? 97.384  -3.135  9.632   1.00 211.31 ?  376 ASP A OD2 1 
ATOM   2745  N  N   . PHE A  1  377 ? 98.799  -7.774  13.060  1.00 170.76 ?  377 PHE A N   1 
ATOM   2746  C  CA  . PHE A  1  377 ? 99.743  -8.884  13.350  1.00 170.69 ?  377 PHE A CA  1 
ATOM   2747  C  C   . PHE A  1  377 ? 98.946  -10.190 13.381  1.00 178.69 ?  377 PHE A C   1 
ATOM   2748  O  O   . PHE A  1  377 ? 99.558  -11.267 13.243  1.00 173.05 ?  377 PHE A O   1 
ATOM   2749  C  CB  . PHE A  1  377 ? 100.429 -8.655  14.699  1.00 164.46 ?  377 PHE A CB  1 
ATOM   2750  C  CG  . PHE A  1  377 ? 101.735 -7.898  14.687  1.00 165.27 ?  377 PHE A CG  1 
ATOM   2751  C  CD1 . PHE A  1  377 ? 102.378 -7.576  13.502  1.00 169.50 ?  377 PHE A CD1 1 
ATOM   2752  C  CD2 . PHE A  1  377 ? 102.328 -7.511  15.880  1.00 172.43 ?  377 PHE A CD2 1 
ATOM   2753  C  CE1 . PHE A  1  377 ? 103.581 -6.888  13.513  1.00 166.36 ?  377 PHE A CE1 1 
ATOM   2754  C  CE2 . PHE A  1  377 ? 103.528 -6.817  15.890  1.00 181.20 ?  377 PHE A CE2 1 
ATOM   2755  C  CZ  . PHE A  1  377 ? 104.154 -6.514  14.706  1.00 187.33 ?  377 PHE A CZ  1 
ATOM   2756  N  N   . GLU A  1  378 ? 97.622  -10.097 13.549  1.00 198.55 ?  378 GLU A N   1 
ATOM   2757  C  CA  . GLU A  1  378 ? 96.766  -11.311 13.679  1.00 199.37 ?  378 GLU A CA  1 
ATOM   2758  C  C   . GLU A  1  378 ? 96.901  -12.246 12.471  1.00 198.34 ?  378 GLU A C   1 
ATOM   2759  O  O   . GLU A  1  378 ? 97.054  -13.456 12.696  1.00 199.38 ?  378 GLU A O   1 
ATOM   2760  C  CB  . GLU A  1  378 ? 95.302  -10.907 13.870  1.00 199.95 ?  378 GLU A CB  1 
ATOM   2761  C  CG  . GLU A  1  378 ? 95.128  -9.543  14.510  1.00 213.26 ?  378 GLU A CG  1 
ATOM   2762  C  CD  . GLU A  1  378 ? 93.693  -9.044  14.540  1.00 218.81 ?  378 GLU A CD  1 
ATOM   2763  O  OE1 . GLU A  1  378 ? 93.002  -9.175  13.510  1.00 202.44 ?  378 GLU A OE1 1 
ATOM   2764  O  OE2 . GLU A  1  378 ? 93.270  -8.528  15.594  1.00 228.23 ?  378 GLU A OE2 1 
ATOM   2765  N  N   . PRO A  1  379 ? 96.814  -11.772 11.208  1.00 157.89 ?  379 PRO A N   1 
ATOM   2766  C  CA  . PRO A  1  379 ? 96.858  -12.675 10.055  1.00 142.84 ?  379 PRO A CA  1 
ATOM   2767  C  C   . PRO A  1  379 ? 97.985  -13.707 10.192  1.00 147.39 ?  379 PRO A C   1 
ATOM   2768  O  O   . PRO A  1  379 ? 97.773  -14.847 9.823   1.00 142.69 ?  379 PRO A O   1 
ATOM   2769  C  CB  . PRO A  1  379 ? 97.157  -11.719 8.894   1.00 139.25 ?  379 PRO A CB  1 
ATOM   2770  C  CG  . PRO A  1  379 ? 96.497  -10.424 9.310   1.00 135.03 ?  379 PRO A CG  1 
ATOM   2771  C  CD  . PRO A  1  379 ? 96.658  -10.369 10.815  1.00 158.07 ?  379 PRO A CD  1 
ATOM   2772  N  N   . VAL A  1  380 ? 99.137  -13.291 10.723  1.00 152.94 ?  380 VAL A N   1 
ATOM   2773  C  CA  . VAL A  1  380 ? 100.312 -14.196 10.864  1.00 157.61 ?  380 VAL A CA  1 
ATOM   2774  C  C   . VAL A  1  380 ? 99.868  -15.351 11.763  1.00 154.19 ?  380 VAL A C   1 
ATOM   2775  O  O   . VAL A  1  380 ? 100.458 -16.445 11.665  1.00 150.03 ?  380 VAL A O   1 
ATOM   2776  C  CB  . VAL A  1  380 ? 101.528 -13.454 11.449  1.00 140.87 ?  380 VAL A CB  1 
ATOM   2777  C  CG1 . VAL A  1  380 ? 102.781 -14.315 11.433  1.00 134.70 ?  380 VAL A CG1 1 
ATOM   2778  C  CG2 . VAL A  1  380 ? 101.775 -12.132 10.738  1.00 130.32 ?  380 VAL A CG2 1 
ATOM   2779  N  N   . LEU A  1  381 ? 98.853  -15.105 12.597  1.00 154.96 ?  381 LEU A N   1 
ATOM   2780  C  CA  . LEU A  1  381 ? 98.352  -16.157 13.520  1.00 149.58 ?  381 LEU A CA  1 
ATOM   2781  C  C   . LEU A  1  381 ? 97.408  -17.113 12.781  1.00 145.94 ?  381 LEU A C   1 
ATOM   2782  O  O   . LEU A  1  381 ? 97.577  -18.339 12.932  1.00 141.75 ?  381 LEU A O   1 
ATOM   2783  C  CB  . LEU A  1  381 ? 97.680  -15.506 14.735  1.00 164.12 ?  381 LEU A CB  1 
ATOM   2784  C  CG  . LEU A  1  381 ? 98.643  -15.030 15.822  1.00 162.22 ?  381 LEU A CG  1 
ATOM   2785  C  CD1 . LEU A  1  381 ? 99.232  -13.672 15.474  1.00 136.55 ?  381 LEU A CD1 1 
ATOM   2786  C  CD2 . LEU A  1  381 ? 97.960  -14.984 17.180  1.00 164.69 ?  381 LEU A CD2 1 
ATOM   2787  N  N   . GLU A  1  382 ? 96.467  -16.571 12.008  1.00 145.17 ?  382 GLU A N   1 
ATOM   2788  C  CA  . GLU A  1  382 ? 95.522  -17.424 11.242  1.00 118.51 ?  382 GLU A CA  1 
ATOM   2789  C  C   . GLU A  1  382 ? 96.315  -18.451 10.425  1.00 133.27 ?  382 GLU A C   1 
ATOM   2790  O  O   . GLU A  1  382 ? 95.821  -19.584 10.276  1.00 136.64 ?  382 GLU A O   1 
ATOM   2791  C  CB  . GLU A  1  382 ? 94.643  -16.556 10.341  1.00 128.02 ?  382 GLU A CB  1 
ATOM   2792  C  CG  . GLU A  1  382 ? 94.310  -15.207 10.948  1.00 142.56 ?  382 GLU A CG  1 
ATOM   2793  C  CD  . GLU A  1  382 ? 92.970  -15.152 11.659  1.00 148.67 ?  382 GLU A CD  1 
ATOM   2794  O  OE1 . GLU A  1  382 ? 92.326  -16.212 11.784  1.00 131.42 ?  382 GLU A OE1 1 
ATOM   2795  O  OE2 . GLU A  1  382 ? 92.574  -14.049 12.087  1.00 173.81 ?  382 GLU A OE2 1 
ATOM   2796  N  N   . ARG A  1  383 ? 97.501  -18.078 9.930   1.00 144.00 ?  383 ARG A N   1 
ATOM   2797  C  CA  . ARG A  1  383 ? 98.270  -18.999 9.051   1.00 143.11 ?  383 ARG A CA  1 
ATOM   2798  C  C   . ARG A  1  383 ? 98.871  -20.118 9.906   1.00 148.68 ?  383 ARG A C   1 
ATOM   2799  O  O   . ARG A  1  383 ? 98.741  -21.294 9.515   1.00 134.23 ?  383 ARG A O   1 
ATOM   2800  C  CB  . ARG A  1  383 ? 99.369  -18.237 8.306   1.00 129.49 ?  383 ARG A CB  1 
ATOM   2801  C  CG  . ARG A  1  383 ? 100.298 -19.127 7.492   1.00 115.42 ?  383 ARG A CG  1 
ATOM   2802  C  CD  . ARG A  1  383 ? 99.574  -19.820 6.354   1.00 117.78 ?  383 ARG A CD  1 
ATOM   2803  N  NE  . ARG A  1  383 ? 100.407 -20.804 5.678   1.00 125.52 ?  383 ARG A NE  1 
ATOM   2804  C  CZ  . ARG A  1  383 ? 99.942  -21.884 5.062   1.00 132.03 ?  383 ARG A CZ  1 
ATOM   2805  N  NH1 . ARG A  1  383 ? 98.645  -22.134 5.053   1.00 117.48 ?  383 ARG A NH1 1 
ATOM   2806  N  NH2 . ARG A  1  383 ? 100.776 -22.711 4.455   1.00 135.79 ?  383 ARG A NH2 1 
ATOM   2807  N  N   . ARG A  1  384 ? 99.502  -19.760 11.028  1.00 161.49 ?  384 ARG A N   1 
ATOM   2808  C  CA  . ARG A  1  384 ? 100.141 -20.767 11.871  1.00 155.84 ?  384 ARG A CA  1 
ATOM   2809  C  C   . ARG A  1  384 ? 99.151  -21.813 12.396  1.00 151.36 ?  384 ARG A C   1 
ATOM   2810  O  O   . ARG A  1  384 ? 99.577  -22.925 12.686  1.00 157.72 ?  384 ARG A O   1 
ATOM   2811  C  CB  . ARG A  1  384 ? 100.940 -20.125 13.022  1.00 138.94 ?  384 ARG A CB  1 
ATOM   2812  C  CG  . ARG A  1  384 ? 102.255 -19.445 12.599  1.00 141.92 ?  384 ARG A CG  1 
ATOM   2813  C  CD  . ARG A  1  384 ? 103.300 -20.361 11.965  1.00 143.24 ?  384 ARG A CD  1 
ATOM   2814  N  NE  . ARG A  1  384 ? 103.606 -21.535 12.786  1.00 135.37 ?  384 ARG A NE  1 
ATOM   2815  C  CZ  . ARG A  1  384 ? 104.322 -22.578 12.373  1.00 147.41 ?  384 ARG A CZ  1 
ATOM   2816  N  NH1 . ARG A  1  384 ? 104.814 -22.612 11.140  1.00 148.07 ?  384 ARG A NH1 1 
ATOM   2817  N  NH2 . ARG A  1  384 ? 104.549 -23.598 13.190  1.00 157.95 ?  384 ARG A NH2 1 
ATOM   2818  N  N   . LEU A  1  385 ? 97.838  -21.499 12.474  1.00 140.52 ?  385 LEU A N   1 
ATOM   2819  C  CA  . LEU A  1  385 ? 96.841  -22.480 12.935  1.00 134.73 ?  385 LEU A CA  1 
ATOM   2820  C  C   . LEU A  1  385 ? 96.865  -23.707 12.026  1.00 137.09 ?  385 LEU A C   1 
ATOM   2821  O  O   . LEU A  1  385 ? 96.784  -24.831 12.511  1.00 144.81 ?  385 LEU A O   1 
ATOM   2822  C  CB  . LEU A  1  385 ? 95.417  -21.901 12.923  1.00 124.62 ?  385 LEU A CB  1 
ATOM   2823  C  CG  . LEU A  1  385 ? 95.145  -20.663 13.758  1.00 121.17 ?  385 LEU A CG  1 
ATOM   2824  C  CD1 . LEU A  1  385 ? 93.760  -20.143 13.480  1.00 117.81 ?  385 LEU A CD1 1 
ATOM   2825  C  CD2 . LEU A  1  385 ? 95.287  -20.944 15.235  1.00 128.49 ?  385 LEU A CD2 1 
ATOM   2826  N  N   . HIS A  1  386 ? 96.987  -23.482 10.704  1.00 130.53 ?  386 HIS A N   1 
ATOM   2827  C  CA  . HIS A  1  386 ? 97.055  -24.541 9.694   1.00 139.47 ?  386 HIS A CA  1 
ATOM   2828  C  C   . HIS A  1  386 ? 98.174  -25.531 10.028  1.00 144.58 ?  386 HIS A C   1 
ATOM   2829  O  O   . HIS A  1  386 ? 97.979  -26.738 9.905   1.00 149.06 ?  386 HIS A O   1 
ATOM   2830  C  CB  . HIS A  1  386 ? 97.270  -23.919 8.290   1.00 138.74 ?  386 HIS A CB  1 
ATOM   2831  C  CG  . HIS A  1  386 ? 97.966  -24.805 7.297   1.00 135.81 ?  386 HIS A CG  1 
ATOM   2832  N  ND1 . HIS A  1  386 ? 97.301  -25.826 6.646   1.00 147.88 ?  386 HIS A ND1 1 
ATOM   2833  C  CD2 . HIS A  1  386 ? 99.245  -24.775 6.857   1.00 136.06 ?  386 HIS A CD2 1 
ATOM   2834  C  CE1 . HIS A  1  386 ? 98.192  -26.393 5.848   1.00 136.04 ?  386 HIS A CE1 1 
ATOM   2835  N  NE2 . HIS A  1  386 ? 99.377  -25.790 5.939   1.00 117.48 ?  386 HIS A NE2 1 
ATOM   2836  N  N   . TYR A  1  387 ? 99.334  -25.022 10.463  1.00 157.64 ?  387 TYR A N   1 
ATOM   2837  C  CA  . TYR A  1  387 ? 100.472 -25.866 10.810  1.00 159.46 ?  387 TYR A CA  1 
ATOM   2838  C  C   . TYR A  1  387 ? 100.234 -26.619 12.125  1.00 154.45 ?  387 TYR A C   1 
ATOM   2839  O  O   . TYR A  1  387 ? 100.476 -27.820 12.180  1.00 161.29 ?  387 TYR A O   1 
ATOM   2840  C  CB  . TYR A  1  387 ? 101.764 -25.030 10.879  1.00 154.33 ?  387 TYR A CB  1 
ATOM   2841  C  CG  . TYR A  1  387 ? 102.154 -24.437 9.541   1.00 144.66 ?  387 TYR A CG  1 
ATOM   2842  C  CD1 . TYR A  1  387 ? 101.591 -23.248 9.099   1.00 137.49 ?  387 TYR A CD1 1 
ATOM   2843  C  CD2 . TYR A  1  387 ? 103.061 -25.075 8.710   1.00 145.20 ?  387 TYR A CD2 1 
ATOM   2844  C  CE1 . TYR A  1  387 ? 101.930 -22.707 7.866   1.00 137.40 ?  387 TYR A CE1 1 
ATOM   2845  C  CE2 . TYR A  1  387 ? 103.406 -24.544 7.474   1.00 135.13 ?  387 TYR A CE2 1 
ATOM   2846  C  CZ  . TYR A  1  387 ? 102.833 -23.359 7.052   1.00 141.34 ?  387 TYR A CZ  1 
ATOM   2847  O  OH  . TYR A  1  387 ? 103.158 -22.814 5.832   1.00 150.82 ?  387 TYR A OH  1 
ATOM   2848  N  N   . PHE A  1  388 ? 99.741  -25.936 13.170  1.00 143.31 ?  388 PHE A N   1 
ATOM   2849  C  CA  . PHE A  1  388 ? 99.485  -26.590 14.457  1.00 138.06 ?  388 PHE A CA  1 
ATOM   2850  C  C   . PHE A  1  388 ? 98.449  -27.709 14.314  1.00 142.51 ?  388 PHE A C   1 
ATOM   2851  O  O   . PHE A  1  388 ? 98.638  -28.792 14.862  1.00 145.92 ?  388 PHE A O   1 
ATOM   2852  C  CB  . PHE A  1  388 ? 98.988  -25.584 15.518  1.00 141.58 ?  388 PHE A CB  1 
ATOM   2853  C  CG  . PHE A  1  388 ? 99.779  -24.307 15.697  1.00 150.90 ?  388 PHE A CG  1 
ATOM   2854  C  CD1 . PHE A  1  388 ? 101.158 -24.299 15.570  1.00 154.05 ?  388 PHE A CD1 1 
ATOM   2855  C  CD2 . PHE A  1  388 ? 99.144  -23.120 16.022  1.00 155.09 ?  388 PHE A CD2 1 
ATOM   2856  C  CE1 . PHE A  1  388 ? 101.879 -23.124 15.739  1.00 161.54 ?  388 PHE A CE1 1 
ATOM   2857  C  CE2 . PHE A  1  388 ? 99.869  -21.948 16.195  1.00 154.11 ?  388 PHE A CE2 1 
ATOM   2858  C  CZ  . PHE A  1  388 ? 101.231 -21.958 16.059  1.00 155.04 ?  388 PHE A CZ  1 
ATOM   2859  N  N   . LEU A  1  389 ? 97.356  -27.453 13.583  1.00 145.09 ?  389 LEU A N   1 
ATOM   2860  C  CA  . LEU A  1  389 ? 96.301  -28.449 13.401  1.00 148.95 ?  389 LEU A CA  1 
ATOM   2861  C  C   . LEU A  1  389 ? 96.743  -29.618 12.506  1.00 153.02 ?  389 LEU A C   1 
ATOM   2862  O  O   . LEU A  1  389 ? 96.207  -30.715 12.647  1.00 164.91 ?  389 LEU A O   1 
ATOM   2863  C  CB  . LEU A  1  389 ? 95.023  -27.796 12.840  1.00 142.39 ?  389 LEU A CB  1 
ATOM   2864  C  CG  . LEU A  1  389 ? 94.403  -26.662 13.672  1.00 129.51 ?  389 LEU A CG  1 
ATOM   2865  C  CD1 . LEU A  1  389 ? 93.260  -26.006 12.925  1.00 130.03 ?  389 LEU A CD1 1 
ATOM   2866  C  CD2 . LEU A  1  389 ? 93.919  -27.158 15.015  1.00 118.22 ?  389 LEU A CD2 1 
ATOM   2867  N  N   . ASN A  1  390 ? 97.724  -29.383 11.633  1.00 149.77 ?  390 ASN A N   1 
ATOM   2868  C  CA  . ASN A  1  390 ? 98.214  -30.456 10.726  1.00 149.18 ?  390 ASN A CA  1 
ATOM   2869  C  C   . ASN A  1  390 ? 99.072  -31.447 11.517  1.00 160.67 ?  390 ASN A C   1 
ATOM   2870  O  O   . ASN A  1  390 ? 98.965  -32.658 11.249  1.00 159.74 ?  390 ASN A O   1 
ATOM   2871  C  CB  . ASN A  1  390 ? 99.002  -29.887 9.546   1.00 137.86 ?  390 ASN A CB  1 
ATOM   2872  C  CG  . ASN A  1  390 ? 98.257  -29.999 8.234   1.00 141.96 ?  390 ASN A CG  1 
ATOM   2873  O  OD1 . ASN A  1  390 ? 98.145  -31.083 7.667   1.00 147.15 ?  390 ASN A OD1 1 
ATOM   2874  N  ND2 . ASN A  1  390 ? 97.741  -28.883 7.749   1.00 142.42 ?  390 ASN A ND2 1 
ATOM   2875  N  N   . TYR A  1  391 ? 99.879  -30.952 12.459  1.00 167.74 ?  391 TYR A N   1 
ATOM   2876  C  CA  . TYR A  1  391 ? 100.789 -31.818 13.217  1.00 161.76 ?  391 TYR A CA  1 
ATOM   2877  C  C   . TYR A  1  391 ? 100.027 -32.830 14.079  1.00 165.16 ?  391 TYR A C   1 
ATOM   2878  O  O   . TYR A  1  391 ? 100.600 -33.852 14.450  1.00 163.72 ?  391 TYR A O   1 
ATOM   2879  C  CB  . TYR A  1  391 ? 101.736 -30.999 14.116  1.00 149.90 ?  391 TYR A CB  1 
ATOM   2880  C  CG  . TYR A  1  391 ? 102.599 -29.979 13.400  1.00 154.73 ?  391 TYR A CG  1 
ATOM   2881  C  CD1 . TYR A  1  391 ? 102.973 -30.156 12.075  1.00 163.30 ?  391 TYR A CD1 1 
ATOM   2882  C  CD2 . TYR A  1  391 ? 103.045 -28.840 14.054  1.00 146.65 ?  391 TYR A CD2 1 
ATOM   2883  C  CE1 . TYR A  1  391 ? 103.761 -29.221 11.417  1.00 161.65 ?  391 TYR A CE1 1 
ATOM   2884  C  CE2 . TYR A  1  391 ? 103.833 -27.898 13.405  1.00 138.69 ?  391 TYR A CE2 1 
ATOM   2885  C  CZ  . TYR A  1  391 ? 104.192 -28.093 12.086  1.00 155.71 ?  391 TYR A CZ  1 
ATOM   2886  O  OH  . TYR A  1  391 ? 104.977 -27.172 11.434  1.00 153.09 ?  391 TYR A OH  1 
ATOM   2887  N  N   . ILE A  1  392 ? 98.747  -32.561 14.401  1.00 169.83 ?  392 ILE A N   1 
ATOM   2888  C  CA  . ILE A  1  392 ? 97.942  -33.482 15.203  1.00 167.49 ?  392 ILE A CA  1 
ATOM   2889  C  C   . ILE A  1  392 ? 97.753  -34.772 14.387  1.00 173.77 ?  392 ILE A C   1 
ATOM   2890  O  O   . ILE A  1  392 ? 97.331  -34.708 13.232  1.00 169.51 ?  392 ILE A O   1 
ATOM   2891  C  CB  . ILE A  1  392 ? 96.589  -32.831 15.615  1.00 157.69 ?  392 ILE A CB  1 
ATOM   2892  C  CG1 . ILE A  1  392 ? 96.816  -31.662 16.604  1.00 155.54 ?  392 ILE A CG1 1 
ATOM   2893  C  CG2 . ILE A  1  392 ? 95.647  -33.879 16.221  1.00 167.49 ?  392 ILE A CG2 1 
ATOM   2894  C  CD1 . ILE A  1  392 ? 95.640  -30.713 16.746  1.00 143.89 ?  392 ILE A CD1 1 
ATOM   2895  N  N   . GLU A  1  393 ? 98.109  -35.928 14.970  1.00 177.61 ?  393 GLU A N   1 
ATOM   2896  C  CA  . GLU A  1  393 ? 98.010  -37.223 14.294  1.00 184.28 ?  393 GLU A CA  1 
ATOM   2897  C  C   . GLU A  1  393 ? 96.569  -37.580 13.922  1.00 193.80 ?  393 GLU A C   1 
ATOM   2898  O  O   . GLU A  1  393 ? 95.743  -37.829 14.802  1.00 190.59 ?  393 GLU A O   1 
ATOM   2899  C  CB  . GLU A  1  393 ? 98.613  -38.327 15.179  1.00 182.15 ?  393 GLU A CB  1 
ATOM   2900  C  CG  . GLU A  1  393 ? 98.595  -39.707 14.547  1.00 185.18 ?  393 GLU A CG  1 
ATOM   2901  C  CD  . GLU A  1  393 ? 99.494  -40.716 15.236  1.00 177.92 ?  393 GLU A CD  1 
ATOM   2902  O  OE1 . GLU A  1  393 ? 99.647  -40.629 16.476  1.00 158.91 ?  393 GLU A OE1 1 
ATOM   2903  O  OE2 . GLU A  1  393 ? 100.044 -41.596 14.535  1.00 182.05 ?  393 GLU A OE2 1 
ATOM   2904  N  N   . GLY A  1  394 ? 96.292  -37.610 12.622  1.00 207.42 ?  394 GLY A N   1 
ATOM   2905  C  CA  . GLY A  1  394 ? 94.974  -37.944 12.097  1.00 201.19 ?  394 GLY A CA  1 
ATOM   2906  C  C   . GLY A  1  394 ? 94.075  -36.755 11.814  1.00 199.92 ?  394 GLY A C   1 
ATOM   2907  O  O   . GLY A  1  394 ? 92.887  -36.939 11.542  1.00 207.33 ?  394 GLY A O   1 
ATOM   2908  N  N   . VAL A  1  395 ? 94.615  -35.526 11.865  1.00 163.99 ?  395 VAL A N   1 
ATOM   2909  C  CA  . VAL A  1  395 ? 93.832  -34.322 11.582  1.00 152.60 ?  395 VAL A CA  1 
ATOM   2910  C  C   . VAL A  1  395 ? 94.545  -33.528 10.487  1.00 159.14 ?  395 VAL A C   1 
ATOM   2911  O  O   . VAL A  1  395 ? 95.768  -33.405 10.512  1.00 157.61 ?  395 VAL A O   1 
ATOM   2912  C  CB  . VAL A  1  395 ? 93.597  -33.467 12.849  1.00 148.24 ?  395 VAL A CB  1 
ATOM   2913  C  CG1 . VAL A  1  395 ? 92.906  -32.151 12.500  1.00 144.08 ?  395 VAL A CG1 1 
ATOM   2914  C  CG2 . VAL A  1  395 ? 92.787  -34.239 13.886  1.00 146.95 ?  395 VAL A CG2 1 
ATOM   2915  N  N   . MET A  1  396 ? 93.779  -33.005 9.519   1.00 147.41 ?  396 MET A N   1 
ATOM   2916  C  CA  . MET A  1  396 ? 94.318  -32.235 8.400   1.00 143.27 ?  396 MET A CA  1 
ATOM   2917  C  C   . MET A  1  396 ? 93.560  -30.911 8.281   1.00 150.21 ?  396 MET A C   1 
ATOM   2918  O  O   . MET A  1  396 ? 92.350  -30.883 8.493   1.00 140.68 ?  396 MET A O   1 
ATOM   2919  C  CB  . MET A  1  396 ? 94.174  -33.051 7.105   1.00 153.88 ?  396 MET A CB  1 
ATOM   2920  C  CG  . MET A  1  396 ? 94.914  -32.464 5.923   1.00 166.96 ?  396 MET A CG  1 
ATOM   2921  S  SD  . MET A  1  396 ? 94.928  -33.569 4.489   1.00 171.54 ?  396 MET A SD  1 
ATOM   2922  C  CE  . MET A  1  396 ? 93.253  -33.395 3.934   1.00 111.19 ?  396 MET A CE  1 
ATOM   2923  N  N   . HIS A  1  397 ? 94.293  -29.828 8.013   1.00 148.95 ?  397 HIS A N   1 
ATOM   2924  C  CA  . HIS A  1  397 ? 93.655  -28.489 7.914   1.00 141.14 ?  397 HIS A CA  1 
ATOM   2925  C  C   . HIS A  1  397 ? 94.062  -27.833 6.596   1.00 145.19 ?  397 HIS A C   1 
ATOM   2926  O  O   . HIS A  1  397 ? 95.276  -27.712 6.328   1.00 148.34 ?  397 HIS A O   1 
ATOM   2927  C  CB  . HIS A  1  397 ? 94.050  -27.596 9.094   1.00 130.14 ?  397 HIS A CB  1 
ATOM   2928  C  CG  . HIS A  1  397 ? 93.677  -26.165 8.894   1.00 141.70 ?  397 HIS A CG  1 
ATOM   2929  N  ND1 . HIS A  1  397 ? 94.368  -25.323 8.050   1.00 154.96 ?  397 HIS A ND1 1 
ATOM   2930  C  CD2 . HIS A  1  397 ? 92.684  -25.432 9.414   1.00 142.41 ?  397 HIS A CD2 1 
ATOM   2931  C  CE1 . HIS A  1  397 ? 93.806  -24.123 8.071   1.00 147.37 ?  397 HIS A CE1 1 
ATOM   2932  N  NE2 . HIS A  1  397 ? 92.782  -24.167 8.894   1.00 152.72 ?  397 HIS A NE2 1 
ATOM   2933  N  N   . VAL A  1  398 ? 93.087  -27.407 5.800   1.00 154.23 ?  398 VAL A N   1 
ATOM   2934  C  CA  . VAL A  1  398 ? 93.441  -26.633 4.576   1.00 154.84 ?  398 VAL A CA  1 
ATOM   2935  C  C   . VAL A  1  398 ? 92.395  -25.530 4.440   1.00 156.89 ?  398 VAL A C   1 
ATOM   2936  O  O   . VAL A  1  398 ? 91.452  -25.509 5.254   1.00 162.82 ?  398 VAL A O   1 
ATOM   2937  C  CB  . VAL A  1  398 ? 93.532  -27.508 3.313   1.00 141.01 ?  398 VAL A CB  1 
ATOM   2938  C  CG1 . VAL A  1  398 ? 94.784  -28.371 3.309   1.00 133.99 ?  398 VAL A CG1 1 
ATOM   2939  C  CG2 . VAL A  1  398 ? 92.294  -28.362 3.144   1.00 157.97 ?  398 VAL A CG2 1 
ATOM   2940  N  N   . GLY A  1  399 ? 92.554  -24.657 3.451   1.00 159.18 ?  399 GLY A N   1 
ATOM   2941  C  CA  . GLY A  1  399 ? 91.638  -23.506 3.338   1.00 169.31 ?  399 GLY A CA  1 
ATOM   2942  C  C   . GLY A  1  399 ? 92.134  -22.376 4.220   1.00 169.22 ?  399 GLY A C   1 
ATOM   2943  O  O   . GLY A  1  399 ? 92.864  -22.671 5.186   1.00 172.05 ?  399 GLY A O   1 
ATOM   2944  N  N   . GLN A  1  400 ? 91.741  -21.125 3.970   1.00 168.18 ?  400 GLN A N   1 
ATOM   2945  C  CA  . GLN A  1  400 ? 92.372  -20.022 4.751   1.00 165.31 ?  400 GLN A CA  1 
ATOM   2946  C  C   . GLN A  1  400 ? 91.672  -19.427 5.978   1.00 168.81 ?  400 GLN A C   1 
ATOM   2947  O  O   . GLN A  1  400 ? 92.223  -19.577 7.085   1.00 178.15 ?  400 GLN A O   1 
ATOM   2948  C  CB  . GLN A  1  400 ? 92.697  -18.828 3.847   1.00 162.99 ?  400 GLN A CB  1 
ATOM   2949  C  CG  . GLN A  1  400 ? 91.623  -18.532 2.816   1.00 172.70 ?  400 GLN A CG  1 
ATOM   2950  C  CD  . GLN A  1  400 ? 91.832  -17.218 2.114   1.00 184.79 ?  400 GLN A CD  1 
ATOM   2951  O  OE1 . GLN A  1  400 ? 92.642  -17.094 1.198   1.00 187.70 ?  400 GLN A OE1 1 
ATOM   2952  N  NE2 . GLN A  1  400 ? 91.079  -16.226 2.545   1.00 181.10 ?  400 GLN A NE2 1 
ATOM   2953  N  N   . ARG A  1  401 ? 90.543  -18.735 5.799   1.00 139.35 ?  401 ARG A N   1 
ATOM   2954  C  CA  . ARG A  1  401 ? 89.884  -18.080 6.960   1.00 150.76 ?  401 ARG A CA  1 
ATOM   2955  C  C   . ARG A  1  401 ? 88.418  -18.496 7.031   1.00 152.55 ?  401 ARG A C   1 
ATOM   2956  O  O   . ARG A  1  401 ? 88.063  -19.270 7.941   1.00 162.43 ?  401 ARG A O   1 
ATOM   2957  C  CB  . ARG A  1  401 ? 89.883  -16.553 6.855   1.00 152.75 ?  401 ARG A CB  1 
ATOM   2958  C  CG  . ARG A  1  401 ? 91.161  -15.931 6.321   1.00 149.42 ?  401 ARG A CG  1 
ATOM   2959  C  CD  . ARG A  1  401 ? 90.813  -14.658 5.580   1.00 155.54 ?  401 ARG A CD  1 
ATOM   2960  N  NE  . ARG A  1  401 ? 92.013  -13.862 5.365   1.00 149.28 ?  401 ARG A NE  1 
ATOM   2961  C  CZ  . ARG A  1  401 ? 92.020  -12.629 4.875   1.00 141.14 ?  401 ARG A CZ  1 
ATOM   2962  N  NH1 . ARG A  1  401 ? 90.917  -12.119 4.360   1.00 135.08 ?  401 ARG A NH1 1 
ATOM   2963  N  NH2 . ARG A  1  401 ? 93.130  -11.911 4.900   1.00 135.57 ?  401 ARG A NH2 1 
ATOM   2964  N  N   . ASN A  1  402 ? 87.600  -17.977 6.114   1.00 127.61 ?  402 ASN A N   1 
ATOM   2965  C  CA  . ASN A  1  402 ? 86.141  -18.254 6.194   1.00 139.97 ?  402 ASN A CA  1 
ATOM   2966  C  C   . ASN A  1  402 ? 86.039  -19.594 5.459   1.00 158.86 ?  402 ASN A C   1 
ATOM   2967  O  O   . ASN A  1  402 ? 85.338  -20.489 5.964   1.00 171.48 ?  402 ASN A O   1 
ATOM   2968  C  CB  . ASN A  1  402 ? 85.258  -17.197 5.528   1.00 135.07 ?  402 ASN A CB  1 
ATOM   2969  C  CG  . ASN A  1  402 ? 83.869  -17.711 5.217   1.00 146.09 ?  402 ASN A CG  1 
ATOM   2970  O  OD1 . ASN A  1  402 ? 83.441  -17.702 4.065   1.00 145.93 ?  402 ASN A OD1 1 
ATOM   2971  N  ND2 . ASN A  1  402 ? 83.160  -18.167 6.236   1.00 153.73 ?  402 ASN A ND2 1 
ATOM   2972  N  N   . LEU A  1  403 ? 86.717  -19.721 4.314   1.00 155.85 ?  403 LEU A N   1 
ATOM   2973  C  CA  . LEU A  1  403 ? 86.670  -20.979 3.522   1.00 140.30 ?  403 LEU A CA  1 
ATOM   2974  C  C   . LEU A  1  403 ? 87.692  -21.964 4.096   1.00 143.75 ?  403 LEU A C   1 
ATOM   2975  O  O   . LEU A  1  403 ? 88.790  -22.068 3.525   1.00 146.71 ?  403 LEU A O   1 
ATOM   2976  C  CB  . LEU A  1  403 ? 86.984  -20.661 2.057   1.00 123.99 ?  403 LEU A CB  1 
ATOM   2977  C  CG  . LEU A  1  403 ? 86.515  -19.293 1.564   1.00 141.97 ?  403 LEU A CG  1 
ATOM   2978  C  CD1 . LEU A  1  403 ? 87.146  -18.958 0.221   1.00 130.04 ?  403 LEU A CD1 1 
ATOM   2979  C  CD2 . LEU A  1  403 ? 84.998  -19.243 1.467   1.00 131.87 ?  403 LEU A CD2 1 
ATOM   2980  N  N   . THR A  1  404 ? 87.336  -22.677 5.163   1.00 147.17 ?  404 THR A N   1 
ATOM   2981  C  CA  . THR A  1  404 ? 88.343  -23.566 5.801   1.00 156.59 ?  404 THR A CA  1 
ATOM   2982  C  C   . THR A  1  404 ? 87.853  -25.019 5.739   1.00 146.84 ?  404 THR A C   1 
ATOM   2983  O  O   . THR A  1  404 ? 86.630  -25.230 5.838   1.00 142.58 ?  404 THR A O   1 
ATOM   2984  C  CB  . THR A  1  404 ? 88.721  -23.025 7.187   1.00 170.59 ?  404 THR A CB  1 
ATOM   2985  O  OG1 . THR A  1  404 ? 87.515  -22.756 7.903   1.00 163.67 ?  404 THR A OG1 1 
ATOM   2986  C  CG2 . THR A  1  404 ? 89.564  -21.769 7.101   1.00 173.12 ?  404 THR A CG2 1 
ATOM   2987  N  N   . TRP A  1  405 ? 88.781  -25.964 5.572   1.00 149.31 ?  405 TRP A N   1 
ATOM   2988  C  CA  . TRP A  1  405 ? 88.393  -27.392 5.436   1.00 148.58 ?  405 TRP A CA  1 
ATOM   2989  C  C   . TRP A  1  405 ? 89.231  -28.256 6.380   1.00 145.76 ?  405 TRP A C   1 
ATOM   2990  O  O   . TRP A  1  405 ? 90.465  -28.294 6.208   1.00 136.11 ?  405 TRP A O   1 
ATOM   2991  C  CB  . TRP A  1  405 ? 88.535  -27.842 3.979   1.00 150.12 ?  405 TRP A CB  1 
ATOM   2992  C  CG  . TRP A  1  405 ? 88.109  -29.257 3.745   1.00 152.10 ?  405 TRP A CG  1 
ATOM   2993  C  CD1 . TRP A  1  405 ? 87.190  -29.975 4.454   1.00 150.63 ?  405 TRP A CD1 1 
ATOM   2994  C  CD2 . TRP A  1  405 ? 88.597  -30.134 2.717   1.00 150.48 ?  405 TRP A CD2 1 
ATOM   2995  N  NE1 . TRP A  1  405 ? 87.073  -31.237 3.936   1.00 145.51 ?  405 TRP A NE1 1 
ATOM   2996  C  CE2 . TRP A  1  405 ? 87.923  -31.364 2.870   1.00 149.13 ?  405 TRP A CE2 1 
ATOM   2997  C  CE3 . TRP A  1  405 ? 89.533  -29.997 1.687   1.00 146.79 ?  405 TRP A CE3 1 
ATOM   2998  C  CZ2 . TRP A  1  405 ? 88.160  -32.447 2.027   1.00 155.35 ?  405 TRP A CZ2 1 
ATOM   2999  C  CZ3 . TRP A  1  405 ? 89.766  -31.069 0.856   1.00 133.12 ?  405 TRP A CZ3 1 
ATOM   3000  C  CH2 . TRP A  1  405 ? 89.088  -32.276 1.026   1.00 155.27 ?  405 TRP A CH2 1 
ATOM   3001  N  N   . VAL A  1  406 ? 88.579  -28.917 7.338   1.00 143.06 ?  406 VAL A N   1 
ATOM   3002  C  CA  . VAL A  1  406 ? 89.268  -29.795 8.283   1.00 142.27 ?  406 VAL A CA  1 
ATOM   3003  C  C   . VAL A  1  406 ? 88.601  -31.168 8.264   1.00 150.82 ?  406 VAL A C   1 
ATOM   3004  O  O   . VAL A  1  406 ? 87.373  -31.258 8.247   1.00 146.70 ?  406 VAL A O   1 
ATOM   3005  C  CB  . VAL A  1  406 ? 89.273  -29.193 9.712   1.00 131.70 ?  406 VAL A CB  1 
ATOM   3006  C  CG1 . VAL A  1  406 ? 89.846  -30.179 10.728  1.00 132.52 ?  406 VAL A CG1 1 
ATOM   3007  C  CG2 . VAL A  1  406 ? 90.047  -27.880 9.748   1.00 139.02 ?  406 VAL A CG2 1 
ATOM   3008  N  N   . ARG A  1  407 ? 89.409  -32.230 8.295   1.00 160.52 ?  407 ARG A N   1 
ATOM   3009  C  CA  . ARG A  1  407 ? 88.848  -33.608 8.323   1.00 154.47 ?  407 ARG A CA  1 
ATOM   3010  C  C   . ARG A  1  407 ? 89.476  -34.391 9.481   1.00 157.93 ?  407 ARG A C   1 
ATOM   3011  O  O   . ARG A  1  407 ? 90.673  -34.726 9.382   1.00 161.58 ?  407 ARG A O   1 
ATOM   3012  C  CB  . ARG A  1  407 ? 89.095  -34.311 6.985   1.00 149.00 ?  407 ARG A CB  1 
ATOM   3013  C  CG  . ARG A  1  407 ? 88.246  -33.780 5.839   1.00 147.83 ?  407 ARG A CG  1 
ATOM   3014  C  CD  . ARG A  1  407 ? 88.501  -34.541 4.553   1.00 156.79 ?  407 ARG A CD  1 
ATOM   3015  N  NE  . ARG A  1  407 ? 87.284  -34.769 3.787   1.00 168.48 ?  407 ARG A NE  1 
ATOM   3016  C  CZ  . ARG A  1  407 ? 87.242  -35.381 2.609   1.00 156.12 ?  407 ARG A CZ  1 
ATOM   3017  N  NH1 . ARG A  1  407 ? 88.328  -35.898 2.063   1.00 132.56 ?  407 ARG A NH1 1 
ATOM   3018  N  NH2 . ARG A  1  407 ? 86.059  -35.452 1.998   1.00 161.59 ?  407 ARG A NH2 1 
ATOM   3019  N  N   . ILE A  1  408 ? 88.696  -34.674 10.529  1.00 160.14 ?  408 ILE A N   1 
ATOM   3020  C  CA  . ILE A  1  408 ? 89.212  -35.474 11.681  1.00 171.51 ?  408 ILE A CA  1 
ATOM   3021  C  C   . ILE A  1  408 ? 89.209  -36.970 11.349  1.00 174.64 ?  408 ILE A C   1 
ATOM   3022  O  O   . ILE A  1  408 ? 88.224  -37.434 10.742  1.00 176.83 ?  408 ILE A O   1 
ATOM   3023  C  CB  . ILE A  1  408 ? 88.351  -35.249 12.941  1.00 160.67 ?  408 ILE A CB  1 
ATOM   3024  C  CG1 . ILE A  1  408 ? 87.180  -36.233 13.017  1.00 172.61 ?  408 ILE A CG1 1 
ATOM   3025  C  CG2 . ILE A  1  408 ? 87.883  -33.805 13.021  1.00 154.38 ?  408 ILE A CG2 1 
ATOM   3026  C  CD1 . ILE A  1  408 ? 87.282  -37.219 14.157  1.00 169.49 ?  408 ILE A CD1 1 
ATOM   3027  N  N   . GLY A  1  409 ? 90.271  -37.688 11.726  1.00 189.42 ?  409 GLY A N   1 
ATOM   3028  C  CA  . GLY A  1  409 ? 90.372  -39.124 11.400  1.00 191.72 ?  409 GLY A CA  1 
ATOM   3029  C  C   . GLY A  1  409 ? 89.782  -40.092 12.409  1.00 197.26 ?  409 GLY A C   1 
ATOM   3030  O  O   . GLY A  1  409 ? 89.678  -39.720 13.595  1.00 200.29 ?  409 GLY A O   1 
ATOM   3031  N  N   . LYS A  1  410 ? 89.413  -41.295 11.958  1.00 180.07 ?  410 LYS A N   1 
ATOM   3032  C  CA  . LYS A  1  410 ? 88.842  -42.302 12.853  1.00 163.83 ?  410 LYS A CA  1 
ATOM   3033  C  C   . LYS A  1  410 ? 89.868  -42.669 13.920  1.00 168.96 ?  410 LYS A C   1 
ATOM   3034  O  O   . LYS A  1  410 ? 89.514  -42.809 15.090  1.00 181.35 ?  410 LYS A O   1 
ATOM   3035  C  CB  . LYS A  1  410 ? 88.402  -43.542 12.061  1.00 158.28 ?  410 LYS A CB  1 
ATOM   3036  C  CG  . LYS A  1  410 ? 87.264  -43.259 11.089  1.00 147.73 ?  410 LYS A CG  1 
ATOM   3037  C  CD  . LYS A  1  410 ? 86.790  -44.513 10.382  1.00 140.27 ?  410 LYS A CD  1 
ATOM   3038  C  CE  . LYS A  1  410 ? 85.479  -44.285 9.676   1.00 137.29 ?  410 LYS A CE  1 
ATOM   3039  N  NZ  . LYS A  1  410 ? 85.109  -45.430 8.805   1.00 137.90 ?  410 LYS A NZ  1 
ATOM   3040  N  N   . GLU A  1  411 ? 91.119  -42.860 13.499  1.00 171.23 ?  411 GLU A N   1 
ATOM   3041  C  CA  . GLU A  1  411 ? 92.195  -43.235 14.453  1.00 173.48 ?  411 GLU A CA  1 
ATOM   3042  C  C   . GLU A  1  411 ? 92.133  -42.267 15.637  1.00 190.63 ?  411 GLU A C   1 
ATOM   3043  O  O   . GLU A  1  411 ? 92.183  -42.737 16.788  1.00 195.43 ?  411 GLU A O   1 
ATOM   3044  C  CB  . GLU A  1  411 ? 93.555  -43.205 13.755  1.00 176.59 ?  411 GLU A CB  1 
ATOM   3045  C  CG  . GLU A  1  411 ? 93.730  -42.019 12.823  1.00 178.91 ?  411 GLU A CG  1 
ATOM   3046  C  CD  . GLU A  1  411 ? 93.160  -42.219 11.429  1.00 181.27 ?  411 GLU A CD  1 
ATOM   3047  O  OE1 . GLU A  1  411 ? 93.824  -42.884 10.610  1.00 170.08 ?  411 GLU A OE1 1 
ATOM   3048  O  OE2 . GLU A  1  411 ? 92.051  -41.713 11.168  1.00 188.87 ?  411 GLU A OE2 1 
ATOM   3049  N  N   . ALA A  1  412 ? 92.027  -40.966 15.355  1.00 214.41 ?  412 ALA A N   1 
ATOM   3050  C  CA  . ALA A  1  412 ? 91.956  -39.953 16.431  1.00 215.02 ?  412 ALA A CA  1 
ATOM   3051  C  C   . ALA A  1  412 ? 90.756  -40.239 17.336  1.00 217.11 ?  412 ALA A C   1 
ATOM   3052  O  O   . ALA A  1  412 ? 90.920  -40.195 18.570  1.00 217.49 ?  412 ALA A O   1 
ATOM   3053  C  CB  . ALA A  1  412 ? 91.876  -38.572 15.831  1.00 217.24 ?  412 ALA A CB  1 
ATOM   3054  N  N   . PHE A  1  413 ? 89.597  -40.515 16.734  1.00 207.11 ?  413 PHE A N   1 
ATOM   3055  C  CA  . PHE A  1  413 ? 88.405  -40.885 17.538  1.00 198.10 ?  413 PHE A CA  1 
ATOM   3056  C  C   . PHE A  1  413 ? 88.759  -42.126 18.360  1.00 205.76 ?  413 PHE A C   1 
ATOM   3057  O  O   . PHE A  1  413 ? 88.408  -42.176 19.554  1.00 208.60 ?  413 PHE A O   1 
ATOM   3058  C  CB  . PHE A  1  413 ? 87.205  -41.127 16.622  1.00 191.66 ?  413 PHE A CB  1 
ATOM   3059  C  CG  . PHE A  1  413 ? 85.954  -41.566 17.336  1.00 203.05 ?  413 PHE A CG  1 
ATOM   3060  C  CD1 . PHE A  1  413 ? 85.071  -40.634 17.857  1.00 195.63 ?  413 PHE A CD1 1 
ATOM   3061  C  CD2 . PHE A  1  413 ? 85.663  -42.911 17.492  1.00 209.60 ?  413 PHE A CD2 1 
ATOM   3062  C  CE1 . PHE A  1  413 ? 83.921  -41.039 18.515  1.00 202.02 ?  413 PHE A CE1 1 
ATOM   3063  C  CE2 . PHE A  1  413 ? 84.514  -43.315 18.151  1.00 207.91 ?  413 PHE A CE2 1 
ATOM   3064  C  CZ  . PHE A  1  413 ? 83.646  -42.379 18.661  1.00 209.60 ?  413 PHE A CZ  1 
ATOM   3065  N  N   . GLU A  1  414 ? 89.442  -43.091 17.736  1.00 202.37 ?  414 GLU A N   1 
ATOM   3066  C  CA  . GLU A  1  414 ? 89.888  -44.307 18.467  1.00 195.45 ?  414 GLU A CA  1 
ATOM   3067  C  C   . GLU A  1  414 ? 90.898  -43.874 19.532  1.00 193.71 ?  414 GLU A C   1 
ATOM   3068  O  O   . GLU A  1  414 ? 90.953  -44.525 20.592  1.00 182.46 ?  414 GLU A O   1 
ATOM   3069  C  CB  . GLU A  1  414 ? 90.499  -45.320 17.498  1.00 190.65 ?  414 GLU A CB  1 
ATOM   3070  C  CG  . GLU A  1  414 ? 89.494  -45.909 16.526  1.00 180.06 ?  414 GLU A CG  1 
ATOM   3071  C  CD  . GLU A  1  414 ? 90.084  -46.865 15.503  1.00 175.42 ?  414 GLU A CD  1 
ATOM   3072  O  OE1 . GLU A  1  414 ? 91.325  -46.942 15.415  1.00 185.33 ?  414 GLU A OE1 1 
ATOM   3073  O  OE2 . GLU A  1  414 ? 89.300  -47.532 14.797  1.00 172.24 ?  414 GLU A OE2 1 
ATOM   3074  N  N   . LYS A  1  415 ? 91.674  -42.820 19.244  1.00 206.18 ?  415 LYS A N   1 
ATOM   3075  C  CA  . LYS A  1  415 ? 92.650  -42.284 20.230  1.00 206.07 ?  415 LYS A CA  1 
ATOM   3076  C  C   . LYS A  1  415 ? 91.881  -41.474 21.281  1.00 201.90 ?  415 LYS A C   1 
ATOM   3077  O  O   . LYS A  1  415 ? 92.491  -41.117 22.307  1.00 187.93 ?  415 LYS A O   1 
ATOM   3078  C  CB  . LYS A  1  415 ? 93.709  -41.404 19.551  1.00 200.50 ?  415 LYS A CB  1 
ATOM   3079  C  CG  . LYS A  1  415 ? 94.665  -42.080 18.569  1.00 183.51 ?  415 LYS A CG  1 
ATOM   3080  C  CD  . LYS A  1  415 ? 95.384  -43.296 19.112  1.00 168.93 ?  415 LYS A CD  1 
ATOM   3081  C  CE  . LYS A  1  415 ? 96.271  -43.988 18.100  1.00 148.28 ?  415 LYS A CE  1 
ATOM   3082  N  NZ  . LYS A  1  415 ? 97.060  -45.079 18.720  1.00 160.39 ?  415 LYS A NZ  1 
ATOM   3083  N  N   . GLY A  1  416 ? 90.595  -41.193 21.031  1.00 196.88 ?  416 GLY A N   1 
ATOM   3084  C  CA  . GLY A  1  416 ? 89.770  -40.441 21.995  1.00 183.03 ?  416 GLY A CA  1 
ATOM   3085  C  C   . GLY A  1  416 ? 90.077  -38.956 21.963  1.00 201.12 ?  416 GLY A C   1 
ATOM   3086  O  O   . GLY A  1  416 ? 89.626  -38.243 22.882  1.00 197.14 ?  416 GLY A O   1 
ATOM   3087  N  N   . PHE A  1  417 ? 90.815  -38.501 20.946  1.00 208.59 ?  417 PHE A N   1 
ATOM   3088  C  CA  . PHE A  1  417 ? 91.115  -37.052 20.806  1.00 205.10 ?  417 PHE A CA  1 
ATOM   3089  C  C   . PHE A  1  417 ? 89.812  -36.257 20.933  1.00 203.93 ?  417 PHE A C   1 
ATOM   3090  O  O   . PHE A  1  417 ? 88.769  -36.745 20.457  1.00 192.13 ?  417 PHE A O   1 
ATOM   3091  C  CB  . PHE A  1  417 ? 91.784  -36.763 19.462  1.00 195.14 ?  417 PHE A CB  1 
ATOM   3092  C  CG  . PHE A  1  417 ? 91.731  -35.314 19.048  1.00 203.07 ?  417 PHE A CG  1 
ATOM   3093  C  CD1 . PHE A  1  417 ? 92.715  -34.425 19.450  1.00 202.46 ?  417 PHE A CD1 1 
ATOM   3094  C  CD2 . PHE A  1  417 ? 90.689  -34.834 18.271  1.00 194.45 ?  417 PHE A CD2 1 
ATOM   3095  C  CE1 . PHE A  1  417 ? 92.663  -33.092 19.075  1.00 190.87 ?  417 PHE A CE1 1 
ATOM   3096  C  CE2 . PHE A  1  417 ? 90.637  -33.500 17.899  1.00 182.40 ?  417 PHE A CE2 1 
ATOM   3097  C  CZ  . PHE A  1  417 ? 91.624  -32.631 18.302  1.00 185.11 ?  417 PHE A CZ  1 
ATOM   3098  N  N   . ARG A  1  418 ? 89.869  -35.065 21.537  1.00 235.34 ?  418 ARG A N   1 
ATOM   3099  C  CA  . ARG A  1  418 ? 88.643  -34.226 21.601  1.00 227.39 ?  418 ARG A CA  1 
ATOM   3100  C  C   . ARG A  1  418 ? 88.899  -32.806 21.096  1.00 230.07 ?  418 ARG A C   1 
ATOM   3101  O  O   . ARG A  1  418 ? 90.064  -32.361 21.134  1.00 235.21 ?  418 ARG A O   1 
ATOM   3102  C  CB  . ARG A  1  418 ? 88.116  -34.176 23.039  1.00 221.99 ?  418 ARG A CB  1 
ATOM   3103  C  CG  . ARG A  1  418 ? 86.831  -33.378 23.210  1.00 222.58 ?  418 ARG A CG  1 
ATOM   3104  C  CD  . ARG A  1  418 ? 85.691  -33.875 22.340  1.00 214.93 ?  418 ARG A CD  1 
ATOM   3105  N  NE  . ARG A  1  418 ? 85.385  -35.278 22.574  1.00 218.39 ?  418 ARG A NE  1 
ATOM   3106  C  CZ  . ARG A  1  418 ? 84.583  -35.727 23.533  1.00 226.39 ?  418 ARG A CZ  1 
ATOM   3107  N  NH1 . ARG A  1  418 ? 84.232  -34.935 24.529  1.00 221.33 ?  418 ARG A NH1 1 
ATOM   3108  N  NH2 . ARG A  1  418 ? 84.135  -36.970 23.490  1.00 229.15 ?  418 ARG A NH2 1 
ATOM   3109  N  N   . LEU A  1  419 ? 87.844  -32.123 20.640  1.00 191.91 ?  419 LEU A N   1 
ATOM   3110  C  CA  . LEU A  1  419 ? 87.990  -30.702 20.235  1.00 196.08 ?  419 LEU A CA  1 
ATOM   3111  C  C   . LEU A  1  419 ? 88.666  -29.895 21.339  1.00 193.33 ?  419 LEU A C   1 
ATOM   3112  O  O   . LEU A  1  419 ? 89.243  -28.838 21.037  1.00 197.32 ?  419 LEU A O   1 
ATOM   3113  C  CB  . LEU A  1  419 ? 86.599  -30.073 20.133  1.00 188.73 ?  419 LEU A CB  1 
ATOM   3114  C  CG  . LEU A  1  419 ? 85.937  -30.145 18.762  1.00 182.35 ?  419 LEU A CG  1 
ATOM   3115  C  CD1 . LEU A  1  419 ? 85.908  -31.578 18.272  1.00 176.71 ?  419 LEU A CD1 1 
ATOM   3116  C  CD2 . LEU A  1  419 ? 84.527  -29.579 18.821  1.00 177.61 ?  419 LEU A CD2 1 
ATOM   3117  N  N   . LYS A  1  420 ? 88.585  -30.385 22.578  1.00 177.52 ?  420 LYS A N   1 
ATOM   3118  C  CA  . LYS A  1  420 ? 89.229  -29.688 23.722  1.00 179.39 ?  420 LYS A CA  1 
ATOM   3119  C  C   . LYS A  1  420 ? 90.730  -29.581 23.434  1.00 195.23 ?  420 LYS A C   1 
ATOM   3120  O  O   . LYS A  1  420 ? 91.314  -28.518 23.721  1.00 195.15 ?  420 LYS A O   1 
ATOM   3121  C  CB  . LYS A  1  420 ? 88.954  -30.448 25.024  1.00 168.67 ?  420 LYS A CB  1 
ATOM   3122  C  CG  . LYS A  1  420 ? 87.506  -30.447 25.495  1.00 158.12 ?  420 LYS A CG  1 
ATOM   3123  C  CD  . LYS A  1  420 ? 87.292  -31.232 26.771  1.00 146.84 ?  420 LYS A CD  1 
ATOM   3124  C  CE  . LYS A  1  420 ? 85.855  -31.207 27.245  1.00 152.78 ?  420 LYS A CE  1 
ATOM   3125  N  NZ  . LYS A  1  420 ? 85.667  -32.001 28.481  1.00 152.61 ?  420 LYS A NZ  1 
ATOM   3126  N  N   . HIS A  1  421 ? 91.318  -30.631 22.860  1.00 208.44 ?  421 HIS A N   1 
ATOM   3127  C  CA  . HIS A  1  421 ? 92.784  -30.634 22.605  1.00 210.37 ?  421 HIS A CA  1 
ATOM   3128  C  C   . HIS A  1  421 ? 93.122  -29.614 21.511  1.00 203.61 ?  421 HIS A C   1 
ATOM   3129  O  O   . HIS A  1  421 ? 94.294  -29.185 21.429  1.00 207.93 ?  421 HIS A O   1 
ATOM   3130  C  CB  . HIS A  1  421 ? 93.256  -32.054 22.277  1.00 210.87 ?  421 HIS A CB  1 
ATOM   3131  C  CG  . HIS A  1  421 ? 92.954  -33.008 23.381  1.00 210.10 ?  421 HIS A CG  1 
ATOM   3132  N  ND1 . HIS A  1  421 ? 92.675  -34.343 23.183  1.00 195.03 ?  421 HIS A ND1 1 
ATOM   3133  C  CD2 . HIS A  1  421 ? 92.873  -32.800 24.702  1.00 197.96 ?  421 HIS A CD2 1 
ATOM   3134  C  CE1 . HIS A  1  421 ? 92.442  -34.916 24.356  1.00 182.86 ?  421 HIS A CE1 1 
ATOM   3135  N  NE2 . HIS A  1  421 ? 92.560  -33.998 25.291  1.00 182.41 ?  421 HIS A NE2 1 
ATOM   3136  N  N   . PHE A  1  422 ? 92.129  -29.228 20.704  1.00 184.21 ?  422 PHE A N   1 
ATOM   3137  C  CA  . PHE A  1  422 ? 92.381  -28.235 19.665  1.00 177.40 ?  422 PHE A CA  1 
ATOM   3138  C  C   . PHE A  1  422 ? 92.713  -26.917 20.370  1.00 171.47 ?  422 PHE A C   1 
ATOM   3139  O  O   . PHE A  1  422 ? 93.770  -26.343 20.127  1.00 161.64 ?  422 PHE A O   1 
ATOM   3140  C  CB  . PHE A  1  422 ? 91.176  -28.094 18.711  1.00 162.79 ?  422 PHE A CB  1 
ATOM   3141  C  CG  . PHE A  1  422 ? 91.062  -29.095 17.582  1.00 154.53 ?  422 PHE A CG  1 
ATOM   3142  C  CD1 . PHE A  1  422 ? 92.176  -29.473 16.850  1.00 146.57 ?  422 PHE A CD1 1 
ATOM   3143  C  CD2 . PHE A  1  422 ? 89.830  -29.597 17.203  1.00 160.40 ?  422 PHE A CD2 1 
ATOM   3144  C  CE1 . PHE A  1  422 ? 92.063  -30.366 15.794  1.00 146.03 ?  422 PHE A CE1 1 
ATOM   3145  C  CE2 . PHE A  1  422 ? 89.721  -30.489 16.145  1.00 155.97 ?  422 PHE A CE2 1 
ATOM   3146  C  CZ  . PHE A  1  422 ? 90.837  -30.870 15.449  1.00 149.62 ?  422 PHE A CZ  1 
ATOM   3147  N  N   . GLY A  1  423 ? 91.825  -26.464 21.248  1.00 169.09 ?  423 GLY A N   1 
ATOM   3148  C  CA  . GLY A  1  423 ? 92.043  -25.233 21.994  1.00 169.42 ?  423 GLY A CA  1 
ATOM   3149  C  C   . GLY A  1  423 ? 93.333  -25.223 22.791  1.00 182.44 ?  423 GLY A C   1 
ATOM   3150  O  O   . GLY A  1  423 ? 93.972  -24.178 22.921  1.00 186.81 ?  423 GLY A O   1 
ATOM   3151  N  N   . GLU A  1  424 ? 93.730  -26.390 23.330  1.00 181.48 ?  424 GLU A N   1 
ATOM   3152  C  CA  . GLU A  1  424 ? 94.963  -26.522 24.111  1.00 174.18 ?  424 GLU A CA  1 
ATOM   3153  C  C   . GLU A  1  424 ? 96.198  -26.402 23.212  1.00 174.75 ?  424 GLU A C   1 
ATOM   3154  O  O   . GLU A  1  424 ? 97.118  -25.663 23.550  1.00 177.41 ?  424 GLU A O   1 
ATOM   3155  C  CB  . GLU A  1  424 ? 94.997  -27.863 24.862  1.00 168.12 ?  424 GLU A CB  1 
ATOM   3156  C  CG  . GLU A  1  424 ? 93.969  -27.969 25.971  1.00 178.00 ?  424 GLU A CG  1 
ATOM   3157  C  CD  . GLU A  1  424 ? 94.142  -29.181 26.862  1.00 173.05 ?  424 GLU A CD  1 
ATOM   3158  O  OE1 . GLU A  1  424 ? 94.760  -30.171 26.408  1.00 177.89 ?  424 GLU A OE1 1 
ATOM   3159  O  OE2 . GLU A  1  424 ? 93.655  -29.144 28.014  1.00 159.81 ?  424 GLU A OE2 1 
ATOM   3160  N  N   . VAL A  1  425 ? 96.222  -27.124 22.077  1.00 180.11 ?  425 VAL A N   1 
ATOM   3161  C  CA  . VAL A  1  425 ? 97.344  -27.082 21.130  1.00 171.23 ?  425 VAL A CA  1 
ATOM   3162  C  C   . VAL A  1  425 ? 97.522  -25.654 20.595  1.00 169.40 ?  425 VAL A C   1 
ATOM   3163  O  O   . VAL A  1  425 ? 98.652  -25.197 20.439  1.00 170.34 ?  425 VAL A O   1 
ATOM   3164  C  CB  . VAL A  1  425 ? 97.150  -28.107 19.964  1.00 135.02 ?  425 VAL A CB  1 
ATOM   3165  C  CG1 . VAL A  1  425 ? 97.963  -27.725 18.727  1.00 130.20 ?  425 VAL A CG1 1 
ATOM   3166  C  CG2 . VAL A  1  425 ? 97.495  -29.526 20.405  1.00 135.35 ?  425 VAL A CG2 1 
ATOM   3167  N  N   . ILE A  1  426 ? 96.413  -24.953 20.317  1.00 163.72 ?  426 ILE A N   1 
ATOM   3168  C  CA  . ILE A  1  426 ? 96.471  -23.595 19.781  1.00 166.01 ?  426 ILE A CA  1 
ATOM   3169  C  C   . ILE A  1  426 ? 97.071  -22.673 20.862  1.00 174.08 ?  426 ILE A C   1 
ATOM   3170  O  O   . ILE A  1  426 ? 98.148  -22.116 20.644  1.00 170.26 ?  426 ILE A O   1 
ATOM   3171  C  CB  . ILE A  1  426 ? 95.100  -23.176 19.183  1.00 155.12 ?  426 ILE A CB  1 
ATOM   3172  C  CG1 . ILE A  1  426 ? 94.663  -24.118 18.024  1.00 156.29 ?  426 ILE A CG1 1 
ATOM   3173  C  CG2 . ILE A  1  426 ? 95.120  -21.715 18.727  1.00 170.24 ?  426 ILE A CG2 1 
ATOM   3174  C  CD1 . ILE A  1  426 ? 95.632  -24.256 16.825  1.00 158.48 ?  426 ILE A CD1 1 
ATOM   3175  N  N   . TYR A  1  427 ? 96.402  -22.528 22.005  1.00 181.33 ?  427 TYR A N   1 
ATOM   3176  C  CA  . TYR A  1  427 ? 96.948  -21.674 23.092  1.00 180.43 ?  427 TYR A CA  1 
ATOM   3177  C  C   . TYR A  1  427 ? 98.397  -21.981 23.461  1.00 184.19 ?  427 TYR A C   1 
ATOM   3178  O  O   . TYR A  1  427 ? 99.182  -21.030 23.646  1.00 189.48 ?  427 TYR A O   1 
ATOM   3179  C  CB  . TYR A  1  427 ? 96.127  -21.820 24.370  1.00 195.61 ?  427 TYR A CB  1 
ATOM   3180  C  CG  . TYR A  1  427 ? 94.987  -20.847 24.500  1.00 209.65 ?  427 TYR A CG  1 
ATOM   3181  C  CD1 . TYR A  1  427 ? 95.158  -19.496 24.249  1.00 185.69 ?  427 TYR A CD1 1 
ATOM   3182  C  CD2 . TYR A  1  427 ? 93.732  -21.286 24.875  1.00 224.73 ?  427 TYR A CD2 1 
ATOM   3183  C  CE1 . TYR A  1  427 ? 94.106  -18.603 24.369  1.00 179.63 ?  427 TYR A CE1 1 
ATOM   3184  C  CE2 . TYR A  1  427 ? 92.669  -20.406 25.000  1.00 216.91 ?  427 TYR A CE2 1 
ATOM   3185  C  CZ  . TYR A  1  427 ? 92.856  -19.060 24.746  1.00 191.23 ?  427 TYR A CZ  1 
ATOM   3186  O  OH  . TYR A  1  427 ? 91.807  -18.181 24.867  1.00 159.80 ?  427 TYR A OH  1 
ATOM   3187  N  N   . ALA A  1  428 ? 98.740  -23.264 23.562  1.00 168.82 ?  428 ALA A N   1 
ATOM   3188  C  CA  . ALA A  1  428 ? 100.077 -23.658 24.022  1.00 167.02 ?  428 ALA A CA  1 
ATOM   3189  C  C   . ALA A  1  428 ? 101.125 -23.247 22.984  1.00 180.32 ?  428 ALA A C   1 
ATOM   3190  O  O   . ALA A  1  428 ? 102.194 -22.762 23.351  1.00 177.52 ?  428 ALA A O   1 
ATOM   3191  C  CB  . ALA A  1  428 ? 100.140 -25.159 24.256  1.00 152.93 ?  428 ALA A CB  1 
ATOM   3192  N  N   . LYS A  1  429 ? 100.821 -23.442 21.688  1.00 184.71 ?  429 LYS A N   1 
ATOM   3193  C  CA  . LYS A  1  429 ? 101.732 -23.060 20.606  1.00 171.84 ?  429 LYS A CA  1 
ATOM   3194  C  C   . LYS A  1  429 ? 101.755 -21.537 20.434  1.00 169.79 ?  429 LYS A C   1 
ATOM   3195  O  O   . LYS A  1  429 ? 102.780 -20.993 20.028  1.00 178.06 ?  429 LYS A O   1 
ATOM   3196  C  CB  . LYS A  1  429 ? 101.327 -23.727 19.280  1.00 153.31 ?  429 LYS A CB  1 
ATOM   3197  C  CG  . LYS A  1  429 ? 101.639 -25.220 19.202  1.00 149.39 ?  429 LYS A CG  1 
ATOM   3198  C  CD  . LYS A  1  429 ? 103.115 -25.516 18.903  1.00 138.05 ?  429 LYS A CD  1 
ATOM   3199  C  CE  . LYS A  1  429 ? 103.849 -26.110 20.079  1.00 162.87 ?  429 LYS A CE  1 
ATOM   3200  N  NZ  . LYS A  1  429 ? 105.099 -26.789 19.656  1.00 164.31 ?  429 LYS A NZ  1 
ATOM   3201  N  N   . MET A  1  430 ? 100.638 -20.873 20.740  1.00 166.64 ?  430 MET A N   1 
ATOM   3202  C  CA  . MET A  1  430 ? 100.582 -19.390 20.630  1.00 160.54 ?  430 MET A CA  1 
ATOM   3203  C  C   . MET A  1  430 ? 101.538 -18.776 21.659  1.00 167.62 ?  430 MET A C   1 
ATOM   3204  O  O   . MET A  1  430 ? 102.222 -17.797 21.308  1.00 171.86 ?  430 MET A O   1 
ATOM   3205  C  CB  . MET A  1  430 ? 99.161  -18.869 20.871  1.00 153.13 ?  430 MET A CB  1 
ATOM   3206  C  CG  . MET A  1  430 ? 98.187  -19.206 19.752  1.00 158.26 ?  430 MET A CG  1 
ATOM   3207  S  SD  . MET A  1  430 ? 98.599  -18.410 18.177  1.00 198.29 ?  430 MET A SD  1 
ATOM   3208  C  CE  . MET A  1  430 ? 97.121  -18.747 17.220  1.00 140.50 ?  430 MET A CE  1 
ATOM   3209  N  N   . LEU A  1  431 ? 101.586 -19.333 22.874  1.00 156.34 ?  431 LEU A N   1 
ATOM   3210  C  CA  . LEU A  1  431 ? 102.459 -18.810 23.924  1.00 166.77 ?  431 LEU A CA  1 
ATOM   3211  C  C   . LEU A  1  431 ? 103.930 -19.147 23.621  1.00 184.74 ?  431 LEU A C   1 
ATOM   3212  O  O   . LEU A  1  431 ? 104.817 -18.371 23.969  1.00 194.74 ?  431 LEU A O   1 
ATOM   3213  C  CB  . LEU A  1  431 ? 102.076 -19.394 25.296  1.00 173.33 ?  431 LEU A CB  1 
ATOM   3214  C  CG  . LEU A  1  431 ? 100.797 -18.854 25.944  1.00 173.75 ?  431 LEU A CG  1 
ATOM   3215  C  CD1 . LEU A  1  431 ? 100.348 -19.757 27.084  1.00 175.33 ?  431 LEU A CD1 1 
ATOM   3216  C  CD2 . LEU A  1  431 ? 100.994 -17.432 26.460  1.00 185.74 ?  431 LEU A CD2 1 
ATOM   3217  N  N   . ASP A  1  432 ? 104.188 -20.301 22.985  1.00 171.28 ?  432 ASP A N   1 
ATOM   3218  C  CA  . ASP A  1  432 ? 105.543 -20.733 22.643  1.00 176.39 ?  432 ASP A CA  1 
ATOM   3219  C  C   . ASP A  1  432 ? 106.129 -19.894 21.498  1.00 179.90 ?  432 ASP A C   1 
ATOM   3220  O  O   . ASP A  1  432 ? 107.238 -19.377 21.631  1.00 179.37 ?  432 ASP A O   1 
ATOM   3221  C  CB  . ASP A  1  432 ? 105.538 -22.234 22.280  1.00 163.41 ?  432 ASP A CB  1 
ATOM   3222  C  CG  . ASP A  1  432 ? 106.872 -22.789 21.821  1.00 155.02 ?  432 ASP A CG  1 
ATOM   3223  O  OD1 . ASP A  1  432 ? 107.874 -22.592 22.538  1.00 166.36 ?  432 ASP A OD1 1 
ATOM   3224  O  OD2 . ASP A  1  432 ? 106.910 -23.432 20.750  1.00 160.60 ?  432 ASP A OD2 1 
ATOM   3225  N  N   . GLU A  1  433 ? 105.391 -19.749 20.385  1.00 203.28 ?  433 GLU A N   1 
ATOM   3226  C  CA  . GLU A  1  433 ? 105.865 -18.985 19.228  1.00 206.69 ?  433 GLU A CA  1 
ATOM   3227  C  C   . GLU A  1  433 ? 105.676 -17.471 19.401  1.00 204.79 ?  433 GLU A C   1 
ATOM   3228  O  O   . GLU A  1  433 ? 106.621 -16.709 19.195  1.00 203.65 ?  433 GLU A O   1 
ATOM   3229  C  CB  . GLU A  1  433 ? 105.154 -19.452 17.934  1.00 209.10 ?  433 GLU A CB  1 
ATOM   3230  C  CG  . GLU A  1  433 ? 105.458 -20.885 17.515  1.00 196.42 ?  433 GLU A CG  1 
ATOM   3231  C  CD  . GLU A  1  433 ? 106.921 -21.200 17.282  1.00 217.75 ?  433 GLU A CD  1 
ATOM   3232  O  OE1 . GLU A  1  433 ? 107.634 -20.347 16.706  1.00 241.97 ?  433 GLU A OE1 1 
ATOM   3233  O  OE2 . GLU A  1  433 ? 107.352 -22.311 17.667  1.00 213.04 ?  433 GLU A OE2 1 
ATOM   3234  N  N   . PHE A  1  434 ? 104.483 -17.047 19.830  1.00 193.86 ?  434 PHE A N   1 
ATOM   3235  C  CA  . PHE A  1  434 ? 104.185 -15.587 19.915  1.00 191.72 ?  434 PHE A CA  1 
ATOM   3236  C  C   . PHE A  1  434 ? 104.356 -15.080 21.351  1.00 194.81 ?  434 PHE A C   1 
ATOM   3237  O  O   . PHE A  1  434 ? 103.722 -14.068 21.706  1.00 194.93 ?  434 PHE A O   1 
ATOM   3238  C  CB  . PHE A  1  434 ? 102.807 -15.337 19.298  1.00 185.24 ?  434 PHE A CB  1 
ATOM   3239  C  CG  . PHE A  1  434 ? 102.685 -15.990 17.946  1.00 198.07 ?  434 PHE A CG  1 
ATOM   3240  C  CD1 . PHE A  1  434 ? 103.737 -15.926 17.046  1.00 192.37 ?  434 PHE A CD1 1 
ATOM   3241  C  CD2 . PHE A  1  434 ? 101.555 -16.707 17.589  1.00 197.91 ?  434 PHE A CD2 1 
ATOM   3242  C  CE1 . PHE A  1  434 ? 103.655 -16.541 15.809  1.00 183.50 ?  434 PHE A CE1 1 
ATOM   3243  C  CE2 . PHE A  1  434 ? 101.471 -17.318 16.347  1.00 189.61 ?  434 PHE A CE2 1 
ATOM   3244  C  CZ  . PHE A  1  434 ? 102.518 -17.232 15.460  1.00 186.26 ?  434 PHE A CZ  1 
ATOM   3245  N  N   . GLY A  1  435 ? 105.198 -15.748 22.139  1.00 186.09 ?  435 GLY A N   1 
ATOM   3246  C  CA  . GLY A  1  435 ? 105.498 -15.325 23.500  1.00 181.09 ?  435 GLY A CA  1 
ATOM   3247  C  C   . GLY A  1  435 ? 105.884 -13.880 23.734  1.00 191.83 ?  435 GLY A C   1 
ATOM   3248  O  O   . GLY A  1  435 ? 105.539 -13.301 24.766  1.00 196.13 ?  435 GLY A O   1 
ATOM   3249  N  N   . SER A  1  436 ? 106.604 -13.283 22.775  1.00 206.60 ?  436 SER A N   1 
ATOM   3250  C  CA  . SER A  1  436 ? 107.050 -11.896 22.866  1.00 207.77 ?  436 SER A CA  1 
ATOM   3251  C  C   . SER A  1  436 ? 105.929 -10.885 22.584  1.00 202.93 ?  436 SER A C   1 
ATOM   3252  O  O   . SER A  1  436 ? 106.026 -9.739  23.026  1.00 196.06 ?  436 SER A O   1 
ATOM   3253  C  CB  . SER A  1  436 ? 108.203 -11.658 21.896  1.00 213.48 ?  436 SER A CB  1 
ATOM   3254  O  OG  . SER A  1  436 ? 107.873 -12.090 20.586  1.00 203.57 ?  436 SER A OG  1 
ATOM   3255  N  N   . VAL A  1  437 ? 104.876 -11.292 21.852  1.00 189.90 ?  437 VAL A N   1 
ATOM   3256  C  CA  . VAL A  1  437 ? 103.771 -10.388 21.517  1.00 187.41 ?  437 VAL A CA  1 
ATOM   3257  C  C   . VAL A  1  437 ? 102.462 -10.737 22.253  1.00 178.79 ?  437 VAL A C   1 
ATOM   3258  O  O   . VAL A  1  437 ? 101.578 -9.885  22.324  1.00 168.91 ?  437 VAL A O   1 
ATOM   3259  C  CB  . VAL A  1  437 ? 103.564 -10.266 19.981  1.00 177.56 ?  437 VAL A CB  1 
ATOM   3260  C  CG1 . VAL A  1  437 ? 104.796 -9.665  19.309  1.00 171.50 ?  437 VAL A CG1 1 
ATOM   3261  C  CG2 . VAL A  1  437 ? 103.213 -11.606 19.345  1.00 171.91 ?  437 VAL A CG2 1 
ATOM   3262  N  N   . VAL A  1  438 ? 102.369 -11.966 22.770  1.00 185.17 ?  438 VAL A N   1 
ATOM   3263  C  CA  . VAL A  1  438 ? 101.144 -12.415 23.499  1.00 172.92 ?  438 VAL A CA  1 
ATOM   3264  C  C   . VAL A  1  438 ? 101.322 -12.104 24.989  1.00 177.82 ?  438 VAL A C   1 
ATOM   3265  O  O   . VAL A  1  438 ? 102.335 -12.568 25.548  1.00 173.92 ?  438 VAL A O   1 
ATOM   3266  C  CB  . VAL A  1  438 ? 100.880 -13.915 23.270  1.00 160.72 ?  438 VAL A CB  1 
ATOM   3267  C  CG1 . VAL A  1  438 ? 99.922  -14.491 24.301  1.00 161.98 ?  438 VAL A CG1 1 
ATOM   3268  C  CG2 . VAL A  1  438 ? 100.394 -14.197 21.856  1.00 160.09 ?  438 VAL A CG2 1 
ATOM   3269  N  N   . THR A  1  444 ? 88.093  -20.672 21.284  1.00 137.25 ?  444 THR A N   1 
ATOM   3270  C  CA  . THR A  1  444 ? 86.695  -21.120 21.529  1.00 141.05 ?  444 THR A CA  1 
ATOM   3271  C  C   . THR A  1  444 ? 86.180  -21.876 20.299  1.00 154.24 ?  444 THR A C   1 
ATOM   3272  O  O   . THR A  1  444 ? 86.060  -21.244 19.230  1.00 155.84 ?  444 THR A O   1 
ATOM   3273  C  CB  . THR A  1  444 ? 85.794  -19.932 21.888  1.00 140.60 ?  444 THR A CB  1 
ATOM   3274  O  OG1 . THR A  1  444 ? 86.243  -19.396 23.133  1.00 144.90 ?  444 THR A OG1 1 
ATOM   3275  C  CG2 . THR A  1  444 ? 84.334  -20.314 21.991  1.00 154.14 ?  444 THR A CG2 1 
ATOM   3276  N  N   . ILE A  1  445 ? 85.907  -23.177 20.442  1.00 159.31 ?  445 ILE A N   1 
ATOM   3277  C  CA  . ILE A  1  445 ? 85.389  -23.990 19.301  1.00 153.63 ?  445 ILE A CA  1 
ATOM   3278  C  C   . ILE A  1  445 ? 83.860  -23.918 19.297  1.00 149.68 ?  445 ILE A C   1 
ATOM   3279  O  O   . ILE A  1  445 ? 83.267  -23.862 20.392  1.00 158.30 ?  445 ILE A O   1 
ATOM   3280  C  CB  . ILE A  1  445 ? 85.880  -25.449 19.372  1.00 136.98 ?  445 ILE A CB  1 
ATOM   3281  C  CG1 . ILE A  1  445 ? 87.386  -25.528 19.625  1.00 127.69 ?  445 ILE A CG1 1 
ATOM   3282  C  CG2 . ILE A  1  445 ? 85.481  -26.213 18.119  1.00 147.77 ?  445 ILE A CG2 1 
ATOM   3283  C  CD1 . ILE A  1  445 ? 87.734  -25.866 21.048  1.00 160.83 ?  445 ILE A CD1 1 
ATOM   3284  N  N   . ILE A  1  446 ? 83.257  -23.922 18.107  1.00 143.31 ?  446 ILE A N   1 
ATOM   3285  C  CA  . ILE A  1  446 ? 81.768  -23.875 17.992  1.00 145.49 ?  446 ILE A CA  1 
ATOM   3286  C  C   . ILE A  1  446 ? 81.297  -24.936 16.992  1.00 160.93 ?  446 ILE A C   1 
ATOM   3287  O  O   . ILE A  1  446 ? 81.504  -24.736 15.780  1.00 166.24 ?  446 ILE A O   1 
ATOM   3288  C  CB  . ILE A  1  446 ? 81.288  -22.464 17.596  1.00 154.50 ?  446 ILE A CB  1 
ATOM   3289  C  CG1 . ILE A  1  446 ? 81.530  -21.450 18.717  1.00 159.11 ?  446 ILE A CG1 1 
ATOM   3290  C  CG2 . ILE A  1  446 ? 79.829  -22.493 17.170  1.00 157.76 ?  446 ILE A CG2 1 
ATOM   3291  C  CD1 . ILE A  1  446 ? 82.790  -20.635 18.545  1.00 154.73 ?  446 ILE A CD1 1 
ATOM   3292  N  N   . THR A  1  447 ? 80.715  -26.030 17.482  1.00 180.28 ?  447 THR A N   1 
ATOM   3293  C  CA  . THR A  1  447 ? 80.159  -27.052 16.554  1.00 181.72 ?  447 THR A CA  1 
ATOM   3294  C  C   . THR A  1  447 ? 78.632  -26.865 16.524  1.00 184.67 ?  447 THR A C   1 
ATOM   3295  O  O   . THR A  1  447 ? 77.954  -27.731 15.939  1.00 170.16 ?  447 THR A O   1 
ATOM   3296  C  CB  . THR A  1  447 ? 80.721  -28.446 16.891  1.00 171.77 ?  447 THR A CB  1 
ATOM   3297  O  OG1 . THR A  1  447 ? 80.438  -28.716 18.264  1.00 176.46 ?  447 THR A OG1 1 
ATOM   3298  C  CG2 . THR A  1  447 ? 82.215  -28.579 16.635  1.00 177.02 ?  447 THR A CG2 1 
ATOM   3299  N  N   . ASP A  1  448 ? 78.143  -25.750 17.076  1.00 202.54 ?  448 ASP A N   1 
ATOM   3300  C  CA  . ASP A  1  448 ? 76.690  -25.438 17.059  1.00 201.46 ?  448 ASP A CA  1 
ATOM   3301  C  C   . ASP A  1  448 ? 76.407  -24.512 15.873  1.00 206.32 ?  448 ASP A C   1 
ATOM   3302  O  O   . ASP A  1  448 ? 77.099  -23.483 15.750  1.00 212.66 ?  448 ASP A O   1 
ATOM   3303  C  CB  . ASP A  1  448 ? 76.260  -24.806 18.384  1.00 198.61 ?  448 ASP A CB  1 
ATOM   3304  C  CG  . ASP A  1  448 ? 74.845  -24.254 18.395  1.00 198.52 ?  448 ASP A CG  1 
ATOM   3305  O  OD1 . ASP A  1  448 ? 74.490  -23.509 17.460  1.00 197.77 ?  448 ASP A OD1 1 
ATOM   3306  O  OD2 . ASP A  1  448 ? 74.115  -24.559 19.354  1.00 203.83 -1 448 ASP A OD2 1 
ATOM   3307  N  N   . PRO A  1  449 ? 75.421  -24.821 15.004  1.00 188.96 ?  449 PRO A N   1 
ATOM   3308  C  CA  . PRO A  1  449 ? 75.157  -24.002 13.818  1.00 185.53 ?  449 PRO A CA  1 
ATOM   3309  C  C   . PRO A  1  449 ? 74.888  -22.527 14.142  1.00 191.50 ?  449 PRO A C   1 
ATOM   3310  O  O   . PRO A  1  449 ? 75.488  -21.683 13.501  1.00 187.58 ?  449 PRO A O   1 
ATOM   3311  C  CB  . PRO A  1  449 ? 73.877  -24.624 13.241  1.00 169.33 ?  449 PRO A CB  1 
ATOM   3312  C  CG  . PRO A  1  449 ? 73.913  -26.056 13.723  1.00 153.27 ?  449 PRO A CG  1 
ATOM   3313  C  CD  . PRO A  1  449 ? 74.526  -25.975 15.105  1.00 171.02 ?  449 PRO A CD  1 
ATOM   3314  N  N   . GLY A  1  450 ? 74.015  -22.245 15.115  1.00 198.88 ?  450 GLY A N   1 
ATOM   3315  C  CA  . GLY A  1  450 ? 73.658  -20.859 15.372  1.00 194.14 ?  450 GLY A CA  1 
ATOM   3316  C  C   . GLY A  1  450 ? 74.862  -20.000 15.711  1.00 198.75 ?  450 GLY A C   1 
ATOM   3317  O  O   . GLY A  1  450 ? 75.067  -18.936 15.119  1.00 203.67 ?  450 GLY A O   1 
ATOM   3318  N  N   . LYS A  1  451 ? 75.684  -20.455 16.662  1.00 191.75 ?  451 LYS A N   1 
ATOM   3319  C  CA  . LYS A  1  451 ? 76.830  -19.657 17.085  1.00 192.49 ?  451 LYS A CA  1 
ATOM   3320  C  C   . LYS A  1  451 ? 77.794  -19.508 15.914  1.00 198.66 ?  451 LYS A C   1 
ATOM   3321  O  O   . LYS A  1  451 ? 78.255  -18.395 15.637  1.00 203.77 ?  451 LYS A O   1 
ATOM   3322  C  CB  . LYS A  1  451 ? 77.415  -20.212 18.384  1.00 187.45 ?  451 LYS A CB  1 
ATOM   3323  C  CG  . LYS A  1  451 ? 76.539  -19.969 19.603  1.00 190.46 ?  451 LYS A CG  1 
ATOM   3324  C  CD  . LYS A  1  451 ? 77.355  -19.979 20.886  1.00 189.41 ?  451 LYS A CD  1 
ATOM   3325  C  CE  . LYS A  1  451 ? 77.913  -18.601 21.214  1.00 194.13 ?  451 LYS A CE  1 
ATOM   3326  N  NZ  . LYS A  1  451 ? 76.850  -17.650 21.638  1.00 178.72 ?  451 LYS A NZ  1 
ATOM   3327  N  N   . ALA A  1  452 ? 78.117  -20.603 15.221  1.00 192.50 ?  452 ALA A N   1 
ATOM   3328  C  CA  . ALA A  1  452 ? 78.879  -20.474 13.983  1.00 192.03 ?  452 ALA A CA  1 
ATOM   3329  C  C   . ALA A  1  452 ? 78.391  -19.376 13.050  1.00 197.71 ?  452 ALA A C   1 
ATOM   3330  O  O   . ALA A  1  452 ? 79.192  -18.604 12.512  1.00 189.12 ?  452 ALA A O   1 
ATOM   3331  C  CB  . ALA A  1  452 ? 78.974  -21.808 13.243  1.00 167.66 ?  452 ALA A CB  1 
ATOM   3332  N  N   . GLU A  1  453 ? 77.071  -19.304 12.857  1.00 207.95 ?  453 GLU A N   1 
ATOM   3333  C  CA  . GLU A  1  453 ? 76.499  -18.313 11.906  1.00 204.09 ?  453 GLU A CA  1 
ATOM   3334  C  C   . GLU A  1  453 ? 76.806  -16.887 12.375  1.00 213.46 ?  453 GLU A C   1 
ATOM   3335  O  O   . GLU A  1  453 ? 77.616  -16.213 11.708  1.00 214.25 ?  453 GLU A O   1 
ATOM   3336  C  CB  . GLU A  1  453 ? 74.988  -18.514 11.780  1.00 197.49 ?  453 GLU A CB  1 
ATOM   3337  C  CG  . GLU A  1  453 ? 74.606  -19.824 11.117  1.00 197.26 ?  453 GLU A CG  1 
ATOM   3338  C  CD  . GLU A  1  453 ? 73.111  -20.078 11.046  1.00 207.84 ?  453 GLU A CD  1 
ATOM   3339  O  OE1 . GLU A  1  453 ? 72.353  -19.321 11.683  1.00 203.43 ?  453 GLU A OE1 1 
ATOM   3340  O  OE2 . GLU A  1  453 ? 72.708  -21.034 10.353  1.00 215.39 -1 453 GLU A OE2 1 
ATOM   3341  N  N   . GLU A  1  454 ? 76.176  -16.452 13.468  1.00 205.33 ?  454 GLU A N   1 
ATOM   3342  C  CA  . GLU A  1  454 ? 76.361  -15.061 13.961  1.00 199.95 ?  454 GLU A CA  1 
ATOM   3343  C  C   . GLU A  1  454 ? 77.863  -14.764 14.006  1.00 206.07 ?  454 GLU A C   1 
ATOM   3344  O  O   . GLU A  1  454 ? 78.288  -13.816 13.324  1.00 207.61 ?  454 GLU A O   1 
ATOM   3345  C  CB  . GLU A  1  454 ? 75.699  -14.891 15.329  1.00 191.78 ?  454 GLU A CB  1 
ATOM   3346  C  CG  . GLU A  1  454 ? 74.185  -14.996 15.281  1.00 200.59 ?  454 GLU A CG  1 
ATOM   3347  C  CD  . GLU A  1  454 ? 73.496  -14.904 16.632  1.00 222.29 ?  454 GLU A CD  1 
ATOM   3348  O  OE1 . GLU A  1  454 ? 74.202  -14.944 17.660  1.00 221.29 ?  454 GLU A OE1 1 
ATOM   3349  O  OE2 . GLU A  1  454 ? 72.255  -14.791 16.651  1.00 239.74 -1 454 GLU A OE2 1 
ATOM   3350  N  N   . LEU A  1  455 ? 78.627  -15.540 14.777  1.00 205.63 ?  455 LEU A N   1 
ATOM   3351  C  CA  . LEU A  1  455 ? 80.080  -15.261 14.938  1.00 203.75 ?  455 LEU A CA  1 
ATOM   3352  C  C   . LEU A  1  455 ? 80.787  -15.128 13.586  1.00 207.95 ?  455 LEU A C   1 
ATOM   3353  O  O   . LEU A  1  455 ? 81.647  -14.235 13.460  1.00 219.10 ?  455 LEU A O   1 
ATOM   3354  C  CB  . LEU A  1  455 ? 80.706  -16.393 15.757  1.00 201.48 ?  455 LEU A CB  1 
ATOM   3355  C  CG  . LEU A  1  455 ? 80.939  -16.078 17.233  1.00 179.89 ?  455 LEU A CG  1 
ATOM   3356  C  CD1 . LEU A  1  455 ? 81.989  -17.006 17.823  1.00 178.10 ?  455 LEU A CD1 1 
ATOM   3357  C  CD2 . LEU A  1  455 ? 81.350  -14.625 17.412  1.00 180.36 ?  455 LEU A CD2 1 
ATOM   3358  N  N   . GLU A  1  456 ? 80.481  -16.017 12.632  1.00 201.58 ?  456 GLU A N   1 
ATOM   3359  C  CA  . GLU A  1  456 ? 81.124  -15.958 11.291  1.00 198.38 ?  456 GLU A CA  1 
ATOM   3360  C  C   . GLU A  1  456 ? 81.149  -14.500 10.838  1.00 203.73 ?  456 GLU A C   1 
ATOM   3361  O  O   . GLU A  1  456 ? 82.240  -13.995 10.509  1.00 200.43 ?  456 GLU A O   1 
ATOM   3362  C  CB  . GLU A  1  456 ? 80.349  -16.761 10.245  1.00 186.98 ?  456 GLU A CB  1 
ATOM   3363  C  CG  . GLU A  1  456 ? 81.231  -17.430 9.218   1.00 169.76 ?  456 GLU A CG  1 
ATOM   3364  C  CD  . GLU A  1  456 ? 80.711  -18.795 8.811   1.00 174.05 ?  456 GLU A CD  1 
ATOM   3365  O  OE1 . GLU A  1  456 ? 79.490  -19.022 8.919   1.00 184.24 ?  456 GLU A OE1 1 
ATOM   3366  O  OE2 . GLU A  1  456 ? 81.537  -19.629 8.391   1.00 173.12 -1 456 GLU A OE2 1 
ATOM   3367  N  N   . GLY A  1  457 ? 79.979  -13.860 10.825  1.00 206.73 ?  457 GLY A N   1 
ATOM   3368  C  CA  . GLY A  1  457 ? 79.895  -12.464 10.353  1.00 196.25 ?  457 GLY A CA  1 
ATOM   3369  C  C   . GLY A  1  457 ? 79.986  -11.366 11.398  1.00 199.48 ?  457 GLY A C   1 
ATOM   3370  O  O   . GLY A  1  457 ? 80.126  -10.193 11.003  1.00 199.54 ?  457 GLY A O   1 
ATOM   3371  N  N   . LYS A  1  458 ? 79.899  -11.729 12.682  1.00 191.10 ?  458 LYS A N   1 
ATOM   3372  C  CA  . LYS A  1  458 ? 79.959  -10.728 13.780  1.00 176.88 ?  458 LYS A CA  1 
ATOM   3373  C  C   . LYS A  1  458 ? 81.403  -10.243 13.890  1.00 193.07 ?  458 LYS A C   1 
ATOM   3374  O  O   . LYS A  1  458 ? 81.601  -9.029  14.086  1.00 189.75 ?  458 LYS A O   1 
ATOM   3375  C  CB  . LYS A  1  458 ? 79.603  -11.362 15.127  1.00 183.09 ?  458 LYS A CB  1 
ATOM   3376  C  CG  . LYS A  1  458 ? 79.697  -10.463 16.352  1.00 194.27 ?  458 LYS A CG  1 
ATOM   3377  C  CD  . LYS A  1  458 ? 78.766  -9.275  16.331  1.00 195.27 ?  458 LYS A CD  1 
ATOM   3378  C  CE  . LYS A  1  458 ? 78.779  -8.515  17.640  1.00 188.48 ?  458 LYS A CE  1 
ATOM   3379  N  NZ  . LYS A  1  458 ? 78.033  -7.239  17.541  1.00 180.25 ?  458 LYS A NZ  1 
ATOM   3380  N  N   . TYR A  1  459 ? 82.378  -11.147 13.771  1.00 226.87 ?  459 TYR A N   1 
ATOM   3381  C  CA  . TYR A  1  459 ? 83.790  -10.736 13.993  1.00 225.06 ?  459 TYR A CA  1 
ATOM   3382  C  C   . TYR A  1  459 ? 84.692  -11.103 12.811  1.00 229.54 ?  459 TYR A C   1 
ATOM   3383  O  O   . TYR A  1  459 ? 85.463  -10.231 12.362  1.00 237.68 ?  459 TYR A O   1 
ATOM   3384  C  CB  . TYR A  1  459 ? 84.323  -11.389 15.270  1.00 225.31 ?  459 TYR A CB  1 
ATOM   3385  C  CG  . TYR A  1  459 ? 83.606  -10.964 16.525  1.00 231.88 ?  459 TYR A CG  1 
ATOM   3386  C  CD1 . TYR A  1  459 ? 83.249  -9.642  16.729  1.00 233.86 ?  459 TYR A CD1 1 
ATOM   3387  C  CD2 . TYR A  1  459 ? 83.279  -11.882 17.508  1.00 224.78 ?  459 TYR A CD2 1 
ATOM   3388  C  CE1 . TYR A  1  459 ? 82.587  -9.241  17.877  1.00 237.40 ?  459 TYR A CE1 1 
ATOM   3389  C  CE2 . TYR A  1  459 ? 82.617  -11.498 18.663  1.00 225.87 ?  459 TYR A CE2 1 
ATOM   3390  C  CZ  . TYR A  1  459 ? 82.269  -10.173 18.848  1.00 237.14 ?  459 TYR A CZ  1 
ATOM   3391  O  OH  . TYR A  1  459 ? 81.613  -9.783  19.990  1.00 235.33 ?  459 TYR A OH  1 
ATOM   3392  N  N   . ALA A  1  460 ? 84.611  -12.346 12.333  1.00 233.00 ?  460 ALA A N   1 
ATOM   3393  C  CA  . ALA A  1  460 ? 85.525  -12.787 11.253  1.00 231.52 ?  460 ALA A CA  1 
ATOM   3394  C  C   . ALA A  1  460 ? 85.276  -11.930 10.008  1.00 232.18 ?  460 ALA A C   1 
ATOM   3395  O  O   . ALA A  1  460 ? 86.192  -11.177 9.627   1.00 237.87 ?  460 ALA A O   1 
ATOM   3396  C  CB  . ALA A  1  460 ? 85.332  -14.251 10.963  1.00 229.95 ?  460 ALA A CB  1 
ATOM   3397  N  N   . VAL A  1  461 ? 84.094  -12.044 9.393   1.00 199.64 ?  461 VAL A N   1 
ATOM   3398  C  CA  . VAL A  1  461 ? 83.883  -11.292 8.119   1.00 191.78 ?  461 VAL A CA  1 
ATOM   3399  C  C   . VAL A  1  461 ? 84.393  -9.855  8.279   1.00 197.25 ?  461 VAL A C   1 
ATOM   3400  O  O   . VAL A  1  461 ? 85.180  -9.419  7.417   1.00 192.51 ?  461 VAL A O   1 
ATOM   3401  C  CB  . VAL A  1  461 ? 82.405  -11.329 7.684   1.00 171.43 ?  461 VAL A CB  1 
ATOM   3402  C  CG1 . VAL A  1  461 ? 82.023  -10.100 6.874   1.00 164.06 ?  461 VAL A CG1 1 
ATOM   3403  C  CG2 . VAL A  1  461 ? 82.090  -12.600 6.913   1.00 175.34 ?  461 VAL A CG2 1 
ATOM   3404  N  N   . PRO A  1  462 ? 84.002  -9.100  9.330   1.00 192.97 ?  462 PRO A N   1 
ATOM   3405  C  CA  . PRO A  1  462 ? 84.536  -7.757  9.545   1.00 169.04 ?  462 PRO A CA  1 
ATOM   3406  C  C   . PRO A  1  462 ? 86.067  -7.790  9.489   1.00 186.88 ?  462 PRO A C   1 
ATOM   3407  O  O   . PRO A  1  462 ? 86.635  -7.128  8.639   1.00 184.04 ?  462 PRO A O   1 
ATOM   3408  C  CB  . PRO A  1  462 ? 84.080  -7.419  10.969  1.00 155.53 ?  462 PRO A CB  1 
ATOM   3409  C  CG  . PRO A  1  462 ? 82.804  -8.208  11.141  1.00 168.97 ?  462 PRO A CG  1 
ATOM   3410  C  CD  . PRO A  1  462 ? 83.032  -9.484  10.358  1.00 193.90 ?  462 PRO A CD  1 
ATOM   3411  N  N   . ARG A  1  463 ? 86.688  -8.561  10.386  1.00 221.46 ?  463 ARG A N   1 
ATOM   3412  C  CA  . ARG A  1  463 ? 88.172  -8.650  10.427  1.00 215.27 ?  463 ARG A CA  1 
ATOM   3413  C  C   . ARG A  1  463 ? 88.701  -8.893  9.012   1.00 216.11 ?  463 ARG A C   1 
ATOM   3414  O  O   . ARG A  1  463 ? 89.653  -8.198  8.610   1.00 218.47 ?  463 ARG A O   1 
ATOM   3415  C  CB  . ARG A  1  463 ? 88.600  -9.787  11.359  1.00 214.71 ?  463 ARG A CB  1 
ATOM   3416  C  CG  . ARG A  1  463 ? 89.652  -9.392  12.384  1.00 212.29 ?  463 ARG A CG  1 
ATOM   3417  C  CD  . ARG A  1  463 ? 89.307  -8.100  13.098  1.00 209.03 ?  463 ARG A CD  1 
ATOM   3418  N  NE  . ARG A  1  463 ? 90.498  -7.342  13.451  1.00 216.95 ?  463 ARG A NE  1 
ATOM   3419  C  CZ  . ARG A  1  463 ? 91.269  -6.703  12.578  1.00 217.71 ?  463 ARG A CZ  1 
ATOM   3420  N  NH1 . ARG A  1  463 ? 90.871  -6.557  11.326  1.00 209.11 ?  463 ARG A NH1 1 
ATOM   3421  N  NH2 . ARG A  1  463 ? 92.434  -6.211  12.961  1.00 217.97 ?  463 ARG A NH2 1 
ATOM   3422  N  N   . TYR A  1  464 ? 88.114  -9.848  8.287   1.00 199.60 ?  464 TYR A N   1 
ATOM   3423  C  CA  . TYR A  1  464 ? 88.557  -10.142 6.901   1.00 189.40 ?  464 TYR A CA  1 
ATOM   3424  C  C   . TYR A  1  464 ? 88.359  -8.916  6.019   1.00 185.37 ?  464 TYR A C   1 
ATOM   3425  O  O   . TYR A  1  464 ? 89.330  -8.443  5.406   1.00 183.41 ?  464 TYR A O   1 
ATOM   3426  C  CB  . TYR A  1  464 ? 87.695  -11.221 6.253   1.00 185.04 ?  464 TYR A CB  1 
ATOM   3427  C  CG  . TYR A  1  464 ? 87.650  -12.527 6.993   1.00 179.91 ?  464 TYR A CG  1 
ATOM   3428  C  CD1 . TYR A  1  464 ? 88.623  -12.852 7.920   1.00 178.27 ?  464 TYR A CD1 1 
ATOM   3429  C  CD2 . TYR A  1  464 ? 86.632  -13.434 6.758   1.00 166.13 ?  464 TYR A CD2 1 
ATOM   3430  C  CE1 . TYR A  1  464 ? 88.585  -14.052 8.605   1.00 172.68 ?  464 TYR A CE1 1 
ATOM   3431  C  CE2 . TYR A  1  464 ? 86.579  -14.639 7.431   1.00 161.52 ?  464 TYR A CE2 1 
ATOM   3432  C  CZ  . TYR A  1  464 ? 87.562  -14.945 8.352   1.00 176.47 ?  464 TYR A CZ  1 
ATOM   3433  O  OH  . TYR A  1  464 ? 87.515  -16.141 9.028   1.00 183.38 ?  464 TYR A OH  1 
ATOM   3434  N  N   . LYS A  1  465 ? 87.117  -8.443  5.935   1.00 183.92 ?  465 LYS A N   1 
ATOM   3435  C  CA  . LYS A  1  465 ? 86.830  -7.332  5.034   1.00 178.40 ?  465 LYS A CA  1 
ATOM   3436  C  C   . LYS A  1  465 ? 87.805  -6.183  5.255   1.00 186.58 ?  465 LYS A C   1 
ATOM   3437  O  O   . LYS A  1  465 ? 88.384  -5.652  4.300   1.00 179.61 ?  465 LYS A O   1 
ATOM   3438  C  CB  . LYS A  1  465 ? 85.388  -6.864  5.229   1.00 170.14 ?  465 LYS A CB  1 
ATOM   3439  C  CG  . LYS A  1  465 ? 84.987  -5.687  4.355   1.00 183.42 ?  465 LYS A CG  1 
ATOM   3440  C  CD  . LYS A  1  465 ? 83.650  -5.112  4.794   1.00 181.03 ?  465 LYS A CD  1 
ATOM   3441  C  CE  . LYS A  1  465 ? 83.074  -4.188  3.735   1.00 177.44 ?  465 LYS A CE  1 
ATOM   3442  N  NZ  . LYS A  1  465 ? 81.698  -3.734  4.084   1.00 167.90 ?  465 LYS A NZ  1 
ATOM   3443  N  N   . GLU A  1  466 ? 87.996  -5.784  6.515   1.00 197.82 ?  466 GLU A N   1 
ATOM   3444  C  CA  . GLU A  1  466 ? 88.992  -4.765  6.830   1.00 198.23 ?  466 GLU A CA  1 
ATOM   3445  C  C   . GLU A  1  466 ? 90.385  -5.218  6.413   1.00 197.10 ?  466 GLU A C   1 
ATOM   3446  O  O   . GLU A  1  466 ? 91.212  -4.404  5.984   1.00 189.83 ?  466 GLU A O   1 
ATOM   3447  C  CB  . GLU A  1  466 ? 88.957  -4.449  8.324   1.00 197.63 ?  466 GLU A CB  1 
ATOM   3448  C  CG  . GLU A  1  466 ? 89.339  -3.023  8.679   1.00 216.04 ?  466 GLU A CG  1 
ATOM   3449  C  CD  . GLU A  1  466 ? 89.034  -2.690  10.127  1.00 228.88 ?  466 GLU A CD  1 
ATOM   3450  O  OE1 . GLU A  1  466 ? 88.903  -3.630  10.940  1.00 217.49 ?  466 GLU A OE1 1 
ATOM   3451  O  OE2 . GLU A  1  466 ? 88.923  -1.489  10.452  1.00 234.16 -1 466 GLU A OE2 1 
ATOM   3452  N  N   . ARG A  1  467 ? 90.659  -6.518  6.530   1.00 191.65 ?  467 ARG A N   1 
ATOM   3453  C  CA  . ARG A  1  467 ? 91.947  -7.063  6.114   1.00 177.88 ?  467 ARG A CA  1 
ATOM   3454  C  C   . ARG A  1  467 ? 92.125  -6.946  4.605   1.00 180.66 ?  467 ARG A C   1 
ATOM   3455  O  O   . ARG A  1  467 ? 93.081  -6.325  4.124   1.00 184.45 ?  467 ARG A O   1 
ATOM   3456  C  CB  . ARG A  1  467 ? 92.051  -8.524  6.556   1.00 174.22 ?  467 ARG A CB  1 
ATOM   3457  C  CG  . ARG A  1  467 ? 93.421  -8.960  7.026   1.00 166.21 ?  467 ARG A CG  1 
ATOM   3458  C  CD  . ARG A  1  467 ? 93.334  -10.309 7.727   1.00 168.00 ?  467 ARG A CD  1 
ATOM   3459  N  NE  . ARG A  1  467 ? 92.709  -10.222 9.045   1.00 153.29 ?  467 ARG A NE  1 
ATOM   3460  C  CZ  . ARG A  1  467 ? 92.807  -11.166 9.977   1.00 153.31 ?  467 ARG A CZ  1 
ATOM   3461  N  NH1 . ARG A  1  467 ? 93.504  -12.266 9.736   1.00 150.54 ?  467 ARG A NH1 1 
ATOM   3462  N  NH2 . ARG A  1  467 ? 92.210  -11.010 11.150  1.00 158.79 ?  467 ARG A NH2 1 
ATOM   3463  N  N   . ASP A  1  468 ? 91.208  -7.548  3.848   1.00 179.16 ?  468 ASP A N   1 
ATOM   3464  C  CA  . ASP A  1  468 ? 91.290  -7.468  2.366   1.00 176.84 ?  468 ASP A CA  1 
ATOM   3465  C  C   . ASP A  1  468 ? 91.252  -6.000  1.941   1.00 189.05 ?  468 ASP A C   1 
ATOM   3466  O  O   . ASP A  1  468 ? 91.913  -5.658  0.941   1.00 182.11 ?  468 ASP A O   1 
ATOM   3467  C  CB  . ASP A  1  468 ? 90.150  -8.240  1.704   1.00 158.99 ?  468 ASP A CB  1 
ATOM   3468  C  CG  . ASP A  1  468 ? 90.258  -9.735  1.924   1.00 158.61 ?  468 ASP A CG  1 
ATOM   3469  O  OD1 . ASP A  1  468 ? 91.397  -10.227 2.052   1.00 154.68 ?  468 ASP A OD1 1 
ATOM   3470  O  OD2 . ASP A  1  468 ? 89.202  -10.396 1.977   1.00 177.84 -1 468 ASP A OD2 1 
ATOM   3471  N  N   . ALA A  1  469 ? 90.516  -5.171  2.682   1.00 194.06 ?  469 ALA A N   1 
ATOM   3472  C  CA  . ALA A  1  469 ? 90.350  -3.752  2.291   1.00 180.85 ?  469 ALA A CA  1 
ATOM   3473  C  C   . ALA A  1  469 ? 91.728  -3.119  2.076   1.00 174.19 ?  469 ALA A C   1 
ATOM   3474  O  O   . ALA A  1  469 ? 91.865  -2.298  1.150   1.00 188.17 ?  469 ALA A O   1 
ATOM   3475  C  CB  . ALA A  1  469 ? 89.569  -3.013  3.347   1.00 177.78 ?  469 ALA A CB  1 
ATOM   3476  N  N   . ARG A  1  470 ? 92.716  -3.517  2.882   1.00 173.79 ?  470 ARG A N   1 
ATOM   3477  C  CA  . ARG A  1  470 ? 94.092  -2.965  2.755   1.00 162.71 ?  470 ARG A CA  1 
ATOM   3478  C  C   . ARG A  1  470 ? 94.544  -3.032  1.292   1.00 195.55 ?  470 ARG A C   1 
ATOM   3479  O  O   . ARG A  1  470 ? 94.747  -1.959  0.691   1.00 194.63 ?  470 ARG A O   1 
ATOM   3480  C  CB  . ARG A  1  470 ? 95.058  -3.738  3.658   1.00 159.20 ?  470 ARG A CB  1 
ATOM   3481  C  CG  . ARG A  1  470 ? 94.745  -3.629  5.144   1.00 165.56 ?  470 ARG A CG  1 
ATOM   3482  C  CD  . ARG A  1  470 ? 94.931  -2.217  5.668   1.00 158.40 ?  470 ARG A CD  1 
ATOM   3483  N  NE  . ARG A  1  470 ? 94.654  -2.115  7.094   1.00 169.05 ?  470 ARG A NE  1 
ATOM   3484  C  CZ  . ARG A  1  470 ? 94.518  -0.972  7.757   1.00 197.37 ?  470 ARG A CZ  1 
ATOM   3485  N  NH1 . ARG A  1  470 ? 94.435  0.169   7.098   1.00 194.78 ?  470 ARG A NH1 1 
ATOM   3486  N  NH2 . ARG A  1  470 ? 94.466  -0.975  9.079   1.00 193.47 ?  470 ARG A NH2 1 
ATOM   3487  N  N   . LEU A  1  471 ? 94.682  -4.245  0.751   1.00 217.79 ?  471 LEU A N   1 
ATOM   3488  C  CA  . LEU A  1  471 ? 95.158  -4.418  -0.647  1.00 220.25 ?  471 LEU A CA  1 
ATOM   3489  C  C   . LEU A  1  471 ? 93.975  -4.271  -1.609  1.00 218.43 ?  471 LEU A C   1 
ATOM   3490  O  O   . LEU A  1  471 ? 94.158  -4.550  -2.809  1.00 220.61 ?  471 LEU A O   1 
ATOM   3491  C  CB  . LEU A  1  471 ? 95.804  -5.800  -0.777  1.00 211.63 ?  471 LEU A CB  1 
ATOM   3492  C  CG  . LEU A  1  471 ? 97.073  -6.010  0.047   1.00 197.95 ?  471 LEU A CG  1 
ATOM   3493  C  CD1 . LEU A  1  471 ? 97.545  -7.454  -0.041  1.00 186.64 ?  471 LEU A CD1 1 
ATOM   3494  C  CD2 . LEU A  1  471 ? 98.174  -5.061  -0.402  1.00 203.44 ?  471 LEU A CD2 1 
ATOM   3495  N  N   . GLU A  1  472 ? 92.815  -3.847  -1.102  1.00 217.54 ?  472 GLU A N   1 
ATOM   3496  C  CA  . GLU A  1  472 ? 91.605  -3.739  -1.961  1.00 215.55 ?  472 GLU A CA  1 
ATOM   3497  C  C   . GLU A  1  472 ? 91.884  -2.754  -3.100  1.00 213.99 ?  472 GLU A C   1 
ATOM   3498  O  O   . GLU A  1  472 ? 91.486  -3.052  -4.243  1.00 220.73 ?  472 GLU A O   1 
ATOM   3499  C  CB  . GLU A  1  472 ? 90.393  -3.290  -1.144  1.00 212.47 ?  472 GLU A CB  1 
ATOM   3500  C  CG  . GLU A  1  472 ? 89.111  -3.221  -1.952  1.00 216.47 ?  472 GLU A CG  1 
ATOM   3501  C  CD  . GLU A  1  472 ? 88.958  -1.960  -2.785  1.00 226.18 ?  472 GLU A CD  1 
ATOM   3502  O  OE1 . GLU A  1  472 ? 89.435  -0.898  -2.338  1.00 233.50 ?  472 GLU A OE1 1 
ATOM   3503  O  OE2 . GLU A  1  472 ? 88.368  -2.044  -3.880  1.00 229.05 -1 472 GLU A OE2 1 
ATOM   3504  N  N   . SER A  1  473 ? 92.537  -1.629  -2.797  1.00 189.53 ?  473 SER A N   1 
ATOM   3505  C  CA  . SER A  1  473 ? 92.793  -0.596  -3.834  1.00 190.36 ?  473 SER A CA  1 
ATOM   3506  C  C   . SER A  1  473 ? 94.299  -0.404  -4.033  1.00 183.87 ?  473 SER A C   1 
ATOM   3507  O  O   . SER A  1  473 ? 94.682  0.267   -5.010  1.00 170.91 ?  473 SER A O   1 
ATOM   3508  C  CB  . SER A  1  473 ? 92.124  0.702   -3.471  1.00 183.00 ?  473 SER A CB  1 
ATOM   3509  O  OG  . SER A  1  473 ? 92.541  1.138   -2.186  1.00 172.94 ?  473 SER A OG  1 
ATOM   3510  N  N   . LEU A  1  474 ? 95.117  -0.971  -3.142  1.00 180.68 ?  474 LEU A N   1 
ATOM   3511  C  CA  . LEU A  1  474 ? 96.589  -0.783  -3.228  1.00 185.35 ?  474 LEU A CA  1 
ATOM   3512  C  C   . LEU A  1  474 ? 97.105  -1.397  -4.532  1.00 183.89 ?  474 LEU A C   1 
ATOM   3513  O  O   . LEU A  1  474 ? 96.520  -2.401  -4.982  1.00 175.22 ?  474 LEU A O   1 
ATOM   3514  C  CB  . LEU A  1  474 ? 97.245  -1.451  -2.018  1.00 175.16 ?  474 LEU A CB  1 
ATOM   3515  C  CG  . LEU A  1  474 ? 98.639  -0.944  -1.652  1.00 168.94 ?  474 LEU A CG  1 
ATOM   3516  C  CD1 . LEU A  1  474 ? 98.881  -1.071  -0.156  1.00 139.20 ?  474 LEU A CD1 1 
ATOM   3517  C  CD2 . LEU A  1  474 ? 99.712  -1.695  -2.426  1.00 152.92 ?  474 LEU A CD2 1 
ATOM   3518  N  N   . VAL A  1  475 ? 98.168  -0.821  -5.101  1.00 199.13 ?  475 VAL A N   1 
ATOM   3519  C  CA  . VAL A  1  475 ? 98.768  -1.362  -6.357  1.00 181.44 ?  475 VAL A CA  1 
ATOM   3520  C  C   . VAL A  1  475 ? 100.280 -1.497  -6.148  1.00 189.03 ?  475 VAL A C   1 
ATOM   3521  O  O   . VAL A  1  475 ? 100.844 -0.696  -5.378  1.00 202.32 ?  475 VAL A O   1 
ATOM   3522  C  CB  . VAL A  1  475 ? 98.412  -0.491  -7.576  1.00 173.91 ?  475 VAL A CB  1 
ATOM   3523  C  CG1 . VAL A  1  475 ? 97.012  -0.791  -8.089  1.00 155.66 ?  475 VAL A CG1 1 
ATOM   3524  C  CG2 . VAL A  1  475 ? 98.565  0.991   -7.270  1.00 193.98 ?  475 VAL A CG2 1 
ATOM   3525  N  N   . ASP A  1  476 ? 100.902 -2.473  -6.809  1.00 180.83 ?  476 ASP A N   1 
ATOM   3526  C  CA  . ASP A  1  476 ? 102.367 -2.709  -6.685  1.00 176.31 ?  476 ASP A CA  1 
ATOM   3527  C  C   . ASP A  1  476 ? 103.109 -1.497  -7.232  1.00 194.52 ?  476 ASP A C   1 
ATOM   3528  O  O   . ASP A  1  476 ? 104.349 -1.447  -7.105  1.00 194.16 ?  476 ASP A O   1 
ATOM   3529  C  CB  . ASP A  1  476 ? 102.794 -3.980  -7.424  1.00 160.52 ?  476 ASP A CB  1 
ATOM   3530  C  CG  . ASP A  1  476 ? 102.060 -5.229  -6.968  1.00 178.39 ?  476 ASP A CG  1 
ATOM   3531  O  OD1 . ASP A  1  476 ? 101.158 -5.099  -6.119  1.00 200.16 ?  476 ASP A OD1 1 
ATOM   3532  O  OD2 . ASP A  1  476 ? 102.395 -6.321  -7.467  1.00 166.30 ?  476 ASP A OD2 1 
ATOM   3533  N  N   . GLU A  1  477 ? 102.350 -0.571  -7.818  1.00 206.11 ?  477 GLU A N   1 
ATOM   3534  C  CA  . GLU A  1  477 ? 102.959 0.635   -8.429  1.00 199.87 ?  477 GLU A CA  1 
ATOM   3535  C  C   . GLU A  1  477 ? 103.759 1.405   -7.378  1.00 186.58 ?  477 GLU A C   1 
ATOM   3536  O  O   . GLU A  1  477 ? 104.534 2.291   -7.785  1.00 195.63 ?  477 GLU A O   1 
ATOM   3537  C  CB  . GLU A  1  477 ? 101.869 1.523   -9.032  1.00 205.46 ?  477 GLU A CB  1 
ATOM   3538  C  CG  . GLU A  1  477 ? 100.924 0.770   -9.948  1.00 203.49 ?  477 GLU A CG  1 
ATOM   3539  C  CD  . GLU A  1  477 ? 101.611 -0.234  -10.857 1.00 187.07 ?  477 GLU A CD  1 
ATOM   3540  O  OE1 . GLU A  1  477 ? 102.458 0.191   -11.669 1.00 212.53 ?  477 GLU A OE1 1 
ATOM   3541  O  OE2 . GLU A  1  477 ? 101.303 -1.437  -10.747 1.00 164.34 ?  477 GLU A OE2 1 
ATOM   3542  N  N   . LYS A  1  478 ? 103.630 1.089   -6.077  1.00 168.16 ?  478 LYS A N   1 
ATOM   3543  C  CA  . LYS A  1  478 ? 104.284 1.941   -5.034  1.00 166.88 ?  478 LYS A CA  1 
ATOM   3544  C  C   . LYS A  1  478 ? 105.061 1.174   -3.948  1.00 166.02 ?  478 LYS A C   1 
ATOM   3545  O  O   . LYS A  1  478 ? 105.304 1.770   -2.850  1.00 173.68 ?  478 LYS A O   1 
ATOM   3546  C  CB  . LYS A  1  478 ? 103.227 2.838   -4.382  1.00 171.93 ?  478 LYS A CB  1 
ATOM   3547  C  CG  . LYS A  1  478 ? 102.625 3.898   -5.296  1.00 189.79 ?  478 LYS A CG  1 
ATOM   3548  C  CD  . LYS A  1  478 ? 101.566 4.749   -4.625  1.00 195.88 ?  478 LYS A CD  1 
ATOM   3549  C  CE  . LYS A  1  478 ? 100.994 5.813   -5.538  1.00 205.97 ?  478 LYS A CE  1 
ATOM   3550  N  NZ  . LYS A  1  478 ? 99.946  6.613   -4.861  1.00 201.80 ?  478 LYS A NZ  1 
ATOM   3551  N  N   . VAL A  1  479 ? 105.481 -0.063  -4.224  1.00 165.81 ?  479 VAL A N   1 
ATOM   3552  C  CA  . VAL A  1  479 ? 106.321 -0.812  -3.239  1.00 162.43 ?  479 VAL A CA  1 
ATOM   3553  C  C   . VAL A  1  479 ? 107.804 -0.692  -3.612  1.00 175.90 ?  479 VAL A C   1 
ATOM   3554  O  O   . VAL A  1  479 ? 108.091 -0.540  -4.815  1.00 169.91 ?  479 VAL A O   1 
ATOM   3555  C  CB  . VAL A  1  479 ? 105.876 -2.285  -3.157  1.00 156.71 ?  479 VAL A CB  1 
ATOM   3556  C  CG1 . VAL A  1  479 ? 104.588 -2.440  -2.364  1.00 145.86 ?  479 VAL A CG1 1 
ATOM   3557  C  CG2 . VAL A  1  479 ? 105.736 -2.911  -4.535  1.00 178.06 ?  479 VAL A CG2 1 
ATOM   3558  N  N   . ASP A  1  480 ? 108.707 -0.749  -2.626  1.00 189.09 ?  480 ASP A N   1 
ATOM   3559  C  CA  . ASP A  1  480 ? 110.140 -0.709  -2.946  1.00 185.88 ?  480 ASP A CA  1 
ATOM   3560  C  C   . ASP A  1  480 ? 110.831 -2.055  -2.668  1.00 182.18 ?  480 ASP A C   1 
ATOM   3561  O  O   . ASP A  1  480 ? 111.989 -2.226  -3.045  1.00 187.28 ?  480 ASP A O   1 
ATOM   3562  C  CB  . ASP A  1  480 ? 110.859 0.401   -2.149  1.00 195.61 ?  480 ASP A CB  1 
ATOM   3563  C  CG  . ASP A  1  480 ? 110.536 1.818   -2.579  1.00 205.26 ?  480 ASP A CG  1 
ATOM   3564  O  OD1 . ASP A  1  480 ? 109.972 1.989   -3.682  1.00 206.36 ?  480 ASP A OD1 1 
ATOM   3565  O  OD2 . ASP A  1  480 ? 110.851 2.756   -1.815  1.00 215.09 ?  480 ASP A OD2 1 
ATOM   3566  N  N   . THR A  1  481 ? 110.139 -3.001  -2.008  1.00 186.19 ?  481 THR A N   1 
ATOM   3567  C  CA  . THR A  1  481 ? 110.707 -4.303  -1.676  1.00 182.03 ?  481 THR A CA  1 
ATOM   3568  C  C   . THR A  1  481 ? 109.614 -5.371  -1.599  1.00 165.11 ?  481 THR A C   1 
ATOM   3569  O  O   . THR A  1  481 ? 108.520 -5.108  -1.099  1.00 164.19 ?  481 THR A O   1 
ATOM   3570  C  CB  . THR A  1  481 ? 111.506 -4.214  -0.353  1.00 184.62 ?  481 THR A CB  1 
ATOM   3571  O  OG1 . THR A  1  481 ? 111.870 -5.525  0.077   1.00 184.84 ?  481 THR A OG1 1 
ATOM   3572  C  CG2 . THR A  1  481 ? 110.735 -3.510  0.763   1.00 176.98 ?  481 THR A CG2 1 
ATOM   3573  N  N   . PHE A  1  482 ? 109.919 -6.575  -2.097  1.00 147.68 ?  482 PHE A N   1 
ATOM   3574  C  CA  . PHE A  1  482 ? 108.999 -7.710  -2.065  1.00 147.83 ?  482 PHE A CA  1 
ATOM   3575  C  C   . PHE A  1  482 ? 109.414 -8.654  -0.926  1.00 156.08 ?  482 PHE A C   1 
ATOM   3576  O  O   . PHE A  1  482 ? 110.479 -8.465  -0.339  1.00 159.04 ?  482 PHE A O   1 
ATOM   3577  C  CB  . PHE A  1  482 ? 108.994 -8.449  -3.419  1.00 152.79 ?  482 PHE A CB  1 
ATOM   3578  C  CG  . PHE A  1  482 ? 108.356 -7.695  -4.566  1.00 149.36 ?  482 PHE A CG  1 
ATOM   3579  C  CD1 . PHE A  1  482 ? 107.108 -7.110  -4.426  1.00 149.18 ?  482 PHE A CD1 1 
ATOM   3580  C  CD2 . PHE A  1  482 ? 108.979 -7.622  -5.800  1.00 135.16 ?  482 PHE A CD2 1 
ATOM   3581  C  CE1 . PHE A  1  482 ? 106.517 -6.435  -5.485  1.00 151.23 ?  482 PHE A CE1 1 
ATOM   3582  C  CE2 . PHE A  1  482 ? 108.381 -6.949  -6.858  1.00 125.07 ?  482 PHE A CE2 1 
ATOM   3583  C  CZ  . PHE A  1  482 ? 107.154 -6.362  -6.694  1.00 133.01 ?  482 PHE A CZ  1 
ATOM   3584  N  N   . TYR A  1  483 ? 108.578 -9.651  -0.593  1.00 157.08 ?  483 TYR A N   1 
ATOM   3585  C  CA  . TYR A  1  483 ? 108.902 -10.586 0.487   1.00 159.54 ?  483 TYR A CA  1 
ATOM   3586  C  C   . TYR A  1  483 ? 108.939 -12.025 -0.017  1.00 142.87 ?  483 TYR A C   1 
ATOM   3587  O  O   . TYR A  1  483 ? 108.027 -12.456 -0.720  1.00 136.72 ?  483 TYR A O   1 
ATOM   3588  C  CB  . TYR A  1  483 ? 107.905 -10.436 1.644   1.00 149.19 ?  483 TYR A CB  1 
ATOM   3589  C  CG  . TYR A  1  483 ? 107.799 -9.013  2.145   1.00 154.88 ?  483 TYR A CG  1 
ATOM   3590  C  CD1 . TYR A  1  483 ? 108.897 -8.362  2.689   1.00 153.10 ?  483 TYR A CD1 1 
ATOM   3591  C  CD2 . TYR A  1  483 ? 106.609 -8.308  2.048   1.00 156.81 ?  483 TYR A CD2 1 
ATOM   3592  C  CE1 . TYR A  1  483 ? 108.811 -7.049  3.134   1.00 148.76 ?  483 TYR A CE1 1 
ATOM   3593  C  CE2 . TYR A  1  483 ? 106.508 -6.997  2.493   1.00 164.41 ?  483 TYR A CE2 1 
ATOM   3594  C  CZ  . TYR A  1  483 ? 107.613 -6.368  3.033   1.00 159.97 ?  483 TYR A CZ  1 
ATOM   3595  O  OH  . TYR A  1  483 ? 107.521 -5.070  3.476   1.00 156.71 ?  483 TYR A OH  1 
ATOM   3596  N  N   . SER A  1  484 ? 110.002 -12.761 0.342   1.00 133.46 ?  484 SER A N   1 
ATOM   3597  C  CA  . SER A  1  484 ? 110.194 -14.151 -0.068  1.00 140.21 ?  484 SER A CA  1 
ATOM   3598  C  C   . SER A  1  484 ? 109.952 -15.114 1.090   1.00 144.81 ?  484 SER A C   1 
ATOM   3599  O  O   . SER A  1  484 ? 110.609 -14.998 2.122   1.00 133.19 ?  484 SER A O   1 
ATOM   3600  C  CB  . SER A  1  484 ? 111.616 -14.350 -0.580  1.00 142.42 ?  484 SER A CB  1 
ATOM   3601  O  OG  . SER A  1  484 ? 112.571 -13.877 0.357   1.00 126.05 ?  484 SER A OG  1 
ATOM   3602  N  N   . CYS A  1  485 ? 109.038 -16.080 0.912   1.00 139.52 ?  485 CYS A N   1 
ATOM   3603  C  CA  . CYS A  1  485 ? 108.737 -17.071 1.943   1.00 130.03 ?  485 CYS A CA  1 
ATOM   3604  C  C   . CYS A  1  485 ? 109.270 -18.440 1.526   1.00 144.27 ?  485 CYS A C   1 
ATOM   3605  O  O   . CYS A  1  485 ? 109.185 -18.805 0.354   1.00 148.62 ?  485 CYS A O   1 
ATOM   3606  C  CB  . CYS A  1  485 ? 107.239 -17.125 2.222   1.00 110.39 ?  485 CYS A CB  1 
ATOM   3607  S  SG  . CYS A  1  485 ? 106.755 -18.419 3.395   1.00 132.02 ?  485 CYS A SG  1 
ATOM   3608  N  N   . ASN A  1  486 ? 109.810 -19.197 2.490   1.00 151.32 ?  486 ASN A N   1 
ATOM   3609  C  CA  . ASN A  1  486 ? 110.353 -20.534 2.243   1.00 140.27 ?  486 ASN A CA  1 
ATOM   3610  C  C   . ASN A  1  486 ? 109.795 -21.550 3.251   1.00 142.46 ?  486 ASN A C   1 
ATOM   3611  O  O   . ASN A  1  486 ? 110.455 -22.542 3.550   1.00 146.89 ?  486 ASN A O   1 
ATOM   3612  C  CB  . ASN A  1  486 ? 111.882 -20.498 2.310   1.00 130.41 ?  486 ASN A CB  1 
ATOM   3613  C  CG  . ASN A  1  486 ? 112.422 -20.116 3.667   1.00 132.27 ?  486 ASN A CG  1 
ATOM   3614  O  OD1 . ASN A  1  486 ? 112.441 -18.940 4.041   1.00 144.10 ?  486 ASN A OD1 1 
ATOM   3615  N  ND2 . ASN A  1  486 ? 112.870 -21.097 4.440   1.00 129.42 ?  486 ASN A ND2 1 
ATOM   3616  N  N   . LEU A  1  487 ? 108.578 -21.312 3.766   1.00 143.18 ?  487 LEU A N   1 
ATOM   3617  C  CA  . LEU A  1  487 ? 107.952 -22.212 4.733   1.00 129.76 ?  487 LEU A CA  1 
ATOM   3618  C  C   . LEU A  1  487 ? 107.505 -23.502 4.043   1.00 128.36 ?  487 LEU A C   1 
ATOM   3619  O  O   . LEU A  1  487 ? 107.598 -24.578 4.632   1.00 122.98 ?  487 LEU A O   1 
ATOM   3620  C  CB  . LEU A  1  487 ? 106.765 -21.497 5.418   1.00 119.63 ?  487 LEU A CB  1 
ATOM   3621  C  CG  . LEU A  1  487 ? 106.435 -21.868 6.874   1.00 134.02 ?  487 LEU A CG  1 
ATOM   3622  C  CD1 . LEU A  1  487 ? 107.690 -21.896 7.762   1.00 135.12 ?  487 LEU A CD1 1 
ATOM   3623  C  CD2 . LEU A  1  487 ? 105.404 -20.900 7.451   1.00 129.87 ?  487 LEU A CD2 1 
ATOM   3624  N  N   . CYS A  1  488 ? 107.113 -23.406 2.771   1.00 135.97 ?  488 CYS A N   1 
ATOM   3625  C  CA  . CYS A  1  488 ? 106.670 -24.608 2.012   1.00 124.25 ?  488 CYS A CA  1 
ATOM   3626  C  C   . CYS A  1  488 ? 107.876 -25.451 1.585   1.00 128.83 ?  488 CYS A C   1 
ATOM   3627  O  O   . CYS A  1  488 ? 107.661 -26.498 0.944   1.00 130.55 ?  488 CYS A O   1 
ATOM   3628  C  CB  . CYS A  1  488 ? 105.895 -24.197 0.769   1.00 131.37 ?  488 CYS A CB  1 
ATOM   3629  S  SG  . CYS A  1  488 ? 104.205 -23.674 1.144   1.00 122.17 ?  488 CYS A SG  1 
ATOM   3630  N  N   . GLN A  1  489 ? 109.091 -25.013 1.922   1.00 130.53 ?  489 GLN A N   1 
ATOM   3631  C  CA  . GLN A  1  489 ? 110.291 -25.731 1.502   1.00 129.52 ?  489 GLN A CA  1 
ATOM   3632  C  C   . GLN A  1  489 ? 110.447 -27.077 2.243   1.00 127.16 ?  489 GLN A C   1 
ATOM   3633  O  O   . GLN A  1  489 ? 111.345 -27.851 1.911   1.00 133.95 ?  489 GLN A O   1 
ATOM   3634  C  CB  . GLN A  1  489 ? 111.540 -24.854 1.700   1.00 138.99 ?  489 GLN A CB  1 
ATOM   3635  C  CG  . GLN A  1  489 ? 112.678 -25.166 0.731   1.00 141.81 ?  489 GLN A CG  1 
ATOM   3636  C  CD  . GLN A  1  489 ? 113.826 -24.192 0.832   1.00 135.57 ?  489 GLN A CD  1 
ATOM   3637  O  OE1 . GLN A  1  489 ? 113.701 -23.095 1.382   1.00 154.97 ?  489 GLN A OE1 1 
ATOM   3638  N  NE2 . GLN A  1  489 ? 114.979 -24.574 0.298   1.00 121.17 ?  489 GLN A NE2 1 
ATOM   3639  N  N   . SER A  1  490 ? 109.579 -27.357 3.237   1.00 123.00 ?  490 SER A N   1 
ATOM   3640  C  CA  . SER A  1  490 ? 109.611 -28.612 3.981   1.00 125.75 ?  490 SER A CA  1 
ATOM   3641  C  C   . SER A  1  490 ? 109.315 -29.783 3.033   1.00 132.89 ?  490 SER A C   1 
ATOM   3642  O  O   . SER A  1  490 ? 109.963 -30.825 3.125   1.00 133.02 ?  490 SER A O   1 
ATOM   3643  C  CB  . SER A  1  490 ? 108.594 -28.583 5.121   1.00 121.73 ?  490 SER A CB  1 
ATOM   3644  O  OG  . SER A  1  490 ? 107.352 -28.023 4.722   1.00 113.67 ?  490 SER A OG  1 
ATOM   3645  N  N   . PHE A  1  491 ? 108.352 -29.600 2.110   1.00 128.47 ?  491 PHE A N   1 
ATOM   3646  C  CA  . PHE A  1  491 ? 107.980 -30.626 1.132   1.00 120.66 ?  491 PHE A CA  1 
ATOM   3647  C  C   . PHE A  1  491 ? 108.563 -30.314 -0.254  1.00 131.57 ?  491 PHE A C   1 
ATOM   3648  O  O   . PHE A  1  491 ? 109.056 -31.222 -0.920  1.00 140.72 ?  491 PHE A O   1 
ATOM   3649  C  CB  . PHE A  1  491 ? 106.453 -30.814 1.065   1.00 120.37 ?  491 PHE A CB  1 
ATOM   3650  C  CG  . PHE A  1  491 ? 105.620 -29.563 0.910   1.00 111.28 ?  491 PHE A CG  1 
ATOM   3651  C  CD1 . PHE A  1  491 ? 105.326 -28.769 2.003   1.00 108.10 ?  491 PHE A CD1 1 
ATOM   3652  C  CD2 . PHE A  1  491 ? 105.061 -29.232 -0.311  1.00 104.13 ?  491 PHE A CD2 1 
ATOM   3653  C  CE1 . PHE A  1  491 ? 104.532 -27.640 1.867   1.00 111.35 ?  491 PHE A CE1 1 
ATOM   3654  C  CE2 . PHE A  1  491 ? 104.268 -28.103 -0.444  1.00 116.48 ?  491 PHE A CE2 1 
ATOM   3655  C  CZ  . PHE A  1  491 ? 104.005 -27.316 0.646   1.00 120.28 ?  491 PHE A CZ  1 
ATOM   3656  N  N   . ALA A  1  492 ? 108.512 -29.042 -0.684  1.00 125.64 ?  492 ALA A N   1 
ATOM   3657  C  CA  . ALA A  1  492 ? 109.062 -28.622 -1.974  1.00 121.15 ?  492 ALA A CA  1 
ATOM   3658  C  C   . ALA A  1  492 ? 110.462 -28.017 -1.770  1.00 138.18 ?  492 ALA A C   1 
ATOM   3659  O  O   . ALA A  1  492 ? 110.559 -26.817 -1.525  1.00 141.04 ?  492 ALA A O   1 
ATOM   3660  C  CB  . ALA A  1  492 ? 108.159 -27.578 -2.608  1.00 116.47 ?  492 ALA A CB  1 
ATOM   3661  N  N   . PRO A  1  493 ? 111.555 -28.803 -1.835  1.00 156.55 ?  493 PRO A N   1 
ATOM   3662  C  CA  . PRO A  1  493 ? 112.887 -28.225 -1.569  1.00 149.99 ?  493 PRO A CA  1 
ATOM   3663  C  C   . PRO A  1  493 ? 113.382 -27.028 -2.386  1.00 149.35 ?  493 PRO A C   1 
ATOM   3664  O  O   . PRO A  1  493 ? 114.313 -26.360 -1.937  1.00 144.12 ?  493 PRO A O   1 
ATOM   3665  C  CB  . PRO A  1  493 ? 113.828 -29.422 -1.727  1.00 143.65 ?  493 PRO A CB  1 
ATOM   3666  C  CG  . PRO A  1  493 ? 113.118 -30.362 -2.614  1.00 151.01 ?  493 PRO A CG  1 
ATOM   3667  C  CD  . PRO A  1  493 ? 111.660 -30.182 -2.352  1.00 150.43 ?  493 PRO A CD  1 
ATOM   3668  N  N   . ALA A  1  494 ? 112.800 -26.750 -3.561  1.00 138.20 ?  494 ALA A N   1 
ATOM   3669  C  CA  . ALA A  1  494 ? 113.239 -25.610 -4.372  1.00 131.22 ?  494 ALA A CA  1 
ATOM   3670  C  C   . ALA A  1  494 ? 112.159 -24.524 -4.498  1.00 131.75 ?  494 ALA A C   1 
ATOM   3671  O  O   . ALA A  1  494 ? 112.283 -23.651 -5.357  1.00 127.54 ?  494 ALA A O   1 
ATOM   3672  C  CB  . ALA A  1  494 ? 113.658 -26.088 -5.753  1.00 124.78 ?  494 ALA A CB  1 
ATOM   3673  N  N   . HIS A  1  495 ? 111.118 -24.556 -3.649  1.00 132.88 ?  495 HIS A N   1 
ATOM   3674  C  CA  . HIS A  1  495 ? 110.054 -23.563 -3.717  1.00 124.52 ?  495 HIS A CA  1 
ATOM   3675  C  C   . HIS A  1  495 ? 110.400 -22.309 -2.935  1.00 136.59 ?  495 HIS A C   1 
ATOM   3676  O  O   . HIS A  1  495 ? 110.658 -22.379 -1.734  1.00 145.19 ?  495 HIS A O   1 
ATOM   3677  C  CB  . HIS A  1  495 ? 108.733 -24.138 -3.198  1.00 118.58 ?  495 HIS A CB  1 
ATOM   3678  C  CG  . HIS A  1  495 ? 107.605 -23.156 -3.239  1.00 108.95 ?  495 HIS A CG  1 
ATOM   3679  N  ND1 . HIS A  1  495 ? 106.888 -22.930 -4.397  1.00 114.15 ?  495 HIS A ND1 1 
ATOM   3680  C  CD2 . HIS A  1  495 ? 107.113 -22.360 -2.262  1.00 125.48 ?  495 HIS A CD2 1 
ATOM   3681  C  CE1 . HIS A  1  495 ? 105.982 -22.016 -4.093  1.00 117.09 ?  495 HIS A CE1 1 
ATOM   3682  N  NE2 . HIS A  1  495 ? 106.081 -21.642 -2.818  1.00 121.25 ?  495 HIS A NE2 1 
ATOM   3683  N  N   . VAL A  1  496 ? 110.386 -21.158 -3.620  1.00 145.93 ?  496 VAL A N   1 
ATOM   3684  C  CA  . VAL A  1  496 ? 110.653 -19.856 -3.015  1.00 146.82 ?  496 VAL A CA  1 
ATOM   3685  C  C   . VAL A  1  496 ? 109.479 -18.979 -3.433  1.00 145.18 ?  496 VAL A C   1 
ATOM   3686  O  O   . VAL A  1  496 ? 109.475 -18.470 -4.550  1.00 157.57 ?  496 VAL A O   1 
ATOM   3687  C  CB  . VAL A  1  496 ? 112.005 -19.235 -3.478  1.00 156.50 ?  496 VAL A CB  1 
ATOM   3688  C  CG1 . VAL A  1  496 ? 112.430 -18.105 -2.543  1.00 147.44 ?  496 VAL A CG1 1 
ATOM   3689  C  CG2 . VAL A  1  496 ? 113.101 -20.292 -3.593  1.00 153.01 ?  496 VAL A CG2 1 
ATOM   3690  N  N   . CYS A  1  497 ? 108.519 -18.786 -2.529  1.00 124.53 ?  497 CYS A N   1 
ATOM   3691  C  CA  . CYS A  1  497 ? 107.296 -18.034 -2.913  1.00 120.34 ?  497 CYS A CA  1 
ATOM   3692  C  C   . CYS A  1  497 ? 107.505 -16.522 -2.794  1.00 131.35 ?  497 CYS A C   1 
ATOM   3693  O  O   . CYS A  1  497 ? 107.568 -16.026 -1.652  1.00 132.19 ?  497 CYS A O   1 
ATOM   3694  C  CB  . CYS A  1  497 ? 106.105 -18.449 -2.052  1.00 121.52 ?  497 CYS A CB  1 
ATOM   3695  S  SG  . CYS A  1  497 ? 104.489 -18.008 -2.747  1.00 131.97 ?  497 CYS A SG  1 
ATOM   3696  N  N   . ILE A  1  498 ? 107.604 -15.824 -3.929  1.00 144.68 ?  498 ILE A N   1 
ATOM   3697  C  CA  . ILE A  1  498 ? 107.687 -14.334 -3.890  1.00 135.42 ?  498 ILE A CA  1 
ATOM   3698  C  C   . ILE A  1  498 ? 106.269 -13.821 -3.627  1.00 131.80 ?  498 ILE A C   1 
ATOM   3699  O  O   . ILE A  1  498 ? 105.314 -14.499 -4.051  1.00 120.92 ?  498 ILE A O   1 
ATOM   3700  C  CB  . ILE A  1  498 ? 108.275 -13.775 -5.200  1.00 113.81 ?  498 ILE A CB  1 
ATOM   3701  C  CG1 . ILE A  1  498 ? 109.658 -14.363 -5.493  1.00 119.70 ?  498 ILE A CG1 1 
ATOM   3702  C  CG2 . ILE A  1  498 ? 108.303 -12.255 -5.176  1.00 109.98 ?  498 ILE A CG2 1 
ATOM   3703  C  CD1 . ILE A  1  498 ? 110.653 -14.173 -4.372  1.00 122.68 ?  498 ILE A CD1 1 
ATOM   3704  N  N   . VAL A  1  499 ? 106.131 -12.687 -2.942  1.00 126.51 ?  499 VAL A N   1 
ATOM   3705  C  CA  . VAL A  1  499 ? 104.769 -12.202 -2.571  1.00 131.91 ?  499 VAL A CA  1 
ATOM   3706  C  C   . VAL A  1  499 ? 104.663 -10.714 -2.912  1.00 132.06 ?  499 VAL A C   1 
ATOM   3707  O  O   . VAL A  1  499 ? 105.590 -9.960  -2.558  1.00 129.16 ?  499 VAL A O   1 
ATOM   3708  C  CB  . VAL A  1  499 ? 104.496 -12.450 -1.078  1.00 142.67 ?  499 VAL A CB  1 
ATOM   3709  C  CG1 . VAL A  1  499 ? 103.101 -12.027 -0.670  1.00 137.33 ?  499 VAL A CG1 1 
ATOM   3710  C  CG2 . VAL A  1  499 ? 104.756 -13.897 -0.686  1.00 131.12 ?  499 VAL A CG2 1 
ATOM   3711  N  N   . THR A  1  500 ? 103.573 -10.319 -3.577  1.00 152.51 ?  500 THR A N   1 
ATOM   3712  C  CA  . THR A  1  500 ? 103.424 -8.896  -3.973  1.00 151.46 ?  500 THR A CA  1 
ATOM   3713  C  C   . THR A  1  500 ? 101.999 -8.447  -3.639  1.00 148.35 ?  500 THR A C   1 
ATOM   3714  O  O   . THR A  1  500 ? 101.104 -9.311  -3.601  1.00 158.12 ?  500 THR A O   1 
ATOM   3715  C  CB  . THR A  1  500 ? 103.696 -8.709  -5.465  1.00 135.15 ?  500 THR A CB  1 
ATOM   3716  O  OG1 . THR A  1  500 ? 102.470 -9.066  -6.097  1.00 141.53 ?  500 THR A OG1 1 
ATOM   3717  C  CG2 . THR A  1  500 ? 104.826 -9.568  -5.985  1.00 126.17 ?  500 THR A CG2 1 
ATOM   3718  N  N   . PRO A  1  501 ? 101.748 -7.144  -3.400  1.00 140.06 ?  501 PRO A N   1 
ATOM   3719  C  CA  . PRO A  1  501 ? 100.393 -6.671  -3.122  1.00 150.43 ?  501 PRO A CA  1 
ATOM   3720  C  C   . PRO A  1  501 ? 99.399  -7.191  -4.172  1.00 132.92 ?  501 PRO A C   1 
ATOM   3721  O  O   . PRO A  1  501 ? 98.210  -7.136  -3.919  1.00 131.16 ?  501 PRO A O   1 
ATOM   3722  C  CB  . PRO A  1  501 ? 100.533 -5.146  -3.217  1.00 149.78 ?  501 PRO A CB  1 
ATOM   3723  C  CG  . PRO A  1  501 ? 101.967 -4.888  -2.807  1.00 149.80 ?  501 PRO A CG  1 
ATOM   3724  C  CD  . PRO A  1  501 ? 102.747 -6.073  -3.339  1.00 137.28 ?  501 PRO A CD  1 
ATOM   3725  N  N   . GLU A  1  502 ? 99.904  -7.678  -5.311  1.00 139.24 ?  502 GLU A N   1 
ATOM   3726  C  CA  . GLU A  1  502 ? 99.015  -8.228  -6.372  1.00 142.47 ?  502 GLU A CA  1 
ATOM   3727  C  C   . GLU A  1  502 ? 99.225  -9.742  -6.519  1.00 143.69 ?  502 GLU A C   1 
ATOM   3728  O  O   . GLU A  1  502 ? 98.207  -10.449 -6.650  1.00 119.50 ?  502 GLU A O   1 
ATOM   3729  C  CB  . GLU A  1  502 ? 99.228  -7.492  -7.697  1.00 133.56 ?  502 GLU A CB  1 
ATOM   3730  C  CG  . GLU A  1  502 ? 98.723  -6.060  -7.673  1.00 149.99 ?  502 GLU A CG  1 
ATOM   3731  C  CD  . GLU A  1  502 ? 98.882  -5.302  -8.980  1.00 160.37 ?  502 GLU A CD  1 
ATOM   3732  O  OE1 . GLU A  1  502 ? 98.036  -5.490  -9.875  1.00 157.95 ?  502 GLU A OE1 1 
ATOM   3733  O  OE2 . GLU A  1  502 ? 99.849  -4.524  -9.097  1.00 157.63 ?  502 GLU A OE2 1 
ATOM   3734  N  N   . ARG A  1  503 ? 100.461 -10.243 -6.521  1.00 161.41 ?  503 ARG A N   1 
ATOM   3735  C  CA  . ARG A  1  503 ? 100.664 -11.719 -6.560  1.00 144.06 ?  503 ARG A CA  1 
ATOM   3736  C  C   . ARG A  1  503 ? 100.680 -12.232 -5.118  1.00 145.05 ?  503 ARG A C   1 
ATOM   3737  O  O   . ARG A  1  503 ? 101.606 -11.847 -4.379  1.00 156.49 ?  503 ARG A O   1 
ATOM   3738  C  CB  . ARG A  1  503 ? 101.962 -12.061 -7.296  1.00 136.78 ?  503 ARG A CB  1 
ATOM   3739  C  CG  . ARG A  1  503 ? 102.567 -13.405 -6.916  1.00 147.12 ?  503 ARG A CG  1 
ATOM   3740  C  CD  . ARG A  1  503 ? 103.680 -13.809 -7.865  1.00 134.48 ?  503 ARG A CD  1 
ATOM   3741  N  NE  . ARG A  1  503 ? 103.859 -15.253 -7.930  1.00 146.10 ?  503 ARG A NE  1 
ATOM   3742  C  CZ  . ARG A  1  503 ? 104.645 -15.948 -7.117  1.00 152.23 ?  503 ARG A CZ  1 
ATOM   3743  N  NH1 . ARG A  1  503 ? 105.532 -15.324 -6.364  1.00 151.98 ?  503 ARG A NH1 1 
ATOM   3744  N  NH2 . ARG A  1  503 ? 104.541 -17.265 -7.060  1.00 143.63 ?  503 ARG A NH2 1 
ATOM   3745  N  N   . LEU A  1  504 ? 99.711  -13.069 -4.722  1.00 117.64 ?  504 LEU A N   1 
ATOM   3746  C  CA  . LEU A  1  504 ? 99.685  -13.445 -3.284  1.00 126.77 ?  504 LEU A CA  1 
ATOM   3747  C  C   . LEU A  1  504 ? 100.372 -14.792 -3.060  1.00 128.08 ?  504 LEU A C   1 
ATOM   3748  O  O   . LEU A  1  504 ? 100.584 -15.520 -4.048  1.00 128.94 ?  504 LEU A O   1 
ATOM   3749  C  CB  . LEU A  1  504 ? 98.220  -13.503 -2.850  1.00 122.44 ?  504 LEU A CB  1 
ATOM   3750  C  CG  . LEU A  1  504 ? 97.570  -12.135 -2.676  1.00 139.91 ?  504 LEU A CG  1 
ATOM   3751  C  CD1 . LEU A  1  504 ? 96.061  -12.212 -2.831  1.00 128.20 ?  504 LEU A CD1 1 
ATOM   3752  C  CD2 . LEU A  1  504 ? 97.943  -11.561 -1.325  1.00 159.58 ?  504 LEU A CD2 1 
ATOM   3753  N  N   . GLY A  1  505 ? 100.707 -15.099 -1.804  1.00 121.85 ?  505 GLY A N   1 
ATOM   3754  C  CA  . GLY A  1  505 ? 101.292 -16.415 -1.488  1.00 122.81 ?  505 GLY A CA  1 
ATOM   3755  C  C   . GLY A  1  505 ? 100.397 -17.516 -2.016  1.00 126.38 ?  505 GLY A C   1 
ATOM   3756  O  O   . GLY A  1  505 ? 99.184  -17.472 -1.736  1.00 125.85 ?  505 GLY A O   1 
ATOM   3757  N  N   . LEU A  1  506 ? 100.964 -18.462 -2.762  1.00 127.60 ?  506 LEU A N   1 
ATOM   3758  C  CA  . LEU A  1  506 ? 100.156 -19.521 -3.380  1.00 108.87 ?  506 LEU A CA  1 
ATOM   3759  C  C   . LEU A  1  506 ? 99.200  -20.165 -2.370  1.00 115.37 ?  506 LEU A C   1 
ATOM   3760  O  O   . LEU A  1  506 ? 98.168  -20.707 -2.759  1.00 125.49 ?  506 LEU A O   1 
ATOM   3761  C  CB  . LEU A  1  506 ? 101.043 -20.600 -4.031  1.00 116.81 ?  506 LEU A CB  1 
ATOM   3762  C  CG  . LEU A  1  506 ? 102.182 -20.127 -4.951  1.00 123.76 ?  506 LEU A CG  1 
ATOM   3763  C  CD1 . LEU A  1  506 ? 102.795 -21.297 -5.681  1.00 126.17 ?  506 LEU A CD1 1 
ATOM   3764  C  CD2 . LEU A  1  506 ? 101.709 -19.087 -5.960  1.00 124.73 ?  506 LEU A CD2 1 
ATOM   3765  N  N   . CYS A  1  507 ? 99.495  -20.088 -1.075  1.00 125.33 ?  507 CYS A N   1 
ATOM   3766  C  CA  . CYS A  1  507 ? 98.572  -20.783 -0.139  1.00 126.16 ?  507 CYS A CA  1 
ATOM   3767  C  C   . CYS A  1  507 ? 97.275  -19.977 0.008   1.00 118.32 ?  507 CYS A C   1 
ATOM   3768  O  O   . CYS A  1  507 ? 96.262  -20.581 0.410   1.00 116.86 ?  507 CYS A O   1 
ATOM   3769  C  CB  . CYS A  1  507 ? 99.214  -20.983 1.224   1.00 143.27 ?  507 CYS A CB  1 
ATOM   3770  S  SG  . CYS A  1  507 ? 99.604  -19.411 2.024   1.00 138.92 ?  507 CYS A SG  1 
ATOM   3771  N  N   . GLY A  1  508 ? 97.303  -18.688 -0.345  1.00 118.94 ?  508 GLY A N   1 
ATOM   3772  C  CA  . GLY A  1  508 ? 96.087  -17.853 -0.295  1.00 113.74 ?  508 GLY A CA  1 
ATOM   3773  C  C   . GLY A  1  508 ? 95.994  -17.063 0.997   1.00 118.79 ?  508 GLY A C   1 
ATOM   3774  O  O   . GLY A  1  508 ? 95.152  -16.149 1.067   1.00 122.73 ?  508 GLY A O   1 
ATOM   3775  N  N   . ALA A  1  509 ? 96.834  -17.392 1.982   1.00 100.45 ?  509 ALA A N   1 
ATOM   3776  C  CA  . ALA A  1  509 ? 96.757  -16.720 3.299   1.00 114.07 ?  509 ALA A CA  1 
ATOM   3777  C  C   . ALA A  1  509 ? 97.777  -15.580 3.370   1.00 135.40 ?  509 ALA A C   1 
ATOM   3778  O  O   . ALA A  1  509 ? 97.348  -14.412 3.458   1.00 136.76 ?  509 ALA A O   1 
ATOM   3779  C  CB  . ALA A  1  509 ? 96.988  -17.730 4.396   1.00 114.87 ?  509 ALA A CB  1 
ATOM   3780  N  N   . VAL A  1  510 ? 99.071  -15.907 3.331   1.00 139.20 ?  510 VAL A N   1 
ATOM   3781  C  CA  . VAL A  1  510 ? 100.132 -14.867 3.477   1.00 141.11 ?  510 VAL A CA  1 
ATOM   3782  C  C   . VAL A  1  510 ? 99.946  -13.795 2.400   1.00 132.43 ?  510 VAL A C   1 
ATOM   3783  O  O   . VAL A  1  510 ? 100.021 -14.142 1.206   1.00 130.22 ?  510 VAL A O   1 
ATOM   3784  C  CB  . VAL A  1  510 ? 101.540 -15.488 3.411   1.00 122.95 ?  510 VAL A CB  1 
ATOM   3785  C  CG1 . VAL A  1  510 ? 102.626 -14.425 3.472   1.00 123.43 ?  510 VAL A CG1 1 
ATOM   3786  C  CG2 . VAL A  1  510 ? 101.746 -16.532 4.497   1.00 144.61 ?  510 VAL A CG2 1 
ATOM   3787  N  N   . SER A  1  511 ? 99.718  -12.545 2.814   1.00 161.32 ?  511 SER A N   1 
ATOM   3788  C  CA  . SER A  1  511 ? 99.593  -11.422 1.849   1.00 155.07 ?  511 SER A CA  1 
ATOM   3789  C  C   . SER A  1  511 ? 100.857 -10.563 1.941   1.00 160.86 ?  511 SER A C   1 
ATOM   3790  O  O   . SER A  1  511 ? 101.593 -10.715 2.937   1.00 170.37 ?  511 SER A O   1 
ATOM   3791  C  CB  . SER A  1  511 ? 98.361  -10.607 2.124   1.00 155.08 ?  511 SER A CB  1 
ATOM   3792  O  OG  . SER A  1  511 ? 98.636  -9.587  3.073   1.00 176.61 ?  511 SER A OG  1 
ATOM   3793  N  N   . TRP A  1  512 ? 101.123 -9.708  0.950   1.00 145.19 ?  512 TRP A N   1 
ATOM   3794  C  CA  . TRP A  1  512 ? 102.396 -8.937  0.984   1.00 156.22 ?  512 TRP A CA  1 
ATOM   3795  C  C   . TRP A  1  512 ? 102.543 -8.263  2.354   1.00 156.53 ?  512 TRP A C   1 
ATOM   3796  O  O   . TRP A  1  512 ? 103.690 -7.985  2.752   1.00 157.06 ?  512 TRP A O   1 
ATOM   3797  C  CB  . TRP A  1  512 ? 102.479 -7.927  -0.170  1.00 146.60 ?  512 TRP A CB  1 
ATOM   3798  C  CG  . TRP A  1  512 ? 103.740 -7.115  -0.182  1.00 142.05 ?  512 TRP A CG  1 
ATOM   3799  C  CD1 . TRP A  1  512 ? 104.958 -7.470  -0.687  1.00 149.68 ?  512 TRP A CD1 1 
ATOM   3800  C  CD2 . TRP A  1  512 ? 103.909 -5.788  0.339   1.00 145.91 ?  512 TRP A CD2 1 
ATOM   3801  N  NE1 . TRP A  1  512 ? 105.869 -6.466  -0.523  1.00 156.01 ?  512 TRP A NE1 1 
ATOM   3802  C  CE2 . TRP A  1  512 ? 105.253 -5.421  0.106   1.00 162.45 ?  512 TRP A CE2 1 
ATOM   3803  C  CE3 . TRP A  1  512 ? 103.058 -4.882  0.977   1.00 138.73 ?  512 TRP A CE3 1 
ATOM   3804  C  CZ2 . TRP A  1  512 ? 105.765 -4.189  0.491   1.00 165.55 ?  512 TRP A CZ2 1 
ATOM   3805  C  CZ3 . TRP A  1  512 ? 103.565 -3.661  1.357   1.00 136.01 ?  512 TRP A CZ3 1 
ATOM   3806  C  CH2 . TRP A  1  512 ? 104.896 -3.329  1.113   1.00 142.95 ?  512 TRP A CH2 1 
ATOM   3807  N  N   . LEU A  1  513 ? 101.425 -8.020  3.048   1.00 140.45 ?  513 LEU A N   1 
ATOM   3808  C  CA  . LEU A  1  513 ? 101.486 -7.336  4.368   1.00 135.93 ?  513 LEU A CA  1 
ATOM   3809  C  C   . LEU A  1  513 ? 101.674 -8.310  5.537   1.00 148.43 ?  513 LEU A C   1 
ATOM   3810  O  O   . LEU A  1  513 ? 102.377 -7.943  6.496   1.00 159.73 ?  513 LEU A O   1 
ATOM   3811  C  CB  . LEU A  1  513 ? 100.159 -6.608  4.603   1.00 138.79 ?  513 LEU A CB  1 
ATOM   3812  C  CG  . LEU A  1  513 ? 99.957  -5.348  3.763   1.00 133.67 ?  513 LEU A CG  1 
ATOM   3813  C  CD1 . LEU A  1  513 ? 98.541  -4.814  3.916   1.00 133.30 ?  513 LEU A CD1 1 
ATOM   3814  C  CD2 . LEU A  1  513 ? 100.976 -4.280  4.134   1.00 137.08 ?  513 LEU A CD2 1 
ATOM   3815  N  N   . ASP A  1  514 ? 101.059 -9.493  5.466   1.00 148.53 ?  514 ASP A N   1 
ATOM   3816  C  CA  . ASP A  1  514 ? 101.199 -10.477 6.533   1.00 162.28 ?  514 ASP A CA  1 
ATOM   3817  C  C   . ASP A  1  514 ? 102.674 -10.909 6.516   1.00 164.27 ?  514 ASP A C   1 
ATOM   3818  O  O   . ASP A  1  514 ? 103.248 -11.153 7.576   1.00 163.39 ?  514 ASP A O   1 
ATOM   3819  C  CB  . ASP A  1  514 ? 100.283 -11.686 6.269   1.00 169.17 ?  514 ASP A CB  1 
ATOM   3820  C  CG  . ASP A  1  514 ? 98.839  -11.329 5.959   1.00 169.56 ?  514 ASP A CG  1 
ATOM   3821  O  OD1 . ASP A  1  514 ? 98.453  -10.159 6.181   1.00 167.61 ?  514 ASP A OD1 1 
ATOM   3822  O  OD2 . ASP A  1  514 ? 98.095  -12.220 5.495   1.00 157.39 ?  514 ASP A OD2 1 
ATOM   3823  N  N   . ALA A  1  515 ? 103.287 -10.996 5.316   1.00 152.90 ?  515 ALA A N   1 
ATOM   3824  C  CA  . ALA A  1  515 ? 104.701 -11.354 5.160   1.00 144.16 ?  515 ALA A CA  1 
ATOM   3825  C  C   . ALA A  1  515 ? 105.604 -10.280 5.791   1.00 149.89 ?  515 ALA A C   1 
ATOM   3826  O  O   . ALA A  1  515 ? 106.690 -10.592 6.274   1.00 150.43 ?  515 ALA A O   1 
ATOM   3827  C  CB  . ALA A  1  515 ? 105.036 -11.513 3.686   1.00 144.31 ?  515 ALA A CB  1 
ATOM   3828  N  N   . LYS A  1  516 ? 105.150 -9.016  5.773   1.00 164.14 ?  516 LYS A N   1 
ATOM   3829  C  CA  . LYS A  1  516 ? 105.858 -7.881  6.367   1.00 159.55 ?  516 LYS A CA  1 
ATOM   3830  C  C   . LYS A  1  516 ? 105.817 -8.033  7.894   1.00 154.48 ?  516 LYS A C   1 
ATOM   3831  O  O   . LYS A  1  516 ? 106.832 -7.845  8.562   1.00 154.04 ?  516 LYS A O   1 
ATOM   3832  C  CB  . LYS A  1  516 ? 105.185 -6.566  5.916   1.00 163.76 ?  516 LYS A CB  1 
ATOM   3833  C  CG  . LYS A  1  516 ? 105.497 -5.322  6.752   1.00 176.12 ?  516 LYS A CG  1 
ATOM   3834  C  CD  . LYS A  1  516 ? 104.320 -4.332  6.778   1.00 169.94 ?  516 LYS A CD  1 
ATOM   3835  C  CE  . LYS A  1  516 ? 103.879 -3.828  5.416   1.00 164.28 ?  516 LYS A CE  1 
ATOM   3836  N  NZ  . LYS A  1  516 ? 104.956 -3.093  4.701   1.00 161.48 ?  516 LYS A NZ  1 
ATOM   3837  N  N   . ALA A  1  517 ? 104.637 -8.379  8.435   1.00 141.03 ?  517 ALA A N   1 
ATOM   3838  C  CA  . ALA A  1  517 ? 104.454 -8.589  9.866   1.00 141.79 ?  517 ALA A CA  1 
ATOM   3839  C  C   . ALA A  1  517 ? 105.266 -9.803  10.342  1.00 158.09 ?  517 ALA A C   1 
ATOM   3840  O  O   . ALA A  1  517 ? 105.791 -9.783  11.452  1.00 164.54 ?  517 ALA A O   1 
ATOM   3841  C  CB  . ALA A  1  517 ? 102.978 -8.793  10.176  1.00 138.10 ?  517 ALA A CB  1 
ATOM   3842  N  N   . THR A  1  518 ? 105.381 -10.850 9.502   1.00 145.21 ?  518 THR A N   1 
ATOM   3843  C  CA  . THR A  1  518 ? 106.147 -12.058 9.832   1.00 141.53 ?  518 THR A CA  1 
ATOM   3844  C  C   . THR A  1  518 ? 107.627 -11.711 10.048  1.00 151.96 ?  518 THR A C   1 
ATOM   3845  O  O   . THR A  1  518 ? 108.273 -12.303 10.908  1.00 155.94 ?  518 THR A O   1 
ATOM   3846  C  CB  . THR A  1  518 ? 105.966 -13.122 8.736   1.00 128.56 ?  518 THR A CB  1 
ATOM   3847  O  OG1 . THR A  1  518 ? 104.599 -13.538 8.708   1.00 133.80 ?  518 THR A OG1 1 
ATOM   3848  C  CG2 . THR A  1  518 ? 106.864 -14.342 8.940   1.00 127.90 ?  518 THR A CG2 1 
ATOM   3849  N  N   . LEU A  1  519 ? 108.163 -10.755 9.274   1.00 163.80 ?  519 LEU A N   1 
ATOM   3850  C  CA  . LEU A  1  519 ? 109.554 -10.322 9.418   1.00 165.05 ?  519 LEU A CA  1 
ATOM   3851  C  C   . LEU A  1  519 ? 109.722 -9.492  10.704  1.00 169.41 ?  519 LEU A C   1 
ATOM   3852  O  O   . LEU A  1  519 ? 110.773 -9.557  11.339  1.00 174.10 ?  519 LEU A O   1 
ATOM   3853  C  CB  . LEU A  1  519 ? 109.979 -9.503  8.184   1.00 158.67 ?  519 LEU A CB  1 
ATOM   3854  C  CG  . LEU A  1  519 ? 111.414 -8.964  8.171   1.00 179.21 ?  519 LEU A CG  1 
ATOM   3855  C  CD1 . LEU A  1  519 ? 112.426 -10.089 8.070   1.00 167.13 ?  519 LEU A CD1 1 
ATOM   3856  C  CD2 . LEU A  1  519 ? 111.614 -7.991  7.026   1.00 184.96 ?  519 LEU A CD2 1 
ATOM   3857  N  N   . GLU A  1  520 ? 108.691 -8.720  11.089  1.00 158.04 ?  520 GLU A N   1 
ATOM   3858  C  CA  . GLU A  1  520 ? 108.734 -7.908  12.304  1.00 155.80 ?  520 GLU A CA  1 
ATOM   3859  C  C   . GLU A  1  520 ? 108.769 -8.830  13.524  1.00 157.72 ?  520 GLU A C   1 
ATOM   3860  O  O   . GLU A  1  520 ? 109.572 -8.622  14.431  1.00 159.91 ?  520 GLU A O   1 
ATOM   3861  C  CB  . GLU A  1  520 ? 107.504 -6.982  12.387  1.00 154.02 ?  520 GLU A CB  1 
ATOM   3862  C  CG  . GLU A  1  520 ? 107.423 -5.942  11.284  1.00 168.91 ?  520 GLU A CG  1 
ATOM   3863  C  CD  . GLU A  1  520 ? 108.513 -4.890  11.325  1.00 186.23 ?  520 GLU A CD  1 
ATOM   3864  O  OE1 . GLU A  1  520 ? 108.776 -4.347  12.423  1.00 170.17 ?  520 GLU A OE1 1 
ATOM   3865  O  OE2 . GLU A  1  520 ? 109.103 -4.606  10.259  1.00 172.95 ?  520 GLU A OE2 1 
ATOM   3866  N  N   . LEU A  1  521 ? 107.901 -9.853  13.539  1.00 157.59 ?  521 LEU A N   1 
ATOM   3867  C  CA  . LEU A  1  521 ? 107.825 -10.815 14.635  1.00 161.46 ?  521 LEU A CA  1 
ATOM   3868  C  C   . LEU A  1  521 ? 109.059 -11.725 14.644  1.00 170.48 ?  521 LEU A C   1 
ATOM   3869  O  O   . LEU A  1  521 ? 109.730 -11.834 15.670  1.00 178.17 ?  521 LEU A O   1 
ATOM   3870  C  CB  . LEU A  1  521 ? 106.541 -11.657 14.496  1.00 155.17 ?  521 LEU A CB  1 
ATOM   3871  C  CG  . LEU A  1  521 ? 105.209 -10.908 14.640  1.00 152.11 ?  521 LEU A CG  1 
ATOM   3872  C  CD1 . LEU A  1  521 ? 104.029 -11.815 14.339  1.00 171.17 ?  521 LEU A CD1 1 
ATOM   3873  C  CD2 . LEU A  1  521 ? 105.064 -10.319 16.028  1.00 151.73 ?  521 LEU A CD2 1 
ATOM   3874  N  N   . ASN A  1  522 ? 109.352 -12.380 13.510  1.00 157.88 ?  522 ASN A N   1 
ATOM   3875  C  CA  . ASN A  1  522 ? 110.491 -13.286 13.381  1.00 150.83 ?  522 ASN A CA  1 
ATOM   3876  C  C   . ASN A  1  522 ? 111.497 -12.714 12.385  1.00 154.44 ?  522 ASN A C   1 
ATOM   3877  O  O   . ASN A  1  522 ? 111.420 -13.031 11.200  1.00 162.77 ?  522 ASN A O   1 
ATOM   3878  C  CB  . ASN A  1  522 ? 110.018 -14.662 12.905  1.00 142.16 ?  522 ASN A CB  1 
ATOM   3879  C  CG  . ASN A  1  522 ? 109.203 -15.416 13.927  1.00 160.15 ?  522 ASN A CG  1 
ATOM   3880  O  OD1 . ASN A  1  522 ? 109.354 -15.232 15.139  1.00 169.34 ?  522 ASN A OD1 1 
ATOM   3881  N  ND2 . ASN A  1  522 ? 108.316 -16.289 13.463  1.00 138.26 ?  522 ASN A ND2 1 
ATOM   3882  N  N   . PRO A  1  523 ? 112.456 -11.878 12.825  1.00 159.98 ?  523 PRO A N   1 
ATOM   3883  C  CA  . PRO A  1  523 ? 113.436 -11.328 11.872  1.00 173.60 ?  523 PRO A CA  1 
ATOM   3884  C  C   . PRO A  1  523 ? 114.175 -12.398 11.067  1.00 182.05 ?  523 PRO A C   1 
ATOM   3885  O  O   . PRO A  1  523 ? 114.524 -12.165 9.911   1.00 185.66 ?  523 PRO A O   1 
ATOM   3886  C  CB  . PRO A  1  523 ? 114.388 -10.525 12.763  1.00 185.84 ?  523 PRO A CB  1 
ATOM   3887  C  CG  . PRO A  1  523 ? 113.602 -10.211 13.981  1.00 176.98 ?  523 PRO A CG  1 
ATOM   3888  C  CD  . PRO A  1  523 ? 112.699 -11.383 14.194  1.00 163.87 ?  523 PRO A CD  1 
ATOM   3889  N  N   . THR A  1  524 ? 114.400 -13.576 11.674  1.00 190.69 ?  524 THR A N   1 
ATOM   3890  C  CA  . THR A  1  524 ? 115.079 -14.694 11.010  1.00 188.70 ?  524 THR A CA  1 
ATOM   3891  C  C   . THR A  1  524 ? 114.057 -15.786 10.658  1.00 182.19 ?  524 THR A C   1 
ATOM   3892  O  O   . THR A  1  524 ? 114.335 -16.975 10.810  1.00 188.42 ?  524 THR A O   1 
ATOM   3893  C  CB  . THR A  1  524 ? 116.250 -15.215 11.874  1.00 189.70 ?  524 THR A CB  1 
ATOM   3894  O  OG1 . THR A  1  524 ? 116.976 -16.202 11.136  1.00 187.73 ?  524 THR A OG1 1 
ATOM   3895  C  CG2 . THR A  1  524 ? 115.803 -15.787 13.225  1.00 186.23 ?  524 THR A CG2 1 
ATOM   3896  N  N   . GLY A  1  525 ? 112.892 -15.365 10.174  1.00 169.16 ?  525 GLY A N   1 
ATOM   3897  C  CA  . GLY A  1  525 ? 111.809 -16.265 9.803   1.00 149.46 ?  525 GLY A CA  1 
ATOM   3898  C  C   . GLY A  1  525 ? 111.772 -16.584 8.321   1.00 140.60 ?  525 GLY A C   1 
ATOM   3899  O  O   . GLY A  1  525 ? 112.745 -16.340 7.604   1.00 146.42 ?  525 GLY A O   1 
ATOM   3900  N  N   . PRO A  1  526 ? 110.650 -17.141 7.826   1.00 158.20 ?  526 PRO A N   1 
ATOM   3901  C  CA  . PRO A  1  526 ? 110.577 -17.475 6.396   1.00 163.17 ?  526 PRO A CA  1 
ATOM   3902  C  C   . PRO A  1  526 ? 110.413 -16.250 5.501   1.00 157.98 ?  526 PRO A C   1 
ATOM   3903  O  O   . PRO A  1  526 ? 111.065 -16.158 4.463   1.00 165.60 ?  526 PRO A O   1 
ATOM   3904  C  CB  . PRO A  1  526 ? 109.371 -18.415 6.315   1.00 150.52 ?  526 PRO A CB  1 
ATOM   3905  C  CG  . PRO A  1  526 ? 108.500 -18.013 7.449   1.00 153.26 ?  526 PRO A CG  1 
ATOM   3906  C  CD  . PRO A  1  526 ? 109.405 -17.501 8.537   1.00 157.23 ?  526 PRO A CD  1 
ATOM   3907  N  N   . CYS A  1  527 ? 109.549 -15.309 5.900   1.00 149.48 ?  527 CYS A N   1 
ATOM   3908  C  CA  . CYS A  1  527 ? 109.303 -14.096 5.127   1.00 147.15 ?  527 CYS A CA  1 
ATOM   3909  C  C   . CYS A  1  527 ? 110.460 -13.121 5.295   1.00 165.00 ?  527 CYS A C   1 
ATOM   3910  O  O   . CYS A  1  527 ? 110.589 -12.495 6.346   1.00 164.33 ?  527 CYS A O   1 
ATOM   3911  C  CB  . CYS A  1  527 ? 107.980 -13.465 5.543   1.00 124.01 ?  527 CYS A CB  1 
ATOM   3912  S  SG  . CYS A  1  527 ? 106.545 -14.544 5.310   1.00 144.39 ?  527 CYS A SG  1 
ATOM   3913  N  N   . GLN A  1  528 ? 111.304 -12.999 4.260   1.00 189.99 ?  528 GLN A N   1 
ATOM   3914  C  CA  . GLN A  1  528 ? 112.458 -12.103 4.277   1.00 179.68 ?  528 GLN A CA  1 
ATOM   3915  C  C   . GLN A  1  528 ? 112.355 -11.059 3.165   1.00 174.15 ?  528 GLN A C   1 
ATOM   3916  O  O   . GLN A  1  528 ? 111.717 -11.298 2.141   1.00 170.98 ?  528 GLN A O   1 
ATOM   3917  C  CB  . GLN A  1  528 ? 113.759 -12.910 4.171   1.00 184.40 ?  528 GLN A CB  1 
ATOM   3918  C  CG  . GLN A  1  528 ? 113.988 -13.805 5.386   1.00 185.88 ?  528 GLN A CG  1 
ATOM   3919  C  CD  . GLN A  1  528 ? 115.236 -14.643 5.277   1.00 207.96 ?  528 GLN A CD  1 
ATOM   3920  O  OE1 . GLN A  1  528 ? 115.756 -14.894 4.184   1.00 226.61 ?  528 GLN A OE1 1 
ATOM   3921  N  NE2 . GLN A  1  528 ? 115.744 -15.104 6.415   1.00 182.81 ?  528 GLN A NE2 1 
ATOM   3922  N  N   . ALA A  1  529 ? 112.969 -9.894  3.376   1.00 178.05 ?  529 ALA A N   1 
ATOM   3923  C  CA  . ALA A  1  529 ? 112.924 -8.799  2.413   1.00 157.59 ?  529 ALA A CA  1 
ATOM   3924  C  C   . ALA A  1  529 ? 113.755 -9.070  1.159   1.00 156.82 ?  529 ALA A C   1 
ATOM   3925  O  O   . ALA A  1  529 ? 114.822 -9.674  1.234   1.00 162.74 ?  529 ALA A O   1 
ATOM   3926  C  CB  . ALA A  1  529 ? 113.396 -7.516  3.076   1.00 142.03 ?  529 ALA A CB  1 
ATOM   3927  N  N   . VAL A  1  530 ? 113.250 -8.611  0.006   1.00 155.40 ?  530 VAL A N   1 
ATOM   3928  C  CA  . VAL A  1  530 ? 113.887 -8.743  -1.305  1.00 155.25 ?  530 VAL A CA  1 
ATOM   3929  C  C   . VAL A  1  530 ? 113.748 -7.365  -1.970  1.00 169.28 ?  530 VAL A C   1 
ATOM   3930  O  O   . VAL A  1  530 ? 112.660 -7.055  -2.452  1.00 168.63 ?  530 VAL A O   1 
ATOM   3931  C  CB  . VAL A  1  530 ? 113.188 -9.833  -2.156  1.00 145.89 ?  530 VAL A CB  1 
ATOM   3932  C  CG1 . VAL A  1  530 ? 113.751 -9.873  -3.572  1.00 130.00 ?  530 VAL A CG1 1 
ATOM   3933  C  CG2 . VAL A  1  530 ? 113.298 -11.201 -1.495  1.00 139.48 ?  530 VAL A CG2 1 
ATOM   3934  N  N   . PRO A  1  531 ? 114.784 -6.500  -1.985  1.00 184.86 ?  531 PRO A N   1 
ATOM   3935  C  CA  . PRO A  1  531 ? 114.596 -5.169  -2.593  1.00 185.07 ?  531 PRO A CA  1 
ATOM   3936  C  C   . PRO A  1  531 ? 114.298 -5.201  -4.093  1.00 183.76 ?  531 PRO A C   1 
ATOM   3937  O  O   . PRO A  1  531 ? 114.920 -5.956  -4.836  1.00 181.52 ?  531 PRO A O   1 
ATOM   3938  C  CB  . PRO A  1  531 ? 115.884 -4.417  -2.243  1.00 185.40 ?  531 PRO A CB  1 
ATOM   3939  C  CG  . PRO A  1  531 ? 116.882 -5.454  -1.920  1.00 179.21 ?  531 PRO A CG  1 
ATOM   3940  C  CD  . PRO A  1  531 ? 116.148 -6.672  -1.445  1.00 180.74 ?  531 PRO A CD  1 
ATOM   3941  N  N   . LYS A  1  532 ? 113.323 -4.385  -4.530  1.00 173.15 ?  532 LYS A N   1 
ATOM   3942  C  CA  . LYS A  1  532 ? 112.909 -4.315  -5.930  1.00 159.02 ?  532 LYS A CA  1 
ATOM   3943  C  C   . LYS A  1  532 ? 113.891 -3.481  -6.756  1.00 156.23 ?  532 LYS A C   1 
ATOM   3944  O  O   . LYS A  1  532 ? 113.674 -2.286  -6.953  1.00 144.30 ?  532 LYS A O   1 
ATOM   3945  C  CB  . LYS A  1  532 ? 111.485 -3.725  -6.027  1.00 139.07 ?  532 LYS A CB  1 
ATOM   3946  C  CG  . LYS A  1  532 ? 110.730 -4.131  -7.291  1.00 149.93 ?  532 LYS A CG  1 
ATOM   3947  C  CD  . LYS A  1  532 ? 109.759 -3.065  -7.785  1.00 137.66 ?  532 LYS A CD  1 
ATOM   3948  C  CE  . LYS A  1  532 ? 108.612 -2.823  -6.831  1.00 133.21 ?  532 LYS A CE  1 
ATOM   3949  N  NZ  . LYS A  1  532 ? 107.506 -2.037  -7.447  1.00 133.79 ?  532 LYS A NZ  1 
ATOM   3950  N  N   . GLU A  1  533 ? 114.967 -4.115  -7.245  1.00 173.38 ?  533 GLU A N   1 
ATOM   3951  C  CA  . GLU A  1  533 ? 115.982 -3.430  -8.052  1.00 181.70 ?  533 GLU A CA  1 
ATOM   3952  C  C   . GLU A  1  533 ? 116.275 -4.203  -9.338  1.00 188.91 ?  533 GLU A C   1 
ATOM   3953  O  O   . GLU A  1  533 ? 116.038 -5.409  -9.411  1.00 180.27 ?  533 GLU A O   1 
ATOM   3954  C  CB  . GLU A  1  533 ? 117.296 -3.190  -7.269  1.00 176.99 ?  533 GLU A CB  1 
ATOM   3955  C  CG  . GLU A  1  533 ? 117.213 -2.213  -6.112  1.00 175.57 ?  533 GLU A CG  1 
ATOM   3956  C  CD  . GLU A  1  533 ? 118.505 -2.067  -5.334  1.00 199.69 ?  533 GLU A CD  1 
ATOM   3957  O  OE1 . GLU A  1  533 ? 119.435 -2.870  -5.570  1.00 193.89 ?  533 GLU A OE1 1 
ATOM   3958  O  OE2 . GLU A  1  533 ? 118.589 -1.149  -4.488  1.00 211.85 ?  533 GLU A OE2 1 
ATOM   3959  N  N   . GLY A  1  534 ? 116.788 -3.493  -10.339 1.00 188.70 ?  534 GLY A N   1 
ATOM   3960  C  CA  . GLY A  1  534 ? 117.122 -4.079  -11.627 1.00 180.58 ?  534 GLY A CA  1 
ATOM   3961  C  C   . GLY A  1  534 ? 115.890 -4.452  -12.419 1.00 178.52 ?  534 GLY A C   1 
ATOM   3962  O  O   . GLY A  1  534 ? 115.679 -5.625  -12.731 1.00 182.19 ?  534 GLY A O   1 
ATOM   3963  N  N   . VAL A  1  535 ? 115.067 -3.457  -12.752 1.00 151.26 ?  535 VAL A N   1 
ATOM   3964  C  CA  . VAL A  1  535 ? 113.842 -3.701  -13.507 1.00 143.48 ?  535 VAL A CA  1 
ATOM   3965  C  C   . VAL A  1  535 ? 114.203 -4.070  -14.944 1.00 147.85 ?  535 VAL A C   1 
ATOM   3966  O  O   . VAL A  1  535 ? 114.900 -3.309  -15.613 1.00 151.84 ?  535 VAL A O   1 
ATOM   3967  C  CB  . VAL A  1  535 ? 112.894 -2.479  -13.465 1.00 144.82 ?  535 VAL A CB  1 
ATOM   3968  C  CG1 . VAL A  1  535 ? 111.573 -2.793  -14.160 1.00 136.30 ?  535 VAL A CG1 1 
ATOM   3969  C  CG2 . VAL A  1  535 ? 112.656 -2.021  -12.028 1.00 136.89 ?  535 VAL A CG2 1 
ATOM   3970  N  N   . VAL A  1  536 ? 113.741 -5.238  -15.415 1.00 141.32 ?  536 VAL A N   1 
ATOM   3971  C  CA  . VAL A  1  536 ? 114.013 -5.700  -16.774 1.00 132.78 ?  536 VAL A CA  1 
ATOM   3972  C  C   . VAL A  1  536 ? 112.723 -5.672  -17.598 1.00 137.22 ?  536 VAL A C   1 
ATOM   3973  O  O   . VAL A  1  536 ? 112.736 -5.194  -18.731 1.00 149.66 ?  536 VAL A O   1 
ATOM   3974  C  CB  . VAL A  1  536 ? 114.661 -7.105  -16.766 1.00 123.74 ?  536 VAL A CB  1 
ATOM   3975  C  CG1 . VAL A  1  536 ? 114.925 -7.593  -18.187 1.00 135.02 ?  536 VAL A CG1 1 
ATOM   3976  C  CG2 . VAL A  1  536 ? 115.951 -7.104  -15.953 1.00 133.46 ?  536 VAL A CG2 1 
ATOM   3977  N  N   . ASP A  1  537 ? 111.611 -6.170  -17.036 1.00 141.89 ?  537 ASP A N   1 
ATOM   3978  C  CA  . ASP A  1  537 ? 110.322 -6.184  -17.733 1.00 152.24 ?  537 ASP A CA  1 
ATOM   3979  C  C   . ASP A  1  537 ? 109.186 -5.981  -16.732 1.00 145.24 ?  537 ASP A C   1 
ATOM   3980  O  O   . ASP A  1  537 ? 109.163 -6.637  -15.694 1.00 147.53 ?  537 ASP A O   1 
ATOM   3981  C  CB  . ASP A  1  537 ? 110.135 -7.514  -18.483 1.00 147.13 ?  537 ASP A CB  1 
ATOM   3982  C  CG  . ASP A  1  537 ? 109.188 -7.436  -19.666 1.00 150.24 ?  537 ASP A CG  1 
ATOM   3983  O  OD1 . ASP A  1  537 ? 108.210 -6.660  -19.595 1.00 160.71 ?  537 ASP A OD1 1 
ATOM   3984  O  OD2 . ASP A  1  537 ? 109.423 -8.153  -20.660 1.00 148.48 ?  537 ASP A OD2 1 
ATOM   3985  N  N   . GLU A  1  538 ? 108.247 -5.077  -17.044 1.00 154.23 ?  538 GLU A N   1 
ATOM   3986  C  CA  . GLU A  1  538 ? 107.111 -4.793  -16.166 1.00 155.93 ?  538 GLU A CA  1 
ATOM   3987  C  C   . GLU A  1  538 ? 105.910 -5.693  -16.476 1.00 159.07 ?  538 GLU A C   1 
ATOM   3988  O  O   . GLU A  1  538 ? 105.124 -5.986  -15.577 1.00 168.54 ?  538 GLU A O   1 
ATOM   3989  C  CB  . GLU A  1  538 ? 106.697 -3.316  -16.277 1.00 154.02 ?  538 GLU A CB  1 
ATOM   3990  C  CG  . GLU A  1  538 ? 107.753 -2.342  -15.781 1.00 163.33 ?  538 GLU A CG  1 
ATOM   3991  C  CD  . GLU A  1  538 ? 107.747 -2.099  -14.285 1.00 174.37 ?  538 GLU A CD  1 
ATOM   3992  O  OE1 . GLU A  1  538 ? 108.236 -2.976  -13.536 1.00 177.54 ?  538 GLU A OE1 1 
ATOM   3993  O  OE2 . GLU A  1  538 ? 107.260 -1.027  -13.859 1.00 166.36 ?  538 GLU A OE2 1 
ATOM   3994  N  N   . ASN A  1  539 ? 105.758 -6.125  -17.736 1.00 166.50 ?  539 ASN A N   1 
ATOM   3995  C  CA  . ASN A  1  539 ? 104.645 -6.990  -18.129 1.00 167.82 ?  539 ASN A CA  1 
ATOM   3996  C  C   . ASN A  1  539 ? 104.867 -8.427  -17.655 1.00 160.87 ?  539 ASN A C   1 
ATOM   3997  O  O   . ASN A  1  539 ? 103.926 -9.064  -17.182 1.00 159.30 ?  539 ASN A O   1 
ATOM   3998  C  CB  . ASN A  1  539 ? 104.456 -6.961  -19.645 1.00 173.57 ?  539 ASN A CB  1 
ATOM   3999  C  CG  . ASN A  1  539 ? 104.051 -5.608  -20.175 1.00 181.78 ?  539 ASN A CG  1 
ATOM   4000  O  OD1 . ASN A  1  539 ? 103.468 -4.782  -19.463 1.00 167.46 ?  539 ASN A OD1 1 
ATOM   4001  N  ND2 . ASN A  1  539 ? 104.347 -5.348  -21.441 1.00 194.96 ?  539 ASN A ND2 1 
ATOM   4002  N  N   . LEU A  1  540 ? 106.101 -8.938  -17.776 1.00 156.89 ?  540 LEU A N   1 
ATOM   4003  C  CA  . LEU A  1  540 ? 106.427 -10.300 -17.346 1.00 152.14 ?  540 LEU A CA  1 
ATOM   4004  C  C   . LEU A  1  540 ? 106.857 -10.367 -15.872 1.00 148.48 ?  540 LEU A C   1 
ATOM   4005  O  O   . LEU A  1  540 ? 106.761 -11.427 -15.261 1.00 136.35 ?  540 LEU A O   1 
ATOM   4006  C  CB  . LEU A  1  540 ? 107.545 -10.895 -18.218 1.00 145.60 ?  540 LEU A CB  1 
ATOM   4007  C  CG  . LEU A  1  540 ? 107.356 -10.845 -19.733 1.00 142.62 ?  540 LEU A CG  1 
ATOM   4008  C  CD1 . LEU A  1  540 ? 108.549 -11.467 -20.432 1.00 147.16 ?  540 LEU A CD1 1 
ATOM   4009  C  CD2 . LEU A  1  540 ? 106.080 -11.549 -20.158 1.00 148.94 ?  540 LEU A CD2 1 
ATOM   4010  N  N   . GLY A  1  541 ? 107.338 -9.255  -15.322 1.00 149.49 ?  541 GLY A N   1 
ATOM   4011  C  CA  . GLY A  1  541 ? 107.781 -9.202  -13.937 1.00 131.74 ?  541 GLY A CA  1 
ATOM   4012  C  C   . GLY A  1  541 ? 109.145 -9.827  -13.744 1.00 132.87 ?  541 GLY A C   1 
ATOM   4013  O  O   . GLY A  1  541 ? 109.256 -10.914 -13.176 1.00 135.76 ?  541 GLY A O   1 
ATOM   4014  N  N   . ILE A  1  542 ? 110.196 -9.150  -14.223 1.00 125.12 ?  542 ILE A N   1 
ATOM   4015  C  CA  . ILE A  1  542 ? 111.562 -9.657  -14.104 1.00 131.45 ?  542 ILE A CA  1 
ATOM   4016  C  C   . ILE A  1  542 ? 112.461 -8.629  -13.421 1.00 127.01 ?  542 ILE A C   1 
ATOM   4017  O  O   . ILE A  1  542 ? 112.803 -7.617  -14.030 1.00 141.33 ?  542 ILE A O   1 
ATOM   4018  C  CB  . ILE A  1  542 ? 112.127 -10.043 -15.497 1.00 125.75 ?  542 ILE A CB  1 
ATOM   4019  C  CG1 . ILE A  1  542 ? 111.258 -11.124 -16.174 1.00 120.70 ?  542 ILE A CG1 1 
ATOM   4020  C  CG2 . ILE A  1  542 ? 113.577 -10.528 -15.372 1.00 125.91 ?  542 ILE A CG2 1 
ATOM   4021  C  CD1 . ILE A  1  542 ? 111.397 -11.186 -17.693 1.00 126.96 ?  542 ILE A CD1 1 
ATOM   4022  N  N   . TRP A  1  543 ? 112.847 -8.888  -12.165 1.00 134.89 ?  543 TRP A N   1 
ATOM   4023  C  CA  . TRP A  1  543 ? 113.739 -8.007  -11.411 1.00 146.88 ?  543 TRP A CA  1 
ATOM   4024  C  C   . TRP A  1  543 ? 115.003 -8.808  -11.104 1.00 159.27 ?  543 TRP A C   1 
ATOM   4025  O  O   . TRP A  1  543 ? 114.908 -9.950  -10.660 1.00 155.42 ?  543 TRP A O   1 
ATOM   4026  C  CB  . TRP A  1  543 ? 113.076 -7.511  -10.119 1.00 143.60 ?  543 TRP A CB  1 
ATOM   4027  C  CG  . TRP A  1  543 ? 111.979 -6.517  -10.347 1.00 140.39 ?  543 TRP A CG  1 
ATOM   4028  C  CD1 . TRP A  1  543 ? 112.096 -5.160  -10.394 1.00 142.40 ?  543 TRP A CD1 1 
ATOM   4029  C  CD2 . TRP A  1  543 ? 110.591 -6.809  -10.551 1.00 138.54 ?  543 TRP A CD2 1 
ATOM   4030  N  NE1 . TRP A  1  543 ? 110.865 -4.588  -10.617 1.00 138.96 ?  543 TRP A NE1 1 
ATOM   4031  C  CE2 . TRP A  1  543 ? 109.925 -5.580  -10.720 1.00 142.98 ?  543 TRP A CE2 1 
ATOM   4032  C  CE3 . TRP A  1  543 ? 109.846 -7.991  -10.609 1.00 141.83 ?  543 TRP A CE3 1 
ATOM   4033  C  CZ2 . TRP A  1  543 ? 108.552 -5.502  -10.942 1.00 138.59 ?  543 TRP A CZ2 1 
ATOM   4034  C  CZ3 . TRP A  1  543 ? 108.486 -7.910  -10.826 1.00 142.10 ?  543 TRP A CZ3 1 
ATOM   4035  C  CH2 . TRP A  1  543 ? 107.855 -6.679  -10.997 1.00 137.79 ?  543 TRP A CH2 1 
ATOM   4036  N  N   . GLU A  1  544 ? 116.182 -8.222  -11.359 1.00 165.79 ?  544 GLU A N   1 
ATOM   4037  C  CA  . GLU A  1  544 ? 117.467 -8.898  -11.152 1.00 164.16 ?  544 GLU A CA  1 
ATOM   4038  C  C   . GLU A  1  544 ? 117.681 -9.377  -9.716  1.00 169.65 ?  544 GLU A C   1 
ATOM   4039  O  O   . GLU A  1  544 ? 118.273 -10.439 -9.520  1.00 179.95 ?  544 GLU A O   1 
ATOM   4040  C  CB  . GLU A  1  544 ? 118.634 -7.995  -11.585 1.00 175.50 ?  544 GLU A CB  1 
ATOM   4041  C  CG  . GLU A  1  544 ? 118.642 -7.679  -13.071 1.00 187.31 ?  544 GLU A CG  1 
ATOM   4042  C  CD  . GLU A  1  544 ? 119.743 -6.740  -13.523 1.00 198.80 ?  544 GLU A CD  1 
ATOM   4043  O  OE1 . GLU A  1  544 ? 120.459 -6.191  -12.653 1.00 193.48 ?  544 GLU A OE1 1 
ATOM   4044  O  OE2 . GLU A  1  544 ? 119.890 -6.552  -14.752 1.00 197.50 ?  544 GLU A OE2 1 
ATOM   4045  N  N   . LYS A  1  545 ? 117.207 -8.605  -8.736  1.00 162.22 ?  545 LYS A N   1 
ATOM   4046  C  CA  . LYS A  1  545 ? 117.346 -9.012  -7.313  1.00 167.35 ?  545 LYS A CA  1 
ATOM   4047  C  C   . LYS A  1  545 ? 116.388 -10.171 -7.029  1.00 164.85 ?  545 LYS A C   1 
ATOM   4048  O  O   . LYS A  1  545 ? 116.808 -11.134 -6.358  1.00 158.96 ?  545 LYS A O   1 
ATOM   4049  C  CB  . LYS A  1  545 ? 117.050 -7.827  -6.390  1.00 163.36 ?  545 LYS A CB  1 
ATOM   4050  C  CG  . LYS A  1  545 ? 117.286 -8.083  -4.908  1.00 172.78 ?  545 LYS A CG  1 
ATOM   4051  C  CD  . LYS A  1  545 ? 118.750 -8.064  -4.528  1.00 166.04 ?  545 LYS A CD  1 
ATOM   4052  C  CE  . LYS A  1  545 ? 119.071 -8.965  -3.355  1.00 172.69 ?  545 LYS A CE  1 
ATOM   4053  N  NZ  . LYS A  1  545 ? 120.476 -9.435  -3.393  1.00 168.20 ?  545 LYS A NZ  1 
ATOM   4054  N  N   . VAL A  1  546 ? 115.155 -10.082 -7.532  1.00 156.40 ?  546 VAL A N   1 
ATOM   4055  C  CA  . VAL A  1  546 ? 114.144 -11.112 -7.268  1.00 135.05 ?  546 VAL A CA  1 
ATOM   4056  C  C   . VAL A  1  546 ? 114.667 -12.459 -7.775  1.00 140.43 ?  546 VAL A C   1 
ATOM   4057  O  O   . VAL A  1  546 ? 114.543 -13.467 -7.088  1.00 156.68 ?  546 VAL A O   1 
ATOM   4058  C  CB  . VAL A  1  546 ? 112.779 -10.752 -7.907  1.00 120.22 ?  546 VAL A CB  1 
ATOM   4059  C  CG1 . VAL A  1  546 ? 111.817 -11.936 -7.861  1.00 115.79 ?  546 VAL A CG1 1 
ATOM   4060  C  CG2 . VAL A  1  546 ? 112.158 -9.535  -7.226  1.00 119.47 ?  546 VAL A CG2 1 
ATOM   4061  N  N   . ASN A  1  547 ? 115.252 -12.477 -8.971  1.00 147.04 ?  547 ASN A N   1 
ATOM   4062  C  CA  . ASN A  1  547 ? 115.840 -13.742 -9.480  1.00 158.97 ?  547 ASN A CA  1 
ATOM   4063  C  C   . ASN A  1  547 ? 116.975 -14.180 -8.557  1.00 164.15 ?  547 ASN A C   1 
ATOM   4064  O  O   . ASN A  1  547 ? 117.029 -15.377 -8.213  1.00 168.62 ?  547 ASN A O   1 
ATOM   4065  C  CB  . ASN A  1  547 ? 116.400 -13.586 -10.892 1.00 148.18 ?  547 ASN A CB  1 
ATOM   4066  C  CG  . ASN A  1  547 ? 115.339 -13.289 -11.927 1.00 147.23 ?  547 ASN A CG  1 
ATOM   4067  O  OD1 . ASN A  1  547 ? 114.194 -12.996 -11.591 1.00 144.54 ?  547 ASN A OD1 1 
ATOM   4068  N  ND2 . ASN A  1  547 ? 115.721 -13.362 -13.190 1.00 151.42 ?  547 ASN A ND2 1 
ATOM   4069  N  N   . GLU A  1  548 ? 117.838 -13.243 -8.168  1.00 191.43 ?  548 GLU A N   1 
ATOM   4070  C  CA  . GLU A  1  548 ? 119.012 -13.574 -7.360  1.00 192.22 ?  548 GLU A CA  1 
ATOM   4071  C  C   . GLU A  1  548 ? 118.630 -14.199 -6.009  1.00 191.90 ?  548 GLU A C   1 
ATOM   4072  O  O   . GLU A  1  548 ? 119.188 -15.233 -5.644  1.00 193.59 ?  548 GLU A O   1 
ATOM   4073  C  CB  . GLU A  1  548 ? 119.877 -12.313 -7.153  1.00 199.09 ?  548 GLU A CB  1 
ATOM   4074  C  CG  . GLU A  1  548 ? 121.077 -12.495 -6.236  1.00 214.74 ?  548 GLU A CG  1 
ATOM   4075  C  CD  . GLU A  1  548 ? 122.016 -13.626 -6.605  1.00 225.34 ?  548 GLU A CD  1 
ATOM   4076  O  OE1 . GLU A  1  548 ? 122.430 -13.696 -7.785  1.00 236.72 ?  548 GLU A OE1 1 
ATOM   4077  O  OE2 . GLU A  1  548 ? 122.343 -14.442 -5.712  1.00 217.87 ?  548 GLU A OE2 1 
ATOM   4078  N  N   . THR A  1  549 ? 117.688 -13.592 -5.272  1.00 158.14 ?  549 THR A N   1 
ATOM   4079  C  CA  . THR A  1  549 ? 117.278 -14.121 -3.967  1.00 154.68 ?  549 THR A CA  1 
ATOM   4080  C  C   . THR A  1  549 ? 116.654 -15.515 -4.089  1.00 137.17 ?  549 THR A C   1 
ATOM   4081  O  O   . THR A  1  549 ? 116.807 -16.331 -3.181  1.00 127.62 ?  549 THR A O   1 
ATOM   4082  C  CB  . THR A  1  549 ? 116.335 -13.140 -3.266  1.00 152.30 ?  549 THR A CB  1 
ATOM   4083  O  OG1 . THR A  1  549 ? 115.264 -12.819 -4.153  1.00 156.30 ?  549 THR A OG1 1 
ATOM   4084  C  CG2 . THR A  1  549 ? 117.048 -11.866 -2.820  1.00 148.18 ?  549 THR A CG2 1 
ATOM   4085  N  N   . VAL A  1  550 ? 115.962 -15.793 -5.206  1.00 143.27 ?  550 VAL A N   1 
ATOM   4086  C  CA  . VAL A  1  550 ? 115.352 -17.104 -5.437  1.00 139.84 ?  550 VAL A CA  1 
ATOM   4087  C  C   . VAL A  1  550 ? 116.462 -18.147 -5.638  1.00 145.07 ?  550 VAL A C   1 
ATOM   4088  O  O   . VAL A  1  550 ? 116.340 -19.268 -5.150  1.00 153.81 ?  550 VAL A O   1 
ATOM   4089  C  CB  . VAL A  1  550 ? 114.362 -17.070 -6.635  1.00 116.77 ?  550 VAL A CB  1 
ATOM   4090  C  CG1 . VAL A  1  550 ? 113.986 -18.476 -7.090  1.00 109.69 ?  550 VAL A CG1 1 
ATOM   4091  C  CG2 . VAL A  1  550 ? 113.108 -16.270 -6.289  1.00 108.98 ?  550 VAL A CG2 1 
ATOM   4092  N  N   . SER A  1  551 ? 117.547 -17.776 -6.337  1.00 146.27 ?  551 SER A N   1 
ATOM   4093  C  CA  . SER A  1  551 ? 118.675 -18.673 -6.585  1.00 143.52 ?  551 SER A CA  1 
ATOM   4094  C  C   . SER A  1  551 ? 119.350 -19.120 -5.285  1.00 148.58 ?  551 SER A C   1 
ATOM   4095  O  O   . SER A  1  551 ? 119.800 -20.261 -5.193  1.00 151.69 ?  551 SER A O   1 
ATOM   4096  C  CB  . SER A  1  551 ? 119.705 -17.994 -7.483  1.00 144.38 ?  551 SER A CB  1 
ATOM   4097  O  OG  . SER A  1  551 ? 119.101 -17.461 -8.650  1.00 156.75 ?  551 SER A OG  1 
ATOM   4098  N  N   . LYS A  1  552 ? 119.425 -18.229 -4.284  1.00 164.52 ?  552 LYS A N   1 
ATOM   4099  C  CA  . LYS A  1  552 ? 120.054 -18.554 -3.004  1.00 159.43 ?  552 LYS A CA  1 
ATOM   4100  C  C   . LYS A  1  552 ? 119.218 -19.541 -2.196  1.00 155.92 ?  552 LYS A C   1 
ATOM   4101  O  O   . LYS A  1  552 ? 119.759 -20.512 -1.668  1.00 166.23 ?  552 LYS A O   1 
ATOM   4102  C  CB  . LYS A  1  552 ? 120.277 -17.281 -2.169  1.00 169.44 ?  552 LYS A CB  1 
ATOM   4103  C  CG  . LYS A  1  552 ? 121.423 -16.405 -2.648  1.00 174.87 ?  552 LYS A CG  1 
ATOM   4104  C  CD  . LYS A  1  552 ? 121.633 -15.226 -1.709  1.00 181.63 ?  552 LYS A CD  1 
ATOM   4105  C  CE  . LYS A  1  552 ? 122.650 -14.242 -2.228  1.00 193.16 ?  552 LYS A CE  1 
ATOM   4106  N  NZ  . LYS A  1  552 ? 122.683 -13.001 -1.409  1.00 180.56 ?  552 LYS A NZ  1 
ATOM   4107  N  N   . ILE A  1  553 ? 117.908 -19.297 -2.083  1.00 130.62 ?  553 ILE A N   1 
ATOM   4108  C  CA  . ILE A  1  553 ? 117.031 -20.171 -1.310  1.00 130.68 ?  553 ILE A CA  1 
ATOM   4109  C  C   . ILE A  1  553 ? 116.839 -21.518 -2.018  1.00 134.05 ?  553 ILE A C   1 
ATOM   4110  O  O   . ILE A  1  553 ? 116.891 -22.558 -1.363  1.00 145.69 ?  553 ILE A O   1 
ATOM   4111  C  CB  . ILE A  1  553 ? 115.695 -19.446 -0.993  1.00 119.71 ?  553 ILE A CB  1 
ATOM   4112  C  CG1 . ILE A  1  553 ? 115.952 -18.201 -0.098  1.00 120.70 ?  553 ILE A CG1 1 
ATOM   4113  C  CG2 . ILE A  1  553 ? 114.708 -20.393 -0.312  1.00 126.90 ?  553 ILE A CG2 1 
ATOM   4114  C  CD1 . ILE A  1  553 ? 114.975 -17.073 -0.271  1.00 119.87 ?  553 ILE A CD1 1 
ATOM   4115  N  N   . SER A  1  554 ? 116.648 -21.514 -3.345  1.00 129.63 ?  554 SER A N   1 
ATOM   4116  C  CA  . SER A  1  554 ? 116.466 -22.757 -4.099  1.00 134.18 ?  554 SER A CA  1 
ATOM   4117  C  C   . SER A  1  554 ? 117.750 -23.597 -4.219  1.00 145.78 ?  554 SER A C   1 
ATOM   4118  O  O   . SER A  1  554 ? 117.675 -24.747 -4.649  1.00 148.05 ?  554 SER A O   1 
ATOM   4119  C  CB  . SER A  1  554 ? 115.922 -22.459 -5.493  1.00 136.07 ?  554 SER A CB  1 
ATOM   4120  O  OG  . SER A  1  554 ? 116.900 -21.844 -6.315  1.00 135.04 ?  554 SER A OG  1 
ATOM   4121  N  N   . GLN A  1  555 ? 118.916 -23.035 -3.848  1.00 139.84 ?  555 GLN A N   1 
ATOM   4122  C  CA  . GLN A  1  555 ? 120.207 -23.724 -3.907  1.00 133.06 ?  555 GLN A CA  1 
ATOM   4123  C  C   . GLN A  1  555 ? 120.656 -24.009 -5.344  1.00 142.28 ?  555 GLN A C   1 
ATOM   4124  O  O   . GLN A  1  555 ? 121.173 -25.088 -5.633  1.00 149.95 ?  555 GLN A O   1 
ATOM   4125  C  CB  . GLN A  1  555 ? 120.189 -25.018 -3.074  1.00 142.01 ?  555 GLN A CB  1 
ATOM   4126  C  CG  . GLN A  1  555 ? 119.920 -24.791 -1.593  1.00 145.77 ?  555 GLN A CG  1 
ATOM   4127  C  CD  . GLN A  1  555 ? 120.078 -26.064 -0.795  1.00 160.87 ?  555 GLN A CD  1 
ATOM   4128  O  OE1 . GLN A  1  555 ? 119.904 -27.177 -1.309  1.00 178.47 ?  555 GLN A OE1 1 
ATOM   4129  N  NE2 . GLN A  1  555 ? 120.410 -25.938 0.481   1.00 140.38 ?  555 GLN A NE2 1 
ATOM   4130  N  N   . GLY A  1  556 ? 120.469 -23.033 -6.226  1.00 149.67 ?  556 GLY A N   1 
ATOM   4131  C  CA  . GLY A  1  556 ? 120.871 -23.150 -7.622  1.00 145.89 ?  556 GLY A CA  1 
ATOM   4132  C  C   . GLY A  1  556 ? 119.890 -23.865 -8.531  1.00 147.16 ?  556 GLY A C   1 
ATOM   4133  O  O   . GLY A  1  556 ? 120.133 -23.957 -9.737  1.00 151.88 ?  556 GLY A O   1 
ATOM   4134  N  N   . ALA A  1  557 ? 118.778 -24.380 -7.981  1.00 135.44 ?  557 ALA A N   1 
ATOM   4135  C  CA  . ALA A  1  557 ? 117.783 -25.085 -8.788  1.00 138.28 ?  557 ALA A CA  1 
ATOM   4136  C  C   . ALA A  1  557 ? 116.975 -24.108 -9.650  1.00 147.37 ?  557 ALA A C   1 
ATOM   4137  O  O   . ALA A  1  557 ? 116.802 -24.354 -10.842 1.00 147.74 ?  557 ALA A O   1 
ATOM   4138  C  CB  . ALA A  1  557 ? 116.855 -25.894 -7.890  1.00 143.43 ?  557 ALA A CB  1 
ATOM   4139  N  N   . VAL A  1  558 ? 116.494 -23.000 -9.056  1.00 142.91 ?  558 VAL A N   1 
ATOM   4140  C  CA  . VAL A  1  558 ? 115.714 -21.991 -9.773  1.00 147.11 ?  558 VAL A CA  1 
ATOM   4141  C  C   . VAL A  1  558 ? 116.568 -20.727 -9.901  1.00 145.60 ?  558 VAL A C   1 
ATOM   4142  O  O   . VAL A  1  558 ? 116.863 -20.092 -8.891  1.00 137.91 ?  558 VAL A O   1 
ATOM   4143  C  CB  . VAL A  1  558 ? 114.374 -21.697 -9.053  1.00 130.13 ?  558 VAL A CB  1 
ATOM   4144  C  CG1 . VAL A  1  558 ? 113.500 -20.765 -9.887  1.00 125.39 ?  558 VAL A CG1 1 
ATOM   4145  C  CG2 . VAL A  1  558 ? 113.625 -22.988 -8.734  1.00 130.00 ?  558 VAL A CG2 1 
ATOM   4146  N  N   . THR A  1  559 ? 116.971 -20.365 -11.134 1.00 141.90 ?  559 THR A N   1 
ATOM   4147  C  CA  . THR A  1  559 ? 117.809 -19.188 -11.373 1.00 136.81 ?  559 THR A CA  1 
ATOM   4148  C  C   . THR A  1  559 ? 117.020 -18.048 -12.045 1.00 147.15 ?  559 THR A C   1 
ATOM   4149  O  O   . THR A  1  559 ? 116.999 -16.934 -11.523 1.00 147.21 ?  559 THR A O   1 
ATOM   4150  C  CB  . THR A  1  559 ? 119.048 -19.593 -12.186 1.00 142.38 ?  559 THR A CB  1 
ATOM   4151  O  OG1 . THR A  1  559 ? 118.629 -20.189 -13.414 1.00 164.38 ?  559 THR A OG1 1 
ATOM   4152  C  CG2 . THR A  1  559 ? 119.946 -20.562 -11.432 1.00 128.33 ?  559 THR A CG2 1 
ATOM   4153  N  N   . SER A  1  560 ? 116.375 -18.317 -13.195 1.00 147.66 ?  560 SER A N   1 
ATOM   4154  C  CA  . SER A  1  560 ? 115.590 -17.304 -13.907 1.00 140.56 ?  560 SER A CA  1 
ATOM   4155  C  C   . SER A  1  560 ? 114.117 -17.458 -13.543 1.00 134.75 ?  560 SER A C   1 
ATOM   4156  O  O   . SER A  1  560 ? 113.644 -18.583 -13.396 1.00 131.03 ?  560 SER A O   1 
ATOM   4157  C  CB  . SER A  1  560 ? 115.768 -17.452 -15.415 1.00 138.33 ?  560 SER A CB  1 
ATOM   4158  O  OG  . SER A  1  560 ? 115.126 -16.394 -16.109 1.00 136.28 ?  560 SER A OG  1 
ATOM   4159  N  N   . VAL A  1  561 ? 113.389 -16.337 -13.386 1.00 139.34 ?  561 VAL A N   1 
ATOM   4160  C  CA  . VAL A  1  561 ? 111.972 -16.397 -13.022 1.00 140.15 ?  561 VAL A CA  1 
ATOM   4161  C  C   . VAL A  1  561 ? 111.199 -15.141 -13.458 1.00 142.39 ?  561 VAL A C   1 
ATOM   4162  O  O   . VAL A  1  561 ? 111.772 -14.058 -13.586 1.00 133.68 ?  561 VAL A O   1 
ATOM   4163  C  CB  . VAL A  1  561 ? 111.797 -16.668 -11.495 1.00 136.10 ?  561 VAL A CB  1 
ATOM   4164  C  CG1 . VAL A  1  561 ? 111.999 -15.396 -10.679 1.00 129.75 ?  561 VAL A CG1 1 
ATOM   4165  C  CG2 . VAL A  1  561 ? 110.440 -17.291 -11.195 1.00 149.28 ?  561 VAL A CG2 1 
ATOM   4166  N  N   . THR A  1  562 ? 109.888 -15.313 -13.687 1.00 147.13 ?  562 THR A N   1 
ATOM   4167  C  CA  . THR A  1  562 ? 108.953 -14.264 -14.088 1.00 138.76 ?  562 THR A CA  1 
ATOM   4168  C  C   . THR A  1  562 ? 107.801 -14.276 -13.084 1.00 145.49 ?  562 THR A C   1 
ATOM   4169  O  O   . THR A  1  562 ? 107.361 -15.346 -12.665 1.00 153.42 ?  562 THR A O   1 
ATOM   4170  C  CB  . THR A  1  562 ? 108.432 -14.517 -15.507 1.00 141.84 ?  562 THR A CB  1 
ATOM   4171  O  OG1 . THR A  1  562 ? 107.836 -15.820 -15.550 1.00 148.85 ?  562 THR A OG1 1 
ATOM   4172  C  CG2 . THR A  1  562 ? 109.524 -14.377 -16.564 1.00 142.79 ?  562 THR A CG2 1 
ATOM   4173  N  N   . LEU A  1  563 ? 107.313 -13.094 -12.703 1.00 133.29 ?  563 LEU A N   1 
ATOM   4174  C  CA  . LEU A  1  563 ? 106.232 -12.974 -11.724 1.00 126.31 ?  563 LEU A CA  1 
ATOM   4175  C  C   . LEU A  1  563 ? 104.836 -12.985 -12.361 1.00 133.14 ?  563 LEU A C   1 
ATOM   4176  O  O   . LEU A  1  563 ? 103.899 -13.494 -11.746 1.00 139.46 ?  563 LEU A O   1 
ATOM   4177  C  CB  . LEU A  1  563 ? 106.432 -11.673 -10.907 1.00 117.32 ?  563 LEU A CB  1 
ATOM   4178  C  CG  . LEU A  1  563 ? 106.470 -11.771 -9.376  1.00 112.19 ?  563 LEU A CG  1 
ATOM   4179  C  CD1 . LEU A  1  563 ? 107.471 -12.825 -8.892  1.00 122.08 ?  563 LEU A CD1 1 
ATOM   4180  C  CD2 . LEU A  1  563 ? 106.799 -10.424 -8.772  1.00 117.79 ?  563 LEU A CD2 1 
ATOM   4181  N  N   . TYR A  1  564 ? 104.687 -12.433 -13.577 1.00 133.52 ?  564 TYR A N   1 
ATOM   4182  C  CA  . TYR A  1  564 ? 103.388 -12.380 -14.259 1.00 131.29 ?  564 TYR A CA  1 
ATOM   4183  C  C   . TYR A  1  564 ? 103.417 -13.139 -15.599 1.00 131.47 ?  564 TYR A C   1 
ATOM   4184  O  O   . TYR A  1  564 ? 103.010 -12.601 -16.629 1.00 134.87 ?  564 TYR A O   1 
ATOM   4185  C  CB  . TYR A  1  564 ? 102.943 -10.915 -14.480 1.00 128.87 ?  564 TYR A CB  1 
ATOM   4186  C  CG  . TYR A  1  564 ? 103.382 -9.951  -13.399 1.00 127.79 ?  564 TYR A CG  1 
ATOM   4187  C  CD1 . TYR A  1  564 ? 102.975 -10.118 -12.083 1.00 121.67 ?  564 TYR A CD1 1 
ATOM   4188  C  CD2 . TYR A  1  564 ? 104.195 -8.867  -13.695 1.00 140.25 ?  564 TYR A CD2 1 
ATOM   4189  C  CE1 . TYR A  1  564 ? 103.377 -9.237  -11.087 1.00 126.83 ?  564 TYR A CE1 1 
ATOM   4190  C  CE2 . TYR A  1  564 ? 104.601 -7.979  -12.707 1.00 135.12 ?  564 TYR A CE2 1 
ATOM   4191  C  CZ  . TYR A  1  564 ? 104.192 -8.169  -11.403 1.00 130.69 ?  564 TYR A CZ  1 
ATOM   4192  O  OH  . TYR A  1  564 ? 104.585 -7.286  -10.426 1.00 148.87 ?  564 TYR A OH  1 
ATOM   4193  N  N   . SER A  1  565 ? 103.881 -14.392 -15.584 1.00 131.18 ?  565 SER A N   1 
ATOM   4194  C  CA  . SER A  1  565 ? 103.943 -15.209 -16.795 1.00 129.36 ?  565 SER A CA  1 
ATOM   4195  C  C   . SER A  1  565 ? 103.930 -16.687 -16.420 1.00 126.03 ?  565 SER A C   1 
ATOM   4196  O  O   . SER A  1  565 ? 104.658 -17.093 -15.513 1.00 132.41 ?  565 SER A O   1 
ATOM   4197  C  CB  . SER A  1  565 ? 105.199 -14.882 -17.598 1.00 132.77 ?  565 SER A CB  1 
ATOM   4198  O  OG  . SER A  1  565 ? 105.441 -15.836 -18.620 1.00 121.42 ?  565 SER A OG  1 
ATOM   4199  N  N   . ILE A  1  566 ? 103.112 -17.489 -17.116 1.00 115.27 ?  566 ILE A N   1 
ATOM   4200  C  CA  . ILE A  1  566 ? 103.010 -18.923 -16.836 1.00 112.62 ?  566 ILE A CA  1 
ATOM   4201  C  C   . ILE A  1  566 ? 103.842 -19.780 -17.795 1.00 117.23 ?  566 ILE A C   1 
ATOM   4202  O  O   . ILE A  1  566 ? 104.061 -20.950 -17.499 1.00 120.23 ?  566 ILE A O   1 
ATOM   4203  C  CB  . ILE A  1  566 ? 101.530 -19.393 -16.782 1.00 94.79  ?  566 ILE A CB  1 
ATOM   4204  C  CG1 . ILE A  1  566 ? 100.889 -19.464 -18.184 1.00 99.22  ?  566 ILE A CG1 1 
ATOM   4205  C  CG2 . ILE A  1  566 ? 100.730 -18.493 -15.855 1.00 120.04 ?  566 ILE A CG2 1 
ATOM   4206  C  CD1 . ILE A  1  566 ? 99.542  -20.166 -18.229 1.00 111.55 ?  566 ILE A CD1 1 
ATOM   4207  N  N   . LEU A  1  567 ? 104.305 -19.223 -18.930 1.00 104.60 ?  567 LEU A N   1 
ATOM   4208  C  CA  . LEU A  1  567 ? 105.096 -19.988 -19.894 1.00 109.26 ?  567 LEU A CA  1 
ATOM   4209  C  C   . LEU A  1  567 ? 106.602 -19.682 -19.789 1.00 116.41 ?  567 LEU A C   1 
ATOM   4210  O  O   . LEU A  1  567 ? 107.403 -20.609 -19.663 1.00 124.71 ?  567 LEU A O   1 
ATOM   4211  C  CB  . LEU A  1  567 ? 104.597 -19.720 -21.327 1.00 102.18 ?  567 LEU A CB  1 
ATOM   4212  C  CG  . LEU A  1  567 ? 103.170 -20.178 -21.649 1.00 94.25  ?  567 LEU A CG  1 
ATOM   4213  C  CD1 . LEU A  1  567 ? 102.675 -19.552 -22.928 1.00 108.02 ?  567 LEU A CD1 1 
ATOM   4214  C  CD2 . LEU A  1  567 ? 103.086 -21.689 -21.770 1.00 93.48  ?  567 LEU A CD2 1 
ATOM   4215  N  N   . GLN A  1  568 ? 106.993 -18.399 -19.846 1.00 117.23 ?  568 GLN A N   1 
ATOM   4216  C  CA  . GLN A  1  568 ? 108.406 -18.024 -19.761 1.00 118.30 ?  568 GLN A CA  1 
ATOM   4217  C  C   . GLN A  1  568 ? 108.869 -18.073 -18.314 1.00 118.10 ?  568 GLN A C   1 
ATOM   4218  O  O   . GLN A  1  568 ? 108.341 -17.328 -17.490 1.00 122.03 ?  568 GLN A O   1 
ATOM   4219  C  CB  . GLN A  1  568 ? 108.631 -16.614 -20.334 1.00 124.98 ?  568 GLN A CB  1 
ATOM   4220  C  CG  . GLN A  1  568 ? 110.076 -16.119 -20.206 1.00 127.79 ?  568 GLN A CG  1 
ATOM   4221  C  CD  . GLN A  1  568 ? 110.303 -14.799 -20.902 1.00 135.05 ?  568 GLN A CD  1 
ATOM   4222  O  OE1 . GLN A  1  568 ? 109.665 -14.482 -21.911 1.00 137.56 ?  568 GLN A OE1 1 
ATOM   4223  N  NE2 . GLN A  1  568 ? 111.224 -13.995 -20.380 1.00 123.04 ?  568 GLN A NE2 1 
ATOM   4224  N  N   . ASP A  1  569 ? 109.850 -18.953 -17.994 1.00 132.03 ?  569 ASP A N   1 
ATOM   4225  C  CA  . ASP A  1  569 ? 110.421 -19.131 -16.643 1.00 136.74 ?  569 ASP A CA  1 
ATOM   4226  C  C   . ASP A  1  569 ? 109.391 -18.846 -15.525 1.00 133.06 ?  569 ASP A C   1 
ATOM   4227  O  O   . ASP A  1  569 ? 109.498 -17.833 -14.841 1.00 138.59 ?  569 ASP A O   1 
ATOM   4228  C  CB  . ASP A  1  569 ? 111.665 -18.233 -16.472 1.00 139.59 ?  569 ASP A CB  1 
ATOM   4229  C  CG  . ASP A  1  569 ? 112.740 -18.447 -17.521 1.00 132.59 ?  569 ASP A CG  1 
ATOM   4230  O  OD1 . ASP A  1  569 ? 113.230 -19.591 -17.644 1.00 127.18 ?  569 ASP A OD1 1 
ATOM   4231  O  OD2 . ASP A  1  569 ? 113.100 -17.468 -18.211 1.00 129.25 ?  569 ASP A OD2 1 
ATOM   4232  N  N   . PRO A  1  570 ? 108.353 -19.684 -15.360 1.00 120.13 ?  570 PRO A N   1 
ATOM   4233  C  CA  . PRO A  1  570 ? 107.330 -19.386 -14.348 1.00 123.73 ?  570 PRO A CA  1 
ATOM   4234  C  C   . PRO A  1  570 ? 107.780 -19.540 -12.904 1.00 129.65 ?  570 PRO A C   1 
ATOM   4235  O  O   . PRO A  1  570 ? 108.819 -20.135 -12.624 1.00 113.69 ?  570 PRO A O   1 
ATOM   4236  C  CB  . PRO A  1  570 ? 106.229 -20.394 -14.677 1.00 119.41 ?  570 PRO A CB  1 
ATOM   4237  C  CG  . PRO A  1  570 ? 106.965 -21.550 -15.224 1.00 114.24 ?  570 PRO A CG  1 
ATOM   4238  C  CD  . PRO A  1  570 ? 108.028 -20.926 -16.087 1.00 121.75 ?  570 PRO A CD  1 
ATOM   4239  N  N   . MET A  1  571 ? 106.968 -19.007 -11.984 1.00 130.04 ?  571 MET A N   1 
ATOM   4240  C  CA  . MET A  1  571 ? 107.231 -19.107 -10.556 1.00 134.36 ?  571 MET A CA  1 
ATOM   4241  C  C   . MET A  1  571 ? 106.890 -20.532 -10.127 1.00 134.47 ?  571 MET A C   1 
ATOM   4242  O  O   . MET A  1  571 ? 105.851 -21.057 -10.529 1.00 132.04 ?  571 MET A O   1 
ATOM   4243  C  CB  . MET A  1  571 ? 106.351 -18.115 -9.777  1.00 140.23 ?  571 MET A CB  1 
ATOM   4244  C  CG  . MET A  1  571 ? 106.954 -16.722 -9.620  1.00 150.08 ?  571 MET A CG  1 
ATOM   4245  S  SD  . MET A  1  571 ? 108.491 -16.599 -8.653  1.00 159.53 ?  571 MET A SD  1 
ATOM   4246  C  CE  . MET A  1  571 ? 108.131 -17.663 -7.257  1.00 159.32 ?  571 MET A CE  1 
ATOM   4247  N  N   . THR A  1  572 ? 107.752 -21.161 -9.323  1.00 129.93 ?  572 THR A N   1 
ATOM   4248  C  CA  . THR A  1  572 ? 107.522 -22.535 -8.874  1.00 118.76 ?  572 THR A CA  1 
ATOM   4249  C  C   . THR A  1  572 ? 106.266 -22.646 -8.004  1.00 117.26 ?  572 THR A C   1 
ATOM   4250  O  O   . THR A  1  572 ? 105.871 -21.675 -7.357  1.00 124.73 ?  572 THR A O   1 
ATOM   4251  C  CB  . THR A  1  572 ? 108.766 -23.066 -8.138  1.00 108.28 ?  572 THR A CB  1 
ATOM   4252  O  OG1 . THR A  1  572 ? 109.172 -22.116 -7.151  1.00 127.33 ?  572 THR A OG1 1 
ATOM   4253  C  CG2 . THR A  1  572 ? 109.927 -23.361 -9.079  1.00 121.65 ?  572 THR A CG2 1 
ATOM   4254  N  N   . SER A  1  573 ? 105.635 -23.831 -8.004  1.00 112.96 ?  573 SER A N   1 
ATOM   4255  C  CA  . SER A  1  573 ? 104.428 -24.092 -7.215  1.00 115.90 ?  573 SER A CA  1 
ATOM   4256  C  C   . SER A  1  573 ? 104.739 -25.107 -6.102  1.00 111.31 ?  573 SER A C   1 
ATOM   4257  O  O   . SER A  1  573 ? 105.650 -25.916 -6.250  1.00 105.73 ?  573 SER A O   1 
ATOM   4258  C  CB  . SER A  1  573 ? 103.301 -24.587 -8.116  1.00 119.20 ?  573 SER A CB  1 
ATOM   4259  O  OG  . SER A  1  573 ? 103.048 -23.673 -9.171  1.00 111.81 ?  573 SER A OG  1 
ATOM   4260  N  N   . CYS A  1  574 ? 103.999 -25.055 -4.982  1.00 115.48 ?  574 CYS A N   1 
ATOM   4261  C  CA  . CYS A  1  574 ? 104.236 -25.942 -3.836  1.00 115.92 ?  574 CYS A CA  1 
ATOM   4262  C  C   . CYS A  1  574 ? 103.215 -27.101 -3.714  1.00 121.78 ?  574 CYS A C   1 
ATOM   4263  O  O   . CYS A  1  574 ? 103.507 -28.210 -4.157  1.00 119.03 ?  574 CYS A O   1 
ATOM   4264  C  CB  . CYS A  1  574 ? 104.322 -25.122 -2.550  1.00 110.48 ?  574 CYS A CB  1 
ATOM   4265  S  SG  . CYS A  1  574 ? 103.090 -23.798 -2.430  1.00 139.60 ?  574 CYS A SG  1 
ATOM   4266  N  N   . GLY A  1  575 ? 102.054 -26.852 -3.107  1.00 115.82 ?  575 GLY A N   1 
ATOM   4267  C  CA  . GLY A  1  575 ? 101.035 -27.884 -2.940  1.00 109.11 ?  575 GLY A CA  1 
ATOM   4268  C  C   . GLY A  1  575 ? 99.800  -27.452 -2.168  1.00 112.21 ?  575 GLY A C   1 
ATOM   4269  O  O   . GLY A  1  575 ? 98.882  -28.250 -1.973  1.00 110.33 ?  575 GLY A O   1 
ATOM   4270  N  N   . CYS A  1  576 ? 99.761  -26.188 -1.724  1.00 104.32 ?  576 CYS A N   1 
ATOM   4271  C  CA  . CYS A  1  576 ? 98.644  -25.624 -0.960  1.00 88.12  ?  576 CYS A CA  1 
ATOM   4272  C  C   . CYS A  1  576 ? 97.726  -24.740 -1.811  1.00 95.62  ?  576 CYS A C   1 
ATOM   4273  O  O   . CYS A  1  576 ? 96.851  -24.076 -1.263  1.00 105.06 ?  576 CYS A O   1 
ATOM   4274  C  CB  . CYS A  1  576 ? 99.191  -24.842 0.227   1.00 115.83 ?  576 CYS A CB  1 
ATOM   4275  S  SG  . CYS A  1  576 ? 100.443 -23.614 -0.223  1.00 110.32 ?  576 CYS A SG  1 
ATOM   4276  N  N   . PHE A  1  577 ? 97.925  -24.781 -3.133  1.00 103.29 ?  577 PHE A N   1 
ATOM   4277  C  CA  . PHE A  1  577 ? 97.112  -23.951 -4.060  1.00 93.34  ?  577 PHE A CA  1 
ATOM   4278  C  C   . PHE A  1  577 ? 95.647  -24.396 -4.016  1.00 101.29 ?  577 PHE A C   1 
ATOM   4279  O  O   . PHE A  1  577 ? 95.392  -25.609 -4.129  1.00 98.19  ?  577 PHE A O   1 
ATOM   4280  C  CB  . PHE A  1  577 ? 97.682  -24.015 -5.483  1.00 96.75  ?  577 PHE A CB  1 
ATOM   4281  C  CG  . PHE A  1  577 ? 98.317  -25.316 -5.917  1.00 94.99  ?  577 PHE A CG  1 
ATOM   4282  C  CD1 . PHE A  1  577 ? 97.546  -26.427 -6.218  1.00 99.05  ?  577 PHE A CD1 1 
ATOM   4283  C  CD2 . PHE A  1  577 ? 99.691  -25.418 -6.081  1.00 100.22 ?  577 PHE A CD2 1 
ATOM   4284  C  CE1 . PHE A  1  577 ? 98.132  -27.612 -6.639  1.00 109.81 ?  577 PHE A CE1 1 
ATOM   4285  C  CE2 . PHE A  1  577 ? 100.276 -26.603 -6.503  1.00 92.17  ?  577 PHE A CE2 1 
ATOM   4286  C  CZ  . PHE A  1  577 ? 99.498  -27.702 -6.789  1.00 106.96 ?  577 PHE A CZ  1 
ATOM   4287  N  N   . GLU A  1  578 ? 94.717  -23.456 -3.874  1.00 105.30 ?  578 GLU A N   1 
ATOM   4288  C  CA  . GLU A  1  578 ? 93.282  -23.837 -3.891  1.00 107.96 ?  578 GLU A CA  1 
ATOM   4289  C  C   . GLU A  1  578 ? 92.805  -23.945 -5.344  1.00 112.02 ?  578 GLU A C   1 
ATOM   4290  O  O   . GLU A  1  578 ? 91.945  -24.805 -5.616  1.00 123.04 ?  578 GLU A O   1 
ATOM   4291  C  CB  . GLU A  1  578 ? 92.475  -22.833 -3.071  1.00 109.62 ?  578 GLU A CB  1 
ATOM   4292  C  CG  . GLU A  1  578 ? 90.999  -22.875 -3.380  1.00 115.39 ?  578 GLU A CG  1 
ATOM   4293  C  CD  . GLU A  1  578 ? 90.236  -24.096 -2.894  1.00 141.68 ?  578 GLU A CD  1 
ATOM   4294  O  OE1 . GLU A  1  578 ? 90.179  -24.301 -1.667  1.00 150.21 ?  578 GLU A OE1 1 
ATOM   4295  O  OE2 . GLU A  1  578 ? 89.682  -24.831 -3.743  1.00 143.70 ?  578 GLU A OE2 1 
ATOM   4296  N  N   . CYS A  1  579 ? 93.353  -23.119 -6.241  1.00 105.24 ?  579 CYS A N   1 
ATOM   4297  C  CA  . CYS A  1  579 ? 92.982  -23.176 -7.649  1.00 97.64  ?  579 CYS A CA  1 
ATOM   4298  C  C   . CYS A  1  579 ? 94.198  -23.449 -8.521  1.00 99.48  ?  579 CYS A C   1 
ATOM   4299  O  O   . CYS A  1  579 ? 95.316  -23.078 -8.165  1.00 101.57 ?  579 CYS A O   1 
ATOM   4300  C  CB  . CYS A  1  579 ? 92.285  -21.886 -8.066  1.00 94.65  ?  579 CYS A CB  1 
ATOM   4301  S  SG  . CYS A  1  579 ? 90.831  -21.477 -7.070  1.00 128.25 ?  579 CYS A SG  1 
ATOM   4302  N  N   . ILE A  1  580 ? 93.979  -24.100 -9.667  1.00 89.65  ?  580 ILE A N   1 
ATOM   4303  C  CA  . ILE A  1  580 ? 95.047  -24.398 -10.614 1.00 88.70  ?  580 ILE A CA  1 
ATOM   4304  C  C   . ILE A  1  580 ? 94.632  -23.830 -11.966 1.00 90.95  ?  580 ILE A C   1 
ATOM   4305  O  O   . ILE A  1  580 ? 93.444  -23.804 -12.291 1.00 90.52  ?  580 ILE A O   1 
ATOM   4306  C  CB  . ILE A  1  580 ? 95.366  -25.916 -10.691 1.00 83.11  ?  580 ILE A CB  1 
ATOM   4307  C  CG1 . ILE A  1  580 ? 95.958  -26.420 -9.357  1.00 98.25  ?  580 ILE A CG1 1 
ATOM   4308  C  CG2 . ILE A  1  580 ? 96.333  -26.205 -11.851 1.00 84.72  ?  580 ILE A CG2 1 
ATOM   4309  C  CD1 . ILE A  1  580 ? 95.834  -27.905 -9.136  1.00 93.68  ?  580 ILE A CD1 1 
ATOM   4310  N  N   . THR A  1  581 ? 95.609  -23.353 -12.742 1.00 91.81  ?  581 THR A N   1 
ATOM   4311  C  CA  . THR A  1  581 ? 95.371  -22.780 -14.061 1.00 95.52  ?  581 THR A CA  1 
ATOM   4312  C  C   . THR A  1  581 ? 96.253  -23.490 -15.091 1.00 97.90  ?  581 THR A C   1 
ATOM   4313  O  O   . THR A  1  581 ? 97.476  -23.371 -15.043 1.00 93.66  ?  581 THR A O   1 
ATOM   4314  C  CB  . THR A  1  581 ? 95.626  -21.265 -14.018 1.00 90.15  ?  581 THR A CB  1 
ATOM   4315  O  OG1 . THR A  1  581 ? 94.576  -20.635 -13.284 1.00 95.10  ?  581 THR A OG1 1 
ATOM   4316  C  CG2 . THR A  1  581 ? 95.721  -20.656 -15.392 1.00 99.00  ?  581 THR A CG2 1 
ATOM   4317  N  N   . GLY A  1  582 ? 95.617  -24.217 -16.010 1.00 111.19 ?  582 GLY A N   1 
ATOM   4318  C  CA  . GLY A  1  582 ? 96.306  -24.965 -17.056 1.00 113.17 ?  582 GLY A CA  1 
ATOM   4319  C  C   . GLY A  1  582 ? 96.049  -24.437 -18.453 1.00 112.35 ?  582 GLY A C   1 
ATOM   4320  O  O   . GLY A  1  582 ? 94.931  -24.030 -18.770 1.00 110.01 ?  582 GLY A O   1 
ATOM   4321  N  N   . ILE A  1  583 ? 97.079  -24.455 -19.307 1.00 101.31 ?  583 ILE A N   1 
ATOM   4322  C  CA  . ILE A  1  583 ? 96.966  -23.962 -20.684 1.00 103.46 ?  583 ILE A CA  1 
ATOM   4323  C  C   . ILE A  1  583 ? 96.143  -24.888 -21.595 1.00 101.38 ?  583 ILE A C   1 
ATOM   4324  O  O   . ILE A  1  583 ? 96.318  -26.105 -21.574 1.00 102.02 ?  583 ILE A O   1 
ATOM   4325  C  CB  . ILE A  1  583 ? 98.372  -23.661 -21.288 1.00 93.36  ?  583 ILE A CB  1 
ATOM   4326  C  CG1 . ILE A  1  583 ? 98.246  -22.823 -22.573 1.00 88.07  ?  583 ILE A CG1 1 
ATOM   4327  C  CG2 . ILE A  1  583 ? 99.157  -24.951 -21.563 1.00 98.70  ?  583 ILE A CG2 1 
ATOM   4328  C  CD1 . ILE A  1  583 ? 99.500  -22.125 -22.988 1.00 90.57  ?  583 ILE A CD1 1 
ATOM   4329  N  N   . MET A  1  584 ? 95.246  -24.295 -22.400 1.00 97.14  ?  584 MET A N   1 
ATOM   4330  C  CA  . MET A  1  584 ? 94.402  -25.018 -23.351 1.00 87.50  ?  584 MET A CA  1 
ATOM   4331  C  C   . MET A  1  584 ? 94.659  -24.398 -24.729 1.00 96.18  ?  584 MET A C   1 
ATOM   4332  O  O   . MET A  1  584 ? 93.941  -23.487 -25.135 1.00 102.15 ?  584 MET A O   1 
ATOM   4333  C  CB  . MET A  1  584 ? 92.923  -24.899 -22.960 1.00 85.52  ?  584 MET A CB  1 
ATOM   4334  C  CG  . MET A  1  584 ? 91.995  -25.687 -23.857 1.00 93.12  ?  584 MET A CG  1 
ATOM   4335  S  SD  . MET A  1  584 ? 90.300  -25.716 -23.230 1.00 93.61  ?  584 MET A SD  1 
ATOM   4336  C  CE  . MET A  1  584 ? 89.499  -26.668 -24.489 1.00 102.31 ?  584 MET A CE  1 
ATOM   4337  N  N   . PRO A  1  585 ? 95.704  -24.843 -25.450 1.00 102.90 ?  585 PRO A N   1 
ATOM   4338  C  CA  . PRO A  1  585 ? 96.001  -24.239 -26.761 1.00 100.54 ?  585 PRO A CA  1 
ATOM   4339  C  C   . PRO A  1  585 ? 94.898  -24.335 -27.816 1.00 105.15 ?  585 PRO A C   1 
ATOM   4340  O  O   . PRO A  1  585 ? 94.764  -23.414 -28.620 1.00 105.53 ?  585 PRO A O   1 
ATOM   4341  C  CB  . PRO A  1  585 ? 97.268  -24.972 -27.216 1.00 94.84  ?  585 PRO A CB  1 
ATOM   4342  C  CG  . PRO A  1  585 ? 97.841  -25.576 -25.987 1.00 94.75  ?  585 PRO A CG  1 
ATOM   4343  C  CD  . PRO A  1  585 ? 96.681  -25.894 -25.109 1.00 105.81 ?  585 PRO A CD  1 
ATOM   4344  N  N   . GLU A  1  586 ? 94.117  -25.429 -27.832 1.00 112.34 ?  586 GLU A N   1 
ATOM   4345  C  CA  . GLU A  1  586 ? 93.040  -25.585 -28.818 1.00 114.08 ?  586 GLU A CA  1 
ATOM   4346  C  C   . GLU A  1  586 ? 92.008  -24.443 -28.737 1.00 116.53 ?  586 GLU A C   1 
ATOM   4347  O  O   . GLU A  1  586 ? 91.407  -24.091 -29.754 1.00 121.92 ?  586 GLU A O   1 
ATOM   4348  C  CB  . GLU A  1  586 ? 92.359  -26.962 -28.695 1.00 112.87 ?  586 GLU A CB  1 
ATOM   4349  C  CG  . GLU A  1  586 ? 91.701  -27.242 -27.354 1.00 118.84 ?  586 GLU A CG  1 
ATOM   4350  C  CD  . GLU A  1  586 ? 92.542  -28.075 -26.408 1.00 121.79 ?  586 GLU A CD  1 
ATOM   4351  O  OE1 . GLU A  1  586 ? 93.730  -27.734 -26.208 1.00 108.64 ?  586 GLU A OE1 1 
ATOM   4352  O  OE2 . GLU A  1  586 ? 92.008  -29.066 -25.860 1.00 135.73 ?  586 GLU A OE2 1 
ATOM   4353  N  N   . ALA A  1  587 ? 91.811  -23.861 -27.537 1.00 112.12 ?  587 ALA A N   1 
ATOM   4354  C  CA  . ALA A  1  587 ? 90.881  -22.745 -27.332 1.00 101.14 ?  587 ALA A CA  1 
ATOM   4355  C  C   . ALA A  1  587 ? 91.627  -21.404 -27.170 1.00 90.13  ?  587 ALA A C   1 
ATOM   4356  O  O   . ALA A  1  587 ? 91.028  -20.435 -26.712 1.00 98.15  ?  587 ALA A O   1 
ATOM   4357  C  CB  . ALA A  1  587 ? 90.027  -23.005 -26.101 1.00 85.42  ?  587 ALA A CB  1 
ATOM   4358  N  N   . ASN A  1  588 ? 92.926  -21.347 -27.540 1.00 95.46  ?  588 ASN A N   1 
ATOM   4359  C  CA  . ASN A  1  588 ? 93.775  -20.154 -27.432 1.00 102.93 ?  588 ASN A CA  1 
ATOM   4360  C  C   . ASN A  1  588 ? 93.654  -19.485 -26.064 1.00 101.24 ?  588 ASN A C   1 
ATOM   4361  O  O   . ASN A  1  588 ? 93.735  -18.263 -25.964 1.00 117.76 ?  588 ASN A O   1 
ATOM   4362  C  CB  . ASN A  1  588 ? 93.449  -19.157 -28.551 1.00 113.72 ?  588 ASN A CB  1 
ATOM   4363  C  CG  . ASN A  1  588 ? 94.516  -18.107 -28.773 1.00 107.46 ?  588 ASN A CG  1 
ATOM   4364  O  OD1 . ASN A  1  588 ? 95.611  -18.160 -28.204 1.00 97.42  ?  588 ASN A OD1 1 
ATOM   4365  N  ND2 . ASN A  1  588 ? 94.218  -17.122 -29.609 1.00 114.39 ?  588 ASN A ND2 1 
ATOM   4366  N  N   . GLY A  1  589 ? 93.464  -20.287 -25.022 1.00 106.21 ?  589 GLY A N   1 
ATOM   4367  C  CA  . GLY A  1  589 ? 93.303  -19.754 -23.679 1.00 102.14 ?  589 GLY A CA  1 
ATOM   4368  C  C   . GLY A  1  589 ? 93.842  -20.606 -22.551 1.00 98.00  ?  589 GLY A C   1 
ATOM   4369  O  O   . GLY A  1  589 ? 94.882  -21.256 -22.678 1.00 82.49  ?  589 GLY A O   1 
ATOM   4370  N  N   . VAL A  1  590 ? 93.123  -20.561 -21.423 1.00 104.57 ?  590 VAL A N   1 
ATOM   4371  C  CA  . VAL A  1  590 ? 93.515  -21.369 -20.233 1.00 95.80  ?  590 VAL A CA  1 
ATOM   4372  C  C   . VAL A  1  590 ? 92.244  -21.805 -19.498 1.00 87.73  ?  590 VAL A C   1 
ATOM   4373  O  O   . VAL A  1  590 ? 91.187  -21.189 -19.736 1.00 101.90 ?  590 VAL A O   1 
ATOM   4374  C  CB  . VAL A  1  590 ? 94.460  -20.598 -19.290 1.00 87.60  ?  590 VAL A CB  1 
ATOM   4375  C  CG1 . VAL A  1  590 ? 95.813  -20.322 -19.928 1.00 109.17 ?  590 VAL A CG1 1 
ATOM   4376  C  CG2 . VAL A  1  590 ? 93.832  -19.314 -18.773 1.00 95.43  ?  590 VAL A CG2 1 
ATOM   4377  N  N   . VAL A  1  591 ? 92.348  -22.820 -18.644 1.00 89.69  ?  591 VAL A N   1 
ATOM   4378  C  CA  . VAL A  1  591 ? 91.223  -23.353 -17.861 1.00 107.17 ?  591 VAL A CA  1 
ATOM   4379  C  C   . VAL A  1  591 ? 91.552  -23.197 -16.366 1.00 100.24 ?  591 VAL A C   1 
ATOM   4380  O  O   . VAL A  1  591 ? 92.719  -23.040 -16.003 1.00 85.24  ?  591 VAL A O   1 
ATOM   4381  C  CB  . VAL A  1  591 ? 90.851  -24.822 -18.209 1.00 86.98  ?  591 VAL A CB  1 
ATOM   4382  C  CG1 . VAL A  1  591 ? 90.571  -24.985 -19.696 1.00 94.35  ?  591 VAL A CG1 1 
ATOM   4383  C  CG2 . VAL A  1  591 ? 91.920  -25.804 -17.743 1.00 89.45  ?  591 VAL A CG2 1 
ATOM   4384  N  N   . MET A  1  592 ? 90.531  -23.229 -15.501 1.00 94.15  ?  592 MET A N   1 
ATOM   4385  C  CA  . MET A  1  592 ? 90.745  -23.091 -14.062 1.00 88.86  ?  592 MET A CA  1 
ATOM   4386  C  C   . MET A  1  592 ? 89.961  -24.143 -13.305 1.00 99.15  ?  592 MET A C   1 
ATOM   4387  O  O   . MET A  1  592 ? 88.862  -24.505 -13.717 1.00 108.06 ?  592 MET A O   1 
ATOM   4388  C  CB  . MET A  1  592 ? 90.325  -21.697 -13.594 1.00 94.95  ?  592 MET A CB  1 
ATOM   4389  C  CG  . MET A  1  592 ? 91.073  -21.228 -12.369 1.00 90.16  ?  592 MET A CG  1 
ATOM   4390  S  SD  . MET A  1  592 ? 90.767  -19.493 -11.998 1.00 127.09 ?  592 MET A SD  1 
ATOM   4391  C  CE  . MET A  1  592 ? 91.616  -18.723 -13.351 1.00 97.45  ?  592 MET A CE  1 
ATOM   4392  N  N   . VAL A  1  593 ? 90.534  -24.634 -12.203 1.00 94.25  ?  593 VAL A N   1 
ATOM   4393  C  CA  . VAL A  1  593 ? 89.853  -25.684 -11.390 1.00 93.29  ?  593 VAL A CA  1 
ATOM   4394  C  C   . VAL A  1  593 ? 90.121  -25.425 -9.906  1.00 101.50 ?  593 VAL A C   1 
ATOM   4395  O  O   . VAL A  1  593 ? 91.261  -25.057 -9.568  1.00 110.37 ?  593 VAL A O   1 
ATOM   4396  C  CB  . VAL A  1  593 ? 90.304  -27.097 -11.805 1.00 93.76  ?  593 VAL A CB  1 
ATOM   4397  C  CG1 . VAL A  1  593 ? 91.807  -27.270 -11.663 1.00 109.22 ?  593 VAL A CG1 1 
ATOM   4398  C  CG2 . VAL A  1  593 ? 89.562  -28.176 -11.031 1.00 97.77  ?  593 VAL A CG2 1 
ATOM   4399  N  N   . ASN A  1  594 ? 89.105  -25.608 -9.060  1.00 103.61 ?  594 ASN A N   1 
ATOM   4400  C  CA  . ASN A  1  594 ? 89.249  -25.404 -7.615  1.00 95.46  ?  594 ASN A CA  1 
ATOM   4401  C  C   . ASN A  1  594 ? 89.365  -26.769 -6.926  1.00 96.37  ?  594 ASN A C   1 
ATOM   4402  O  O   . ASN A  1  594 ? 88.935  -27.778 -7.484  1.00 104.86 ?  594 ASN A O   1 
ATOM   4403  C  CB  . ASN A  1  594 ? 88.095  -24.570 -7.027  1.00 98.11  ?  594 ASN A CB  1 
ATOM   4404  C  CG  . ASN A  1  594 ? 86.706  -24.999 -7.434  1.00 107.87 ?  594 ASN A CG  1 
ATOM   4405  O  OD1 . ASN A  1  594 ? 86.512  -26.002 -8.125  1.00 122.67 ?  594 ASN A OD1 1 
ATOM   4406  N  ND2 . ASN A  1  594 ? 85.700  -24.243 -7.016  1.00 115.58 ?  594 ASN A ND2 1 
ATOM   4407  N  N   . ARG A  1  595 ? 89.958  -26.810 -5.728  1.00 102.85 ?  595 ARG A N   1 
ATOM   4408  C  CA  . ARG A  1  595 ? 90.142  -28.065 -4.995  1.00 92.92  ?  595 ARG A CA  1 
ATOM   4409  C  C   . ARG A  1  595 ? 88.817  -28.793 -4.711  1.00 96.77  ?  595 ARG A C   1 
ATOM   4410  O  O   . ARG A  1  595 ? 88.813  -30.014 -4.555  1.00 93.03  ?  595 ARG A O   1 
ATOM   4411  C  CB  . ARG A  1  595 ? 90.892  -27.803 -3.676  1.00 100.50 ?  595 ARG A CB  1 
ATOM   4412  C  CG  . ARG A  1  595 ? 91.585  -29.036 -3.098  1.00 107.23 ?  595 ARG A CG  1 
ATOM   4413  C  CD  . ARG A  1  595 ? 92.053  -28.851 -1.661  1.00 118.89 ?  595 ARG A CD  1 
ATOM   4414  N  NE  . ARG A  1  595 ? 93.166  -27.904 -1.546  1.00 117.95 ?  595 ARG A NE  1 
ATOM   4415  C  CZ  . ARG A  1  595 ? 93.058  -26.611 -1.240  1.00 123.23 ?  595 ARG A CZ  1 
ATOM   4416  N  NH1 . ARG A  1  595 ? 91.865  -26.068 -1.011  1.00 119.37 ?  595 ARG A NH1 1 
ATOM   4417  N  NH2 . ARG A  1  595 ? 94.141  -25.849 -1.161  1.00 129.22 ?  595 ARG A NH2 1 
ATOM   4418  N  N   . GLU A  1  596 ? 87.699  -28.055 -4.659  1.00 105.01 ?  596 GLU A N   1 
ATOM   4419  C  CA  . GLU A  1  596 ? 86.381  -28.632 -4.381  1.00 111.39 ?  596 GLU A CA  1 
ATOM   4420  C  C   . GLU A  1  596 ? 85.864  -29.503 -5.534  1.00 110.79 ?  596 GLU A C   1 
ATOM   4421  O  O   . GLU A  1  596 ? 85.159  -30.484 -5.294  1.00 105.03 ?  596 GLU A O   1 
ATOM   4422  C  CB  . GLU A  1  596 ? 85.361  -27.514 -4.101  1.00 120.45 ?  596 GLU A CB  1 
ATOM   4423  C  CG  . GLU A  1  596 ? 85.766  -26.552 -2.997  1.00 130.37 ?  596 GLU A CG  1 
ATOM   4424  C  CD  . GLU A  1  596 ? 84.677  -25.577 -2.593  1.00 150.30 ?  596 GLU A CD  1 
ATOM   4425  O  OE1 . GLU A  1  596 ? 83.720  -25.391 -3.381  1.00 143.85 ?  596 GLU A OE1 1 
ATOM   4426  O  OE2 . GLU A  1  596 ? 84.782  -24.995 -1.488  1.00 152.67 ?  596 GLU A OE2 1 
ATOM   4427  N  N   . PHE A  1  597 ? 86.195  -29.135 -6.778  1.00 112.05 ?  597 PHE A N   1 
ATOM   4428  C  CA  . PHE A  1  597 ? 85.746  -29.856 -7.969  1.00 90.78  ?  597 PHE A CA  1 
ATOM   4429  C  C   . PHE A  1  597 ? 86.353  -31.252 -8.049  1.00 88.08  ?  597 PHE A C   1 
ATOM   4430  O  O   . PHE A  1  597 ? 87.570  -31.398 -7.978  1.00 107.31 ?  597 PHE A O   1 
ATOM   4431  C  CB  . PHE A  1  597 ? 86.111  -29.053 -9.228  1.00 89.62  ?  597 PHE A CB  1 
ATOM   4432  C  CG  . PHE A  1  597 ? 85.291  -29.386 -10.448 1.00 96.55  ?  597 PHE A CG  1 
ATOM   4433  C  CD1 . PHE A  1  597 ? 83.942  -29.092 -10.495 1.00 89.81  ?  597 PHE A CD1 1 
ATOM   4434  C  CD2 . PHE A  1  597 ? 85.879  -29.951 -11.564 1.00 103.86 ?  597 PHE A CD2 1 
ATOM   4435  C  CE1 . PHE A  1  597 ? 83.190  -29.386 -11.623 1.00 95.47  ?  597 PHE A CE1 1 
ATOM   4436  C  CE2 . PHE A  1  597 ? 85.125  -30.243 -12.691 1.00 98.86  ?  597 PHE A CE2 1 
ATOM   4437  C  CZ  . PHE A  1  597 ? 83.786  -29.958 -12.714 1.00 106.20 ?  597 PHE A CZ  1 
ATOM   4438  N  N   . GLY A  1  598 ? 85.500  -32.259 -8.207  1.00 112.26 ?  598 GLY A N   1 
ATOM   4439  C  CA  . GLY A  1  598 ? 85.936  -33.649 -8.293  1.00 113.73 ?  598 GLY A CA  1 
ATOM   4440  C  C   . GLY A  1  598 ? 85.676  -34.320 -9.628  1.00 110.37 ?  598 GLY A C   1 
ATOM   4441  O  O   . GLY A  1  598 ? 85.846  -35.535 -9.745  1.00 119.71 ?  598 GLY A O   1 
ATOM   4442  N  N   . ALA A  1  599 ? 85.272  -33.549 -10.647 1.00 101.33 ?  599 ALA A N   1 
ATOM   4443  C  CA  . ALA A  1  599 ? 85.000  -34.085 -11.979 1.00 88.24  ?  599 ALA A CA  1 
ATOM   4444  C  C   . ALA A  1  599 ? 86.145  -33.717 -12.948 1.00 90.93  ?  599 ALA A C   1 
ATOM   4445  O  O   . ALA A  1  599 ? 86.991  -32.891 -12.607 1.00 96.10  ?  599 ALA A O   1 
ATOM   4446  C  CB  . ALA A  1  599 ? 83.671  -33.539 -12.485 1.00 96.71  ?  599 ALA A CB  1 
ATOM   4447  N  N   . THR A  1  600 ? 86.190  -34.336 -14.143 1.00 105.07 ?  600 THR A N   1 
ATOM   4448  C  CA  . THR A  1  600 ? 87.244  -34.047 -15.119 1.00 88.10  ?  600 THR A CA  1 
ATOM   4449  C  C   . THR A  1  600 ? 87.074  -32.643 -15.706 1.00 87.53  ?  600 THR A C   1 
ATOM   4450  O  O   . THR A  1  600 ? 86.011  -32.034 -15.582 1.00 93.65  ?  600 THR A O   1 
ATOM   4451  C  CB  . THR A  1  600 ? 87.289  -35.126 -16.215 1.00 87.57  ?  600 THR A CB  1 
ATOM   4452  O  OG1 . THR A  1  600 ? 85.994  -35.257 -16.800 1.00 108.91 ?  600 THR A OG1 1 
ATOM   4453  C  CG2 . THR A  1  600 ? 87.765  -36.476 -15.690 1.00 91.55  ?  600 THR A CG2 1 
ATOM   4454  N  N   . THR A  1  601 ? 88.136  -32.127 -16.328 1.00 91.66  ?  601 THR A N   1 
ATOM   4455  C  CA  . THR A  1  601 ? 88.150  -30.792 -16.920 1.00 91.91  ?  601 THR A CA  1 
ATOM   4456  C  C   . THR A  1  601 ? 88.402  -30.904 -18.429 1.00 86.28  ?  601 THR A C   1 
ATOM   4457  O  O   . THR A  1  601 ? 88.638  -32.014 -18.911 1.00 92.31  ?  601 THR A O   1 
ATOM   4458  C  CB  . THR A  1  601 ? 89.212  -29.954 -16.194 1.00 88.37  ?  601 THR A CB  1 
ATOM   4459  O  OG1 . THR A  1  601 ? 90.511  -30.457 -16.518 1.00 84.21  ?  601 THR A OG1 1 
ATOM   4460  C  CG2 . THR A  1  601 ? 89.006  -29.944 -14.681 1.00 90.23  ?  601 THR A CG2 1 
ATOM   4461  N  N   . PRO A  1  602 ? 88.360  -29.806 -19.214 1.00 85.00  ?  602 PRO A N   1 
ATOM   4462  C  CA  . PRO A  1  602 ? 88.605  -29.945 -20.659 1.00 82.13  ?  602 PRO A CA  1 
ATOM   4463  C  C   . PRO A  1  602 ? 89.956  -30.569 -20.992 1.00 83.11  ?  602 PRO A C   1 
ATOM   4464  O  O   . PRO A  1  602 ? 90.082  -31.219 -22.025 1.00 100.22 ?  602 PRO A O   1 
ATOM   4465  C  CB  . PRO A  1  602 ? 88.491  -28.508 -21.182 1.00 87.39  ?  602 PRO A CB  1 
ATOM   4466  C  CG  . PRO A  1  602 ? 87.690  -27.798 -20.166 1.00 95.21  ?  602 PRO A CG  1 
ATOM   4467  C  CD  . PRO A  1  602 ? 88.094  -28.400 -18.861 1.00 88.71  ?  602 PRO A CD  1 
ATOM   4468  N  N   . LEU A  1  603 ? 90.961  -30.398 -20.116 1.00 85.83  ?  603 LEU A N   1 
ATOM   4469  C  CA  . LEU A  1  603 ? 92.288  -30.977 -20.341 1.00 76.89  ?  603 LEU A CA  1 
ATOM   4470  C  C   . LEU A  1  603 ? 92.342  -32.485 -20.019 1.00 77.57  ?  603 LEU A C   1 
ATOM   4471  O  O   . LEU A  1  603 ? 93.420  -33.074 -20.058 1.00 95.85  ?  603 LEU A O   1 
ATOM   4472  C  CB  . LEU A  1  603 ? 93.345  -30.235 -19.507 1.00 78.24  ?  603 LEU A CB  1 
ATOM   4473  C  CG  . LEU A  1  603 ? 93.480  -28.736 -19.754 1.00 76.61  ?  603 LEU A CG  1 
ATOM   4474  C  CD1 . LEU A  1  603 ? 94.411  -28.115 -18.742 1.00 84.01  ?  603 LEU A CD1 1 
ATOM   4475  C  CD2 . LEU A  1  603 ? 93.975  -28.445 -21.160 1.00 96.49  ?  603 LEU A CD2 1 
ATOM   4476  N  N   . GLY A  1  604 ? 91.198  -33.094 -19.717 1.00 89.33  ?  604 GLY A N   1 
ATOM   4477  C  CA  . GLY A  1  604 ? 91.119  -34.511 -19.399 1.00 89.73  ?  604 GLY A CA  1 
ATOM   4478  C  C   . GLY A  1  604 ? 91.788  -34.872 -18.091 1.00 90.53  ?  604 GLY A C   1 
ATOM   4479  O  O   . GLY A  1  604 ? 92.219  -36.014 -17.914 1.00 99.88  ?  604 GLY A O   1 
ATOM   4480  N  N   . MET A  1  605 ? 91.879  -33.911 -17.159 1.00 91.00  ?  605 MET A N   1 
ATOM   4481  C  CA  . MET A  1  605 ? 92.518  -34.148 -15.870 1.00 88.02  ?  605 MET A CA  1 
ATOM   4482  C  C   . MET A  1  605 ? 91.671  -33.624 -14.722 1.00 96.45  ?  605 MET A C   1 
ATOM   4483  O  O   . MET A  1  605 ? 90.997  -32.607 -14.865 1.00 84.91  ?  605 MET A O   1 
ATOM   4484  C  CB  . MET A  1  605 ? 93.878  -33.439 -15.824 1.00 88.98  ?  605 MET A CB  1 
ATOM   4485  C  CG  . MET A  1  605 ? 94.946  -34.096 -16.650 1.00 82.84  ?  605 MET A CG  1 
ATOM   4486  S  SD  . MET A  1  605 ? 96.532  -33.257 -16.440 1.00 83.66  ?  605 MET A SD  1 
ATOM   4487  C  CE  . MET A  1  605 ? 96.351  -31.919 -17.591 1.00 91.04  ?  605 MET A CE  1 
ATOM   4488  N  N   . THR A  1  606 ? 91.728  -34.307 -13.574 1.00 94.30  ?  606 THR A N   1 
ATOM   4489  C  CA  . THR A  1  606 ? 91.005  -33.878 -12.375 1.00 88.23  ?  606 THR A CA  1 
ATOM   4490  C  C   . THR A  1  606 ? 91.925  -32.939 -11.585 1.00 89.77  ?  606 THR A C   1 
ATOM   4491  O  O   . THR A  1  606 ? 93.106  -32.835 -11.907 1.00 92.90  ?  606 THR A O   1 
ATOM   4492  C  CB  . THR A  1  606 ? 90.530  -35.090 -11.537 1.00 89.72  ?  606 THR A CB  1 
ATOM   4493  O  OG1 . THR A  1  606 ? 89.638  -34.628 -10.518 1.00 116.70 ?  606 THR A OG1 1 
ATOM   4494  C  CG2 . THR A  1  606 ? 91.675  -35.853 -10.883 1.00 80.73  ?  606 THR A CG2 1 
ATOM   4495  N  N   . PHE A  1  607 ? 91.403  -32.257 -10.552 1.00 99.78  ?  607 PHE A N   1 
ATOM   4496  C  CA  . PHE A  1  607 ? 92.214  -31.334 -9.754  1.00 93.69  ?  607 PHE A CA  1 
ATOM   4497  C  C   . PHE A  1  607 ? 93.492  -31.985 -9.212  1.00 88.37  ?  607 PHE A C   1 
ATOM   4498  O  O   . PHE A  1  607 ? 94.561  -31.384 -9.286  1.00 95.22  ?  607 PHE A O   1 
ATOM   4499  C  CB  . PHE A  1  607 ? 91.396  -30.746 -8.597  1.00 100.96 ?  607 PHE A CB  1 
ATOM   4500  C  CG  . PHE A  1  607 ? 92.144  -29.664 -7.858  1.00 94.76  ?  607 PHE A CG  1 
ATOM   4501  C  CD1 . PHE A  1  607 ? 92.148  -28.363 -8.324  1.00 93.70  ?  607 PHE A CD1 1 
ATOM   4502  C  CD2 . PHE A  1  607 ? 92.881  -29.959 -6.725  1.00 95.34  ?  607 PHE A CD2 1 
ATOM   4503  C  CE1 . PHE A  1  607 ? 92.846  -27.372 -7.651  1.00 99.96  ?  607 PHE A CE1 1 
ATOM   4504  C  CE2 . PHE A  1  607 ? 93.597  -28.969 -6.066  1.00 87.73  ?  607 PHE A CE2 1 
ATOM   4505  C  CZ  . PHE A  1  607 ? 93.567  -27.680 -6.527  1.00 98.52  ?  607 PHE A CZ  1 
ATOM   4506  N  N   . GLY A  1  608 ? 93.366  -33.197 -8.681  1.00 90.18  ?  608 GLY A N   1 
ATOM   4507  C  CA  . GLY A  1  608 ? 94.496  -33.941 -8.137  1.00 90.74  ?  608 GLY A CA  1 
ATOM   4508  C  C   . GLY A  1  608 ? 95.553  -34.257 -9.177  1.00 97.15  ?  608 GLY A C   1 
ATOM   4509  O  O   . GLY A  1  608 ? 96.746  -34.256 -8.864  1.00 98.38  ?  608 GLY A O   1 
ATOM   4510  N  N   . GLU A  1  609 ? 95.126  -34.537 -10.422 1.00 99.55  ?  609 GLU A N   1 
ATOM   4511  C  CA  . GLU A  1  609 ? 96.046  -34.832 -11.519 1.00 79.96  ?  609 GLU A CA  1 
ATOM   4512  C  C   . GLU A  1  609 ? 96.751  -33.547 -11.953 1.00 78.35  ?  609 GLU A C   1 
ATOM   4513  O  O   . GLU A  1  609 ? 97.945  -33.579 -12.228 1.00 87.40  ?  609 GLU A O   1 
ATOM   4514  C  CB  . GLU A  1  609 ? 95.302  -35.481 -12.704 1.00 86.54  ?  609 GLU A CB  1 
ATOM   4515  C  CG  . GLU A  1  609 ? 94.980  -36.953 -12.480 1.00 88.71  ?  609 GLU A CG  1 
ATOM   4516  C  CD  . GLU A  1  609 ? 94.079  -37.602 -13.514 1.00 92.90  ?  609 GLU A CD  1 
ATOM   4517  O  OE1 . GLU A  1  609 ? 93.296  -36.876 -14.168 1.00 101.08 ?  609 GLU A OE1 1 
ATOM   4518  O  OE2 . GLU A  1  609 ? 94.154  -38.842 -13.667 1.00 79.96  ?  609 GLU A OE2 1 
ATOM   4519  N  N   . LEU A  1  610 ? 96.008  -32.431 -11.978 1.00 78.04  ?  610 LEU A N   1 
ATOM   4520  C  CA  . LEU A  1  610 ? 96.576  -31.100 -12.327 1.00 77.57  ?  610 LEU A CA  1 
ATOM   4521  C  C   . LEU A  1  610 ? 97.609  -30.711 -11.269 1.00 90.89  ?  610 LEU A C   1 
ATOM   4522  O  O   . LEU A  1  610 ? 98.686  -30.216 -11.651 1.00 98.06  ?  610 LEU A O   1 
ATOM   4523  C  CB  . LEU A  1  610 ? 95.424  -30.088 -12.290 1.00 90.53  ?  610 LEU A CB  1 
ATOM   4524  C  CG  . LEU A  1  610 ? 94.902  -29.533 -13.617 1.00 79.93  ?  610 LEU A CG  1 
ATOM   4525  C  CD1 . LEU A  1  610 ? 95.951  -29.670 -14.709 1.00 78.82  ?  610 LEU A CD1 1 
ATOM   4526  C  CD2 . LEU A  1  610 ? 93.614  -30.233 -14.024 1.00 79.14  ?  610 LEU A CD2 1 
ATOM   4527  N  N   . ALA A  1  611 ? 97.290  -30.928 -9.991  1.00 96.14  ?  611 ALA A N   1 
ATOM   4528  C  CA  . ALA A  1  611 ? 98.147  -30.527 -8.869  1.00 91.12  ?  611 ALA A CA  1 
ATOM   4529  C  C   . ALA A  1  611 ? 99.506  -31.219 -8.968  1.00 97.82  ?  611 ALA A C   1 
ATOM   4530  O  O   . ALA A  1  611 ? 100.531 -30.612 -8.661  1.00 103.47 ?  611 ALA A O   1 
ATOM   4531  C  CB  . ALA A  1  611 ? 97.482  -30.881 -7.550  1.00 95.98  ?  611 ALA A CB  1 
ATOM   4532  N  N   . SER A  1  612 ? 99.517  -32.485 -9.406  1.00 95.23  ?  612 SER A N   1 
ATOM   4533  C  CA  . SER A  1  612 ? 100.755 -33.239 -9.579  1.00 97.44  ?  612 SER A CA  1 
ATOM   4534  C  C   . SER A  1  612 ? 101.588 -32.713 -10.781 1.00 94.85  ?  612 SER A C   1 
ATOM   4535  O  O   . SER A  1  612 ? 102.715 -33.161 -10.980 1.00 91.26  ?  612 SER A O   1 
ATOM   4536  C  CB  . SER A  1  612 ? 100.438 -34.722 -9.754  1.00 89.21  ?  612 SER A CB  1 
ATOM   4537  O  OG  . SER A  1  612 ? 99.942  -35.018 -11.049 1.00 103.89 ?  612 SER A OG  1 
ATOM   4538  N  N   . MET A  1  613 ? 101.035 -31.745 -11.519 1.00 99.16  ?  613 MET A N   1 
ATOM   4539  C  CA  . MET A  1  613 ? 101.741 -31.195 -12.708 1.00 96.19  ?  613 MET A CA  1 
ATOM   4540  C  C   . MET A  1  613 ? 102.243 -29.780 -12.394 1.00 100.71 ?  613 MET A C   1 
ATOM   4541  O  O   . MET A  1  613 ? 103.076 -29.272 -13.168 1.00 111.09 ?  613 MET A O   1 
ATOM   4542  C  CB  . MET A  1  613 ? 100.834 -31.241 -13.941 1.00 95.47  ?  613 MET A CB  1 
ATOM   4543  C  CG  . MET A  1  613 ? 100.166 -32.584 -14.147 1.00 95.25  ?  613 MET A CG  1 
ATOM   4544  S  SD  . MET A  1  613 ? 101.134 -33.664 -15.229 1.00 99.15  ?  613 MET A SD  1 
ATOM   4545  C  CE  . MET A  1  613 ? 101.096 -32.717 -16.750 1.00 105.01 ?  613 MET A CE  1 
ATOM   4546  N  N   . THR A  1  614 ? 101.754 -29.170 -11.311 1.00 97.32  ?  614 THR A N   1 
ATOM   4547  C  CA  . THR A  1  614 ? 102.152 -27.784 -10.965 1.00 104.52 ?  614 THR A CA  1 
ATOM   4548  C  C   . THR A  1  614 ? 103.130 -27.702 -9.792  1.00 116.18 ?  614 THR A C   1 
ATOM   4549  O  O   . THR A  1  614 ? 104.163 -27.024 -9.942  1.00 124.39 ?  614 THR A O   1 
ATOM   4550  C  CB  . THR A  1  614 ? 100.865 -27.020 -10.641 1.00 99.72  ?  614 THR A CB  1 
ATOM   4551  O  OG1 . THR A  1  614 ? 100.242 -27.657 -9.525  1.00 118.41 ?  614 THR A OG1 1 
ATOM   4552  C  CG2 . THR A  1  614 ? 99.906  -26.973 -11.807 1.00 94.75  ?  614 THR A CG2 1 
ATOM   4553  N  N   . GLY A  1  615 ? 102.823 -28.369 -8.677  1.00 107.60 ?  615 GLY A N   1 
ATOM   4554  C  CA  . GLY A  1  615 ? 103.658 -28.266 -7.468  1.00 103.24 ?  615 GLY A CA  1 
ATOM   4555  C  C   . GLY A  1  615 ? 104.991 -28.981 -7.538  1.00 98.98  ?  615 GLY A C   1 
ATOM   4556  O  O   . GLY A  1  615 ? 105.474 -29.237 -8.658  1.00 98.14  ?  615 GLY A O   1 
ATOM   4557  N  N   . GLY A  1  616 ? 105.563 -29.291 -6.377  1.00 95.97  ?  616 GLY A N   1 
ATOM   4558  C  CA  . GLY A  1  616 ? 106.859 -29.945 -6.253  1.00 94.55  ?  616 GLY A CA  1 
ATOM   4559  C  C   . GLY A  1  616 ? 108.059 -29.020 -6.321  1.00 105.83 ?  616 GLY A C   1 
ATOM   4560  O  O   . GLY A  1  616 ? 109.195 -29.492 -6.346  1.00 125.36 ?  616 GLY A O   1 
ATOM   4561  N  N   . GLY A  1  617 ? 107.822 -27.714 -6.345  1.00 109.40 ?  617 GLY A N   1 
ATOM   4562  C  CA  . GLY A  1  617 ? 108.894 -26.733 -6.422  1.00 99.18  ?  617 GLY A CA  1 
ATOM   4563  C  C   . GLY A  1  617 ? 109.631 -26.766 -7.748  1.00 109.10 ?  617 GLY A C   1 
ATOM   4564  O  O   . GLY A  1  617 ? 110.835 -26.510 -7.789  1.00 105.66 ?  617 GLY A O   1 
ATOM   4565  N  N   . VAL A  1  618 ? 108.925 -27.092 -8.846  1.00 115.34 ?  618 VAL A N   1 
ATOM   4566  C  CA  . VAL A  1  618 ? 109.545 -27.183 -10.171 1.00 114.71 ?  618 VAL A CA  1 
ATOM   4567  C  C   . VAL A  1  618 ? 108.988 -26.113 -11.104 1.00 117.85 ?  618 VAL A C   1 
ATOM   4568  O  O   . VAL A  1  618 ? 107.810 -25.770 -11.012 1.00 123.06 ?  618 VAL A O   1 
ATOM   4569  C  CB  . VAL A  1  618 ? 109.343 -28.595 -10.781 1.00 113.56 ?  618 VAL A CB  1 
ATOM   4570  C  CG1 . VAL A  1  618 ? 110.137 -28.754 -12.075 1.00 116.18 ?  618 VAL A CG1 1 
ATOM   4571  C  CG2 . VAL A  1  618 ? 109.724 -29.688 -9.785  1.00 116.97 ?  618 VAL A CG2 1 
ATOM   4572  N  N   . GLN A  1  619 ? 109.833 -25.590 -12.010 1.00 99.26  ?  619 GLN A N   1 
ATOM   4573  C  CA  . GLN A  1  619 ? 109.404 -24.579 -12.974 1.00 101.63 ?  619 GLN A CA  1 
ATOM   4574  C  C   . GLN A  1  619 ? 108.565 -25.288 -14.037 1.00 111.79 ?  619 GLN A C   1 
ATOM   4575  O  O   . GLN A  1  619 ? 109.116 -25.968 -14.902 1.00 102.18 ?  619 GLN A O   1 
ATOM   4576  C  CB  . GLN A  1  619 ? 110.614 -23.883 -13.618 1.00 105.98 ?  619 GLN A CB  1 
ATOM   4577  C  CG  . GLN A  1  619 ? 111.416 -23.019 -12.653 1.00 100.09 ?  619 GLN A CG  1 
ATOM   4578  C  CD  . GLN A  1  619 ? 112.223 -21.975 -13.386 1.00 104.64 ?  619 GLN A CD  1 
ATOM   4579  O  OE1 . GLN A  1  619 ? 113.382 -22.196 -13.755 1.00 107.98 ?  619 GLN A OE1 1 
ATOM   4580  N  NE2 . GLN A  1  619 ? 111.632 -20.811 -13.615 1.00 118.81 ?  619 GLN A NE2 1 
ATOM   4581  N  N   . THR A  1  620 ? 107.240 -25.149 -13.954 1.00 114.68 ?  620 THR A N   1 
ATOM   4582  C  CA  . THR A  1  620 ? 106.350 -25.873 -14.901 1.00 103.53 ?  620 THR A CA  1 
ATOM   4583  C  C   . THR A  1  620 ? 105.677 -24.876 -15.850 1.00 104.57 ?  620 THR A C   1 
ATOM   4584  O  O   . THR A  1  620 ? 104.687 -24.246 -15.433 1.00 107.19 ?  620 THR A O   1 
ATOM   4585  C  CB  . THR A  1  620 ? 105.315 -26.711 -14.140 1.00 102.14 ?  620 THR A CB  1 
ATOM   4586  O  OG1 . THR A  1  620 ? 104.453 -25.820 -13.431 1.00 118.45 ?  620 THR A OG1 1 
ATOM   4587  C  CG2 . THR A  1  620 ? 105.947 -27.684 -13.170 1.00 99.52  ?  620 THR A CG2 1 
ATOM   4588  N  N   . PRO A  1  621 ? 106.158 -24.704 -17.101 1.00 107.10 ?  621 PRO A N   1 
ATOM   4589  C  CA  . PRO A  1  621 ? 105.498 -23.816 -18.073 1.00 102.70 ?  621 PRO A CA  1 
ATOM   4590  C  C   . PRO A  1  621 ? 104.123 -24.328 -18.496 1.00 105.14 ?  621 PRO A C   1 
ATOM   4591  O  O   . PRO A  1  621 ? 103.954 -25.521 -18.736 1.00 103.94 ?  621 PRO A O   1 
ATOM   4592  C  CB  . PRO A  1  621 ? 106.471 -23.794 -19.261 1.00 88.55  ?  621 PRO A CB  1 
ATOM   4593  C  CG  . PRO A  1  621 ? 107.748 -24.359 -18.752 1.00 85.85  ?  621 PRO A CG  1 
ATOM   4594  C  CD  . PRO A  1  621 ? 107.368 -25.317 -17.678 1.00 100.93 ?  621 PRO A CD  1 
ATOM   4595  N  N   . GLY A  1  622 ? 103.159 -23.417 -18.581 1.00 95.19  ?  622 GLY A N   1 
ATOM   4596  C  CA  . GLY A  1  622 ? 101.798 -23.740 -18.983 1.00 101.83 ?  622 GLY A CA  1 
ATOM   4597  C  C   . GLY A  1  622 ? 100.846 -23.957 -17.828 1.00 100.55 ?  622 GLY A C   1 
ATOM   4598  O  O   . GLY A  1  622 ? 99.655  -23.671 -17.952 1.00 108.79 ?  622 GLY A O   1 
ATOM   4599  N  N   . PHE A  1  623 ? 101.346 -24.473 -16.700 1.00 102.07 ?  623 PHE A N   1 
ATOM   4600  C  CA  . PHE A  1  623 ? 100.498 -24.739 -15.540 1.00 113.55 ?  623 PHE A CA  1 
ATOM   4601  C  C   . PHE A  1  623 ? 101.005 -24.007 -14.292 1.00 110.16 ?  623 PHE A C   1 
ATOM   4602  O  O   . PHE A  1  623 ? 102.213 -23.869 -14.107 1.00 110.03 ?  623 PHE A O   1 
ATOM   4603  C  CB  . PHE A  1  623 ? 100.418 -26.251 -15.280 1.00 103.33 ?  623 PHE A CB  1 
ATOM   4604  C  CG  . PHE A  1  623 ? 99.866  -27.062 -16.426 1.00 100.39 ?  623 PHE A CG  1 
ATOM   4605  C  CD1 . PHE A  1  623 ? 100.658 -27.386 -17.511 1.00 101.91 ?  623 PHE A CD1 1 
ATOM   4606  C  CD2 . PHE A  1  623 ? 98.566  -27.531 -16.399 1.00 102.47 ?  623 PHE A CD2 1 
ATOM   4607  C  CE1 . PHE A  1  623 ? 100.147 -28.131 -18.564 1.00 104.29 ?  623 PHE A CE1 1 
ATOM   4608  C  CE2 . PHE A  1  623 ? 98.058  -28.276 -17.451 1.00 110.15 ?  623 PHE A CE2 1 
ATOM   4609  C  CZ  . PHE A  1  623 ? 98.852  -28.574 -18.526 1.00 118.79 ?  623 PHE A CZ  1 
ATOM   4610  N  N   . MET A  1  624 ? 100.080 -23.538 -13.437 1.00 114.35 ?  624 MET A N   1 
ATOM   4611  C  CA  . MET A  1  624 ? 100.449 -22.822 -12.218 1.00 114.34 ?  624 MET A CA  1 
ATOM   4612  C  C   . MET A  1  624 ? 99.390  -22.958 -11.117 1.00 114.21 ?  624 MET A C   1 
ATOM   4613  O  O   . MET A  1  624 ? 98.217  -23.189 -11.403 1.00 109.31 ?  624 MET A O   1 
ATOM   4614  C  CB  . MET A  1  624 ? 100.667 -21.334 -12.534 1.00 113.07 ?  624 MET A CB  1 
ATOM   4615  C  CG  . MET A  1  624 ? 99.404  -20.615 -12.957 1.00 113.46 ?  624 MET A CG  1 
ATOM   4616  S  SD  . MET A  1  624 ? 99.488  -18.837 -12.671 1.00 113.14 ?  624 MET A SD  1 
ATOM   4617  C  CE  . MET A  1  624 ? 97.989  -18.340 -13.416 1.00 113.58 ?  624 MET A CE  1 
ATOM   4618  N  N   . GLY A  1  625 ? 99.822  -22.782 -9.870  1.00 124.60 ?  625 GLY A N   1 
ATOM   4619  C  CA  . GLY A  1  625 ? 98.954  -22.844 -8.700  1.00 116.59 ?  625 GLY A CA  1 
ATOM   4620  C  C   . GLY A  1  625 ? 98.785  -21.470 -8.084  1.00 114.80 ?  625 GLY A C   1 
ATOM   4621  O  O   . GLY A  1  625 ? 99.754  -20.716 -7.991  1.00 113.80 ?  625 GLY A O   1 
ATOM   4622  N  N   . HIS A  1  626 ? 97.560  -21.122 -7.669  1.00 106.07 ?  626 HIS A N   1 
ATOM   4623  C  CA  . HIS A  1  626 ? 97.278  -19.805 -7.088  1.00 109.25 ?  626 HIS A CA  1 
ATOM   4624  C  C   . HIS A  1  626 ? 96.026  -19.835 -6.192  1.00 125.54 ?  626 HIS A C   1 
ATOM   4625  O  O   . HIS A  1  626 ? 95.267  -20.804 -6.210  1.00 125.17 ?  626 HIS A O   1 
ATOM   4626  C  CB  . HIS A  1  626 ? 97.080  -18.784 -8.224  1.00 102.07 ?  626 HIS A CB  1 
ATOM   4627  C  CG  . HIS A  1  626 ? 96.015  -19.183 -9.195  1.00 95.86  ?  626 HIS A CG  1 
ATOM   4628  N  ND1 . HIS A  1  626 ? 94.726  -18.699 -9.093  1.00 94.17  ?  626 HIS A ND1 1 
ATOM   4629  C  CD2 . HIS A  1  626 ? 96.081  -20.025 -10.251 1.00 98.24  ?  626 HIS A CD2 1 
ATOM   4630  C  CE1 . HIS A  1  626 ? 94.050  -19.256 -10.083 1.00 102.47 ?  626 HIS A CE1 1 
ATOM   4631  N  NE2 . HIS A  1  626 ? 94.827  -20.061 -10.808 1.00 109.62 ?  626 HIS A NE2 1 
ATOM   4632  N  N   . GLY A  1  627 ? 95.823  -18.768 -5.422  1.00 120.82 ?  627 GLY A N   1 
ATOM   4633  C  CA  . GLY A  1  627 ? 94.669  -18.650 -4.539  1.00 120.62 ?  627 GLY A CA  1 
ATOM   4634  C  C   . GLY A  1  627 ? 93.417  -18.200 -5.266  1.00 123.74 ?  627 GLY A C   1 
ATOM   4635  O  O   . GLY A  1  627 ? 93.409  -18.082 -6.492  1.00 127.36 ?  627 GLY A O   1 
ATOM   4636  N  N   . ARG A  1  628 ? 92.356  -17.907 -4.509  1.00 122.19 ?  628 ARG A N   1 
ATOM   4637  C  CA  . ARG A  1  628 ? 91.067  -17.504 -5.135  1.00 111.95 ?  628 ARG A CA  1 
ATOM   4638  C  C   . ARG A  1  628 ? 91.067  -15.996 -5.409  1.00 131.00 ?  628 ARG A C   1 
ATOM   4639  O  O   . ARG A  1  628 ? 90.155  -15.532 -6.120  1.00 125.48 ?  628 ARG A O   1 
ATOM   4640  C  CB  . ARG A  1  628 ? 89.896  -17.895 -4.230  1.00 104.08 ?  628 ARG A CB  1 
ATOM   4641  C  CG  . ARG A  1  628 ? 89.974  -19.317 -3.694  1.00 112.88 ?  628 ARG A CG  1 
ATOM   4642  C  CD  . ARG A  1  628 ? 88.927  -20.218 -4.320  1.00 112.51 ?  628 ARG A CD  1 
ATOM   4643  N  NE  . ARG A  1  628 ? 87.575  -19.834 -3.945  1.00 100.92 ?  628 ARG A NE  1 
ATOM   4644  C  CZ  . ARG A  1  628 ? 86.803  -20.523 -3.114  1.00 112.14 ?  628 ARG A CZ  1 
ATOM   4645  N  NH1 . ARG A  1  628 ? 87.259  -21.628 -2.549  1.00 124.56 ?  628 ARG A NH1 1 
ATOM   4646  N  NH2 . ARG A  1  628 ? 85.577  -20.105 -2.850  1.00 122.23 ?  628 ARG A NH2 1 
ATOM   4647  N  N   . GLN A  1  629 ? 92.045  -15.264 -4.867  1.00 147.20 ?  629 GLN A N   1 
ATOM   4648  C  CA  . GLN A  1  629 ? 92.085  -13.786 -5.030  1.00 141.06 ?  629 GLN A CA  1 
ATOM   4649  C  C   . GLN A  1  629 ? 92.827  -13.393 -6.311  1.00 129.05 ?  629 GLN A C   1 
ATOM   4650  O  O   . GLN A  1  629 ? 92.427  -12.391 -6.933  1.00 129.53 ?  629 GLN A O   1 
ATOM   4651  C  CB  . GLN A  1  629 ? 92.759  -13.209 -3.783  1.00 136.38 ?  629 GLN A CB  1 
ATOM   4652  C  CG  . GLN A  1  629 ? 92.363  -13.920 -2.489  1.00 137.71 ?  629 GLN A CG  1 
ATOM   4653  C  CD  . GLN A  1  629 ? 93.286  -15.037 -2.054  1.00 151.51 ?  629 GLN A CD  1 
ATOM   4654  O  OE1 . GLN A  1  629 ? 93.945  -15.677 -2.870  1.00 161.75 ?  629 GLN A OE1 1 
ATOM   4655  N  NE2 . GLN A  1  629 ? 93.339  -15.278 -0.754  1.00 146.21 ?  629 GLN A NE2 1 
ATOM   4656  N  N   . PHE A  1  630 ? 93.855  -14.151 -6.693  1.00 123.55 ?  630 PHE A N   1 
ATOM   4657  C  CA  . PHE A  1  630 ? 94.689  -13.814 -7.877  1.00 128.23 ?  630 PHE A CA  1 
ATOM   4658  C  C   . PHE A  1  630 ? 93.824  -13.778 -9.141  1.00 123.47 ?  630 PHE A C   1 
ATOM   4659  O  O   . PHE A  1  630 ? 94.138  -12.994 -10.057 1.00 112.51 ?  630 PHE A O   1 
ATOM   4660  C  CB  . PHE A  1  630 ? 95.830  -14.822 -8.022  1.00 124.03 ?  630 PHE A CB  1 
ATOM   4661  C  CG  . PHE A  1  630 ? 96.907  -14.390 -8.982  1.00 114.18 ?  630 PHE A CG  1 
ATOM   4662  C  CD1 . PHE A  1  630 ? 97.223  -13.050 -9.129  1.00 118.08 ?  630 PHE A CD1 1 
ATOM   4663  C  CD2 . PHE A  1  630 ? 97.597  -15.321 -9.740  1.00 110.47 ?  630 PHE A CD2 1 
ATOM   4664  C  CE1 . PHE A  1  630 ? 98.210  -12.649 -10.014 1.00 119.35 ?  630 PHE A CE1 1 
ATOM   4665  C  CE2 . PHE A  1  630 ? 98.584  -14.919 -10.625 1.00 99.96  ?  630 PHE A CE2 1 
ATOM   4666  C  CZ  . PHE A  1  630 ? 98.886  -13.585 -10.758 1.00 114.46 ?  630 PHE A CZ  1 
ATOM   4667  N  N   . ILE A  1  631 ? 92.777  -14.604 -9.191  1.00 120.87 ?  631 ILE A N   1 
ATOM   4668  C  CA  . ILE A  1  631 ? 91.902  -14.676 -10.399 1.00 116.89 ?  631 ILE A CA  1 
ATOM   4669  C  C   . ILE A  1  631 ? 91.549  -13.260 -10.863 1.00 129.16 ?  631 ILE A C   1 
ATOM   4670  O  O   . ILE A  1  631 ? 91.791  -12.958 -12.046 1.00 125.48 ?  631 ILE A O   1 
ATOM   4671  C  CB  . ILE A  1  631 ? 90.639  -15.507 -10.100 1.00 125.10 ?  631 ILE A CB  1 
ATOM   4672  C  CG1 . ILE A  1  631 ? 90.966  -16.761 -9.284  1.00 130.68 ?  631 ILE A CG1 1 
ATOM   4673  C  CG2 . ILE A  1  631 ? 89.900  -15.846 -11.385 1.00 130.32 ?  631 ILE A CG2 1 
ATOM   4674  C  CD1 . ILE A  1  631 ? 89.751  -17.549 -8.855  1.00 121.51 ?  631 ILE A CD1 1 
ATOM   4675  N  N   . ALA A  1  632 ? 91.002  -12.426 -9.972  1.00 139.38 ?  632 ALA A N   1 
ATOM   4676  C  CA  . ALA A  1  632 ? 90.558  -11.085 -10.368 1.00 136.68 ?  632 ALA A CA  1 
ATOM   4677  C  C   . ALA A  1  632 ? 91.708  -10.099 -10.602 1.00 130.52 ?  632 ALA A C   1 
ATOM   4678  O  O   . ALA A  1  632 ? 91.521  -9.107  -11.304 1.00 128.14 ?  632 ALA A O   1 
ATOM   4679  C  CB  . ALA A  1  632 ? 89.609  -10.527 -9.320  1.00 145.23 ?  632 ALA A CB  1 
ATOM   4680  N  N   . SER A  1  633 ? 92.886  -10.359 -10.017 1.00 131.43 ?  633 SER A N   1 
ATOM   4681  C  CA  . SER A  1  633 ? 94.054  -9.486  -10.160 1.00 125.90 ?  633 SER A CA  1 
ATOM   4682  C  C   . SER A  1  633 ? 94.402  -9.201  -11.622 1.00 131.20 ?  633 SER A C   1 
ATOM   4683  O  O   . SER A  1  633 ? 94.321  -10.093 -12.466 1.00 133.93 ?  633 SER A O   1 
ATOM   4684  C  CB  . SER A  1  633 ? 95.260  -10.105 -9.455  1.00 122.24 ?  633 SER A CB  1 
ATOM   4685  O  OG  . SER A  1  633 ? 96.487  -9.465  -9.772  1.00 117.20 ?  633 SER A OG  1 
ATOM   4686  N  N   . LYS A  1  634 ? 94.805  -7.956  -11.912 1.00 126.27 ?  634 LYS A N   1 
ATOM   4687  C  CA  . LYS A  1  634 ? 95.189  -7.566  -13.267 1.00 123.46 ?  634 LYS A CA  1 
ATOM   4688  C  C   . LYS A  1  634 ? 96.468  -8.297  -13.690 1.00 121.08 ?  634 LYS A C   1 
ATOM   4689  O  O   . LYS A  1  634 ? 96.633  -8.608  -14.868 1.00 131.54 ?  634 LYS A O   1 
ATOM   4690  C  CB  . LYS A  1  634 ? 95.409  -6.048  -13.356 1.00 130.57 ?  634 LYS A CB  1 
ATOM   4691  C  CG  . LYS A  1  634 ? 94.134  -5.227  -13.228 1.00 122.09 ?  634 LYS A CG  1 
ATOM   4692  C  CD  . LYS A  1  634 ? 94.402  -3.756  -13.507 1.00 138.15 ?  634 LYS A CD  1 
ATOM   4693  C  CE  . LYS A  1  634 ? 93.169  -2.905  -13.346 1.00 141.53 ?  634 LYS A CE  1 
ATOM   4694  N  NZ  . LYS A  1  634 ? 93.452  -1.464  -13.582 1.00 144.54 ?  634 LYS A NZ  1 
ATOM   4695  N  N   . LYS A  1  635 ? 97.351  -8.572  -12.725 1.00 120.08 ?  635 LYS A N   1 
ATOM   4696  C  CA  . LYS A  1  635 ? 98.651  -9.225  -13.044 1.00 132.49 ?  635 LYS A CA  1 
ATOM   4697  C  C   . LYS A  1  635 ? 98.455  -10.736 -13.213 1.00 129.92 ?  635 LYS A C   1 
ATOM   4698  O  O   . LYS A  1  635 ? 99.468  -11.461 -13.214 1.00 124.54 ?  635 LYS A O   1 
ATOM   4699  C  CB  . LYS A  1  635 ? 99.674  -8.934  -11.942 1.00 120.73 ?  635 LYS A CB  1 
ATOM   4700  C  CG  . LYS A  1  635 ? 99.871  -7.461  -11.611 1.00 128.31 ?  635 LYS A CG  1 
ATOM   4701  C  CD  . LYS A  1  635 ? 101.004 -6.822  -12.384 1.00 110.77 ?  635 LYS A CD  1 
ATOM   4702  C  CE  . LYS A  1  635 ? 101.747 -5.774  -11.584 1.00 119.27 ?  635 LYS A CE  1 
ATOM   4703  N  NZ  . LYS A  1  635 ? 102.039 -6.245  -10.209 1.00 164.55 ?  635 LYS A NZ  1 
ATOM   4704  N  N   . PHE A  1  636 ? 97.203  -11.170 -13.349 1.00 124.65 ?  636 PHE A N   1 
ATOM   4705  C  CA  . PHE A  1  636 ? 96.935  -12.609 -13.577 1.00 105.64 ?  636 PHE A CA  1 
ATOM   4706  C  C   . PHE A  1  636 ? 97.172  -12.974 -15.044 1.00 118.81 ?  636 PHE A C   1 
ATOM   4707  O  O   . PHE A  1  636 ? 96.326  -12.629 -15.890 1.00 124.86 ?  636 PHE A O   1 
ATOM   4708  C  CB  . PHE A  1  636 ? 95.500  -12.967 -13.194 1.00 124.01 ?  636 PHE A CB  1 
ATOM   4709  C  CG  . PHE A  1  636 ? 95.120  -14.356 -13.628 1.00 117.18 ?  636 PHE A CG  1 
ATOM   4710  C  CD1 . PHE A  1  636 ? 95.552  -15.457 -12.911 1.00 109.42 ?  636 PHE A CD1 1 
ATOM   4711  C  CD2 . PHE A  1  636 ? 94.377  -14.563 -14.777 1.00 130.47 ?  636 PHE A CD2 1 
ATOM   4712  C  CE1 . PHE A  1  636 ? 95.225  -16.737 -13.322 1.00 101.69 ?  636 PHE A CE1 1 
ATOM   4713  C  CE2 . PHE A  1  636 ? 94.053  -15.845 -15.186 1.00 123.25 ?  636 PHE A CE2 1 
ATOM   4714  C  CZ  . PHE A  1  636 ? 94.474  -16.931 -14.455 1.00 115.79 ?  636 PHE A CZ  1 
ATOM   4715  N  N   . MET A  1  637 ? 98.294  -13.639 -15.331 1.00 133.36 ?  637 MET A N   1 
ATOM   4716  C  CA  . MET A  1  637 ? 98.588  -14.090 -16.718 1.00 133.41 ?  637 MET A CA  1 
ATOM   4717  C  C   . MET A  1  637 ? 98.557  -12.866 -17.639 1.00 138.57 ?  637 MET A C   1 
ATOM   4718  O  O   . MET A  1  637 ? 98.211  -13.032 -18.825 1.00 161.29 ?  637 MET A O   1 
ATOM   4719  C  CB  . MET A  1  637 ? 97.567  -15.117 -17.216 1.00 129.67 ?  637 MET A CB  1 
ATOM   4720  C  CG  . MET A  1  637 ? 97.752  -16.495 -16.618 1.00 125.68 ?  637 MET A CG  1 
ATOM   4721  S  SD  . MET A  1  637 ? 97.000  -17.774 -17.652 1.00 126.17 ?  637 MET A SD  1 
ATOM   4722  C  CE  . MET A  1  637 ? 96.848  -16.890 -19.203 1.00 127.31 ?  637 MET A CE  1 
ATOM   4723  N  N   . LYS A  1  638 ? 98.861  -11.683 -17.097 1.00 117.69 ?  638 LYS A N   1 
ATOM   4724  C  CA  . LYS A  1  638 ? 98.810  -10.436 -17.905 1.00 125.35 ?  638 LYS A CA  1 
ATOM   4725  C  C   . LYS A  1  638 ? 99.754  -10.585 -19.101 1.00 127.25 ?  638 LYS A C   1 
ATOM   4726  O  O   . LYS A  1  638 ? 99.397  -10.111 -20.196 1.00 114.96 ?  638 LYS A O   1 
ATOM   4727  C  CB  . LYS A  1  638 ? 99.194  -9.226  -17.049 1.00 122.67 ?  638 LYS A CB  1 
ATOM   4728  C  CG  . LYS A  1  638 ? 99.161  -7.887  -17.773 1.00 137.22 ?  638 LYS A CG  1 
ATOM   4729  C  CD  . LYS A  1  638 ? 99.498  -6.720  -16.872 1.00 131.32 ?  638 LYS A CD  1 
ATOM   4730  C  CE  . LYS A  1  638 ? 99.439  -5.384  -17.583 1.00 141.85 ?  638 LYS A CE  1 
ATOM   4731  N  NZ  . LYS A  1  638 ? 99.775  -4.261  -16.675 1.00 165.79 ?  638 LYS A NZ  1 
ATOM   4732  N  N   . GLY A  1  639 ? 100.904 -11.233 -18.893 1.00 117.85 ?  639 GLY A N   1 
ATOM   4733  C  CA  . GLY A  1  639 ? 101.874 -11.439 -19.986 1.00 118.24 ?  639 GLY A CA  1 
ATOM   4734  C  C   . GLY A  1  639 ? 101.284 -12.295 -21.092 1.00 122.03 ?  639 GLY A C   1 
ATOM   4735  O  O   . GLY A  1  639 ? 101.871 -12.324 -22.190 1.00 118.89 ?  639 GLY A O   1 
ATOM   4736  N  N   . GLU A  1  640 ? 100.168 -12.973 -20.811 1.00 130.83 ?  640 GLU A N   1 
ATOM   4737  C  CA  . GLU A  1  640 ? 99.531  -13.865 -21.816 1.00 117.55 ?  640 GLU A CA  1 
ATOM   4738  C  C   . GLU A  1  640 ? 98.178  -13.285 -22.248 1.00 119.06 ?  640 GLU A C   1 
ATOM   4739  O  O   . GLU A  1  640 ? 97.508  -13.931 -23.070 1.00 116.24 ?  640 GLU A O   1 
ATOM   4740  C  CB  . GLU A  1  640 ? 99.366  -15.272 -21.241 1.00 121.56 ?  640 GLU A CB  1 
ATOM   4741  C  CG  . GLU A  1  640 ? 100.675 -16.031 -21.115 1.00 115.02 ?  640 GLU A CG  1 
ATOM   4742  C  CD  . GLU A  1  640 ? 101.352 -15.915 -19.760 1.00 133.98 ?  640 GLU A CD  1 
ATOM   4743  O  OE1 . GLU A  1  640 ? 100.821 -15.190 -18.895 1.00 153.17 ?  640 GLU A OE1 1 
ATOM   4744  O  OE2 . GLU A  1  640 ? 102.409 -16.550 -19.574 1.00 133.07 ?  640 GLU A OE2 1 
ATOM   4745  N  N   . GLY A  1  641 ? 97.803  -12.114 -21.723 1.00 114.71 ?  641 GLY A N   1 
ATOM   4746  C  CA  . GLY A  1  641 ? 96.521  -11.479 -22.093 1.00 104.09 ?  641 GLY A CA  1 
ATOM   4747  C  C   . GLY A  1  641 ? 95.628  -11.206 -20.896 1.00 129.47 ?  641 GLY A C   1 
ATOM   4748  O  O   . GLY A  1  641 ? 94.519  -10.654 -21.093 1.00 123.94 ?  641 GLY A O   1 
ATOM   4749  N  N   . GLY A  1  642 ? 96.076  -11.587 -19.696 1.00 125.81 ?  642 GLY A N   1 
ATOM   4750  C  CA  . GLY A  1  642 ? 95.302  -11.308 -18.471 1.00 112.89 ?  642 GLY A CA  1 
ATOM   4751  C  C   . GLY A  1  642 ? 94.213  -12.355 -18.324 1.00 122.75 ?  642 GLY A C   1 
ATOM   4752  O  O   . GLY A  1  642 ? 94.377  -13.457 -18.882 1.00 131.99 ?  642 GLY A O   1 
ATOM   4753  N  N   . LEU A  1  643 ? 93.134  -12.011 -17.605 1.00 132.88 ?  643 LEU A N   1 
ATOM   4754  C  CA  . LEU A  1  643 ? 92.026  -12.971 -17.339 1.00 127.55 ?  643 LEU A CA  1 
ATOM   4755  C  C   . LEU A  1  643 ? 91.246  -13.255 -18.630 1.00 129.34 ?  643 LEU A C   1 
ATOM   4756  O  O   . LEU A  1  643 ? 90.506  -14.256 -18.653 1.00 133.55 ?  643 LEU A O   1 
ATOM   4757  C  CB  . LEU A  1  643 ? 91.121  -12.405 -16.232 1.00 114.93 ?  643 LEU A CB  1 
ATOM   4758  C  CG  . LEU A  1  643 ? 90.746  -10.924 -16.328 1.00 115.90 ?  643 LEU A CG  1 
ATOM   4759  C  CD1 . LEU A  1  643 ? 89.493  -10.747 -17.171 1.00 130.14 ?  643 LEU A CD1 1 
ATOM   4760  C  CD2 . LEU A  1  643 ? 90.541  -10.300 -14.945 1.00 135.93 ?  643 LEU A CD2 1 
ATOM   4761  N  N   . GLY A  1  644 ? 91.408  -12.418 -19.659 1.00 128.05 ?  644 GLY A N   1 
ATOM   4762  C  CA  . GLY A  1  644 ? 90.740  -12.642 -20.955 1.00 130.05 ?  644 GLY A CA  1 
ATOM   4763  C  C   . GLY A  1  644 ? 90.949  -14.061 -21.454 1.00 115.75 ?  644 GLY A C   1 
ATOM   4764  O  O   . GLY A  1  644 ? 90.098  -14.544 -22.226 1.00 111.42 ?  644 GLY A O   1 
ATOM   4765  N  N   . ARG A  1  645 ? 92.036  -14.710 -21.026 1.00 113.10 ?  645 ARG A N   1 
ATOM   4766  C  CA  . ARG A  1  645 ? 92.358  -16.086 -21.488 1.00 103.87 ?  645 ARG A CA  1 
ATOM   4767  C  C   . ARG A  1  645 ? 91.479  -17.106 -20.756 1.00 106.60 ?  645 ARG A C   1 
ATOM   4768  O  O   . ARG A  1  645 ? 91.517  -18.287 -21.149 1.00 109.83 ?  645 ARG A O   1 
ATOM   4769  C  CB  . ARG A  1  645 ? 93.843  -16.385 -21.263 1.00 90.82  ?  645 ARG A CB  1 
ATOM   4770  C  CG  . ARG A  1  645 ? 94.784  -15.480 -22.045 1.00 110.08 ?  645 ARG A CG  1 
ATOM   4771  C  CD  . ARG A  1  645 ? 94.953  -15.927 -23.485 1.00 118.83 ?  645 ARG A CD  1 
ATOM   4772  N  NE  . ARG A  1  645 ? 95.635  -14.927 -24.295 1.00 114.95 ?  645 ARG A NE  1 
ATOM   4773  C  CZ  . ARG A  1  645 ? 96.017  -15.110 -25.554 1.00 109.41 ?  645 ARG A CZ  1 
ATOM   4774  N  NH1 . ARG A  1  645 ? 95.743  -16.246 -26.171 1.00 115.28 ?  645 ARG A NH1 1 
ATOM   4775  N  NH2 . ARG A  1  645 ? 96.671  -14.155 -26.192 1.00 120.10 ?  645 ARG A NH2 1 
ATOM   4776  N  N   . ILE A  1  646 ? 90.820  -16.748 -19.647 1.00 116.00 ?  646 ILE A N   1 
ATOM   4777  C  CA  . ILE A  1  646 ? 90.070  -17.811 -18.900 1.00 111.21 ?  646 ILE A CA  1 
ATOM   4778  C  C   . ILE A  1  646 ? 88.916  -18.303 -19.780 1.00 112.30 ?  646 ILE A C   1 
ATOM   4779  O  O   . ILE A  1  646 ? 88.054  -17.478 -20.136 1.00 114.70 ?  646 ILE A O   1 
ATOM   4780  C  CB  . ILE A  1  646 ? 89.596  -17.366 -17.498 1.00 109.81 ?  646 ILE A CB  1 
ATOM   4781  C  CG1 . ILE A  1  646 ? 90.771  -16.951 -16.609 1.00 90.28  ?  646 ILE A CG1 1 
ATOM   4782  C  CG2 . ILE A  1  646 ? 88.747  -18.447 -16.847 1.00 113.26 ?  646 ILE A CG2 1 
ATOM   4783  C  CD1 . ILE A  1  646 ? 90.412  -15.930 -15.556 1.00 112.39 ?  646 ILE A CD1 1 
ATOM   4784  N  N   . VAL A  1  647 ? 88.903  -19.600 -20.088 1.00 103.07 ?  647 VAL A N   1 
ATOM   4785  C  CA  . VAL A  1  647 ? 87.873  -20.152 -21.012 1.00 102.93 ?  647 VAL A CA  1 
ATOM   4786  C  C   . VAL A  1  647 ? 86.918  -21.054 -20.226 1.00 106.41 ?  647 VAL A C   1 
ATOM   4787  O  O   . VAL A  1  647 ? 85.692  -20.882 -20.374 1.00 104.64 ?  647 VAL A O   1 
ATOM   4788  C  CB  . VAL A  1  647 ? 88.563  -20.913 -22.157 1.00 101.05 ?  647 VAL A CB  1 
ATOM   4789  C  CG1 . VAL A  1  647 ? 87.733  -22.089 -22.632 1.00 112.02 ?  647 VAL A CG1 1 
ATOM   4790  C  CG2 . VAL A  1  647 ? 88.927  -19.992 -23.311 1.00 100.35 ?  647 VAL A CG2 1 
ATOM   4791  N  N   . TRP A  1  648 ? 87.458  -21.977 -19.424 1.00 104.67 ?  648 TRP A N   1 
ATOM   4792  C  CA  . TRP A  1  648 ? 86.616  -22.891 -18.663 1.00 100.32 ?  648 TRP A CA  1 
ATOM   4793  C  C   . TRP A  1  648 ? 86.853  -22.685 -17.172 1.00 105.46 ?  648 TRP A C   1 
ATOM   4794  O  O   . TRP A  1  648 ? 87.964  -22.353 -16.759 1.00 95.17  ?  648 TRP A O   1 
ATOM   4795  C  CB  . TRP A  1  648 ? 86.923  -24.336 -19.065 1.00 105.95 ?  648 TRP A CB  1 
ATOM   4796  C  CG  . TRP A  1  648 ? 85.910  -25.336 -18.605 1.00 101.74 ?  648 TRP A CG  1 
ATOM   4797  C  CD1 . TRP A  1  648 ? 84.819  -25.775 -19.293 1.00 95.92  ?  648 TRP A CD1 1 
ATOM   4798  C  CD2 . TRP A  1  648 ? 85.947  -26.090 -17.387 1.00 105.42 ?  648 TRP A CD2 1 
ATOM   4799  N  NE1 . TRP A  1  648 ? 84.157  -26.736 -18.566 1.00 109.69 ?  648 TRP A NE1 1 
ATOM   4800  C  CE2 . TRP A  1  648 ? 84.832  -26.950 -17.391 1.00 113.61 ?  648 TRP A CE2 1 
ATOM   4801  C  CE3 . TRP A  1  648 ? 86.818  -26.124 -16.292 1.00 99.21  ?  648 TRP A CE3 1 
ATOM   4802  C  CZ2 . TRP A  1  648 ? 84.557  -27.819 -16.337 1.00 111.75 ?  648 TRP A CZ2 1 
ATOM   4803  C  CZ3 . TRP A  1  648 ? 86.541  -26.982 -15.248 1.00 103.61 ?  648 TRP A CZ3 1 
ATOM   4804  C  CH2 . TRP A  1  648 ? 85.423  -27.816 -15.277 1.00 101.76 ?  648 TRP A CH2 1 
ATOM   4805  N  N   . MET A  1  649 ? 85.802  -22.874 -16.368 1.00 113.84 ?  649 MET A N   1 
ATOM   4806  C  CA  . MET A  1  649 ? 85.868  -22.689 -14.921 1.00 103.64 ?  649 MET A CA  1 
ATOM   4807  C  C   . MET A  1  649 ? 84.670  -23.396 -14.265 1.00 106.82 ?  649 MET A C   1 
ATOM   4808  O  O   . MET A  1  649 ? 83.570  -23.306 -14.810 1.00 118.45 ?  649 MET A O   1 
ATOM   4809  C  CB  . MET A  1  649 ? 85.793  -21.185 -14.625 1.00 105.88 ?  649 MET A CB  1 
ATOM   4810  C  CG  . MET A  1  649 ? 86.038  -20.818 -13.199 1.00 105.90 ?  649 MET A CG  1 
ATOM   4811  S  SD  . MET A  1  649 ? 85.818  -19.041 -12.965 1.00 117.67 ?  649 MET A SD  1 
ATOM   4812  C  CE  . MET A  1  649 ? 87.480  -18.488 -13.191 1.00 106.90 ?  649 MET A CE  1 
ATOM   4813  N  N   . PRO A  1  650 ? 84.811  -24.086 -13.111 1.00 102.92 ?  650 PRO A N   1 
ATOM   4814  C  CA  . PRO A  1  650 ? 83.626  -24.723 -12.504 1.00 96.04  ?  650 PRO A CA  1 
ATOM   4815  C  C   . PRO A  1  650 ? 82.562  -23.696 -12.121 1.00 105.75 ?  650 PRO A C   1 
ATOM   4816  O  O   . PRO A  1  650 ? 82.906  -22.577 -11.749 1.00 119.48 ?  650 PRO A O   1 
ATOM   4817  C  CB  . PRO A  1  650 ? 84.184  -25.431 -11.263 1.00 104.23 ?  650 PRO A CB  1 
ATOM   4818  C  CG  . PRO A  1  650 ? 85.648  -25.484 -11.452 1.00 97.83  ?  650 PRO A CG  1 
ATOM   4819  C  CD  . PRO A  1  650 ? 86.020  -24.314 -12.296 1.00 104.28 ?  650 PRO A CD  1 
ATOM   4820  N  N   . LYS A  1  651 ? 81.275  -24.064 -12.206 1.00 101.25 ?  651 LYS A N   1 
ATOM   4821  C  CA  . LYS A  1  651 ? 80.184  -23.148 -11.867 1.00 109.81 ?  651 LYS A CA  1 
ATOM   4822  C  C   . LYS A  1  651 ? 80.395  -22.601 -10.445 1.00 128.79 ?  651 LYS A C   1 
ATOM   4823  O  O   . LYS A  1  651 ? 80.317  -21.391 -10.246 1.00 127.83 ?  651 LYS A O   1 
ATOM   4824  C  CB  . LYS A  1  651 ? 78.820  -23.819 -12.092 1.00 94.98  ?  651 LYS A CB  1 
ATOM   4825  C  CG  . LYS A  1  651 ? 77.649  -22.849 -11.971 1.00 106.80 ?  651 LYS A CG  1 
ATOM   4826  C  CD  . LYS A  1  651 ? 76.311  -23.540 -12.135 1.00 106.88 ?  651 LYS A CD  1 
ATOM   4827  C  CE  . LYS A  1  651 ? 75.156  -22.639 -11.772 1.00 113.16 ?  651 LYS A CE  1 
ATOM   4828  N  NZ  . LYS A  1  651 ? 73.885  -23.397 -11.638 1.00 117.20 ?  651 LYS A NZ  1 
ATOM   4829  N  N   . GLU A  1  652 ? 80.670  -23.479 -9.468  1.00 144.11 ?  652 GLU A N   1 
ATOM   4830  C  CA  . GLU A  1  652 ? 80.890  -23.060 -8.079  1.00 145.23 ?  652 GLU A CA  1 
ATOM   4831  C  C   . GLU A  1  652 ? 81.866  -21.889 -7.925  1.00 143.66 ?  652 GLU A C   1 
ATOM   4832  O  O   . GLU A  1  652 ? 81.562  -20.929 -7.219  1.00 143.48 ?  652 GLU A O   1 
ATOM   4833  C  CB  . GLU A  1  652 ? 81.368  -24.244 -7.226  1.00 150.97 ?  652 GLU A CB  1 
ATOM   4834  C  CG  . GLU A  1  652 ? 80.358  -25.371 -7.126  1.00 177.91 ?  652 GLU A CG  1 
ATOM   4835  C  CD  . GLU A  1  652 ? 80.803  -26.512 -6.233  1.00 192.58 ?  652 GLU A CD  1 
ATOM   4836  O  OE1 . GLU A  1  652 ? 82.019  -26.814 -6.212  1.00 176.74 ?  652 GLU A OE1 1 
ATOM   4837  O  OE2 . GLU A  1  652 ? 79.935  -27.100 -5.549  1.00 193.89 ?  652 GLU A OE2 1 
ATOM   4838  N  N   . LEU A  1  653 ? 83.034  -21.970 -8.580  1.00 127.70 ?  653 LEU A N   1 
ATOM   4839  C  CA  . LEU A  1  653 ? 84.040  -20.911 -8.528  1.00 112.77 ?  653 LEU A CA  1 
ATOM   4840  C  C   . LEU A  1  653 ? 83.583  -19.712 -9.355  1.00 116.48 ?  653 LEU A C   1 
ATOM   4841  O  O   . LEU A  1  653 ? 83.801  -18.574 -8.954  1.00 129.90 ?  653 LEU A O   1 
ATOM   4842  C  CB  . LEU A  1  653 ? 85.382  -21.437 -9.064  1.00 109.84 ?  653 LEU A CB  1 
ATOM   4843  C  CG  . LEU A  1  653 ? 86.600  -20.531 -8.864  1.00 110.96 ?  653 LEU A CG  1 
ATOM   4844  C  CD1 . LEU A  1  653 ? 87.000  -20.462 -7.407  1.00 122.00 ?  653 LEU A CD1 1 
ATOM   4845  C  CD2 . LEU A  1  653 ? 87.778  -21.023 -9.683  1.00 117.34 ?  653 LEU A CD2 1 
ATOM   4846  N  N   . LYS A  1  654 ? 82.955  -19.989 -10.488 1.00 115.89 ?  654 LYS A N   1 
ATOM   4847  C  CA  . LYS A  1  654 ? 82.464  -18.891 -11.348 1.00 119.40 ?  654 LYS A CA  1 
ATOM   4848  C  C   . LYS A  1  654 ? 81.521  -17.996 -10.542 1.00 132.31 ?  654 LYS A C   1 
ATOM   4849  O  O   . LYS A  1  654 ? 81.749  -16.772 -10.520 1.00 140.01 ?  654 LYS A O   1 
ATOM   4850  C  CB  . LYS A  1  654 ? 81.741  -19.516 -12.534 1.00 119.40 ?  654 LYS A CB  1 
ATOM   4851  C  CG  . LYS A  1  654 ? 81.983  -18.826 -13.860 1.00 118.40 ?  654 LYS A CG  1 
ATOM   4852  C  CD  . LYS A  1  654 ? 80.824  -19.100 -14.748 1.00 107.10 ?  654 LYS A CD  1 
ATOM   4853  C  CE  . LYS A  1  654 ? 80.818  -20.518 -15.276 1.00 119.80 ?  654 LYS A CE  1 
ATOM   4854  N  NZ  . LYS A  1  654 ? 80.490  -20.565 -16.721 1.00 122.71 ?  654 LYS A NZ  1 
ATOM   4855  N  N   . ASP A  1  655 ? 80.513  -18.588 -9.898  1.00 137.87 ?  655 ASP A N   1 
ATOM   4856  C  CA  . ASP A  1  655 ? 79.524  -17.805 -9.161  1.00 141.57 ?  655 ASP A CA  1 
ATOM   4857  C  C   . ASP A  1  655 ? 80.163  -17.023 -8.012  1.00 138.04 ?  655 ASP A C   1 
ATOM   4858  O  O   . ASP A  1  655 ? 79.787  -15.875 -7.783  1.00 149.28 ?  655 ASP A O   1 
ATOM   4859  C  CB  . ASP A  1  655 ? 78.394  -18.711 -8.646  1.00 148.70 ?  655 ASP A CB  1 
ATOM   4860  C  CG  . ASP A  1  655 ? 77.534  -19.299 -9.751  1.00 147.50 ?  655 ASP A CG  1 
ATOM   4861  O  OD1 . ASP A  1  655 ? 77.459  -18.683 -10.838 1.00 139.21 ?  655 ASP A OD1 1 
ATOM   4862  O  OD2 . ASP A  1  655 ? 76.936  -20.374 -9.529  1.00 139.16 ?  655 ASP A OD2 1 
ATOM   4863  N  N   . PHE A  1  656 ? 81.130  -17.620 -7.300  1.00 124.00 ?  656 PHE A N   1 
ATOM   4864  C  CA  . PHE A  1  656 ? 81.795  -16.930 -6.196  1.00 115.35 ?  656 PHE A CA  1 
ATOM   4865  C  C   . PHE A  1  656 ? 82.558  -15.709 -6.731  1.00 123.80 ?  656 PHE A C   1 
ATOM   4866  O  O   . PHE A  1  656 ? 82.269  -14.587 -6.320  1.00 129.37 ?  656 PHE A O   1 
ATOM   4867  C  CB  . PHE A  1  656 ? 82.725  -17.891 -5.438  1.00 118.75 ?  656 PHE A CB  1 
ATOM   4868  C  CG  . PHE A  1  656 ? 83.509  -17.243 -4.322  1.00 123.29 ?  656 PHE A CG  1 
ATOM   4869  C  CD1 . PHE A  1  656 ? 82.881  -16.833 -3.161  1.00 125.04 ?  656 PHE A CD1 1 
ATOM   4870  C  CD2 . PHE A  1  656 ? 84.875  -17.059 -4.430  1.00 132.69 ?  656 PHE A CD2 1 
ATOM   4871  C  CE1 . PHE A  1  656 ? 83.606  -16.245 -2.132  1.00 138.35 ?  656 PHE A CE1 1 
ATOM   4872  C  CE2 . PHE A  1  656 ? 85.598  -16.481 -3.396  1.00 129.97 ?  656 PHE A CE2 1 
ATOM   4873  C  CZ  . PHE A  1  656 ? 84.960  -16.075 -2.255  1.00 123.15 ?  656 PHE A CZ  1 
ATOM   4874  N  N   . VAL A  1  657 ? 83.494  -15.914 -7.670  1.00 129.03 ?  657 VAL A N   1 
ATOM   4875  C  CA  . VAL A  1  657 ? 84.230  -14.794 -8.259  1.00 131.68 ?  657 VAL A CA  1 
ATOM   4876  C  C   . VAL A  1  657 ? 83.514  -14.415 -9.551  1.00 125.04 ?  657 VAL A C   1 
ATOM   4877  O  O   . VAL A  1  657 ? 83.969  -14.772 -10.631 1.00 139.96 ?  657 VAL A O   1 
ATOM   4878  C  CB  . VAL A  1  657 ? 85.753  -15.061 -8.490  1.00 138.71 ?  657 VAL A CB  1 
ATOM   4879  C  CG1 . VAL A  1  657 ? 86.522  -15.075 -7.173  1.00 132.13 ?  657 VAL A CG1 1 
ATOM   4880  C  CG2 . VAL A  1  657 ? 86.011  -16.345 -9.281  1.00 125.03 ?  657 VAL A CG2 1 
ATOM   4881  N  N   . ALA A  1  658 ? 82.370  -13.725 -9.442  1.00 125.97 ?  658 ALA A N   1 
ATOM   4882  C  CA  . ALA A  1  658 ? 81.608  -13.322 -10.623 1.00 118.15 ?  658 ALA A CA  1 
ATOM   4883  C  C   . ALA A  1  658 ? 81.619  -11.794 -10.777 1.00 139.68 ?  658 ALA A C   1 
ATOM   4884  O  O   . ALA A  1  658 ? 81.991  -11.299 -11.835 1.00 144.21 ?  658 ALA A O   1 
ATOM   4885  C  CB  . ALA A  1  658 ? 80.179  -13.851 -10.546 1.00 124.27 ?  658 ALA A CB  1 
ATOM   4886  N  N   . GLU A  1  659 ? 81.237  -11.045 -9.729  1.00 154.87 ?  659 GLU A N   1 
ATOM   4887  C  CA  . GLU A  1  659 ? 81.230  -9.585  -9.796  1.00 150.61 ?  659 GLU A CA  1 
ATOM   4888  C  C   . GLU A  1  659 ? 82.656  -9.027  -9.758  1.00 151.67 ?  659 GLU A C   1 
ATOM   4889  O  O   . GLU A  1  659 ? 82.918  -7.984  -10.354 1.00 154.53 ?  659 GLU A O   1 
ATOM   4890  C  CB  . GLU A  1  659 ? 80.398  -8.991  -8.650  1.00 157.96 ?  659 GLU A CB  1 
ATOM   4891  C  CG  . GLU A  1  659 ? 78.902  -9.203  -8.807  1.00 155.64 ?  659 GLU A CG  1 
ATOM   4892  C  CD  . GLU A  1  659 ? 78.050  -8.475  -7.785  1.00 171.57 ?  659 GLU A CD  1 
ATOM   4893  O  OE1 . GLU A  1  659 ? 78.619  -7.886  -6.837  1.00 156.11 ?  659 GLU A OE1 1 
ATOM   4894  O  OE2 . GLU A  1  659 ? 76.807  -8.494  -7.933  1.00 191.09 ?  659 GLU A OE2 1 
ATOM   4895  N  N   . LYS A  1  660 ? 83.578  -9.716  -9.070  1.00 152.25 ?  660 LYS A N   1 
ATOM   4896  C  CA  . LYS A  1  660 ? 84.966  -9.271  -8.991  1.00 155.06 ?  660 LYS A CA  1 
ATOM   4897  C  C   . LYS A  1  660 ? 85.682  -9.454  -10.338 1.00 159.60 ?  660 LYS A C   1 
ATOM   4898  O  O   . LYS A  1  660 ? 86.590  -8.684  -10.646 1.00 160.30 ?  660 LYS A O   1 
ATOM   4899  C  CB  . LYS A  1  660 ? 85.703  -10.002 -7.861  1.00 158.59 ?  660 LYS A CB  1 
ATOM   4900  C  CG  . LYS A  1  660 ? 85.134  -9.671  -6.487  1.00 157.11 ?  660 LYS A CG  1 
ATOM   4901  C  CD  . LYS A  1  660 ? 85.948  -10.272 -5.361  1.00 147.17 ?  660 LYS A CD  1 
ATOM   4902  C  CE  . LYS A  1  660 ? 85.360  -9.923  -4.017  1.00 143.58 ?  660 LYS A CE  1 
ATOM   4903  N  NZ  . LYS A  1  660 ? 86.077  -10.599 -2.907  1.00 153.37 ?  660 LYS A NZ  1 
ATOM   4904  N  N   . LEU A  1  661 ? 85.273  -10.450 -11.146 1.00 169.84 ?  661 LEU A N   1 
ATOM   4905  C  CA  . LEU A  1  661 ? 85.869  -10.662 -12.465 1.00 165.32 ?  661 LEU A CA  1 
ATOM   4906  C  C   . LEU A  1  661 ? 85.190  -9.760  -13.487 1.00 172.00 ?  661 LEU A C   1 
ATOM   4907  O  O   . LEU A  1  661 ? 85.864  -9.219  -14.352 1.00 184.33 ?  661 LEU A O   1 
ATOM   4908  C  CB  . LEU A  1  661 ? 85.734  -12.124 -12.933 1.00 159.16 ?  661 LEU A CB  1 
ATOM   4909  C  CG  . LEU A  1  661 ? 86.438  -13.210 -12.119 1.00 167.85 ?  661 LEU A CG  1 
ATOM   4910  C  CD1 . LEU A  1  661 ? 86.426  -14.534 -12.866 1.00 157.74 ?  661 LEU A CD1 1 
ATOM   4911  C  CD2 . LEU A  1  661 ? 87.863  -12.834 -11.776 1.00 172.54 ?  661 LEU A CD2 1 
ATOM   4912  N  N   . ASN A  1  662 ? 83.861  -9.601  -13.401 1.00 149.48 ?  662 ASN A N   1 
ATOM   4913  C  CA  . ASN A  1  662 ? 83.115  -8.762  -14.339 1.00 146.02 ?  662 ASN A CA  1 
ATOM   4914  C  C   . ASN A  1  662 ? 83.567  -7.298  -14.298 1.00 158.65 ?  662 ASN A C   1 
ATOM   4915  O  O   . ASN A  1  662 ? 83.496  -6.615  -15.319 1.00 157.06 ?  662 ASN A O   1 
ATOM   4916  C  CB  . ASN A  1  662 ? 81.612  -8.861  -14.067 1.00 162.47 ?  662 ASN A CB  1 
ATOM   4917  C  CG  . ASN A  1  662 ? 81.039  -10.230 -14.342 1.00 156.36 ?  662 ASN A CG  1 
ATOM   4918  O  OD1 . ASN A  1  662 ? 81.673  -11.081 -14.974 1.00 152.80 ?  662 ASN A OD1 1 
ATOM   4919  N  ND2 . ASN A  1  662 ? 79.824  -10.481 -13.867 1.00 162.55 ?  662 ASN A ND2 1 
ATOM   4920  N  N   . LYS A  1  663 ? 84.034  -6.814  -13.135 1.00 175.13 ?  663 LYS A N   1 
ATOM   4921  C  CA  . LYS A  1  663 ? 84.506  -5.435  -13.010 1.00 181.49 ?  663 LYS A CA  1 
ATOM   4922  C  C   . LYS A  1  663 ? 85.939  -5.316  -13.531 1.00 179.41 ?  663 LYS A C   1 
ATOM   4923  O  O   . LYS A  1  663 ? 86.226  -4.416  -14.320 1.00 190.25 ?  663 LYS A O   1 
ATOM   4924  C  CB  . LYS A  1  663 ? 84.427  -4.947  -11.552 1.00 179.06 ?  663 LYS A CB  1 
ATOM   4925  C  CG  . LYS A  1  663 ? 83.027  -4.518  -11.119 1.00 178.97 ?  663 LYS A CG  1 
ATOM   4926  C  CD  . LYS A  1  663 ? 83.030  -3.746  -9.794  1.00 182.62 ?  663 LYS A CD  1 
ATOM   4927  C  CE  . LYS A  1  663 ? 82.755  -4.611  -8.583  1.00 185.76 ?  663 LYS A CE  1 
ATOM   4928  N  NZ  . LYS A  1  663 ? 83.811  -5.636  -8.356  1.00 191.05 ?  663 LYS A NZ  1 
ATOM   4929  N  N   . THR A  1  664 ? 86.839  -6.221  -13.110 1.00 152.21 ?  664 THR A N   1 
ATOM   4930  C  CA  . THR A  1  664 ? 88.229  -6.185  -13.576 1.00 157.30 ?  664 THR A CA  1 
ATOM   4931  C  C   . THR A  1  664 ? 88.277  -6.420  -15.094 1.00 152.37 ?  664 THR A C   1 
ATOM   4932  O  O   . THR A  1  664 ? 89.102  -5.812  -15.772 1.00 157.39 ?  664 THR A O   1 
ATOM   4933  C  CB  . THR A  1  664 ? 89.120  -7.110  -12.738 1.00 151.19 ?  664 THR A CB  1 
ATOM   4934  O  OG1 . THR A  1  664 ? 88.582  -8.434  -12.745 1.00 153.21 ?  664 THR A OG1 1 
ATOM   4935  C  CG2 . THR A  1  664 ? 89.301  -6.605  -11.303 1.00 161.54 ?  664 THR A CG2 1 
ATOM   4936  N  N   . ALA A  1  665 ? 87.394  -7.284  -15.630 1.00 151.78 ?  665 ALA A N   1 
ATOM   4937  C  CA  . ALA A  1  665 ? 87.320  -7.541  -17.070 1.00 137.74 ?  665 ALA A CA  1 
ATOM   4938  C  C   . ALA A  1  665 ? 86.885  -6.286  -17.829 1.00 141.74 ?  665 ALA A C   1 
ATOM   4939  O  O   . ALA A  1  665 ? 87.384  -6.034  -18.921 1.00 152.95 ?  665 ALA A O   1 
ATOM   4940  C  CB  . ALA A  1  665 ? 86.350  -8.677  -17.352 1.00 129.62 ?  665 ALA A CB  1 
ATOM   4941  N  N   . LYS A  1  666 ? 85.957  -5.500  -17.258 1.00 141.24 ?  666 LYS A N   1 
ATOM   4942  C  CA  . LYS A  1  666 ? 85.507  -4.267  -17.888 1.00 144.86 ?  666 LYS A CA  1 
ATOM   4943  C  C   . LYS A  1  666 ? 86.649  -3.235  -17.911 1.00 143.94 ?  666 LYS A C   1 
ATOM   4944  O  O   . LYS A  1  666 ? 86.759  -2.465  -18.862 1.00 146.93 ?  666 LYS A O   1 
ATOM   4945  C  CB  . LYS A  1  666 ? 84.280  -3.700  -17.157 1.00 141.56 ?  666 LYS A CB  1 
ATOM   4946  C  CG  . LYS A  1  666 ? 83.610  -2.543  -17.893 1.00 131.94 ?  666 LYS A CG  1 
ATOM   4947  C  CD  . LYS A  1  666 ? 82.564  -1.841  -17.033 1.00 135.67 ?  666 LYS A CD  1 
ATOM   4948  C  CE  . LYS A  1  666 ? 82.412  -0.381  -17.389 1.00 147.41 ?  666 LYS A CE  1 
ATOM   4949  N  NZ  . LYS A  1  666 ? 81.382  0.291   -16.555 1.00 150.12 ?  666 LYS A NZ  1 
ATOM   4950  N  N   . GLU A  1  667 ? 87.479  -3.244  -16.865 1.00 145.48 ?  667 GLU A N   1 
ATOM   4951  C  CA  . GLU A  1  667 ? 88.620  -2.295  -16.792 1.00 144.02 ?  667 GLU A CA  1 
ATOM   4952  C  C   . GLU A  1  667 ? 89.626  -2.631  -17.896 1.00 142.19 ?  667 GLU A C   1 
ATOM   4953  O  O   . GLU A  1  667 ? 90.504  -1.790  -18.165 1.00 146.10 ?  667 GLU A O   1 
ATOM   4954  C  CB  . GLU A  1  667 ? 89.289  -2.371  -15.419 1.00 150.62 ?  667 GLU A CB  1 
ATOM   4955  C  CG  . GLU A  1  667 ? 88.328  -2.163  -14.265 1.00 157.43 ?  667 GLU A CG  1 
ATOM   4956  C  CD  . GLU A  1  667 ? 88.663  -2.965  -13.019 1.00 184.56 ?  667 GLU A CD  1 
ATOM   4957  O  OE1 . GLU A  1  667 ? 89.823  -3.405  -12.897 1.00 188.58 ?  667 GLU A OE1 1 
ATOM   4958  O  OE2 . GLU A  1  667 ? 87.762  -3.149  -12.176 1.00 194.05 ?  667 GLU A OE2 1 
ATOM   4959  N  N   . LEU A  1  668 ? 89.516  -3.818  -18.498 1.00 140.62 ?  668 LEU A N   1 
ATOM   4960  C  CA  . LEU A  1  668 ? 90.524  -4.237  -19.508 1.00 144.28 ?  668 LEU A CA  1 
ATOM   4961  C  C   . LEU A  1  668 ? 89.853  -4.413  -20.872 1.00 149.12 ?  668 LEU A C   1 
ATOM   4962  O  O   . LEU A  1  668 ? 90.107  -3.582  -21.764 1.00 142.51 ?  668 LEU A O   1 
ATOM   4963  C  CB  . LEU A  1  668 ? 91.163  -5.551  -19.050 1.00 137.38 ?  668 LEU A CB  1 
ATOM   4964  C  CG  . LEU A  1  668 ? 91.542  -5.620  -17.572 1.00 123.21 ?  668 LEU A CG  1 
ATOM   4965  C  CD1 . LEU A  1  668 ? 92.015  -7.017  -17.200 1.00 109.77 ?  668 LEU A CD1 1 
ATOM   4966  C  CD2 . LEU A  1  668 ? 92.605  -4.588  -17.234 1.00 137.20 ?  668 LEU A CD2 1 
ATOM   4967  N  N   . TYR A  1  669 ? 89.009  -5.432  -21.052 1.00 160.61 ?  669 TYR A N   1 
ATOM   4968  C  CA  . TYR A  1  669 ? 88.402  -5.681  -22.390 1.00 154.66 ?  669 TYR A CA  1 
ATOM   4969  C  C   . TYR A  1  669 ? 86.999  -5.086  -22.428 1.00 157.50 ?  669 TYR A C   1 
ATOM   4970  O  O   . TYR A  1  669 ? 86.291  -5.280  -23.434 1.00 167.42 ?  669 TYR A O   1 
ATOM   4971  C  CB  . TYR A  1  669 ? 88.394  -7.176  -22.690 1.00 158.29 ?  669 TYR A CB  1 
ATOM   4972  C  CG  . TYR A  1  669 ? 89.419  -7.858  -21.838 1.00 158.42 ?  669 TYR A CG  1 
ATOM   4973  C  CD1 . TYR A  1  669 ? 90.757  -7.793  -22.178 1.00 155.15 ?  669 TYR A CD1 1 
ATOM   4974  C  CD2 . TYR A  1  669 ? 89.061  -8.452  -20.642 1.00 159.82 ?  669 TYR A CD2 1 
ATOM   4975  C  CE1 . TYR A  1  669 ? 91.723  -8.369  -21.379 1.00 138.66 ?  669 TYR A CE1 1 
ATOM   4976  C  CE2 . TYR A  1  669 ? 90.013  -9.034  -19.829 1.00 159.99 ?  669 TYR A CE2 1 
ATOM   4977  C  CZ  . TYR A  1  669 ? 91.342  -8.976  -20.200 1.00 145.96 ?  669 TYR A CZ  1 
ATOM   4978  O  OH  . TYR A  1  669 ? 92.293  -9.565  -19.403 1.00 146.39 ?  669 TYR A OH  1 
ATOM   4979  N  N   . ASN A  1  670 ? 86.624  -4.345  -21.379 1.00 181.03 ?  670 ASN A N   1 
ATOM   4980  C  CA  . ASN A  1  670 ? 85.284  -3.696  -21.311 1.00 183.17 ?  670 ASN A CA  1 
ATOM   4981  C  C   . ASN A  1  670 ? 84.186  -4.765  -21.269 1.00 188.43 ?  670 ASN A C   1 
ATOM   4982  O  O   . ASN A  1  670 ? 82.999  -4.386  -21.239 1.00 200.03 ?  670 ASN A O   1 
ATOM   4983  C  CB  . ASN A  1  670 ? 85.046  -2.704  -22.454 1.00 176.70 ?  670 ASN A CB  1 
ATOM   4984  C  CG  . ASN A  1  670 ? 84.051  -1.622  -22.088 1.00 187.63 ?  670 ASN A CG  1 
ATOM   4985  O  OD1 . ASN A  1  670 ? 84.072  -1.110  -20.971 1.00 191.05 ?  670 ASN A OD1 1 
ATOM   4986  N  ND2 . ASN A  1  670 ? 83.172  -1.271  -23.014 1.00 178.95 ?  670 ASN A ND2 1 
ATOM   4987  N  N   . ILE A  1  671 ? 84.568  -6.044  -21.261 1.00 165.60 ?  671 ILE A N   1 
ATOM   4988  C  CA  . ILE A  1  671 ? 83.556  -7.134  -21.146 1.00 157.42 ?  671 ILE A CA  1 
ATOM   4989  C  C   . ILE A  1  671 ? 82.749  -6.893  -19.868 1.00 141.09 ?  671 ILE A C   1 
ATOM   4990  O  O   . ILE A  1  671 ? 83.372  -6.705  -18.805 1.00 136.02 ?  671 ILE A O   1 
ATOM   4991  C  CB  . ILE A  1  671 ? 84.233  -8.518  -21.144 1.00 166.17 ?  671 ILE A CB  1 
ATOM   4992  C  CG1 . ILE A  1  671 ? 84.904  -8.822  -22.485 1.00 130.41 ?  671 ILE A CG1 1 
ATOM   4993  C  CG2 . ILE A  1  671 ? 83.241  -9.602  -20.751 1.00 160.99 ?  671 ILE A CG2 1 
ATOM   4994  C  CD1 . ILE A  1  671 ? 85.799  -10.036 -22.457 1.00 155.50 ?  671 ILE A CD1 1 
ATOM   4995  N  N   . ASP A  1  672 ? 81.419  -6.895  -19.976 1.00 142.13 ?  672 ASP A N   1 
ATOM   4996  C  CA  . ASP A  1  672 ? 80.564  -6.597  -18.798 1.00 167.11 ?  672 ASP A CA  1 
ATOM   4997  C  C   . ASP A  1  672 ? 80.028  -7.905  -18.208 1.00 158.17 ?  672 ASP A C   1 
ATOM   4998  O  O   . ASP A  1  672 ? 79.618  -7.897  -17.031 1.00 155.70 ?  672 ASP A O   1 
ATOM   4999  C  CB  . ASP A  1  672 ? 79.440  -5.626  -19.168 1.00 182.68 ?  672 ASP A CB  1 
ATOM   5000  C  CG  . ASP A  1  672 ? 79.939  -4.386  -19.889 1.00 181.96 ?  672 ASP A CG  1 
ATOM   5001  O  OD1 . ASP A  1  672 ? 80.777  -3.670  -19.306 1.00 172.68 ?  672 ASP A OD1 1 
ATOM   5002  O  OD2 . ASP A  1  672 ? 79.490  -4.150  -21.027 1.00 190.00 ?  672 ASP A OD2 1 
ATOM   5003  N  N   . ASN A  1  673 ? 80.038  -8.983  -18.998 1.00 139.57 ?  673 ASN A N   1 
ATOM   5004  C  CA  . ASN A  1  673 ? 79.556  -10.295 -18.489 1.00 134.76 ?  673 ASN A CA  1 
ATOM   5005  C  C   . ASN A  1  673 ? 80.580  -11.384 -18.825 1.00 130.17 ?  673 ASN A C   1 
ATOM   5006  O  O   . ASN A  1  673 ? 80.187  -12.392 -19.444 1.00 134.38 ?  673 ASN A O   1 
ATOM   5007  C  CB  . ASN A  1  673 ? 78.174  -10.642 -19.047 1.00 142.88 ?  673 ASN A CB  1 
ATOM   5008  C  CG  . ASN A  1  673 ? 77.045  -10.116 -18.188 1.00 159.68 ?  673 ASN A CG  1 
ATOM   5009  O  OD1 . ASN A  1  673 ? 76.775  -8.918  -18.174 1.00 150.34 ?  673 ASN A OD1 1 
ATOM   5010  N  ND2 . ASN A  1  673 ? 76.382  -11.005 -17.467 1.00 163.05 ?  673 ASN A ND2 1 
ATOM   5011  N  N   . PHE A  1  674 ? 81.839  -11.186 -18.425 1.00 130.44 ?  674 PHE A N   1 
ATOM   5012  C  CA  . PHE A  1  674 ? 82.871  -12.175 -18.716 1.00 136.90 ?  674 PHE A CA  1 
ATOM   5013  C  C   . PHE A  1  674 ? 82.375  -13.523 -18.190 1.00 144.94 ?  674 PHE A C   1 
ATOM   5014  O  O   . PHE A  1  674 ? 82.350  -14.490 -18.947 1.00 154.68 ?  674 PHE A O   1 
ATOM   5015  C  CB  . PHE A  1  674 ? 84.242  -11.708 -18.186 1.00 139.01 ?  674 PHE A CB  1 
ATOM   5016  C  CG  . PHE A  1  674 ? 85.429  -12.469 -18.734 1.00 140.18 ?  674 PHE A CG  1 
ATOM   5017  C  CD1 . PHE A  1  674 ? 85.630  -12.586 -20.100 1.00 133.42 ?  674 PHE A CD1 1 
ATOM   5018  C  CD2 . PHE A  1  674 ? 86.355  -13.048 -17.884 1.00 139.17 ?  674 PHE A CD2 1 
ATOM   5019  C  CE1 . PHE A  1  674 ? 86.722  -13.283 -20.600 1.00 137.84 ?  674 PHE A CE1 1 
ATOM   5020  C  CE2 . PHE A  1  674 ? 87.447  -13.741 -18.389 1.00 115.23 ?  674 PHE A CE2 1 
ATOM   5021  C  CZ  . PHE A  1  674 ? 87.620  -13.859 -19.743 1.00 128.46 ?  674 PHE A CZ  1 
ATOM   5022  N  N   . ALA A  1  675 ? 81.960  -13.592 -16.913 1.00 139.42 ?  675 ALA A N   1 
ATOM   5023  C  CA  . ALA A  1  675 ? 81.452  -14.831 -16.321 1.00 125.98 ?  675 ALA A CA  1 
ATOM   5024  C  C   . ALA A  1  675 ? 80.482  -15.605 -17.219 1.00 133.94 ?  675 ALA A C   1 
ATOM   5025  O  O   . ALA A  1  675 ? 80.539  -16.830 -17.262 1.00 132.20 ?  675 ALA A O   1 
ATOM   5026  C  CB  . ALA A  1  675 ? 80.802  -14.549 -14.975 1.00 137.80 ?  675 ALA A CB  1 
ATOM   5027  N  N   . ASP A  1  676 ? 79.597  -14.894 -17.933 1.00 156.44 ?  676 ASP A N   1 
ATOM   5028  C  CA  . ASP A  1  676 ? 78.639  -15.521 -18.844 1.00 160.15 ?  676 ASP A CA  1 
ATOM   5029  C  C   . ASP A  1  676 ? 79.365  -16.157 -20.050 1.00 153.44 ?  676 ASP A C   1 
ATOM   5030  O  O   . ASP A  1  676 ? 78.907  -17.171 -20.578 1.00 154.44 ?  676 ASP A O   1 
ATOM   5031  C  CB  . ASP A  1  676 ? 77.617  -14.475 -19.326 1.00 161.07 ?  676 ASP A CB  1 
ATOM   5032  C  CG  . ASP A  1  676 ? 76.567  -15.002 -20.288 1.00 165.83 ?  676 ASP A CG  1 
ATOM   5033  O  OD1 . ASP A  1  676 ? 76.380  -16.237 -20.347 1.00 179.72 ?  676 ASP A OD1 1 
ATOM   5034  O  OD2 . ASP A  1  676 ? 75.929  -14.178 -20.977 1.00 150.98 ?  676 ASP A OD2 1 
ATOM   5035  N  N   . MET A  1  677 ? 80.493  -15.568 -20.473 1.00 136.01 ?  677 MET A N   1 
ATOM   5036  C  CA  . MET A  1  677 ? 81.279  -16.068 -21.602 1.00 124.63 ?  677 MET A CA  1 
ATOM   5037  C  C   . MET A  1  677 ? 82.120  -17.299 -21.225 1.00 118.42 ?  677 MET A C   1 
ATOM   5038  O  O   . MET A  1  677 ? 82.497  -18.070 -22.104 1.00 123.49 ?  677 MET A O   1 
ATOM   5039  C  CB  . MET A  1  677 ? 82.208  -14.963 -22.128 1.00 123.10 ?  677 MET A CB  1 
ATOM   5040  C  CG  . MET A  1  677 ? 81.499  -13.656 -22.412 1.00 128.21 ?  677 MET A CG  1 
ATOM   5041  S  SD  . MET A  1  677 ? 82.256  -12.721 -23.754 1.00 131.37 ?  677 MET A SD  1 
ATOM   5042  C  CE  . MET A  1  677 ? 81.465  -13.470 -25.129 1.00 127.09 ?  677 MET A CE  1 
ATOM   5043  N  N   . ILE A  1  678 ? 82.384  -17.464 -19.926 1.00 123.29 ?  678 ILE A N   1 
ATOM   5044  C  CA  . ILE A  1  678 ? 83.204  -18.618 -19.455 1.00 109.13 ?  678 ILE A CA  1 
ATOM   5045  C  C   . ILE A  1  678 ? 82.353  -19.885 -19.520 1.00 117.89 ?  678 ILE A C   1 
ATOM   5046  O  O   . ILE A  1  678 ? 81.169  -19.823 -19.140 1.00 126.92 ?  678 ILE A O   1 
ATOM   5047  C  CB  . ILE A  1  678 ? 83.749  -18.390 -18.032 1.00 115.75 ?  678 ILE A CB  1 
ATOM   5048  C  CG1 . ILE A  1  678 ? 85.017  -17.537 -18.040 1.00 104.65 ?  678 ILE A CG1 1 
ATOM   5049  C  CG2 . ILE A  1  678 ? 83.985  -19.717 -17.331 1.00 121.24 ?  678 ILE A CG2 1 
ATOM   5050  C  CD1 . ILE A  1  678 ? 84.830  -16.201 -18.693 1.00 122.08 ?  678 ILE A CD1 1 
ATOM   5051  N  N   . CYS A  1  679 ? 82.942  -20.984 -19.986 1.00 114.62 ?  679 CYS A N   1 
ATOM   5052  C  CA  . CYS A  1  679 ? 82.240  -22.262 -20.047 1.00 112.88 ?  679 CYS A CA  1 
ATOM   5053  C  C   . CYS A  1  679 ? 82.340  -22.957 -18.681 1.00 110.64 ?  679 CYS A C   1 
ATOM   5054  O  O   . CYS A  1  679 ? 83.218  -22.624 -17.887 1.00 114.20 ?  679 CYS A O   1 
ATOM   5055  C  CB  . CYS A  1  679 ? 82.827  -23.126 -21.161 1.00 115.91 ?  679 CYS A CB  1 
ATOM   5056  S  SG  . CYS A  1  679 ? 81.854  -24.603 -21.549 1.00 114.55 ?  679 CYS A SG  1 
ATOM   5057  N  N   . ASP A  1  680 ? 81.446  -23.912 -18.399 1.00 121.31 ?  680 ASP A N   1 
ATOM   5058  C  CA  . ASP A  1  680 ? 81.457  -24.639 -17.126 1.00 119.34 ?  680 ASP A CA  1 
ATOM   5059  C  C   . ASP A  1  680 ? 80.942  -26.073 -17.312 1.00 124.90 ?  680 ASP A C   1 
ATOM   5060  O  O   . ASP A  1  680 ? 80.425  -26.400 -18.380 1.00 132.20 ?  680 ASP A O   1 
ATOM   5061  C  CB  . ASP A  1  680 ? 80.626  -23.888 -16.067 1.00 117.54 ?  680 ASP A CB  1 
ATOM   5062  C  CG  . ASP A  1  680 ? 79.182  -23.641 -16.453 1.00 132.85 ?  680 ASP A CG  1 
ATOM   5063  O  OD1 . ASP A  1  680 ? 78.672  -24.362 -17.331 1.00 135.74 ?  680 ASP A OD1 1 
ATOM   5064  O  OD2 . ASP A  1  680 ? 78.561  -22.726 -15.873 1.00 139.44 ?  680 ASP A OD2 1 
ATOM   5065  N  N   . GLU A  1  681 ? 81.079  -26.929 -16.284 1.00 118.86 ?  681 GLU A N   1 
ATOM   5066  C  CA  . GLU A  1  681 ? 80.618  -28.320 -16.362 1.00 115.10 ?  681 GLU A CA  1 
ATOM   5067  C  C   . GLU A  1  681 ? 79.132  -28.426 -16.745 1.00 129.98 ?  681 GLU A C   1 
ATOM   5068  O  O   . GLU A  1  681 ? 78.723  -29.433 -17.321 1.00 124.45 ?  681 GLU A O   1 
ATOM   5069  C  CB  . GLU A  1  681 ? 80.909  -29.074 -15.046 1.00 112.38 ?  681 GLU A CB  1 
ATOM   5070  C  CG  . GLU A  1  681 ? 79.978  -28.756 -13.882 1.00 122.29 ?  681 GLU A CG  1 
ATOM   5071  C  CD  . GLU A  1  681 ? 80.415  -27.619 -12.978 1.00 115.74 ?  681 GLU A CD  1 
ATOM   5072  O  OE1 . GLU A  1  681 ? 81.076  -26.678 -13.473 1.00 118.16 ?  681 GLU A OE1 1 
ATOM   5073  O  OE2 . GLU A  1  681 ? 80.085  -27.666 -11.771 1.00 115.73 ?  681 GLU A OE2 1 
ATOM   5074  N  N   . THR A  1  682 ? 78.331  -27.388 -16.430 1.00 133.80 ?  682 THR A N   1 
ATOM   5075  C  CA  . THR A  1  682 ? 76.905  -27.358 -16.754 1.00 117.10 ?  682 THR A CA  1 
ATOM   5076  C  C   . THR A  1  682 ? 76.722  -27.261 -18.264 1.00 124.61 ?  682 THR A C   1 
ATOM   5077  O  O   . THR A  1  682 ? 75.888  -27.965 -18.828 1.00 138.19 ?  682 THR A O   1 
ATOM   5078  C  CB  . THR A  1  682 ? 76.228  -26.177 -16.042 1.00 110.98 ?  682 THR A CB  1 
ATOM   5079  O  OG1 . THR A  1  682 ? 76.328  -26.379 -14.632 1.00 130.95 ?  682 THR A OG1 1 
ATOM   5080  C  CG2 . THR A  1  682 ? 74.771  -26.004 -16.455 1.00 114.59 ?  682 THR A CG2 1 
ATOM   5081  N  N   . ILE A  1  683 ? 77.504  -26.392 -18.918 1.00 128.14 ?  683 ILE A N   1 
ATOM   5082  C  CA  . ILE A  1  683 ? 77.425  -26.215 -20.366 1.00 122.14 ?  683 ILE A CA  1 
ATOM   5083  C  C   . ILE A  1  683 ? 78.072  -27.426 -21.062 1.00 118.70 ?  683 ILE A C   1 
ATOM   5084  O  O   . ILE A  1  683 ? 77.396  -28.119 -21.824 1.00 114.83 ?  683 ILE A O   1 
ATOM   5085  C  CB  . ILE A  1  683 ? 78.069  -24.866 -20.795 1.00 112.33 ?  683 ILE A CB  1 
ATOM   5086  C  CG1 . ILE A  1  683 ? 77.263  -23.661 -20.239 1.00 108.80 ?  683 ILE A CG1 1 
ATOM   5087  C  CG2 . ILE A  1  683 ? 78.178  -24.791 -22.318 1.00 112.13 ?  683 ILE A CG2 1 
ATOM   5088  C  CD1 . ILE A  1  683 ? 78.092  -22.411 -19.962 1.00 118.69 ?  683 ILE A CD1 1 
ATOM   5089  N  N   . ALA A  1  684 ? 79.369  -27.692 -20.795 1.00 121.75 ?  684 ALA A N   1 
ATOM   5090  C  CA  . ALA A  1  684 ? 80.105  -28.822 -21.383 1.00 120.83 ?  684 ALA A CA  1 
ATOM   5091  C  C   . ALA A  1  684 ? 81.539  -28.884 -20.846 1.00 113.76 ?  684 ALA A C   1 
ATOM   5092  O  O   . ALA A  1  684 ? 82.070  -27.872 -20.392 1.00 116.39 ?  684 ALA A O   1 
ATOM   5093  C  CB  . ALA A  1  684 ? 80.139  -28.707 -22.905 1.00 116.97 ?  684 ALA A CB  1 
ATOM   5094  N  N   . THR A  1  685 ? 82.164  -30.067 -20.907 1.00 125.43 ?  685 THR A N   1 
ATOM   5095  C  CA  . THR A  1  685 ? 83.541  -30.254 -20.449 1.00 124.13 ?  685 THR A CA  1 
ATOM   5096  C  C   . THR A  1  685 ? 84.461  -30.605 -21.629 1.00 122.82 ?  685 THR A C   1 
ATOM   5097  O  O   . THR A  1  685 ? 85.592  -30.133 -21.673 1.00 117.98 ?  685 THR A O   1 
ATOM   5098  C  CB  . THR A  1  685 ? 83.597  -31.331 -19.368 1.00 126.08 ?  685 THR A CB  1 
ATOM   5099  O  OG1 . THR A  1  685 ? 83.064  -32.544 -19.899 1.00 156.72 ?  685 THR A OG1 1 
ATOM   5100  C  CG2 . THR A  1  685 ? 82.836  -30.936 -18.114 1.00 122.52 ?  685 THR A CG2 1 
ATOM   5101  N  N   . GLU A  1  686 ? 83.975  -31.427 -22.581 1.00 119.99 ?  686 GLU A N   1 
ATOM   5102  C  CA  . GLU A  1  686 ? 84.741  -31.843 -23.764 1.00 113.46 ?  686 GLU A CA  1 
ATOM   5103  C  C   . GLU A  1  686 ? 85.268  -30.626 -24.541 1.00 118.60 ?  686 GLU A C   1 
ATOM   5104  O  O   . GLU A  1  686 ? 84.501  -29.712 -24.829 1.00 131.50 ?  686 GLU A O   1 
ATOM   5105  C  CB  . GLU A  1  686 ? 83.856  -32.726 -24.669 1.00 115.58 ?  686 GLU A CB  1 
ATOM   5106  C  CG  . GLU A  1  686 ? 84.467  -33.110 -26.007 1.00 120.91 ?  686 GLU A CG  1 
ATOM   5107  C  CD  . GLU A  1  686 ? 85.740  -33.930 -25.932 1.00 139.02 ?  686 GLU A CD  1 
ATOM   5108  O  OE1 . GLU A  1  686 ? 85.903  -34.694 -24.953 1.00 148.92 ?  686 GLU A OE1 1 
ATOM   5109  O  OE2 . GLU A  1  686 ? 86.575  -33.811 -26.859 1.00 140.93 ?  686 GLU A OE2 1 
ATOM   5110  N  N   . SER A  1  687 ? 86.572  -30.616 -24.877 1.00 118.62 ?  687 SER A N   1 
ATOM   5111  C  CA  . SER A  1  687 ? 87.211  -29.510 -25.599 1.00 109.45 ?  687 SER A CA  1 
ATOM   5112  C  C   . SER A  1  687 ? 86.454  -29.091 -26.864 1.00 116.60 ?  687 SER A C   1 
ATOM   5113  O  O   . SER A  1  687 ? 86.243  -27.898 -27.069 1.00 124.26 ?  687 SER A O   1 
ATOM   5114  C  CB  . SER A  1  687 ? 88.650  -29.867 -25.960 1.00 97.87  ?  687 SER A CB  1 
ATOM   5115  O  OG  . SER A  1  687 ? 88.695  -30.865 -26.966 1.00 132.44 ?  687 SER A OG  1 
ATOM   5116  N  N   . GLU A  1  688 ? 86.043  -30.053 -27.710 1.00 122.74 ?  688 GLU A N   1 
ATOM   5117  C  CA  . GLU A  1  688 ? 85.309  -29.737 -28.940 1.00 113.22 ?  688 GLU A CA  1 
ATOM   5118  C  C   . GLU A  1  688 ? 84.013  -28.987 -28.641 1.00 111.40 ?  688 GLU A C   1 
ATOM   5119  O  O   . GLU A  1  688 ? 83.678  -28.040 -29.348 1.00 116.56 ?  688 GLU A O   1 
ATOM   5120  C  CB  . GLU A  1  688 ? 84.987  -31.015 -29.737 1.00 118.69 ?  688 GLU A CB  1 
ATOM   5121  C  CG  . GLU A  1  688 ? 86.103  -31.494 -30.652 1.00 133.24 ?  688 GLU A CG  1 
ATOM   5122  C  CD  . GLU A  1  688 ? 85.615  -31.961 -32.009 1.00 129.87 ?  688 GLU A CD  1 
ATOM   5123  O  OE1 . GLU A  1  688 ? 84.742  -32.857 -32.052 1.00 138.48 ?  688 GLU A OE1 1 
ATOM   5124  O  OE2 . GLU A  1  688 ? 86.106  -31.429 -33.030 1.00 122.46 ?  688 GLU A OE2 1 
ATOM   5125  N  N   . GLU A  1  689 ? 83.280  -29.404 -27.604 1.00 119.72 ?  689 GLU A N   1 
ATOM   5126  C  CA  . GLU A  1  689 ? 82.032  -28.739 -27.234 1.00 126.65 ?  689 GLU A CA  1 
ATOM   5127  C  C   . GLU A  1  689 ? 82.315  -27.383 -26.578 1.00 129.58 ?  689 GLU A C   1 
ATOM   5128  O  O   . GLU A  1  689 ? 81.526  -26.455 -26.743 1.00 142.52 ?  689 GLU A O   1 
ATOM   5129  C  CB  . GLU A  1  689 ? 81.198  -29.626 -26.296 1.00 141.96 ?  689 GLU A CB  1 
ATOM   5130  C  CG  . GLU A  1  689 ? 80.600  -30.844 -26.978 1.00 142.68 ?  689 GLU A CG  1 
ATOM   5131  C  CD  . GLU A  1  689 ? 79.685  -31.675 -26.099 1.00 159.94 ?  689 GLU A CD  1 
ATOM   5132  O  OE1 . GLU A  1  689 ? 79.870  -31.656 -24.861 1.00 156.93 ?  689 GLU A OE1 1 
ATOM   5133  O  OE2 . GLU A  1  689 ? 78.783  -32.347 -26.650 1.00 159.27 ?  689 GLU A OE2 1 
ATOM   5134  N  N   . VAL A  1  690 ? 83.434  -27.259 -25.843 1.00 113.34 ?  690 VAL A N   1 
ATOM   5135  C  CA  . VAL A  1  690 ? 83.796  -26.005 -25.186 1.00 112.41 ?  690 VAL A CA  1 
ATOM   5136  C  C   . VAL A  1  690 ? 84.164  -24.961 -26.247 1.00 119.07 ?  690 VAL A C   1 
ATOM   5137  O  O   . VAL A  1  690 ? 83.725  -23.817 -26.141 1.00 127.08 ?  690 VAL A O   1 
ATOM   5138  C  CB  . VAL A  1  690 ? 84.932  -26.203 -24.145 1.00 112.40 ?  690 VAL A CB  1 
ATOM   5139  C  CG1 . VAL A  1  690 ? 85.494  -24.863 -23.677 1.00 114.60 ?  690 VAL A CG1 1 
ATOM   5140  C  CG2 . VAL A  1  690 ? 84.444  -27.019 -22.951 1.00 112.20 ?  690 VAL A CG2 1 
ATOM   5141  N  N   . VAL A  1  691 ? 84.948  -25.343 -27.273 1.00 119.60 ?  691 VAL A N   1 
ATOM   5142  C  CA  . VAL A  1  691 ? 85.325  -24.386 -28.321 1.00 104.19 ?  691 VAL A CA  1 
ATOM   5143  C  C   . VAL A  1  691 ? 84.092  -23.918 -29.104 1.00 123.63 ?  691 VAL A C   1 
ATOM   5144  O  O   . VAL A  1  691 ? 84.055  -22.768 -29.537 1.00 132.55 ?  691 VAL A O   1 
ATOM   5145  C  CB  . VAL A  1  691 ? 86.458  -24.870 -29.264 1.00 98.15  ?  691 VAL A CB  1 
ATOM   5146  C  CG1 . VAL A  1  691 ? 87.726  -25.194 -28.483 1.00 87.98  ?  691 VAL A CG1 1 
ATOM   5147  C  CG2 . VAL A  1  691 ? 86.019  -26.051 -30.125 1.00 105.20 ?  691 VAL A CG2 1 
ATOM   5148  N  N   . LYS A  1  692 ? 83.079  -24.786 -29.273 1.00 139.17 ?  692 LYS A N   1 
ATOM   5149  C  CA  . LYS A  1  692 ? 81.860  -24.412 -29.988 1.00 137.15 ?  692 LYS A CA  1 
ATOM   5150  C  C   . LYS A  1  692 ? 81.125  -23.321 -29.211 1.00 137.94 ?  692 LYS A C   1 
ATOM   5151  O  O   . LYS A  1  692 ? 80.714  -22.325 -29.800 1.00 150.18 ?  692 LYS A O   1 
ATOM   5152  C  CB  . LYS A  1  692 ? 80.952  -25.636 -30.181 1.00 137.03 ?  692 LYS A CB  1 
ATOM   5153  C  CG  . LYS A  1  692 ? 79.703  -25.347 -31.006 1.00 152.48 ?  692 LYS A CG  1 
ATOM   5154  C  CD  . LYS A  1  692 ? 78.771  -26.549 -31.056 1.00 167.02 ?  692 LYS A CD  1 
ATOM   5155  C  CE  . LYS A  1  692 ? 77.497  -26.249 -31.810 1.00 166.31 ?  692 LYS A CE  1 
ATOM   5156  N  NZ  . LYS A  1  692 ? 76.572  -27.413 -31.829 1.00 159.38 ?  692 LYS A NZ  1 
ATOM   5157  N  N   . PHE A  1  693 ? 80.970  -23.506 -27.891 1.00 125.29 ?  693 PHE A N   1 
ATOM   5158  C  CA  . PHE A  1  693 ? 80.305  -22.537 -27.020 1.00 120.78 ?  693 PHE A CA  1 
ATOM   5159  C  C   . PHE A  1  693 ? 81.040  -21.189 -27.061 1.00 129.85 ?  693 PHE A C   1 
ATOM   5160  O  O   . PHE A  1  693 ? 80.401  -20.139 -27.075 1.00 140.38 ?  693 PHE A O   1 
ATOM   5161  C  CB  . PHE A  1  693 ? 80.252  -23.083 -25.580 1.00 119.11 ?  693 PHE A CB  1 
ATOM   5162  C  CG  . PHE A  1  693 ? 79.858  -22.082 -24.522 1.00 120.39 ?  693 PHE A CG  1 
ATOM   5163  C  CD1 . PHE A  1  693 ? 78.532  -21.763 -24.307 1.00 114.16 ?  693 PHE A CD1 1 
ATOM   5164  C  CD2 . PHE A  1  693 ? 80.814  -21.484 -23.720 1.00 119.26 ?  693 PHE A CD2 1 
ATOM   5165  C  CE1 . PHE A  1  693 ? 78.171  -20.851 -23.325 1.00 112.33 ?  693 PHE A CE1 1 
ATOM   5166  C  CE2 . PHE A  1  693 ? 80.451  -20.571 -22.742 1.00 122.24 ?  693 PHE A CE2 1 
ATOM   5167  C  CZ  . PHE A  1  693 ? 79.132  -20.256 -22.554 1.00 120.75 ?  693 PHE A CZ  1 
ATOM   5168  N  N   . LEU A  1  694 ? 82.379  -21.227 -27.078 1.00 121.27 ?  694 LEU A N   1 
ATOM   5169  C  CA  . LEU A  1  694 ? 83.222  -20.028 -27.128 1.00 120.91 ?  694 LEU A CA  1 
ATOM   5170  C  C   . LEU A  1  694 ? 83.014  -19.260 -28.435 1.00 128.13 ?  694 LEU A C   1 
ATOM   5171  O  O   . LEU A  1  694 ? 83.015  -18.030 -28.429 1.00 130.76 ?  694 LEU A O   1 
ATOM   5172  C  CB  . LEU A  1  694 ? 84.705  -20.430 -27.018 1.00 122.98 ?  694 LEU A CB  1 
ATOM   5173  C  CG  . LEU A  1  694 ? 85.415  -20.244 -25.681 1.00 117.88 ?  694 LEU A CG  1 
ATOM   5174  C  CD1 . LEU A  1  694 ? 84.720  -20.992 -24.552 1.00 118.44 ?  694 LEU A CD1 1 
ATOM   5175  C  CD2 . LEU A  1  694 ? 86.849  -20.678 -25.801 1.00 95.03  ?  694 LEU A CD2 1 
ATOM   5176  N  N   . GLU A  1  695 ? 82.856  -19.980 -29.555 1.00 133.10 ?  695 GLU A N   1 
ATOM   5177  C  CA  . GLU A  1  695 ? 82.636  -19.359 -30.861 1.00 131.87 ?  695 GLU A CA  1 
ATOM   5178  C  C   . GLU A  1  695 ? 81.253  -18.707 -30.914 1.00 138.34 ?  695 GLU A C   1 
ATOM   5179  O  O   . GLU A  1  695 ? 81.108  -17.619 -31.469 1.00 140.91 ?  695 GLU A O   1 
ATOM   5180  C  CB  . GLU A  1  695 ? 82.761  -20.404 -31.983 1.00 115.83 ?  695 GLU A CB  1 
ATOM   5181  C  CG  . GLU A  1  695 ? 84.195  -20.812 -32.280 1.00 127.66 ?  695 GLU A CG  1 
ATOM   5182  C  CD  . GLU A  1  695 ? 84.351  -22.100 -33.064 1.00 144.82 ?  695 GLU A CD  1 
ATOM   5183  O  OE1 . GLU A  1  695 ? 83.324  -22.753 -33.359 1.00 155.25 ?  695 GLU A OE1 1 
ATOM   5184  O  OE2 . GLU A  1  695 ? 85.508  -22.458 -33.384 1.00 120.87 ?  695 GLU A OE2 1 
ATOM   5185  N  N   . GLU A  1  696 ? 80.242  -19.369 -30.336 1.00 138.52 ?  696 GLU A N   1 
ATOM   5186  C  CA  . GLU A  1  696 ? 78.871  -18.859 -30.316 1.00 148.72 ?  696 GLU A CA  1 
ATOM   5187  C  C   . GLU A  1  696 ? 78.785  -17.541 -29.547 1.00 150.89 ?  696 GLU A C   1 
ATOM   5188  O  O   . GLU A  1  696 ? 78.141  -16.602 -30.013 1.00 158.86 ?  696 GLU A O   1 
ATOM   5189  C  CB  . GLU A  1  696 ? 77.923  -19.884 -29.669 1.00 156.99 ?  696 GLU A CB  1 
ATOM   5190  C  CG  . GLU A  1  696 ? 77.729  -21.153 -30.482 1.00 170.27 ?  696 GLU A CG  1 
ATOM   5191  C  CD  . GLU A  1  696 ? 77.084  -22.302 -29.728 1.00 183.71 ?  696 GLU A CD  1 
ATOM   5192  O  OE1 . GLU A  1  696 ? 76.734  -22.122 -28.538 1.00 179.25 ?  696 GLU A OE1 1 
ATOM   5193  O  OE2 . GLU A  1  696 ? 76.931  -23.388 -30.332 1.00 192.68 ?  696 GLU A OE2 1 
ATOM   5194  N  N   . LYS A  1  697 ? 79.429  -17.470 -28.374 1.00 141.69 ?  697 LYS A N   1 
ATOM   5195  C  CA  . LYS A  1  697 ? 79.406  -16.267 -27.543 1.00 144.34 ?  697 LYS A CA  1 
ATOM   5196  C  C   . LYS A  1  697 ? 80.322  -15.168 -28.094 1.00 149.50 ?  697 LYS A C   1 
ATOM   5197  O  O   . LYS A  1  697 ? 79.933  -14.002 -28.113 1.00 162.72 ?  697 LYS A O   1 
ATOM   5198  C  CB  . LYS A  1  697 ? 79.802  -16.601 -26.091 1.00 132.54 ?  697 LYS A CB  1 
ATOM   5199  C  CG  . LYS A  1  697 ? 78.847  -17.557 -25.376 1.00 128.96 ?  697 LYS A CG  1 
ATOM   5200  C  CD  . LYS A  1  697 ? 77.672  -16.836 -24.724 1.00 141.79 ?  697 LYS A CD  1 
ATOM   5201  C  CE  . LYS A  1  697 ? 76.554  -17.789 -24.383 1.00 136.68 ?  697 LYS A CE  1 
ATOM   5202  N  NZ  . LYS A  1  697 ? 75.394  -17.095 -23.766 1.00 130.47 ?  697 LYS A NZ  1 
ATOM   5203  N  N   . GLY A  1  698 ? 81.553  -15.539 -28.462 1.00 131.09 ?  698 GLY A N   1 
ATOM   5204  C  CA  . GLY A  1  698 ? 82.529  -14.542 -28.946 1.00 120.03 ?  698 GLY A CA  1 
ATOM   5205  C  C   . GLY A  1  698 ? 83.534  -14.169 -27.870 1.00 114.84 ?  698 GLY A C   1 
ATOM   5206  O  O   . GLY A  1  698 ? 83.635  -12.968 -27.553 1.00 109.53 ?  698 GLY A O   1 
ATOM   5207  N  N   . HIS A  1  699 ? 84.254  -15.157 -27.327 1.00 136.75 ?  699 HIS A N   1 
ATOM   5208  C  CA  . HIS A  1  699 ? 85.264  -14.911 -26.260 1.00 132.84 ?  699 HIS A CA  1 
ATOM   5209  C  C   . HIS A  1  699 ? 86.447  -14.131 -26.844 1.00 134.76 ?  699 HIS A C   1 
ATOM   5210  O  O   . HIS A  1  699 ? 86.842  -14.411 -27.996 1.00 141.76 ?  699 HIS A O   1 
ATOM   5211  C  CB  . HIS A  1  699 ? 85.722  -16.245 -25.660 1.00 122.44 ?  699 HIS A CB  1 
ATOM   5212  C  CG  . HIS A  1  699 ? 86.143  -16.188 -24.229 1.00 123.76 ?  699 HIS A CG  1 
ATOM   5213  N  ND1 . HIS A  1  699 ? 85.345  -16.636 -23.198 1.00 130.22 ?  699 HIS A ND1 1 
ATOM   5214  C  CD2 . HIS A  1  699 ? 87.276  -15.759 -23.661 1.00 126.98 ?  699 HIS A CD2 1 
ATOM   5215  C  CE1 . HIS A  1  699 ? 85.983  -16.470 -22.048 1.00 137.32 ?  699 HIS A CE1 1 
ATOM   5216  N  NE2 . HIS A  1  699 ? 87.157  -15.937 -22.306 1.00 138.28 ?  699 HIS A NE2 1 
ATOM   5217  N  N   . PRO A  1  700 ? 87.049  -13.169 -26.108 1.00 123.03 ?  700 PRO A N   1 
ATOM   5218  C  CA  . PRO A  1  700 ? 88.216  -12.438 -26.597 1.00 124.19 ?  700 PRO A CA  1 
ATOM   5219  C  C   . PRO A  1  700 ? 89.376  -13.402 -26.873 1.00 114.55 ?  700 PRO A C   1 
ATOM   5220  O  O   . PRO A  1  700 ? 90.124  -13.156 -27.801 1.00 119.79 ?  700 PRO A O   1 
ATOM   5221  C  CB  . PRO A  1  700 ? 88.592  -11.504 -25.438 1.00 127.60 ?  700 PRO A CB  1 
ATOM   5222  C  CG  . PRO A  1  700 ? 87.958  -12.146 -24.229 1.00 117.44 ?  700 PRO A CG  1 
ATOM   5223  C  CD  . PRO A  1  700 ? 86.670  -12.732 -24.765 1.00 122.54 ?  700 PRO A CD  1 
ATOM   5224  N  N   . ALA A  1  701 ? 89.500  -14.462 -26.068 1.00 124.39 ?  701 ALA A N   1 
ATOM   5225  C  CA  . ALA A  1  701 ? 90.639  -15.356 -26.258 1.00 124.44 ?  701 ALA A CA  1 
ATOM   5226  C  C   . ALA A  1  701 ? 90.756  -15.833 -27.711 1.00 120.42 ?  701 ALA A C   1 
ATOM   5227  O  O   . ALA A  1  701 ? 91.869  -16.025 -28.196 1.00 118.33 ?  701 ALA A O   1 
ATOM   5228  C  CB  . ALA A  1  701 ? 90.521  -16.555 -25.327 1.00 104.51 ?  701 ALA A CB  1 
ATOM   5229  N  N   . LEU A  1  702 ? 89.626  -16.016 -28.407 1.00 116.46 ?  702 LEU A N   1 
ATOM   5230  C  CA  . LEU A  1  702 ? 89.650  -16.467 -29.798 1.00 114.04 ?  702 LEU A CA  1 
ATOM   5231  C  C   . LEU A  1  702 ? 90.254  -15.400 -30.717 1.00 115.71 ?  702 LEU A C   1 
ATOM   5232  O  O   . LEU A  1  702 ? 90.968  -15.738 -31.661 1.00 110.11 ?  702 LEU A O   1 
ATOM   5233  C  CB  . LEU A  1  702 ? 88.235  -16.824 -30.284 1.00 114.19 ?  702 LEU A CB  1 
ATOM   5234  C  CG  . LEU A  1  702 ? 87.463  -17.917 -29.527 1.00 110.26 ?  702 LEU A CG  1 
ATOM   5235  C  CD1 . LEU A  1  702 ? 86.172  -18.244 -30.257 1.00 109.07 ?  702 LEU A CD1 1 
ATOM   5236  C  CD2 . LEU A  1  702 ? 88.296  -19.185 -29.342 1.00 94.61  ?  702 LEU A CD2 1 
ATOM   5237  N  N   . LYS A  1  703 ? 89.965  -14.120 -30.449 1.00 125.83 ?  703 LYS A N   1 
ATOM   5238  C  CA  . LYS A  1  703 ? 90.494  -13.016 -31.253 1.00 121.23 ?  703 LYS A CA  1 
ATOM   5239  C  C   . LYS A  1  703 ? 91.822  -12.452 -30.693 1.00 114.59 ?  703 LYS A C   1 
ATOM   5240  O  O   . LYS A  1  703 ? 92.350  -11.486 -31.243 1.00 114.17 ?  703 LYS A O   1 
ATOM   5241  C  CB  . LYS A  1  703 ? 89.438  -11.906 -31.378 1.00 126.86 ?  703 LYS A CB  1 
ATOM   5242  C  CG  . LYS A  1  703 ? 88.190  -12.353 -32.134 1.00 125.21 ?  703 LYS A CG  1 
ATOM   5243  C  CD  . LYS A  1  703 ? 87.201  -11.214 -32.328 1.00 160.15 ?  703 LYS A CD  1 
ATOM   5244  C  CE  . LYS A  1  703 ? 86.064  -11.594 -33.245 1.00 161.67 ?  703 LYS A CE  1 
ATOM   5245  N  NZ  . LYS A  1  703 ? 85.066  -10.497 -33.377 1.00 156.29 ?  703 LYS A NZ  1 
ATOM   5246  N  N   . MET A  1  704 ? 92.365  -13.056 -29.621 1.00 116.23 ?  704 MET A N   1 
ATOM   5247  C  CA  . MET A  1  704 ? 93.629  -12.623 -29.023 1.00 109.87 ?  704 MET A CA  1 
ATOM   5248  C  C   . MET A  1  704 ? 94.802  -13.230 -29.805 1.00 111.73 ?  704 MET A C   1 
ATOM   5249  O  O   . MET A  1  704 ? 94.599  -14.105 -30.650 1.00 112.04 ?  704 MET A O   1 
ATOM   5250  C  CB  . MET A  1  704 ? 93.708  -13.088 -27.551 1.00 103.59 ?  704 MET A CB  1 
ATOM   5251  C  CG  . MET A  1  704 ? 93.217  -12.066 -26.546 1.00 109.46 ?  704 MET A CG  1 
ATOM   5252  S  SD  . MET A  1  704 ? 93.118  -12.764 -24.879 1.00 116.57 ?  704 MET A SD  1 
ATOM   5253  C  CE  . MET A  1  704 ? 93.576  -11.347 -23.906 1.00 118.94 ?  704 MET A CE  1 
ATOM   5254  N  N   . ASP A  1  705 ? 96.031  -12.780 -29.520 1.00 118.22 ?  705 ASP A N   1 
ATOM   5255  C  CA  . ASP A  1  705 ? 97.216  -13.309 -30.194 1.00 112.84 ?  705 ASP A CA  1 
ATOM   5256  C  C   . ASP A  1  705 ? 97.449  -14.764 -29.744 1.00 111.72 ?  705 ASP A C   1 
ATOM   5257  O  O   . ASP A  1  705 ? 97.000  -15.130 -28.655 1.00 115.40 ?  705 ASP A O   1 
ATOM   5258  C  CB  . ASP A  1  705 ? 98.447  -12.454 -29.854 1.00 112.48 ?  705 ASP A CB  1 
ATOM   5259  C  CG  . ASP A  1  705 ? 98.252  -10.979 -30.120 1.00 135.90 ?  705 ASP A CG  1 
ATOM   5260  O  OD1 . ASP A  1  705 ? 98.413  -10.560 -31.288 1.00 129.98 ?  705 ASP A OD1 1 
ATOM   5261  O  OD2 . ASP A  1  705 ? 97.935  -10.241 -29.160 1.00 149.54 ?  705 ASP A OD2 1 
ATOM   5262  N  N   . PRO A  1  706 ? 98.145  -15.621 -30.525 1.00 106.30 ?  706 PRO A N   1 
ATOM   5263  C  CA  . PRO A  1  706 ? 98.363  -17.004 -30.060 1.00 103.38 ?  706 PRO A CA  1 
ATOM   5264  C  C   . PRO A  1  706 ? 99.050  -17.054 -28.693 1.00 110.90 ?  706 PRO A C   1 
ATOM   5265  O  O   . PRO A  1  706 ? 100.109 -16.452 -28.517 1.00 111.90 ?  706 PRO A O   1 
ATOM   5266  C  CB  . PRO A  1  706 ? 99.231  -17.625 -31.162 1.00 93.35  ?  706 PRO A CB  1 
ATOM   5267  C  CG  . PRO A  1  706 ? 99.010  -16.782 -32.354 1.00 95.98  ?  706 PRO A CG  1 
ATOM   5268  C  CD  . PRO A  1  706 ? 98.762  -15.397 -31.847 1.00 106.31 ?  706 PRO A CD  1 
ATOM   5269  N  N   . ILE A  1  707 ? 98.433  -17.745 -27.720 1.00 105.39 ?  707 ILE A N   1 
ATOM   5270  C  CA  . ILE A  1  707 ? 98.981  -17.855 -26.364 1.00 100.30 ?  707 ILE A CA  1 
ATOM   5271  C  C   . ILE A  1  707 ? 100.418 -18.406 -26.350 1.00 97.60  ?  707 ILE A C   1 
ATOM   5272  O  O   . ILE A  1  707 ? 101.259 -17.890 -25.615 1.00 98.86  ?  707 ILE A O   1 
ATOM   5273  C  CB  . ILE A  1  707 ? 98.033  -18.663 -25.435 1.00 99.54  ?  707 ILE A CB  1 
ATOM   5274  C  CG1 . ILE A  1  707 ? 98.512  -18.567 -23.966 1.00 93.28  ?  707 ILE A CG1 1 
ATOM   5275  C  CG2 . ILE A  1  707 ? 97.903  -20.124 -25.897 1.00 88.47  ?  707 ILE A CG2 1 
ATOM   5276  C  CD1 . ILE A  1  707 ? 97.460  -18.841 -22.927 1.00 95.13  ?  707 ILE A CD1 1 
ATOM   5277  N  N   . MET A  1  708 ? 100.703 -19.435 -27.164 1.00 96.23  ?  708 MET A N   1 
ATOM   5278  C  CA  . MET A  1  708 ? 102.037 -20.026 -27.239 1.00 90.55  ?  708 MET A CA  1 
ATOM   5279  C  C   . MET A  1  708 ? 102.681 -19.688 -28.579 1.00 91.15  ?  708 MET A C   1 
ATOM   5280  O  O   . MET A  1  708 ? 102.233 -20.171 -29.615 1.00 90.41  ?  708 MET A O   1 
ATOM   5281  C  CB  . MET A  1  708 ? 101.954 -21.554 -27.077 1.00 97.18  ?  708 MET A CB  1 
ATOM   5282  C  CG  . MET A  1  708 ? 102.254 -22.042 -25.677 1.00 88.44  ?  708 MET A CG  1 
ATOM   5283  S  SD  . MET A  1  708 ? 102.464 -23.831 -25.601 1.00 86.67  ?  708 MET A SD  1 
ATOM   5284  C  CE  . MET A  1  708 ? 104.157 -23.979 -26.104 1.00 89.10  ?  708 MET A CE  1 
ATOM   5285  N  N   . GLU B  2  3   ? 133.504 38.228  33.673  1.00 96.28  ?  3   GLU B N   1 
ATOM   5286  C  CA  . GLU B  2  3   ? 132.095 38.050  33.326  1.00 100.28 ?  3   GLU B CA  1 
ATOM   5287  C  C   . GLU B  2  3   ? 131.713 36.570  33.401  1.00 106.01 ?  3   GLU B C   1 
ATOM   5288  O  O   . GLU B  2  3   ? 132.515 35.708  33.039  1.00 114.26 ?  3   GLU B O   1 
ATOM   5289  C  CB  . GLU B  2  3   ? 131.819 38.606  31.914  1.00 106.58 ?  3   GLU B CB  1 
ATOM   5290  C  CG  . GLU B  2  3   ? 130.340 38.762  31.592  1.00 114.71 ?  3   GLU B CG  1 
ATOM   5291  C  CD  . GLU B  2  3   ? 130.034 39.387  30.243  1.00 120.29 ?  3   GLU B CD  1 
ATOM   5292  O  OE1 . GLU B  2  3   ? 130.982 39.838  29.559  1.00 117.19 ?  3   GLU B OE1 1 
ATOM   5293  O  OE2 . GLU B  2  3   ? 128.839 39.425  29.870  1.00 120.31 ?  3   GLU B OE2 1 
ATOM   5294  N  N   . LYS B  2  4   ? 130.493 36.273  33.875  1.00 90.11  ?  4   LYS B N   1 
ATOM   5295  C  CA  . LYS B  2  4   ? 130.018 34.896  33.984  1.00 79.43  ?  4   LYS B CA  1 
ATOM   5296  C  C   . LYS B  2  4   ? 129.631 34.364  32.594  1.00 75.73  ?  4   LYS B C   1 
ATOM   5297  O  O   . LYS B  2  4   ? 129.222 35.147  31.734  1.00 79.41  ?  4   LYS B O   1 
ATOM   5298  C  CB  . LYS B  2  4   ? 128.812 34.835  34.941  1.00 74.36  ?  4   LYS B CB  1 
ATOM   5299  C  CG  . LYS B  2  4   ? 128.513 33.434  35.473  1.00 97.04  ?  4   LYS B CG  1 
ATOM   5300  C  CD  . LYS B  2  4   ? 127.658 33.447  36.749  1.00 94.73  ?  4   LYS B CD  1 
ATOM   5301  C  CE  . LYS B  2  4   ? 126.221 33.853  36.503  1.00 88.70  ?  4   LYS B CE  1 
ATOM   5302  N  NZ  . LYS B  2  4   ? 125.311 33.328  37.556  1.00 78.93  ?  4   LYS B NZ  1 
ATOM   5303  N  N   . ALA B  2  5   ? 129.765 33.046  32.369  1.00 61.74  ?  5   ALA B N   1 
ATOM   5304  C  CA  . ALA B  2  5   ? 129.415 32.446  31.080  1.00 53.87  ?  5   ALA B CA  1 
ATOM   5305  C  C   . ALA B  2  5   ? 127.915 32.577  30.833  1.00 56.94  ?  5   ALA B C   1 
ATOM   5306  O  O   . ALA B  2  5   ? 127.132 32.452  31.769  1.00 65.68  ?  5   ALA B O   1 
ATOM   5307  C  CB  . ALA B  2  5   ? 129.818 30.985  31.057  1.00 56.36  ?  5   ALA B CB  1 
ATOM   5308  N  N   . LYS B  2  6   ? 127.510 32.792  29.578  1.00 49.09  ?  6   LYS B N   1 
ATOM   5309  C  CA  . LYS B  2  6   ? 126.068 33.002  29.270  1.00 47.70  ?  6   LYS B CA  1 
ATOM   5310  C  C   . LYS B  2  6   ? 125.356 31.652  29.145  1.00 57.71  ?  6   LYS B C   1 
ATOM   5311  O  O   . LYS B  2  6   ? 124.146 31.600  29.439  1.00 63.97  ?  6   LYS B O   1 
ATOM   5312  C  CB  . LYS B  2  6   ? 125.917 33.810  27.978  1.00 56.40  ?  6   LYS B CB  1 
ATOM   5313  C  CG  . LYS B  2  6   ? 126.463 35.231  28.032  1.00 66.92  ?  6   LYS B CG  1 
ATOM   5314  C  CD  . LYS B  2  6   ? 126.004 36.095  26.878  1.00 57.17  ?  6   LYS B CD  1 
ATOM   5315  C  CE  . LYS B  2  6   ? 126.269 37.569  27.104  1.00 68.83  ?  6   LYS B CE  1 
ATOM   5316  N  NZ  . LYS B  2  6   ? 126.115 38.356  25.858  1.00 105.60 ?  6   LYS B NZ  1 
ATOM   5317  N  N   . SER B  2  7   ? 126.074 30.607  28.731  1.00 58.90  ?  7   SER B N   1 
ATOM   5318  C  CA  . SER B  2  7   ? 125.485 29.284  28.533  1.00 51.29  ?  7   SER B CA  1 
ATOM   5319  C  C   . SER B  2  7   ? 126.560 28.199  28.561  1.00 50.48  ?  7   SER B C   1 
ATOM   5320  O  O   . SER B  2  7   ? 127.748 28.497  28.462  1.00 53.11  ?  7   SER B O   1 
ATOM   5321  C  CB  . SER B  2  7   ? 124.774 29.241  27.183  1.00 54.11  ?  7   SER B CB  1 
ATOM   5322  O  OG  . SER B  2  7   ? 124.308 27.940  26.865  1.00 55.57  ?  7   SER B OG  1 
ATOM   5323  N  N   . ILE B  2  8   ? 126.140 26.937  28.685  1.00 57.14  ?  8   ILE B N   1 
ATOM   5324  C  CA  . ILE B  2  8   ? 127.061 25.796  28.673  1.00 50.04  ?  8   ILE B CA  1 
ATOM   5325  C  C   . ILE B  2  8   ? 127.098 25.162  27.269  1.00 52.83  ?  8   ILE B C   1 
ATOM   5326  O  O   . ILE B  2  8   ? 128.102 24.552  26.910  1.00 63.04  ?  8   ILE B O   1 
ATOM   5327  C  CB  . ILE B  2  8   ? 126.713 24.753  29.770  1.00 42.89  ?  8   ILE B CB  1 
ATOM   5328  C  CG1 . ILE B  2  8   ? 125.329 24.109  29.539  1.00 56.05  ?  8   ILE B CG1 1 
ATOM   5329  C  CG2 . ILE B  2  8   ? 126.777 25.404  31.137  1.00 49.52  ?  8   ILE B CG2 1 
ATOM   5330  C  CD1 . ILE B  2  8   ? 125.135 22.772  30.216  1.00 55.74  ?  8   ILE B CD1 1 
ATOM   5331  N  N   . ASP B  2  9   ? 126.013 25.314  26.477  1.00 50.37  ?  9   ASP B N   1 
ATOM   5332  C  CA  . ASP B  2  9   ? 125.900 24.754  25.128  1.00 53.71  ?  9   ASP B CA  1 
ATOM   5333  C  C   . ASP B  2  9   ? 126.824 25.466  24.139  1.00 57.78  ?  9   ASP B C   1 
ATOM   5334  O  O   . ASP B  2  9   ? 126.784 26.689  24.037  1.00 60.01  ?  9   ASP B O   1 
ATOM   5335  C  CB  . ASP B  2  9   ? 124.437 24.838  24.660  1.00 55.64  ?  9   ASP B CB  1 
ATOM   5336  C  CG  . ASP B  2  9   ? 124.173 24.287  23.276  1.00 67.38  ?  9   ASP B CG  1 
ATOM   5337  O  OD1 . ASP B  2  9   ? 124.931 23.391  22.836  1.00 80.35  ?  9   ASP B OD1 1 
ATOM   5338  O  OD2 . ASP B  2  9   ? 123.207 24.744  22.634  1.00 76.98  ?  9   ASP B OD2 1 
ATOM   5339  N  N   . GLN B  2  10  ? 127.645 24.701  23.397  1.00 62.95  ?  10  GLN B N   1 
ATOM   5340  C  CA  . GLN B  2  10  ? 128.580 25.285  22.436  1.00 52.98  ?  10  GLN B CA  1 
ATOM   5341  C  C   . GLN B  2  10  ? 127.889 25.943  21.250  1.00 58.75  ?  10  GLN B C   1 
ATOM   5342  O  O   . GLN B  2  10  ? 128.343 26.991  20.797  1.00 67.07  ?  10  GLN B O   1 
ATOM   5343  C  CB  . GLN B  2  10  ? 129.591 24.236  21.943  1.00 58.37  ?  10  GLN B CB  1 
ATOM   5344  C  CG  . GLN B  2  10  ? 130.946 24.827  21.532  1.00 60.66  ?  10  GLN B CG  1 
ATOM   5345  C  CD  . GLN B  2  10  ? 131.630 25.544  22.681  1.00 79.12  ?  10  GLN B CD  1 
ATOM   5346  O  OE1 . GLN B  2  10  ? 131.512 25.155  23.855  1.00 71.67  ?  10  GLN B OE1 1 
ATOM   5347  N  NE2 . GLN B  2  10  ? 132.358 26.616  22.373  1.00 87.36  ?  10  GLN B NE2 1 
ATOM   5348  N  N   . ALA B  2  11  ? 126.802 25.352  20.740  1.00 58.40  ?  11  ALA B N   1 
ATOM   5349  C  CA  . ALA B  2  11  ? 126.071 25.942  19.613  1.00 56.70  ?  11  ALA B CA  1 
ATOM   5350  C  C   . ALA B  2  11  ? 125.532 27.328  20.007  1.00 51.99  ?  11  ALA B C   1 
ATOM   5351  O  O   . ALA B  2  11  ? 125.612 28.269  19.221  1.00 53.48  ?  11  ALA B O   1 
ATOM   5352  C  CB  . ALA B  2  11  ? 124.922 25.032  19.206  1.00 49.20  ?  11  ALA B CB  1 
ATOM   5353  N  N   . THR B  2  12  ? 125.011 27.445  21.241  1.00 47.65  ?  12  THR B N   1 
ATOM   5354  C  CA  . THR B  2  12  ? 124.472 28.697  21.784  1.00 45.04  ?  12  THR B CA  1 
ATOM   5355  C  C   . THR B  2  12  ? 125.578 29.750  21.888  1.00 54.32  ?  12  THR B C   1 
ATOM   5356  O  O   . THR B  2  12  ? 125.380 30.900  21.504  1.00 59.30  ?  12  THR B O   1 
ATOM   5357  C  CB  . THR B  2  12  ? 123.836 28.423  23.158  1.00 49.10  ?  12  THR B CB  1 
ATOM   5358  O  OG1 . THR B  2  12  ? 122.724 27.545  22.981  1.00 64.90  ?  12  THR B OG1 1 
ATOM   5359  C  CG2 . THR B  2  12  ? 123.392 29.686  23.876  1.00 51.85  ?  12  THR B CG2 1 
ATOM   5360  N  N   . LEU B  2  13  ? 126.745 29.358  22.402  1.00 53.94  ?  13  LEU B N   1 
ATOM   5361  C  CA  . LEU B  2  13  ? 127.869 30.277  22.553  1.00 48.35  ?  13  LEU B CA  1 
ATOM   5362  C  C   . LEU B  2  13  ? 128.386 30.741  21.189  1.00 55.32  ?  13  LEU B C   1 
ATOM   5363  O  O   . LEU B  2  13  ? 128.784 31.897  21.049  1.00 57.27  ?  13  LEU B O   1 
ATOM   5364  C  CB  . LEU B  2  13  ? 128.992 29.613  23.374  1.00 45.97  ?  13  LEU B CB  1 
ATOM   5365  C  CG  . LEU B  2  13  ? 128.637 29.273  24.836  1.00 45.33  ?  13  LEU B CG  1 
ATOM   5366  C  CD1 . LEU B  2  13  ? 129.568 28.226  25.396  1.00 51.47  ?  13  LEU B CD1 1 
ATOM   5367  C  CD2 . LEU B  2  13  ? 128.669 30.508  25.721  1.00 58.90  ?  13  LEU B CD2 1 
ATOM   5368  N  N   . GLN B  2  14  ? 128.366 29.855  20.181  1.00 52.18  ?  14  GLN B N   1 
ATOM   5369  C  CA  . GLN B  2  14  ? 128.821 30.211  18.841  1.00 50.28  ?  14  GLN B CA  1 
ATOM   5370  C  C   . GLN B  2  14  ? 127.939 31.313  18.256  1.00 47.58  ?  14  GLN B C   1 
ATOM   5371  O  O   . GLN B  2  14  ? 128.450 32.338  17.810  1.00 50.31  ?  14  GLN B O   1 
ATOM   5372  C  CB  . GLN B  2  14  ? 128.805 28.981  17.907  1.00 47.04  ?  14  GLN B CB  1 
ATOM   5373  C  CG  . GLN B  2  14  ? 130.001 28.056  18.081  1.00 51.19  ?  14  GLN B CG  1 
ATOM   5374  C  CD  . GLN B  2  14  ? 129.957 26.865  17.152  1.00 62.18  ?  14  GLN B CD  1 
ATOM   5375  O  OE1 . GLN B  2  14  ? 129.301 26.879  16.099  1.00 60.12  ?  14  GLN B OE1 1 
ATOM   5376  N  NE2 . GLN B  2  14  ? 130.666 25.802  17.525  1.00 58.24  ?  14  GLN B NE2 1 
ATOM   5377  N  N   . LEU B  2  15  ? 126.618 31.110  18.267  1.00 54.92  ?  15  LEU B N   1 
ATOM   5378  C  CA  . LEU B  2  15  ? 125.688 32.093  17.722  1.00 54.82  ?  15  LEU B CA  1 
ATOM   5379  C  C   . LEU B  2  15  ? 125.634 33.370  18.543  1.00 58.90  ?  15  LEU B C   1 
ATOM   5380  O  O   . LEU B  2  15  ? 125.313 34.413  17.984  1.00 68.02  ?  15  LEU B O   1 
ATOM   5381  C  CB  . LEU B  2  15  ? 124.290 31.491  17.555  1.00 43.57  ?  15  LEU B CB  1 
ATOM   5382  C  CG  . LEU B  2  15  ? 124.148 30.490  16.401  1.00 43.61  ?  15  LEU B CG  1 
ATOM   5383  C  CD1 . LEU B  2  15  ? 122.967 29.600  16.620  1.00 44.93  ?  15  LEU B CD1 1 
ATOM   5384  C  CD2 . LEU B  2  15  ? 124.007 31.200  15.063  1.00 44.38  ?  15  LEU B CD2 1 
ATOM   5385  N  N   . LEU B  2  16  ? 125.970 33.320  19.843  1.00 56.98  ?  16  LEU B N   1 
ATOM   5386  C  CA  . LEU B  2  16  ? 126.003 34.537  20.653  1.00 45.22  ?  16  LEU B CA  1 
ATOM   5387  C  C   . LEU B  2  16  ? 127.122 35.455  20.128  1.00 56.39  ?  16  LEU B C   1 
ATOM   5388  O  O   . LEU B  2  16  ? 126.963 36.674  20.122  1.00 54.74  ?  16  LEU B O   1 
ATOM   5389  C  CB  . LEU B  2  16  ? 126.225 34.207  22.135  1.00 44.91  ?  16  LEU B CB  1 
ATOM   5390  C  CG  . LEU B  2  16  ? 124.970 33.868  22.935  1.00 43.42  ?  16  LEU B CG  1 
ATOM   5391  C  CD1 . LEU B  2  16  ? 125.322 33.141  24.226  1.00 58.06  ?  16  LEU B CD1 1 
ATOM   5392  C  CD2 . LEU B  2  16  ? 124.168 35.124  23.251  1.00 51.43  ?  16  LEU B CD2 1 
ATOM   5393  N  N   . ASP B  2  17  ? 128.238 34.868  19.651  1.00 55.04  ?  17  ASP B N   1 
ATOM   5394  C  CA  . ASP B  2  17  ? 129.328 35.640  19.069  1.00 55.10  ?  17  ASP B CA  1 
ATOM   5395  C  C   . ASP B  2  17  ? 128.815 36.256  17.773  1.00 52.04  ?  17  ASP B C   1 
ATOM   5396  O  O   . ASP B  2  17  ? 129.024 37.441  17.548  1.00 67.59  ?  17  ASP B O   1 
ATOM   5397  C  CB  . ASP B  2  17  ? 130.554 34.753  18.782  1.00 67.60  ?  17  ASP B CB  1 
ATOM   5398  C  CG  . ASP B  2  17  ? 131.285 34.286  20.027  1.00 74.43  ?  17  ASP B CG  1 
ATOM   5399  O  OD1 . ASP B  2  17  ? 131.720 35.151  20.822  1.00 81.87  ?  17  ASP B OD1 1 
ATOM   5400  O  OD2 . ASP B  2  17  ? 131.430 33.055  20.204  1.00 85.87  ?  17  ASP B OD2 1 
ATOM   5401  N  N   . LYS B  2  18  ? 128.115 35.469  16.934  1.00 59.91  ?  18  LYS B N   1 
ATOM   5402  C  CA  . LYS B  2  18  ? 127.564 35.976  15.678  1.00 56.20  ?  18  LYS B CA  1 
ATOM   5403  C  C   . LYS B  2  18  ? 126.594 37.118  15.950  1.00 56.56  ?  18  LYS B C   1 
ATOM   5404  O  O   . LYS B  2  18  ? 126.612 38.110  15.235  1.00 61.09  ?  18  LYS B O   1 
ATOM   5405  C  CB  . LYS B  2  18  ? 126.850 34.868  14.891  1.00 48.67  ?  18  LYS B CB  1 
ATOM   5406  C  CG  . LYS B  2  18  ? 126.263 35.363  13.568  1.00 51.89  ?  18  LYS B CG  1 
ATOM   5407  C  CD  . LYS B  2  18  ? 125.688 34.242  12.718  1.00 49.53  ?  18  LYS B CD  1 
ATOM   5408  C  CE  . LYS B  2  18  ? 125.444 34.650  11.280  1.00 56.05  ?  18  LYS B CE  1 
ATOM   5409  N  NZ  . LYS B  2  18  ? 124.308 35.601  11.128  1.00 51.28  ?  18  LYS B NZ  1 
ATOM   5410  N  N   . ALA B  2  19  ? 125.762 36.997  16.992  1.00 56.45  ?  19  ALA B N   1 
ATOM   5411  C  CA  . ALA B  2  19  ? 124.804 38.042  17.350  1.00 55.56  ?  19  ALA B CA  1 
ATOM   5412  C  C   . ALA B  2  19  ? 125.525 39.362  17.628  1.00 55.58  ?  19  ALA B C   1 
ATOM   5413  O  O   . ALA B  2  19  ? 125.039 40.421  17.239  1.00 60.24  ?  19  ALA B O   1 
ATOM   5414  C  CB  . ALA B  2  19  ? 124.000 37.623  18.572  1.00 47.52  ?  19  ALA B CB  1 
ATOM   5415  N  N   . LYS B  2  20  ? 126.691 39.288  18.289  1.00 54.67  ?  20  LYS B N   1 
ATOM   5416  C  CA  . LYS B  2  20  ? 127.504 40.456  18.604  1.00 56.61  ?  20  LYS B CA  1 
ATOM   5417  C  C   . LYS B  2  20  ? 128.045 41.059  17.312  1.00 52.08  ?  20  LYS B C   1 
ATOM   5418  O  O   . LYS B  2  20  ? 127.934 42.267  17.115  1.00 58.95  ?  20  LYS B O   1 
ATOM   5419  C  CB  . LYS B  2  20  ? 128.662 40.058  19.531  1.00 51.16  ?  20  LYS B CB  1 
ATOM   5420  C  CG  . LYS B  2  20  ? 129.415 41.230  20.144  1.00 52.50  ?  20  LYS B CG  1 
ATOM   5421  C  CD  . LYS B  2  20  ? 130.810 40.805  20.595  1.00 79.38  ?  20  LYS B CD  1 
ATOM   5422  C  CE  . LYS B  2  20  ? 131.373 41.664  21.700  1.00 72.31  ?  20  LYS B CE  1 
ATOM   5423  N  NZ  . LYS B  2  20  ? 132.815 41.379  21.931  1.00 82.69  ?  20  LYS B NZ  1 
ATOM   5424  N  N   . GLN B  2  21  ? 128.600 40.219  16.421  1.00 56.32  ?  21  GLN B N   1 
ATOM   5425  C  CA  . GLN B  2  21  ? 129.150 40.662  15.138  1.00 61.04  ?  21  GLN B CA  1 
ATOM   5426  C  C   . GLN B  2  21  ? 128.064 41.277  14.266  1.00 55.63  ?  21  GLN B C   1 
ATOM   5427  O  O   . GLN B  2  21  ? 128.300 42.298  13.626  1.00 66.91  ?  21  GLN B O   1 
ATOM   5428  C  CB  . GLN B  2  21  ? 129.810 39.490  14.404  1.00 68.51  ?  21  GLN B CB  1 
ATOM   5429  C  CG  . GLN B  2  21  ? 131.111 39.023  15.053  1.00 93.80  ?  21  GLN B CG  1 
ATOM   5430  C  CD  . GLN B  2  21  ? 131.326 37.532  14.913  1.00 116.60 ?  21  GLN B CD  1 
ATOM   5431  O  OE1 . GLN B  2  21  ? 130.794 36.878  14.001  1.00 116.71 ?  21  GLN B OE1 1 
ATOM   5432  N  NE2 . GLN B  2  21  ? 132.119 36.957  15.818  1.00 104.00 ?  21  GLN B NE2 1 
ATOM   5433  N  N   . ASP B  2  22  ? 126.877 40.666  14.237  1.00 61.10  ?  22  ASP B N   1 
ATOM   5434  C  CA  . ASP B  2  22  ? 125.751 41.194  13.467  1.00 62.50  ?  22  ASP B CA  1 
ATOM   5435  C  C   . ASP B  2  22  ? 125.198 42.488  14.100  1.00 60.95  ?  22  ASP B C   1 
ATOM   5436  O  O   . ASP B  2  22  ? 124.471 43.224  13.440  1.00 72.52  ?  22  ASP B O   1 
ATOM   5437  C  CB  . ASP B  2  22  ? 124.621 40.149  13.369  1.00 64.80  ?  22  ASP B CB  1 
ATOM   5438  C  CG  . ASP B  2  22  ? 124.934 38.951  12.488  1.00 69.82  ?  22  ASP B CG  1 
ATOM   5439  O  OD1 . ASP B  2  22  ? 126.014 38.942  11.852  1.00 67.48  ?  22  ASP B OD1 1 
ATOM   5440  O  OD2 . ASP B  2  22  ? 124.099 38.020  12.435  1.00 56.40  ?  22  ASP B OD2 1 
ATOM   5441  N  N   . GLY B  2  23  ? 125.535 42.746  15.363  1.00 58.81  ?  23  GLY B N   1 
ATOM   5442  C  CA  . GLY B  2  23  ? 125.077 43.928  16.074  1.00 52.75  ?  23  GLY B CA  1 
ATOM   5443  C  C   . GLY B  2  23  ? 123.618 43.834  16.467  1.00 60.48  ?  23  GLY B C   1 
ATOM   5444  O  O   . GLY B  2  23  ? 122.872 44.799  16.284  1.00 71.05  ?  23  GLY B O   1 
ATOM   5445  N  N   . VAL B  2  24  ? 123.197 42.673  17.014  1.00 56.43  ?  24  VAL B N   1 
ATOM   5446  C  CA  . VAL B  2  24  ? 121.805 42.460  17.426  1.00 56.95  ?  24  VAL B CA  1 
ATOM   5447  C  C   . VAL B  2  24  ? 121.700 42.210  18.938  1.00 67.67  ?  24  VAL B C   1 
ATOM   5448  O  O   . VAL B  2  24  ? 122.639 41.708  19.559  1.00 74.15  ?  24  VAL B O   1 
ATOM   5449  C  CB  . VAL B  2  24  ? 121.104 41.351  16.602  1.00 49.25  ?  24  VAL B CB  1 
ATOM   5450  C  CG1 . VAL B  2  24  ? 121.073 41.703  15.122  1.00 55.70  ?  24  VAL B CG1 1 
ATOM   5451  C  CG2 . VAL B  2  24  ? 121.752 39.994  16.816  1.00 49.36  ?  24  VAL B CG2 1 
ATOM   5452  N  N   . GLU B  2  25  ? 120.552 42.567  19.527  1.00 52.68  ?  25  GLU B N   1 
ATOM   5453  C  CA  . GLU B  2  25  ? 120.328 42.409  20.960  1.00 48.32  ?  25  GLU B CA  1 
ATOM   5454  C  C   . GLU B  2  25  ? 119.767 41.037  21.292  1.00 57.86  ?  25  GLU B C   1 
ATOM   5455  O  O   . GLU B  2  25  ? 118.973 40.492  20.527  1.00 64.17  ?  25  GLU B O   1 
ATOM   5456  C  CB  . GLU B  2  25  ? 119.341 43.479  21.468  1.00 55.92  ?  25  GLU B CB  1 
ATOM   5457  C  CG  . GLU B  2  25  ? 119.983 44.683  22.138  1.00 84.72  ?  25  GLU B CG  1 
ATOM   5458  C  CD  . GLU B  2  25  ? 119.003 45.562  22.892  1.00 108.29 ?  25  GLU B CD  1 
ATOM   5459  O  OE1 . GLU B  2  25  ? 117.797 45.539  22.550  1.00 105.75 ?  25  GLU B OE1 1 
ATOM   5460  O  OE2 . GLU B  2  25  ? 119.441 46.273  23.826  1.00 106.27 ?  25  GLU B OE2 1 
ATOM   5461  N  N   . THR B  2  26  ? 120.168 40.487  22.450  1.00 62.01  ?  26  THR B N   1 
ATOM   5462  C  CA  . THR B  2  26  ? 119.703 39.187  22.935  1.00 50.59  ?  26  THR B CA  1 
ATOM   5463  C  C   . THR B  2  26  ? 119.217 39.331  24.376  1.00 52.04  ?  26  THR B C   1 
ATOM   5464  O  O   . THR B  2  26  ? 119.500 40.338  25.021  1.00 59.77  ?  26  THR B O   1 
ATOM   5465  C  CB  . THR B  2  26  ? 120.822 38.136  22.842  1.00 48.14  ?  26  THR B CB  1 
ATOM   5466  O  OG1 . THR B  2  26  ? 121.845 38.441  23.794  1.00 62.45  ?  26  THR B OG1 1 
ATOM   5467  C  CG2 . THR B  2  26  ? 121.408 38.022  21.442  1.00 66.00  ?  26  THR B CG2 1 
ATOM   5468  N  N   . VAL B  2  27  ? 118.491 38.324  24.887  1.00 52.50  ?  27  VAL B N   1 
ATOM   5469  C  CA  . VAL B  2  27  ? 117.978 38.319  26.258  1.00 49.41  ?  27  VAL B CA  1 
ATOM   5470  C  C   . VAL B  2  27  ? 119.114 38.574  27.274  1.00 55.92  ?  27  VAL B C   1 
ATOM   5471  O  O   . VAL B  2  27  ? 118.885 39.215  28.300  1.00 62.78  ?  27  VAL B O   1 
ATOM   5472  C  CB  . VAL B  2  27  ? 117.195 37.008  26.546  1.00 40.42  ?  27  VAL B CB  1 
ATOM   5473  C  CG1 . VAL B  2  27  ? 118.104 35.785  26.512  1.00 44.24  ?  27  VAL B CG1 1 
ATOM   5474  C  CG2 . VAL B  2  27  ? 116.442 37.087  27.866  1.00 45.15  ?  27  VAL B CG2 1 
ATOM   5475  N  N   . TRP B  2  28  ? 120.338 38.110  26.969  1.00 53.02  ?  28  TRP B N   1 
ATOM   5476  C  CA  . TRP B  2  28  ? 121.484 38.320  27.848  1.00 52.70  ?  28  TRP B CA  1 
ATOM   5477  C  C   . TRP B  2  28  ? 121.906 39.789  27.865  1.00 59.08  ?  28  TRP B C   1 
ATOM   5478  O  O   . TRP B  2  28  ? 122.313 40.298  28.910  1.00 66.64  ?  28  TRP B O   1 
ATOM   5479  C  CB  . TRP B  2  28  ? 122.666 37.469  27.395  1.00 54.43  ?  28  TRP B CB  1 
ATOM   5480  C  CG  . TRP B  2  28  ? 122.516 36.006  27.674  1.00 52.95  ?  28  TRP B CG  1 
ATOM   5481  C  CD1 . TRP B  2  28  ? 122.868 35.351  28.814  1.00 44.18  ?  28  TRP B CD1 1 
ATOM   5482  C  CD2 . TRP B  2  28  ? 122.029 35.006  26.768  1.00 56.42  ?  28  TRP B CD2 1 
ATOM   5483  N  NE1 . TRP B  2  28  ? 122.613 34.004  28.683  1.00 61.60  ?  28  TRP B NE1 1 
ATOM   5484  C  CE2 . TRP B  2  28  ? 122.097 33.767  27.435  1.00 53.85  ?  28  TRP B CE2 1 
ATOM   5485  C  CE3 . TRP B  2  28  ? 121.509 35.042  25.471  1.00 52.81  ?  28  TRP B CE3 1 
ATOM   5486  C  CZ2 . TRP B  2  28  ? 121.686 32.580  26.840  1.00 49.39  ?  28  TRP B CZ2 1 
ATOM   5487  C  CZ3 . TRP B  2  28  ? 121.112 33.862  24.881  1.00 39.97  ?  28  TRP B CZ3 1 
ATOM   5488  C  CH2 . TRP B  2  28  ? 121.204 32.650  25.562  1.00 45.37  ?  28  TRP B CH2 1 
ATOM   5489  N  N   . ASP B  2  29  ? 121.822 40.471  26.711  1.00 65.18  ?  29  ASP B N   1 
ATOM   5490  C  CA  . ASP B  2  29  ? 122.185 41.885  26.610  1.00 64.28  ?  29  ASP B CA  1 
ATOM   5491  C  C   . ASP B  2  29  ? 121.195 42.715  27.409  1.00 56.03  ?  29  ASP B C   1 
ATOM   5492  O  O   . ASP B  2  29  ? 121.602 43.593  28.166  1.00 53.82  ?  29  ASP B O   1 
ATOM   5493  C  CB  . ASP B  2  29  ? 122.189 42.350  25.142  1.00 51.18  ?  29  ASP B CB  1 
ATOM   5494  C  CG  . ASP B  2  29  ? 123.124 41.571  24.240  1.00 69.39  ?  29  ASP B CG  1 
ATOM   5495  O  OD1 . ASP B  2  29  ? 123.847 40.683  24.753  1.00 75.73  ?  29  ASP B OD1 1 
ATOM   5496  O  OD2 . ASP B  2  29  ? 123.125 41.839  23.016  1.00 82.69  ?  29  ASP B OD2 1 
ATOM   5497  N  N   . ARG B  2  30  ? 119.894 42.426  27.257  1.00 52.92  ?  30  ARG B N   1 
ATOM   5498  C  CA  . ARG B  2  30  ? 118.862 43.161  27.979  1.00 53.49  ?  30  ARG B CA  1 
ATOM   5499  C  C   . ARG B  2  30  ? 118.920 42.887  29.480  1.00 59.33  ?  30  ARG B C   1 
ATOM   5500  O  O   . ARG B  2  30  ? 118.558 43.766  30.260  1.00 68.73  ?  30  ARG B O   1 
ATOM   5501  C  CB  . ARG B  2  30  ? 117.471 42.862  27.410  1.00 49.34  ?  30  ARG B CB  1 
ATOM   5502  C  CG  . ARG B  2  30  ? 117.261 43.429  26.009  1.00 50.48  ?  30  ARG B CG  1 
ATOM   5503  C  CD  . ARG B  2  30  ? 115.823 43.288  25.559  1.00 61.35  ?  30  ARG B CD  1 
ATOM   5504  N  NE  . ARG B  2  30  ? 115.419 41.885  25.463  1.00 57.38  ?  30  ARG B NE  1 
ATOM   5505  C  CZ  . ARG B  2  30  ? 115.678 41.088  24.429  1.00 61.24  ?  30  ARG B CZ  1 
ATOM   5506  N  NH1 . ARG B  2  30  ? 116.348 41.547  23.375  1.00 67.70  ?  30  ARG B NH1 1 
ATOM   5507  N  NH2 . ARG B  2  30  ? 115.270 39.824  24.442  1.00 46.02  ?  30  ARG B NH2 1 
ATOM   5508  N  N   . LYS B  2  31  ? 119.386 41.696  29.898  1.00 59.97  ?  31  LYS B N   1 
ATOM   5509  C  CA  . LYS B  2  31  ? 119.518 41.392  31.324  1.00 54.17  ?  31  LYS B CA  1 
ATOM   5510  C  C   . LYS B  2  31  ? 120.608 42.290  31.909  1.00 59.73  ?  31  LYS B C   1 
ATOM   5511  O  O   . LYS B  2  31  ? 120.432 42.838  32.997  1.00 65.21  ?  31  LYS B O   1 
ATOM   5512  C  CB  . LYS B  2  31  ? 119.863 39.910  31.544  1.00 46.48  ?  31  LYS B CB  1 
ATOM   5513  C  CG  . LYS B  2  31  ? 120.255 39.559  32.986  1.00 54.53  ?  31  LYS B CG  1 
ATOM   5514  C  CD  . LYS B  2  31  ? 119.064 39.574  33.948  1.00 62.88  ?  31  LYS B CD  1 
ATOM   5515  C  CE  . LYS B  2  31  ? 119.381 39.026  35.321  1.00 64.30  ?  31  LYS B CE  1 
ATOM   5516  N  NZ  . LYS B  2  31  ? 120.175 39.981  36.134  1.00 70.74  ?  31  LYS B NZ  1 
ATOM   5517  N  N   . ALA B  2  32  ? 121.728 42.443  31.187  1.00 53.08  ?  32  ALA B N   1 
ATOM   5518  C  CA  . ALA B  2  32  ? 122.831 43.280  31.636  1.00 49.94  ?  32  ALA B CA  1 
ATOM   5519  C  C   . ALA B  2  32  ? 122.387 44.732  31.742  1.00 61.66  ?  32  ALA B C   1 
ATOM   5520  O  O   . ALA B  2  32  ? 122.757 45.414  32.698  1.00 71.86  ?  32  ALA B O   1 
ATOM   5521  C  CB  . ALA B  2  32  ? 123.997 43.165  30.672  1.00 52.41  ?  32  ALA B CB  1 
ATOM   5522  N  N   . ASP B  2  33  ? 121.586 45.203  30.770  1.00 62.44  ?  33  ASP B N   1 
ATOM   5523  C  CA  . ASP B  2  33  ? 121.082 46.578  30.753  1.00 66.60  ?  33  ASP B CA  1 
ATOM   5524  C  C   . ASP B  2  33  ? 120.223 46.890  31.974  1.00 59.38  ?  33  ASP B C   1 
ATOM   5525  O  O   . ASP B  2  33  ? 120.156 48.046  32.385  1.00 71.66  ?  33  ASP B O   1 
ATOM   5526  C  CB  . ASP B  2  33  ? 120.270 46.840  29.472  1.00 63.56  ?  33  ASP B CB  1 
ATOM   5527  C  CG  . ASP B  2  33  ? 121.100 46.894  28.205  1.00 91.31  ?  33  ASP B CG  1 
ATOM   5528  O  OD1 . ASP B  2  33  ? 122.292 47.267  28.291  1.00 93.99  ?  33  ASP B OD1 1 
ATOM   5529  O  OD2 . ASP B  2  33  ? 120.558 46.564  27.124  1.00 79.31  ?  33  ASP B OD2 1 
ATOM   5530  N  N   . MET B  2  34  ? 119.569 45.875  32.556  1.00 61.08  ?  34  MET B N   1 
ATOM   5531  C  CA  . MET B  2  34  ? 118.727 46.073  33.735  1.00 60.38  ?  34  MET B CA  1 
ATOM   5532  C  C   . MET B  2  34  ? 119.561 46.328  35.017  1.00 65.94  ?  34  MET B C   1 
ATOM   5533  O  O   . MET B  2  34  ? 118.978 46.660  36.052  1.00 69.23  ?  34  MET B O   1 
ATOM   5534  C  CB  . MET B  2  34  ? 117.785 44.859  33.924  1.00 54.11  ?  34  MET B CB  1 
ATOM   5535  C  CG  . MET B  2  34  ? 116.369 45.212  34.377  1.00 42.83  ?  34  MET B CG  1 
ATOM   5536  S  SD  . MET B  2  34  ? 115.542 46.514  33.421  1.00 62.53  ?  34  MET B SD  1 
ATOM   5537  C  CE  . MET B  2  34  ? 115.355 45.719  31.854  1.00 65.07  ?  34  MET B CE  1 
ATOM   5538  N  N   . LYS B  2  35  ? 120.911 46.177  34.953  1.00 69.65  ?  35  LYS B N   1 
ATOM   5539  C  CA  . LYS B  2  35  ? 121.836 46.419  36.071  1.00 59.71  ?  35  LYS B CA  1 
ATOM   5540  C  C   . LYS B  2  35  ? 121.309 45.812  37.395  1.00 66.69  ?  35  LYS B C   1 
ATOM   5541  O  O   . LYS B  2  35  ? 120.788 44.699  37.350  1.00 68.44  ?  35  LYS B O   1 
ATOM   5542  C  CB  . LYS B  2  35  ? 122.133 47.930  36.185  1.00 53.43  ?  35  LYS B CB  1 
ATOM   5543  C  CG  . LYS B  2  35  ? 122.477 48.611  34.866  1.00 68.25  ?  35  LYS B CG  1 
ATOM   5544  C  CD  . LYS B  2  35  ? 123.921 48.391  34.440  1.00 62.33  ?  35  LYS B CD  1 
ATOM   5545  C  CE  . LYS B  2  35  ? 124.157 48.742  32.986  1.00 76.62  ?  35  LYS B CE  1 
ATOM   5546  N  NZ  . LYS B  2  35  ? 123.657 50.103  32.624  1.00 86.31  ?  35  LYS B NZ  1 
ATOM   5547  N  N   . VAL B  2  36  ? 121.437 46.501  38.556  1.00 70.47  ?  36  VAL B N   1 
ATOM   5548  C  CA  . VAL B  2  36  ? 120.921 45.955  39.813  1.00 62.23  ?  36  VAL B CA  1 
ATOM   5549  C  C   . VAL B  2  36  ? 119.410 46.127  39.781  1.00 61.31  ?  36  VAL B C   1 
ATOM   5550  O  O   . VAL B  2  36  ? 118.918 47.254  39.740  1.00 66.93  ?  36  VAL B O   1 
ATOM   5551  C  CB  . VAL B  2  36  ? 121.542 46.630  41.056  1.00 53.74  ?  36  VAL B CB  1 
ATOM   5552  C  CG1 . VAL B  2  36  ? 120.801 46.216  42.323  1.00 49.49  ?  36  VAL B CG1 1 
ATOM   5553  C  CG2 . VAL B  2  36  ? 123.023 46.295  41.170  1.00 68.26  ?  36  VAL B CG2 1 
ATOM   5554  N  N   . GLN B  2  37  ? 118.728 44.991  39.616  1.00 63.38  ?  37  GLN B N   1 
ATOM   5555  C  CA  . GLN B  2  37  ? 117.251 45.016  39.511  1.00 67.83  ?  37  GLN B CA  1 
ATOM   5556  C  C   . GLN B  2  37  ? 116.703 45.491  40.851  1.00 67.79  ?  37  GLN B C   1 
ATOM   5557  O  O   . GLN B  2  37  ? 117.444 45.435  41.849  1.00 69.07  ?  37  GLN B O   1 
ATOM   5558  C  CB  . GLN B  2  37  ? 116.726 43.631  39.131  1.00 49.70  ?  37  GLN B CB  1 
ATOM   5559  C  CG  . GLN B  2  37  ? 117.438 43.020  37.934  1.00 50.01  ?  37  GLN B CG  1 
ATOM   5560  C  CD  . GLN B  2  37  ? 116.552 42.071  37.167  1.00 43.67  ?  37  GLN B CD  1 
ATOM   5561  O  OE1 . GLN B  2  37  ? 115.940 42.435  36.166  1.00 59.94  ?  37  GLN B OE1 1 
ATOM   5562  N  NE2 . GLN B  2  37  ? 116.476 40.837  37.635  1.00 55.71  ?  37  GLN B NE2 1 
ATOM   5563  N  N   . CYS B  2  38  ? 115.452 45.931  40.864  1.00 59.20  ?  38  CYS B N   1 
ATOM   5564  C  CA  . CYS B  2  38  ? 114.920 46.508  42.118  1.00 65.81  ?  38  CYS B CA  1 
ATOM   5565  C  C   . CYS B  2  38  ? 114.886 45.455  43.226  1.00 62.99  ?  38  CYS B C   1 
ATOM   5566  O  O   . CYS B  2  38  ? 114.641 44.279  42.914  1.00 68.78  ?  38  CYS B O   1 
ATOM   5567  C  CB  . CYS B  2  38  ? 113.517 47.046  41.922  1.00 51.55  ?  38  CYS B CB  1 
ATOM   5568  S  SG  . CYS B  2  38  ? 113.012 47.928  43.410  1.00 72.86  ?  38  CYS B SG  1 
ATOM   5569  N  N   . GLY B  2  39  ? 115.104 45.884  44.471  1.00 62.49  ?  39  GLY B N   1 
ATOM   5570  C  CA  . GLY B  2  39  ? 115.111 44.949  45.609  1.00 62.59  ?  39  GLY B CA  1 
ATOM   5571  C  C   . GLY B  2  39  ? 113.741 44.825  46.246  1.00 65.14  ?  39  GLY B C   1 
ATOM   5572  O  O   . GLY B  2  39  ? 113.488 43.790  46.888  1.00 75.46  ?  39  GLY B O   1 
ATOM   5573  N  N   . PHE B  2  40  ? 112.870 45.824  46.098  1.00 56.83  ?  40  PHE B N   1 
ATOM   5574  C  CA  . PHE B  2  40  ? 111.491 45.674  46.634  1.00 57.91  ?  40  PHE B CA  1 
ATOM   5575  C  C   . PHE B  2  40  ? 110.732 44.667  45.771  1.00 69.98  ?  40  PHE B C   1 
ATOM   5576  O  O   . PHE B  2  40  ? 110.008 43.820  46.326  1.00 79.99  ?  40  PHE B O   1 
ATOM   5577  C  CB  . PHE B  2  40  ? 110.786 47.029  46.686  1.00 66.30  ?  40  PHE B CB  1 
ATOM   5578  C  CG  . PHE B  2  40  ? 111.502 48.019  47.562  1.00 68.08  ?  40  PHE B CG  1 
ATOM   5579  C  CD1 . PHE B  2  40  ? 111.304 48.019  48.932  1.00 69.35  ?  40  PHE B CD1 1 
ATOM   5580  C  CD2 . PHE B  2  40  ? 112.407 48.915  47.020  1.00 68.21  ?  40  PHE B CD2 1 
ATOM   5581  C  CE1 . PHE B  2  40  ? 111.978 48.916  49.741  1.00 67.07  ?  40  PHE B CE1 1 
ATOM   5582  C  CE2 . PHE B  2  40  ? 113.081 49.812  47.830  1.00 62.48  ?  40  PHE B CE2 1 
ATOM   5583  C  CZ  . PHE B  2  40  ? 112.869 49.803  49.187  1.00 59.35  ?  40  PHE B CZ  1 
ATOM   5584  N  N   . GLY B  2  41  ? 110.902 44.764  44.454  1.00 62.66  ?  41  GLY B N   1 
ATOM   5585  C  CA  . GLY B  2  41  ? 110.254 43.830  43.547  1.00 63.02  ?  41  GLY B CA  1 
ATOM   5586  C  C   . GLY B  2  41  ? 110.819 42.431  43.692  1.00 57.65  ?  41  GLY B C   1 
ATOM   5587  O  O   . GLY B  2  41  ? 110.076 41.451  43.599  1.00 66.10  ?  41  GLY B O   1 
ATOM   5588  N  N   . SER B  2  42  ? 112.144 42.329  43.932  1.00 54.06  ?  42  SER B N   1 
ATOM   5589  C  CA  . SER B  2  42  ? 112.844 41.057  44.105  1.00 43.87  ?  42  SER B CA  1 
ATOM   5590  C  C   . SER B  2  42  ? 112.399 40.352  45.379  1.00 58.05  ?  42  SER B C   1 
ATOM   5591  O  O   . SER B  2  42  ? 112.190 39.142  45.365  1.00 63.38  ?  42  SER B O   1 
ATOM   5592  C  CB  . SER B  2  42  ? 114.352 41.280  44.155  1.00 56.26  ?  42  SER B CB  1 
ATOM   5593  O  OG  . SER B  2  42  ? 114.829 41.830  42.938  1.00 76.23  ?  42  SER B OG  1 
ATOM   5594  N  N   . ALA B  2  43  ? 112.273 41.096  46.485  1.00 60.85  ?  43  ALA B N   1 
ATOM   5595  C  CA  . ALA B  2  43  ? 111.829 40.516  47.753  1.00 66.62  ?  43  ALA B CA  1 
ATOM   5596  C  C   . ALA B  2  43  ? 110.300 40.360  47.810  1.00 57.32  ?  43  ALA B C   1 
ATOM   5597  O  O   . ALA B  2  43  ? 109.793 39.690  48.704  1.00 65.55  ?  43  ALA B O   1 
ATOM   5598  C  CB  . ALA B  2  43  ? 112.308 41.369  48.915  1.00 62.88  ?  43  ALA B CB  1 
ATOM   5599  N  N   . GLY B  2  44  ? 109.586 40.977  46.873  1.00 60.65  ?  44  GLY B N   1 
ATOM   5600  C  CA  . GLY B  2  44  ? 108.135 40.899  46.796  1.00 55.39  ?  44  GLY B CA  1 
ATOM   5601  C  C   . GLY B  2  44  ? 107.415 41.843  47.733  1.00 63.21  ?  44  GLY B C   1 
ATOM   5602  O  O   . GLY B  2  44  ? 106.245 41.617  48.042  1.00 80.82  ?  44  GLY B O   1 
ATOM   5603  N  N   . VAL B  2  45  ? 108.081 42.920  48.177  1.00 54.18  ?  45  VAL B N   1 
ATOM   5604  C  CA  . VAL B  2  45  ? 107.459 43.868  49.105  1.00 56.20  ?  45  VAL B CA  1 
ATOM   5605  C  C   . VAL B  2  45  ? 107.003 45.166  48.436  1.00 67.55  ?  45  VAL B C   1 
ATOM   5606  O  O   . VAL B  2  45  ? 106.867 46.182  49.115  1.00 70.99  ?  45  VAL B O   1 
ATOM   5607  C  CB  . VAL B  2  45  ? 108.361 44.145  50.333  1.00 57.38  ?  45  VAL B CB  1 
ATOM   5608  C  CG1 . VAL B  2  45  ? 108.381 42.944  51.270  1.00 70.95  ?  45  VAL B CG1 1 
ATOM   5609  C  CG2 . VAL B  2  45  ? 109.775 44.530  49.909  1.00 69.49  ?  45  VAL B CG2 1 
ATOM   5610  N  N   . CYS B  2  46  ? 106.730 45.134  47.125  1.00 52.17  ?  46  CYS B N   1 
ATOM   5611  C  CA  . CYS B  2  46  ? 106.234 46.307  46.419  1.00 48.33  ?  46  CYS B CA  1 
ATOM   5612  C  C   . CYS B  2  46  ? 104.801 45.998  46.009  1.00 61.47  ?  46  CYS B C   1 
ATOM   5613  O  O   . CYS B  2  46  ? 104.561 44.945  45.423  1.00 67.34  ?  46  CYS B O   1 
ATOM   5614  C  CB  . CYS B  2  46  ? 107.097 46.629  45.207  1.00 56.59  ?  46  CYS B CB  1 
ATOM   5615  S  SG  . CYS B  2  46  ? 106.476 48.011  44.221  1.00 59.83  ?  46  CYS B SG  1 
ATOM   5616  N  N   . CYS B  2  47  ? 103.848 46.888  46.319  1.00 54.74  ?  47  CYS B N   1 
ATOM   5617  C  CA  . CYS B  2  47  ? 102.449 46.653  45.975  1.00 53.69  ?  47  CYS B CA  1 
ATOM   5618  C  C   . CYS B  2  47  ? 101.883 47.722  45.060  1.00 70.14  ?  47  CYS B C   1 
ATOM   5619  O  O   . CYS B  2  47  ? 102.057 48.913  45.318  1.00 72.65  ?  47  CYS B O   1 
ATOM   5620  C  CB  . CYS B  2  47  ? 101.609 46.529  47.238  1.00 65.78  ?  47  CYS B CB  1 
ATOM   5621  S  SG  . CYS B  2  47  ? 99.896  46.032  46.930  1.00 76.04  ?  47  CYS B SG  1 
ATOM   5622  N  N   . ARG B  2  48  ? 101.183 47.296  43.999  1.00 61.02  ?  48  ARG B N   1 
ATOM   5623  C  CA  . ARG B  2  48  ? 100.543 48.205  43.053  1.00 59.19  ?  48  ARG B CA  1 
ATOM   5624  C  C   . ARG B  2  48  ? 99.118  47.705  42.782  1.00 59.02  ?  48  ARG B C   1 
ATOM   5625  O  O   . ARG B  2  48  ? 98.671  47.697  41.636  1.00 59.27  ?  48  ARG B O   1 
ATOM   5626  C  CB  . ARG B  2  48  ? 101.342 48.276  41.745  1.00 66.04  ?  48  ARG B CB  1 
ATOM   5627  C  CG  . ARG B  2  48  ? 102.739 48.860  41.903  1.00 70.52  ?  48  ARG B CG  1 
ATOM   5628  C  CD  . ARG B  2  48  ? 103.330 49.336  40.579  1.00 74.51  ?  48  ARG B CD  1 
ATOM   5629  N  NE  . ARG B  2  48  ? 104.369 48.429  40.075  1.00 103.96 ?  48  ARG B NE  1 
ATOM   5630  C  CZ  . ARG B  2  48  ? 104.159 47.361  39.305  1.00 96.74  ?  48  ARG B CZ  1 
ATOM   5631  N  NH1 . ARG B  2  48  ? 102.927 47.037  38.925  1.00 90.06  ?  48  ARG B NH1 1 
ATOM   5632  N  NH2 . ARG B  2  48  ? 105.181 46.613  38.902  1.00 72.17  ?  48  ARG B NH2 1 
ATOM   5633  N  N   . ASN B  2  49  ? 98.404  47.318  43.843  1.00 55.48  ?  49  ASN B N   1 
ATOM   5634  C  CA  . ASN B  2  49  ? 97.039  46.752  43.670  1.00 58.58  ?  49  ASN B CA  1 
ATOM   5635  C  C   . ASN B  2  49  ? 95.983  47.860  43.774  1.00 58.00  ?  49  ASN B C   1 
ATOM   5636  O  O   . ASN B  2  49  ? 94.786  47.537  43.657  1.00 58.60  ?  49  ASN B O   1 
ATOM   5637  C  CB  . ASN B  2  49  ? 96.771  45.621  44.667  1.00 53.87  ?  49  ASN B CB  1 
ATOM   5638  C  CG  . ASN B  2  49  ? 97.524  44.351  44.334  1.00 66.61  ?  49  ASN B CG  1 
ATOM   5639  O  OD1 . ASN B  2  49  ? 98.640  44.402  43.821  1.00 72.05  ?  49  ASN B OD1 1 
ATOM   5640  N  ND2 . ASN B  2  49  ? 96.924  43.208  44.623  1.00 75.15  ?  49  ASN B ND2 1 
ATOM   5641  N  N   . CYS B  2  50  ? 96.411  49.109  43.955  1.00 47.70  ?  50  CYS B N   1 
ATOM   5642  C  CA  . CYS B  2  50  ? 95.437  50.232  43.955  1.00 60.15  ?  50  CYS B CA  1 
ATOM   5643  C  C   . CYS B  2  50  ? 96.177  51.541  43.665  1.00 56.09  ?  50  CYS B C   1 
ATOM   5644  O  O   . CYS B  2  50  ? 97.416  51.554  43.789  1.00 57.84  ?  50  CYS B O   1 
ATOM   5645  C  CB  . CYS B  2  50  ? 94.664  50.300  45.266  1.00 64.70  ?  50  CYS B CB  1 
ATOM   5646  S  SG  . CYS B  2  50  ? 95.600  51.059  46.613  1.00 55.61  ?  50  CYS B SG  1 
ATOM   5647  N  N   . SER B  2  51  ? 95.445  52.594  43.304  1.00 52.88  ?  51  SER B N   1 
ATOM   5648  C  CA  . SER B  2  51  ? 96.078  53.876  42.891  1.00 55.59  ?  51  SER B CA  1 
ATOM   5649  C  C   . SER B  2  51  ? 96.488  54.708  44.112  1.00 61.16  ?  51  SER B C   1 
ATOM   5650  O  O   . SER B  2  51  ? 96.963  55.841  43.913  1.00 72.16  ?  51  SER B O   1 
ATOM   5651  C  CB  . SER B  2  51  ? 95.163  54.654  41.983  1.00 50.40  ?  51  SER B CB  1 
ATOM   5652  O  OG  . SER B  2  51  ? 94.382  55.579  42.724  1.00 86.18  ?  51  SER B OG  1 
ATOM   5653  N  N   . MET B  2  52  ? 96.246  54.200  45.321  1.00 60.94  ?  52  MET B N   1 
ATOM   5654  C  CA  . MET B  2  52  ? 96.758  54.914  46.518  1.00 57.46  ?  52  MET B CA  1 
ATOM   5655  C  C   . MET B  2  52  ? 98.270  54.709  46.471  1.00 63.67  ?  52  MET B C   1 
ATOM   5656  O  O   . MET B  2  52  ? 99.004  55.560  47.002  1.00 61.72  ?  52  MET B O   1 
ATOM   5657  C  CB  . MET B  2  52  ? 96.154  54.354  47.808  1.00 57.27  ?  52  MET B CB  1 
ATOM   5658  C  CG  . MET B  2  52  ? 94.672  54.638  47.954  1.00 76.09  ?  52  MET B CG  1 
ATOM   5659  S  SD  . MET B  2  52  ? 94.141  54.705  49.684  1.00 61.36  ?  52  MET B SD  1 
ATOM   5660  C  CE  . MET B  2  52  ? 94.368  52.995  50.168  1.00 55.59  ?  52  MET B CE  1 
ATOM   5661  N  N   . GLY B  2  53  ? 98.701  53.622  45.825  1.00 68.84  ?  53  GLY B N   1 
ATOM   5662  C  CA  . GLY B  2  53  ? 100.140 53.327  45.693  1.00 52.43  ?  53  GLY B CA  1 
ATOM   5663  C  C   . GLY B  2  53  ? 100.789 54.059  44.531  1.00 63.15  ?  53  GLY B C   1 
ATOM   5664  O  O   . GLY B  2  53  ? 100.130 54.942  43.952  1.00 73.55  ?  53  GLY B O   1 
ATOM   5665  N  N   . PRO B  2  54  ? 102.050 53.743  44.154  1.00 67.27  ?  54  PRO B N   1 
ATOM   5666  C  CA  . PRO B  2  54  ? 102.704 52.491  44.545  1.00 54.96  ?  54  PRO B CA  1 
ATOM   5667  C  C   . PRO B  2  54  ? 103.190 52.517  46.001  1.00 66.52  ?  54  PRO B C   1 
ATOM   5668  O  O   . PRO B  2  54  ? 103.426 53.592  46.512  1.00 70.71  ?  54  PRO B O   1 
ATOM   5669  C  CB  . PRO B  2  54  ? 103.932 52.405  43.623  1.00 47.92  ?  54  PRO B CB  1 
ATOM   5670  C  CG  . PRO B  2  54  ? 103.734 53.497  42.594  1.00 48.06  ?  54  PRO B CG  1 
ATOM   5671  C  CD  . PRO B  2  54  ? 102.917 54.555  43.302  1.00 71.86  ?  54  PRO B CD  1 
ATOM   5672  N  N   . CYS B  2  55  ? 103.325 51.343  46.625  1.00 59.09  ?  55  CYS B N   1 
ATOM   5673  C  CA  . CYS B  2  55  ? 103.841 51.269  48.019  1.00 59.20  ?  55  CYS B CA  1 
ATOM   5674  C  C   . CYS B  2  55  ? 105.007 50.275  48.088  1.00 61.19  ?  55  CYS B C   1 
ATOM   5675  O  O   . CYS B  2  55  ? 104.974 49.280  47.340  1.00 65.14  ?  55  CYS B O   1 
ATOM   5676  C  CB  . CYS B  2  55  ? 102.743 50.840  48.985  1.00 50.96  ?  55  CYS B CB  1 
ATOM   5677  S  SG  . CYS B  2  55  ? 101.205 51.780  48.808  1.00 65.38  ?  55  CYS B SG  1 
ATOM   5678  N  N   . ARG B  2  56  ? 105.993 50.538  48.953  1.00 50.72  ?  56  ARG B N   1 
ATOM   5679  C  CA  . ARG B  2  56  ? 107.167 49.638  49.107  1.00 56.76  ?  56  ARG B CA  1 
ATOM   5680  C  C   . ARG B  2  56  ? 107.561 49.560  50.585  1.00 68.92  ?  56  ARG B C   1 
ATOM   5681  O  O   . ARG B  2  56  ? 108.121 50.542  51.103  1.00 73.78  ?  56  ARG B O   1 
ATOM   5682  C  CB  . ARG B  2  56  ? 108.336 50.060  48.208  1.00 58.40  ?  56  ARG B CB  1 
ATOM   5683  C  CG  . ARG B  2  56  ? 108.743 51.521  48.292  1.00 71.67  ?  56  ARG B CG  1 
ATOM   5684  C  CD  . ARG B  2  56  ? 109.846 51.767  47.281  1.00 67.42  ?  56  ARG B CD  1 
ATOM   5685  N  NE  . ARG B  2  56  ? 109.988 53.201  47.081  1.00 74.00  ?  56  ARG B NE  1 
ATOM   5686  C  CZ  . ARG B  2  56  ? 110.772 53.613  46.096  1.00 66.99  ?  56  ARG B CZ  1 
ATOM   5687  N  NH1 . ARG B  2  56  ? 111.370 52.696  45.346  1.00 78.71  ?  56  ARG B NH1 1 
ATOM   5688  N  NH2 . ARG B  2  56  ? 110.957 54.900  45.867  1.00 96.28  ?  56  ARG B NH2 1 
ATOM   5689  N  N   . VAL B  2  57  ? 107.270 48.428  51.225  1.00 58.85  ?  57  VAL B N   1 
ATOM   5690  C  CA  . VAL B  2  57  ? 107.613 48.219  52.664  1.00 57.87  ?  57  VAL B CA  1 
ATOM   5691  C  C   . VAL B  2  57  ? 109.016 47.609  52.751  1.00 75.15  ?  57  VAL B C   1 
ATOM   5692  O  O   . VAL B  2  57  ? 109.570 47.259  51.692  1.00 71.37  ?  57  VAL B O   1 
ATOM   5693  C  CB  . VAL B  2  57  ? 106.568 47.333  53.367  1.00 69.05  ?  57  VAL B CB  1 
ATOM   5694  C  CG1 . VAL B  2  57  ? 105.238 48.052  53.528  1.00 59.09  ?  57  VAL B CG1 1 
ATOM   5695  C  CG2 . VAL B  2  57  ? 106.377 46.009  52.646  1.00 61.66  ?  57  VAL B CG2 1 
ATOM   5696  N  N   . SER B  2  58  ? 109.575 47.499  53.963  1.00 66.36  ?  58  SER B N   1 
ATOM   5697  C  CA  . SER B  2  58  ? 110.952 46.960  54.139  1.00 71.00  ?  58  SER B CA  1 
ATOM   5698  C  C   . SER B  2  58  ? 110.917 45.438  54.272  1.00 77.48  ?  58  SER B C   1 
ATOM   5699  O  O   . SER B  2  58  ? 110.127 44.933  55.089  1.00 92.21  ?  58  SER B O   1 
ATOM   5700  C  CB  . SER B  2  58  ? 111.656 47.566  55.329  1.00 71.12  ?  58  SER B CB  1 
ATOM   5701  O  OG  . SER B  2  58  ? 112.787 46.783  55.708  1.00 83.70  ?  58  SER B OG  1 
ATOM   5702  N  N   . PRO B  2  59  ? 111.742 44.690  53.512  1.00 71.49  ?  59  PRO B N   1 
ATOM   5703  C  CA  . PRO B  2  59  ? 111.819 43.237  53.665  1.00 67.03  ?  59  PRO B CA  1 
ATOM   5704  C  C   . PRO B  2  59  ? 112.539 42.895  54.975  1.00 75.50  ?  59  PRO B C   1 
ATOM   5705  O  O   . PRO B  2  59  ? 112.365 41.793  55.460  1.00 93.06  ?  59  PRO B O   1 
ATOM   5706  C  CB  . PRO B  2  59  ? 112.664 42.805  52.461  1.00 71.95  ?  59  PRO B CB  1 
ATOM   5707  C  CG  . PRO B  2  59  ? 113.521 44.012  52.159  1.00 76.06  ?  59  PRO B CG  1 
ATOM   5708  C  CD  . PRO B  2  59  ? 112.634 45.200  52.469  1.00 75.95  ?  59  PRO B CD  1 
ATOM   5709  N  N   . VAL B  2  60  ? 113.319 43.839  55.508  1.00 75.31  ?  60  VAL B N   1 
ATOM   5710  C  CA  . VAL B  2  60  ? 114.037 43.617  56.757  1.00 76.94  ?  60  VAL B CA  1 
ATOM   5711  C  C   . VAL B  2  60  ? 113.126 44.064  57.904  1.00 80.50  ?  60  VAL B C   1 
ATOM   5712  O  O   . VAL B  2  60  ? 112.921 45.267  58.072  1.00 82.85  ?  60  VAL B O   1 
ATOM   5713  C  CB  . VAL B  2  60  ? 115.359 44.416  56.769  1.00 72.80  ?  60  VAL B CB  1 
ATOM   5714  C  CG1 . VAL B  2  60  ? 116.049 44.306  58.123  1.00 81.69  ?  60  VAL B CG1 1 
ATOM   5715  C  CG2 . VAL B  2  60  ? 116.284 43.956  55.648  1.00 70.71  ?  60  VAL B CG2 1 
ATOM   5716  N  N   . PRO B  2  61  ? 112.559 43.143  58.706  1.00 81.39  ?  61  PRO B N   1 
ATOM   5717  C  CA  . PRO B  2  61  ? 111.682 43.586  59.798  1.00 74.62  ?  61  PRO B CA  1 
ATOM   5718  C  C   . PRO B  2  61  ? 112.381 44.519  60.784  1.00 94.56  ?  61  PRO B C   1 
ATOM   5719  O  O   . PRO B  2  61  ? 113.582 44.389  61.020  1.00 101.97 ?  61  PRO B O   1 
ATOM   5720  C  CB  . PRO B  2  61  ? 111.252 42.276  60.470  1.00 69.64  ?  61  PRO B CB  1 
ATOM   5721  C  CG  . PRO B  2  61  ? 111.503 41.218  59.478  1.00 66.69  ?  61  PRO B CG  1 
ATOM   5722  C  CD  . PRO B  2  61  ? 112.668 41.672  58.667  1.00 83.48  ?  61  PRO B CD  1 
ATOM   5723  N  N   . GLY B  2  62  ? 111.621 45.453  61.347  1.00 97.44  ?  62  GLY B N   1 
ATOM   5724  C  CA  . GLY B  2  62  ? 112.143 46.402  62.320  1.00 80.85  ?  62  GLY B CA  1 
ATOM   5725  C  C   . GLY B  2  62  ? 112.497 47.757  61.745  1.00 94.32  ?  62  GLY B C   1 
ATOM   5726  O  O   . GLY B  2  62  ? 112.138 48.782  62.330  1.00 114.72 ?  62  GLY B O   1 
ATOM   5727  N  N   . LYS B  2  63  ? 113.205 47.786  60.605  1.00 121.69 ?  63  LYS B N   1 
ATOM   5728  C  CA  . LYS B  2  63  ? 113.618 49.049  59.981  1.00 127.43 ?  63  LYS B CA  1 
ATOM   5729  C  C   . LYS B  2  63  ? 112.767 49.406  58.755  1.00 117.49 ?  63  LYS B C   1 
ATOM   5730  O  O   . LYS B  2  63  ? 112.088 48.544  58.205  1.00 119.28 ?  63  LYS B O   1 
ATOM   5731  C  CB  . LYS B  2  63  ? 115.113 48.990  59.599  1.00 122.82 ?  63  LYS B CB  1 
ATOM   5732  C  CG  . LYS B  2  63  ? 116.046 48.617  60.761  1.00 146.96 ?  63  LYS B CG  1 
ATOM   5733  C  CD  . LYS B  2  63  ? 116.213 49.748  61.800  1.00 168.83 ?  63  LYS B CD  1 
ATOM   5734  C  CE  . LYS B  2  63  ? 117.069 49.341  62.982  1.00 153.21 ?  63  LYS B CE  1 
ATOM   5735  N  NZ  . LYS B  2  63  ? 117.160 50.420  64.007  1.00 120.97 ?  63  LYS B NZ  1 
ATOM   5736  N  N   . GLY B  2  64  ? 112.808 50.675  58.354  1.00 94.88  ?  64  GLY B N   1 
ATOM   5737  C  CA  . GLY B  2  64  ? 112.066 51.175  57.201  1.00 93.73  ?  64  GLY B CA  1 
ATOM   5738  C  C   . GLY B  2  64  ? 110.564 51.254  57.404  1.00 86.52  ?  64  GLY B C   1 
ATOM   5739  O  O   . GLY B  2  64  ? 110.081 51.166  58.537  1.00 86.71  ?  64  GLY B O   1 
ATOM   5740  N  N   . VAL B  2  65  ? 109.809 51.417  56.298  1.00 74.60  ?  65  VAL B N   1 
ATOM   5741  C  CA  . VAL B  2  65  ? 108.345 51.504  56.349  1.00 66.60  ?  65  VAL B CA  1 
ATOM   5742  C  C   . VAL B  2  65  ? 107.769 50.120  56.660  1.00 77.84  ?  65  VAL B C   1 
ATOM   5743  O  O   . VAL B  2  65  ? 108.155 49.140  56.025  1.00 80.88  ?  65  VAL B O   1 
ATOM   5744  C  CB  . VAL B  2  65  ? 107.760 52.077  55.042  1.00 69.38  ?  65  VAL B CB  1 
ATOM   5745  C  CG1 . VAL B  2  65  ? 106.240 52.131  55.112  1.00 79.27  ?  65  VAL B CG1 1 
ATOM   5746  C  CG2 . VAL B  2  65  ? 108.327 53.464  54.753  1.00 81.52  ?  65  VAL B CG2 1 
ATOM   5747  N  N   . GLU B  2  66  ? 106.850 50.038  57.629  1.00 69.12  ?  66  GLU B N   1 
ATOM   5748  C  CA  . GLU B  2  66  ? 106.264 48.766  58.056  1.00 63.67  ?  66  GLU B CA  1 
ATOM   5749  C  C   . GLU B  2  66  ? 105.011 48.326  57.283  1.00 61.05  ?  66  GLU B C   1 
ATOM   5750  O  O   . GLU B  2  66  ? 104.859 47.134  57.015  1.00 73.25  ?  66  GLU B O   1 
ATOM   5751  C  CB  . GLU B  2  66  ? 105.939 48.845  59.558  1.00 72.18  ?  66  GLU B CB  1 
ATOM   5752  C  CG  . GLU B  2  66  ? 105.656 47.503  60.216  1.00 94.47  ?  66  GLU B CG  1 
ATOM   5753  C  CD  . GLU B  2  66  ? 105.191 47.591  61.658  1.00 108.70 ?  66  GLU B CD  1 
ATOM   5754  O  OE1 . GLU B  2  66  ? 104.741 48.683  62.076  1.00 98.21  ?  66  GLU B OE1 1 
ATOM   5755  O  OE2 . GLU B  2  66  ? 105.267 46.562  62.369  1.00 97.85  ?  66  GLU B OE2 1 
ATOM   5756  N  N   . ARG B  2  67  ? 104.098 49.255  56.961  1.00 60.01  ?  67  ARG B N   1 
ATOM   5757  C  CA  . ARG B  2  67  ? 102.850 48.902  56.277  1.00 57.44  ?  67  ARG B CA  1 
ATOM   5758  C  C   . ARG B  2  67  ? 102.580 49.788  55.058  1.00 66.43  ?  67  ARG B C   1 
ATOM   5759  O  O   . ARG B  2  67  ? 103.156 50.866  54.925  1.00 62.58  ?  67  ARG B O   1 
ATOM   5760  C  CB  . ARG B  2  67  ? 101.665 49.017  57.264  1.00 58.84  ?  67  ARG B CB  1 
ATOM   5761  C  CG  . ARG B  2  67  ? 101.881 48.301  58.604  1.00 60.20  ?  67  ARG B CG  1 
ATOM   5762  C  CD  . ARG B  2  67  ? 100.937 48.777  59.695  1.00 62.01  ?  67  ARG B CD  1 
ATOM   5763  N  NE  . ARG B  2  67  ? 99.753  47.923  59.801  1.00 81.62  ?  67  ARG B NE  1 
ATOM   5764  C  CZ  . ARG B  2  67  ? 99.651  46.835  60.561  1.00 83.76  ?  67  ARG B CZ  1 
ATOM   5765  N  NH1 . ARG B  2  67  ? 100.678 46.439  61.311  1.00 68.77  ?  67  ARG B NH1 1 
ATOM   5766  N  NH2 . ARG B  2  67  ? 98.525  46.133  60.581  1.00 75.72  ?  67  ARG B NH2 1 
ATOM   5767  N  N   . GLY B  2  68  ? 101.692 49.326  54.181  1.00 62.31  ?  68  GLY B N   1 
ATOM   5768  C  CA  . GLY B  2  68  ? 101.305 50.071  52.990  1.00 64.20  ?  68  GLY B CA  1 
ATOM   5769  C  C   . GLY B  2  68  ? 100.336 51.188  53.325  1.00 70.37  ?  68  GLY B C   1 
ATOM   5770  O  O   . GLY B  2  68  ? 99.988  51.375  54.491  1.00 57.08  ?  68  GLY B O   1 
ATOM   5771  N  N   . ILE B  2  69  ? 99.823  51.900  52.324  1.00 72.92  ?  69  ILE B N   1 
ATOM   5772  C  CA  . ILE B  2  69  ? 98.931  53.048  52.665  1.00 60.13  ?  69  ILE B CA  1 
ATOM   5773  C  C   . ILE B  2  69  ? 97.627  52.497  53.258  1.00 61.00  ?  69  ILE B C   1 
ATOM   5774  O  O   . ILE B  2  69  ? 97.111  53.121  54.204  1.00 66.34  ?  69  ILE B O   1 
ATOM   5775  C  CB  . ILE B  2  69  ? 98.716  53.956  51.439  1.00 60.97  ?  69  ILE B CB  1 
ATOM   5776  C  CG1 . ILE B  2  69  ? 100.022 54.652  51.050  1.00 55.51  ?  69  ILE B CG1 1 
ATOM   5777  C  CG2 . ILE B  2  69  ? 97.594  54.951  51.684  1.00 65.30  ?  69  ILE B CG2 1 
ATOM   5778  C  CD1 . ILE B  2  69  ? 99.870  55.662  49.941  1.00 60.25  ?  69  ILE B CD1 1 
ATOM   5779  N  N   . CYS B  2  70  ? 97.124  51.369  52.743  1.00 61.61  ?  70  CYS B N   1 
ATOM   5780  C  CA  . CYS B  2  70  ? 95.929  50.739  53.303  1.00 56.76  ?  70  CYS B CA  1 
ATOM   5781  C  C   . CYS B  2  70  ? 96.166  50.069  54.664  1.00 64.92  ?  70  CYS B C   1 
ATOM   5782  O  O   . CYS B  2  70  ? 95.200  49.716  55.336  1.00 67.06  ?  70  CYS B O   1 
ATOM   5783  C  CB  . CYS B  2  70  ? 95.344  49.747  52.302  1.00 55.48  ?  70  CYS B CB  1 
ATOM   5784  S  SG  . CYS B  2  70  ? 96.466  48.398  51.841  1.00 53.91  ?  70  CYS B SG  1 
ATOM   5785  N  N   . GLY B  2  71  ? 97.426  49.887  55.048  1.00 69.93  ?  71  GLY B N   1 
ATOM   5786  C  CA  . GLY B  2  71  ? 97.791  49.245  56.306  1.00 63.00  ?  71  GLY B CA  1 
ATOM   5787  C  C   . GLY B  2  71  ? 98.265  47.815  56.139  1.00 62.59  ?  71  GLY B C   1 
ATOM   5788  O  O   . GLY B  2  71  ? 98.438  47.104  57.130  1.00 71.35  ?  71  GLY B O   1 
ATOM   5789  N  N   . ALA B  2  72  ? 98.479  47.379  54.882  1.00 67.24  ?  72  ALA B N   1 
ATOM   5790  C  CA  . ALA B  2  72  ? 98.922  46.022  54.573  1.00 68.03  ?  72  ALA B CA  1 
ATOM   5791  C  C   . ALA B  2  72  ? 100.366 45.778  54.994  1.00 66.77  ?  72  ALA B C   1 
ATOM   5792  O  O   . ALA B  2  72  ? 101.266 46.499  54.570  1.00 61.10  ?  72  ALA B O   1 
ATOM   5793  C  CB  . ALA B  2  72  ? 98.775  45.758  53.082  1.00 70.74  ?  72  ALA B CB  1 
ATOM   5794  N  N   . THR B  2  73  ? 100.587 44.754  55.823  1.00 68.48  ?  73  THR B N   1 
ATOM   5795  C  CA  . THR B  2  73  ? 101.933 44.420  56.277  1.00 58.50  ?  73  THR B CA  1 
ATOM   5796  C  C   . THR B  2  73  ? 102.705 43.703  55.166  1.00 74.83  ?  73  THR B C   1 
ATOM   5797  O  O   . THR B  2  73  ? 102.101 43.228  54.203  1.00 75.60  ?  73  THR B O   1 
ATOM   5798  C  CB  . THR B  2  73  ? 101.885 43.616  57.585  1.00 63.01  ?  73  THR B CB  1 
ATOM   5799  O  OG1 . THR B  2  73  ? 103.221 43.469  58.069  1.00 115.28 ?  73  THR B OG1 1 
ATOM   5800  C  CG2 . THR B  2  73  ? 101.245 42.236  57.424  1.00 64.45  ?  73  THR B CG2 1 
ATOM   5801  N  N   . ALA B  2  74  ? 104.037 43.626  55.285  1.00 68.91  ?  74  ALA B N   1 
ATOM   5802  C  CA  . ALA B  2  74  ? 104.870 42.978  54.270  1.00 58.83  ?  74  ALA B CA  1 
ATOM   5803  C  C   . ALA B  2  74  ? 104.396 41.564  53.906  1.00 63.91  ?  74  ALA B C   1 
ATOM   5804  O  O   . ALA B  2  74  ? 104.286 41.247  52.727  1.00 60.64  ?  74  ALA B O   1 
ATOM   5805  C  CB  . ALA B  2  74  ? 106.316 42.940  54.735  1.00 76.46  ?  74  ALA B CB  1 
ATOM   5806  N  N   . ASP B  2  75  ? 104.087 40.730  54.906  1.00 68.14  ?  75  ASP B N   1 
ATOM   5807  C  CA  . ASP B  2  75  ? 103.630 39.359  54.664  1.00 66.02  ?  75  ASP B CA  1 
ATOM   5808  C  C   . ASP B  2  75  ? 102.362 39.323  53.807  1.00 66.35  ?  75  ASP B C   1 
ATOM   5809  O  O   . ASP B  2  75  ? 102.184 38.398  53.018  1.00 66.84  ?  75  ASP B O   1 
ATOM   5810  C  CB  . ASP B  2  75  ? 103.387 38.637  55.994  1.00 77.49  ?  75  ASP B CB  1 
ATOM   5811  C  CG  . ASP B  2  75  ? 104.605 38.624  56.889  1.00 87.25  ?  75  ASP B CG  1 
ATOM   5812  O  OD1 . ASP B  2  75  ? 105.567 37.905  56.564  1.00 73.64  ?  75  ASP B OD1 1 
ATOM   5813  O  OD2 . ASP B  2  75  ? 104.596 39.343  57.912  1.00 92.24  ?  75  ASP B OD2 1 
ATOM   5814  N  N   . VAL B  2  76  ? 101.489 40.324  53.955  1.00 67.29  ?  76  VAL B N   1 
ATOM   5815  C  CA  . VAL B  2  76  ? 100.257 40.398  53.177  1.00 59.05  ?  76  VAL B CA  1 
ATOM   5816  C  C   . VAL B  2  76  ? 100.668 40.728  51.743  1.00 66.14  ?  76  VAL B C   1 
ATOM   5817  O  O   . VAL B  2  76  ? 100.338 39.982  50.822  1.00 67.76  ?  76  VAL B O   1 
ATOM   5818  C  CB  . VAL B  2  76  ? 99.274  41.413  53.810  1.00 56.46  ?  76  VAL B CB  1 
ATOM   5819  C  CG1 . VAL B  2  76  ? 98.120  41.735  52.867  1.00 57.16  ?  76  VAL B CG1 1 
ATOM   5820  C  CG2 . VAL B  2  76  ? 98.751  40.890  55.138  1.00 66.98  ?  76  VAL B CG2 1 
ATOM   5821  N  N   . ILE B  2  77  ? 101.414 41.825  51.554  1.00 60.51  ?  77  ILE B N   1 
ATOM   5822  C  CA  . ILE B  2  77  ? 101.877 42.243  50.227  1.00 60.53  ?  77  ILE B CA  1 
ATOM   5823  C  C   . ILE B  2  77  ? 102.556 41.095  49.473  1.00 66.03  ?  77  ILE B C   1 
ATOM   5824  O  O   . ILE B  2  77  ? 102.198 40.816  48.332  1.00 69.83  ?  77  ILE B O   1 
ATOM   5825  C  CB  . ILE B  2  77  ? 102.809 43.477  50.342  1.00 51.31  ?  77  ILE B CB  1 
ATOM   5826  C  CG1 . ILE B  2  77  ? 102.027 44.705  50.863  1.00 61.88  ?  77  ILE B CG1 1 
ATOM   5827  C  CG2 . ILE B  2  77  ? 103.484 43.775  49.001  1.00 54.53  ?  77  ILE B CG2 1 
ATOM   5828  C  CD1 . ILE B  2  77  ? 102.871 45.722  51.576  1.00 50.89  ?  77  ILE B CD1 1 
ATOM   5829  N  N   . VAL B  2  78  ? 103.514 40.422  50.122  1.00 58.41  ?  78  VAL B N   1 
ATOM   5830  C  CA  . VAL B  2  78  ? 104.242 39.304  49.531  1.00 55.46  ?  78  VAL B CA  1 
ATOM   5831  C  C   . VAL B  2  78  ? 103.279 38.165  49.150  1.00 67.25  ?  78  VAL B C   1 
ATOM   5832  O  O   . VAL B  2  78  ? 103.318 37.691  48.014  1.00 69.55  ?  78  VAL B O   1 
ATOM   5833  C  CB  . VAL B  2  78  ? 105.349 38.811  50.494  1.00 54.18  ?  78  VAL B CB  1 
ATOM   5834  C  CG1 . VAL B  2  78  ? 105.952 37.504  50.007  1.00 53.61  ?  78  VAL B CG1 1 
ATOM   5835  C  CG2 . VAL B  2  78  ? 106.437 39.863  50.674  1.00 59.17  ?  78  VAL B CG2 1 
ATOM   5836  N  N   . SER B  2  79  ? 102.418 37.729  50.090  1.00 65.48  ?  79  SER B N   1 
ATOM   5837  C  CA  . SER B  2  79  ? 101.465 36.642  49.842  1.00 60.17  ?  79  SER B CA  1 
ATOM   5838  C  C   . SER B  2  79  ? 100.472 36.968  48.718  1.00 58.78  ?  79  SER B C   1 
ATOM   5839  O  O   . SER B  2  79  ? 100.080 36.065  47.985  1.00 60.98  ?  79  SER B O   1 
ATOM   5840  C  CB  . SER B  2  79  ? 100.713 36.278  51.121  1.00 55.72  ?  79  SER B CB  1 
ATOM   5841  O  OG  . SER B  2  79  ? 99.727  37.241  51.455  1.00 68.38  ?  79  SER B OG  1 
ATOM   5842  N  N   . ARG B  2  80  ? 100.065 38.238  48.574  1.00 58.55  ?  80  ARG B N   1 
ATOM   5843  C  CA  . ARG B  2  80  ? 99.136  38.613  47.506  1.00 57.14  ?  80  ARG B CA  1 
ATOM   5844  C  C   . ARG B  2  80  ? 99.871  38.577  46.168  1.00 59.75  ?  80  ARG B C   1 
ATOM   5845  O  O   . ARG B  2  80  ? 99.320  38.107  45.175  1.00 59.75  ?  80  ARG B O   1 
ATOM   5846  C  CB  . ARG B  2  80  ? 98.537  40.007  47.746  1.00 54.18  ?  80  ARG B CB  1 
ATOM   5847  C  CG  . ARG B  2  80  ? 97.690  40.078  49.012  1.00 57.19  ?  80  ARG B CG  1 
ATOM   5848  C  CD  . ARG B  2  80  ? 96.870  41.349  49.125  1.00 55.30  ?  80  ARG B CD  1 
ATOM   5849  N  NE  . ARG B  2  80  ? 97.690  42.562  49.100  1.00 61.11  ?  80  ARG B NE  1 
ATOM   5850  C  CZ  . ARG B  2  80  ? 97.235  43.781  49.372  1.00 49.39  ?  80  ARG B CZ  1 
ATOM   5851  N  NH1 . ARG B  2  80  ? 95.960  43.963  49.703  1.00 66.51  ?  80  ARG B NH1 1 
ATOM   5852  N  NH2 . ARG B  2  80  ? 98.049  44.828  49.321  1.00 74.53  ?  80  ARG B NH2 1 
ATOM   5853  N  N   . ASN B  2  81  ? 101.119 39.065  46.144  1.00 59.19  ?  81  ASN B N   1 
ATOM   5854  C  CA  . ASN B  2  81  ? 101.928 39.063  44.933  1.00 65.10  ?  81  ASN B CA  1 
ATOM   5855  C  C   . ASN B  2  81  ? 102.199 37.628  44.478  1.00 64.38  ?  81  ASN B C   1 
ATOM   5856  O  O   . ASN B  2  81  ? 102.158 37.341  43.280  1.00 66.21  ?  81  ASN B O   1 
ATOM   5857  C  CB  . ASN B  2  81  ? 103.237 39.811  45.172  1.00 49.07  ?  81  ASN B CB  1 
ATOM   5858  C  CG  . ASN B  2  81  ? 103.058 41.312  45.250  1.00 58.88  ?  81  ASN B CG  1 
ATOM   5859  O  OD1 . ASN B  2  81  ? 102.031 41.866  44.825  1.00 50.18  ?  81  ASN B OD1 1 
ATOM   5860  N  ND2 . ASN B  2  81  ? 104.051 42.009  45.796  1.00 51.51  ?  81  ASN B ND2 1 
ATOM   5861  N  N   . PHE B  2  82  ? 102.460 36.725  45.430  1.00 54.72  ?  82  PHE B N   1 
ATOM   5862  C  CA  . PHE B  2  82  ? 102.715 35.325  45.117  1.00 55.86  ?  82  PHE B CA  1 
ATOM   5863  C  C   . PHE B  2  82  ? 101.457 34.668  44.555  1.00 59.58  ?  82  PHE B C   1 
ATOM   5864  O  O   . PHE B  2  82  ? 101.532 33.942  43.567  1.00 65.02  ?  82  PHE B O   1 
ATOM   5865  C  CB  . PHE B  2  82  ? 103.185 34.578  46.373  1.00 44.91  ?  82  PHE B CB  1 
ATOM   5866  C  CG  . PHE B  2  82  ? 103.426 33.107  46.147  1.00 56.29  ?  82  PHE B CG  1 
ATOM   5867  C  CD1 . PHE B  2  82  ? 104.644 32.655  45.676  1.00 46.75  ?  82  PHE B CD1 1 
ATOM   5868  C  CD2 . PHE B  2  82  ? 102.436 32.176  46.414  1.00 59.62  ?  82  PHE B CD2 1 
ATOM   5869  C  CE1 . PHE B  2  82  ? 104.866 31.302  45.469  1.00 50.73  ?  82  PHE B CE1 1 
ATOM   5870  C  CE2 . PHE B  2  82  ? 102.659 30.823  46.204  1.00 54.54  ?  82  PHE B CE2 1 
ATOM   5871  C  CZ  . PHE B  2  82  ? 103.871 30.394  45.730  1.00 59.88  ?  82  PHE B CZ  1 
ATOM   5872  N  N   . ALA B  2  83  ? 100.301 34.913  45.182  1.00 55.89  ?  83  ALA B N   1 
ATOM   5873  C  CA  . ALA B  2  83  ? 99.046  34.327  44.728  1.00 55.36  ?  83  ALA B CA  1 
ATOM   5874  C  C   . ALA B  2  83  ? 98.704  34.773  43.312  1.00 58.87  ?  83  ALA B C   1 
ATOM   5875  O  O   . ALA B  2  83  ? 98.217  33.959  42.532  1.00 64.97  ?  83  ALA B O   1 
ATOM   5876  C  CB  . ALA B  2  83  ? 97.921  34.692  45.680  1.00 48.44  ?  83  ALA B CB  1 
ATOM   5877  N  N   . ARG B  2  84  ? 98.968  36.041  42.963  1.00 49.48  ?  84  ARG B N   1 
ATOM   5878  C  CA  . ARG B  2  84  ? 98.667  36.518  41.610  1.00 57.09  ?  84  ARG B CA  1 
ATOM   5879  C  C   . ARG B  2  84  ? 99.525  35.791  40.567  1.00 51.60  ?  84  ARG B C   1 
ATOM   5880  O  O   . ARG B  2  84  ? 99.060  35.563  39.456  1.00 48.10  ?  84  ARG B O   1 
ATOM   5881  C  CB  . ARG B  2  84  ? 98.811  38.047  41.506  1.00 54.52  ?  84  ARG B CB  1 
ATOM   5882  C  CG  . ARG B  2  84  ? 97.696  38.801  42.234  1.00 67.16  ?  84  ARG B CG  1 
ATOM   5883  C  CD  . ARG B  2  84  ? 97.326  40.122  41.581  1.00 58.38  ?  84  ARG B CD  1 
ATOM   5884  N  NE  . ARG B  2  84  ? 96.095  40.670  42.152  1.00 67.27  ?  84  ARG B NE  1 
ATOM   5885  C  CZ  . ARG B  2  84  ? 95.640  41.901  41.936  1.00 70.84  ?  84  ARG B CZ  1 
ATOM   5886  N  NH1 . ARG B  2  84  ? 96.314  42.738  41.154  1.00 66.68  ?  84  ARG B NH1 1 
ATOM   5887  N  NH2 . ARG B  2  84  ? 94.509  42.305  42.499  1.00 58.53  ?  84  ARG B NH2 1 
ATOM   5888  N  N   . MET B  2  85  ? 100.751 35.392  40.925  1.00 51.14  ?  85  MET B N   1 
ATOM   5889  C  CA  . MET B  2  85  ? 101.611 34.650  40.003  1.00 47.20  ?  85  MET B CA  1 
ATOM   5890  C  C   . MET B  2  85  ? 100.963 33.285  39.711  1.00 59.85  ?  85  MET B C   1 
ATOM   5891  O  O   . MET B  2  85  ? 100.964 32.828  38.568  1.00 57.58  ?  85  MET B O   1 
ATOM   5892  C  CB  . MET B  2  85  ? 103.004 34.440  40.613  1.00 47.73  ?  85  MET B CB  1 
ATOM   5893  C  CG  . MET B  2  85  ? 103.758 35.722  40.841  1.00 61.87  ?  85  MET B CG  1 
ATOM   5894  S  SD  . MET B  2  85  ? 105.517 35.435  41.126  1.00 65.75  ?  85  MET B SD  1 
ATOM   5895  C  CE  . MET B  2  85  ? 106.144 35.637  39.464  1.00 70.76  ?  85  MET B CE  1 
ATOM   5896  N  N   . VAL B  2  86  ? 100.403 32.645  40.752  1.00 51.52  ?  86  VAL B N   1 
ATOM   5897  C  CA  . VAL B  2  86  ? 99.738  31.353  40.620  1.00 51.89  ?  86  VAL B CA  1 
ATOM   5898  C  C   . VAL B  2  86  ? 98.481  31.518  39.758  1.00 59.54  ?  86  VAL B C   1 
ATOM   5899  O  O   . VAL B  2  86  ? 98.256  30.722  38.849  1.00 66.88  ?  86  VAL B O   1 
ATOM   5900  C  CB  . VAL B  2  86  ? 99.402  30.770  42.009  1.00 46.75  ?  86  VAL B CB  1 
ATOM   5901  C  CG1 . VAL B  2  86  ? 98.492  29.550  41.894  1.00 44.38  ?  86  VAL B CG1 1 
ATOM   5902  C  CG2 . VAL B  2  86  ? 100.675 30.423  42.772  1.00 63.69  ?  86  VAL B CG2 1 
ATOM   5903  N  N   . ALA B  2  87  ? 97.674  32.560  40.029  1.00 51.30  ?  87  ALA B N   1 
ATOM   5904  C  CA  . ALA B  2  87  ? 96.454  32.827  39.273  1.00 45.82  ?  87  ALA B CA  1 
ATOM   5905  C  C   . ALA B  2  87  ? 96.768  33.026  37.793  1.00 55.64  ?  87  ALA B C   1 
ATOM   5906  O  O   . ALA B  2  87  ? 96.059  32.491  36.945  1.00 64.99  ?  87  ALA B O   1 
ATOM   5907  C  CB  . ALA B  2  87  ? 95.756  34.061  39.829  1.00 51.63  ?  87  ALA B CB  1 
ATOM   5908  N  N   . ALA B  2  88  ? 97.841  33.775  37.484  1.00 50.69  ?  88  ALA B N   1 
ATOM   5909  C  CA  . ALA B  2  88  ? 98.243  34.024  36.106  1.00 50.60  ?  88  ALA B CA  1 
ATOM   5910  C  C   . ALA B  2  88  ? 98.748  32.737  35.454  1.00 51.71  ?  88  ALA B C   1 
ATOM   5911  O  O   . ALA B  2  88  ? 98.385  32.444  34.318  1.00 49.70  ?  88  ALA B O   1 
ATOM   5912  C  CB  . ALA B  2  88  ? 99.316  35.097  36.065  1.00 49.90  ?  88  ALA B CB  1 
ATOM   5913  N  N   . GLY B  2  89  ? 99.556  31.968  36.180  1.00 54.51  ?  89  GLY B N   1 
ATOM   5914  C  CA  . GLY B  2  89  ? 100.085 30.707  35.680  1.00 48.69  ?  89  GLY B CA  1 
ATOM   5915  C  C   . GLY B  2  89  ? 98.971  29.729  35.375  1.00 47.38  ?  89  GLY B C   1 
ATOM   5916  O  O   . GLY B  2  89  ? 99.000  29.043  34.352  1.00 56.57  ?  89  GLY B O   1 
ATOM   5917  N  N   . THR B  2  90  ? 97.969  29.678  36.263  1.00 50.61  ?  90  THR B N   1 
ATOM   5918  C  CA  . THR B  2  90  ? 96.803  28.806  36.111  1.00 54.73  ?  90  THR B CA  1 
ATOM   5919  C  C   . THR B  2  90  ? 95.975  29.257  34.915  1.00 61.59  ?  90  THR B C   1 
ATOM   5920  O  O   . THR B  2  90  ? 95.474  28.421  34.165  1.00 69.64  ?  90  THR B O   1 
ATOM   5921  C  CB  . THR B  2  90  ? 95.955  28.834  37.382  1.00 57.94  ?  90  THR B CB  1 
ATOM   5922  O  OG1 . THR B  2  90  ? 96.733  28.320  38.462  1.00 69.30  ?  90  THR B OG1 1 
ATOM   5923  C  CG2 . THR B  2  90  ? 94.674  28.036  37.244  1.00 57.62  ?  90  THR B CG2 1 
ATOM   5924  N  N   . ALA B  2  91  ? 95.827  30.578  34.735  1.00 55.68  ?  91  ALA B N   1 
ATOM   5925  C  CA  . ALA B  2  91  ? 95.073  31.126  33.616  1.00 54.05  ?  91  ALA B CA  1 
ATOM   5926  C  C   . ALA B  2  91  ? 95.711  30.732  32.292  1.00 57.27  ?  91  ALA B C   1 
ATOM   5927  O  O   . ALA B  2  91  ? 94.994  30.382  31.358  1.00 57.60  ?  91  ALA B O   1 
ATOM   5928  C  CB  . ALA B  2  91  ? 95.002  32.643  33.726  1.00 53.41  ?  91  ALA B CB  1 
ATOM   5929  N  N   . ALA B  2  92  ? 97.055  30.773  32.207  1.00 53.59  ?  92  ALA B N   1 
ATOM   5930  C  CA  . ALA B  2  92  ? 97.755  30.422  30.978  1.00 46.09  ?  92  ALA B CA  1 
ATOM   5931  C  C   . ALA B  2  92  ? 97.447  28.983  30.572  1.00 54.38  ?  92  ALA B C   1 
ATOM   5932  O  O   . ALA B  2  92  ? 97.103  28.740  29.421  1.00 61.61  ?  92  ALA B O   1 
ATOM   5933  C  CB  . ALA B  2  92  ? 99.251  30.627  31.146  1.00 44.52  ?  92  ALA B CB  1 
ATOM   5934  N  N   . HIS B  2  93  ? 97.526  28.037  31.517  1.00 50.83  ?  93  HIS B N   1 
ATOM   5935  C  CA  . HIS B  2  93  ? 97.227  26.639  31.223  1.00 50.85  ?  93  HIS B CA  1 
ATOM   5936  C  C   . HIS B  2  93  ? 95.728  26.429  31.003  1.00 58.97  ?  93  HIS B C   1 
ATOM   5937  O  O   . HIS B  2  93  ? 95.345  25.587  30.193  1.00 65.73  ?  93  HIS B O   1 
ATOM   5938  C  CB  . HIS B  2  93  ? 97.736  25.735  32.350  1.00 42.16  ?  93  HIS B CB  1 
ATOM   5939  C  CG  . HIS B  2  93  ? 99.224  25.586  32.369  1.00 51.20  ?  93  HIS B CG  1 
ATOM   5940  N  ND1 . HIS B  2  93  ? 99.941  25.659  33.547  1.00 66.60  ?  93  HIS B ND1 1 
ATOM   5941  C  CD2 . HIS B  2  93  ? 100.086 25.373  31.347  1.00 61.46  ?  93  HIS B CD2 1 
ATOM   5942  C  CE1 . HIS B  2  93  ? 101.210 25.479  33.213  1.00 66.03  ?  93  HIS B CE1 1 
ATOM   5943  N  NE2 . HIS B  2  93  ? 101.346 25.311  31.897  1.00 72.09  ?  93  HIS B NE2 1 
ATOM   5944  N  N   . SER B  2  94  ? 94.882  27.196  31.711  1.00 57.06  ?  94  SER B N   1 
ATOM   5945  C  CA  . SER B  2  94  ? 93.427  27.114  31.580  1.00 62.54  ?  94  SER B CA  1 
ATOM   5946  C  C   . SER B  2  94  ? 93.001  27.377  30.129  1.00 59.97  ?  94  SER B C   1 
ATOM   5947  O  O   . SER B  2  94  ? 92.289  26.560  29.554  1.00 61.93  ?  94  SER B O   1 
ATOM   5948  C  CB  . SER B  2  94  ? 92.753  28.124  32.508  1.00 57.60  ?  94  SER B CB  1 
ATOM   5949  O  OG  . SER B  2  94  ? 91.358  28.233  32.268  1.00 60.57  ?  94  SER B OG  1 
ATOM   5950  N  N   . ASP B  2  95  ? 93.488  28.466  29.534  1.00 51.38  ?  95  ASP B N   1 
ATOM   5951  C  CA  . ASP B  2  95  ? 93.089  28.815  28.144  1.00 59.20  ?  95  ASP B CA  1 
ATOM   5952  C  C   . ASP B  2  95  ? 93.635  27.771  27.167  1.00 63.06  ?  95  ASP B C   1 
ATOM   5953  O  O   . ASP B  2  95  ? 92.993  27.553  26.123  1.00 74.65  ?  95  ASP B O   1 
ATOM   5954  C  CB  . ASP B  2  95  ? 93.549  30.225  27.776  1.00 51.52  ?  95  ASP B CB  1 
ATOM   5955  C  CG  . ASP B  2  95  ? 92.426  31.237  27.881  1.00 60.76  ?  95  ASP B CG  1 
ATOM   5956  O  OD1 . ASP B  2  95  ? 91.320  30.817  28.248  1.00 66.90  ?  95  ASP B OD1 1 
ATOM   5957  O  OD2 . ASP B  2  95  ? 92.670  32.424  27.597  1.00 76.36  ?  95  ASP B OD2 1 
ATOM   5958  N  N   . HIS B  2  96  ? 94.770  27.155  27.494  1.00 53.68  ?  96  HIS B N   1 
ATOM   5959  C  CA  . HIS B  2  96  ? 95.393  26.177  26.614  1.00 57.16  ?  96  HIS B CA  1 
ATOM   5960  C  C   . HIS B  2  96  ? 94.450  24.970  26.563  1.00 55.68  ?  96  HIS B C   1 
ATOM   5961  O  O   . HIS B  2  96  ? 93.968  24.625  25.488  1.00 61.00  ?  96  HIS B O   1 
ATOM   5962  C  CB  . HIS B  2  96  ? 96.811  25.842  27.124  1.00 48.66  ?  96  HIS B CB  1 
ATOM   5963  C  CG  . HIS B  2  96  ? 97.510  24.715  26.420  1.00 45.52  ?  96  HIS B CG  1 
ATOM   5964  N  ND1 . HIS B  2  96  ? 96.902  23.483  26.230  1.00 66.05  ?  96  HIS B ND1 1 
ATOM   5965  C  CD2 . HIS B  2  96  ? 98.773  24.651  25.944  1.00 55.15  ?  96  HIS B CD2 1 
ATOM   5966  C  CE1 . HIS B  2  96  ? 97.796  22.722  25.619  1.00 42.48  ?  96  HIS B CE1 1 
ATOM   5967  N  NE2 . HIS B  2  96  ? 98.939  23.380  25.427  1.00 83.05  ?  96  HIS B NE2 1 
ATOM   5968  N  N   . GLY B  2  97  ? 94.169  24.368  27.716  1.00 53.34  ?  97  GLY B N   1 
ATOM   5969  C  CA  . GLY B  2  97  ? 93.289  23.209  27.797  1.00 51.06  ?  97  GLY B CA  1 
ATOM   5970  C  C   . GLY B  2  97  ? 91.874  23.467  27.319  1.00 56.64  ?  97  GLY B C   1 
ATOM   5971  O  O   . GLY B  2  97  ? 91.246  22.589  26.723  1.00 56.75  ?  97  GLY B O   1 
ATOM   5972  N  N   . ARG B  2  98  ? 91.354  24.672  27.584  1.00 50.46  ?  98  ARG B N   1 
ATOM   5973  C  CA  . ARG B  2  98  ? 90.003  25.064  27.172  1.00 48.51  ?  98  ARG B CA  1 
ATOM   5974  C  C   . ARG B  2  98  ? 89.904  25.036  25.649  1.00 56.88  ?  98  ARG B C   1 
ATOM   5975  O  O   . ARG B  2  98  ? 88.899  24.591  25.100  1.00 55.36  ?  98  ARG B O   1 
ATOM   5976  C  CB  . ARG B  2  98  ? 89.697  26.473  27.688  1.00 48.97  ?  98  ARG B CB  1 
ATOM   5977  C  CG  . ARG B  2  98  ? 88.285  26.970  27.412  1.00 40.60  ?  98  ARG B CG  1 
ATOM   5978  C  CD  . ARG B  2  98  ? 88.231  28.486  27.298  1.00 55.19  ?  98  ARG B CD  1 
ATOM   5979  N  NE  . ARG B  2  98  ? 89.061  29.161  28.301  1.00 51.14  ?  98  ARG B NE  1 
ATOM   5980  C  CZ  . ARG B  2  98  ? 88.719  29.340  29.574  1.00 50.83  ?  98  ARG B CZ  1 
ATOM   5981  N  NH1 . ARG B  2  98  ? 87.550  28.900  30.024  1.00 56.54  ?  98  ARG B NH1 1 
ATOM   5982  N  NH2 . ARG B  2  98  ? 89.545  29.960  30.408  1.00 57.46  ?  98  ARG B NH2 1 
ATOM   5983  N  N   . SER B  2  99  ? 90.950  25.509  24.967  1.00 60.87  ?  99  SER B N   1 
ATOM   5984  C  CA  . SER B  2  99  ? 90.983  25.512  23.512  1.00 55.77  ?  99  SER B CA  1 
ATOM   5985  C  C   . SER B  2  99  ? 90.990  24.072  22.980  1.00 52.46  ?  99  SER B C   1 
ATOM   5986  O  O   . SER B  2  99  ? 90.396  23.804  21.939  1.00 56.16  ?  99  SER B O   1 
ATOM   5987  C  CB  . SER B  2  99  ? 92.222  26.257  23.019  1.00 51.52  ?  99  SER B CB  1 
ATOM   5988  O  OG  . SER B  2  99  ? 92.051  26.776  21.710  1.00 84.29  ?  99  SER B OG  1 
ATOM   5989  N  N   . ILE B  2  100 ? 91.649  23.147  23.703  1.00 60.83  ?  100 ILE B N   1 
ATOM   5990  C  CA  . ILE B  2  100 ? 91.734  21.737  23.319  1.00 48.38  ?  100 ILE B CA  1 
ATOM   5991  C  C   . ILE B  2  100 ? 90.352  21.117  23.480  1.00 61.47  ?  100 ILE B C   1 
ATOM   5992  O  O   . ILE B  2  100 ? 89.888  20.408  22.587  1.00 68.11  ?  100 ILE B O   1 
ATOM   5993  C  CB  . ILE B  2  100 ? 92.777  20.961  24.178  1.00 50.42  ?  100 ILE B CB  1 
ATOM   5994  C  CG1 . ILE B  2  100 ? 94.146  21.665  24.257  1.00 51.27  ?  100 ILE B CG1 1 
ATOM   5995  C  CG2 . ILE B  2  100 ? 92.943  19.536  23.677  1.00 67.68  ?  100 ILE B CG2 1 
ATOM   5996  C  CD1 . ILE B  2  100 ? 94.763  22.066  22.973  1.00 62.18  ?  100 ILE B CD1 1 
ATOM   5997  N  N   . ALA B  2  101 ? 89.687  21.383  24.616  1.00 55.15  ?  101 ALA B N   1 
ATOM   5998  C  CA  . ALA B  2  101 ? 88.352  20.848  24.865  1.00 55.20  ?  101 ALA B CA  1 
ATOM   5999  C  C   . ALA B  2  101 ? 87.361  21.321  23.794  1.00 59.95  ?  101 ALA B C   1 
ATOM   6000  O  O   . ALA B  2  101 ? 86.513  20.541  23.366  1.00 59.58  ?  101 ALA B O   1 
ATOM   6001  C  CB  . ALA B  2  101 ? 87.876  21.260  26.246  1.00 49.90  ?  101 ALA B CB  1 
ATOM   6002  N  N   . LEU B  2  102 ? 87.478  22.579  23.342  1.00 61.55  ?  102 LEU B N   1 
ATOM   6003  C  CA  . LEU B  2  102 ? 86.591  23.094  22.302  1.00 48.76  ?  102 LEU B CA  1 
ATOM   6004  C  C   . LEU B  2  102 ? 86.864  22.384  20.983  1.00 62.11  ?  102 LEU B C   1 
ATOM   6005  O  O   . LEU B  2  102 ? 85.932  22.153  20.219  1.00 70.30  ?  102 LEU B O   1 
ATOM   6006  C  CB  . LEU B  2  102 ? 86.748  24.611  22.148  1.00 42.00  ?  102 LEU B CB  1 
ATOM   6007  C  CG  . LEU B  2  102 ? 86.121  25.458  23.264  1.00 42.46  ?  102 LEU B CG  1 
ATOM   6008  C  CD1 . LEU B  2  102 ? 86.741  26.834  23.333  1.00 41.87  ?  102 LEU B CD1 1 
ATOM   6009  C  CD2 . LEU B  2  102 ? 84.620  25.577  23.087  1.00 43.93  ?  102 LEU B CD2 1 
ATOM   6010  N  N   . SER B  2  103 ? 88.126  22.020  20.713  1.00 59.19  ?  103 SER B N   1 
ATOM   6011  C  CA  . SER B  2  103 ? 88.475  21.305  19.489  1.00 57.90  ?  103 SER B CA  1 
ATOM   6012  C  C   . SER B  2  103 ? 87.858  19.911  19.535  1.00 59.69  ?  103 SER B C   1 
ATOM   6013  O  O   . SER B  2  103 ? 87.292  19.459  18.541  1.00 67.01  ?  103 SER B O   1 
ATOM   6014  C  CB  . SER B  2  103 ? 89.991  21.210  19.332  1.00 54.76  ?  103 SER B CB  1 
ATOM   6015  O  OG  . SER B  2  103 ? 90.557  22.458  18.964  1.00 60.97  ?  103 SER B OG  1 
ATOM   6016  N  N   . LEU B  2  104 ? 87.939  19.238  20.695  1.00 60.96  ?  104 LEU B N   1 
ATOM   6017  C  CA  . LEU B  2  104 ? 87.357  17.907  20.883  1.00 54.88  ?  104 LEU B CA  1 
ATOM   6018  C  C   . LEU B  2  104 ? 85.838  17.938  20.619  1.00 64.14  ?  104 LEU B C   1 
ATOM   6019  O  O   . LEU B  2  104 ? 85.270  16.952  20.153  1.00 66.48  ?  104 LEU B O   1 
ATOM   6020  C  CB  . LEU B  2  104 ? 87.649  17.410  22.309  1.00 48.50  ?  104 LEU B CB  1 
ATOM   6021  C  CG  . LEU B  2  104 ? 87.249  15.973  22.635  1.00 48.44  ?  104 LEU B CG  1 
ATOM   6022  C  CD1 . LEU B  2  104 ? 88.091  14.971  21.853  1.00 52.42  ?  104 LEU B CD1 1 
ATOM   6023  C  CD2 . LEU B  2  104 ? 87.385  15.706  24.123  1.00 54.68  ?  104 LEU B CD2 1 
ATOM   6024  N  N   . TYR B  2  105 ? 85.191  19.079  20.910  1.00 61.99  ?  105 TYR B N   1 
ATOM   6025  C  CA  . TYR B  2  105 ? 83.760  19.281  20.693  1.00 54.89  ?  105 TYR B CA  1 
ATOM   6026  C  C   . TYR B  2  105 ? 83.431  19.484  19.203  1.00 64.82  ?  105 TYR B C   1 
ATOM   6027  O  O   . TYR B  2  105 ? 82.270  19.366  18.822  1.00 66.14  ?  105 TYR B O   1 
ATOM   6028  C  CB  . TYR B  2  105 ? 83.295  20.500  21.503  1.00 51.87  ?  105 TYR B CB  1 
ATOM   6029  C  CG  . TYR B  2  105 ? 81.799  20.720  21.498  1.00 65.33  ?  105 TYR B CG  1 
ATOM   6030  C  CD1 . TYR B  2  105 ? 80.954  19.897  22.227  1.00 67.44  ?  105 TYR B CD1 1 
ATOM   6031  C  CD2 . TYR B  2  105 ? 81.234  21.784  20.809  1.00 63.95  ?  105 TYR B CD2 1 
ATOM   6032  C  CE1 . TYR B  2  105 ? 79.580  20.098  22.235  1.00 67.41  ?  105 TYR B CE1 1 
ATOM   6033  C  CE2 . TYR B  2  105 ? 79.861  21.998  20.813  1.00 61.44  ?  105 TYR B CE2 1 
ATOM   6034  C  CZ  . TYR B  2  105 ? 79.036  21.151  21.529  1.00 66.00  ?  105 TYR B CZ  1 
ATOM   6035  O  OH  . TYR B  2  105 ? 77.675  21.345  21.556  1.00 74.42  ?  105 TYR B OH  1 
ATOM   6036  N  N   . HIS B  2  106 ? 84.432  19.792  18.360  1.00 60.74  ?  106 HIS B N   1 
ATOM   6037  C  CA  . HIS B  2  106 ? 84.207  20.010  16.934  1.00 68.39  ?  106 HIS B CA  1 
ATOM   6038  C  C   . HIS B  2  106 ? 84.881  18.955  16.064  1.00 62.34  ?  106 HIS B C   1 
ATOM   6039  O  O   . HIS B  2  106 ? 85.270  19.252  14.938  1.00 73.41  ?  106 HIS B O   1 
ATOM   6040  C  CB  . HIS B  2  106 ? 84.695  21.408  16.540  1.00 57.35  ?  106 HIS B CB  1 
ATOM   6041  C  CG  . HIS B  2  106 ? 84.044  22.498  17.325  1.00 62.15  ?  106 HIS B CG  1 
ATOM   6042  N  ND1 . HIS B  2  106 ? 84.787  23.496  17.925  1.00 81.15  ?  106 HIS B ND1 1 
ATOM   6043  C  CD2 . HIS B  2  106 ? 82.733  22.705  17.595  1.00 78.81  ?  106 HIS B CD2 1 
ATOM   6044  C  CE1 . HIS B  2  106 ? 83.911  24.283  18.533  1.00 97.96  ?  106 HIS B CE1 1 
ATOM   6045  N  NE2 . HIS B  2  106 ? 82.661  23.845  18.360  1.00 88.49  ?  106 HIS B NE2 1 
ATOM   6046  N  N   . THR B  2  107 ? 85.002  17.723  16.562  1.00 55.58  ?  107 THR B N   1 
ATOM   6047  C  CA  . THR B  2  107 ? 85.626  16.649  15.791  1.00 58.52  ?  107 THR B CA  1 
ATOM   6048  C  C   . THR B  2  107 ? 84.606  16.041  14.824  1.00 66.87  ?  107 THR B C   1 
ATOM   6049  O  O   . THR B  2  107 ? 83.402  16.148  15.046  1.00 72.52  ?  107 THR B O   1 
ATOM   6050  C  CB  . THR B  2  107 ? 86.228  15.595  16.728  1.00 59.36  ?  107 THR B CB  1 
ATOM   6051  O  OG1 . THR B  2  107 ? 85.209  15.074  17.586  1.00 73.28  ?  107 THR B OG1 1 
ATOM   6052  C  CG2 . THR B  2  107 ? 87.376  16.144  17.551  1.00 60.32  ?  107 THR B CG2 1 
ATOM   6053  N  N   . SER B  2  108 ? 85.111  15.412  13.758  1.00 68.11  ?  108 SER B N   1 
ATOM   6054  C  CA  . SER B  2  108 ? 84.219  14.810  12.734  1.00 62.02  ?  108 SER B CA  1 
ATOM   6055  C  C   . SER B  2  108 ? 84.927  13.639  12.047  1.00 65.59  ?  108 SER B C   1 
ATOM   6056  O  O   . SER B  2  108 ? 86.167  13.670  11.963  1.00 74.84  ?  108 SER B O   1 
ATOM   6057  C  CB  . SER B  2  108 ? 83.787  15.844  11.732  1.00 58.51  ?  108 SER B CB  1 
ATOM   6058  O  OG  . SER B  2  108 ? 82.983  16.839  12.347  1.00 107.60 ?  108 SER B OG  1 
ATOM   6059  N  N   . LYS B  2  109 ? 84.163  12.654  11.571  1.00 70.29  ?  109 LYS B N   1 
ATOM   6060  C  CA  . LYS B  2  109 ? 84.740  11.486  10.907  1.00 74.32  ?  109 LYS B CA  1 
ATOM   6061  C  C   . LYS B  2  109 ? 85.533  11.936  9.675   1.00 88.05  ?  109 LYS B C   1 
ATOM   6062  O  O   . LYS B  2  109 ? 86.663  11.491  9.469   1.00 83.35  ?  109 LYS B O   1 
ATOM   6063  C  CB  . LYS B  2  109 ? 83.625  10.508  10.502  1.00 83.37  ?  109 LYS B CB  1 
ATOM   6064  C  CG  . LYS B  2  109 ? 84.108  9.289   9.716   1.00 94.40  ?  109 LYS B CG  1 
ATOM   6065  C  CD  . LYS B  2  109 ? 82.952  8.381   9.272   1.00 105.32 ?  109 LYS B CD  1 
ATOM   6066  C  CE  . LYS B  2  109 ? 82.044  9.015   8.235   1.00 93.43  ?  109 LYS B CE  1 
ATOM   6067  N  NZ  . LYS B  2  109 ? 81.597  8.037   7.206   1.00 101.64 ?  109 LYS B NZ  1 
ATOM   6068  N  N   . ASP B  2  110 ? 84.939  12.831  8.872   1.00 101.32 ?  110 ASP B N   1 
ATOM   6069  C  CA  . ASP B  2  110 ? 85.572  13.368  7.671   1.00 98.86  ?  110 ASP B CA  1 
ATOM   6070  C  C   . ASP B  2  110 ? 85.917  14.848  7.890   1.00 97.20  ?  110 ASP B C   1 
ATOM   6071  O  O   . ASP B  2  110 ? 85.716  15.677  7.000   1.00 108.39 ?  110 ASP B O   1 
ATOM   6072  C  CB  . ASP B  2  110 ? 84.633  13.202  6.464   1.00 106.92 ?  110 ASP B CB  1 
ATOM   6073  C  CG  . ASP B  2  110 ? 84.194  11.769  6.245   1.00 106.42 ?  110 ASP B CG  1 
ATOM   6074  O  OD1 . ASP B  2  110 ? 85.067  10.869  6.278   1.00 110.99 ?  110 ASP B OD1 1 
ATOM   6075  O  OD2 . ASP B  2  110 ? 82.979  11.544  6.041   1.00 100.28 ?  110 ASP B OD2 1 
ATOM   6076  N  N   . GLY B  2  111 ? 86.433  15.157  9.074   1.00 80.86  ?  111 GLY B N   1 
ATOM   6077  C  CA  . GLY B  2  111 ? 86.814  16.510  9.448   1.00 79.06  ?  111 GLY B CA  1 
ATOM   6078  C  C   . GLY B  2  111 ? 88.306  16.628  9.660   1.00 67.42  ?  111 GLY B C   1 
ATOM   6079  O  O   . GLY B  2  111 ? 89.007  15.619  9.735   1.00 74.69  ?  111 GLY B O   1 
ATOM   6080  N  N   . ASP B  2  112 ? 88.807  17.860  9.750   1.00 75.91  ?  112 ASP B N   1 
ATOM   6081  C  CA  . ASP B  2  112 ? 90.234  18.096  9.950   1.00 55.43  ?  112 ASP B CA  1 
ATOM   6082  C  C   . ASP B  2  112 ? 90.707  17.526  11.293  1.00 55.66  ?  112 ASP B C   1 
ATOM   6083  O  O   . ASP B  2  112 ? 91.760  16.895  11.344  1.00 62.29  ?  112 ASP B O   1 
ATOM   6084  C  CB  . ASP B  2  112 ? 90.541  19.601  9.850   1.00 59.76  ?  112 ASP B CB  1 
ATOM   6085  C  CG  . ASP B  2  112 ? 90.801  20.099  8.438   1.00 70.53  ?  112 ASP B CG  1 
ATOM   6086  O  OD1 . ASP B  2  112 ? 90.878  19.257  7.512   1.00 72.04  ?  112 ASP B OD1 1 
ATOM   6087  O  OD2 . ASP B  2  112 ? 90.931  21.331  8.257   1.00 63.58  ?  112 ASP B OD2 1 
ATOM   6088  N  N   . ILE B  2  113 ? 89.925  17.725  12.367  1.00 56.07  ?  113 ILE B N   1 
ATOM   6089  C  CA  . ILE B  2  113 ? 90.261  17.213  13.700  1.00 53.10  ?  113 ILE B CA  1 
ATOM   6090  C  C   . ILE B  2  113 ? 89.449  15.944  13.938  1.00 62.21  ?  113 ILE B C   1 
ATOM   6091  O  O   . ILE B  2  113 ? 88.219  15.981  13.894  1.00 60.27  ?  113 ILE B O   1 
ATOM   6092  C  CB  . ILE B  2  113 ? 89.992  18.264  14.799  1.00 53.69  ?  113 ILE B CB  1 
ATOM   6093  C  CG1 . ILE B  2  113 ? 90.647  19.605  14.437  1.00 49.53  ?  113 ILE B CG1 1 
ATOM   6094  C  CG2 . ILE B  2  113 ? 90.499  17.762  16.157  1.00 66.62  ?  113 ILE B CG2 1 
ATOM   6095  C  CD1 . ILE B  2  113 ? 90.223  20.766  15.304  1.00 77.62  ?  113 ILE B CD1 1 
ATOM   6096  N  N   . LYS B  2  114 ? 90.133  14.825  14.186  1.00 58.50  ?  114 LYS B N   1 
ATOM   6097  C  CA  . LYS B  2  114 ? 89.478  13.536  14.381  1.00 59.55  ?  114 LYS B CA  1 
ATOM   6098  C  C   . LYS B  2  114 ? 89.853  12.892  15.723  1.00 61.86  ?  114 LYS B C   1 
ATOM   6099  O  O   . LYS B  2  114 ? 90.677  13.433  16.459  1.00 69.91  ?  114 LYS B O   1 
ATOM   6100  C  CB  . LYS B  2  114 ? 89.884  12.606  13.220  1.00 63.19  ?  114 LYS B CB  1 
ATOM   6101  C  CG  . LYS B  2  114 ? 89.522  13.144  11.840  1.00 67.58  ?  114 LYS B CG  1 
ATOM   6102  C  CD  . LYS B  2  114 ? 90.364  12.512  10.737  1.00 73.41  ?  114 LYS B CD  1 
ATOM   6103  C  CE  . LYS B  2  114 ? 89.822  12.777  9.349   1.00 83.86  ?  114 LYS B CE  1 
ATOM   6104  N  NZ  . LYS B  2  114 ? 89.931  11.581  8.471   1.00 96.94  ?  114 LYS B NZ  1 
ATOM   6105  N  N   . VAL B  2  115 ? 89.237  11.740  16.042  1.00 60.49  ?  115 VAL B N   1 
ATOM   6106  C  CA  . VAL B  2  115 ? 89.516  10.981  17.261  1.00 53.89  ?  115 VAL B CA  1 
ATOM   6107  C  C   . VAL B  2  115 ? 90.522  9.893   16.867  1.00 64.29  ?  115 VAL B C   1 
ATOM   6108  O  O   . VAL B  2  115 ? 90.115  8.822   16.411  1.00 77.96  ?  115 VAL B O   1 
ATOM   6109  C  CB  . VAL B  2  115 ? 88.225  10.360  17.849  1.00 47.29  ?  115 VAL B CB  1 
ATOM   6110  C  CG1 . VAL B  2  115 ? 88.541  9.487   19.054  1.00 56.39  ?  115 VAL B CG1 1 
ATOM   6111  C  CG2 . VAL B  2  115 ? 87.224  11.442  18.227  1.00 50.83  ?  115 VAL B CG2 1 
ATOM   6112  N  N   . LYS B  2  116 ? 91.829  10.170  17.016  1.00 55.02  ?  116 LYS B N   1 
ATOM   6113  C  CA  . LYS B  2  116 ? 92.868  9.208   16.642  1.00 53.60  ?  116 LYS B CA  1 
ATOM   6114  C  C   . LYS B  2  116 ? 93.002  8.056   17.649  1.00 65.86  ?  116 LYS B C   1 
ATOM   6115  O  O   . LYS B  2  116 ? 93.063  6.895   17.238  1.00 68.47  ?  116 LYS B O   1 
ATOM   6116  C  CB  . LYS B  2  116 ? 94.213  9.915   16.437  1.00 50.90  ?  116 LYS B CB  1 
ATOM   6117  C  CG  . LYS B  2  116 ? 94.285  10.703  15.134  1.00 48.40  ?  116 LYS B CG  1 
ATOM   6118  C  CD  . LYS B  2  116 ? 95.672  11.248  14.901  1.00 66.36  ?  116 LYS B CD  1 
ATOM   6119  C  CE  . LYS B  2  116 ? 95.780  12.054  13.636  1.00 56.00  ?  116 LYS B CE  1 
ATOM   6120  N  NZ  . LYS B  2  116 ? 97.017  12.880  13.618  1.00 78.68  ?  116 LYS B NZ  1 
ATOM   6121  N  N   . ASP B  2  117 ? 93.048  8.358   18.956  1.00 62.56  ?  117 ASP B N   1 
ATOM   6122  C  CA  . ASP B  2  117 ? 93.144  7.308   19.973  1.00 58.00  ?  117 ASP B CA  1 
ATOM   6123  C  C   . ASP B  2  117 ? 91.753  7.066   20.549  1.00 57.80  ?  117 ASP B C   1 
ATOM   6124  O  O   . ASP B  2  117 ? 91.312  7.809   21.422  1.00 65.14  ?  117 ASP B O   1 
ATOM   6125  C  CB  . ASP B  2  117 ? 94.136  7.692   21.083  1.00 56.68  ?  117 ASP B CB  1 
ATOM   6126  C  CG  . ASP B  2  117 ? 94.586  6.517   21.930  1.00 74.88  ?  117 ASP B CG  1 
ATOM   6127  O  OD1 . ASP B  2  117 ? 93.732  5.662   22.266  1.00 77.26  ?  117 ASP B OD1 1 
ATOM   6128  O  OD2 . ASP B  2  117 ? 95.789  6.452   22.260  1.00 67.87  ?  117 ASP B OD2 1 
ATOM   6129  N  N   . GLU B  2  118 ? 91.055  6.038   20.054  1.00 63.37  ?  118 GLU B N   1 
ATOM   6130  C  CA  . GLU B  2  118 ? 89.709  5.734   20.533  1.00 60.73  ?  118 GLU B CA  1 
ATOM   6131  C  C   . GLU B  2  118 ? 89.763  5.098   21.914  1.00 75.54  ?  118 GLU B C   1 
ATOM   6132  O  O   . GLU B  2  118 ? 88.922  5.408   22.752  1.00 79.02  ?  118 GLU B O   1 
ATOM   6133  C  CB  . GLU B  2  118 ? 88.961  4.818   19.554  1.00 71.57  ?  118 GLU B CB  1 
ATOM   6134  C  CG  . GLU B  2  118 ? 88.809  5.419   18.167  1.00 81.82  ?  118 GLU B CG  1 
ATOM   6135  C  CD  . GLU B  2  118 ? 87.755  4.774   17.288  1.00 89.36  ?  118 GLU B CD  1 
ATOM   6136  O  OE1 . GLU B  2  118 ? 87.126  3.785   17.729  1.00 91.04  ?  118 GLU B OE1 1 
ATOM   6137  O  OE2 . GLU B  2  118 ? 87.558  5.262   16.151  1.00 90.92  ?  118 GLU B OE2 1 
ATOM   6138  N  N   . ASN B  2  119 ? 90.756  4.226   22.165  1.00 81.38  ?  119 ASN B N   1 
ATOM   6139  C  CA  . ASN B  2  119 ? 90.904  3.562   23.463  1.00 68.72  ?  119 ASN B CA  1 
ATOM   6140  C  C   . ASN B  2  119 ? 91.033  4.581   24.591  1.00 73.07  ?  119 ASN B C   1 
ATOM   6141  O  O   . ASN B  2  119 ? 90.381  4.432   25.626  1.00 79.50  ?  119 ASN B O   1 
ATOM   6142  C  CB  . ASN B  2  119 ? 92.129  2.638   23.467  1.00 79.51  ?  119 ASN B CB  1 
ATOM   6143  C  CG  . ASN B  2  119 ? 91.918  1.316   22.762  1.00 94.70  ?  119 ASN B CG  1 
ATOM   6144  O  OD1 . ASN B  2  119 ? 90.868  0.671   22.893  1.00 96.84  ?  119 ASN B OD1 1 
ATOM   6145  N  ND2 . ASN B  2  119 ? 92.920  0.869   22.006  1.00 109.25 ?  119 ASN B ND2 1 
ATOM   6146  N  N   . LYS B  2  120 ? 91.861  5.619   24.396  1.00 73.67  ?  120 LYS B N   1 
ATOM   6147  C  CA  . LYS B  2  120 ? 92.050  6.639   25.422  1.00 63.34  ?  120 LYS B CA  1 
ATOM   6148  C  C   . LYS B  2  120 ? 90.755  7.385   25.686  1.00 67.53  ?  120 LYS B C   1 
ATOM   6149  O  O   . LYS B  2  120 ? 90.418  7.614   26.844  1.00 78.87  ?  120 LYS B O   1 
ATOM   6150  C  CB  . LYS B  2  120 ? 93.166  7.625   25.040  1.00 67.33  ?  120 LYS B CB  1 
ATOM   6151  C  CG  . LYS B  2  120 ? 93.514  8.600   26.169  1.00 61.58  ?  120 LYS B CG  1 
ATOM   6152  C  CD  . LYS B  2  120 ? 95.003  8.738   26.395  1.00 59.95  ?  120 LYS B CD  1 
ATOM   6153  C  CE  . LYS B  2  120 ? 95.295  9.611   27.586  1.00 59.86  ?  120 LYS B CE  1 
ATOM   6154  N  NZ  . LYS B  2  120 ? 96.754  9.767   27.806  1.00 65.10  ?  120 LYS B NZ  1 
ATOM   6155  N  N   . LEU B  2  121 ? 90.011  7.750   24.633  1.00 64.53  ?  121 LEU B N   1 
ATOM   6156  C  CA  . LEU B  2  121 ? 88.751  8.466   24.817  1.00 63.81  ?  121 LEU B CA  1 
ATOM   6157  C  C   . LEU B  2  121 ? 87.756  7.632   25.616  1.00 73.97  ?  121 LEU B C   1 
ATOM   6158  O  O   . LEU B  2  121 ? 87.030  8.178   26.446  1.00 75.85  ?  121 LEU B O   1 
ATOM   6159  C  CB  . LEU B  2  121 ? 88.141  8.870   23.465  1.00 57.70  ?  121 LEU B CB  1 
ATOM   6160  C  CG  . LEU B  2  121 ? 86.711  9.436   23.505  1.00 62.20  ?  121 LEU B CG  1 
ATOM   6161  C  CD1 . LEU B  2  121 ? 86.657  10.798  24.175  1.00 60.62  ?  121 LEU B CD1 1 
ATOM   6162  C  CD2 . LEU B  2  121 ? 86.133  9.516   22.135  1.00 56.86  ?  121 LEU B CD2 1 
ATOM   6163  N  N   . LYS B  2  122 ? 87.729  6.315   25.380  1.00 76.28  ?  122 LYS B N   1 
ATOM   6164  C  CA  . LYS B  2  122 ? 86.817  5.424   26.089  1.00 62.23  ?  122 LYS B CA  1 
ATOM   6165  C  C   . LYS B  2  122 ? 87.165  5.415   27.574  1.00 76.13  ?  122 LYS B C   1 
ATOM   6166  O  O   . LYS B  2  122 ? 86.268  5.501   28.411  1.00 88.82  ?  122 LYS B O   1 
ATOM   6167  C  CB  . LYS B  2  122 ? 86.879  4.008   25.500  1.00 65.67  ?  122 LYS B CB  1 
ATOM   6168  C  CG  . LYS B  2  122 ? 86.508  3.936   24.011  1.00 75.24  ?  122 LYS B CG  1 
ATOM   6169  C  CD  . LYS B  2  122 ? 85.082  3.451   23.743  1.00 68.17  ?  122 LYS B CD  1 
ATOM   6170  C  CE  . LYS B  2  122 ? 84.912  2.909   22.338  1.00 75.30  ?  122 LYS B CE  1 
ATOM   6171  N  NZ  . LYS B  2  122 ? 85.739  1.692   22.083  1.00 92.65  ?  122 LYS B NZ  1 
ATOM   6172  N  N   . GLU B  2  123 ? 88.465  5.346   27.907  1.00 77.31  ?  123 GLU B N   1 
ATOM   6173  C  CA  . GLU B  2  123 ? 88.894  5.365   29.304  1.00 72.30  ?  123 GLU B CA  1 
ATOM   6174  C  C   . GLU B  2  123 ? 88.609  6.724   29.937  1.00 71.89  ?  123 GLU B C   1 
ATOM   6175  O  O   . GLU B  2  123 ? 88.215  6.781   31.098  1.00 82.63  ?  123 GLU B O   1 
ATOM   6176  C  CB  . GLU B  2  123 ? 90.391  5.027   29.432  1.00 66.17  ?  123 GLU B CB  1 
ATOM   6177  C  CG  . GLU B  2  123 ? 90.705  3.541   29.338  1.00 81.07  ?  123 GLU B CG  1 
ATOM   6178  C  CD  . GLU B  2  123 ? 90.192  2.681   30.481  1.00 114.50 ?  123 GLU B CD  1 
ATOM   6179  O  OE1 . GLU B  2  123 ? 89.820  3.242   31.539  1.00 102.17 ?  123 GLU B OE1 1 
ATOM   6180  O  OE2 . GLU B  2  123 ? 90.162  1.439   30.316  1.00 125.08 ?  123 GLU B OE2 1 
ATOM   6181  N  N   . VAL B  2  124 ? 88.802  7.817   29.187  1.00 68.04  ?  124 VAL B N   1 
ATOM   6182  C  CA  . VAL B  2  124 ? 88.542  9.163   29.698  1.00 59.90  ?  124 VAL B CA  1 
ATOM   6183  C  C   . VAL B  2  124 ? 87.039  9.337   29.942  1.00 71.06  ?  124 VAL B C   1 
ATOM   6184  O  O   . VAL B  2  124 ? 86.649  9.988   30.909  1.00 80.01  ?  124 VAL B O   1 
ATOM   6185  C  CB  . VAL B  2  124 ? 89.117  10.251  28.749  1.00 60.15  ?  124 VAL B CB  1 
ATOM   6186  C  CG1 . VAL B  2  124 ? 88.575  11.635  29.094  1.00 62.19  ?  124 VAL B CG1 1 
ATOM   6187  C  CG2 . VAL B  2  124 ? 90.643  10.255  28.791  1.00 62.30  ?  124 VAL B CG2 1 
ATOM   6188  N  N   . ALA B  2  125 ? 86.195  8.743   29.089  1.00 72.52  ?  125 ALA B N   1 
ATOM   6189  C  CA  . ALA B  2  125 ? 84.745  8.828   29.243  1.00 69.11  ?  125 ALA B CA  1 
ATOM   6190  C  C   . ALA B  2  125 ? 84.302  8.220   30.567  1.00 66.86  ?  125 ALA B C   1 
ATOM   6191  O  O   . ALA B  2  125 ? 83.358  8.715   31.173  1.00 75.65  ?  125 ALA B O   1 
ATOM   6192  C  CB  . ALA B  2  125 ? 84.060  8.117   28.097  1.00 62.83  ?  125 ALA B CB  1 
ATOM   6193  N  N   . LYS B  2  126 ? 84.983  7.162   31.034  1.00 69.16  ?  126 LYS B N   1 
ATOM   6194  C  CA  . LYS B  2  126 ? 84.643  6.535   32.311  1.00 74.49  ?  126 LYS B CA  1 
ATOM   6195  C  C   . LYS B  2  126 ? 84.836  7.554   33.433  1.00 74.52  ?  126 LYS B C   1 
ATOM   6196  O  O   . LYS B  2  126 ? 83.981  7.669   34.309  1.00 103.58 ?  126 LYS B O   1 
ATOM   6197  C  CB  . LYS B  2  126 ? 85.534  5.309   32.587  1.00 82.14  ?  126 LYS B CB  1 
ATOM   6198  C  CG  . LYS B  2  126 ? 85.292  4.119   31.665  1.00 90.25  ?  126 LYS B CG  1 
ATOM   6199  C  CD  . LYS B  2  126 ? 86.307  2.994   31.906  1.00 105.68 ?  126 LYS B CD  1 
ATOM   6200  C  CE  . LYS B  2  126 ? 86.545  2.147   30.671  1.00 111.80 ?  126 LYS B CE  1 
ATOM   6201  N  NZ  . LYS B  2  126 ? 87.524  1.045   30.904  1.00 109.34 ?  126 LYS B NZ  1 
ATOM   6202  N  N   . SER B  2  127 ? 85.944  8.308   33.396  1.00 70.81  ?  127 SER B N   1 
ATOM   6203  C  CA  . SER B  2  127 ? 86.237  9.311   34.412  1.00 71.08  ?  127 SER B CA  1 
ATOM   6204  C  C   . SER B  2  127 ? 85.157  10.386  34.469  1.00 80.83  ?  127 SER B C   1 
ATOM   6205  O  O   . SER B  2  127 ? 84.822  10.845  35.556  1.00 84.55  ?  127 SER B O   1 
ATOM   6206  C  CB  . SER B  2  127 ? 87.598  9.946   34.155  1.00 78.98  ?  127 SER B CB  1 
ATOM   6207  O  OG  . SER B  2  127 ? 88.573  8.960   33.855  1.00 92.54  ?  127 SER B OG  1 
ATOM   6208  N  N   . PHE B  2  128 ? 84.604  10.783  33.317  1.00 81.04  ?  128 PHE B N   1 
ATOM   6209  C  CA  . PHE B  2  128 ? 83.549  11.800  33.278  1.00 82.75  ?  128 PHE B CA  1 
ATOM   6210  C  C   . PHE B  2  128 ? 82.132  11.211  33.349  1.00 85.60  ?  128 PHE B C   1 
ATOM   6211  O  O   . PHE B  2  128 ? 81.161  11.964  33.280  1.00 97.25  ?  128 PHE B O   1 
ATOM   6212  C  CB  . PHE B  2  128 ? 83.697  12.663  32.016  1.00 63.93  ?  128 PHE B CB  1 
ATOM   6213  C  CG  . PHE B  2  128 ? 84.844  13.639  32.091  1.00 62.95  ?  128 PHE B CG  1 
ATOM   6214  C  CD1 . PHE B  2  128 ? 84.703  14.847  32.747  1.00 62.58  ?  128 PHE B CD1 1 
ATOM   6215  C  CD2 . PHE B  2  128 ? 86.066  13.343  31.516  1.00 69.75  ?  128 PHE B CD2 1 
ATOM   6216  C  CE1 . PHE B  2  128 ? 85.758  15.745  32.815  1.00 71.88  ?  128 PHE B CE1 1 
ATOM   6217  C  CE2 . PHE B  2  128 ? 87.120  14.243  31.585  1.00 68.63  ?  128 PHE B CE2 1 
ATOM   6218  C  CZ  . PHE B  2  128 ? 86.960  15.438  32.234  1.00 66.06  ?  128 PHE B CZ  1 
ATOM   6219  N  N   . ASN B  2  129 ? 82.009  9.885   33.507  1.00 82.27  ?  129 ASN B N   1 
ATOM   6220  C  CA  . ASN B  2  129 ? 80.726  9.194   33.582  1.00 91.98  ?  129 ASN B CA  1 
ATOM   6221  C  C   . ASN B  2  129 ? 79.906  9.384   32.307  1.00 90.31  ?  129 ASN B C   1 
ATOM   6222  O  O   . ASN B  2  129 ? 78.725  9.728   32.365  1.00 99.20  ?  129 ASN B O   1 
ATOM   6223  C  CB  . ASN B  2  129 ? 79.940  9.595   34.834  1.00 110.42 ?  129 ASN B CB  1 
ATOM   6224  C  CG  . ASN B  2  129 ? 80.558  9.073   36.111  1.00 120.82 ?  129 ASN B CG  1 
ATOM   6225  O  OD1 . ASN B  2  129 ? 81.772  8.844   36.196  1.00 115.93 ?  129 ASN B OD1 1 
ATOM   6226  N  ND2 . ASN B  2  129 ? 79.737  8.865   37.136  1.00 110.75 ?  129 ASN B ND2 1 
ATOM   6227  N  N   . VAL B  2  130 ? 80.547  9.150   31.154  1.00 79.86  ?  130 VAL B N   1 
ATOM   6228  C  CA  . VAL B  2  130 ? 79.924  9.233   29.835  1.00 74.06  ?  130 VAL B CA  1 
ATOM   6229  C  C   . VAL B  2  130 ? 79.860  7.787   29.315  1.00 86.53  ?  130 VAL B C   1 
ATOM   6230  O  O   . VAL B  2  130 ? 80.828  7.039   29.463  1.00 97.34  ?  130 VAL B O   1 
ATOM   6231  C  CB  . VAL B  2  130 ? 80.720  10.171  28.888  1.00 68.29  ?  130 VAL B CB  1 
ATOM   6232  C  CG1 . VAL B  2  130 ? 80.155  10.140  27.472  1.00 67.68  ?  130 VAL B CG1 1 
ATOM   6233  C  CG2 . VAL B  2  130 ? 80.737  11.598  29.425  1.00 71.79  ?  130 VAL B CG2 1 
ATOM   6234  N  N   . GLU B  2  131 ? 78.718  7.379   28.746  1.00 92.89  ?  131 GLU B N   1 
ATOM   6235  C  CA  . GLU B  2  131 ? 78.547  6.017   28.245  1.00 82.76  ?  131 GLU B CA  1 
ATOM   6236  C  C   . GLU B  2  131 ? 79.378  5.772   26.974  1.00 93.64  ?  131 GLU B C   1 
ATOM   6237  O  O   . GLU B  2  131 ? 79.530  6.678   26.159  1.00 87.40  ?  131 GLU B O   1 
ATOM   6238  C  CB  . GLU B  2  131 ? 77.052  5.743   27.994  1.00 93.87  ?  131 GLU B CB  1 
ATOM   6239  C  CG  . GLU B  2  131 ? 76.682  4.271   27.867  1.00 135.28 ?  131 GLU B CG  1 
ATOM   6240  C  CD  . GLU B  2  131 ? 77.294  3.337   28.896  1.00 138.44 ?  131 GLU B CD  1 
ATOM   6241  O  OE1 . GLU B  2  131 ? 76.836  3.352   30.063  1.00 121.12 ?  131 GLU B OE1 1 
ATOM   6242  O  OE2 . GLU B  2  131 ? 78.238  2.596   28.535  1.00 123.21 ?  131 GLU B OE2 1 
ATOM   6243  N  N   . THR B  2  132 ? 79.931  4.555   26.818  1.00 99.00  ?  132 THR B N   1 
ATOM   6244  C  CA  . THR B  2  132 ? 80.764  4.190   25.668  1.00 91.60  ?  132 THR B CA  1 
ATOM   6245  C  C   . THR B  2  132 ? 80.327  2.853   25.056  1.00 104.97 ?  132 THR B C   1 
ATOM   6246  O  O   . THR B  2  132 ? 81.163  2.123   24.524  1.00 127.15 ?  132 THR B O   1 
ATOM   6247  C  CB  . THR B  2  132 ? 82.243  4.093   26.117  1.00 84.23  ?  132 THR B CB  1 
ATOM   6248  O  OG1 . THR B  2  132 ? 82.324  3.361   27.343  1.00 98.98  ?  132 THR B OG1 1 
ATOM   6249  C  CG2 . THR B  2  132 ? 82.884  5.438   26.296  1.00 74.99  ?  132 THR B CG2 1 
ATOM   6250  N  N   . GLU B  2  133 ? 79.031  2.532   25.111  1.00 101.44 ?  133 GLU B N   1 
ATOM   6251  C  CA  . GLU B  2  133 ? 78.540  1.259   24.595  1.00 102.93 ?  133 GLU B CA  1 
ATOM   6252  C  C   . GLU B  2  133 ? 77.634  1.436   23.385  1.00 104.12 ?  133 GLU B C   1 
ATOM   6253  O  O   . GLU B  2  133 ? 76.579  2.060   23.488  1.00 117.34 ?  133 GLU B O   1 
ATOM   6254  C  CB  . GLU B  2  133 ? 77.787  0.506   25.704  1.00 129.22 ?  133 GLU B CB  1 
ATOM   6255  C  CG  . GLU B  2  133 ? 77.559  -0.969  25.417  1.00 147.43 ?  133 GLU B CG  1 
ATOM   6256  C  CD  . GLU B  2  133 ? 78.825  -1.794  25.295  1.00 153.66 ?  133 GLU B CD  1 
ATOM   6257  O  OE1 . GLU B  2  133 ? 79.806  -1.489  26.012  1.00 157.89 ?  133 GLU B OE1 1 
ATOM   6258  O  OE2 . GLU B  2  133 ? 78.838  -2.744  24.479  1.00 157.75 ?  133 GLU B OE2 1 
ATOM   6259  N  N   . GLY B  2  134 ? 78.049  0.872   22.257  1.00 105.00 ?  134 GLY B N   1 
ATOM   6260  C  CA  . GLY B  2  134 ? 77.286  0.927   21.017  1.00 106.34 ?  134 GLY B CA  1 
ATOM   6261  C  C   . GLY B  2  134 ? 76.900  2.322   20.575  1.00 92.67  ?  134 GLY B C   1 
ATOM   6262  O  O   . GLY B  2  134 ? 75.761  2.544   20.158  1.00 119.33 ?  134 GLY B O   1 
ATOM   6263  N  N   . ARG B  2  135 ? 77.858  3.248   20.698  1.00 85.50  ?  135 ARG B N   1 
ATOM   6264  C  CA  . ARG B  2  135 ? 77.616  4.655   20.296  1.00 82.11  ?  135 ARG B CA  1 
ATOM   6265  C  C   . ARG B  2  135 ? 78.748  5.144   19.396  1.00 79.33  ?  135 ARG B C   1 
ATOM   6266  O  O   . ARG B  2  135 ? 79.885  4.664   19.564  1.00 90.47  ?  135 ARG B O   1 
ATOM   6267  C  CB  . ARG B  2  135 ? 77.606  5.590   21.506  1.00 79.96  ?  135 ARG B CB  1 
ATOM   6268  C  CG  . ARG B  2  135 ? 76.825  5.094   22.711  1.00 89.38  ?  135 ARG B CG  1 
ATOM   6269  C  CD  . ARG B  2  135 ? 76.839  6.234   23.721  1.00 82.46  ?  135 ARG B CD  1 
ATOM   6270  N  NE  . ARG B  2  135 ? 76.745  7.577   23.178  1.00 86.41  ?  135 ARG B NE  1 
ATOM   6271  C  CZ  . ARG B  2  135 ? 76.791  8.673   23.923  1.00 85.83  ?  135 ARG B CZ  1 
ATOM   6272  N  NH1 . ARG B  2  135 ? 76.964  8.578   25.230  1.00 90.08  ?  135 ARG B NH1 1 
ATOM   6273  N  NH2 . ARG B  2  135 ? 76.675  9.862   23.359  1.00 95.38  ?  135 ARG B NH2 1 
ATOM   6274  N  N   . ASP B  2  136 ? 78.446  6.071   18.491  1.00 87.73  ?  136 ASP B N   1 
ATOM   6275  C  CA  . ASP B  2  136 ? 79.458  6.680   17.626  1.00 73.79  ?  136 ASP B CA  1 
ATOM   6276  C  C   . ASP B  2  136 ? 80.570  7.322   18.457  1.00 73.29  ?  136 ASP B C   1 
ATOM   6277  O  O   . ASP B  2  136 ? 80.288  7.966   19.468  1.00 77.99  ?  136 ASP B O   1 
ATOM   6278  C  CB  . ASP B  2  136 ? 78.789  7.705   16.692  1.00 73.20  ?  136 ASP B CB  1 
ATOM   6279  C  CG  . ASP B  2  136 ? 79.738  8.505   15.827  1.00 88.37  ?  136 ASP B CG  1 
ATOM   6280  O  OD1 . ASP B  2  136 ? 80.610  7.890   15.175  1.00 100.62 ?  136 ASP B OD1 1 
ATOM   6281  O  OD2 . ASP B  2  136 ? 79.606  9.749   15.798  1.00 101.24 ?  136 ASP B OD2 1 
ATOM   6282  N  N   . ILE B  2  137 ? 81.828  7.119   18.056  1.00 75.59  ?  137 ILE B N   1 
ATOM   6283  C  CA  . ILE B  2  137 ? 82.961  7.662   18.799  1.00 65.84  ?  137 ILE B CA  1 
ATOM   6284  C  C   . ILE B  2  137 ? 82.914  9.191   18.874  1.00 71.68  ?  137 ILE B C   1 
ATOM   6285  O  O   . ILE B  2  137 ? 83.341  9.756   19.879  1.00 82.18  ?  137 ILE B O   1 
ATOM   6286  C  CB  . ILE B  2  137 ? 84.323  7.119   18.263  1.00 63.94  ?  137 ILE B CB  1 
ATOM   6287  C  CG1 . ILE B  2  137 ? 85.411  7.172   19.347  1.00 87.11  ?  137 ILE B CG1 1 
ATOM   6288  C  CG2 . ILE B  2  137 ? 84.779  7.872   17.026  1.00 72.98  ?  137 ILE B CG2 1 
ATOM   6289  C  CD1 . ILE B  2  137 ? 85.137  6.284   20.567  1.00 86.22  ?  137 ILE B CD1 1 
ATOM   6290  N  N   . TYR B  2  138 ? 82.373  9.860   17.849  1.00 67.13  ?  138 TYR B N   1 
ATOM   6291  C  CA  . TYR B  2  138 ? 82.274  11.317  17.859  1.00 68.88  ?  138 TYR B CA  1 
ATOM   6292  C  C   . TYR B  2  138 ? 81.158  11.803  18.781  1.00 73.25  ?  138 TYR B C   1 
ATOM   6293  O  O   . TYR B  2  138 ? 81.248  12.917  19.293  1.00 84.02  ?  138 TYR B O   1 
ATOM   6294  C  CB  . TYR B  2  138 ? 82.159  11.867  16.435  1.00 63.93  ?  138 TYR B CB  1 
ATOM   6295  C  CG  . TYR B  2  138 ? 83.406  11.561  15.641  1.00 62.41  ?  138 TYR B CG  1 
ATOM   6296  C  CD1 . TYR B  2  138 ? 84.519  12.384  15.716  1.00 56.05  ?  138 TYR B CD1 1 
ATOM   6297  C  CD2 . TYR B  2  138 ? 83.520  10.382  14.921  1.00 68.92  ?  138 TYR B CD2 1 
ATOM   6298  C  CE1 . TYR B  2  138 ? 85.694  12.072  15.044  1.00 63.26  ?  138 TYR B CE1 1 
ATOM   6299  C  CE2 . TYR B  2  138 ? 84.688  10.060  14.244  1.00 70.05  ?  138 TYR B CE2 1 
ATOM   6300  C  CZ  . TYR B  2  138 ? 85.776  10.906  14.310  1.00 57.71  ?  138 TYR B CZ  1 
ATOM   6301  O  OH  . TYR B  2  138 ? 86.922  10.593  13.626  1.00 73.01  ?  138 TYR B OH  1 
ATOM   6302  N  N   . ASP B  2  139 ? 80.133  10.971  19.032  1.00 71.86  ?  139 ASP B N   1 
ATOM   6303  C  CA  . ASP B  2  139 ? 79.069  11.327  19.971  1.00 73.90  ?  139 ASP B CA  1 
ATOM   6304  C  C   . ASP B  2  139 ? 79.654  11.258  21.391  1.00 73.77  ?  139 ASP B C   1 
ATOM   6305  O  O   . ASP B  2  139 ? 79.323  12.097  22.224  1.00 76.51  ?  139 ASP B O   1 
ATOM   6306  C  CB  . ASP B  2  139 ? 77.872  10.375  19.843  1.00 67.77  ?  139 ASP B CB  1 
ATOM   6307  C  CG  . ASP B  2  139 ? 77.092  10.524  18.550  1.00 96.16  ?  139 ASP B CG  1 
ATOM   6308  O  OD1 . ASP B  2  139 ? 77.218  11.587  17.895  1.00 93.00  ?  139 ASP B OD1 1 
ATOM   6309  O  OD2 . ASP B  2  139 ? 76.352  9.579   18.193  1.00 105.49 ?  139 ASP B OD2 1 
ATOM   6310  N  N   . ILE B  2  140 ? 80.542  10.270  21.656  1.00 76.82  ?  140 ILE B N   1 
ATOM   6311  C  CA  . ILE B  2  140 ? 81.201  10.128  22.956  1.00 70.08  ?  140 ILE B CA  1 
ATOM   6312  C  C   . ILE B  2  140 ? 82.156  11.309  23.127  1.00 64.65  ?  140 ILE B C   1 
ATOM   6313  O  O   . ILE B  2  140 ? 82.166  11.935  24.181  1.00 77.05  ?  140 ILE B O   1 
ATOM   6314  C  CB  . ILE B  2  140 ? 81.980  8.789   23.075  1.00 57.09  ?  140 ILE B CB  1 
ATOM   6315  C  CG1 . ILE B  2  140 ? 81.035  7.571   23.013  1.00 73.90  ?  140 ILE B CG1 1 
ATOM   6316  C  CG2 . ILE B  2  140 ? 82.800  8.764   24.371  1.00 56.17  ?  140 ILE B CG2 1 
ATOM   6317  C  CD1 . ILE B  2  140 ? 81.708  6.275   22.557  1.00 89.22  ?  140 ILE B CD1 1 
ATOM   6318  N  N   . ALA B  2  141 ? 82.963  11.607  22.095  1.00 59.72  ?  141 ALA B N   1 
ATOM   6319  C  CA  . ALA B  2  141 ? 83.925  12.707  22.131  1.00 64.08  ?  141 ALA B CA  1 
ATOM   6320  C  C   . ALA B  2  141 ? 83.276  14.043  22.495  1.00 68.93  ?  141 ALA B C   1 
ATOM   6321  O  O   . ALA B  2  141 ? 83.820  14.778  23.315  1.00 67.48  ?  141 ALA B O   1 
ATOM   6322  C  CB  . ALA B  2  141 ? 84.633  12.824  20.789  1.00 53.58  ?  141 ALA B CB  1 
ATOM   6323  N  N   . HIS B  2  142 ? 82.115  14.354  21.903  1.00 60.87  ?  142 HIS B N   1 
ATOM   6324  C  CA  . HIS B  2  142 ? 81.427  15.612  22.177  1.00 65.52  ?  142 HIS B CA  1 
ATOM   6325  C  C   . HIS B  2  142 ? 80.895  15.664  23.603  1.00 67.98  ?  142 HIS B C   1 
ATOM   6326  O  O   . HIS B  2  142 ? 80.945  16.720  24.232  1.00 68.97  ?  142 HIS B O   1 
ATOM   6327  C  CB  . HIS B  2  142 ? 80.309  15.844  21.154  1.00 71.26  ?  142 HIS B CB  1 
ATOM   6328  C  CG  . HIS B  2  142 ? 80.799  15.882  19.736  1.00 74.09  ?  142 HIS B CG  1 
ATOM   6329  N  ND1 . HIS B  2  142 ? 79.989  15.502  18.683  1.00 71.07  ?  142 HIS B ND1 1 
ATOM   6330  C  CD2 . HIS B  2  142 ? 82.008  16.247  19.245  1.00 67.87  ?  142 HIS B CD2 1 
ATOM   6331  C  CE1 . HIS B  2  142 ? 80.721  15.653  17.590  1.00 74.24  ?  142 HIS B CE1 1 
ATOM   6332  N  NE2 . HIS B  2  142 ? 81.943  16.099  17.881  1.00 65.09  ?  142 HIS B NE2 1 
ATOM   6333  N  N   . ASP B  2  143 ? 80.405  14.531  24.128  1.00 73.67  ?  143 ASP B N   1 
ATOM   6334  C  CA  . ASP B  2  143 ? 79.902  14.466  25.501  1.00 68.90  ?  143 ASP B CA  1 
ATOM   6335  C  C   . ASP B  2  143 ? 81.070  14.628  26.481  1.00 66.15  ?  143 ASP B C   1 
ATOM   6336  O  O   . ASP B  2  143 ? 80.941  15.330  27.479  1.00 70.75  ?  143 ASP B O   1 
ATOM   6337  C  CB  . ASP B  2  143 ? 79.176  13.131  25.751  1.00 70.61  ?  143 ASP B CB  1 
ATOM   6338  C  CG  . ASP B  2  143 ? 77.787  13.029  25.136  1.00 82.83  ?  143 ASP B CG  1 
ATOM   6339  O  OD1 . ASP B  2  143 ? 77.363  13.993  24.455  1.00 77.45  ?  143 ASP B OD1 1 
ATOM   6340  O  OD2 . ASP B  2  143 ? 77.126  11.984  25.334  1.00 83.92  ?  143 ASP B OD2 1 
ATOM   6341  N  N   . VAL B  2  144 ? 82.212  13.996  26.189  1.00 69.38  ?  144 VAL B N   1 
ATOM   6342  C  CA  . VAL B  2  144 ? 83.402  14.102  27.032  1.00 58.85  ?  144 VAL B CA  1 
ATOM   6343  C  C   . VAL B  2  144 ? 83.914  15.550  26.996  1.00 64.24  ?  144 VAL B C   1 
ATOM   6344  O  O   . VAL B  2  144 ? 84.324  16.078  28.027  1.00 68.68  ?  144 VAL B O   1 
ATOM   6345  C  CB  . VAL B  2  144 ? 84.496  13.105  26.583  1.00 57.50  ?  144 VAL B CB  1 
ATOM   6346  C  CG1 . VAL B  2  144 ? 85.812  13.364  27.309  1.00 60.46  ?  144 VAL B CG1 1 
ATOM   6347  C  CG2 . VAL B  2  144 ? 84.043  11.666  26.797  1.00 62.06  ?  144 VAL B CG2 1 
ATOM   6348  N  N   . ALA B  2  145 ? 83.888  16.190  25.811  1.00 59.97  ?  145 ALA B N   1 
ATOM   6349  C  CA  . ALA B  2  145 ? 84.325  17.575  25.664  1.00 60.18  ?  145 ALA B CA  1 
ATOM   6350  C  C   . ALA B  2  145 ? 83.422  18.501  26.482  1.00 70.49  ?  145 ALA B C   1 
ATOM   6351  O  O   . ALA B  2  145 ? 83.923  19.401  27.156  1.00 64.85  ?  145 ALA B O   1 
ATOM   6352  C  CB  . ALA B  2  145 ? 84.288  17.979  24.200  1.00 56.75  ?  145 ALA B CB  1 
ATOM   6353  N  N   . LYS B  2  146 ? 82.096  18.278  26.439  1.00 61.46  ?  146 LYS B N   1 
ATOM   6354  C  CA  . LYS B  2  146 ? 81.146  19.094  27.193  1.00 59.58  ?  146 LYS B CA  1 
ATOM   6355  C  C   . LYS B  2  146 ? 81.382  18.944  28.696  1.00 72.08  ?  146 LYS B C   1 
ATOM   6356  O  O   . LYS B  2  146 ? 81.375  19.942  29.417  1.00 67.12  ?  146 LYS B O   1 
ATOM   6357  C  CB  . LYS B  2  146 ? 79.698  18.709  26.844  1.00 67.59  ?  146 LYS B CB  1 
ATOM   6358  C  CG  . LYS B  2  146 ? 79.183  19.363  25.569  1.00 76.20  ?  146 LYS B CG  1 
ATOM   6359  C  CD  . LYS B  2  146 ? 77.703  19.052  25.284  1.00 86.90  ?  146 LYS B CD  1 
ATOM   6360  C  CE  . LYS B  2  146 ? 77.486  17.895  24.326  1.00 101.67 ?  146 LYS B CE  1 
ATOM   6361  N  NZ  . LYS B  2  146 ? 76.522  18.236  23.243  1.00 88.42  ?  146 LYS B NZ  1 
ATOM   6362  N  N   . GLU B  2  147 ? 81.597  17.706  29.171  1.00 72.08  ?  147 GLU B N   1 
ATOM   6363  C  CA  . GLU B  2  147 ? 81.848  17.459  30.593  1.00 66.25  ?  147 GLU B CA  1 
ATOM   6364  C  C   . GLU B  2  147 ? 83.184  18.056  31.024  1.00 62.23  ?  147 GLU B C   1 
ATOM   6365  O  O   . GLU B  2  147 ? 83.310  18.518  32.154  1.00 65.66  ?  147 GLU B O   1 
ATOM   6366  C  CB  . GLU B  2  147 ? 81.798  15.955  30.916  1.00 66.73  ?  147 GLU B CB  1 
ATOM   6367  C  CG  . GLU B  2  147 ? 80.397  15.375  30.904  1.00 67.07  ?  147 GLU B CG  1 
ATOM   6368  C  CD  . GLU B  2  147 ? 79.443  16.082  31.845  1.00 96.31  ?  147 GLU B CD  1 
ATOM   6369  O  OE1 . GLU B  2  147 ? 79.562  15.880  33.076  1.00 103.16 ?  147 GLU B OE1 1 
ATOM   6370  O  OE2 . GLU B  2  147 ? 78.584  16.849  31.352  1.00 97.11  ?  147 GLU B OE2 1 
ATOM   6371  N  N   . GLY B  2  148 ? 84.163  18.047  30.127  1.00 59.08  ?  148 GLY B N   1 
ATOM   6372  C  CA  . GLY B  2  148 ? 85.465  18.627  30.401  1.00 58.85  ?  148 GLY B CA  1 
ATOM   6373  C  C   . GLY B  2  148 ? 85.347  20.131  30.504  1.00 69.86  ?  148 GLY B C   1 
ATOM   6374  O  O   . GLY B  2  148 ? 85.931  20.744  31.400  1.00 75.85  ?  148 GLY B O   1 
ATOM   6375  N  N   . LEU B  2  149 ? 84.566  20.738  29.598  1.00 59.42  ?  149 LEU B N   1 
ATOM   6376  C  CA  . LEU B  2  149 ? 84.358  22.181  29.614  1.00 58.41  ?  149 LEU B CA  1 
ATOM   6377  C  C   . LEU B  2  149 ? 83.645  22.635  30.895  1.00 62.30  ?  149 LEU B C   1 
ATOM   6378  O  O   . LEU B  2  149 ? 83.866  23.755  31.344  1.00 63.10  ?  149 LEU B O   1 
ATOM   6379  C  CB  . LEU B  2  149 ? 83.570  22.634  28.381  1.00 60.72  ?  149 LEU B CB  1 
ATOM   6380  C  CG  . LEU B  2  149 ? 84.343  22.658  27.068  1.00 55.25  ?  149 LEU B CG  1 
ATOM   6381  C  CD1 . LEU B  2  149 ? 83.404  22.816  25.890  1.00 62.16  ?  149 LEU B CD1 1 
ATOM   6382  C  CD2 . LEU B  2  149 ? 85.369  23.773  27.055  1.00 49.00  ?  149 LEU B CD2 1 
ATOM   6383  N  N   . SER B  2  150 ? 82.808  21.766  31.462  1.00 61.18  ?  150 SER B N   1 
ATOM   6384  C  CA  . SER B  2  150 ? 82.098  22.108  32.720  1.00 55.34  ?  150 SER B CA  1 
ATOM   6385  C  C   . SER B  2  150 ? 83.119  22.435  33.810  1.00 66.40  ?  150 SER B C   1 
ATOM   6386  O  O   . SER B  2  150 ? 82.884  23.392  34.567  1.00 71.52  ?  150 SER B O   1 
ATOM   6387  C  CB  . SER B  2  150 ? 81.197  20.985  33.141  1.00 54.95  ?  150 SER B CB  1 
ATOM   6388  O  OG  . SER B  2  150 ? 81.933  19.970  33.806  1.00 99.59  ?  150 SER B OG  1 
ATOM   6389  N  N   . ASN B  2  151 ? 84.210  21.672  33.878  1.00 67.53  ?  151 ASN B N   1 
ATOM   6390  C  CA  . ASN B  2  151 ? 85.219  21.877  34.911  1.00 59.83  ?  151 ASN B CA  1 
ATOM   6391  C  C   . ASN B  2  151 ? 85.829  23.286  34.865  1.00 58.98  ?  151 ASN B C   1 
ATOM   6392  O  O   . ASN B  2  151 ? 86.482  23.682  35.825  1.00 63.94  ?  151 ASN B O   1 
ATOM   6393  C  CB  . ASN B  2  151 ? 86.323  20.833  34.779  1.00 54.80  ?  151 ASN B CB  1 
ATOM   6394  C  CG  . ASN B  2  151 ? 85.995  19.494  35.390  1.00 68.14  ?  151 ASN B CG  1 
ATOM   6395  O  OD1 . ASN B  2  151 ? 84.921  19.283  35.969  1.00 65.84  ?  151 ASN B OD1 1 
ATOM   6396  N  ND2 . ASN B  2  151 ? 86.925  18.555  35.275  1.00 77.94  ?  151 ASN B ND2 1 
ATOM   6397  N  N   . TYR B  2  152 ? 85.622  24.044  33.776  1.00 56.11  ?  152 TYR B N   1 
ATOM   6398  C  CA  . TYR B  2  152 ? 86.168  25.394  33.675  1.00 55.81  ?  152 TYR B CA  1 
ATOM   6399  C  C   . TYR B  2  152 ? 85.257  26.452  34.272  1.00 58.22  ?  152 TYR B C   1 
ATOM   6400  O  O   . TYR B  2  152 ? 85.760  27.478  34.725  1.00 71.57  ?  152 TYR B O   1 
ATOM   6401  C  CB  . TYR B  2  152 ? 86.469  25.763  32.212  1.00 46.73  ?  152 TYR B CB  1 
ATOM   6402  C  CG  . TYR B  2  152 ? 87.680  25.049  31.668  1.00 49.64  ?  152 TYR B CG  1 
ATOM   6403  C  CD1 . TYR B  2  152 ? 88.954  25.554  31.863  1.00 48.26  ?  152 TYR B CD1 1 
ATOM   6404  C  CD2 . TYR B  2  152 ? 87.556  23.835  31.014  1.00 54.98  ?  152 TYR B CD2 1 
ATOM   6405  C  CE1 . TYR B  2  152 ? 90.075  24.883  31.394  1.00 52.57  ?  152 TYR B CE1 1 
ATOM   6406  C  CE2 . TYR B  2  152 ? 88.666  23.155  30.535  1.00 56.20  ?  152 TYR B CE2 1 
ATOM   6407  C  CZ  . TYR B  2  152 ? 89.927  23.680  30.730  1.00 57.10  ?  152 TYR B CZ  1 
ATOM   6408  O  OH  . TYR B  2  152 ? 91.034  23.009  30.266  1.00 67.28  ?  152 TYR B OH  1 
ATOM   6409  N  N   . GLY B  2  153 ? 83.946  26.232  34.250  1.00 52.08  ?  153 GLY B N   1 
ATOM   6410  C  CA  . GLY B  2  153 ? 83.025  27.235  34.760  1.00 55.20  ?  153 GLY B CA  1 
ATOM   6411  C  C   . GLY B  2  153 ? 81.740  26.770  35.406  1.00 68.77  ?  153 GLY B C   1 
ATOM   6412  O  O   . GLY B  2  153 ? 80.754  27.514  35.373  1.00 78.70  ?  153 GLY B O   1 
ATOM   6413  N  N   . LYS B  2  154 ? 81.732  25.571  35.989  1.00 62.18  ?  154 LYS B N   1 
ATOM   6414  C  CA  . LYS B  2  154 ? 80.507  25.117  36.700  1.00 56.82  ?  154 LYS B CA  1 
ATOM   6415  C  C   . LYS B  2  154 ? 80.398  25.834  38.048  1.00 73.64  ?  154 LYS B C   1 
ATOM   6416  O  O   . LYS B  2  154 ? 81.389  25.831  38.801  1.00 64.97  ?  154 LYS B O   1 
ATOM   6417  C  CB  . LYS B  2  154 ? 80.466  23.593  36.834  1.00 59.69  ?  154 LYS B CB  1 
ATOM   6418  C  CG  . LYS B  2  154 ? 81.673  22.940  37.485  1.00 77.08  ?  154 LYS B CG  1 
ATOM   6419  C  CD  . LYS B  2  154 ? 81.495  21.446  37.558  1.00 66.39  ?  154 LYS B CD  1 
ATOM   6420  C  CE  . LYS B  2  154 ? 80.067  21.039  37.848  1.00 81.23  ?  154 LYS B CE  1 
ATOM   6421  N  NZ  . LYS B  2  154 ? 79.925  19.566  37.918  1.00 100.80 ?  154 LYS B NZ  1 
ATOM   6422  N  N   . GLN B  2  155 ? 79.236  26.428  38.323  1.00 74.33  ?  155 GLN B N   1 
ATOM   6423  C  CA  . GLN B  2  155 ? 79.008  27.160  39.569  1.00 73.98  ?  155 GLN B CA  1 
ATOM   6424  C  C   . GLN B  2  155 ? 78.332  26.284  40.627  1.00 78.05  ?  155 GLN B C   1 
ATOM   6425  O  O   . GLN B  2  155 ? 78.466  26.563  41.819  1.00 74.25  ?  155 GLN B O   1 
ATOM   6426  C  CB  . GLN B  2  155 ? 78.169  28.415  39.300  1.00 66.58  ?  155 GLN B CB  1 
ATOM   6427  C  CG  . GLN B  2  155 ? 78.791  29.354  38.269  1.00 67.96  ?  155 GLN B CG  1 
ATOM   6428  C  CD  . GLN B  2  155 ? 80.127  29.884  38.727  1.00 68.91  ?  155 GLN B CD  1 
ATOM   6429  O  OE1 . GLN B  2  155 ? 80.286  30.302  39.880  1.00 61.35  ?  155 GLN B OE1 1 
ATOM   6430  N  NE2 . GLN B  2  155 ? 81.120  29.881  37.845  1.00 59.51  ?  155 GLN B NE2 1 
ATOM   6431  N  N   . LEU B  2  156 ? 77.607  25.234  40.196  1.00 82.09  ?  156 LEU B N   1 
ATOM   6432  C  CA  . LEU B  2  156 ? 76.923  24.305  41.098  1.00 78.02  ?  156 LEU B CA  1 
ATOM   6433  C  C   . LEU B  2  156 ? 77.399  22.885  40.806  1.00 77.02  ?  156 LEU B C   1 
ATOM   6434  O  O   . LEU B  2  156 ? 77.688  22.554  39.657  1.00 82.25  ?  156 LEU B O   1 
ATOM   6435  C  CB  . LEU B  2  156 ? 75.399  24.388  40.910  1.00 68.47  ?  156 LEU B CB  1 
ATOM   6436  C  CG  . LEU B  2  156 ? 74.770  25.760  41.135  1.00 69.85  ?  156 LEU B CG  1 
ATOM   6437  C  CD1 . LEU B  2  156 ? 73.351  25.797  40.612  1.00 72.10  ?  156 LEU B CD1 1 
ATOM   6438  C  CD2 . LEU B  2  156 ? 74.795  26.141  42.599  1.00 80.48  ?  156 LEU B CD2 1 
ATOM   6439  N  N   . GLY B  2  157 ? 77.470  22.061  41.839  1.00 67.66  ?  157 GLY B N   1 
ATOM   6440  C  CA  . GLY B  2  157 ? 77.921  20.682  41.699  1.00 75.04  ?  157 GLY B CA  1 
ATOM   6441  C  C   . GLY B  2  157 ? 79.413  20.551  41.925  1.00 78.06  ?  157 GLY B C   1 
ATOM   6442  O  O   . GLY B  2  157 ? 80.092  21.553  42.170  1.00 91.36  ?  157 GLY B O   1 
ATOM   6443  N  N   . GLU B  2  158 ? 79.943  19.323  41.847  1.00 77.91  ?  158 GLU B N   1 
ATOM   6444  C  CA  . GLU B  2  158 ? 81.374  19.101  42.058  1.00 82.68  ?  158 GLU B CA  1 
ATOM   6445  C  C   . GLU B  2  158 ? 82.113  18.887  40.746  1.00 80.36  ?  158 GLU B C   1 
ATOM   6446  O  O   . GLU B  2  158 ? 81.544  18.387  39.777  1.00 89.66  ?  158 GLU B O   1 
ATOM   6447  C  CB  . GLU B  2  158 ? 81.617  17.890  42.970  1.00 98.32  ?  158 GLU B CB  1 
ATOM   6448  C  CG  . GLU B  2  158 ? 81.357  18.159  44.439  1.00 109.04 ?  158 GLU B CG  1 
ATOM   6449  C  CD  . GLU B  2  158 ? 82.015  17.173  45.388  1.00 132.71 ?  158 GLU B CD  1 
ATOM   6450  O  OE1 . GLU B  2  158 ? 82.990  16.500  44.981  1.00 120.78 ?  158 GLU B OE1 1 
ATOM   6451  O  OE2 . GLU B  2  158 ? 81.552  17.076  46.548  1.00 161.89 ?  158 GLU B OE2 1 
ATOM   6452  N  N   . VAL B  2  159 ? 83.394  19.258  40.727  1.00 76.66  ?  159 VAL B N   1 
ATOM   6453  C  CA  . VAL B  2  159 ? 84.233  19.100  39.544  1.00 64.96  ?  159 VAL B CA  1 
ATOM   6454  C  C   . VAL B  2  159 ? 84.705  17.650  39.430  1.00 67.42  ?  159 VAL B C   1 
ATOM   6455  O  O   . VAL B  2  159 ? 84.717  16.922  40.423  1.00 84.66  ?  159 VAL B O   1 
ATOM   6456  C  CB  . VAL B  2  159 ? 85.428  20.086  39.558  1.00 66.45  ?  159 VAL B CB  1 
ATOM   6457  C  CG1 . VAL B  2  159 ? 84.956  21.518  39.344  1.00 73.02  ?  159 VAL B CG1 1 
ATOM   6458  C  CG2 . VAL B  2  159 ? 86.239  19.973  40.848  1.00 61.32  ?  159 VAL B CG2 1 
ATOM   6459  N  N   . THR B  2  160 ? 85.087  17.229  38.219  1.00 67.19  ?  160 THR B N   1 
ATOM   6460  C  CA  . THR B  2  160 ? 85.565  15.869  37.970  1.00 54.08  ?  160 THR B CA  1 
ATOM   6461  C  C   . THR B  2  160 ? 87.087  15.829  37.983  1.00 59.44  ?  160 THR B C   1 
ATOM   6462  O  O   . THR B  2  160 ? 87.715  16.516  37.181  1.00 77.02  ?  160 THR B O   1 
ATOM   6463  C  CB  . THR B  2  160 ? 85.037  15.382  36.623  1.00 63.49  ?  160 THR B CB  1 
ATOM   6464  O  OG1 . THR B  2  160 ? 83.612  15.308  36.688  1.00 74.12  ?  160 THR B OG1 1 
ATOM   6465  C  CG2 . THR B  2  160 ? 85.618  14.033  36.226  1.00 58.50  ?  160 THR B CG2 1 
ATOM   6466  N  N   . LEU B  2  161 ? 87.662  15.009  38.866  1.00 62.20  ?  161 LEU B N   1 
ATOM   6467  C  CA  . LEU B  2  161 ? 89.142  14.869  38.932  1.00 52.99  ?  161 LEU B CA  1 
ATOM   6468  C  C   . LEU B  2  161 ? 89.540  13.473  38.439  1.00 54.88  ?  161 LEU B C   1 
ATOM   6469  O  O   . LEU B  2  161 ? 88.726  12.542  38.577  1.00 68.39  ?  161 LEU B O   1 
ATOM   6470  C  CB  . LEU B  2  161 ? 89.597  15.103  40.376  1.00 50.59  ?  161 LEU B CB  1 
ATOM   6471  C  CG  . LEU B  2  161 ? 89.343  16.506  40.922  1.00 50.39  ?  161 LEU B CG  1 
ATOM   6472  C  CD1 . LEU B  2  161 ? 89.906  16.650  42.328  1.00 66.29  ?  161 LEU B CD1 1 
ATOM   6473  C  CD2 . LEU B  2  161 ? 89.936  17.560  40.000  1.00 60.93  ?  161 LEU B CD2 1 
ATOM   6474  N  N   . PRO B  2  162 ? 90.750  13.292  37.867  1.00 54.94  ?  162 PRO B N   1 
ATOM   6475  C  CA  . PRO B  2  162 ? 91.188  11.997  37.335  1.00 57.11  ?  162 PRO B CA  1 
ATOM   6476  C  C   . PRO B  2  162 ? 91.322  10.914  38.413  1.00 57.77  ?  162 PRO B C   1 
ATOM   6477  O  O   . PRO B  2  162 ? 91.582  11.246  39.555  1.00 70.50  ?  162 PRO B O   1 
ATOM   6478  C  CB  . PRO B  2  162 ? 92.575  12.294  36.747  1.00 60.78  ?  162 PRO B CB  1 
ATOM   6479  C  CG  . PRO B  2  162 ? 93.030  13.535  37.474  1.00 58.35  ?  162 PRO B CG  1 
ATOM   6480  C  CD  . PRO B  2  162 ? 91.759  14.328  37.678  1.00 57.26  ?  162 PRO B CD  1 
ATOM   6481  N  N   . PRO B  2  163 ? 91.153  9.621   38.061  1.00 63.43  ?  163 PRO B N   1 
ATOM   6482  C  CA  . PRO B  2  163 ? 91.227  8.531   39.037  1.00 68.35  ?  163 PRO B CA  1 
ATOM   6483  C  C   . PRO B  2  163 ? 92.605  8.389   39.698  1.00 68.50  ?  163 PRO B C   1 
ATOM   6484  O  O   . PRO B  2  163 ? 92.647  8.046   40.863  1.00 67.72  ?  163 PRO B O   1 
ATOM   6485  C  CB  . PRO B  2  163 ? 90.971  7.276   38.190  1.00 54.96  ?  163 PRO B CB  1 
ATOM   6486  C  CG  . PRO B  2  163 ? 90.240  7.787   36.971  1.00 71.40  ?  163 PRO B CG  1 
ATOM   6487  C  CD  . PRO B  2  163 ? 90.852  9.145   36.710  1.00 56.98  ?  163 PRO B CD  1 
ATOM   6488  N  N   . SER B  2  164 ? 93.685  8.647   38.954  1.00 64.78  ?  164 SER B N   1 
ATOM   6489  C  CA  . SER B  2  164 ? 95.042  8.422   39.515  1.00 53.46  ?  164 SER B CA  1 
ATOM   6490  C  C   . SER B  2  164 ? 95.137  9.139   40.862  1.00 58.44  ?  164 SER B C   1 
ATOM   6491  O  O   . SER B  2  164 ? 95.943  8.703   41.700  1.00 74.91  ?  164 SER B O   1 
ATOM   6492  C  CB  . SER B  2  164 ? 96.089  8.751   38.494  1.00 48.93  ?  164 SER B CB  1 
ATOM   6493  O  OG  . SER B  2  164 ? 96.147  10.150  38.267  1.00 68.94  ?  164 SER B OG  1 
ATOM   6494  N  N   . LEU B  2  165 ? 94.350  10.197  41.059  1.00 62.51  ?  165 LEU B N   1 
ATOM   6495  C  CA  . LEU B  2  165 ? 94.455  10.964  42.291  1.00 54.92  ?  165 LEU B CA  1 
ATOM   6496  C  C   . LEU B  2  165 ? 93.981  10.208  43.545  1.00 59.80  ?  165 LEU B C   1 
ATOM   6497  O  O   . LEU B  2  165 ? 92.784  9.945   43.664  1.00 69.74  ?  165 LEU B O   1 
ATOM   6498  C  CB  . LEU B  2  165 ? 93.644  12.244  42.088  1.00 50.37  ?  165 LEU B CB  1 
ATOM   6499  C  CG  . LEU B  2  165 ? 93.625  13.219  43.254  1.00 56.28  ?  165 LEU B CG  1 
ATOM   6500  C  CD1 . LEU B  2  165 ? 95.017  13.719  43.600  1.00 59.28  ?  165 LEU B CD1 1 
ATOM   6501  C  CD2 . LEU B  2  165 ? 92.758  14.377  42.931  1.00 60.91  ?  165 LEU B CD2 1 
ATOM   6502  N  N   . PRO B  2  166 ? 94.874  9.835   44.487  1.00 58.82  ?  166 PRO B N   1 
ATOM   6503  C  CA  . PRO B  2  166 ? 94.413  9.085   45.670  1.00 67.49  ?  166 PRO B CA  1 
ATOM   6504  C  C   . PRO B  2  166 ? 93.304  9.736   46.486  1.00 72.64  ?  166 PRO B C   1 
ATOM   6505  O  O   . PRO B  2  166 ? 93.264  10.957  46.617  1.00 62.27  ?  166 PRO B O   1 
ATOM   6506  C  CB  . PRO B  2  166 ? 95.682  8.944   46.515  1.00 68.57  ?  166 PRO B CB  1 
ATOM   6507  C  CG  . PRO B  2  166 ? 96.789  9.039   45.553  1.00 67.60  ?  166 PRO B CG  1 
ATOM   6508  C  CD  . PRO B  2  166 ? 96.338  10.024  44.519  1.00 67.44  ?  166 PRO B CD  1 
ATOM   6509  N  N   . GLU B  2  167 ? 92.416  8.906   47.061  1.00 75.72  ?  167 GLU B N   1 
ATOM   6510  C  CA  . GLU B  2  167 ? 91.318  9.399   47.895  1.00 74.56  ?  167 GLU B CA  1 
ATOM   6511  C  C   . GLU B  2  167 ? 91.856  10.027  49.178  1.00 67.17  ?  167 GLU B C   1 
ATOM   6512  O  O   . GLU B  2  167 ? 91.206  10.903  49.749  1.00 79.10  ?  167 GLU B O   1 
ATOM   6513  C  CB  . GLU B  2  167 ? 90.335  8.270   48.246  1.00 86.79  ?  167 GLU B CB  1 
ATOM   6514  C  CG  . GLU B  2  167 ? 89.414  7.877   47.105  1.00 91.70  ?  167 GLU B CG  1 
ATOM   6515  C  CD  . GLU B  2  167 ? 88.374  8.914   46.729  1.00 103.35 ?  167 GLU B CD  1 
ATOM   6516  O  OE1 . GLU B  2  167 ? 88.013  9.749   47.591  1.00 116.57 ?  167 GLU B OE1 1 
ATOM   6517  O  OE2 . GLU B  2  167 ? 87.914  8.887   45.564  1.00 97.39  ?  167 GLU B OE2 1 
ATOM   6518  N  N   . LYS B  2  168 ? 93.039  9.589   49.635  1.00 62.67  ?  168 LYS B N   1 
ATOM   6519  C  CA  . LYS B  2  168 ? 93.657  10.143  50.832  1.00 63.06  ?  168 LYS B CA  1 
ATOM   6520  C  C   . LYS B  2  168 ? 94.004  11.611  50.569  1.00 61.90  ?  168 LYS B C   1 
ATOM   6521  O  O   . LYS B  2  168 ? 93.751  12.470  51.409  1.00 77.09  ?  168 LYS B O   1 
ATOM   6522  C  CB  . LYS B  2  168 ? 94.918  9.344   51.196  1.00 63.38  ?  168 LYS B CB  1 
ATOM   6523  C  CG  . LYS B  2  168 ? 94.617  7.898   51.568  1.00 66.16  ?  168 LYS B CG  1 
ATOM   6524  C  CD  . LYS B  2  168 ? 95.859  7.135   51.980  1.00 66.73  ?  168 LYS B CD  1 
ATOM   6525  C  CE  . LYS B  2  168 ? 95.526  5.949   52.850  1.00 70.18  ?  168 LYS B CE  1 
ATOM   6526  N  NZ  . LYS B  2  168 ? 96.591  4.916   52.800  1.00 94.99  ?  168 LYS B NZ  1 
ATOM   6527  N  N   . ARG B  2  169 ? 94.551  11.894  49.377  1.00 67.01  ?  169 ARG B N   1 
ATOM   6528  C  CA  . ARG B  2  169 ? 94.922  13.241  48.957  1.00 60.46  ?  169 ARG B CA  1 
ATOM   6529  C  C   . ARG B  2  169 ? 93.672  14.115  48.829  1.00 65.03  ?  169 ARG B C   1 
ATOM   6530  O  O   . ARG B  2  169 ? 93.686  15.265  49.260  1.00 72.35  ?  169 ARG B O   1 
ATOM   6531  C  CB  . ARG B  2  169 ? 95.685  13.171  47.616  1.00 63.61  ?  169 ARG B CB  1 
ATOM   6532  C  CG  . ARG B  2  169 ? 96.248  14.491  47.091  1.00 54.73  ?  169 ARG B CG  1 
ATOM   6533  C  CD  . ARG B  2  169 ? 97.034  15.325  48.094  1.00 60.93  ?  169 ARG B CD  1 
ATOM   6534  N  NE  . ARG B  2  169 ? 97.974  14.551  48.909  1.00 61.56  ?  169 ARG B NE  1 
ATOM   6535  C  CZ  . ARG B  2  169 ? 98.860  15.089  49.739  1.00 64.37  ?  169 ARG B CZ  1 
ATOM   6536  N  NH1 . ARG B  2  169 ? 98.945  16.408  49.870  1.00 61.51  ?  169 ARG B NH1 1 
ATOM   6537  N  NH2 . ARG B  2  169 ? 99.672  14.314  50.446  1.00 58.72  ?  169 ARG B NH2 1 
ATOM   6538  N  N   . LYS B  2  170 ? 92.589  13.570  48.257  1.00 73.22  ?  170 LYS B N   1 
ATOM   6539  C  CA  . LYS B  2  170 ? 91.344  14.322  48.094  1.00 67.47  ?  170 LYS B CA  1 
ATOM   6540  C  C   . LYS B  2  170 ? 90.761  14.725  49.451  1.00 69.31  ?  170 LYS B C   1 
ATOM   6541  O  O   . LYS B  2  170 ? 90.394  15.885  49.633  1.00 69.66  ?  170 LYS B O   1 
ATOM   6542  C  CB  . LYS B  2  170 ? 90.318  13.516  47.282  1.00 58.23  ?  170 LYS B CB  1 
ATOM   6543  C  CG  . LYS B  2  170 ? 90.758  13.270  45.844  1.00 64.31  ?  170 LYS B CG  1 
ATOM   6544  C  CD  . LYS B  2  170 ? 89.592  13.056  44.887  1.00 60.49  ?  170 LYS B CD  1 
ATOM   6545  C  CE  . LYS B  2  170 ? 89.354  11.601  44.575  1.00 67.51  ?  170 LYS B CE  1 
ATOM   6546  N  NZ  . LYS B  2  170 ? 88.037  11.377  43.919  1.00 82.50  ?  170 LYS B NZ  1 
ATOM   6547  N  N   . GLU B  2  171 ? 90.688  13.775  50.401  1.00 69.05  ?  171 GLU B N   1 
ATOM   6548  C  CA  . GLU B  2  171 ? 90.164  14.046  51.744  1.00 67.95  ?  171 GLU B CA  1 
ATOM   6549  C  C   . GLU B  2  171 ? 91.057  15.024  52.507  1.00 63.12  ?  171 GLU B C   1 
ATOM   6550  O  O   . GLU B  2  171 ? 90.555  15.805  53.306  1.00 70.12  ?  171 GLU B O   1 
ATOM   6551  C  CB  . GLU B  2  171 ? 90.028  12.742  52.554  1.00 70.54  ?  171 GLU B CB  1 
ATOM   6552  C  CG  . GLU B  2  171 ? 88.610  12.210  52.644  1.00 88.64  ?  171 GLU B CG  1 
ATOM   6553  C  CD  . GLU B  2  171 ? 87.657  13.145  53.364  1.00 107.71 ?  171 GLU B CD  1 
ATOM   6554  O  OE1 . GLU B  2  171 ? 87.739  13.232  54.611  1.00 117.43 ?  171 GLU B OE1 1 
ATOM   6555  O  OE2 . GLU B  2  171 ? 86.832  13.796  52.682  1.00 109.97 ?  171 GLU B OE2 1 
ATOM   6556  N  N   . LEU B  2  172 ? 92.372  14.986  52.268  1.00 64.33  ?  172 LEU B N   1 
ATOM   6557  C  CA  . LEU B  2  172 ? 93.300  15.900  52.922  1.00 60.48  ?  172 LEU B CA  1 
ATOM   6558  C  C   . LEU B  2  172 ? 93.015  17.324  52.442  1.00 67.75  ?  172 LEU B C   1 
ATOM   6559  O  O   . LEU B  2  172 ? 92.979  18.247  53.258  1.00 75.38  ?  172 LEU B O   1 
ATOM   6560  C  CB  . LEU B  2  172 ? 94.748  15.503  52.592  1.00 58.87  ?  172 LEU B CB  1 
ATOM   6561  C  CG  . LEU B  2  172 ? 95.865  16.435  53.076  1.00 57.70  ?  172 LEU B CG  1 
ATOM   6562  C  CD1 . LEU B  2  172 ? 95.723  16.781  54.558  1.00 78.70  ?  172 LEU B CD1 1 
ATOM   6563  C  CD2 . LEU B  2  172 ? 97.215  15.803  52.834  1.00 75.60  ?  172 LEU B CD2 1 
ATOM   6564  N  N   . TRP B  2  173 ? 92.790  17.503  51.122  1.00 63.33  ?  173 TRP B N   1 
ATOM   6565  C  CA  . TRP B  2  173 ? 92.476  18.822  50.571  1.00 61.72  ?  173 TRP B CA  1 
ATOM   6566  C  C   . TRP B  2  173 ? 91.164  19.315  51.161  1.00 70.04  ?  173 TRP B C   1 
ATOM   6567  O  O   . TRP B  2  173 ? 91.067  20.475  51.547  1.00 78.09  ?  173 TRP B O   1 
ATOM   6568  C  CB  . TRP B  2  173 ? 92.344  18.786  49.040  1.00 57.50  ?  173 TRP B CB  1 
ATOM   6569  C  CG  . TRP B  2  173 ? 93.606  18.518  48.283  1.00 52.07  ?  173 TRP B CG  1 
ATOM   6570  C  CD1 . TRP B  2  173 ? 94.890  18.654  48.726  1.00 55.41  ?  173 TRP B CD1 1 
ATOM   6571  C  CD2 . TRP B  2  173 ? 93.693  18.106  46.919  1.00 54.96  ?  173 TRP B CD2 1 
ATOM   6572  N  NE1 . TRP B  2  173 ? 95.771  18.315  47.729  1.00 55.97  ?  173 TRP B NE1 1 
ATOM   6573  C  CE2 . TRP B  2  173 ? 95.061  17.975  46.606  1.00 62.21  ?  173 TRP B CE2 1 
ATOM   6574  C  CE3 . TRP B  2  173 ? 92.746  17.812  45.935  1.00 61.83  ?  173 TRP B CE3 1 
ATOM   6575  C  CZ2 . TRP B  2  173 ? 95.499  17.555  45.353  1.00 69.01  ?  173 TRP B CZ2 1 
ATOM   6576  C  CZ3 . TRP B  2  173 ? 93.182  17.412  44.690  1.00 49.24  ?  173 TRP B CZ3 1 
ATOM   6577  C  CH2 . TRP B  2  173 ? 94.542  17.284  44.409  1.00 56.24  ?  173 TRP B CH2 1 
ATOM   6578  N  N   . ARG B  2  174 ? 90.156  18.432  51.240  1.00 64.38  ?  174 ARG B N   1 
ATOM   6579  C  CA  . ARG B  2  174 ? 88.854  18.781  51.803  1.00 61.89  ?  174 ARG B CA  1 
ATOM   6580  C  C   . ARG B  2  174 ? 89.010  19.270  53.248  1.00 63.49  ?  174 ARG B C   1 
ATOM   6581  O  O   . ARG B  2  174 ? 88.479  20.322  53.601  1.00 64.21  ?  174 ARG B O   1 
ATOM   6582  C  CB  . ARG B  2  174 ? 87.901  17.573  51.758  1.00 63.85  ?  174 ARG B CB  1 
ATOM   6583  C  CG  . ARG B  2  174 ? 87.309  17.280  50.379  1.00 72.15  ?  174 ARG B CG  1 
ATOM   6584  C  CD  . ARG B  2  174 ? 86.148  16.302  50.463  1.00 80.33  ?  174 ARG B CD  1 
ATOM   6585  N  NE  . ARG B  2  174 ? 86.444  15.014  49.831  1.00 81.61  ?  174 ARG B NE  1 
ATOM   6586  C  CZ  . ARG B  2  174 ? 86.149  14.685  48.573  1.00 100.40 ?  174 ARG B CZ  1 
ATOM   6587  N  NH1 . ARG B  2  174 ? 85.542  15.557  47.771  1.00 73.61  ?  174 ARG B NH1 1 
ATOM   6588  N  NH2 . ARG B  2  174 ? 86.463  13.482  48.106  1.00 100.52 ?  174 ARG B NH2 1 
ATOM   6589  N  N   . LYS B  2  175 ? 89.757  18.521  54.071  1.00 73.82  ?  175 LYS B N   1 
ATOM   6590  C  CA  . LYS B  2  175 ? 89.984  18.873  55.474  1.00 66.24  ?  175 LYS B CA  1 
ATOM   6591  C  C   . LYS B  2  175 ? 90.702  20.221  55.606  1.00 64.43  ?  175 LYS B C   1 
ATOM   6592  O  O   . LYS B  2  175 ? 90.431  20.967  56.541  1.00 76.70  ?  175 LYS B O   1 
ATOM   6593  C  CB  . LYS B  2  175 ? 90.798  17.768  56.166  1.00 83.84  ?  175 LYS B CB  1 
ATOM   6594  C  CG  . LYS B  2  175 ? 90.711  17.794  57.685  1.00 96.89  ?  175 LYS B CG  1 
ATOM   6595  C  CD  . LYS B  2  175 ? 91.965  17.212  58.349  1.00 110.86 ?  175 LYS B CD  1 
ATOM   6596  C  CE  . LYS B  2  175 ? 91.924  17.276  59.864  1.00 109.83 ?  175 LYS B CE  1 
ATOM   6597  N  NZ  . LYS B  2  175 ? 91.842  18.675  60.380  1.00 125.73 ?  175 LYS B NZ  1 
ATOM   6598  N  N   . LEU B  2  176 ? 91.613  20.531  54.680  1.00 69.07  ?  176 LEU B N   1 
ATOM   6599  C  CA  . LEU B  2  176 ? 92.366  21.787  54.695  1.00 72.27  ?  176 LEU B CA  1 
ATOM   6600  C  C   . LEU B  2  176 ? 91.578  22.980  54.089  1.00 70.29  ?  176 LEU B C   1 
ATOM   6601  O  O   . LEU B  2  176 ? 91.909  24.136  54.348  1.00 66.37  ?  176 LEU B O   1 
ATOM   6602  C  CB  . LEU B  2  176 ? 93.683  21.564  53.927  1.00 57.76  ?  176 LEU B CB  1 
ATOM   6603  C  CG  . LEU B  2  176 ? 94.737  22.659  54.022  1.00 56.31  ?  176 LEU B CG  1 
ATOM   6604  C  CD1 . LEU B  2  176 ? 95.271  22.796  55.432  1.00 65.38  ?  176 LEU B CD1 1 
ATOM   6605  C  CD2 . LEU B  2  176 ? 95.882  22.371  53.090  1.00 67.85  ?  176 LEU B CD2 1 
ATOM   6606  N  N   . GLY B  2  177 ? 90.551  22.684  53.301  1.00 68.20  ?  177 GLY B N   1 
ATOM   6607  C  CA  . GLY B  2  177 ? 89.726  23.695  52.655  1.00 63.33  ?  177 GLY B CA  1 
ATOM   6608  C  C   . GLY B  2  177 ? 90.282  24.155  51.323  1.00 60.85  ?  177 GLY B C   1 
ATOM   6609  O  O   . GLY B  2  177 ? 89.954  25.255  50.869  1.00 71.74  ?  177 GLY B O   1 
ATOM   6610  N  N   . VAL B  2  178 ? 91.126  23.320  50.675  1.00 68.68  ?  178 VAL B N   1 
ATOM   6611  C  CA  . VAL B  2  178 ? 91.736  23.660  49.383  1.00 59.37  ?  178 VAL B CA  1 
ATOM   6612  C  C   . VAL B  2  178 ? 91.283  22.732  48.256  1.00 58.10  ?  178 VAL B C   1 
ATOM   6613  O  O   . VAL B  2  178 ? 91.950  22.682  47.229  1.00 59.95  ?  178 VAL B O   1 
ATOM   6614  C  CB  . VAL B  2  178 ? 93.285  23.732  49.449  1.00 51.50  ?  178 VAL B CB  1 
ATOM   6615  C  CG1 . VAL B  2  178 ? 93.743  24.742  50.493  1.00 64.45  ?  178 VAL B CG1 1 
ATOM   6616  C  CG2 . VAL B  2  178 ? 93.903  22.361  49.711  1.00 54.13  ?  178 VAL B CG2 1 
ATOM   6617  N  N   . TYR B  2  179 ? 90.160  22.033  48.440  1.00 61.57  ?  179 TYR B N   1 
ATOM   6618  C  CA  . TYR B  2  179 ? 89.627  21.187  47.340  1.00 54.02  ?  179 TYR B CA  1 
ATOM   6619  C  C   . TYR B  2  179 ? 89.316  22.087  46.140  1.00 61.54  ?  179 TYR B C   1 
ATOM   6620  O  O   . TYR B  2  179 ? 88.836  23.215  46.348  1.00 71.18  ?  179 TYR B O   1 
ATOM   6621  C  CB  . TYR B  2  179 ? 88.405  20.386  47.795  1.00 65.37  ?  179 TYR B CB  1 
ATOM   6622  C  CG  . TYR B  2  179 ? 88.139  19.151  46.972  1.00 60.20  ?  179 TYR B CG  1 
ATOM   6623  C  CD1 . TYR B  2  179 ? 88.852  17.984  47.183  1.00 75.17  ?  179 TYR B CD1 1 
ATOM   6624  C  CD2 . TYR B  2  179 ? 87.185  19.154  45.968  1.00 58.67  ?  179 TYR B CD2 1 
ATOM   6625  C  CE1 . TYR B  2  179 ? 88.619  16.847  46.426  1.00 84.06  ?  179 TYR B CE1 1 
ATOM   6626  C  CE2 . TYR B  2  179 ? 86.939  18.028  45.201  1.00 56.53  ?  179 TYR B CE2 1 
ATOM   6627  C  CZ  . TYR B  2  179 ? 87.659  16.869  45.431  1.00 71.11  ?  179 TYR B CZ  1 
ATOM   6628  O  OH  . TYR B  2  179 ? 87.419  15.749  44.675  1.00 82.88  ?  179 TYR B OH  1 
ATOM   6629  N  N   . PRO B  2  180 ? 89.560  21.640  44.890  1.00 64.94  ?  180 PRO B N   1 
ATOM   6630  C  CA  . PRO B  2  180 ? 89.382  22.507  43.715  1.00 60.32  ?  180 PRO B CA  1 
ATOM   6631  C  C   . PRO B  2  180 ? 87.939  22.795  43.275  1.00 64.85  ?  180 PRO B C   1 
ATOM   6632  O  O   . PRO B  2  180 ? 87.121  21.899  43.353  1.00 72.13  ?  180 PRO B O   1 
ATOM   6633  C  CB  . PRO B  2  180 ? 90.082  21.703  42.608  1.00 51.64  ?  180 PRO B CB  1 
ATOM   6634  C  CG  . PRO B  2  180 ? 89.910  20.265  43.033  1.00 60.99  ?  180 PRO B CG  1 
ATOM   6635  C  CD  . PRO B  2  180 ? 90.038  20.300  44.541  1.00 71.26  ?  180 PRO B CD  1 
ATOM   6636  N  N   . ARG B  2  181 ? 87.668  24.027  42.834  1.00 61.36  ?  181 ARG B N   1 
ATOM   6637  C  CA  . ARG B  2  181 ? 86.352  24.402  42.310  1.00 52.41  ?  181 ARG B CA  1 
ATOM   6638  C  C   . ARG B  2  181 ? 86.556  24.557  40.784  1.00 54.73  ?  181 ARG B C   1 
ATOM   6639  O  O   . ARG B  2  181 ? 87.540  24.019  40.282  1.00 56.54  ?  181 ARG B O   1 
ATOM   6640  C  CB  . ARG B  2  181 ? 85.847  25.700  42.984  1.00 53.60  ?  181 ARG B CB  1 
ATOM   6641  C  CG  . ARG B  2  181 ? 85.596  25.543  44.481  1.00 61.38  ?  181 ARG B CG  1 
ATOM   6642  C  CD  . ARG B  2  181 ? 85.112  26.818  45.147  1.00 56.62  ?  181 ARG B CD  1 
ATOM   6643  N  NE  . ARG B  2  181 ? 86.178  27.811  45.289  1.00 66.89  ?  181 ARG B NE  1 
ATOM   6644  C  CZ  . ARG B  2  181 ? 86.036  28.996  45.877  1.00 74.41  ?  181 ARG B CZ  1 
ATOM   6645  N  NH1 . ARG B  2  181 ? 84.864  29.360  46.381  1.00 75.05  ?  181 ARG B NH1 1 
ATOM   6646  N  NH2 . ARG B  2  181 ? 87.066  29.828  45.962  1.00 71.29  ?  181 ARG B NH2 1 
ATOM   6647  N  N   . ALA B  2  182 ? 85.670  25.248  40.036  1.00 53.98  ?  182 ALA B N   1 
ATOM   6648  C  CA  . ALA B  2  182 ? 85.874  25.397  38.589  1.00 57.56  ?  182 ALA B CA  1 
ATOM   6649  C  C   . ALA B  2  182 ? 87.177  26.163  38.303  1.00 62.67  ?  182 ALA B C   1 
ATOM   6650  O  O   . ALA B  2  182 ? 87.608  26.972  39.123  1.00 61.24  ?  182 ALA B O   1 
ATOM   6651  C  CB  . ALA B  2  182 ? 84.690  26.098  37.953  1.00 64.26  ?  182 ALA B CB  1 
ATOM   6652  N  N   . VAL B  2  183 ? 87.805  25.904  37.149  1.00 57.66  ?  183 VAL B N   1 
ATOM   6653  C  CA  . VAL B  2  183 ? 89.086  26.535  36.822  1.00 58.72  ?  183 VAL B CA  1 
ATOM   6654  C  C   . VAL B  2  183 ? 89.013  28.071  36.853  1.00 60.52  ?  183 VAL B C   1 
ATOM   6655  O  O   . VAL B  2  183 ? 89.682  28.706  37.674  1.00 59.79  ?  183 VAL B O   1 
ATOM   6656  C  CB  . VAL B  2  183 ? 89.704  26.033  35.486  1.00 52.36  ?  183 VAL B CB  1 
ATOM   6657  C  CG1 . VAL B  2  183 ? 91.115  26.582  35.313  1.00 51.87  ?  183 VAL B CG1 1 
ATOM   6658  C  CG2 . VAL B  2  183 ? 89.711  24.509  35.399  1.00 55.96  ?  183 VAL B CG2 1 
ATOM   6659  N  N   . ASP B  2  184 ? 88.243  28.656  35.932  1.00 58.57  ?  184 ASP B N   1 
ATOM   6660  C  CA  . ASP B  2  184 ? 88.184  30.140  35.828  1.00 59.16  ?  184 ASP B CA  1 
ATOM   6661  C  C   . ASP B  2  184 ? 87.629  30.738  37.126  1.00 60.72  ?  184 ASP B C   1 
ATOM   6662  O  O   . ASP B  2  184 ? 88.042  31.859  37.477  1.00 64.09  ?  184 ASP B O   1 
ATOM   6663  C  CB  . ASP B  2  184 ? 87.376  30.569  34.601  1.00 60.30  ?  184 ASP B CB  1 
ATOM   6664  C  CG  . ASP B  2  184 ? 87.686  29.752  33.359  1.00 71.22  ?  184 ASP B CG  1 
ATOM   6665  O  OD1 . ASP B  2  184 ? 88.857  29.359  33.195  1.00 60.65  ?  184 ASP B OD1 1 
ATOM   6666  O  OD2 . ASP B  2  184 ? 86.753  29.516  32.567  1.00 84.11  ?  184 ASP B OD2 1 
ATOM   6667  N  N   . ARG B  2  185 ? 86.731  30.018  37.802  1.00 56.58  ?  185 ARG B N   1 
ATOM   6668  C  CA  . ARG B  2  185 ? 86.103  30.528  39.051  1.00 64.73  ?  185 ARG B CA  1 
ATOM   6669  C  C   . ARG B  2  185 ? 87.187  30.771  40.105  1.00 59.22  ?  185 ARG B C   1 
ATOM   6670  O  O   . ARG B  2  185 ? 87.114  31.803  40.798  1.00 66.06  ?  185 ARG B O   1 
ATOM   6671  C  CB  . ARG B  2  185 ? 85.066  29.523  39.560  1.00 54.09  ?  185 ARG B CB  1 
ATOM   6672  C  CG  . ARG B  2  185 ? 84.294  29.983  40.787  1.00 56.65  ?  185 ARG B CG  1 
ATOM   6673  C  CD  . ARG B  2  185 ? 84.933  29.515  42.081  1.00 61.83  ?  185 ARG B CD  1 
ATOM   6674  N  NE  . ARG B  2  185 ? 84.234  30.002  43.262  1.00 69.88  ?  185 ARG B NE  1 
ATOM   6675  C  CZ  . ARG B  2  185 ? 83.956  31.278  43.502  1.00 58.64  ?  185 ARG B CZ  1 
ATOM   6676  N  NH1 . ARG B  2  185 ? 84.497  32.226  42.759  1.00 65.23  ?  185 ARG B NH1 1 
ATOM   6677  N  NH2 . ARG B  2  185 ? 83.135  31.601  44.486  1.00 72.08  ?  185 ARG B NH2 1 
ATOM   6678  N  N   . GLU B  2  186 ? 88.149  29.854  40.217  1.00 57.99  ?  186 GLU B N   1 
ATOM   6679  C  CA  . GLU B  2  186 ? 89.217  29.974  41.244  1.00 63.70  ?  186 GLU B CA  1 
ATOM   6680  C  C   . GLU B  2  186 ? 90.141  31.143  40.887  1.00 60.86  ?  186 GLU B C   1 
ATOM   6681  O  O   . GLU B  2  186 ? 90.584  31.847  41.814  1.00 58.85  ?  186 GLU B O   1 
ATOM   6682  C  CB  . GLU B  2  186 ? 89.998  28.663  41.350  1.00 59.86  ?  186 GLU B CB  1 
ATOM   6683  C  CG  . GLU B  2  186 ? 89.203  27.539  41.987  1.00 66.18  ?  186 GLU B CG  1 
ATOM   6684  C  CD  . GLU B  2  186 ? 89.238  27.522  43.505  1.00 79.86  ?  186 GLU B CD  1 
ATOM   6685  O  OE1 . GLU B  2  186 ? 89.921  28.386  44.090  1.00 72.54  ?  186 GLU B OE1 1 
ATOM   6686  O  OE2 . GLU B  2  186 ? 88.583  26.644  44.098  1.00 81.02  ?  186 GLU B OE2 1 
ATOM   6687  N  N   . ILE B  2  187 ? 90.422  31.335  39.595  1.00 56.22  ?  187 ILE B N   1 
ATOM   6688  C  CA  . ILE B  2  187 ? 91.281  32.442  39.179  1.00 53.66  ?  187 ILE B CA  1 
ATOM   6689  C  C   . ILE B  2  187 ? 90.611  33.740  39.664  1.00 59.89  ?  187 ILE B C   1 
ATOM   6690  O  O   . ILE B  2  187 ? 91.282  34.616  40.202  1.00 67.25  ?  187 ILE B O   1 
ATOM   6691  C  CB  . ILE B  2  187 ? 91.501  32.445  37.640  1.00 45.97  ?  187 ILE B CB  1 
ATOM   6692  C  CG1 . ILE B  2  187 ? 92.200  31.142  37.178  1.00 48.51  ?  187 ILE B CG1 1 
ATOM   6693  C  CG2 . ILE B  2  187 ? 92.312  33.677  37.213  1.00 40.50  ?  187 ILE B CG2 1 
ATOM   6694  C  CD1 . ILE B  2  187 ? 92.170  30.917  35.713  1.00 54.51  ?  187 ILE B CD1 1 
ATOM   6695  N  N   . ALA B  2  188 ? 89.275  33.837  39.500  1.00 54.30  ?  188 ALA B N   1 
ATOM   6696  C  CA  . ALA B  2  188 ? 88.507  34.995  39.942  1.00 57.27  ?  188 ALA B CA  1 
ATOM   6697  C  C   . ALA B  2  188 ? 88.612  35.142  41.462  1.00 59.32  ?  188 ALA B C   1 
ATOM   6698  O  O   . ALA B  2  188 ? 88.764  36.253  41.959  1.00 60.87  ?  188 ALA B O   1 
ATOM   6699  C  CB  . ALA B  2  188 ? 87.049  34.841  39.531  1.00 47.06  ?  188 ALA B CB  1 
ATOM   6700  N  N   . ALA B  2  189 ? 88.546  34.025  42.198  1.00 53.92  ?  189 ALA B N   1 
ATOM   6701  C  CA  . ALA B  2  189 ? 88.647  34.049  43.652  1.00 50.26  ?  189 ALA B CA  1 
ATOM   6702  C  C   . ALA B  2  189 ? 89.992  34.629  44.115  1.00 59.06  ?  189 ALA B C   1 
ATOM   6703  O  O   . ALA B  2  189 ? 90.025  35.385  45.085  1.00 68.06  ?  189 ALA B O   1 
ATOM   6704  C  CB  . ALA B  2  189 ? 88.472  32.645  44.205  1.00 50.88  ?  189 ALA B CB  1 
ATOM   6705  N  N   . VAL B  2  190 ? 91.095  34.280  43.436  1.00 55.68  ?  190 VAL B N   1 
ATOM   6706  C  CA  . VAL B  2  190 ? 92.412  34.788  43.816  1.00 44.57  ?  190 VAL B CA  1 
ATOM   6707  C  C   . VAL B  2  190 ? 92.487  36.259  43.455  1.00 58.65  ?  190 VAL B C   1 
ATOM   6708  O  O   . VAL B  2  190 ? 92.897  37.072  44.280  1.00 72.67  ?  190 VAL B O   1 
ATOM   6709  C  CB  . VAL B  2  190 ? 93.565  33.994  43.156  1.00 59.34  ?  190 VAL B CB  1 
ATOM   6710  C  CG1 . VAL B  2  190 ? 94.912  34.663  43.427  1.00 51.70  ?  190 VAL B CG1 1 
ATOM   6711  C  CG2 . VAL B  2  190 ? 93.576  32.547  43.636  1.00 63.44  ?  190 VAL B CG2 1 
ATOM   6712  N  N   . MET B  2  191 ? 92.079  36.613  42.231  1.00 55.33  ?  191 MET B N   1 
ATOM   6713  C  CA  . MET B  2  191 ? 92.111  38.009  41.796  1.00 57.21  ?  191 MET B CA  1 
ATOM   6714  C  C   . MET B  2  191 ? 91.228  38.891  42.682  1.00 58.05  ?  191 MET B C   1 
ATOM   6715  O  O   . MET B  2  191 ? 91.536  40.066  42.862  1.00 61.75  ?  191 MET B O   1 
ATOM   6716  C  CB  . MET B  2  191 ? 91.689  38.134  40.323  1.00 47.25  ?  191 MET B CB  1 
ATOM   6717  C  CG  . MET B  2  191 ? 92.701  37.562  39.337  1.00 63.50  ?  191 MET B CG  1 
ATOM   6718  S  SD  . MET B  2  191 ? 94.421  38.100  39.555  1.00 56.65  ?  191 MET B SD  1 
ATOM   6719  C  CE  . MET B  2  191 ? 94.262  39.852  39.264  1.00 61.74  ?  191 MET B CE  1 
ATOM   6720  N  N   . HIS B  2  192 ? 90.152  38.331  43.250  1.00 56.94  ?  192 HIS B N   1 
ATOM   6721  C  CA  . HIS B  2  192 ? 89.254  39.077  44.121  1.00 62.71  ?  192 HIS B CA  1 
ATOM   6722  C  C   . HIS B  2  192 ? 89.894  39.294  45.494  1.00 60.42  ?  192 HIS B C   1 
ATOM   6723  O  O   . HIS B  2  192 ? 90.026  40.434  45.927  1.00 63.49  ?  192 HIS B O   1 
ATOM   6724  C  CB  . HIS B  2  192 ? 87.908  38.342  44.253  1.00 64.07  ?  192 HIS B CB  1 
ATOM   6725  C  CG  . HIS B  2  192 ? 86.992  38.899  45.299  1.00 57.33  ?  192 HIS B CG  1 
ATOM   6726  N  ND1 . HIS B  2  192 ? 86.184  38.077  46.052  1.00 61.80  ?  192 HIS B ND1 1 
ATOM   6727  C  CD2 . HIS B  2  192 ? 86.780  40.181  45.679  1.00 68.85  ?  192 HIS B CD2 1 
ATOM   6728  C  CE1 . HIS B  2  192 ? 85.501  38.873  46.858  1.00 71.66  ?  192 HIS B CE1 1 
ATOM   6729  N  NE2 . HIS B  2  192 ? 85.833  40.150  46.674  1.00 67.64  ?  192 HIS B NE2 1 
ATOM   6730  N  N   . SER B  2  193 ? 90.299  38.218  46.178  1.00 68.55  ?  193 SER B N   1 
ATOM   6731  C  CA  . SER B  2  193 ? 90.900  38.329  47.505  1.00 62.39  ?  193 SER B CA  1 
ATOM   6732  C  C   . SER B  2  193 ? 92.201  39.140  47.520  1.00 62.55  ?  193 SER B C   1 
ATOM   6733  O  O   . SER B  2  193 ? 92.563  39.688  48.561  1.00 67.45  ?  193 SER B O   1 
ATOM   6734  C  CB  . SER B  2  193 ? 91.122  36.944  48.094  1.00 59.28  ?  193 SER B CB  1 
ATOM   6735  O  OG  . SER B  2  193 ? 89.884  36.263  48.219  1.00 62.67  ?  193 SER B OG  1 
ATOM   6736  N  N   . THR B  2  194 ? 92.899  39.231  46.381  1.00 56.64  ?  194 THR B N   1 
ATOM   6737  C  CA  . THR B  2  194 ? 94.131  40.020  46.300  1.00 60.04  ?  194 THR B CA  1 
ATOM   6738  C  C   . THR B  2  194 ? 93.815  41.519  46.104  1.00 66.27  ?  194 THR B C   1 
ATOM   6739  O  O   . THR B  2  194 ? 94.699  42.352  46.291  1.00 64.97  ?  194 THR B O   1 
ATOM   6740  C  CB  . THR B  2  194 ? 95.039  39.494  45.181  1.00 59.13  ?  194 THR B CB  1 
ATOM   6741  O  OG1 . THR B  2  194 ? 94.280  39.378  43.973  1.00 64.45  ?  194 THR B OG1 1 
ATOM   6742  C  CG2 . THR B  2  194 ? 95.708  38.166  45.541  1.00 59.10  ?  194 THR B CG2 1 
ATOM   6743  N  N   . HIS B  2  195 ? 92.569  41.864  45.727  1.00 59.64  ?  195 HIS B N   1 
ATOM   6744  C  CA  . HIS B  2  195 ? 92.161  43.252  45.535  1.00 62.83  ?  195 HIS B CA  1 
ATOM   6745  C  C   . HIS B  2  195 ? 92.257  43.999  46.868  1.00 61.34  ?  195 HIS B C   1 
ATOM   6746  O  O   . HIS B  2  195 ? 92.129  43.391  47.933  1.00 75.28  ?  195 HIS B O   1 
ATOM   6747  C  CB  . HIS B  2  195 ? 90.729  43.309  44.967  1.00 61.41  ?  195 HIS B CB  1 
ATOM   6748  C  CG  . HIS B  2  195 ? 90.149  44.686  44.851  1.00 65.82  ?  195 HIS B CG  1 
ATOM   6749  N  ND1 . HIS B  2  195 ? 90.887  45.750  44.362  1.00 73.96  ?  195 HIS B ND1 1 
ATOM   6750  C  CD2 . HIS B  2  195 ? 88.899  45.120  45.133  1.00 73.08  ?  195 HIS B CD2 1 
ATOM   6751  C  CE1 . HIS B  2  195 ? 90.080  46.797  44.402  1.00 77.09  ?  195 HIS B CE1 1 
ATOM   6752  N  NE2 . HIS B  2  195 ? 88.865  46.461  44.835  1.00 56.32  ?  195 HIS B NE2 1 
ATOM   6753  N  N   . ILE B  2  196 ? 92.436  45.318  46.776  1.00 61.35  ?  196 ILE B N   1 
ATOM   6754  C  CA  . ILE B  2  196 ? 92.614  46.153  47.998  1.00 54.04  ?  196 ILE B CA  1 
ATOM   6755  C  C   . ILE B  2  196 ? 91.444  45.957  48.961  1.00 68.76  ?  196 ILE B C   1 
ATOM   6756  O  O   . ILE B  2  196 ? 90.297  45.833  48.490  1.00 79.93  ?  196 ILE B O   1 
ATOM   6757  C  CB  . ILE B  2  196 ? 92.802  47.637  47.617  1.00 64.42  ?  196 ILE B CB  1 
ATOM   6758  C  CG1 . ILE B  2  196 ? 93.510  48.422  48.725  1.00 62.90  ?  196 ILE B CG1 1 
ATOM   6759  C  CG2 . ILE B  2  196 ? 91.476  48.273  47.228  1.00 77.10  ?  196 ILE B CG2 1 
ATOM   6760  C  CD1 . ILE B  2  196 ? 92.572  49.060  49.721  1.00 64.62  ?  196 ILE B CD1 1 
ATOM   6761  N  N   . GLY B  2  197 ? 91.738  45.913  50.259  1.00 68.98  ?  197 GLY B N   1 
ATOM   6762  C  CA  . GLY B  2  197 ? 90.725  45.798  51.291  1.00 57.92  ?  197 GLY B CA  1 
ATOM   6763  C  C   . GLY B  2  197 ? 90.071  44.439  51.417  1.00 65.16  ?  197 GLY B C   1 
ATOM   6764  O  O   . GLY B  2  197 ? 88.964  44.354  51.950  1.00 65.40  ?  197 GLY B O   1 
ATOM   6765  N  N   . CYS B  2  198 ? 90.731  43.363  50.955  1.00 67.61  ?  198 CYS B N   1 
ATOM   6766  C  CA  . CYS B  2  198 ? 90.153  42.024  51.066  1.00 60.75  ?  198 CYS B CA  1 
ATOM   6767  C  C   . CYS B  2  198 ? 90.965  41.146  52.042  1.00 71.42  ?  198 CYS B C   1 
ATOM   6768  O  O   . CYS B  2  198 ? 90.972  41.439  53.237  1.00 64.71  ?  198 CYS B O   1 
ATOM   6769  C  CB  . CYS B  2  198 ? 89.996  41.374  49.693  1.00 55.14  ?  198 CYS B CB  1 
ATOM   6770  S  SG  . CYS B  2  198 ? 88.753  42.155  48.637  1.00 91.63  ?  198 CYS B SG  1 
ATOM   6771  N  N   . ASN B  2  199 ? 91.635  40.086  51.563  1.00 64.52  ?  199 ASN B N   1 
ATOM   6772  C  CA  . ASN B  2  199 ? 92.400  39.203  52.427  1.00 60.14  ?  199 ASN B CA  1 
ATOM   6773  C  C   . ASN B  2  199 ? 93.675  39.880  52.906  1.00 68.16  ?  199 ASN B C   1 
ATOM   6774  O  O   . ASN B  2  199 ? 94.388  40.493  52.117  1.00 75.44  ?  199 ASN B O   1 
ATOM   6775  C  CB  . ASN B  2  199 ? 92.719  37.908  51.689  1.00 61.03  ?  199 ASN B CB  1 
ATOM   6776  C  CG  . ASN B  2  199 ? 93.375  36.867  52.552  1.00 74.39  ?  199 ASN B CG  1 
ATOM   6777  O  OD1 . ASN B  2  199 ? 92.705  36.017  53.154  1.00 70.04  ?  199 ASN B OD1 1 
ATOM   6778  N  ND2 . ASN B  2  199 ? 94.698  36.909  52.632  1.00 67.95  ?  199 ASN B ND2 1 
ATOM   6779  N  N   . ALA B  2  200 ? 93.948  39.785  54.208  1.00 68.59  ?  200 ALA B N   1 
ATOM   6780  C  CA  . ALA B  2  200 ? 95.135  40.364  54.821  1.00 61.89  ?  200 ALA B CA  1 
ATOM   6781  C  C   . ALA B  2  200 ? 95.697  39.373  55.842  1.00 74.65  ?  200 ALA B C   1 
ATOM   6782  O  O   . ALA B  2  200 ? 96.013  39.742  56.974  1.00 70.08  ?  200 ALA B O   1 
ATOM   6783  C  CB  . ALA B  2  200 ? 94.797  41.689  55.485  1.00 76.73  ?  200 ALA B CB  1 
ATOM   6784  N  N   . ASP B  2  201 ? 95.819  38.104  55.420  1.00 69.78  ?  201 ASP B N   1 
ATOM   6785  C  CA  . ASP B  2  201 ? 96.354  37.011  56.227  1.00 67.14  ?  201 ASP B CA  1 
ATOM   6786  C  C   . ASP B  2  201 ? 97.191  36.134  55.297  1.00 68.85  ?  201 ASP B C   1 
ATOM   6787  O  O   . ASP B  2  201 ? 96.658  35.583  54.335  1.00 68.63  ?  201 ASP B O   1 
ATOM   6788  C  CB  . ASP B  2  201 ? 95.217  36.200  56.870  1.00 60.05  ?  201 ASP B CB  1 
ATOM   6789  C  CG  . ASP B  2  201 ? 95.683  35.158  57.871  1.00 77.87  ?  201 ASP B CG  1 
ATOM   6790  O  OD1 . ASP B  2  201 ? 96.898  34.853  57.894  1.00 80.59  ?  201 ASP B OD1 1 
ATOM   6791  O  OD2 . ASP B  2  201 ? 94.836  34.648  58.632  1.00 81.78  ?  201 ASP B OD2 1 
ATOM   6792  N  N   . ALA B  2  202 ? 98.498  36.021  55.562  1.00 69.30  ?  202 ALA B N   1 
ATOM   6793  C  CA  . ALA B  2  202 ? 99.385  35.229  54.713  1.00 58.51  ?  202 ALA B CA  1 
ATOM   6794  C  C   . ALA B  2  202 ? 98.945  33.762  54.600  1.00 67.93  ?  202 ALA B C   1 
ATOM   6795  O  O   . ALA B  2  202 ? 98.860  33.242  53.492  1.00 70.12  ?  202 ALA B O   1 
ATOM   6796  C  CB  . ALA B  2  202 ? 100.815 35.314  55.231  1.00 65.45  ?  202 ALA B CB  1 
ATOM   6797  N  N   . GLU B  2  203 ? 98.644  33.101  55.726  1.00 70.76  ?  203 GLU B N   1 
ATOM   6798  C  CA  . GLU B  2  203 ? 98.233  31.698  55.701  1.00 66.93  ?  203 GLU B CA  1 
ATOM   6799  C  C   . GLU B  2  203 ? 97.004  31.454  54.826  1.00 68.29  ?  203 GLU B C   1 
ATOM   6800  O  O   . GLU B  2  203 ? 96.975  30.476  54.082  1.00 57.15  ?  203 GLU B O   1 
ATOM   6801  C  CB  . GLU B  2  203 ? 97.963  31.186  57.125  1.00 71.34  ?  203 GLU B CB  1 
ATOM   6802  C  CG  . GLU B  2  203 ? 99.221  30.995  57.951  1.00 83.21  ?  203 GLU B CG  1 
ATOM   6803  C  CD  . GLU B  2  203 ? 99.052  30.104  59.164  1.00 91.47  ?  203 GLU B CD  1 
ATOM   6804  O  OE1 . GLU B  2  203 ? 98.145  29.240  59.150  1.00 97.79  ?  203 GLU B OE1 1 
ATOM   6805  O  OE2 . GLU B  2  203 ? 99.833  30.266  60.130  1.00 98.62  ?  203 GLU B OE2 1 
ATOM   6806  N  N   . ALA B  2  204 ? 95.992  32.323  54.917  1.00 73.13  ?  204 ALA B N   1 
ATOM   6807  C  CA  . ALA B  2  204 ? 94.770  32.165  54.134  1.00 48.04  ?  204 ALA B CA  1 
ATOM   6808  C  C   . ALA B  2  204 ? 95.051  32.401  52.659  1.00 64.29  ?  204 ALA B C   1 
ATOM   6809  O  O   . ALA B  2  204 ? 94.570  31.637  51.826  1.00 77.17  ?  204 ALA B O   1 
ATOM   6810  C  CB  . ALA B  2  204 ? 93.693  33.092  54.663  1.00 69.69  ?  204 ALA B CB  1 
ATOM   6811  N  N   . MET B  2  205 ? 95.817  33.448  52.325  1.00 58.13  ?  205 MET B N   1 
ATOM   6812  C  CA  . MET B  2  205 ? 96.133  33.747  50.931  1.00 58.36  ?  205 MET B CA  1 
ATOM   6813  C  C   . MET B  2  205 ? 96.920  32.625  50.251  1.00 62.00  ?  205 MET B C   1 
ATOM   6814  O  O   . MET B  2  205 ? 96.606  32.258  49.118  1.00 58.29  ?  205 MET B O   1 
ATOM   6815  C  CB  . MET B  2  205 ? 96.918  35.063  50.838  1.00 62.76  ?  205 MET B CB  1 
ATOM   6816  C  CG  . MET B  2  205 ? 97.018  35.606  49.430  1.00 54.05  ?  205 MET B CG  1 
ATOM   6817  S  SD  . MET B  2  205 ? 95.531  36.502  48.927  1.00 71.12  ?  205 MET B SD  1 
ATOM   6818  C  CE  . MET B  2  205 ? 94.799  35.333  47.806  1.00 50.72  ?  205 MET B CE  1 
ATOM   6819  N  N   . ILE B  2  206 ? 97.936  32.079  50.939  1.00 66.94  ?  206 ILE B N   1 
ATOM   6820  C  CA  . ILE B  2  206 ? 98.753  30.995  50.386  1.00 56.36  ?  206 ILE B CA  1 
ATOM   6821  C  C   . ILE B  2  206 ? 97.875  29.740  50.211  1.00 63.40  ?  206 ILE B C   1 
ATOM   6822  O  O   . ILE B  2  206 ? 98.085  28.997  49.256  1.00 65.59  ?  206 ILE B O   1 
ATOM   6823  C  CB  . ILE B  2  206 ? 100.044 30.738  51.228  1.00 45.99  ?  206 ILE B CB  1 
ATOM   6824  C  CG1 . ILE B  2  206 ? 100.908 32.017  51.390  1.00 54.93  ?  206 ILE B CG1 1 
ATOM   6825  C  CG2 . ILE B  2  206 ? 100.886 29.633  50.623  1.00 49.84  ?  206 ILE B CG2 1 
ATOM   6826  C  CD1 . ILE B  2  206 ? 101.569 32.597  50.098  1.00 56.76  ?  206 ILE B CD1 1 
ATOM   6827  N  N   . LYS B  2  207 ? 96.871  29.522  51.088  1.00 59.22  ?  207 LYS B N   1 
ATOM   6828  C  CA  . LYS B  2  207 ? 95.964  28.376  50.950  1.00 58.53  ?  207 LYS B CA  1 
ATOM   6829  C  C   . LYS B  2  207 ? 95.040  28.590  49.740  1.00 64.55  ?  207 LYS B C   1 
ATOM   6830  O  O   . LYS B  2  207 ? 94.719  27.630  49.043  1.00 75.87  ?  207 LYS B O   1 
ATOM   6831  C  CB  . LYS B  2  207 ? 95.121  28.161  52.225  1.00 49.54  ?  207 LYS B CB  1 
ATOM   6832  C  CG  . LYS B  2  207 ? 95.884  27.509  53.384  1.00 64.38  ?  207 LYS B CG  1 
ATOM   6833  C  CD  . LYS B  2  207 ? 95.083  26.421  54.129  1.00 56.58  ?  207 LYS B CD  1 
ATOM   6834  C  CE  . LYS B  2  207 ? 94.435  26.911  55.404  1.00 73.01  ?  207 LYS B CE  1 
ATOM   6835  N  NZ  . LYS B  2  207 ? 95.408  27.048  56.524  1.00 79.63  ?  207 LYS B NZ  1 
ATOM   6836  N  N   . MET B  2  208 ? 94.618  29.837  49.482  1.00 46.91  ?  208 MET B N   1 
ATOM   6837  C  CA  . MET B  2  208 ? 93.763  30.133  48.334  1.00 54.84  ?  208 MET B CA  1 
ATOM   6838  C  C   . MET B  2  208 ? 94.520  29.886  47.035  1.00 61.84  ?  208 MET B C   1 
ATOM   6839  O  O   . MET B  2  208 ? 93.941  29.368  46.081  1.00 69.73  ?  208 MET B O   1 
ATOM   6840  C  CB  . MET B  2  208 ? 93.306  31.596  48.354  1.00 55.81  ?  208 MET B CB  1 
ATOM   6841  C  CG  . MET B  2  208 ? 92.056  31.831  49.139  1.00 66.05  ?  208 MET B CG  1 
ATOM   6842  S  SD  . MET B  2  208 ? 91.479  33.519  48.903  1.00 50.36  ?  208 MET B SD  1 
ATOM   6843  C  CE  . MET B  2  208 ? 91.819  34.189  50.507  1.00 81.07  ?  208 MET B CE  1 
ATOM   6844  N  N   . SER B  2  209 ? 95.807  30.271  46.984  1.00 57.34  ?  209 SER B N   1 
ATOM   6845  C  CA  . SER B  2  209 ? 96.622  30.060  45.791  1.00 59.08  ?  209 SER B CA  1 
ATOM   6846  C  C   . SER B  2  209 ? 96.815  28.559  45.540  1.00 61.15  ?  209 SER B C   1 
ATOM   6847  O  O   . SER B  2  209 ? 96.843  28.136  44.387  1.00 56.69  ?  209 SER B O   1 
ATOM   6848  C  CB  . SER B  2  209 ? 97.974  30.751  45.936  1.00 54.06  ?  209 SER B CB  1 
ATOM   6849  O  OG  . SER B  2  209 ? 98.797  30.087  46.879  1.00 64.11  ?  209 SER B OG  1 
ATOM   6850  N  N   . MET B  2  210 ? 96.934  27.771  46.610  1.00 57.21  ?  210 MET B N   1 
ATOM   6851  C  CA  . MET B  2  210 ? 97.127  26.303  46.459  1.00 57.12  ?  210 MET B CA  1 
ATOM   6852  C  C   . MET B  2  210 ? 95.863  25.690  45.849  1.00 59.63  ?  210 MET B C   1 
ATOM   6853  O  O   . MET B  2  210 ? 95.999  24.821  44.969  1.00 53.38  ?  210 MET B O   1 
ATOM   6854  C  CB  . MET B  2  210 ? 97.418  25.655  47.815  1.00 64.97  ?  210 MET B CB  1 
ATOM   6855  C  CG  . MET B  2  210 ? 98.716  26.135  48.434  1.00 57.93  ?  210 MET B CG  1 
ATOM   6856  S  SD  . MET B  2  210 ? 98.799  25.800  50.207  1.00 60.89  ?  210 MET B SD  1 
ATOM   6857  C  CE  . MET B  2  210 ? 98.360  24.064  50.221  1.00 59.28  ?  210 MET B CE  1 
ATOM   6858  N  N   . ARG B  2  211 ? 94.686  26.132  46.295  1.00 57.16  ?  211 ARG B N   1 
ATOM   6859  C  CA  . ARG B  2  211 ? 93.419  25.639  45.761  1.00 58.21  ?  211 ARG B CA  1 
ATOM   6860  C  C   . ARG B  2  211 ? 93.321  25.983  44.265  1.00 65.00  ?  211 ARG B C   1 
ATOM   6861  O  O   . ARG B  2  211 ? 92.865  25.165  43.469  1.00 69.47  ?  211 ARG B O   1 
ATOM   6862  C  CB  . ARG B  2  211 ? 92.259  26.277  46.533  1.00 54.88  ?  211 ARG B CB  1 
ATOM   6863  C  CG  . ARG B  2  211 ? 90.896  25.692  46.241  1.00 50.67  ?  211 ARG B CG  1 
ATOM   6864  C  CD  . ARG B  2  211 ? 89.827  26.486  46.964  1.00 66.94  ?  211 ARG B CD  1 
ATOM   6865  N  NE  . ARG B  2  211 ? 88.650  25.674  47.260  1.00 77.25  ?  211 ARG B NE  1 
ATOM   6866  C  CZ  . ARG B  2  211 ? 87.630  26.077  48.010  1.00 79.85  ?  211 ARG B CZ  1 
ATOM   6867  N  NH1 . ARG B  2  211 ? 87.628  27.293  48.545  1.00 87.93  ?  211 ARG B NH1 1 
ATOM   6868  N  NH2 . ARG B  2  211 ? 86.600  25.268  48.231  1.00 74.08  ?  211 ARG B NH2 1 
ATOM   6869  N  N   . CYS B  2  212 ? 93.754  27.192  43.891  1.00 58.36  ?  212 CYS B N   1 
ATOM   6870  C  CA  . CYS B  2  212 ? 93.728  27.634  42.505  1.00 58.20  ?  212 CYS B CA  1 
ATOM   6871  C  C   . CYS B  2  212 ? 94.705  26.799  41.672  1.00 63.30  ?  212 CYS B C   1 
ATOM   6872  O  O   . CYS B  2  212 ? 94.337  26.309  40.603  1.00 63.17  ?  212 CYS B O   1 
ATOM   6873  C  CB  . CYS B  2  212 ? 94.047  29.126  42.423  1.00 49.09  ?  212 CYS B CB  1 
ATOM   6874  S  SG  . CYS B  2  212 ? 94.205  29.770  40.736  1.00 64.38  ?  212 CYS B SG  1 
ATOM   6875  N  N   . SER B  2  213 ? 95.941  26.613  42.168  1.00 66.92  ?  213 SER B N   1 
ATOM   6876  C  CA  . SER B  2  213 ? 96.959  25.832  41.467  1.00 56.25  ?  213 SER B CA  1 
ATOM   6877  C  C   . SER B  2  213 ? 96.479  24.413  41.184  1.00 52.26  ?  213 SER B C   1 
ATOM   6878  O  O   . SER B  2  213 ? 96.833  23.858  40.150  1.00 56.35  ?  213 SER B O   1 
ATOM   6879  C  CB  . SER B  2  213 ? 98.255  25.797  42.271  1.00 54.08  ?  213 SER B CB  1 
ATOM   6880  O  OG  . SER B  2  213 ? 98.180  24.879  43.349  1.00 56.95  ?  213 SER B OG  1 
ATOM   6881  N  N   . LEU B  2  214 ? 95.663  23.826  42.077  1.00 54.24  ?  214 LEU B N   1 
ATOM   6882  C  CA  . LEU B  2  214 ? 95.155  22.468  41.855  1.00 54.51  ?  214 LEU B CA  1 
ATOM   6883  C  C   . LEU B  2  214 ? 94.266  22.400  40.623  1.00 51.98  ?  214 LEU B C   1 
ATOM   6884  O  O   . LEU B  2  214 ? 94.235  21.364  39.962  1.00 58.90  ?  214 LEU B O   1 
ATOM   6885  C  CB  . LEU B  2  214 ? 94.408  21.928  43.081  1.00 47.76  ?  214 LEU B CB  1 
ATOM   6886  C  CG  . LEU B  2  214 ? 95.262  21.643  44.304  1.00 52.41  ?  214 LEU B CG  1 
ATOM   6887  C  CD1 . LEU B  2  214 ? 94.402  21.200  45.448  1.00 59.45  ?  214 LEU B CD1 1 
ATOM   6888  C  CD2 . LEU B  2  214 ? 96.333  20.599  44.010  1.00 52.46  ?  214 LEU B CD2 1 
ATOM   6889  N  N   . THR B  2  215 ? 93.563  23.490  40.291  1.00 50.04  ?  215 THR B N   1 
ATOM   6890  C  CA  . THR B  2  215 ? 92.733  23.503  39.089  1.00 51.67  ?  215 THR B CA  1 
ATOM   6891  C  C   . THR B  2  215 ? 93.601  23.508  37.820  1.00 54.42  ?  215 THR B C   1 
ATOM   6892  O  O   . THR B  2  215 ? 93.060  23.415  36.727  1.00 58.23  ?  215 THR B O   1 
ATOM   6893  C  CB  . THR B  2  215 ? 91.807  24.719  39.055  1.00 61.49  ?  215 THR B CB  1 
ATOM   6894  O  OG1 . THR B  2  215 ? 92.578  25.911  38.907  1.00 57.35  ?  215 THR B OG1 1 
ATOM   6895  C  CG2 . THR B  2  215 ? 90.907  24.810  40.266  1.00 70.00  ?  215 THR B CG2 1 
ATOM   6896  N  N   . ASP B  2  216 ? 94.929  23.638  37.957  1.00 62.81  ?  216 ASP B N   1 
ATOM   6897  C  CA  . ASP B  2  216 ? 95.845  23.648  36.833  1.00 54.57  ?  216 ASP B CA  1 
ATOM   6898  C  C   . ASP B  2  216 ? 96.361  22.230  36.569  1.00 61.09  ?  216 ASP B C   1 
ATOM   6899  O  O   . ASP B  2  216 ? 96.231  21.737  35.455  1.00 56.73  ?  216 ASP B O   1 
ATOM   6900  C  CB  . ASP B  2  216 ? 97.020  24.605  37.119  1.00 53.08  ?  216 ASP B CB  1 
ATOM   6901  C  CG  . ASP B  2  216 ? 98.049  24.692  36.011  1.00 59.92  ?  216 ASP B CG  1 
ATOM   6902  O  OD1 . ASP B  2  216 ? 97.788  24.159  34.912  1.00 75.86  ?  216 ASP B OD1 1 
ATOM   6903  O  OD2 . ASP B  2  216 ? 99.117  25.299  36.240  1.00 65.90  ?  216 ASP B OD2 1 
ATOM   6904  N  N   . GLY B  2  217 ? 96.928  21.586  37.583  1.00 65.60  ?  217 GLY B N   1 
ATOM   6905  C  CA  . GLY B  2  217 ? 97.491  20.251  37.442  1.00 52.83  ?  217 GLY B CA  1 
ATOM   6906  C  C   . GLY B  2  217 ? 96.487  19.142  37.236  1.00 48.11  ?  217 GLY B C   1 
ATOM   6907  O  O   . GLY B  2  217 ? 96.593  18.385  36.274  1.00 53.55  ?  217 GLY B O   1 
ATOM   6908  N  N   . TRP B  2  218 ? 95.529  19.013  38.155  1.00 56.82  ?  218 TRP B N   1 
ATOM   6909  C  CA  . TRP B  2  218 ? 94.582  17.868  38.084  1.00 59.19  ?  218 TRP B CA  1 
ATOM   6910  C  C   . TRP B  2  218 ? 93.421  18.144  37.126  1.00 62.99  ?  218 TRP B C   1 
ATOM   6911  O  O   . TRP B  2  218 ? 92.570  17.252  36.968  1.00 63.29  ?  218 TRP B O   1 
ATOM   6912  C  CB  . TRP B  2  218 ? 94.213  17.401  39.497  1.00 38.99  ?  218 TRP B CB  1 
ATOM   6913  C  CG  . TRP B  2  218 ? 95.368  16.840  40.267  1.00 54.55  ?  218 TRP B CG  1 
ATOM   6914  C  CD1 . TRP B  2  218 ? 96.146  17.495  41.177  1.00 39.00  ?  218 TRP B CD1 1 
ATOM   6915  C  CD2 . TRP B  2  218 ? 95.881  15.499  40.193  1.00 58.76  ?  218 TRP B CD2 1 
ATOM   6916  N  NE1 . TRP B  2  218 ? 97.105  16.654  41.674  1.00 49.24  ?  218 TRP B NE1 1 
ATOM   6917  C  CE2 . TRP B  2  218 ? 96.968  15.424  41.089  1.00 58.33  ?  218 TRP B CE2 1 
ATOM   6918  C  CE3 . TRP B  2  218 ? 95.531  14.359  39.462  1.00 52.29  ?  218 TRP B CE3 1 
ATOM   6919  C  CZ2 . TRP B  2  218 ? 97.703  14.254  41.269  1.00 54.55  ?  218 TRP B CZ2 1 
ATOM   6920  C  CZ3 . TRP B  2  218 ? 96.258  13.204  39.640  1.00 69.38  ?  218 TRP B CZ3 1 
ATOM   6921  C  CH2 . TRP B  2  218 ? 97.328  13.154  40.532  1.00 68.64  ?  218 TRP B CH2 1 
ATOM   6922  N  N   . MET B  2  219 ? 93.401  19.324  36.501  1.00 59.22  ?  219 MET B N   1 
ATOM   6923  C  CA  . MET B  2  219 ? 92.266  19.682  35.608  1.00 50.78  ?  219 MET B CA  1 
ATOM   6924  C  C   . MET B  2  219 ? 92.696  20.220  34.241  1.00 51.47  ?  219 MET B C   1 
ATOM   6925  O  O   . MET B  2  219 ? 92.778  19.417  33.300  1.00 70.07  ?  219 MET B O   1 
ATOM   6926  C  CB  . MET B  2  219 ? 91.510  20.775  36.366  1.00 63.33  ?  219 MET B CB  1 
ATOM   6927  C  CG  . MET B  2  219 ? 90.595  20.220  37.432  1.00 65.42  ?  219 MET B CG  1 
ATOM   6928  S  SD  . MET B  2  219 ? 89.851  21.501  38.471  1.00 72.09  ?  219 MET B SD  1 
ATOM   6929  C  CE  . MET B  2  219 ? 88.249  21.669  37.688  1.00 63.24  ?  219 MET B CE  1 
ATOM   6930  N  N   . GLY B  2  220 ? 92.959  21.524  34.138  1.00 43.05  ?  220 GLY B N   1 
ATOM   6931  C  CA  . GLY B  2  220 ? 93.282  22.119  32.826  1.00 61.39  ?  220 GLY B CA  1 
ATOM   6932  C  C   . GLY B  2  220 ? 94.455  21.430  32.152  1.00 56.99  ?  220 GLY B C   1 
ATOM   6933  O  O   . GLY B  2  220 ? 94.306  21.020  30.986  1.00 60.53  ?  220 GLY B O   1 
ATOM   6934  N  N   . SER B  2  221 ? 95.577  21.297  32.863  1.00 43.17  ?  221 SER B N   1 
ATOM   6935  C  CA  . SER B  2  221 ? 96.778  20.640  32.288  1.00 50.77  ?  221 SER B CA  1 
ATOM   6936  C  C   . SER B  2  221 ? 96.480  19.157  32.054  1.00 52.71  ?  221 SER B C   1 
ATOM   6937  O  O   . SER B  2  221 ? 96.919  18.623  31.018  1.00 67.99  ?  221 SER B O   1 
ATOM   6938  C  CB  . SER B  2  221 ? 97.978  20.829  33.177  1.00 59.20  ?  221 SER B CB  1 
ATOM   6939  O  OG  . SER B  2  221 ? 98.362  22.195  33.220  1.00 67.20  ?  221 SER B OG  1 
ATOM   6940  N  N   . PHE B  2  222 ? 95.753  18.526  32.980  1.00 46.39  ?  222 PHE B N   1 
ATOM   6941  C  CA  . PHE B  2  222 ? 95.436  17.114  32.846  1.00 50.16  ?  222 PHE B CA  1 
ATOM   6942  C  C   . PHE B  2  222 ? 94.467  16.942  31.682  1.00 57.04  ?  222 PHE B C   1 
ATOM   6943  O  O   . PHE B  2  222 ? 94.666  16.058  30.851  1.00 65.03  ?  222 PHE B O   1 
ATOM   6944  C  CB  . PHE B  2  222 ? 94.801  16.586  34.148  1.00 42.66  ?  222 PHE B CB  1 
ATOM   6945  C  CG  . PHE B  2  222 ? 95.166  15.170  34.520  1.00 51.31  ?  222 PHE B CG  1 
ATOM   6946  C  CD1 . PHE B  2  222 ? 94.556  14.095  33.901  1.00 54.05  ?  222 PHE B CD1 1 
ATOM   6947  C  CD2 . PHE B  2  222 ? 96.096  14.916  35.512  1.00 58.70  ?  222 PHE B CD2 1 
ATOM   6948  C  CE1 . PHE B  2  222 ? 94.880  12.793  34.256  1.00 54.94  ?  222 PHE B CE1 1 
ATOM   6949  C  CE2 . PHE B  2  222 ? 96.423  13.614  35.862  1.00 57.90  ?  222 PHE B CE2 1 
ATOM   6950  C  CZ  . PHE B  2  222 ? 95.813  12.560  35.233  1.00 57.52  ?  222 PHE B CZ  1 
ATOM   6951  N  N   . MET B  2  223 ? 93.430  17.790  31.602  1.00 57.82  ?  223 MET B N   1 
ATOM   6952  C  CA  . MET B  2  223 ? 92.464  17.694  30.508  1.00 55.68  ?  223 MET B CA  1 
ATOM   6953  C  C   . MET B  2  223 ? 93.138  17.996  29.175  1.00 57.24  ?  223 MET B C   1 
ATOM   6954  O  O   . MET B  2  223 ? 92.893  17.295  28.200  1.00 56.32  ?  223 MET B O   1 
ATOM   6955  C  CB  . MET B  2  223 ? 91.284  18.654  30.719  1.00 57.35  ?  223 MET B CB  1 
ATOM   6956  C  CG  . MET B  2  223 ? 90.331  18.203  31.790  1.00 69.04  ?  223 MET B CG  1 
ATOM   6957  S  SD  . MET B  2  223 ? 88.796  19.148  31.777  1.00 77.36  ?  223 MET B SD  1 
ATOM   6958  C  CE  . MET B  2  223 ? 89.287  20.550  32.725  1.00 77.87  ?  223 MET B CE  1 
ATOM   6959  N  N   . GLY B  2  224 ? 93.978  19.028  29.144  1.00 54.03  ?  224 GLY B N   1 
ATOM   6960  C  CA  . GLY B  2  224 ? 94.699  19.438  27.945  1.00 49.22  ?  224 GLY B CA  1 
ATOM   6961  C  C   . GLY B  2  224 ? 95.532  18.312  27.385  1.00 54.47  ?  224 GLY B C   1 
ATOM   6962  O  O   . GLY B  2  224 ? 95.507  18.054  26.181  1.00 58.34  ?  224 GLY B O   1 
ATOM   6963  N  N   . THR B  2  225 ? 96.246  17.608  28.267  1.00 49.28  ?  225 THR B N   1 
ATOM   6964  C  CA  . THR B  2  225 ? 97.064  16.470  27.859  1.00 52.56  ?  225 THR B CA  1 
ATOM   6965  C  C   . THR B  2  225 ? 96.161  15.319  27.382  1.00 54.67  ?  225 THR B C   1 
ATOM   6966  O  O   . THR B  2  225 ? 96.337  14.833  26.266  1.00 58.54  ?  225 THR B O   1 
ATOM   6967  C  CB  . THR B  2  225 ? 97.972  16.039  29.018  1.00 40.29  ?  225 THR B CB  1 
ATOM   6968  O  OG1 . THR B  2  225 ? 98.911  17.080  29.279  1.00 48.04  ?  225 THR B OG1 1 
ATOM   6969  C  CG2 . THR B  2  225 ? 98.698  14.744  28.734  1.00 52.55  ?  225 THR B CG2 1 
ATOM   6970  N  N   . GLU B  2  226 ? 95.187  14.904  28.210  1.00 44.85  ?  226 GLU B N   1 
ATOM   6971  C  CA  . GLU B  2  226 ? 94.270  13.810  27.882  1.00 52.72  ?  226 GLU B CA  1 
ATOM   6972  C  C   . GLU B  2  226 ? 93.541  14.006  26.553  1.00 54.18  ?  226 GLU B C   1 
ATOM   6973  O  O   . GLU B  2  226 ? 93.488  13.080  25.749  1.00 56.39  ?  226 GLU B O   1 
ATOM   6974  C  CB  . GLU B  2  226 ? 93.222  13.644  28.990  1.00 64.83  ?  226 GLU B CB  1 
ATOM   6975  C  CG  . GLU B  2  226 ? 93.678  12.828  30.184  1.00 75.58  ?  226 GLU B CG  1 
ATOM   6976  C  CD  . GLU B  2  226 ? 92.555  12.529  31.157  1.00 97.79  ?  226 GLU B CD  1 
ATOM   6977  O  OE1 . GLU B  2  226 ? 91.534  13.258  31.136  1.00 70.21  ?  226 GLU B OE1 1 
ATOM   6978  O  OE2 . GLU B  2  226 ? 92.697  11.561  31.941  1.00 117.69 ?  226 GLU B OE2 1 
ATOM   6979  N  N   . PHE B  2  227 ? 92.956  15.188  26.329  1.00 53.00  ?  227 PHE B N   1 
ATOM   6980  C  CA  . PHE B  2  227 ? 92.235  15.469  25.090  1.00 50.20  ?  227 PHE B CA  1 
ATOM   6981  C  C   . PHE B  2  227 ? 93.194  15.576  23.908  1.00 58.69  ?  227 PHE B C   1 
ATOM   6982  O  O   . PHE B  2  227 ? 92.804  15.240  22.792  1.00 64.39  ?  227 PHE B O   1 
ATOM   6983  C  CB  . PHE B  2  227 ? 91.368  16.734  25.229  1.00 49.97  ?  227 PHE B CB  1 
ATOM   6984  C  CG  . PHE B  2  227 ? 90.242  16.682  26.247  1.00 49.93  ?  227 PHE B CG  1 
ATOM   6985  C  CD1 . PHE B  2  227 ? 89.855  15.484  26.828  1.00 51.34  ?  227 PHE B CD1 1 
ATOM   6986  C  CD2 . PHE B  2  227 ? 89.586  17.837  26.636  1.00 61.07  ?  227 PHE B CD2 1 
ATOM   6987  C  CE1 . PHE B  2  227 ? 88.832  15.446  27.765  1.00 57.76  ?  227 PHE B CE1 1 
ATOM   6988  C  CE2 . PHE B  2  227 ? 88.566  17.795  27.578  1.00 55.07  ?  227 PHE B CE2 1 
ATOM   6989  C  CZ  . PHE B  2  227 ? 88.193  16.601  28.134  1.00 58.73  ?  227 PHE B CZ  1 
ATOM   6990  N  N   . SER B  2  228 ? 94.449  16.008  24.134  1.00 48.04  ?  228 SER B N   1 
ATOM   6991  C  CA  . SER B  2  228 ? 95.423  16.095  23.050  1.00 43.50  ?  228 SER B CA  1 
ATOM   6992  C  C   . SER B  2  228 ? 95.780  14.687  22.580  1.00 51.42  ?  228 SER B C   1 
ATOM   6993  O  O   . SER B  2  228 ? 95.817  14.435  21.381  1.00 54.30  ?  228 SER B O   1 
ATOM   6994  C  CB  . SER B  2  228 ? 96.670  16.837  23.508  1.00 43.29  ?  228 SER B CB  1 
ATOM   6995  O  OG  . SER B  2  228 ? 96.355  18.190  23.788  1.00 60.37  ?  228 SER B OG  1 
ATOM   6996  N  N   . ASP B  2  229 ? 96.012  13.763  23.517  1.00 47.53  ?  229 ASP B N   1 
ATOM   6997  C  CA  . ASP B  2  229 ? 96.328  12.380  23.165  1.00 49.73  ?  229 ASP B CA  1 
ATOM   6998  C  C   . ASP B  2  229 ? 95.162  11.722  22.423  1.00 51.96  ?  229 ASP B C   1 
ATOM   6999  O  O   . ASP B  2  229 ? 95.392  10.841  21.602  1.00 61.96  ?  229 ASP B O   1 
ATOM   7000  C  CB  . ASP B  2  229 ? 96.661  11.558  24.422  1.00 52.04  ?  229 ASP B CB  1 
ATOM   7001  C  CG  . ASP B  2  229 ? 97.968  11.930  25.097  1.00 56.57  ?  229 ASP B CG  1 
ATOM   7002  O  OD1 . ASP B  2  229 ? 98.714  12.761  24.537  1.00 61.44  ?  229 ASP B OD1 1 
ATOM   7003  O  OD2 . ASP B  2  229 ? 98.245  11.389  26.185  1.00 58.51  ?  229 ASP B OD2 1 
ATOM   7004  N  N   . ILE B  2  230 ? 93.920  12.132  22.701  1.00 52.69  ?  230 ILE B N   1 
ATOM   7005  C  CA  . ILE B  2  230 ? 92.756  11.557  22.037  1.00 50.85  ?  230 ILE B CA  1 
ATOM   7006  C  C   . ILE B  2  230 ? 92.726  11.968  20.567  1.00 53.95  ?  230 ILE B C   1 
ATOM   7007  O  O   . ILE B  2  230 ? 92.575  11.118  19.689  1.00 56.01  ?  230 ILE B O   1 
ATOM   7008  C  CB  . ILE B  2  230 ? 91.443  11.959  22.776  1.00 49.52  ?  230 ILE B CB  1 
ATOM   7009  C  CG1 . ILE B  2  230 ? 91.346  11.213  24.129  1.00 60.63  ?  230 ILE B CG1 1 
ATOM   7010  C  CG2 . ILE B  2  230 ? 90.224  11.663  21.897  1.00 45.43  ?  230 ILE B CG2 1 
ATOM   7011  C  CD1 . ILE B  2  230 ? 90.309  11.720  25.123  1.00 58.01  ?  230 ILE B CD1 1 
ATOM   7012  N  N   . MET B  2  231 ? 92.872  13.268  20.299  1.00 50.14  ?  231 MET B N   1 
ATOM   7013  C  CA  . MET B  2  231 ? 92.803  13.800  18.941  1.00 56.24  ?  231 MET B CA  1 
ATOM   7014  C  C   . MET B  2  231 ? 94.074  13.618  18.129  1.00 54.34  ?  231 MET B C   1 
ATOM   7015  O  O   . MET B  2  231 ? 93.991  13.337  16.935  1.00 59.17  ?  231 MET B O   1 
ATOM   7016  C  CB  . MET B  2  231 ? 92.458  15.298  18.981  1.00 40.49  ?  231 MET B CB  1 
ATOM   7017  C  CG  . MET B  2  231 ? 91.181  15.605  19.723  1.00 53.71  ?  231 MET B CG  1 
ATOM   7018  S  SD  . MET B  2  231 ? 90.743  17.356  19.674  1.00 64.54  ?  231 MET B SD  1 
ATOM   7019  C  CE  . MET B  2  231 ? 91.813  17.983  20.916  1.00 56.29  ?  231 MET B CE  1 
ATOM   7020  N  N   . PHE B  2  232 ? 95.238  13.813  18.743  1.00 45.66  ?  232 PHE B N   1 
ATOM   7021  C  CA  . PHE B  2  232 ? 96.506  13.731  18.020  1.00 54.32  ?  232 PHE B CA  1 
ATOM   7022  C  C   . PHE B  2  232 ? 97.295  12.434  18.229  1.00 55.77  ?  232 PHE B C   1 
ATOM   7023  O  O   . PHE B  2  232 ? 98.293  12.227  17.541  1.00 56.51  ?  232 PHE B O   1 
ATOM   7024  C  CB  . PHE B  2  232 ? 97.372  14.947  18.373  1.00 49.85  ?  232 PHE B CB  1 
ATOM   7025  C  CG  . PHE B  2  232 ? 96.603  16.250  18.395  1.00 47.00  ?  232 PHE B CG  1 
ATOM   7026  C  CD1 . PHE B  2  232 ? 95.847  16.648  17.305  1.00 43.29  ?  232 PHE B CD1 1 
ATOM   7027  C  CD2 . PHE B  2  232 ? 96.610  17.057  19.519  1.00 51.73  ?  232 PHE B CD2 1 
ATOM   7028  C  CE1 . PHE B  2  232 ? 95.123  17.830  17.336  1.00 47.94  ?  232 PHE B CE1 1 
ATOM   7029  C  CE2 . PHE B  2  232 ? 95.892  18.245  19.543  1.00 52.00  ?  232 PHE B CE2 1 
ATOM   7030  C  CZ  . PHE B  2  232 ? 95.150  18.621  18.453  1.00 53.01  ?  232 PHE B CZ  1 
ATOM   7031  N  N   . GLY B  2  233 ? 96.847  11.584  19.150  1.00 52.80  ?  233 GLY B N   1 
ATOM   7032  C  CA  . GLY B  2  233 ? 97.499  10.316  19.450  1.00 42.95  ?  233 GLY B CA  1 
ATOM   7033  C  C   . GLY B  2  233 ? 98.293  10.354  20.742  1.00 55.07  ?  233 GLY B C   1 
ATOM   7034  O  O   . GLY B  2  233 ? 98.871  11.388  21.084  1.00 51.07  ?  233 GLY B O   1 
ATOM   7035  N  N   . THR B  2  234 ? 98.326  9.228   21.480  1.00 52.17  ?  234 THR B N   1 
ATOM   7036  C  CA  . THR B  2  234 ? 99.078  9.150   22.732  1.00 47.99  ?  234 THR B CA  1 
ATOM   7037  C  C   . THR B  2  234 ? 100.556 8.923   22.390  1.00 52.06  ?  234 THR B C   1 
ATOM   7038  O  O   . THR B  2  234 ? 100.849 8.020   21.607  1.00 56.83  ?  234 THR B O   1 
ATOM   7039  C  CB  . THR B  2  234 ? 98.563  8.007   23.606  1.00 53.88  ?  234 THR B CB  1 
ATOM   7040  O  OG1 . THR B  2  234 ? 97.151  8.133   23.751  1.00 65.27  ?  234 THR B OG1 1 
ATOM   7041  C  CG2 . THR B  2  234 ? 99.210  7.990   24.980  1.00 54.39  ?  234 THR B CG2 1 
ATOM   7042  N  N   . PRO B  2  235 ? 101.512 9.694   22.946  1.00 48.71  ?  235 PRO B N   1 
ATOM   7043  C  CA  . PRO B  2  235 ? 102.919 9.453   22.595  1.00 44.65  ?  235 PRO B CA  1 
ATOM   7044  C  C   . PRO B  2  235 ? 103.448 8.076   22.977  1.00 53.45  ?  235 PRO B C   1 
ATOM   7045  O  O   . PRO B  2  235 ? 103.043 7.501   23.988  1.00 62.11  ?  235 PRO B O   1 
ATOM   7046  C  CB  . PRO B  2  235 ? 103.681 10.530  23.373  1.00 43.84  ?  235 PRO B CB  1 
ATOM   7047  C  CG  . PRO B  2  235 ? 102.684 11.513  23.783  1.00 49.23  ?  235 PRO B CG  1 
ATOM   7048  C  CD  . PRO B  2  235 ? 101.378 10.819  23.888  1.00 51.29  ?  235 PRO B CD  1 
ATOM   7049  N  N   . HIS B  2  236 ? 104.381 7.565   22.160  1.00 59.97  ?  236 HIS B N   1 
ATOM   7050  C  CA  . HIS B  2  236 ? 105.078 6.294   22.373  1.00 54.79  ?  236 HIS B CA  1 
ATOM   7051  C  C   . HIS B  2  236 ? 106.559 6.567   22.081  1.00 55.32  ?  236 HIS B C   1 
ATOM   7052  O  O   . HIS B  2  236 ? 106.866 7.576   21.442  1.00 55.54  ?  236 HIS B O   1 
ATOM   7053  C  CB  . HIS B  2  236 ? 104.510 5.173   21.488  1.00 54.07  ?  236 HIS B CB  1 
ATOM   7054  C  CG  . HIS B  2  236 ? 104.717 5.378   20.020  1.00 62.05  ?  236 HIS B CG  1 
ATOM   7055  N  ND1 . HIS B  2  236 ? 103.845 6.148   19.267  1.00 83.11  ?  236 HIS B ND1 1 
ATOM   7056  C  CD2 . HIS B  2  236 ? 105.680 4.889   19.205  1.00 68.67  ?  236 HIS B CD2 1 
ATOM   7057  C  CE1 . HIS B  2  236 ? 104.309 6.115   18.027  1.00 72.13  ?  236 HIS B CE1 1 
ATOM   7058  N  NE2 . HIS B  2  236 ? 105.411 5.368   17.941  1.00 73.73  ?  236 HIS B NE2 1 
ATOM   7059  N  N   . SER B  2  237 ? 107.484 5.705   22.543  1.00 48.08  ?  237 SER B N   1 
ATOM   7060  C  CA  . SER B  2  237 ? 108.924 5.918   22.339  1.00 49.59  ?  237 SER B CA  1 
ATOM   7061  C  C   . SER B  2  237 ? 109.246 6.237   20.874  1.00 50.23  ?  237 SER B C   1 
ATOM   7062  O  O   . SER B  2  237 ? 108.830 5.508   19.977  1.00 51.02  ?  237 SER B O   1 
ATOM   7063  C  CB  . SER B  2  237 ? 109.728 4.721   22.836  1.00 42.49  ?  237 SER B CB  1 
ATOM   7064  O  OG  . SER B  2  237 ? 109.348 3.524   22.181  1.00 77.85  ?  237 SER B OG  1 
ATOM   7065  N  N   . ILE B  2  238 ? 109.938 7.361   20.645  1.00 48.58  ?  238 ILE B N   1 
ATOM   7066  C  CA  . ILE B  2  238 ? 110.263 7.829   19.301  1.00 45.71  ?  238 ILE B CA  1 
ATOM   7067  C  C   . ILE B  2  238 ? 111.625 8.504   19.266  1.00 48.57  ?  238 ILE B C   1 
ATOM   7068  O  O   . ILE B  2  238 ? 112.080 9.040   20.273  1.00 55.24  ?  238 ILE B O   1 
ATOM   7069  C  CB  . ILE B  2  238 ? 109.146 8.793   18.799  1.00 40.87  ?  238 ILE B CB  1 
ATOM   7070  C  CG1 . ILE B  2  238 ? 109.340 9.142   17.309  1.00 46.20  ?  238 ILE B CG1 1 
ATOM   7071  C  CG2 . ILE B  2  238 ? 109.083 10.070  19.649  1.00 48.48  ?  238 ILE B CG2 1 
ATOM   7072  C  CD1 . ILE B  2  238 ? 108.083 9.512   16.570  1.00 43.96  ?  238 ILE B CD1 1 
ATOM   7073  N  N   . ASP B  2  239 ? 112.267 8.489   18.096  1.00 43.59  ?  239 ASP B N   1 
ATOM   7074  C  CA  . ASP B  2  239 ? 113.571 9.104   17.913  1.00 49.98  ?  239 ASP B CA  1 
ATOM   7075  C  C   . ASP B  2  239 ? 113.431 10.509  17.334  1.00 48.81  ?  239 ASP B C   1 
ATOM   7076  O  O   . ASP B  2  239 ? 112.501 10.777  16.576  1.00 58.01  ?  239 ASP B O   1 
ATOM   7077  C  CB  . ASP B  2  239 ? 114.430 8.252   16.969  1.00 57.23  ?  239 ASP B CB  1 
ATOM   7078  C  CG  . ASP B  2  239 ? 114.868 6.926   17.551  1.00 64.36  ?  239 ASP B CG  1 
ATOM   7079  O  OD1 . ASP B  2  239 ? 115.542 6.935   18.613  1.00 57.09  ?  239 ASP B OD1 1 
ATOM   7080  O  OD2 . ASP B  2  239 ? 114.553 5.878   16.939  1.00 70.25  ?  239 ASP B OD2 1 
ATOM   7081  N  N   . THR B  2  240 ? 114.372 11.399  17.679  1.00 42.93  ?  240 THR B N   1 
ATOM   7082  C  CA  . THR B  2  240 ? 114.401 12.786  17.195  1.00 43.33  ?  240 THR B CA  1 
ATOM   7083  C  C   . THR B  2  240 ? 115.835 13.328  17.348  1.00 40.48  ?  240 THR B C   1 
ATOM   7084  O  O   . THR B  2  240 ? 116.699 12.630  17.876  1.00 50.46  ?  240 THR B O   1 
ATOM   7085  C  CB  . THR B  2  240 ? 113.360 13.670  17.971  1.00 51.56  ?  240 THR B CB  1 
ATOM   7086  O  OG1 . THR B  2  240 ? 113.039 14.837  17.206  1.00 55.43  ?  240 THR B OG1 1 
ATOM   7087  C  CG2 . THR B  2  240 ? 113.870 14.118  19.333  1.00 54.03  ?  240 THR B CG2 1 
ATOM   7088  N  N   . GLU B  2  241 ? 116.087 14.555  16.871  1.00 39.99  ?  241 GLU B N   1 
ATOM   7089  C  CA  . GLU B  2  241 ? 117.375 15.222  17.001  1.00 42.22  ?  241 GLU B CA  1 
ATOM   7090  C  C   . GLU B  2  241 ? 117.109 16.565  17.665  1.00 45.26  ?  241 GLU B C   1 
ATOM   7091  O  O   . GLU B  2  241 ? 116.054 17.157  17.445  1.00 55.49  ?  241 GLU B O   1 
ATOM   7092  C  CB  . GLU B  2  241 ? 118.055 15.406  15.641  1.00 38.47  ?  241 GLU B CB  1 
ATOM   7093  C  CG  . GLU B  2  241 ? 118.947 14.238  15.266  1.00 50.63  ?  241 GLU B CG  1 
ATOM   7094  C  CD  . GLU B  2  241 ? 119.402 14.200  13.821  1.00 65.13  ?  241 GLU B CD  1 
ATOM   7095  O  OE1 . GLU B  2  241 ? 118.740 14.829  12.963  1.00 60.43  ?  241 GLU B OE1 1 
ATOM   7096  O  OE2 . GLU B  2  241 ? 120.428 13.535  13.546  1.00 81.55  ?  241 GLU B OE2 1 
ATOM   7097  N  N   . ALA B  2  242 ? 118.040 17.037  18.498  1.00 39.09  ?  242 ALA B N   1 
ATOM   7098  C  CA  . ALA B  2  242 ? 117.873 18.288  19.226  1.00 37.42  ?  242 ALA B CA  1 
ATOM   7099  C  C   . ALA B  2  242 ? 119.029 19.266  18.994  1.00 39.93  ?  242 ALA B C   1 
ATOM   7100  O  O   . ALA B  2  242 ? 120.098 18.865  18.547  1.00 42.56  ?  242 ALA B O   1 
ATOM   7101  C  CB  . ALA B  2  242 ? 117.733 17.987  20.713  1.00 39.28  ?  242 ALA B CB  1 
ATOM   7102  N  N   . ASN B  2  243 ? 118.795 20.553  19.299  1.00 40.31  ?  243 ASN B N   1 
ATOM   7103  C  CA  . ASN B  2  243 ? 119.752 21.653  19.189  1.00 46.35  ?  243 ASN B CA  1 
ATOM   7104  C  C   . ASN B  2  243 ? 119.749 22.315  17.816  1.00 51.19  ?  243 ASN B C   1 
ATOM   7105  O  O   . ASN B  2  243 ? 119.330 21.711  16.834  1.00 56.62  ?  243 ASN B O   1 
ATOM   7106  C  CB  . ASN B  2  243 ? 121.162 21.236  19.606  1.00 44.10  ?  243 ASN B CB  1 
ATOM   7107  C  CG  . ASN B  2  243 ? 121.914 22.312  20.342  1.00 52.85  ?  243 ASN B CG  1 
ATOM   7108  O  OD1 . ASN B  2  243 ? 121.477 23.472  20.426  1.00 41.24  ?  243 ASN B OD1 1 
ATOM   7109  N  ND2 . ASN B  2  243 ? 123.065 21.944  20.894  1.00 59.24  ?  243 ASN B ND2 1 
ATOM   7110  N  N   . LEU B  2  244 ? 120.210 23.570  17.757  1.00 51.47  ?  244 LEU B N   1 
ATOM   7111  C  CA  . LEU B  2  244 ? 120.195 24.385  16.542  1.00 44.11  ?  244 LEU B CA  1 
ATOM   7112  C  C   . LEU B  2  244 ? 120.867 23.769  15.307  1.00 43.51  ?  244 LEU B C   1 
ATOM   7113  O  O   . LEU B  2  244 ? 120.653 24.271  14.204  1.00 48.77  ?  244 LEU B O   1 
ATOM   7114  C  CB  . LEU B  2  244 ? 120.759 25.784  16.833  1.00 43.25  ?  244 LEU B CB  1 
ATOM   7115  C  CG  . LEU B  2  244 ? 119.945 26.607  17.850  1.00 45.51  ?  244 LEU B CG  1 
ATOM   7116  C  CD1 . LEU B  2  244 ? 120.733 27.780  18.363  1.00 36.20  ?  244 LEU B CD1 1 
ATOM   7117  C  CD2 . LEU B  2  244 ? 118.626 27.074  17.252  1.00 44.34  ?  244 LEU B CD2 1 
ATOM   7118  N  N   . GLY B  2  245 ? 121.629 22.691  15.474  1.00 47.18  ?  245 GLY B N   1 
ATOM   7119  C  CA  . GLY B  2  245 ? 122.253 22.022  14.336  1.00 41.02  ?  245 GLY B CA  1 
ATOM   7120  C  C   . GLY B  2  245 ? 121.244 21.330  13.430  1.00 39.97  ?  245 GLY B C   1 
ATOM   7121  O  O   . GLY B  2  245 ? 121.580 20.934  12.317  1.00 36.39  ?  245 GLY B O   1 
ATOM   7122  N  N   . VAL B  2  246 ? 119.993 21.172  13.903  1.00 47.48  ?  246 VAL B N   1 
ATOM   7123  C  CA  . VAL B  2  246 ? 118.900 20.546  13.146  1.00 49.95  ?  246 VAL B CA  1 
ATOM   7124  C  C   . VAL B  2  246 ? 118.452 21.388  11.935  1.00 48.81  ?  246 VAL B C   1 
ATOM   7125  O  O   . VAL B  2  246 ? 117.848 20.844  11.009  1.00 49.42  ?  246 VAL B O   1 
ATOM   7126  C  CB  . VAL B  2  246 ? 117.687 20.220  14.052  1.00 38.34  ?  246 VAL B CB  1 
ATOM   7127  C  CG1 . VAL B  2  246 ? 118.079 19.259  15.171  1.00 48.43  ?  246 VAL B CG1 1 
ATOM   7128  C  CG2 . VAL B  2  246 ? 117.034 21.484  14.604  1.00 46.43  ?  246 VAL B CG2 1 
ATOM   7129  N  N   . LEU B  2  247 ? 118.725 22.701  11.942  1.00 41.03  ?  247 LEU B N   1 
ATOM   7130  C  CA  . LEU B  2  247 ? 118.345 23.563  10.831  1.00 45.42  ?  247 LEU B CA  1 
ATOM   7131  C  C   . LEU B  2  247 ? 119.191 23.202  9.619   1.00 53.43  ?  247 LEU B C   1 
ATOM   7132  O  O   . LEU B  2  247 ? 120.388 22.970  9.766   1.00 55.05  ?  247 LEU B O   1 
ATOM   7133  C  CB  . LEU B  2  247 ? 118.573 25.032  11.198  1.00 34.86  ?  247 LEU B CB  1 
ATOM   7134  C  CG  . LEU B  2  247 ? 117.741 25.567  12.356  1.00 31.52  ?  247 LEU B CG  1 
ATOM   7135  C  CD1 . LEU B  2  247 ? 118.340 26.847  12.900  1.00 39.32  ?  247 LEU B CD1 1 
ATOM   7136  C  CD2 . LEU B  2  247 ? 116.305 25.796  11.937  1.00 41.47  ?  247 LEU B CD2 1 
ATOM   7137  N  N   . GLU B  2  248 ? 118.587 23.156  8.426   1.00 39.97  ?  248 GLU B N   1 
ATOM   7138  C  CA  . GLU B  2  248 ? 119.312 22.799  7.208   1.00 44.69  ?  248 GLU B CA  1 
ATOM   7139  C  C   . GLU B  2  248 ? 119.486 24.008  6.273   1.00 45.98  ?  248 GLU B C   1 
ATOM   7140  O  O   . GLU B  2  248 ? 118.508 24.671  5.947   1.00 50.00  ?  248 GLU B O   1 
ATOM   7141  C  CB  . GLU B  2  248 ? 118.569 21.660  6.498   1.00 43.29  ?  248 GLU B CB  1 
ATOM   7142  C  CG  . GLU B  2  248 ? 118.723 20.308  7.176   1.00 46.80  ?  248 GLU B CG  1 
ATOM   7143  C  CD  . GLU B  2  248 ? 117.559 19.354  6.982   1.00 87.27  ?  248 GLU B CD  1 
ATOM   7144  O  OE1 . GLU B  2  248 ? 116.695 19.625  6.117   1.00 85.57  ?  248 GLU B OE1 1 
ATOM   7145  O  OE2 . GLU B  2  248 ? 117.512 18.330  7.702   1.00 103.24 ?  248 GLU B OE2 1 
ATOM   7146  N  N   . LYS B  2  249 ? 120.725 24.290  5.835   1.00 48.42  ?  249 LYS B N   1 
ATOM   7147  C  CA  . LYS B  2  249 ? 121.003 25.432  4.957   1.00 44.92  ?  249 LYS B CA  1 
ATOM   7148  C  C   . LYS B  2  249 ? 120.340 25.368  3.585   1.00 53.47  ?  249 LYS B C   1 
ATOM   7149  O  O   . LYS B  2  249 ? 120.013 26.421  3.034   1.00 55.25  ?  249 LYS B O   1 
ATOM   7150  C  CB  . LYS B  2  249 ? 122.514 25.598  4.741   1.00 43.95  ?  249 LYS B CB  1 
ATOM   7151  C  CG  . LYS B  2  249 ? 122.884 26.684  3.719   1.00 43.74  ?  249 LYS B CG  1 
ATOM   7152  C  CD  . LYS B  2  249 ? 124.050 27.552  4.170   1.00 60.94  ?  249 LYS B CD  1 
ATOM   7153  C  CE  . LYS B  2  249 ? 124.848 28.106  3.015   1.00 50.98  ?  249 LYS B CE  1 
ATOM   7154  N  NZ  . LYS B  2  249 ? 125.934 29.020  3.469   1.00 72.16  ?  249 LYS B NZ  1 
ATOM   7155  N  N   . ASN B  2  250 ? 120.164 24.169  3.014   1.00 52.15  ?  250 ASN B N   1 
ATOM   7156  C  CA  . ASN B  2  250 ? 119.553 24.060  1.686   1.00 50.28  ?  250 ASN B CA  1 
ATOM   7157  C  C   . ASN B  2  250 ? 118.086 23.641  1.744   1.00 49.75  ?  250 ASN B C   1 
ATOM   7158  O  O   . ASN B  2  250 ? 117.542 23.228  0.725   1.00 50.00  ?  250 ASN B O   1 
ATOM   7159  C  CB  . ASN B  2  250 ? 120.346 23.120  0.794   1.00 48.20  ?  250 ASN B CB  1 
ATOM   7160  C  CG  . ASN B  2  250 ? 121.781 23.543  0.659   1.00 60.28  ?  250 ASN B CG  1 
ATOM   7161  O  OD1 . ASN B  2  250 ? 122.095 24.741  0.615   1.00 64.65  ?  250 ASN B OD1 1 
ATOM   7162  N  ND2 . ASN B  2  250 ? 122.688 22.576  0.595   1.00 72.97  ?  250 ASN B ND2 1 
ATOM   7163  N  N   . SER B  2  251 ? 117.435 23.760  2.906   1.00 52.15  ?  251 SER B N   1 
ATOM   7164  C  CA  . SER B  2  251 ? 116.022 23.404  3.029   1.00 52.60  ?  251 SER B CA  1 
ATOM   7165  C  C   . SER B  2  251 ? 115.230 24.591  3.545   1.00 55.65  ?  251 SER B C   1 
ATOM   7166  O  O   . SER B  2  251 ? 115.811 25.564  4.038   1.00 58.41  ?  251 SER B O   1 
ATOM   7167  C  CB  . SER B  2  251 ? 115.837 22.228  3.983   1.00 46.83  ?  251 SER B CB  1 
ATOM   7168  O  OG  . SER B  2  251 ? 116.702 21.156  3.653   1.00 66.67  ?  251 SER B OG  1 
ATOM   7169  N  N   . VAL B  2  252 ? 113.901 24.515  3.436   1.00 50.48  ?  252 VAL B N   1 
ATOM   7170  C  CA  . VAL B  2  252 ? 113.058 25.580  3.939   1.00 44.66  ?  252 VAL B CA  1 
ATOM   7171  C  C   . VAL B  2  252 ? 112.932 25.315  5.423   1.00 45.62  ?  252 VAL B C   1 
ATOM   7172  O  O   . VAL B  2  252 ? 112.365 24.301  5.804   1.00 53.65  ?  252 VAL B O   1 
ATOM   7173  C  CB  . VAL B  2  252 ? 111.690 25.611  3.240   1.00 36.29  ?  252 VAL B CB  1 
ATOM   7174  C  CG1 . VAL B  2  252 ? 110.785 26.669  3.857   1.00 45.30  ?  252 VAL B CG1 1 
ATOM   7175  C  CG2 . VAL B  2  252 ? 111.861 25.853  1.748   1.00 47.41  ?  252 VAL B CG2 1 
ATOM   7176  N  N   . ASN B  2  253 ? 113.486 26.191  6.260   1.00 41.33  ?  253 ASN B N   1 
ATOM   7177  C  CA  . ASN B  2  253 ? 113.415 26.008  7.704   1.00 39.96  ?  253 ASN B CA  1 
ATOM   7178  C  C   . ASN B  2  253 ? 112.202 26.710  8.280   1.00 54.03  ?  253 ASN B C   1 
ATOM   7179  O  O   . ASN B  2  253 ? 112.142 27.938  8.292   1.00 62.12  ?  253 ASN B O   1 
ATOM   7180  C  CB  . ASN B  2  253 ? 114.663 26.540  8.369   1.00 47.35  ?  253 ASN B CB  1 
ATOM   7181  C  CG  . ASN B  2  253 ? 115.872 25.718  8.056   1.00 45.51  ?  253 ASN B CG  1 
ATOM   7182  O  OD1 . ASN B  2  253 ? 115.922 24.523  8.355   1.00 54.39  ?  253 ASN B OD1 1 
ATOM   7183  N  ND2 . ASN B  2  253 ? 116.877 26.330  7.451   1.00 41.47  ?  253 ASN B ND2 1 
ATOM   7184  N  N   . VAL B  2  254 ? 111.236 25.934  8.756   1.00 48.05  ?  254 VAL B N   1 
ATOM   7185  C  CA  . VAL B  2  254 ? 110.035 26.481  9.359   1.00 44.00  ?  254 VAL B CA  1 
ATOM   7186  C  C   . VAL B  2  254 ? 110.083 26.082  10.824  1.00 46.32  ?  254 VAL B C   1 
ATOM   7187  O  O   . VAL B  2  254 ? 109.955 24.899  11.141  1.00 54.51  ?  254 VAL B O   1 
ATOM   7188  C  CB  . VAL B  2  254 ? 108.762 25.959  8.659   1.00 41.66  ?  254 VAL B CB  1 
ATOM   7189  C  CG1 . VAL B  2  254 ? 107.515 26.604  9.254   1.00 40.49  ?  254 VAL B CG1 1 
ATOM   7190  C  CG2 . VAL B  2  254 ? 108.830 26.209  7.156   1.00 34.24  ?  254 VAL B CG2 1 
ATOM   7191  N  N   . VAL B  2  255 ? 110.301 27.062  11.713  1.00 46.97  ?  255 VAL B N   1 
ATOM   7192  C  CA  . VAL B  2  255 ? 110.385 26.818  13.149  1.00 42.49  ?  255 VAL B CA  1 
ATOM   7193  C  C   . VAL B  2  255 ? 109.058 27.164  13.827  1.00 50.58  ?  255 VAL B C   1 
ATOM   7194  O  O   . VAL B  2  255 ? 108.564 28.283  13.687  1.00 48.90  ?  255 VAL B O   1 
ATOM   7195  C  CB  . VAL B  2  255 ? 111.547 27.616  13.774  1.00 37.82  ?  255 VAL B CB  1 
ATOM   7196  C  CG1 . VAL B  2  255 ? 111.679 27.294  15.255  1.00 47.71  ?  255 VAL B CG1 1 
ATOM   7197  C  CG2 . VAL B  2  255 ? 112.857 27.344  13.044  1.00 31.56  ?  255 VAL B CG2 1 
ATOM   7198  N  N   . LEU B  2  256 ? 108.487 26.194  14.564  1.00 51.82  ?  256 LEU B N   1 
ATOM   7199  C  CA  . LEU B  2  256 ? 107.228 26.346  15.288  1.00 41.77  ?  256 LEU B CA  1 
ATOM   7200  C  C   . LEU B  2  256 ? 107.554 26.613  16.740  1.00 43.18  ?  256 LEU B C   1 
ATOM   7201  O  O   . LEU B  2  256 ? 108.118 25.759  17.412  1.00 45.07  ?  256 LEU B O   1 
ATOM   7202  C  CB  . LEU B  2  256 ? 106.394 25.066  15.179  1.00 29.12  ?  256 LEU B CB  1 
ATOM   7203  C  CG  . LEU B  2  256 ? 105.978 24.664  13.771  1.00 39.20  ?  256 LEU B CG  1 
ATOM   7204  C  CD1 . LEU B  2  256 ? 105.426 23.255  13.746  1.00 35.50  ?  256 LEU B CD1 1 
ATOM   7205  C  CD2 . LEU B  2  256 ? 104.982 25.647  13.194  1.00 49.58  ?  256 LEU B CD2 1 
ATOM   7206  N  N   . HIS B  2  257 ? 107.213 27.792  17.224  1.00 44.15  ?  257 HIS B N   1 
ATOM   7207  C  CA  . HIS B  2  257 ? 107.478 28.184  18.596  1.00 42.59  ?  257 HIS B CA  1 
ATOM   7208  C  C   . HIS B  2  257 ? 106.091 28.418  19.196  1.00 47.82  ?  257 HIS B C   1 
ATOM   7209  O  O   . HIS B  2  257 ? 105.118 28.591  18.462  1.00 50.56  ?  257 HIS B O   1 
ATOM   7210  C  CB  . HIS B  2  257 ? 108.508 29.329  18.589  1.00 54.64  ?  257 HIS B CB  1 
ATOM   7211  C  CG  . HIS B  2  257 ? 108.841 29.913  19.924  1.00 51.02  ?  257 HIS B CG  1 
ATOM   7212  N  ND1 . HIS B  2  257 ? 108.875 29.141  21.066  1.00 49.37  ?  257 HIS B ND1 1 
ATOM   7213  C  CD2 . HIS B  2  257 ? 109.201 31.177  20.241  1.00 42.85  ?  257 HIS B CD2 1 
ATOM   7214  C  CE1 . HIS B  2  257 ? 109.221 29.959  22.045  1.00 50.61  ?  257 HIS B CE1 1 
ATOM   7215  N  NE2 . HIS B  2  257 ? 109.429 31.196  21.593  1.00 53.63  ?  257 HIS B NE2 1 
ATOM   7216  N  N   . GLY B  2  258 ? 105.997 28.363  20.519  1.00 44.29  ?  258 GLY B N   1 
ATOM   7217  C  CA  . GLY B  2  258 ? 104.726 28.538  21.211  1.00 54.55  ?  258 GLY B CA  1 
ATOM   7218  C  C   . GLY B  2  258 ? 104.294 27.429  22.148  1.00 51.53  ?  258 GLY B C   1 
ATOM   7219  O  O   . GLY B  2  258 ? 105.145 26.749  22.725  1.00 58.50  ?  258 GLY B O   1 
ATOM   7220  N  N   . HIS B  2  259 ? 102.981 27.248  22.320  1.00 52.06  ?  259 HIS B N   1 
ATOM   7221  C  CA  . HIS B  2  259 ? 102.494 26.241  23.303  1.00 47.73  ?  259 HIS B CA  1 
ATOM   7222  C  C   . HIS B  2  259 ? 101.292 25.473  22.739  1.00 64.59  ?  259 HIS B C   1 
ATOM   7223  O  O   . HIS B  2  259 ? 101.181 24.257  22.998  1.00 69.23  ?  259 HIS B O   1 
ATOM   7224  C  CB  . HIS B  2  259 ? 102.177 26.918  24.640  1.00 37.16  ?  259 HIS B CB  1 
ATOM   7225  C  CG  . HIS B  2  259 ? 103.381 27.151  25.486  1.00 46.26  ?  259 HIS B CG  1 
ATOM   7226  N  ND1 . HIS B  2  259 ? 104.317 28.119  25.199  1.00 57.19  ?  259 HIS B ND1 1 
ATOM   7227  C  CD2 . HIS B  2  259 ? 103.805 26.544  26.600  1.00 54.90  ?  259 HIS B CD2 1 
ATOM   7228  C  CE1 . HIS B  2  259 ? 105.271 28.088  26.117  1.00 84.68  ?  259 HIS B CE1 1 
ATOM   7229  N  NE2 . HIS B  2  259 ? 104.981 27.137  26.977  1.00 66.40  ?  259 HIS B NE2 1 
ATOM   7230  N  N   . GLU B  2  260 ? 100.420 26.155  21.995  1.00 63.83  ?  260 GLU B N   1 
ATOM   7231  C  CA  . GLU B  2  260 ? 99.204  25.501  21.442  1.00 57.23  ?  260 GLU B CA  1 
ATOM   7232  C  C   . GLU B  2  260 ? 99.620  24.352  20.519  1.00 57.89  ?  260 GLU B C   1 
ATOM   7233  O  O   . GLU B  2  260 ? 100.565 24.541  19.733  1.00 81.12  ?  260 GLU B O   1 
ATOM   7234  C  CB  . GLU B  2  260 ? 98.347  26.515  20.685  1.00 63.65  ?  260 GLU B CB  1 
ATOM   7235  C  CG  . GLU B  2  260 ? 98.165  27.824  21.428  1.00 81.98  ?  260 GLU B CG  1 
ATOM   7236  C  CD  . GLU B  2  260 ? 96.885  27.915  22.240  1.00 75.43  ?  260 GLU B CD  1 
ATOM   7237  O  OE1 . GLU B  2  260 ? 96.827  27.292  23.318  1.00 86.15  ?  260 GLU B OE1 1 
ATOM   7238  O  OE2 . GLU B  2  260 ? 95.951  28.608  21.792  1.00 65.27  ?  260 GLU B OE2 1 
ATOM   7239  N  N   . PRO B  2  261 ? 98.956  23.178  20.576  1.00 58.00  ?  261 PRO B N   1 
ATOM   7240  C  CA  . PRO B  2  261 ? 99.349  22.022  19.769  1.00 52.18  ?  261 PRO B CA  1 
ATOM   7241  C  C   . PRO B  2  261 ? 98.601  21.870  18.436  1.00 53.48  ?  261 PRO B C   1 
ATOM   7242  O  O   . PRO B  2  261 ? 99.156  21.273  17.536  1.00 63.16  ?  261 PRO B O   1 
ATOM   7243  C  CB  . PRO B  2  261 ? 98.930  20.875  20.695  1.00 53.24  ?  261 PRO B CB  1 
ATOM   7244  C  CG  . PRO B  2  261 ? 97.658  21.376  21.343  1.00 59.64  ?  261 PRO B CG  1 
ATOM   7245  C  CD  . PRO B  2  261 ? 97.826  22.878  21.457  1.00 79.19  ?  261 PRO B CD  1 
ATOM   7246  N  N   . LEU B  2  262 ? 97.377  22.393  18.340  1.00 57.47  ?  262 LEU B N   1 
ATOM   7247  C  CA  . LEU B  2  262 ? 96.583  22.210  17.120  1.00 46.86  ?  262 LEU B CA  1 
ATOM   7248  C  C   . LEU B  2  262 ? 97.239  22.839  15.895  1.00 54.15  ?  262 LEU B C   1 
ATOM   7249  O  O   . LEU B  2  262 ? 97.307  22.195  14.848  1.00 60.12  ?  262 LEU B O   1 
ATOM   7250  C  CB  . LEU B  2  262 ? 95.152  22.738  17.291  1.00 47.01  ?  262 LEU B CB  1 
ATOM   7251  C  CG  . LEU B  2  262 ? 94.246  22.608  16.056  1.00 49.00  ?  262 LEU B CG  1 
ATOM   7252  C  CD1 . LEU B  2  262 ? 93.870  21.168  15.788  1.00 35.38  ?  262 LEU B CD1 1 
ATOM   7253  C  CD2 . LEU B  2  262 ? 92.988  23.426  16.217  1.00 65.54  ?  262 LEU B CD2 1 
ATOM   7254  N  N   . LEU B  2  263 ? 97.730  24.083  16.006  1.00 51.02  ?  263 LEU B N   1 
ATOM   7255  C  CA  . LEU B  2  263 ? 98.392  24.738  14.876  1.00 40.06  ?  263 LEU B CA  1 
ATOM   7256  C  C   . LEU B  2  263 ? 99.612  23.925  14.444  1.00 45.56  ?  263 LEU B C   1 
ATOM   7257  O  O   . LEU B  2  263 ? 99.758  23.635  13.263  1.00 57.64  ?  263 LEU B O   1 
ATOM   7258  C  CB  . LEU B  2  263 ? 98.816  26.168  15.247  1.00 43.01  ?  263 LEU B CB  1 
ATOM   7259  C  CG  . LEU B  2  263 ? 99.757  26.874  14.264  1.00 41.39  ?  263 LEU B CG  1 
ATOM   7260  C  CD1 . LEU B  2  263 ? 99.037  27.266  12.987  1.00 34.67  ?  263 LEU B CD1 1 
ATOM   7261  C  CD2 . LEU B  2  263 ? 100.368 28.089  14.899  1.00 51.45  ?  263 LEU B CD2 1 
ATOM   7262  N  N   . SER B  2  264 ? 100.473 23.573  15.398  1.00 45.24  ?  264 SER B N   1 
ATOM   7263  C  CA  . SER B  2  264 ? 101.683 22.774  15.079  1.00 47.61  ?  264 SER B CA  1 
ATOM   7264  C  C   . SER B  2  264 ? 101.266 21.468  14.401  1.00 46.38  ?  264 SER B C   1 
ATOM   7265  O  O   . SER B  2  264 ? 101.866 21.121  13.369  1.00 54.39  ?  264 SER B O   1 
ATOM   7266  C  CB  . SER B  2  264 ? 102.482 22.513  16.322  1.00 38.01  ?  264 SER B CB  1 
ATOM   7267  O  OG  . SER B  2  264 ? 101.748 21.716  17.239  1.00 69.74  ?  264 SER B OG  1 
ATOM   7268  N  N   . GLU B  2  265 ? 100.270 20.782  14.959  1.00 42.37  ?  265 GLU B N   1 
ATOM   7269  C  CA  . GLU B  2  265 ? 99.813  19.514  14.404  1.00 44.82  ?  265 GLU B CA  1 
ATOM   7270  C  C   . GLU B  2  265 ? 99.380  19.706  12.952  1.00 48.46  ?  265 GLU B C   1 
ATOM   7271  O  O   . GLU B  2  265 ? 99.653  18.846  12.120  1.00 57.13  ?  265 GLU B O   1 
ATOM   7272  C  CB  . GLU B  2  265 ? 98.637  18.971  15.229  1.00 52.53  ?  265 GLU B CB  1 
ATOM   7273  C  CG  . GLU B  2  265 ? 98.363  17.492  15.010  1.00 59.50  ?  265 GLU B CG  1 
ATOM   7274  C  CD  . GLU B  2  265 ? 99.210  16.531  15.821  1.00 63.56  ?  265 GLU B CD  1 
ATOM   7275  O  OE1 . GLU B  2  265 ? 99.881  16.976  16.781  1.00 58.76  ?  265 GLU B OE1 1 
ATOM   7276  O  OE2 . GLU B  2  265 ? 99.202  15.323  15.490  1.00 67.62  ?  265 GLU B OE2 1 
ATOM   7277  N  N   . MET B  2  266 ? 98.774  20.855  12.656  1.00 39.36  ?  266 MET B N   1 
ATOM   7278  C  CA  . MET B  2  266 ? 98.266  21.107  11.283  1.00 40.27  ?  266 MET B CA  1 
ATOM   7279  C  C   . MET B  2  266 ? 99.418  21.522  10.356  1.00 56.56  ?  266 MET B C   1 
ATOM   7280  O  O   . MET B  2  266 ? 99.375  21.139  9.174   1.00 54.70  ?  266 MET B O   1 
ATOM   7281  C  CB  . MET B  2  266 ? 97.192  22.197  11.295  1.00 42.97  ?  266 MET B CB  1 
ATOM   7282  C  CG  . MET B  2  266 ? 95.904  21.766  11.964  1.00 43.67  ?  266 MET B CG  1 
ATOM   7283  S  SD  . MET B  2  266 ? 95.139  20.353  11.132  1.00 53.11  ?  266 MET B SD  1 
ATOM   7284  C  CE  . MET B  2  266 ? 95.419  19.066  12.346  1.00 53.14  ?  266 MET B CE  1 
ATOM   7285  N  N   . VAL B  2  267 ? 100.409 22.260  10.868  1.00 47.26  ?  267 VAL B N   1 
ATOM   7286  C  CA  . VAL B  2  267 ? 101.546 22.640  10.024  1.00 40.53  ?  267 VAL B CA  1 
ATOM   7287  C  C   . VAL B  2  267 ? 102.314 21.360  9.616   1.00 46.40  ?  267 VAL B C   1 
ATOM   7288  O  O   . VAL B  2  267 ? 102.853 21.293  8.515   1.00 51.18  ?  267 VAL B O   1 
ATOM   7289  C  CB  . VAL B  2  267 ? 102.464 23.701  10.678  1.00 39.51  ?  267 VAL B CB  1 
ATOM   7290  C  CG1 . VAL B  2  267 ? 103.627 24.050  9.757   1.00 41.88  ?  267 VAL B CG1 1 
ATOM   7291  C  CG2 . VAL B  2  267 ? 101.677 24.961  11.020  1.00 39.27  ?  267 VAL B CG2 1 
ATOM   7292  N  N   . VAL B  2  268 ? 102.327 20.333  10.478  1.00 43.34  ?  268 VAL B N   1 
ATOM   7293  C  CA  . VAL B  2  268 ? 102.977 19.066  10.159  1.00 40.94  ?  268 VAL B CA  1 
ATOM   7294  C  C   . VAL B  2  268 ? 102.221 18.403  9.004   1.00 47.33  ?  268 VAL B C   1 
ATOM   7295  O  O   . VAL B  2  268 ? 102.845 17.970  8.037   1.00 53.13  ?  268 VAL B O   1 
ATOM   7296  C  CB  . VAL B  2  268 ? 103.024 18.143  11.399  1.00 41.74  ?  268 VAL B CB  1 
ATOM   7297  C  CG1 . VAL B  2  268 ? 103.392 16.714  11.012  1.00 44.07  ?  268 VAL B CG1 1 
ATOM   7298  C  CG2 . VAL B  2  268 ? 103.997 18.680  12.429  1.00 39.58  ?  268 VAL B CG2 1 
ATOM   7299  N  N   . GLU B  2  269 ? 100.882 18.332  9.102   1.00 47.07  ?  269 GLU B N   1 
ATOM   7300  C  CA  . GLU B  2  269 ? 100.056 17.725  8.058   1.00 49.31  ?  269 GLU B CA  1 
ATOM   7301  C  C   . GLU B  2  269 ? 100.147 18.535  6.764   1.00 53.68  ?  269 GLU B C   1 
ATOM   7302  O  O   . GLU B  2  269 ? 100.146 17.951  5.677   1.00 56.80  ?  269 GLU B O   1 
ATOM   7303  C  CB  . GLU B  2  269 ? 98.590  17.617  8.517   1.00 39.65  ?  269 GLU B CB  1 
ATOM   7304  C  CG  . GLU B  2  269 ? 97.909  16.323  8.102   1.00 50.76  ?  269 GLU B CG  1 
ATOM   7305  C  CD  . GLU B  2  269 ? 96.402  16.315  8.263   1.00 81.71  ?  269 GLU B CD  1 
ATOM   7306  O  OE1 . GLU B  2  269 ? 95.920  16.542  9.397   1.00 83.04  ?  269 GLU B OE1 1 
ATOM   7307  O  OE2 . GLU B  2  269 ? 95.701  16.070  7.255   1.00 97.19  ?  269 GLU B OE2 1 
ATOM   7308  N  N   . ALA B  2  270 ? 100.235 19.874  6.880   1.00 49.17  ?  270 ALA B N   1 
ATOM   7309  C  CA  . ALA B  2  270 ? 100.359 20.768  5.732   1.00 46.54  ?  270 ALA B CA  1 
ATOM   7310  C  C   . ALA B  2  270 ? 101.680 20.519  5.015   1.00 50.32  ?  270 ALA B C   1 
ATOM   7311  O  O   . ALA B  2  270 ? 101.719 20.551  3.789   1.00 60.67  ?  270 ALA B O   1 
ATOM   7312  C  CB  . ALA B  2  270 ? 100.288 22.217  6.186   1.00 42.45  ?  270 ALA B CB  1 
ATOM   7313  N  N   . ALA B  2  271 ? 102.763 20.263  5.764   1.00 44.85  ?  271 ALA B N   1 
ATOM   7314  C  CA  . ALA B  2  271 ? 104.066 20.007  5.154   1.00 49.15  ?  271 ALA B CA  1 
ATOM   7315  C  C   . ALA B  2  271 ? 104.067 18.781  4.227   1.00 61.77  ?  271 ALA B C   1 
ATOM   7316  O  O   . ALA B  2  271 ? 105.005 18.626  3.445   1.00 65.93  ?  271 ALA B O   1 
ATOM   7317  C  CB  . ALA B  2  271 ? 105.129 19.859  6.229   1.00 42.86  ?  271 ALA B CB  1 
ATOM   7318  N  N   . SER B  2  272 ? 103.027 17.927  4.298   1.00 45.52  ?  272 SER B N   1 
ATOM   7319  C  CA  . SER B  2  272 ? 102.918 16.751  3.438   1.00 47.53  ?  272 SER B CA  1 
ATOM   7320  C  C   . SER B  2  272 ? 102.028 16.994  2.209   1.00 56.30  ?  272 SER B C   1 
ATOM   7321  O  O   . SER B  2  272 ? 101.933 16.123  1.345   1.00 57.41  ?  272 SER B O   1 
ATOM   7322  C  CB  . SER B  2  272 ? 102.381 15.571  4.233   1.00 45.40  ?  272 SER B CB  1 
ATOM   7323  O  OG  . SER B  2  272 ? 103.297 15.240  5.262   1.00 71.02  ?  272 SER B OG  1 
ATOM   7324  N  N   . ASP B  2  273 ? 101.387 18.168  2.111   1.00 62.97  ?  273 ASP B N   1 
ATOM   7325  C  CA  . ASP B  2  273 ? 100.530 18.494  0.977   1.00 46.47  ?  273 ASP B CA  1 
ATOM   7326  C  C   . ASP B  2  273 ? 101.376 18.494  -0.292  1.00 55.54  ?  273 ASP B C   1 
ATOM   7327  O  O   . ASP B  2  273 ? 102.330 19.266  -0.375  1.00 64.01  ?  273 ASP B O   1 
ATOM   7328  C  CB  . ASP B  2  273 ? 99.890  19.875  1.179   1.00 48.13  ?  273 ASP B CB  1 
ATOM   7329  C  CG  . ASP B  2  273 ? 99.003  20.312  0.037   1.00 62.83  ?  273 ASP B CG  1 
ATOM   7330  O  OD1 . ASP B  2  273 ? 98.304  19.451  -0.534  1.00 72.19  ?  273 ASP B OD1 1 
ATOM   7331  O  OD2 . ASP B  2  273 ? 99.006  21.517  -0.286  1.00 80.60  ?  273 ASP B OD2 1 
ATOM   7332  N  N   . PRO B  2  274 ? 101.076 17.638  -1.287  1.00 57.01  ?  274 PRO B N   1 
ATOM   7333  C  CA  . PRO B  2  274 ? 101.899 17.625  -2.509  1.00 57.47  ?  274 PRO B CA  1 
ATOM   7334  C  C   . PRO B  2  274 ? 102.167 19.001  -3.107  1.00 50.55  ?  274 PRO B C   1 
ATOM   7335  O  O   . PRO B  2  274 ? 103.274 19.245  -3.563  1.00 61.73  ?  274 PRO B O   1 
ATOM   7336  C  CB  . PRO B  2  274 ? 101.091 16.755  -3.471  1.00 67.63  ?  274 PRO B CB  1 
ATOM   7337  C  CG  . PRO B  2  274 ? 100.280 15.885  -2.615  1.00 55.43  ?  274 PRO B CG  1 
ATOM   7338  C  CD  . PRO B  2  274 ? 99.988  16.644  -1.358  1.00 55.00  ?  274 PRO B CD  1 
ATOM   7339  N  N   . GLU B  2  275 ? 101.169 19.891  -3.097  1.00 50.31  ?  275 GLU B N   1 
ATOM   7340  C  CA  . GLU B  2  275 ? 101.324 21.235  -3.642  1.00 55.07  ?  275 GLU B CA  1 
ATOM   7341  C  C   . GLU B  2  275 ? 102.406 22.011  -2.897  1.00 58.47  ?  275 GLU B C   1 
ATOM   7342  O  O   . GLU B  2  275 ? 103.226 22.678  -3.535  1.00 65.68  ?  275 GLU B O   1 
ATOM   7343  C  CB  . GLU B  2  275 ? 99.997  22.006  -3.576  1.00 62.78  ?  275 GLU B CB  1 
ATOM   7344  C  CG  . GLU B  2  275 ? 98.997  21.598  -4.646  1.00 79.87  ?  275 GLU B CG  1 
ATOM   7345  C  CD  . GLU B  2  275 ? 97.786  22.504  -4.762  1.00 116.25 ?  275 GLU B CD  1 
ATOM   7346  O  OE1 . GLU B  2  275 ? 97.907  23.710  -4.444  1.00 123.89 ?  275 GLU B OE1 1 
ATOM   7347  O  OE2 . GLU B  2  275 ? 96.714  22.005  -5.180  1.00 126.67 ?  275 GLU B OE2 1 
ATOM   7348  N  N   . LEU B  2  276 ? 102.416 21.926  -1.553  1.00 51.10  ?  276 LEU B N   1 
ATOM   7349  C  CA  . LEU B  2  276 ? 103.421 22.624  -0.747  1.00 50.67  ?  276 LEU B CA  1 
ATOM   7350  C  C   . LEU B  2  276 ? 104.788 21.947  -0.847  1.00 53.95  ?  276 LEU B C   1 
ATOM   7351  O  O   . LEU B  2  276 ? 105.808 22.628  -0.763  1.00 60.23  ?  276 LEU B O   1 
ATOM   7352  C  CB  . LEU B  2  276 ? 102.978 22.741  0.718   1.00 45.51  ?  276 LEU B CB  1 
ATOM   7353  C  CG  . LEU B  2  276 ? 101.775 23.643  0.977   1.00 49.37  ?  276 LEU B CG  1 
ATOM   7354  C  CD1 . LEU B  2  276 ? 101.447 23.687  2.449   1.00 54.41  ?  276 LEU B CD1 1 
ATOM   7355  C  CD2 . LEU B  2  276 ? 102.011 25.069  0.457   1.00 51.21  ?  276 LEU B CD2 1 
ATOM   7356  N  N   . VAL B  2  277 ? 104.825 20.622  -1.055  1.00 52.30  ?  277 VAL B N   1 
ATOM   7357  C  CA  . VAL B  2  277 ? 106.088 19.907  -1.219  1.00 48.14  ?  277 VAL B CA  1 
ATOM   7358  C  C   . VAL B  2  277 ? 106.732 20.378  -2.523  1.00 55.97  ?  277 VAL B C   1 
ATOM   7359  O  O   . VAL B  2  277 ? 107.937 20.630  -2.557  1.00 58.54  ?  277 VAL B O   1 
ATOM   7360  C  CB  . VAL B  2  277 ? 105.870 18.377  -1.223  1.00 45.68  ?  277 VAL B CB  1 
ATOM   7361  C  CG1 . VAL B  2  277 ? 107.117 17.639  -1.707  1.00 44.05  ?  277 VAL B CG1 1 
ATOM   7362  C  CG2 . VAL B  2  277 ? 105.456 17.887  0.161   1.00 52.07  ?  277 VAL B CG2 1 
ATOM   7363  N  N   . GLU B  2  278 ? 105.926 20.513  -3.588  1.00 47.37  ?  278 GLU B N   1 
ATOM   7364  C  CA  . GLU B  2  278 ? 106.412 20.974  -4.878  1.00 42.94  ?  278 GLU B CA  1 
ATOM   7365  C  C   . GLU B  2  278 ? 106.792 22.436  -4.813  1.00 52.65  ?  278 GLU B C   1 
ATOM   7366  O  O   . GLU B  2  278 ? 107.775 22.827  -5.440  1.00 58.72  ?  278 GLU B O   1 
ATOM   7367  C  CB  . GLU B  2  278 ? 105.355 20.773  -5.970  1.00 47.21  ?  278 GLU B CB  1 
ATOM   7368  C  CG  . GLU B  2  278 ? 105.211 19.335  -6.420  1.00 62.59  ?  278 GLU B CG  1 
ATOM   7369  C  CD  . GLU B  2  278 ? 106.496 18.715  -6.930  1.00 78.55  ?  278 GLU B CD  1 
ATOM   7370  O  OE1 . GLU B  2  278 ? 106.979 19.135  -8.007  1.00 72.69  ?  278 GLU B OE1 1 
ATOM   7371  O  OE2 . GLU B  2  278 ? 107.022 17.808  -6.245  1.00 78.15  ?  278 GLU B OE2 1 
ATOM   7372  N  N   . LEU B  2  279 ? 106.043 23.258  -4.056  1.00 52.93  ?  279 LEU B N   1 
ATOM   7373  C  CA  . LEU B  2  279 ? 106.369 24.683  -3.944  1.00 53.34  ?  279 LEU B CA  1 
ATOM   7374  C  C   . LEU B  2  279 ? 107.764 24.867  -3.350  1.00 55.24  ?  279 LEU B C   1 
ATOM   7375  O  O   . LEU B  2  279 ? 108.506 25.737  -3.801  1.00 65.79  ?  279 LEU B O   1 
ATOM   7376  C  CB  . LEU B  2  279 ? 105.326 25.430  -3.104  1.00 47.43  ?  279 LEU B CB  1 
ATOM   7377  C  CG  . LEU B  2  279 ? 105.513 26.943  -3.015  1.00 38.16  ?  279 LEU B CG  1 
ATOM   7378  C  CD1 . LEU B  2  279 ? 105.279 27.607  -4.353  1.00 39.42  ?  279 LEU B CD1 1 
ATOM   7379  C  CD2 . LEU B  2  279 ? 104.597 27.536  -1.973  1.00 52.68  ?  279 LEU B CD2 1 
ATOM   7380  N  N   . ALA B  2  280 ? 108.134 24.032  -2.363  1.00 52.52  ?  280 ALA B N   1 
ATOM   7381  C  CA  . ALA B  2  280 ? 109.463 24.086  -1.758  1.00 45.30  ?  280 ALA B CA  1 
ATOM   7382  C  C   . ALA B  2  280 ? 110.532 23.800  -2.822  1.00 52.12  ?  280 ALA B C   1 
ATOM   7383  O  O   . ALA B  2  280 ? 111.633 24.333  -2.739  1.00 53.62  ?  280 ALA B O   1 
ATOM   7384  C  CB  . ALA B  2  280 ? 109.564 23.074  -0.634  1.00 46.06  ?  280 ALA B CB  1 
ATOM   7385  N  N   . LYS B  2  281 ? 110.206 22.984  -3.829  1.00 45.61  ?  281 LYS B N   1 
ATOM   7386  C  CA  . LYS B  2  281 ? 111.139 22.684  -4.906  1.00 54.23  ?  281 LYS B CA  1 
ATOM   7387  C  C   . LYS B  2  281 ? 111.201 23.871  -5.879  1.00 58.52  ?  281 LYS B C   1 
ATOM   7388  O  O   . LYS B  2  281 ? 112.281 24.208  -6.360  1.00 64.51  ?  281 LYS B O   1 
ATOM   7389  C  CB  . LYS B  2  281 ? 110.720 21.412  -5.648  1.00 50.76  ?  281 LYS B CB  1 
ATOM   7390  C  CG  . LYS B  2  281 ? 110.510 20.212  -4.739  1.00 44.17  ?  281 LYS B CG  1 
ATOM   7391  C  CD  . LYS B  2  281 ? 110.776 18.908  -5.465  1.00 56.41  ?  281 LYS B CD  1 
ATOM   7392  C  CE  . LYS B  2  281 ? 110.018 17.726  -4.911  1.00 47.51  ?  281 LYS B CE  1 
ATOM   7393  N  NZ  . LYS B  2  281 ? 109.390 16.919  -5.991  1.00 52.73  ?  281 LYS B NZ  1 
ATOM   7394  N  N   . SER B  2  282 ? 110.051 24.509  -6.161  1.00 53.95  ?  282 SER B N   1 
ATOM   7395  C  CA  . SER B  2  282 ? 109.980 25.662  -7.062  1.00 56.26  ?  282 SER B CA  1 
ATOM   7396  C  C   . SER B  2  282 ? 110.891 26.786  -6.592  1.00 65.17  ?  282 SER B C   1 
ATOM   7397  O  O   . SER B  2  282 ? 111.515 27.455  -7.416  1.00 72.31  ?  282 SER B O   1 
ATOM   7398  C  CB  . SER B  2  282 ? 108.551 26.187  -7.146  1.00 47.96  ?  282 SER B CB  1 
ATOM   7399  O  OG  . SER B  2  282 ? 107.681 25.221  -7.712  1.00 80.39  ?  282 SER B OG  1 
ATOM   7400  N  N   . VAL B  2  283 ? 110.970 26.998  -5.271  1.00 52.27  ?  283 VAL B N   1 
ATOM   7401  C  CA  . VAL B  2  283 ? 111.830 28.051  -4.728  1.00 50.07  ?  283 VAL B CA  1 
ATOM   7402  C  C   . VAL B  2  283 ? 113.326 27.626  -4.671  1.00 61.92  ?  283 VAL B C   1 
ATOM   7403  O  O   . VAL B  2  283 ? 114.181 28.455  -4.358  1.00 65.61  ?  283 VAL B O   1 
ATOM   7404  C  CB  . VAL B  2  283 ? 111.319 28.595  -3.372  1.00 52.35  ?  283 VAL B CB  1 
ATOM   7405  C  CG1 . VAL B  2  283 ? 109.875 29.072  -3.485  1.00 47.02  ?  283 VAL B CG1 1 
ATOM   7406  C  CG2 . VAL B  2  283 ? 111.469 27.570  -2.255  1.00 51.64  ?  283 VAL B CG2 1 
ATOM   7407  N  N   . GLY B  2  284 ? 113.622 26.362  -4.989  1.00 49.88  ?  284 GLY B N   1 
ATOM   7408  C  CA  . GLY B  2  284 ? 114.980 25.836  -5.012  1.00 47.54  ?  284 GLY B CA  1 
ATOM   7409  C  C   . GLY B  2  284 ? 115.462 25.252  -3.701  1.00 47.00  ?  284 GLY B C   1 
ATOM   7410  O  O   . GLY B  2  284 ? 116.614 25.468  -3.323  1.00 56.38  ?  284 GLY B O   1 
ATOM   7411  N  N   . ALA B  2  285 ? 114.614 24.489  -3.008  1.00 49.14  ?  285 ALA B N   1 
ATOM   7412  C  CA  . ALA B  2  285 ? 114.998 23.890  -1.731  1.00 50.40  ?  285 ALA B CA  1 
ATOM   7413  C  C   . ALA B  2  285 ? 114.999 22.358  -1.788  1.00 54.25  ?  285 ALA B C   1 
ATOM   7414  O  O   . ALA B  2  285 ? 114.364 21.769  -2.661  1.00 62.96  ?  285 ALA B O   1 
ATOM   7415  C  CB  . ALA B  2  285 ? 114.053 24.371  -0.637  1.00 50.63  ?  285 ALA B CB  1 
ATOM   7416  N  N   . ASP B  2  286 ? 115.719 21.718  -0.852  1.00 55.47  ?  286 ASP B N   1 
ATOM   7417  C  CA  . ASP B  2  286 ? 115.775 20.258  -0.754  1.00 58.71  ?  286 ASP B CA  1 
ATOM   7418  C  C   . ASP B  2  286 ? 114.407 19.703  -0.322  1.00 52.46  ?  286 ASP B C   1 
ATOM   7419  O  O   . ASP B  2  286 ? 114.037 18.598  -0.712  1.00 53.38  ?  286 ASP B O   1 
ATOM   7420  C  CB  . ASP B  2  286 ? 116.833 19.826  0.275   1.00 51.11  ?  286 ASP B CB  1 
ATOM   7421  C  CG  . ASP B  2  286 ? 118.270 20.026  -0.162  1.00 76.26  ?  286 ASP B CG  1 
ATOM   7422  O  OD1 . ASP B  2  286 ? 118.523 20.058  -1.392  1.00 85.39  ?  286 ASP B OD1 1 
ATOM   7423  O  OD2 . ASP B  2  286 ? 119.146 20.139  0.722   1.00 83.36  ?  286 ASP B OD2 1 
ATOM   7424  N  N   . GLY B  2  287 ? 113.690 20.472  0.495   1.00 45.86  ?  287 GLY B N   1 
ATOM   7425  C  CA  . GLY B  2  287 ? 112.373 20.116  1.005   1.00 50.97  ?  287 GLY B CA  1 
ATOM   7426  C  C   . GLY B  2  287 ? 111.949 21.046  2.124   1.00 50.31  ?  287 GLY B C   1 
ATOM   7427  O  O   . GLY B  2  287 ? 112.507 22.137  2.268   1.00 54.57  ?  287 GLY B O   1 
ATOM   7428  N  N   . ILE B  2  288 ? 110.968 20.627  2.932   1.00 46.57  ?  288 ILE B N   1 
ATOM   7429  C  CA  . ILE B  2  288 ? 110.503 21.443  4.053   1.00 42.55  ?  288 ILE B CA  1 
ATOM   7430  C  C   . ILE B  2  288 ? 111.061 20.866  5.359   1.00 41.95  ?  288 ILE B C   1 
ATOM   7431  O  O   . ILE B  2  288 ? 110.662 19.779  5.774   1.00 53.36  ?  288 ILE B O   1 
ATOM   7432  C  CB  . ILE B  2  288 ? 108.956 21.554  4.083   1.00 35.71  ?  288 ILE B CB  1 
ATOM   7433  C  CG1 . ILE B  2  288 ? 108.415 22.029  2.724   1.00 36.34  ?  288 ILE B CG1 1 
ATOM   7434  C  CG2 . ILE B  2  288 ? 108.510 22.508  5.191   1.00 35.43  ?  288 ILE B CG2 1 
ATOM   7435  C  CD1 . ILE B  2  288 ? 106.963 21.738  2.498   1.00 47.64  ?  288 ILE B CD1 1 
ATOM   7436  N  N   . ASN B  2  289 ? 111.996 21.584  5.996   1.00 49.12  ?  289 ASN B N   1 
ATOM   7437  C  CA  . ASN B  2  289 ? 112.593 21.158  7.258   1.00 43.32  ?  289 ASN B CA  1 
ATOM   7438  C  C   . ASN B  2  289 ? 111.789 21.780  8.391   1.00 42.10  ?  289 ASN B C   1 
ATOM   7439  O  O   . ASN B  2  289 ? 111.905 22.975  8.649   1.00 54.19  ?  289 ASN B O   1 
ATOM   7440  C  CB  . ASN B  2  289 ? 114.054 21.588  7.342   1.00 47.07  ?  289 ASN B CB  1 
ATOM   7441  C  CG  . ASN B  2  289 ? 114.771 21.021  8.543   1.00 47.45  ?  289 ASN B CG  1 
ATOM   7442  O  OD1 . ASN B  2  289 ? 114.656 19.833  8.862   1.00 45.65  ?  289 ASN B OD1 1 
ATOM   7443  N  ND2 . ASN B  2  289 ? 115.537 21.847  9.237   1.00 53.22  ?  289 ASN B ND2 1 
ATOM   7444  N  N   . LEU B  2  290 ? 110.987 20.940  9.054   1.00 50.06  ?  290 LEU B N   1 
ATOM   7445  C  CA  . LEU B  2  290 ? 110.125 21.407  10.170  1.00 42.37  ?  290 LEU B CA  1 
ATOM   7446  C  C   . LEU B  2  290 ? 110.876 21.265  11.492  1.00 50.71  ?  290 LEU B C   1 
ATOM   7447  O  O   . LEU B  2  290 ? 111.351 20.151  11.780  1.00 66.89  ?  290 LEU B O   1 
ATOM   7448  C  CB  . LEU B  2  290 ? 108.871 20.531  10.195  1.00 48.95  ?  290 LEU B CB  1 
ATOM   7449  C  CG  . LEU B  2  290 ? 107.707 21.016  9.336   1.00 55.20  ?  290 LEU B CG  1 
ATOM   7450  C  CD1 . LEU B  2  290 ? 106.425 20.284  9.701   1.00 45.37  ?  290 LEU B CD1 1 
ATOM   7451  C  CD2 . LEU B  2  290 ? 107.527 22.511  9.505   1.00 55.47  ?  290 LEU B CD2 1 
ATOM   7452  N  N   . CYS B  2  291 ? 110.971 22.347  12.263  1.00 44.55  ?  291 CYS B N   1 
ATOM   7453  C  CA  . CYS B  2  291 ? 111.595 22.276  13.582  1.00 39.11  ?  291 CYS B CA  1 
ATOM   7454  C  C   . CYS B  2  291 ? 110.657 22.898  14.593  1.00 43.16  ?  291 CYS B C   1 
ATOM   7455  O  O   . CYS B  2  291 ? 109.759 23.649  14.224  1.00 41.22  ?  291 CYS B O   1 
ATOM   7456  C  CB  . CYS B  2  291 ? 112.949 22.975  13.593  1.00 34.28  ?  291 CYS B CB  1 
ATOM   7457  S  SG  . CYS B  2  291 ? 114.035 22.516  12.223  1.00 60.78  ?  291 CYS B SG  1 
ATOM   7458  N  N   . GLY B  2  292 ? 110.875 22.586  15.859  1.00 37.80  ?  292 GLY B N   1 
ATOM   7459  C  CA  . GLY B  2  292 ? 110.061 23.114  16.937  1.00 28.81  ?  292 GLY B CA  1 
ATOM   7460  C  C   . GLY B  2  292 ? 110.900 23.691  18.049  1.00 42.55  ?  292 GLY B C   1 
ATOM   7461  O  O   . GLY B  2  292 ? 112.095 23.414  18.136  1.00 50.64  ?  292 GLY B O   1 
ATOM   7462  N  N   . MET B  2  293 ? 110.279 24.506  18.906  1.00 40.17  ?  293 MET B N   1 
ATOM   7463  C  CA  . MET B  2  293 ? 110.946 25.135  20.043  1.00 41.51  ?  293 MET B CA  1 
ATOM   7464  C  C   . MET B  2  293 ? 109.974 25.210  21.196  1.00 53.68  ?  293 MET B C   1 
ATOM   7465  O  O   . MET B  2  293 ? 108.777 25.366  20.970  1.00 65.49  ?  293 MET B O   1 
ATOM   7466  C  CB  . MET B  2  293 ? 111.406 26.550  19.679  1.00 38.27  ?  293 MET B CB  1 
ATOM   7467  C  CG  . MET B  2  293 ? 112.575 26.567  18.728  1.00 45.30  ?  293 MET B CG  1 
ATOM   7468  S  SD  . MET B  2  293 ? 113.589 28.049  18.853  1.00 47.34  ?  293 MET B SD  1 
ATOM   7469  C  CE  . MET B  2  293 ? 112.429 29.274  18.312  1.00 62.74  ?  293 MET B CE  1 
ATOM   7470  N  N   . CYS B  2  294 ? 110.499 25.111  22.419  1.00 44.15  ?  294 CYS B N   1 
ATOM   7471  C  CA  . CYS B  2  294 ? 109.652 25.227  23.636  1.00 51.79  ?  294 CYS B CA  1 
ATOM   7472  C  C   . CYS B  2  294 ? 108.569 24.143  23.644  1.00 51.81  ?  294 CYS B C   1 
ATOM   7473  O  O   . CYS B  2  294 ? 108.740 23.135  22.933  1.00 49.86  ?  294 CYS B O   1 
ATOM   7474  C  CB  . CYS B  2  294 ? 109.036 26.619  23.731  1.00 59.07  ?  294 CYS B CB  1 
ATOM   7475  S  SG  . CYS B  2  294 ? 110.162 27.845  24.445  1.00 53.16  ?  294 CYS B SG  1 
ATOM   7476  N  N   . CYS B  2  295 ? 107.499 24.347  24.415  1.00 53.10  ?  295 CYS B N   1 
ATOM   7477  C  CA  . CYS B  2  295 ? 106.452 23.299  24.567  1.00 48.73  ?  295 CYS B CA  1 
ATOM   7478  C  C   . CYS B  2  295 ? 105.895 22.867  23.203  1.00 43.73  ?  295 CYS B C   1 
ATOM   7479  O  O   . CYS B  2  295 ? 105.828 21.646  22.973  1.00 59.33  ?  295 CYS B O   1 
ATOM   7480  C  CB  . CYS B  2  295 ? 105.344 23.783  25.497  1.00 50.30  ?  295 CYS B CB  1 
ATOM   7481  S  SG  . CYS B  2  295 ? 105.766 23.606  27.251  1.00 85.00  ?  295 CYS B SG  1 
ATOM   7482  N  N   . THR B  2  296 ? 105.496 23.804  22.338  1.00 44.88  ?  296 THR B N   1 
ATOM   7483  C  CA  . THR B  2  296 ? 104.893 23.373  21.066  1.00 47.49  ?  296 THR B CA  1 
ATOM   7484  C  C   . THR B  2  296 ? 105.805 22.390  20.340  1.00 42.42  ?  296 THR B C   1 
ATOM   7485  O  O   . THR B  2  296 ? 105.325 21.404  19.804  1.00 52.85  ?  296 THR B O   1 
ATOM   7486  C  CB  . THR B  2  296 ? 104.526 24.548  20.153  1.00 51.29  ?  296 THR B CB  1 
ATOM   7487  O  OG1 . THR B  2  296 ? 103.643 24.082  19.133  1.00 51.37  ?  296 THR B OG1 1 
ATOM   7488  C  CG2 . THR B  2  296 ? 105.727 25.158  19.485  1.00 48.54  ?  296 THR B CG2 1 
ATOM   7489  N  N   . GLY B  2  297 ? 107.106 22.651  20.353  1.00 49.97  ?  297 GLY B N   1 
ATOM   7490  C  CA  . GLY B  2  297 ? 108.077 21.773  19.719  1.00 42.76  ?  297 GLY B CA  1 
ATOM   7491  C  C   . GLY B  2  297 ? 108.139 20.421  20.393  1.00 46.26  ?  297 GLY B C   1 
ATOM   7492  O  O   . GLY B  2  297 ? 108.411 19.418  19.734  1.00 56.15  ?  297 GLY B O   1 
ATOM   7493  N  N   . ASN B  2  298 ? 107.882 20.381  21.711  1.00 43.95  ?  298 ASN B N   1 
ATOM   7494  C  CA  . ASN B  2  298 ? 107.873 19.138  22.474  1.00 40.12  ?  298 ASN B CA  1 
ATOM   7495  C  C   . ASN B  2  298 ? 106.651 18.316  22.086  1.00 52.09  ?  298 ASN B C   1 
ATOM   7496  O  O   . ASN B  2  298 ? 106.768 17.113  21.886  1.00 50.66  ?  298 ASN B O   1 
ATOM   7497  C  CB  . ASN B  2  298 ? 107.824 19.422  23.980  1.00 43.63  ?  298 ASN B CB  1 
ATOM   7498  C  CG  . ASN B  2  298 ? 109.166 19.696  24.602  1.00 47.79  ?  298 ASN B CG  1 
ATOM   7499  O  OD1 . ASN B  2  298 ? 110.142 18.986  24.348  1.00 55.05  ?  298 ASN B OD1 1 
ATOM   7500  N  ND2 . ASN B  2  298 ? 109.253 20.715  25.451  1.00 54.14  ?  298 ASN B ND2 1 
ATOM   7501  N  N   . GLU B  2  299 ? 105.477 18.959  21.974  1.00 46.52  ?  299 GLU B N   1 
ATOM   7502  C  CA  . GLU B  2  299 ? 104.239 18.257  21.627  1.00 51.02  ?  299 GLU B CA  1 
ATOM   7503  C  C   . GLU B  2  299 ? 104.346 17.574  20.264  1.00 55.18  ?  299 GLU B C   1 
ATOM   7504  O  O   . GLU B  2  299 ? 103.860 16.455  20.101  1.00 63.12  ?  299 GLU B O   1 
ATOM   7505  C  CB  . GLU B  2  299 ? 103.029 19.217  21.637  1.00 40.90  ?  299 GLU B CB  1 
ATOM   7506  C  CG  . GLU B  2  299 ? 102.734 19.854  22.987  1.00 63.64  ?  299 GLU B CG  1 
ATOM   7507  C  CD  . GLU B  2  299 ? 101.774 19.106  23.892  1.00 79.87  ?  299 GLU B CD  1 
ATOM   7508  O  OE1 . GLU B  2  299 ? 101.907 17.866  24.022  1.00 71.15  ?  299 GLU B OE1 1 
ATOM   7509  O  OE2 . GLU B  2  299 ? 100.896 19.769  24.490  1.00 79.35  ?  299 GLU B OE2 1 
ATOM   7510  N  N   . VAL B  2  300 ? 104.988 18.228  19.292  1.00 46.40  ?  300 VAL B N   1 
ATOM   7511  C  CA  . VAL B  2  300 ? 105.121 17.664  17.950  1.00 44.54  ?  300 VAL B CA  1 
ATOM   7512  C  C   . VAL B  2  300 ? 106.238 16.623  17.892  1.00 58.20  ?  300 VAL B C   1 
ATOM   7513  O  O   . VAL B  2  300 ? 106.148 15.669  17.122  1.00 51.90  ?  300 VAL B O   1 
ATOM   7514  C  CB  . VAL B  2  300 ? 105.347 18.755  16.885  1.00 37.30  ?  300 VAL B CB  1 
ATOM   7515  C  CG1 . VAL B  2  300 ? 105.187 18.172  15.501  1.00 54.75  ?  300 VAL B CG1 1 
ATOM   7516  C  CG2 . VAL B  2  300 ? 104.379 19.910  17.058  1.00 53.17  ?  300 VAL B CG2 1 
ATOM   7517  N  N   . SER B  2  301 ? 107.300 16.813  18.678  1.00 56.27  ?  301 SER B N   1 
ATOM   7518  C  CA  . SER B  2  301 ? 108.408 15.871  18.721  1.00 43.07  ?  301 SER B CA  1 
ATOM   7519  C  C   . SER B  2  301 ? 107.984 14.581  19.465  1.00 54.94  ?  301 SER B C   1 
ATOM   7520  O  O   . SER B  2  301 ? 108.462 13.498  19.133  1.00 49.91  ?  301 SER B O   1 
ATOM   7521  C  CB  . SER B  2  301 ? 109.608 16.518  19.400  1.00 33.27  ?  301 SER B CB  1 
ATOM   7522  O  OG  . SER B  2  301 ? 110.786 15.753  19.210  1.00 59.31  ?  301 SER B OG  1 
ATOM   7523  N  N   . MET B  2  302 ? 107.073 14.690  20.448  1.00 53.53  ?  302 MET B N   1 
ATOM   7524  C  CA  . MET B  2  302 ? 106.593 13.534  21.206  1.00 42.89  ?  302 MET B CA  1 
ATOM   7525  C  C   . MET B  2  302 ? 105.741 12.620  20.329  1.00 50.72  ?  302 MET B C   1 
ATOM   7526  O  O   . MET B  2  302 ? 105.824 11.393  20.449  1.00 56.41  ?  302 MET B O   1 
ATOM   7527  C  CB  . MET B  2  302 ? 105.723 13.993  22.390  1.00 48.86  ?  302 MET B CB  1 
ATOM   7528  C  CG  . MET B  2  302 ? 106.495 14.594  23.546  1.00 48.38  ?  302 MET B CG  1 
ATOM   7529  S  SD  . MET B  2  302 ? 107.267 13.402  24.668  1.00 47.72  ?  302 MET B SD  1 
ATOM   7530  C  CE  . MET B  2  302 ? 105.830 12.787  25.523  1.00 52.22  ?  302 MET B CE  1 
ATOM   7531  N  N   . ARG B  2  303 ? 104.904 13.216  19.463  1.00 44.98  ?  303 ARG B N   1 
ATOM   7532  C  CA  . ARG B  2  303 ? 104.003 12.452  18.600  1.00 47.41  ?  303 ARG B CA  1 
ATOM   7533  C  C   . ARG B  2  303 ? 104.533 12.202  17.190  1.00 56.27  ?  303 ARG B C   1 
ATOM   7534  O  O   . ARG B  2  303 ? 104.137 11.210  16.579  1.00 75.63  ?  303 ARG B O   1 
ATOM   7535  C  CB  . ARG B  2  303 ? 102.645 13.162  18.504  1.00 41.17  ?  303 ARG B CB  1 
ATOM   7536  C  CG  . ARG B  2  303 ? 102.018 13.436  19.857  1.00 52.19  ?  303 ARG B CG  1 
ATOM   7537  C  CD  . ARG B  2  303 ? 100.598 13.951  19.750  1.00 42.55  ?  303 ARG B CD  1 
ATOM   7538  N  NE  . ARG B  2  303 ? 99.952  14.021  21.064  1.00 48.98  ?  303 ARG B NE  1 
ATOM   7539  C  CZ  . ARG B  2  303 ? 100.124 15.002  21.946  1.00 51.76  ?  303 ARG B CZ  1 
ATOM   7540  N  NH1 . ARG B  2  303 ? 100.928 16.022  21.669  1.00 57.07  ?  303 ARG B NH1 1 
ATOM   7541  N  NH2 . ARG B  2  303 ? 99.494  14.972  23.113  1.00 42.03  ?  303 ARG B NH2 1 
ATOM   7542  N  N   . HIS B  2  304 ? 105.391 13.081  16.651  1.00 44.21  ?  304 HIS B N   1 
ATOM   7543  C  CA  . HIS B  2  304 ? 105.883 12.911  15.282  1.00 45.00  ?  304 HIS B CA  1 
ATOM   7544  C  C   . HIS B  2  304 ? 107.397 12.956  15.116  1.00 49.62  ?  304 HIS B C   1 
ATOM   7545  O  O   . HIS B  2  304 ? 107.875 12.954  13.984  1.00 47.25  ?  304 HIS B O   1 
ATOM   7546  C  CB  . HIS B  2  304 ? 105.236 13.966  14.379  1.00 49.20  ?  304 HIS B CB  1 
ATOM   7547  C  CG  . HIS B  2  304 ? 103.758 14.041  14.547  1.00 50.47  ?  304 HIS B CG  1 
ATOM   7548  N  ND1 . HIS B  2  304 ? 102.931 13.034  14.091  1.00 63.02  ?  304 HIS B ND1 1 
ATOM   7549  C  CD2 . HIS B  2  304 ? 103.007 14.979  15.165  1.00 51.81  ?  304 HIS B CD2 1 
ATOM   7550  C  CE1 . HIS B  2  304 ? 101.703 13.398  14.426  1.00 74.33  ?  304 HIS B CE1 1 
ATOM   7551  N  NE2 . HIS B  2  304 ? 101.704 14.560  15.079  1.00 54.64  ?  304 HIS B NE2 1 
ATOM   7552  N  N   . GLY B  2  305 ? 108.139 12.989  16.214  1.00 49.22  ?  305 GLY B N   1 
ATOM   7553  C  CA  . GLY B  2  305 ? 109.594 13.024  16.157  1.00 47.37  ?  305 GLY B CA  1 
ATOM   7554  C  C   . GLY B  2  305 ? 110.170 14.232  15.444  1.00 48.31  ?  305 GLY B C   1 
ATOM   7555  O  O   . GLY B  2  305 ? 111.329 14.203  15.024  1.00 43.13  ?  305 GLY B O   1 
ATOM   7556  N  N   . ILE B  2  306 ? 109.383 15.311  15.298  1.00 46.80  ?  306 ILE B N   1 
ATOM   7557  C  CA  . ILE B  2  306 ? 109.862 16.522  14.630  1.00 44.86  ?  306 ILE B CA  1 
ATOM   7558  C  C   . ILE B  2  306 ? 111.065 17.087  15.394  1.00 36.01  ?  306 ILE B C   1 
ATOM   7559  O  O   . ILE B  2  306 ? 110.981 17.318  16.592  1.00 41.08  ?  306 ILE B O   1 
ATOM   7560  C  CB  . ILE B  2  306 ? 108.709 17.561  14.489  1.00 42.89  ?  306 ILE B CB  1 
ATOM   7561  C  CG1 . ILE B  2  306 ? 107.624 17.080  13.494  1.00 29.94  ?  306 ILE B CG1 1 
ATOM   7562  C  CG2 . ILE B  2  306 ? 109.241 18.942  14.112  1.00 43.67  ?  306 ILE B CG2 1 
ATOM   7563  C  CD1 . ILE B  2  306 ? 108.041 16.760  12.108  1.00 52.03  ?  306 ILE B CD1 1 
ATOM   7564  N  N   . LYS B  2  307 ? 112.184 17.294  14.704  1.00 38.10  ?  307 LYS B N   1 
ATOM   7565  C  CA  . LYS B  2  307 ? 113.416 17.800  15.313  1.00 44.78  ?  307 LYS B CA  1 
ATOM   7566  C  C   . LYS B  2  307 ? 113.185 19.047  16.191  1.00 51.67  ?  307 LYS B C   1 
ATOM   7567  O  O   . LYS B  2  307 ? 112.368 19.902  15.840  1.00 48.01  ?  307 LYS B O   1 
ATOM   7568  C  CB  . LYS B  2  307 ? 114.463 18.089  14.219  1.00 42.81  ?  307 LYS B CB  1 
ATOM   7569  C  CG  . LYS B  2  307 ? 114.895 16.833  13.467  1.00 43.61  ?  307 LYS B CG  1 
ATOM   7570  C  CD  . LYS B  2  307 ? 116.138 17.016  12.622  1.00 53.46  ?  307 LYS B CD  1 
ATOM   7571  C  CE  . LYS B  2  307 ? 115.898 17.817  11.366  1.00 58.41  ?  307 LYS B CE  1 
ATOM   7572  N  NZ  . LYS B  2  307 ? 117.003 17.626  10.387  1.00 91.14  ?  307 LYS B NZ  1 
ATOM   7573  N  N   . ILE B  2  308 ? 113.889 19.127  17.339  1.00 46.56  ?  308 ILE B N   1 
ATOM   7574  C  CA  . ILE B  2  308 ? 113.779 20.238  18.287  1.00 29.76  ?  308 ILE B CA  1 
ATOM   7575  C  C   . ILE B  2  308 ? 114.934 21.214  18.077  1.00 43.37  ?  308 ILE B C   1 
ATOM   7576  O  O   . ILE B  2  308 ? 116.081 20.877  18.361  1.00 45.02  ?  308 ILE B O   1 
ATOM   7577  C  CB  . ILE B  2  308 ? 113.771 19.698  19.736  1.00 38.59  ?  308 ILE B CB  1 
ATOM   7578  C  CG1 . ILE B  2  308 ? 112.505 18.866  19.995  1.00 46.82  ?  308 ILE B CG1 1 
ATOM   7579  C  CG2 . ILE B  2  308 ? 113.870 20.844  20.740  1.00 40.96  ?  308 ILE B CG2 1 
ATOM   7580  C  CD1 . ILE B  2  308 ? 112.550 18.019  21.265  1.00 43.64  ?  308 ILE B CD1 1 
ATOM   7581  N  N   . ALA B  2  309 ? 114.638 22.429  17.603  1.00 52.65  ?  309 ALA B N   1 
ATOM   7582  C  CA  . ALA B  2  309 ? 115.671 23.436  17.366  1.00 46.22  ?  309 ALA B CA  1 
ATOM   7583  C  C   . ALA B  2  309 ? 116.278 23.986  18.660  1.00 44.97  ?  309 ALA B C   1 
ATOM   7584  O  O   . ALA B  2  309 ? 117.481 24.228  18.699  1.00 49.04  ?  309 ALA B O   1 
ATOM   7585  C  CB  . ALA B  2  309 ? 115.115 24.575  16.524  1.00 43.48  ?  309 ALA B CB  1 
ATOM   7586  N  N   . GLY B  2  310 ? 115.464 24.185  19.695  1.00 42.30  ?  310 GLY B N   1 
ATOM   7587  C  CA  . GLY B  2  310 ? 115.978 24.703  20.956  1.00 46.11  ?  310 GLY B CA  1 
ATOM   7588  C  C   . GLY B  2  310 ? 114.932 25.037  21.995  1.00 44.60  ?  310 GLY B C   1 
ATOM   7589  O  O   . GLY B  2  310 ? 113.736 24.867  21.761  1.00 45.16  ?  310 GLY B O   1 
ATOM   7590  N  N   . ASN B  2  311 ? 115.393 25.529  23.154  1.00 38.77  ?  311 ASN B N   1 
ATOM   7591  C  CA  . ASN B  2  311 ? 114.524 25.893  24.273  1.00 43.34  ?  311 ASN B CA  1 
ATOM   7592  C  C   . ASN B  2  311 ? 114.400 27.422  24.441  1.00 48.61  ?  311 ASN B C   1 
ATOM   7593  O  O   . ASN B  2  311 ? 114.925 28.171  23.619  1.00 47.36  ?  311 ASN B O   1 
ATOM   7594  C  CB  . ASN B  2  311 ? 114.974 25.182  25.563  1.00 43.21  ?  311 ASN B CB  1 
ATOM   7595  C  CG  . ASN B  2  311 ? 116.415 25.385  25.926  1.00 52.52  ?  311 ASN B CG  1 
ATOM   7596  O  OD1 . ASN B  2  311 ? 117.155 26.084  25.235  1.00 61.16  ?  311 ASN B OD1 1 
ATOM   7597  N  ND2 . ASN B  2  311 ? 116.852 24.775  27.020  1.00 44.98  ?  311 ASN B ND2 1 
ATOM   7598  N  N   . PHE B  2  312 ? 113.673 27.877  25.481  1.00 50.21  ?  312 PHE B N   1 
ATOM   7599  C  CA  . PHE B  2  312 ? 113.392 29.283  25.747  1.00 47.78  ?  312 PHE B CA  1 
ATOM   7600  C  C   . PHE B  2  312 ? 114.492 30.299  25.363  1.00 47.23  ?  312 PHE B C   1 
ATOM   7601  O  O   . PHE B  2  312 ? 114.271 31.079  24.437  1.00 54.22  ?  312 PHE B O   1 
ATOM   7602  C  CB  . PHE B  2  312 ? 112.972 29.499  27.211  1.00 51.05  ?  312 PHE B CB  1 
ATOM   7603  C  CG  . PHE B  2  312 ? 112.533 30.919  27.505  1.00 49.66  ?  312 PHE B CG  1 
ATOM   7604  C  CD1 . PHE B  2  312 ? 111.430 31.466  26.872  1.00 57.37  ?  312 PHE B CD1 1 
ATOM   7605  C  CD2 . PHE B  2  312 ? 113.227 31.705  28.411  1.00 49.97  ?  312 PHE B CD2 1 
ATOM   7606  C  CE1 . PHE B  2  312 ? 111.034 32.768  27.134  1.00 45.96  ?  312 PHE B CE1 1 
ATOM   7607  C  CE2 . PHE B  2  312 ? 112.825 33.007  28.675  1.00 47.83  ?  312 PHE B CE2 1 
ATOM   7608  C  CZ  . PHE B  2  312 ? 111.734 33.531  28.033  1.00 52.19  ?  312 PHE B CZ  1 
ATOM   7609  N  N   . MET B  2  313 ? 115.651 30.326  26.055  1.00 50.32  ?  313 MET B N   1 
ATOM   7610  C  CA  . MET B  2  313 ? 116.669 31.340  25.749  1.00 40.73  ?  313 MET B CA  1 
ATOM   7611  C  C   . MET B  2  313 ? 117.439 31.133  24.440  1.00 46.58  ?  313 MET B C   1 
ATOM   7612  O  O   . MET B  2  313 ? 118.277 31.970  24.105  1.00 52.68  ?  313 MET B O   1 
ATOM   7613  C  CB  . MET B  2  313 ? 117.628 31.534  26.930  1.00 47.48  ?  313 MET B CB  1 
ATOM   7614  C  CG  . MET B  2  313 ? 116.962 32.208  28.123  1.00 39.24  ?  313 MET B CG  1 
ATOM   7615  S  SD  . MET B  2  313 ? 118.049 33.125  29.240  1.00 49.66  ?  313 MET B SD  1 
ATOM   7616  C  CE  . MET B  2  313 ? 119.317 31.959  29.554  1.00 70.65  ?  313 MET B CE  1 
ATOM   7617  N  N   . GLN B  2  314 ? 117.128 30.087  23.669  1.00 48.78  ?  314 GLN B N   1 
ATOM   7618  C  CA  . GLN B  2  314 ? 117.785 29.867  22.380  1.00 41.08  ?  314 GLN B CA  1 
ATOM   7619  C  C   . GLN B  2  314 ? 116.959 30.450  21.214  1.00 52.16  ?  314 GLN B C   1 
ATOM   7620  O  O   . GLN B  2  314 ? 117.499 30.604  20.118  1.00 51.80  ?  314 GLN B O   1 
ATOM   7621  C  CB  . GLN B  2  314 ? 117.989 28.368  22.135  1.00 44.62  ?  314 GLN B CB  1 
ATOM   7622  C  CG  . GLN B  2  314 ? 119.149 27.763  22.892  1.00 44.88  ?  314 GLN B CG  1 
ATOM   7623  C  CD  . GLN B  2  314 ? 119.433 26.382  22.373  1.00 56.77  ?  314 GLN B CD  1 
ATOM   7624  O  OE1 . GLN B  2  314 ? 118.569 25.504  22.394  1.00 51.94  ?  314 GLN B OE1 1 
ATOM   7625  N  NE2 . GLN B  2  314 ? 120.644 26.154  21.887  1.00 60.97  ?  314 GLN B NE2 1 
ATOM   7626  N  N   . GLN B  2  315 ? 115.659 30.757  21.439  1.00 51.16  ?  315 GLN B N   1 
ATOM   7627  C  CA  . GLN B  2  315 ? 114.760 31.273  20.401  1.00 41.63  ?  315 GLN B CA  1 
ATOM   7628  C  C   . GLN B  2  315 ? 115.324 32.435  19.569  1.00 52.83  ?  315 GLN B C   1 
ATOM   7629  O  O   . GLN B  2  315 ? 115.143 32.445  18.348  1.00 64.18  ?  315 GLN B O   1 
ATOM   7630  C  CB  . GLN B  2  315 ? 113.381 31.644  20.981  1.00 36.94  ?  315 GLN B CB  1 
ATOM   7631  C  CG  . GLN B  2  315 ? 113.370 32.784  21.988  1.00 48.66  ?  315 GLN B CG  1 
ATOM   7632  C  CD  . GLN B  2  315 ? 111.994 32.960  22.576  1.00 46.88  ?  315 GLN B CD  1 
ATOM   7633  O  OE1 . GLN B  2  315 ? 111.210 33.790  22.121  1.00 54.05  ?  315 GLN B OE1 1 
ATOM   7634  N  NE2 . GLN B  2  315 ? 111.660 32.178  23.591  1.00 46.27  ?  315 GLN B NE2 1 
ATOM   7635  N  N   . GLU B  2  316 ? 115.992 33.407  20.201  1.00 51.11  ?  316 GLU B N   1 
ATOM   7636  C  CA  . GLU B  2  316 ? 116.556 34.531  19.449  1.00 46.68  ?  316 GLU B CA  1 
ATOM   7637  C  C   . GLU B  2  316 ? 117.723 34.058  18.609  1.00 53.45  ?  316 GLU B C   1 
ATOM   7638  O  O   . GLU B  2  316 ? 117.884 34.501  17.474  1.00 58.35  ?  316 GLU B O   1 
ATOM   7639  C  CB  . GLU B  2  316 ? 117.044 35.627  20.390  1.00 45.43  ?  316 GLU B CB  1 
ATOM   7640  C  CG  . GLU B  2  316 ? 115.928 36.390  21.063  1.00 52.46  ?  316 GLU B CG  1 
ATOM   7641  C  CD  . GLU B  2  316 ? 116.428 37.166  22.258  1.00 59.15  ?  316 GLU B CD  1 
ATOM   7642  O  OE1 . GLU B  2  316 ? 116.937 36.523  23.205  1.00 55.20  ?  316 GLU B OE1 1 
ATOM   7643  O  OE2 . GLU B  2  316 ? 116.331 38.415  22.241  1.00 49.19  ?  316 GLU B OE2 1 
ATOM   7644  N  N   . LEU B  2  317 ? 118.537 33.152  19.159  1.00 49.33  ?  317 LEU B N   1 
ATOM   7645  C  CA  . LEU B  2  317 ? 119.696 32.633  18.457  1.00 42.61  ?  317 LEU B CA  1 
ATOM   7646  C  C   . LEU B  2  317 ? 119.314 31.783  17.246  1.00 47.90  ?  317 LEU B C   1 
ATOM   7647  O  O   . LEU B  2  317 ? 120.117 31.656  16.323  1.00 55.45  ?  317 LEU B O   1 
ATOM   7648  C  CB  . LEU B  2  317 ? 120.602 31.875  19.422  1.00 41.97  ?  317 LEU B CB  1 
ATOM   7649  C  CG  . LEU B  2  317 ? 121.091 32.699  20.614  1.00 36.32  ?  317 LEU B CG  1 
ATOM   7650  C  CD1 . LEU B  2  317 ? 121.674 31.813  21.668  1.00 47.00  ?  317 LEU B CD1 1 
ATOM   7651  C  CD2 . LEU B  2  317 ? 122.105 33.740  20.186  1.00 47.13  ?  317 LEU B CD2 1 
ATOM   7652  N  N   . ALA B  2  318 ? 118.087 31.236  17.214  1.00 46.36  ?  318 ALA B N   1 
ATOM   7653  C  CA  . ALA B  2  318 ? 117.631 30.472  16.056  1.00 42.48  ?  318 ALA B CA  1 
ATOM   7654  C  C   . ALA B  2  318 ? 117.496 31.439  14.873  1.00 44.64  ?  318 ALA B C   1 
ATOM   7655  O  O   . ALA B  2  318 ? 117.903 31.110  13.762  1.00 53.91  ?  318 ALA B O   1 
ATOM   7656  C  CB  . ALA B  2  318 ? 116.291 29.813  16.349  1.00 43.69  ?  318 ALA B CB  1 
ATOM   7657  N  N   . VAL B  2  319 ? 116.957 32.646  15.118  1.00 41.17  ?  319 VAL B N   1 
ATOM   7658  C  CA  . VAL B  2  319 ? 116.806 33.654  14.069  1.00 45.58  ?  319 VAL B CA  1 
ATOM   7659  C  C   . VAL B  2  319 ? 118.197 34.120  13.620  1.00 50.03  ?  319 VAL B C   1 
ATOM   7660  O  O   . VAL B  2  319 ? 118.422 34.268  12.420  1.00 52.44  ?  319 VAL B O   1 
ATOM   7661  C  CB  . VAL B  2  319 ? 115.933 34.845  14.551  1.00 46.60  ?  319 VAL B CB  1 
ATOM   7662  C  CG1 . VAL B  2  319 ? 115.878 35.953  13.503  1.00 43.67  ?  319 VAL B CG1 1 
ATOM   7663  C  CG2 . VAL B  2  319 ? 114.524 34.383  14.915  1.00 41.09  ?  319 VAL B CG2 1 
ATOM   7664  N  N   . VAL B  2  320 ? 119.134 34.316  14.586  1.00 43.69  ?  320 VAL B N   1 
ATOM   7665  C  CA  . VAL B  2  320 ? 120.515 34.761  14.322  1.00 49.39  ?  320 VAL B CA  1 
ATOM   7666  C  C   . VAL B  2  320 ? 121.267 33.837  13.346  1.00 51.29  ?  320 VAL B C   1 
ATOM   7667  O  O   . VAL B  2  320 ? 122.185 34.307  12.681  1.00 50.72  ?  320 VAL B O   1 
ATOM   7668  C  CB  . VAL B  2  320 ? 121.322 34.977  15.635  1.00 45.00  ?  320 VAL B CB  1 
ATOM   7669  C  CG1 . VAL B  2  320 ? 122.789 35.282  15.350  1.00 41.50  ?  320 VAL B CG1 1 
ATOM   7670  C  CG2 . VAL B  2  320 ? 120.708 36.088  16.478  1.00 44.62  ?  320 VAL B CG2 1 
ATOM   7671  N  N   . THR B  2  321 ? 120.891 32.544  13.232  1.00 48.72  ?  321 THR B N   1 
ATOM   7672  C  CA  . THR B  2  321 ? 121.561 31.649  12.266  1.00 45.92  ?  321 THR B CA  1 
ATOM   7673  C  C   . THR B  2  321 ? 121.412 32.215  10.841  1.00 47.26  ?  321 THR B C   1 
ATOM   7674  O  O   . THR B  2  321 ? 122.292 32.030  10.007  1.00 59.80  ?  321 THR B O   1 
ATOM   7675  C  CB  . THR B  2  321 ? 120.958 30.225  12.264  1.00 44.29  ?  321 THR B CB  1 
ATOM   7676  O  OG1 . THR B  2  321 ? 119.563 30.295  11.971  1.00 49.52  ?  321 THR B OG1 1 
ATOM   7677  C  CG2 . THR B  2  321 ? 121.195 29.466  13.557  1.00 41.72  ?  321 THR B CG2 1 
ATOM   7678  N  N   . GLY B  2  322 ? 120.297 32.899  10.591  1.00 53.08  ?  322 GLY B N   1 
ATOM   7679  C  CA  . GLY B  2  322 ? 119.980 33.483  9.297   1.00 47.08  ?  322 GLY B CA  1 
ATOM   7680  C  C   . GLY B  2  322 ? 119.330 32.476  8.373   1.00 53.21  ?  322 GLY B C   1 
ATOM   7681  O  O   . GLY B  2  322 ? 119.150 32.759  7.186   1.00 61.77  ?  322 GLY B O   1 
ATOM   7682  N  N   . ALA B  2  323 ? 118.972 31.289  8.906   1.00 45.77  ?  323 ALA B N   1 
ATOM   7683  C  CA  . ALA B  2  323 ? 118.376 30.220  8.123   1.00 45.55  ?  323 ALA B CA  1 
ATOM   7684  C  C   . ALA B  2  323 ? 116.902 29.974  8.433   1.00 47.59  ?  323 ALA B C   1 
ATOM   7685  O  O   . ALA B  2  323 ? 116.307 29.101  7.807   1.00 51.40  ?  323 ALA B O   1 
ATOM   7686  C  CB  . ALA B  2  323 ? 119.165 28.942  8.337   1.00 36.53  ?  323 ALA B CB  1 
ATOM   7687  N  N   . VAL B  2  324 ? 116.301 30.714  9.374   1.00 46.61  ?  324 VAL B N   1 
ATOM   7688  C  CA  . VAL B  2  324 ? 114.888 30.506  9.685   1.00 43.12  ?  324 VAL B CA  1 
ATOM   7689  C  C   . VAL B  2  324 ? 114.092 31.297  8.663   1.00 49.93  ?  324 VAL B C   1 
ATOM   7690  O  O   . VAL B  2  324 ? 114.122 32.524  8.686   1.00 53.96  ?  324 VAL B O   1 
ATOM   7691  C  CB  . VAL B  2  324 ? 114.545 30.914  11.138  1.00 39.02  ?  324 VAL B CB  1 
ATOM   7692  C  CG1 . VAL B  2  324 ? 113.040 30.859  11.386  1.00 39.19  ?  324 VAL B CG1 1 
ATOM   7693  C  CG2 . VAL B  2  324 ? 115.283 30.023  12.130  1.00 32.53  ?  324 VAL B CG2 1 
ATOM   7694  N  N   . ASP B  2  325 ? 113.415 30.608  7.742   1.00 38.84  ?  325 ASP B N   1 
ATOM   7695  C  CA  . ASP B  2  325 ? 112.621 31.283  6.721   1.00 34.22  ?  325 ASP B CA  1 
ATOM   7696  C  C   . ASP B  2  325 ? 111.306 31.787  7.296   1.00 44.90  ?  325 ASP B C   1 
ATOM   7697  O  O   . ASP B  2  325 ? 110.839 32.858  6.922   1.00 44.07  ?  325 ASP B O   1 
ATOM   7698  C  CB  . ASP B  2  325 ? 112.352 30.340  5.557   1.00 40.45  ?  325 ASP B CB  1 
ATOM   7699  C  CG  . ASP B  2  325 ? 113.625 29.865  4.907   1.00 57.61  ?  325 ASP B CG  1 
ATOM   7700  O  OD1 . ASP B  2  325 ? 114.509 30.709  4.637   1.00 51.27  ?  325 ASP B OD1 1 
ATOM   7701  O  OD2 . ASP B  2  325 ? 113.753 28.650  4.684   1.00 64.02  ?  325 ASP B OD2 1 
ATOM   7702  N  N   . GLY B  2  326 ? 110.719 31.013  8.196   1.00 45.61  ?  326 GLY B N   1 
ATOM   7703  C  CA  . GLY B  2  326 ? 109.469 31.378  8.834   1.00 36.61  ?  326 GLY B CA  1 
ATOM   7704  C  C   . GLY B  2  326 ? 109.426 30.904  10.268  1.00 49.47  ?  326 GLY B C   1 
ATOM   7705  O  O   . GLY B  2  326 ? 109.700 29.736  10.547  1.00 48.80  ?  326 GLY B O   1 
ATOM   7706  N  N   . LEU B  2  327 ? 109.097 31.813  11.187  1.00 42.51  ?  327 LEU B N   1 
ATOM   7707  C  CA  . LEU B  2  327 ? 108.987 31.500  12.603  1.00 46.51  ?  327 LEU B CA  1 
ATOM   7708  C  C   . LEU B  2  327 ? 107.510 31.697  12.957  1.00 46.40  ?  327 LEU B C   1 
ATOM   7709  O  O   . LEU B  2  327 ? 107.058 32.826  13.143  1.00 52.76  ?  327 LEU B O   1 
ATOM   7710  C  CB  . LEU B  2  327 ? 109.913 32.427  13.424  1.00 42.76  ?  327 LEU B CB  1 
ATOM   7711  C  CG  . LEU B  2  327 ? 109.896 32.290  14.954  1.00 39.29  ?  327 LEU B CG  1 
ATOM   7712  C  CD1 . LEU B  2  327 ? 110.283 30.891  15.398  1.00 44.80  ?  327 LEU B CD1 1 
ATOM   7713  C  CD2 . LEU B  2  327 ? 110.852 33.276  15.585  1.00 37.59  ?  327 LEU B CD2 1 
ATOM   7714  N  N   . ILE B  2  328 ? 106.746 30.598  12.993  1.00 40.11  ?  328 ILE B N   1 
ATOM   7715  C  CA  . ILE B  2  328 ? 105.317 30.662  13.287  1.00 39.96  ?  328 ILE B CA  1 
ATOM   7716  C  C   . ILE B  2  328 ? 105.113 30.526  14.785  1.00 47.91  ?  328 ILE B C   1 
ATOM   7717  O  O   . ILE B  2  328 ? 105.597 29.571  15.386  1.00 57.56  ?  328 ILE B O   1 
ATOM   7718  C  CB  . ILE B  2  328 ? 104.542 29.573  12.509  1.00 36.59  ?  328 ILE B CB  1 
ATOM   7719  C  CG1 . ILE B  2  328 ? 104.870 29.631  10.996  1.00 37.85  ?  328 ILE B CG1 1 
ATOM   7720  C  CG2 . ILE B  2  328 ? 103.042 29.722  12.745  1.00 45.20  ?  328 ILE B CG2 1 
ATOM   7721  C  CD1 . ILE B  2  328 ? 104.605 28.367  10.267  1.00 38.94  ?  328 ILE B CD1 1 
ATOM   7722  N  N   . VAL B  2  329 ? 104.395 31.477  15.391  1.00 49.61  ?  329 VAL B N   1 
ATOM   7723  C  CA  . VAL B  2  329 ? 104.154 31.466  16.831  1.00 51.81  ?  329 VAL B CA  1 
ATOM   7724  C  C   . VAL B  2  329 ? 102.666 31.562  17.158  1.00 53.20  ?  329 VAL B C   1 
ATOM   7725  O  O   . VAL B  2  329 ? 101.865 31.966  16.313  1.00 47.26  ?  329 VAL B O   1 
ATOM   7726  C  CB  . VAL B  2  329 ? 104.959 32.592  17.529  1.00 43.33  ?  329 VAL B CB  1 
ATOM   7727  C  CG1 . VAL B  2  329 ? 106.432 32.526  17.149  1.00 41.45  ?  329 VAL B CG1 1 
ATOM   7728  C  CG2 . VAL B  2  329 ? 104.382 33.967  17.212  1.00 35.33  ?  329 VAL B CG2 1 
ATOM   7729  N  N   . ASP B  2  330 ? 102.336 31.215  18.416  1.00 45.50  ?  330 ASP B N   1 
ATOM   7730  C  CA  . ASP B  2  330 ? 100.936 31.283  18.922  1.00 50.68  ?  330 ASP B CA  1 
ATOM   7731  C  C   . ASP B  2  330 ? 100.919 32.024  20.270  1.00 59.51  ?  330 ASP B C   1 
ATOM   7732  O  O   . ASP B  2  330 ? 100.836 33.264  20.238  1.00 54.58  ?  330 ASP B O   1 
ATOM   7733  C  CB  . ASP B  2  330 ? 100.308 29.892  19.039  1.00 42.75  ?  330 ASP B CB  1 
ATOM   7734  C  CG  . ASP B  2  330 ? 101.202 28.853  19.692  1.00 60.94  ?  330 ASP B CG  1 
ATOM   7735  O  OD1 . ASP B  2  330 ? 101.960 29.222  20.604  1.00 69.12  ?  330 ASP B OD1 1 
ATOM   7736  O  OD2 . ASP B  2  330 ? 101.122 27.681  19.288  1.00 67.27  ?  330 ASP B OD2 1 
ATOM   7737  N  N   . VAL B  2  331 ? 100.997 31.308  21.406  1.00 50.91  ?  331 VAL B N   1 
ATOM   7738  C  CA  . VAL B  2  331 ? 100.925 31.945  22.733  1.00 43.75  ?  331 VAL B CA  1 
ATOM   7739  C  C   . VAL B  2  331 ? 102.033 31.473  23.685  1.00 57.54  ?  331 VAL B C   1 
ATOM   7740  O  O   . VAL B  2  331 ? 102.659 30.446  23.449  1.00 61.51  ?  331 VAL B O   1 
ATOM   7741  C  CB  . VAL B  2  331 ? 99.529  31.745  23.372  1.00 38.15  ?  331 VAL B CB  1 
ATOM   7742  C  CG1 . VAL B  2  331 ? 98.427  32.379  22.537  1.00 49.52  ?  331 VAL B CG1 1 
ATOM   7743  C  CG2 . VAL B  2  331 ? 99.246  30.270  23.620  1.00 51.03  ?  331 VAL B CG2 1 
ATOM   7744  N  N   . GLN B  2  332 ? 102.231 32.233  24.768  1.00 59.57  ?  332 GLN B N   1 
ATOM   7745  C  CA  . GLN B  2  332 ? 103.158 31.813  25.858  1.00 50.96  ?  332 GLN B CA  1 
ATOM   7746  C  C   . GLN B  2  332 ? 104.651 31.798  25.513  1.00 49.12  ?  332 GLN B C   1 
ATOM   7747  O  O   . GLN B  2  332 ? 105.045 31.010  24.634  1.00 43.39  ?  332 GLN B O   1 
ATOM   7748  C  CB  . GLN B  2  332 ? 102.691 30.458  26.402  1.00 52.59  ?  332 GLN B CB  1 
ATOM   7749  C  CG  . GLN B  2  332 ? 101.637 30.579  27.493  1.00 36.79  ?  332 GLN B CG  1 
ATOM   7750  C  CD  . GLN B  2  332 ? 100.772 29.346  27.594  1.00 63.41  ?  332 GLN B CD  1 
ATOM   7751  O  OE1 . GLN B  2  332 ? 101.227 28.275  27.988  1.00 74.01  ?  332 GLN B OE1 1 
ATOM   7752  N  NE2 . GLN B  2  332 ? 99.507  29.491  27.236  1.00 48.80  ?  332 GLN B NE2 1 
ATOM   7753  N  N   . CYS B  2  333 ? 105.438 32.644  26.186  1.00 53.63  ?  333 CYS B N   1 
ATOM   7754  C  CA  . CYS B  2  333 ? 106.922 32.610  26.054  1.00 48.08  ?  333 CYS B CA  1 
ATOM   7755  C  C   . CYS B  2  333 ? 107.412 32.845  24.623  1.00 53.54  ?  333 CYS B C   1 
ATOM   7756  O  O   . CYS B  2  333 ? 108.372 32.164  24.218  1.00 50.22  ?  333 CYS B O   1 
ATOM   7757  C  CB  . CYS B  2  333 ? 107.418 31.286  26.617  1.00 38.34  ?  333 CYS B CB  1 
ATOM   7758  S  SG  . CYS B  2  333 ? 106.422 30.798  28.048  1.00 56.48  ?  333 CYS B SG  1 
ATOM   7759  N  N   . ILE B  2  334 ? 106.798 33.781  23.900  1.00 51.41  ?  334 ILE B N   1 
ATOM   7760  C  CA  . ILE B  2  334 ? 107.322 34.159  22.555  1.00 43.45  ?  334 ILE B CA  1 
ATOM   7761  C  C   . ILE B  2  334 ? 107.939 35.546  22.732  1.00 48.95  ?  334 ILE B C   1 
ATOM   7762  O  O   . ILE B  2  334 ? 107.212 36.538  22.536  1.00 59.28  ?  334 ILE B O   1 
ATOM   7763  C  CB  . ILE B  2  334 ? 106.208 34.129  21.492  1.00 44.63  ?  334 ILE B CB  1 
ATOM   7764  C  CG1 . ILE B  2  334 ? 105.584 32.737  21.372  1.00 42.76  ?  334 ILE B CG1 1 
ATOM   7765  C  CG2 . ILE B  2  334 ? 106.727 34.630  20.154  1.00 49.56  ?  334 ILE B CG2 1 
ATOM   7766  C  CD1 . ILE B  2  334 ? 104.088 32.751  21.172  1.00 38.86  ?  334 ILE B CD1 1 
ATOM   7767  N  N   . MET B  2  335 ? 109.216 35.615  23.123  1.00 43.84  ?  335 MET B N   1 
ATOM   7768  C  CA  . MET B  2  335 ? 109.822 36.912  23.429  1.00 43.14  ?  335 MET B CA  1 
ATOM   7769  C  C   . MET B  2  335 ? 109.395 37.983  22.418  1.00 52.19  ?  335 MET B C   1 
ATOM   7770  O  O   . MET B  2  335 ? 109.577 37.771  21.221  1.00 47.79  ?  335 MET B O   1 
ATOM   7771  C  CB  . MET B  2  335 ? 111.353 36.803  23.443  1.00 33.86  ?  335 MET B CB  1 
ATOM   7772  C  CG  . MET B  2  335 ? 111.885 36.047  24.630  1.00 35.91  ?  335 MET B CG  1 
ATOM   7773  S  SD  . MET B  2  335 ? 113.680 36.058  24.645  1.00 48.54  ?  335 MET B SD  1 
ATOM   7774  C  CE  . MET B  2  335 ? 114.001 34.549  25.459  1.00 53.67  ?  335 MET B CE  1 
ATOM   7775  N  N   . PRO B  2  336 ? 108.830 39.138  22.848  1.00 49.64  ?  336 PRO B N   1 
ATOM   7776  C  CA  . PRO B  2  336 ? 108.451 40.163  21.860  1.00 44.28  ?  336 PRO B CA  1 
ATOM   7777  C  C   . PRO B  2  336 ? 109.646 40.674  21.054  1.00 59.63  ?  336 PRO B C   1 
ATOM   7778  O  O   . PRO B  2  336 ? 109.465 41.199  19.954  1.00 65.01  ?  336 PRO B O   1 
ATOM   7779  C  CB  . PRO B  2  336 ? 107.847 41.283  22.708  1.00 44.06  ?  336 PRO B CB  1 
ATOM   7780  C  CG  . PRO B  2  336 ? 107.553 40.683  24.010  1.00 48.97  ?  336 PRO B CG  1 
ATOM   7781  C  CD  . PRO B  2  336 ? 108.532 39.586  24.220  1.00 42.82  ?  336 PRO B CD  1 
ATOM   7782  N  N   . ALA B  2  337 ? 110.871 40.523  21.601  1.00 50.16  ?  337 ALA B N   1 
ATOM   7783  C  CA  . ALA B  2  337 ? 112.094 40.949  20.926  1.00 49.31  ?  337 ALA B CA  1 
ATOM   7784  C  C   . ALA B  2  337 ? 112.219 40.353  19.522  1.00 49.94  ?  337 ALA B C   1 
ATOM   7785  O  O   . ALA B  2  337 ? 112.878 40.942  18.668  1.00 61.86  ?  337 ALA B O   1 
ATOM   7786  C  CB  . ALA B  2  337 ? 113.303 40.544  21.750  1.00 54.52  ?  337 ALA B CB  1 
ATOM   7787  N  N   . LEU B  2  338 ? 111.595 39.193  19.280  1.00 43.35  ?  338 LEU B N   1 
ATOM   7788  C  CA  . LEU B  2  338 ? 111.657 38.539  17.979  1.00 46.28  ?  338 LEU B CA  1 
ATOM   7789  C  C   . LEU B  2  338 ? 111.151 39.436  16.850  1.00 55.98  ?  338 LEU B C   1 
ATOM   7790  O  O   . LEU B  2  338 ? 111.637 39.304  15.731  1.00 55.90  ?  338 LEU B O   1 
ATOM   7791  C  CB  . LEU B  2  338 ? 110.862 37.225  17.998  1.00 45.35  ?  338 LEU B CB  1 
ATOM   7792  C  CG  . LEU B  2  338 ? 111.444 36.084  18.843  1.00 41.39  ?  338 LEU B CG  1 
ATOM   7793  C  CD1 . LEU B  2  338 ? 110.376 35.054  19.169  1.00 40.39  ?  338 LEU B CD1 1 
ATOM   7794  C  CD2 . LEU B  2  338 ? 112.613 35.418  18.140  1.00 38.89  ?  338 LEU B CD2 1 
ATOM   7795  N  N   . ALA B  2  339 ? 110.192 40.344  17.121  1.00 55.60  ?  339 ALA B N   1 
ATOM   7796  C  CA  . ALA B  2  339 ? 109.677 41.234  16.076  1.00 52.03  ?  339 ALA B CA  1 
ATOM   7797  C  C   . ALA B  2  339 ? 110.775 42.179  15.558  1.00 56.97  ?  339 ALA B C   1 
ATOM   7798  O  O   . ALA B  2  339 ? 110.936 42.312  14.341  1.00 70.42  ?  339 ALA B O   1 
ATOM   7799  C  CB  . ALA B  2  339 ? 108.489 42.028  16.591  1.00 47.78  ?  339 ALA B CB  1 
ATOM   7800  N  N   . LYS B  2  340 ? 111.543 42.808  16.468  1.00 54.40  ?  340 LYS B N   1 
ATOM   7801  C  CA  . LYS B  2  340 ? 112.630 43.713  16.087  1.00 45.78  ?  340 LYS B CA  1 
ATOM   7802  C  C   . LYS B  2  340 ? 113.821 42.926  15.516  1.00 49.18  ?  340 LYS B C   1 
ATOM   7803  O  O   . LYS B  2  340 ? 114.386 43.310  14.493  1.00 57.52  ?  340 LYS B O   1 
ATOM   7804  C  CB  . LYS B  2  340 ? 113.082 44.549  17.303  1.00 66.15  ?  340 LYS B CB  1 
ATOM   7805  C  CG  . LYS B  2  340 ? 114.245 45.500  17.006  1.00 69.19  ?  340 LYS B CG  1 
ATOM   7806  C  CD  . LYS B  2  340 ? 114.397 46.634  18.040  1.00 64.70  ?  340 LYS B CD  1 
ATOM   7807  C  CE  . LYS B  2  340 ? 115.660 46.536  18.867  1.00 84.14  ?  340 LYS B CE  1 
ATOM   7808  N  NZ  . LYS B  2  340 ? 115.983 47.815  19.557  1.00 102.94 ?  340 LYS B NZ  1 
ATOM   7809  N  N   . LEU B  2  341 ? 114.202 41.828  16.179  1.00 53.95  ?  341 LEU B N   1 
ATOM   7810  C  CA  . LEU B  2  341 ? 115.324 40.998  15.744  1.00 52.27  ?  341 LEU B CA  1 
ATOM   7811  C  C   . LEU B  2  341 ? 115.119 40.488  14.322  1.00 52.42  ?  341 LEU B C   1 
ATOM   7812  O  O   . LEU B  2  341 ? 116.066 40.487  13.537  1.00 59.36  ?  341 LEU B O   1 
ATOM   7813  C  CB  . LEU B  2  341 ? 115.504 39.815  16.715  1.00 45.70  ?  341 LEU B CB  1 
ATOM   7814  C  CG  . LEU B  2  341 ? 116.654 38.846  16.428  1.00 36.24  ?  341 LEU B CG  1 
ATOM   7815  C  CD1 . LEU B  2  341 ? 117.984 39.463  16.754  1.00 47.32  ?  341 LEU B CD1 1 
ATOM   7816  C  CD2 . LEU B  2  341 ? 116.506 37.587  17.234  1.00 45.80  ?  341 LEU B CD2 1 
ATOM   7817  N  N   . SER B  2  342 ? 113.892 40.064  13.984  1.00 48.57  ?  342 SER B N   1 
ATOM   7818  C  CA  . SER B  2  342 ? 113.586 39.551  12.647  1.00 47.70  ?  342 SER B CA  1 
ATOM   7819  C  C   . SER B  2  342 ? 113.773 40.598  11.545  1.00 54.22  ?  342 SER B C   1 
ATOM   7820  O  O   . SER B  2  342 ? 113.935 40.235  10.383  1.00 59.59  ?  342 SER B O   1 
ATOM   7821  C  CB  . SER B  2  342 ? 112.165 39.006  12.600  1.00 50.41  ?  342 SER B CB  1 
ATOM   7822  O  OG  . SER B  2  342 ? 112.015 37.921  13.498  1.00 59.94  ?  342 SER B OG  1 
ATOM   7823  N  N   . LYS B  2  343 ? 113.749 41.888  11.898  1.00 56.62  ?  343 LYS B N   1 
ATOM   7824  C  CA  . LYS B  2  343 ? 113.937 42.952  10.919  1.00 47.71  ?  343 LYS B CA  1 
ATOM   7825  C  C   . LYS B  2  343 ? 115.385 42.977  10.409  1.00 51.00  ?  343 LYS B C   1 
ATOM   7826  O  O   . LYS B  2  343 ? 115.626 43.462  9.306   1.00 66.01  ?  343 LYS B O   1 
ATOM   7827  C  CB  . LYS B  2  343 ? 113.539 44.307  11.518  1.00 50.89  ?  343 LYS B CB  1 
ATOM   7828  C  CG  . LYS B  2  343 ? 112.069 44.354  11.905  1.00 58.47  ?  343 LYS B CG  1 
ATOM   7829  C  CD  . LYS B  2  343 ? 111.612 45.738  12.322  1.00 82.55  ?  343 LYS B CD  1 
ATOM   7830  C  CE  . LYS B  2  343 ? 110.109 45.797  12.491  1.00 84.88  ?  343 LYS B CE  1 
ATOM   7831  N  NZ  . LYS B  2  343 ? 109.398 45.994  11.194  1.00 99.52  ?  343 LYS B NZ  1 
ATOM   7832  N  N   . SER B  2  344 ? 116.343 42.449  11.193  1.00 47.20  ?  344 SER B N   1 
ATOM   7833  C  CA  . SER B  2  344 ? 117.748 42.399  10.791  1.00 56.66  ?  344 SER B CA  1 
ATOM   7834  C  C   . SER B  2  344 ? 118.052 41.185  9.892   1.00 55.64  ?  344 SER B C   1 
ATOM   7835  O  O   . SER B  2  344 ? 119.175 41.060  9.401   1.00 58.89  ?  344 SER B O   1 
ATOM   7836  C  CB  . SER B  2  344 ? 118.648 42.342  12.022  1.00 45.57  ?  344 SER B CB  1 
ATOM   7837  O  OG  . SER B  2  344 ? 118.216 43.233  13.038  1.00 63.92  ?  344 SER B OG  1 
ATOM   7838  N  N   . TYR B  2  345 ? 117.074 40.288  9.692   1.00 48.63  ?  345 TYR B N   1 
ATOM   7839  C  CA  . TYR B  2  345 ? 117.239 39.089  8.875   1.00 53.44  ?  345 TYR B CA  1 
ATOM   7840  C  C   . TYR B  2  345 ? 116.056 38.957  7.914   1.00 57.35  ?  345 TYR B C   1 
ATOM   7841  O  O   . TYR B  2  345 ? 115.115 39.748  7.992   1.00 58.25  ?  345 TYR B O   1 
ATOM   7842  C  CB  . TYR B  2  345 ? 117.330 37.862  9.796   1.00 45.30  ?  345 TYR B CB  1 
ATOM   7843  C  CG  . TYR B  2  345 ? 118.483 37.948  10.771  1.00 49.28  ?  345 TYR B CG  1 
ATOM   7844  C  CD1 . TYR B  2  345 ? 119.759 37.545  10.405  1.00 43.25  ?  345 TYR B CD1 1 
ATOM   7845  C  CD2 . TYR B  2  345 ? 118.303 38.460  12.048  1.00 44.59  ?  345 TYR B CD2 1 
ATOM   7846  C  CE1 . TYR B  2  345 ? 120.825 37.630  11.292  1.00 43.45  ?  345 TYR B CE1 1 
ATOM   7847  C  CE2 . TYR B  2  345 ? 119.365 38.567  12.938  1.00 54.47  ?  345 TYR B CE2 1 
ATOM   7848  C  CZ  . TYR B  2  345 ? 120.626 38.144  12.559  1.00 57.84  ?  345 TYR B CZ  1 
ATOM   7849  O  OH  . TYR B  2  345 ? 121.679 38.242  13.442  1.00 53.10  ?  345 TYR B OH  1 
ATOM   7850  N  N   . HIS B  2  346 ? 116.094 37.976  7.001   1.00 53.55  ?  346 HIS B N   1 
ATOM   7851  C  CA  . HIS B  2  346 ? 114.990 37.780  6.061   1.00 53.48  ?  346 HIS B CA  1 
ATOM   7852  C  C   . HIS B  2  346 ? 113.772 37.110  6.725   1.00 47.95  ?  346 HIS B C   1 
ATOM   7853  O  O   . HIS B  2  346 ? 112.659 37.235  6.215   1.00 51.09  ?  346 HIS B O   1 
ATOM   7854  C  CB  . HIS B  2  346 ? 115.453 36.953  4.854   1.00 48.69  ?  346 HIS B CB  1 
ATOM   7855  C  CG  . HIS B  2  346 ? 115.488 35.482  5.110   1.00 43.60  ?  346 HIS B CG  1 
ATOM   7856  N  ND1 . HIS B  2  346 ? 116.381 34.929  6.008   1.00 53.73  ?  346 HIS B ND1 1 
ATOM   7857  C  CD2 . HIS B  2  346 ? 114.732 34.495  4.578   1.00 53.63  ?  346 HIS B CD2 1 
ATOM   7858  C  CE1 . HIS B  2  346 ? 116.144 33.627  5.995   1.00 56.35  ?  346 HIS B CE1 1 
ATOM   7859  N  NE2 . HIS B  2  346 ? 115.161 33.319  5.147   1.00 53.62  ?  346 HIS B NE2 1 
ATOM   7860  N  N   . THR B  2  347 ? 113.990 36.394  7.851   1.00 55.43  ?  347 THR B N   1 
ATOM   7861  C  CA  . THR B  2  347 ? 112.956 35.669  8.605   1.00 49.44  ?  347 THR B CA  1 
ATOM   7862  C  C   . THR B  2  347 ? 111.610 36.379  8.698   1.00 50.09  ?  347 THR B C   1 
ATOM   7863  O  O   . THR B  2  347 ? 111.557 37.580  8.973   1.00 63.87  ?  347 THR B O   1 
ATOM   7864  C  CB  . THR B  2  347 ? 113.461 35.374  10.023  1.00 39.85  ?  347 THR B CB  1 
ATOM   7865  O  OG1 . THR B  2  347 ? 114.696 34.657  9.937   1.00 59.09  ?  347 THR B OG1 1 
ATOM   7866  C  CG2 . THR B  2  347 ? 112.451 34.587  10.848  1.00 46.92  ?  347 THR B CG2 1 
ATOM   7867  N  N   . LYS B  2  348 ? 110.519 35.625  8.490   1.00 51.06  ?  348 LYS B N   1 
ATOM   7868  C  CA  . LYS B  2  348 ? 109.170 36.169  8.590   1.00 58.57  ?  348 LYS B CA  1 
ATOM   7869  C  C   . LYS B  2  348 ? 108.587 35.731  9.929   1.00 55.35  ?  348 LYS B C   1 
ATOM   7870  O  O   . LYS B  2  348 ? 108.249 34.560  10.104  1.00 56.54  ?  348 LYS B O   1 
ATOM   7871  C  CB  . LYS B  2  348 ? 108.283 35.676  7.435   1.00 34.94  ?  348 LYS B CB  1 
ATOM   7872  C  CG  . LYS B  2  348 ? 108.087 36.698  6.324   1.00 53.61  ?  348 LYS B CG  1 
ATOM   7873  C  CD  . LYS B  2  348 ? 107.236 36.135  5.204   1.00 72.42  ?  348 LYS B CD  1 
ATOM   7874  C  CE  . LYS B  2  348 ? 107.004 37.118  4.088   1.00 63.14  ?  348 LYS B CE  1 
ATOM   7875  N  NZ  . LYS B  2  348 ? 105.908 36.666  3.193   1.00 84.66  ?  348 LYS B NZ  1 
ATOM   7876  N  N   . PHE B  2  349 ? 108.496 36.666  10.884  1.00 58.44  ?  349 PHE B N   1 
ATOM   7877  C  CA  . PHE B  2  349 ? 107.951 36.375  12.206  1.00 49.71  ?  349 PHE B CA  1 
ATOM   7878  C  C   . PHE B  2  349 ? 106.437 36.450  12.094  1.00 50.51  ?  349 PHE B C   1 
ATOM   7879  O  O   . PHE B  2  349 ? 105.887 37.540  11.949  1.00 50.78  ?  349 PHE B O   1 
ATOM   7880  C  CB  . PHE B  2  349 ? 108.491 37.384  13.232  1.00 42.42  ?  349 PHE B CB  1 
ATOM   7881  C  CG  . PHE B  2  349 ? 108.058 37.139  14.653  1.00 39.02  ?  349 PHE B CG  1 
ATOM   7882  C  CD1 . PHE B  2  349 ? 108.233 35.902  15.245  1.00 48.68  ?  349 PHE B CD1 1 
ATOM   7883  C  CD2 . PHE B  2  349 ? 107.513 38.158  15.412  1.00 40.50  ?  349 PHE B CD2 1 
ATOM   7884  C  CE1 . PHE B  2  349 ? 107.842 35.682  16.557  1.00 41.83  ?  349 PHE B CE1 1 
ATOM   7885  C  CE2 . PHE B  2  349 ? 107.117 37.935  16.721  1.00 39.40  ?  349 PHE B CE2 1 
ATOM   7886  C  CZ  . PHE B  2  349 ? 107.286 36.699  17.287  1.00 48.66  ?  349 PHE B CZ  1 
ATOM   7887  N  N   . ILE B  2  350 ? 105.764 35.290  12.114  1.00 45.32  ?  350 ILE B N   1 
ATOM   7888  C  CA  . ILE B  2  350 ? 104.312 35.232  11.963  1.00 53.58  ?  350 ILE B CA  1 
ATOM   7889  C  C   . ILE B  2  350 ? 103.598 34.935  13.272  1.00 48.44  ?  350 ILE B C   1 
ATOM   7890  O  O   . ILE B  2  350 ? 103.879 33.923  13.904  1.00 53.24  ?  350 ILE B O   1 
ATOM   7891  C  CB  . ILE B  2  350 ? 103.928 34.179  10.885  1.00 46.12  ?  350 ILE B CB  1 
ATOM   7892  C  CG1 . ILE B  2  350 ? 104.549 34.532  9.515   1.00 33.39  ?  350 ILE B CG1 1 
ATOM   7893  C  CG2 . ILE B  2  350 ? 102.404 34.040  10.777  1.00 48.47  ?  350 ILE B CG2 1 
ATOM   7894  C  CD1 . ILE B  2  350 ? 104.776 33.340  8.611   1.00 47.55  ?  350 ILE B CD1 1 
ATOM   7895  N  N   . THR B  2  351 ? 102.660 35.812  13.659  1.00 49.53  ?  351 THR B N   1 
ATOM   7896  C  CA  . THR B  2  351 ? 101.834 35.646  14.851  1.00 46.31  ?  351 THR B CA  1 
ATOM   7897  C  C   . THR B  2  351 ? 100.497 35.117  14.343  1.00 52.54  ?  351 THR B C   1 
ATOM   7898  O  O   . THR B  2  351 ? 99.986  35.622  13.341  1.00 57.05  ?  351 THR B O   1 
ATOM   7899  C  CB  . THR B  2  351 ? 101.694 36.967  15.629  1.00 50.52  ?  351 THR B CB  1 
ATOM   7900  O  OG1 . THR B  2  351 ? 101.424 38.052  14.732  1.00 51.38  ?  351 THR B OG1 1 
ATOM   7901  C  CG2 . THR B  2  351 ? 102.914 37.273  16.482  1.00 40.86  ?  351 THR B CG2 1 
ATOM   7902  N  N   . THR B  2  352 ? 99.946  34.080  14.997  1.00 53.29  ?  352 THR B N   1 
ATOM   7903  C  CA  . THR B  2  352 ? 98.699  33.471  14.538  1.00 44.63  ?  352 THR B CA  1 
ATOM   7904  C  C   . THR B  2  352 ? 97.549  33.489  15.547  1.00 47.49  ?  352 THR B C   1 
ATOM   7905  O  O   . THR B  2  352 ? 96.430  33.140  15.170  1.00 61.76  ?  352 THR B O   1 
ATOM   7906  C  CB  . THR B  2  352 ? 98.968  32.013  14.127  1.00 45.57  ?  352 THR B CB  1 
ATOM   7907  O  OG1 . THR B  2  352 ? 99.249  31.234  15.292  1.00 58.24  ?  352 THR B OG1 1 
ATOM   7908  C  CG2 . THR B  2  352 ? 100.108 31.875  13.128  1.00 43.74  ?  352 THR B CG2 1 
ATOM   7909  N  N   . SER B  2  353 ? 97.798  33.861  16.813  1.00 52.87  ?  353 SER B N   1 
ATOM   7910  C  CA  . SER B  2  353 ? 96.735  33.849  17.820  1.00 54.83  ?  353 SER B CA  1 
ATOM   7911  C  C   . SER B  2  353 ? 96.200  35.229  18.199  1.00 48.07  ?  353 SER B C   1 
ATOM   7912  O  O   . SER B  2  353 ? 96.987  36.119  18.517  1.00 57.44  ?  353 SER B O   1 
ATOM   7913  C  CB  . SER B  2  353 ? 97.226  33.163  19.090  1.00 60.84  ?  353 SER B CB  1 
ATOM   7914  O  OG  . SER B  2  353 ? 96.171  33.006  20.026  1.00 45.94  ?  353 SER B OG  1 
ATOM   7915  N  N   . PRO B  2  354 ? 94.865  35.423  18.245  1.00 45.95  ?  354 PRO B N   1 
ATOM   7916  C  CA  . PRO B  2  354 ? 94.343  36.720  18.699  1.00 55.93  ?  354 PRO B CA  1 
ATOM   7917  C  C   . PRO B  2  354 ? 94.615  36.937  20.196  1.00 62.40  ?  354 PRO B C   1 
ATOM   7918  O  O   . PRO B  2  354 ? 94.491  38.057  20.687  1.00 64.24  ?  354 PRO B O   1 
ATOM   7919  C  CB  . PRO B  2  354 ? 92.850  36.636  18.380  1.00 66.63  ?  354 PRO B CB  1 
ATOM   7920  C  CG  . PRO B  2  354 ? 92.538  35.194  18.405  1.00 50.85  ?  354 PRO B CG  1 
ATOM   7921  C  CD  . PRO B  2  354 ? 93.772  34.473  17.949  1.00 52.34  ?  354 PRO B CD  1 
ATOM   7922  N  N   . LYS B  2  355 ? 95.000  35.868  20.919  1.00 54.95  ?  355 LYS B N   1 
ATOM   7923  C  CA  . LYS B  2  355 ? 95.342  35.955  22.338  1.00 57.85  ?  355 LYS B CA  1 
ATOM   7924  C  C   . LYS B  2  355 ? 96.735  36.584  22.499  1.00 59.93  ?  355 LYS B C   1 
ATOM   7925  O  O   . LYS B  2  355 ? 97.026  37.135  23.558  1.00 53.88  ?  355 LYS B O   1 
ATOM   7926  C  CB  . LYS B  2  355 ? 95.389  34.561  22.982  1.00 52.16  ?  355 LYS B CB  1 
ATOM   7927  C  CG  . LYS B  2  355 ? 94.126  33.729  22.843  1.00 67.99  ?  355 LYS B CG  1 
ATOM   7928  C  CD  . LYS B  2  355 ? 94.351  32.337  23.400  1.00 64.77  ?  355 LYS B CD  1 
ATOM   7929  C  CE  . LYS B  2  355 ? 93.161  31.433  23.231  1.00 83.00  ?  355 LYS B CE  1 
ATOM   7930  N  NZ  . LYS B  2  355 ? 93.470  30.051  23.687  1.00 102.71 ?  355 LYS B NZ  1 
ATOM   7931  N  N   . ALA B  2  356 ? 97.608  36.459  21.472  1.00 53.90  ?  356 ALA B N   1 
ATOM   7932  C  CA  . ALA B  2  356 ? 98.960  36.992  21.517  1.00 50.45  ?  356 ALA B CA  1 
ATOM   7933  C  C   . ALA B  2  356 ? 99.348  37.748  20.238  1.00 61.43  ?  356 ALA B C   1 
ATOM   7934  O  O   . ALA B  2  356 ? 100.007 37.183  19.357  1.00 49.04  ?  356 ALA B O   1 
ATOM   7935  C  CB  . ALA B  2  356 ? 99.945  35.865  21.771  1.00 45.32  ?  356 ALA B CB  1 
ATOM   7936  N  N   . HIS B  2  357 ? 98.949  39.032  20.150  1.00 53.54  ?  357 HIS B N   1 
ATOM   7937  C  CA  . HIS B  2  357 ? 99.297  39.902  19.024  1.00 43.98  ?  357 HIS B CA  1 
ATOM   7938  C  C   . HIS B  2  357 ? 100.636 40.533  19.377  1.00 47.09  ?  357 HIS B C   1 
ATOM   7939  O  O   . HIS B  2  357 ? 100.827 40.911  20.525  1.00 60.50  ?  357 HIS B O   1 
ATOM   7940  C  CB  . HIS B  2  357 ? 98.265  41.032  18.845  1.00 54.39  ?  357 HIS B CB  1 
ATOM   7941  C  CG  . HIS B  2  357 ? 96.988  40.619  18.180  1.00 58.32  ?  357 HIS B CG  1 
ATOM   7942  N  ND1 . HIS B  2  357 ? 96.844  40.661  16.801  1.00 47.88  ?  357 HIS B ND1 1 
ATOM   7943  C  CD2 . HIS B  2  357 ? 95.826  40.194  18.728  1.00 59.36  ?  357 HIS B CD2 1 
ATOM   7944  C  CE1 . HIS B  2  357 ? 95.611  40.246  16.555  1.00 51.12  ?  357 HIS B CE1 1 
ATOM   7945  N  NE2 . HIS B  2  357 ? 94.961  39.952  17.685  1.00 62.39  ?  357 HIS B NE2 1 
ATOM   7946  N  N   . ILE B  2  358 ? 101.561 40.653  18.423  1.00 59.59  ?  358 ILE B N   1 
ATOM   7947  C  CA  . ILE B  2  358 ? 102.865 41.270  18.689  1.00 48.19  ?  358 ILE B CA  1 
ATOM   7948  C  C   . ILE B  2  358 ? 103.062 42.332  17.629  1.00 45.87  ?  358 ILE B C   1 
ATOM   7949  O  O   . ILE B  2  358 ? 103.021 42.023  16.443  1.00 53.74  ?  358 ILE B O   1 
ATOM   7950  C  CB  . ILE B  2  358 ? 104.023 40.237  18.699  1.00 40.62  ?  358 ILE B CB  1 
ATOM   7951  C  CG1 . ILE B  2  358 ? 103.848 39.223  19.853  1.00 38.77  ?  358 ILE B CG1 1 
ATOM   7952  C  CG2 . ILE B  2  358 ? 105.369 40.948  18.790  1.00 45.09  ?  358 ILE B CG2 1 
ATOM   7953  C  CD1 . ILE B  2  358 ? 104.563 37.918  19.671  1.00 39.32  ?  358 ILE B CD1 1 
ATOM   7954  N  N   . THR B  2  359 ? 103.245 43.586  18.047  1.00 52.48  ?  359 THR B N   1 
ATOM   7955  C  CA  . THR B  2  359 ? 103.419 44.701  17.120  1.00 46.37  ?  359 THR B CA  1 
ATOM   7956  C  C   . THR B  2  359 ? 104.633 44.484  16.228  1.00 56.50  ?  359 THR B C   1 
ATOM   7957  O  O   . THR B  2  359 ? 105.658 43.994  16.703  1.00 61.88  ?  359 THR B O   1 
ATOM   7958  C  CB  . THR B  2  359 ? 103.534 46.017  17.895  1.00 49.03  ?  359 THR B CB  1 
ATOM   7959  O  OG1 . THR B  2  359 ? 102.373 46.174  18.711  1.00 56.95  ?  359 THR B OG1 1 
ATOM   7960  C  CG2 . THR B  2  359 ? 103.684 47.222  16.985  1.00 51.00  ?  359 THR B CG2 1 
ATOM   7961  N  N   . ASP B  2  360 ? 104.502 44.841  14.934  1.00 50.48  ?  360 ASP B N   1 
ATOM   7962  C  CA  . ASP B  2  360 ? 105.548 44.726  13.913  1.00 58.26  ?  360 ASP B CA  1 
ATOM   7963  C  C   . ASP B  2  360 ? 105.842 43.289  13.482  1.00 55.90  ?  360 ASP B C   1 
ATOM   7964  O  O   . ASP B  2  360 ? 106.950 42.998  13.032  1.00 65.37  ?  360 ASP B O   1 
ATOM   7965  C  CB  . ASP B  2  360 ? 106.845 45.431  14.352  1.00 61.96  ?  360 ASP B CB  1 
ATOM   7966  C  CG  . ASP B  2  360 ? 106.802 46.942  14.272  1.00 69.72  ?  360 ASP B CG  1 
ATOM   7967  O  OD1 . ASP B  2  360 ? 105.730 47.492  13.919  1.00 76.17  ?  360 ASP B OD1 1 
ATOM   7968  O  OD2 . ASP B  2  360 ? 107.840 47.578  14.559  1.00 93.91  ?  360 ASP B OD2 1 
ATOM   7969  N  N   . SER B  2  361 ? 104.849 42.402  13.582  1.00 43.66  ?  361 SER B N   1 
ATOM   7970  C  CA  . SER B  2  361 ? 105.003 41.010  13.170  1.00 50.63  ?  361 SER B CA  1 
ATOM   7971  C  C   . SER B  2  361 ? 103.909 40.691  12.154  1.00 46.83  ?  361 SER B C   1 
ATOM   7972  O  O   . SER B  2  361 ? 102.829 41.269  12.242  1.00 71.02  ?  361 SER B O   1 
ATOM   7973  C  CB  . SER B  2  361 ? 104.895 40.084  14.376  1.00 44.01  ?  361 SER B CB  1 
ATOM   7974  O  OG  . SER B  2  361 ? 103.583 40.076  14.914  1.00 51.09  ?  361 SER B OG  1 
ATOM   7975  N  N   . ILE B  2  362 ? 104.167 39.793  11.188  1.00 47.80  ?  362 ILE B N   1 
ATOM   7976  C  CA  . ILE B  2  362 ? 103.146 39.448  10.192  1.00 46.88  ?  362 ILE B CA  1 
ATOM   7977  C  C   . ILE B  2  362 ? 102.043 38.685  10.923  1.00 53.52  ?  362 ILE B C   1 
ATOM   7978  O  O   . ILE B  2  362 ? 102.345 37.696  11.577  1.00 52.68  ?  362 ILE B O   1 
ATOM   7979  C  CB  . ILE B  2  362 ? 103.732 38.616  9.023   1.00 41.28  ?  362 ILE B CB  1 
ATOM   7980  C  CG1 . ILE B  2  362 ? 104.748 39.443  8.189   1.00 38.23  ?  362 ILE B CG1 1 
ATOM   7981  C  CG2 . ILE B  2  362 ? 102.612 38.103  8.134   1.00 38.91  ?  362 ILE B CG2 1 
ATOM   7982  C  CD1 . ILE B  2  362 ? 106.217 39.265  8.574   1.00 67.52  ?  362 ILE B CD1 1 
ATOM   7983  N  N   . TYR B  2  363 ? 100.783 39.146  10.851  1.00 53.36  ?  363 TYR B N   1 
ATOM   7984  C  CA  . TYR B  2  363 ? 99.693  38.470  11.552  1.00 47.67  ?  363 TYR B CA  1 
ATOM   7985  C  C   . TYR B  2  363 ? 98.809  37.661  10.620  1.00 48.46  ?  363 TYR B C   1 
ATOM   7986  O  O   . TYR B  2  363 ? 98.071  38.231  9.819   1.00 59.77  ?  363 TYR B O   1 
ATOM   7987  C  CB  . TYR B  2  363 ? 98.833  39.472  12.332  1.00 52.56  ?  363 TYR B CB  1 
ATOM   7988  C  CG  . TYR B  2  363 ? 97.741  38.802  13.137  1.00 46.33  ?  363 TYR B CG  1 
ATOM   7989  C  CD1 . TYR B  2  363 ? 98.025  38.171  14.338  1.00 52.31  ?  363 TYR B CD1 1 
ATOM   7990  C  CD2 . TYR B  2  363 ? 96.430  38.784  12.689  1.00 49.82  ?  363 TYR B CD2 1 
ATOM   7991  C  CE1 . TYR B  2  363 ? 97.032  37.538  15.073  1.00 55.88  ?  363 TYR B CE1 1 
ATOM   7992  C  CE2 . TYR B  2  363 ? 95.427  38.157  13.416  1.00 50.37  ?  363 TYR B CE2 1 
ATOM   7993  C  CZ  . TYR B  2  363 ? 95.732  37.538  14.612  1.00 46.57  ?  363 TYR B CZ  1 
ATOM   7994  O  OH  . TYR B  2  363 ? 94.749  36.917  15.345  1.00 60.27  ?  363 TYR B OH  1 
ATOM   7995  N  N   . MET B  2  364 ? 98.862  36.332  10.750  1.00 48.79  ?  364 MET B N   1 
ATOM   7996  C  CA  . MET B  2  364 ? 98.048  35.412  9.963   1.00 51.13  ?  364 MET B CA  1 
ATOM   7997  C  C   . MET B  2  364 ? 97.221  34.614  10.954  1.00 48.91  ?  364 MET B C   1 
ATOM   7998  O  O   . MET B  2  364 ? 97.714  33.638  11.513  1.00 43.97  ?  364 MET B O   1 
ATOM   7999  C  CB  . MET B  2  364 ? 98.943  34.481  9.145   1.00 39.41  ?  364 MET B CB  1 
ATOM   8000  C  CG  . MET B  2  364 ? 99.817  35.218  8.188   1.00 37.77  ?  364 MET B CG  1 
ATOM   8001  S  SD  . MET B  2  364 ? 100.662 34.129  7.032   1.00 54.05  ?  364 MET B SD  1 
ATOM   8002  C  CE  . MET B  2  364 ? 99.348  33.808  5.844   1.00 55.56  ?  364 MET B CE  1 
ATOM   8003  N  N   . GLU B  2  365 ? 95.977  35.039  11.207  1.00 49.30  ?  365 GLU B N   1 
ATOM   8004  C  CA  . GLU B  2  365 ? 95.123  34.357  12.177  1.00 49.92  ?  365 GLU B CA  1 
ATOM   8005  C  C   . GLU B  2  365 ? 94.898  32.896  11.803  1.00 52.11  ?  365 GLU B C   1 
ATOM   8006  O  O   . GLU B  2  365 ? 94.632  32.593  10.639  1.00 56.13  ?  365 GLU B O   1 
ATOM   8007  C  CB  . GLU B  2  365 ? 93.780  35.089  12.325  1.00 46.63  ?  365 GLU B CB  1 
ATOM   8008  C  CG  . GLU B  2  365 ? 92.967  34.626  13.522  1.00 54.16  ?  365 GLU B CG  1 
ATOM   8009  C  CD  . GLU B  2  365 ? 91.906  35.611  13.972  1.00 81.79  ?  365 GLU B CD  1 
ATOM   8010  O  OE1 . GLU B  2  365 ? 92.221  36.475  14.821  1.00 90.27  ?  365 GLU B OE1 1 
ATOM   8011  O  OE2 . GLU B  2  365 ? 90.758  35.518  13.479  1.00 86.04  ?  365 GLU B OE2 1 
ATOM   8012  N  N   . PHE B  2  366 ? 95.030  31.989  12.780  1.00 41.61  ?  366 PHE B N   1 
ATOM   8013  C  CA  . PHE B  2  366 ? 94.829  30.572  12.530  1.00 41.21  ?  366 PHE B CA  1 
ATOM   8014  C  C   . PHE B  2  366 ? 93.340  30.271  12.650  1.00 48.16  ?  366 PHE B C   1 
ATOM   8015  O  O   . PHE B  2  366 ? 92.825  30.189  13.763  1.00 61.61  ?  366 PHE B O   1 
ATOM   8016  C  CB  . PHE B  2  366 ? 95.641  29.720  13.520  1.00 47.29  ?  366 PHE B CB  1 
ATOM   8017  C  CG  . PHE B  2  366 ? 95.419  28.234  13.376  1.00 40.03  ?  366 PHE B CG  1 
ATOM   8018  C  CD1 . PHE B  2  366 ? 95.641  27.596  12.169  1.00 56.34  ?  366 PHE B CD1 1 
ATOM   8019  C  CD2 . PHE B  2  366 ? 95.006  27.472  14.449  1.00 42.06  ?  366 PHE B CD2 1 
ATOM   8020  C  CE1 . PHE B  2  366 ? 95.442  26.228  12.040  1.00 58.16  ?  366 PHE B CE1 1 
ATOM   8021  C  CE2 . PHE B  2  366 ? 94.812  26.104  14.316  1.00 59.09  ?  366 PHE B CE2 1 
ATOM   8022  C  CZ  . PHE B  2  366 ? 95.030  25.491  13.114  1.00 49.23  ?  366 PHE B CZ  1 
ATOM   8023  N  N   . ASP B  2  367 ? 92.641  30.130  11.511  1.00 55.35  ?  367 ASP B N   1 
ATOM   8024  C  CA  . ASP B  2  367 ? 91.204  29.856  11.505  1.00 49.85  ?  367 ASP B CA  1 
ATOM   8025  C  C   . ASP B  2  367 ? 90.916  28.474  12.074  1.00 55.10  ?  367 ASP B C   1 
ATOM   8026  O  O   . ASP B  2  367 ? 91.218  27.471  11.439  1.00 69.29  ?  367 ASP B O   1 
ATOM   8027  C  CB  . ASP B  2  367 ? 90.646  29.971  10.078  1.00 54.43  ?  367 ASP B CB  1 
ATOM   8028  C  CG  . ASP B  2  367 ? 89.165  29.688  9.970   1.00 67.18  ?  367 ASP B CG  1 
ATOM   8029  O  OD1 . ASP B  2  367 ? 88.452  29.854  10.986  1.00 82.97  ?  367 ASP B OD1 1 
ATOM   8030  O  OD2 . ASP B  2  367 ? 88.718  29.287  8.876   1.00 80.10  ?  367 ASP B OD2 1 
ATOM   8031  N  N   . GLU B  2  368 ? 90.266  28.412  13.238  1.00 65.13  ?  368 GLU B N   1 
ATOM   8032  C  CA  . GLU B  2  368 ? 90.001  27.102  13.897  1.00 51.33  ?  368 GLU B CA  1 
ATOM   8033  C  C   . GLU B  2  368 ? 88.830  26.388  13.210  1.00 68.76  ?  368 GLU B C   1 
ATOM   8034  O  O   . GLU B  2  368 ? 88.584  25.220  13.552  1.00 70.26  ?  368 GLU B O   1 
ATOM   8035  C  CB  . GLU B  2  368 ? 89.749  27.310  15.391  1.00 53.84  ?  368 GLU B CB  1 
ATOM   8036  C  CG  . GLU B  2  368 ? 88.822  28.474  15.691  1.00 115.66 ?  368 GLU B CG  1 
ATOM   8037  C  CD  . GLU B  2  368 ? 89.478  29.845  15.708  1.00 116.26 ?  368 GLU B CD  1 
ATOM   8038  O  OE1 . GLU B  2  368 ? 90.103  30.186  16.730  1.00 118.82 ?  368 GLU B OE1 1 
ATOM   8039  O  OE2 . GLU B  2  368 ? 89.356  30.568  14.700  1.00 101.85 ?  368 GLU B OE2 1 
ATOM   8040  N  N   . GLU B  2  369 ? 88.138  27.058  12.285  1.00 78.10  ?  369 GLU B N   1 
ATOM   8041  C  CA  . GLU B  2  369 ? 87.036  26.453  11.533  1.00 93.69  ?  369 GLU B CA  1 
ATOM   8042  C  C   . GLU B  2  369 ? 87.567  25.652  10.333  1.00 85.44  ?  369 GLU B C   1 
ATOM   8043  O  O   . GLU B  2  369 ? 87.034  24.588  10.021  1.00 97.63  ?  369 GLU B O   1 
ATOM   8044  C  CB  . GLU B  2  369 ? 86.058  27.538  11.060  1.00 101.47 ?  369 GLU B CB  1 
ATOM   8045  C  CG  . GLU B  2  369 ? 85.257  28.163  12.189  1.00 113.53 ?  369 GLU B CG  1 
ATOM   8046  C  CD  . GLU B  2  369 ? 84.264  29.210  11.728  1.00 132.85 ?  369 GLU B CD  1 
ATOM   8047  O  OE1 . GLU B  2  369 ? 84.520  29.856  10.685  1.00 132.99 ?  369 GLU B OE1 1 
ATOM   8048  O  OE2 . GLU B  2  369 ? 83.228  29.386  12.410  1.00 136.61 ?  369 GLU B OE2 1 
ATOM   8049  N  N   . ASN B  2  370 ? 88.609  26.157  9.663   1.00 57.45  ?  370 ASN B N   1 
ATOM   8050  C  CA  . ASN B  2  370 ? 89.249  25.480  8.534   1.00 67.71  ?  370 ASN B CA  1 
ATOM   8051  C  C   . ASN B  2  370 ? 90.718  25.376  8.941   1.00 57.35  ?  370 ASN B C   1 
ATOM   8052  O  O   . ASN B  2  370 ? 91.547  26.142  8.452   1.00 62.09  ?  370 ASN B O   1 
ATOM   8053  C  CB  . ASN B  2  370 ? 89.086  26.296  7.242   1.00 64.54  ?  370 ASN B CB  1 
ATOM   8054  C  CG  . ASN B  2  370 ? 87.647  26.523  6.847   1.00 79.24  ?  370 ASN B CG  1 
ATOM   8055  O  OD1 . ASN B  2  370 ? 86.740  25.795  7.262   1.00 96.47  ?  370 ASN B OD1 1 
ATOM   8056  N  ND2 . ASN B  2  370 ? 87.398  27.537  6.028   1.00 100.94 ?  370 ASN B ND2 1 
ATOM   8057  N  N   . PRO B  2  371 ? 91.063  24.481  9.887   1.00 48.75  ?  371 PRO B N   1 
ATOM   8058  C  CA  . PRO B  2  371 ? 92.450  24.435  10.368  1.00 53.56  ?  371 PRO B CA  1 
ATOM   8059  C  C   . PRO B  2  371 ? 93.522  24.006  9.358   1.00 57.65  ?  371 PRO B C   1 
ATOM   8060  O  O   . PRO B  2  371 ? 94.565  24.659  9.284   1.00 55.97  ?  371 PRO B O   1 
ATOM   8061  C  CB  . PRO B  2  371 ? 92.381  23.488  11.574  1.00 55.09  ?  371 PRO B CB  1 
ATOM   8062  C  CG  . PRO B  2  371 ? 90.953  23.324  11.888  1.00 48.78  ?  371 PRO B CG  1 
ATOM   8063  C  CD  . PRO B  2  371 ? 90.219  23.518  10.615  1.00 55.83  ?  371 PRO B CD  1 
ATOM   8064  N  N   . LEU B  2  372 ? 93.299  22.924  8.601   1.00 59.74  ?  372 LEU B N   1 
ATOM   8065  C  CA  . LEU B  2  372 ? 94.308  22.475  7.648   1.00 57.35  ?  372 LEU B CA  1 
ATOM   8066  C  C   . LEU B  2  372 ? 94.518  23.504  6.542   1.00 58.89  ?  372 LEU B C   1 
ATOM   8067  O  O   . LEU B  2  372 ? 95.662  23.768  6.180   1.00 62.97  ?  372 LEU B O   1 
ATOM   8068  C  CB  . LEU B  2  372 ? 93.960  21.096  7.064   1.00 49.11  ?  372 LEU B CB  1 
ATOM   8069  C  CG  . LEU B  2  372 ? 95.036  20.398  6.218   1.00 42.64  ?  372 LEU B CG  1 
ATOM   8070  C  CD1 . LEU B  2  372 ? 96.394  20.366  6.920   1.00 41.55  ?  372 LEU B CD1 1 
ATOM   8071  C  CD2 . LEU B  2  372 ? 94.609  18.990  5.874   1.00 44.40  ?  372 LEU B CD2 1 
ATOM   8072  N  N   . ASP B  2  373 ? 93.437  24.105  6.015   1.00 48.70  ?  373 ASP B N   1 
ATOM   8073  C  CA  . ASP B  2  373 ? 93.575  25.119  4.966   1.00 47.59  ?  373 ASP B CA  1 
ATOM   8074  C  C   . ASP B  2  373 ? 94.323  26.337  5.507   1.00 54.60  ?  373 ASP B C   1 
ATOM   8075  O  O   . ASP B  2  373 ? 95.155  26.907  4.805   1.00 63.18  ?  373 ASP B O   1 
ATOM   8076  C  CB  . ASP B  2  373 ? 92.203  25.546  4.426   1.00 58.45  ?  373 ASP B CB  1 
ATOM   8077  C  CG  . ASP B  2  373 ? 91.490  24.486  3.604   1.00 91.36  ?  373 ASP B CG  1 
ATOM   8078  O  OD1 . ASP B  2  373 ? 92.134  23.459  3.264   1.00 81.26  ?  373 ASP B OD1 1 
ATOM   8079  O  OD2 . ASP B  2  373 ? 90.288  24.681  3.295   1.00 89.61  ?  373 ASP B OD2 1 
ATOM   8080  N  N   . SER B  2  374 ? 94.032  26.724  6.759   1.00 55.13  ?  374 SER B N   1 
ATOM   8081  C  CA  . SER B  2  374 ? 94.686  27.855  7.415   1.00 51.25  ?  374 SER B CA  1 
ATOM   8082  C  C   . SER B  2  374 ? 96.192  27.581  7.562   1.00 56.98  ?  374 SER B C   1 
ATOM   8083  O  O   . SER B  2  374 ? 97.011  28.431  7.210   1.00 59.32  ?  374 SER B O   1 
ATOM   8084  C  CB  . SER B  2  374 ? 94.062  28.095  8.787   1.00 44.82  ?  374 SER B CB  1 
ATOM   8085  O  OG  . SER B  2  374 ? 94.486  29.323  9.352   1.00 57.97  ?  374 SER B OG  1 
ATOM   8086  N  N   . ALA B  2  375 ? 96.559  26.388  8.070   1.00 58.00  ?  375 ALA B N   1 
ATOM   8087  C  CA  . ALA B  2  375 ? 97.961  26.016  8.240   1.00 53.48  ?  375 ALA B CA  1 
ATOM   8088  C  C   . ALA B  2  375 ? 98.678  25.995  6.896   1.00 49.59  ?  375 ALA B C   1 
ATOM   8089  O  O   . ALA B  2  375 ? 99.831  26.408  6.824   1.00 46.87  ?  375 ALA B O   1 
ATOM   8090  C  CB  . ALA B  2  375 ? 98.068  24.661  8.918   1.00 42.35  ?  375 ALA B CB  1 
ATOM   8091  N  N   . LYS B  2  376 ? 98.007  25.534  5.833   1.00 44.35  ?  376 LYS B N   1 
ATOM   8092  C  CA  . LYS B  2  376 ? 98.616  25.502  4.504   1.00 48.38  ?  376 LYS B CA  1 
ATOM   8093  C  C   . LYS B  2  376 ? 98.933  26.928  4.027   1.00 57.84  ?  376 LYS B C   1 
ATOM   8094  O  O   . LYS B  2  376 ? 99.992  27.160  3.443   1.00 54.10  ?  376 LYS B O   1 
ATOM   8095  C  CB  . LYS B  2  376 ? 97.690  24.806  3.492   1.00 39.28  ?  376 LYS B CB  1 
ATOM   8096  C  CG  . LYS B  2  376 ? 97.697  23.286  3.588   1.00 39.99  ?  376 LYS B CG  1 
ATOM   8097  C  CD  . LYS B  2  376 ? 97.168  22.610  2.313   1.00 58.40  ?  376 LYS B CD  1 
ATOM   8098  C  CE  . LYS B  2  376 ? 95.743  22.101  2.402   1.00 64.16  ?  376 LYS B CE  1 
ATOM   8099  N  NZ  . LYS B  2  376 ? 95.651  20.646  2.084   1.00 74.39  ?  376 LYS B NZ  1 
ATOM   8100  N  N   . LYS B  2  377 ? 98.019  27.883  4.300   1.00 50.55  ?  377 LYS B N   1 
ATOM   8101  C  CA  . LYS B  2  377 ? 98.191  29.282  3.907   1.00 45.04  ?  377 LYS B CA  1 
ATOM   8102  C  C   . LYS B  2  377 ? 99.325  29.959  4.673   1.00 44.49  ?  377 LYS B C   1 
ATOM   8103  O  O   . LYS B  2  377 ? 99.999  30.828  4.118   1.00 53.48  ?  377 LYS B O   1 
ATOM   8104  C  CB  . LYS B  2  377 ? 96.884  30.066  4.102   1.00 43.52  ?  377 LYS B CB  1 
ATOM   8105  C  CG  . LYS B  2  377 ? 95.775  29.643  3.148   1.00 59.40  ?  377 LYS B CG  1 
ATOM   8106  C  CD  . LYS B  2  377 ? 94.631  30.659  3.118   1.00 76.20  ?  377 LYS B CD  1 
ATOM   8107  C  CE  . LYS B  2  377 ? 93.336  30.111  2.538   1.00 88.10  ?  377 LYS B CE  1 
ATOM   8108  N  NZ  . LYS B  2  377 ? 92.190  30.241  3.488   1.00 79.84  ?  377 LYS B NZ  1 
ATOM   8109  N  N   . ILE B  2  378 ? 99.536  29.580  5.941   1.00 52.03  ?  378 ILE B N   1 
ATOM   8110  C  CA  . ILE B  2  378 ? 100.611 30.169  6.737   1.00 50.27  ?  378 ILE B CA  1 
ATOM   8111  C  C   . ILE B  2  378 ? 101.930 29.581  6.265   1.00 52.59  ?  378 ILE B C   1 
ATOM   8112  O  O   . ILE B  2  378 ? 102.860 30.327  5.956   1.00 61.66  ?  378 ILE B O   1 
ATOM   8113  C  CB  . ILE B  2  378 ? 100.400 29.944  8.258   1.00 34.91  ?  378 ILE B CB  1 
ATOM   8114  C  CG1 . ILE B  2  378 ? 99.186  30.747  8.757   1.00 41.29  ?  378 ILE B CG1 1 
ATOM   8115  C  CG2 . ILE B  2  378 ? 101.660 30.348  9.028   1.00 36.57  ?  378 ILE B CG2 1 
ATOM   8116  C  CD1 . ILE B  2  378 ? 98.610  30.285  10.030  1.00 56.93  ?  378 ILE B CD1 1 
ATOM   8117  N  N   . LEU B  2  379 ? 102.006 28.242  6.191   1.00 50.77  ?  379 LEU B N   1 
ATOM   8118  C  CA  . LEU B  2  379 ? 103.210 27.541  5.762   1.00 44.35  ?  379 LEU B CA  1 
ATOM   8119  C  C   . LEU B  2  379 ? 103.653 27.988  4.374   1.00 52.01  ?  379 LEU B C   1 
ATOM   8120  O  O   . LEU B  2  379 ? 104.856 28.086  4.129   1.00 53.53  ?  379 LEU B O   1 
ATOM   8121  C  CB  . LEU B  2  379 ? 102.974 26.022  5.802   1.00 45.03  ?  379 LEU B CB  1 
ATOM   8122  C  CG  . LEU B  2  379 ? 104.125 25.111  5.377   1.00 37.13  ?  379 LEU B CG  1 
ATOM   8123  C  CD1 . LEU B  2  379 ? 105.369 25.365  6.193   1.00 42.88  ?  379 LEU B CD1 1 
ATOM   8124  C  CD2 . LEU B  2  379 ? 103.739 23.665  5.532   1.00 33.47  ?  379 LEU B CD2 1 
ATOM   8125  N  N   . LYS B  2  380 ? 102.707 28.297  3.471   1.00 49.04  ?  380 LYS B N   1 
ATOM   8126  C  CA  . LYS B  2  380 ? 103.062 28.751  2.124   1.00 46.16  ?  380 LYS B CA  1 
ATOM   8127  C  C   . LYS B  2  380 ? 103.906 30.024  2.187   1.00 42.86  ?  380 LYS B C   1 
ATOM   8128  O  O   . LYS B  2  380 ? 104.873 30.151  1.443   1.00 50.79  ?  380 LYS B O   1 
ATOM   8129  C  CB  . LYS B  2  380 ? 101.801 28.997  1.285   1.00 37.38  ?  380 LYS B CB  1 
ATOM   8130  C  CG  . LYS B  2  380 ? 102.093 29.509  -0.121  1.00 40.60  ?  380 LYS B CG  1 
ATOM   8131  C  CD  . LYS B  2  380 ? 100.868 29.441  -1.018  1.00 57.71  ?  380 LYS B CD  1 
ATOM   8132  C  CE  . LYS B  2  380 ? 101.116 29.989  -2.404  1.00 62.45  ?  380 LYS B CE  1 
ATOM   8133  N  NZ  . LYS B  2  380 ? 100.309 29.277  -3.432  1.00 75.60  ?  380 LYS B NZ  1 
ATOM   8134  N  N   . GLU B  2  381 ? 103.555 30.953  3.078   1.00 45.36  ?  381 GLU B N   1 
ATOM   8135  C  CA  . GLU B  2  381 ? 104.304 32.200  3.208   1.00 57.29  ?  381 GLU B CA  1 
ATOM   8136  C  C   . GLU B  2  381 ? 105.731 31.951  3.675   1.00 56.23  ?  381 GLU B C   1 
ATOM   8137  O  O   . GLU B  2  381 ? 106.650 32.646  3.231   1.00 62.22  ?  381 GLU B O   1 
ATOM   8138  C  CB  . GLU B  2  381 ? 103.582 33.172  4.156   1.00 49.17  ?  381 GLU B CB  1 
ATOM   8139  C  CG  . GLU B  2  381 ? 102.330 33.776  3.547   1.00 61.88  ?  381 GLU B CG  1 
ATOM   8140  C  CD  . GLU B  2  381 ? 102.568 34.427  2.199   1.00 78.96  ?  381 GLU B CD  1 
ATOM   8141  O  OE1 . GLU B  2  381 ? 103.294 35.448  2.155   1.00 84.65  ?  381 GLU B OE1 1 
ATOM   8142  O  OE2 . GLU B  2  381 ? 102.047 33.906  1.185   1.00 69.74  ?  381 GLU B OE2 1 
ATOM   8143  N  N   . ALA B  2  382 ? 105.924 30.956  4.563   1.00 45.99  ?  382 ALA B N   1 
ATOM   8144  C  CA  . ALA B  2  382 ? 107.253 30.608  5.061   1.00 49.67  ?  382 ALA B CA  1 
ATOM   8145  C  C   . ALA B  2  382 ? 108.074 29.997  3.933   1.00 43.95  ?  382 ALA B C   1 
ATOM   8146  O  O   . ALA B  2  382 ? 109.250 30.316  3.803   1.00 52.99  ?  382 ALA B O   1 
ATOM   8147  C  CB  . ALA B  2  382 ? 107.139 29.629  6.220   1.00 46.58  ?  382 ALA B CB  1 
ATOM   8148  N  N   . ILE B  2  383 ? 107.451 29.139  3.109   1.00 45.88  ?  383 ILE B N   1 
ATOM   8149  C  CA  . ILE B  2  383 ? 108.118 28.500  1.971   1.00 44.44  ?  383 ILE B CA  1 
ATOM   8150  C  C   . ILE B  2  383 ? 108.561 29.554  0.958   1.00 45.72  ?  383 ILE B C   1 
ATOM   8151  O  O   . ILE B  2  383 ? 109.700 29.523  0.491   1.00 49.89  ?  383 ILE B O   1 
ATOM   8152  C  CB  . ILE B  2  383 ? 107.200 27.438  1.295   1.00 39.37  ?  383 ILE B CB  1 
ATOM   8153  C  CG1 . ILE B  2  383 ? 107.021 26.203  2.206   1.00 41.90  ?  383 ILE B CG1 1 
ATOM   8154  C  CG2 . ILE B  2  383 ? 107.765 27.022  -0.077  1.00 38.96  ?  383 ILE B CG2 1 
ATOM   8155  C  CD1 . ILE B  2  383 ? 105.757 25.413  1.962   1.00 47.63  ?  383 ILE B CD1 1 
ATOM   8156  N  N   . LEU B  2  384 ? 107.662 30.473  0.604   1.00 46.77  ?  384 LEU B N   1 
ATOM   8157  C  CA  . LEU B  2  384 ? 107.985 31.507  -0.372  1.00 47.25  ?  384 LEU B CA  1 
ATOM   8158  C  C   . LEU B  2  384 ? 109.110 32.414  0.127   1.00 49.93  ?  384 LEU B C   1 
ATOM   8159  O  O   . LEU B  2  384 ? 109.875 32.924  -0.687  1.00 54.54  ?  384 LEU B O   1 
ATOM   8160  C  CB  . LEU B  2  384 ? 106.736 32.328  -0.725  1.00 42.11  ?  384 LEU B CB  1 
ATOM   8161  C  CG  . LEU B  2  384 ? 105.589 31.552  -1.386  1.00 39.80  ?  384 LEU B CG  1 
ATOM   8162  C  CD1 . LEU B  2  384 ? 104.295 32.351  -1.339  1.00 56.44  ?  384 LEU B CD1 1 
ATOM   8163  C  CD2 . LEU B  2  384 ? 105.932 31.150  -2.805  1.00 41.64  ?  384 LEU B CD2 1 
ATOM   8164  N  N   . ASN B  2  385 ? 109.231 32.603  1.450   1.00 48.00  ?  385 ASN B N   1 
ATOM   8165  C  CA  . ASN B  2  385 ? 110.281 33.449  2.003   1.00 38.97  ?  385 ASN B CA  1 
ATOM   8166  C  C   . ASN B  2  385 ? 111.673 32.877  1.781   1.00 47.67  ?  385 ASN B C   1 
ATOM   8167  O  O   . ASN B  2  385 ? 112.639 33.618  1.908   1.00 63.41  ?  385 ASN B O   1 
ATOM   8168  C  CB  . ASN B  2  385 ? 110.063 33.692  3.489   1.00 37.15  ?  385 ASN B CB  1 
ATOM   8169  C  CG  . ASN B  2  385 ? 110.779 34.923  3.998   1.00 48.90  ?  385 ASN B CG  1 
ATOM   8170  O  OD1 . ASN B  2  385 ? 110.647 36.024  3.448   1.00 61.21  ?  385 ASN B OD1 1 
ATOM   8171  N  ND2 . ASN B  2  385 ? 111.563 34.774  5.054   1.00 57.94  ?  385 ASN B ND2 1 
ATOM   8172  N  N   . PHE B  2  386 ? 111.802 31.582  1.446   1.00 47.73  ?  386 PHE B N   1 
ATOM   8173  C  CA  . PHE B  2  386 ? 113.112 30.977  1.184   1.00 48.67  ?  386 PHE B CA  1 
ATOM   8174  C  C   . PHE B  2  386 ? 113.851 31.747  0.087   1.00 49.33  ?  386 PHE B C   1 
ATOM   8175  O  O   . PHE B  2  386 ? 115.074 31.876  0.142   1.00 53.93  ?  386 PHE B O   1 
ATOM   8176  C  CB  . PHE B  2  386 ? 112.939 29.523  0.740   1.00 47.13  ?  386 PHE B CB  1 
ATOM   8177  C  CG  . PHE B  2  386 ? 114.230 28.792  0.455   1.00 44.98  ?  386 PHE B CG  1 
ATOM   8178  C  CD1 . PHE B  2  386 ? 114.964 28.223  1.481   1.00 52.86  ?  386 PHE B CD1 1 
ATOM   8179  C  CD2 . PHE B  2  386 ? 114.676 28.622  -0.843  1.00 40.93  ?  386 PHE B CD2 1 
ATOM   8180  C  CE1 . PHE B  2  386 ? 116.135 27.524  1.216   1.00 43.72  ?  386 PHE B CE1 1 
ATOM   8181  C  CE2 . PHE B  2  386 ? 115.846 27.922  -1.104  1.00 41.99  ?  386 PHE B CE2 1 
ATOM   8182  C  CZ  . PHE B  2  386 ? 116.568 27.379  -0.074  1.00 40.95  ?  386 PHE B CZ  1 
ATOM   8183  N  N   . LYS B  2  387 ? 113.093 32.271  -0.898  1.00 44.79  ?  387 LYS B N   1 
ATOM   8184  C  CA  . LYS B  2  387 ? 113.633 33.053  -2.013  1.00 48.29  ?  387 LYS B CA  1 
ATOM   8185  C  C   . LYS B  2  387 ? 114.357 34.314  -1.533  1.00 51.09  ?  387 LYS B C   1 
ATOM   8186  O  O   . LYS B  2  387 ? 115.207 34.831  -2.256  1.00 71.28  ?  387 LYS B O   1 
ATOM   8187  C  CB  . LYS B  2  387 ? 112.508 33.446  -2.984  1.00 44.69  ?  387 LYS B CB  1 
ATOM   8188  C  CG  . LYS B  2  387 ? 111.856 32.258  -3.680  1.00 46.99  ?  387 LYS B CG  1 
ATOM   8189  C  CD  . LYS B  2  387 ? 110.979 32.682  -4.857  1.00 56.74  ?  387 LYS B CD  1 
ATOM   8190  C  CE  . LYS B  2  387 ? 111.656 32.562  -6.211  1.00 73.04  ?  387 LYS B CE  1 
ATOM   8191  N  NZ  . LYS B  2  387 ? 110.971 31.572  -7.093  1.00 92.53  ?  387 LYS B NZ  1 
ATOM   8192  N  N   . ASN B  2  388 ? 114.031 34.809  -0.326  1.00 47.71  ?  388 ASN B N   1 
ATOM   8193  C  CA  . ASN B  2  388 ? 114.658 36.005  0.227   1.00 56.05  ?  388 ASN B CA  1 
ATOM   8194  C  C   . ASN B  2  388 ? 115.823 35.696  1.171   1.00 51.51  ?  388 ASN B C   1 
ATOM   8195  O  O   . ASN B  2  388 ? 116.249 36.591  1.899   1.00 54.37  ?  388 ASN B O   1 
ATOM   8196  C  CB  . ASN B  2  388 ? 113.622 36.843  0.961   1.00 55.12  ?  388 ASN B CB  1 
ATOM   8197  C  CG  . ASN B  2  388 ? 112.438 37.200  0.109   1.00 55.34  ?  388 ASN B CG  1 
ATOM   8198  O  OD1 . ASN B  2  388 ? 112.585 37.640  -1.038  1.00 57.41  ?  388 ASN B OD1 1 
ATOM   8199  N  ND2 . ASN B  2  388 ? 111.237 37.023  0.650   1.00 68.41  ?  388 ASN B ND2 1 
ATOM   8200  N  N   . ARG B  2  389 ? 116.353 34.463  1.163   1.00 60.28  ?  389 ARG B N   1 
ATOM   8201  C  CA  . ARG B  2  389 ? 117.475 34.132  2.033   1.00 49.48  ?  389 ARG B CA  1 
ATOM   8202  C  C   . ARG B  2  389 ? 118.775 34.690  1.460   1.00 51.97  ?  389 ARG B C   1 
ATOM   8203  O  O   . ARG B  2  389 ? 118.928 34.770  0.244   1.00 67.97  ?  389 ARG B O   1 
ATOM   8204  C  CB  . ARG B  2  389 ? 117.603 32.612  2.220   1.00 41.78  ?  389 ARG B CB  1 
ATOM   8205  C  CG  . ARG B  2  389 ? 118.371 32.249  3.487   1.00 67.49  ?  389 ARG B CG  1 
ATOM   8206  C  CD  . ARG B  2  389 ? 118.600 30.768  3.644   1.00 55.05  ?  389 ARG B CD  1 
ATOM   8207  N  NE  . ARG B  2  389 ? 117.493 30.078  4.309   1.00 48.49  ?  389 ARG B NE  1 
ATOM   8208  C  CZ  . ARG B  2  389 ? 117.467 28.769  4.523   1.00 60.95  ?  389 ARG B CZ  1 
ATOM   8209  N  NH1 . ARG B  2  389 ? 118.480 28.004  4.130   1.00 60.48  ?  389 ARG B NH1 1 
ATOM   8210  N  NH2 . ARG B  2  389 ? 116.429 28.209  5.125   1.00 53.03  ?  389 ARG B NH2 1 
ATOM   8211  N  N   . ASP B  2  390 ? 119.699 35.090  2.335   1.00 53.71  ?  390 ASP B N   1 
ATOM   8212  C  CA  . ASP B  2  390 ? 121.011 35.605  1.945   1.00 64.51  ?  390 ASP B CA  1 
ATOM   8213  C  C   . ASP B  2  390 ? 121.980 34.527  2.411   1.00 75.87  ?  390 ASP B C   1 
ATOM   8214  O  O   . ASP B  2  390 ? 122.488 34.587  3.529   1.00 85.17  ?  390 ASP B O   1 
ATOM   8215  C  CB  . ASP B  2  390 ? 121.292 36.955  2.628   1.00 68.81  ?  390 ASP B CB  1 
ATOM   8216  C  CG  . ASP B  2  390 ? 122.604 37.600  2.225   1.00 79.94  ?  390 ASP B CG  1 
ATOM   8217  O  OD1 . ASP B  2  390 ? 123.496 36.876  1.732   1.00 96.30  ?  390 ASP B OD1 1 
ATOM   8218  O  OD2 . ASP B  2  390 ? 122.740 38.832  2.406   1.00 98.74  ?  390 ASP B OD2 1 
ATOM   8219  N  N   . GLN B  2  391 ? 122.205 33.518  1.571   1.00 69.69  ?  391 GLN B N   1 
ATOM   8220  C  CA  . GLN B  2  391 ? 123.060 32.388  1.931   1.00 60.82  ?  391 GLN B CA  1 
ATOM   8221  C  C   . GLN B  2  391 ? 124.471 32.780  2.388   1.00 71.19  ?  391 GLN B C   1 
ATOM   8222  O  O   . GLN B  2  391 ? 125.132 31.976  3.043   1.00 77.10  ?  391 GLN B O   1 
ATOM   8223  C  CB  . GLN B  2  391 ? 123.114 31.364  0.787   1.00 70.44  ?  391 GLN B CB  1 
ATOM   8224  C  CG  . GLN B  2  391 ? 121.758 30.725  0.452   1.00 60.95  ?  391 GLN B CG  1 
ATOM   8225  C  CD  . GLN B  2  391 ? 121.267 29.748  1.497   1.00 60.59  ?  391 GLN B CD  1 
ATOM   8226  O  OE1 . GLN B  2  391 ? 121.714 29.742  2.645   1.00 71.65  ?  391 GLN B OE1 1 
ATOM   8227  N  NE2 . GLN B  2  391 ? 120.323 28.894  1.124   1.00 67.61  ?  391 GLN B NE2 1 
ATOM   8228  N  N   . SER B  2  392 ? 124.934 33.999  2.070   1.00 80.82  ?  392 SER B N   1 
ATOM   8229  C  CA  . SER B  2  392 ? 126.270 34.442  2.485   1.00 87.95  ?  392 SER B CA  1 
ATOM   8230  C  C   . SER B  2  392 ? 126.324 34.760  3.986   1.00 84.56  ?  392 SER B C   1 
ATOM   8231  O  O   . SER B  2  392 ? 127.380 34.609  4.599   1.00 96.74  ?  392 SER B O   1 
ATOM   8232  C  CB  . SER B  2  392 ? 126.708 35.661  1.677   1.00 85.14  ?  392 SER B CB  1 
ATOM   8233  O  OG  . SER B  2  392 ? 126.105 36.857  2.148   1.00 94.69  ?  392 SER B OG  1 
ATOM   8234  N  N   . LYS B  2  393 ? 125.198 35.203  4.574   1.00 74.88  ?  393 LYS B N   1 
ATOM   8235  C  CA  . LYS B  2  393 ? 125.148 35.538  5.999   1.00 76.00  ?  393 LYS B CA  1 
ATOM   8236  C  C   . LYS B  2  393 ? 124.568 34.378  6.871   1.00 72.84  ?  393 LYS B C   1 
ATOM   8237  O  O   . LYS B  2  393 ? 124.311 34.580  8.058   1.00 71.39  ?  393 LYS B O   1 
ATOM   8238  C  CB  . LYS B  2  393 ? 124.402 36.888  6.196   1.00 82.45  ?  393 LYS B CB  1 
ATOM   8239  C  CG  . LYS B  2  393 ? 125.090 38.147  5.647   1.00 119.98 ?  393 LYS B CG  1 
ATOM   8240  C  CD  . LYS B  2  393 ? 124.265 39.424  5.869   1.00 138.31 ?  393 LYS B CD  1 
ATOM   8241  C  CE  . LYS B  2  393 ? 124.942 40.675  5.354   1.00 102.66 ?  393 LYS B CE  1 
ATOM   8242  N  NZ  . LYS B  2  393 ? 124.102 41.885  5.565   1.00 114.42 ?  393 LYS B NZ  1 
ATOM   8243  N  N   . VAL B  2  394 ? 124.399 33.171  6.302   1.00 70.48  ?  394 VAL B N   1 
ATOM   8244  C  CA  . VAL B  2  394 ? 123.862 32.035  7.057   1.00 55.21  ?  394 VAL B CA  1 
ATOM   8245  C  C   . VAL B  2  394 ? 124.981 31.343  7.813   1.00 61.51  ?  394 VAL B C   1 
ATOM   8246  O  O   . VAL B  2  394 ? 126.093 31.217  7.293   1.00 63.25  ?  394 VAL B O   1 
ATOM   8247  C  CB  . VAL B  2  394 ? 123.130 31.022  6.143   1.00 48.75  ?  394 VAL B CB  1 
ATOM   8248  C  CG1 . VAL B  2  394 ? 122.718 29.772  6.917   1.00 44.42  ?  394 VAL B CG1 1 
ATOM   8249  C  CG2 . VAL B  2  394 ? 121.920 31.660  5.478   1.00 71.47  ?  394 VAL B CG2 1 
ATOM   8250  N  N   . MET B  2  395 ? 124.677 30.872  9.031   1.00 54.36  ?  395 MET B N   1 
ATOM   8251  C  CA  . MET B  2  395 ? 125.634 30.165  9.870   1.00 53.27  ?  395 MET B CA  1 
ATOM   8252  C  C   . MET B  2  395 ? 124.892 29.272  10.856  1.00 47.42  ?  395 MET B C   1 
ATOM   8253  O  O   . MET B  2  395 ? 124.423 29.749  11.884  1.00 54.53  ?  395 MET B O   1 
ATOM   8254  C  CB  . MET B  2  395 ? 126.523 31.161  10.627  1.00 51.89  ?  395 MET B CB  1 
ATOM   8255  C  CG  . MET B  2  395 ? 127.756 30.529  11.242  1.00 60.86  ?  395 MET B CG  1 
ATOM   8256  S  SD  . MET B  2  395 ? 127.454 29.750  12.851  1.00 74.98  ?  395 MET B SD  1 
ATOM   8257  C  CE  . MET B  2  395 ? 128.231 30.936  13.936  1.00 84.40  ?  395 MET B CE  1 
ATOM   8258  N  N   . ILE B  2  396 ? 124.779 27.981  10.544  1.00 52.82  ?  396 ILE B N   1 
ATOM   8259  C  CA  . ILE B  2  396 ? 124.106 27.025  11.424  1.00 44.18  ?  396 ILE B CA  1 
ATOM   8260  C  C   . ILE B  2  396 ? 125.188 26.209  12.142  1.00 46.40  ?  396 ILE B C   1 
ATOM   8261  O  O   . ILE B  2  396 ? 125.904 25.466  11.474  1.00 51.63  ?  396 ILE B O   1 
ATOM   8262  C  CB  . ILE B  2  396 ? 123.164 26.092  10.621  1.00 42.27  ?  396 ILE B CB  1 
ATOM   8263  C  CG1 . ILE B  2  396 ? 122.067 26.892  9.886   1.00 48.41  ?  396 ILE B CG1 1 
ATOM   8264  C  CG2 . ILE B  2  396 ? 122.538 25.058  11.552  1.00 49.77  ?  396 ILE B CG2 1 
ATOM   8265  C  CD1 . ILE B  2  396 ? 121.446 26.166  8.704   1.00 39.74  ?  396 ILE B CD1 1 
ATOM   8266  N  N   . PRO B  2  397 ? 125.341 26.298  13.481  1.00 47.52  ?  397 PRO B N   1 
ATOM   8267  C  CA  . PRO B  2  397 ? 126.377 25.490  14.145  1.00 49.00  ?  397 PRO B CA  1 
ATOM   8268  C  C   . PRO B  2  397 ? 126.241 24.012  13.805  1.00 48.74  ?  397 PRO B C   1 
ATOM   8269  O  O   . PRO B  2  397 ? 125.129 23.493  13.824  1.00 59.89  ?  397 PRO B O   1 
ATOM   8270  C  CB  . PRO B  2  397 ? 126.120 25.738  15.633  1.00 48.38  ?  397 PRO B CB  1 
ATOM   8271  C  CG  . PRO B  2  397 ? 125.417 27.027  15.694  1.00 46.78  ?  397 PRO B CG  1 
ATOM   8272  C  CD  . PRO B  2  397 ? 124.589 27.112  14.454  1.00 54.82  ?  397 PRO B CD  1 
ATOM   8273  N  N   . GLU B  2  398 ? 127.348 23.344  13.475  1.00 51.79  ?  398 GLU B N   1 
ATOM   8274  C  CA  . GLU B  2  398 ? 127.321 21.928  13.127  1.00 52.10  ?  398 GLU B CA  1 
ATOM   8275  C  C   . GLU B  2  398 ? 127.249 21.127  14.429  1.00 60.60  ?  398 GLU B C   1 
ATOM   8276  O  O   . GLU B  2  398 ? 128.168 20.377  14.756  1.00 76.07  ?  398 GLU B O   1 
ATOM   8277  C  CB  . GLU B  2  398 ? 128.580 21.583  12.318  1.00 59.66  ?  398 GLU B CB  1 
ATOM   8278  C  CG  . GLU B  2  398 ? 128.472 20.321  11.481  1.00 73.68  ?  398 GLU B CG  1 
ATOM   8279  C  CD  . GLU B  2  398 ? 129.575 20.159  10.449  1.00 116.60 ?  398 GLU B CD  1 
ATOM   8280  O  OE1 . GLU B  2  398 ? 130.548 20.949  10.477  1.00 115.82 ?  398 GLU B OE1 1 
ATOM   8281  O  OE2 . GLU B  2  398 ? 129.464 19.237  9.607   1.00 148.26 ?  398 GLU B OE2 1 
ATOM   8282  N  N   . LEU B  2  399 ? 126.157 21.303  15.185  1.00 59.75  ?  399 LEU B N   1 
ATOM   8283  C  CA  . LEU B  2  399 ? 125.976 20.647  16.471  1.00 49.08  ?  399 LEU B CA  1 
ATOM   8284  C  C   . LEU B  2  399 ? 124.517 20.282  16.741  1.00 58.00  ?  399 LEU B C   1 
ATOM   8285  O  O   . LEU B  2  399 ? 123.705 21.145  17.068  1.00 50.79  ?  399 LEU B O   1 
ATOM   8286  C  CB  . LEU B  2  399 ? 126.469 21.592  17.575  1.00 50.22  ?  399 LEU B CB  1 
ATOM   8287  C  CG  . LEU B  2  399 ? 127.973 21.904  17.584  1.00 54.15  ?  399 LEU B CG  1 
ATOM   8288  C  CD1 . LEU B  2  399 ? 128.241 23.262  18.178  1.00 54.75  ?  399 LEU B CD1 1 
ATOM   8289  C  CD2 . LEU B  2  399 ? 128.745 20.852  18.339  1.00 56.96  ?  399 LEU B CD2 1 
ATOM   8290  N  N   . LYS B  2  400 ? 124.199 18.991  16.629  1.00 58.10  ?  400 LYS B N   1 
ATOM   8291  C  CA  . LYS B  2  400 ? 122.868 18.440  16.887  1.00 43.24  ?  400 LYS B CA  1 
ATOM   8292  C  C   . LYS B  2  400 ? 123.062 17.211  17.777  1.00 44.74  ?  400 LYS B C   1 
ATOM   8293  O  O   . LYS B  2  400 ? 124.187 16.731  17.911  1.00 58.32  ?  400 LYS B O   1 
ATOM   8294  C  CB  . LYS B  2  400 ? 122.149 18.071  15.577  1.00 41.81  ?  400 LYS B CB  1 
ATOM   8295  C  CG  . LYS B  2  400 ? 122.924 17.090  14.701  1.00 58.71  ?  400 LYS B CG  1 
ATOM   8296  C  CD  . LYS B  2  400 ? 122.062 16.431  13.636  1.00 42.81  ?  400 LYS B CD  1 
ATOM   8297  C  CE  . LYS B  2  400 ? 121.714 17.361  12.506  1.00 62.92  ?  400 LYS B CE  1 
ATOM   8298  N  NZ  . LYS B  2  400 ? 121.051 16.643  11.387  1.00 98.12  ?  400 LYS B NZ  1 
ATOM   8299  N  N   . CYS B  2  401 ? 121.992 16.699  18.385  1.00 51.67  ?  401 CYS B N   1 
ATOM   8300  C  CA  . CYS B  2  401 ? 122.116 15.543  19.266  1.00 49.74  ?  401 CYS B CA  1 
ATOM   8301  C  C   . CYS B  2  401 ? 120.941 14.589  19.120  1.00 56.51  ?  401 CYS B C   1 
ATOM   8302  O  O   . CYS B  2  401 ? 119.816 15.042  18.966  1.00 47.91  ?  401 CYS B O   1 
ATOM   8303  C  CB  . CYS B  2  401 ? 122.261 16.020  20.706  1.00 45.66  ?  401 CYS B CB  1 
ATOM   8304  S  SG  . CYS B  2  401 ? 122.843 14.750  21.852  1.00 58.45  ?  401 CYS B SG  1 
ATOM   8305  N  N   . LYS B  2  402 ? 121.186 13.269  19.184  1.00 49.95  ?  402 LYS B N   1 
ATOM   8306  C  CA  . LYS B  2  402 ? 120.097 12.298  19.083  1.00 39.77  ?  402 LYS B CA  1 
ATOM   8307  C  C   . LYS B  2  402 ? 119.371 12.209  20.422  1.00 51.57  ?  402 LYS B C   1 
ATOM   8308  O  O   . LYS B  2  402 ? 119.999 12.328  21.479  1.00 59.11  ?  402 LYS B O   1 
ATOM   8309  C  CB  . LYS B  2  402 ? 120.620 10.915  18.691  1.00 37.73  ?  402 LYS B CB  1 
ATOM   8310  C  CG  . LYS B  2  402 ? 121.115 10.848  17.258  1.00 55.69  ?  402 LYS B CG  1 
ATOM   8311  C  CD  . LYS B  2  402 ? 121.107 9.424   16.730  1.00 62.47  ?  402 LYS B CD  1 
ATOM   8312  C  CE  . LYS B  2  402 ? 121.868 9.283   15.439  1.00 70.07  ?  402 LYS B CE  1 
ATOM   8313  N  NZ  . LYS B  2  402 ? 121.922 7.868   14.994  1.00 94.76  ?  402 LYS B NZ  1 
ATOM   8314  N  N   . ALA B  2  403 ? 118.052 12.002  20.388  1.00 47.58  ?  403 ALA B N   1 
ATOM   8315  C  CA  . ALA B  2  403 ? 117.278 11.901  21.614  1.00 36.23  ?  403 ALA B CA  1 
ATOM   8316  C  C   . ALA B  2  403 ? 116.062 11.012  21.431  1.00 46.22  ?  403 ALA B C   1 
ATOM   8317  O  O   . ALA B  2  403 ? 115.525 10.910  20.329  1.00 51.64  ?  403 ALA B O   1 
ATOM   8318  C  CB  . ALA B  2  403 ? 116.845 13.283  22.062  1.00 36.80  ?  403 ALA B CB  1 
ATOM   8319  N  N   . ILE B  2  404 ? 115.634 10.363  22.521  1.00 44.06  ?  404 ILE B N   1 
ATOM   8320  C  CA  . ILE B  2  404 ? 114.458 9.497   22.541  1.00 49.01  ?  404 ILE B CA  1 
ATOM   8321  C  C   . ILE B  2  404 ? 113.455 10.144  23.476  1.00 42.16  ?  404 ILE B C   1 
ATOM   8322  O  O   . ILE B  2  404 ? 113.818 10.556  24.576  1.00 47.61  ?  404 ILE B O   1 
ATOM   8323  C  CB  . ILE B  2  404 ? 114.784 8.054   23.013  1.00 51.77  ?  404 ILE B CB  1 
ATOM   8324  C  CG1 . ILE B  2  404 ? 115.982 7.480   22.229  1.00 52.30  ?  404 ILE B CG1 1 
ATOM   8325  C  CG2 . ILE B  2  404 ? 113.538 7.158   22.868  1.00 50.76  ?  404 ILE B CG2 1 
ATOM   8326  C  CD1 . ILE B  2  404 ? 116.380 6.057   22.606  1.00 70.64  ?  404 ILE B CD1 1 
ATOM   8327  N  N   . LEU B  2  405 ? 112.197 10.217  23.056  1.00 45.86  ?  405 LEU B N   1 
ATOM   8328  C  CA  . LEU B  2  405 ? 111.140 10.813  23.868  1.00 49.84  ?  405 LEU B CA  1 
ATOM   8329  C  C   . LEU B  2  405 ? 109.819 10.070  23.602  1.00 46.41  ?  405 LEU B C   1 
ATOM   8330  O  O   . LEU B  2  405 ? 109.843 8.995   23.007  1.00 50.43  ?  405 LEU B O   1 
ATOM   8331  C  CB  . LEU B  2  405 ? 111.042 12.334  23.609  1.00 42.22  ?  405 LEU B CB  1 
ATOM   8332  C  CG  . LEU B  2  405 ? 110.541 12.795  22.248  1.00 49.66  ?  405 LEU B CG  1 
ATOM   8333  C  CD1 . LEU B  2  405 ? 110.181 14.261  22.293  1.00 51.68  ?  405 LEU B CD1 1 
ATOM   8334  C  CD2 . LEU B  2  405 ? 111.567 12.544  21.160  1.00 46.35  ?  405 LEU B CD2 1 
ATOM   8335  N  N   . GLY B  2  406 ? 108.697 10.605  24.061  1.00 46.53  ?  406 GLY B N   1 
ATOM   8336  C  CA  . GLY B  2  406 ? 107.404 9.963   23.870  1.00 47.07  ?  406 GLY B CA  1 
ATOM   8337  C  C   . GLY B  2  406 ? 107.026 9.067   25.032  1.00 44.10  ?  406 GLY B C   1 
ATOM   8338  O  O   . GLY B  2  406 ? 106.169 8.197   24.886  1.00 52.49  ?  406 GLY B O   1 
ATOM   8339  N  N   . TYR B  2  407 ? 107.647 9.276   26.200  1.00 43.18  ?  407 TYR B N   1 
ATOM   8340  C  CA  . TYR B  2  407 ? 107.364 8.463   27.366  1.00 27.67  ?  407 TYR B CA  1 
ATOM   8341  C  C   . TYR B  2  407 ? 106.147 8.943   28.125  1.00 37.69  ?  407 TYR B C   1 
ATOM   8342  O  O   . TYR B  2  407 ? 106.264 9.553   29.182  1.00 42.46  ?  407 TYR B O   1 
ATOM   8343  C  CB  . TYR B  2  407 ? 108.592 8.390   28.278  1.00 34.89  ?  407 TYR B CB  1 
ATOM   8344  C  CG  . TYR B  2  407 ? 109.704 7.582   27.652  1.00 46.05  ?  407 TYR B CG  1 
ATOM   8345  C  CD1 . TYR B  2  407 ? 109.636 6.197   27.598  1.00 50.08  ?  407 TYR B CD1 1 
ATOM   8346  C  CD2 . TYR B  2  407 ? 110.787 8.204   27.046  1.00 52.93  ?  407 TYR B CD2 1 
ATOM   8347  C  CE1 . TYR B  2  407 ? 110.636 5.449   26.994  1.00 49.40  ?  407 TYR B CE1 1 
ATOM   8348  C  CE2 . TYR B  2  407 ? 111.796 7.465   26.439  1.00 53.96  ?  407 TYR B CE2 1 
ATOM   8349  C  CZ  . TYR B  2  407 ? 111.712 6.087   26.409  1.00 50.73  ?  407 TYR B CZ  1 
ATOM   8350  O  OH  . TYR B  2  407 ? 112.684 5.337   25.797  1.00 60.96  ?  407 TYR B OH  1 
ATOM   8351  N  N   . SER B  2  408 ? 104.967 8.647   27.589  1.00 42.93  ?  408 SER B N   1 
ATOM   8352  C  CA  . SER B  2  408 ? 103.718 8.971   28.259  1.00 46.21  ?  408 SER B CA  1 
ATOM   8353  C  C   . SER B  2  408 ? 103.539 7.898   29.345  1.00 49.32  ?  408 SER B C   1 
ATOM   8354  O  O   . SER B  2  408 ? 104.287 6.917   29.360  1.00 47.86  ?  408 SER B O   1 
ATOM   8355  C  CB  . SER B  2  408 ? 102.555 8.925   27.270  1.00 48.82  ?  408 SER B CB  1 
ATOM   8356  O  OG  . SER B  2  408 ? 102.545 7.719   26.520  1.00 43.97  ?  408 SER B OG  1 
ATOM   8357  N  N   . VAL B  2  409 ? 102.550 8.044   30.240  1.00 55.03  ?  409 VAL B N   1 
ATOM   8358  C  CA  . VAL B  2  409 ? 102.347 7.030   31.281  1.00 48.53  ?  409 VAL B CA  1 
ATOM   8359  C  C   . VAL B  2  409 ? 102.018 5.682   30.615  1.00 55.34  ?  409 VAL B C   1 
ATOM   8360  O  O   . VAL B  2  409 ? 102.530 4.648   31.037  1.00 60.11  ?  409 VAL B O   1 
ATOM   8361  C  CB  . VAL B  2  409 ? 101.281 7.452   32.309  1.00 49.41  ?  409 VAL B CB  1 
ATOM   8362  C  CG1 . VAL B  2  409 ? 101.069 6.360   33.354  1.00 43.98  ?  409 VAL B CG1 1 
ATOM   8363  C  CG2 . VAL B  2  409 ? 101.671 8.765   32.979  1.00 53.15  ?  409 VAL B CG2 1 
ATOM   8364  N  N   . GLU B  2  410 ? 101.216 5.709   29.540  1.00 54.21  ?  410 GLU B N   1 
ATOM   8365  C  CA  . GLU B  2  410 ? 100.847 4.510   28.792  1.00 45.59  ?  410 GLU B CA  1 
ATOM   8366  C  C   . GLU B  2  410 ? 102.093 3.828   28.236  1.00 52.20  ?  410 GLU B C   1 
ATOM   8367  O  O   . GLU B  2  410 ? 102.199 2.606   28.300  1.00 60.70  ?  410 GLU B O   1 
ATOM   8368  C  CB  . GLU B  2  410 ? 99.914  4.875   27.623  1.00 37.43  ?  410 GLU B CB  1 
ATOM   8369  C  CG  . GLU B  2  410 ? 98.520  5.303   28.044  1.00 59.85  ?  410 GLU B CG  1 
ATOM   8370  C  CD  . GLU B  2  410 ? 98.348  6.745   28.483  1.00 65.36  ?  410 GLU B CD  1 
ATOM   8371  O  OE1 . GLU B  2  410 ? 99.329  7.523   28.431  1.00 61.93  ?  410 GLU B OE1 1 
ATOM   8372  O  OE2 . GLU B  2  410 ? 97.216  7.096   28.884  1.00 69.54  ?  410 GLU B OE2 1 
ATOM   8373  N  N   . GLU B  2  411 ? 103.036 4.613   27.691  1.00 48.82  ?  411 GLU B N   1 
ATOM   8374  C  CA  . GLU B  2  411 ? 104.260 4.064   27.120  1.00 46.38  ?  411 GLU B CA  1 
ATOM   8375  C  C   . GLU B  2  411 ? 105.202 3.556   28.192  1.00 48.17  ?  411 GLU B C   1 
ATOM   8376  O  O   . GLU B  2  411 ? 105.831 2.519   27.998  1.00 54.50  ?  411 GLU B O   1 
ATOM   8377  C  CB  . GLU B  2  411 ? 104.957 5.095   26.240  1.00 43.24  ?  411 GLU B CB  1 
ATOM   8378  C  CG  . GLU B  2  411 ? 106.193 4.556   25.540  1.00 52.06  ?  411 GLU B CG  1 
ATOM   8379  C  CD  . GLU B  2  411 ? 105.992 3.351   24.636  1.00 64.95  ?  411 GLU B CD  1 
ATOM   8380  O  OE1 . GLU B  2  411 ? 104.884 2.766   24.642  1.00 71.28  ?  411 GLU B OE1 1 
ATOM   8381  O  OE2 . GLU B  2  411 ? 106.952 2.988   23.919  1.00 68.23  ?  411 GLU B OE2 1 
ATOM   8382  N  N   . ILE B  2  412 ? 105.298 4.255   29.334  1.00 48.00  ?  412 ILE B N   1 
ATOM   8383  C  CA  . ILE B  2  412 ? 106.152 3.812   30.444  1.00 45.04  ?  412 ILE B CA  1 
ATOM   8384  C  C   . ILE B  2  412 ? 105.630 2.452   30.911  1.00 54.31  ?  412 ILE B C   1 
ATOM   8385  O  O   . ILE B  2  412 ? 106.404 1.502   31.025  1.00 53.35  ?  412 ILE B O   1 
ATOM   8386  C  CB  . ILE B  2  412 ? 106.169 4.856   31.596  1.00 39.16  ?  412 ILE B CB  1 
ATOM   8387  C  CG1 . ILE B  2  412 ? 107.005 6.085   31.190  1.00 40.13  ?  412 ILE B CG1 1 
ATOM   8388  C  CG2 . ILE B  2  412 ? 106.718 4.248   32.892  1.00 35.94  ?  412 ILE B CG2 1 
ATOM   8389  C  CD1 . ILE B  2  412 ? 106.680 7.326   31.918  1.00 55.02  ?  412 ILE B CD1 1 
ATOM   8390  N  N   . ILE B  2  413 ? 104.306 2.345   31.116  1.00 45.79  ?  413 ILE B N   1 
ATOM   8391  C  CA  . ILE B  2  413 ? 103.681 1.090   31.522  1.00 43.81  ?  413 ILE B CA  1 
ATOM   8392  C  C   . ILE B  2  413 ? 103.944 0.003   30.460  1.00 53.67  ?  413 ILE B C   1 
ATOM   8393  O  O   . ILE B  2  413 ? 104.387 -1.089  30.809  1.00 67.35  ?  413 ILE B O   1 
ATOM   8394  C  CB  . ILE B  2  413 ? 102.162 1.285   31.807  1.00 47.57  ?  413 ILE B CB  1 
ATOM   8395  C  CG1 . ILE B  2  413 ? 101.945 1.938   33.193  1.00 49.33  ?  413 ILE B CG1 1 
ATOM   8396  C  CG2 . ILE B  2  413 ? 101.431 -0.042  31.733  1.00 48.43  ?  413 ILE B CG2 1 
ATOM   8397  C  CD1 . ILE B  2  413 ? 100.598 2.579   33.395  1.00 45.62  ?  413 ILE B CD1 1 
ATOM   8398  N  N   . ASN B  2  414 ? 103.707 0.296   29.173  1.00 50.37  ?  414 ASN B N   1 
ATOM   8399  C  CA  . ASN B  2  414 ? 103.949 -0.677  28.103  1.00 55.87  ?  414 ASN B CA  1 
ATOM   8400  C  C   . ASN B  2  414 ? 105.387 -1.193  28.124  1.00 50.40  ?  414 ASN B C   1 
ATOM   8401  O  O   . ASN B  2  414 ? 105.621 -2.370  27.865  1.00 57.08  ?  414 ASN B O   1 
ATOM   8402  C  CB  . ASN B  2  414 ? 103.664 -0.059  26.736  1.00 53.76  ?  414 ASN B CB  1 
ATOM   8403  C  CG  . ASN B  2  414 ? 102.196 0.070   26.418  1.00 68.49  ?  414 ASN B CG  1 
ATOM   8404  O  OD1 . ASN B  2  414 ? 101.323 -0.137  27.271  1.00 74.99  ?  414 ASN B OD1 1 
ATOM   8405  N  ND2 . ASN B  2  414 ? 101.888 0.422   25.177  1.00 76.67  ?  414 ASN B ND2 1 
ATOM   8406  N  N   . LYS B  2  415 ? 106.344 -0.310  28.428  1.00 47.48  ?  415 LYS B N   1 
ATOM   8407  C  CA  . LYS B  2  415 ? 107.753 -0.680  28.487  1.00 51.76  ?  415 LYS B CA  1 
ATOM   8408  C  C   . LYS B  2  415 ? 108.065 -1.500  29.741  1.00 58.71  ?  415 LYS B C   1 
ATOM   8409  O  O   . LYS B  2  415 ? 108.904 -2.400  29.685  1.00 61.07  ?  415 LYS B O   1 
ATOM   8410  C  CB  . LYS B  2  415 ? 108.638 0.575   28.419  1.00 31.31  ?  415 LYS B CB  1 
ATOM   8411  C  CG  . LYS B  2  415 ? 108.836 1.103   26.992  1.00 47.80  ?  415 LYS B CG  1 
ATOM   8412  C  CD  . LYS B  2  415 ? 110.302 1.340   26.668  1.00 73.57  ?  415 LYS B CD  1 
ATOM   8413  C  CE  . LYS B  2  415 ? 110.585 1.557   25.200  1.00 86.30  ?  415 LYS B CE  1 
ATOM   8414  N  NZ  . LYS B  2  415 ? 111.963 2.085   24.980  1.00 85.25  ?  415 LYS B NZ  1 
ATOM   8415  N  N   . LEU B  2  416 ? 107.391 -1.205  30.862  1.00 55.37  ?  416 LEU B N   1 
ATOM   8416  C  CA  . LEU B  2  416 ? 107.607 -1.941  32.106  1.00 53.70  ?  416 LEU B CA  1 
ATOM   8417  C  C   . LEU B  2  416 ? 107.062 -3.373  32.009  1.00 55.20  ?  416 LEU B C   1 
ATOM   8418  O  O   . LEU B  2  416 ? 107.535 -4.243  32.730  1.00 63.45  ?  416 LEU B O   1 
ATOM   8419  C  CB  . LEU B  2  416 ? 106.948 -1.218  33.299  1.00 55.80  ?  416 LEU B CB  1 
ATOM   8420  C  CG  . LEU B  2  416 ? 107.529 0.135   33.724  1.00 52.69  ?  416 LEU B CG  1 
ATOM   8421  C  CD1 . LEU B  2  416 ? 106.618 0.816   34.727  1.00 45.01  ?  416 LEU B CD1 1 
ATOM   8422  C  CD2 . LEU B  2  416 ? 108.938 -0.005  34.304  1.00 30.85  ?  416 LEU B CD2 1 
ATOM   8423  N  N   . ASP B  2  417 ? 106.074 -3.628  31.137  1.00 48.38  ?  417 ASP B N   1 
ATOM   8424  C  CA  . ASP B  2  417 ? 105.511 -4.972  30.982  1.00 55.33  ?  417 ASP B CA  1 
ATOM   8425  C  C   . ASP B  2  417 ? 106.546 -5.999  30.502  1.00 59.81  ?  417 ASP B C   1 
ATOM   8426  O  O   . ASP B  2  417 ? 106.304 -7.198  30.610  1.00 70.97  ?  417 ASP B O   1 
ATOM   8427  C  CB  . ASP B  2  417 ? 104.334 -4.954  29.989  1.00 62.79  ?  417 ASP B CB  1 
ATOM   8428  C  CG  . ASP B  2  417 ? 103.011 -4.502  30.572  1.00 78.36  ?  417 ASP B CG  1 
ATOM   8429  O  OD1 . ASP B  2  417 ? 102.989 -4.092  31.760  1.00 76.61  ?  417 ASP B OD1 1 
ATOM   8430  O  OD2 . ASP B  2  417 ? 101.991 -4.561  29.845  1.00 75.04  ?  417 ASP B OD2 1 
ATOM   8431  N  N   . LYS B  2  418 ? 107.687 -5.550  29.972  1.00 55.27  ?  418 LYS B N   1 
ATOM   8432  C  CA  . LYS B  2  418 ? 108.711 -6.474  29.488  1.00 51.00  ?  418 LYS B CA  1 
ATOM   8433  C  C   . LYS B  2  418 ? 109.529 -7.073  30.626  1.00 60.36  ?  418 LYS B C   1 
ATOM   8434  O  O   . LYS B  2  418 ? 110.266 -8.033  30.391  1.00 71.46  ?  418 LYS B O   1 
ATOM   8435  C  CB  . LYS B  2  418 ? 109.619 -5.792  28.454  1.00 63.73  ?  418 LYS B CB  1 
ATOM   8436  C  CG  . LYS B  2  418 ? 108.860 -5.040  27.352  1.00 82.91  ?  418 LYS B CG  1 
ATOM   8437  C  CD  . LYS B  2  418 ? 108.002 -5.950  26.452  1.00 71.03  ?  418 LYS B CD  1 
ATOM   8438  C  CE  . LYS B  2  418 ? 106.944 -5.184  25.696  1.00 87.73  ?  418 LYS B CE  1 
ATOM   8439  N  NZ  . LYS B  2  418 ? 106.837 -5.638  24.286  1.00 123.09 ?  418 LYS B NZ  1 
ATOM   8440  N  N   . VAL B  2  419 ? 109.397 -6.531  31.852  1.00 50.92  ?  419 VAL B N   1 
ATOM   8441  C  CA  . VAL B  2  419 ? 110.103 -7.047  33.018  1.00 48.05  ?  419 VAL B CA  1 
ATOM   8442  C  C   . VAL B  2  419 ? 109.127 -7.757  33.971  1.00 60.72  ?  419 VAL B C   1 
ATOM   8443  O  O   . VAL B  2  419 ? 109.451 -7.929  35.147  1.00 73.64  ?  419 VAL B O   1 
ATOM   8444  C  CB  . VAL B  2  419 ? 110.936 -5.956  33.738  1.00 41.77  ?  419 VAL B CB  1 
ATOM   8445  C  CG1 . VAL B  2  419 ? 111.927 -5.309  32.778  1.00 51.45  ?  419 VAL B CG1 1 
ATOM   8446  C  CG2 . VAL B  2  419 ? 110.052 -4.903  34.398  1.00 37.29  ?  419 VAL B CG2 1 
ATOM   8447  N  N   . VAL B  2  420 ? 108.006 -8.235  33.430  1.00 56.24  ?  420 VAL B N   1 
ATOM   8448  C  CA  . VAL B  2  420 ? 106.958 -8.862  34.284  1.00 61.02  ?  420 VAL B CA  1 
ATOM   8449  C  C   . VAL B  2  420 ? 106.725 -10.306 33.820  1.00 56.46  ?  420 VAL B C   1 
ATOM   8450  O  O   . VAL B  2  420 ? 106.472 -10.497 32.616  1.00 59.02  ?  420 VAL B O   1 
ATOM   8451  C  CB  . VAL B  2  420 ? 105.683 -8.003  34.207  1.00 49.62  ?  420 VAL B CB  1 
ATOM   8452  C  CG1 . VAL B  2  420 ? 104.443 -8.775  34.591  1.00 41.50  ?  420 VAL B CG1 1 
ATOM   8453  C  CG2 . VAL B  2  420 ? 105.807 -6.738  35.038  1.00 58.93  ?  420 VAL B CG2 1 
ATOM   8454  N  N   . ASN B  2  421 ? 106.813 -11.283 34.735  1.00 51.89  ?  421 ASN B N   1 
ATOM   8455  C  CA  . ASN B  2  421 ? 106.671 -12.712 34.347  1.00 51.24  ?  421 ASN B CA  1 
ATOM   8456  C  C   . ASN B  2  421 ? 105.224 -12.970 33.922  1.00 54.26  ?  421 ASN B C   1 
ATOM   8457  O  O   . ASN B  2  421 ? 104.314 -12.414 34.563  1.00 66.81  ?  421 ASN B O   1 
ATOM   8458  C  CB  . ASN B  2  421 ? 107.109 -13.659 35.467  1.00 49.26  ?  421 ASN B CB  1 
ATOM   8459  C  CG  . ASN B  2  421 ? 107.419 -15.055 34.972  1.00 62.65  ?  421 ASN B CG  1 
ATOM   8460  O  OD1 . ASN B  2  421 ? 106.546 -15.739 34.443  1.00 80.27  ?  421 ASN B OD1 1 
ATOM   8461  N  ND2 . ASN B  2  421 ? 108.658 -15.487 35.137  1.00 63.22  ?  421 ASN B ND2 1 
ATOM   8462  N  N   . THR B  2  422 ? 105.031 -13.788 32.886  1.00 62.94  ?  422 THR B N   1 
ATOM   8463  C  CA  . THR B  2  422 ? 103.667 -14.076 32.371  1.00 58.82  ?  422 THR B CA  1 
ATOM   8464  C  C   . THR B  2  422 ? 102.873 -14.869 33.414  1.00 58.07  ?  422 THR B C   1 
ATOM   8465  O  O   . THR B  2  422 ? 101.633 -14.901 33.302  1.00 80.44  ?  422 THR B O   1 
ATOM   8466  C  CB  . THR B  2  422 ? 103.739 -14.838 31.044  1.00 49.81  ?  422 THR B CB  1 
ATOM   8467  O  OG1 . THR B  2  422 ? 104.731 -14.212 30.230  1.00 58.89  ?  422 THR B OG1 1 
ATOM   8468  C  CG2 . THR B  2  422 ? 102.417 -14.870 30.311  1.00 97.28  ?  422 THR B CG2 1 
ATOM   8469  N  N   . GLN B  2  423 ? 103.545 -15.388 34.446  1.00 55.42  ?  423 GLN B N   1 
ATOM   8470  C  CA  . GLN B  2  423 ? 102.850 -16.239 35.450  1.00 61.37  ?  423 GLN B CA  1 
ATOM   8471  C  C   . GLN B  2  423 ? 102.811 -15.571 36.832  1.00 69.26  ?  423 GLN B C   1 
ATOM   8472  O  O   . GLN B  2  423 ? 102.407 -16.262 37.784  1.00 82.19  ?  423 GLN B O   1 
ATOM   8473  C  CB  . GLN B  2  423 ? 103.543 -17.598 35.565  1.00 55.01  ?  423 GLN B CB  1 
ATOM   8474  C  CG  . GLN B  2  423 ? 104.382 -17.966 34.352  1.00 56.69  ?  423 GLN B CG  1 
ATOM   8475  C  CD  . GLN B  2  423 ? 103.610 -18.830 33.387  1.00 68.98  ?  423 GLN B CD  1 
ATOM   8476  O  OE1 . GLN B  2  423 ? 103.135 -19.910 33.732  1.00 71.42  ?  423 GLN B OE1 1 
ATOM   8477  N  NE2 . GLN B  2  423 ? 103.474 -18.352 32.162  1.00 78.21  ?  423 GLN B NE2 1 
ATOM   8478  N  N   . ILE B  2  424 ? 103.183 -14.292 36.954  1.00 54.72  ?  424 ILE B N   1 
ATOM   8479  C  CA  . ILE B  2  424 ? 103.058 -13.631 38.290  1.00 63.16  ?  424 ILE B CA  1 
ATOM   8480  C  C   . ILE B  2  424 ? 102.480 -12.218 38.415  1.00 72.08  ?  424 ILE B C   1 
ATOM   8481  O  O   . ILE B  2  424 ? 101.383 -12.083 38.988  1.00 99.59  ?  424 ILE B O   1 
ATOM   8482  C  CB  . ILE B  2  424 ? 104.422 -13.545 39.005  1.00 51.63  ?  424 ILE B CB  1 
ATOM   8483  C  CG1 . ILE B  2  424 ? 105.192 -14.866 38.938  1.00 66.37  ?  424 ILE B CG1 1 
ATOM   8484  C  CG2 . ILE B  2  424 ? 104.245 -13.069 40.438  1.00 80.45  ?  424 ILE B CG2 1 
ATOM   8485  C  CD1 . ILE B  2  424 ? 106.462 -14.873 39.755  1.00 73.19  ?  424 ILE B CD1 1 
ATOM   8486  N  N   . GLY B  2  425 ? 103.192 -11.212 37.898  1.00 84.18  ?  425 GLY B N   1 
ATOM   8487  C  CA  . GLY B  2  425 ? 102.778 -9.806  38.074  1.00 68.46  ?  425 GLY B CA  1 
ATOM   8488  C  C   . GLY B  2  425 ? 101.690 -9.549  37.050  1.00 81.33  ?  425 GLY B C   1 
ATOM   8489  O  O   . GLY B  2  425 ? 101.662 -10.249 36.020  1.00 87.03  ?  425 GLY B O   1 
ATOM   8490  N  N   . PRO B  2  426 ? 100.790 -8.571  37.292  1.00 69.16  ?  426 PRO B N   1 
ATOM   8491  C  CA  . PRO B  2  426 ? 99.747  -8.222  36.330  1.00 59.08  ?  426 PRO B CA  1 
ATOM   8492  C  C   . PRO B  2  426 ? 100.313 -7.367  35.190  1.00 67.18  ?  426 PRO B C   1 
ATOM   8493  O  O   . PRO B  2  426 ? 101.406 -6.854  35.337  1.00 68.81  ?  426 PRO B O   1 
ATOM   8494  C  CB  . PRO B  2  426 ? 98.781  -7.385  37.176  1.00 57.99  ?  426 PRO B CB  1 
ATOM   8495  C  CG  . PRO B  2  426 ? 99.678  -6.712  38.187  1.00 68.59  ?  426 PRO B CG  1 
ATOM   8496  C  CD  . PRO B  2  426 ? 100.739 -7.745  38.501  1.00 64.42  ?  426 PRO B CD  1 
ATOM   8497  N  N   . MET B  2  427 ? 99.562  -7.233  34.095  1.00 59.90  ?  427 MET B N   1 
ATOM   8498  C  CA  . MET B  2  427 ? 100.025 -6.454  32.961  1.00 53.99  ?  427 MET B CA  1 
ATOM   8499  C  C   . MET B  2  427 ? 99.342  -5.086  32.949  1.00 65.90  ?  427 MET B C   1 
ATOM   8500  O  O   . MET B  2  427 ? 98.261  -4.916  33.511  1.00 68.28  ?  427 MET B O   1 
ATOM   8501  C  CB  . MET B  2  427 ? 99.721  -7.196  31.656  1.00 60.73  ?  427 MET B CB  1 
ATOM   8502  C  CG  . MET B  2  427 ? 100.295 -8.595  31.596  1.00 71.82  ?  427 MET B CG  1 
ATOM   8503  S  SD  . MET B  2  427 ? 102.099 -8.664  31.660  1.00 53.27  ?  427 MET B SD  1 
ATOM   8504  C  CE  . MET B  2  427 ? 102.487 -8.253  29.972  1.00 81.91  ?  427 MET B CE  1 
ATOM   8505  N  N   . GLN B  2  428 ? 99.980  -4.115  32.295  1.00 65.61  ?  428 GLN B N   1 
ATOM   8506  C  CA  . GLN B  2  428 ? 99.492  -2.746  32.167  1.00 56.75  ?  428 GLN B CA  1 
ATOM   8507  C  C   . GLN B  2  428 ? 99.333  -2.035  33.510  1.00 60.50  ?  428 GLN B C   1 
ATOM   8508  O  O   . GLN B  2  428 ? 98.418  -1.233  33.669  1.00 69.04  ?  428 GLN B O   1 
ATOM   8509  C  CB  . GLN B  2  428 ? 98.198  -2.675  31.337  1.00 44.76  ?  428 GLN B CB  1 
ATOM   8510  C  CG  . GLN B  2  428 ? 98.388  -3.074  29.880  1.00 51.31  ?  428 GLN B CG  1 
ATOM   8511  C  CD  . GLN B  2  428 ? 99.290  -2.120  29.131  1.00 71.41  ?  428 GLN B CD  1 
ATOM   8512  O  OE1 . GLN B  2  428 ? 98.947  -0.953  28.895  1.00 75.64  ?  428 GLN B OE1 1 
ATOM   8513  N  NE2 . GLN B  2  428 ? 100.472 -2.589  28.736  1.00 79.22  ?  428 GLN B NE2 1 
ATOM   8514  N  N   . THR B  2  429 ? 100.238 -2.299  34.462  1.00 60.56  ?  429 THR B N   1 
ATOM   8515  C  CA  . THR B  2  429 ? 100.210 -1.640  35.769  1.00 60.75  ?  429 THR B CA  1 
ATOM   8516  C  C   . THR B  2  429 ? 101.602 -1.074  36.078  1.00 59.84  ?  429 THR B C   1 
ATOM   8517  O  O   . THR B  2  429 ? 102.586 -1.467  35.450  1.00 67.04  ?  429 THR B O   1 
ATOM   8518  C  CB  . THR B  2  429 ? 99.728  -2.594  36.895  1.00 57.61  ?  429 THR B CB  1 
ATOM   8519  O  OG1 . THR B  2  429 ? 100.809 -3.420  37.342  1.00 70.51  ?  429 THR B OG1 1 
ATOM   8520  C  CG2 . THR B  2  429 ? 98.536  -3.447  36.482  1.00 65.60  ?  429 THR B CG2 1 
ATOM   8521  N  N   . VAL B  2  430 ? 101.684 -0.163  37.054  1.00 64.08  ?  430 VAL B N   1 
ATOM   8522  C  CA  . VAL B  2  430 ? 102.960 0.438   37.449  1.00 53.96  ?  430 VAL B CA  1 
ATOM   8523  C  C   . VAL B  2  430 ? 103.688 -0.406  38.502  1.00 62.91  ?  430 VAL B C   1 
ATOM   8524  O  O   . VAL B  2  430 ? 104.683 0.064   39.051  1.00 57.65  ?  430 VAL B O   1 
ATOM   8525  C  CB  . VAL B  2  430 ? 102.800 1.910   37.932  1.00 52.31  ?  430 VAL B CB  1 
ATOM   8526  C  CG1 . VAL B  2  430 ? 102.113 2.765   36.872  1.00 63.37  ?  430 VAL B CG1 1 
ATOM   8527  C  CG2 . VAL B  2  430 ? 102.061 2.002   39.269  1.00 52.00  ?  430 VAL B CG2 1 
ATOM   8528  N  N   . LYS B  2  431 ? 103.225 -1.646  38.785  1.00 55.35  ?  431 LYS B N   1 
ATOM   8529  C  CA  . LYS B  2  431 ? 103.870 -2.482  39.800  1.00 56.40  ?  431 LYS B CA  1 
ATOM   8530  C  C   . LYS B  2  431 ? 105.402 -2.612  39.613  1.00 58.55  ?  431 LYS B C   1 
ATOM   8531  O  O   . LYS B  2  431 ? 106.119 -2.447  40.595  1.00 58.21  ?  431 LYS B O   1 
ATOM   8532  C  CB  . LYS B  2  431 ? 103.214 -3.875  39.907  1.00 50.39  ?  431 LYS B CB  1 
ATOM   8533  C  CG  . LYS B  2  431 ? 103.368 -4.516  41.293  1.00 62.25  ?  431 LYS B CG  1 
ATOM   8534  C  CD  . LYS B  2  431 ? 102.994 -5.992  41.319  1.00 69.86  ?  431 LYS B CD  1 
ATOM   8535  C  CE  . LYS B  2  431 ? 104.180 -6.921  41.155  1.00 84.99  ?  431 LYS B CE  1 
ATOM   8536  N  NZ  . LYS B  2  431 ? 104.829 -7.282  42.452  1.00 84.34  ?  431 LYS B NZ  1 
ATOM   8537  N  N   . PRO B  2  432 ? 105.952 -2.872  38.404  1.00 51.22  ?  432 PRO B N   1 
ATOM   8538  C  CA  . PRO B  2  432 ? 107.418 -2.985  38.287  1.00 47.79  ?  432 PRO B CA  1 
ATOM   8539  C  C   . PRO B  2  432 ? 108.175 -1.757  38.789  1.00 49.78  ?  432 PRO B C   1 
ATOM   8540  O  O   . PRO B  2  432 ? 109.233 -1.902  39.394  1.00 47.70  ?  432 PRO B O   1 
ATOM   8541  C  CB  . PRO B  2  432 ? 107.632 -3.220  36.791  1.00 46.28  ?  432 PRO B CB  1 
ATOM   8542  C  CG  . PRO B  2  432 ? 106.367 -3.798  36.321  1.00 48.25  ?  432 PRO B CG  1 
ATOM   8543  C  CD  . PRO B  2  432 ? 105.305 -3.100  37.097  1.00 53.70  ?  432 PRO B CD  1 
ATOM   8544  N  N   . LEU B  2  433 ? 107.643 -0.553  38.546  1.00 56.56  ?  433 LEU B N   1 
ATOM   8545  C  CA  . LEU B  2  433 ? 108.286 0.675   39.003  1.00 50.80  ?  433 LEU B CA  1 
ATOM   8546  C  C   . LEU B  2  433 ? 108.161 0.768   40.528  1.00 61.41  ?  433 LEU B C   1 
ATOM   8547  O  O   . LEU B  2  433 ? 109.137 1.084   41.207  1.00 63.70  ?  433 LEU B O   1 
ATOM   8548  C  CB  . LEU B  2  433 ? 107.659 1.900   38.322  1.00 40.08  ?  433 LEU B CB  1 
ATOM   8549  C  CG  . LEU B  2  433 ? 108.143 3.264   38.804  1.00 38.42  ?  433 LEU B CG  1 
ATOM   8550  C  CD1 . LEU B  2  433 ? 109.627 3.446   38.557  1.00 29.81  ?  433 LEU B CD1 1 
ATOM   8551  C  CD2 . LEU B  2  433 ? 107.359 4.374   38.136  1.00 45.99  ?  433 LEU B CD2 1 
ATOM   8552  N  N   . ALA B  2  434 ? 106.981 0.500   41.079  1.00 55.03  ?  434 ALA B N   1 
ATOM   8553  C  CA  . ALA B  2  434 ? 106.883 0.540   42.553  1.00 51.68  ?  434 ALA B CA  1 
ATOM   8554  C  C   . ALA B  2  434 ? 107.783 -0.535  43.173  1.00 59.16  ?  434 ALA B C   1 
ATOM   8555  O  O   . ALA B  2  434 ? 108.389 -0.255  44.224  1.00 61.06  ?  434 ALA B O   1 
ATOM   8556  C  CB  . ALA B  2  434 ? 105.448 0.382   42.963  1.00 43.62  ?  434 ALA B CB  1 
ATOM   8557  N  N   . ASP B  2  435 ? 107.871 -1.710  42.545  1.00 55.73  ?  435 ASP B N   1 
ATOM   8558  C  CA  . ASP B  2  435 ? 108.713 -2.797  43.048  1.00 48.76  ?  435 ASP B CA  1 
ATOM   8559  C  C   . ASP B  2  435 ? 110.161 -2.331  43.233  1.00 52.79  ?  435 ASP B C   1 
ATOM   8560  O  O   . ASP B  2  435 ? 110.701 -2.480  44.323  1.00 56.74  ?  435 ASP B O   1 
ATOM   8561  C  CB  . ASP B  2  435 ? 108.688 -4.005  42.087  1.00 62.97  ?  435 ASP B CB  1 
ATOM   8562  C  CG  . ASP B  2  435 ? 107.455 -4.884  42.173  1.00 78.27  ?  435 ASP B CG  1 
ATOM   8563  O  OD1 . ASP B  2  435 ? 106.531 -4.543  42.956  1.00 76.28  ?  435 ASP B OD1 1 
ATOM   8564  O  OD2 . ASP B  2  435 ? 107.409 -5.913  41.455  1.00 69.67  ?  435 ASP B OD2 1 
ATOM   8565  N  N   . VAL B  2  436 ? 110.795 -1.773  42.180  1.00 53.20  ?  436 VAL B N   1 
ATOM   8566  C  CA  . VAL B  2  436 ? 112.186 -1.306  42.284  1.00 50.19  ?  436 VAL B CA  1 
ATOM   8567  C  C   . VAL B  2  436 ? 112.320 -0.177  43.293  1.00 52.37  ?  436 VAL B C   1 
ATOM   8568  O  O   . VAL B  2  436 ? 113.358 -0.076  43.944  1.00 61.40  ?  436 VAL B O   1 
ATOM   8569  C  CB  . VAL B  2  436 ? 112.831 -0.902  40.928  1.00 44.28  ?  436 VAL B CB  1 
ATOM   8570  C  CG1 . VAL B  2  436 ? 113.053 -2.115  40.037  1.00 40.77  ?  436 VAL B CG1 1 
ATOM   8571  C  CG2 . VAL B  2  436 ? 112.014 0.162   40.203  1.00 41.04  ?  436 VAL B CG2 1 
ATOM   8572  N  N   . LEU B  2  437 ? 111.295 0.671   43.426  1.00 47.79  ?  437 LEU B N   1 
ATOM   8573  C  CA  . LEU B  2  437 ? 111.348 1.773   44.377  1.00 50.81  ?  437 LEU B CA  1 
ATOM   8574  C  C   . LEU B  2  437 ? 111.300 1.245   45.805  1.00 65.22  ?  437 LEU B C   1 
ATOM   8575  O  O   . LEU B  2  437 ? 112.030 1.745   46.659  1.00 68.24  ?  437 LEU B O   1 
ATOM   8576  C  CB  . LEU B  2  437 ? 110.199 2.754   44.138  1.00 44.09  ?  437 LEU B CB  1 
ATOM   8577  C  CG  . LEU B  2  437 ? 110.288 3.577   42.857  1.00 54.48  ?  437 LEU B CG  1 
ATOM   8578  C  CD1 . LEU B  2  437 ? 108.971 4.245   42.562  1.00 39.12  ?  437 LEU B CD1 1 
ATOM   8579  C  CD2 . LEU B  2  437 ? 111.401 4.611   42.934  1.00 48.99  ?  437 LEU B CD2 1 
ATOM   8580  N  N   . VAL B  2  438 ? 110.455 0.242   46.053  1.00 57.34  ?  438 VAL B N   1 
ATOM   8581  C  CA  . VAL B  2  438 ? 110.336 -0.346  47.421  1.00 51.29  ?  438 VAL B CA  1 
ATOM   8582  C  C   . VAL B  2  438 ? 111.582 -1.191  47.704  1.00 52.01  ?  438 VAL B C   1 
ATOM   8583  O  O   . VAL B  2  438 ? 112.078 -1.143  48.845  1.00 66.81  ?  438 VAL B O   1 
ATOM   8584  C  CB  . VAL B  2  438 ? 109.046 -1.175  47.568  1.00 44.17  ?  438 VAL B CB  1 
ATOM   8585  C  CG1 . VAL B  2  438 ? 109.042 -1.991  48.852  1.00 43.40  ?  438 VAL B CG1 1 
ATOM   8586  C  CG2 . VAL B  2  438 ? 107.805 -0.300  47.485  1.00 52.34  ?  438 VAL B CG2 1 
ATOM   8587  N  N   . SER B  2  439 ? 112.069 -1.925  46.700  1.00 57.76  ?  439 SER B N   1 
ATOM   8588  C  CA  . SER B  2  439 ? 113.248 -2.809  46.890  1.00 66.40  ?  439 SER B CA  1 
ATOM   8589  C  C   . SER B  2  439 ? 114.476 -1.975  47.266  1.00 51.88  ?  439 SER B C   1 
ATOM   8590  O  O   . SER B  2  439 ? 115.284 -2.451  48.085  1.00 60.24  ?  439 SER B O   1 
ATOM   8591  C  CB  . SER B  2  439 ? 113.503 -3.638  45.661  1.00 54.44  ?  439 SER B CB  1 
ATOM   8592  O  OG  . SER B  2  439 ? 113.853 -2.814  44.561  1.00 62.48  ?  439 SER B OG  1 
ATOM   8593  N  N   . GLY B  2  440 ? 114.605 -0.778  46.688  1.00 55.11  ?  440 GLY B N   1 
ATOM   8594  C  CA  . GLY B  2  440 ? 115.749 0.101   46.997  1.00 68.42  ?  440 GLY B CA  1 
ATOM   8595  C  C   . GLY B  2  440 ? 116.722 0.198   45.835  1.00 65.37  ?  440 GLY B C   1 
ATOM   8596  O  O   . GLY B  2  440 ? 117.672 0.997   45.934  1.00 71.70  ?  440 GLY B O   1 
ATOM   8597  N  N   . VAL B  2  441 ? 116.500 -0.582  44.774  1.00 62.45  ?  441 VAL B N   1 
ATOM   8598  C  CA  . VAL B  2  441 ? 117.365 -0.476  43.562  1.00 55.29  ?  441 VAL B CA  1 
ATOM   8599  C  C   . VAL B  2  441 ? 117.263 0.964   43.057  1.00 58.88  ?  441 VAL B C   1 
ATOM   8600  O  O   . VAL B  2  441 ? 118.319 1.573   42.801  1.00 69.14  ?  441 VAL B O   1 
ATOM   8601  C  CB  . VAL B  2  441 ? 116.945 -1.489  42.481  1.00 56.96  ?  441 VAL B CB  1 
ATOM   8602  C  CG1 . VAL B  2  441 ? 117.699 -1.271  41.179  1.00 54.39  ?  441 VAL B CG1 1 
ATOM   8603  C  CG2 . VAL B  2  441 ? 117.104 -2.923  42.961  1.00 42.96  ?  441 VAL B CG2 1 
ATOM   8604  N  N   . LEU B  2  442 ? 116.040 1.486   42.934  1.00 51.75  ?  442 LEU B N   1 
ATOM   8605  C  CA  . LEU B  2  442 ? 115.854 2.909   42.548  1.00 53.23  ?  442 LEU B CA  1 
ATOM   8606  C  C   . LEU B  2  442 ? 115.566 3.690   43.831  1.00 64.92  ?  442 LEU B C   1 
ATOM   8607  O  O   . LEU B  2  442 ? 114.480 3.490   44.405  1.00 63.14  ?  442 LEU B O   1 
ATOM   8608  C  CB  . LEU B  2  442 ? 114.697 3.015   41.553  1.00 44.24  ?  442 LEU B CB  1 
ATOM   8609  C  CG  . LEU B  2  442 ? 115.072 2.786   40.090  1.00 39.51  ?  442 LEU B CG  1 
ATOM   8610  C  CD1 . LEU B  2  442 ? 113.952 3.238   39.166  1.00 42.57  ?  442 LEU B CD1 1 
ATOM   8611  C  CD2 . LEU B  2  442 ? 116.368 3.503   39.747  1.00 54.74  ?  442 LEU B CD2 1 
ATOM   8612  N  N   . ARG B  2  443 ? 116.492 4.542   44.280  1.00 54.24  ?  443 ARG B N   1 
ATOM   8613  C  CA  . ARG B  2  443 ? 116.323 5.243   45.586  1.00 48.73  ?  443 ARG B CA  1 
ATOM   8614  C  C   . ARG B  2  443 ? 115.115 6.189   45.564  1.00 58.70  ?  443 ARG B C   1 
ATOM   8615  O  O   . ARG B  2  443 ? 114.677 6.594   46.657  1.00 64.69  ?  443 ARG B O   1 
ATOM   8616  C  CB  . ARG B  2  443 ? 117.608 5.998   45.939  1.00 35.52  ?  443 ARG B CB  1 
ATOM   8617  C  CG  . ARG B  2  443 ? 118.883 5.252   45.575  1.00 49.98  ?  443 ARG B CG  1 
ATOM   8618  C  CD  . ARG B  2  443 ? 119.148 4.087   46.509  1.00 51.48  ?  443 ARG B CD  1 
ATOM   8619  N  NE  . ARG B  2  443 ? 118.732 4.373   47.874  1.00 53.72  ?  443 ARG B NE  1 
ATOM   8620  C  CZ  . ARG B  2  443 ? 118.129 3.502   48.674  1.00 71.16  ?  443 ARG B CZ  1 
ATOM   8621  N  NH1 . ARG B  2  443 ? 118.082 2.224   48.344  1.00 69.78  ?  443 ARG B NH1 1 
ATOM   8622  N  NH2 . ARG B  2  443 ? 117.578 3.911   49.804  1.00 72.61  ?  443 ARG B NH2 1 
ATOM   8623  N  N   . GLY B  2  444 ? 114.600 6.529   44.381  1.00 49.39  ?  444 GLY B N   1 
ATOM   8624  C  CA  . GLY B  2  444 ? 113.465 7.435   44.260  1.00 47.41  ?  444 GLY B CA  1 
ATOM   8625  C  C   . GLY B  2  444 ? 113.220 7.855   42.826  1.00 38.62  ?  444 GLY B C   1 
ATOM   8626  O  O   . GLY B  2  444 ? 113.820 7.296   41.907  1.00 44.14  ?  444 GLY B O   1 
ATOM   8627  N  N   . ALA B  2  445 ? 112.335 8.840   42.613  1.00 36.31  ?  445 ALA B N   1 
ATOM   8628  C  CA  . ALA B  2  445 ? 112.048 9.336   41.267  1.00 43.96  ?  445 ALA B CA  1 
ATOM   8629  C  C   . ALA B  2  445 ? 111.848 10.846  41.313  1.00 51.75  ?  445 ALA B C   1 
ATOM   8630  O  O   . ALA B  2  445 ? 110.948 11.332  41.994  1.00 56.26  ?  445 ALA B O   1 
ATOM   8631  C  CB  . ALA B  2  445 ? 110.817 8.655   40.693  1.00 32.52  ?  445 ALA B CB  1 
ATOM   8632  N  N   . ALA B  2  446 ? 112.700 11.590  40.601  1.00 48.76  ?  446 ALA B N   1 
ATOM   8633  C  CA  . ALA B  2  446 ? 112.631 13.047  40.567  1.00 41.73  ?  446 ALA B CA  1 
ATOM   8634  C  C   . ALA B  2  446 ? 112.133 13.550  39.219  1.00 48.73  ?  446 ALA B C   1 
ATOM   8635  O  O   . ALA B  2  446 ? 112.387 12.935  38.184  1.00 52.81  ?  446 ALA B O   1 
ATOM   8636  C  CB  . ALA B  2  446 ? 114.004 13.633  40.851  1.00 44.02  ?  446 ALA B CB  1 
ATOM   8637  N  N   . ALA B  2  447 ? 111.438 14.684  39.235  1.00 44.71  ?  447 ALA B N   1 
ATOM   8638  C  CA  . ALA B  2  447 ? 110.913 15.301  38.032  1.00 39.76  ?  447 ALA B CA  1 
ATOM   8639  C  C   . ALA B  2  447 ? 111.611 16.630  37.860  1.00 48.31  ?  447 ALA B C   1 
ATOM   8640  O  O   . ALA B  2  447 ? 111.403 17.515  38.681  1.00 56.50  ?  447 ALA B O   1 
ATOM   8641  C  CB  . ALA B  2  447 ? 109.420 15.530  38.181  1.00 36.44  ?  447 ALA B CB  1 
ATOM   8642  N  N   . VAL B  2  448 ? 112.448 16.781  36.829  1.00 42.10  ?  448 VAL B N   1 
ATOM   8643  C  CA  . VAL B  2  448 ? 113.127 18.048  36.589  1.00 37.03  ?  448 VAL B CA  1 
ATOM   8644  C  C   . VAL B  2  448 ? 112.373 18.746  35.458  1.00 50.83  ?  448 VAL B C   1 
ATOM   8645  O  O   . VAL B  2  448 ? 112.337 18.255  34.332  1.00 52.55  ?  448 VAL B O   1 
ATOM   8646  C  CB  . VAL B  2  448 ? 114.630 17.880  36.291  1.00 39.66  ?  448 VAL B CB  1 
ATOM   8647  C  CG1 . VAL B  2  448 ? 115.296 19.236  36.088  1.00 36.75  ?  448 VAL B CG1 1 
ATOM   8648  C  CG2 . VAL B  2  448 ? 115.315 17.103  37.412  1.00 49.93  ?  448 VAL B CG2 1 
ATOM   8649  N  N   . VAL B  2  449 ? 111.731 19.873  35.786  1.00 55.72  ?  449 VAL B N   1 
ATOM   8650  C  CA  . VAL B  2  449 ? 110.914 20.668  34.863  1.00 48.24  ?  449 VAL B CA  1 
ATOM   8651  C  C   . VAL B  2  449 ? 111.389 22.128  34.931  1.00 52.02  ?  449 VAL B C   1 
ATOM   8652  O  O   . VAL B  2  449 ? 112.196 22.452  35.801  1.00 71.03  ?  449 VAL B O   1 
ATOM   8653  C  CB  . VAL B  2  449 ? 109.414 20.549  35.275  1.00 48.67  ?  449 VAL B CB  1 
ATOM   8654  C  CG1 . VAL B  2  449 ? 108.994 19.089  35.432  1.00 49.38  ?  449 VAL B CG1 1 
ATOM   8655  C  CG2 . VAL B  2  449 ? 109.122 21.320  36.559  1.00 30.32  ?  449 VAL B CG2 1 
ATOM   8656  N  N   . GLY B  2  450 ? 110.904 22.993  34.042  1.00 40.05  ?  450 GLY B N   1 
ATOM   8657  C  CA  . GLY B  2  450 ? 111.284 24.400  34.103  1.00 48.46  ?  450 GLY B CA  1 
ATOM   8658  C  C   . GLY B  2  450 ? 111.709 25.071  32.818  1.00 41.21  ?  450 GLY B C   1 
ATOM   8659  O  O   . GLY B  2  450 ? 112.038 24.416  31.831  1.00 51.95  ?  450 GLY B O   1 
ATOM   8660  N  N   . CYS B  2  451 ? 111.725 26.415  32.878  1.00 41.21  ?  451 CYS B N   1 
ATOM   8661  C  CA  . CYS B  2  451 ? 112.116 27.279  31.735  1.00 58.04  ?  451 CYS B CA  1 
ATOM   8662  C  C   . CYS B  2  451 ? 113.593 27.645  31.895  1.00 53.65  ?  451 CYS B C   1 
ATOM   8663  O  O   . CYS B  2  451 ? 114.317 26.892  32.542  1.00 57.33  ?  451 CYS B O   1 
ATOM   8664  C  CB  . CYS B  2  451 ? 111.266 28.545  31.795  1.00 54.72  ?  451 CYS B CB  1 
ATOM   8665  S  SG  . CYS B  2  451 ? 110.082 28.438  33.144  1.00 48.92  ?  451 CYS B SG  1 
ATOM   8666  N  N   . ASN B  2  452 ? 114.080 28.739  31.282  1.00 44.61  ?  452 ASN B N   1 
ATOM   8667  C  CA  . ASN B  2  452 ? 115.461 29.180  31.450  1.00 45.04  ?  452 ASN B CA  1 
ATOM   8668  C  C   . ASN B  2  452 ? 115.512 30.643  31.905  1.00 53.92  ?  452 ASN B C   1 
ATOM   8669  O  O   . ASN B  2  452 ? 114.746 31.462  31.395  1.00 71.27  ?  452 ASN B O   1 
ATOM   8670  C  CB  . ASN B  2  452 ? 116.215 29.226  30.124  1.00 55.33  ?  452 ASN B CB  1 
ATOM   8671  C  CG  . ASN B  2  452 ? 116.822 27.920  29.658  1.00 63.75  ?  452 ASN B CG  1 
ATOM   8672  O  OD1 . ASN B  2  452 ? 116.671 27.540  28.494  1.00 68.17  ?  452 ASN B OD1 1 
ATOM   8673  N  ND2 . ASN B  2  452 ? 117.555 27.211  30.518  1.00 76.66  ?  452 ASN B ND2 1 
ATOM   8674  N  N   . ASN B  2  453 ? 116.380 30.979  32.867  1.00 54.01  ?  453 ASN B N   1 
ATOM   8675  C  CA  . ASN B  2  453 ? 116.471 32.359  33.346  1.00 50.04  ?  453 ASN B CA  1 
ATOM   8676  C  C   . ASN B  2  453 ? 117.864 32.989  33.265  1.00 50.30  ?  453 ASN B C   1 
ATOM   8677  O  O   . ASN B  2  453 ? 118.819 32.348  33.697  1.00 61.76  ?  453 ASN B O   1 
ATOM   8678  C  CB  . ASN B  2  453 ? 116.021 32.253  34.805  1.00 47.84  ?  453 ASN B CB  1 
ATOM   8679  C  CG  . ASN B  2  453 ? 115.527 33.557  35.379  1.00 55.47  ?  453 ASN B CG  1 
ATOM   8680  O  OD1 . ASN B  2  453 ? 115.985 34.643  35.007  1.00 69.48  ?  453 ASN B OD1 1 
ATOM   8681  N  ND2 . ASN B  2  453 ? 114.579 33.490  36.305  1.00 46.64  ?  453 ASN B ND2 1 
ATOM   8682  N  N   . PRO B  2  454 ? 118.030 34.225  32.736  1.00 48.00  ?  454 PRO B N   1 
ATOM   8683  C  CA  . PRO B  2  454 ? 119.382 34.808  32.673  1.00 55.81  ?  454 PRO B CA  1 
ATOM   8684  C  C   . PRO B  2  454 ? 120.118 34.863  34.011  1.00 63.20  ?  454 PRO B C   1 
ATOM   8685  O  O   . PRO B  2  454 ? 121.343 34.982  34.016  1.00 80.20  ?  454 PRO B O   1 
ATOM   8686  C  CB  . PRO B  2  454 ? 119.148 36.212  32.115  1.00 40.14  ?  454 PRO B CB  1 
ATOM   8687  C  CG  . PRO B  2  454 ? 117.867 36.139  31.413  1.00 49.78  ?  454 PRO B CG  1 
ATOM   8688  C  CD  . PRO B  2  454 ? 117.030 35.141  32.155  1.00 51.57  ?  454 PRO B CD  1 
ATOM   8689  N  N   . LYS B  2  455 ? 119.404 34.748  35.134  1.00 49.47  ?  455 LYS B N   1 
ATOM   8690  C  CA  . LYS B  2  455 ? 120.059 34.759  36.474  1.00 55.69  ?  455 LYS B CA  1 
ATOM   8691  C  C   . LYS B  2  455 ? 120.925 33.506  36.635  1.00 55.11  ?  455 LYS B C   1 
ATOM   8692  O  O   . LYS B  2  455 ? 121.854 33.540  37.463  1.00 63.27  ?  455 LYS B O   1 
ATOM   8693  C  CB  . LYS B  2  455 ? 118.997 34.854  37.573  1.00 42.38  ?  455 LYS B CB  1 
ATOM   8694  C  CG  . LYS B  2  455 ? 117.858 35.819  37.275  1.00 68.54  ?  455 LYS B CG  1 
ATOM   8695  C  CD  . LYS B  2  455 ? 116.859 35.956  38.389  1.00 57.78  ?  455 LYS B CD  1 
ATOM   8696  C  CE  . LYS B  2  455 ? 116.174 37.301  38.322  1.00 63.25  ?  455 LYS B CE  1 
ATOM   8697  N  NZ  . LYS B  2  455 ? 114.884 37.310  39.051  1.00 52.55  ?  455 LYS B NZ  1 
ATOM   8698  N  N   . VAL B  2  456 ? 120.631 32.449  35.882  1.00 56.03  ?  456 VAL B N   1 
ATOM   8699  C  CA  . VAL B  2  456 ? 121.356 31.185  35.909  1.00 46.42  ?  456 VAL B CA  1 
ATOM   8700  C  C   . VAL B  2  456 ? 121.999 30.976  34.533  1.00 60.85  ?  456 VAL B C   1 
ATOM   8701  O  O   . VAL B  2  456 ? 121.428 31.392  33.521  1.00 64.78  ?  456 VAL B O   1 
ATOM   8702  C  CB  . VAL B  2  456 ? 120.389 30.018  36.228  1.00 42.99  ?  456 VAL B CB  1 
ATOM   8703  C  CG1 . VAL B  2  456 ? 121.155 28.722  36.454  1.00 57.48  ?  456 VAL B CG1 1 
ATOM   8704  C  CG2 . VAL B  2  456 ? 119.497 30.338  37.427  1.00 50.06  ?  456 VAL B CG2 1 
ATOM   8705  N  N   . VAL B  2  457 ? 123.178 30.318  34.488  1.00 67.18  ?  457 VAL B N   1 
ATOM   8706  C  CA  . VAL B  2  457 ? 123.881 30.039  33.228  1.00 47.75  ?  457 VAL B CA  1 
ATOM   8707  C  C   . VAL B  2  457 ? 123.014 29.069  32.435  1.00 60.44  ?  457 VAL B C   1 
ATOM   8708  O  O   . VAL B  2  457 ? 122.702 27.997  32.946  1.00 65.98  ?  457 VAL B O   1 
ATOM   8709  C  CB  . VAL B  2  457 ? 125.278 29.445  33.494  1.00 40.04  ?  457 VAL B CB  1 
ATOM   8710  C  CG1 . VAL B  2  457 ? 125.945 29.021  32.191  1.00 53.70  ?  457 VAL B CG1 1 
ATOM   8711  C  CG2 . VAL B  2  457 ? 126.150 30.434  34.252  1.00 42.00  ?  457 VAL B CG2 1 
ATOM   8712  N  N   . GLN B  2  458 ? 122.600 29.440  31.212  1.00 56.95  ?  458 GLN B N   1 
ATOM   8713  C  CA  . GLN B  2  458 ? 121.716 28.607  30.383  1.00 48.05  ?  458 GLN B CA  1 
ATOM   8714  C  C   . GLN B  2  458 ? 122.065 27.110  30.391  1.00 57.30  ?  458 GLN B C   1 
ATOM   8715  O  O   . GLN B  2  458 ? 123.198 26.734  30.087  1.00 54.55  ?  458 GLN B O   1 
ATOM   8716  C  CB  . GLN B  2  458 ? 121.681 29.129  28.935  1.00 55.43  ?  458 GLN B CB  1 
ATOM   8717  C  CG  . GLN B  2  458 ? 120.326 29.018  28.244  1.00 48.64  ?  458 GLN B CG  1 
ATOM   8718  C  CD  . GLN B  2  458 ? 120.245 27.927  27.212  1.00 63.19  ?  458 GLN B CD  1 
ATOM   8719  O  OE1 . GLN B  2  458 ? 121.251 27.389  26.730  1.00 66.99  ?  458 GLN B OE1 1 
ATOM   8720  N  NE2 . GLN B  2  458 ? 119.024 27.582  26.834  1.00 75.18  ?  458 GLN B NE2 1 
ATOM   8721  N  N   . ASP B  2  459 ? 121.078 26.270  30.780  1.00 58.03  ?  459 ASP B N   1 
ATOM   8722  C  CA  . ASP B  2  459 ? 121.179 24.809  30.863  1.00 52.00  ?  459 ASP B CA  1 
ATOM   8723  C  C   . ASP B  2  459 ? 122.105 24.276  31.976  1.00 57.04  ?  459 ASP B C   1 
ATOM   8724  O  O   . ASP B  2  459 ? 122.034 23.088  32.285  1.00 63.07  ?  459 ASP B O   1 
ATOM   8725  C  CB  . ASP B  2  459 ? 121.588 24.207  29.503  1.00 61.57  ?  459 ASP B CB  1 
ATOM   8726  C  CG  . ASP B  2  459 ? 120.447 24.045  28.518  1.00 68.11  ?  459 ASP B CG  1 
ATOM   8727  O  OD1 . ASP B  2  459 ? 119.387 24.691  28.720  1.00 52.11  ?  459 ASP B OD1 1 
ATOM   8728  O  OD2 . ASP B  2  459 ? 120.610 23.269  27.549  1.00 64.61  ?  459 ASP B OD2 1 
ATOM   8729  N  N   . SER B  2  460 ? 122.947 25.122  32.586  1.00 56.05  ?  460 SER B N   1 
ATOM   8730  C  CA  . SER B  2  460 ? 123.864 24.673  33.629  1.00 53.00  ?  460 SER B CA  1 
ATOM   8731  C  C   . SER B  2  460 ? 123.167 23.946  34.793  1.00 58.46  ?  460 SER B C   1 
ATOM   8732  O  O   . SER B  2  460 ? 123.520 22.802  35.095  1.00 58.73  ?  460 SER B O   1 
ATOM   8733  C  CB  . SER B  2  460 ? 124.681 25.844  34.161  1.00 41.55  ?  460 SER B CB  1 
ATOM   8734  O  OG  . SER B  2  460 ? 125.752 25.382  34.965  1.00 82.32  ?  460 SER B OG  1 
ATOM   8735  N  N   . ALA B  2  461 ? 122.189 24.593  35.447  1.00 53.26  ?  461 ALA B N   1 
ATOM   8736  C  CA  . ALA B  2  461 ? 121.500 23.965  36.574  1.00 53.45  ?  461 ALA B CA  1 
ATOM   8737  C  C   . ALA B  2  461 ? 120.715 22.735  36.146  1.00 54.72  ?  461 ALA B C   1 
ATOM   8738  O  O   . ALA B  2  461 ? 120.706 21.750  36.878  1.00 61.42  ?  461 ALA B O   1 
ATOM   8739  C  CB  . ALA B  2  461 ? 120.581 24.958  37.255  1.00 61.45  ?  461 ALA B CB  1 
ATOM   8740  N  N   . HIS B  2  462 ? 120.062 22.775  34.967  1.00 56.16  ?  462 HIS B N   1 
ATOM   8741  C  CA  . HIS B  2  462 ? 119.289 21.634  34.469  1.00 45.36  ?  462 HIS B CA  1 
ATOM   8742  C  C   . HIS B  2  462 ? 120.173 20.393  34.341  1.00 56.11  ?  462 HIS B C   1 
ATOM   8743  O  O   . HIS B  2  462 ? 119.844 19.343  34.884  1.00 49.86  ?  462 HIS B O   1 
ATOM   8744  C  CB  . HIS B  2  462 ? 118.666 21.939  33.091  1.00 46.57  ?  462 HIS B CB  1 
ATOM   8745  C  CG  . HIS B  2  462 ? 117.501 22.875  33.118  1.00 45.53  ?  462 HIS B CG  1 
ATOM   8746  N  ND1 . HIS B  2  462 ? 116.441 22.681  33.976  1.00 62.98  ?  462 HIS B ND1 1 
ATOM   8747  C  CD2 . HIS B  2  462 ? 117.256 23.968  32.360  1.00 56.44  ?  462 HIS B CD2 1 
ATOM   8748  C  CE1 . HIS B  2  462 ? 115.592 23.666  33.729  1.00 69.42  ?  462 HIS B CE1 1 
ATOM   8749  N  NE2 . HIS B  2  462 ? 116.042 24.465  32.762  1.00 52.64  ?  462 HIS B NE2 1 
ATOM   8750  N  N   . ILE B  2  463 ? 121.302 20.521  33.639  1.00 56.02  ?  463 ILE B N   1 
ATOM   8751  C  CA  . ILE B  2  463 ? 122.203 19.399  33.420  1.00 46.43  ?  463 ILE B CA  1 
ATOM   8752  C  C   . ILE B  2  463 ? 122.866 18.940  34.725  1.00 54.37  ?  463 ILE B C   1 
ATOM   8753  O  O   . ILE B  2  463 ? 122.914 17.736  34.987  1.00 56.68  ?  463 ILE B O   1 
ATOM   8754  C  CB  . ILE B  2  463 ? 123.234 19.756  32.318  1.00 36.12  ?  463 ILE B CB  1 
ATOM   8755  C  CG1 . ILE B  2  463 ? 122.540 20.134  30.987  1.00 42.88  ?  463 ILE B CG1 1 
ATOM   8756  C  CG2 . ILE B  2  463 ? 124.230 18.626  32.105  1.00 52.11  ?  463 ILE B CG2 1 
ATOM   8757  C  CD1 . ILE B  2  463 ? 121.507 19.145  30.438  1.00 45.37  ?  463 ILE B CD1 1 
ATOM   8758  N  N   . GLU B  2  464 ? 123.363 19.878  35.554  1.00 47.79  ?  464 GLU B N   1 
ATOM   8759  C  CA  . GLU B  2  464 ? 124.011 19.491  36.812  1.00 49.29  ?  464 GLU B CA  1 
ATOM   8760  C  C   . GLU B  2  464 ? 123.049 18.802  37.778  1.00 50.68  ?  464 GLU B C   1 
ATOM   8761  O  O   . GLU B  2  464 ? 123.461 17.896  38.496  1.00 57.33  ?  464 GLU B O   1 
ATOM   8762  C  CB  . GLU B  2  464 ? 124.687 20.692  37.491  1.00 46.50  ?  464 GLU B CB  1 
ATOM   8763  C  CG  . GLU B  2  464 ? 125.955 21.154  36.796  1.00 63.33  ?  464 GLU B CG  1 
ATOM   8764  C  CD  . GLU B  2  464 ? 126.990 20.064  36.593  1.00 81.80  ?  464 GLU B CD  1 
ATOM   8765  O  OE1 . GLU B  2  464 ? 127.366 19.411  37.593  1.00 88.20  ?  464 GLU B OE1 1 
ATOM   8766  O  OE2 . GLU B  2  464 ? 127.417 19.856  35.433  1.00 91.07  ?  464 GLU B OE2 1 
ATOM   8767  N  N   . THR B  2  465 ? 121.778 19.210  37.796  1.00 45.30  ?  465 THR B N   1 
ATOM   8768  C  CA  . THR B  2  465 ? 120.794 18.596  38.680  1.00 43.01  ?  465 THR B CA  1 
ATOM   8769  C  C   . THR B  2  465 ? 120.442 17.198  38.173  1.00 53.63  ?  465 THR B C   1 
ATOM   8770  O  O   . THR B  2  465 ? 120.479 16.248  38.952  1.00 56.56  ?  465 THR B O   1 
ATOM   8771  C  CB  . THR B  2  465 ? 119.537 19.478  38.762  1.00 46.37  ?  465 THR B CB  1 
ATOM   8772  O  OG1 . THR B  2  465 ? 119.895 20.767  39.260  1.00 52.89  ?  465 THR B OG1 1 
ATOM   8773  C  CG2 . THR B  2  465 ? 118.445 18.872  39.631  1.00 41.61  ?  465 THR B CG2 1 
ATOM   8774  N  N   . ILE B  2  466 ? 120.103 17.068  36.872  1.00 55.30  ?  466 ILE B N   1 
ATOM   8775  C  CA  . ILE B  2  466 ? 119.711 15.783  36.291  1.00 46.92  ?  466 ILE B CA  1 
ATOM   8776  C  C   . ILE B  2  466 ? 120.844 14.777  36.424  1.00 49.55  ?  466 ILE B C   1 
ATOM   8777  O  O   . ILE B  2  466 ? 120.621 13.658  36.883  1.00 50.49  ?  466 ILE B O   1 
ATOM   8778  C  CB  . ILE B  2  466 ? 119.260 15.916  34.810  1.00 38.21  ?  466 ILE B CB  1 
ATOM   8779  C  CG1 . ILE B  2  466 ? 118.003 16.810  34.673  1.00 43.19  ?  466 ILE B CG1 1 
ATOM   8780  C  CG2 . ILE B  2  466 ? 119.001 14.532  34.218  1.00 35.21  ?  466 ILE B CG2 1 
ATOM   8781  C  CD1 . ILE B  2  466 ? 117.733 17.357  33.243  1.00 31.16  ?  466 ILE B CD1 1 
ATOM   8782  N  N   . LYS B  2  467 ? 122.065 15.171  36.033  1.00 48.17  ?  467 LYS B N   1 
ATOM   8783  C  CA  . LYS B  2  467 ? 123.224 14.282  36.110  1.00 47.89  ?  467 LYS B CA  1 
ATOM   8784  C  C   . LYS B  2  467 ? 123.454 13.788  37.535  1.00 50.94  ?  467 LYS B C   1 
ATOM   8785  O  O   . LYS B  2  467 ? 123.735 12.609  37.737  1.00 58.99  ?  467 LYS B O   1 
ATOM   8786  C  CB  . LYS B  2  467 ? 124.492 14.983  35.587  1.00 39.42  ?  467 LYS B CB  1 
ATOM   8787  C  CG  . LYS B  2  467 ? 124.617 14.980  34.068  1.00 41.21  ?  467 LYS B CG  1 
ATOM   8788  C  CD  . LYS B  2  467 ? 125.730 15.895  33.580  1.00 46.75  ?  467 LYS B CD  1 
ATOM   8789  C  CE  . LYS B  2  467 ? 127.094 15.249  33.578  1.00 51.16  ?  467 LYS B CE  1 
ATOM   8790  N  NZ  . LYS B  2  467 ? 128.171 16.240  33.316  1.00 46.43  ?  467 LYS B NZ  1 
ATOM   8791  N  N   . GLY B  2  468 ? 123.324 14.683  38.502  1.00 46.07  ?  468 GLY B N   1 
ATOM   8792  C  CA  . GLY B  2  468 ? 123.521 14.337  39.902  1.00 49.94  ?  468 GLY B CA  1 
ATOM   8793  C  C   . GLY B  2  468 ? 122.469 13.397  40.453  1.00 42.75  ?  468 GLY B C   1 
ATOM   8794  O  O   . GLY B  2  468 ? 122.788 12.528  41.261  1.00 47.74  ?  468 GLY B O   1 
ATOM   8795  N  N   . LEU B  2  469 ? 121.210 13.556  40.034  1.00 44.34  ?  469 LEU B N   1 
ATOM   8796  C  CA  . LEU B  2  469 ? 120.134 12.694  40.516  1.00 45.83  ?  469 LEU B CA  1 
ATOM   8797  C  C   . LEU B  2  469 ? 120.256 11.286  39.940  1.00 52.49  ?  469 LEU B C   1 
ATOM   8798  O  O   . LEU B  2  469 ? 120.076 10.320  40.675  1.00 48.56  ?  469 LEU B O   1 
ATOM   8799  C  CB  . LEU B  2  469 ? 118.767 13.287  40.161  1.00 40.36  ?  469 LEU B CB  1 
ATOM   8800  C  CG  . LEU B  2  469 ? 118.399 14.588  40.874  1.00 47.00  ?  469 LEU B CG  1 
ATOM   8801  C  CD1 . LEU B  2  469 ? 117.348 15.349  40.093  1.00 53.35  ?  469 LEU B CD1 1 
ATOM   8802  C  CD2 . LEU B  2  469 ? 117.911 14.327  42.295  1.00 47.70  ?  469 LEU B CD2 1 
ATOM   8803  N  N   . ILE B  2  470 ? 120.555 11.162  38.637  1.00 48.31  ?  470 ILE B N   1 
ATOM   8804  C  CA  . ILE B  2  470 ? 120.691 9.841   38.019  1.00 43.16  ?  470 ILE B CA  1 
ATOM   8805  C  C   . ILE B  2  470 ? 121.919 9.106   38.577  1.00 49.98  ?  470 ILE B C   1 
ATOM   8806  O  O   . ILE B  2  470 ? 121.866 7.889   38.748  1.00 60.42  ?  470 ILE B O   1 
ATOM   8807  C  CB  . ILE B  2  470 ? 120.652 9.873   36.458  1.00 36.02  ?  470 ILE B CB  1 
ATOM   8808  C  CG1 . ILE B  2  470 ? 121.722 10.798  35.858  1.00 45.99  ?  470 ILE B CG1 1 
ATOM   8809  C  CG2 . ILE B  2  470 ? 119.261 10.271  35.964  1.00 43.17  ?  470 ILE B CG2 1 
ATOM   8810  C  CD1 . ILE B  2  470 ? 121.935 10.606  34.375  1.00 46.34  ?  470 ILE B CD1 1 
ATOM   8811  N  N   . LYS B  2  471 ? 123.001 9.827   38.875  1.00 45.36  ?  471 LYS B N   1 
ATOM   8812  C  CA  . LYS B  2  471 ? 124.184 9.157   39.482  1.00 46.57  ?  471 LYS B CA  1 
ATOM   8813  C  C   . LYS B  2  471 ? 123.790 8.526   40.821  1.00 51.15  ?  471 LYS B C   1 
ATOM   8814  O  O   . LYS B  2  471 ? 124.280 7.421   41.114  1.00 65.84  ?  471 LYS B O   1 
ATOM   8815  C  CB  . LYS B  2  471 ? 125.350 10.131  39.669  1.00 41.03  ?  471 LYS B CB  1 
ATOM   8816  C  CG  . LYS B  2  471 ? 126.715 9.465   39.802  1.00 59.22  ?  471 LYS B CG  1 
ATOM   8817  C  CD  . LYS B  2  471 ? 127.243 8.858   38.524  1.00 101.04 ?  471 LYS B CD  1 
ATOM   8818  C  CE  . LYS B  2  471 ? 128.653 8.332   38.684  1.00 70.38  ?  471 LYS B CE  1 
ATOM   8819  N  NZ  . LYS B  2  471 ? 128.960 7.279   37.687  1.00 63.95  ?  471 LYS B NZ  1 
ATOM   8820  N  N   . ASN B  2  472 ? 122.944 9.204   41.600  1.00 48.75  ?  472 ASN B N   1 
ATOM   8821  C  CA  . ASN B  2  472 ? 122.545 8.692   42.906  1.00 48.61  ?  472 ASN B CA  1 
ATOM   8822  C  C   . ASN B  2  472 ? 121.346 7.735   42.783  1.00 49.67  ?  472 ASN B C   1 
ATOM   8823  O  O   . ASN B  2  472 ? 120.520 7.670   43.690  1.00 66.23  ?  472 ASN B O   1 
ATOM   8824  C  CB  . ASN B  2  472 ? 122.210 9.855   43.845  1.00 45.63  ?  472 ASN B CB  1 
ATOM   8825  C  CG  . ASN B  2  472 ? 123.437 10.560  44.362  1.00 42.05  ?  472 ASN B CG  1 
ATOM   8826  O  OD1 . ASN B  2  472 ? 123.883 10.327  45.486  1.00 61.26  ?  472 ASN B OD1 1 
ATOM   8827  N  ND2 . ASN B  2  472 ? 124.024 11.429  43.560  1.00 49.62  ?  472 ASN B ND2 1 
ATOM   8828  N  N   . ASP B  2  473 ? 121.265 6.973   41.681  1.00 45.09  ?  473 ASP B N   1 
ATOM   8829  C  CA  . ASP B  2  473 ? 120.194 6.002   41.440  1.00 48.49  ?  473 ASP B CA  1 
ATOM   8830  C  C   . ASP B  2  473 ? 118.755 6.538   41.584  1.00 49.95  ?  473 ASP B C   1 
ATOM   8831  O  O   . ASP B  2  473 ? 117.875 5.800   42.018  1.00 56.52  ?  473 ASP B O   1 
ATOM   8832  C  CB  . ASP B  2  473 ? 120.413 4.775   42.345  1.00 54.02  ?  473 ASP B CB  1 
ATOM   8833  C  CG  . ASP B  2  473 ? 121.499 3.839   41.863  1.00 65.20  ?  473 ASP B CG  1 
ATOM   8834  O  OD1 . ASP B  2  473 ? 121.784 3.837   40.647  1.00 58.86  ?  473 ASP B OD1 1 
ATOM   8835  O  OD2 . ASP B  2  473 ? 122.045 3.082   42.695  1.00 69.42  ?  473 ASP B OD2 1 
ATOM   8836  N  N   . VAL B  2  474 ? 118.509 7.797   41.193  1.00 43.46  ?  474 VAL B N   1 
ATOM   8837  C  CA  . VAL B  2  474 ? 117.171 8.392   41.242  1.00 37.44  ?  474 VAL B CA  1 
ATOM   8838  C  C   . VAL B  2  474 ? 116.704 8.562   39.794  1.00 44.43  ?  474 VAL B C   1 
ATOM   8839  O  O   . VAL B  2  474 ? 117.266 9.389   39.085  1.00 57.58  ?  474 VAL B O   1 
ATOM   8840  C  CB  . VAL B  2  474 ? 117.181 9.753   41.977  1.00 44.35  ?  474 VAL B CB  1 
ATOM   8841  C  CG1 . VAL B  2  474 ? 115.785 10.370  42.009  1.00 41.98  ?  474 VAL B CG1 1 
ATOM   8842  C  CG2 . VAL B  2  474 ? 117.735 9.605   43.388  1.00 56.22  ?  474 VAL B CG2 1 
ATOM   8843  N  N   . ILE B  2  475 ? 115.701 7.783   39.335  1.00 40.22  ?  475 ILE B N   1 
ATOM   8844  C  CA  . ILE B  2  475 ? 115.221 7.912   37.952  1.00 38.53  ?  475 ILE B CA  1 
ATOM   8845  C  C   . ILE B  2  475 ? 114.672 9.324   37.746  1.00 48.86  ?  475 ILE B C   1 
ATOM   8846  O  O   . ILE B  2  475 ? 113.974 9.844   38.618  1.00 46.05  ?  475 ILE B O   1 
ATOM   8847  C  CB  . ILE B  2  475 ? 114.210 6.802   37.535  1.00 44.27  ?  475 ILE B CB  1 
ATOM   8848  C  CG1 . ILE B  2  475 ? 113.919 6.895   36.015  1.00 40.77  ?  475 ILE B CG1 1 
ATOM   8849  C  CG2 . ILE B  2  475 ? 112.915 6.875   38.351  1.00 28.56  ?  475 ILE B CG2 1 
ATOM   8850  C  CD1 . ILE B  2  475 ? 113.372 5.669   35.397  1.00 31.93  ?  475 ILE B CD1 1 
ATOM   8851  N  N   . VAL B  2  476 ? 115.029 9.966   36.621  1.00 45.80  ?  476 VAL B N   1 
ATOM   8852  C  CA  . VAL B  2  476 ? 114.598 11.339  36.361  1.00 44.57  ?  476 VAL B CA  1 
ATOM   8853  C  C   . VAL B  2  476 ? 113.639 11.418  35.185  1.00 47.04  ?  476 VAL B C   1 
ATOM   8854  O  O   . VAL B  2  476 ? 113.888 10.830  34.136  1.00 44.96  ?  476 VAL B O   1 
ATOM   8855  C  CB  . VAL B  2  476 ? 115.813 12.287  36.137  1.00 37.10  ?  476 VAL B CB  1 
ATOM   8856  C  CG1 . VAL B  2  476 ? 115.352 13.697  35.789  1.00 28.38  ?  476 VAL B CG1 1 
ATOM   8857  C  CG2 . VAL B  2  476 ? 116.721 12.317  37.362  1.00 41.68  ?  476 VAL B CG2 1 
ATOM   8858  N  N   . VAL B  2  477 ? 112.548 12.164  35.365  1.00 38.58  ?  477 VAL B N   1 
ATOM   8859  C  CA  . VAL B  2  477 ? 111.564 12.398  34.321  1.00 33.64  ?  477 VAL B CA  1 
ATOM   8860  C  C   . VAL B  2  477 ? 111.651 13.898  34.035  1.00 39.98  ?  477 VAL B C   1 
ATOM   8861  O  O   . VAL B  2  477 ? 111.838 14.677  34.967  1.00 43.77  ?  477 VAL B O   1 
ATOM   8862  C  CB  . VAL B  2  477 ? 110.138 11.940  34.703  1.00 36.62  ?  477 VAL B CB  1 
ATOM   8863  C  CG1 . VAL B  2  477 ? 110.093 10.443  34.958  1.00 32.73  ?  477 VAL B CG1 1 
ATOM   8864  C  CG2 . VAL B  2  477 ? 109.591 12.705  35.901  1.00 45.13  ?  477 VAL B CG2 1 
ATOM   8865  N  N   . VAL B  2  478 ? 111.565 14.306  32.757  1.00 45.07  ?  478 VAL B N   1 
ATOM   8866  C  CA  . VAL B  2  478 ? 111.696 15.717  32.374  1.00 36.86  ?  478 VAL B CA  1 
ATOM   8867  C  C   . VAL B  2  478 ? 110.598 16.179  31.428  1.00 47.70  ?  478 VAL B C   1 
ATOM   8868  O  O   . VAL B  2  478 ? 110.018 15.367  30.708  1.00 53.27  ?  478 VAL B O   1 
ATOM   8869  C  CB  . VAL B  2  478 ? 113.083 15.996  31.738  1.00 33.28  ?  478 VAL B CB  1 
ATOM   8870  C  CG1 . VAL B  2  478 ? 114.197 15.839  32.752  1.00 37.06  ?  478 VAL B CG1 1 
ATOM   8871  C  CG2 . VAL B  2  478 ? 113.337 15.096  30.531  1.00 41.67  ?  478 VAL B CG2 1 
ATOM   8872  N  N   . THR B  2  479 ? 110.329 17.500  31.428  1.00 37.63  ?  479 THR B N   1 
ATOM   8873  C  CA  . THR B  2  479 ? 109.328 18.138  30.563  1.00 51.47  ?  479 THR B CA  1 
ATOM   8874  C  C   . THR B  2  479 ? 109.745 19.588  30.256  1.00 54.21  ?  479 THR B C   1 
ATOM   8875  O  O   . THR B  2  479 ? 110.560 20.156  30.980  1.00 66.29  ?  479 THR B O   1 
ATOM   8876  C  CB  . THR B  2  479 ? 107.940 18.161  31.230  1.00 47.88  ?  479 THR B CB  1 
ATOM   8877  O  OG1 . THR B  2  479 ? 108.007 18.994  32.396  1.00 52.98  ?  479 THR B OG1 1 
ATOM   8878  C  CG2 . THR B  2  479 ? 107.432 16.783  31.590  1.00 50.82  ?  479 THR B CG2 1 
ATOM   8879  N  N   . GLY B  2  480 ? 109.169 20.176  29.212  1.00 46.29  ?  480 GLY B N   1 
ATOM   8880  C  CA  . GLY B  2  480 ? 109.450 21.557  28.838  1.00 57.66  ?  480 GLY B CA  1 
ATOM   8881  C  C   . GLY B  2  480 ? 110.896 21.835  28.486  1.00 52.07  ?  480 GLY B C   1 
ATOM   8882  O  O   . GLY B  2  480 ? 111.582 20.966  27.947  1.00 63.90  ?  480 GLY B O   1 
ATOM   8883  N  N   . CYS B  2  481 ? 111.373 23.054  28.782  1.00 47.18  ?  481 CYS B N   1 
ATOM   8884  C  CA  . CYS B  2  481 ? 112.749 23.443  28.476  1.00 50.71  ?  481 CYS B CA  1 
ATOM   8885  C  C   . CYS B  2  481 ? 113.782 22.601  29.204  1.00 49.05  ?  481 CYS B C   1 
ATOM   8886  O  O   . CYS B  2  481 ? 114.902 22.482  28.711  1.00 57.01  ?  481 CYS B O   1 
ATOM   8887  C  CB  . CYS B  2  481 ? 112.962 24.926  28.738  1.00 42.09  ?  481 CYS B CB  1 
ATOM   8888  S  SG  . CYS B  2  481 ? 111.999 26.009  27.653  1.00 53.16  ?  481 CYS B SG  1 
ATOM   8889  N  N   . ALA B  2  482 ? 113.432 22.019  30.364  1.00 46.52  ?  482 ALA B N   1 
ATOM   8890  C  CA  . ALA B  2  482 ? 114.365 21.162  31.089  1.00 43.04  ?  482 ALA B CA  1 
ATOM   8891  C  C   . ALA B  2  482 ? 114.582 19.890  30.264  1.00 53.89  ?  482 ALA B C   1 
ATOM   8892  O  O   . ALA B  2  482 ? 115.714 19.430  30.139  1.00 47.71  ?  482 ALA B O   1 
ATOM   8893  C  CB  . ALA B  2  482 ? 113.807 20.815  32.456  1.00 44.30  ?  482 ALA B CB  1 
ATOM   8894  N  N   . ALA B  2  483 ? 113.503 19.336  29.674  1.00 54.75  ?  483 ALA B N   1 
ATOM   8895  C  CA  . ALA B  2  483 ? 113.603 18.142  28.838  1.00 43.22  ?  483 ALA B CA  1 
ATOM   8896  C  C   . ALA B  2  483 ? 114.420 18.450  27.599  1.00 46.40  ?  483 ALA B C   1 
ATOM   8897  O  O   . ALA B  2  483 ? 115.254 17.641  27.205  1.00 54.21  ?  483 ALA B O   1 
ATOM   8898  C  CB  . ALA B  2  483 ? 112.219 17.653  28.438  1.00 40.90  ?  483 ALA B CB  1 
ATOM   8899  N  N   . GLN B  2  484 ? 114.203 19.622  26.990  1.00 51.40  ?  484 GLN B N   1 
ATOM   8900  C  CA  . GLN B  2  484 ? 114.951 20.022  25.801  1.00 46.40  ?  484 GLN B CA  1 
ATOM   8901  C  C   . GLN B  2  484 ? 116.428 20.221  26.153  1.00 50.30  ?  484 GLN B C   1 
ATOM   8902  O  O   . GLN B  2  484 ? 117.293 19.827  25.380  1.00 51.61  ?  484 GLN B O   1 
ATOM   8903  C  CB  . GLN B  2  484 ? 114.299 21.243  25.156  1.00 38.30  ?  484 GLN B CB  1 
ATOM   8904  C  CG  . GLN B  2  484 ? 112.939 20.907  24.565  1.00 40.21  ?  484 GLN B CG  1 
ATOM   8905  C  CD  . GLN B  2  484 ? 112.300 22.074  23.875  1.00 48.97  ?  484 GLN B CD  1 
ATOM   8906  O  OE1 . GLN B  2  484 ? 112.607 23.233  24.155  1.00 65.54  ?  484 GLN B OE1 1 
ATOM   8907  N  NE2 . GLN B  2  484 ? 111.380 21.801  22.964  1.00 53.36  ?  484 GLN B NE2 1 
ATOM   8908  N  N   . ALA B  2  485 ? 116.724 20.782  27.329  1.00 47.89  ?  485 ALA B N   1 
ATOM   8909  C  CA  . ALA B  2  485 ? 118.101 20.959  27.778  1.00 47.54  ?  485 ALA B CA  1 
ATOM   8910  C  C   . ALA B  2  485 ? 118.824 19.605  27.827  1.00 49.82  ?  485 ALA B C   1 
ATOM   8911  O  O   . ALA B  2  485 ? 119.968 19.498  27.396  1.00 49.43  ?  485 ALA B O   1 
ATOM   8912  C  CB  . ALA B  2  485 ? 118.117 21.606  29.158  1.00 54.68  ?  485 ALA B CB  1 
ATOM   8913  N  N   . ALA B  2  486 ? 118.143 18.574  28.350  1.00 56.85  ?  486 ALA B N   1 
ATOM   8914  C  CA  . ALA B  2  486 ? 118.687 17.222  28.456  1.00 45.41  ?  486 ALA B CA  1 
ATOM   8915  C  C   . ALA B  2  486 ? 118.827 16.584  27.078  1.00 51.64  ?  486 ALA B C   1 
ATOM   8916  O  O   . ALA B  2  486 ? 119.771 15.831  26.850  1.00 63.15  ?  486 ALA B O   1 
ATOM   8917  C  CB  . ALA B  2  486 ? 117.779 16.371  29.325  1.00 34.79  ?  486 ALA B CB  1 
ATOM   8918  N  N   . ALA B  2  487 ? 117.891 16.878  26.159  1.00 53.22  ?  487 ALA B N   1 
ATOM   8919  C  CA  . ALA B  2  487 ? 117.929 16.341  24.803  1.00 47.78  ?  487 ALA B CA  1 
ATOM   8920  C  C   . ALA B  2  487 ? 119.187 16.828  24.084  1.00 48.16  ?  487 ALA B C   1 
ATOM   8921  O  O   . ALA B  2  487 ? 119.857 16.030  23.426  1.00 51.02  ?  487 ALA B O   1 
ATOM   8922  C  CB  . ALA B  2  487 ? 116.687 16.778  24.034  1.00 31.39  ?  487 ALA B CB  1 
ATOM   8923  N  N   . LYS B  2  488 ? 119.519 18.128  24.245  1.00 42.95  ?  488 LYS B N   1 
ATOM   8924  C  CA  . LYS B  2  488 ? 120.681 18.769  23.619  1.00 44.52  ?  488 LYS B CA  1 
ATOM   8925  C  C   . LYS B  2  488 ? 121.998 18.234  24.163  1.00 46.54  ?  488 LYS B C   1 
ATOM   8926  O  O   . LYS B  2  488 ? 122.938 18.048  23.391  1.00 48.58  ?  488 LYS B O   1 
ATOM   8927  C  CB  . LYS B  2  488 ? 120.653 20.291  23.840  1.00 44.87  ?  488 LYS B CB  1 
ATOM   8928  C  CG  . LYS B  2  488 ? 119.412 21.002  23.306  1.00 41.72  ?  488 LYS B CG  1 
ATOM   8929  C  CD  . LYS B  2  488 ? 119.549 22.528  23.334  1.00 45.65  ?  488 LYS B CD  1 
ATOM   8930  C  CE  . LYS B  2  488 ? 119.429 23.125  24.721  1.00 55.30  ?  488 LYS B CE  1 
ATOM   8931  N  NZ  . LYS B  2  488 ? 119.781 24.574  24.755  1.00 51.04  ?  488 LYS B NZ  1 
ATOM   8932  N  N   . TYR B  2  489 ? 122.082 18.014  25.485  1.00 46.27  ?  489 TYR B N   1 
ATOM   8933  C  CA  . TYR B  2  489 ? 123.303 17.521  26.125  1.00 44.52  ?  489 TYR B CA  1 
ATOM   8934  C  C   . TYR B  2  489 ? 123.605 16.077  25.743  1.00 43.61  ?  489 TYR B C   1 
ATOM   8935  O  O   . TYR B  2  489 ? 124.768 15.717  25.594  1.00 44.63  ?  489 TYR B O   1 
ATOM   8936  C  CB  . TYR B  2  489 ? 123.196 17.653  27.649  1.00 48.64  ?  489 TYR B CB  1 
ATOM   8937  C  CG  . TYR B  2  489 ? 124.486 17.343  28.377  1.00 45.66  ?  489 TYR B CG  1 
ATOM   8938  C  CD1 . TYR B  2  489 ? 125.474 18.304  28.522  1.00 46.11  ?  489 TYR B CD1 1 
ATOM   8939  C  CD2 . TYR B  2  489 ? 124.708 16.096  28.940  1.00 54.79  ?  489 TYR B CD2 1 
ATOM   8940  C  CE1 . TYR B  2  489 ? 126.657 18.027  29.195  1.00 55.68  ?  489 TYR B CE1 1 
ATOM   8941  C  CE2 . TYR B  2  489 ? 125.888 15.805  29.611  1.00 63.75  ?  489 TYR B CE2 1 
ATOM   8942  C  CZ  . TYR B  2  489 ? 126.863 16.773  29.739  1.00 59.41  ?  489 TYR B CZ  1 
ATOM   8943  O  OH  . TYR B  2  489 ? 128.025 16.469  30.413  1.00 60.01  ?  489 TYR B OH  1 
ATOM   8944  N  N   . GLY B  2  490 ? 122.561 15.270  25.604  1.00 44.92  ?  490 GLY B N   1 
ATOM   8945  C  CA  . GLY B  2  490 ? 122.689 13.869  25.231  1.00 43.10  ?  490 GLY B CA  1 
ATOM   8946  C  C   . GLY B  2  490 ? 122.293 12.894  26.316  1.00 49.49  ?  490 GLY B C   1 
ATOM   8947  O  O   . GLY B  2  490 ? 122.700 11.729  26.268  1.00 59.41  ?  490 GLY B O   1 
ATOM   8948  N  N   . LEU B  2  491 ? 121.495 13.340  27.296  1.00 40.60  ?  491 LEU B N   1 
ATOM   8949  C  CA  . LEU B  2  491 ? 121.065 12.459  28.380  1.00 39.03  ?  491 LEU B CA  1 
ATOM   8950  C  C   . LEU B  2  491 ? 119.831 11.638  27.995  1.00 47.25  ?  491 LEU B C   1 
ATOM   8951  O  O   . LEU B  2  491 ? 119.564 10.625  28.637  1.00 62.48  ?  491 LEU B O   1 
ATOM   8952  C  CB  . LEU B  2  491 ? 120.764 13.248  29.663  1.00 50.07  ?  491 LEU B CB  1 
ATOM   8953  C  CG  . LEU B  2  491 ? 121.796 14.265  30.125  1.00 43.96  ?  491 LEU B CG  1 
ATOM   8954  C  CD1 . LEU B  2  491 ? 121.271 15.058  31.294  1.00 44.79  ?  491 LEU B CD1 1 
ATOM   8955  C  CD2 . LEU B  2  491 ? 123.099 13.592  30.506  1.00 43.62  ?  491 LEU B CD2 1 
ATOM   8956  N  N   . LEU B  2  492 ? 119.077 12.058  26.966  1.00 52.26  ?  492 LEU B N   1 
ATOM   8957  C  CA  . LEU B  2  492 ? 117.882 11.335  26.523  1.00 44.04  ?  492 LEU B CA  1 
ATOM   8958  C  C   . LEU B  2  492 ? 118.278 10.219  25.547  1.00 47.27  ?  492 LEU B C   1 
ATOM   8959  O  O   . LEU B  2  492 ? 117.640 10.037  24.512  1.00 54.12  ?  492 LEU B O   1 
ATOM   8960  C  CB  . LEU B  2  492 ? 116.904 12.316  25.838  1.00 48.33  ?  492 LEU B CB  1 
ATOM   8961  C  CG  . LEU B  2  492 ? 115.800 12.952  26.683  1.00 47.62  ?  492 LEU B CG  1 
ATOM   8962  C  CD1 . LEU B  2  492 ? 116.328 13.517  27.993  1.00 47.73  ?  492 LEU B CD1 1 
ATOM   8963  C  CD2 . LEU B  2  492 ? 115.096 14.022  25.891  1.00 35.90  ?  492 LEU B CD2 1 
ATOM   8964  N  N   . GLN B  2  493 ? 119.330 9.467   25.875  1.00 43.27  ?  493 GLN B N   1 
ATOM   8965  C  CA  . GLN B  2  493 ? 119.813 8.378   25.034  1.00 48.60  ?  493 GLN B CA  1 
ATOM   8966  C  C   . GLN B  2  493 ? 119.963 7.136   25.870  1.00 46.69  ?  493 GLN B C   1 
ATOM   8967  O  O   . GLN B  2  493 ? 120.182 7.230   27.079  1.00 48.31  ?  493 GLN B O   1 
ATOM   8968  C  CB  . GLN B  2  493 ? 121.193 8.722   24.453  1.00 49.22  ?  493 GLN B CB  1 
ATOM   8969  C  CG  . GLN B  2  493 ? 121.183 9.827   23.412  1.00 50.69  ?  493 GLN B CG  1 
ATOM   8970  C  CD  . GLN B  2  493 ? 122.573 10.232  22.985  1.00 43.95  ?  493 GLN B CD  1 
ATOM   8971  O  OE1 . GLN B  2  493 ? 123.586 9.812   23.555  1.00 58.01  ?  493 GLN B OE1 1 
ATOM   8972  N  NE2 . GLN B  2  493 ? 122.651 11.069  21.964  1.00 63.52  ?  493 GLN B NE2 1 
ATOM   8973  N  N   . LYS B  2  494 ? 119.892 5.964   25.235  1.00 51.10  ?  494 LYS B N   1 
ATOM   8974  C  CA  . LYS B  2  494 ? 120.080 4.711   25.959  1.00 50.16  ?  494 LYS B CA  1 
ATOM   8975  C  C   . LYS B  2  494 ? 121.540 4.632   26.457  1.00 50.75  ?  494 LYS B C   1 
ATOM   8976  O  O   . LYS B  2  494 ? 121.799 4.155   27.561  1.00 54.50  ?  494 LYS B O   1 
ATOM   8977  C  CB  . LYS B  2  494 ? 119.708 3.521   25.069  1.00 41.48  ?  494 LYS B CB  1 
ATOM   8978  C  CG  . LYS B  2  494 ? 118.236 3.536   24.669  1.00 40.39  ?  494 LYS B CG  1 
ATOM   8979  C  CD  . LYS B  2  494 ? 117.682 2.147   24.398  1.00 47.55  ?  494 LYS B CD  1 
ATOM   8980  C  CE  . LYS B  2  494 ? 116.191 2.151   24.151  1.00 49.26  ?  494 LYS B CE  1 
ATOM   8981  N  NZ  . LYS B  2  494 ? 115.826 1.424   22.909  1.00 67.42  ?  494 LYS B NZ  1 
ATOM   8982  N  N   . GLU B  2  495 ? 122.476 5.161   25.656  1.00 48.82  ?  495 GLU B N   1 
ATOM   8983  C  CA  . GLU B  2  495 ? 123.904 5.193   25.963  1.00 50.76  ?  495 GLU B CA  1 
ATOM   8984  C  C   . GLU B  2  495 ? 124.225 6.015   27.219  1.00 52.38  ?  495 GLU B C   1 
ATOM   8985  O  O   . GLU B  2  495 ? 125.298 5.841   27.790  1.00 55.17  ?  495 GLU B O   1 
ATOM   8986  C  CB  . GLU B  2  495 ? 124.683 5.787   24.772  1.00 45.10  ?  495 GLU B CB  1 
ATOM   8987  C  CG  . GLU B  2  495 ? 124.643 4.939   23.512  1.00 64.98  ?  495 GLU B CG  1 
ATOM   8988  C  CD  . GLU B  2  495 ? 123.378 5.038   22.683  1.00 79.49  ?  495 GLU B CD  1 
ATOM   8989  O  OE1 . GLU B  2  495 ? 122.695 6.087   22.753  1.00 79.20  ?  495 GLU B OE1 1 
ATOM   8990  O  OE2 . GLU B  2  495 ? 123.066 4.061   21.963  1.00 77.47  ?  495 GLU B OE2 1 
ATOM   8991  N  N   . ALA B  2  496 ? 123.330 6.920   27.637  1.00 44.65  ?  496 ALA B N   1 
ATOM   8992  C  CA  . ALA B  2  496 ? 123.581 7.762   28.803  1.00 51.94  ?  496 ALA B CA  1 
ATOM   8993  C  C   . ALA B  2  496 ? 123.510 7.004   30.132  1.00 53.09  ?  496 ALA B C   1 
ATOM   8994  O  O   . ALA B  2  496 ? 124.052 7.486   31.125  1.00 61.57  ?  496 ALA B O   1 
ATOM   8995  C  CB  . ALA B  2  496 ? 122.612 8.933   28.817  1.00 52.35  ?  496 ALA B CB  1 
ATOM   8996  N  N   . ALA B  2  497 ? 122.861 5.831   30.164  1.00 57.49  ?  497 ALA B N   1 
ATOM   8997  C  CA  . ALA B  2  497 ? 122.743 5.056   31.397  1.00 47.39  ?  497 ALA B CA  1 
ATOM   8998  C  C   . ALA B  2  497 ? 124.103 4.560   31.885  1.00 46.06  ?  497 ALA B C   1 
ATOM   8999  O  O   . ALA B  2  497 ? 124.409 4.707   33.066  1.00 52.69  ?  497 ALA B O   1 
ATOM   9000  C  CB  . ALA B  2  497 ? 121.795 3.885   31.189  1.00 58.61  ?  497 ALA B CB  1 
ATOM   9001  N  N   . GLU B  2  498 ? 124.923 3.987   30.995  1.00 42.04  ?  498 GLU B N   1 
ATOM   9002  C  CA  . GLU B  2  498 ? 126.238 3.507   31.405  1.00 52.46  ?  498 GLU B CA  1 
ATOM   9003  C  C   . GLU B  2  498 ? 127.180 4.663   31.683  1.00 49.37  ?  498 GLU B C   1 
ATOM   9004  O  O   . GLU B  2  498 ? 128.026 4.547   32.562  1.00 72.17  ?  498 GLU B O   1 
ATOM   9005  C  CB  . GLU B  2  498 ? 126.853 2.580   30.346  1.00 49.63  ?  498 GLU B CB  1 
ATOM   9006  C  CG  . GLU B  2  498 ? 126.240 1.190   30.321  1.00 84.66  ?  498 GLU B CG  1 
ATOM   9007  C  CD  . GLU B  2  498 ? 126.352 0.416   31.623  1.00 109.00 ?  498 GLU B CD  1 
ATOM   9008  O  OE1 . GLU B  2  498 ? 127.495 0.149   32.061  1.00 116.74 ?  498 GLU B OE1 1 
ATOM   9009  O  OE2 . GLU B  2  498 ? 125.295 0.075   32.205  1.00 99.47  ?  498 GLU B OE2 1 
ATOM   9010  N  N   . LYS B  2  499 ? 127.038 5.778   30.963  1.00 45.03  ?  499 LYS B N   1 
ATOM   9011  C  CA  . LYS B  2  499 ? 127.922 6.920   31.145  1.00 49.91  ?  499 LYS B CA  1 
ATOM   9012  C  C   . LYS B  2  499 ? 127.645 7.755   32.386  1.00 60.16  ?  499 LYS B C   1 
ATOM   9013  O  O   . LYS B  2  499 ? 128.601 8.237   32.995  1.00 58.52  ?  499 LYS B O   1 
ATOM   9014  C  CB  . LYS B  2  499 ? 127.845 7.858   29.935  1.00 61.39  ?  499 LYS B CB  1 
ATOM   9015  C  CG  . LYS B  2  499 ? 128.092 7.188   28.593  1.00 60.66  ?  499 LYS B CG  1 
ATOM   9016  C  CD  . LYS B  2  499 ? 128.624 8.160   27.530  1.00 88.73  ?  499 LYS B CD  1 
ATOM   9017  C  CE  . LYS B  2  499 ? 127.829 9.443   27.387  1.00 73.32  ?  499 LYS B CE  1 
ATOM   9018  N  NZ  . LYS B  2  499 ? 128.162 10.169  26.135  1.00 79.97  ?  499 LYS B NZ  1 
ATOM   9019  N  N   . TYR B  2  500 ? 126.363 7.980   32.745  1.00 48.83  ?  500 TYR B N   1 
ATOM   9020  C  CA  . TYR B  2  500 ? 126.028 8.858   33.871  1.00 50.37  ?  500 TYR B CA  1 
ATOM   9021  C  C   . TYR B  2  500 ? 125.158 8.298   35.005  1.00 57.30  ?  500 TYR B C   1 
ATOM   9022  O  O   . TYR B  2  500 ? 125.031 8.979   36.027  1.00 59.89  ?  500 TYR B O   1 
ATOM   9023  C  CB  . TYR B  2  500 ? 125.304 10.098  33.327  1.00 46.53  ?  500 TYR B CB  1 
ATOM   9024  C  CG  . TYR B  2  500 ? 126.006 10.807  32.191  1.00 53.24  ?  500 TYR B CG  1 
ATOM   9025  C  CD1 . TYR B  2  500 ? 127.047 11.693  32.438  1.00 56.38  ?  500 TYR B CD1 1 
ATOM   9026  C  CD2 . TYR B  2  500 ? 125.575 10.662  30.881  1.00 50.65  ?  500 TYR B CD2 1 
ATOM   9027  C  CE1 . TYR B  2  500 ? 127.667 12.384  31.405  1.00 56.15  ?  500 TYR B CE1 1 
ATOM   9028  C  CE2 . TYR B  2  500 ? 126.184 11.350  29.840  1.00 62.16  ?  500 TYR B CE2 1 
ATOM   9029  C  CZ  . TYR B  2  500 ? 127.238 12.206  30.104  1.00 62.22  ?  500 TYR B CZ  1 
ATOM   9030  O  OH  . TYR B  2  500 ? 127.847 12.896  29.080  1.00 60.40  ?  500 TYR B OH  1 
ATOM   9031  N  N   . ALA B  2  501 ? 124.522 7.126   34.841  1.00 48.76  ?  501 ALA B N   1 
ATOM   9032  C  CA  . ALA B  2  501 ? 123.643 6.595   35.889  1.00 48.15  ?  501 ALA B CA  1 
ATOM   9033  C  C   . ALA B  2  501 ? 124.349 5.692   36.905  1.00 58.10  ?  501 ALA B C   1 
ATOM   9034  O  O   . ALA B  2  501 ? 125.358 5.062   36.589  1.00 54.87  ?  501 ALA B O   1 
ATOM   9035  C  CB  . ALA B  2  501 ? 122.471 5.862   35.261  1.00 52.67  ?  501 ALA B CB  1 
ATOM   9036  N  N   . GLY B  2  502 ? 123.792 5.637   38.116  1.00 52.05  ?  502 GLY B N   1 
ATOM   9037  C  CA  . GLY B  2  502 ? 124.325 4.834   39.206  1.00 52.51  ?  502 GLY B CA  1 
ATOM   9038  C  C   . GLY B  2  502 ? 124.172 3.341   38.989  1.00 56.74  ?  502 GLY B C   1 
ATOM   9039  O  O   . GLY B  2  502 ? 123.688 2.915   37.941  1.00 63.03  ?  502 GLY B O   1 
ATOM   9040  N  N   . PRO B  2  503 ? 124.542 2.472   39.957  1.00 56.52  ?  503 PRO B N   1 
ATOM   9041  C  CA  . PRO B  2  503 ? 124.484 1.025   39.731  1.00 53.48  ?  503 PRO B CA  1 
ATOM   9042  C  C   . PRO B  2  503 ? 123.042 0.540   39.532  1.00 60.04  ?  503 PRO B C   1 
ATOM   9043  O  O   . PRO B  2  503 ? 122.796 -0.161  38.569  1.00 63.07  ?  503 PRO B O   1 
ATOM   9044  C  CB  . PRO B  2  503 ? 125.061 0.434   41.026  1.00 50.56  ?  503 PRO B CB  1 
ATOM   9045  C  CG  . PRO B  2  503 ? 124.832 1.508   42.064  1.00 77.25  ?  503 PRO B CG  1 
ATOM   9046  C  CD  . PRO B  2  503 ? 125.009 2.807   41.307  1.00 61.39  ?  503 PRO B CD  1 
ATOM   9047  N  N   . GLY B  2  504 ? 122.133 0.923   40.430  1.00 48.49  ?  504 GLY B N   1 
ATOM   9048  C  CA  . GLY B  2  504 ? 120.745 0.492   40.356  1.00 60.72  ?  504 GLY B CA  1 
ATOM   9049  C  C   . GLY B  2  504 ? 120.016 1.002   39.129  1.00 57.58  ?  504 GLY B C   1 
ATOM   9050  O  O   . GLY B  2  504 ? 119.373 0.222   38.425  1.00 58.35  ?  504 GLY B O   1 
ATOM   9051  N  N   . LEU B  2  505 ? 120.108 2.308   38.857  1.00 53.25  ?  505 LEU B N   1 
ATOM   9052  C  CA  . LEU B  2  505 ? 119.434 2.890   37.705  1.00 55.54  ?  505 LEU B CA  1 
ATOM   9053  C  C   . LEU B  2  505 ? 119.985 2.336   36.387  1.00 52.97  ?  505 LEU B C   1 
ATOM   9054  O  O   . LEU B  2  505 ? 119.200 2.050   35.488  1.00 57.24  ?  505 LEU B O   1 
ATOM   9055  C  CB  . LEU B  2  505 ? 119.514 4.423   37.753  1.00 48.49  ?  505 LEU B CB  1 
ATOM   9056  C  CG  . LEU B  2  505 ? 118.904 5.196   36.576  1.00 40.97  ?  505 LEU B CG  1 
ATOM   9057  C  CD1 . LEU B  2  505 ? 117.409 4.940   36.424  1.00 41.72  ?  505 LEU B CD1 1 
ATOM   9058  C  CD2 . LEU B  2  505 ? 119.107 6.666   36.767  1.00 46.92  ?  505 LEU B CD2 1 
ATOM   9059  N  N   . ALA B  2  506 ? 121.307 2.150   36.269  1.00 42.38  ?  506 ALA B N   1 
ATOM   9060  C  CA  . ALA B  2  506 ? 121.878 1.590   35.043  1.00 42.77  ?  506 ALA B CA  1 
ATOM   9061  C  C   . ALA B  2  506 ? 121.366 0.165   34.815  1.00 49.48  ?  506 ALA B C   1 
ATOM   9062  O  O   . ALA B  2  506 ? 121.190 -0.249  33.672  1.00 58.30  ?  506 ALA B O   1 
ATOM   9063  C  CB  . ALA B  2  506 ? 123.391 1.584   35.120  1.00 47.27  ?  506 ALA B CB  1 
ATOM   9064  N  N   . THR B  2  507 ? 121.135 -0.581  35.901  1.00 48.14  ?  507 THR B N   1 
ATOM   9065  C  CA  . THR B  2  507 ? 120.620 -1.946  35.836  1.00 50.13  ?  507 THR B CA  1 
ATOM   9066  C  C   . THR B  2  507 ? 119.173 -1.910  35.342  1.00 56.88  ?  507 THR B C   1 
ATOM   9067  O  O   . THR B  2  507 ? 118.814 -2.683  34.451  1.00 57.38  ?  507 THR B O   1 
ATOM   9068  C  CB  . THR B  2  507 ? 120.701 -2.609  37.222  1.00 48.03  ?  507 THR B CB  1 
ATOM   9069  O  OG1 . THR B  2  507 ? 122.073 -2.780  37.582  1.00 50.80  ?  507 THR B OG1 1 
ATOM   9070  C  CG2 . THR B  2  507 ? 119.973 -3.940  37.274  1.00 37.19  ?  507 THR B CG2 1 
ATOM   9071  N  N   . VAL B  2  508 ? 118.343 -1.008  35.916  1.00 49.67  ?  508 VAL B N   1 
ATOM   9072  C  CA  . VAL B  2  508 ? 116.937 -0.875  35.530  1.00 37.71  ?  508 VAL B CA  1 
ATOM   9073  C  C   . VAL B  2  508 ? 116.843 -0.448  34.068  1.00 45.72  ?  508 VAL B C   1 
ATOM   9074  O  O   . VAL B  2  508 ? 116.003 -0.963  33.337  1.00 49.67  ?  508 VAL B O   1 
ATOM   9075  C  CB  . VAL B  2  508 ? 116.180 0.098   36.466  1.00 37.28  ?  508 VAL B CB  1 
ATOM   9076  C  CG1 . VAL B  2  508 ? 114.804 0.445   35.908  1.00 34.23  ?  508 VAL B CG1 1 
ATOM   9077  C  CG2 . VAL B  2  508 ? 116.050 -0.485  37.868  1.00 45.19  ?  508 VAL B CG2 1 
ATOM   9078  N  N   . CYS B  2  509 ? 117.713 0.468   33.630  1.00 45.94  ?  509 CYS B N   1 
ATOM   9079  C  CA  . CYS B  2  509 ? 117.722 0.930   32.246  1.00 41.39  ?  509 CYS B CA  1 
ATOM   9080  C  C   . CYS B  2  509 ? 117.994 -0.226  31.298  1.00 45.23  ?  509 CYS B C   1 
ATOM   9081  O  O   . CYS B  2  509 ? 117.380 -0.304  30.242  1.00 53.24  ?  509 CYS B O   1 
ATOM   9082  C  CB  . CYS B  2  509 ? 118.750 2.040   32.059  1.00 48.66  ?  509 CYS B CB  1 
ATOM   9083  S  SG  . CYS B  2  509 ? 118.302 3.607   32.846  1.00 54.99  ?  509 CYS B SG  1 
ATOM   9084  N  N   . LYS B  2  510 ? 118.921 -1.117  31.665  1.00 49.01  ?  510 LYS B N   1 
ATOM   9085  C  CA  . LYS B  2  510 ? 119.273 -2.264  30.832  1.00 45.14  ?  510 LYS B CA  1 
ATOM   9086  C  C   . LYS B  2  510 ? 118.110 -3.250  30.721  1.00 49.94  ?  510 LYS B C   1 
ATOM   9087  O  O   . LYS B  2  510 ? 117.896 -3.818  29.654  1.00 63.33  ?  510 LYS B O   1 
ATOM   9088  C  CB  . LYS B  2  510 ? 120.514 -2.966  31.403  1.00 38.76  ?  510 LYS B CB  1 
ATOM   9089  C  CG  . LYS B  2  510 ? 121.182 -3.931  30.438  1.00 37.14  ?  510 LYS B CG  1 
ATOM   9090  C  CD  . LYS B  2  510 ? 122.466 -4.516  31.025  1.00 64.25  ?  510 LYS B CD  1 
ATOM   9091  C  CE  . LYS B  2  510 ? 123.474 -4.899  29.964  1.00 79.63  ?  510 LYS B CE  1 
ATOM   9092  N  NZ  . LYS B  2  510 ? 124.781 -5.286  30.557  1.00 74.87  ?  510 LYS B NZ  1 
ATOM   9093  N  N   . LEU B  2  511 ? 117.354 -3.450  31.809  1.00 48.88  ?  511 LEU B N   1 
ATOM   9094  C  CA  . LEU B  2  511 ? 116.226 -4.383  31.819  1.00 46.62  ?  511 LEU B CA  1 
ATOM   9095  C  C   . LEU B  2  511 ? 114.999 -3.819  31.096  1.00 49.94  ?  511 LEU B C   1 
ATOM   9096  O  O   . LEU B  2  511 ? 114.414 -4.508  30.260  1.00 63.86  ?  511 LEU B O   1 
ATOM   9097  C  CB  . LEU B  2  511 ? 115.842 -4.737  33.266  1.00 46.20  ?  511 LEU B CB  1 
ATOM   9098  C  CG  . LEU B  2  511 ? 116.915 -5.426  34.104  1.00 36.07  ?  511 LEU B CG  1 
ATOM   9099  C  CD1 . LEU B  2  511 ? 116.612 -5.296  35.583  1.00 39.51  ?  511 LEU B CD1 1 
ATOM   9100  C  CD2 . LEU B  2  511 ? 117.047 -6.884  33.732  1.00 47.41  ?  511 LEU B CD2 1 
ATOM   9101  N  N   . VAL B  2  512 ? 114.605 -2.578  31.416  1.00 44.52  ?  512 VAL B N   1 
ATOM   9102  C  CA  . VAL B  2  512 ? 113.432 -1.951  30.800  1.00 47.80  ?  512 VAL B CA  1 
ATOM   9103  C  C   . VAL B  2  512 ? 113.745 -1.408  29.389  1.00 51.94  ?  512 VAL B C   1 
ATOM   9104  O  O   . VAL B  2  512 ? 112.813 -1.172  28.616  1.00 58.37  ?  512 VAL B O   1 
ATOM   9105  C  CB  . VAL B  2  512 ? 112.830 -0.848  31.715  1.00 40.02  ?  512 VAL B CB  1 
ATOM   9106  C  CG1 . VAL B  2  512 ? 111.481 -0.370  31.189  1.00 50.45  ?  512 VAL B CG1 1 
ATOM   9107  C  CG2 . VAL B  2  512 ? 112.676 -1.341  33.148  1.00 39.10  ?  512 VAL B CG2 1 
ATOM   9108  N  N   . ASP B  2  513 ? 115.041 -1.219  29.049  1.00 41.82  ?  513 ASP B N   1 
ATOM   9109  C  CA  . ASP B  2  513 ? 115.482 -0.707  27.746  1.00 40.60  ?  513 ASP B CA  1 
ATOM   9110  C  C   . ASP B  2  513 ? 115.039 0.746   27.567  1.00 51.60  ?  513 ASP B C   1 
ATOM   9111  O  O   . ASP B  2  513 ? 114.317 1.080   26.623  1.00 60.65  ?  513 ASP B O   1 
ATOM   9112  C  CB  . ASP B  2  513 ? 114.967 -1.598  26.607  1.00 42.45  ?  513 ASP B CB  1 
ATOM   9113  C  CG  . ASP B  2  513 ? 115.602 -1.302  25.269  1.00 55.13  ?  513 ASP B CG  1 
ATOM   9114  O  OD1 . ASP B  2  513 ? 116.838 -1.135  25.224  1.00 65.55  ?  513 ASP B OD1 1 
ATOM   9115  O  OD2 . ASP B  2  513 ? 114.863 -1.241  24.264  1.00 70.94  ?  513 ASP B OD2 1 
ATOM   9116  N  N   . ILE B  2  514 ? 115.486 1.615   28.478  1.00 44.12  ?  514 ILE B N   1 
ATOM   9117  C  CA  . ILE B  2  514 ? 115.122 3.029   28.462  1.00 44.39  ?  514 ILE B CA  1 
ATOM   9118  C  C   . ILE B  2  514 ? 116.320 3.915   28.783  1.00 47.41  ?  514 ILE B C   1 
ATOM   9119  O  O   . ILE B  2  514 ? 117.264 3.443   29.413  1.00 59.19  ?  514 ILE B O   1 
ATOM   9120  C  CB  . ILE B  2  514 ? 114.011 3.279   29.527  1.00 46.08  ?  514 ILE B CB  1 
ATOM   9121  C  CG1 . ILE B  2  514 ? 114.470 2.796   30.934  1.00 53.01  ?  514 ILE B CG1 1 
ATOM   9122  C  CG2 . ILE B  2  514 ? 112.704 2.634   29.101  1.00 48.07  ?  514 ILE B CG2 1 
ATOM   9123  C  CD1 . ILE B  2  514 ? 113.449 2.960   32.099  1.00 39.36  ?  514 ILE B CD1 1 
ATOM   9124  N  N   . PRO B  2  515 ? 116.300 5.216   28.432  1.00 45.85  ?  515 PRO B N   1 
ATOM   9125  C  CA  . PRO B  2  515 ? 117.409 6.087   28.852  1.00 38.99  ?  515 PRO B CA  1 
ATOM   9126  C  C   . PRO B  2  515 ? 117.303 6.351   30.362  1.00 49.27  ?  515 PRO B C   1 
ATOM   9127  O  O   . PRO B  2  515 ? 116.255 6.082   30.964  1.00 54.10  ?  515 PRO B O   1 
ATOM   9128  C  CB  . PRO B  2  515 ? 117.179 7.381   28.058  1.00 40.21  ?  515 PRO B CB  1 
ATOM   9129  C  CG  . PRO B  2  515 ? 116.009 7.134   27.174  1.00 50.69  ?  515 PRO B CG  1 
ATOM   9130  C  CD  . PRO B  2  515 ? 115.260 5.980   27.720  1.00 44.08  ?  515 PRO B CD  1 
ATOM   9131  N  N   . PRO B  2  516 ? 118.349 6.882   31.016  1.00 51.27  ?  516 PRO B N   1 
ATOM   9132  C  CA  . PRO B  2  516 ? 118.231 7.157   32.462  1.00 32.43  ?  516 PRO B CA  1 
ATOM   9133  C  C   . PRO B  2  516 ? 117.318 8.349   32.778  1.00 44.46  ?  516 PRO B C   1 
ATOM   9134  O  O   . PRO B  2  516 ? 116.925 8.526   33.931  1.00 46.64  ?  516 PRO B O   1 
ATOM   9135  C  CB  . PRO B  2  516 ? 119.672 7.419   32.883  1.00 46.04  ?  516 PRO B CB  1 
ATOM   9136  C  CG  . PRO B  2  516 ? 120.326 7.960   31.653  1.00 53.09  ?  516 PRO B CG  1 
ATOM   9137  C  CD  . PRO B  2  516 ? 119.663 7.290   30.483  1.00 47.41  ?  516 PRO B CD  1 
ATOM   9138  N  N   . VAL B  2  517 ? 116.989 9.170   31.750  1.00 46.87  ?  517 VAL B N   1 
ATOM   9139  C  CA  . VAL B  2  517 ? 116.136 10.358  31.849  1.00 40.33  ?  517 VAL B CA  1 
ATOM   9140  C  C   . VAL B  2  517 ? 114.975 10.197  30.857  1.00 42.93  ?  517 VAL B C   1 
ATOM   9141  O  O   . VAL B  2  517 ? 115.226 10.076  29.654  1.00 50.07  ?  517 VAL B O   1 
ATOM   9142  C  CB  . VAL B  2  517 ? 116.958 11.631  31.524  1.00 35.83  ?  517 VAL B CB  1 
ATOM   9143  C  CG1 . VAL B  2  517 ? 116.112 12.884  31.686  1.00 49.06  ?  517 VAL B CG1 1 
ATOM   9144  C  CG2 . VAL B  2  517 ? 118.209 11.715  32.384  1.00 36.44  ?  517 VAL B CG2 1 
ATOM   9145  N  N   . LEU B  2  518 ? 113.713 10.205  31.347  1.00 42.09  ?  518 LEU B N   1 
ATOM   9146  C  CA  . LEU B  2  518 ? 112.536 10.031  30.483  1.00 44.85  ?  518 LEU B CA  1 
ATOM   9147  C  C   . LEU B  2  518 ? 111.830 11.345  30.159  1.00 49.28  ?  518 LEU B C   1 
ATOM   9148  O  O   . LEU B  2  518 ? 111.371 12.034  31.062  1.00 59.29  ?  518 LEU B O   1 
ATOM   9149  C  CB  . LEU B  2  518 ? 111.516 9.069   31.115  1.00 30.53  ?  518 LEU B CB  1 
ATOM   9150  C  CG  . LEU B  2  518 ? 112.048 7.756   31.672  1.00 31.51  ?  518 LEU B CG  1 
ATOM   9151  C  CD1 . LEU B  2  518 ? 110.942 6.973   32.330  1.00 32.31  ?  518 LEU B CD1 1 
ATOM   9152  C  CD2 . LEU B  2  518 ? 112.692 6.916   30.591  1.00 46.85  ?  518 LEU B CD2 1 
ATOM   9153  N  N   . HIS B  2  519 ? 111.715 11.676  28.867  1.00 52.03  ?  519 HIS B N   1 
ATOM   9154  C  CA  . HIS B  2  519 ? 111.043 12.895  28.416  1.00 48.98  ?  519 HIS B CA  1 
ATOM   9155  C  C   . HIS B  2  519 ? 109.528 12.643  28.361  1.00 47.72  ?  519 HIS B C   1 
ATOM   9156  O  O   . HIS B  2  519 ? 109.068 11.877  27.513  1.00 49.22  ?  519 HIS B O   1 
ATOM   9157  C  CB  . HIS B  2  519 ? 111.586 13.269  27.034  1.00 38.94  ?  519 HIS B CB  1 
ATOM   9158  C  CG  . HIS B  2  519 ? 111.160 14.612  26.527  1.00 44.82  ?  519 HIS B CG  1 
ATOM   9159  N  ND1 . HIS B  2  519 ? 109.963 15.187  26.910  1.00 52.38  ?  519 HIS B ND1 1 
ATOM   9160  C  CD2 . HIS B  2  519 ? 111.786 15.442  25.661  1.00 41.55  ?  519 HIS B CD2 1 
ATOM   9161  C  CE1 . HIS B  2  519 ? 109.901 16.348  26.277  1.00 48.36  ?  519 HIS B CE1 1 
ATOM   9162  N  NE2 . HIS B  2  519 ? 110.978 16.544  25.514  1.00 38.97  ?  519 HIS B NE2 1 
ATOM   9163  N  N   . MET B  2  520 ? 108.748 13.337  29.194  1.00 44.54  ?  520 MET B N   1 
ATOM   9164  C  CA  . MET B  2  520 ? 107.287 13.043  29.251  1.00 43.34  ?  520 MET B CA  1 
ATOM   9165  C  C   . MET B  2  520 ? 106.456 14.144  28.583  1.00 50.07  ?  520 MET B C   1 
ATOM   9166  O  O   . MET B  2  520 ? 105.223 14.119  28.746  1.00 45.52  ?  520 MET B O   1 
ATOM   9167  C  CB  . MET B  2  520 ? 106.840 12.862  30.701  1.00 37.48  ?  520 MET B CB  1 
ATOM   9168  C  CG  . MET B  2  520 ? 107.524 11.689  31.348  1.00 43.34  ?  520 MET B CG  1 
ATOM   9169  S  SD  . MET B  2  520 ? 106.856 11.307  32.986  1.00 50.38  ?  520 MET B SD  1 
ATOM   9170  C  CE  . MET B  2  520 ? 105.277 10.589  32.539  1.00 52.81  ?  520 MET B CE  1 
ATOM   9171  N  N   . GLY B  2  521 ? 107.094 15.064  27.858  1.00 48.66  ?  521 GLY B N   1 
ATOM   9172  C  CA  . GLY B  2  521 ? 106.363 16.082  27.115  1.00 46.77  ?  521 GLY B CA  1 
ATOM   9173  C  C   . GLY B  2  521 ? 106.551 17.534  27.493  1.00 53.75  ?  521 GLY B C   1 
ATOM   9174  O  O   . GLY B  2  521 ? 107.618 17.946  27.946  1.00 52.85  ?  521 GLY B O   1 
ATOM   9175  N  N   . SER B  2  522 ? 105.485 18.310  27.287  1.00 50.18  ?  522 SER B N   1 
ATOM   9176  C  CA  . SER B  2  522 ? 105.516 19.748  27.643  1.00 53.81  ?  522 SER B CA  1 
ATOM   9177  C  C   . SER B  2  522 ? 105.153 19.897  29.120  1.00 53.66  ?  522 SER B C   1 
ATOM   9178  O  O   . SER B  2  522 ? 105.136 18.878  29.832  1.00 67.17  ?  522 SER B O   1 
ATOM   9179  C  CB  . SER B  2  522 ? 104.564 20.519  26.776  1.00 66.98  ?  522 SER B CB  1 
ATOM   9180  O  OG  . SER B  2  522 ? 103.373 19.779  26.554  1.00 51.77  ?  522 SER B OG  1 
ATOM   9181  N  N   . CYS B  2  523 ? 104.864 21.127  29.546  1.00 45.61  ?  523 CYS B N   1 
ATOM   9182  C  CA  . CYS B  2  523 ? 104.499 21.378  30.964  1.00 64.15  ?  523 CYS B CA  1 
ATOM   9183  C  C   . CYS B  2  523 ? 103.037 20.970  31.173  1.00 63.19  ?  523 CYS B C   1 
ATOM   9184  O  O   . CYS B  2  523 ? 102.725 20.462  32.263  1.00 66.87  ?  523 CYS B O   1 
ATOM   9185  C  CB  . CYS B  2  523 ? 104.790 22.827  31.331  1.00 49.49  ?  523 CYS B CB  1 
ATOM   9186  S  SG  . CYS B  2  523 ? 106.571 23.146  31.432  1.00 111.17 ?  523 CYS B SG  1 
ATOM   9187  N  N   . VAL B  2  524 ? 102.174 21.185  30.175  1.00 62.74  ?  524 VAL B N   1 
ATOM   9188  C  CA  . VAL B  2  524 ? 100.786 20.659  30.289  1.00 50.58  ?  524 VAL B CA  1 
ATOM   9189  C  C   . VAL B  2  524 ? 100.936 19.150  30.481  1.00 62.93  ?  524 VAL B C   1 
ATOM   9190  O  O   . VAL B  2  524 ? 100.010 18.528  31.033  1.00 73.58  ?  524 VAL B O   1 
ATOM   9191  C  CB  . VAL B  2  524 ? 99.936  20.999  29.052  1.00 47.64  ?  524 VAL B CB  1 
ATOM   9192  C  CG1 . VAL B  2  524 ? 100.147 22.437  28.604  1.00 72.77  ?  524 VAL B CG1 1 
ATOM   9193  C  CG2 . VAL B  2  524 ? 100.194 20.035  27.905  1.00 76.82  ?  524 VAL B CG2 1 
ATOM   9194  N  N   . ASP B  2  525 ? 102.080 18.598  30.058  1.00 59.15  ?  525 ASP B N   1 
ATOM   9195  C  CA  . ASP B  2  525 ? 102.324 17.172  30.242  1.00 45.82  ?  525 ASP B CA  1 
ATOM   9196  C  C   . ASP B  2  525 ? 102.932 16.852  31.613  1.00 45.34  ?  525 ASP B C   1 
ATOM   9197  O  O   . ASP B  2  525 ? 103.208 15.686  31.882  1.00 51.54  ?  525 ASP B O   1 
ATOM   9198  C  CB  . ASP B  2  525 ? 103.154 16.583  29.089  1.00 58.26  ?  525 ASP B CB  1 
ATOM   9199  C  CG  . ASP B  2  525 ? 102.406 16.481  27.765  1.00 74.80  ?  525 ASP B CG  1 
ATOM   9200  O  OD1 . ASP B  2  525 ? 101.182 16.750  27.747  1.00 75.23  ?  525 ASP B OD1 1 
ATOM   9201  O  OD2 . ASP B  2  525 ? 103.048 16.133  26.743  1.00 72.74  ?  525 ASP B OD2 1 
ATOM   9202  N  N   . ILE B  2  526 ? 103.104 17.854  32.504  1.00 47.93  ?  526 ILE B N   1 
ATOM   9203  C  CA  . ILE B  2  526 ? 103.552 17.587  33.875  1.00 45.91  ?  526 ILE B CA  1 
ATOM   9204  C  C   . ILE B  2  526 ? 102.408 16.804  34.568  1.00 50.97  ?  526 ILE B C   1 
ATOM   9205  O  O   . ILE B  2  526 ? 102.658 16.087  35.536  1.00 56.98  ?  526 ILE B O   1 
ATOM   9206  C  CB  . ILE B  2  526 ? 103.926 18.884  34.639  1.00 45.67  ?  526 ILE B CB  1 
ATOM   9207  C  CG1 . ILE B  2  526 ? 105.270 19.413  34.116  1.00 46.43  ?  526 ILE B CG1 1 
ATOM   9208  C  CG2 . ILE B  2  526 ? 103.978 18.653  36.164  1.00 28.32  ?  526 ILE B CG2 1 
ATOM   9209  C  CD1 . ILE B  2  526 ? 105.657 20.761  34.590  1.00 48.04  ?  526 ILE B CD1 1 
ATOM   9210  N  N   . SER B  2  527 ? 101.158 16.913  34.044  1.00 42.85  ?  527 SER B N   1 
ATOM   9211  C  CA  . SER B  2  527 ? 100.008 16.164  34.541  1.00 53.56  ?  527 SER B CA  1 
ATOM   9212  C  C   . SER B  2  527 ? 100.303 14.650  34.455  1.00 55.87  ?  527 SER B C   1 
ATOM   9213  O  O   . SER B  2  527 ? 99.779  13.878  35.257  1.00 60.30  ?  527 SER B O   1 
ATOM   9214  C  CB  . SER B  2  527 ? 98.766  16.493  33.720  1.00 50.39  ?  527 SER B CB  1 
ATOM   9215  O  OG  . SER B  2  527 ? 98.994  16.255  32.341  1.00 50.18  ?  527 SER B OG  1 
ATOM   9216  N  N   . ARG B  2  528 ? 101.151 14.233  33.489  1.00 49.64  ?  528 ARG B N   1 
ATOM   9217  C  CA  . ARG B  2  528 ? 101.556 12.839  33.336  1.00 56.49  ?  528 ARG B CA  1 
ATOM   9218  C  C   . ARG B  2  528 ? 102.370 12.425  34.575  1.00 61.48  ?  528 ARG B C   1 
ATOM   9219  O  O   . ARG B  2  528 ? 102.213 11.309  35.062  1.00 62.20  ?  528 ARG B O   1 
ATOM   9220  C  CB  . ARG B  2  528 ? 102.415 12.651  32.070  1.00 50.61  ?  528 ARG B CB  1 
ATOM   9221  C  CG  . ARG B  2  528 ? 101.695 12.939  30.758  1.00 46.77  ?  528 ARG B CG  1 
ATOM   9222  C  CD  . ARG B  2  528 ? 102.407 12.288  29.587  1.00 44.44  ?  528 ARG B CD  1 
ATOM   9223  N  NE  . ARG B  2  528 ? 102.285 13.065  28.350  1.00 52.26  ?  528 ARG B NE  1 
ATOM   9224  C  CZ  . ARG B  2  528 ? 101.373 12.865  27.400  1.00 60.49  ?  528 ARG B CZ  1 
ATOM   9225  N  NH1 . ARG B  2  528 ? 100.464 11.903  27.528  1.00 51.92  ?  528 ARG B NH1 1 
ATOM   9226  N  NH2 . ARG B  2  528 ? 101.359 13.630  26.313  1.00 60.55  ?  528 ARG B NH2 1 
ATOM   9227  N  N   . ILE B  2  529 ? 103.226 13.331  35.094  1.00 50.09  ?  529 ILE B N   1 
ATOM   9228  C  CA  . ILE B  2  529 ? 104.043 13.062  36.280  1.00 43.57  ?  529 ILE B CA  1 
ATOM   9229  C  C   . ILE B  2  529 ? 103.094 12.845  37.463  1.00 52.56  ?  529 ILE B C   1 
ATOM   9230  O  O   . ILE B  2  529 ? 103.241 11.870  38.200  1.00 52.07  ?  529 ILE B O   1 
ATOM   9231  C  CB  . ILE B  2  529 ? 105.067 14.209  36.545  1.00 46.28  ?  529 ILE B CB  1 
ATOM   9232  C  CG1 . ILE B  2  529 ? 106.039 14.358  35.357  1.00 37.34  ?  529 ILE B CG1 1 
ATOM   9233  C  CG2 . ILE B  2  529 ? 105.843 13.954  37.837  1.00 36.69  ?  529 ILE B CG2 1 
ATOM   9234  C  CD1 . ILE B  2  529 ? 106.839 15.591  35.314  1.00 58.42  ?  529 ILE B CD1 1 
ATOM   9235  N  N   . LEU B  2  530 ? 102.089 13.726  37.621  1.00 54.34  ?  530 LEU B N   1 
ATOM   9236  C  CA  . LEU B  2  530 ? 101.110 13.585  38.701  1.00 53.69  ?  530 LEU B CA  1 
ATOM   9237  C  C   . LEU B  2  530 ? 100.370 12.246  38.571  1.00 49.34  ?  530 LEU B C   1 
ATOM   9238  O  O   . LEU B  2  530 ? 100.150 11.565  39.565  1.00 53.98  ?  530 LEU B O   1 
ATOM   9239  C  CB  . LEU B  2  530 ? 100.088 14.734  38.663  1.00 47.75  ?  530 LEU B CB  1 
ATOM   9240  C  CG  . LEU B  2  530 ? 100.604 16.137  38.929  1.00 46.93  ?  530 LEU B CG  1 
ATOM   9241  C  CD1 . LEU B  2  530 ? 99.501  17.157  38.703  1.00 53.64  ?  530 LEU B CD1 1 
ATOM   9242  C  CD2 . LEU B  2  530 ? 101.151 16.269  40.343  1.00 43.51  ?  530 LEU B CD2 1 
ATOM   9243  N  N   . ASP B  2  531 ? 99.996  11.877  37.341  1.00 55.15  ?  531 ASP B N   1 
ATOM   9244  C  CA  . ASP B  2  531 ? 99.292  10.632  37.063  1.00 52.35  ?  531 ASP B CA  1 
ATOM   9245  C  C   . ASP B  2  531 ? 100.186 9.475   37.500  1.00 57.82  ?  531 ASP B C   1 
ATOM   9246  O  O   . ASP B  2  531 ? 99.764  8.662   38.315  1.00 68.52  ?  531 ASP B O   1 
ATOM   9247  C  CB  . ASP B  2  531 ? 98.907  10.563  35.571  1.00 58.86  ?  531 ASP B CB  1 
ATOM   9248  C  CG  . ASP B  2  531 ? 98.156  9.314   35.155  1.00 61.31  ?  531 ASP B CG  1 
ATOM   9249  O  OD1 . ASP B  2  531 ? 97.452  8.735   36.004  1.00 64.73  ?  531 ASP B OD1 1 
ATOM   9250  O  OD2 . ASP B  2  531 ? 98.264  8.922   33.975  1.00 61.62  ?  531 ASP B OD2 1 
ATOM   9251  N  N   . LEU B  2  532 ? 101.419 9.409   36.980  1.00 60.24  ?  532 LEU B N   1 
ATOM   9252  C  CA  . LEU B  2  532 ? 102.362 8.345   37.314  1.00 50.40  ?  532 LEU B CA  1 
ATOM   9253  C  C   . LEU B  2  532 ? 102.584 8.204   38.817  1.00 51.52  ?  532 LEU B C   1 
ATOM   9254  O  O   . LEU B  2  532 ? 102.433 7.109   39.353  1.00 57.71  ?  532 LEU B O   1 
ATOM   9255  C  CB  . LEU B  2  532 ? 103.703 8.593   36.599  1.00 44.85  ?  532 LEU B CB  1 
ATOM   9256  C  CG  . LEU B  2  532 ? 104.725 7.461   36.677  1.00 44.91  ?  532 LEU B CG  1 
ATOM   9257  C  CD1 . LEU B  2  532 ? 104.385 6.351   35.701  1.00 61.03  ?  532 LEU B CD1 1 
ATOM   9258  C  CD2 . LEU B  2  532 ? 106.120 7.968   36.397  1.00 27.83  ?  532 LEU B CD2 1 
ATOM   9259  N  N   . VAL B  2  533 ? 102.919 9.301   39.509  1.00 50.35  ?  533 VAL B N   1 
ATOM   9260  C  CA  . VAL B  2  533 ? 103.148 9.255   40.953  1.00 46.24  ?  533 VAL B CA  1 
ATOM   9261  C  C   . VAL B  2  533 ? 101.866 8.807   41.669  1.00 57.51  ?  533 VAL B C   1 
ATOM   9262  O  O   . VAL B  2  533 ? 101.917 7.954   42.555  1.00 59.16  ?  533 VAL B O   1 
ATOM   9263  C  CB  . VAL B  2  533 ? 103.660 10.614  41.481  1.00 45.67  ?  533 VAL B CB  1 
ATOM   9264  C  CG1 . VAL B  2  533 ? 103.722 10.618  43.002  1.00 51.20  ?  533 VAL B CG1 1 
ATOM   9265  C  CG2 . VAL B  2  533 ? 105.029 10.936  40.895  1.00 39.55  ?  533 VAL B CG2 1 
ATOM   9266  N  N   . GLY B  2  534 ? 100.731 9.358   41.253  1.00 56.25  ?  534 GLY B N   1 
ATOM   9267  C  CA  . GLY B  2  534 ? 99.439  9.001   41.818  1.00 51.91  ?  534 GLY B CA  1 
ATOM   9268  C  C   . GLY B  2  534 ? 99.121  7.528   41.660  1.00 58.57  ?  534 GLY B C   1 
ATOM   9269  O  O   . GLY B  2  534 ? 98.559  6.911   42.569  1.00 56.98  ?  534 GLY B O   1 
ATOM   9270  N  N   . ARG B  2  535 ? 99.482  6.950   40.507  1.00 54.89  ?  535 ARG B N   1 
ATOM   9271  C  CA  . ARG B  2  535 ? 99.242  5.535   40.229  1.00 51.19  ?  535 ARG B CA  1 
ATOM   9272  C  C   . ARG B  2  535 ? 100.076 4.659   41.148  1.00 54.18  ?  535 ARG B C   1 
ATOM   9273  O  O   . ARG B  2  535 ? 99.593  3.624   41.606  1.00 55.17  ?  535 ARG B O   1 
ATOM   9274  C  CB  . ARG B  2  535 ? 99.571  5.209   38.771  1.00 48.85  ?  535 ARG B CB  1 
ATOM   9275  C  CG  . ARG B  2  535 ? 98.570  5.772   37.779  1.00 48.93  ?  535 ARG B CG  1 
ATOM   9276  C  CD  . ARG B  2  535 ? 99.009  5.505   36.363  1.00 58.66  ?  535 ARG B CD  1 
ATOM   9277  N  NE  . ARG B  2  535 ? 98.515  4.213   35.882  1.00 61.52  ?  535 ARG B NE  1 
ATOM   9278  C  CZ  . ARG B  2  535 ? 97.563  4.040   34.967  1.00 79.15  ?  535 ARG B CZ  1 
ATOM   9279  N  NH1 . ARG B  2  535 ? 96.966  5.089   34.404  1.00 65.05  ?  535 ARG B NH1 1 
ATOM   9280  N  NH2 . ARG B  2  535 ? 97.199  2.814   34.606  1.00 70.28  ?  535 ARG B NH2 1 
ATOM   9281  N  N   . VAL B  2  536 ? 101.327 5.068   41.417  1.00 51.73  ?  536 VAL B N   1 
ATOM   9282  C  CA  . VAL B  2  536 ? 102.215 4.325   42.309  1.00 51.45  ?  536 VAL B CA  1 
ATOM   9283  C  C   . VAL B  2  536 ? 101.632 4.407   43.727  1.00 57.12  ?  536 VAL B C   1 
ATOM   9284  O  O   . VAL B  2  536 ? 101.543 3.397   44.418  1.00 54.79  ?  536 VAL B O   1 
ATOM   9285  C  CB  . VAL B  2  536 ? 103.666 4.876   42.259  1.00 46.47  ?  536 VAL B CB  1 
ATOM   9286  C  CG1 . VAL B  2  536 ? 104.543 4.217   43.320  1.00 46.80  ?  536 VAL B CG1 1 
ATOM   9287  C  CG2 . VAL B  2  536 ? 104.278 4.690   40.875  1.00 38.12  ?  536 VAL B CG2 1 
ATOM   9288  N  N   . ALA B  2  537 ? 101.208 5.605   44.150  1.00 56.15  ?  537 ALA B N   1 
ATOM   9289  C  CA  . ALA B  2  537 ? 100.625 5.791   45.472  1.00 54.40  ?  537 ALA B CA  1 
ATOM   9290  C  C   . ALA B  2  537 ? 99.414  4.872   45.680  1.00 55.26  ?  537 ALA B C   1 
ATOM   9291  O  O   . ALA B  2  537 ? 99.344  4.192   46.700  1.00 68.54  ?  537 ALA B O   1 
ATOM   9292  C  CB  . ALA B  2  537 ? 100.230 7.249   45.669  1.00 54.60  ?  537 ALA B CB  1 
ATOM   9293  N  N   . ASN B  2  538 ? 98.486  4.825   44.709  1.00 59.61  ?  538 ASN B N   1 
ATOM   9294  C  CA  . ASN B  2  538 ? 97.297  3.970   44.804  1.00 66.39  ?  538 ASN B CA  1 
ATOM   9295  C  C   . ASN B  2  538 ? 97.666  2.492   44.806  1.00 55.34  ?  538 ASN B C   1 
ATOM   9296  O  O   . ASN B  2  538 ? 97.080  1.712   45.555  1.00 59.34  ?  538 ASN B O   1 
ATOM   9297  C  CB  . ASN B  2  538 ? 96.340  4.252   43.650  1.00 58.99  ?  538 ASN B CB  1 
ATOM   9298  C  CG  . ASN B  2  538 ? 95.587  5.535   43.819  1.00 52.59  ?  538 ASN B CG  1 
ATOM   9299  O  OD1 . ASN B  2  538 ? 95.294  5.963   44.939  1.00 65.53  ?  538 ASN B OD1 1 
ATOM   9300  N  ND2 . ASN B  2  538 ? 95.248  6.178   42.709  1.00 77.20  ?  538 ASN B ND2 1 
ATOM   9301  N  N   . LEU B  2  539 ? 98.646  2.109   43.984  1.00 57.31  ?  539 LEU B N   1 
ATOM   9302  C  CA  . LEU B  2  539 ? 99.069  0.683   43.917  1.00 61.10  ?  539 LEU B CA  1 
ATOM   9303  C  C   . LEU B  2  539 ? 99.682  0.275   45.262  1.00 62.79  ?  539 LEU B C   1 
ATOM   9304  O  O   . LEU B  2  539 ? 99.476  -0.883  45.672  1.00 71.41  ?  539 LEU B O   1 
ATOM   9305  C  CB  . LEU B  2  539 ? 100.066 0.492   42.770  1.00 61.75  ?  539 LEU B CB  1 
ATOM   9306  C  CG  . LEU B  2  539 ? 100.621 -0.924  42.614  1.00 44.87  ?  539 LEU B CG  1 
ATOM   9307  C  CD1 . LEU B  2  539 ? 99.818  -1.726  41.597  1.00 67.38  ?  539 LEU B CD1 1 
ATOM   9308  C  CD2 . LEU B  2  539 ? 102.089 -0.886  42.224  1.00 63.90  ?  539 LEU B CD2 1 
ATOM   9309  N  N   . LEU B  2  540 ? 100.399 1.191   45.920  1.00 66.72  ?  540 LEU B N   1 
ATOM   9310  C  CA  . LEU B  2  540 ? 101.004 0.888   47.220  1.00 59.70  ?  540 LEU B CA  1 
ATOM   9311  C  C   . LEU B  2  540 ? 100.065 1.218   48.405  1.00 70.44  ?  540 LEU B C   1 
ATOM   9312  O  O   . LEU B  2  540 ? 100.458 1.046   49.556  1.00 79.12  ?  540 LEU B O   1 
ATOM   9313  C  CB  . LEU B  2  540 ? 102.332 1.647   47.383  1.00 48.62  ?  540 LEU B CB  1 
ATOM   9314  C  CG  . LEU B  2  540 ? 103.473 1.233   46.457  1.00 52.82  ?  540 LEU B CG  1 
ATOM   9315  C  CD1 . LEU B  2  540 ? 104.613 2.236   46.520  1.00 39.05  ?  540 LEU B CD1 1 
ATOM   9316  C  CD2 . LEU B  2  540 ? 103.998 -0.138  46.811  1.00 68.07  ?  540 LEU B CD2 1 
ATOM   9317  N  N   . GLY B  2  541 ? 98.848  1.673   48.123  1.00 72.32  ?  541 GLY B N   1 
ATOM   9318  C  CA  . GLY B  2  541 ? 97.867  2.008   49.147  1.00 76.73  ?  541 GLY B CA  1 
ATOM   9319  C  C   . GLY B  2  541 ? 98.305  3.094   50.109  1.00 69.14  ?  541 GLY B C   1 
ATOM   9320  O  O   . GLY B  2  541 ? 97.958  3.051   51.292  1.00 81.91  ?  541 GLY B O   1 
ATOM   9321  N  N   . VAL B  2  542 ? 99.060  4.081   49.610  1.00 60.29  ?  542 VAL B N   1 
ATOM   9322  C  CA  . VAL B  2  542 ? 99.563  5.188   50.422  1.00 61.00  ?  542 VAL B CA  1 
ATOM   9323  C  C   . VAL B  2  542 ? 99.215  6.525   49.736  1.00 71.35  ?  542 VAL B C   1 
ATOM   9324  O  O   . VAL B  2  542 ? 98.632  6.524   48.652  1.00 71.98  ?  542 VAL B O   1 
ATOM   9325  C  CB  . VAL B  2  542 ? 101.093 5.039   50.663  1.00 45.25  ?  542 VAL B CB  1 
ATOM   9326  C  CG1 . VAL B  2  542 ? 101.406 3.766   51.431  1.00 61.22  ?  542 VAL B CG1 1 
ATOM   9327  C  CG2 . VAL B  2  542 ? 101.863 5.078   49.354  1.00 49.11  ?  542 VAL B CG2 1 
ATOM   9328  N  N   . ASP B  2  543 ? 99.550  7.660   50.369  1.00 64.63  ?  543 ASP B N   1 
ATOM   9329  C  CA  . ASP B  2  543 ? 99.308  8.976   49.788  1.00 59.01  ?  543 ASP B CA  1 
ATOM   9330  C  C   . ASP B  2  543 ? 100.544 9.352   48.953  1.00 67.27  ?  543 ASP B C   1 
ATOM   9331  O  O   . ASP B  2  543 ? 101.566 8.669   49.033  1.00 66.20  ?  543 ASP B O   1 
ATOM   9332  C  CB  . ASP B  2  543 ? 99.071  10.008  50.907  1.00 72.84  ?  543 ASP B CB  1 
ATOM   9333  C  CG  . ASP B  2  543 ? 98.253  11.215  50.488  1.00 77.99  ?  543 ASP B CG  1 
ATOM   9334  O  OD1 . ASP B  2  543 ? 98.064  11.413  49.266  1.00 83.48  ?  543 ASP B OD1 1 
ATOM   9335  O  OD2 . ASP B  2  543 ? 97.803  11.967  51.384  1.00 79.23  ?  543 ASP B OD2 1 
ATOM   9336  N  N   . MET B  2  544 ? 100.463 10.442  48.187  1.00 71.49  ?  544 MET B N   1 
ATOM   9337  C  CA  . MET B  2  544 ? 101.605 10.849  47.323  1.00 57.53  ?  544 MET B CA  1 
ATOM   9338  C  C   . MET B  2  544 ? 102.739 11.392  48.199  1.00 62.20  ?  544 MET B C   1 
ATOM   9339  O  O   . MET B  2  544 ? 103.909 11.239  47.801  1.00 59.50  ?  544 MET B O   1 
ATOM   9340  C  CB  . MET B  2  544 ? 101.169 11.908  46.305  1.00 56.51  ?  544 MET B CB  1 
ATOM   9341  C  CG  . MET B  2  544 ? 100.625 11.307  45.021  1.00 57.78  ?  544 MET B CG  1 
ATOM   9342  S  SD  . MET B  2  544 ? 99.431  12.373  44.174  1.00 77.03  ?  544 MET B SD  1 
ATOM   9343  C  CE  . MET B  2  544 ? 100.424 12.940  42.795  1.00 68.13  ?  544 MET B CE  1 
ATOM   9344  N  N   . SER B  2  545 ? 102.409 11.993  49.345  1.00 57.93  ?  545 SER B N   1 
ATOM   9345  C  CA  . SER B  2  545 ? 103.409 12.512  50.265  1.00 59.99  ?  545 SER B CA  1 
ATOM   9346  C  C   . SER B  2  545 ? 104.218 11.401  50.941  1.00 72.50  ?  545 SER B C   1 
ATOM   9347  O  O   . SER B  2  545 ? 105.243 11.701  51.541  1.00 93.09  ?  545 SER B O   1 
ATOM   9348  C  CB  . SER B  2  545 ? 102.744 13.375  51.332  1.00 67.64  ?  545 SER B CB  1 
ATOM   9349  O  OG  . SER B  2  545 ? 101.515 12.813  51.763  1.00 72.87  ?  545 SER B OG  1 
ATOM   9350  N  N   . ASP B  2  546 ? 103.780 10.133  50.860  1.00 63.11  ?  546 ASP B N   1 
ATOM   9351  C  CA  . ASP B  2  546 ? 104.496 9.032   51.499  1.00 60.47  ?  546 ASP B CA  1 
ATOM   9352  C  C   . ASP B  2  546 ? 105.600 8.427   50.623  1.00 67.34  ?  546 ASP B C   1 
ATOM   9353  O  O   . ASP B  2  546 ? 106.439 7.691   51.136  1.00 75.46  ?  546 ASP B O   1 
ATOM   9354  C  CB  . ASP B  2  546 ? 103.497 7.932   51.902  1.00 57.53  ?  546 ASP B CB  1 
ATOM   9355  C  CG  . ASP B  2  546 ? 102.438 8.400   52.882  1.00 72.09  ?  546 ASP B CG  1 
ATOM   9356  O  OD1 . ASP B  2  546 ? 102.793 9.111   53.848  1.00 77.49  ?  546 ASP B OD1 1 
ATOM   9357  O  OD2 . ASP B  2  546 ? 101.252 8.053   52.685  1.00 76.22  ?  546 ASP B OD2 1 
ATOM   9358  N  N   . LEU B  2  547 ? 105.587 8.722   49.320  1.00 64.45  ?  547 LEU B N   1 
ATOM   9359  C  CA  . LEU B  2  547 ? 106.567 8.091   48.392  1.00 58.06  ?  547 LEU B CA  1 
ATOM   9360  C  C   . LEU B  2  547 ? 107.870 8.897   48.360  1.00 57.75  ?  547 LEU B C   1 
ATOM   9361  O  O   . LEU B  2  547 ? 107.821 10.107  48.649  1.00 56.13  ?  547 LEU B O   1 
ATOM   9362  C  CB  . LEU B  2  547 ? 105.936 8.016   46.999  1.00 46.91  ?  547 LEU B CB  1 
ATOM   9363  C  CG  . LEU B  2  547 ? 104.554 7.369   46.946  1.00 65.93  ?  547 LEU B CG  1 
ATOM   9364  C  CD1 . LEU B  2  547 ? 103.885 7.647   45.611  1.00 53.64  ?  547 LEU B CD1 1 
ATOM   9365  C  CD2 . LEU B  2  547 ? 104.649 5.872   47.191  1.00 60.81  ?  547 LEU B CD2 1 
ATOM   9366  N  N   . PRO B  2  548 ? 109.028 8.285   48.020  1.00 57.70  ?  548 PRO B N   1 
ATOM   9367  C  CA  . PRO B  2  548 ? 110.295 9.022   47.903  1.00 52.22  ?  548 PRO B CA  1 
ATOM   9368  C  C   . PRO B  2  548 ? 110.418 9.676   46.523  1.00 55.17  ?  548 PRO B C   1 
ATOM   9369  O  O   . PRO B  2  548 ? 111.201 9.235   45.686  1.00 63.48  ?  548 PRO B O   1 
ATOM   9370  C  CB  . PRO B  2  548 ? 111.341 7.931   48.105  1.00 54.66  ?  548 PRO B CB  1 
ATOM   9371  C  CG  . PRO B  2  548 ? 110.711 6.711   47.541  1.00 51.61  ?  548 PRO B CG  1 
ATOM   9372  C  CD  . PRO B  2  548 ? 109.216 6.848   47.729  1.00 49.45  ?  548 PRO B CD  1 
ATOM   9373  N  N   . VAL B  2  549 ? 109.615 10.713  46.283  1.00 51.96  ?  549 VAL B N   1 
ATOM   9374  C  CA  . VAL B  2  549 ? 109.606 11.449  45.018  1.00 51.90  ?  549 VAL B CA  1 
ATOM   9375  C  C   . VAL B  2  549 ? 109.891 12.926  45.290  1.00 51.29  ?  549 VAL B C   1 
ATOM   9376  O  O   . VAL B  2  549 ? 109.766 13.379  46.428  1.00 63.41  ?  549 VAL B O   1 
ATOM   9377  C  CB  . VAL B  2  549 ? 108.270 11.277  44.252  1.00 53.92  ?  549 VAL B CB  1 
ATOM   9378  C  CG1 . VAL B  2  549 ? 108.074 9.835   43.815  1.00 48.29  ?  549 VAL B CG1 1 
ATOM   9379  C  CG2 . VAL B  2  549 ? 107.082 11.767  45.076  1.00 60.98  ?  549 VAL B CG2 1 
ATOM   9380  N  N   . ALA B  2  550 ? 110.268 13.677  44.248  1.00 49.10  ?  550 ALA B N   1 
ATOM   9381  C  CA  . ALA B  2  550 ? 110.558 15.102  44.371  1.00 41.14  ?  550 ALA B CA  1 
ATOM   9382  C  C   . ALA B  2  550 ? 110.486 15.777  43.000  1.00 53.22  ?  550 ALA B C   1 
ATOM   9383  O  O   . ALA B  2  550 ? 110.651 15.122  41.975  1.00 58.18  ?  550 ALA B O   1 
ATOM   9384  C  CB  . ALA B  2  550 ? 111.944 15.307  44.970  1.00 39.49  ?  550 ALA B CB  1 
ATOM   9385  N  N   . GLY B  2  551 ? 110.245 17.081  43.005  1.00 51.20  ?  551 GLY B N   1 
ATOM   9386  C  CA  . GLY B  2  551 ? 110.183 17.897  41.802  1.00 35.28  ?  551 GLY B CA  1 
ATOM   9387  C  C   . GLY B  2  551 ? 111.241 18.977  41.873  1.00 49.31  ?  551 GLY B C   1 
ATOM   9388  O  O   . GLY B  2  551 ? 111.559 19.446  42.967  1.00 53.26  ?  551 GLY B O   1 
ATOM   9389  N  N   . VAL B  2  552 ? 111.817 19.371  40.720  1.00 44.96  ?  552 VAL B N   1 
ATOM   9390  C  CA  . VAL B  2  552 ? 112.856 20.404  40.683  1.00 41.64  ?  552 VAL B CA  1 
ATOM   9391  C  C   . VAL B  2  552 ? 112.626 21.356  39.506  1.00 49.25  ?  552 VAL B C   1 
ATOM   9392  O  O   . VAL B  2  552 ? 112.315 20.912  38.405  1.00 57.24  ?  552 VAL B O   1 
ATOM   9393  C  CB  . VAL B  2  552 ? 114.298 19.815  40.614  1.00 45.62  ?  552 VAL B CB  1 
ATOM   9394  C  CG1 . VAL B  2  552 ? 115.328 20.849  41.061  1.00 60.51  ?  552 VAL B CG1 1 
ATOM   9395  C  CG2 . VAL B  2  552 ? 114.437 18.533  41.432  1.00 44.78  ?  552 VAL B CG2 1 
ATOM   9396  N  N   . ALA B  2  553 ? 112.802 22.663  39.745  1.00 48.32  ?  553 ALA B N   1 
ATOM   9397  C  CA  . ALA B  2  553 ? 112.661 23.722  38.745  1.00 47.66  ?  553 ALA B CA  1 
ATOM   9398  C  C   . ALA B  2  553 ? 113.983 24.497  38.797  1.00 53.74  ?  553 ALA B C   1 
ATOM   9399  O  O   . ALA B  2  553 ? 114.054 25.570  39.397  1.00 63.04  ?  553 ALA B O   1 
ATOM   9400  C  CB  . ALA B  2  553 ? 111.496 24.624  39.113  1.00 40.99  ?  553 ALA B CB  1 
ATOM   9401  N  N   . PRO B  2  554 ? 115.063 23.936  38.214  1.00 49.40  ?  554 PRO B N   1 
ATOM   9402  C  CA  . PRO B  2  554 ? 116.379 24.581  38.323  1.00 39.38  ?  554 PRO B CA  1 
ATOM   9403  C  C   . PRO B  2  554 ? 116.531 25.997  37.781  1.00 48.65  ?  554 PRO B C   1 
ATOM   9404  O  O   . PRO B  2  554 ? 117.310 26.758  38.355  1.00 53.77  ?  554 PRO B O   1 
ATOM   9405  C  CB  . PRO B  2  554 ? 117.309 23.610  37.591  1.00 43.51  ?  554 PRO B CB  1 
ATOM   9406  C  CG  . PRO B  2  554 ? 116.604 22.321  37.587  1.00 49.84  ?  554 PRO B CG  1 
ATOM   9407  C  CD  . PRO B  2  554 ? 115.160 22.645  37.508  1.00 52.63  ?  554 PRO B CD  1 
ATOM   9408  N  N   . GLU B  2  555 ? 115.844 26.356  36.681  1.00 53.11  ?  555 GLU B N   1 
ATOM   9409  C  CA  . GLU B  2  555 ? 115.986 27.693  36.092  1.00 39.71  ?  555 GLU B CA  1 
ATOM   9410  C  C   . GLU B  2  555 ? 114.628 28.219  35.621  1.00 47.26  ?  555 GLU B C   1 
ATOM   9411  O  O   . GLU B  2  555 ? 114.450 28.500  34.439  1.00 75.04  ?  555 GLU B O   1 
ATOM   9412  C  CB  . GLU B  2  555 ? 116.972 27.648  34.898  1.00 55.51  ?  555 GLU B CB  1 
ATOM   9413  C  CG  . GLU B  2  555 ? 118.136 26.688  35.051  1.00 51.47  ?  555 GLU B CG  1 
ATOM   9414  C  CD  . GLU B  2  555 ? 119.033 26.568  33.836  1.00 59.77  ?  555 GLU B CD  1 
ATOM   9415  O  OE1 . GLU B  2  555 ? 118.925 27.416  32.920  1.00 71.38  ?  555 GLU B OE1 1 
ATOM   9416  O  OE2 . GLU B  2  555 ? 119.847 25.616  33.803  1.00 55.56  ?  555 GLU B OE2 1 
ATOM   9417  N  N   . TRP B  2  556 ? 113.683 28.383  36.549  1.00 48.37  ?  556 TRP B N   1 
ATOM   9418  C  CA  . TRP B  2  556 ? 112.308 28.802  36.158  1.00 48.31  ?  556 TRP B CA  1 
ATOM   9419  C  C   . TRP B  2  556 ? 112.218 30.324  35.998  1.00 50.27  ?  556 TRP B C   1 
ATOM   9420  O  O   . TRP B  2  556 ? 113.148 31.019  36.449  1.00 45.09  ?  556 TRP B O   1 
ATOM   9421  C  CB  . TRP B  2  556 ? 111.294 28.291  37.186  1.00 49.20  ?  556 TRP B CB  1 
ATOM   9422  C  CG  . TRP B  2  556 ? 111.433 28.930  38.533  1.00 46.20  ?  556 TRP B CG  1 
ATOM   9423  C  CD1 . TRP B  2  556 ? 112.214 28.507  39.568  1.00 46.82  ?  556 TRP B CD1 1 
ATOM   9424  C  CD2 . TRP B  2  556 ? 110.770 30.121  38.992  1.00 48.88  ?  556 TRP B CD2 1 
ATOM   9425  N  NE1 . TRP B  2  556 ? 112.081 29.349  40.639  1.00 59.42  ?  556 TRP B NE1 1 
ATOM   9426  C  CE2 . TRP B  2  556 ? 111.203 30.349  40.315  1.00 50.59  ?  556 TRP B CE2 1 
ATOM   9427  C  CE3 . TRP B  2  556 ? 109.857 31.012  38.418  1.00 47.22  ?  556 TRP B CE3 1 
ATOM   9428  C  CZ2 . TRP B  2  556 ? 110.752 31.431  41.069  1.00 56.45  ?  556 TRP B CZ2 1 
ATOM   9429  C  CZ3 . TRP B  2  556 ? 109.412 32.081  39.164  1.00 48.45  ?  556 TRP B CZ3 1 
ATOM   9430  C  CH2 . TRP B  2  556 ? 109.855 32.285  40.471  1.00 53.98  ?  556 TRP B CH2 1 
ATOM   9431  N  N   . MET B  2  557 ? 111.119 30.807  35.415  1.00 48.18  ?  557 MET B N   1 
ATOM   9432  C  CA  . MET B  2  557 ? 110.915 32.270  35.261  1.00 44.21  ?  557 MET B CA  1 
ATOM   9433  C  C   . MET B  2  557 ? 109.423 32.546  35.046  1.00 46.21  ?  557 MET B C   1 
ATOM   9434  O  O   . MET B  2  557 ? 108.940 33.572  35.556  1.00 57.72  ?  557 MET B O   1 
ATOM   9435  C  CB  . MET B  2  557 ? 111.717 32.801  34.072  1.00 49.56  ?  557 MET B CB  1 
ATOM   9436  C  CG  . MET B  2  557 ? 111.554 31.962  32.827  1.00 67.46  ?  557 MET B CG  1 
ATOM   9437  S  SD  . MET B  2  557 ? 110.194 32.597  31.822  1.00 47.96  ?  557 MET B SD  1 
ATOM   9438  C  CE  . MET B  2  557 ? 110.642 34.340  31.758  1.00 55.00  ?  557 MET B CE  1 
ATOM   9439  N  N   . SER B  2  558 ? 108.724 31.659  34.329  1.00 47.47  ?  558 SER B N   1 
ATOM   9440  C  CA  . SER B  2  558 ? 107.286 31.898  34.025  1.00 50.31  ?  558 SER B CA  1 
ATOM   9441  C  C   . SER B  2  558 ? 106.376 31.839  35.251  1.00 50.37  ?  558 SER B C   1 
ATOM   9442  O  O   . SER B  2  558 ? 106.708 31.099  36.192  1.00 54.39  ?  558 SER B O   1 
ATOM   9443  C  CB  . SER B  2  558 ? 106.822 30.917  32.988  1.00 50.11  ?  558 SER B CB  1 
ATOM   9444  O  OG  . SER B  2  558 ? 106.594 29.642  33.570  1.00 60.69  ?  558 SER B OG  1 
ATOM   9445  N  N   . GLU B  2  559 ? 105.265 32.583  35.229  1.00 60.52  ?  559 GLU B N   1 
ATOM   9446  C  CA  . GLU B  2  559 ? 104.301 32.477  36.326  1.00 50.24  ?  559 GLU B CA  1 
ATOM   9447  C  C   . GLU B  2  559 ? 103.710 31.055  36.322  1.00 53.71  ?  559 GLU B C   1 
ATOM   9448  O  O   . GLU B  2  559 ? 103.298 30.567  37.375  1.00 66.71  ?  559 GLU B O   1 
ATOM   9449  C  CB  . GLU B  2  559 ? 103.182 33.518  36.191  1.00 46.40  ?  559 GLU B CB  1 
ATOM   9450  C  CG  . GLU B  2  559 ? 103.610 34.922  36.577  1.00 58.83  ?  559 GLU B CG  1 
ATOM   9451  C  CD  . GLU B  2  559 ? 102.763 36.022  35.970  1.00 63.38  ?  559 GLU B CD  1 
ATOM   9452  O  OE1 . GLU B  2  559 ? 102.601 36.037  34.727  1.00 64.08  ?  559 GLU B OE1 1 
ATOM   9453  O  OE2 . GLU B  2  559 ? 102.273 36.881  36.737  1.00 72.71  ?  559 GLU B OE2 1 
ATOM   9454  N  N   . LYS B  2  560 ? 103.702 30.376  35.145  1.00 53.78  ?  560 LYS B N   1 
ATOM   9455  C  CA  . LYS B  2  560 ? 103.234 28.994  35.014  1.00 53.08  ?  560 LYS B CA  1 
ATOM   9456  C  C   . LYS B  2  560 ? 104.068 28.103  35.931  1.00 53.68  ?  560 LYS B C   1 
ATOM   9457  O  O   . LYS B  2  560 ? 103.520 27.236  36.602  1.00 62.02  ?  560 LYS B O   1 
ATOM   9458  C  CB  . LYS B  2  560 ? 103.378 28.502  33.569  1.00 41.26  ?  560 LYS B CB  1 
ATOM   9459  C  CG  . LYS B  2  560 ? 102.366 29.119  32.613  1.00 52.79  ?  560 LYS B CG  1 
ATOM   9460  C  CD  . LYS B  2  560 ? 102.489 28.588  31.194  1.00 59.93  ?  560 LYS B CD  1 
ATOM   9461  C  CE  . LYS B  2  560 ? 103.767 29.010  30.506  1.00 54.94  ?  560 LYS B CE  1 
ATOM   9462  N  NZ  . LYS B  2  560 ? 103.777 28.630  29.076  1.00 60.00  ?  560 LYS B NZ  1 
ATOM   9463  N  N   . ALA B  2  561 ? 105.391 28.335  35.978  1.00 42.86  ?  561 ALA B N   1 
ATOM   9464  C  CA  . ALA B  2  561 ? 106.283 27.568  36.835  1.00 42.99  ?  561 ALA B CA  1 
ATOM   9465  C  C   . ALA B  2  561 ? 105.883 27.710  38.309  1.00 51.40  ?  561 ALA B C   1 
ATOM   9466  O  O   . ALA B  2  561 ? 105.972 26.737  39.053  1.00 55.19  ?  561 ALA B O   1 
ATOM   9467  C  CB  . ALA B  2  561 ? 107.716 28.026  36.638  1.00 41.06  ?  561 ALA B CB  1 
ATOM   9468  N  N   . VAL B  2  562 ? 105.419 28.902  38.729  1.00 51.91  ?  562 VAL B N   1 
ATOM   9469  C  CA  . VAL B  2  562 ? 104.997 29.108  40.121  1.00 47.37  ?  562 VAL B CA  1 
ATOM   9470  C  C   . VAL B  2  562 ? 103.733 28.287  40.375  1.00 52.81  ?  562 VAL B C   1 
ATOM   9471  O  O   . VAL B  2  562 ? 103.626 27.630  41.408  1.00 52.90  ?  562 VAL B O   1 
ATOM   9472  C  CB  . VAL B  2  562 ? 104.768 30.600  40.472  1.00 45.31  ?  562 VAL B CB  1 
ATOM   9473  C  CG1 . VAL B  2  562 ? 104.347 30.757  41.932  1.00 41.07  ?  562 VAL B CG1 1 
ATOM   9474  C  CG2 . VAL B  2  562 ? 106.012 31.430  40.188  1.00 43.37  ?  562 VAL B CG2 1 
ATOM   9475  N  N   . ALA B  2  563 ? 102.777 28.312  39.434  1.00 52.06  ?  563 ALA B N   1 
ATOM   9476  C  CA  . ALA B  2  563 ? 101.547 27.541  39.577  1.00 49.62  ?  563 ALA B CA  1 
ATOM   9477  C  C   . ALA B  2  563 ? 101.876 26.042  39.600  1.00 53.43  ?  563 ALA B C   1 
ATOM   9478  O  O   . ALA B  2  563 ? 101.306 25.306  40.402  1.00 56.69  ?  563 ALA B O   1 
ATOM   9479  C  CB  . ALA B  2  563 ? 100.601 27.856  38.433  1.00 44.94  ?  563 ALA B CB  1 
ATOM   9480  N  N   . ILE B  2  564 ? 102.815 25.601  38.742  1.00 56.02  ?  564 ILE B N   1 
ATOM   9481  C  CA  . ILE B  2  564 ? 103.239 24.201  38.675  1.00 50.84  ?  564 ILE B CA  1 
ATOM   9482  C  C   . ILE B  2  564 ? 103.796 23.836  40.054  1.00 58.58  ?  564 ILE B C   1 
ATOM   9483  O  O   . ILE B  2  564 ? 103.251 22.965  40.725  1.00 62.38  ?  564 ILE B O   1 
ATOM   9484  C  CB  . ILE B  2  564 ? 104.219 23.957  37.486  1.00 45.35  ?  564 ILE B CB  1 
ATOM   9485  C  CG1 . ILE B  2  564 ? 103.445 23.878  36.148  1.00 48.86  ?  564 ILE B CG1 1 
ATOM   9486  C  CG2 . ILE B  2  564 ? 105.043 22.683  37.702  1.00 50.24  ?  564 ILE B CG2 1 
ATOM   9487  C  CD1 . ILE B  2  564 ? 104.260 24.251  34.914  1.00 54.73  ?  564 ILE B CD1 1 
ATOM   9488  N  N   . GLY B  2  565 ? 104.857 24.515  40.478  1.00 49.68  ?  565 GLY B N   1 
ATOM   9489  C  CA  . GLY B  2  565 ? 105.464 24.264  41.776  1.00 39.37  ?  565 GLY B CA  1 
ATOM   9490  C  C   . GLY B  2  565 ? 104.457 24.202  42.903  1.00 52.82  ?  565 GLY B C   1 
ATOM   9491  O  O   . GLY B  2  565 ? 104.484 23.275  43.711  1.00 58.75  ?  565 GLY B O   1 
ATOM   9492  N  N   . THR B  2  566 ? 103.526 25.158  42.931  1.00 48.73  ?  566 THR B N   1 
ATOM   9493  C  CA  . THR B  2  566 ? 102.502 25.193  43.966  1.00 50.15  ?  566 THR B CA  1 
ATOM   9494  C  C   . THR B  2  566 ? 101.612 23.939  43.926  1.00 61.87  ?  566 THR B C   1 
ATOM   9495  O  O   . THR B  2  566 ? 101.389 23.334  44.977  1.00 60.03  ?  566 THR B O   1 
ATOM   9496  C  CB  . THR B  2  566 ? 101.694 26.488  43.875  1.00 47.38  ?  566 THR B CB  1 
ATOM   9497  O  OG1 . THR B  2  566 ? 102.593 27.590  43.999  1.00 55.25  ?  566 THR B OG1 1 
ATOM   9498  C  CG2 . THR B  2  566 ? 100.634 26.582  44.955  1.00 43.37  ?  566 THR B CG2 1 
ATOM   9499  N  N   . TYR B  2  567 ? 101.102 23.538  42.742  1.00 60.04  ?  567 TYR B N   1 
ATOM   9500  C  CA  . TYR B  2  567 ? 100.258 22.343  42.695  1.00 55.48  ?  567 TYR B CA  1 
ATOM   9501  C  C   . TYR B  2  567 ? 101.067 21.073  42.930  1.00 56.33  ?  567 TYR B C   1 
ATOM   9502  O  O   . TYR B  2  567 ? 100.516 20.109  43.446  1.00 55.27  ?  567 TYR B O   1 
ATOM   9503  C  CB  . TYR B  2  567 ? 99.358  22.265  41.442  1.00 51.41  ?  567 TYR B CB  1 
ATOM   9504  C  CG  . TYR B  2  567 ? 99.990  21.944  40.101  1.00 61.03  ?  567 TYR B CG  1 
ATOM   9505  C  CD1 . TYR B  2  567 ? 100.573 20.706  39.863  1.00 51.88  ?  567 TYR B CD1 1 
ATOM   9506  C  CD2 . TYR B  2  567 ? 99.812  22.787  39.012  1.00 68.03  ?  567 TYR B CD2 1 
ATOM   9507  C  CE1 . TYR B  2  567 ? 101.076 20.372  38.610  1.00 44.88  ?  567 TYR B CE1 1 
ATOM   9508  C  CE2 . TYR B  2  567 ? 100.294 22.459  37.752  1.00 66.58  ?  567 TYR B CE2 1 
ATOM   9509  C  CZ  . TYR B  2  567 ? 100.931 21.251  37.553  1.00 61.55  ?  567 TYR B CZ  1 
ATOM   9510  O  OH  . TYR B  2  567 ? 101.409 20.935  36.303  1.00 63.12  ?  567 TYR B OH  1 
ATOM   9511  N  N   . VAL B  2  568 ? 102.370 21.073  42.603  1.00 57.41  ?  568 VAL B N   1 
ATOM   9512  C  CA  . VAL B  2  568 ? 103.211 19.901  42.833  1.00 53.66  ?  568 VAL B CA  1 
ATOM   9513  C  C   . VAL B  2  568 ? 103.371 19.721  44.350  1.00 61.12  ?  568 VAL B C   1 
ATOM   9514  O  O   . VAL B  2  568 ? 103.243 18.600  44.845  1.00 65.98  ?  568 VAL B O   1 
ATOM   9515  C  CB  . VAL B  2  568 ? 104.568 20.006  42.085  1.00 47.92  ?  568 VAL B CB  1 
ATOM   9516  C  CG1 . VAL B  2  568 ? 105.525 18.906  42.519  1.00 47.42  ?  568 VAL B CG1 1 
ATOM   9517  C  CG2 . VAL B  2  568 ? 104.361 19.945  40.574  1.00 38.30  ?  568 VAL B CG2 1 
ATOM   9518  N  N   . VAL B  2  569 ? 103.597 20.823  45.096  1.00 59.33  ?  569 VAL B N   1 
ATOM   9519  C  CA  . VAL B  2  569 ? 103.729 20.754  46.557  1.00 53.79  ?  569 VAL B CA  1 
ATOM   9520  C  C   . VAL B  2  569 ? 102.369 20.404  47.179  1.00 55.65  ?  569 VAL B C   1 
ATOM   9521  O  O   . VAL B  2  569 ? 102.293 19.503  48.009  1.00 57.89  ?  569 VAL B O   1 
ATOM   9522  C  CB  . VAL B  2  569 ? 104.306 22.054  47.164  1.00 47.63  ?  569 VAL B CB  1 
ATOM   9523  C  CG1 . VAL B  2  569 ? 104.384 21.952  48.681  1.00 54.17  ?  569 VAL B CG1 1 
ATOM   9524  C  CG2 . VAL B  2  569 ? 105.685 22.354  46.596  1.00 52.81  ?  569 VAL B CG2 1 
ATOM   9525  N  N   . THR B  2  570 ? 101.296 21.091  46.765  1.00 53.20  ?  570 THR B N   1 
ATOM   9526  C  CA  . THR B  2  570 ? 99.953  20.815  47.282  1.00 51.83  ?  570 THR B CA  1 
ATOM   9527  C  C   . THR B  2  570 ? 99.536  19.359  47.014  1.00 65.98  ?  570 THR B C   1 
ATOM   9528  O  O   . THR B  2  570 ? 98.810  18.772  47.820  1.00 70.93  ?  570 THR B O   1 
ATOM   9529  C  CB  . THR B  2  570 ? 98.951  21.812  46.711  1.00 53.97  ?  570 THR B CB  1 
ATOM   9530  O  OG1 . THR B  2  570 ? 99.442  23.130  46.955  1.00 61.11  ?  570 THR B OG1 1 
ATOM   9531  C  CG2 . THR B  2  570 ? 97.575  21.673  47.330  1.00 45.52  ?  570 THR B CG2 1 
ATOM   9532  N  N   . SER B  2  571 ? 100.000 18.775  45.894  1.00 62.73  ?  571 SER B N   1 
ATOM   9533  C  CA  . SER B  2  571 ? 99.699  17.383  45.551  1.00 55.92  ?  571 SER B CA  1 
ATOM   9534  C  C   . SER B  2  571 ? 100.487 16.383  46.436  1.00 58.35  ?  571 SER B C   1 
ATOM   9535  O  O   . SER B  2  571 ? 100.230 15.184  46.365  1.00 67.32  ?  571 SER B O   1 
ATOM   9536  C  CB  . SER B  2  571 ? 99.976  17.121  44.072  1.00 57.24  ?  571 SER B CB  1 
ATOM   9537  O  OG  . SER B  2  571 ? 99.081  17.832  43.231  1.00 55.11  ?  571 SER B OG  1 
ATOM   9538  N  N   . GLY B  2  572 ? 101.415 16.874  47.260  1.00 64.89  ?  572 GLY B N   1 
ATOM   9539  C  CA  . GLY B  2  572 ? 102.193 16.040  48.170  1.00 63.75  ?  572 GLY B CA  1 
ATOM   9540  C  C   . GLY B  2  572 ? 103.635 15.787  47.779  1.00 56.68  ?  572 GLY B C   1 
ATOM   9541  O  O   . GLY B  2  572 ? 104.325 15.034  48.469  1.00 69.37  ?  572 GLY B O   1 
ATOM   9542  N  N   . ILE B  2  573 ? 104.117 16.413  46.690  1.00 55.31  ?  573 ILE B N   1 
ATOM   9543  C  CA  . ILE B  2  573 ? 105.492 16.213  46.218  1.00 54.95  ?  573 ILE B CA  1 
ATOM   9544  C  C   . ILE B  2  573 ? 106.380 17.405  46.571  1.00 61.71  ?  573 ILE B C   1 
ATOM   9545  O  O   . ILE B  2  573 ? 106.042 18.535  46.226  1.00 66.97  ?  573 ILE B O   1 
ATOM   9546  C  CB  . ILE B  2  573 ? 105.487 15.971  44.693  1.00 44.29  ?  573 ILE B CB  1 
ATOM   9547  C  CG1 . ILE B  2  573 ? 104.693 14.692  44.336  1.00 37.09  ?  573 ILE B CG1 1 
ATOM   9548  C  CG2 . ILE B  2  573 ? 106.916 15.900  44.158  1.00 48.36  ?  573 ILE B CG2 1 
ATOM   9549  C  CD1 . ILE B  2  573 ? 104.086 14.694  42.970  1.00 40.56  ?  573 ILE B CD1 1 
ATOM   9550  N  N   . ASP B  2  574 ? 107.520 17.159  47.239  1.00 52.02  ?  574 ASP B N   1 
ATOM   9551  C  CA  . ASP B  2  574 ? 108.441 18.232  47.616  1.00 44.50  ?  574 ASP B CA  1 
ATOM   9552  C  C   . ASP B  2  574 ? 109.024 18.871  46.369  1.00 54.12  ?  574 ASP B C   1 
ATOM   9553  O  O   . ASP B  2  574 ? 109.420 18.154  45.459  1.00 54.41  ?  574 ASP B O   1 
ATOM   9554  C  CB  . ASP B  2  574 ? 109.579 17.683  48.471  1.00 56.51  ?  574 ASP B CB  1 
ATOM   9555  C  CG  . ASP B  2  574 ? 109.111 17.144  49.796  1.00 73.39  ?  574 ASP B CG  1 
ATOM   9556  O  OD1 . ASP B  2  574 ? 108.549 17.930  50.587  1.00 72.94  ?  574 ASP B OD1 1 
ATOM   9557  O  OD2 . ASP B  2  574 ? 109.309 15.933  50.045  1.00 67.89  ?  574 ASP B OD2 1 
ATOM   9558  N  N   . THR B  2  575 ? 109.084 20.207  46.323  1.00 51.83  ?  575 THR B N   1 
ATOM   9559  C  CA  . THR B  2  575 ? 109.612 20.909  45.161  1.00 42.06  ?  575 THR B CA  1 
ATOM   9560  C  C   . THR B  2  575 ? 110.815 21.771  45.508  1.00 51.08  ?  575 THR B C   1 
ATOM   9561  O  O   . THR B  2  575 ? 110.805 22.479  46.511  1.00 53.29  ?  575 THR B O   1 
ATOM   9562  C  CB  . THR B  2  575 ? 108.507 21.761  44.531  1.00 49.24  ?  575 THR B CB  1 
ATOM   9563  O  OG1 . THR B  2  575 ? 107.434 20.903  44.148  1.00 58.63  ?  575 THR B OG1 1 
ATOM   9564  C  CG2 . THR B  2  575 ? 108.989 22.544  43.318  1.00 49.65  ?  575 THR B CG2 1 
ATOM   9565  N  N   . TRP B  2  576 ? 111.844 21.721  44.656  1.00 54.47  ?  576 TRP B N   1 
ATOM   9566  C  CA  . TRP B  2  576 ? 113.062 22.507  44.801  1.00 51.32  ?  576 TRP B CA  1 
ATOM   9567  C  C   . TRP B  2  576 ? 113.053 23.585  43.724  1.00 56.56  ?  576 TRP B C   1 
ATOM   9568  O  O   . TRP B  2  576 ? 112.667 23.314  42.588  1.00 59.08  ?  576 TRP B O   1 
ATOM   9569  C  CB  . TRP B  2  576 ? 114.306 21.622  44.617  1.00 52.49  ?  576 TRP B CB  1 
ATOM   9570  C  CG  . TRP B  2  576 ? 114.864 21.068  45.889  1.00 47.50  ?  576 TRP B CG  1 
ATOM   9571  C  CD1 . TRP B  2  576 ? 115.950 21.520  46.578  1.00 49.10  ?  576 TRP B CD1 1 
ATOM   9572  C  CD2 . TRP B  2  576 ? 114.370 19.938  46.611  1.00 54.39  ?  576 TRP B CD2 1 
ATOM   9573  N  NE1 . TRP B  2  576 ? 116.155 20.745  47.695  1.00 47.85  ?  576 TRP B NE1 1 
ATOM   9574  C  CE2 . TRP B  2  576 ? 115.200 19.761  47.734  1.00 54.14  ?  576 TRP B CE2 1 
ATOM   9575  C  CE3 . TRP B  2  576 ? 113.305 19.051  46.414  1.00 61.54  ?  576 TRP B CE3 1 
ATOM   9576  C  CZ2 . TRP B  2  576 ? 114.991 18.743  48.660  1.00 58.21  ?  576 TRP B CZ2 1 
ATOM   9577  C  CZ3 . TRP B  2  576 ? 113.102 18.042  47.331  1.00 56.27  ?  576 TRP B CZ3 1 
ATOM   9578  C  CH2 . TRP B  2  576 ? 113.935 17.898  48.440  1.00 59.79  ?  576 TRP B CH2 1 
ATOM   9579  N  N   . LEU B  2  577 ? 113.475 24.802  44.077  1.00 51.42  ?  577 LEU B N   1 
ATOM   9580  C  CA  . LEU B  2  577 ? 113.521 25.913  43.136  1.00 41.97  ?  577 LEU B CA  1 
ATOM   9581  C  C   . LEU B  2  577 ? 114.959 26.398  42.981  1.00 48.67  ?  577 LEU B C   1 
ATOM   9582  O  O   . LEU B  2  577 ? 115.641 26.630  43.973  1.00 56.09  ?  577 LEU B O   1 
ATOM   9583  C  CB  . LEU B  2  577 ? 112.622 27.058  43.632  1.00 45.77  ?  577 LEU B CB  1 
ATOM   9584  C  CG  . LEU B  2  577 ? 111.137 26.733  43.832  1.00 46.28  ?  577 LEU B CG  1 
ATOM   9585  C  CD1 . LEU B  2  577 ? 110.376 27.968  44.264  1.00 42.01  ?  577 LEU B CD1 1 
ATOM   9586  C  CD2 . LEU B  2  577 ? 110.506 26.159  42.569  1.00 32.13  ?  577 LEU B CD2 1 
ATOM   9587  N  N   . GLY B  2  578 ? 115.408 26.526  41.738  1.00 48.08  ?  578 GLY B N   1 
ATOM   9588  C  CA  . GLY B  2  578 ? 116.757 26.986  41.414  1.00 51.93  ?  578 GLY B CA  1 
ATOM   9589  C  C   . GLY B  2  578 ? 116.866 28.493  41.327  1.00 51.20  ?  578 GLY B C   1 
ATOM   9590  O  O   . GLY B  2  578 ? 117.969 29.042  41.329  1.00 63.80  ?  578 GLY B O   1 
ATOM   9591  N  N   . VAL B  2  579 ? 115.719 29.167  41.219  1.00 41.41  ?  579 VAL B N   1 
ATOM   9592  C  CA  . VAL B  2  579 ? 115.625 30.614  41.168  1.00 49.10  ?  579 VAL B CA  1 
ATOM   9593  C  C   . VAL B  2  579 ? 114.754 30.973  42.362  1.00 58.89  ?  579 VAL B C   1 
ATOM   9594  O  O   . VAL B  2  579 ? 113.697 30.363  42.551  1.00 53.10  ?  579 VAL B O   1 
ATOM   9595  C  CB  . VAL B  2  579 ? 114.992 31.079  39.842  1.00 47.11  ?  579 VAL B CB  1 
ATOM   9596  C  CG1 . VAL B  2  579 ? 114.691 32.571  39.873  1.00 55.32  ?  579 VAL B CG1 1 
ATOM   9597  C  CG2 . VAL B  2  579 ? 115.895 30.737  38.668  1.00 54.53  ?  579 VAL B CG2 1 
ATOM   9598  N  N   . ALA B  2  580 ? 115.197 31.924  43.189  1.00 55.33  ?  580 ALA B N   1 
ATOM   9599  C  CA  . ALA B  2  580 ? 114.423 32.309  44.362  1.00 46.43  ?  580 ALA B CA  1 
ATOM   9600  C  C   . ALA B  2  580 ? 113.184 33.117  43.953  1.00 54.12  ?  580 ALA B C   1 
ATOM   9601  O  O   . ALA B  2  580 ? 113.319 34.109  43.234  1.00 64.97  ?  580 ALA B O   1 
ATOM   9602  C  CB  . ALA B  2  580 ? 115.287 33.136  45.298  1.00 62.93  ?  580 ALA B CB  1 
ATOM   9603  N  N   . PRO B  2  581 ? 111.968 32.729  44.384  1.00 54.87  ?  581 PRO B N   1 
ATOM   9604  C  CA  . PRO B  2  581 ? 110.786 33.534  44.025  1.00 47.15  ?  581 PRO B CA  1 
ATOM   9605  C  C   . PRO B  2  581 ? 110.733 34.836  44.844  1.00 60.09  ?  581 PRO B C   1 
ATOM   9606  O  O   . PRO B  2  581 ? 111.474 34.964  45.825  1.00 66.02  ?  581 PRO B O   1 
ATOM   9607  C  CB  . PRO B  2  581 ? 109.615 32.604  44.348  1.00 48.24  ?  581 PRO B CB  1 
ATOM   9608  C  CG  . PRO B  2  581 ? 110.123 31.697  45.402  1.00 52.17  ?  581 PRO B CG  1 
ATOM   9609  C  CD  . PRO B  2  581 ? 111.613 31.587  45.249  1.00 60.31  ?  581 PRO B CD  1 
ATOM   9610  N  N   . PRO B  2  582 ? 109.883 35.825  44.489  1.00 62.74  ?  582 PRO B N   1 
ATOM   9611  C  CA  . PRO B  2  582 ? 109.841 37.066  45.284  1.00 67.94  ?  582 PRO B CA  1 
ATOM   9612  C  C   . PRO B  2  582 ? 109.085 36.906  46.611  1.00 65.36  ?  582 PRO B C   1 
ATOM   9613  O  O   . PRO B  2  582 ? 107.960 37.394  46.753  1.00 61.03  ?  582 PRO B O   1 
ATOM   9614  C  CB  . PRO B  2  582 ? 109.169 38.059  44.335  1.00 55.00  ?  582 PRO B CB  1 
ATOM   9615  C  CG  . PRO B  2  582 ? 108.279 37.226  43.501  1.00 52.14  ?  582 PRO B CG  1 
ATOM   9616  C  CD  . PRO B  2  582 ? 108.927 35.872  43.365  1.00 51.85  ?  582 PRO B CD  1 
ATOM   9617  N  N   . VAL B  2  583 ? 109.711 36.215  47.585  1.00 55.69  ?  583 VAL B N   1 
ATOM   9618  C  CA  . VAL B  2  583 ? 109.101 35.972  48.892  1.00 51.43  ?  583 VAL B CA  1 
ATOM   9619  C  C   . VAL B  2  583 ? 109.992 36.357  50.085  1.00 65.68  ?  583 VAL B C   1 
ATOM   9620  O  O   . VAL B  2  583 ? 109.505 36.366  51.209  1.00 72.54  ?  583 VAL B O   1 
ATOM   9621  C  CB  . VAL B  2  583 ? 108.607 34.508  49.032  1.00 50.87  ?  583 VAL B CB  1 
ATOM   9622  C  CG1 . VAL B  2  583 ? 107.530 34.183  48.004  1.00 53.53  ?  583 VAL B CG1 1 
ATOM   9623  C  CG2 . VAL B  2  583 ? 109.764 33.517  48.945  1.00 48.19  ?  583 VAL B CG2 1 
ATOM   9624  N  N   . THR B  2  584 ? 111.271 36.667  49.859  1.00 61.87  ?  584 THR B N   1 
ATOM   9625  C  CA  . THR B  2  584 ? 112.212 37.034  50.927  1.00 48.59  ?  584 THR B CA  1 
ATOM   9626  C  C   . THR B  2  584 ? 111.673 38.052  51.949  1.00 66.59  ?  584 THR B C   1 
ATOM   9627  O  O   . THR B  2  584 ? 111.879 37.882  53.151  1.00 79.82  ?  584 THR B O   1 
ATOM   9628  C  CB  . THR B  2  584 ? 113.505 37.586  50.304  1.00 62.60  ?  584 THR B CB  1 
ATOM   9629  O  OG1 . THR B  2  584 ? 113.939 36.699  49.275  1.00 76.01  ?  584 THR B OG1 1 
ATOM   9630  C  CG2 . THR B  2  584 ? 114.618 37.769  51.324  1.00 88.65  ?  584 THR B CG2 1 
ATOM   9631  N  N   . GLY B  2  585 ? 111.007 39.098  51.473  1.00 73.32  ?  585 GLY B N   1 
ATOM   9632  C  CA  . GLY B  2  585 ? 110.491 40.158  52.334  1.00 62.03  ?  585 GLY B CA  1 
ATOM   9633  C  C   . GLY B  2  585 ? 109.351 39.814  53.273  1.00 64.52  ?  585 GLY B C   1 
ATOM   9634  O  O   . GLY B  2  585 ? 109.013 40.616  54.145  1.00 74.64  ?  585 GLY B O   1 
ATOM   9635  N  N   . GLY B  2  586 ? 108.757 38.639  53.107  1.00 71.38  ?  586 GLY B N   1 
ATOM   9636  C  CA  . GLY B  2  586 ? 107.651 38.186  53.942  1.00 68.22  ?  586 GLY B CA  1 
ATOM   9637  C  C   . GLY B  2  586 ? 108.058 37.026  54.826  1.00 64.00  ?  586 GLY B C   1 
ATOM   9638  O  O   . GLY B  2  586 ? 107.882 35.871  54.441  1.00 63.70  ?  586 GLY B O   1 
ATOM   9639  N  N   . PRO B  2  587 ? 108.610 37.291  56.024  1.00 58.82  ?  587 PRO B N   1 
ATOM   9640  C  CA  . PRO B  2  587 ? 109.036 36.183  56.901  1.00 59.94  ?  587 PRO B CA  1 
ATOM   9641  C  C   . PRO B  2  587 ? 108.000 35.084  57.136  1.00 65.12  ?  587 PRO B C   1 
ATOM   9642  O  O   . PRO B  2  587 ? 108.361 33.908  57.174  1.00 70.11  ?  587 PRO B O   1 
ATOM   9643  C  CB  . PRO B  2  587 ? 109.402 36.893  58.203  1.00 60.81  ?  587 PRO B CB  1 
ATOM   9644  C  CG  . PRO B  2  587 ? 109.773 38.263  57.795  1.00 72.00  ?  587 PRO B CG  1 
ATOM   9645  C  CD  . PRO B  2  587 ? 108.903 38.603  56.631  1.00 62.04  ?  587 PRO B CD  1 
ATOM   9646  N  N   . GLU B  2  588 ? 106.724 35.460  57.304  1.00 67.23  ?  588 GLU B N   1 
ATOM   9647  C  CA  . GLU B  2  588 ? 105.639 34.503  57.515  1.00 65.64  ?  588 GLU B CA  1 
ATOM   9648  C  C   . GLU B  2  588 ? 105.433 33.688  56.230  1.00 70.75  ?  588 GLU B C   1 
ATOM   9649  O  O   . GLU B  2  588 ? 105.291 32.470  56.296  1.00 70.00  ?  588 GLU B O   1 
ATOM   9650  C  CB  . GLU B  2  588 ? 104.339 35.240  57.899  1.00 71.03  ?  588 GLU B CB  1 
ATOM   9651  C  CG  . GLU B  2  588 ? 103.263 34.352  58.508  1.00 87.18  ?  588 GLU B CG  1 
ATOM   9652  C  CD  . GLU B  2  588 ? 101.921 35.032  58.724  1.00 96.59  ?  588 GLU B CD  1 
ATOM   9653  O  OE1 . GLU B  2  588 ? 101.880 36.285  58.737  1.00 82.08  ?  588 GLU B OE1 1 
ATOM   9654  O  OE2 . GLU B  2  588 ? 100.909 34.310  58.884  1.00 74.14  ?  588 GLU B OE2 1 
ATOM   9655  N  N   . VAL B  2  589 ? 105.454 34.351  55.060  1.00 70.69  ?  589 VAL B N   1 
ATOM   9656  C  CA  . VAL B  2  589 ? 105.280 33.665  53.778  1.00 58.55  ?  589 VAL B CA  1 
ATOM   9657  C  C   . VAL B  2  589 ? 106.418 32.666  53.558  1.00 65.97  ?  589 VAL B C   1 
ATOM   9658  O  O   . VAL B  2  589 ? 106.172 31.544  53.119  1.00 72.45  ?  589 VAL B O   1 
ATOM   9659  C  CB  . VAL B  2  589 ? 105.167 34.651  52.591  1.00 54.95  ?  589 VAL B CB  1 
ATOM   9660  C  CG1 . VAL B  2  589 ? 104.998 33.889  51.278  1.00 60.44  ?  589 VAL B CG1 1 
ATOM   9661  C  CG2 . VAL B  2  589 ? 104.012 35.622  52.800  1.00 63.11  ?  589 VAL B CG2 1 
ATOM   9662  N  N   . VAL B  2  590 ? 107.661 33.056  53.886  1.00 64.25  ?  590 VAL B N   1 
ATOM   9663  C  CA  . VAL B  2  590 ? 108.818 32.171  53.739  1.00 58.56  ?  590 VAL B CA  1 
ATOM   9664  C  C   . VAL B  2  590 ? 108.601 30.942  54.623  1.00 63.22  ?  590 VAL B C   1 
ATOM   9665  O  O   . VAL B  2  590 ? 108.743 29.815  54.157  1.00 60.48  ?  590 VAL B O   1 
ATOM   9666  C  CB  . VAL B  2  590 ? 110.135 32.898  54.107  1.00 54.97  ?  590 VAL B CB  1 
ATOM   9667  C  CG1 . VAL B  2  590 ? 111.303 31.921  54.169  1.00 52.95  ?  590 VAL B CG1 1 
ATOM   9668  C  CG2 . VAL B  2  590 ? 110.431 34.027  53.131  1.00 48.69  ?  590 VAL B CG2 1 
ATOM   9669  N  N   . ASP B  2  591 ? 108.210 31.168  55.886  1.00 55.53  ?  591 ASP B N   1 
ATOM   9670  C  CA  . ASP B  2  591 ? 107.954 30.088  56.831  1.00 57.22  ?  591 ASP B CA  1 
ATOM   9671  C  C   . ASP B  2  591 ? 106.861 29.173  56.280  1.00 68.09  ?  591 ASP B C   1 
ATOM   9672  O  O   . ASP B  2  591 ? 107.014 27.955  56.315  1.00 69.98  ?  591 ASP B O   1 
ATOM   9673  C  CB  . ASP B  2  591 ? 107.599 30.661  58.210  1.00 55.24  ?  591 ASP B CB  1 
ATOM   9674  C  CG  . ASP B  2  591 ? 107.374 29.596  59.265  1.00 94.05  ?  591 ASP B CG  1 
ATOM   9675  O  OD1 . ASP B  2  591 ? 108.261 28.723  59.429  1.00 89.20  ?  591 ASP B OD1 1 
ATOM   9676  O  OD2 . ASP B  2  591 ? 106.311 29.632  59.929  1.00 96.41  ?  591 ASP B OD2 1 
ATOM   9677  N  N   . ILE B  2  592 ? 105.760 29.747  55.775  1.00 70.80  ?  592 ILE B N   1 
ATOM   9678  C  CA  . ILE B  2  592 ? 104.666 28.943  55.234  1.00 66.93  ?  592 ILE B CA  1 
ATOM   9679  C  C   . ILE B  2  592 ? 105.117 28.026  54.088  1.00 64.52  ?  592 ILE B C   1 
ATOM   9680  O  O   . ILE B  2  592 ? 104.953 26.811  54.171  1.00 65.02  ?  592 ILE B O   1 
ATOM   9681  C  CB  . ILE B  2  592 ? 103.450 29.830  54.832  1.00 53.67  ?  592 ILE B CB  1 
ATOM   9682  C  CG1 . ILE B  2  592 ? 102.824 30.504  56.075  1.00 56.59  ?  592 ILE B CG1 1 
ATOM   9683  C  CG2 . ILE B  2  592 ? 102.399 29.000  54.084  1.00 56.79  ?  592 ILE B CG2 1 
ATOM   9684  C  CD1 . ILE B  2  592 ? 102.087 31.828  55.780  1.00 73.14  ?  592 ILE B CD1 1 
ATOM   9685  N  N   . LEU B  2  593 ? 105.706 28.603  53.034  1.00 61.90  ?  593 LEU B N   1 
ATOM   9686  C  CA  . LEU B  2  593 ? 106.143 27.832  51.872  1.00 68.81  ?  593 LEU B CA  1 
ATOM   9687  C  C   . LEU B  2  593 ? 107.259 26.830  52.192  1.00 66.70  ?  593 LEU B C   1 
ATOM   9688  O  O   . LEU B  2  593 ? 107.187 25.683  51.753  1.00 67.96  ?  593 LEU B O   1 
ATOM   9689  C  CB  . LEU B  2  593 ? 106.607 28.776  50.744  1.00 54.74  ?  593 LEU B CB  1 
ATOM   9690  C  CG  . LEU B  2  593 ? 105.584 29.796  50.228  1.00 55.29  ?  593 LEU B CG  1 
ATOM   9691  C  CD1 . LEU B  2  593 ? 106.265 30.895  49.449  1.00 55.68  ?  593 LEU B CD1 1 
ATOM   9692  C  CD2 . LEU B  2  593 ? 104.526 29.137  49.360  1.00 63.58  ?  593 LEU B CD2 1 
ATOM   9693  N  N   . THR B  2  594 ? 108.285 27.250  52.948  1.00 64.45  ?  594 THR B N   1 
ATOM   9694  C  CA  . THR B  2  594 ? 109.419 26.378  53.257  1.00 65.52  ?  594 THR B CA  1 
ATOM   9695  C  C   . THR B  2  594 ? 109.357 25.663  54.614  1.00 64.08  ?  594 THR B C   1 
ATOM   9696  O  O   . THR B  2  594 ? 110.378 25.112  55.019  1.00 75.23  ?  594 THR B O   1 
ATOM   9697  C  CB  . THR B  2  594 ? 110.736 27.166  53.153  1.00 68.19  ?  594 THR B CB  1 
ATOM   9698  O  OG1 . THR B  2  594 ? 110.886 27.995  54.309  1.00 53.60  ?  594 THR B OG1 1 
ATOM   9699  C  CG2 . THR B  2  594 ? 110.829 28.004  51.876  1.00 48.19  ?  594 THR B CG2 1 
ATOM   9700  N  N   . ASN B  2  595 ? 108.201 25.647  55.315  1.00 67.25  ?  595 ASN B N   1 
ATOM   9701  C  CA  . ASN B  2  595 ? 108.126 24.969  56.614  1.00 56.21  ?  595 ASN B CA  1 
ATOM   9702  C  C   . ASN B  2  595 ? 106.702 24.480  56.991  1.00 58.43  ?  595 ASN B C   1 
ATOM   9703  O  O   . ASN B  2  595 ? 106.463 23.274  56.951  1.00 66.45  ?  595 ASN B O   1 
ATOM   9704  C  CB  . ASN B  2  595 ? 108.722 25.862  57.714  1.00 62.13  ?  595 ASN B CB  1 
ATOM   9705  C  CG  . ASN B  2  595 ? 108.701 25.241  59.092  1.00 83.21  ?  595 ASN B CG  1 
ATOM   9706  O  OD1 . ASN B  2  595 ? 109.127 24.092  59.295  1.00 82.58  ?  595 ASN B OD1 1 
ATOM   9707  N  ND2 . ASN B  2  595 ? 108.207 25.989  60.075  1.00 93.36  ?  595 ASN B ND2 1 
ATOM   9708  N  N   . LYS B  2  596 ? 105.763 25.382  57.363  1.00 58.41  ?  596 LYS B N   1 
ATOM   9709  C  CA  . LYS B  2  596 ? 104.415 24.950  57.770  1.00 64.23  ?  596 LYS B CA  1 
ATOM   9710  C  C   . LYS B  2  596 ? 103.688 24.115  56.723  1.00 62.65  ?  596 LYS B C   1 
ATOM   9711  O  O   . LYS B  2  596 ? 102.845 23.304  57.092  1.00 69.83  ?  596 LYS B O   1 
ATOM   9712  C  CB  . LYS B  2  596 ? 103.505 26.134  58.141  1.00 62.02  ?  596 LYS B CB  1 
ATOM   9713  C  CG  . LYS B  2  596 ? 103.812 26.826  59.459  1.00 73.61  ?  596 LYS B CG  1 
ATOM   9714  C  CD  . LYS B  2  596 ? 102.750 27.894  59.750  1.00 80.66  ?  596 LYS B CD  1 
ATOM   9715  C  CE  . LYS B  2  596 ? 103.188 28.950  60.741  1.00 110.02 ?  596 LYS B CE  1 
ATOM   9716  N  NZ  . LYS B  2  596 ? 102.834 30.327  60.282  1.00 106.95 ?  596 LYS B NZ  1 
ATOM   9717  N  N   . MET B  2  597 ? 104.007 24.297  55.440  1.00 51.23  ?  597 MET B N   1 
ATOM   9718  C  CA  . MET B  2  597 ? 103.286 23.566  54.361  1.00 56.85  ?  597 MET B CA  1 
ATOM   9719  C  C   . MET B  2  597 ? 103.382 22.057  54.613  1.00 62.95  ?  597 MET B C   1 
ATOM   9720  O  O   . MET B  2  597 ? 102.385 21.357  54.359  1.00 61.81  ?  597 MET B O   1 
ATOM   9721  C  CB  . MET B  2  597 ? 103.897 23.893  52.995  1.00 56.56  ?  597 MET B CB  1 
ATOM   9722  C  CG  . MET B  2  597 ? 103.073 23.398  51.826  1.00 58.09  ?  597 MET B CG  1 
ATOM   9723  S  SD  . MET B  2  597 ? 101.867 24.627  51.267  1.00 95.93  ?  597 MET B SD  1 
ATOM   9724  C  CE  . MET B  2  597 ? 102.915 25.717  50.305  1.00 56.44  ?  597 MET B CE  1 
ATOM   9725  N  N   . GLU B  2  598 ? 104.533 21.582  55.092  1.00 70.88  ?  598 GLU B N   1 
ATOM   9726  C  CA  . GLU B  2  598 ? 104.766 20.159  55.361  1.00 62.65  ?  598 GLU B CA  1 
ATOM   9727  C  C   . GLU B  2  598 ? 103.675 19.616  56.291  1.00 61.98  ?  598 GLU B C   1 
ATOM   9728  O  O   . GLU B  2  598 ? 103.235 18.481  56.141  1.00 74.23  ?  598 GLU B O   1 
ATOM   9729  C  CB  . GLU B  2  598 ? 106.144 19.976  56.017  1.00 70.42  ?  598 GLU B CB  1 
ATOM   9730  C  CG  . GLU B  2  598 ? 106.590 18.532  56.144  1.00 85.25  ?  598 GLU B CG  1 
ATOM   9731  C  CD  . GLU B  2  598 ? 107.970 18.350  56.748  1.00 92.22  ?  598 GLU B CD  1 
ATOM   9732  O  OE1 . GLU B  2  598 ? 108.611 19.367  57.100  1.00 73.88  ?  598 GLU B OE1 1 
ATOM   9733  O  OE2 . GLU B  2  598 ? 108.408 17.184  56.875  1.00 104.56 ?  598 GLU B OE2 1 
ATOM   9734  N  N   . ASP B  2  599 ? 103.234 20.438  57.244  1.00 67.13  ?  599 ASP B N   1 
ATOM   9735  C  CA  . ASP B  2  599 ? 102.190 20.058  58.188  1.00 75.92  ?  599 ASP B CA  1 
ATOM   9736  C  C   . ASP B  2  599 ? 100.783 20.166  57.568  1.00 62.41  ?  599 ASP B C   1 
ATOM   9737  O  O   . ASP B  2  599 ? 99.830  19.685  58.173  1.00 78.53  ?  599 ASP B O   1 
ATOM   9738  C  CB  . ASP B  2  599 ? 102.291 20.919  59.459  1.00 73.04  ?  599 ASP B CB  1 
ATOM   9739  C  CG  . ASP B  2  599 ? 103.697 21.010  60.024  1.00 86.46  ?  599 ASP B CG  1 
ATOM   9740  O  OD1 . ASP B  2  599 ? 104.328 19.944  60.227  1.00 94.46  ?  599 ASP B OD1 1 
ATOM   9741  O  OD2 . ASP B  2  599 ? 104.170 22.145  60.257  1.00 85.27  ?  599 ASP B OD2 1 
ATOM   9742  N  N   . TRP B  2  600 ? 100.640 20.778  56.378  1.00 58.98  ?  600 TRP B N   1 
ATOM   9743  C  CA  . TRP B  2  600 ? 99.337  20.906  55.734  1.00 65.96  ?  600 TRP B CA  1 
ATOM   9744  C  C   . TRP B  2  600 ? 99.152  19.876  54.622  1.00 74.24  ?  600 TRP B C   1 
ATOM   9745  O  O   . TRP B  2  600 ? 98.081  19.283  54.519  1.00 78.67  ?  600 TRP B O   1 
ATOM   9746  C  CB  . TRP B  2  600 ? 99.156  22.308  55.119  1.00 67.98  ?  600 TRP B CB  1 
ATOM   9747  C  CG  . TRP B  2  600 ? 99.245  23.471  56.063  1.00 52.75  ?  600 TRP B CG  1 
ATOM   9748  C  CD1 . TRP B  2  600 ? 99.314  23.436  57.424  1.00 61.57  ?  600 TRP B CD1 1 
ATOM   9749  C  CD2 . TRP B  2  600 ? 99.255  24.854  55.697  1.00 61.48  ?  600 TRP B CD2 1 
ATOM   9750  N  NE1 . TRP B  2  600 ? 99.388  24.714  57.925  1.00 58.40  ?  600 TRP B NE1 1 
ATOM   9751  C  CE2 . TRP B  2  600 ? 99.357  25.603  56.885  1.00 64.49  ?  600 TRP B CE2 1 
ATOM   9752  C  CE3 . TRP B  2  600 ? 99.208  25.533  54.476  1.00 62.55  ?  600 TRP B CE3 1 
ATOM   9753  C  CZ2 . TRP B  2  600 ? 99.407  26.996  56.884  1.00 77.24  ?  600 TRP B CZ2 1 
ATOM   9754  C  CZ3 . TRP B  2  600 ? 99.263  26.913  54.476  1.00 62.21  ?  600 TRP B CZ3 1 
ATOM   9755  C  CH2 . TRP B  2  600 ? 99.355  27.630  55.669  1.00 65.50  ?  600 TRP B CH2 1 
ATOM   9756  N  N   . VAL B  2  601 ? 100.176 19.676  53.771  1.00 59.62  ?  601 VAL B N   1 
ATOM   9757  C  CA  . VAL B  2  601 ? 100.067 18.759  52.633  1.00 59.62  ?  601 VAL B CA  1 
ATOM   9758  C  C   . VAL B  2  601 ? 101.118 17.634  52.590  1.00 66.30  ?  601 VAL B C   1 
ATOM   9759  O  O   . VAL B  2  601 ? 101.135 16.863  51.633  1.00 56.17  ?  601 VAL B O   1 
ATOM   9760  C  CB  . VAL B  2  601 ? 100.074 19.570  51.319  1.00 65.23  ?  601 VAL B CB  1 
ATOM   9761  C  CG1 . VAL B  2  601 ? 98.917  20.564  51.295  1.00 59.27  ?  601 VAL B CG1 1 
ATOM   9762  C  CG2 . VAL B  2  601 ? 101.406 20.285  51.125  1.00 62.44  ?  601 VAL B CG2 1 
ATOM   9763  N  N   . GLY B  2  602 ? 101.969 17.537  53.601  1.00 65.07  ?  602 GLY B N   1 
ATOM   9764  C  CA  . GLY B  2  602 ? 102.990 16.496  53.651  1.00 70.75  ?  602 GLY B CA  1 
ATOM   9765  C  C   . GLY B  2  602 ? 104.181 16.737  52.745  1.00 71.47  ?  602 GLY B C   1 
ATOM   9766  O  O   . GLY B  2  602 ? 104.956 15.813  52.477  1.00 70.77  ?  602 GLY B O   1 
ATOM   9767  N  N   . ALA B  2  603 ? 104.341 17.979  52.267  1.00 68.08  ?  603 ALA B N   1 
ATOM   9768  C  CA  . ALA B  2  603 ? 105.440 18.367  51.384  1.00 63.68  ?  603 ALA B CA  1 
ATOM   9769  C  C   . ALA B  2  603 ? 105.684 19.867  51.519  1.00 64.04  ?  603 ALA B C   1 
ATOM   9770  O  O   . ALA B  2  603 ? 104.794 20.590  51.963  1.00 64.32  ?  603 ALA B O   1 
ATOM   9771  C  CB  . ALA B  2  603 ? 105.104 18.019  49.942  1.00 55.17  ?  603 ALA B CB  1 
ATOM   9772  N  N   . LYS B  2  604 ? 106.876 20.341  51.143  1.00 62.23  ?  604 LYS B N   1 
ATOM   9773  C  CA  . LYS B  2  604 ? 107.193 21.763  51.259  1.00 54.24  ?  604 LYS B CA  1 
ATOM   9774  C  C   . LYS B  2  604 ? 108.109 22.244  50.126  1.00 58.82  ?  604 LYS B C   1 
ATOM   9775  O  O   . LYS B  2  604 ? 108.573 21.440  49.318  1.00 66.01  ?  604 LYS B O   1 
ATOM   9776  C  CB  . LYS B  2  604 ? 107.840 22.030  52.632  1.00 53.81  ?  604 LYS B CB  1 
ATOM   9777  C  CG  . LYS B  2  604 ? 109.197 21.358  52.804  1.00 55.69  ?  604 LYS B CG  1 
ATOM   9778  C  CD  . LYS B  2  604 ? 110.102 22.080  53.806  1.00 56.82  ?  604 LYS B CD  1 
ATOM   9779  C  CE  . LYS B  2  604 ? 110.150 21.401  55.154  1.00 67.29  ?  604 LYS B CE  1 
ATOM   9780  N  NZ  . LYS B  2  604 ? 110.878 20.096  55.124  1.00 75.05  ?  604 LYS B NZ  1 
ATOM   9781  N  N   . PHE B  2  605 ? 108.367 23.561  50.071  1.00 58.13  ?  605 PHE B N   1 
ATOM   9782  C  CA  . PHE B  2  605 ? 109.250 24.158  49.073  1.00 56.81  ?  605 PHE B CA  1 
ATOM   9783  C  C   . PHE B  2  605 ? 110.678 24.208  49.620  1.00 62.94  ?  605 PHE B C   1 
ATOM   9784  O  O   . PHE B  2  605 ? 110.878 24.358  50.823  1.00 62.93  ?  605 PHE B O   1 
ATOM   9785  C  CB  . PHE B  2  605 ? 108.797 25.591  48.740  1.00 50.97  ?  605 PHE B CB  1 
ATOM   9786  C  CG  . PHE B  2  605 ? 107.719 25.701  47.691  1.00 47.07  ?  605 PHE B CG  1 
ATOM   9787  C  CD1 . PHE B  2  605 ? 108.025 25.592  46.347  1.00 43.71  ?  605 PHE B CD1 1 
ATOM   9788  C  CD2 . PHE B  2  605 ? 106.405 25.954  48.048  1.00 53.86  ?  605 PHE B CD2 1 
ATOM   9789  C  CE1 . PHE B  2  605 ? 107.036 25.715  45.381  1.00 47.95  ?  605 PHE B CE1 1 
ATOM   9790  C  CE2 . PHE B  2  605 ? 105.416 26.076  47.079  1.00 47.71  ?  605 PHE B CE2 1 
ATOM   9791  C  CZ  . PHE B  2  605 ? 105.739 25.963  45.751  1.00 45.06  ?  605 PHE B CZ  1 
ATOM   9792  N  N   . PHE B  2  606 ? 111.667 24.095  48.734  1.00 54.97  ?  606 PHE B N   1 
ATOM   9793  C  CA  . PHE B  2  606 ? 113.079 24.156  49.096  1.00 53.93  ?  606 PHE B CA  1 
ATOM   9794  C  C   . PHE B  2  606 ? 113.728 25.082  48.087  1.00 60.04  ?  606 PHE B C   1 
ATOM   9795  O  O   . PHE B  2  606 ? 113.703 24.763  46.901  1.00 61.51  ?  606 PHE B O   1 
ATOM   9796  C  CB  . PHE B  2  606 ? 113.743 22.774  48.976  1.00 58.19  ?  606 PHE B CB  1 
ATOM   9797  C  CG  . PHE B  2  606 ? 113.318 21.723  49.973  1.00 61.72  ?  606 PHE B CG  1 
ATOM   9798  C  CD1 . PHE B  2  606 ? 112.172 20.974  49.769  1.00 72.15  ?  606 PHE B CD1 1 
ATOM   9799  C  CD2 . PHE B  2  606 ? 114.115 21.416  51.060  1.00 46.88  ?  606 PHE B CD2 1 
ATOM   9800  C  CE1 . PHE B  2  606 ? 111.806 19.974  50.664  1.00 64.55  ?  606 PHE B CE1 1 
ATOM   9801  C  CE2 . PHE B  2  606 ? 113.746 20.418  51.952  1.00 55.15  ?  606 PHE B CE2 1 
ATOM   9802  C  CZ  . PHE B  2  606 ? 112.595 19.703  51.749  1.00 61.40  ?  606 PHE B CZ  1 
ATOM   9803  N  N   . ILE B  2  607 ? 114.291 26.220  48.515  1.00 60.72  ?  607 ILE B N   1 
ATOM   9804  C  CA  . ILE B  2  607 ? 114.938 27.132  47.568  1.00 48.38  ?  607 ILE B CA  1 
ATOM   9805  C  C   . ILE B  2  607 ? 116.438 26.889  47.600  1.00 55.99  ?  607 ILE B C   1 
ATOM   9806  O  O   . ILE B  2  607 ? 117.068 27.110  48.634  1.00 67.92  ?  607 ILE B O   1 
ATOM   9807  C  CB  . ILE B  2  607 ? 114.605 28.609  47.864  1.00 51.32  ?  607 ILE B CB  1 
ATOM   9808  C  CG1 . ILE B  2  607 ? 113.083 28.853  47.785  1.00 46.15  ?  607 ILE B CG1 1 
ATOM   9809  C  CG2 . ILE B  2  607 ? 115.354 29.516  46.887  1.00 40.11  ?  607 ILE B CG2 1 
ATOM   9810  C  CD1 . ILE B  2  607 ? 112.600 30.049  48.553  1.00 49.73  ?  607 ILE B CD1 1 
ATOM   9811  N  N   . GLU B  2  608 ? 117.016 26.424  46.483  1.00 57.39  ?  608 GLU B N   1 
ATOM   9812  C  CA  . GLU B  2  608 ? 118.451 26.169  46.422  1.00 61.06  ?  608 GLU B CA  1 
ATOM   9813  C  C   . GLU B  2  608 ? 118.995 26.513  45.045  1.00 58.79  ?  608 GLU B C   1 
ATOM   9814  O  O   . GLU B  2  608 ? 118.659 25.855  44.060  1.00 54.01  ?  608 GLU B O   1 
ATOM   9815  C  CB  . GLU B  2  608 ? 118.774 24.711  46.783  1.00 52.38  ?  608 GLU B CB  1 
ATOM   9816  C  CG  . GLU B  2  608 ? 120.263 24.435  46.919  1.00 60.14  ?  608 GLU B CG  1 
ATOM   9817  C  CD  . GLU B  2  608 ? 121.001 25.376  47.851  1.00 75.80  ?  608 GLU B CD  1 
ATOM   9818  O  OE1 . GLU B  2  608 ? 120.905 25.188  49.086  1.00 72.76  ?  608 GLU B OE1 1 
ATOM   9819  O  OE2 . GLU B  2  608 ? 121.668 26.309  47.346  1.00 87.48  ?  608 GLU B OE2 1 
ATOM   9820  N  N   . THR B  2  609 ? 119.851 27.542  44.984  1.00 65.19  ?  609 THR B N   1 
ATOM   9821  C  CA  . THR B  2  609 ? 120.447 27.999  43.733  1.00 61.97  ?  609 THR B CA  1 
ATOM   9822  C  C   . THR B  2  609 ? 121.600 27.096  43.293  1.00 66.80  ?  609 THR B C   1 
ATOM   9823  O  O   . THR B  2  609 ? 121.819 26.948  42.093  1.00 85.35  ?  609 THR B O   1 
ATOM   9824  C  CB  . THR B  2  609 ? 120.891 29.447  43.862  1.00 55.05  ?  609 THR B CB  1 
ATOM   9825  O  OG1 . THR B  2  609 ? 121.976 29.517  44.785  1.00 78.35  ?  609 THR B OG1 1 
ATOM   9826  C  CG2 . THR B  2  609 ? 119.763 30.357  44.299  1.00 51.83  ?  609 THR B CG2 1 
ATOM   9827  N  N   . ASP B  2  610 ? 122.337 26.499  44.236  1.00 57.15  ?  610 ASP B N   1 
ATOM   9828  C  CA  . ASP B  2  610 ? 123.434 25.602  43.883  1.00 65.51  ?  610 ASP B CA  1 
ATOM   9829  C  C   . ASP B  2  610 ? 122.842 24.222  43.517  1.00 69.71  ?  610 ASP B C   1 
ATOM   9830  O  O   . ASP B  2  610 ? 122.231 23.596  44.383  1.00 67.31  ?  610 ASP B O   1 
ATOM   9831  C  CB  . ASP B  2  610 ? 124.405 25.466  45.060  1.00 58.37  ?  610 ASP B CB  1 
ATOM   9832  C  CG  . ASP B  2  610 ? 125.589 24.553  44.800  1.00 67.33  ?  610 ASP B CG  1 
ATOM   9833  O  OD1 . ASP B  2  610 ? 125.598 23.871  43.752  1.00 62.84  ?  610 ASP B OD1 1 
ATOM   9834  O  OD2 . ASP B  2  610 ? 126.504 24.516  45.647  1.00 79.51  ?  610 ASP B OD2 1 
ATOM   9835  N  N   . PRO B  2  611 ? 122.993 23.717  42.269  1.00 61.24  ?  611 PRO B N   1 
ATOM   9836  C  CA  . PRO B  2  611 ? 122.403 22.411  41.942  1.00 54.50  ?  611 PRO B CA  1 
ATOM   9837  C  C   . PRO B  2  611 ? 123.034 21.238  42.681  1.00 62.10  ?  611 PRO B C   1 
ATOM   9838  O  O   . PRO B  2  611 ? 122.350 20.249  42.930  1.00 59.76  ?  611 PRO B O   1 
ATOM   9839  C  CB  . PRO B  2  611 ? 122.605 22.298  40.430  1.00 45.00  ?  611 PRO B CB  1 
ATOM   9840  C  CG  . PRO B  2  611 ? 123.756 23.148  40.140  1.00 58.84  ?  611 PRO B CG  1 
ATOM   9841  C  CD  . PRO B  2  611 ? 123.677 24.295  41.097  1.00 65.38  ?  611 PRO B CD  1 
ATOM   9842  N  N   . HIS B  2  612 ? 124.320 21.336  43.038  1.00 58.41  ?  612 HIS B N   1 
ATOM   9843  C  CA  . HIS B  2  612 ? 124.997 20.255  43.749  1.00 58.14  ?  612 HIS B CA  1 
ATOM   9844  C  C   . HIS B  2  612 ? 124.443 20.111  45.153  1.00 56.03  ?  612 HIS B C   1 
ATOM   9845  O  O   . HIS B  2  612 ? 124.249 18.991  45.616  1.00 65.90  ?  612 HIS B O   1 
ATOM   9846  C  CB  . HIS B  2  612 ? 126.504 20.488  43.759  1.00 64.66  ?  612 HIS B CB  1 
ATOM   9847  C  CG  . HIS B  2  612 ? 127.067 20.551  42.376  1.00 70.77  ?  612 HIS B CG  1 
ATOM   9848  N  ND1 . HIS B  2  612 ? 127.167 21.750  41.694  1.00 83.38  ?  612 HIS B ND1 1 
ATOM   9849  C  CD2 . HIS B  2  612 ? 127.491 19.552  41.569  1.00 59.11  ?  612 HIS B CD2 1 
ATOM   9850  C  CE1 . HIS B  2  612 ? 127.672 21.449  40.508  1.00 84.21  ?  612 HIS B CE1 1 
ATOM   9851  N  NE2 . HIS B  2  612 ? 127.885 20.137  40.389  1.00 72.31  ?  612 HIS B NE2 1 
ATOM   9852  N  N   . LYS B  2  613 ? 124.157 21.231  45.824  1.00 59.10  ?  613 LYS B N   1 
ATOM   9853  C  CA  . LYS B  2  613 ? 123.576 21.182  47.160  1.00 55.13  ?  613 LYS B CA  1 
ATOM   9854  C  C   . LYS B  2  613 ? 122.150 20.643  47.039  1.00 54.09  ?  613 LYS B C   1 
ATOM   9855  O  O   . LYS B  2  613 ? 121.749 19.796  47.830  1.00 68.94  ?  613 LYS B O   1 
ATOM   9856  C  CB  . LYS B  2  613 ? 123.570 22.571  47.824  1.00 58.91  ?  613 LYS B CB  1 
ATOM   9857  C  CG  . LYS B  2  613 ? 124.962 23.073  48.212  1.00 76.52  ?  613 LYS B CG  1 
ATOM   9858  C  CD  . LYS B  2  613 ? 124.962 24.528  48.694  1.00 70.82  ?  613 LYS B CD  1 
ATOM   9859  C  CE  . LYS B  2  613 ? 124.663 24.668  50.170  1.00 86.55  ?  613 LYS B CE  1 
ATOM   9860  N  NZ  . LYS B  2  613 ? 124.437 26.086  50.587  1.00 95.54  ?  613 LYS B NZ  1 
ATOM   9861  N  N   . ALA B  2  614 ? 121.395 21.109  46.032  1.00 49.52  ?  614 ALA B N   1 
ATOM   9862  C  CA  . ALA B  2  614 ? 120.022 20.660  45.805  1.00 51.67  ?  614 ALA B CA  1 
ATOM   9863  C  C   . ALA B  2  614 ? 119.934 19.142  45.647  1.00 55.16  ?  614 ALA B C   1 
ATOM   9864  O  O   . ALA B  2  614 ? 119.030 18.528  46.203  1.00 62.88  ?  614 ALA B O   1 
ATOM   9865  C  CB  . ALA B  2  614 ? 119.453 21.336  44.572  1.00 41.09  ?  614 ALA B CB  1 
ATOM   9866  N  N   . VAL B  2  615 ? 120.872 18.532  44.910  1.00 57.15  ?  615 VAL B N   1 
ATOM   9867  C  CA  . VAL B  2  615 ? 120.864 17.081  44.710  1.00 56.11  ?  615 VAL B CA  1 
ATOM   9868  C  C   . VAL B  2  615 ? 121.069 16.371  46.049  1.00 60.98  ?  615 VAL B C   1 
ATOM   9869  O  O   . VAL B  2  615 ? 120.371 15.397  46.339  1.00 62.27  ?  615 VAL B O   1 
ATOM   9870  C  CB  . VAL B  2  615 ? 121.893 16.635  43.646  1.00 37.00  ?  615 VAL B CB  1 
ATOM   9871  C  CG1 . VAL B  2  615 ? 121.984 15.116  43.581  1.00 44.49  ?  615 VAL B CG1 1 
ATOM   9872  C  CG2 . VAL B  2  615 ? 121.531 17.203  42.277  1.00 52.80  ?  615 VAL B CG2 1 
ATOM   9873  N  N   . GLU B  2  616 ? 121.989 16.874  46.889  1.00 57.14  ?  616 GLU B N   1 
ATOM   9874  C  CA  . GLU B  2  616 ? 122.229 16.273  48.203  1.00 62.93  ?  616 GLU B CA  1 
ATOM   9875  C  C   . GLU B  2  616 ? 120.960 16.359  49.047  1.00 56.21  ?  616 GLU B C   1 
ATOM   9876  O  O   . GLU B  2  616 ? 120.557 15.379  49.663  1.00 64.81  ?  616 GLU B O   1 
ATOM   9877  C  CB  . GLU B  2  616 ? 123.385 16.982  48.926  1.00 51.10  ?  616 GLU B CB  1 
ATOM   9878  C  CG  . GLU B  2  616 ? 124.758 16.595  48.408  1.00 78.38  ?  616 GLU B CG  1 
ATOM   9879  C  CD  . GLU B  2  616 ? 125.900 17.134  49.249  1.00 119.00 ?  616 GLU B CD  1 
ATOM   9880  O  OE1 . GLU B  2  616 ? 125.760 18.253  49.794  1.00 110.47 ?  616 GLU B OE1 1 
ATOM   9881  O  OE2 . GLU B  2  616 ? 126.936 16.438  49.362  1.00 122.33 ?  616 GLU B OE2 1 
ATOM   9882  N  N   . GLN B  2  617 ? 120.318 17.521  49.044  1.00 40.39  ?  617 GLN B N   1 
ATOM   9883  C  CA  . GLN B  2  617 ? 119.097 17.731  49.803  1.00 48.97  ?  617 GLN B CA  1 
ATOM   9884  C  C   . GLN B  2  617 ? 117.965 16.822  49.333  1.00 58.75  ?  617 GLN B C   1 
ATOM   9885  O  O   . GLN B  2  617 ? 117.175 16.366  50.159  1.00 61.71  ?  617 GLN B O   1 
ATOM   9886  C  CB  . GLN B  2  617 ? 118.653 19.186  49.684  1.00 45.61  ?  617 GLN B CB  1 
ATOM   9887  C  CG  . GLN B  2  617 ? 119.620 20.160  50.320  1.00 40.58  ?  617 GLN B CG  1 
ATOM   9888  C  CD  . GLN B  2  617 ? 119.388 21.562  49.830  1.00 59.62  ?  617 GLN B CD  1 
ATOM   9889  O  OE1 . GLN B  2  617 ? 118.268 21.950  49.473  1.00 58.95  ?  617 GLN B OE1 1 
ATOM   9890  N  NE2 . GLN B  2  617 ? 120.448 22.360  49.806  1.00 77.05  ?  617 GLN B NE2 1 
ATOM   9891  N  N   . ILE B  2  618 ? 117.873 16.571  48.014  1.00 48.47  ?  618 ILE B N   1 
ATOM   9892  C  CA  . ILE B  2  618 ? 116.818 15.718  47.464  1.00 53.53  ?  618 ILE B CA  1 
ATOM   9893  C  C   . ILE B  2  618 ? 117.030 14.275  47.920  1.00 56.37  ?  618 ILE B C   1 
ATOM   9894  O  O   . ILE B  2  618 ? 116.104 13.645  48.424  1.00 52.83  ?  618 ILE B O   1 
ATOM   9895  C  CB  . ILE B  2  618 ? 116.750 15.821  45.914  1.00 49.84  ?  618 ILE B CB  1 
ATOM   9896  C  CG1 . ILE B  2  618 ? 116.243 17.210  45.480  1.00 49.24  ?  618 ILE B CG1 1 
ATOM   9897  C  CG2 . ILE B  2  618 ? 115.849 14.725  45.331  1.00 44.01  ?  618 ILE B CG2 1 
ATOM   9898  C  CD1 . ILE B  2  618 ? 116.641 17.618  44.065  1.00 54.54  ?  618 ILE B CD1 1 
ATOM   9899  N  N   . VAL B  2  619 ? 118.253 13.758  47.758  1.00 58.33  ?  619 VAL B N   1 
ATOM   9900  C  CA  . VAL B  2  619 ? 118.582 12.389  48.155  1.00 57.29  ?  619 VAL B CA  1 
ATOM   9901  C  C   . VAL B  2  619 ? 118.321 12.184  49.648  1.00 53.93  ?  619 VAL B C   1 
ATOM   9902  O  O   . VAL B  2  619 ? 117.728 11.180  50.029  1.00 57.69  ?  619 VAL B O   1 
ATOM   9903  C  CB  . VAL B  2  619 ? 120.043 12.043  47.782  1.00 47.56  ?  619 VAL B CB  1 
ATOM   9904  C  CG1 . VAL B  2  619 ? 120.454 10.699  48.369  1.00 47.57  ?  619 VAL B CG1 1 
ATOM   9905  C  CG2 . VAL B  2  619 ? 120.236 12.051  46.265  1.00 42.92  ?  619 VAL B CG2 1 
ATOM   9906  N  N   . ASN B  2  620 ? 118.740 13.134  50.487  1.00 53.67  ?  620 ASN B N   1 
ATOM   9907  C  CA  . ASN B  2  620 ? 118.523 13.024  51.926  1.00 59.99  ?  620 ASN B CA  1 
ATOM   9908  C  C   . ASN B  2  620 ? 117.030 13.038  52.254  1.00 58.78  ?  620 ASN B C   1 
ATOM   9909  O  O   . ASN B  2  620 ? 116.574 12.217  53.050  1.00 63.81  ?  620 ASN B O   1 
ATOM   9910  C  CB  . ASN B  2  620 ? 119.233 14.153  52.668  1.00 50.44  ?  620 ASN B CB  1 
ATOM   9911  C  CG  . ASN B  2  620 ? 120.737 14.050  52.636  1.00 68.59  ?  620 ASN B CG  1 
ATOM   9912  O  OD1 . ASN B  2  620 ? 121.319 12.954  52.653  1.00 79.11  ?  620 ASN B OD1 1 
ATOM   9913  N  ND2 . ASN B  2  620 ? 121.408 15.196  52.592  1.00 95.93  ?  620 ASN B ND2 1 
ATOM   9914  N  N   . ARG B  2  621 ? 116.269 13.958  51.648  1.00 55.79  ?  621 ARG B N   1 
ATOM   9915  C  CA  . ARG B  2  621 ? 114.831 14.047  51.886  1.00 59.41  ?  621 ARG B CA  1 
ATOM   9916  C  C   . ARG B  2  621 ? 114.126 12.756  51.440  1.00 63.01  ?  621 ARG B C   1 
ATOM   9917  O  O   . ARG B  2  621 ? 113.190 12.318  52.108  1.00 72.42  ?  621 ARG B O   1 
ATOM   9918  C  CB  . ARG B  2  621 ? 114.251 15.270  51.158  1.00 62.39  ?  621 ARG B CB  1 
ATOM   9919  C  CG  . ARG B  2  621 ? 112.730 15.384  51.205  1.00 66.70  ?  621 ARG B CG  1 
ATOM   9920  C  CD  . ARG B  2  621 ? 112.207 15.659  52.594  1.00 62.86  ?  621 ARG B CD  1 
ATOM   9921  N  NE  . ARG B  2  621 ? 110.821 16.114  52.550  1.00 70.84  ?  621 ARG B NE  1 
ATOM   9922  C  CZ  . ARG B  2  621 ? 110.156 16.607  53.591  1.00 83.94  ?  621 ARG B CZ  1 
ATOM   9923  N  NH1 . ARG B  2  621 ? 110.746 16.713  54.776  1.00 77.40  ?  621 ARG B NH1 1 
ATOM   9924  N  NH2 . ARG B  2  621 ? 108.894 16.997  53.455  1.00 78.40  ?  621 ARG B NH2 1 
ATOM   9925  N  N   . MET B  2  622 ? 114.566 12.147  50.322  1.00 57.89  ?  622 MET B N   1 
ATOM   9926  C  CA  . MET B  2  622 ? 113.963 10.901  49.843  1.00 48.74  ?  622 MET B CA  1 
ATOM   9927  C  C   . MET B  2  622 ? 114.253 9.791   50.839  1.00 62.91  ?  622 MET B C   1 
ATOM   9928  O  O   . MET B  2  622 ? 113.345 9.042   51.183  1.00 68.12  ?  622 MET B O   1 
ATOM   9929  C  CB  . MET B  2  622 ? 114.493 10.510  48.454  1.00 42.07  ?  622 MET B CB  1 
ATOM   9930  C  CG  . MET B  2  622 ? 113.726 11.142  47.321  1.00 49.02  ?  622 MET B CG  1 
ATOM   9931  S  SD  . MET B  2  622 ? 114.602 11.050  45.746  1.00 57.37  ?  622 MET B SD  1 
ATOM   9932  C  CE  . MET B  2  622 ? 113.511 11.978  44.733  1.00 52.94  ?  622 MET B CE  1 
ATOM   9933  N  N   . ASN B  2  623 ? 115.495 9.694   51.334  1.00 59.26  ?  623 ASN B N   1 
ATOM   9934  C  CA  . ASN B  2  623 ? 115.843 8.678   52.328  1.00 53.30  ?  623 ASN B CA  1 
ATOM   9935  C  C   . ASN B  2  623 ? 115.006 8.856   53.600  1.00 64.08  ?  623 ASN B C   1 
ATOM   9936  O  O   . ASN B  2  623 ? 114.597 7.874   54.217  1.00 69.60  ?  623 ASN B O   1 
ATOM   9937  C  CB  . ASN B  2  623 ? 117.320 8.754   52.665  1.00 67.02  ?  623 ASN B CB  1 
ATOM   9938  C  CG  . ASN B  2  623 ? 118.201 8.223   51.570  1.00 68.49  ?  623 ASN B CG  1 
ATOM   9939  O  OD1 . ASN B  2  623 ? 117.924 7.173   50.978  1.00 66.59  ?  623 ASN B OD1 1 
ATOM   9940  N  ND2 . ASN B  2  623 ? 119.285 8.934   51.274  1.00 74.33  ?  623 ASN B ND2 1 
ATOM   9941  N  N   . GLU B  2  624 ? 114.733 10.111  53.977  1.00 68.67  ?  624 GLU B N   1 
ATOM   9942  C  CA  . GLU B  2  624 ? 113.907 10.434  55.137  1.00 69.00  ?  624 GLU B CA  1 
ATOM   9943  C  C   . GLU B  2  624 ? 112.503 9.825   54.933  1.00 68.54  ?  624 GLU B C   1 
ATOM   9944  O  O   . GLU B  2  624 ? 112.000 9.130   55.815  1.00 65.28  ?  624 GLU B O   1 
ATOM   9945  C  CB  . GLU B  2  624 ? 113.837 11.970  55.315  1.00 68.61  ?  624 GLU B CB  1 
ATOM   9946  C  CG  . GLU B  2  624 ? 112.880 12.460  56.392  1.00 98.46  ?  624 GLU B CG  1 
ATOM   9947  C  CD  . GLU B  2  624 ? 112.505 13.929  56.295  1.00 109.06 ?  624 GLU B CD  1 
ATOM   9948  O  OE1 . GLU B  2  624 ? 113.380 14.745  55.923  1.00 106.92 ?  624 GLU B OE1 1 
ATOM   9949  O  OE2 . GLU B  2  624 ? 111.335 14.265  56.597  1.00 94.52  ?  624 GLU B OE2 1 
ATOM   9950  N  N   . LYS B  2  625 ? 111.894 10.055  53.755  1.00 58.26  ?  625 LYS B N   1 
ATOM   9951  C  CA  . LYS B  2  625 ? 110.564 9.518   53.453  1.00 60.55  ?  625 LYS B CA  1 
ATOM   9952  C  C   . LYS B  2  625 ? 110.579 7.990   53.322  1.00 68.64  ?  625 LYS B C   1 
ATOM   9953  O  O   . LYS B  2  625 ? 109.573 7.347   53.620  1.00 63.03  ?  625 LYS B O   1 
ATOM   9954  C  CB  . LYS B  2  625 ? 109.982 10.164  52.183  1.00 54.63  ?  625 LYS B CB  1 
ATOM   9955  C  CG  . LYS B  2  625 ? 109.545 11.613  52.381  1.00 60.16  ?  625 LYS B CG  1 
ATOM   9956  C  CD  . LYS B  2  625 ? 108.598 12.089  51.289  1.00 71.22  ?  625 LYS B CD  1 
ATOM   9957  C  CE  . LYS B  2  625 ? 107.983 13.430  51.614  1.00 60.95  ?  625 LYS B CE  1 
ATOM   9958  N  NZ  . LYS B  2  625 ? 106.942 13.817  50.623  1.00 80.60  ?  625 LYS B NZ  1 
ATOM   9959  N  N   . ARG B  2  626 ? 111.710 7.413   52.879  1.00 62.47  ?  626 ARG B N   1 
ATOM   9960  C  CA  . ARG B  2  626 ? 111.851 5.963   52.745  1.00 52.24  ?  626 ARG B CA  1 
ATOM   9961  C  C   . ARG B  2  626 ? 111.890 5.332   54.130  1.00 65.03  ?  626 ARG B C   1 
ATOM   9962  O  O   . ARG B  2  626 ? 111.336 4.253   54.321  1.00 72.93  ?  626 ARG B O   1 
ATOM   9963  C  CB  . ARG B  2  626 ? 113.153 5.594   52.017  1.00 63.98  ?  626 ARG B CB  1 
ATOM   9964  C  CG  . ARG B  2  626 ? 113.208 5.974   50.546  1.00 65.77  ?  626 ARG B CG  1 
ATOM   9965  C  CD  . ARG B  2  626 ? 114.481 5.460   49.891  1.00 64.71  ?  626 ARG B CD  1 
ATOM   9966  N  NE  . ARG B  2  626 ? 114.506 4.000   49.830  1.00 62.61  ?  626 ARG B NE  1 
ATOM   9967  C  CZ  . ARG B  2  626 ? 113.916 3.268   48.888  1.00 62.07  ?  626 ARG B CZ  1 
ATOM   9968  N  NH1 . ARG B  2  626 ? 113.248 3.853   47.900  1.00 67.19  ?  626 ARG B NH1 1 
ATOM   9969  N  NH2 . ARG B  2  626 ? 113.993 1.946   48.923  1.00 67.32  ?  626 ARG B NH2 1 
ATOM   9970  N  N   . LYS B  2  627 ? 112.572 5.985   55.089  1.00 64.95  ?  627 LYS B N   1 
ATOM   9971  C  CA  . LYS B  2  627 ? 112.675 5.468   56.451  1.00 73.40  ?  627 LYS B CA  1 
ATOM   9972  C  C   . LYS B  2  627 ? 111.305 5.458   57.115  1.00 66.15  ?  627 LYS B C   1 
ATOM   9973  O  O   . LYS B  2  627 ? 110.946 4.466   57.744  1.00 74.90  ?  627 LYS B O   1 
ATOM   9974  C  CB  . LYS B  2  627 ? 113.668 6.302   57.285  1.00 78.51  ?  627 LYS B CB  1 
ATOM   9975  C  CG  . LYS B  2  627 ? 115.120 5.840   57.147  1.00 84.91  ?  627 LYS B CG  1 
ATOM   9976  C  CD  . LYS B  2  627 ? 116.123 6.971   57.322  1.00 124.01 ?  627 LYS B CD  1 
ATOM   9977  C  CE  . LYS B  2  627 ? 117.536 6.507   57.050  1.00 136.35 ?  627 LYS B CE  1 
ATOM   9978  N  NZ  . LYS B  2  627 ? 118.536 7.579   57.304  1.00 146.70 ?  627 LYS B NZ  1 
ATOM   9979  N  N   . LYS B  2  628 ? 110.531 6.543   56.958  1.00 71.34  ?  628 LYS B N   1 
ATOM   9980  C  CA  . LYS B  2  628 ? 109.190 6.631   57.541  1.00 66.13  ?  628 LYS B CA  1 
ATOM   9981  C  C   . LYS B  2  628 ? 108.274 5.523   57.004  1.00 66.06  ?  628 LYS B C   1 
ATOM   9982  O  O   . LYS B  2  628 ? 107.407 5.037   57.726  1.00 81.19  ?  628 LYS B O   1 
ATOM   9983  C  CB  . LYS B  2  628 ? 108.557 8.006   57.251  1.00 72.79  ?  628 LYS B CB  1 
ATOM   9984  C  CG  . LYS B  2  628 ? 109.166 9.148   58.057  1.00 81.49  ?  628 LYS B CG  1 
ATOM   9985  C  CD  . LYS B  2  628 ? 108.514 10.493  57.728  1.00 84.98  ?  628 LYS B CD  1 
ATOM   9986  C  CE  . LYS B  2  628 ? 109.353 11.672  58.187  1.00 115.46 ?  628 LYS B CE  1 
ATOM   9987  N  NZ  . LYS B  2  628 ? 108.992 12.954  57.505  1.00 118.45 ?  628 LYS B NZ  1 
ATOM   9988  N  N   . LEU B  2  629 ? 108.467 5.127   55.743  1.00 65.56  ?  629 LEU B N   1 
ATOM   9989  C  CA  . LEU B  2  629 ? 107.671 4.087   55.094  1.00 58.41  ?  629 LEU B CA  1 
ATOM   9990  C  C   . LEU B  2  629 ? 108.248 2.659   55.299  1.00 60.96  ?  629 LEU B C   1 
ATOM   9991  O  O   . LEU B  2  629 ? 107.553 1.674   55.053  1.00 72.42  ?  629 LEU B O   1 
ATOM   9992  C  CB  . LEU B  2  629 ? 107.600 4.433   53.600  1.00 61.05  ?  629 LEU B CB  1 
ATOM   9993  C  CG  . LEU B  2  629 ? 106.484 3.809   52.782  1.00 56.27  ?  629 LEU B CG  1 
ATOM   9994  C  CD1 . LEU B  2  629 ? 105.130 4.336   53.211  1.00 69.91  ?  629 LEU B CD1 1 
ATOM   9995  C  CD2 . LEU B  2  629 ? 106.706 4.066   51.306  1.00 49.48  ?  629 LEU B CD2 1 
ATOM   9996  N  N   . GLY B  2  630 ? 109.498 2.565   55.748  1.00 65.88  ?  630 GLY B N   1 
ATOM   9997  C  CA  . GLY B  2  630 ? 110.162 1.291   55.996  1.00 60.74  ?  630 GLY B CA  1 
ATOM   9998  C  C   . GLY B  2  630 ? 110.654 0.605   54.737  1.00 71.94  ?  630 GLY B C   1 
ATOM   9999  O  O   . GLY B  2  630 ? 110.601 -0.624  54.653  1.00 75.05  ?  630 GLY B O   1 
ATOM   10000 N  N   . ILE B  2  631 ? 111.150 1.390   53.749  1.00 68.71  ?  631 ILE B N   1 
ATOM   10001 C  CA  . ILE B  2  631 ? 111.649 0.859   52.469  1.00 72.16  ?  631 ILE B CA  1 
ATOM   10002 C  C   . ILE B  2  631 ? 113.072 1.351   52.145  1.00 72.77  ?  631 ILE B C   1 
ATOM   10003 O  O   . ILE B  2  631 ? 113.930 1.462   53.020  1.00 72.66  ?  631 ILE B O   1 
ATOM   10004 C  CB  . ILE B  2  631 ? 110.676 1.204   51.304  1.00 57.14  ?  631 ILE B CB  1 
ATOM   10005 C  CG1 . ILE B  2  631 ? 110.667 2.721   51.007  1.00 57.10  ?  631 ILE B CG1 1 
ATOM   10006 C  CG2 . ILE B  2  631 ? 109.263 0.691   51.592  1.00 53.50  ?  631 ILE B CG2 1 
ATOM   10007 C  CD1 . ILE B  2  631 ? 110.204 3.094   49.609  1.00 64.03  ?  631 ILE B CD1 1 
ATOM   10008 N  N   . GLU C  2  2   ? 100.082 75.711  55.428  1.00 140.61 ?  2   GLU C N   1 
ATOM   10009 C  CA  . GLU C  2  2   ? 101.394 75.181  55.066  1.00 155.43 ?  2   GLU C CA  1 
ATOM   10010 C  C   . GLU C  2  2   ? 101.238 73.764  54.495  1.00 152.64 ?  2   GLU C C   1 
ATOM   10011 O  O   . GLU C  2  2   ? 101.462 73.562  53.302  1.00 152.30 ?  2   GLU C O   1 
ATOM   10012 C  CB  . GLU C  2  2   ? 102.340 75.197  56.281  1.00 157.81 ?  2   GLU C CB  1 
ATOM   10013 C  CG  . GLU C  2  2   ? 102.524 76.575  56.894  1.00 160.04 ?  2   GLU C CG  1 
ATOM   10014 C  CD  . GLU C  2  2   ? 103.163 76.573  58.268  1.00 166.39 ?  2   GLU C CD  1 
ATOM   10015 O  OE1 . GLU C  2  2   ? 103.727 75.526  58.665  1.00 164.32 ?  2   GLU C OE1 1 
ATOM   10016 O  OE2 . GLU C  2  2   ? 103.099 77.621  58.950  1.00 163.96 ?  2   GLU C OE2 1 
ATOM   10017 N  N   . GLU C  2  3   ? 100.837 72.790  55.331  1.00 145.05 ?  3   GLU C N   1 
ATOM   10018 C  CA  . GLU C  2  3   ? 100.629 71.415  54.883  1.00 146.52 ?  3   GLU C CA  1 
ATOM   10019 C  C   . GLU C  2  3   ? 99.241  71.351  54.230  1.00 137.69 ?  3   GLU C C   1 
ATOM   10020 O  O   . GLU C  2  3   ? 98.314  72.009  54.709  1.00 137.37 ?  3   GLU C O   1 
ATOM   10021 C  CB  . GLU C  2  3   ? 100.718 70.453  56.085  1.00 146.59 ?  3   GLU C CB  1 
ATOM   10022 C  CG  . GLU C  2  3   ? 100.669 68.979  55.719  1.00 162.71 ?  3   GLU C CG  1 
ATOM   10023 C  CD  . GLU C  2  3   ? 100.673 68.038  56.909  1.00 165.16 ?  3   GLU C CD  1 
ATOM   10024 O  OE1 . GLU C  2  3   ? 101.083 68.469  58.011  1.00 167.72 ?  3   GLU C OE1 1 
ATOM   10025 O  OE2 . GLU C  2  3   ? 100.266 66.866  56.738  1.00 145.57 ?  3   GLU C OE2 1 
ATOM   10026 N  N   . LYS C  2  4   ? 99.090  70.587  53.137  1.00 118.71 ?  4   LYS C N   1 
ATOM   10027 C  CA  . LYS C  2  4   ? 97.794  70.482  52.456  1.00 104.34 ?  4   LYS C CA  1 
ATOM   10028 C  C   . LYS C  2  4   ? 96.741  69.895  53.395  1.00 106.75 ?  4   LYS C C   1 
ATOM   10029 O  O   . LYS C  2  4   ? 97.059  69.022  54.199  1.00 134.99 ?  4   LYS C O   1 
ATOM   10030 C  CB  . LYS C  2  4   ? 97.913  69.626  51.177  1.00 106.14 ?  4   LYS C CB  1 
ATOM   10031 C  CG  . LYS C  2  4   ? 98.421  70.405  49.957  1.00 125.41 ?  4   LYS C CG  1 
ATOM   10032 C  CD  . LYS C  2  4   ? 99.422  69.622  49.111  1.00 122.53 ?  4   LYS C CD  1 
ATOM   10033 C  CE  . LYS C  2  4   ? 100.097 70.486  48.067  1.00 125.65 ?  4   LYS C CE  1 
ATOM   10034 N  NZ  . LYS C  2  4   ? 101.037 71.477  48.663  1.00 103.50 ?  4   LYS C NZ  1 
ATOM   10035 N  N   . ALA C  2  5   ? 95.499  70.386  53.314  1.00 90.82  ?  5   ALA C N   1 
ATOM   10036 C  CA  . ALA C  2  5   ? 94.425  69.903  54.178  1.00 80.66  ?  5   ALA C CA  1 
ATOM   10037 C  C   . ALA C  2  5   ? 94.180  68.412  53.980  1.00 84.23  ?  5   ALA C C   1 
ATOM   10038 O  O   . ALA C  2  5   ? 94.331  67.900  52.874  1.00 89.76  ?  5   ALA C O   1 
ATOM   10039 C  CB  . ALA C  2  5   ? 93.148  70.679  53.902  1.00 98.98  ?  5   ALA C CB  1 
ATOM   10040 N  N   . LYS C  2  6   ? 93.808  67.714  55.051  1.00 77.20  ?  6   LYS C N   1 
ATOM   10041 C  CA  . LYS C  2  6   ? 93.556  66.278  54.980  1.00 79.68  ?  6   LYS C CA  1 
ATOM   10042 C  C   . LYS C  2  6   ? 92.168  66.008  54.407  1.00 76.64  ?  6   LYS C C   1 
ATOM   10043 O  O   . LYS C  2  6   ? 91.990  65.067  53.636  1.00 88.02  ?  6   LYS C O   1 
ATOM   10044 C  CB  . LYS C  2  6   ? 93.668  65.635  56.371  1.00 86.86  ?  6   LYS C CB  1 
ATOM   10045 C  CG  . LYS C  2  6   ? 94.947  65.979  57.141  1.00 97.02  ?  6   LYS C CG  1 
ATOM   10046 C  CD  . LYS C  2  6   ? 96.075  64.994  56.898  1.00 87.19  ?  6   LYS C CD  1 
ATOM   10047 C  CE  . LYS C  2  6   ? 97.141  65.059  57.967  1.00 78.53  ?  6   LYS C CE  1 
ATOM   10048 N  NZ  . LYS C  2  6   ? 96.774  64.272  59.173  1.00 83.77  ?  6   LYS C NZ  1 
ATOM   10049 N  N   . SER C  2  7   ? 91.182  66.824  54.786  1.00 78.53  ?  7   SER C N   1 
ATOM   10050 C  CA  . SER C  2  7   ? 89.814  66.652  54.320  1.00 77.52  ?  7   SER C CA  1 
ATOM   10051 C  C   . SER C  2  7   ? 89.049  67.981  54.359  1.00 82.17  ?  7   SER C C   1 
ATOM   10052 O  O   . SER C  2  7   ? 89.517  68.949  54.956  1.00 82.54  ?  7   SER C O   1 
ATOM   10053 C  CB  . SER C  2  7   ? 89.105  65.629  55.204  1.00 79.34  ?  7   SER C CB  1 
ATOM   10054 O  OG  . SER C  2  7   ? 87.779  65.381  54.770  1.00 85.09  ?  7   SER C OG  1 
ATOM   10055 N  N   . ILE C  2  8   ? 87.875  68.024  53.718  1.00 80.75  ?  8   ILE C N   1 
ATOM   10056 C  CA  . ILE C  2  8   ? 87.021  69.217  53.712  1.00 74.21  ?  8   ILE C CA  1 
ATOM   10057 C  C   . ILE C  2  8   ? 85.879  69.089  54.738  1.00 67.91  ?  8   ILE C C   1 
ATOM   10058 O  O   . ILE C  2  8   ? 85.189  70.070  55.000  1.00 86.25  ?  8   ILE C O   1 
ATOM   10059 C  CB  . ILE C  2  8   ? 86.467  69.527  52.299  1.00 62.46  ?  8   ILE C CB  1 
ATOM   10060 C  CG1 . ILE C  2  8   ? 85.539  68.398  51.778  1.00 75.76  ?  8   ILE C CG1 1 
ATOM   10061 C  CG2 . ILE C  2  8   ? 87.612  69.786  51.336  1.00 67.97  ?  8   ILE C CG2 1 
ATOM   10062 C  CD1 . ILE C  2  8   ? 84.489  68.847  50.778  1.00 75.70  ?  8   ILE C CD1 1 
ATOM   10063 N  N   . ASP C  2  9   ? 85.675  67.889  55.308  1.00 69.56  ?  9   ASP C N   1 
ATOM   10064 C  CA  . ASP C  2  9   ? 84.626  67.638  56.289  1.00 86.84  ?  9   ASP C CA  1 
ATOM   10065 C  C   . ASP C  2  9   ? 85.135  67.974  57.691  1.00 93.30  ?  9   ASP C C   1 
ATOM   10066 O  O   . ASP C  2  9   ? 86.158  67.437  58.111  1.00 89.53  ?  9   ASP C O   1 
ATOM   10067 C  CB  . ASP C  2  9   ? 84.197  66.169  56.204  1.00 82.71  ?  9   ASP C CB  1 
ATOM   10068 C  CG  . ASP C  2  9   ? 83.051  65.808  57.118  1.00 97.07  ?  9   ASP C CG  1 
ATOM   10069 O  OD1 . ASP C  2  9   ? 82.207  66.690  57.388  1.00 115.97 ?  9   ASP C OD1 1 
ATOM   10070 O  OD2 . ASP C  2  9   ? 82.993  64.641  57.561  1.00 106.84 ?  9   ASP C OD2 1 
ATOM   10071 N  N   . GLN C  2  10  ? 84.424  68.857  58.416  1.00 89.55  ?  10  GLN C N   1 
ATOM   10072 C  CA  . GLN C  2  10  ? 84.845  69.260  59.756  1.00 84.00  ?  10  GLN C CA  1 
ATOM   10073 C  C   . GLN C  2  10  ? 84.814  68.112  60.755  1.00 90.59  ?  10  GLN C C   1 
ATOM   10074 O  O   . GLN C  2  10  ? 85.638  68.092  61.667  1.00 96.13  ?  10  GLN C O   1 
ATOM   10075 C  CB  . GLN C  2  10  ? 84.013  70.452  60.268  1.00 103.79 ?  10  GLN C CB  1 
ATOM   10076 C  CG  . GLN C  2  10  ? 84.775  71.380  61.219  1.00 107.22 ?  10  GLN C CG  1 
ATOM   10077 C  CD  . GLN C  2  10  ? 86.006  71.981  60.573  1.00 109.39 ?  10  GLN C CD  1 
ATOM   10078 O  OE1 . GLN C  2  10  ? 86.013  72.316  59.379  1.00 96.55  ?  10  GLN C OE1 1 
ATOM   10079 N  NE2 . GLN C  2  10  ? 87.080  72.130  61.342  1.00 109.55 ?  10  GLN C NE2 1 
ATOM   10080 N  N   . ALA C  2  11  ? 83.893  67.154  60.596  1.00 88.56  ?  11  ALA C N   1 
ATOM   10081 C  CA  . ALA C  2  11  ? 83.827  66.002  61.496  1.00 90.21  ?  11  ALA C CA  1 
ATOM   10082 C  C   . ALA C  2  11  ? 85.100  65.159  61.342  1.00 89.31  ?  11  ALA C C   1 
ATOM   10083 O  O   . ALA C  2  11  ? 85.652  64.685  62.337  1.00 88.96  ?  11  ALA C O   1 
ATOM   10084 C  CB  . ALA C  2  11  ? 82.604  65.161  61.175  1.00 97.17  ?  11  ALA C CB  1 
ATOM   10085 N  N   . THR C  2  12  ? 85.567  64.991  60.089  1.00 86.45  ?  12  THR C N   1 
ATOM   10086 C  CA  . THR C  2  12  ? 86.783  64.236  59.774  1.00 92.51  ?  12  THR C CA  1 
ATOM   10087 C  C   . THR C  2  12  ? 88.002  64.950  60.378  1.00 91.12  ?  12  THR C C   1 
ATOM   10088 O  O   . THR C  2  12  ? 88.836  64.315  61.024  1.00 92.78  ?  12  THR C O   1 
ATOM   10089 C  CB  . THR C  2  12  ? 86.919  64.078  58.241  1.00 87.56  ?  12  THR C CB  1 
ATOM   10090 O  OG1 . THR C  2  12  ? 85.851  63.264  57.750  1.00 91.16  ?  12  THR C OG1 1 
ATOM   10091 C  CG2 . THR C  2  12  ? 88.249  63.478  57.824  1.00 90.93  ?  12  THR C CG2 1 
ATOM   10092 N  N   . LEU C  2  13  ? 88.097  66.268  60.174  1.00 86.58  ?  13  LEU C N   1 
ATOM   10093 C  CA  . LEU C  2  13  ? 89.212  67.057  60.687  1.00 75.63  ?  13  LEU C CA  1 
ATOM   10094 C  C   . LEU C  2  13  ? 89.290  67.023  62.213  1.00 82.06  ?  13  LEU C C   1 
ATOM   10095 O  O   . LEU C  2  13  ? 90.390  67.036  62.763  1.00 81.55  ?  13  LEU C O   1 
ATOM   10096 C  CB  . LEU C  2  13  ? 89.101  68.509  60.193  1.00 68.88  ?  13  LEU C CB  1 
ATOM   10097 C  CG  . LEU C  2  13  ? 89.349  68.726  58.694  1.00 73.84  ?  13  LEU C CG  1 
ATOM   10098 C  CD1 . LEU C  2  13  ? 88.717  70.012  58.218  1.00 84.95  ?  13  LEU C CD1 1 
ATOM   10099 C  CD2 . LEU C  2  13  ? 90.835  68.739  58.376  1.00 78.49  ?  13  LEU C CD2 1 
ATOM   10100 N  N   . GLN C  2  14  ? 88.131  66.978  62.896  1.00 80.82  ?  14  GLN C N   1 
ATOM   10101 C  CA  . GLN C  2  14  ? 88.087  66.944  64.360  1.00 87.15  ?  14  GLN C CA  1 
ATOM   10102 C  C   . GLN C  2  14  ? 88.622  65.617  64.890  1.00 96.27  ?  14  GLN C C   1 
ATOM   10103 O  O   . GLN C  2  14  ? 89.439  65.614  65.813  1.00 92.32  ?  14  GLN C O   1 
ATOM   10104 C  CB  . GLN C  2  14  ? 86.653  67.180  64.879  1.00 86.63  ?  14  GLN C CB  1 
ATOM   10105 C  CG  . GLN C  2  14  ? 86.231  68.651  64.874  1.00 110.94 ?  14  GLN C CG  1 
ATOM   10106 C  CD  . GLN C  2  14  ? 84.752  68.844  65.120  1.00 111.14 ?  14  GLN C CD  1 
ATOM   10107 O  OE1 . GLN C  2  14  ? 84.072  67.983  65.692  1.00 104.51 ?  14  GLN C OE1 1 
ATOM   10108 N  NE2 . GLN C  2  14  ? 84.220  69.987  64.697  1.00 93.67  ?  14  GLN C NE2 1 
ATOM   10109 N  N   . LEU C  2  15  ? 88.175  64.491  64.314  1.00 89.54  ?  15  LEU C N   1 
ATOM   10110 C  CA  . LEU C  2  15  ? 88.652  63.188  64.767  1.00 86.09  ?  15  LEU C CA  1 
ATOM   10111 C  C   . LEU C  2  15  ? 90.108  62.954  64.405  1.00 89.07  ?  15  LEU C C   1 
ATOM   10112 O  O   . LEU C  2  15  ? 90.772  62.176  65.086  1.00 94.61  ?  15  LEU C O   1 
ATOM   10113 C  CB  . LEU C  2  15  ? 87.772  62.051  64.240  1.00 69.56  ?  15  LEU C CB  1 
ATOM   10114 C  CG  . LEU C  2  15  ? 86.440  61.868  64.972  1.00 84.09  ?  15  LEU C CG  1 
ATOM   10115 C  CD1 . LEU C  2  15  ? 85.463  61.133  64.119  1.00 78.59  ?  15  LEU C CD1 1 
ATOM   10116 C  CD2 . LEU C  2  15  ? 86.626  61.120  66.286  1.00 74.49  ?  15  LEU C CD2 1 
ATOM   10117 N  N   . LEU C  2  16  ? 90.624  63.629  63.363  1.00 83.23  ?  16  LEU C N   1 
ATOM   10118 C  CA  . LEU C  2  16  ? 92.033  63.480  62.998  1.00 89.98  ?  16  LEU C CA  1 
ATOM   10119 C  C   . LEU C  2  16  ? 92.908  64.064  64.113  1.00 95.72  ?  16  LEU C C   1 
ATOM   10120 O  O   . LEU C  2  16  ? 93.970  63.515  64.401  1.00 87.16  ?  16  LEU C O   1 
ATOM   10121 C  CB  . LEU C  2  16  ? 92.346  64.158  61.649  1.00 84.98  ?  16  LEU C CB  1 
ATOM   10122 C  CG  . LEU C  2  16  ? 92.138  63.294  60.393  1.00 77.02  ?  16  LEU C CG  1 
ATOM   10123 C  CD1 . LEU C  2  16  ? 91.997  64.147  59.158  1.00 80.67  ?  16  LEU C CD1 1 
ATOM   10124 C  CD2 . LEU C  2  16  ? 93.285  62.311  60.203  1.00 80.96  ?  16  LEU C CD2 1 
ATOM   10125 N  N   . ASP C  2  17  ? 92.456  65.154  64.759  1.00 92.66  ?  17  ASP C N   1 
ATOM   10126 C  CA  . ASP C  2  17  ? 93.195  65.753  65.867  1.00 93.50  ?  17  ASP C CA  1 
ATOM   10127 C  C   . ASP C  2  17  ? 93.162  64.791  67.055  1.00 95.00  ?  17  ASP C C   1 
ATOM   10128 O  O   . ASP C  2  17  ? 94.180  64.619  67.725  1.00 98.18  ?  17  ASP C O   1 
ATOM   10129 C  CB  . ASP C  2  17  ? 92.585  67.105  66.262  1.00 89.70  ?  17  ASP C CB  1 
ATOM   10130 C  CG  . ASP C  2  17  ? 92.700  68.161  65.184  1.00 109.45 ?  17  ASP C CG  1 
ATOM   10131 O  OD1 . ASP C  2  17  ? 93.590  68.028  64.313  1.00 107.90 ?  17  ASP C OD1 1 
ATOM   10132 O  OD2 . ASP C  2  17  ? 91.898  69.124  65.208  1.00 117.38 ?  17  ASP C OD2 1 
ATOM   10133 N  N   . LYS C  2  18  ? 92.001  64.147  67.306  1.00 88.16  ?  18  LYS C N   1 
ATOM   10134 C  CA  . LYS C  2  18  ? 91.866  63.180  68.393  1.00 91.36  ?  18  LYS C CA  1 
ATOM   10135 C  C   . LYS C  2  18  ? 92.817  62.015  68.160  1.00 96.01  ?  18  LYS C C   1 
ATOM   10136 O  O   . LYS C  2  18  ? 93.474  61.581  69.098  1.00 97.74  ?  18  LYS C O   1 
ATOM   10137 C  CB  . LYS C  2  18  ? 90.422  62.660  68.508  1.00 86.92  ?  18  LYS C CB  1 
ATOM   10138 C  CG  . LYS C  2  18  ? 90.262  61.592  69.595  1.00 79.48  ?  18  LYS C CG  1 
ATOM   10139 C  CD  . LYS C  2  18  ? 88.813  61.302  69.943  1.00 85.34  ?  18  LYS C CD  1 
ATOM   10140 C  CE  . LYS C  2  18  ? 88.659  60.545  71.244  1.00 88.03  ?  18  LYS C CE  1 
ATOM   10141 N  NZ  . LYS C  2  18  ? 89.169  59.148  71.163  1.00 82.68  ?  18  LYS C NZ  1 
ATOM   10142 N  N   . ALA C  2  19  ? 92.906  61.523  66.915  1.00 91.30  ?  19  ALA C N   1 
ATOM   10143 C  CA  . ALA C  2  19  ? 93.798  60.417  66.573  1.00 82.74  ?  19  ALA C CA  1 
ATOM   10144 C  C   . ALA C  2  19  ? 95.257  60.756  66.895  1.00 85.90  ?  19  ALA C C   1 
ATOM   10145 O  O   . ALA C  2  19  ? 95.996  59.883  67.346  1.00 96.21  ?  19  ALA C O   1 
ATOM   10146 C  CB  . ALA C  2  19  ? 93.654  60.070  65.102  1.00 67.95  ?  19  ALA C CB  1 
ATOM   10147 N  N   . LYS C  2  20  ? 95.672  62.014  66.683  1.00 76.86  ?  20  LYS C N   1 
ATOM   10148 C  CA  . LYS C  2  20  ? 97.038  62.427  66.989  1.00 75.58  ?  20  LYS C CA  1 
ATOM   10149 C  C   . LYS C  2  20  ? 97.242  62.425  68.502  1.00 85.05  ?  20  LYS C C   1 
ATOM   10150 O  O   . LYS C  2  20  ? 98.265  61.933  68.984  1.00 92.49  ?  20  LYS C O   1 
ATOM   10151 C  CB  . LYS C  2  20  ? 97.324  63.824  66.419  1.00 79.89  ?  20  LYS C CB  1 
ATOM   10152 C  CG  . LYS C  2  20  ? 98.806  64.168  66.368  1.00 75.09  ?  20  LYS C CG  1 
ATOM   10153 C  CD  . LYS C  2  20  ? 99.016  65.650  66.156  1.00 103.23 ?  20  LYS C CD  1 
ATOM   10154 C  CE  . LYS C  2  20  ? 100.437 65.976  65.777  1.00 105.28 ?  20  LYS C CE  1 
ATOM   10155 N  NZ  . LYS C  2  20  ? 100.631 67.438  65.589  1.00 117.48 ?  20  LYS C NZ  1 
ATOM   10156 N  N   . GLN C  2  21  ? 96.262  62.961  69.252  1.00 85.17  ?  21  GLN C N   1 
ATOM   10157 C  CA  . GLN C  2  21  ? 96.316  63.012  70.715  1.00 88.32  ?  21  GLN C CA  1 
ATOM   10158 C  C   . GLN C  2  21  ? 96.279  61.604  71.322  1.00 96.92  ?  21  GLN C C   1 
ATOM   10159 O  O   . GLN C  2  21  ? 96.863  61.383  72.384  1.00 107.64 ?  21  GLN C O   1 
ATOM   10160 C  CB  . GLN C  2  21  ? 95.153  63.847  71.271  1.00 104.01 ?  21  GLN C CB  1 
ATOM   10161 C  CG  . GLN C  2  21  ? 95.224  65.328  70.913  1.00 121.50 ?  21  GLN C CG  1 
ATOM   10162 C  CD  . GLN C  2  21  ? 96.412  66.022  71.534  1.00 127.23 ?  21  GLN C CD  1 
ATOM   10163 O  OE1 . GLN C  2  21  ? 96.773  65.773  72.691  1.00 124.06 ?  21  GLN C OE1 1 
ATOM   10164 N  NE2 . GLN C  2  21  ? 97.047  66.916  70.783  1.00 128.69 ?  21  GLN C NE2 1 
ATOM   10165 N  N   . ASP C  2  22  ? 95.592  60.658  70.658  1.00 92.81  ?  22  ASP C N   1 
ATOM   10166 C  CA  . ASP C  2  22  ? 95.506  59.270  71.114  1.00 91.69  ?  22  ASP C CA  1 
ATOM   10167 C  C   . ASP C  2  22  ? 96.775  58.476  70.749  1.00 88.80  ?  22  ASP C C   1 
ATOM   10168 O  O   . ASP C  2  22  ? 97.043  57.445  71.363  1.00 94.61  ?  22  ASP C O   1 
ATOM   10169 C  CB  . ASP C  2  22  ? 94.261  58.577  70.528  1.00 77.72  ?  22  ASP C CB  1 
ATOM   10170 C  CG  . ASP C  2  22  ? 92.935  59.088  71.068  1.00 96.10  ?  22  ASP C CG  1 
ATOM   10171 O  OD1 . ASP C  2  22  ? 92.952  59.908  72.015  1.00 92.67  ?  22  ASP C OD1 1 
ATOM   10172 O  OD2 . ASP C  2  22  ? 91.881  58.668  70.545  1.00 96.01  ?  22  ASP C OD2 1 
ATOM   10173 N  N   . GLY C  2  23  ? 97.534  58.953  69.763  1.00 81.96  ?  23  GLY C N   1 
ATOM   10174 C  CA  . GLY C  2  23  ? 98.769  58.312  69.331  1.00 94.33  ?  23  GLY C CA  1 
ATOM   10175 C  C   . GLY C  2  23  ? 98.584  57.232  68.285  1.00 86.53  ?  23  GLY C C   1 
ATOM   10176 O  O   . GLY C  2  23  ? 99.502  56.446  68.044  1.00 93.34  ?  23  GLY C O   1 
ATOM   10177 N  N   . VAL C  2  24  ? 97.411  57.188  67.641  1.00 80.90  ?  24  VAL C N   1 
ATOM   10178 C  CA  . VAL C  2  24  ? 97.147  56.181  66.616  1.00 71.53  ?  24  VAL C CA  1 
ATOM   10179 C  C   . VAL C  2  24  ? 97.507  56.720  65.233  1.00 81.24  ?  24  VAL C C   1 
ATOM   10180 O  O   . VAL C  2  24  ? 97.525  57.934  65.018  1.00 82.20  ?  24  VAL C O   1 
ATOM   10181 C  CB  . VAL C  2  24  ? 95.693  55.639  66.670  1.00 68.18  ?  24  VAL C CB  1 
ATOM   10182 C  CG1 . VAL C  2  24  ? 95.333  55.155  68.070  1.00 65.45  ?  24  VAL C CG1 1 
ATOM   10183 C  CG2 . VAL C  2  24  ? 94.683  56.671  66.179  1.00 84.36  ?  24  VAL C CG2 1 
ATOM   10184 N  N   . GLU C  2  25  ? 97.808  55.809  64.300  1.00 81.95  ?  25  GLU C N   1 
ATOM   10185 C  CA  . GLU C  2  25  ? 98.164  56.179  62.931  1.00 79.20  ?  25  GLU C CA  1 
ATOM   10186 C  C   . GLU C  2  25  ? 96.974  55.946  61.996  1.00 81.69  ?  25  GLU C C   1 
ATOM   10187 O  O   . GLU C  2  25  ? 96.197  55.010  62.193  1.00 75.01  ?  25  GLU C O   1 
ATOM   10188 C  CB  . GLU C  2  25  ? 99.422  55.425  62.447  1.00 85.43  ?  25  GLU C CB  1 
ATOM   10189 C  CG  . GLU C  2  25  ? 99.249  53.928  62.237  1.00 111.34 ?  25  GLU C CG  1 
ATOM   10190 C  CD  . GLU C  2  25  ? 100.353 53.272  61.427  1.00 109.75 ?  25  GLU C CD  1 
ATOM   10191 O  OE1 . GLU C  2  25  ? 101.451 53.866  61.323  1.00 99.13  ?  25  GLU C OE1 1 
ATOM   10192 O  OE2 . GLU C  2  25  ? 100.119 52.161  60.899  1.00 110.32 ?  25  GLU C OE2 1 
ATOM   10193 N  N   . THR C  2  26  ? 96.828  56.816  60.989  1.00 82.95  ?  26  THR C N   1 
ATOM   10194 C  CA  . THR C  2  26  ? 95.741  56.751  60.013  1.00 69.33  ?  26  THR C CA  1 
ATOM   10195 C  C   . THR C  2  26  ? 96.320  56.669  58.598  1.00 71.90  ?  26  THR C C   1 
ATOM   10196 O  O   . THR C  2  26  ? 97.527  56.809  58.417  1.00 77.83  ?  26  THR C O   1 
ATOM   10197 C  CB  . THR C  2  26  ? 94.827  57.991  60.167  1.00 80.76  ?  26  THR C CB  1 
ATOM   10198 O  OG1 . THR C  2  26  ? 95.563  59.171  59.830  1.00 90.47  ?  26  THR C OG1 1 
ATOM   10199 C  CG2 . THR C  2  26  ? 94.246  58.123  61.564  1.00 89.27  ?  26  THR C CG2 1 
ATOM   10200 N  N   . VAL C  2  27  ? 95.456  56.439  57.599  1.00 71.39  ?  27  VAL C N   1 
ATOM   10201 C  CA  . VAL C  2  27  ? 95.832  56.362  56.185  1.00 78.45  ?  27  VAL C CA  1 
ATOM   10202 C  C   . VAL C  2  27  ? 96.609  57.616  55.747  1.00 73.26  ?  27  VAL C C   1 
ATOM   10203 O  O   . VAL C  2  27  ? 97.553  57.514  54.965  1.00 70.44  ?  27  VAL C O   1 
ATOM   10204 C  CB  . VAL C  2  27  ? 94.573  56.127  55.313  1.00 71.23  ?  27  VAL C CB  1 
ATOM   10205 C  CG1 . VAL C  2  27  ? 93.590  57.290  55.424  1.00 69.95  ?  27  VAL C CG1 1 
ATOM   10206 C  CG2 . VAL C  2  27  ? 94.943  55.865  53.861  1.00 68.25  ?  27  VAL C CG2 1 
ATOM   10207 N  N   . TRP C  2  28  ? 96.224  58.792  56.259  1.00 69.16  ?  28  TRP C N   1 
ATOM   10208 C  CA  . TRP C  2  28  ? 96.912  60.037  55.934  1.00 72.31  ?  28  TRP C CA  1 
ATOM   10209 C  C   . TRP C  2  28  ? 98.349  60.021  56.461  1.00 80.85  ?  28  TRP C C   1 
ATOM   10210 O  O   . TRP C  2  28  ? 99.242  60.575  55.821  1.00 78.47  ?  28  TRP C O   1 
ATOM   10211 C  CB  . TRP C  2  28  ? 96.179  61.225  56.556  1.00 76.14  ?  28  TRP C CB  1 
ATOM   10212 C  CG  . TRP C  2  28  ? 94.910  61.614  55.862  1.00 72.70  ?  28  TRP C CG  1 
ATOM   10213 C  CD1 . TRP C  2  28  ? 94.782  62.464  54.804  1.00 70.99  ?  28  TRP C CD1 1 
ATOM   10214 C  CD2 . TRP C  2  28  ? 93.578  61.244  56.244  1.00 74.48  ?  28  TRP C CD2 1 
ATOM   10215 N  NE1 . TRP C  2  28  ? 93.454  62.624  54.485  1.00 70.48  ?  28  TRP C NE1 1 
ATOM   10216 C  CE2 . TRP C  2  28  ? 92.693  61.889  55.357  1.00 76.16  ?  28  TRP C CE2 1 
ATOM   10217 C  CE3 . TRP C  2  28  ? 93.048  60.411  57.235  1.00 81.50  ?  28  TRP C CE3 1 
ATOM   10218 C  CZ2 . TRP C  2  28  ? 91.310  61.732  55.438  1.00 85.67  ?  28  TRP C CZ2 1 
ATOM   10219 C  CZ3 . TRP C  2  28  ? 91.677  60.262  57.316  1.00 77.84  ?  28  TRP C CZ3 1 
ATOM   10220 C  CH2 . TRP C  2  28  ? 90.825  60.914  56.423  1.00 71.56  ?  28  TRP C CH2 1 
ATOM   10221 N  N   . ASP C  2  29  ? 98.569  59.404  57.636  1.00 88.34  ?  29  ASP C N   1 
ATOM   10222 C  CA  . ASP C  2  29  ? 99.891  59.313  58.254  1.00 82.82  ?  29  ASP C CA  1 
ATOM   10223 C  C   . ASP C  2  29  ? 100.766 58.347  57.458  1.00 77.16  ?  29  ASP C C   1 
ATOM   10224 O  O   . ASP C  2  29  ? 101.926 58.654  57.187  1.00 74.01  ?  29  ASP C O   1 
ATOM   10225 C  CB  . ASP C  2  29  ? 99.776  58.855  59.720  1.00 66.34  ?  29  ASP C CB  1 
ATOM   10226 C  CG  . ASP C  2  29  ? 98.895  59.745  60.573  1.00 92.68  ?  29  ASP C CG  1 
ATOM   10227 O  OD1 . ASP C  2  29  ? 98.691  60.919  60.194  1.00 100.38 ?  29  ASP C OD1 1 
ATOM   10228 O  OD2 . ASP C  2  29  ? 98.403  59.266  61.618  1.00 89.81  ?  29  ASP C OD2 1 
ATOM   10229 N  N   . ARG C  2  30  ? 100.208 57.193  57.062  1.00 69.20  ?  30  ARG C N   1 
ATOM   10230 C  CA  . ARG C  2  30  ? 100.947 56.211  56.271  1.00 63.76  ?  30  ARG C CA  1 
ATOM   10231 C  C   . ARG C  2  30  ? 101.303 56.765  54.881  1.00 79.12  ?  30  ARG C C   1 
ATOM   10232 O  O   . ARG C  2  30  ? 102.300 56.340  54.294  1.00 79.02  ?  30  ARG C O   1 
ATOM   10233 C  CB  . ARG C  2  30  ? 100.151 54.910  56.157  1.00 53.01  ?  30  ARG C CB  1 
ATOM   10234 C  CG  . ARG C  2  30  ? 100.079 54.162  57.475  1.00 67.50  ?  30  ARG C CG  1 
ATOM   10235 C  CD  . ARG C  2  30  ? 99.503  52.780  57.300  1.00 69.53  ?  30  ARG C CD  1 
ATOM   10236 N  NE  . ARG C  2  30  ? 98.095  52.826  56.923  1.00 71.02  ?  30  ARG C NE  1 
ATOM   10237 C  CZ  . ARG C  2  30  ? 97.085  52.983  57.773  1.00 80.94  ?  30  ARG C CZ  1 
ATOM   10238 N  NH1 . ARG C  2  30  ? 97.314  53.115  59.076  1.00 76.25  ?  30  ARG C NH1 1 
ATOM   10239 N  NH2 . ARG C  2  30  ? 95.835  53.012  57.328  1.00 84.44  ?  30  ARG C NH2 1 
ATOM   10240 N  N   . LYS C  2  31  ? 100.509 57.723  54.362  1.00 78.23  ?  31  LYS C N   1 
ATOM   10241 C  CA  . LYS C  2  31  ? 100.786 58.351  53.075  1.00 61.21  ?  31  LYS C CA  1 
ATOM   10242 C  C   . LYS C  2  31  ? 102.055 59.183  53.199  1.00 68.57  ?  31  LYS C C   1 
ATOM   10243 O  O   . LYS C  2  31  ? 102.908 59.133  52.314  1.00 80.18  ?  31  LYS C O   1 
ATOM   10244 C  CB  . LYS C  2  31  ? 99.602  59.218  52.628  1.00 62.59  ?  31  LYS C CB  1 
ATOM   10245 C  CG  . LYS C  2  31  ? 99.831  59.970  51.320  1.00 61.52  ?  31  LYS C CG  1 
ATOM   10246 C  CD  . LYS C  2  31  ? 99.827  59.054  50.098  1.00 66.61  ?  31  LYS C CD  1 
ATOM   10247 C  CE  . LYS C  2  31  ? 99.768  59.825  48.806  1.00 74.84  ?  31  LYS C CE  1 
ATOM   10248 N  NZ  . LYS C  2  31  ? 101.001 60.628  48.582  1.00 85.63  ?  31  LYS C NZ  1 
ATOM   10249 N  N   . ALA C  2  32  ? 102.198 59.932  54.299  1.00 66.48  ?  32  ALA C N   1 
ATOM   10250 C  CA  . ALA C  2  32  ? 103.394 60.731  54.525  1.00 71.86  ?  32  ALA C CA  1 
ATOM   10251 C  C   . ALA C  2  32  ? 104.615 59.813  54.665  1.00 80.50  ?  32  ALA C C   1 
ATOM   10252 O  O   . ALA C  2  32  ? 105.686 60.133  54.154  1.00 80.79  ?  32  ALA C O   1 
ATOM   10253 C  CB  . ALA C  2  32  ? 103.229 61.565  55.779  1.00 68.69  ?  32  ALA C CB  1 
ATOM   10254 N  N   . ASP C  2  33  ? 104.445 58.666  55.343  1.00 81.37  ?  33  ASP C N   1 
ATOM   10255 C  CA  . ASP C  2  33  ? 105.519 57.693  55.538  1.00 82.41  ?  33  ASP C CA  1 
ATOM   10256 C  C   . ASP C  2  33  ? 106.015 57.130  54.204  1.00 80.41  ?  33  ASP C C   1 
ATOM   10257 O  O   . ASP C  2  33  ? 107.196 56.801  54.088  1.00 92.45  ?  33  ASP C O   1 
ATOM   10258 C  CB  . ASP C  2  33  ? 105.048 56.544  56.449  1.00 88.96  ?  33  ASP C CB  1 
ATOM   10259 C  CG  . ASP C  2  33  ? 104.758 56.949  57.885  1.00 105.43 ?  33  ASP C CG  1 
ATOM   10260 O  OD1 . ASP C  2  33  ? 105.023 58.124  58.240  1.00 100.60 ?  33  ASP C OD1 1 
ATOM   10261 O  OD2 . ASP C  2  33  ? 104.261 56.094  58.654  1.00 98.60  ?  33  ASP C OD2 1 
ATOM   10262 N  N   . MET C  2  34  ? 105.132 57.015  53.198  1.00 76.21  ?  34  MET C N   1 
ATOM   10263 C  CA  . MET C  2  34  ? 105.537 56.501  51.886  1.00 68.37  ?  34  MET C CA  1 
ATOM   10264 C  C   . MET C  2  34  ? 106.437 57.492  51.137  1.00 77.58  ?  34  MET C C   1 
ATOM   10265 O  O   . MET C  2  34  ? 107.192 57.074  50.261  1.00 83.23  ?  34  MET C O   1 
ATOM   10266 C  CB  . MET C  2  34  ? 104.309 56.156  51.019  1.00 65.22  ?  34  MET C CB  1 
ATOM   10267 C  CG  . MET C  2  34  ? 103.919 54.675  51.042  1.00 72.16  ?  34  MET C CG  1 
ATOM   10268 S  SD  . MET C  2  34  ? 105.269 53.516  50.691  1.00 77.83  ?  34  MET C SD  1 
ATOM   10269 C  CE  . MET C  2  34  ? 105.809 54.135  49.090  1.00 105.80 ?  34  MET C CE  1 
ATOM   10270 N  N   . LYS C  2  35  ? 106.357 58.774  51.506  1.00 83.99  ?  35  LYS C N   1 
ATOM   10271 C  CA  . LYS C  2  35  ? 107.219 59.815  50.883  1.00 80.85  ?  35  LYS C CA  1 
ATOM   10272 C  C   . LYS C  2  35  ? 107.061 59.779  49.360  1.00 74.76  ?  35  LYS C C   1 
ATOM   10273 O  O   . LYS C  2  35  ? 105.953 59.459  48.889  1.00 77.96  ?  35  LYS C O   1 
ATOM   10274 C  CB  . LYS C  2  35  ? 108.682 59.601  51.285  1.00 80.75  ?  35  LYS C CB  1 
ATOM   10275 C  CG  . LYS C  2  35  ? 108.903 59.180  52.731  1.00 87.88  ?  35  LYS C CG  1 
ATOM   10276 C  CD  . LYS C  2  35  ? 108.835 60.335  53.707  1.00 94.46  ?  35  LYS C CD  1 
ATOM   10277 C  CE  . LYS C  2  35  ? 108.676 59.890  55.145  1.00 115.61 ?  35  LYS C CE  1 
ATOM   10278 N  NZ  . LYS C  2  35  ? 109.060 58.470  55.328  1.00 126.28 ?  35  LYS C NZ  1 
ATOM   10279 N  N   . VAL C  2  36  ? 108.130 60.107  48.629  1.00 88.60  ?  36  VAL C N   1 
ATOM   10280 C  CA  . VAL C  2  36  ? 108.086 60.072  47.138  1.00 73.22  ?  36  VAL C CA  1 
ATOM   10281 C  C   . VAL C  2  36  ? 107.707 58.652  46.710  1.00 77.06  ?  36  VAL C C   1 
ATOM   10282 O  O   . VAL C  2  36  ? 108.256 57.698  47.292  1.00 99.16  ?  36  VAL C O   1 
ATOM   10283 C  CB  . VAL C  2  36  ? 109.426 60.510  46.520  1.00 82.30  ?  36  VAL C CB  1 
ATOM   10284 C  CG1 . VAL C  2  36  ? 109.487 60.205  45.031  1.00 77.45  ?  36  VAL C CG1 1 
ATOM   10285 C  CG2 . VAL C  2  36  ? 109.709 61.982  46.778  1.00 89.01  ?  36  VAL C CG2 1 
ATOM   10286 N  N   . GLN C  2  37  ? 106.757 58.523  45.782  1.00 57.87  ?  37  GLN C N   1 
ATOM   10287 C  CA  . GLN C  2  37  ? 106.301 57.179  45.339  1.00 61.99  ?  37  GLN C CA  1 
ATOM   10288 C  C   . GLN C  2  37  ? 107.071 56.805  44.070  1.00 66.02  ?  37  GLN C C   1 
ATOM   10289 O  O   . GLN C  2  37  ? 107.343 57.713  43.262  1.00 85.42  ?  37  GLN C O   1 
ATOM   10290 C  CB  . GLN C  2  37  ? 104.785 57.172  45.139  1.00 66.73  ?  37  GLN C CB  1 
ATOM   10291 C  CG  . GLN C  2  37  ? 104.003 57.247  46.444  1.00 59.98  ?  37  GLN C CG  1 
ATOM   10292 C  CD  . GLN C  2  37  ? 102.563 56.833  46.242  1.00 77.96  ?  37  GLN C CD  1 
ATOM   10293 O  OE1 . GLN C  2  37  ? 101.926 57.238  45.272  1.00 104.51 ?  37  GLN C OE1 1 
ATOM   10294 N  NE2 . GLN C  2  37  ? 102.021 56.024  47.137  1.00 63.86  ?  37  GLN C NE2 1 
ATOM   10295 N  N   . CYS C  2  38  ? 107.408 55.525  43.904  1.00 56.64  ?  38  CYS C N   1 
ATOM   10296 C  CA  . CYS C  2  38  ? 108.246 55.111  42.749  1.00 54.20  ?  38  CYS C CA  1 
ATOM   10297 C  C   . CYS C  2  38  ? 107.653 55.642  41.442  1.00 58.18  ?  38  CYS C C   1 
ATOM   10298 O  O   . CYS C  2  38  ? 106.478 55.342  41.164  1.00 71.42  ?  38  CYS C O   1 
ATOM   10299 C  CB  . CYS C  2  38  ? 108.364 53.599  42.660  1.00 49.95  ?  38  CYS C CB  1 
ATOM   10300 S  SG  . CYS C  2  38  ? 109.586 53.107  41.422  1.00 72.83  ?  38  CYS C SG  1 
ATOM   10301 N  N   . GLY C  2  39  ? 108.450 56.384  40.672  1.00 52.74  ?  39  GLY C N   1 
ATOM   10302 C  CA  . GLY C  2  39  ? 107.988 56.914  39.375  1.00 72.21  ?  39  GLY C CA  1 
ATOM   10303 C  C   . GLY C  2  39  ? 107.764 55.796  38.375  1.00 66.63  ?  39  GLY C C   1 
ATOM   10304 O  O   . GLY C  2  39  ? 106.762 55.857  37.638  1.00 80.52  ?  39  GLY C O   1 
ATOM   10305 N  N   . PHE C  2  40  ? 108.663 54.810  38.350  1.00 59.42  ?  40  PHE C N   1 
ATOM   10306 C  CA  . PHE C  2  40  ? 108.501 53.649  37.439  1.00 55.16  ?  40  PHE C CA  1 
ATOM   10307 C  C   . PHE C  2  40  ? 107.116 53.036  37.658  1.00 58.48  ?  40  PHE C C   1 
ATOM   10308 O  O   . PHE C  2  40  ? 106.383 52.841  36.670  1.00 70.38  ?  40  PHE C O   1 
ATOM   10309 C  CB  . PHE C  2  40  ? 109.609 52.622  37.681  1.00 61.54  ?  40  PHE C CB  1 
ATOM   10310 C  CG  . PHE C  2  40  ? 110.954 53.000  37.118  1.00 58.57  ?  40  PHE C CG  1 
ATOM   10311 C  CD1 . PHE C  2  40  ? 111.179 52.994  35.751  1.00 64.69  ?  40  PHE C CD1 1 
ATOM   10312 C  CD2 . PHE C  2  40  ? 111.997 53.362  37.955  1.00 50.42  ?  40  PHE C CD2 1 
ATOM   10313 C  CE1 . PHE C  2  40  ? 112.417 53.341  35.234  1.00 67.34  ?  40  PHE C CE1 1 
ATOM   10314 C  CE2 . PHE C  2  40  ? 113.234 53.709  37.437  1.00 53.19  ?  40  PHE C CE2 1 
ATOM   10315 C  CZ  . PHE C  2  40  ? 113.442 53.698  36.078  1.00 72.91  ?  40  PHE C CZ  1 
ATOM   10316 N  N   . GLY C  2  41  ? 106.770 52.751  38.917  1.00 56.81  ?  41  GLY C N   1 
ATOM   10317 C  CA  . GLY C  2  41  ? 105.467 52.172  39.212  1.00 57.91  ?  41  GLY C CA  1 
ATOM   10318 C  C   . GLY C  2  41  ? 104.324 53.139  38.970  1.00 58.06  ?  41  GLY C C   1 
ATOM   10319 O  O   . GLY C  2  41  ? 103.239 52.725  38.553  1.00 66.26  ?  41  GLY C O   1 
ATOM   10320 N  N   . SER C  2  42  ? 104.559 54.441  39.230  1.00 56.35  ?  42  SER C N   1 
ATOM   10321 C  CA  . SER C  2  42  ? 103.561 55.497  39.038  1.00 45.92  ?  42  SER C CA  1 
ATOM   10322 C  C   . SER C  2  42  ? 103.283 55.742  37.556  1.00 52.98  ?  42  SER C C   1 
ATOM   10323 O  O   . SER C  2  42  ? 102.160 56.099  37.200  1.00 67.40  ?  42  SER C O   1 
ATOM   10324 C  CB  . SER C  2  42  ? 104.034 56.793  39.687  1.00 47.52  ?  42  SER C CB  1 
ATOM   10325 O  OG  . SER C  2  42  ? 104.306 56.605  41.066  1.00 56.23  ?  42  SER C OG  1 
ATOM   10326 N  N   . ALA C  2  43  ? 104.301 55.570  36.697  1.00 60.89  ?  43  ALA C N   1 
ATOM   10327 C  CA  . ALA C  2  43  ? 104.148 55.738  35.246  1.00 63.54  ?  43  ALA C CA  1 
ATOM   10328 C  C   . ALA C  2  43  ? 103.693 54.430  34.559  1.00 59.90  ?  43  ALA C C   1 
ATOM   10329 O  O   . ALA C  2  43  ? 103.341 54.447  33.385  1.00 64.43  ?  43  ALA C O   1 
ATOM   10330 C  CB  . ALA C  2  43  ? 105.458 56.215  34.633  1.00 51.61  ?  43  ALA C CB  1 
ATOM   10331 N  N   . GLY C  2  44  ? 103.706 53.321  35.297  1.00 66.31  ?  44  GLY C N   1 
ATOM   10332 C  CA  . GLY C  2  44  ? 103.313 52.014  34.796  1.00 59.79  ?  44  GLY C CA  1 
ATOM   10333 C  C   . GLY C  2  44  ? 104.408 51.295  34.035  1.00 59.25  ?  44  GLY C C   1 
ATOM   10334 O  O   . GLY C  2  44  ? 104.130 50.276  33.405  1.00 72.51  ?  44  GLY C O   1 
ATOM   10335 N  N   . VAL C  2  45  ? 105.664 51.791  34.090  1.00 64.57  ?  45  VAL C N   1 
ATOM   10336 C  CA  . VAL C  2  45  ? 106.777 51.172  33.354  1.00 56.26  ?  45  VAL C CA  1 
ATOM   10337 C  C   . VAL C  2  45  ? 107.589 50.137  34.142  1.00 65.19  ?  45  VAL C C   1 
ATOM   10338 O  O   . VAL C  2  45  ? 108.706 49.810  33.742  1.00 66.02  ?  45  VAL C O   1 
ATOM   10339 C  CB  . VAL C  2  45  ? 107.672 52.225  32.656  1.00 42.55  ?  45  VAL C CB  1 
ATOM   10340 C  CG1 . VAL C  2  45  ? 106.928 52.865  31.496  1.00 60.63  ?  45  VAL C CG1 1 
ATOM   10341 C  CG2 . VAL C  2  45  ? 108.162 53.285  33.636  1.00 61.20  ?  45  VAL C CG2 1 
ATOM   10342 N  N   . CYS C  2  46  ? 107.015 49.643  35.230  1.00 55.34  ?  46  CYS C N   1 
ATOM   10343 C  CA  . CYS C  2  46  ? 107.725 48.568  35.955  1.00 50.80  ?  46  CYS C CA  1 
ATOM   10344 C  C   . CYS C  2  46  ? 106.967 47.256  35.757  1.00 58.60  ?  46  CYS C C   1 
ATOM   10345 O  O   . CYS C  2  46  ? 105.743 47.239  35.985  1.00 77.28  ?  46  CYS C O   1 
ATOM   10346 C  CB  . CYS C  2  46  ? 107.813 48.866  37.439  1.00 42.31  ?  46  CYS C CB  1 
ATOM   10347 S  SG  . CYS C  2  46  ? 108.421 47.407  38.307  1.00 48.60  ?  46  CYS C SG  1 
ATOM   10348 N  N   . CYS C  2  47  ? 107.677 46.206  35.343  1.00 48.05  ?  47  CYS C N   1 
ATOM   10349 C  CA  . CYS C  2  47  ? 107.006 44.887  35.078  1.00 56.93  ?  47  CYS C CA  1 
ATOM   10350 C  C   . CYS C  2  47  ? 107.542 43.831  36.062  1.00 58.24  ?  47  CYS C C   1 
ATOM   10351 O  O   . CYS C  2  47  ? 108.765 43.820  36.300  1.00 57.56  ?  47  CYS C O   1 
ATOM   10352 C  CB  . CYS C  2  47  ? 107.206 44.409  33.633  1.00 42.91  ?  47  CYS C CB  1 
ATOM   10353 S  SG  . CYS C  2  47  ? 105.886 43.399  32.877  1.00 69.30  ?  47  CYS C SG  1 
ATOM   10354 N  N   . ARG C  2  48  ? 106.655 42.988  36.615  1.00 56.17  ?  48  ARG C N   1 
ATOM   10355 C  CA  . ARG C  2  48  ? 107.013 41.856  37.516  1.00 48.17  ?  48  ARG C CA  1 
ATOM   10356 C  C   . ARG C  2  48  ? 106.206 40.619  37.103  1.00 61.03  ?  48  ARG C C   1 
ATOM   10357 O  O   . ARG C  2  48  ? 105.918 39.790  37.985  1.00 57.35  ?  48  ARG C O   1 
ATOM   10358 C  CB  . ARG C  2  48  ? 106.756 42.236  38.977  1.00 46.36  ?  48  ARG C CB  1 
ATOM   10359 C  CG  . ARG C  2  48  ? 107.497 43.482  39.441  1.00 63.71  ?  48  ARG C CG  1 
ATOM   10360 C  CD  . ARG C  2  48  ? 107.429 43.664  40.946  1.00 64.97  ?  48  ARG C CD  1 
ATOM   10361 N  NE  . ARG C  2  48  ? 106.662 44.839  41.334  1.00 87.06  ?  48  ARG C NE  1 
ATOM   10362 C  CZ  . ARG C  2  48  ? 105.432 44.804  41.832  1.00 81.02  ?  48  ARG C CZ  1 
ATOM   10363 N  NH1 . ARG C  2  48  ? 104.724 43.691  41.765  1.00 56.43  ?  48  ARG C NH1 1 
ATOM   10364 N  NH2 . ARG C  2  48  ? 104.913 45.882  42.394  1.00 95.19  ?  48  ARG C NH2 1 
ATOM   10365 N  N   . ASN C  2  49  ? 105.860 40.499  35.818  1.00 67.65  ?  49  ASN C N   1 
ATOM   10366 C  CA  . ASN C  2  49  ? 105.090 39.372  35.290  1.00 44.51  ?  49  ASN C CA  1 
ATOM   10367 C  C   . ASN C  2  49  ? 105.890 38.068  35.146  1.00 47.38  ?  49  ASN C C   1 
ATOM   10368 O  O   . ASN C  2  49  ? 105.339 37.069  34.673  1.00 59.03  ?  49  ASN C O   1 
ATOM   10369 C  CB  . ASN C  2  49  ? 104.430 39.760  33.967  1.00 38.51  ?  49  ASN C CB  1 
ATOM   10370 C  CG  . ASN C  2  49  ? 103.338 40.782  34.154  1.00 58.91  ?  49  ASN C CG  1 
ATOM   10371 O  OD1 . ASN C  2  49  ? 103.404 41.631  35.045  1.00 64.20  ?  49  ASN C OD1 1 
ATOM   10372 N  ND2 . ASN C  2  49  ? 102.302 40.724  33.331  1.00 63.93  ?  49  ASN C ND2 1 
ATOM   10373 N  N   . CYS C  2  50  ? 107.104 38.066  35.685  1.00 50.30  ?  50  CYS C N   1 
ATOM   10374 C  CA  . CYS C  2  50  ? 107.884 36.805  35.705  1.00 59.35  ?  50  CYS C CA  1 
ATOM   10375 C  C   . CYS C  2  50  ? 109.173 37.056  36.488  1.00 52.96  ?  50  CYS C C   1 
ATOM   10376 O  O   . CYS C  2  50  ? 109.394 38.207  36.907  1.00 58.74  ?  50  CYS C O   1 
ATOM   10377 C  CB  . CYS C  2  50  ? 108.150 36.288  34.299  1.00 62.14  ?  50  CYS C CB  1 
ATOM   10378 S  SG  . CYS C  2  50  ? 109.464 37.197  33.460  1.00 56.17  ?  50  CYS C SG  1 
ATOM   10379 N  N   . SER C  2  51  ? 109.986 36.022  36.669  1.00 42.99  ?  51  SER C N   1 
ATOM   10380 C  CA  . SER C  2  51  ? 111.197 36.141  37.527  1.00 52.46  ?  51  SER C CA  1 
ATOM   10381 C  C   . SER C  2  51  ? 112.449 36.416  36.692  1.00 54.26  ?  51  SER C C   1 
ATOM   10382 O  O   . SER C  2  51  ? 113.550 36.145  37.199  1.00 68.04  ?  51  SER C O   1 
ATOM   10383 C  CB  . SER C  2  51  ? 111.385 34.891  38.349  1.00 44.72  ?  51  SER C CB  1 
ATOM   10384 O  OG  . SER C  2  51  ? 112.090 33.903  37.613  1.00 65.05  ?  51  SER C OG  1 
ATOM   10385 N  N   . MET C  2  52  ? 112.302 36.912  35.465  1.00 44.13  ?  52  MET C N   1 
ATOM   10386 C  CA  . MET C  2  52  ? 113.520 37.289  34.702  1.00 49.01  ?  52  MET C CA  1 
ATOM   10387 C  C   . MET C  2  52  ? 113.904 38.690  35.183  1.00 58.54  ?  52  MET C C   1 
ATOM   10388 O  O   . MET C  2  52  ? 115.104 39.015  35.139  1.00 55.70  ?  52  MET C O   1 
ATOM   10389 C  CB  . MET C  2  52  ? 113.279 37.280  33.190  1.00 50.81  ?  52  MET C CB  1 
ATOM   10390 C  CG  . MET C  2  52  ? 113.429 35.898  32.582  1.00 47.71  ?  52  MET C CG  1 
ATOM   10391 S  SD  . MET C  2  52  ? 113.893 35.911  30.833  1.00 45.44  ?  52  MET C SD  1 
ATOM   10392 C  CE  . MET C  2  52  ? 112.554 36.880  30.141  1.00 43.92  ?  52  MET C CE  1 
ATOM   10393 N  N   . GLY C  2  53  ? 112.925 39.465  35.662  1.00 55.51  ?  53  GLY C N   1 
ATOM   10394 C  CA  . GLY C  2  53  ? 113.199 40.812  36.201  1.00 60.44  ?  53  GLY C CA  1 
ATOM   10395 C  C   . GLY C  2  53  ? 113.314 40.795  37.715  1.00 49.84  ?  53  GLY C C   1 
ATOM   10396 O  O   . GLY C  2  53  ? 113.761 39.761  38.248  1.00 79.11  ?  53  GLY C O   1 
ATOM   10397 N  N   . PRO C  2  54  ? 112.926 41.869  38.442  1.00 55.66  ?  54  PRO C N   1 
ATOM   10398 C  CA  . PRO C  2  54  ? 111.925 42.823  37.954  1.00 59.30  ?  54  PRO C CA  1 
ATOM   10399 C  C   . PRO C  2  54  ? 112.511 43.841  36.963  1.00 61.90  ?  54  PRO C C   1 
ATOM   10400 O  O   . PRO C  2  54  ? 113.625 44.284  37.165  1.00 58.89  ?  54  PRO C O   1 
ATOM   10401 C  CB  . PRO C  2  54  ? 111.486 43.533  39.242  1.00 58.06  ?  54  PRO C CB  1 
ATOM   10402 C  CG  . PRO C  2  54  ? 112.716 43.497  40.119  1.00 67.46  ?  54  PRO C CG  1 
ATOM   10403 C  CD  . PRO C  2  54  ? 113.372 42.169  39.805  1.00 66.63  ?  54  PRO C CD  1 
ATOM   10404 N  N   . CYS C  2  55  ? 111.738 44.180  35.926  1.00 55.93  ?  55  CYS C N   1 
ATOM   10405 C  CA  . CYS C  2  55  ? 112.207 45.067  34.828  1.00 49.10  ?  55  CYS C CA  1 
ATOM   10406 C  C   . CYS C  2  55  ? 111.625 46.472  35.025  1.00 58.29  ?  55  CYS C C   1 
ATOM   10407 O  O   . CYS C  2  55  ? 110.482 46.572  35.509  1.00 52.65  ?  55  CYS C O   1 
ATOM   10408 C  CB  . CYS C  2  55  ? 111.770 44.521  33.474  1.00 42.00  ?  55  CYS C CB  1 
ATOM   10409 S  SG  . CYS C  2  55  ? 112.572 42.966  33.005  1.00 48.47  ?  55  CYS C SG  1 
ATOM   10410 N  N   . ARG C  2  56  ? 112.386 47.510  34.659  1.00 45.55  ?  56  ARG C N   1 
ATOM   10411 C  CA  . ARG C  2  56  ? 111.923 48.890  34.749  1.00 53.35  ?  56  ARG C CA  1 
ATOM   10412 C  C   . ARG C  2  56  ? 112.502 49.682  33.583  1.00 58.31  ?  56  ARG C C   1 
ATOM   10413 O  O   . ARG C  2  56  ? 113.688 50.010  33.580  1.00 63.41  ?  56  ARG C O   1 
ATOM   10414 C  CB  . ARG C  2  56  ? 112.252 49.538  36.104  1.00 44.56  ?  56  ARG C CB  1 
ATOM   10415 C  CG  . ARG C  2  56  ? 113.641 49.263  36.644  1.00 65.08  ?  56  ARG C CG  1 
ATOM   10416 C  CD  . ARG C  2  56  ? 113.947 50.183  37.809  1.00 53.69  ?  56  ARG C CD  1 
ATOM   10417 N  NE  . ARG C  2  56  ? 115.081 49.693  38.591  1.00 72.13  ?  56  ARG C NE  1 
ATOM   10418 C  CZ  . ARG C  2  56  ? 115.224 49.829  39.908  1.00 75.47  ?  56  ARG C CZ  1 
ATOM   10419 N  NH1 . ARG C  2  56  ? 114.294 50.451  40.627  1.00 84.25  ?  56  ARG C NH1 1 
ATOM   10420 N  NH2 . ARG C  2  56  ? 116.297 49.340  40.518  1.00 86.93  ?  56  ARG C NH2 1 
ATOM   10421 N  N   . VAL C  2  57  ? 111.659 49.961  32.577  1.00 51.22  ?  57  VAL C N   1 
ATOM   10422 C  CA  . VAL C  2  57  ? 112.064 50.709  31.390  1.00 44.13  ?  57  VAL C CA  1 
ATOM   10423 C  C   . VAL C  2  57  ? 111.834 52.213  31.623  1.00 54.50  ?  57  VAL C C   1 
ATOM   10424 O  O   . VAL C  2  57  ? 111.194 52.589  32.605  1.00 67.23  ?  57  VAL C O   1 
ATOM   10425 C  CB  . VAL C  2  57  ? 111.371 50.178  30.113  1.00 54.50  ?  57  VAL C CB  1 
ATOM   10426 C  CG1 . VAL C  2  57  ? 111.543 48.672  29.994  1.00 46.28  ?  57  VAL C CG1 1 
ATOM   10427 C  CG2 . VAL C  2  57  ? 109.897 50.549  30.075  1.00 56.94  ?  57  VAL C CG2 1 
ATOM   10428 N  N   . SER C  2  58  ? 112.361 53.072  30.743  1.00 45.77  ?  58  SER C N   1 
ATOM   10429 C  CA  . SER C  2  58  ? 112.231 54.519  30.892  1.00 57.44  ?  58  SER C CA  1 
ATOM   10430 C  C   . SER C  2  58  ? 110.839 55.072  30.520  1.00 70.33  ?  58  SER C C   1 
ATOM   10431 O  O   . SER C  2  58  ? 110.327 54.728  29.454  1.00 71.64  ?  58  SER C O   1 
ATOM   10432 C  CB  . SER C  2  58  ? 113.277 55.219  30.034  1.00 58.37  ?  58  SER C CB  1 
ATOM   10433 O  OG  . SER C  2  58  ? 113.193 56.631  30.164  1.00 59.78  ?  58  SER C OG  1 
ATOM   10434 N  N   . PRO C  2  59  ? 110.221 55.964  31.338  1.00 73.26  ?  59  PRO C N   1 
ATOM   10435 C  CA  . PRO C  2  59  ? 108.924 56.541  30.931  1.00 63.47  ?  59  PRO C CA  1 
ATOM   10436 C  C   . PRO C  2  59  ? 109.071 57.629  29.864  1.00 67.55  ?  59  PRO C C   1 
ATOM   10437 O  O   . PRO C  2  59  ? 108.092 57.977  29.207  1.00 82.08  ?  59  PRO C O   1 
ATOM   10438 C  CB  . PRO C  2  59  ? 108.347 57.115  32.226  1.00 61.48  ?  59  PRO C CB  1 
ATOM   10439 C  CG  . PRO C  2  59  ? 109.446 57.105  33.219  1.00 64.33  ?  59  PRO C CG  1 
ATOM   10440 C  CD  . PRO C  2  59  ? 110.680 56.523  32.624  1.00 64.98  ?  59  PRO C CD  1 
ATOM   10441 N  N   . VAL C  2  60  ? 110.292 58.175  29.703  1.00 67.56  ?  60  VAL C N   1 
ATOM   10442 C  CA  . VAL C  2  60  ? 110.586 59.203  28.715  1.00 64.81  ?  60  VAL C CA  1 
ATOM   10443 C  C   . VAL C  2  60  ? 111.231 58.501  27.513  1.00 72.84  ?  60  VAL C C   1 
ATOM   10444 O  O   . VAL C  2  60  ? 112.374 58.055  27.623  1.00 69.42  ?  60  VAL C O   1 
ATOM   10445 C  CB  . VAL C  2  60  ? 111.516 60.284  29.308  1.00 54.16  ?  60  VAL C CB  1 
ATOM   10446 C  CG1 . VAL C  2  60  ? 111.886 61.322  28.253  1.00 68.60  ?  60  VAL C CG1 1 
ATOM   10447 C  CG2 . VAL C  2  60  ? 110.867 60.955  30.515  1.00 65.92  ?  60  VAL C CG2 1 
ATOM   10448 N  N   . PRO C  2  61  ? 110.532 58.368  26.363  1.00 79.24  ?  61  PRO C N   1 
ATOM   10449 C  CA  . PRO C  2  61  ? 111.146 57.674  25.215  1.00 66.10  ?  61  PRO C CA  1 
ATOM   10450 C  C   . PRO C  2  61  ? 112.407 58.333  24.678  1.00 72.81  ?  61  PRO C C   1 
ATOM   10451 O  O   . PRO C  2  61  ? 112.587 59.543  24.805  1.00 68.41  ?  61  PRO C O   1 
ATOM   10452 C  CB  . PRO C  2  61  ? 110.049 57.685  24.144  1.00 60.55  ?  61  PRO C CB  1 
ATOM   10453 C  CG  . PRO C  2  61  ? 108.804 58.042  24.835  1.00 81.15  ?  61  PRO C CG  1 
ATOM   10454 C  CD  . PRO C  2  61  ? 109.161 58.818  26.055  1.00 76.35  ?  61  PRO C CD  1 
ATOM   10455 N  N   . GLY C  2  62  ? 113.257 57.527  24.059  1.00 70.69  ?  62  GLY C N   1 
ATOM   10456 C  CA  . GLY C  2  62  ? 114.501 58.012  23.482  1.00 77.53  ?  62  GLY C CA  1 
ATOM   10457 C  C   . GLY C  2  62  ? 115.677 58.016  24.437  1.00 67.82  ?  62  GLY C C   1 
ATOM   10458 O  O   . GLY C  2  62  ? 116.806 58.261  24.009  1.00 91.65  ?  62  GLY C O   1 
ATOM   10459 N  N   . LYS C  2  63  ? 115.444 57.750  25.728  1.00 65.64  ?  63  LYS C N   1 
ATOM   10460 C  CA  . LYS C  2  63  ? 116.527 57.731  26.712  1.00 69.19  ?  63  LYS C CA  1 
ATOM   10461 C  C   . LYS C  2  63  ? 116.316 56.611  27.725  1.00 73.08  ?  63  LYS C C   1 
ATOM   10462 O  O   . LYS C  2  63  ? 115.193 56.144  27.909  1.00 83.44  ?  63  LYS C O   1 
ATOM   10463 C  CB  . LYS C  2  63  ? 116.658 59.095  27.422  1.00 69.23  ?  63  LYS C CB  1 
ATOM   10464 C  CG  . LYS C  2  63  ? 115.341 59.693  27.911  1.00 67.33  ?  63  LYS C CG  1 
ATOM   10465 C  CD  . LYS C  2  63  ? 115.540 61.054  28.584  1.00 77.87  ?  63  LYS C CD  1 
ATOM   10466 C  CE  . LYS C  2  63  ? 115.567 62.205  27.601  1.00 86.64  ?  63  LYS C CE  1 
ATOM   10467 N  NZ  . LYS C  2  63  ? 115.633 63.524  28.284  1.00 91.98  ?  63  LYS C NZ  1 
ATOM   10468 N  N   . GLY C  2  64  ? 117.397 56.181  28.361  1.00 71.55  ?  64  GLY C N   1 
ATOM   10469 C  CA  . GLY C  2  64  ? 117.338 55.122  29.356  1.00 69.64  ?  64  GLY C CA  1 
ATOM   10470 C  C   . GLY C  2  64  ? 117.088 53.756  28.755  1.00 57.56  ?  64  GLY C C   1 
ATOM   10471 O  O   . GLY C  2  64  ? 117.261 53.565  27.550  1.00 68.80  ?  64  GLY C O   1 
ATOM   10472 N  N   . VAL C  2  65  ? 116.688 52.793  29.599  1.00 52.24  ?  65  VAL C N   1 
ATOM   10473 C  CA  . VAL C  2  65  ? 116.407 51.419  29.159  1.00 50.49  ?  65  VAL C CA  1 
ATOM   10474 C  C   . VAL C  2  65  ? 115.076 51.385  28.398  1.00 57.43  ?  65  VAL C C   1 
ATOM   10475 O  O   . VAL C  2  65  ? 114.035 51.717  28.950  1.00 65.38  ?  65  VAL C O   1 
ATOM   10476 C  CB  . VAL C  2  65  ? 116.446 50.385  30.325  1.00 47.15  ?  65  VAL C CB  1 
ATOM   10477 C  CG1 . VAL C  2  65  ? 116.029 48.997  29.844  1.00 68.75  ?  65  VAL C CG1 1 
ATOM   10478 C  CG2 . VAL C  2  65  ? 117.821 50.332  30.989  1.00 52.17  ?  65  VAL C CG2 1 
ATOM   10479 N  N   . GLU C  2  66  ? 115.103 50.913  27.155  1.00 53.97  ?  66  GLU C N   1 
ATOM   10480 C  CA  . GLU C  2  66  ? 113.864 50.976  26.336  1.00 53.41  ?  66  GLU C CA  1 
ATOM   10481 C  C   . GLU C  2  66  ? 113.007 49.714  26.515  1.00 53.13  ?  66  GLU C C   1 
ATOM   10482 O  O   . GLU C  2  66  ? 111.775 49.865  26.612  1.00 69.08  ?  66  GLU C O   1 
ATOM   10483 C  CB  . GLU C  2  66  ? 114.253 51.222  24.880  1.00 76.19  ?  66  GLU C CB  1 
ATOM   10484 C  CG  . GLU C  2  66  ? 113.152 50.899  23.901  1.00 105.24 ?  66  GLU C CG  1 
ATOM   10485 C  CD  . GLU C  2  66  ? 113.726 50.516  22.553  1.00 102.35 ?  66  GLU C CD  1 
ATOM   10486 O  OE1 . GLU C  2  66  ? 114.925 50.181  22.496  1.00 106.25 ?  66  GLU C OE1 1 
ATOM   10487 O  OE2 . GLU C  2  66  ? 112.972 50.549  21.561  1.00 98.42  ?  66  GLU C OE2 1 
ATOM   10488 N  N   . ARG C  2  67  ? 113.615 48.524  26.548  1.00 52.09  ?  67  ARG C N   1 
ATOM   10489 C  CA  . ARG C  2  67  ? 112.814 47.306  26.638  1.00 54.89  ?  67  ARG C CA  1 
ATOM   10490 C  C   . ARG C  2  67  ? 113.121 46.457  27.879  1.00 57.68  ?  67  ARG C C   1 
ATOM   10491 O  O   . ARG C  2  67  ? 114.184 46.591  28.485  1.00 48.11  ?  67  ARG C O   1 
ATOM   10492 C  CB  . ARG C  2  67  ? 113.053 46.453  25.373  1.00 54.54  ?  67  ARG C CB  1 
ATOM   10493 C  CG  . ARG C  2  67  ? 112.955 47.236  24.057  1.00 63.53  ?  67  ARG C CG  1 
ATOM   10494 C  CD  . ARG C  2  67  ? 113.490 46.476  22.855  1.00 58.47  ?  67  ARG C CD  1 
ATOM   10495 N  NE  . ARG C  2  67  ? 112.422 45.781  22.131  1.00 69.73  ?  67  ARG C NE  1 
ATOM   10496 C  CZ  . ARG C  2  67  ? 111.751 46.256  21.079  1.00 74.34  ?  67  ARG C CZ  1 
ATOM   10497 N  NH1 . ARG C  2  67  ? 112.030 47.462  20.588  1.00 62.36  ?  67  ARG C NH1 1 
ATOM   10498 N  NH2 . ARG C  2  67  ? 110.799 45.528  20.508  1.00 77.38  ?  67  ARG C NH2 1 
ATOM   10499 N  N   . GLY C  2  68  ? 112.173 45.585  28.231  1.00 55.54  ?  68  GLY C N   1 
ATOM   10500 C  CA  . GLY C  2  68  ? 112.297 44.650  29.343  1.00 44.03  ?  68  GLY C CA  1 
ATOM   10501 C  C   . GLY C  2  68  ? 113.204 43.500  28.951  1.00 50.07  ?  68  GLY C C   1 
ATOM   10502 O  O   . GLY C  2  68  ? 113.599 43.402  27.788  1.00 54.13  ?  68  GLY C O   1 
ATOM   10503 N  N   . ILE C  2  69  ? 113.532 42.605  29.887  1.00 50.73  ?  69  ILE C N   1 
ATOM   10504 C  CA  . ILE C  2  69  ? 114.445 41.491  29.586  1.00 44.03  ?  69  ILE C CA  1 
ATOM   10505 C  C   . ILE C  2  69  ? 113.924 40.601  28.446  1.00 51.01  ?  69  ILE C C   1 
ATOM   10506 O  O   . ILE C  2  69  ? 114.712 40.141  27.620  1.00 43.15  ?  69  ILE C O   1 
ATOM   10507 C  CB  . ILE C  2  69  ? 114.802 40.698  30.865  1.00 52.20  ?  69  ILE C CB  1 
ATOM   10508 C  CG1 . ILE C  2  69  ? 115.525 41.629  31.866  1.00 49.49  ?  69  ILE C CG1 1 
ATOM   10509 C  CG2 . ILE C  2  69  ? 115.677 39.490  30.520  1.00 44.11  ?  69  ILE C CG2 1 
ATOM   10510 C  CD1 . ILE C  2  69  ? 115.777 41.075  33.185  1.00 44.62  ?  69  ILE C CD1 1 
ATOM   10511 N  N   . CYS C  2  70  ? 112.597 40.449  28.378  1.00 55.50  ?  70  CYS C N   1 
ATOM   10512 C  CA  . CYS C  2  70  ? 111.913 39.602  27.362  1.00 42.42  ?  70  CYS C CA  1 
ATOM   10513 C  C   . CYS C  2  70  ? 111.857 40.335  26.016  1.00 53.44  ?  70  CYS C C   1 
ATOM   10514 O  O   . CYS C  2  70  ? 111.805 39.656  24.973  1.00 57.84  ?  70  CYS C O   1 
ATOM   10515 C  CB  . CYS C  2  70  ? 110.500 39.260  27.820  1.00 40.75  ?  70  CYS C CB  1 
ATOM   10516 S  SG  . CYS C  2  70  ? 109.248 40.486  27.358  1.00 51.96  ?  70  CYS C SG  1 
ATOM   10517 N  N   . GLY C  2  71  ? 111.864 41.669  26.054  1.00 52.46  ?  71  GLY C N   1 
ATOM   10518 C  CA  . GLY C  2  71  ? 111.724 42.514  24.875  1.00 46.45  ?  71  GLY C CA  1 
ATOM   10519 C  C   . GLY C  2  71  ? 110.504 43.414  24.924  1.00 53.47  ?  71  GLY C C   1 
ATOM   10520 O  O   . GLY C  2  71  ? 110.277 44.202  24.002  1.00 70.70  ?  71  GLY C O   1 
ATOM   10521 N  N   . ALA C  2  72  ? 109.705 43.318  25.994  1.00 42.37  ?  72  ALA C N   1 
ATOM   10522 C  CA  . ALA C  2  72  ? 108.507 44.130  26.131  1.00 41.46  ?  72  ALA C CA  1 
ATOM   10523 C  C   . ALA C  2  72  ? 108.863 45.612  26.157  1.00 51.23  ?  72  ALA C C   1 
ATOM   10524 O  O   . ALA C  2  72  ? 109.746 46.012  26.904  1.00 53.17  ?  72  ALA C O   1 
ATOM   10525 C  CB  . ALA C  2  72  ? 107.767 43.749  27.408  1.00 47.35  ?  72  ALA C CB  1 
ATOM   10526 N  N   . THR C  2  73  ? 108.182 46.420  25.343  1.00 53.12  ?  73  THR C N   1 
ATOM   10527 C  CA  . THR C  2  73  ? 108.413 47.864  25.296  1.00 45.23  ?  73  THR C CA  1 
ATOM   10528 C  C   . THR C  2  73  ? 107.598 48.529  26.417  1.00 51.96  ?  73  THR C C   1 
ATOM   10529 O  O   . THR C  2  73  ? 106.777 47.865  27.053  1.00 56.16  ?  73  THR C O   1 
ATOM   10530 C  CB  . THR C  2  73  ? 107.995 48.404  23.922  1.00 55.17  ?  73  THR C CB  1 
ATOM   10531 O  OG1 . THR C  2  73  ? 106.595 48.172  23.740  1.00 56.74  ?  73  THR C OG1 1 
ATOM   10532 C  CG2 . THR C  2  73  ? 108.786 47.781  22.780  1.00 62.74  ?  73  THR C CG2 1 
ATOM   10533 N  N   . ALA C  2  74  ? 107.805 49.835  26.666  1.00 56.07  ?  74  ALA C N   1 
ATOM   10534 C  CA  . ALA C  2  74  ? 107.049 50.544  27.707  1.00 45.36  ?  74  ALA C CA  1 
ATOM   10535 C  C   . ALA C  2  74  ? 105.543 50.458  27.460  1.00 55.30  ?  74  ALA C C   1 
ATOM   10536 O  O   . ALA C  2  74  ? 104.779 50.264  28.397  1.00 60.77  ?  74  ALA C O   1 
ATOM   10537 C  CB  . ALA C  2  74  ? 107.479 52.001  27.761  1.00 55.25  ?  74  ALA C CB  1 
ATOM   10538 N  N   . ASP C  2  75  ? 105.123 50.579  26.200  1.00 54.06  ?  75  ASP C N   1 
ATOM   10539 C  CA  . ASP C  2  75  ? 103.709 50.506  25.847  1.00 57.67  ?  75  ASP C CA  1 
ATOM   10540 C  C   . ASP C  2  75  ? 103.132 49.135  26.180  1.00 59.44  ?  75  ASP C C   1 
ATOM   10541 O  O   . ASP C  2  75  ? 102.003 49.046  26.655  1.00 60.61  ?  75  ASP C O   1 
ATOM   10542 C  CB  . ASP C  2  75  ? 103.526 50.820  24.361  1.00 66.37  ?  75  ASP C CB  1 
ATOM   10543 C  CG  . ASP C  2  75  ? 103.856 52.257  24.037  1.00 66.36  ?  75  ASP C CG  1 
ATOM   10544 O  OD1 . ASP C  2  75  ? 103.295 53.155  24.699  1.00 63.28  ?  75  ASP C OD1 1 
ATOM   10545 O  OD2 . ASP C  2  75  ? 104.672 52.485  23.120  1.00 71.34  ?  75  ASP C OD2 1 
ATOM   10546 N  N   . VAL C  2  76  ? 103.905 48.067  25.947  1.00 54.83  ?  76  VAL C N   1 
ATOM   10547 C  CA  . VAL C  2  76  ? 103.449 46.714  26.256  1.00 50.25  ?  76  VAL C CA  1 
ATOM   10548 C  C   . VAL C  2  76  ? 103.328 46.591  27.776  1.00 56.70  ?  76  VAL C C   1 
ATOM   10549 O  O   . VAL C  2  76  ? 102.276 46.206  28.276  1.00 61.65  ?  76  VAL C O   1 
ATOM   10550 C  CB  . VAL C  2  76  ? 104.407 45.641  25.681  1.00 40.36  ?  76  VAL C CB  1 
ATOM   10551 C  CG1 . VAL C  2  76  ? 104.050 44.253  26.200  1.00 38.96  ?  76  VAL C CG1 1 
ATOM   10552 C  CG2 . VAL C  2  76  ? 104.403 45.667  24.161  1.00 58.61  ?  76  VAL C CG2 1 
ATOM   10553 N  N   . ILE C  2  77  ? 104.394 46.957  28.510  1.00 56.21  ?  77  ILE C N   1 
ATOM   10554 C  CA  . ILE C  2  77  ? 104.409 46.873  29.973  1.00 64.94  ?  77  ILE C CA  1 
ATOM   10555 C  C   . ILE C  2  77  ? 103.217 47.625  30.587  1.00 63.16  ?  77  ILE C C   1 
ATOM   10556 O  O   . ILE C  2  77  ? 102.464 47.053  31.374  1.00 64.92  ?  77  ILE C O   1 
ATOM   10557 C  CB  . ILE C  2  77  ? 105.775 47.365  30.543  1.00 50.34  ?  77  ILE C CB  1 
ATOM   10558 C  CG1 . ILE C  2  77  ? 106.902 46.368  30.179  1.00 44.10  ?  77  ILE C CG1 1 
ATOM   10559 C  CG2 . ILE C  2  77  ? 105.687 47.556  32.064  1.00 47.48  ?  77  ILE C CG2 1 
ATOM   10560 C  CD1 . ILE C  2  77  ? 108.300 46.899  30.309  1.00 41.73  ?  77  ILE C CD1 1 
ATOM   10561 N  N   . VAL C  2  78  ? 103.041 48.894  30.193  1.00 60.31  ?  78  VAL C N   1 
ATOM   10562 C  CA  . VAL C  2  78  ? 101.963 49.760  30.676  1.00 50.44  ?  78  VAL C CA  1 
ATOM   10563 C  C   . VAL C  2  78  ? 100.572 49.190  30.334  1.00 53.17  ?  78  VAL C C   1 
ATOM   10564 O  O   . VAL C  2  78  ? 99.693  49.192  31.190  1.00 59.97  ?  78  VAL C O   1 
ATOM   10565 C  CB  . VAL C  2  78  ? 102.132 51.195  30.107  1.00 44.81  ?  78  VAL C CB  1 
ATOM   10566 C  CG1 . VAL C  2  78  ? 100.897 52.036  30.363  1.00 47.82  ?  78  VAL C CG1 1 
ATOM   10567 C  CG2 . VAL C  2  78  ? 103.368 51.880  30.682  1.00 50.01  ?  78  VAL C CG2 1 
ATOM   10568 N  N   . SER C  2  79  ? 100.363 48.726  29.093  1.00 50.67  ?  79  SER C N   1 
ATOM   10569 C  CA  . SER C  2  79  ? 99.063  48.187  28.682  1.00 49.23  ?  79  SER C CA  1 
ATOM   10570 C  C   . SER C  2  79  ? 98.692  46.919  29.452  1.00 53.41  ?  79  SER C C   1 
ATOM   10571 O  O   . SER C  2  79  ? 97.523  46.738  29.793  1.00 57.63  ?  79  SER C O   1 
ATOM   10572 C  CB  . SER C  2  79  ? 99.036  47.918  27.177  1.00 49.96  ?  79  SER C CB  1 
ATOM   10573 O  OG  . SER C  2  79  ? 99.762  46.754  26.815  1.00 60.44  ?  79  SER C OG  1 
ATOM   10574 N  N   . ARG C  2  80  ? 99.676  46.043  29.731  1.00 55.47  ?  80  ARG C N   1 
ATOM   10575 C  CA  . ARG C  2  80  ? 99.416  44.809  30.473  1.00 42.33  ?  80  ARG C CA  1 
ATOM   10576 C  C   . ARG C  2  80  ? 99.081  45.158  31.916  1.00 48.33  ?  80  ARG C C   1 
ATOM   10577 O  O   . ARG C  2  80  ? 98.123  44.623  32.467  1.00 52.78  ?  80  ARG C O   1 
ATOM   10578 C  CB  . ARG C  2  80  ? 100.623 43.869  30.420  1.00 50.05  ?  80  ARG C CB  1 
ATOM   10579 C  CG  . ARG C  2  80  ? 100.921 43.354  29.021  1.00 58.73  ?  80  ARG C CG  1 
ATOM   10580 C  CD  . ARG C  2  80  ? 101.960 42.249  29.016  1.00 54.95  ?  80  ARG C CD  1 
ATOM   10581 N  NE  . ARG C  2  80  ? 103.235 42.675  29.595  1.00 48.96  ?  80  ARG C NE  1 
ATOM   10582 C  CZ  . ARG C  2  80  ? 104.339 41.938  29.599  1.00 51.90  ?  80  ARG C CZ  1 
ATOM   10583 N  NH1 . ARG C  2  80  ? 104.342 40.727  29.053  1.00 61.61  ?  80  ARG C NH1 1 
ATOM   10584 N  NH2 . ARG C  2  80  ? 105.453 42.408  30.146  1.00 62.68  ?  80  ARG C NH2 1 
ATOM   10585 N  N   . ASN C  2  81  ? 99.851  46.079  32.522  1.00 55.65  ?  81  ASN C N   1 
ATOM   10586 C  CA  . ASN C  2  81  ? 99.615  46.534  33.892  1.00 52.17  ?  81  ASN C CA  1 
ATOM   10587 C  C   . ASN C  2  81  ? 98.191  47.093  34.012  1.00 58.31  ?  81  ASN C C   1 
ATOM   10588 O  O   . ASN C  2  81  ? 97.495  46.817  34.990  1.00 64.04  ?  81  ASN C O   1 
ATOM   10589 C  CB  . ASN C  2  81  ? 100.634 47.616  34.285  1.00 48.57  ?  81  ASN C CB  1 
ATOM   10590 C  CG  . ASN C  2  81  ? 102.013 47.082  34.595  1.00 55.23  ?  81  ASN C CG  1 
ATOM   10591 O  OD1 . ASN C  2  81  ? 102.210 45.878  34.786  1.00 60.07  ?  81  ASN C OD1 1 
ATOM   10592 N  ND2 . ASN C  2  81  ? 103.003 47.967  34.654  1.00 53.03  ?  81  ASN C ND2 1 
ATOM   10593 N  N   . PHE C  2  82  ? 97.755  47.859  33.007  1.00 46.89  ?  82  PHE C N   1 
ATOM   10594 C  CA  . PHE C  2  82  ? 96.417  48.428  33.000  1.00 47.67  ?  82  PHE C CA  1 
ATOM   10595 C  C   . PHE C  2  82  ? 95.377  47.303  32.934  1.00 52.92  ?  82  PHE C C   1 
ATOM   10596 O  O   . PHE C  2  82  ? 94.441  47.282  33.730  1.00 63.81  ?  82  PHE C O   1 
ATOM   10597 C  CB  . PHE C  2  82  ? 96.262  49.389  31.804  1.00 42.08  ?  82  PHE C CB  1 
ATOM   10598 C  CG  . PHE C  2  82  ? 94.911  50.055  31.716  1.00 50.17  ?  82  PHE C CG  1 
ATOM   10599 C  CD1 . PHE C  2  82  ? 94.655  51.231  32.398  1.00 43.48  ?  82  PHE C CD1 1 
ATOM   10600 C  CD2 . PHE C  2  82  ? 93.897  49.504  30.952  1.00 57.44  ?  82  PHE C CD2 1 
ATOM   10601 C  CE1 . PHE C  2  82  ? 93.407  51.836  32.329  1.00 39.75  ?  82  PHE C CE1 1 
ATOM   10602 C  CE2 . PHE C  2  82  ? 92.650  50.112  30.885  1.00 57.58  ?  82  PHE C CE2 1 
ATOM   10603 C  CZ  . PHE C  2  82  ? 92.413  51.274  31.573  1.00 47.29  ?  82  PHE C CZ  1 
ATOM   10604 N  N   . ALA C  2  83  ? 95.584  46.381  31.991  1.00 53.52  ?  83  ALA C N   1 
ATOM   10605 C  CA  . ALA C  2  83  ? 94.677  45.227  31.806  1.00 52.64  ?  83  ALA C CA  1 
ATOM   10606 C  C   . ALA C  2  83  ? 94.448  44.508  33.131  1.00 49.41  ?  83  ALA C C   1 
ATOM   10607 O  O   . ALA C  2  83  ? 93.278  44.273  33.485  1.00 60.86  ?  83  ALA C O   1 
ATOM   10608 C  CB  . ALA C  2  83  ? 95.338  44.288  30.831  1.00 43.97  ?  83  ALA C CB  1 
ATOM   10609 N  N   . ARG C  2  84  ? 95.529  44.169  33.828  1.00 47.44  ?  84  ARG C N   1 
ATOM   10610 C  CA  . ARG C  2  84  ? 95.423  43.381  35.054  1.00 50.27  ?  84  ARG C CA  1 
ATOM   10611 C  C   . ARG C  2  84  ? 94.565  44.096  36.104  1.00 49.74  ?  84  ARG C C   1 
ATOM   10612 O  O   . ARG C  2  84  ? 93.888  43.427  36.880  1.00 50.03  ?  84  ARG C O   1 
ATOM   10613 C  CB  . ARG C  2  84  ? 96.813  43.020  35.613  1.00 46.13  ?  84  ARG C CB  1 
ATOM   10614 C  CG  . ARG C  2  84  ? 97.552  41.960  34.784  1.00 53.52  ?  84  ARG C CG  1 
ATOM   10615 C  CD  . ARG C  2  84  ? 98.392  41.023  35.632  1.00 47.96  ?  84  ARG C CD  1 
ATOM   10616 N  NE  . ARG C  2  84  ? 98.916  39.909  34.841  1.00 58.48  ?  84  ARG C NE  1 
ATOM   10617 C  CZ  . ARG C  2  84  ? 99.831  39.044  35.269  1.00 64.46  ?  84  ARG C CZ  1 
ATOM   10618 N  NH1 . ARG C  2  84  ? 100.341 39.155  36.492  1.00 63.63  ?  84  ARG C NH1 1 
ATOM   10619 N  NH2 . ARG C  2  84  ? 100.249 38.066  34.475  1.00 48.92  ?  84  ARG C NH2 1 
ATOM   10620 N  N   . MET C  2  85  ? 94.567  45.441  36.120  1.00 49.43  ?  85  MET C N   1 
ATOM   10621 C  CA  . MET C  2  85  ? 93.748  46.196  37.071  1.00 51.24  ?  85  MET C CA  1 
ATOM   10622 C  C   . MET C  2  85  ? 92.278  45.998  36.734  1.00 53.58  ?  85  MET C C   1 
ATOM   10623 O  O   . MET C  2  85  ? 91.456  45.848  37.633  1.00 60.76  ?  85  MET C O   1 
ATOM   10624 C  CB  . MET C  2  85  ? 94.076  47.688  37.020  1.00 45.37  ?  85  MET C CB  1 
ATOM   10625 C  CG  . MET C  2  85  ? 95.468  48.012  37.466  1.00 51.84  ?  85  MET C CG  1 
ATOM   10626 S  SD  . MET C  2  85  ? 95.710  49.796  37.580  1.00 69.20  ?  85  MET C SD  1 
ATOM   10627 C  CE  . MET C  2  85  ? 95.107  50.090  39.249  1.00 75.43  ?  85  MET C CE  1 
ATOM   10628 N  N   . VAL C  2  86  ? 91.943  45.991  35.438  1.00 52.90  ?  86  VAL C N   1 
ATOM   10629 C  CA  . VAL C  2  86  ? 90.571  45.787  34.986  1.00 49.28  ?  86  VAL C CA  1 
ATOM   10630 C  C   . VAL C  2  86  ? 90.138  44.371  35.372  1.00 57.00  ?  86  VAL C C   1 
ATOM   10631 O  O   . VAL C  2  86  ? 89.062  44.193  35.939  1.00 64.03  ?  86  VAL C O   1 
ATOM   10632 C  CB  . VAL C  2  86  ? 90.456  46.020  33.462  1.00 38.08  ?  86  VAL C CB  1 
ATOM   10633 C  CG1 . VAL C  2  86  ? 89.113  45.536  32.931  1.00 45.54  ?  86  VAL C CG1 1 
ATOM   10634 C  CG2 . VAL C  2  86  ? 90.669  47.489  33.122  1.00 52.15  ?  86  VAL C CG2 1 
ATOM   10635 N  N   . ALA C  2  87  ? 90.986  43.369  35.084  1.00 55.19  ?  87  ALA C N   1 
ATOM   10636 C  CA  . ALA C  2  87  ? 90.699  41.973  35.407  1.00 42.53  ?  87  ALA C CA  1 
ATOM   10637 C  C   . ALA C  2  87  ? 90.506  41.773  36.908  1.00 55.39  ?  87  ALA C C   1 
ATOM   10638 O  O   . ALA C  2  87  ? 89.668  40.966  37.310  1.00 62.00  ?  87  ALA C O   1 
ATOM   10639 C  CB  . ALA C  2  87  ? 91.822  41.088  34.909  1.00 55.04  ?  87  ALA C CB  1 
ATOM   10640 N  N   . ALA C  2  88  ? 91.271  42.498  37.740  1.00 62.72  ?  88  ALA C N   1 
ATOM   10641 C  CA  . ALA C  2  88  ? 91.135  42.392  39.188  1.00 51.82  ?  88  ALA C CA  1 
ATOM   10642 C  C   . ALA C  2  88  ? 89.837  43.072  39.638  1.00 51.94  ?  88  ALA C C   1 
ATOM   10643 O  O   . ALA C  2  88  ? 89.114  42.520  40.468  1.00 58.25  ?  88  ALA C O   1 
ATOM   10644 C  CB  . ALA C  2  88  ? 92.330  43.024  39.876  1.00 47.07  ?  88  ALA C CB  1 
ATOM   10645 N  N   . GLY C  2  89  ? 89.534  44.242  39.073  1.00 50.89  ?  89  GLY C N   1 
ATOM   10646 C  CA  . GLY C  2  89  ? 88.310  44.970  39.391  1.00 50.65  ?  89  GLY C CA  1 
ATOM   10647 C  C   . GLY C  2  89  ? 87.086  44.164  39.006  1.00 59.32  ?  89  GLY C C   1 
ATOM   10648 O  O   . GLY C  2  89  ? 86.127  44.067  39.774  1.00 67.17  ?  89  GLY C O   1 
ATOM   10649 N  N   . THR C  2  90  ? 87.132  43.553  37.815  1.00 56.77  ?  90  THR C N   1 
ATOM   10650 C  CA  . THR C  2  90  ? 86.052  42.712  37.302  1.00 51.00  ?  90  THR C CA  1 
ATOM   10651 C  C   . THR C  2  90  ? 85.817  41.530  38.245  1.00 57.73  ?  90  THR C C   1 
ATOM   10652 O  O   . THR C  2  90  ? 84.668  41.162  38.483  1.00 63.34  ?  90  THR C O   1 
ATOM   10653 C  CB  . THR C  2  90  ? 86.396  42.230  35.884  1.00 57.92  ?  90  THR C CB  1 
ATOM   10654 O  OG1 . THR C  2  90  ? 86.496  43.370  35.028  1.00 59.74  ?  90  THR C OG1 1 
ATOM   10655 C  CG2 . THR C  2  90  ? 85.373  41.243  35.327  1.00 47.41  ?  90  THR C CG2 1 
ATOM   10656 N  N   . ALA C  2  91  ? 86.906  40.941  38.779  1.00 55.93  ?  91  ALA C N   1 
ATOM   10657 C  CA  . ALA C  2  91  ? 86.835  39.806  39.697  1.00 53.83  ?  91  ALA C CA  1 
ATOM   10658 C  C   . ALA C  2  91  ? 86.137  40.173  41.003  1.00 67.53  ?  91  ALA C C   1 
ATOM   10659 O  O   . ALA C  2  91  ? 85.361  39.369  41.524  1.00 70.36  ?  91  ALA C O   1 
ATOM   10660 C  CB  . ALA C  2  91  ? 88.230  39.283  39.989  1.00 49.50  ?  91  ALA C CB  1 
ATOM   10661 N  N   . ALA C  2  92  ? 86.392  41.381  41.533  1.00 62.27  ?  92  ALA C N   1 
ATOM   10662 C  CA  . ALA C  2  92  ? 85.757  41.810  42.773  1.00 51.25  ?  92  ALA C CA  1 
ATOM   10663 C  C   . ALA C  2  92  ? 84.240  41.878  42.593  1.00 65.11  ?  92  ALA C C   1 
ATOM   10664 O  O   . ALA C  2  92  ? 83.510  41.361  43.435  1.00 74.56  ?  92  ALA C O   1 
ATOM   10665 C  CB  . ALA C  2  92  ? 86.304  43.157  43.209  1.00 51.47  ?  92  ALA C CB  1 
ATOM   10666 N  N   . HIS C  2  93  ? 83.761  42.478  41.492  1.00 61.35  ?  93  HIS C N   1 
ATOM   10667 C  CA  . HIS C  2  93  ? 82.322  42.558  41.242  1.00 56.44  ?  93  HIS C CA  1 
ATOM   10668 C  C   . HIS C  2  93  ? 81.755  41.199  40.827  1.00 60.30  ?  93  HIS C C   1 
ATOM   10669 O  O   . HIS C  2  93  ? 80.587  40.928  41.091  1.00 72.87  ?  93  HIS C O   1 
ATOM   10670 C  CB  . HIS C  2  93  ? 82.008  43.606  40.170  1.00 53.59  ?  93  HIS C CB  1 
ATOM   10671 C  CG  . HIS C  2  93  ? 82.177  45.016  40.634  1.00 65.16  ?  93  HIS C CG  1 
ATOM   10672 N  ND1 . HIS C  2  93  ? 82.881  45.940  39.888  1.00 70.59  ?  93  HIS C ND1 1 
ATOM   10673 C  CD2 . HIS C  2  93  ? 81.734  45.616  41.762  1.00 69.32  ?  93  HIS C CD2 1 
ATOM   10674 C  CE1 . HIS C  2  93  ? 82.842  47.069  40.574  1.00 68.04  ?  93  HIS C CE1 1 
ATOM   10675 N  NE2 . HIS C  2  93  ? 82.156  46.924  41.708  1.00 75.69  ?  93  HIS C NE2 1 
ATOM   10676 N  N   . SER C  2  94  ? 82.568  40.348  40.178  1.00 67.05  ?  94  SER C N   1 
ATOM   10677 C  CA  . SER C  2  94  ? 82.135  39.021  39.749  1.00 73.66  ?  94  SER C CA  1 
ATOM   10678 C  C   . SER C  2  94  ? 81.746  38.177  40.960  1.00 64.44  ?  94  SER C C   1 
ATOM   10679 O  O   . SER C  2  94  ? 80.622  37.690  41.019  1.00 68.97  ?  94  SER C O   1 
ATOM   10680 C  CB  . SER C  2  94  ? 83.246  38.323  38.966  1.00 78.60  ?  94  SER C CB  1 
ATOM   10681 O  OG  . SER C  2  94  ? 82.918  36.975  38.668  1.00 66.55  ?  94  SER C OG  1 
ATOM   10682 N  N   . ASP C  2  95  ? 82.647  38.042  41.932  1.00 68.92  ?  95  ASP C N   1 
ATOM   10683 C  CA  . ASP C  2  95  ? 82.346  37.219  43.135  1.00 83.08  ?  95  ASP C CA  1 
ATOM   10684 C  C   . ASP C  2  95  ? 81.140  37.821  43.865  1.00 79.04  ?  95  ASP C C   1 
ATOM   10685 O  O   . ASP C  2  95  ? 80.333  37.040  44.402  1.00 83.85  ?  95  ASP C O   1 
ATOM   10686 C  CB  . ASP C  2  95  ? 83.573  37.079  44.040  1.00 80.15  ?  95  ASP C CB  1 
ATOM   10687 C  CG  . ASP C  2  95  ? 84.344  35.789  43.818  1.00 82.44  ?  95  ASP C CG  1 
ATOM   10688 O  OD1 . ASP C  2  95  ? 83.903  34.980  42.979  1.00 80.05  ?  95  ASP C OD1 1 
ATOM   10689 O  OD2 . ASP C  2  95  ? 85.379  35.605  44.488  1.00 86.54  ?  95  ASP C OD2 1 
ATOM   10690 N  N   . HIS C  2  96  ? 81.019  39.151  43.873  1.00 62.15  ?  96  HIS C N   1 
ATOM   10691 C  CA  . HIS C  2  96  ? 79.920  39.827  44.549  1.00 57.95  ?  96  HIS C CA  1 
ATOM   10692 C  C   . HIS C  2  96  ? 78.601  39.302  43.962  1.00 60.93  ?  96  HIS C C   1 
ATOM   10693 O  O   . HIS C  2  96  ? 77.804  38.714  44.690  1.00 66.91  ?  96  HIS C O   1 
ATOM   10694 C  CB  . HIS C  2  96  ? 80.072  41.355  44.412  1.00 54.89  ?  96  HIS C CB  1 
ATOM   10695 C  CG  . HIS C  2  96  ? 78.987  42.151  45.073  1.00 55.72  ?  96  HIS C CG  1 
ATOM   10696 N  ND1 . HIS C  2  96  ? 77.668  42.067  44.656  1.00 77.58  ?  96  HIS C ND1 1 
ATOM   10697 C  CD2 . HIS C  2  96  ? 79.067  43.048  46.081  1.00 72.63  ?  96  HIS C CD2 1 
ATOM   10698 C  CE1 . HIS C  2  96  ? 76.987  42.896  45.432  1.00 75.68  ?  96  HIS C CE1 1 
ATOM   10699 N  NE2 . HIS C  2  96  ? 77.788  43.513  46.303  1.00 90.95  ?  96  HIS C NE2 1 
ATOM   10700 N  N   . GLY C  2  97  ? 78.391  39.494  42.665  1.00 56.96  ?  97  GLY C N   1 
ATOM   10701 C  CA  . GLY C  2  97  ? 77.178  39.038  42.001  1.00 57.82  ?  97  GLY C CA  1 
ATOM   10702 C  C   . GLY C  2  97  ? 76.970  37.537  42.037  1.00 65.39  ?  97  GLY C C   1 
ATOM   10703 O  O   . GLY C  2  97  ? 75.833  37.066  42.107  1.00 64.51  ?  97  GLY C O   1 
ATOM   10704 N  N   . ARG C  2  98  ? 78.066  36.770  41.980  1.00 66.01  ?  98  ARG C N   1 
ATOM   10705 C  CA  . ARG C  2  98  ? 78.022  35.303  42.019  1.00 67.66  ?  98  ARG C CA  1 
ATOM   10706 C  C   . ARG C  2  98  ? 77.398  34.836  43.335  1.00 72.57  ?  98  ARG C C   1 
ATOM   10707 O  O   . ARG C  2  98  ? 76.606  33.893  43.349  1.00 70.23  ?  98  ARG C O   1 
ATOM   10708 C  CB  . ARG C  2  98  ? 79.445  34.738  41.897  1.00 62.01  ?  98  ARG C CB  1 
ATOM   10709 C  CG  . ARG C  2  98  ? 79.518  33.234  41.674  1.00 54.12  ?  98  ARG C CG  1 
ATOM   10710 C  CD  . ARG C  2  98  ? 80.834  32.650  42.171  1.00 61.80  ?  98  ARG C CD  1 
ATOM   10711 N  NE  . ARG C  2  98  ? 82.001  33.435  41.758  1.00 64.34  ?  98  ARG C NE  1 
ATOM   10712 C  CZ  . ARG C  2  98  ? 82.555  33.399  40.549  1.00 64.35  ?  98  ARG C CZ  1 
ATOM   10713 N  NH1 . ARG C  2  98  ? 82.054  32.615  39.601  1.00 52.65  ?  98  ARG C NH1 1 
ATOM   10714 N  NH2 . ARG C  2  98  ? 83.615  34.150  40.276  1.00 67.40  ?  98  ARG C NH2 1 
ATOM   10715 N  N   . SER C  2  99  ? 77.769  35.499  44.438  1.00 78.36  ?  99  SER C N   1 
ATOM   10716 C  CA  . SER C  2  99  ? 77.259  35.190  45.767  1.00 65.50  ?  99  SER C CA  1 
ATOM   10717 C  C   . SER C  2  99  ? 75.765  35.517  45.843  1.00 73.34  ?  99  SER C C   1 
ATOM   10718 O  O   . SER C  2  99  ? 75.001  34.738  46.414  1.00 82.20  ?  99  SER C O   1 
ATOM   10719 C  CB  . SER C  2  99  ? 78.022  35.992  46.819  1.00 47.83  ?  99  SER C CB  1 
ATOM   10720 O  OG  . SER C  2  99  ? 77.832  35.468  48.122  1.00 80.00  ?  99  SER C OG  1 
ATOM   10721 N  N   . ILE C  2  100 ? 75.346  36.655  45.247  1.00 71.03  ?  100 ILE C N   1 
ATOM   10722 C  CA  . ILE C  2  100 ? 73.942  37.086  45.244  1.00 65.41  ?  100 ILE C CA  1 
ATOM   10723 C  C   . ILE C  2  100 ? 73.115  36.042  44.495  1.00 73.21  ?  100 ILE C C   1 
ATOM   10724 O  O   . ILE C  2  100 ? 72.052  35.641  44.969  1.00 74.78  ?  100 ILE C O   1 
ATOM   10725 C  CB  . ILE C  2  100 ? 73.746  38.490  44.588  1.00 67.07  ?  100 ILE C CB  1 
ATOM   10726 C  CG1 . ILE C  2  100 ? 74.702  39.576  45.140  1.00 67.58  ?  100 ILE C CG1 1 
ATOM   10727 C  CG2 . ILE C  2  100 ? 72.294  38.950  44.693  1.00 60.46  ?  100 ILE C CG2 1 
ATOM   10728 C  CD1 . ILE C  2  100 ? 74.767  39.732  46.582  1.00 67.03  ?  100 ILE C CD1 1 
ATOM   10729 N  N   . ALA C  2  101 ? 73.605  35.602  43.325  1.00 61.32  ?  101 ALA C N   1 
ATOM   10730 C  CA  . ALA C  2  101 ? 72.911  34.606  42.512  1.00 64.27  ?  101 ALA C CA  1 
ATOM   10731 C  C   . ALA C  2  101 ? 72.769  33.282  43.257  1.00 69.90  ?  101 ALA C C   1 
ATOM   10732 O  O   . ALA C  2  101 ? 71.725  32.639  43.158  1.00 70.17  ?  101 ALA C O   1 
ATOM   10733 C  CB  . ALA C  2  101 ? 73.652  34.391  41.203  1.00 63.64  ?  101 ALA C CB  1 
ATOM   10734 N  N   . LEU C  2  102 ? 73.806  32.869  44.004  1.00 72.16  ?  102 LEU C N   1 
ATOM   10735 C  CA  . LEU C  2  102 ? 73.737  31.624  44.768  1.00 71.20  ?  102 LEU C CA  1 
ATOM   10736 C  C   . LEU C  2  102 ? 72.677  31.743  45.861  1.00 74.74  ?  102 LEU C C   1 
ATOM   10737 O  O   . LEU C  2  102 ? 71.995  30.762  46.149  1.00 75.49  ?  102 LEU C O   1 
ATOM   10738 C  CB  . LEU C  2  102 ? 75.101  31.264  45.381  1.00 67.09  ?  102 LEU C CB  1 
ATOM   10739 C  CG  . LEU C  2  102 ? 76.167  30.761  44.396  1.00 52.87  ?  102 LEU C CG  1 
ATOM   10740 C  CD1 . LEU C  2  102 ? 77.545  30.842  45.004  1.00 61.29  ?  102 LEU C CD1 1 
ATOM   10741 C  CD2 . LEU C  2  102 ? 75.888  29.334  43.947  1.00 53.75  ?  102 LEU C CD2 1 
ATOM   10742 N  N   . SER C  2  103 ? 72.522  32.943  46.455  1.00 79.98  ?  103 SER C N   1 
ATOM   10743 C  CA  . SER C  2  103 ? 71.511  33.183  47.482  1.00 73.35  ?  103 SER C CA  1 
ATOM   10744 C  C   . SER C  2  103 ? 70.124  33.058  46.848  1.00 74.37  ?  103 SER C C   1 
ATOM   10745 O  O   . SER C  2  103 ? 69.250  32.427  47.435  1.00 83.79  ?  103 SER C O   1 
ATOM   10746 C  CB  . SER C  2  103 ? 71.690  34.565  48.106  1.00 63.98  ?  103 SER C CB  1 
ATOM   10747 O  OG  . SER C  2  103 ? 72.832  34.621  48.945  1.00 64.31  ?  103 SER C OG  1 
ATOM   10748 N  N   . LEU C  2  104 ? 69.929  33.631  45.644  1.00 74.18  ?  104 LEU C N   1 
ATOM   10749 C  CA  . LEU C  2  104 ? 68.654  33.547  44.923  1.00 81.07  ?  104 LEU C CA  1 
ATOM   10750 C  C   . LEU C  2  104 ? 68.280  32.080  44.640  1.00 88.87  ?  104 LEU C C   1 
ATOM   10751 O  O   . LEU C  2  104 ? 67.100  31.729  44.646  1.00 84.26  ?  104 LEU C O   1 
ATOM   10752 C  CB  . LEU C  2  104 ? 68.738  34.345  43.609  1.00 73.85  ?  104 LEU C CB  1 
ATOM   10753 C  CG  . LEU C  2  104 ? 67.456  34.444  42.777  1.00 57.76  ?  104 LEU C CG  1 
ATOM   10754 C  CD1 . LEU C  2  104 ? 66.406  35.280  43.481  1.00 58.49  ?  104 LEU C CD1 1 
ATOM   10755 C  CD2 . LEU C  2  104 ? 67.745  35.035  41.414  1.00 56.97  ?  104 LEU C CD2 1 
ATOM   10756 N  N   . TYR C  2  105 ? 69.285  31.228  44.399  1.00 82.44  ?  105 TYR C N   1 
ATOM   10757 C  CA  . TYR C  2  105 ? 69.082  29.802  44.140  1.00 78.68  ?  105 TYR C CA  1 
ATOM   10758 C  C   . TYR C  2  105 ? 68.615  29.055  45.407  1.00 78.78  ?  105 TYR C C   1 
ATOM   10759 O  O   . TYR C  2  105 ? 68.035  27.977  45.291  1.00 85.25  ?  105 TYR C O   1 
ATOM   10760 C  CB  . TYR C  2  105 ? 70.392  29.191  43.611  1.00 75.14  ?  105 TYR C CB  1 
ATOM   10761 C  CG  . TYR C  2  105 ? 70.291  27.741  43.190  1.00 80.64  ?  105 TYR C CG  1 
ATOM   10762 C  CD1 . TYR C  2  105 ? 69.513  27.364  42.106  1.00 88.12  ?  105 TYR C CD1 1 
ATOM   10763 C  CD2 . TYR C  2  105 ? 71.030  26.758  43.832  1.00 71.87  ?  105 TYR C CD2 1 
ATOM   10764 C  CE1 . TYR C  2  105 ? 69.442  26.039  41.694  1.00 91.44  ?  105 TYR C CE1 1 
ATOM   10765 C  CE2 . TYR C  2  105 ? 70.968  25.430  43.430  1.00 81.60  ?  105 TYR C CE2 1 
ATOM   10766 C  CZ  . TYR C  2  105 ? 70.170  25.072  42.359  1.00 87.71  ?  105 TYR C CZ  1 
ATOM   10767 O  OH  . TYR C  2  105 ? 70.095  23.761  41.951  1.00 87.80  ?  105 TYR C OH  1 
ATOM   10768 N  N   . HIS C  2  106 ? 68.864  29.620  46.608  1.00 75.82  ?  106 HIS C N   1 
ATOM   10769 C  CA  . HIS C  2  106 ? 68.470  29.009  47.879  1.00 82.71  ?  106 HIS C CA  1 
ATOM   10770 C  C   . HIS C  2  106 ? 67.352  29.807  48.584  1.00 82.26  ?  106 HIS C C   1 
ATOM   10771 O  O   . HIS C  2  106 ? 67.377  29.948  49.805  1.00 91.64  ?  106 HIS C O   1 
ATOM   10772 C  CB  . HIS C  2  106 ? 69.694  28.884  48.803  1.00 84.56  ?  106 HIS C CB  1 
ATOM   10773 C  CG  . HIS C  2  106 ? 70.835  28.132  48.195  1.00 96.97  ?  106 HIS C CG  1 
ATOM   10774 N  ND1 . HIS C  2  106 ? 72.125  28.634  48.220  1.00 105.08 ?  106 HIS C ND1 1 
ATOM   10775 C  CD2 . HIS C  2  106 ? 70.844  26.934  47.565  1.00 94.91  ?  106 HIS C CD2 1 
ATOM   10776 C  CE1 . HIS C  2  106 ? 72.876  27.730  47.607  1.00 103.47 ?  106 HIS C CE1 1 
ATOM   10777 N  NE2 . HIS C  2  106 ? 72.148  26.690  47.196  1.00 91.61  ?  106 HIS C NE2 1 
ATOM   10778 N  N   . THR C  2  107 ? 66.370  30.314  47.827  1.00 80.38  ?  107 THR C N   1 
ATOM   10779 C  CA  . THR C  2  107 ? 65.261  31.068  48.413  1.00 82.81  ?  107 THR C CA  1 
ATOM   10780 C  C   . THR C  2  107 ? 64.088  30.126  48.679  1.00 92.13  ?  107 THR C C   1 
ATOM   10781 O  O   . THR C  2  107 ? 63.865  29.194  47.910  1.00 94.82  ?  107 THR C O   1 
ATOM   10782 C  CB  . THR C  2  107 ? 64.827  32.213  47.487  1.00 88.95  ?  107 THR C CB  1 
ATOM   10783 O  OG1 . THR C  2  107 ? 64.581  31.703  46.172  1.00 90.35  ?  107 THR C OG1 1 
ATOM   10784 C  CG2 . THR C  2  107 ? 65.835  33.350  47.451  1.00 79.16  ?  107 THR C CG2 1 
ATOM   10785 N  N   . SER C  2  108 ? 63.341  30.367  49.763  1.00 92.31  ?  108 SER C N   1 
ATOM   10786 C  CA  . SER C  2  108 ? 62.185  29.541  50.120  1.00 93.02  ?  108 SER C CA  1 
ATOM   10787 C  C   . SER C  2  108 ? 61.111  30.406  50.770  1.00 107.19 ?  108 SER C C   1 
ATOM   10788 O  O   . SER C  2  108 ? 61.427  31.451  51.338  1.00 115.32 ?  108 SER C O   1 
ATOM   10789 C  CB  . SER C  2  108 ? 62.599  28.432  51.077  1.00 96.40  ?  108 SER C CB  1 
ATOM   10790 O  OG  . SER C  2  108 ? 63.264  28.982  52.201  1.00 116.65 ?  108 SER C OG  1 
ATOM   10791 N  N   . LYS C  2  109 ? 59.840  29.975  50.694  1.00 99.66  ?  109 LYS C N   1 
ATOM   10792 C  CA  . LYS C  2  109 ? 58.731  30.733  51.275  1.00 101.58 ?  109 LYS C CA  1 
ATOM   10793 C  C   . LYS C  2  109 ? 58.722  30.860  52.798  1.00 119.14 ?  109 LYS C C   1 
ATOM   10794 O  O   . LYS C  2  109 ? 58.194  31.841  53.329  1.00 138.08 ?  109 LYS C O   1 
ATOM   10795 C  CB  . LYS C  2  109 ? 57.384  30.033  51.006  1.00 113.20 ?  109 LYS C CB  1 
ATOM   10796 C  CG  . LYS C  2  109 ? 56.183  30.876  51.422  1.00 137.89 ?  109 LYS C CG  1 
ATOM   10797 C  CD  . LYS C  2  109 ? 54.853  30.187  51.158  1.00 126.27 ?  109 LYS C CD  1 
ATOM   10798 C  CE  . LYS C  2  109 ? 53.693  31.049  51.596  1.00 119.97 ?  109 LYS C CE  1 
ATOM   10799 N  NZ  . LYS C  2  109 ? 52.385  30.487  51.168  1.00 131.53 ?  109 LYS C NZ  1 
ATOM   10800 N  N   . ASP C  2  110 ? 59.326  29.883  53.491  1.00 135.11 ?  110 ASP C N   1 
ATOM   10801 C  CA  . ASP C  2  110 ? 59.398  29.885  54.946  1.00 136.04 ?  110 ASP C CA  1 
ATOM   10802 C  C   . ASP C  2  110 ? 60.890  29.704  55.231  1.00 124.75 ?  110 ASP C C   1 
ATOM   10803 O  O   . ASP C  2  110 ? 61.285  28.810  55.977  1.00 134.97 ?  110 ASP C O   1 
ATOM   10804 C  CB  . ASP C  2  110 ? 58.553  28.812  55.658  1.00 136.21 ?  110 ASP C CB  1 
ATOM   10805 C  CG  . ASP C  2  110 ? 58.286  29.106  57.122  1.00 171.67 ?  110 ASP C CG  1 
ATOM   10806 O  OD1 . ASP C  2  110 ? 58.137  30.300  57.471  1.00 175.01 ?  110 ASP C OD1 1 
ATOM   10807 O  OD2 . ASP C  2  110 ? 58.218  28.140  57.919  1.00 183.34 ?  110 ASP C OD2 1 
ATOM   10808 N  N   . GLY C  2  111 ? 61.698  30.562  54.620  1.00 107.75 ?  111 GLY C N   1 
ATOM   10809 C  CA  . GLY C  2  111 ? 63.144  30.547  54.787  1.00 111.50 ?  111 GLY C CA  1 
ATOM   10810 C  C   . GLY C  2  111 ? 63.678  31.911  55.169  1.00 106.86 ?  111 GLY C C   1 
ATOM   10811 O  O   . GLY C  2  111 ? 62.958  32.910  55.090  1.00 110.47 ?  111 GLY C O   1 
ATOM   10812 N  N   . ASP C  2  112 ? 64.946  31.962  55.591  1.00 103.95 ?  112 ASP C N   1 
ATOM   10813 C  CA  . ASP C  2  112 ? 65.590  33.209  55.998  1.00 92.19  ?  112 ASP C CA  1 
ATOM   10814 C  C   . ASP C  2  112 ? 65.704  34.183  54.820  1.00 87.58  ?  112 ASP C C   1 
ATOM   10815 O  O   . ASP C  2  112 ? 65.507  35.383  54.997  1.00 98.48  ?  112 ASP C O   1 
ATOM   10816 C  CB  . ASP C  2  112 ? 66.981  32.920  56.593  1.00 95.44  ?  112 ASP C CB  1 
ATOM   10817 C  CG  . ASP C  2  112 ? 66.976  32.484  58.048  1.00 104.99 ?  112 ASP C CG  1 
ATOM   10818 O  OD1 . ASP C  2  112 ? 65.917  32.605  58.703  1.00 116.01 ?  112 ASP C OD1 1 
ATOM   10819 O  OD2 . ASP C  2  112 ? 68.035  32.030  58.536  1.00 112.67 ?  112 ASP C OD2 1 
ATOM   10820 N  N   . ILE C  2  113 ? 66.014  33.667  53.622  1.00 88.84  ?  113 ILE C N   1 
ATOM   10821 C  CA  . ILE C  2  113 ? 66.139  34.480  52.412  1.00 82.02  ?  113 ILE C CA  1 
ATOM   10822 C  C   . ILE C  2  113 ? 64.922  34.182  51.547  1.00 95.09  ?  113 ILE C C   1 
ATOM   10823 O  O   . ILE C  2  113 ? 64.609  33.015  51.315  1.00 106.58 ?  113 ILE C O   1 
ATOM   10824 C  CB  . ILE C  2  113 ? 67.461  34.170  51.660  1.00 82.68  ?  113 ILE C CB  1 
ATOM   10825 C  CG1 . ILE C  2  113 ? 68.661  34.214  52.628  1.00 87.85  ?  113 ILE C CG1 1 
ATOM   10826 C  CG2 . ILE C  2  113 ? 67.662  35.147  50.494  1.00 74.72  ?  113 ILE C CG2 1 
ATOM   10827 C  CD1 . ILE C  2  113 ? 69.982  33.700  52.049  1.00 97.83  ?  113 ILE C CD1 1 
ATOM   10828 N  N   . LYS C  2  114 ? 64.238  35.239  51.090  1.00 86.04  ?  114 LYS C N   1 
ATOM   10829 C  CA  . LYS C  2  114 ? 62.999  35.060  50.284  1.00 91.61  ?  114 LYS C CA  1 
ATOM   10830 C  C   . LYS C  2  114 ? 62.907  36.125  49.185  1.00 87.43  ?  114 LYS C C   1 
ATOM   10831 O  O   . LYS C  2  114 ? 63.639  37.129  49.277  1.00 91.56  ?  114 LYS C O   1 
ATOM   10832 C  CB  . LYS C  2  114 ? 61.755  35.164  51.174  1.00 94.31  ?  114 LYS C CB  1 
ATOM   10833 C  CG  . LYS C  2  114 ? 61.755  34.312  52.436  1.00 115.20 ?  114 LYS C CG  1 
ATOM   10834 C  CD  . LYS C  2  114 ? 61.087  34.976  53.622  1.00 94.07  ?  114 LYS C CD  1 
ATOM   10835 C  CE  . LYS C  2  114 ? 59.869  34.224  54.116  1.00 111.08 ?  114 LYS C CE  1 
ATOM   10836 N  NZ  . LYS C  2  114 ? 60.163  33.407  55.318  1.00 140.39 ?  114 LYS C NZ  1 
ATOM   10837 N  N   . VAL C  2  115 ? 62.036  35.913  48.194  1.00 82.35  ?  115 VAL C N   1 
ATOM   10838 C  CA  . VAL C  2  115 ? 61.807  36.898  47.097  1.00 81.92  ?  115 VAL C CA  1 
ATOM   10839 C  C   . VAL C  2  115 ? 60.815  37.959  47.576  1.00 83.76  ?  115 VAL C C   1 
ATOM   10840 O  O   . VAL C  2  115 ? 59.650  37.602  47.834  1.00 85.35  ?  115 VAL C O   1 
ATOM   10841 C  CB  . VAL C  2  115 ? 61.297  36.203  45.821  1.00 79.85  ?  115 VAL C CB  1 
ATOM   10842 C  CG1 . VAL C  2  115 ? 60.862  37.209  44.766  1.00 90.74  ?  115 VAL C CG1 1 
ATOM   10843 C  CG2 . VAL C  2  115 ? 62.327  35.239  45.254  1.00 97.21  ?  115 VAL C CG2 1 
ATOM   10844 N  N   . LYS C  2  116 ? 61.263  39.207  47.686  1.00 88.81  ?  116 LYS C N   1 
ATOM   10845 C  CA  . LYS C  2  116 ? 60.419  40.324  48.107  1.00 87.56  ?  116 LYS C CA  1 
ATOM   10846 C  C   . LYS C  2  116 ? 59.737  41.007  46.912  1.00 87.11  ?  116 LYS C C   1 
ATOM   10847 O  O   . LYS C  2  116 ? 58.549  41.325  46.993  1.00 102.68 ?  116 LYS C O   1 
ATOM   10848 C  CB  . LYS C  2  116 ? 61.249  41.353  48.888  1.00 81.79  ?  116 LYS C CB  1 
ATOM   10849 C  CG  . LYS C  2  116 ? 61.667  40.881  50.271  1.00 82.60  ?  116 LYS C CG  1 
ATOM   10850 C  CD  . LYS C  2  116 ? 62.280  42.017  51.065  1.00 85.05  ?  116 LYS C CD  1 
ATOM   10851 C  CE  . LYS C  2  116 ? 62.707  41.596  52.445  1.00 83.43  ?  116 LYS C CE  1 
ATOM   10852 N  NZ  . LYS C  2  116 ? 63.697  42.543  53.022  1.00 85.35  ?  116 LYS C NZ  1 
ATOM   10853 N  N   . ASP C  2  117 ? 60.473  41.244  45.814  1.00 80.61  ?  117 ASP C N   1 
ATOM   10854 C  CA  . ASP C  2  117 ? 59.893  41.890  44.638  1.00 83.70  ?  117 ASP C CA  1 
ATOM   10855 C  C   . ASP C  2  117 ? 59.563  40.856  43.568  1.00 85.76  ?  117 ASP C C   1 
ATOM   10856 O  O   . ASP C  2  117 ? 60.418  40.499  42.761  1.00 93.63  ?  117 ASP C O   1 
ATOM   10857 C  CB  . ASP C  2  117 ? 60.837  42.966  44.080  1.00 79.31  ?  117 ASP C CB  1 
ATOM   10858 C  CG  . ASP C  2  117 ? 60.123  44.011  43.248  1.00 91.34  ?  117 ASP C CG  1 
ATOM   10859 O  OD1 . ASP C  2  117 ? 59.311  43.625  42.378  1.00 93.60  ?  117 ASP C OD1 1 
ATOM   10860 O  OD2 . ASP C  2  117 ? 60.369  45.215  43.470  1.00 104.91 ?  117 ASP C OD2 1 
ATOM   10861 N  N   . GLU C  2  118 ? 58.313  40.380  43.556  1.00 92.58  ?  118 GLU C N   1 
ATOM   10862 C  CA  . GLU C  2  118 ? 57.871  39.384  42.584  1.00 89.79  ?  118 GLU C CA  1 
ATOM   10863 C  C   . GLU C  2  118 ? 57.779  39.987  41.188  1.00 90.44  ?  118 GLU C C   1 
ATOM   10864 O  O   . GLU C  2  118 ? 58.124  39.323  40.216  1.00 87.70  ?  118 GLU C O   1 
ATOM   10865 C  CB  . GLU C  2  118 ? 56.506  38.805  42.983  1.00 96.19  ?  118 GLU C CB  1 
ATOM   10866 C  CG  . GLU C  2  118 ? 56.537  37.961  44.245  1.00 110.44 ?  118 GLU C CG  1 
ATOM   10867 C  CD  . GLU C  2  118 ? 55.181  37.444  44.682  1.00 109.98 ?  118 GLU C CD  1 
ATOM   10868 O  OE1 . GLU C  2  118 ? 54.299  37.272  43.811  1.00 116.88 ?  118 GLU C OE1 1 
ATOM   10869 O  OE2 . GLU C  2  118 ? 55.000  37.211  45.899  1.00 124.95 ?  118 GLU C OE2 1 
ATOM   10870 N  N   . ASN C  2  119 ? 57.318  41.241  41.082  1.00 93.31  ?  119 ASN C N   1 
ATOM   10871 C  CA  . ASN C  2  119 ? 57.187  41.906  39.787  1.00 91.20  ?  119 ASN C CA  1 
ATOM   10872 C  C   . ASN C  2  119 ? 58.537  42.030  39.093  1.00 92.67  ?  119 ASN C C   1 
ATOM   10873 O  O   . ASN C  2  119 ? 58.630  41.768  37.894  1.00 97.29  ?  119 ASN C O   1 
ATOM   10874 C  CB  . ASN C  2  119 ? 56.554  43.281  39.955  1.00 90.15  ?  119 ASN C CB  1 
ATOM   10875 C  CG  . ASN C  2  119 ? 55.143  43.217  40.476  1.00 110.69 ?  119 ASN C CG  1 
ATOM   10876 O  OD1 . ASN C  2  119 ? 54.457  42.193  40.355  1.00 108.95 ?  119 ASN C OD1 1 
ATOM   10877 N  ND2 . ASN C  2  119 ? 54.676  44.307  41.072  1.00 136.92 ?  119 ASN C ND2 1 
ATOM   10878 N  N   . LYS C  2  120 ? 59.586  42.414  39.840  1.00 91.21  ?  120 LYS C N   1 
ATOM   10879 C  CA  . LYS C  2  120 ? 60.924  42.541  39.270  1.00 80.33  ?  120 LYS C CA  1 
ATOM   10880 C  C   . LYS C  2  120 ? 61.422  41.182  38.806  1.00 84.19  ?  120 LYS C C   1 
ATOM   10881 O  O   . LYS C  2  120 ? 62.013  41.082  37.735  1.00 91.21  ?  120 LYS C O   1 
ATOM   10882 C  CB  . LYS C  2  120 ? 61.904  43.145  40.284  1.00 76.51  ?  120 LYS C CB  1 
ATOM   10883 C  CG  . LYS C  2  120 ? 63.261  43.475  39.675  1.00 74.17  ?  120 LYS C CG  1 
ATOM   10884 C  CD  . LYS C  2  120 ? 63.864  44.745  40.233  1.00 74.39  ?  120 LYS C CD  1 
ATOM   10885 C  CE  . LYS C  2  120 ? 65.129  45.100  39.500  1.00 88.48  ?  120 LYS C CE  1 
ATOM   10886 N  NZ  . LYS C  2  120 ? 65.682  46.401  39.946  1.00 92.08  ?  120 LYS C NZ  1 
ATOM   10887 N  N   . LEU C  2  121 ? 61.170  40.130  39.592  1.00 84.62  ?  121 LEU C N   1 
ATOM   10888 C  CA  . LEU C  2  121 ? 61.584  38.784  39.223  1.00 77.94  ?  121 LEU C CA  1 
ATOM   10889 C  C   . LEU C  2  121 ? 60.888  38.338  37.940  1.00 88.03  ?  121 LEU C C   1 
ATOM   10890 O  O   . LEU C  2  121 ? 61.510  37.675  37.117  1.00 98.52  ?  121 LEU C O   1 
ATOM   10891 C  CB  . LEU C  2  121 ? 61.287  37.793  40.363  1.00 76.28  ?  121 LEU C CB  1 
ATOM   10892 C  CG  . LEU C  2  121 ? 61.463  36.306  40.037  1.00 76.30  ?  121 LEU C CG  1 
ATOM   10893 C  CD1 . LEU C  2  121 ? 62.920  35.957  39.796  1.00 79.54  ?  121 LEU C CD1 1 
ATOM   10894 C  CD2 . LEU C  2  121 ? 60.927  35.451  41.141  1.00 78.84  ?  121 LEU C CD2 1 
ATOM   10895 N  N   . LYS C  2  122 ? 59.611  38.692  37.764  1.00 80.24  ?  122 LYS C N   1 
ATOM   10896 C  CA  . LYS C  2  122 ? 58.874  38.299  36.562  1.00 82.33  ?  122 LYS C CA  1 
ATOM   10897 C  C   . LYS C  2  122 ? 59.487  38.961  35.321  1.00 90.65  ?  122 LYS C C   1 
ATOM   10898 O  O   . LYS C  2  122 ? 59.542  38.336  34.263  1.00 90.27  ?  122 LYS C O   1 
ATOM   10899 C  CB  . LYS C  2  122 ? 57.384  38.658  36.688  1.00 93.68  ?  122 LYS C CB  1 
ATOM   10900 C  CG  . LYS C  2  122 ? 56.677  38.015  37.892  1.00 91.47  ?  122 LYS C CG  1 
ATOM   10901 C  CD  . LYS C  2  122 ? 55.879  36.761  37.543  1.00 89.79  ?  122 LYS C CD  1 
ATOM   10902 C  CE  . LYS C  2  122 ? 54.909  36.370  38.641  1.00 92.66  ?  122 LYS C CE  1 
ATOM   10903 N  NZ  . LYS C  2  122 ? 53.820  37.371  38.831  1.00 95.91  ?  122 LYS C NZ  1 
ATOM   10904 N  N   . GLU C  2  123 ? 59.955  40.220  35.458  1.00 95.36  ?  123 GLU C N   1 
ATOM   10905 C  CA  . GLU C  2  123 ? 60.580  40.971  34.366  1.00 97.97  ?  123 GLU C CA  1 
ATOM   10906 C  C   . GLU C  2  123 ? 61.971  40.417  34.057  1.00 92.12  ?  123 GLU C C   1 
ATOM   10907 O  O   . GLU C  2  123 ? 62.322  40.258  32.888  1.00 95.29  ?  123 GLU C O   1 
ATOM   10908 C  CB  . GLU C  2  123 ? 60.691  42.464  34.729  1.00 91.47  ?  123 GLU C CB  1 
ATOM   10909 C  CG  . GLU C  2  123 ? 59.396  43.241  34.570  1.00 107.43 ?  123 GLU C CG  1 
ATOM   10910 C  CD  . GLU C  2  123 ? 58.965  43.458  33.133  1.00 133.06 ?  123 GLU C CD  1 
ATOM   10911 O  OE1 . GLU C  2  123 ? 59.826  43.822  32.300  1.00 142.56 ?  123 GLU C OE1 1 
ATOM   10912 O  OE2 . GLU C  2  123 ? 57.763  43.264  32.839  1.00 143.71 ?  123 GLU C OE2 1 
ATOM   10913 N  N   . VAL C  2  124 ? 62.765  40.124  35.097  1.00 75.75  ?  124 VAL C N   1 
ATOM   10914 C  CA  . VAL C  2  124 ? 64.109  39.577  34.914  1.00 73.46  ?  124 VAL C CA  1 
ATOM   10915 C  C   . VAL C  2  124 ? 64.004  38.194  34.271  1.00 84.42  ?  124 VAL C C   1 
ATOM   10916 O  O   . VAL C  2  124 ? 64.778  37.879  33.374  1.00 89.36  ?  124 VAL C O   1 
ATOM   10917 C  CB  . VAL C  2  124 ? 64.887  39.542  36.252  1.00 76.64  ?  124 VAL C CB  1 
ATOM   10918 C  CG1 . VAL C  2  124 ? 66.162  38.716  36.130  1.00 69.61  ?  124 VAL C CG1 1 
ATOM   10919 C  CG2 . VAL C  2  124 ? 65.212  40.955  36.726  1.00 81.75  ?  124 VAL C CG2 1 
ATOM   10920 N  N   . ALA C  2  125 ? 63.033  37.380  34.702  1.00 84.77  ?  125 ALA C N   1 
ATOM   10921 C  CA  . ALA C  2  125 ? 62.833  36.049  34.135  1.00 78.05  ?  125 ALA C CA  1 
ATOM   10922 C  C   . ALA C  2  125 ? 62.569  36.109  32.634  1.00 82.90  ?  125 ALA C C   1 
ATOM   10923 O  O   . ALA C  2  125 ? 62.904  35.163  31.932  1.00 99.45  ?  125 ALA C O   1 
ATOM   10924 C  CB  . ALA C  2  125 ? 61.674  35.353  34.830  1.00 78.58  ?  125 ALA C CB  1 
ATOM   10925 N  N   . LYS C  2  126 ? 61.977  37.206  32.137  1.00 83.07  ?  126 LYS C N   1 
ATOM   10926 C  CA  . LYS C  2  126 ? 61.702  37.341  30.709  1.00 88.29  ?  126 LYS C CA  1 
ATOM   10927 C  C   . LYS C  2  126 ? 63.020  37.462  29.935  1.00 88.38  ?  126 LYS C C   1 
ATOM   10928 O  O   . LYS C  2  126 ? 63.173  36.826  28.892  1.00 84.03  ?  126 LYS C O   1 
ATOM   10929 C  CB  . LYS C  2  126 ? 60.800  38.566  30.427  1.00 84.02  ?  126 LYS C CB  1 
ATOM   10930 C  CG  . LYS C  2  126 ? 60.399  38.744  28.958  1.00 107.00 ?  126 LYS C CG  1 
ATOM   10931 C  CD  . LYS C  2  126 ? 59.467  39.942  28.739  1.00 132.25 ?  126 LYS C CD  1 
ATOM   10932 C  CE  . LYS C  2  126 ? 59.087  40.140  27.288  1.00 136.51 ?  126 LYS C CE  1 
ATOM   10933 N  NZ  . LYS C  2  126 ? 58.181  41.309  27.104  1.00 122.27 ?  126 LYS C NZ  1 
ATOM   10934 N  N   . SER C  2  127 ? 63.974  38.260  30.443  1.00 91.70  ?  127 SER C N   1 
ATOM   10935 C  CA  . SER C  2  127 ? 65.259  38.424  29.768  1.00 91.68  ?  127 SER C CA  1 
ATOM   10936 C  C   . SER C  2  127 ? 66.049  37.107  29.734  1.00 85.94  ?  127 SER C C   1 
ATOM   10937 O  O   . SER C  2  127 ? 66.699  36.817  28.731  1.00 98.39  ?  127 SER C O   1 
ATOM   10938 C  CB  . SER C  2  127 ? 66.081  39.534  30.421  1.00 90.30  ?  127 SER C CB  1 
ATOM   10939 O  OG  . SER C  2  127 ? 66.701  39.110  31.624  1.00 106.42 ?  127 SER C OG  1 
ATOM   10940 N  N   . PHE C  2  128 ? 65.987  36.305  30.807  1.00 81.61  ?  128 PHE C N   1 
ATOM   10941 C  CA  . PHE C  2  128 ? 66.703  35.026  30.845  1.00 86.92  ?  128 PHE C CA  1 
ATOM   10942 C  C   . PHE C  2  128 ? 65.931  33.883  30.169  1.00 87.25  ?  128 PHE C C   1 
ATOM   10943 O  O   . PHE C  2  128 ? 66.390  32.744  30.210  1.00 99.72  ?  128 PHE C O   1 
ATOM   10944 C  CB  . PHE C  2  128 ? 67.052  34.642  32.294  1.00 77.57  ?  128 PHE C CB  1 
ATOM   10945 C  CG  . PHE C  2  128 ? 68.184  35.446  32.887  1.00 75.71  ?  128 PHE C CG  1 
ATOM   10946 C  CD1 . PHE C  2  128 ? 69.498  35.163  32.564  1.00 82.26  ?  128 PHE C CD1 1 
ATOM   10947 C  CD2 . PHE C  2  128 ? 67.933  36.480  33.768  1.00 77.78  ?  128 PHE C CD2 1 
ATOM   10948 C  CE1 . PHE C  2  128 ? 70.538  35.900  33.110  1.00 80.38  ?  128 PHE C CE1 1 
ATOM   10949 C  CE2 . PHE C  2  128 ? 68.976  37.215  34.314  1.00 82.35  ?  128 PHE C CE2 1 
ATOM   10950 C  CZ  . PHE C  2  128 ? 70.271  36.918  33.983  1.00 78.27  ?  128 PHE C CZ  1 
ATOM   10951 N  N   . ASN C  2  129 ? 64.782  34.180  29.539  1.00 79.08  ?  129 ASN C N   1 
ATOM   10952 C  CA  . ASN C  2  129 ? 63.959  33.186  28.854  1.00 84.35  ?  129 ASN C CA  1 
ATOM   10953 C  C   . ASN C  2  129 ? 63.460  32.101  29.815  1.00 86.50  ?  129 ASN C C   1 
ATOM   10954 O  O   . ASN C  2  129 ? 63.468  30.916  29.481  1.00 98.58  ?  129 ASN C O   1 
ATOM   10955 C  CB  . ASN C  2  129 ? 64.718  32.579  27.666  1.00 97.62  ?  129 ASN C CB  1 
ATOM   10956 C  CG  . ASN C  2  129 ? 63.826  31.954  26.618  1.00 101.79 ?  129 ASN C CG  1 
ATOM   10957 O  OD1 . ASN C  2  129 ? 62.681  32.375  26.408  1.00 100.88 ?  129 ASN C OD1 1 
ATOM   10958 N  ND2 . ASN C  2  129 ? 64.331  30.935  25.929  1.00 103.69 ?  129 ASN C ND2 1 
ATOM   10959 N  N   . VAL C  2  130 ? 63.020  32.515  31.008  1.00 83.84  ?  130 VAL C N   1 
ATOM   10960 C  CA  . VAL C  2  130 ? 62.481  31.619  32.028  1.00 84.19  ?  130 VAL C CA  1 
ATOM   10961 C  C   . VAL C  2  130 ? 60.975  31.883  32.083  1.00 98.26  ?  130 VAL C C   1 
ATOM   10962 O  O   . VAL C  2  130 ? 60.560  33.038  32.204  1.00 97.56  ?  130 VAL C O   1 
ATOM   10963 C  CB  . VAL C  2  130 ? 63.157  31.858  33.398  1.00 79.59  ?  130 VAL C CB  1 
ATOM   10964 C  CG1 . VAL C  2  130 ? 62.479  31.041  34.494  1.00 79.49  ?  130 VAL C CG1 1 
ATOM   10965 C  CG2 . VAL C  2  130 ? 64.645  31.535  33.333  1.00 85.53  ?  130 VAL C CG2 1 
ATOM   10966 N  N   . GLU C  2  131 ? 60.155  30.826  31.970  1.00 97.01  ?  131 GLU C N   1 
ATOM   10967 C  CA  . GLU C  2  131 ? 58.698  30.972  31.987  1.00 101.49 ?  131 GLU C CA  1 
ATOM   10968 C  C   . GLU C  2  131 ? 58.178  31.403  33.359  1.00 97.07  ?  131 GLU C C   1 
ATOM   10969 O  O   . GLU C  2  131 ? 58.747  31.025  34.381  1.00 97.24  ?  131 GLU C O   1 
ATOM   10970 C  CB  . GLU C  2  131 ? 58.020  29.659  31.556  1.00 111.30 ?  131 GLU C CB  1 
ATOM   10971 C  CG  . GLU C  2  131 ? 58.106  29.378  30.065  1.00 112.52 ?  131 GLU C CG  1 
ATOM   10972 C  CD  . GLU C  2  131 ? 57.306  30.326  29.190  1.00 132.87 ?  131 GLU C CD  1 
ATOM   10973 O  OE1 . GLU C  2  131 ? 56.312  30.907  29.684  1.00 109.98 ?  131 GLU C OE1 1 
ATOM   10974 O  OE2 . GLU C  2  131 ? 57.676  30.488  28.005  1.00 143.47 ?  131 GLU C OE2 1 
ATOM   10975 N  N   . THR C  2  132 ? 57.100  32.202  33.377  1.00 94.37  ?  132 THR C N   1 
ATOM   10976 C  CA  . THR C  2  132 ? 56.495  32.688  34.619  1.00 99.37  ?  132 THR C CA  1 
ATOM   10977 C  C   . THR C  2  132 ? 55.024  32.269  34.757  1.00 107.64 ?  132 THR C C   1 
ATOM   10978 O  O   . THR C  2  132 ? 54.537  32.125  35.878  1.00 101.75 ?  132 THR C O   1 
ATOM   10979 C  CB  . THR C  2  132 ? 56.595  34.217  34.697  1.00 89.35  ?  132 THR C CB  1 
ATOM   10980 O  OG1 . THR C  2  132 ? 55.940  34.786  33.564  1.00 104.45 ?  132 THR C OG1 1 
ATOM   10981 C  CG2 . THR C  2  132 ? 58.030  34.709  34.766  1.00 92.13  ?  132 THR C CG2 1 
ATOM   10982 N  N   . GLU C  2  133 ? 54.318  32.091  33.628  1.00 109.86 ?  133 GLU C N   1 
ATOM   10983 C  CA  . GLU C  2  133 ? 52.900  31.728  33.618  1.00 116.45 ?  133 GLU C CA  1 
ATOM   10984 C  C   . GLU C  2  133 ? 52.564  30.526  34.504  1.00 116.82 ?  133 GLU C C   1 
ATOM   10985 O  O   . GLU C  2  133 ? 53.082  29.432  34.282  1.00 120.26 ?  133 GLU C O   1 
ATOM   10986 C  CB  . GLU C  2  133 ? 52.434  31.454  32.178  1.00 114.80 ?  133 GLU C CB  1 
ATOM   10987 C  CG  . GLU C  2  133 ? 50.927  31.502  32.000  1.00 138.00 ?  133 GLU C CG  1 
ATOM   10988 C  CD  . GLU C  2  133 ? 50.358  32.906  31.950  1.00 151.38 ?  133 GLU C CD  1 
ATOM   10989 O  OE1 . GLU C  2  133 ? 50.333  33.576  33.008  1.00 153.07 ?  133 GLU C OE1 1 
ATOM   10990 O  OE2 . GLU C  2  133 ? 49.934  33.337  30.853  1.00 166.88 ?  133 GLU C OE2 1 
ATOM   10991 N  N   . GLY C  2  134 ? 51.686  30.747  35.481  1.00 108.51 ?  134 GLY C N   1 
ATOM   10992 C  CA  . GLY C  2  134 ? 51.229  29.719  36.410  1.00 108.50 ?  134 GLY C CA  1 
ATOM   10993 C  C   . GLY C  2  134 ? 52.325  28.879  37.038  1.00 121.10 ?  134 GLY C C   1 
ATOM   10994 O  O   . GLY C  2  134 ? 52.262  27.648  36.989  1.00 129.23 ?  134 GLY C O   1 
ATOM   10995 N  N   . ARG C  2  135 ? 53.335  29.530  37.637  1.00 119.87 ?  135 ARG C N   1 
ATOM   10996 C  CA  . ARG C  2  135 ? 54.452  28.831  38.278  1.00 104.37 ?  135 ARG C CA  1 
ATOM   10997 C  C   . ARG C  2  135 ? 54.782  29.461  39.633  1.00 104.98 ?  135 ARG C C   1 
ATOM   10998 O  O   . ARG C  2  135 ? 54.520  30.647  39.842  1.00 107.25 ?  135 ARG C O   1 
ATOM   10999 C  CB  . ARG C  2  135 ? 55.697  28.882  37.371  1.00 96.37  ?  135 ARG C CB  1 
ATOM   11000 C  CG  . ARG C  2  135 ? 55.760  27.781  36.312  1.00 105.55 ?  135 ARG C CG  1 
ATOM   11001 C  CD  . ARG C  2  135 ? 56.629  28.170  35.124  1.00 97.09  ?  135 ARG C CD  1 
ATOM   11002 N  NE  . ARG C  2  135 ? 57.997  28.523  35.512  1.00 96.42  ?  135 ARG C NE  1 
ATOM   11003 C  CZ  . ARG C  2  135 ? 58.980  27.654  35.735  1.00 93.47  ?  135 ARG C CZ  1 
ATOM   11004 N  NH1 . ARG C  2  135 ? 58.764  26.348  35.614  1.00 93.64  ?  135 ARG C NH1 1 
ATOM   11005 N  NH2 . ARG C  2  135 ? 60.188  28.083  36.080  1.00 94.75  ?  135 ARG C NH2 1 
ATOM   11006 N  N   . ASP C  2  136 ? 55.363  28.670  40.556  1.00 100.48 ?  136 ASP C N   1 
ATOM   11007 C  CA  . ASP C  2  136 ? 55.742  29.166  41.881  1.00 98.32  ?  136 ASP C CA  1 
ATOM   11008 C  C   . ASP C  2  136 ? 56.801  30.236  41.736  1.00 99.61  ?  136 ASP C C   1 
ATOM   11009 O  O   . ASP C  2  136 ? 57.734  30.052  40.958  1.00 96.75  ?  136 ASP C O   1 
ATOM   11010 C  CB  . ASP C  2  136 ? 56.333  28.041  42.749  1.00 99.43  ?  136 ASP C CB  1 
ATOM   11011 C  CG  . ASP C  2  136 ? 55.331  27.260  43.566  1.00 126.78 ?  136 ASP C CG  1 
ATOM   11012 O  OD1 . ASP C  2  136 ? 54.202  27.760  43.760  1.00 154.34 ?  136 ASP C OD1 1 
ATOM   11013 O  OD2 . ASP C  2  136 ? 55.677  26.151  44.022  1.00 153.19 ?  136 ASP C OD2 1 
ATOM   11014 N  N   . ILE C  2  137 ? 56.688  31.338  42.485  1.00 97.20  ?  137 ILE C N   1 
ATOM   11015 C  CA  . ILE C  2  137 ? 57.696  32.402  42.411  1.00 94.84  ?  137 ILE C CA  1 
ATOM   11016 C  C   . ILE C  2  137 ? 59.081  31.873  42.812  1.00 100.56 ?  137 ILE C C   1 
ATOM   11017 O  O   . ILE C  2  137 ? 60.077  32.360  42.288  1.00 96.43  ?  137 ILE C O   1 
ATOM   11018 C  CB  . ILE C  2  137 ? 57.299  33.673  43.217  1.00 97.11  ?  137 ILE C CB  1 
ATOM   11019 C  CG1 . ILE C  2  137 ? 56.772  33.305  44.622  1.00 121.24 ?  137 ILE C CG1 1 
ATOM   11020 C  CG2 . ILE C  2  137 ? 56.268  34.504  42.442  1.00 107.39 ?  137 ILE C CG2 1 
ATOM   11021 C  CD1 . ILE C  2  137 ? 56.836  34.416  45.646  1.00 136.44 ?  137 ILE C CD1 1 
ATOM   11022 N  N   . TYR C  2  138 ? 59.151  30.866  43.700  1.00 97.04  ?  138 TYR C N   1 
ATOM   11023 C  CA  . TYR C  2  138 ? 60.439  30.298  44.104  1.00 83.78  ?  138 TYR C CA  1 
ATOM   11024 C  C   . TYR C  2  138 ? 60.993  29.347  43.048  1.00 90.27  ?  138 TYR C C   1 
ATOM   11025 O  O   . TYR C  2  138 ? 62.211  29.235  42.916  1.00 94.96  ?  138 TYR C O   1 
ATOM   11026 C  CB  . TYR C  2  138 ? 60.341  29.649  45.487  1.00 81.97  ?  138 TYR C CB  1 
ATOM   11027 C  CG  . TYR C  2  138 ? 60.113  30.694  46.552  1.00 82.40  ?  138 TYR C CG  1 
ATOM   11028 C  CD1 . TYR C  2  138 ? 61.176  31.394  47.103  1.00 83.64  ?  138 TYR C CD1 1 
ATOM   11029 C  CD2 . TYR C  2  138 ? 58.831  31.085  46.903  1.00 84.75  ?  138 TYR C CD2 1 
ATOM   11030 C  CE1 . TYR C  2  138 ? 60.971  32.398  48.038  1.00 91.83  ?  138 TYR C CE1 1 
ATOM   11031 C  CE2 . TYR C  2  138 ? 58.612  32.091  47.832  1.00 95.00  ?  138 TYR C CE2 1 
ATOM   11032 C  CZ  . TYR C  2  138 ? 59.686  32.747  48.400  1.00 94.81  ?  138 TYR C CZ  1 
ATOM   11033 O  OH  . TYR C  2  138 ? 59.477  33.745  49.322  1.00 103.60 ?  138 TYR C OH  1 
ATOM   11034 N  N   . ASP C  2  139 ? 60.120  28.688  42.273  1.00 83.45  ?  139 ASP C N   1 
ATOM   11035 C  CA  . ASP C  2  139 ? 60.577  27.824  41.186  1.00 87.19  ?  139 ASP C CA  1 
ATOM   11036 C  C   . ASP C  2  139 ? 61.149  28.731  40.073  1.00 90.68  ?  139 ASP C C   1 
ATOM   11037 O  O   . ASP C  2  139 ? 62.148  28.378  39.452  1.00 92.14  ?  139 ASP C O   1 
ATOM   11038 C  CB  . ASP C  2  139 ? 59.430  26.952  40.639  1.00 82.36  ?  139 ASP C CB  1 
ATOM   11039 C  CG  . ASP C  2  139 ? 59.091  25.743  41.495  1.00 107.76 ?  139 ASP C CG  1 
ATOM   11040 O  OD1 . ASP C  2  139 ? 59.864  25.439  42.433  1.00 121.34 ?  139 ASP C OD1 1 
ATOM   11041 O  OD2 . ASP C  2  139 ? 58.057  25.097  41.223  1.00 112.88 ?  139 ASP C OD2 1 
ATOM   11042 N  N   . ILE C  2  140 ? 60.530  29.906  39.842  1.00 92.67  ?  140 ILE C N   1 
ATOM   11043 C  CA  . ILE C  2  140 ? 61.004  30.865  38.850  1.00 74.77  ?  140 ILE C CA  1 
ATOM   11044 C  C   . ILE C  2  140 ? 62.344  31.421  39.344  1.00 79.00  ?  140 ILE C C   1 
ATOM   11045 O  O   . ILE C  2  140 ? 63.302  31.461  38.581  1.00 92.37  ?  140 ILE C O   1 
ATOM   11046 C  CB  . ILE C  2  140 ? 59.964  32.003  38.629  1.00 75.70  ?  140 ILE C CB  1 
ATOM   11047 C  CG1 . ILE C  2  140 ? 58.705  31.467  37.920  1.00 78.14  ?  140 ILE C CG1 1 
ATOM   11048 C  CG2 . ILE C  2  140 ? 60.575  33.162  37.828  1.00 73.37  ?  140 ILE C CG2 1 
ATOM   11049 C  CD1 . ILE C  2  140 ? 57.470  32.341  38.088  1.00 79.96  ?  140 ILE C CD1 1 
ATOM   11050 N  N   . ALA C  2  141 ? 62.414  31.834  40.620  1.00 73.43  ?  141 ALA C N   1 
ATOM   11051 C  CA  . ALA C  2  141 ? 63.634  32.382  41.219  1.00 76.65  ?  141 ALA C CA  1 
ATOM   11052 C  C   . ALA C  2  141 ? 64.827  31.444  41.087  1.00 87.31  ?  141 ALA C C   1 
ATOM   11053 O  O   . ALA C  2  141 ? 65.945  31.911  40.874  1.00 87.62  ?  141 ALA C O   1 
ATOM   11054 C  CB  . ALA C  2  141 ? 63.398  32.700  42.686  1.00 79.76  ?  141 ALA C CB  1 
ATOM   11055 N  N   . HIS C  2  142 ? 64.605  30.133  41.220  1.00 74.02  ?  142 HIS C N   1 
ATOM   11056 C  CA  . HIS C  2  142 ? 65.693  29.169  41.111  1.00 78.21  ?  142 HIS C CA  1 
ATOM   11057 C  C   . HIS C  2  142 ? 66.131  28.997  39.660  1.00 83.32  ?  142 HIS C C   1 
ATOM   11058 O  O   . HIS C  2  142 ? 67.327  28.916  39.394  1.00 83.03  ?  142 HIS C O   1 
ATOM   11059 C  CB  . HIS C  2  142 ? 65.286  27.836  41.742  1.00 78.06  ?  142 HIS C CB  1 
ATOM   11060 C  CG  . HIS C  2  142 ? 64.958  27.943  43.204  1.00 85.36  ?  142 HIS C CG  1 
ATOM   11061 N  ND1 . HIS C  2  142 ? 64.181  26.993  43.835  1.00 97.03  ?  142 HIS C ND1 1 
ATOM   11062 C  CD2 . HIS C  2  142 ? 65.315  28.885  44.111  1.00 78.91  ?  142 HIS C CD2 1 
ATOM   11063 C  CE1 . HIS C  2  142 ? 64.091  27.379  45.097  1.00 87.61  ?  142 HIS C CE1 1 
ATOM   11064 N  NE2 . HIS C  2  142 ? 64.756  28.515  45.307  1.00 82.71  ?  142 HIS C NE2 1 
ATOM   11065 N  N   . ASP C  2  143 ? 65.182  28.967  38.721  1.00 80.46  ?  143 ASP C N   1 
ATOM   11066 C  CA  . ASP C  2  143 ? 65.508  28.845  37.301  1.00 71.44  ?  143 ASP C CA  1 
ATOM   11067 C  C   . ASP C  2  143 ? 66.248  30.099  36.820  1.00 82.00  ?  143 ASP C C   1 
ATOM   11068 O  O   . ASP C  2  143 ? 67.152  29.992  35.992  1.00 86.23  ?  143 ASP C O   1 
ATOM   11069 C  CB  . ASP C  2  143 ? 64.236  28.634  36.467  1.00 80.29  ?  143 ASP C CB  1 
ATOM   11070 C  CG  . ASP C  2  143 ? 63.659  27.233  36.538  1.00 98.73  ?  143 ASP C CG  1 
ATOM   11071 O  OD1 . ASP C  2  143 ? 64.173  26.415  37.341  1.00 101.16 ?  143 ASP C OD1 1 
ATOM   11072 O  OD2 . ASP C  2  143 ? 62.693  26.953  35.795  1.00 81.88  ?  143 ASP C OD2 1 
ATOM   11073 N  N   . VAL C  2  144 ? 65.872  31.283  37.339  1.00 79.87  ?  144 VAL C N   1 
ATOM   11074 C  CA  . VAL C  2  144 ? 66.524  32.543  36.978  1.00 78.41  ?  144 VAL C CA  1 
ATOM   11075 C  C   . VAL C  2  144 ? 67.953  32.506  37.505  1.00 75.62  ?  144 VAL C C   1 
ATOM   11076 O  O   . VAL C  2  144 ? 68.882  32.838  36.776  1.00 74.90  ?  144 VAL C O   1 
ATOM   11077 C  CB  . VAL C  2  144 ? 65.755  33.769  37.534  1.00 74.16  ?  144 VAL C CB  1 
ATOM   11078 C  CG1 . VAL C  2  144 ? 66.588  35.044  37.419  1.00 68.13  ?  144 VAL C CG1 1 
ATOM   11079 C  CG2 . VAL C  2  144 ? 64.416  33.936  36.824  1.00 78.08  ?  144 VAL C CG2 1 
ATOM   11080 N  N   . ALA C  2  145 ? 68.134  32.085  38.765  1.00 72.14  ?  145 ALA C N   1 
ATOM   11081 C  CA  . ALA C  2  145 ? 69.456  31.991  39.373  1.00 74.22  ?  145 ALA C CA  1 
ATOM   11082 C  C   . ALA C  2  145 ? 70.354  31.050  38.577  1.00 78.93  ?  145 ALA C C   1 
ATOM   11083 O  O   . ALA C  2  145 ? 71.536  31.334  38.417  1.00 68.17  ?  145 ALA C O   1 
ATOM   11084 C  CB  . ALA C  2  145 ? 69.335  31.496  40.805  1.00 72.71  ?  145 ALA C CB  1 
ATOM   11085 N  N   . LYS C  2  146 ? 69.803  29.938  38.072  1.00 80.53  ?  146 LYS C N   1 
ATOM   11086 C  CA  . LYS C  2  146 ? 70.584  28.991  37.280  1.00 70.81  ?  146 LYS C CA  1 
ATOM   11087 C  C   . LYS C  2  146 ? 71.011  29.633  35.966  1.00 74.48  ?  146 LYS C C   1 
ATOM   11088 O  O   . LYS C  2  146 ? 72.142  29.424  35.524  1.00 81.18  ?  146 LYS C O   1 
ATOM   11089 C  CB  . LYS C  2  146 ? 69.784  27.706  37.002  1.00 71.18  ?  146 LYS C CB  1 
ATOM   11090 C  CG  . LYS C  2  146 ? 69.887  26.668  38.114  1.00 70.98  ?  146 LYS C CG  1 
ATOM   11091 C  CD  . LYS C  2  146 ? 69.054  25.419  37.822  1.00 96.30  ?  146 LYS C CD  1 
ATOM   11092 C  CE  . LYS C  2  146 ? 67.610  25.525  38.277  1.00 100.61 ?  146 LYS C CE  1 
ATOM   11093 N  NZ  . LYS C  2  146 ? 67.198  24.356  39.099  1.00 105.28 ?  146 LYS C NZ  1 
ATOM   11094 N  N   . GLU C  2  147 ? 70.115  30.412  35.339  1.00 72.67  ?  147 GLU C N   1 
ATOM   11095 C  CA  . GLU C  2  147 ? 70.425  31.090  34.081  1.00 73.40  ?  147 GLU C CA  1 
ATOM   11096 C  C   . GLU C  2  147 ? 71.427  32.221  34.303  1.00 72.31  ?  147 GLU C C   1 
ATOM   11097 O  O   . GLU C  2  147 ? 72.295  32.449  33.463  1.00 70.47  ?  147 GLU C O   1 
ATOM   11098 C  CB  . GLU C  2  147 ? 69.146  31.629  33.422  1.00 77.15  ?  147 GLU C CB  1 
ATOM   11099 C  CG  . GLU C  2  147 ? 68.296  30.546  32.785  1.00 88.11  ?  147 GLU C CG  1 
ATOM   11100 C  CD  . GLU C  2  147 ? 69.005  29.800  31.672  1.00 112.53 ?  147 GLU C CD  1 
ATOM   11101 O  OE1 . GLU C  2  147 ? 69.371  30.448  30.664  1.00 101.79 ?  147 GLU C OE1 1 
ATOM   11102 O  OE2 . GLU C  2  147 ? 69.204  28.571  31.812  1.00 114.49 ?  147 GLU C OE2 1 
ATOM   11103 N  N   . GLY C  2  148 ? 71.300  32.913  35.426  1.00 66.63  ?  148 GLY C N   1 
ATOM   11104 C  CA  . GLY C  2  148 ? 72.202  33.996  35.777  1.00 73.30  ?  148 GLY C CA  1 
ATOM   11105 C  C   . GLY C  2  148 ? 73.589  33.478  36.096  1.00 72.24  ?  148 GLY C C   1 
ATOM   11106 O  O   . GLY C  2  148 ? 74.583  34.074  35.679  1.00 74.57  ?  148 GLY C O   1 
ATOM   11107 N  N   . LEU C  2  149 ? 73.672  32.355  36.824  1.00 68.02  ?  149 LEU C N   1 
ATOM   11108 C  CA  . LEU C  2  149 ? 74.961  31.773  37.177  1.00 61.32  ?  149 LEU C CA  1 
ATOM   11109 C  C   . LEU C  2  149 ? 75.725  31.322  35.933  1.00 70.10  ?  149 LEU C C   1 
ATOM   11110 O  O   . LEU C  2  149 ? 76.953  31.386  35.932  1.00 67.80  ?  149 LEU C O   1 
ATOM   11111 C  CB  . LEU C  2  149 ? 74.800  30.583  38.140  1.00 59.91  ?  149 LEU C CB  1 
ATOM   11112 C  CG  . LEU C  2  149 ? 74.528  30.910  39.615  1.00 63.77  ?  149 LEU C CG  1 
ATOM   11113 C  CD1 . LEU C  2  149 ? 74.068  29.673  40.366  1.00 59.37  ?  149 LEU C CD1 1 
ATOM   11114 C  CD2 . LEU C  2  149 ? 75.759  31.488  40.300  1.00 60.89  ?  149 LEU C CD2 1 
ATOM   11115 N  N   . SER C  2  150 ? 75.015  30.873  34.876  1.00 64.75  ?  150 SER C N   1 
ATOM   11116 C  CA  . SER C  2  150 ? 75.668  30.419  33.644  1.00 68.42  ?  150 SER C CA  1 
ATOM   11117 C  C   . SER C  2  150 ? 76.491  31.541  33.006  1.00 65.00  ?  150 SER C C   1 
ATOM   11118 O  O   . SER C  2  150 ? 77.555  31.277  32.455  1.00 72.35  ?  150 SER C O   1 
ATOM   11119 C  CB  . SER C  2  150 ? 74.645  29.877  32.650  1.00 64.12  ?  150 SER C CB  1 
ATOM   11120 O  OG  . SER C  2  150 ? 73.948  30.916  31.983  1.00 75.29  ?  150 SER C OG  1 
ATOM   11121 N  N   . ASN C  2  151 ? 76.037  32.787  33.160  1.00 67.63  ?  151 ASN C N   1 
ATOM   11122 C  CA  . ASN C  2  151 ? 76.759  33.948  32.570  1.00 65.20  ?  151 ASN C CA  1 
ATOM   11123 C  C   . ASN C  2  151 ? 78.166  34.062  33.171  1.00 59.42  ?  151 ASN C C   1 
ATOM   11124 O  O   . ASN C  2  151 ? 78.993  34.780  32.580  1.00 68.56  ?  151 ASN C O   1 
ATOM   11125 C  CB  . ASN C  2  151 ? 75.968  35.247  32.740  1.00 59.03  ?  151 ASN C CB  1 
ATOM   11126 C  CG  . ASN C  2  151 ? 74.778  35.341  31.808  1.00 69.35  ?  151 ASN C CG  1 
ATOM   11127 O  OD1 . ASN C  2  151 ? 74.402  34.360  31.172  1.00 79.28  ?  151 ASN C OD1 1 
ATOM   11128 N  ND2 . ASN C  2  151 ? 74.184  36.520  31.717  1.00 68.26  ?  151 ASN C ND2 1 
ATOM   11129 N  N   . TYR C  2  152 ? 78.426  33.392  34.298  1.00 60.98  ?  152 TYR C N   1 
ATOM   11130 C  CA  . TYR C  2  152 ? 79.735  33.460  34.940  1.00 64.71  ?  152 TYR C CA  1 
ATOM   11131 C  C   . TYR C  2  152 ? 80.752  32.479  34.365  1.00 68.14  ?  152 TYR C C   1 
ATOM   11132 O  O   . TYR C  2  152 ? 81.936  32.811  34.325  1.00 70.82  ?  152 TYR C O   1 
ATOM   11133 C  CB  . TYR C  2  152 ? 79.611  33.232  36.453  1.00 45.67  ?  152 TYR C CB  1 
ATOM   11134 C  CG  . TYR C  2  152 ? 79.033  34.421  37.179  1.00 54.45  ?  152 TYR C CG  1 
ATOM   11135 C  CD1 . TYR C  2  152 ? 77.663  34.591  37.292  1.00 66.26  ?  152 TYR C CD1 1 
ATOM   11136 C  CD2 . TYR C  2  152 ? 79.855  35.402  37.709  1.00 59.30  ?  152 TYR C CD2 1 
ATOM   11137 C  CE1 . TYR C  2  152 ? 77.124  35.692  37.943  1.00 67.76  ?  152 TYR C CE1 1 
ATOM   11138 C  CE2 . TYR C  2  152 ? 79.329  36.511  38.358  1.00 64.47  ?  152 TYR C CE2 1 
ATOM   11139 C  CZ  . TYR C  2  152 ? 77.960  36.653  38.474  1.00 66.83  ?  152 TYR C CZ  1 
ATOM   11140 O  OH  . TYR C  2  152 ? 77.435  37.757  39.100  1.00 69.41  ?  152 TYR C OH  1 
ATOM   11141 N  N   . GLY C  2  153 ? 80.316  31.291  33.943  1.00 61.68  ?  153 GLY C N   1 
ATOM   11142 C  CA  . GLY C  2  153 ? 81.253  30.305  33.421  1.00 58.88  ?  153 GLY C CA  1 
ATOM   11143 C  C   . GLY C  2  153 ? 80.804  29.426  32.270  1.00 65.41  ?  153 GLY C C   1 
ATOM   11144 O  O   . GLY C  2  153 ? 81.336  28.322  32.118  1.00 72.33  ?  153 GLY C O   1 
ATOM   11145 N  N   . LYS C  2  154 ? 79.860  29.889  31.430  1.00 58.28  ?  154 LYS C N   1 
ATOM   11146 C  CA  . LYS C  2  154 ? 79.425  29.072  30.295  1.00 54.65  ?  154 LYS C CA  1 
ATOM   11147 C  C   . LYS C  2  154 ? 80.502  29.108  29.205  1.00 64.04  ?  154 LYS C C   1 
ATOM   11148 O  O   . LYS C  2  154 ? 81.042  30.173  28.913  1.00 68.30  ?  154 LYS C O   1 
ATOM   11149 C  CB  . LYS C  2  154 ? 78.038  29.491  29.777  1.00 52.38  ?  154 LYS C CB  1 
ATOM   11150 C  CG  . LYS C  2  154 ? 77.963  30.859  29.109  1.00 55.02  ?  154 LYS C CG  1 
ATOM   11151 C  CD  . LYS C  2  154 ? 76.588  31.523  29.265  1.00 65.03  ?  154 LYS C CD  1 
ATOM   11152 C  CE  . LYS C  2  154 ? 75.439  30.746  28.656  1.00 71.30  ?  154 LYS C CE  1 
ATOM   11153 N  NZ  . LYS C  2  154 ? 75.340  30.945  27.189  1.00 91.98  ?  154 LYS C NZ  1 
ATOM   11154 N  N   . GLN C  2  155 ? 80.852  27.941  28.641  1.00 59.03  ?  155 GLN C N   1 
ATOM   11155 C  CA  . GLN C  2  155 ? 81.894  27.853  27.610  1.00 62.19  ?  155 GLN C CA  1 
ATOM   11156 C  C   . GLN C  2  155 ? 81.330  27.779  26.185  1.00 64.64  ?  155 GLN C C   1 
ATOM   11157 O  O   . GLN C  2  155 ? 82.066  28.009  25.226  1.00 66.75  ?  155 GLN C O   1 
ATOM   11158 C  CB  . GLN C  2  155 ? 82.810  26.647  27.877  1.00 55.95  ?  155 GLN C CB  1 
ATOM   11159 C  CG  . GLN C  2  155 ? 83.425  26.633  29.273  1.00 60.35  ?  155 GLN C CG  1 
ATOM   11160 C  CD  . GLN C  2  155 ? 84.302  27.833  29.518  1.00 54.45  ?  155 GLN C CD  1 
ATOM   11161 O  OE1 . GLN C  2  155 ? 85.126  28.206  28.679  1.00 55.77  ?  155 GLN C OE1 1 
ATOM   11162 N  NE2 . GLN C  2  155 ? 84.153  28.467  30.677  1.00 61.87  ?  155 GLN C NE2 1 
ATOM   11163 N  N   . LEU C  2  156 ? 80.040  27.449  26.045  1.00 65.22  ?  156 LEU C N   1 
ATOM   11164 C  CA  . LEU C  2  156 ? 79.371  27.364  24.748  1.00 62.40  ?  156 LEU C CA  1 
ATOM   11165 C  C   . LEU C  2  156 ? 78.084  28.186  24.806  1.00 67.63  ?  156 LEU C C   1 
ATOM   11166 O  O   . LEU C  2  156 ? 77.557  28.439  25.890  1.00 81.25  ?  156 LEU C O   1 
ATOM   11167 C  CB  . LEU C  2  156 ? 79.047  25.905  24.407  1.00 46.96  ?  156 LEU C CB  1 
ATOM   11168 C  CG  . LEU C  2  156 ? 80.244  24.988  24.203  1.00 56.86  ?  156 LEU C CG  1 
ATOM   11169 C  CD1 . LEU C  2  156 ? 79.831  23.538  24.276  1.00 55.36  ?  156 LEU C CD1 1 
ATOM   11170 C  CD2 . LEU C  2  156 ? 80.922  25.262  22.877  1.00 64.68  ?  156 LEU C CD2 1 
ATOM   11171 N  N   . GLY C  2  157 ? 77.587  28.598  23.649  1.00 66.88  ?  157 GLY C N   1 
ATOM   11172 C  CA  . GLY C  2  157 ? 76.372  29.400  23.582  1.00 70.01  ?  157 GLY C CA  1 
ATOM   11173 C  C   . GLY C  2  157 ? 76.645  30.880  23.756  1.00 84.08  ?  157 GLY C C   1 
ATOM   11174 O  O   . GLY C  2  157 ? 77.800  31.290  23.910  1.00 75.89  ?  157 GLY C O   1 
ATOM   11175 N  N   . GLU C  2  158 ? 75.581  31.697  23.733  1.00 87.98  ?  158 GLU C N   1 
ATOM   11176 C  CA  . GLU C  2  158 ? 75.703  33.147  23.867  1.00 76.64  ?  158 GLU C CA  1 
ATOM   11177 C  C   . GLU C  2  158 ? 75.253  33.625  25.242  1.00 65.57  ?  158 GLU C C   1 
ATOM   11178 O  O   . GLU C  2  158 ? 74.342  33.054  25.837  1.00 72.44  ?  158 GLU C O   1 
ATOM   11179 C  CB  . GLU C  2  158 ? 74.892  33.848  22.769  1.00 95.28  ?  158 GLU C CB  1 
ATOM   11180 C  CG  . GLU C  2  158 ? 75.332  33.481  21.360  1.00 102.23 ?  158 GLU C CG  1 
ATOM   11181 C  CD  . GLU C  2  158 ? 74.221  33.539  20.329  1.00 142.52 ?  158 GLU C CD  1 
ATOM   11182 O  OE1 . GLU C  2  158 ? 73.286  32.709  20.416  1.00 145.79 ?  158 GLU C OE1 1 
ATOM   11183 O  OE2 . GLU C  2  158 ? 74.285  34.412  19.432  1.00 151.09 ?  158 GLU C OE2 1 
ATOM   11184 N  N   . VAL C  2  159 ? 75.896  34.694  25.734  1.00 69.73  ?  159 VAL C N   1 
ATOM   11185 C  CA  . VAL C  2  159 ? 75.580  35.240  27.091  1.00 56.57  ?  159 VAL C CA  1 
ATOM   11186 C  C   . VAL C  2  159 ? 74.330  36.121  27.019  1.00 62.78  ?  159 VAL C C   1 
ATOM   11187 O  O   . VAL C  2  159 ? 74.122  36.764  25.974  1.00 79.06  ?  159 VAL C O   1 
ATOM   11188 C  CB  . VAL C  2  159 ? 76.775  36.009  27.698  1.00 51.31  ?  159 VAL C CB  1 
ATOM   11189 C  CG1 . VAL C  2  159 ? 76.636  36.259  29.201  1.00 81.34  ?  159 VAL C CG1 1 
ATOM   11190 C  CG2 . VAL C  2  159 ? 78.097  35.325  27.389  1.00 70.68  ?  159 VAL C CG2 1 
ATOM   11191 N  N   . THR C  2  160 ? 73.539  36.145  28.090  1.00 65.90  ?  160 THR C N   1 
ATOM   11192 C  CA  . THR C  2  160 ? 72.314  36.937  28.185  1.00 60.60  ?  160 THR C CA  1 
ATOM   11193 C  C   . THR C  2  160 ? 72.660  38.340  28.667  1.00 56.71  ?  160 THR C C   1 
ATOM   11194 O  O   . THR C  2  160 ? 73.270  38.479  29.724  1.00 68.66  ?  160 THR C O   1 
ATOM   11195 C  CB  . THR C  2  160 ? 71.325  36.266  29.155  1.00 57.83  ?  160 THR C CB  1 
ATOM   11196 O  OG1 . THR C  2  160 ? 70.867  35.039  28.584  1.00 75.11  ?  160 THR C OG1 1 
ATOM   11197 C  CG2 . THR C  2  160 ? 70.133  37.150  29.476  1.00 70.88  ?  160 THR C CG2 1 
ATOM   11198 N  N   . LEU C  2  161 ? 72.289  39.345  27.871  1.00 58.86  ?  161 LEU C N   1 
ATOM   11199 C  CA  . LEU C  2  161 ? 72.586  40.756  28.229  1.00 57.21  ?  161 LEU C CA  1 
ATOM   11200 C  C   . LEU C  2  161 ? 71.272  41.480  28.536  1.00 66.48  ?  161 LEU C C   1 
ATOM   11201 O  O   . LEU C  2  161 ? 70.207  40.968  28.144  1.00 68.02  ?  161 LEU C O   1 
ATOM   11202 C  CB  . LEU C  2  161 ? 73.334  41.411  27.065  1.00 52.71  ?  161 LEU C CB  1 
ATOM   11203 C  CG  . LEU C  2  161 ? 74.840  41.157  27.036  1.00 55.05  ?  161 LEU C CG  1 
ATOM   11204 C  CD1 . LEU C  2  161 ? 75.497  41.902  25.884  1.00 51.22  ?  161 LEU C CD1 1 
ATOM   11205 C  CD2 . LEU C  2  161 ? 75.480  41.549  28.358  1.00 50.13  ?  161 LEU C CD2 1 
ATOM   11206 N  N   . PRO C  2  162 ? 71.303  42.644  29.218  1.00 63.24  ?  162 PRO C N   1 
ATOM   11207 C  CA  . PRO C  2  162 ? 70.088  43.358  29.613  1.00 53.04  ?  162 PRO C CA  1 
ATOM   11208 C  C   . PRO C  2  162 ? 69.349  43.954  28.410  1.00 66.13  ?  162 PRO C C   1 
ATOM   11209 O  O   . PRO C  2  162 ? 69.983  44.240  27.412  1.00 80.88  ?  162 PRO C O   1 
ATOM   11210 C  CB  . PRO C  2  162 ? 70.607  44.509  30.489  1.00 57.72  ?  162 PRO C CB  1 
ATOM   11211 C  CG  . PRO C  2  162 ? 72.010  44.100  30.872  1.00 62.23  ?  162 PRO C CG  1 
ATOM   11212 C  CD  . PRO C  2  162 ? 72.514  43.325  29.675  1.00 73.24  ?  162 PRO C CD  1 
ATOM   11213 N  N   . PRO C  2  163 ? 68.016  44.149  28.496  1.00 66.68  ?  163 PRO C N   1 
ATOM   11214 C  CA  . PRO C  2  163 ? 67.249  44.741  27.401  1.00 72.64  ?  163 PRO C CA  1 
ATOM   11215 C  C   . PRO C  2  163 ? 67.590  46.224  27.200  1.00 69.60  ?  163 PRO C C   1 
ATOM   11216 O  O   . PRO C  2  163 ? 67.401  46.712  26.103  1.00 68.89  ?  163 PRO C O   1 
ATOM   11217 C  CB  . PRO C  2  163 ? 65.790  44.614  27.864  1.00 59.97  ?  163 PRO C CB  1 
ATOM   11218 C  CG  . PRO C  2  163 ? 65.827  43.590  28.979  1.00 65.02  ?  163 PRO C CG  1 
ATOM   11219 C  CD  . PRO C  2  163 ? 67.176  43.787  29.635  1.00 72.40  ?  163 PRO C CD  1 
ATOM   11220 N  N   . SER C  2  164 ? 68.081  46.900  28.244  1.00 61.92  ?  164 SER C N   1 
ATOM   11221 C  CA  . SER C  2  164 ? 68.332  48.360  28.123  1.00 63.90  ?  164 SER C CA  1 
ATOM   11222 C  C   . SER C  2  164 ? 69.549  48.629  27.234  1.00 66.01  ?  164 SER C C   1 
ATOM   11223 O  O   . SER C  2  164 ? 69.763  49.801  26.877  1.00 66.20  ?  164 SER C O   1 
ATOM   11224 C  CB  . SER C  2  164 ? 68.520  48.977  29.480  1.00 66.17  ?  164 SER C CB  1 
ATOM   11225 O  OG  . SER C  2  164 ? 69.588  48.351  30.174  1.00 75.55  ?  164 SER C OG  1 
ATOM   11226 N  N   . LEU C  2  165 ? 70.316  47.589  26.898  1.00 66.51  ?  165 LEU C N   1 
ATOM   11227 C  CA  . LEU C  2  165 ? 71.531  47.779  26.112  1.00 62.75  ?  165 LEU C CA  1 
ATOM   11228 C  C   . LEU C  2  165 ? 71.149  47.947  24.628  1.00 65.45  ?  165 LEU C C   1 
ATOM   11229 O  O   . LEU C  2  165 ? 70.685  46.980  24.019  1.00 73.69  ?  165 LEU C O   1 
ATOM   11230 C  CB  . LEU C  2  165 ? 72.447  46.559  26.303  1.00 65.07  ?  165 LEU C CB  1 
ATOM   11231 C  CG  . LEU C  2  165 ? 73.761  46.539  25.535  1.00 62.00  ?  165 LEU C CG  1 
ATOM   11232 C  CD1 . LEU C  2  165 ? 74.622  47.745  25.862  1.00 62.03  ?  165 LEU C CD1 1 
ATOM   11233 C  CD2 . LEU C  2  165 ? 74.525  45.286  25.855  1.00 50.65  ?  165 LEU C CD2 1 
ATOM   11234 N  N   . PRO C  2  166 ? 71.311  49.145  24.020  1.00 63.88  ?  166 PRO C N   1 
ATOM   11235 C  CA  . PRO C  2  166 ? 70.925  49.297  22.605  1.00 62.67  ?  166 PRO C CA  1 
ATOM   11236 C  C   . PRO C  2  166 ? 71.579  48.306  21.650  1.00 64.27  ?  166 PRO C C   1 
ATOM   11237 O  O   . PRO C  2  166 ? 72.743  47.957  21.815  1.00 58.46  ?  166 PRO C O   1 
ATOM   11238 C  CB  . PRO C  2  166 ? 71.353  50.728  22.268  1.00 64.47  ?  166 PRO C CB  1 
ATOM   11239 C  CG  . PRO C  2  166 ? 71.413  51.429  23.553  1.00 70.26  ?  166 PRO C CG  1 
ATOM   11240 C  CD  . PRO C  2  166 ? 71.821  50.415  24.575  1.00 61.16  ?  166 PRO C CD  1 
ATOM   11241 N  N   . GLU C  2  167 ? 70.831  47.867  20.634  1.00 74.94  ?  167 GLU C N   1 
ATOM   11242 C  CA  . GLU C  2  167 ? 71.344  46.928  19.642  1.00 60.00  ?  167 GLU C CA  1 
ATOM   11243 C  C   . GLU C  2  167 ? 72.525  47.534  18.865  1.00 66.31  ?  167 GLU C C   1 
ATOM   11244 O  O   . GLU C  2  167 ? 73.391  46.791  18.397  1.00 73.76  ?  167 GLU C O   1 
ATOM   11245 C  CB  . GLU C  2  167 ? 70.223  46.512  18.677  1.00 63.90  ?  167 GLU C CB  1 
ATOM   11246 C  CG  . GLU C  2  167 ? 70.580  45.336  17.781  1.00 86.40  ?  167 GLU C CG  1 
ATOM   11247 C  CD  . GLU C  2  167 ? 70.839  44.035  18.514  1.00 103.34 ?  167 GLU C CD  1 
ATOM   11248 O  OE1 . GLU C  2  167 ? 70.116  43.758  19.500  1.00 90.72  ?  167 GLU C OE1 1 
ATOM   11249 O  OE2 . GLU C  2  167 ? 71.761  43.293  18.101  1.00 93.24  ?  167 GLU C OE2 1 
ATOM   11250 N  N   . LYS C  2  168 ? 72.568  48.872  18.729  1.00 72.13  ?  168 LYS C N   1 
ATOM   11251 C  CA  . LYS C  2  168 ? 73.661  49.547  18.027  1.00 55.49  ?  168 LYS C CA  1 
ATOM   11252 C  C   . LYS C  2  168 ? 74.973  49.364  18.802  1.00 61.65  ?  168 LYS C C   1 
ATOM   11253 O  O   . LYS C  2  168 ? 76.025  49.173  18.198  1.00 70.60  ?  168 LYS C O   1 
ATOM   11254 C  CB  . LYS C  2  168 ? 73.351  51.042  17.863  1.00 59.14  ?  168 LYS C CB  1 
ATOM   11255 C  CG  . LYS C  2  168 ? 72.156  51.321  16.960  1.00 65.07  ?  168 LYS C CG  1 
ATOM   11256 C  CD  . LYS C  2  168 ? 71.876  52.812  16.826  1.00 60.91  ?  168 LYS C CD  1 
ATOM   11257 C  CE  . LYS C  2  168 ? 71.254  53.155  15.498  1.00 63.38  ?  168 LYS C CE  1 
ATOM   11258 N  NZ  . LYS C  2  168 ? 70.793  54.562  15.462  1.00 95.55  ?  168 LYS C NZ  1 
ATOM   11259 N  N   . ARG C  2  169 ? 74.903  49.420  20.139  1.00 60.04  ?  169 ARG C N   1 
ATOM   11260 C  CA  . ARG C  2  169 ? 76.068  49.241  20.998  1.00 51.23  ?  169 ARG C CA  1 
ATOM   11261 C  C   . ARG C  2  169 ? 76.554  47.794  20.930  1.00 59.48  ?  169 ARG C C   1 
ATOM   11262 O  O   . ARG C  2  169 ? 77.761  47.562  20.913  1.00 72.29  ?  169 ARG C O   1 
ATOM   11263 C  CB  . ARG C  2  169 ? 75.707  49.616  22.448  1.00 61.94  ?  169 ARG C CB  1 
ATOM   11264 C  CG  . ARG C  2  169 ? 76.848  49.547  23.469  1.00 53.03  ?  169 ARG C CG  1 
ATOM   11265 C  CD  . ARG C  2  169 ? 78.163  50.206  23.066  1.00 57.61  ?  169 ARG C CD  1 
ATOM   11266 N  NE  . ARG C  2  169 ? 78.007  51.477  22.354  1.00 55.48  ?  169 ARG C NE  1 
ATOM   11267 C  CZ  . ARG C  2  169 ? 78.991  52.341  22.130  1.00 55.70  ?  169 ARG C CZ  1 
ATOM   11268 N  NH1 . ARG C  2  169 ? 80.217  52.093  22.573  1.00 52.63  ?  169 ARG C NH1 1 
ATOM   11269 N  NH2 . ARG C  2  169 ? 78.757  53.464  21.467  1.00 65.34  ?  169 ARG C NH2 1 
ATOM   11270 N  N   . LYS C  2  170 ? 75.625  46.823  20.877  1.00 64.64  ?  170 LYS C N   1 
ATOM   11271 C  CA  . LYS C  2  170 ? 75.986  45.403  20.801  1.00 57.94  ?  170 LYS C CA  1 
ATOM   11272 C  C   . LYS C  2  170 ? 76.690  45.107  19.477  1.00 65.46  ?  170 LYS C C   1 
ATOM   11273 O  O   . LYS C  2  170 ? 77.721  44.438  19.470  1.00 57.76  ?  170 LYS C O   1 
ATOM   11274 C  CB  . LYS C  2  170 ? 74.747  44.499  20.958  1.00 54.53  ?  170 LYS C CB  1 
ATOM   11275 C  CG  . LYS C  2  170 ? 73.984  44.720  22.265  1.00 70.14  ?  170 LYS C CG  1 
ATOM   11276 C  CD  . LYS C  2  170 ? 73.318  43.460  22.797  1.00 63.51  ?  170 LYS C CD  1 
ATOM   11277 C  CE  . LYS C  2  170 ? 72.218  42.939  21.905  1.00 73.77  ?  170 LYS C CE  1 
ATOM   11278 N  NZ  . LYS C  2  170 ? 71.059  42.444  22.695  1.00 81.85  ?  170 LYS C NZ  1 
ATOM   11279 N  N   . GLU C  2  171 ? 76.143  45.615  18.355  1.00 63.38  ?  171 GLU C N   1 
ATOM   11280 C  CA  . GLU C  2  171 ? 76.748  45.402  17.037  1.00 64.44  ?  171 GLU C CA  1 
ATOM   11281 C  C   . GLU C  2  171 ? 78.116  46.080  16.943  1.00 64.27  ?  171 GLU C C   1 
ATOM   11282 O  O   . GLU C  2  171 ? 79.008  45.557  16.279  1.00 66.11  ?  171 GLU C O   1 
ATOM   11283 C  CB  . GLU C  2  171 ? 75.828  45.917  15.906  1.00 63.94  ?  171 GLU C CB  1 
ATOM   11284 C  CG  . GLU C  2  171 ? 75.054  44.831  15.174  1.00 90.10  ?  171 GLU C CG  1 
ATOM   11285 C  CD  . GLU C  2  171 ? 75.907  43.832  14.414  1.00 93.88  ?  171 GLU C CD  1 
ATOM   11286 O  OE1 . GLU C  2  171 ? 76.807  44.264  13.656  1.00 88.62  ?  171 GLU C OE1 1 
ATOM   11287 O  OE2 . GLU C  2  171 ? 75.673  42.613  14.576  1.00 98.19  ?  171 GLU C OE2 1 
ATOM   11288 N  N   . LEU C  2  172 ? 78.291  47.234  17.605  1.00 63.21  ?  172 LEU C N   1 
ATOM   11289 C  CA  . LEU C  2  172 ? 79.568  47.935  17.587  1.00 55.98  ?  172 LEU C CA  1 
ATOM   11290 C  C   . LEU C  2  172 ? 80.622  47.078  18.278  1.00 53.45  ?  172 LEU C C   1 
ATOM   11291 O  O   . LEU C  2  172 ? 81.732  46.942  17.767  1.00 60.25  ?  172 LEU C O   1 
ATOM   11292 C  CB  . LEU C  2  172 ? 79.437  49.302  18.277  1.00 48.19  ?  172 LEU C CB  1 
ATOM   11293 C  CG  . LEU C  2  172 ? 80.713  50.144  18.395  1.00 51.99  ?  172 LEU C CG  1 
ATOM   11294 C  CD1 . LEU C  2  172 ? 81.388  50.349  17.036  1.00 71.42  ?  172 LEU C CD1 1 
ATOM   11295 C  CD2 . LEU C  2  172 ? 80.404  51.487  19.003  1.00 53.91  ?  172 LEU C CD2 1 
ATOM   11296 N  N   . TRP C  2  173 ? 80.269  46.474  19.424  1.00 53.90  ?  173 TRP C N   1 
ATOM   11297 C  CA  . TRP C  2  173 ? 81.187  45.607  20.159  1.00 57.83  ?  173 TRP C CA  1 
ATOM   11298 C  C   . TRP C  2  173 ? 81.535  44.394  19.310  1.00 54.94  ?  173 TRP C C   1 
ATOM   11299 O  O   . TRP C  2  173 ? 82.703  44.039  19.205  1.00 55.28  ?  173 TRP C O   1 
ATOM   11300 C  CB  . TRP C  2  173 ? 80.557  45.132  21.477  1.00 45.60  ?  173 TRP C CB  1 
ATOM   11301 C  CG  . TRP C  2  173 ? 80.316  46.196  22.508  1.00 55.99  ?  173 TRP C CG  1 
ATOM   11302 C  CD1 . TRP C  2  173 ? 80.858  47.448  22.555  1.00 54.84  ?  173 TRP C CD1 1 
ATOM   11303 C  CD2 . TRP C  2  173 ? 79.505  46.065  23.682  1.00 66.31  ?  173 TRP C CD2 1 
ATOM   11304 N  NE1 . TRP C  2  173 ? 80.415  48.113  23.675  1.00 52.02  ?  173 TRP C NE1 1 
ATOM   11305 C  CE2 . TRP C  2  173 ? 79.590  47.283  24.389  1.00 59.24  ?  173 TRP C CE2 1 
ATOM   11306 C  CE3 . TRP C  2  173 ? 78.703  45.039  24.198  1.00 53.12  ?  173 TRP C CE3 1 
ATOM   11307 C  CZ2 . TRP C  2  173 ? 78.899  47.501  25.576  1.00 62.19  ?  173 TRP C CZ2 1 
ATOM   11308 C  CZ3 . TRP C  2  173 ? 78.027  45.257  25.379  1.00 52.36  ?  173 TRP C CZ3 1 
ATOM   11309 C  CH2 . TRP C  2  173 ? 78.126  46.476  26.054  1.00 59.07  ?  173 TRP C CH2 1 
ATOM   11310 N  N   . ARG C  2  174 ? 80.525  43.768  18.687  1.00 56.79  ?  174 ARG C N   1 
ATOM   11311 C  CA  . ARG C  2  174 ? 80.728  42.596  17.842  1.00 56.47  ?  174 ARG C CA  1 
ATOM   11312 C  C   . ARG C  2  174 ? 81.731  42.881  16.728  1.00 57.78  ?  174 ARG C C   1 
ATOM   11313 O  O   . ARG C  2  174 ? 82.656  42.097  16.522  1.00 62.58  ?  174 ARG C O   1 
ATOM   11314 C  CB  . ARG C  2  174 ? 79.402  42.141  17.212  1.00 46.34  ?  174 ARG C CB  1 
ATOM   11315 C  CG  . ARG C  2  174 ? 78.544  41.251  18.098  1.00 50.99  ?  174 ARG C CG  1 
ATOM   11316 C  CD  . ARG C  2  174 ? 77.398  40.623  17.320  1.00 75.32  ?  174 ARG C CD  1 
ATOM   11317 N  NE  . ARG C  2  174 ? 76.100  41.183  17.700  1.00 84.77  ?  174 ARG C NE  1 
ATOM   11318 C  CZ  . ARG C  2  174 ? 75.352  40.754  18.712  1.00 104.59 ?  174 ARG C CZ  1 
ATOM   11319 N  NH1 . ARG C  2  174 ? 75.762  39.741  19.472  1.00 79.59  ?  174 ARG C NH1 1 
ATOM   11320 N  NH2 . ARG C  2  174 ? 74.186  41.334  18.974  1.00 93.37  ?  174 ARG C NH2 1 
ATOM   11321 N  N   . LYS C  2  175 ? 81.559  43.999  16.016  1.00 58.50  ?  175 LYS C N   1 
ATOM   11322 C  CA  . LYS C  2  175 ? 82.454  44.352  14.921  1.00 60.80  ?  175 LYS C CA  1 
ATOM   11323 C  C   . LYS C  2  175 ? 83.854  44.706  15.442  1.00 59.23  ?  175 LYS C C   1 
ATOM   11324 O  O   . LYS C  2  175 ? 84.846  44.378  14.791  1.00 74.35  ?  175 LYS C O   1 
ATOM   11325 C  CB  . LYS C  2  175 ? 81.853  45.489  14.080  1.00 52.20  ?  175 LYS C CB  1 
ATOM   11326 C  CG  . LYS C  2  175 ? 80.601  45.058  13.307  1.00 65.83  ?  175 LYS C CG  1 
ATOM   11327 C  CD  . LYS C  2  175 ? 79.937  46.206  12.527  1.00 105.25 ?  175 LYS C CD  1 
ATOM   11328 C  CE  . LYS C  2  175 ? 80.670  46.584  11.252  1.00 117.57 ?  175 LYS C CE  1 
ATOM   11329 N  NZ  . LYS C  2  175 ? 79.747  46.786  10.097  1.00 100.81 ?  175 LYS C NZ  1 
ATOM   11330 N  N   . LEU C  2  176 ? 83.942  45.341  16.618  1.00 56.58  ?  176 LEU C N   1 
ATOM   11331 C  CA  . LEU C  2  176 ? 85.232  45.696  17.207  1.00 45.85  ?  176 LEU C CA  1 
ATOM   11332 C  C   . LEU C  2  176 ? 85.956  44.470  17.828  1.00 57.32  ?  176 LEU C C   1 
ATOM   11333 O  O   . LEU C  2  176 ? 87.165  44.522  18.060  1.00 59.25  ?  176 LEU C O   1 
ATOM   11334 C  CB  . LEU C  2  176 ? 85.017  46.795  18.260  1.00 48.29  ?  176 LEU C CB  1 
ATOM   11335 C  CG  . LEU C  2  176 ? 86.264  47.444  18.861  1.00 52.62  ?  176 LEU C CG  1 
ATOM   11336 C  CD1 . LEU C  2  176 ? 87.033  48.251  17.828  1.00 51.15  ?  176 LEU C CD1 1 
ATOM   11337 C  CD2 . LEU C  2  176 ? 85.890  48.346  20.012  1.00 51.84  ?  176 LEU C CD2 1 
ATOM   11338 N  N   . GLY C  2  177 ? 85.214  43.389  18.075  1.00 60.64  ?  177 GLY C N   1 
ATOM   11339 C  CA  . GLY C  2  177 ? 85.744  42.158  18.647  1.00 46.00  ?  177 GLY C CA  1 
ATOM   11340 C  C   . GLY C  2  177 ? 85.834  42.178  20.158  1.00 48.54  ?  177 GLY C C   1 
ATOM   11341 O  O   . GLY C  2  177 ? 86.662  41.473  20.734  1.00 62.41  ?  177 GLY C O   1 
ATOM   11342 N  N   . VAL C  2  178 ? 84.981  42.980  20.815  1.00 55.10  ?  178 VAL C N   1 
ATOM   11343 C  CA  . VAL C  2  178 ? 84.977  43.094  22.275  1.00 47.93  ?  178 VAL C CA  1 
ATOM   11344 C  C   . VAL C  2  178 ? 83.626  42.699  22.887  1.00 57.17  ?  178 VAL C C   1 
ATOM   11345 O  O   . VAL C  2  178 ? 83.360  43.057  24.033  1.00 49.58  ?  178 VAL C O   1 
ATOM   11346 C  CB  . VAL C  2  178 ? 85.409  44.507  22.743  1.00 54.26  ?  178 VAL C CB  1 
ATOM   11347 C  CG1 . VAL C  2  178 ? 86.789  44.863  22.202  1.00 58.07  ?  178 VAL C CG1 1 
ATOM   11348 C  CG2 . VAL C  2  178 ? 84.382  45.570  22.352  1.00 46.65  ?  178 VAL C CG2 1 
ATOM   11349 N  N   . TYR C  2  179 ? 82.806  41.951  22.145  1.00 59.53  ?  179 TYR C N   1 
ATOM   11350 C  CA  . TYR C  2  179 ? 81.532  41.457  22.731  1.00 44.20  ?  179 TYR C CA  1 
ATOM   11351 C  C   . TYR C  2  179 ? 81.872  40.553  23.918  1.00 50.84  ?  179 TYR C C   1 
ATOM   11352 O  O   . TYR C  2  179 ? 82.759  39.691  23.777  1.00 58.73  ?  179 TYR C O   1 
ATOM   11353 C  CB  . TYR C  2  179 ? 80.683  40.741  21.680  1.00 59.33  ?  179 TYR C CB  1 
ATOM   11354 C  CG  . TYR C  2  179 ? 79.209  40.702  21.995  1.00 45.87  ?  179 TYR C CG  1 
ATOM   11355 C  CD1 . TYR C  2  179 ? 78.665  39.668  22.737  1.00 50.69  ?  179 TYR C CD1 1 
ATOM   11356 C  CD2 . TYR C  2  179 ? 78.358  41.703  21.559  1.00 65.61  ?  179 TYR C CD2 1 
ATOM   11357 C  CE1 . TYR C  2  179 ? 77.314  39.625  23.035  1.00 47.18  ?  179 TYR C CE1 1 
ATOM   11358 C  CE2 . TYR C  2  179 ? 77.004  41.675  21.846  1.00 81.44  ?  179 TYR C CE2 1 
ATOM   11359 C  CZ  . TYR C  2  179 ? 76.479  40.632  22.587  1.00 61.64  ?  179 TYR C CZ  1 
ATOM   11360 O  OH  . TYR C  2  179 ? 75.137  40.595  22.879  1.00 77.55  ?  179 TYR C OH  1 
ATOM   11361 N  N   . PRO C  2  180 ? 81.208  40.704  25.084  1.00 49.72  ?  180 PRO C N   1 
ATOM   11362 C  CA  . PRO C  2  180 ? 81.577  39.935  26.283  1.00 49.91  ?  180 PRO C CA  1 
ATOM   11363 C  C   . PRO C  2  180 ? 81.236  38.437  26.243  1.00 57.08  ?  180 PRO C C   1 
ATOM   11364 O  O   . PRO C  2  180 ? 80.316  38.071  25.538  1.00 62.59  ?  180 PRO C O   1 
ATOM   11365 C  CB  . PRO C  2  180 ? 80.746  40.619  27.380  1.00 48.05  ?  180 PRO C CB  1 
ATOM   11366 C  CG  . PRO C  2  180 ? 79.544  41.170  26.649  1.00 46.34  ?  180 PRO C CG  1 
ATOM   11367 C  CD  . PRO C  2  180 ? 80.083  41.613  25.307  1.00 41.25  ?  180 PRO C CD  1 
ATOM   11368 N  N   . ARG C  2  181 ? 81.997  37.619  26.977  1.00 58.12  ?  181 ARG C N   1 
ATOM   11369 C  CA  . ARG C  2  181 ? 81.710  36.162  27.079  1.00 52.06  ?  181 ARG C CA  1 
ATOM   11370 C  C   . ARG C  2  181 ? 81.401  35.878  28.552  1.00 55.99  ?  181 ARG C C   1 
ATOM   11371 O  O   . ARG C  2  181 ? 80.997  36.832  29.243  1.00 64.31  ?  181 ARG C O   1 
ATOM   11372 C  CB  . ARG C  2  181 ? 82.899  35.350  26.554  1.00 56.52  ?  181 ARG C CB  1 
ATOM   11373 C  CG  . ARG C  2  181 ? 83.261  35.643  25.103  1.00 65.70  ?  181 ARG C CG  1 
ATOM   11374 C  CD  . ARG C  2  181 ? 84.613  35.097  24.675  1.00 54.73  ?  181 ARG C CD  1 
ATOM   11375 N  NE  . ARG C  2  181 ? 85.681  36.059  24.904  1.00 65.55  ?  181 ARG C NE  1 
ATOM   11376 C  CZ  . ARG C  2  181 ? 86.971  35.753  24.962  1.00 59.20  ?  181 ARG C CZ  1 
ATOM   11377 N  NH1 . ARG C  2  181 ? 87.373  34.528  24.674  1.00 51.12  ?  181 ARG C NH1 1 
ATOM   11378 N  NH2 . ARG C  2  181 ? 87.855  36.673  25.306  1.00 61.83  ?  181 ARG C NH2 1 
ATOM   11379 N  N   . ALA C  2  182 ? 81.581  34.642  29.033  1.00 56.65  ?  182 ALA C N   1 
ATOM   11380 C  CA  . ALA C  2  182 ? 81.365  34.430  30.466  1.00 53.03  ?  182 ALA C CA  1 
ATOM   11381 C  C   . ALA C  2  182 ? 82.243  35.318  31.354  1.00 54.69  ?  182 ALA C C   1 
ATOM   11382 O  O   . ALA C  2  182 ? 83.349  35.683  30.959  1.00 53.50  ?  182 ALA C O   1 
ATOM   11383 C  CB  . ALA C  2  182 ? 81.547  32.968  30.815  1.00 64.75  ?  182 ALA C CB  1 
ATOM   11384 N  N   . VAL C  2  183 ? 81.746  35.677  32.541  1.00 56.54  ?  183 VAL C N   1 
ATOM   11385 C  CA  . VAL C  2  183 ? 82.472  36.577  33.443  1.00 56.10  ?  183 VAL C CA  1 
ATOM   11386 C  C   . VAL C  2  183 ? 83.876  36.048  33.807  1.00 58.76  ?  183 VAL C C   1 
ATOM   11387 O  O   . VAL C  2  183 ? 84.878  36.704  33.517  1.00 60.22  ?  183 VAL C O   1 
ATOM   11388 C  CB  . VAL C  2  183 ? 81.670  36.951  34.723  1.00 59.20  ?  183 VAL C CB  1 
ATOM   11389 C  CG1 . VAL C  2  183 ? 82.395  38.041  35.505  1.00 52.54  ?  183 VAL C CG1 1 
ATOM   11390 C  CG2 . VAL C  2  183 ? 80.239  37.387  34.402  1.00 56.23  ?  183 VAL C CG2 1 
ATOM   11391 N  N   . ASP C  2  184 ? 83.953  34.874  34.447  1.00 60.10  ?  184 ASP C N   1 
ATOM   11392 C  CA  . ASP C  2  184 ? 85.235  34.304  34.848  1.00 56.55  ?  184 ASP C CA  1 
ATOM   11393 C  C   . ASP C  2  184 ? 86.121  34.014  33.631  1.00 60.00  ?  184 ASP C C   1 
ATOM   11394 O  O   . ASP C  2  184 ? 87.345  34.079  33.741  1.00 58.64  ?  184 ASP C O   1 
ATOM   11395 C  CB  . ASP C  2  184 ? 85.031  33.015  35.669  1.00 62.58  ?  184 ASP C CB  1 
ATOM   11396 C  CG  . ASP C  2  184 ? 84.170  33.163  36.904  1.00 68.69  ?  184 ASP C CG  1 
ATOM   11397 O  OD1 . ASP C  2  184 ? 84.156  34.269  37.490  1.00 67.73  ?  184 ASP C OD1 1 
ATOM   11398 O  OD2 . ASP C  2  184 ? 83.514  32.170  37.291  1.00 65.12  ?  184 ASP C OD2 1 
ATOM   11399 N  N   . ARG C  2  185 ? 85.499  33.710  32.491  1.00 58.73  ?  185 ARG C N   1 
ATOM   11400 C  CA  . ARG C  2  185 ? 86.275  33.384  31.266  1.00 57.75  ?  185 ARG C CA  1 
ATOM   11401 C  C   . ARG C  2  185 ? 87.111  34.600  30.865  1.00 55.73  ?  185 ARG C C   1 
ATOM   11402 O  O   . ARG C  2  185 ? 88.307  34.422  30.578  1.00 62.49  ?  185 ARG C O   1 
ATOM   11403 C  CB  . ARG C  2  185 ? 85.341  32.986  30.122  1.00 49.43  ?  185 ARG C CB  1 
ATOM   11404 C  CG  . ARG C  2  185 ? 86.031  32.249  28.984  1.00 48.18  ?  185 ARG C CG  1 
ATOM   11405 C  CD  . ARG C  2  185 ? 86.395  33.172  27.837  1.00 52.63  ?  185 ARG C CD  1 
ATOM   11406 N  NE  . ARG C  2  185 ? 87.421  32.603  26.976  1.00 47.39  ?  185 ARG C NE  1 
ATOM   11407 C  CZ  . ARG C  2  185 ? 88.686  32.419  27.336  1.00 54.44  ?  185 ARG C CZ  1 
ATOM   11408 N  NH1 . ARG C  2  185 ? 89.148  32.978  28.439  1.00 63.46  ?  185 ARG C NH1 1 
ATOM   11409 N  NH2 . ARG C  2  185 ? 89.485  31.676  26.589  1.00 60.71  ?  185 ARG C NH2 1 
ATOM   11410 N  N   . GLU C  2  186 ? 86.501  35.788  30.849  1.00 56.38  ?  186 GLU C N   1 
ATOM   11411 C  CA  . GLU C  2  186 ? 87.226  36.978  30.399  1.00 62.22  ?  186 GLU C CA  1 
ATOM   11412 C  C   . GLU C  2  186 ? 88.341  37.356  31.363  1.00 58.78  ?  186 GLU C C   1 
ATOM   11413 O  O   . GLU C  2  186 ? 89.363  37.882  30.928  1.00 67.67  ?  186 GLU C O   1 
ATOM   11414 C  CB  . GLU C  2  186 ? 86.296  38.174  30.195  1.00 45.11  ?  186 GLU C CB  1 
ATOM   11415 C  CG  . GLU C  2  186 ? 85.327  38.020  29.041  1.00 50.85  ?  186 GLU C CG  1 
ATOM   11416 C  CD  . GLU C  2  186 ? 85.937  37.961  27.655  1.00 65.49  ?  186 GLU C CD  1 
ATOM   11417 O  OE1 . GLU C  2  186 ? 87.183  38.011  27.530  1.00 65.97  ?  186 GLU C OE1 1 
ATOM   11418 O  OE2 . GLU C  2  186 ? 85.154  37.869  26.685  1.00 75.51  ?  186 GLU C OE2 1 
ATOM   11419 N  N   . ILE C  2  187 ? 88.167  37.084  32.664  1.00 55.78  ?  187 ILE C N   1 
ATOM   11420 C  CA  . ILE C  2  187 ? 89.204  37.390  33.648  1.00 58.55  ?  187 ILE C CA  1 
ATOM   11421 C  C   . ILE C  2  187 ? 90.414  36.501  33.343  1.00 54.17  ?  187 ILE C C   1 
ATOM   11422 O  O   . ILE C  2  187 ? 91.542  36.986  33.322  1.00 61.54  ?  187 ILE C O   1 
ATOM   11423 C  CB  . ILE C  2  187 ? 88.694  37.179  35.095  1.00 48.00  ?  187 ILE C CB  1 
ATOM   11424 C  CG1 . ILE C  2  187 ? 87.496  38.102  35.398  1.00 41.34  ?  187 ILE C CG1 1 
ATOM   11425 C  CG2 . ILE C  2  187 ? 89.824  37.420  36.098  1.00 45.62  ?  187 ILE C CG2 1 
ATOM   11426 C  CD1 . ILE C  2  187 ? 86.765  37.735  36.613  1.00 55.95  ?  187 ILE C CD1 1 
ATOM   11427 N  N   . ALA C  2  188 ? 90.170  35.209  33.073  1.00 52.43  ?  188 ALA C N   1 
ATOM   11428 C  CA  . ALA C  2  188 ? 91.233  34.272  32.743  1.00 45.13  ?  188 ALA C CA  1 
ATOM   11429 C  C   . ALA C  2  188 ? 91.905  34.695  31.444  1.00 50.16  ?  188 ALA C C   1 
ATOM   11430 O  O   . ALA C  2  188 ? 93.126  34.662  31.357  1.00 63.08  ?  188 ALA C O   1 
ATOM   11431 C  CB  . ALA C  2  188 ? 90.667  32.867  32.604  1.00 46.95  ?  188 ALA C CB  1 
ATOM   11432 N  N   . ALA C  2  189 ? 91.120  35.111  30.442  1.00 49.30  ?  189 ALA C N   1 
ATOM   11433 C  CA  . ALA C  2  189 ? 91.659  35.541  29.155  1.00 44.52  ?  189 ALA C CA  1 
ATOM   11434 C  C   . ALA C  2  189 ? 92.669  36.682  29.304  1.00 48.24  ?  189 ALA C C   1 
ATOM   11435 O  O   . ALA C  2  189 ? 93.701  36.667  28.640  1.00 57.78  ?  189 ALA C O   1 
ATOM   11436 C  CB  . ALA C  2  189 ? 90.526  35.972  28.242  1.00 52.64  ?  189 ALA C CB  1 
ATOM   11437 N  N   . VAL C  2  190 ? 92.380  37.667  30.163  1.00 56.59  ?  190 VAL C N   1 
ATOM   11438 C  CA  . VAL C  2  190 ? 93.282  38.802  30.372  1.00 48.23  ?  190 VAL C CA  1 
ATOM   11439 C  C   . VAL C  2  190 ? 94.521  38.337  31.125  1.00 48.61  ?  190 VAL C C   1 
ATOM   11440 O  O   . VAL C  2  190 ? 95.635  38.701  30.762  1.00 54.04  ?  190 VAL C O   1 
ATOM   11441 C  CB  . VAL C  2  190 ? 92.579  39.966  31.114  1.00 40.50  ?  190 VAL C CB  1 
ATOM   11442 C  CG1 . VAL C  2  190 ? 93.582  41.046  31.513  1.00 44.23  ?  190 VAL C CG1 1 
ATOM   11443 C  CG2 . VAL C  2  190 ? 91.462  40.560  30.262  1.00 41.58  ?  190 VAL C CG2 1 
ATOM   11444 N  N   . MET C  2  191 ? 94.333  37.531  32.169  1.00 49.36  ?  191 MET C N   1 
ATOM   11445 C  CA  . MET C  2  191 ? 95.446  37.010  32.961  1.00 55.35  ?  191 MET C CA  1 
ATOM   11446 C  C   . MET C  2  191 ? 96.392  36.164  32.099  1.00 56.04  ?  191 MET C C   1 
ATOM   11447 O  O   . MET C  2  191 ? 97.606  36.211  32.286  1.00 64.15  ?  191 MET C O   1 
ATOM   11448 C  CB  . MET C  2  191 ? 94.913  36.172  34.130  1.00 51.17  ?  191 MET C CB  1 
ATOM   11449 C  CG  . MET C  2  191 ? 94.247  36.993  35.204  1.00 48.95  ?  191 MET C CG  1 
ATOM   11450 S  SD  . MET C  2  191 ? 95.449  38.022  36.066  1.00 53.26  ?  191 MET C SD  1 
ATOM   11451 C  CE  . MET C  2  191 ? 94.841  39.589  35.694  1.00 71.02  ?  191 MET C CE  1 
ATOM   11452 N  N   . HIS C  2  192 ? 95.842  35.402  31.156  1.00 53.13  ?  192 HIS C N   1 
ATOM   11453 C  CA  . HIS C  2  192 ? 96.642  34.567  30.273  1.00 58.05  ?  192 HIS C CA  1 
ATOM   11454 C  C   . HIS C  2  192 ? 97.469  35.434  29.318  1.00 53.02  ?  192 HIS C C   1 
ATOM   11455 O  O   . HIS C  2  192 ? 98.675  35.236  29.200  1.00 58.22  ?  192 HIS C O   1 
ATOM   11456 C  CB  . HIS C  2  192 ? 95.730  33.594  29.494  1.00 52.49  ?  192 HIS C CB  1 
ATOM   11457 C  CG  . HIS C  2  192 ? 96.395  32.905  28.342  1.00 44.81  ?  192 HIS C CG  1 
ATOM   11458 N  ND1 . HIS C  2  192 ? 95.701  32.605  27.191  1.00 43.57  ?  192 HIS C ND1 1 
ATOM   11459 C  CD2 . HIS C  2  192 ? 97.670  32.474  28.203  1.00 52.86  ?  192 HIS C CD2 1 
ATOM   11460 C  CE1 . HIS C  2  192 ? 96.563  32.001  26.391  1.00 52.94  ?  192 HIS C CE1 1 
ATOM   11461 N  NE2 . HIS C  2  192 ? 97.763  31.905  26.959  1.00 56.66  ?  192 HIS C NE2 1 
ATOM   11462 N  N   . SER C  2  193 ? 96.831  36.389  28.641  1.00 50.53  ?  193 SER C N   1 
ATOM   11463 C  CA  . SER C  2  193 ? 97.517  37.250  27.687  1.00 36.39  ?  193 SER C CA  1 
ATOM   11464 C  C   . SER C  2  193 ? 98.518  38.204  28.334  1.00 42.78  ?  193 SER C C   1 
ATOM   11465 O  O   . SER C  2  193 ? 99.466  38.620  27.667  1.00 61.52  ?  193 SER C O   1 
ATOM   11466 C  CB  . SER C  2  193 ? 96.501  38.000  26.843  1.00 46.78  ?  193 SER C CB  1 
ATOM   11467 O  OG  . SER C  2  193 ? 95.718  37.061  26.125  1.00 55.15  ?  193 SER C OG  1 
ATOM   11468 N  N   . THR C  2  194 ? 98.340  38.538  29.623  1.00 43.63  ?  194 THR C N   1 
ATOM   11469 C  CA  . THR C  2  194 ? 99.304  39.404  30.308  1.00 44.84  ?  194 THR C CA  1 
ATOM   11470 C  C   . THR C  2  194 ? 100.542 38.588  30.742  1.00 51.08  ?  194 THR C C   1 
ATOM   11471 O  O   . THR C  2  194 ? 101.571 39.180  31.055  1.00 57.21  ?  194 THR C O   1 
ATOM   11472 C  CB  . THR C  2  194 ? 98.665  40.171  31.480  1.00 51.36  ?  194 THR C CB  1 
ATOM   11473 O  OG1 . THR C  2  194 ? 97.999  39.259  32.352  1.00 60.74  ?  194 THR C OG1 1 
ATOM   11474 C  CG2 . THR C  2  194 ? 97.709  41.264  31.020  1.00 48.46  ?  194 THR C CG2 1 
ATOM   11475 N  N   . HIS C  2  195 ? 100.460 37.238  30.737  1.00 46.31  ?  195 HIS C N   1 
ATOM   11476 C  CA  . HIS C  2  195 ? 101.580 36.363  31.097  1.00 50.45  ?  195 HIS C CA  1 
ATOM   11477 C  C   . HIS C  2  195 ? 102.763 36.634  30.175  1.00 47.19  ?  195 HIS C C   1 
ATOM   11478 O  O   . HIS C  2  195 ? 102.563 37.047  29.034  1.00 53.00  ?  195 HIS C O   1 
ATOM   11479 C  CB  . HIS C  2  195 ? 101.154 34.886  30.958  1.00 46.59  ?  195 HIS C CB  1 
ATOM   11480 C  CG  . HIS C  2  195 ? 102.215 33.892  31.330  1.00 49.37  ?  195 HIS C CG  1 
ATOM   11481 N  ND1 . HIS C  2  195 ? 103.190 33.503  30.431  1.00 51.47  ?  195 HIS C ND1 1 
ATOM   11482 C  CD2 . HIS C  2  195 ? 102.394 33.211  32.484  1.00 58.96  ?  195 HIS C CD2 1 
ATOM   11483 C  CE1 . HIS C  2  195 ? 103.941 32.619  31.068  1.00 44.60  ?  195 HIS C CE1 1 
ATOM   11484 N  NE2 . HIS C  2  195 ? 103.503 32.415  32.308  1.00 58.58  ?  195 HIS C NE2 1 
ATOM   11485 N  N   . ILE C  2  196 ? 103.972 36.322  30.645  1.00 42.56  ?  196 ILE C N   1 
ATOM   11486 C  CA  . ILE C  2  196 ? 105.205 36.574  29.843  1.00 44.11  ?  196 ILE C CA  1 
ATOM   11487 C  C   . ILE C  2  196 ? 105.099 35.888  28.480  1.00 45.19  ?  196 ILE C C   1 
ATOM   11488 O  O   . ILE C  2  196 ? 104.553 34.771  28.418  1.00 65.25  ?  196 ILE C O   1 
ATOM   11489 C  CB  . ILE C  2  196 ? 106.468 36.118  30.603  1.00 37.99  ?  196 ILE C CB  1 
ATOM   11490 C  CG1 . ILE C  2  196 ? 107.749 36.599  29.915  1.00 44.64  ?  196 ILE C CG1 1 
ATOM   11491 C  CG2 . ILE C  2  196 ? 106.470 34.611  30.804  1.00 54.72  ?  196 ILE C CG2 1 
ATOM   11492 C  CD1 . ILE C  2  196 ? 108.351 35.596  28.959  1.00 33.32  ?  196 ILE C CD1 1 
ATOM   11493 N  N   . GLY C  2  197 ? 105.599 36.541  27.434  1.00 38.83  ?  197 GLY C N   1 
ATOM   11494 C  CA  . GLY C  2  197 ? 105.622 35.971  26.101  1.00 52.21  ?  197 GLY C CA  1 
ATOM   11495 C  C   . GLY C  2  197 ? 104.277 35.749  25.452  1.00 53.60  ?  197 GLY C C   1 
ATOM   11496 O  O   . GLY C  2  197 ? 104.153 34.835  24.636  1.00 59.99  ?  197 GLY C O   1 
ATOM   11497 N  N   . CYS C  2  198 ? 103.265 36.563  25.783  1.00 56.60  ?  198 CYS C N   1 
ATOM   11498 C  CA  . CYS C  2  198 ? 101.956 36.426  25.148  1.00 54.49  ?  198 CYS C CA  1 
ATOM   11499 C  C   . CYS C  2  198 ? 101.683 37.699  24.319  1.00 64.66  ?  198 CYS C C   1 
ATOM   11500 O  O   . CYS C  2  198 ? 102.392 37.924  23.334  1.00 58.21  ?  198 CYS C O   1 
ATOM   11501 C  CB  . CYS C  2  198 ? 100.856 36.143  26.170  1.00 48.38  ?  198 CYS C CB  1 
ATOM   11502 S  SG  . CYS C  2  198 ? 100.846 34.448  26.808  1.00 82.24  ?  198 CYS C SG  1 
ATOM   11503 N  N   . ASN C  2  199 ? 100.706 38.539  24.706  1.00 56.62  ?  199 ASN C N   1 
ATOM   11504 C  CA  . ASN C  2  199 ? 100.395 39.743  23.953  1.00 47.49  ?  199 ASN C CA  1 
ATOM   11505 C  C   . ASN C  2  199 ? 101.475 40.796  24.138  1.00 61.82  ?  199 ASN C C   1 
ATOM   11506 O  O   . ASN C  2  199 ? 101.950 41.014  25.250  1.00 66.49  ?  199 ASN C O   1 
ATOM   11507 C  CB  . ASN C  2  199 ? 99.043  40.299  24.390  1.00 53.49  ?  199 ASN C CB  1 
ATOM   11508 C  CG  . ASN C  2  199 ? 98.457  41.289  23.421  1.00 62.11  ?  199 ASN C CG  1 
ATOM   11509 O  OD1 . ASN C  2  199 ? 98.774  42.481  23.458  1.00 67.63  ?  199 ASN C OD1 1 
ATOM   11510 N  ND2 . ASN C  2  199 ? 97.590  40.824  22.529  1.00 61.05  ?  199 ASN C ND2 1 
ATOM   11511 N  N   . ALA C  2  200 ? 101.868 41.436  23.034  1.00 66.58  ?  200 ALA C N   1 
ATOM   11512 C  CA  . ALA C  2  200 ? 102.862 42.502  23.014  1.00 49.07  ?  200 ALA C CA  1 
ATOM   11513 C  C   . ALA C  2  200 ? 102.398 43.562  22.013  1.00 55.86  ?  200 ALA C C   1 
ATOM   11514 O  O   . ALA C  2  200 ? 103.160 43.997  21.155  1.00 55.26  ?  200 ALA C O   1 
ATOM   11515 C  CB  . ALA C  2  200 ? 104.221 41.956  22.619  1.00 61.21  ?  200 ALA C CB  1 
ATOM   11516 N  N   . ASP C  2  201 ? 101.129 43.965  22.132  1.00 56.21  ?  201 ASP C N   1 
ATOM   11517 C  CA  . ASP C  2  201 ? 100.514 44.974  21.280  1.00 51.85  ?  201 ASP C CA  1 
ATOM   11518 C  C   . ASP C  2  201 ? 99.575  45.788  22.169  1.00 61.55  ?  201 ASP C C   1 
ATOM   11519 O  O   . ASP C  2  201 ? 98.635  45.226  22.731  1.00 62.74  ?  201 ASP C O   1 
ATOM   11520 C  CB  . ASP C  2  201 ? 99.753  44.308  20.122  1.00 48.13  ?  201 ASP C CB  1 
ATOM   11521 C  CG  . ASP C  2  201 ? 99.125  45.277  19.137  1.00 63.55  ?  201 ASP C CG  1 
ATOM   11522 O  OD1 . ASP C  2  201 ? 98.659  46.353  19.574  1.00 66.41  ?  201 ASP C OD1 1 
ATOM   11523 O  OD2 . ASP C  2  201 ? 99.099  44.961  17.931  1.00 75.94  ?  201 ASP C OD2 1 
ATOM   11524 N  N   . ALA C  2  202 ? 99.840  47.096  22.325  1.00 58.53  ?  202 ALA C N   1 
ATOM   11525 C  CA  . ALA C  2  202 ? 99.025  47.957  23.180  1.00 56.31  ?  202 ALA C CA  1 
ATOM   11526 C  C   . ALA C  2  202 ? 97.535  47.989  22.784  1.00 58.49  ?  202 ALA C C   1 
ATOM   11527 O  O   . ALA C  2  202 ? 96.679  47.825  23.654  1.00 64.42  ?  202 ALA C O   1 
ATOM   11528 C  CB  . ALA C  2  202 ? 99.596  49.366  23.197  1.00 54.12  ?  202 ALA C CB  1 
ATOM   11529 N  N   . GLU C  2  203 ? 97.219  48.183  21.493  1.00 50.88  ?  203 GLU C N   1 
ATOM   11530 C  CA  . GLU C  2  203 ? 95.826  48.243  21.047  1.00 47.35  ?  203 GLU C CA  1 
ATOM   11531 C  C   . GLU C  2  203 ? 95.070  46.952  21.345  1.00 56.41  ?  203 GLU C C   1 
ATOM   11532 O  O   . GLU C  2  203 ? 93.964  46.999  21.878  1.00 62.76  ?  203 GLU C O   1 
ATOM   11533 C  CB  . GLU C  2  203 ? 95.743  48.542  19.544  1.00 51.66  ?  203 GLU C CB  1 
ATOM   11534 C  CG  . GLU C  2  203 ? 96.138  49.959  19.180  1.00 59.05  ?  203 GLU C CG  1 
ATOM   11535 C  CD  . GLU C  2  203 ? 95.717  50.395  17.793  1.00 70.54  ?  203 GLU C CD  1 
ATOM   11536 O  OE1 . GLU C  2  203 ? 94.841  49.729  17.193  1.00 66.40  ?  203 GLU C OE1 1 
ATOM   11537 O  OE2 . GLU C  2  203 ? 96.264  51.412  17.307  1.00 71.64  ?  203 GLU C OE2 1 
ATOM   11538 N  N   . ALA C  2  204 ? 95.655  45.801  20.999  1.00 50.27  ?  204 ALA C N   1 
ATOM   11539 C  CA  . ALA C  2  204 ? 95.014  44.512  21.237  1.00 51.08  ?  204 ALA C CA  1 
ATOM   11540 C  C   . ALA C  2  204 ? 94.820  44.295  22.735  1.00 51.41  ?  204 ALA C C   1 
ATOM   11541 O  O   . ALA C  2  204 ? 93.763  43.825  23.142  1.00 48.76  ?  204 ALA C O   1 
ATOM   11542 C  CB  . ALA C  2  204 ? 95.830  43.408  20.596  1.00 70.20  ?  204 ALA C CB  1 
ATOM   11543 N  N   . MET C  2  205 ? 95.826  44.642  23.537  1.00 46.05  ?  205 MET C N   1 
ATOM   11544 C  CA  . MET C  2  205 ? 95.725  44.442  25.006  1.00 38.95  ?  205 MET C CA  1 
ATOM   11545 C  C   . MET C  2  205 ? 94.604  45.300  25.594  1.00 51.29  ?  205 MET C C   1 
ATOM   11546 O  O   . MET C  2  205 ? 93.802  44.764  26.378  1.00 61.50  ?  205 MET C O   1 
ATOM   11547 C  CB  . MET C  2  205 ? 97.047  44.793  25.694  1.00 49.44  ?  205 MET C CB  1 
ATOM   11548 C  CG  . MET C  2  205 ? 97.108  44.350  27.141  1.00 48.87  ?  205 MET C CG  1 
ATOM   11549 S  SD  . MET C  2  205 ? 97.542  42.602  27.309  1.00 61.72  ?  205 MET C SD  1 
ATOM   11550 C  CE  . MET C  2  205 ? 95.940  41.897  27.690  1.00 43.52  ?  205 MET C CE  1 
ATOM   11551 N  N   . ILE C  2  206 ? 94.552  46.579  25.218  1.00 57.12  ?  206 ILE C N   1 
ATOM   11552 C  CA  . ILE C  2  206 ? 93.533  47.480  25.752  1.00 49.28  ?  206 ILE C CA  1 
ATOM   11553 C  C   . ILE C  2  206 ? 92.129  47.015  25.313  1.00 55.74  ?  206 ILE C C   1 
ATOM   11554 O  O   . ILE C  2  206 ? 91.175  47.160  26.075  1.00 62.73  ?  206 ILE C O   1 
ATOM   11555 C  CB  . ILE C  2  206 ? 93.845  48.954  25.363  1.00 39.29  ?  206 ILE C CB  1 
ATOM   11556 C  CG1 . ILE C  2  206 ? 95.209  49.434  25.935  1.00 45.36  ?  206 ILE C CG1 1 
ATOM   11557 C  CG2 . ILE C  2  206 ? 92.726  49.882  25.787  1.00 41.10  ?  206 ILE C CG2 1 
ATOM   11558 C  CD1 . ILE C  2  206 ? 95.323  49.589  27.476  1.00 50.92  ?  206 ILE C CD1 1 
ATOM   11559 N  N   . LYS C  2  207 ? 92.006  46.425  24.113  1.00 50.42  ?  207 LYS C N   1 
ATOM   11560 C  CA  . LYS C  2  207 ? 90.723  45.906  23.638  1.00 50.27  ?  207 LYS C CA  1 
ATOM   11561 C  C   . LYS C  2  207 ? 90.308  44.688  24.484  1.00 50.86  ?  207 LYS C C   1 
ATOM   11562 O  O   . LYS C  2  207 ? 89.122  44.481  24.725  1.00 63.61  ?  207 LYS C O   1 
ATOM   11563 C  CB  . LYS C  2  207 ? 90.814  45.506  22.158  1.00 43.72  ?  207 LYS C CB  1 
ATOM   11564 C  CG  . LYS C  2  207 ? 90.860  46.687  21.195  1.00 47.40  ?  207 LYS C CG  1 
ATOM   11565 C  CD  . LYS C  2  207 ? 90.509  46.266  19.775  1.00 45.21  ?  207 LYS C CD  1 
ATOM   11566 C  CE  . LYS C  2  207 ? 90.594  47.394  18.775  1.00 64.23  ?  207 LYS C CE  1 
ATOM   11567 N  NZ  . LYS C  2  207 ? 91.830  47.329  17.946  1.00 87.58  ?  207 LYS C NZ  1 
ATOM   11568 N  N   . MET C  2  208 ? 91.278  43.889  24.942  1.00 47.58  ?  208 MET C N   1 
ATOM   11569 C  CA  . MET C  2  208 ? 90.988  42.718  25.767  1.00 51.50  ?  208 MET C CA  1 
ATOM   11570 C  C   . MET C  2  208 ? 90.434  43.148  27.124  1.00 54.14  ?  208 MET C C   1 
ATOM   11571 O  O   . MET C  2  208 ? 89.571  42.458  27.671  1.00 64.80  ?  208 MET C O   1 
ATOM   11572 C  CB  . MET C  2  208 ? 92.249  41.860  25.953  1.00 51.92  ?  208 MET C CB  1 
ATOM   11573 C  CG  . MET C  2  208 ? 92.686  41.166  24.686  1.00 51.71  ?  208 MET C CG  1 
ATOM   11574 S  SD  . MET C  2  208 ? 93.974  39.931  24.936  1.00 62.07  ?  208 MET C SD  1 
ATOM   11575 C  CE  . MET C  2  208 ? 92.973  38.553  25.509  1.00 46.52  ?  208 MET C CE  1 
ATOM   11576 N  N   . SER C  2  209 ? 90.939  44.274  27.640  1.00 42.71  ?  209 SER C N   1 
ATOM   11577 C  CA  . SER C  2  209 ? 90.445  44.819  28.929  1.00 47.34  ?  209 SER C CA  1 
ATOM   11578 C  C   . SER C  2  209 ? 89.012  45.320  28.734  1.00 53.89  ?  209 SER C C   1 
ATOM   11579 O  O   . SER C  2  209 ? 88.192  45.124  29.647  1.00 60.75  ?  209 SER C O   1 
ATOM   11580 C  CB  . SER C  2  209 ? 91.343  45.926  29.439  1.00 46.72  ?  209 SER C CB  1 
ATOM   11581 O  OG  . SER C  2  209 ? 92.722  45.679  29.181  1.00 65.90  ?  209 SER C OG  1 
ATOM   11582 N  N   . MET C  2  210 ? 88.726  45.932  27.583  1.00 44.84  ?  210 MET C N   1 
ATOM   11583 C  CA  . MET C  2  210 ? 87.402  46.478  27.308  1.00 44.59  ?  210 MET C CA  1 
ATOM   11584 C  C   . MET C  2  210 ? 86.381  45.341  27.318  1.00 51.78  ?  210 MET C C   1 
ATOM   11585 O  O   . MET C  2  210 ? 85.350  45.438  27.978  1.00 54.57  ?  210 MET C O   1 
ATOM   11586 C  CB  . MET C  2  210 ? 87.383  47.181  25.947  1.00 56.31  ?  210 MET C CB  1 
ATOM   11587 C  CG  . MET C  2  210 ? 88.188  48.439  25.910  1.00 44.12  ?  210 MET C CG  1 
ATOM   11588 S  SD  . MET C  2  210 ? 87.976  49.276  24.325  1.00 63.26  ?  210 MET C SD  1 
ATOM   11589 C  CE  . MET C  2  210 ? 89.536  49.933  24.144  1.00 68.74  ?  210 MET C CE  1 
ATOM   11590 N  N   . ARG C  2  211 ? 86.692  44.250  26.608  1.00 50.39  ?  211 ARG C N   1 
ATOM   11591 C  CA  . ARG C  2  211 ? 85.828  43.071  26.532  1.00 53.43  ?  211 ARG C CA  1 
ATOM   11592 C  C   . ARG C  2  211 ? 85.572  42.504  27.934  1.00 54.98  ?  211 ARG C C   1 
ATOM   11593 O  O   . ARG C  2  211 ? 84.445  42.132  28.262  1.00 54.82  ?  211 ARG C O   1 
ATOM   11594 C  CB  . ARG C  2  211 ? 86.497  42.006  25.649  1.00 51.35  ?  211 ARG C CB  1 
ATOM   11595 C  CG  . ARG C  2  211 ? 85.598  40.850  25.278  1.00 51.08  ?  211 ARG C CG  1 
ATOM   11596 C  CD  . ARG C  2  211 ? 86.296  39.923  24.308  1.00 60.15  ?  211 ARG C CD  1 
ATOM   11597 N  NE  . ARG C  2  211 ? 85.345  39.053  23.621  1.00 65.62  ?  211 ARG C NE  1 
ATOM   11598 C  CZ  . ARG C  2  211 ? 85.668  38.198  22.659  1.00 61.30  ?  211 ARG C CZ  1 
ATOM   11599 N  NH1 . ARG C  2  211 ? 86.927  38.082  22.256  1.00 65.00  ?  211 ARG C NH1 1 
ATOM   11600 N  NH2 . ARG C  2  211 ? 84.730  37.447  22.091  1.00 74.77  ?  211 ARG C NH2 1 
ATOM   11601 N  N   . CYS C  2  212 ? 86.625  42.447  28.753  1.00 58.30  ?  212 CYS C N   1 
ATOM   11602 C  CA  . CYS C  2  212 ? 86.551  41.940  30.117  1.00 47.65  ?  212 CYS C CA  1 
ATOM   11603 C  C   . CYS C  2  212 ? 85.686  42.845  31.000  1.00 49.04  ?  212 CYS C C   1 
ATOM   11604 O  O   . CYS C  2  212 ? 84.803  42.357  31.704  1.00 54.30  ?  212 CYS C O   1 
ATOM   11605 C  CB  . CYS C  2  212 ? 87.961  41.777  30.686  1.00 48.09  ?  212 CYS C CB  1 
ATOM   11606 S  SG  . CYS C  2  212 ? 88.021  41.344  32.445  1.00 56.92  ?  212 CYS C SG  1 
ATOM   11607 N  N   . SER C  2  213 ? 85.931  44.157  30.957  1.00 59.83  ?  213 SER C N   1 
ATOM   11608 C  CA  . SER C  2  213 ? 85.182  45.126  31.756  1.00 53.01  ?  213 SER C CA  1 
ATOM   11609 C  C   . SER C  2  213 ? 83.680  45.064  31.476  1.00 48.24  ?  213 SER C C   1 
ATOM   11610 O  O   . SER C  2  213 ? 82.890  45.288  32.386  1.00 58.72  ?  213 SER C O   1 
ATOM   11611 C  CB  . SER C  2  213 ? 85.709  46.535  31.507  1.00 51.90  ?  213 SER C CB  1 
ATOM   11612 O  OG  . SER C  2  213 ? 85.309  47.020  30.238  1.00 50.83  ?  213 SER C OG  1 
ATOM   11613 N  N   . LEU C  2  214 ? 83.276  44.742  30.237  1.00 50.46  ?  214 LEU C N   1 
ATOM   11614 C  CA  . LEU C  2  214 ? 81.853  44.654  29.906  1.00 50.91  ?  214 LEU C CA  1 
ATOM   11615 C  C   . LEU C  2  214 ? 81.182  43.585  30.757  1.00 50.43  ?  214 LEU C C   1 
ATOM   11616 O  O   . LEU C  2  214 ? 80.063  43.798  31.213  1.00 62.62  ?  214 LEU C O   1 
ATOM   11617 C  CB  . LEU C  2  214 ? 81.639  44.410  28.406  1.00 42.92  ?  214 LEU C CB  1 
ATOM   11618 C  CG  . LEU C  2  214 ? 82.082  45.531  27.472  1.00 48.94  ?  214 LEU C CG  1 
ATOM   11619 C  CD1 . LEU C  2  214 ? 81.862  45.140  26.029  1.00 52.50  ?  214 LEU C CD1 1 
ATOM   11620 C  CD2 . LEU C  2  214 ? 81.365  46.838  27.787  1.00 50.21  ?  214 LEU C CD2 1 
ATOM   11621 N  N   . THR C  2  215 ? 81.857  42.448  30.994  1.00 51.17  ?  215 THR C N   1 
ATOM   11622 C  CA  . THR C  2  215 ? 81.278  41.390  31.831  1.00 54.91  ?  215 THR C CA  1 
ATOM   11623 C  C   . THR C  2  215 ? 81.044  41.830  33.277  1.00 60.27  ?  215 THR C C   1 
ATOM   11624 O  O   . THR C  2  215 ? 80.447  41.084  34.047  1.00 66.94  ?  215 THR C O   1 
ATOM   11625 C  CB  . THR C  2  215 ? 82.162  40.145  31.860  1.00 56.79  ?  215 THR C CB  1 
ATOM   11626 O  OG1 . THR C  2  215 ? 83.382  40.424  32.550  1.00 54.61  ?  215 THR C OG1 1 
ATOM   11627 C  CG2 . THR C  2  215 ? 82.421  39.575  30.483  1.00 51.64  ?  215 THR C CG2 1 
ATOM   11628 N  N   . ASP C  2  216 ? 81.526  43.019  33.652  1.00 63.72  ?  216 ASP C N   1 
ATOM   11629 C  CA  . ASP C  2  216 ? 81.342  43.544  34.988  1.00 51.11  ?  216 ASP C CA  1 
ATOM   11630 C  C   . ASP C  2  216 ? 80.056  44.379  34.966  1.00 60.66  ?  216 ASP C C   1 
ATOM   11631 O  O   . ASP C  2  216 ? 79.055  43.962  35.529  1.00 65.55  ?  216 ASP C O   1 
ATOM   11632 C  CB  . ASP C  2  216 ? 82.564  44.381  35.410  1.00 49.54  ?  216 ASP C CB  1 
ATOM   11633 C  CG  . ASP C  2  216 ? 82.463  45.005  36.783  1.00 63.43  ?  216 ASP C CG  1 
ATOM   11634 O  OD1 . ASP C  2  216 ? 81.377  44.919  37.399  1.00 61.68  ?  216 ASP C OD1 1 
ATOM   11635 O  OD2 . ASP C  2  216 ? 83.470  45.583  37.245  1.00 63.26  ?  216 ASP C OD2 1 
ATOM   11636 N  N   . GLY C  2  217 ? 80.075  45.512  34.276  1.00 54.53  ?  217 GLY C N   1 
ATOM   11637 C  CA  . GLY C  2  217 ? 78.932  46.410  34.206  1.00 54.75  ?  217 GLY C CA  1 
ATOM   11638 C  C   . GLY C  2  217 ? 77.620  45.808  33.745  1.00 60.12  ?  217 GLY C C   1 
ATOM   11639 O  O   . GLY C  2  217 ? 76.600  45.970  34.417  1.00 64.89  ?  217 GLY C O   1 
ATOM   11640 N  N   . TRP C  2  218 ? 77.621  45.137  32.592  1.00 54.71  ?  218 TRP C N   1 
ATOM   11641 C  CA  . TRP C  2  218 ? 76.395  44.572  32.038  1.00 55.67  ?  218 TRP C CA  1 
ATOM   11642 C  C   . TRP C  2  218 ? 76.069  43.157  32.512  1.00 57.63  ?  218 TRP C C   1 
ATOM   11643 O  O   . TRP C  2  218 ? 74.994  42.658  32.177  1.00 61.34  ?  218 TRP C O   1 
ATOM   11644 C  CB  . TRP C  2  218 ? 76.441  44.631  30.501  1.00 54.70  ?  218 TRP C CB  1 
ATOM   11645 C  CG  . TRP C  2  218 ? 76.541  46.027  29.963  1.00 46.58  ?  218 TRP C CG  1 
ATOM   11646 C  CD1 . TRP C  2  218 ? 77.675  46.690  29.598  1.00 51.13  ?  218 TRP C CD1 1 
ATOM   11647 C  CD2 . TRP C  2  218 ? 75.460  46.948  29.781  1.00 57.68  ?  218 TRP C CD2 1 
ATOM   11648 N  NE1 . TRP C  2  218 ? 77.366  47.967  29.191  1.00 52.20  ?  218 TRP C NE1 1 
ATOM   11649 C  CE2 . TRP C  2  218 ? 76.011  48.151  29.295  1.00 64.58  ?  218 TRP C CE2 1 
ATOM   11650 C  CE3 . TRP C  2  218 ? 74.078  46.874  29.985  1.00 61.50  ?  218 TRP C CE3 1 
ATOM   11651 C  CZ2 . TRP C  2  218 ? 75.224  49.268  29.014  1.00 63.60  ?  218 TRP C CZ2 1 
ATOM   11652 C  CZ3 . TRP C  2  218 ? 73.302  47.978  29.702  1.00 61.54  ?  218 TRP C CZ3 1 
ATOM   11653 C  CH2 . TRP C  2  218 ? 73.873  49.157  29.220  1.00 59.37  ?  218 TRP C CH2 1 
ATOM   11654 N  N   . MET C  2  219 ? 76.958  42.509  33.291  1.00 54.49  ?  219 MET C N   1 
ATOM   11655 C  CA  . MET C  2  219 ? 76.696  41.146  33.774  1.00 54.70  ?  219 MET C CA  1 
ATOM   11656 C  C   . MET C  2  219 ? 76.869  40.997  35.294  1.00 64.29  ?  219 MET C C   1 
ATOM   11657 O  O   . MET C  2  219 ? 75.884  40.806  35.999  1.00 71.54  ?  219 MET C O   1 
ATOM   11658 C  CB  . MET C  2  219 ? 77.586  40.126  33.047  1.00 67.26  ?  219 MET C CB  1 
ATOM   11659 C  CG  . MET C  2  219 ? 77.349  40.062  31.574  1.00 66.86  ?  219 MET C CG  1 
ATOM   11660 S  SD  . MET C  2  219 ? 78.244  38.690  30.840  1.00 63.43  ?  219 MET C SD  1 
ATOM   11661 C  CE  . MET C  2  219 ? 78.129  39.146  29.168  1.00 75.81  ?  219 MET C CE  1 
ATOM   11662 N  N   . GLY C  2  220 ? 78.104  41.078  35.787  1.00 74.18  ?  220 GLY C N   1 
ATOM   11663 C  CA  . GLY C  2  220 ? 78.387  40.926  37.209  1.00 66.61  ?  220 GLY C CA  1 
ATOM   11664 C  C   . GLY C  2  220 ? 77.652  41.921  38.080  1.00 63.20  ?  220 GLY C C   1 
ATOM   11665 O  O   . GLY C  2  220 ? 76.959  41.531  39.019  1.00 68.17  ?  220 GLY C O   1 
ATOM   11666 N  N   . SER C  2  221 ? 77.754  43.204  37.748  1.00 59.39  ?  221 SER C N   1 
ATOM   11667 C  CA  . SER C  2  221 ? 77.106  44.249  38.575  1.00 54.54  ?  221 SER C CA  1 
ATOM   11668 C  C   . SER C  2  221 ? 75.590  44.213  38.360  1.00 62.55  ?  221 SER C C   1 
ATOM   11669 O  O   . SER C  2  221 ? 74.857  44.185  39.357  1.00 75.20  ?  221 SER C O   1 
ATOM   11670 C  CB  . SER C  2  221 ? 77.682  45.595  38.268  1.00 61.01  ?  221 SER C CB  1 
ATOM   11671 O  OG  . SER C  2  221 ? 79.087  45.594  38.463  1.00 63.44  ?  221 SER C OG  1 
ATOM   11672 N  N   . PHE C  2  222 ? 75.151  44.226  37.100  1.00 58.55  ?  222 PHE C N   1 
ATOM   11673 C  CA  . PHE C  2  222 ? 73.700  44.197  36.787  1.00 67.02  ?  222 PHE C CA  1 
ATOM   11674 C  C   . PHE C  2  222 ? 73.023  43.090  37.597  1.00 75.85  ?  222 PHE C C   1 
ATOM   11675 O  O   . PHE C  2  222 ? 72.159  43.404  38.438  1.00 78.29  ?  222 PHE C O   1 
ATOM   11676 C  CB  . PHE C  2  222 ? 73.491  43.964  35.290  1.00 58.91  ?  222 PHE C CB  1 
ATOM   11677 C  CG  . PHE C  2  222 ? 72.510  44.900  34.633  1.00 60.40  ?  222 PHE C CG  1 
ATOM   11678 C  CD1 . PHE C  2  222 ? 71.154  44.616  34.625  1.00 64.99  ?  222 PHE C CD1 1 
ATOM   11679 C  CD2 . PHE C  2  222 ? 72.943  46.063  34.019  1.00 62.85  ?  222 PHE C CD2 1 
ATOM   11680 C  CE1 . PHE C  2  222 ? 70.253  45.477  34.020  1.00 65.79  ?  222 PHE C CE1 1 
ATOM   11681 C  CE2 . PHE C  2  222 ? 72.040  46.922  33.415  1.00 54.29  ?  222 PHE C CE2 1 
ATOM   11682 C  CZ  . PHE C  2  222 ? 70.697  46.629  33.415  1.00 59.70  ?  222 PHE C CZ  1 
ATOM   11683 N  N   . MET C  2  223 ? 73.407  41.837  37.351  1.00 64.04  ?  223 MET C N   1 
ATOM   11684 C  CA  . MET C  2  223 ? 72.783  40.683  38.043  1.00 70.55  ?  223 MET C CA  1 
ATOM   11685 C  C   . MET C  2  223 ? 72.911  40.880  39.553  1.00 71.08  ?  223 MET C C   1 
ATOM   11686 O  O   . MET C  2  223 ? 71.979  40.507  40.276  1.00 73.03  ?  223 MET C O   1 
ATOM   11687 C  CB  . MET C  2  223 ? 73.480  39.382  37.643  1.00 67.11  ?  223 MET C CB  1 
ATOM   11688 C  CG  . MET C  2  223 ? 73.117  38.906  36.254  1.00 69.27  ?  223 MET C CG  1 
ATOM   11689 S  SD  . MET C  2  223 ? 73.693  37.222  35.949  1.00 88.32  ?  223 MET C SD  1 
ATOM   11690 C  CE  . MET C  2  223 ? 75.384  37.540  35.450  1.00 73.03  ?  223 MET C CE  1 
ATOM   11691 N  N   . GLY C  2  224 ? 74.032  41.432  40.006  1.00 64.00  ?  224 GLY C N   1 
ATOM   11692 C  CA  . GLY C  2  224 ? 74.188  41.703  41.428  1.00 60.14  ?  224 GLY C CA  1 
ATOM   11693 C  C   . GLY C  2  224 ? 73.134  42.670  41.930  1.00 67.76  ?  224 GLY C C   1 
ATOM   11694 O  O   . GLY C  2  224 ? 72.530  42.443  42.980  1.00 77.68  ?  224 GLY C O   1 
ATOM   11695 N  N   . THR C  2  225 ? 72.879  43.740  41.162  1.00 64.00  ?  225 THR C N   1 
ATOM   11696 C  CA  . THR C  2  225 ? 71.873  44.739  41.520  1.00 60.85  ?  225 THR C CA  1 
ATOM   11697 C  C   . THR C  2  225 ? 70.460  44.172  41.336  1.00 66.01  ?  225 THR C C   1 
ATOM   11698 O  O   . THR C  2  225 ? 69.656  44.238  42.258  1.00 83.98  ?  225 THR C O   1 
ATOM   11699 C  CB  . THR C  2  225 ? 72.075  46.021  40.686  1.00 54.26  ?  225 THR C CB  1 
ATOM   11700 O  OG1 . THR C  2  225 ? 73.273  46.674  41.103  1.00 63.89  ?  225 THR C OG1 1 
ATOM   11701 C  CG2 . THR C  2  225 ? 70.914  46.983  40.804  1.00 63.66  ?  225 THR C CG2 1 
ATOM   11702 N  N   . GLU C  2  226 ? 70.156  43.615  40.161  1.00 59.87  ?  226 GLU C N   1 
ATOM   11703 C  CA  . GLU C  2  226 ? 68.830  43.068  39.889  1.00 68.94  ?  226 GLU C CA  1 
ATOM   11704 C  C   . GLU C  2  226 ? 68.402  41.986  40.891  1.00 71.17  ?  226 GLU C C   1 
ATOM   11705 O  O   . GLU C  2  226 ? 67.269  42.015  41.365  1.00 76.09  ?  226 GLU C O   1 
ATOM   11706 C  CB  . GLU C  2  226 ? 68.755  42.525  38.454  1.00 73.74  ?  226 GLU C CB  1 
ATOM   11707 C  CG  . GLU C  2  226 ? 68.653  43.620  37.408  1.00 85.79  ?  226 GLU C CG  1 
ATOM   11708 C  CD  . GLU C  2  226 ? 68.478  43.119  35.991  1.00 95.70  ?  226 GLU C CD  1 
ATOM   11709 O  OE1 . GLU C  2  226 ? 69.137  42.118  35.624  1.00 102.69 ?  226 GLU C OE1 1 
ATOM   11710 O  OE2 . GLU C  2  226 ? 67.685  43.735  35.242  1.00 88.87  ?  226 GLU C OE2 1 
ATOM   11711 N  N   . PHE C  2  227 ? 69.288  41.037  41.211  1.00 70.67  ?  227 PHE C N   1 
ATOM   11712 C  CA  . PHE C  2  227 ? 68.951  39.970  42.154  1.00 69.73  ?  227 PHE C CA  1 
ATOM   11713 C  C   . PHE C  2  227 ? 68.854  40.503  43.591  1.00 72.60  ?  227 PHE C C   1 
ATOM   11714 O  O   . PHE C  2  227 ? 68.055  39.988  44.375  1.00 67.25  ?  227 PHE C O   1 
ATOM   11715 C  CB  . PHE C  2  227 ? 69.955  38.807  42.053  1.00 64.80  ?  227 PHE C CB  1 
ATOM   11716 C  CG  . PHE C  2  227 ? 69.970  38.013  40.760  1.00 59.62  ?  227 PHE C CG  1 
ATOM   11717 C  CD1 . PHE C  2  227 ? 69.018  38.228  39.774  1.00 67.48  ?  227 PHE C CD1 1 
ATOM   11718 C  CD2 . PHE C  2  227 ? 70.954  37.071  40.521  1.00 68.42  ?  227 PHE C CD2 1 
ATOM   11719 C  CE1 . PHE C  2  227 ? 69.043  37.499  38.592  1.00 60.71  ?  227 PHE C CE1 1 
ATOM   11720 C  CE2 . PHE C  2  227 ? 70.974  36.347  39.337  1.00 72.70  ?  227 PHE C CE2 1 
ATOM   11721 C  CZ  . PHE C  2  227 ? 70.016  36.561  38.384  1.00 70.46  ?  227 PHE C CZ  1 
ATOM   11722 N  N   . SER C  2  228 ? 69.637  41.538  43.939  1.00 70.96  ?  228 SER C N   1 
ATOM   11723 C  CA  . SER C  2  228 ? 69.565  42.125  45.276  1.00 64.98  ?  228 SER C CA  1 
ATOM   11724 C  C   . SER C  2  228 ? 68.196  42.794  45.459  1.00 75.21  ?  228 SER C C   1 
ATOM   11725 O  O   . SER C  2  228 ? 67.615  42.709  46.534  1.00 76.35  ?  228 SER C O   1 
ATOM   11726 C  CB  . SER C  2  228 ? 70.680  43.144  45.478  1.00 60.00  ?  228 SER C CB  1 
ATOM   11727 O  OG  . SER C  2  228 ? 71.949  42.514  45.464  1.00 72.95  ?  228 SER C OG  1 
ATOM   11728 N  N   . ASP C  2  229 ? 67.673  43.448  44.412  1.00 70.25  ?  229 ASP C N   1 
ATOM   11729 C  CA  . ASP C  2  229 ? 66.362  44.088  44.474  1.00 66.26  ?  229 ASP C CA  1 
ATOM   11730 C  C   . ASP C  2  229 ? 65.253  43.034  44.547  1.00 75.24  ?  229 ASP C C   1 
ATOM   11731 O  O   . ASP C  2  229 ? 64.222  43.284  45.165  1.00 75.78  ?  229 ASP C O   1 
ATOM   11732 C  CB  . ASP C  2  229 ? 66.142  45.000  43.256  1.00 72.59  ?  229 ASP C CB  1 
ATOM   11733 C  CG  . ASP C  2  229 ? 67.024  46.236  43.225  1.00 78.70  ?  229 ASP C CG  1 
ATOM   11734 O  OD1 . ASP C  2  229 ? 67.844  46.409  44.154  1.00 79.76  ?  229 ASP C OD1 1 
ATOM   11735 O  OD2 . ASP C  2  229 ? 66.896  47.029  42.271  1.00 68.94  ?  229 ASP C OD2 1 
ATOM   11736 N  N   . ILE C  2  230 ? 65.449  41.861  43.928  1.00 79.63  ?  230 ILE C N   1 
ATOM   11737 C  CA  . ILE C  2  230 ? 64.442  40.804  43.971  1.00 67.75  ?  230 ILE C CA  1 
ATOM   11738 C  C   . ILE C  2  230 ? 64.338  40.266  45.402  1.00 75.74  ?  230 ILE C C   1 
ATOM   11739 O  O   . ILE C  2  230 ? 63.245  40.194  45.951  1.00 75.16  ?  230 ILE C O   1 
ATOM   11740 C  CB  . ILE C  2  230 ? 64.748  39.672  42.939  1.00 60.90  ?  230 ILE C CB  1 
ATOM   11741 C  CG1 . ILE C  2  230 ? 64.435  40.146  41.506  1.00 65.92  ?  230 ILE C CG1 1 
ATOM   11742 C  CG2 . ILE C  2  230 ? 63.955  38.401  43.260  1.00 68.91  ?  230 ILE C CG2 1 
ATOM   11743 C  CD1 . ILE C  2  230 ? 65.048  39.306  40.392  1.00 67.12  ?  230 ILE C CD1 1 
ATOM   11744 N  N   . MET C  2  231 ? 65.472  39.905  46.007  1.00 78.80  ?  231 MET C N   1 
ATOM   11745 C  CA  . MET C  2  231 ? 65.491  39.332  47.351  1.00 72.36  ?  231 MET C CA  1 
ATOM   11746 C  C   . MET C  2  231 ? 65.335  40.325  48.496  1.00 75.60  ?  231 MET C C   1 
ATOM   11747 O  O   . MET C  2  231 ? 64.790  39.947  49.529  1.00 87.17  ?  231 MET C O   1 
ATOM   11748 C  CB  . MET C  2  231 ? 66.791  38.551  47.564  1.00 61.77  ?  231 MET C CB  1 
ATOM   11749 C  CG  . MET C  2  231 ? 66.980  37.416  46.587  1.00 72.84  ?  231 MET C CG  1 
ATOM   11750 S  SD  . MET C  2  231 ? 68.455  36.433  46.937  1.00 76.93  ?  231 MET C SD  1 
ATOM   11751 C  CE  . MET C  2  231 ? 69.710  37.609  46.581  1.00 68.46  ?  231 MET C CE  1 
ATOM   11752 N  N   . PHE C  2  232 ? 65.835  41.557  48.355  1.00 77.55  ?  232 PHE C N   1 
ATOM   11753 C  CA  . PHE C  2  232 ? 65.766  42.537  49.442  1.00 73.30  ?  232 PHE C CA  1 
ATOM   11754 C  C   . PHE C  2  232 ? 64.822  43.722  49.193  1.00 77.10  ?  232 PHE C C   1 
ATOM   11755 O  O   . PHE C  2  232 ? 64.630  44.525  50.101  1.00 76.63  ?  232 PHE C O   1 
ATOM   11756 C  CB  . PHE C  2  232 ? 67.174  43.059  49.775  1.00 72.81  ?  232 PHE C CB  1 
ATOM   11757 C  CG  . PHE C  2  232 ? 68.245  41.994  49.839  1.00 62.53  ?  232 PHE C CG  1 
ATOM   11758 C  CD1 . PHE C  2  232 ? 68.060  40.844  50.585  1.00 65.62  ?  232 PHE C CD1 1 
ATOM   11759 C  CD2 . PHE C  2  232 ? 69.444  42.155  49.169  1.00 76.72  ?  232 PHE C CD2 1 
ATOM   11760 C  CE1 . PHE C  2  232 ? 69.043  39.866  50.639  1.00 83.11  ?  232 PHE C CE1 1 
ATOM   11761 C  CE2 . PHE C  2  232 ? 70.427  41.176  49.226  1.00 73.55  ?  232 PHE C CE2 1 
ATOM   11762 C  CZ  . PHE C  2  232 ? 70.220  40.037  49.960  1.00 73.30  ?  232 PHE C CZ  1 
ATOM   11763 N  N   . GLY C  2  233 ? 64.251  43.825  47.994  1.00 77.60  ?  233 GLY C N   1 
ATOM   11764 C  CA  . GLY C  2  233 ? 63.335  44.907  47.642  1.00 66.27  ?  233 GLY C CA  1 
ATOM   11765 C  C   . GLY C  2  233 ? 63.958  45.989  46.775  1.00 78.67  ?  233 GLY C C   1 
ATOM   11766 O  O   . GLY C  2  233 ? 65.098  46.396  47.012  1.00 75.63  ?  233 GLY C O   1 
ATOM   11767 N  N   . THR C  2  234 ? 63.215  46.471  45.756  1.00 81.97  ?  234 THR C N   1 
ATOM   11768 C  CA  . THR C  2  234 ? 63.709  47.522  44.866  1.00 64.45  ?  234 THR C CA  1 
ATOM   11769 C  C   . THR C  2  234 ? 63.741  48.841  45.635  1.00 73.29  ?  234 THR C C   1 
ATOM   11770 O  O   . THR C  2  234 ? 62.713  49.212  46.203  1.00 79.95  ?  234 THR C O   1 
ATOM   11771 C  CB  . THR C  2  234 ? 62.803  47.655  43.644  1.00 75.66  ?  234 THR C CB  1 
ATOM   11772 O  OG1 . THR C  2  234 ? 62.667  46.376  43.027  1.00 91.34  ?  234 THR C OG1 1 
ATOM   11773 C  CG2 . THR C  2  234 ? 63.344  48.652  42.629  1.00 71.06  ?  234 THR C CG2 1 
ATOM   11774 N  N   . PRO C  2  235 ? 64.868  49.581  45.682  1.00 70.44  ?  235 PRO C N   1 
ATOM   11775 C  CA  . PRO C  2  235 ? 64.869  50.836  46.449  1.00 73.44  ?  235 PRO C CA  1 
ATOM   11776 C  C   . PRO C  2  235 ? 63.927  51.920  45.945  1.00 77.92  ?  235 PRO C C   1 
ATOM   11777 O  O   . PRO C  2  235 ? 63.611  51.983  44.757  1.00 77.66  ?  235 PRO C O   1 
ATOM   11778 C  CB  . PRO C  2  235 ? 66.317  51.322  46.359  1.00 64.15  ?  235 PRO C CB  1 
ATOM   11779 C  CG  . PRO C  2  235 ? 67.100  50.177  45.912  1.00 77.48  ?  235 PRO C CG  1 
ATOM   11780 C  CD  . PRO C  2  235 ? 66.195  49.315  45.099  1.00 75.22  ?  235 PRO C CD  1 
ATOM   11781 N  N   A HIS C  2  236 ? 63.489  52.785  46.865  0.60 77.41  ?  236 HIS C N   1 
ATOM   11782 N  N   B HIS C  2  236 ? 63.487  52.785  46.860  0.40 78.80  ?  236 HIS C N   1 
ATOM   11783 C  CA  A HIS C  2  236 ? 62.594  53.902  46.572  0.60 80.38  ?  236 HIS C CA  1 
ATOM   11784 C  CA  B HIS C  2  236 ? 62.592  53.899  46.552  0.40 78.37  ?  236 HIS C CA  1 
ATOM   11785 C  C   A HIS C  2  236 ? 62.999  55.100  47.437  0.60 77.44  ?  236 HIS C C   1 
ATOM   11786 C  C   B HIS C  2  236 ? 62.969  55.090  47.445  0.40 78.36  ?  236 HIS C C   1 
ATOM   11787 O  O   A HIS C  2  236 ? 63.675  54.918  48.449  0.60 76.39  ?  236 HIS C O   1 
ATOM   11788 O  O   B HIS C  2  236 ? 63.612  54.898  48.476  0.40 77.41  ?  236 HIS C O   1 
ATOM   11789 C  CB  A HIS C  2  236 ? 61.135  53.511  46.851  0.60 81.98  ?  236 HIS C CB  1 
ATOM   11790 C  CB  B HIS C  2  236 ? 61.124  53.483  46.746  0.40 81.53  ?  236 HIS C CB  1 
ATOM   11791 C  CG  A HIS C  2  236 ? 60.867  53.163  48.282  0.60 71.32  ?  236 HIS C CG  1 
ATOM   11792 C  CG  B HIS C  2  236 ? 60.673  52.421  45.786  0.40 81.83  ?  236 HIS C CG  1 
ATOM   11793 N  ND1 A HIS C  2  236 ? 60.543  54.134  49.212  0.60 72.72  ?  236 HIS C ND1 1 
ATOM   11794 N  ND1 B HIS C  2  236 ? 60.885  52.543  44.422  0.40 76.78  ?  236 HIS C ND1 1 
ATOM   11795 C  CD2 A HIS C  2  236 ? 60.879  51.959  48.895  0.60 77.04  ?  236 HIS C CD2 1 
ATOM   11796 C  CD2 B HIS C  2  236 ? 60.039  51.250  46.024  0.40 82.02  ?  236 HIS C CD2 1 
ATOM   11797 C  CE1 A HIS C  2  236 ? 60.371  53.495  50.356  0.60 73.66  ?  236 HIS C CE1 1 
ATOM   11798 C  CE1 B HIS C  2  236 ? 60.375  51.450  43.877  0.40 71.65  ?  236 HIS C CE1 1 
ATOM   11799 N  NE2 A HIS C  2  236 ? 60.565  52.184  50.213  0.60 74.97  ?  236 HIS C NE2 1 
ATOM   11800 N  NE2 B HIS C  2  236 ? 59.856  50.642  44.802  0.40 79.98  ?  236 HIS C NE2 1 
ATOM   11801 N  N   . SER C  2  237 ? 62.592  56.322  47.049  1.00 73.52  ?  237 SER C N   1 
ATOM   11802 C  CA  . SER C  2  237 ? 62.927  57.551  47.799  1.00 77.95  ?  237 SER C CA  1 
ATOM   11803 C  C   . SER C  2  237 ? 62.763  57.399  49.320  1.00 80.40  ?  237 SER C C   1 
ATOM   11804 O  O   . SER C  2  237 ? 61.671  57.106  49.804  1.00 87.75  ?  237 SER C O   1 
ATOM   11805 C  CB  . SER C  2  237 ? 62.139  58.747  47.274  1.00 71.28  ?  237 SER C CB  1 
ATOM   11806 O  OG  . SER C  2  237 ? 60.778  58.424  47.041  1.00 107.84 ?  237 SER C OG  1 
ATOM   11807 N  N   . ILE C  2  238 ? 63.878  57.524  50.049  1.00 76.65  ?  238 ILE C N   1 
ATOM   11808 C  CA  . ILE C  2  238 ? 63.899  57.322  51.494  1.00 77.69  ?  238 ILE C CA  1 
ATOM   11809 C  C   . ILE C  2  238 ? 64.832  58.330  52.167  1.00 75.84  ?  238 ILE C C   1 
ATOM   11810 O  O   . ILE C  2  238 ? 65.793  58.787  51.554  1.00 80.65  ?  238 ILE C O   1 
ATOM   11811 C  CB  . ILE C  2  238 ? 64.314  55.845  51.770  1.00 71.92  ?  238 ILE C CB  1 
ATOM   11812 C  CG1 . ILE C  2  238 ? 64.127  55.461  53.253  1.00 76.65  ?  238 ILE C CG1 1 
ATOM   11813 C  CG2 . ILE C  2  238 ? 65.749  55.580  51.307  1.00 71.55  ?  238 ILE C CG2 1 
ATOM   11814 C  CD1 . ILE C  2  238 ? 63.841  53.961  53.489  1.00 73.17  ?  238 ILE C CD1 1 
ATOM   11815 N  N   . ASP C  2  239 ? 64.533  58.662  53.422  1.00 77.47  ?  239 ASP C N   1 
ATOM   11816 C  CA  . ASP C  2  239 ? 65.353  59.673  54.135  1.00 82.19  ?  239 ASP C CA  1 
ATOM   11817 C  C   . ASP C  2  239 ? 66.335  58.983  55.078  1.00 80.07  ?  239 ASP C C   1 
ATOM   11818 O  O   . ASP C  2  239 ? 66.042  57.858  55.521  1.00 90.69  ?  239 ASP C O   1 
ATOM   11819 C  CB  . ASP C  2  239 ? 64.493  60.667  54.917  1.00 76.78  ?  239 ASP C CB  1 
ATOM   11820 C  CG  . ASP C  2  239 ? 63.472  61.381  54.055  1.00 94.48  ?  239 ASP C CG  1 
ATOM   11821 O  OD1 . ASP C  2  239 ? 62.467  60.743  53.715  1.00 114.47 ?  239 ASP C OD1 1 
ATOM   11822 O  OD2 . ASP C  2  239 ? 63.696  62.564  53.732  1.00 99.42  ?  239 ASP C OD2 1 
ATOM   11823 N  N   . THR C  2  240 ? 67.422  59.693  55.398  1.00 74.60  ?  240 THR C N   1 
ATOM   11824 C  CA  . THR C  2  240 ? 68.459  59.143  56.305  1.00 77.70  ?  240 THR C CA  1 
ATOM   11825 C  C   . THR C  2  240 ? 69.431  60.246  56.731  1.00 84.04  ?  240 THR C C   1 
ATOM   11826 O  O   . THR C  2  240 ? 69.334  61.356  56.176  1.00 97.60  ?  240 THR C O   1 
ATOM   11827 C  CB  . THR C  2  240 ? 69.221  58.009  55.619  1.00 86.90  ?  240 THR C CB  1 
ATOM   11828 O  OG1 . THR C  2  240 ? 69.721  57.205  56.680  1.00 86.97  ?  240 THR C OG1 1 
ATOM   11829 C  CG2 . THR C  2  240 ? 70.359  58.495  54.749  1.00 92.23  ?  240 THR C CG2 1 
ATOM   11830 N  N   . GLU C  2  241 ? 70.325  59.951  57.677  1.00 76.16  ?  241 GLU C N   1 
ATOM   11831 C  CA  . GLU C  2  241 ? 71.313  60.908  58.156  1.00 79.09  ?  241 GLU C CA  1 
ATOM   11832 C  C   . GLU C  2  241 ? 72.686  60.354  57.778  1.00 80.15  ?  241 GLU C C   1 
ATOM   11833 O  O   . GLU C  2  241 ? 72.875  59.138  57.734  1.00 78.56  ?  241 GLU C O   1 
ATOM   11834 C  CB  . GLU C  2  241 ? 71.178  61.149  59.673  1.00 82.83  ?  241 GLU C CB  1 
ATOM   11835 C  CG  . GLU C  2  241 ? 70.209  62.273  60.015  1.00 99.51  ?  241 GLU C CG  1 
ATOM   11836 C  CD  . GLU C  2  241 ? 69.612  62.265  61.409  1.00 110.49 ?  241 GLU C CD  1 
ATOM   11837 O  OE1 . GLU C  2  241 ? 69.905  61.328  62.188  1.00 109.59 ?  241 GLU C OE1 1 
ATOM   11838 O  OE2 . GLU C  2  241 ? 68.845  63.204  61.723  1.00 107.05 ?  241 GLU C OE2 1 
ATOM   11839 N  N   . ALA C  2  242 ? 73.627  61.246  57.470  1.00 76.86  ?  242 ALA C N   1 
ATOM   11840 C  CA  . ALA C  2  242 ? 74.973  60.879  57.046  1.00 74.22  ?  242 ALA C CA  1 
ATOM   11841 C  C   . ALA C  2  242 ? 76.047  61.524  57.933  1.00 79.35  ?  242 ALA C C   1 
ATOM   11842 O  O   . ALA C  2  242 ? 75.754  62.457  58.678  1.00 84.60  ?  242 ALA C O   1 
ATOM   11843 C  CB  . ALA C  2  242 ? 75.168  61.301  55.595  1.00 73.50  ?  242 ALA C CB  1 
ATOM   11844 N  N   . ASN C  2  243 ? 77.273  60.994  57.865  1.00 77.55  ?  243 ASN C N   1 
ATOM   11845 C  CA  . ASN C  2  243 ? 78.423  61.558  58.632  1.00 77.60  ?  243 ASN C CA  1 
ATOM   11846 C  C   . ASN C  2  243 ? 78.566  60.875  59.996  1.00 76.64  ?  243 ASN C C   1 
ATOM   11847 O  O   . ASN C  2  243 ? 77.572  60.303  60.479  1.00 77.48  ?  243 ASN C O   1 
ATOM   11848 C  CB  . ASN C  2  243 ? 78.380  63.086  58.751  1.00 87.25  ?  243 ASN C CB  1 
ATOM   11849 C  CG  . ASN C  2  243 ? 79.752  63.717  58.653  1.00 87.29  ?  243 ASN C CG  1 
ATOM   11850 O  OD1 . ASN C  2  243 ? 80.764  63.045  58.841  1.00 69.43  ?  243 ASN C OD1 1 
ATOM   11851 N  ND2 . ASN C  2  243 ? 79.798  65.006  58.359  1.00 103.16 ?  243 ASN C ND2 1 
ATOM   11852 N  N   . LEU C  2  244 ? 79.763  60.940  60.582  1.00 79.27  ?  244 LEU C N   1 
ATOM   11853 C  CA  . LEU C  2  244 ? 80.058  60.318  61.871  1.00 81.09  ?  244 LEU C CA  1 
ATOM   11854 C  C   . LEU C  2  244 ? 79.216  60.818  63.051  1.00 74.36  ?  244 LEU C C   1 
ATOM   11855 O  O   . LEU C  2  244 ? 79.182  60.153  64.084  1.00 79.60  ?  244 LEU C O   1 
ATOM   11856 C  CB  . LEU C  2  244 ? 81.560  60.426  62.176  1.00 70.32  ?  244 LEU C CB  1 
ATOM   11857 C  CG  . LEU C  2  244 ? 82.471  59.655  61.199  1.00 82.78  ?  244 LEU C CG  1 
ATOM   11858 C  CD1 . LEU C  2  244 ? 83.893  60.152  61.260  1.00 87.22  ?  244 LEU C CD1 1 
ATOM   11859 C  CD2 . LEU C  2  244 ? 82.418  58.159  61.458  1.00 77.67  ?  244 LEU C CD2 1 
ATOM   11860 N  N   . GLY C  2  245 ? 78.513  61.935  62.892  1.00 74.09  ?  245 GLY C N   1 
ATOM   11861 C  CA  . GLY C  2  245 ? 77.638  62.435  63.948  1.00 87.60  ?  245 GLY C CA  1 
ATOM   11862 C  C   . GLY C  2  245 ? 76.439  61.529  64.189  1.00 88.33  ?  245 GLY C C   1 
ATOM   11863 O  O   . GLY C  2  245 ? 75.672  61.736  65.132  1.00 96.34  ?  245 GLY C O   1 
ATOM   11864 N  N   . VAL C  2  246 ? 76.315  60.481  63.369  1.00 81.22  ?  246 VAL C N   1 
ATOM   11865 C  CA  . VAL C  2  246 ? 75.142  59.560  63.477  1.00 88.20  ?  246 VAL C CA  1 
ATOM   11866 C  C   . VAL C  2  246 ? 75.329  58.597  64.656  1.00 89.60  ?  246 VAL C C   1 
ATOM   11867 O  O   . VAL C  2  246 ? 74.309  58.113  65.178  1.00 96.96  ?  246 VAL C O   1 
ATOM   11868 C  CB  . VAL C  2  246 ? 74.905  58.789  62.164  1.00 74.07  ?  246 VAL C CB  1 
ATOM   11869 C  CG1 . VAL C  2  246 ? 74.564  59.722  61.013  1.00 81.76  ?  246 VAL C CG1 1 
ATOM   11870 C  CG2 . VAL C  2  246 ? 76.086  57.900  61.809  1.00 82.60  ?  246 VAL C CG2 1 
ATOM   11871 N  N   . LEU C  2  247 ? 76.575  58.323  65.055  1.00 89.05  ?  247 LEU C N   1 
ATOM   11872 C  CA  . LEU C  2  247 ? 76.808  57.443  66.206  1.00 86.91  ?  247 LEU C CA  1 
ATOM   11873 C  C   . LEU C  2  247 ? 76.193  58.038  67.481  1.00 95.47  ?  247 LEU C C   1 
ATOM   11874 O  O   . LEU C  2  247 ? 76.234  59.253  67.672  1.00 100.31 ?  247 LEU C O   1 
ATOM   11875 C  CB  . LEU C  2  247 ? 78.315  57.219  66.419  1.00 82.58  ?  247 LEU C CB  1 
ATOM   11876 C  CG  . LEU C  2  247 ? 79.090  56.575  65.262  1.00 81.48  ?  247 LEU C CG  1 
ATOM   11877 C  CD1 . LEU C  2  247 ? 80.574  56.876  65.367  1.00 81.73  ?  247 LEU C CD1 1 
ATOM   11878 C  CD2 . LEU C  2  247 ? 78.871  55.073  65.213  1.00 78.56  ?  247 LEU C CD2 1 
ATOM   11879 N  N   . GLU C  2  248 ? 75.644  57.163  68.332  1.00 91.72  ?  248 GLU C N   1 
ATOM   11880 C  CA  . GLU C  2  248 ? 75.008  57.605  69.602  1.00 89.31  ?  248 GLU C CA  1 
ATOM   11881 C  C   . GLU C  2  248 ? 75.844  57.121  70.789  1.00 90.66  ?  248 GLU C C   1 
ATOM   11882 O  O   . GLU C  2  248 ? 76.122  55.910  70.856  1.00 100.52 ?  248 GLU C O   1 
ATOM   11883 C  CB  . GLU C  2  248 ? 73.594  57.033  69.697  1.00 91.24  ?  248 GLU C CB  1 
ATOM   11884 C  CG  . GLU C  2  248 ? 72.840  57.069  68.383  1.00 103.18 ?  248 GLU C CG  1 
ATOM   11885 C  CD  . GLU C  2  248 ? 72.190  58.408  68.083  1.00 121.70 ?  248 GLU C CD  1 
ATOM   11886 O  OE1 . GLU C  2  248 ? 72.487  59.378  68.807  1.00 121.28 ?  248 GLU C OE1 1 
ATOM   11887 O  OE2 . GLU C  2  248 ? 71.389  58.475  67.131  1.00 132.04 ?  248 GLU C OE2 1 
ATOM   11888 N  N   . LYS C  2  249 ? 76.211  58.029  71.696  1.00 97.54  ?  249 LYS C N   1 
ATOM   11889 C  CA  . LYS C  2  249 ? 77.023  57.674  72.865  1.00 94.88  ?  249 LYS C CA  1 
ATOM   11890 C  C   . LYS C  2  249 ? 76.354  56.686  73.835  1.00 95.02  ?  249 LYS C C   1 
ATOM   11891 O  O   . LYS C  2  249 ? 77.019  55.768  74.311  1.00 94.60  ?  249 LYS C O   1 
ATOM   11892 C  CB  . LYS C  2  249 ? 77.445  58.952  73.610  1.00 97.92  ?  249 LYS C CB  1 
ATOM   11893 C  CG  . LYS C  2  249 ? 78.246  58.708  74.887  1.00 86.42  ?  249 LYS C CG  1 
ATOM   11894 C  CD  . LYS C  2  249 ? 79.262  59.819  75.163  1.00 99.47  ?  249 LYS C CD  1 
ATOM   11895 C  CE  . LYS C  2  249 ? 79.471  60.082  76.638  1.00 109.16 ?  249 LYS C CE  1 
ATOM   11896 N  NZ  . LYS C  2  249 ? 80.663  60.938  76.896  1.00 103.44 ?  249 LYS C NZ  1 
ATOM   11897 N  N   . ASN C  2  250 ? 75.061  56.863  74.132  1.00 97.26  ?  250 ASN C N   1 
ATOM   11898 C  CA  . ASN C  2  250 ? 74.365  55.987  75.079  1.00 96.74  ?  250 ASN C CA  1 
ATOM   11899 C  C   . ASN C  2  250 ? 73.716  54.731  74.467  1.00 108.99 ?  250 ASN C C   1 
ATOM   11900 O  O   . ASN C  2  250 ? 73.110  53.954  75.206  1.00 99.03  ?  250 ASN C O   1 
ATOM   11901 C  CB  . ASN C  2  250 ? 73.341  56.794  75.862  1.00 102.30 ?  250 ASN C CB  1 
ATOM   11902 C  CG  . ASN C  2  250 ? 73.980  57.891  76.677  1.00 115.60 ?  250 ASN C CG  1 
ATOM   11903 O  OD1 . ASN C  2  250 ? 74.939  57.658  77.426  1.00 124.13 ?  250 ASN C OD1 1 
ATOM   11904 N  ND2 . ASN C  2  250 ? 73.472  59.115  76.549  1.00 109.35 ?  250 ASN C ND2 1 
ATOM   11905 N  N   . SER C  2  251 ? 73.913  54.544  73.161  1.00 104.35 ?  251 SER C N   1 
ATOM   11906 C  CA  . SER C  2  251 ? 73.384  53.335  72.485  1.00 98.56  ?  251 SER C CA  1 
ATOM   11907 C  C   . SER C  2  251 ? 74.538  52.448  72.038  1.00 92.18  ?  251 SER C C   1 
ATOM   11908 O  O   . SER C  2  251 ? 75.669  52.953  71.923  1.00 98.94  ?  251 SER C O   1 
ATOM   11909 C  CB  . SER C  2  251 ? 72.575  53.696  71.286  1.00 85.15  ?  251 SER C CB  1 
ATOM   11910 O  OG  . SER C  2  251 ? 71.447  54.440  71.670  1.00 102.39 ?  251 SER C OG  1 
ATOM   11911 N  N   . VAL C  2  252 ? 74.246  51.176  71.791  1.00 81.34  ?  252 VAL C N   1 
ATOM   11912 C  CA  . VAL C  2  252 ? 75.299  50.286  71.219  1.00 86.14  ?  252 VAL C CA  1 
ATOM   11913 C  C   . VAL C  2  252 ? 75.475  50.634  69.739  1.00 90.10  ?  252 VAL C C   1 
ATOM   11914 O  O   . VAL C  2  252 ? 74.476  50.570  69.000  1.00 95.54  ?  252 VAL C O   1 
ATOM   11915 C  CB  . VAL C  2  252 ? 74.939  48.799  71.396  1.00 78.72  ?  252 VAL C CB  1 
ATOM   11916 C  CG1 . VAL C  2  252 ? 76.013  47.888  70.824  1.00 82.71  ?  252 VAL C CG1 1 
ATOM   11917 C  CG2 . VAL C  2  252 ? 74.663  48.455  72.851  1.00 94.73  ?  252 VAL C CG2 1 
ATOM   11918 N  N   . ASN C  2  253 ? 76.697  50.984  69.328  1.00 85.59  ?  253 ASN C N   1 
ATOM   11919 C  CA  . ASN C  2  253 ? 76.939  51.299  67.928  1.00 78.94  ?  253 ASN C CA  1 
ATOM   11920 C  C   . ASN C  2  253 ? 77.542  50.102  67.207  1.00 89.71  ?  253 ASN C C   1 
ATOM   11921 O  O   . ASN C  2  253 ? 78.617  49.631  67.574  1.00 95.10  ?  253 ASN C O   1 
ATOM   11922 C  CB  . ASN C  2  253 ? 77.855  52.504  67.805  1.00 81.79  ?  253 ASN C CB  1 
ATOM   11923 C  CG  . ASN C  2  253 ? 77.276  53.736  68.450  1.00 89.24  ?  253 ASN C CG  1 
ATOM   11924 O  OD1 . ASN C  2  253 ? 76.232  54.251  68.032  1.00 86.77  ?  253 ASN C OD1 1 
ATOM   11925 N  ND2 . ASN C  2  253 ? 77.933  54.235  69.487  1.00 83.43  ?  253 ASN C ND2 1 
ATOM   11926 N  N   . VAL C  2  254 ? 76.835  49.610  66.184  1.00 93.70  ?  254 VAL C N   1 
ATOM   11927 C  CA  . VAL C  2  254 ? 77.268  48.481  65.369  1.00 78.02  ?  254 VAL C CA  1 
ATOM   11928 C  C   . VAL C  2  254 ? 77.475  49.023  63.963  1.00 81.40  ?  254 VAL C C   1 
ATOM   11929 O  O   . VAL C  2  254 ? 76.501  49.302  63.268  1.00 93.85  ?  254 VAL C O   1 
ATOM   11930 C  CB  . VAL C  2  254 ? 76.212  47.358  65.391  1.00 73.38  ?  254 VAL C CB  1 
ATOM   11931 C  CG1 . VAL C  2  254 ? 76.641  46.186  64.517  1.00 77.33  ?  254 VAL C CG1 1 
ATOM   11932 C  CG2 . VAL C  2  254 ? 75.946  46.898  66.817  1.00 74.05  ?  254 VAL C CG2 1 
ATOM   11933 N  N   . VAL C  2  255 ? 78.738  49.200  63.556  1.00 79.96  ?  255 VAL C N   1 
ATOM   11934 C  CA  . VAL C  2  255 ? 79.070  49.736  62.236  1.00 79.75  ?  255 VAL C CA  1 
ATOM   11935 C  C   . VAL C  2  255 ? 79.304  48.597  61.243  1.00 84.46  ?  255 VAL C C   1 
ATOM   11936 O  O   . VAL C  2  255 ? 80.161  47.745  61.471  1.00 84.95  ?  255 VAL C O   1 
ATOM   11937 C  CB  . VAL C  2  255 ? 80.306  50.663  62.319  1.00 71.01  ?  255 VAL C CB  1 
ATOM   11938 C  CG1 . VAL C  2  255 ? 80.676  51.205  60.944  1.00 66.61  ?  255 VAL C CG1 1 
ATOM   11939 C  CG2 . VAL C  2  255 ? 80.071  51.804  63.301  1.00 67.38  ?  255 VAL C CG2 1 
ATOM   11940 N  N   . LEU C  2  256 ? 78.552  48.590  60.138  1.00 72.63  ?  256 LEU C N   1 
ATOM   11941 C  CA  . LEU C  2  256 ? 78.685  47.569  59.102  1.00 67.86  ?  256 LEU C CA  1 
ATOM   11942 C  C   . LEU C  2  256 ? 79.526  48.144  57.976  1.00 63.64  ?  256 LEU C C   1 
ATOM   11943 O  O   . LEU C  2  256 ? 79.181  49.184  57.426  1.00 79.65  ?  256 LEU C O   1 
ATOM   11944 C  CB  . LEU C  2  256 ? 77.305  47.156  58.564  1.00 70.57  ?  256 LEU C CB  1 
ATOM   11945 C  CG  . LEU C  2  256 ? 76.289  46.674  59.601  1.00 79.15  ?  256 LEU C CG  1 
ATOM   11946 C  CD1 . LEU C  2  256 ? 74.929  46.470  58.964  1.00 70.54  ?  256 LEU C CD1 1 
ATOM   11947 C  CD2 . LEU C  2  256 ? 76.754  45.398  60.272  1.00 89.76  ?  256 LEU C CD2 1 
ATOM   11948 N  N   . HIS C  2  257 ? 80.632  47.486  57.642  1.00 72.49  ?  257 HIS C N   1 
ATOM   11949 C  CA  . HIS C  2  257 ? 81.525  47.945  56.583  1.00 68.73  ?  257 HIS C CA  1 
ATOM   11950 C  C   . HIS C  2  257 ? 81.672  46.761  55.628  1.00 75.76  ?  257 HIS C C   1 
ATOM   11951 O  O   . HIS C  2  257 ? 81.401  45.624  56.009  1.00 73.66  ?  257 HIS C O   1 
ATOM   11952 C  CB  . HIS C  2  257 ? 82.810  48.518  57.205  1.00 68.71  ?  257 HIS C CB  1 
ATOM   11953 C  CG  . HIS C  2  257 ? 83.770  49.115  56.229  1.00 70.03  ?  257 HIS C CG  1 
ATOM   11954 N  ND1 . HIS C  2  257 ? 85.131  49.066  56.445  1.00 65.86  ?  257 HIS C ND1 1 
ATOM   11955 C  CD2 . HIS C  2  257 ? 83.537  49.773  55.072  1.00 74.55  ?  257 HIS C CD2 1 
ATOM   11956 C  CE1 . HIS C  2  257 ? 85.686  49.680  55.415  1.00 60.03  ?  257 HIS C CE1 1 
ATOM   11957 N  NE2 . HIS C  2  257 ? 84.764  50.125  54.564  1.00 81.65  ?  257 HIS C NE2 1 
ATOM   11958 N  N   . GLY C  2  258 ? 82.048  47.038  54.387  1.00 65.14  ?  258 GLY C N   1 
ATOM   11959 C  CA  . GLY C  2  258 ? 82.196  46.003  53.376  1.00 70.62  ?  258 GLY C CA  1 
ATOM   11960 C  C   . GLY C  2  258 ? 81.378  46.228  52.125  1.00 70.60  ?  258 GLY C C   1 
ATOM   11961 O  O   . GLY C  2  258 ? 81.102  47.374  51.771  1.00 73.69  ?  258 GLY C O   1 
ATOM   11962 N  N   . HIS C  2  259 ? 80.981  45.141  51.447  1.00 75.97  ?  259 HIS C N   1 
ATOM   11963 C  CA  . HIS C  2  259 ? 80.205  45.235  50.208  1.00 72.17  ?  259 HIS C CA  1 
ATOM   11964 C  C   . HIS C  2  259 ? 79.052  44.230  50.084  1.00 76.96  ?  259 HIS C C   1 
ATOM   11965 O  O   . HIS C  2  259 ? 78.068  44.528  49.409  1.00 68.69  ?  259 HIS C O   1 
ATOM   11966 C  CB  . HIS C  2  259 ? 81.148  45.051  49.006  1.00 66.12  ?  259 HIS C CB  1 
ATOM   11967 C  CG  . HIS C  2  259 ? 81.918  46.280  48.652  1.00 71.37  ?  259 HIS C CG  1 
ATOM   11968 N  ND1 . HIS C  2  259 ? 82.938  46.748  49.454  1.00 60.19  ?  259 HIS C ND1 1 
ATOM   11969 C  CD2 . HIS C  2  259 ? 81.787  47.101  47.587  1.00 88.78  ?  259 HIS C CD2 1 
ATOM   11970 C  CE1 . HIS C  2  259 ? 83.390  47.840  48.861  1.00 90.63  ?  259 HIS C CE1 1 
ATOM   11971 N  NE2 . HIS C  2  259 ? 82.725  48.092  47.734  1.00 93.32  ?  259 HIS C NE2 1 
ATOM   11972 N  N   . GLU C  2  260 ? 79.190  43.052  50.692  1.00 86.69  ?  260 GLU C N   1 
ATOM   11973 C  CA  . GLU C  2  260 ? 78.149  42.000  50.533  1.00 86.43  ?  260 GLU C CA  1 
ATOM   11974 C  C   . GLU C  2  260 ? 76.854  42.451  51.217  1.00 80.02  ?  260 GLU C C   1 
ATOM   11975 O  O   . GLU C  2  260 ? 76.902  42.766  52.420  1.00 91.65  ?  260 GLU C O   1 
ATOM   11976 C  CB  . GLU C  2  260 ? 78.647  40.676  51.115  1.00 95.14  ?  260 GLU C CB  1 
ATOM   11977 C  CG  . GLU C  2  260 ? 79.689  39.990  50.252  1.00 82.26  ?  260 GLU C CG  1 
ATOM   11978 C  CD  . GLU C  2  260 ? 79.874  38.514  50.559  1.00 107.13 ?  260 GLU C CD  1 
ATOM   11979 O  OE1 . GLU C  2  260 ? 78.939  37.907  51.115  1.00 146.43 ?  260 GLU C OE1 1 
ATOM   11980 O  OE2 . GLU C  2  260 ? 80.953  37.976  50.245  1.00 94.86  ?  260 GLU C OE2 1 
ATOM   11981 N  N   . PRO C  2  261 ? 75.704  42.497  50.508  1.00 64.62  ?  261 PRO C N   1 
ATOM   11982 C  CA  . PRO C  2  261 ? 74.436  42.947  51.099  1.00 74.68  ?  261 PRO C CA  1 
ATOM   11983 C  C   . PRO C  2  261 ? 73.664  41.922  51.935  1.00 77.54  ?  261 PRO C C   1 
ATOM   11984 O  O   . PRO C  2  261 ? 72.832  42.340  52.736  1.00 94.43  ?  261 PRO C O   1 
ATOM   11985 C  CB  . PRO C  2  261 ? 73.621  43.353  49.875  1.00 71.44  ?  261 PRO C CB  1 
ATOM   11986 C  CG  . PRO C  2  261 ? 74.084  42.442  48.810  1.00 63.45  ?  261 PRO C CG  1 
ATOM   11987 C  CD  . PRO C  2  261 ? 75.537  42.159  49.083  1.00 70.08  ?  261 PRO C CD  1 
ATOM   11988 N  N   . LEU C  2  262 ? 73.895  40.607  51.757  1.00 74.45  ?  262 LEU C N   1 
ATOM   11989 C  CA  . LEU C  2  262 ? 73.154  39.605  52.525  1.00 69.22  ?  262 LEU C CA  1 
ATOM   11990 C  C   . LEU C  2  262 ? 73.447  39.689  54.022  1.00 84.90  ?  262 LEU C C   1 
ATOM   11991 O  O   . LEU C  2  262 ? 72.514  39.627  54.823  1.00 90.24  ?  262 LEU C O   1 
ATOM   11992 C  CB  . LEU C  2  262 ? 73.428  38.183  52.013  1.00 75.40  ?  262 LEU C CB  1 
ATOM   11993 C  CG  . LEU C  2  262 ? 72.721  37.051  52.776  1.00 65.72  ?  262 LEU C CG  1 
ATOM   11994 C  CD1 . LEU C  2  262 ? 71.224  37.101  52.576  1.00 70.85  ?  262 LEU C CD1 1 
ATOM   11995 C  CD2 . LEU C  2  262 ? 73.230  35.699  52.341  1.00 80.11  ?  262 LEU C CD2 1 
ATOM   11996 N  N   . LEU C  2  263 ? 74.723  39.823  54.415  1.00 79.64  ?  263 LEU C N   1 
ATOM   11997 C  CA  . LEU C  2  263 ? 75.071  39.921  55.832  1.00 68.41  ?  263 LEU C CA  1 
ATOM   11998 C  C   . LEU C  2  263 ? 74.420  41.156  56.444  1.00 82.29  ?  263 LEU C C   1 
ATOM   11999 O  O   . LEU C  2  263 ? 73.856  41.072  57.531  1.00 88.73  ?  263 LEU C O   1 
ATOM   12000 C  CB  . LEU C  2  263 ? 76.592  40.004  56.006  1.00 76.75  ?  263 LEU C CB  1 
ATOM   12001 C  CG  . LEU C  2  263 ? 77.096  40.394  57.411  1.00 66.15  ?  263 LEU C CG  1 
ATOM   12002 C  CD1 . LEU C  2  263 ? 77.229  39.173  58.300  1.00 63.58  ?  263 LEU C CD1 1 
ATOM   12003 C  CD2 . LEU C  2  263 ? 78.395  41.166  57.323  1.00 73.95  ?  263 LEU C CD2 1 
ATOM   12004 N  N   . SER C  2  264 ? 74.468  42.285  55.735  1.00 81.49  ?  264 SER C N   1 
ATOM   12005 C  CA  . SER C  2  264 ? 73.908  43.538  56.306  1.00 76.06  ?  264 SER C CA  1 
ATOM   12006 C  C   . SER C  2  264 ? 72.378  43.443  56.379  1.00 74.71  ?  264 SER C C   1 
ATOM   12007 O  O   . SER C  2  264 ? 71.812  43.943  57.369  1.00 82.95  ?  264 SER C O   1 
ATOM   12008 C  CB  . SER C  2  264 ? 74.369  44.761  55.549  1.00 75.16  ?  264 SER C CB  1 
ATOM   12009 O  OG  . SER C  2  264 ? 74.230  44.585  54.151  1.00 87.85  ?  264 SER C OG  1 
ATOM   12010 N  N   . GLU C  2  265 ? 71.735  42.811  55.390  1.00 71.20  ?  265 GLU C N   1 
ATOM   12011 C  CA  . GLU C  2  265 ? 70.285  42.634  55.456  1.00 85.05  ?  265 GLU C CA  1 
ATOM   12012 C  C   . GLU C  2  265 ? 69.874  41.774  56.657  1.00 82.18  ?  265 GLU C C   1 
ATOM   12013 O  O   . GLU C  2  265 ? 68.798  41.988  57.214  1.00 90.58  ?  265 GLU C O   1 
ATOM   12014 C  CB  . GLU C  2  265 ? 69.752  42.000  54.160  1.00 83.45  ?  265 GLU C CB  1 
ATOM   12015 C  CG  . GLU C  2  265 ? 69.652  42.969  52.993  1.00 77.70  ?  265 GLU C CG  1 
ATOM   12016 C  CD  . GLU C  2  265 ? 68.455  43.899  53.012  1.00 93.07  ?  265 GLU C CD  1 
ATOM   12017 O  OE1 . GLU C  2  265 ? 67.396  43.514  53.559  1.00 84.10  ?  265 GLU C OE1 1 
ATOM   12018 O  OE2 . GLU C  2  265 ? 68.576  45.020  52.467  1.00 87.91  ?  265 GLU C OE2 1 
ATOM   12019 N  N   . MET C  2  266 ? 70.720  40.805  57.056  1.00 83.58  ?  266 MET C N   1 
ATOM   12020 C  CA  . MET C  2  266 ? 70.424  39.936  58.196  1.00 85.15  ?  266 MET C CA  1 
ATOM   12021 C  C   . MET C  2  266 ? 70.756  40.618  59.515  1.00 85.58  ?  266 MET C C   1 
ATOM   12022 O  O   . MET C  2  266 ? 70.058  40.369  60.494  1.00 99.79  ?  266 MET C O   1 
ATOM   12023 C  CB  . MET C  2  266 ? 71.155  38.586  58.090  1.00 77.34  ?  266 MET C CB  1 
ATOM   12024 C  CG  . MET C  2  266 ? 70.721  37.719  56.914  1.00 81.35  ?  266 MET C CG  1 
ATOM   12025 S  SD  . MET C  2  266 ? 68.955  37.792  56.484  1.00 86.87  ?  266 MET C SD  1 
ATOM   12026 C  CE  . MET C  2  266 ? 68.482  36.136  56.674  1.00 90.01  ?  266 MET C CE  1 
ATOM   12027 N  N   . VAL C  2  267 ? 71.791  41.476  59.562  1.00 77.31  ?  267 VAL C N   1 
ATOM   12028 C  CA  . VAL C  2  267 ? 72.106  42.187  60.806  1.00 70.86  ?  267 VAL C CA  1 
ATOM   12029 C  C   . VAL C  2  267 ? 70.989  43.218  61.087  1.00 89.80  ?  267 VAL C C   1 
ATOM   12030 O  O   . VAL C  2  267 ? 70.723  43.526  62.246  1.00 92.57  ?  267 VAL C O   1 
ATOM   12031 C  CB  . VAL C  2  267 ? 73.517  42.822  60.811  1.00 66.85  ?  267 VAL C CB  1 
ATOM   12032 C  CG1 . VAL C  2  267 ? 73.761  43.603  62.105  1.00 68.07  ?  267 VAL C CG1 1 
ATOM   12033 C  CG2 . VAL C  2  267 ? 74.587  41.753  60.627  1.00 74.11  ?  267 VAL C CG2 1 
ATOM   12034 N  N   . VAL C  2  268 ? 70.312  43.719  60.035  1.00 89.21  ?  268 VAL C N   1 
ATOM   12035 C  CA  . VAL C  2  268 ? 69.202  44.658  60.189  1.00 83.35  ?  268 VAL C CA  1 
ATOM   12036 C  C   . VAL C  2  268 ? 68.033  43.914  60.833  1.00 77.38  ?  268 VAL C C   1 
ATOM   12037 O  O   . VAL C  2  268 ? 67.447  44.408  61.793  1.00 85.70  ?  268 VAL C O   1 
ATOM   12038 C  CB  . VAL C  2  268 ? 68.796  45.282  58.826  1.00 70.34  ?  268 VAL C CB  1 
ATOM   12039 C  CG1 . VAL C  2  268 ? 67.410  45.919  58.891  1.00 71.91  ?  268 VAL C CG1 1 
ATOM   12040 C  CG2 . VAL C  2  268 ? 69.828  46.302  58.371  1.00 82.22  ?  268 VAL C CG2 1 
ATOM   12041 N  N   . GLU C  2  269 ? 67.703  42.723  60.315  1.00 84.85  ?  269 GLU C N   1 
ATOM   12042 C  CA  . GLU C  2  269 ? 66.607  41.921  60.853  1.00 90.41  ?  269 GLU C CA  1 
ATOM   12043 C  C   . GLU C  2  269 ? 66.940  41.459  62.278  1.00 95.41  ?  269 GLU C C   1 
ATOM   12044 O  O   . GLU C  2  269 ? 66.056  41.435  63.138  1.00 95.33  ?  269 GLU C O   1 
ATOM   12045 C  CB  . GLU C  2  269 ? 66.319  40.710  59.939  1.00 87.91  ?  269 GLU C CB  1 
ATOM   12046 C  CG  . GLU C  2  269 ? 64.840  40.418  59.742  1.00 103.99 ?  269 GLU C CG  1 
ATOM   12047 C  CD  . GLU C  2  269 ? 64.541  39.155  58.958  1.00 124.17 ?  269 GLU C CD  1 
ATOM   12048 O  OE1 . GLU C  2  269 ? 65.157  38.959  57.884  1.00 108.11 ?  269 GLU C OE1 1 
ATOM   12049 O  OE2 . GLU C  2  269 ? 63.684  38.363  59.414  1.00 122.65 ?  269 GLU C OE2 1 
ATOM   12050 N  N   . ALA C  2  270 ? 68.211  41.111  62.538  1.00 90.73  ?  270 ALA C N   1 
ATOM   12051 C  CA  . ALA C  2  270 ? 68.648  40.687  63.865  1.00 92.95  ?  270 ALA C CA  1 
ATOM   12052 C  C   . ALA C  2  270 ? 68.446  41.819  64.876  1.00 90.15  ?  270 ALA C C   1 
ATOM   12053 O  O   . ALA C  2  270 ? 68.064  41.554  66.011  1.00 100.86 ?  270 ALA C O   1 
ATOM   12054 C  CB  . ALA C  2  270 ? 70.112  40.278  63.831  1.00 92.43  ?  270 ALA C CB  1 
ATOM   12055 N  N   . ALA C  2  271 ? 68.624  43.072  64.449  1.00 86.92  ?  271 ALA C N   1 
ATOM   12056 C  CA  . ALA C  2  271 ? 68.480  44.226  65.372  1.00 87.16  ?  271 ALA C CA  1 
ATOM   12057 C  C   . ALA C  2  271 ? 67.027  44.365  65.844  1.00 98.58  ?  271 ALA C C   1 
ATOM   12058 O  O   . ALA C  2  271 ? 66.792  45.145  66.786  1.00 92.89  ?  271 ALA C O   1 
ATOM   12059 C  CB  . ALA C  2  271 ? 68.957  45.484  64.695  1.00 75.94  ?  271 ALA C CB  1 
ATOM   12060 N  N   . SER C  2  272 ? 66.094  43.646  65.216  1.00 105.44 ?  272 SER C N   1 
ATOM   12061 C  CA  . SER C  2  272 ? 64.677  43.706  65.571  1.00 97.12  ?  272 SER C CA  1 
ATOM   12062 C  C   . SER C  2  272 ? 64.220  42.482  66.386  1.00 100.89 ?  272 SER C C   1 
ATOM   12063 O  O   . SER C  2  272 ? 63.026  42.353  66.647  1.00 105.80 ?  272 SER C O   1 
ATOM   12064 C  CB  . SER C  2  272 ? 63.827  43.827  64.310  1.00 93.47  ?  272 SER C CB  1 
ATOM   12065 O  OG  . SER C  2  272 ? 64.178  44.981  63.562  1.00 110.08 ?  272 SER C OG  1 
ATOM   12066 N  N   . ASP C  2  273 ? 65.144  41.586  66.787  1.00 104.33 ?  273 ASP C N   1 
ATOM   12067 C  CA  . ASP C  2  273 ? 64.771  40.414  67.573  1.00 106.30 ?  273 ASP C CA  1 
ATOM   12068 C  C   . ASP C  2  273 ? 64.530  40.868  69.014  1.00 110.61 ?  273 ASP C C   1 
ATOM   12069 O  O   . ASP C  2  273 ? 65.433  41.435  69.629  1.00 106.25 ?  273 ASP C O   1 
ATOM   12070 C  CB  . ASP C  2  273 ? 65.875  39.342  67.529  1.00 104.20 ?  273 ASP C CB  1 
ATOM   12071 C  CG  . ASP C  2  273 ? 65.522  38.051  68.250  1.00 119.08 ?  273 ASP C CG  1 
ATOM   12072 O  OD1 . ASP C  2  273 ? 64.318  37.770  68.411  1.00 128.22 ?  273 ASP C OD1 1 
ATOM   12073 O  OD2 . ASP C  2  273 ? 66.452  37.318  68.647  1.00 122.68 ?  273 ASP C OD2 1 
ATOM   12074 N  N   . PRO C  2  274 ? 63.327  40.641  69.577  1.00 111.06 ?  274 PRO C N   1 
ATOM   12075 C  CA  . PRO C  2  274 ? 63.071  41.078  70.961  1.00 103.88 ?  274 PRO C CA  1 
ATOM   12076 C  C   . PRO C  2  274 ? 64.153  40.728  71.988  1.00 102.57 ?  274 PRO C C   1 
ATOM   12077 O  O   . PRO C  2  274 ? 64.446  41.550  72.849  1.00 115.01 ?  274 PRO C O   1 
ATOM   12078 C  CB  . PRO C  2  274 ? 61.748  40.392  71.305  1.00 111.25 ?  274 PRO C CB  1 
ATOM   12079 C  CG  . PRO C  2  274 ? 61.070  40.205  70.011  1.00 100.35 ?  274 PRO C CG  1 
ATOM   12080 C  CD  . PRO C  2  274 ? 62.137  40.000  68.984  1.00 107.87 ?  274 PRO C CD  1 
ATOM   12081 N  N   . GLU C  2  275 ? 64.742  39.525  71.915  1.00 96.82  ?  275 GLU C N   1 
ATOM   12082 C  CA  . GLU C  2  275 ? 65.783  39.129  72.869  1.00 100.17 ?  275 GLU C CA  1 
ATOM   12083 C  C   . GLU C  2  275 ? 66.993  40.061  72.771  1.00 105.70 ?  275 GLU C C   1 
ATOM   12084 O  O   . GLU C  2  275 ? 67.555  40.456  73.791  1.00 101.71 ?  275 GLU C O   1 
ATOM   12085 C  CB  . GLU C  2  275 ? 66.236  37.685  72.614  1.00 109.85 ?  275 GLU C CB  1 
ATOM   12086 C  CG  . GLU C  2  275 ? 65.211  36.632  72.986  1.00 109.35 ?  275 GLU C CG  1 
ATOM   12087 C  CD  . GLU C  2  275 ? 65.573  35.246  72.488  1.00 137.12 ?  275 GLU C CD  1 
ATOM   12088 O  OE1 . GLU C  2  275 ? 66.778  34.902  72.505  1.00 134.92 ?  275 GLU C OE1 1 
ATOM   12089 O  OE2 . GLU C  2  275 ? 64.652  34.506  72.074  1.00 145.47 ?  275 GLU C OE2 1 
ATOM   12090 N  N   . LEU C  2  276 ? 67.353  40.443  71.549  1.00 104.49 ?  276 LEU C N   1 
ATOM   12091 C  CA  . LEU C  2  276 ? 68.565  41.280  71.380  1.00 87.98  ?  276 LEU C CA  1 
ATOM   12092 C  C   . LEU C  2  276 ? 68.259  42.721  71.797  1.00 93.62  ?  276 LEU C C   1 
ATOM   12093 O  O   . LEU C  2  276 ? 69.161  43.373  72.355  1.00 98.81  ?  276 LEU C O   1 
ATOM   12094 C  CB  . LEU C  2  276 ? 69.006  41.209  69.919  1.00 86.82  ?  276 LEU C CB  1 
ATOM   12095 C  CG  . LEU C  2  276 ? 69.817  39.969  69.561  1.00 78.53  ?  276 LEU C CG  1 
ATOM   12096 C  CD1 . LEU C  2  276 ? 70.145  39.974  68.084  1.00 89.77  ?  276 LEU C CD1 1 
ATOM   12097 C  CD2 . LEU C  2  276 ? 71.090  39.899  70.388  1.00 79.87  ?  276 LEU C CD2 1 
ATOM   12098 N  N   . VAL C  2  277 ? 67.032  43.189  71.555  1.00 92.86  ?  277 VAL C N   1 
ATOM   12099 C  CA  . VAL C  2  277 ? 66.711  44.554  71.984  1.00 99.89  ?  277 VAL C CA  1 
ATOM   12100 C  C   . VAL C  2  277 ? 66.758  44.625  73.519  1.00 103.24 ?  277 VAL C C   1 
ATOM   12101 O  O   . VAL C  2  277 ? 67.200  45.635  74.063  1.00 104.34 ?  277 VAL C O   1 
ATOM   12102 C  CB  . VAL C  2  277 ? 65.379  45.116  71.410  1.00 87.18  ?  277 VAL C CB  1 
ATOM   12103 C  CG1 . VAL C  2  277 ? 65.286  44.899  69.903  1.00 96.05  ?  277 VAL C CG1 1 
ATOM   12104 C  CG2 . VAL C  2  277 ? 64.163  44.538  72.126  1.00 106.44 ?  277 VAL C CG2 1 
ATOM   12105 N  N   . GLU C  2  278 ? 66.335  43.549  74.214  1.00 108.54 ?  278 GLU C N   1 
ATOM   12106 C  CA  . GLU C  2  278 ? 66.352  43.501  75.676  1.00 110.05 ?  278 GLU C CA  1 
ATOM   12107 C  C   . GLU C  2  278 ? 67.770  43.311  76.208  1.00 105.21 ?  278 GLU C C   1 
ATOM   12108 O  O   . GLU C  2  278 ? 68.092  43.846  77.266  1.00 108.40 ?  278 GLU C O   1 
ATOM   12109 C  CB  . GLU C  2  278 ? 65.427  42.391  76.202  1.00 113.42 ?  278 GLU C CB  1 
ATOM   12110 C  CG  . GLU C  2  278 ? 63.950  42.684  75.998  1.00 130.30 ?  278 GLU C CG  1 
ATOM   12111 C  CD  . GLU C  2  278 ? 63.486  43.997  76.598  1.00 144.19 ?  278 GLU C CD  1 
ATOM   12112 O  OE1 . GLU C  2  278 ? 63.358  44.069  77.842  1.00 148.11 ?  278 GLU C OE1 1 
ATOM   12113 O  OE2 . GLU C  2  278 ? 63.258  44.955  75.824  1.00 118.63 ?  278 GLU C OE2 1 
ATOM   12114 N  N   . LEU C  2  279 ? 68.622  42.567  75.487  1.00 102.95 ?  279 LEU C N   1 
ATOM   12115 C  CA  . LEU C  2  279 ? 70.007  42.373  75.908  1.00 105.74 ?  279 LEU C CA  1 
ATOM   12116 C  C   . LEU C  2  279 ? 70.744  43.725  75.895  1.00 106.10 ?  279 LEU C C   1 
ATOM   12117 O  O   . LEU C  2  279 ? 71.565  43.982  76.774  1.00 98.14  ?  279 LEU C O   1 
ATOM   12118 C  CB  . LEU C  2  279 ? 70.711  41.370  74.981  1.00 99.68  ?  279 LEU C CB  1 
ATOM   12119 C  CG  . LEU C  2  279 ? 72.174  41.052  75.317  1.00 85.83  ?  279 LEU C CG  1 
ATOM   12120 C  CD1 . LEU C  2  279 ? 72.287  40.238  76.592  1.00 99.73  ?  279 LEU C CD1 1 
ATOM   12121 C  CD2 . LEU C  2  279 ? 72.838  40.312  74.177  1.00 87.06  ?  279 LEU C CD2 1 
ATOM   12122 N  N   . ALA C  2  280 ? 70.437  44.594  74.912  1.00 99.49  ?  280 ALA C N   1 
ATOM   12123 C  CA  . ALA C  2  280 ? 71.048  45.917  74.817  1.00 93.60  ?  280 ALA C CA  1 
ATOM   12124 C  C   . ALA C  2  280 ? 70.710  46.742  76.061  1.00 105.80 ?  280 ALA C C   1 
ATOM   12125 O  O   . ALA C  2  280 ? 71.574  47.441  76.586  1.00 105.28 ?  280 ALA C O   1 
ATOM   12126 C  CB  . ALA C  2  280 ? 70.553  46.633  73.568  1.00 84.66  ?  280 ALA C CB  1 
ATOM   12127 N  N   . LYS C  2  281 ? 69.463  46.645  76.542  1.00 98.15  ?  281 LYS C N   1 
ATOM   12128 C  CA  . LYS C  2  281 ? 69.027  47.367  77.735  1.00 91.83  ?  281 LYS C CA  1 
ATOM   12129 C  C   . LYS C  2  281 ? 69.720  46.773  78.971  1.00 110.18 ?  281 LYS C C   1 
ATOM   12130 O  O   . LYS C  2  281 ? 70.116  47.523  79.860  1.00 116.09 ?  281 LYS C O   1 
ATOM   12131 C  CB  . LYS C  2  281 ? 67.501  47.291  77.897  1.00 101.71 ?  281 LYS C CB  1 
ATOM   12132 C  CG  . LYS C  2  281 ? 66.711  47.632  76.632  1.00 93.23  ?  281 LYS C CG  1 
ATOM   12133 C  CD  . LYS C  2  281 ? 65.893  48.900  76.752  1.00 94.73  ?  281 LYS C CD  1 
ATOM   12134 C  CE  . LYS C  2  281 ? 64.978  49.074  75.565  1.00 104.22 ?  281 LYS C CE  1 
ATOM   12135 N  NZ  . LYS C  2  281 ? 63.760  48.223  75.663  1.00 124.45 ?  281 LYS C NZ  1 
ATOM   12136 N  N   . SER C  2  282 ? 69.883  45.432  79.017  1.00 112.05 ?  282 SER C N   1 
ATOM   12137 C  CA  . SER C  2  282 ? 70.551  44.736  80.125  1.00 105.97 ?  282 SER C CA  1 
ATOM   12138 C  C   . SER C  2  282 ? 71.965  45.275  80.346  1.00 97.15  ?  282 SER C C   1 
ATOM   12139 O  O   . SER C  2  282 ? 72.414  45.371  81.486  1.00 107.73 ?  282 SER C O   1 
ATOM   12140 C  CB  . SER C  2  282 ? 70.650  43.238  79.836  1.00 100.27 ?  282 SER C CB  1 
ATOM   12141 O  OG  . SER C  2  282 ? 69.381  42.623  79.694  1.00 139.72 ?  282 SER C OG  1 
ATOM   12142 N  N   . VAL C  2  283 ? 72.666  45.621  79.256  1.00 102.09 ?  283 VAL C N   1 
ATOM   12143 C  CA  . VAL C  2  283 ? 74.033  46.146  79.326  1.00 101.21 ?  283 VAL C CA  1 
ATOM   12144 C  C   . VAL C  2  283 ? 74.081  47.646  79.710  1.00 106.99 ?  283 VAL C C   1 
ATOM   12145 O  O   . VAL C  2  283 ? 75.142  48.146  80.083  1.00 102.84 ?  283 VAL C O   1 
ATOM   12146 C  CB  . VAL C  2  283 ? 74.789  45.876  78.003  1.00 101.76 ?  283 VAL C CB  1 
ATOM   12147 C  CG1 . VAL C  2  283 ? 76.207  46.429  78.072  1.00 113.81 ?  283 VAL C CG1 1 
ATOM   12148 C  CG2 . VAL C  2  283 ? 74.818  44.381  77.685  1.00 101.19 ?  283 VAL C CG2 1 
ATOM   12149 N  N   . GLY C  2  284 ? 72.951  48.340  79.621  1.00 101.93 ?  284 GLY C N   1 
ATOM   12150 C  CA  . GLY C  2  284 ? 72.867  49.750  79.971  1.00 91.80  ?  284 GLY C CA  1 
ATOM   12151 C  C   . GLY C  2  284 ? 72.871  50.664  78.765  1.00 102.73 ?  284 GLY C C   1 
ATOM   12152 O  O   . GLY C  2  284 ? 73.426  51.764  78.824  1.00 106.26 ?  284 GLY C O   1 
ATOM   12153 N  N   . ALA C  2  285 ? 72.240  50.221  77.667  1.00 102.84 ?  285 ALA C N   1 
ATOM   12154 C  CA  . ALA C  2  285 ? 72.161  50.996  76.430  1.00 97.14  ?  285 ALA C CA  1 
ATOM   12155 C  C   . ALA C  2  285 ? 70.720  51.369  76.115  1.00 105.43 ?  285 ALA C C   1 
ATOM   12156 O  O   . ALA C  2  285 ? 69.793  50.668  76.529  1.00 105.52 ?  285 ALA C O   1 
ATOM   12157 C  CB  . ALA C  2  285 ? 72.737  50.187  75.279  1.00 105.31 ?  285 ALA C CB  1 
ATOM   12158 N  N   . ASP C  2  286 ? 70.533  52.464  75.366  1.00 98.44  ?  286 ASP C N   1 
ATOM   12159 C  CA  . ASP C  2  286 ? 69.199  52.919  74.975  1.00 99.43  ?  286 ASP C CA  1 
ATOM   12160 C  C   . ASP C  2  286 ? 68.589  51.913  73.998  1.00 97.97  ?  286 ASP C C   1 
ATOM   12161 O  O   . ASP C  2  286 ? 67.425  51.535  74.138  1.00 95.90  ?  286 ASP C O   1 
ATOM   12162 C  CB  . ASP C  2  286 ? 69.271  54.307  74.314  1.00 101.96 ?  286 ASP C CB  1 
ATOM   12163 C  CG  . ASP C  2  286 ? 69.790  55.405  75.217  1.00 118.33 ?  286 ASP C CG  1 
ATOM   12164 O  OD1 . ASP C  2  286 ? 69.714  55.241  76.456  1.00 128.07 ?  286 ASP C OD1 1 
ATOM   12165 O  OD2 . ASP C  2  286 ? 70.269  56.433  74.685  1.00 127.02 ?  286 ASP C OD2 1 
ATOM   12166 N  N   . GLY C  2  287 ? 69.384  51.492  73.021  1.00 96.20  ?  287 GLY C N   1 
ATOM   12167 C  CA  . GLY C  2  287 ? 68.963  50.532  72.011  1.00 93.63  ?  287 GLY C CA  1 
ATOM   12168 C  C   . GLY C  2  287 ? 70.120  50.117  71.128  1.00 101.23 ?  287 GLY C C   1 
ATOM   12169 O  O   . GLY C  2  287 ? 71.280  50.255  71.523  1.00 110.35 ?  287 GLY C O   1 
ATOM   12170 N  N   . ILE C  2  288 ? 69.817  49.612  69.922  1.00 92.86  ?  288 ILE C N   1 
ATOM   12171 C  CA  . ILE C  2  288 ? 70.852  49.190  68.979  1.00 84.30  ?  288 ILE C CA  1 
ATOM   12172 C  C   . ILE C  2  288 ? 70.916  50.180  67.822  1.00 84.36  ?  288 ILE C C   1 
ATOM   12173 O  O   . ILE C  2  288 ? 69.992  50.241  67.014  1.00 98.71  ?  288 ILE C O   1 
ATOM   12174 C  CB  . ILE C  2  288 ? 70.627  47.740  68.484  1.00 79.80  ?  288 ILE C CB  1 
ATOM   12175 C  CG1 . ILE C  2  288 ? 70.578  46.752  69.671  1.00 89.92  ?  288 ILE C CG1 1 
ATOM   12176 C  CG2 . ILE C  2  288 ? 71.733  47.341  67.506  1.00 82.46  ?  288 ILE C CG2 1 
ATOM   12177 C  CD1 . ILE C  2  288 ? 69.904  45.430  69.361  1.00 81.86  ?  288 ILE C CD1 1 
ATOM   12178 N  N   . ASN C  2  289 ? 72.004  50.962  67.750  1.00 83.86  ?  289 ASN C N   1 
ATOM   12179 C  CA  . ASN C  2  289 ? 72.202  51.953  66.695  1.00 79.59  ?  289 ASN C CA  1 
ATOM   12180 C  C   . ASN C  2  289 ? 73.029  51.350  65.557  1.00 92.24  ?  289 ASN C C   1 
ATOM   12181 O  O   . ASN C  2  289 ? 74.252  51.248  65.661  1.00 95.97  ?  289 ASN C O   1 
ATOM   12182 C  CB  . ASN C  2  289 ? 72.889  53.196  67.261  1.00 84.06  ?  289 ASN C CB  1 
ATOM   12183 C  CG  . ASN C  2  289 ? 72.981  54.339  66.283  1.00 92.15  ?  289 ASN C CG  1 
ATOM   12184 O  OD1 . ASN C  2  289 ? 74.074  54.799  65.942  1.00 98.41  ?  289 ASN C OD1 1 
ATOM   12185 N  ND2 . ASN C  2  289 ? 71.839  54.840  65.819  1.00 90.20  ?  289 ASN C ND2 1 
ATOM   12186 N  N   . LEU C  2  290 ? 72.333  50.945  64.488  1.00 95.74  ?  290 LEU C N   1 
ATOM   12187 C  CA  . LEU C  2  290 ? 73.010  50.330  63.315  1.00 88.15  ?  290 LEU C CA  1 
ATOM   12188 C  C   . LEU C  2  290 ? 73.496  51.432  62.372  1.00 96.31  ?  290 LEU C C   1 
ATOM   12189 O  O   . LEU C  2  290 ? 72.708  52.354  62.090  1.00 102.43 ?  290 LEU C O   1 
ATOM   12190 C  CB  . LEU C  2  290 ? 72.021  49.404  62.599  1.00 82.47  ?  290 LEU C CB  1 
ATOM   12191 C  CG  . LEU C  2  290 ? 71.878  47.997  63.180  1.00 92.57  ?  290 LEU C CG  1 
ATOM   12192 C  CD1 . LEU C  2  290 ? 71.302  47.033  62.150  1.00 85.84  ?  290 LEU C CD1 1 
ATOM   12193 C  CD2 . LEU C  2  290 ? 73.213  47.489  63.699  1.00 108.26 ?  290 LEU C CD2 1 
ATOM   12194 N  N   . CYS C  2  291 ? 74.741  51.335  61.907  1.00 83.92  ?  291 CYS C N   1 
ATOM   12195 C  CA  . CYS C  2  291 ? 75.315  52.307  60.981  1.00 69.16  ?  291 CYS C CA  1 
ATOM   12196 C  C   . CYS C  2  291 ? 76.013  51.576  59.854  1.00 91.92  ?  291 CYS C C   1 
ATOM   12197 O  O   . CYS C  2  291 ? 76.403  50.422  60.014  1.00 90.38  ?  291 CYS C O   1 
ATOM   12198 C  CB  . CYS C  2  291 ? 76.276  53.243  61.703  1.00 69.53  ?  291 CYS C CB  1 
ATOM   12199 S  SG  . CYS C  2  291 ? 75.547  54.106  63.114  1.00 96.21  ?  291 CYS C SG  1 
ATOM   12200 N  N   . GLY C  2  292 ? 76.171  52.255  58.725  1.00 78.57  ?  292 GLY C N   1 
ATOM   12201 C  CA  . GLY C  2  292 ? 76.819  51.682  57.556  1.00 64.55  ?  292 GLY C CA  1 
ATOM   12202 C  C   . GLY C  2  292 ? 77.993  52.498  57.067  1.00 71.18  ?  292 GLY C C   1 
ATOM   12203 O  O   . GLY C  2  292 ? 78.141  53.660  57.432  1.00 77.04  ?  292 GLY C O   1 
ATOM   12204 N  N   . MET C  2  293 ? 78.840  51.860  56.263  1.00 62.03  ?  293 MET C N   1 
ATOM   12205 C  CA  . MET C  2  293 ? 80.006  52.569  55.685  1.00 61.07  ?  293 MET C CA  1 
ATOM   12206 C  C   . MET C  2  293 ? 80.267  51.986  54.298  1.00 66.78  ?  293 MET C C   1 
ATOM   12207 O  O   . MET C  2  293 ? 80.067  50.771  54.124  1.00 76.64  ?  293 MET C O   1 
ATOM   12208 C  CB  . MET C  2  293 ? 81.247  52.388  56.560  1.00 68.41  ?  293 MET C CB  1 
ATOM   12209 C  CG  . MET C  2  293 ? 81.160  53.122  57.879  1.00 79.94  ?  293 MET C CG  1 
ATOM   12210 S  SD  . MET C  2  293 ? 82.789  53.360  58.617  1.00 79.95  ?  293 MET C SD  1 
ATOM   12211 C  CE  . MET C  2  293 ? 83.031  55.110  58.318  1.00 83.50  ?  293 MET C CE  1 
ATOM   12212 N  N   . CYS C  2  294 ? 80.659  52.832  53.350  1.00 63.08  ?  294 CYS C N   1 
ATOM   12213 C  CA  . CYS C  2  294 ? 80.993  52.356  51.981  1.00 73.33  ?  294 CYS C CA  1 
ATOM   12214 C  C   . CYS C  2  294 ? 79.778  51.652  51.364  1.00 71.17  ?  294 CYS C C   1 
ATOM   12215 O  O   . CYS C  2  294 ? 78.648  51.942  51.800  1.00 76.20  ?  294 CYS C O   1 
ATOM   12216 C  CB  . CYS C  2  294 ? 82.196  51.421  52.015  1.00 71.31  ?  294 CYS C CB  1 
ATOM   12217 S  SG  . CYS C  2  294 ? 83.725  52.251  52.520  1.00 66.39  ?  294 CYS C SG  1 
ATOM   12218 N  N   . CYS C  2  295 ? 80.004  50.757  50.400  1.00 74.32  ?  295 CYS C N   1 
ATOM   12219 C  CA  . CYS C  2  295 ? 78.876  50.101  49.682  1.00 63.53  ?  295 CYS C CA  1 
ATOM   12220 C  C   . CYS C  2  295 ? 77.906  49.442  50.672  1.00 70.84  ?  295 CYS C C   1 
ATOM   12221 O  O   . CYS C  2  295 ? 76.715  49.798  50.635  1.00 83.47  ?  295 CYS C O   1 
ATOM   12222 C  CB  . CYS C  2  295 ? 79.400  49.077  48.682  1.00 84.35  ?  295 CYS C CB  1 
ATOM   12223 S  SG  . CYS C  2  295 ? 80.061  49.834  47.174  1.00 98.33  ?  295 CYS C SG  1 
ATOM   12224 N  N   . THR C  2  296 ? 78.368  48.504  51.496  1.00 72.36  ?  296 THR C N   1 
ATOM   12225 C  CA  . THR C  2  296 ? 77.405  47.783  52.371  1.00 68.95  ?  296 THR C CA  1 
ATOM   12226 C  C   . THR C  2  296 ? 76.499  48.796  53.085  1.00 65.63  ?  296 THR C C   1 
ATOM   12227 O  O   . THR C  2  296 ? 75.340  48.442  53.362  1.00 76.96  ?  296 THR C O   1 
ATOM   12228 C  CB  . THR C  2  296 ? 78.118  46.829  53.336  1.00 71.51  ?  296 THR C CB  1 
ATOM   12229 O  OG1 . THR C  2  296 ? 77.154  45.901  53.834  1.00 80.67  ?  296 THR C OG1 1 
ATOM   12230 C  CG2 . THR C  2  296 ? 78.778  47.548  54.488  1.00 80.33  ?  296 THR C CG2 1 
ATOM   12231 N  N   . GLY C  2  297 ? 76.995  50.010  53.347  1.00 60.22  ?  297 GLY C N   1 
ATOM   12232 C  CA  . GLY C  2  297 ? 76.159  51.002  54.006  1.00 69.17  ?  297 GLY C CA  1 
ATOM   12233 C  C   . GLY C  2  297 ? 75.143  51.587  53.049  1.00 76.45  ?  297 GLY C C   1 
ATOM   12234 O  O   . GLY C  2  297 ? 73.991  51.803  53.426  1.00 86.16  ?  297 GLY C O   1 
ATOM   12235 N  N   . ASN C  2  298 ? 75.560  51.822  51.791  1.00 66.48  ?  298 ASN C N   1 
ATOM   12236 C  CA  . ASN C  2  298 ? 74.677  52.349  50.757  1.00 63.24  ?  298 ASN C CA  1 
ATOM   12237 C  C   . ASN C  2  298 ? 73.547  51.369  50.478  1.00 78.43  ?  298 ASN C C   1 
ATOM   12238 O  O   . ASN C  2  298 ? 72.394  51.777  50.380  1.00 79.34  ?  298 ASN C O   1 
ATOM   12239 C  CB  . ASN C  2  298 ? 75.446  52.586  49.462  1.00 59.52  ?  298 ASN C CB  1 
ATOM   12240 C  CG  . ASN C  2  298 ? 76.227  53.866  49.445  1.00 71.94  ?  298 ASN C CG  1 
ATOM   12241 O  OD1 . ASN C  2  298 ? 75.765  54.909  49.920  1.00 80.40  ?  298 ASN C OD1 1 
ATOM   12242 N  ND2 . ASN C  2  298 ? 77.429  53.827  48.887  1.00 76.52  ?  298 ASN C ND2 1 
ATOM   12243 N  N   . GLU C  2  299 ? 73.873  50.076  50.361  1.00 72.32  ?  299 GLU C N   1 
ATOM   12244 C  CA  . GLU C  2  299 ? 72.877  49.041  50.079  1.00 76.87  ?  299 GLU C CA  1 
ATOM   12245 C  C   . GLU C  2  299 ? 71.797  48.957  51.175  1.00 78.96  ?  299 GLU C C   1 
ATOM   12246 O  O   . GLU C  2  299 ? 70.678  48.530  50.890  1.00 81.82  ?  299 GLU C O   1 
ATOM   12247 C  CB  . GLU C  2  299 ? 73.556  47.663  49.886  1.00 73.64  ?  299 GLU C CB  1 
ATOM   12248 C  CG  . GLU C  2  299 ? 74.548  47.590  48.729  1.00 74.55  ?  299 GLU C CG  1 
ATOM   12249 C  CD  . GLU C  2  299 ? 74.107  46.802  47.509  1.00 93.25  ?  299 GLU C CD  1 
ATOM   12250 O  OE1 . GLU C  2  299 ? 72.929  46.935  47.102  1.00 86.58  ?  299 GLU C OE1 1 
ATOM   12251 O  OE2 . GLU C  2  299 ? 74.949  46.061  46.949  1.00 95.27  ?  299 GLU C OE2 1 
ATOM   12252 N  N   . VAL C  2  300 ? 72.114  49.401  52.396  1.00 70.91  ?  300 VAL C N   1 
ATOM   12253 C  CA  . VAL C  2  300 ? 71.125  49.311  53.515  1.00 80.51  ?  300 VAL C CA  1 
ATOM   12254 C  C   . VAL C  2  300 ? 70.407  50.658  53.675  1.00 88.38  ?  300 VAL C C   1 
ATOM   12255 O  O   . VAL C  2  300 ? 69.220  50.642  54.052  1.00 89.33  ?  300 VAL C O   1 
ATOM   12256 C  CB  . VAL C  2  300 ? 71.764  48.819  54.831  1.00 74.47  ?  300 VAL C CB  1 
ATOM   12257 C  CG1 . VAL C  2  300 ? 72.493  47.499  54.644  1.00 75.01  ?  300 VAL C CG1 1 
ATOM   12258 C  CG2 . VAL C  2  300 ? 72.676  49.853  55.471  1.00 81.15  ?  300 VAL C CG2 1 
ATOM   12259 N  N   . SER C  2  301 ? 71.088  51.774  53.398  1.00 78.67  ?  301 SER C N   1 
ATOM   12260 C  CA  . SER C  2  301 ? 70.448  53.089  53.452  1.00 78.18  ?  301 SER C CA  1 
ATOM   12261 C  C   . SER C  2  301 ? 69.466  53.268  52.297  1.00 74.33  ?  301 SER C C   1 
ATOM   12262 O  O   . SER C  2  301 ? 68.502  54.014  52.428  1.00 79.13  ?  301 SER C O   1 
ATOM   12263 C  CB  . SER C  2  301 ? 71.497  54.193  53.388  1.00 92.39  ?  301 SER C CB  1 
ATOM   12264 O  OG  . SER C  2  301 ? 72.394  54.093  54.480  1.00 108.57 ?  301 SER C OG  1 
ATOM   12265 N  N   . MET C  2  302 ? 69.715  52.605  51.164  1.00 74.40  ?  302 MET C N   1 
ATOM   12266 C  CA  . MET C  2  302 ? 68.842  52.689  50.001  1.00 66.28  ?  302 MET C CA  1 
ATOM   12267 C  C   . MET C  2  302 ? 67.522  51.948  50.240  1.00 73.78  ?  302 MET C C   1 
ATOM   12268 O  O   . MET C  2  302 ? 66.460  52.442  49.856  1.00 77.10  ?  302 MET C O   1 
ATOM   12269 C  CB  . MET C  2  302 ? 69.537  52.058  48.788  1.00 65.90  ?  302 MET C CB  1 
ATOM   12270 C  CG  . MET C  2  302 ? 70.646  52.895  48.214  1.00 62.41  ?  302 MET C CG  1 
ATOM   12271 S  SD  . MET C  2  302 ? 70.059  54.179  47.097  1.00 86.43  ?  302 MET C SD  1 
ATOM   12272 C  CE  . MET C  2  302 ? 69.557  53.182  45.688  1.00 78.44  ?  302 MET C CE  1 
ATOM   12273 N  N   . ARG C  2  303 ? 67.588  50.757  50.861  1.00 79.71  ?  303 ARG C N   1 
ATOM   12274 C  CA  . ARG C  2  303 ? 66.408  49.925  51.101  1.00 77.29  ?  303 ARG C CA  1 
ATOM   12275 C  C   . ARG C  2  303 ? 65.739  50.098  52.458  1.00 77.63  ?  303 ARG C C   1 
ATOM   12276 O  O   . ARG C  2  303 ? 64.523  49.941  52.541  1.00 94.66  ?  303 ARG C O   1 
ATOM   12277 C  CB  . ARG C  2  303 ? 66.768  48.446  50.911  1.00 66.35  ?  303 ARG C CB  1 
ATOM   12278 C  CG  . ARG C  2  303 ? 67.286  48.147  49.520  1.00 67.20  ?  303 ARG C CG  1 
ATOM   12279 C  CD  . ARG C  2  303 ? 67.363  46.664  49.236  1.00 64.00  ?  303 ARG C CD  1 
ATOM   12280 N  NE  . ARG C  2  303 ? 67.823  46.405  47.871  1.00 70.99  ?  303 ARG C NE  1 
ATOM   12281 C  CZ  . ARG C  2  303 ? 69.092  46.454  47.473  1.00 86.92  ?  303 ARG C CZ  1 
ATOM   12282 N  NH1 . ARG C  2  303 ? 70.057  46.751  48.338  1.00 92.95  ?  303 ARG C NH1 1 
ATOM   12283 N  NH2 . ARG C  2  303 ? 69.408  46.208  46.209  1.00 79.74  ?  303 ARG C NH2 1 
ATOM   12284 N  N   . HIS C  2  304 ? 66.502  50.381  53.521  1.00 75.07  ?  304 HIS C N   1 
ATOM   12285 C  CA  . HIS C  2  304 ? 65.922  50.504  54.861  1.00 80.01  ?  304 HIS C CA  1 
ATOM   12286 C  C   . HIS C  2  304 ? 66.212  51.818  55.584  1.00 74.14  ?  304 HIS C C   1 
ATOM   12287 O  O   . HIS C  2  304 ? 65.901  51.938  56.766  1.00 73.43  ?  304 HIS C O   1 
ATOM   12288 C  CB  . HIS C  2  304 ? 66.378  49.317  55.716  1.00 73.85  ?  304 HIS C CB  1 
ATOM   12289 C  CG  . HIS C  2  304 ? 66.146  48.006  55.041  1.00 70.29  ?  304 HIS C CG  1 
ATOM   12290 N  ND1 . HIS C  2  304 ? 64.880  47.613  54.653  1.00 88.87  ?  304 HIS C ND1 1 
ATOM   12291 C  CD2 . HIS C  2  304 ? 67.029  47.052  54.672  1.00 79.73  ?  304 HIS C CD2 1 
ATOM   12292 C  CE1 . HIS C  2  304 ? 65.026  46.431  54.078  1.00 105.45 ?  304 HIS C CE1 1 
ATOM   12293 N  NE2 . HIS C  2  304 ? 66.303  46.052  54.066  1.00 79.02  ?  304 HIS C NE2 1 
ATOM   12294 N  N   . GLY C  2  305 ? 66.781  52.790  54.886  1.00 83.93  ?  305 GLY C N   1 
ATOM   12295 C  CA  . GLY C  2  305 ? 67.081  54.089  55.473  1.00 87.12  ?  305 GLY C CA  1 
ATOM   12296 C  C   . GLY C  2  305 ? 68.052  54.066  56.636  1.00 76.56  ?  305 GLY C C   1 
ATOM   12297 O  O   . GLY C  2  305 ? 68.061  55.000  57.438  1.00 84.48  ?  305 GLY C O   1 
ATOM   12298 N  N   . ILE C  2  306 ? 68.897  53.025  56.740  1.00 85.84  ?  306 ILE C N   1 
ATOM   12299 C  CA  . ILE C  2  306 ? 69.881  52.945  57.824  1.00 82.70  ?  306 ILE C CA  1 
ATOM   12300 C  C   . ILE C  2  306 ? 70.847  54.118  57.683  1.00 79.53  ?  306 ILE C C   1 
ATOM   12301 O  O   . ILE C  2  306 ? 71.212  54.481  56.569  1.00 90.57  ?  306 ILE C O   1 
ATOM   12302 C  CB  . ILE C  2  306 ? 70.604  51.571  57.836  1.00 72.97  ?  306 ILE C CB  1 
ATOM   12303 C  CG1 . ILE C  2  306 ? 69.660  50.446  58.328  1.00 70.78  ?  306 ILE C CG1 1 
ATOM   12304 C  CG2 . ILE C  2  306 ? 71.881  51.617  58.669  1.00 77.12  ?  306 ILE C CG2 1 
ATOM   12305 C  CD1 . ILE C  2  306 ? 69.096  50.565  59.772  1.00 103.03 ?  306 ILE C CD1 1 
ATOM   12306 N  N   . LYS C  2  307 ? 71.224  54.734  58.798  1.00 73.90  ?  307 LYS C N   1 
ATOM   12307 C  CA  . LYS C  2  307 ? 72.100  55.900  58.771  1.00 75.23  ?  307 LYS C CA  1 
ATOM   12308 C  C   . LYS C  2  307 ? 73.519  55.541  58.293  1.00 81.21  ?  307 LYS C C   1 
ATOM   12309 O  O   . LYS C  2  307 ? 73.992  54.436  58.554  1.00 88.53  ?  307 LYS C O   1 
ATOM   12310 C  CB  . LYS C  2  307 ? 72.106  56.572  60.153  1.00 86.58  ?  307 LYS C CB  1 
ATOM   12311 C  CG  . LYS C  2  307 ? 70.703  56.970  60.658  1.00 92.10  ?  307 LYS C CG  1 
ATOM   12312 C  CD  . LYS C  2  307 ? 70.487  56.709  62.160  1.00 101.07 ?  307 LYS C CD  1 
ATOM   12313 C  CE  . LYS C  2  307 ? 70.235  55.255  62.514  1.00 110.40 ?  307 LYS C CE  1 
ATOM   12314 N  NZ  . LYS C  2  307 ? 68.872  54.798  62.124  1.00 117.08 ?  307 LYS C NZ  1 
ATOM   12315 N  N   . ILE C  2  308 ? 74.176  56.466  57.561  1.00 86.08  ?  308 ILE C N   1 
ATOM   12316 C  CA  . ILE C  2  308 ? 75.525  56.265  57.018  1.00 68.40  ?  308 ILE C CA  1 
ATOM   12317 C  C   . ILE C  2  308 ? 76.558  56.936  57.909  1.00 68.81  ?  308 ILE C C   1 
ATOM   12318 O  O   . ILE C  2  308 ? 76.503  58.144  58.101  1.00 77.60  ?  308 ILE C O   1 
ATOM   12319 C  CB  . ILE C  2  308 ? 75.625  56.834  55.576  1.00 77.87  ?  308 ILE C CB  1 
ATOM   12320 C  CG1 . ILE C  2  308 ? 74.678  56.082  54.618  1.00 88.07  ?  308 ILE C CG1 1 
ATOM   12321 C  CG2 . ILE C  2  308 ? 77.073  56.772  55.066  1.00 74.15  ?  308 ILE C CG2 1 
ATOM   12322 C  CD1 . ILE C  2  308 ? 74.242  56.867  53.396  1.00 71.25  ?  308 ILE C CD1 1 
ATOM   12323 N  N   . ALA C  2  309 ? 77.519  56.171  58.422  1.00 75.25  ?  309 ALA C N   1 
ATOM   12324 C  CA  . ALA C  2  309 ? 78.562  56.722  59.278  1.00 74.95  ?  309 ALA C CA  1 
ATOM   12325 C  C   . ALA C  2  309 ? 79.594  57.508  58.473  1.00 70.88  ?  309 ALA C C   1 
ATOM   12326 O  O   . ALA C  2  309 ? 80.038  58.559  58.920  1.00 76.36  ?  309 ALA C O   1 
ATOM   12327 C  CB  . ALA C  2  309 ? 79.244  55.608  60.056  1.00 85.45  ?  309 ALA C CB  1 
ATOM   12328 N  N   . GLY C  2  310 ? 79.970  57.004  57.304  1.00 70.75  ?  310 GLY C N   1 
ATOM   12329 C  CA  . GLY C  2  310 ? 80.957  57.681  56.473  1.00 68.71  ?  310 GLY C CA  1 
ATOM   12330 C  C   . GLY C  2  310 ? 81.461  56.845  55.315  1.00 75.13  ?  310 GLY C C   1 
ATOM   12331 O  O   . GLY C  2  310 ? 81.083  55.680  55.170  1.00 76.72  ?  310 GLY C O   1 
ATOM   12332 N  N   . ASN C  2  311 ? 82.331  57.443  54.487  1.00 71.86  ?  311 ASN C N   1 
ATOM   12333 C  CA  . ASN C  2  311 ? 82.890  56.785  53.307  1.00 72.48  ?  311 ASN C CA  1 
ATOM   12334 C  C   . ASN C  2  311 ? 84.290  56.196  53.549  1.00 71.54  ?  311 ASN C C   1 
ATOM   12335 O  O   . ASN C  2  311 ? 84.803  56.268  54.662  1.00 74.47  ?  311 ASN C O   1 
ATOM   12336 C  CB  . ASN C  2  311 ? 82.863  57.739  52.106  1.00 69.68  ?  311 ASN C CB  1 
ATOM   12337 C  CG  . ASN C  2  311 ? 83.548  59.053  52.334  1.00 79.68  ?  311 ASN C CG  1 
ATOM   12338 O  OD1 . ASN C  2  311 ? 84.299  59.228  53.299  1.00 93.55  ?  311 ASN C OD1 1 
ATOM   12339 N  ND2 . ASN C  2  311 ? 83.300  60.009  51.447  1.00 77.59  ?  311 ASN C ND2 1 
ATOM   12340 N  N   . PHE C  2  312 ? 84.883  55.590  52.509  1.00 76.11  ?  312 PHE C N   1 
ATOM   12341 C  CA  . PHE C  2  312 ? 86.181  54.924  52.541  1.00 76.64  ?  312 PHE C CA  1 
ATOM   12342 C  C   . PHE C  2  312 ? 87.227  55.458  53.554  1.00 74.35  ?  312 PHE C C   1 
ATOM   12343 O  O   . PHE C  2  312 ? 87.536  54.746  54.507  1.00 83.89  ?  312 PHE C O   1 
ATOM   12344 C  CB  . PHE C  2  312 ? 86.795  54.880  51.130  1.00 81.04  ?  312 PHE C CB  1 
ATOM   12345 C  CG  . PHE C  2  312 ? 88.050  54.047  51.062  1.00 67.36  ?  312 PHE C CG  1 
ATOM   12346 C  CD1 . PHE C  2  312 ? 88.030  52.707  51.406  1.00 76.39  ?  312 PHE C CD1 1 
ATOM   12347 C  CD2 . PHE C  2  312 ? 89.252  54.608  50.684  1.00 65.82  ?  312 PHE C CD2 1 
ATOM   12348 C  CE1 . PHE C  2  312 ? 89.188  51.949  51.371  1.00 73.73  ?  312 PHE C CE1 1 
ATOM   12349 C  CE2 . PHE C  2  312 ? 90.405  53.844  50.640  1.00 65.60  ?  312 PHE C CE2 1 
ATOM   12350 C  CZ  . PHE C  2  312 ? 90.368  52.521  50.984  1.00 74.36  ?  312 PHE C CZ  1 
ATOM   12351 N  N   . MET C  2  313 ? 87.793  56.667  53.362  1.00 75.53  ?  313 MET C N   1 
ATOM   12352 C  CA  . MET C  2  313 ? 88.835  57.160  54.275  1.00 62.68  ?  313 MET C CA  1 
ATOM   12353 C  C   . MET C  2  313 ? 88.354  57.531  55.679  1.00 68.57  ?  313 MET C C   1 
ATOM   12354 O  O   . MET C  2  313 ? 89.180  57.863  56.530  1.00 74.81  ?  313 MET C O   1 
ATOM   12355 C  CB  . MET C  2  313 ? 89.562  58.369  53.675  1.00 62.15  ?  313 MET C CB  1 
ATOM   12356 C  CG  . MET C  2  313 ? 90.562  57.977  52.613  1.00 61.14  ?  313 MET C CG  1 
ATOM   12357 S  SD  . MET C  2  313 ? 91.394  59.378  51.844  1.00 81.10  ?  313 MET C SD  1 
ATOM   12358 C  CE  . MET C  2  313 ? 92.766  59.556  52.903  1.00 78.72  ?  313 MET C CE  1 
ATOM   12359 N  N   . GLN C  2  314 ? 87.048  57.441  55.946  1.00 69.01  ?  314 GLN C N   1 
ATOM   12360 C  CA  . GLN C  2  314 ? 86.517  57.752  57.270  1.00 62.35  ?  314 GLN C CA  1 
ATOM   12361 C  C   . GLN C  2  314 ? 86.437  56.481  58.137  1.00 73.11  ?  314 GLN C C   1 
ATOM   12362 O  O   . GLN C  2  314 ? 86.198  56.595  59.337  1.00 74.96  ?  314 GLN C O   1 
ATOM   12363 C  CB  . GLN C  2  314 ? 85.121  58.373  57.169  1.00 64.69  ?  314 GLN C CB  1 
ATOM   12364 C  CG  . GLN C  2  314 ? 85.120  59.776  56.601  1.00 70.32  ?  314 GLN C CG  1 
ATOM   12365 C  CD  . GLN C  2  314 ? 83.840  60.472  56.962  1.00 80.73  ?  314 GLN C CD  1 
ATOM   12366 O  OE1 . GLN C  2  314 ? 82.754  60.045  56.563  1.00 77.66  ?  314 GLN C OE1 1 
ATOM   12367 N  NE2 . GLN C  2  314 ? 83.929  61.544  57.737  1.00 89.79  ?  314 GLN C NE2 1 
ATOM   12368 N  N   . GLN C  2  315 ? 86.621  55.282  57.550  1.00 68.80  ?  315 GLN C N   1 
ATOM   12369 C  CA  . GLN C  2  315 ? 86.530  54.023  58.296  1.00 60.14  ?  315 GLN C CA  1 
ATOM   12370 C  C   . GLN C  2  315 ? 87.441  53.941  59.520  1.00 79.45  ?  315 GLN C C   1 
ATOM   12371 O  O   . GLN C  2  315 ? 87.054  53.325  60.512  1.00 88.71  ?  315 GLN C O   1 
ATOM   12372 C  CB  . GLN C  2  315 ? 86.759  52.819  57.376  1.00 64.36  ?  315 GLN C CB  1 
ATOM   12373 C  CG  . GLN C  2  315 ? 88.170  52.693  56.836  1.00 64.54  ?  315 GLN C CG  1 
ATOM   12374 C  CD  . GLN C  2  315 ? 88.248  51.556  55.859  1.00 62.74  ?  315 GLN C CD  1 
ATOM   12375 O  OE1 . GLN C  2  315 ? 88.591  50.433  56.214  1.00 76.32  ?  315 GLN C OE1 1 
ATOM   12376 N  NE2 . GLN C  2  315 ? 87.915  51.807  54.605  1.00 75.75  ?  315 GLN C NE2 1 
ATOM   12377 N  N   . GLU C  2  316 ? 88.651  54.512  59.457  1.00 82.17  ?  316 GLU C N   1 
ATOM   12378 C  CA  . GLU C  2  316 ? 89.555  54.499  60.645  1.00 77.17  ?  316 GLU C CA  1 
ATOM   12379 C  C   . GLU C  2  316 ? 89.037  55.486  61.697  1.00 84.25  ?  316 GLU C C   1 
ATOM   12380 O  O   . GLU C  2  316 ? 88.994  55.108  62.883  1.00 75.47  ?  316 GLU C O   1 
ATOM   12381 C  CB  . GLU C  2  316 ? 91.016  54.811  60.288  1.00 67.06  ?  316 GLU C CB  1 
ATOM   12382 C  CG  . GLU C  2  316 ? 91.671  53.759  59.412  1.00 85.47  ?  316 GLU C CG  1 
ATOM   12383 C  CD  . GLU C  2  316 ? 93.047  54.150  58.903  1.00 83.62  ?  316 GLU C CD  1 
ATOM   12384 O  OE1 . GLU C  2  316 ? 93.122  55.045  58.039  1.00 78.61  ?  316 GLU C OE1 1 
ATOM   12385 O  OE2 . GLU C  2  316 ? 94.040  53.564  59.376  1.00 85.02  ?  316 GLU C OE2 1 
ATOM   12386 N  N   . LEU C  2  317 ? 88.655  56.696  61.279  1.00 77.86  ?  317 LEU C N   1 
ATOM   12387 C  CA  . LEU C  2  317 ? 88.211  57.711  62.227  1.00 72.85  ?  317 LEU C CA  1 
ATOM   12388 C  C   . LEU C  2  317 ? 86.921  57.307  62.946  1.00 74.20  ?  317 LEU C C   1 
ATOM   12389 O  O   . LEU C  2  317 ? 86.640  57.835  64.018  1.00 81.27  ?  317 LEU C O   1 
ATOM   12390 C  CB  . LEU C  2  317 ? 88.045  59.064  61.532  1.00 69.65  ?  317 LEU C CB  1 
ATOM   12391 C  CG  . LEU C  2  317 ? 89.309  59.621  60.873  1.00 68.24  ?  317 LEU C CG  1 
ATOM   12392 C  CD1 . LEU C  2  317 ? 88.969  60.740  59.936  1.00 75.39  ?  317 LEU C CD1 1 
ATOM   12393 C  CD2 . LEU C  2  317 ? 90.316  60.100  61.905  1.00 77.34  ?  317 LEU C CD2 1 
ATOM   12394 N  N   . ALA C  2  318 ? 86.146  56.364  62.387  1.00 71.85  ?  318 ALA C N   1 
ATOM   12395 C  CA  . ALA C  2  318 ? 84.930  55.893  63.038  1.00 72.75  ?  318 ALA C CA  1 
ATOM   12396 C  C   . ALA C  2  318 ? 85.312  55.179  64.341  1.00 76.57  ?  318 ALA C C   1 
ATOM   12397 O  O   . ALA C  2  318 ? 84.662  55.378  65.366  1.00 80.99  ?  318 ALA C O   1 
ATOM   12398 C  CB  . ALA C  2  318 ? 84.178  54.943  62.119  1.00 72.57  ?  318 ALA C CB  1 
ATOM   12399 N  N   . VAL C  2  319 ? 86.394  54.379  64.309  1.00 81.05  ?  319 VAL C N   1 
ATOM   12400 C  CA  . VAL C  2  319 ? 86.885  53.656  65.488  1.00 95.09  ?  319 VAL C CA  1 
ATOM   12401 C  C   . VAL C  2  319 ? 87.460  54.660  66.514  1.00 94.62  ?  319 VAL C C   1 
ATOM   12402 O  O   . VAL C  2  319 ? 87.266  54.485  67.721  1.00 81.67  ?  319 VAL C O   1 
ATOM   12403 C  CB  . VAL C  2  319 ? 87.933  52.582  65.081  1.00 75.42  ?  319 VAL C CB  1 
ATOM   12404 C  CG1 . VAL C  2  319 ? 88.542  51.904  66.305  1.00 67.47  ?  319 VAL C CG1 1 
ATOM   12405 C  CG2 . VAL C  2  319 ? 87.318  51.544  64.144  1.00 77.12  ?  319 VAL C CG2 1 
ATOM   12406 N  N   . VAL C  2  320 ? 88.139  55.721  66.022  1.00 85.92  ?  320 VAL C N   1 
ATOM   12407 C  CA  . VAL C  2  320 ? 88.738  56.764  66.861  1.00 79.24  ?  320 VAL C CA  1 
ATOM   12408 C  C   . VAL C  2  320 ? 87.678  57.443  67.747  1.00 85.78  ?  320 VAL C C   1 
ATOM   12409 O  O   . VAL C  2  320 ? 88.021  57.904  68.836  1.00 82.63  ?  320 VAL C O   1 
ATOM   12410 C  CB  . VAL C  2  320 ? 89.533  57.790  66.011  1.00 79.32  ?  320 VAL C CB  1 
ATOM   12411 C  CG1 . VAL C  2  320 ? 90.015  58.964  66.860  1.00 90.21  ?  320 VAL C CG1 1 
ATOM   12412 C  CG2 . VAL C  2  320 ? 90.714  57.122  65.311  1.00 67.72  ?  320 VAL C CG2 1 
ATOM   12413 N  N   . THR C  2  321 ? 86.394  57.484  67.320  1.00 81.93  ?  321 THR C N   1 
ATOM   12414 C  CA  . THR C  2  321 ? 85.339  58.076  68.166  1.00 82.00  ?  321 THR C CA  1 
ATOM   12415 C  C   . THR C  2  321 ? 85.250  57.348  69.521  1.00 87.92  ?  321 THR C C   1 
ATOM   12416 O  O   . THR C  2  321 ? 84.755  57.920  70.488  1.00 96.61  ?  321 THR C O   1 
ATOM   12417 C  CB  . THR C  2  321 ? 83.942  58.000  67.509  1.00 77.97  ?  321 THR C CB  1 
ATOM   12418 O  OG1 . THR C  2  321 ? 83.616  56.641  67.220  1.00 85.51  ?  321 THR C OG1 1 
ATOM   12419 C  CG2 . THR C  2  321 ? 83.818  58.854  66.267  1.00 90.93  ?  321 THR C CG2 1 
ATOM   12420 N  N   . GLY C  2  322 ? 85.710  56.098  69.571  1.00 76.09  ?  322 GLY C N   1 
ATOM   12421 C  CA  . GLY C  2  322 ? 85.669  55.297  70.782  1.00 79.75  ?  322 GLY C CA  1 
ATOM   12422 C  C   . GLY C  2  322 ? 84.273  54.814  71.126  1.00 89.14  ?  322 GLY C C   1 
ATOM   12423 O  O   . GLY C  2  322 ? 84.058  54.288  72.219  1.00 102.02 ?  322 GLY C O   1 
ATOM   12424 N  N   . ALA C  2  323 ? 83.315  54.978  70.197  1.00 86.89  ?  323 ALA C N   1 
ATOM   12425 C  CA  . ALA C  2  323 ? 81.927  54.578  70.399  1.00 84.15  ?  323 ALA C CA  1 
ATOM   12426 C  C   . ALA C  2  323 ? 81.524  53.347  69.582  1.00 87.38  ?  323 ALA C C   1 
ATOM   12427 O  O   . ALA C  2  323 ? 80.418  52.846  69.773  1.00 88.06  ?  323 ALA C O   1 
ATOM   12428 C  CB  . ALA C  2  323 ? 81.014  55.740  70.061  1.00 77.46  ?  323 ALA C CB  1 
ATOM   12429 N  N   . VAL C  2  324 ? 82.393  52.852  68.684  1.00 85.85  ?  324 VAL C N   1 
ATOM   12430 C  CA  . VAL C  2  324 ? 82.061  51.674  67.887  1.00 78.54  ?  324 VAL C CA  1 
ATOM   12431 C  C   . VAL C  2  324 ? 82.294  50.449  68.751  1.00 82.69  ?  324 VAL C C   1 
ATOM   12432 O  O   . VAL C  2  324 ? 83.438  50.126  69.059  1.00 88.85  ?  324 VAL C O   1 
ATOM   12433 C  CB  . VAL C  2  324 ? 82.871  51.595  66.571  1.00 76.37  ?  324 VAL C CB  1 
ATOM   12434 C  CG1 . VAL C  2  324 ? 82.531  50.322  65.800  1.00 68.90  ?  324 VAL C CG1 1 
ATOM   12435 C  CG2 . VAL C  2  324 ? 82.622  52.824  65.705  1.00 69.92  ?  324 VAL C CG2 1 
ATOM   12436 N  N   . ASP C  2  325 ? 81.217  49.771  69.153  1.00 88.27  ?  325 ASP C N   1 
ATOM   12437 C  CA  . ASP C  2  325 ? 81.322  48.576  69.984  1.00 80.42  ?  325 ASP C CA  1 
ATOM   12438 C  C   . ASP C  2  325 ? 81.667  47.368  69.113  1.00 85.53  ?  325 ASP C C   1 
ATOM   12439 O  O   . ASP C  2  325 ? 82.537  46.571  69.469  1.00 86.71  ?  325 ASP C O   1 
ATOM   12440 C  CB  . ASP C  2  325 ? 80.017  48.359  70.759  1.00 78.94  ?  325 ASP C CB  1 
ATOM   12441 C  CG  . ASP C  2  325 ? 79.675  49.546  71.636  1.00 90.74  ?  325 ASP C CG  1 
ATOM   12442 O  OD1 . ASP C  2  325 ? 80.395  49.775  72.630  1.00 96.90  ?  325 ASP C OD1 1 
ATOM   12443 O  OD2 . ASP C  2  325 ? 78.701  50.257  71.317  1.00 93.71  ?  325 ASP C OD2 1 
ATOM   12444 N  N   . GLY C  2  326 ? 81.002  47.262  67.969  1.00 83.55  ?  326 GLY C N   1 
ATOM   12445 C  CA  . GLY C  2  326 ? 81.238  46.194  67.009  1.00 73.20  ?  326 GLY C CA  1 
ATOM   12446 C  C   . GLY C  2  326 ? 81.388  46.728  65.598  1.00 79.90  ?  326 GLY C C   1 
ATOM   12447 O  O   . GLY C  2  326 ? 80.550  47.506  65.137  1.00 77.86  ?  326 GLY C O   1 
ATOM   12448 N  N   . LEU C  2  327 ? 82.467  46.323  64.907  1.00 88.34  ?  327 LEU C N   1 
ATOM   12449 C  CA  . LEU C  2  327 ? 82.739  46.724  63.527  1.00 75.47  ?  327 LEU C CA  1 
ATOM   12450 C  C   . LEU C  2  327 ? 82.746  45.448  62.692  1.00 78.60  ?  327 LEU C C   1 
ATOM   12451 O  O   . LEU C  2  327 ? 83.773  44.781  62.582  1.00 81.27  ?  327 LEU C O   1 
ATOM   12452 C  CB  . LEU C  2  327 ? 84.088  47.461  63.431  1.00 65.16  ?  327 LEU C CB  1 
ATOM   12453 C  CG  . LEU C  2  327 ? 84.561  47.887  62.038  1.00 58.43  ?  327 LEU C CG  1 
ATOM   12454 C  CD1 . LEU C  2  327 ? 83.527  48.748  61.330  1.00 62.22  ?  327 LEU C CD1 1 
ATOM   12455 C  CD2 . LEU C  2  327 ? 85.865  48.653  62.131  1.00 59.76  ?  327 LEU C CD2 1 
ATOM   12456 N  N   . ILE C  2  328 ? 81.585  45.093  62.131  1.00 69.62  ?  328 ILE C N   1 
ATOM   12457 C  CA  . ILE C  2  328 ? 81.441  43.873  61.343  1.00 72.41  ?  328 ILE C CA  1 
ATOM   12458 C  C   . ILE C  2  328 ? 81.786  44.139  59.885  1.00 77.46  ?  328 ILE C C   1 
ATOM   12459 O  O   . ILE C  2  328 ? 81.126  44.944  59.232  1.00 92.76  ?  328 ILE C O   1 
ATOM   12460 C  CB  . ILE C  2  328 ? 80.012  43.295  61.493  1.00 73.55  ?  328 ILE C CB  1 
ATOM   12461 C  CG1 . ILE C  2  328 ? 79.627  43.129  62.989  1.00 67.94  ?  328 ILE C CG1 1 
ATOM   12462 C  CG2 . ILE C  2  328 ? 79.905  41.956  60.758  1.00 81.52  ?  328 ILE C CG2 1 
ATOM   12463 C  CD1 . ILE C  2  328 ? 78.143  43.149  63.256  1.00 72.34  ?  328 ILE C CD1 1 
ATOM   12464 N  N   . VAL C  2  329 ? 82.776  43.405  59.366  1.00 71.57  ?  329 VAL C N   1 
ATOM   12465 C  CA  . VAL C  2  329 ? 83.245  43.612  57.966  1.00 78.26  ?  329 VAL C CA  1 
ATOM   12466 C  C   . VAL C  2  329 ? 83.084  42.318  57.164  1.00 80.36  ?  329 VAL C C   1 
ATOM   12467 O  O   . VAL C  2  329 ? 83.102  41.243  57.777  1.00 82.58  ?  329 VAL C O   1 
ATOM   12468 C  CB  . VAL C  2  329 ? 84.707  44.084  57.967  1.00 67.83  ?  329 VAL C CB  1 
ATOM   12469 C  CG1 . VAL C  2  329 ? 84.854  45.439  58.639  1.00 71.44  ?  329 VAL C CG1 1 
ATOM   12470 C  CG2 . VAL C  2  329 ? 85.619  43.063  58.624  1.00 63.50  ?  329 VAL C CG2 1 
ATOM   12471 N  N   . ASP C  2  330 ? 82.914  42.451  55.840  1.00 77.32  ?  330 ASP C N   1 
ATOM   12472 C  CA  . ASP C  2  330 ? 82.737  41.271  54.949  1.00 67.02  ?  330 ASP C CA  1 
ATOM   12473 C  C   . ASP C  2  330 ? 83.904  41.337  53.953  1.00 81.03  ?  330 ASP C C   1 
ATOM   12474 O  O   . ASP C  2  330 ? 84.958  40.752  54.264  1.00 79.12  ?  330 ASP C O   1 
ATOM   12475 C  CB  . ASP C  2  330 ? 81.338  41.226  54.320  1.00 70.32  ?  330 ASP C CB  1 
ATOM   12476 C  CG  . ASP C  2  330 ? 80.927  42.456  53.526  1.00 82.46  ?  330 ASP C CG  1 
ATOM   12477 O  OD1 . ASP C  2  330 ? 81.550  42.722  52.484  1.00 101.90 ?  330 ASP C OD1 1 
ATOM   12478 O  OD2 . ASP C  2  330 ? 79.955  43.116  53.935  1.00 93.81  ?  330 ASP C OD2 1 
ATOM   12479 N  N   . VAL C  2  331 ? 83.748  42.025  52.815  1.00 81.48  ?  331 VAL C N   1 
ATOM   12480 C  CA  . VAL C  2  331 ? 84.850  42.020  51.803  1.00 66.95  ?  331 VAL C CA  1 
ATOM   12481 C  C   . VAL C  2  331 ? 85.047  43.353  51.073  1.00 71.81  ?  331 VAL C C   1 
ATOM   12482 O  O   . VAL C  2  331 ? 84.096  44.155  51.046  1.00 73.94  ?  331 VAL C O   1 
ATOM   12483 C  CB  . VAL C  2  331 ? 84.559  40.906  50.775  1.00 59.58  ?  331 VAL C CB  1 
ATOM   12484 C  CG1 . VAL C  2  331 ? 84.479  39.517  51.386  1.00 71.10  ?  331 VAL C CG1 1 
ATOM   12485 C  CG2 . VAL C  2  331 ? 83.332  41.207  49.940  1.00 70.85  ?  331 VAL C CG2 1 
ATOM   12486 N  N   . GLN C  2  332 ? 86.237  43.567  50.509  1.00 73.88  ?  332 GLN C N   1 
ATOM   12487 C  CA  . GLN C  2  332 ? 86.587  44.747  49.704  1.00 65.33  ?  332 GLN C CA  1 
ATOM   12488 C  C   . GLN C  2  332 ? 86.571  46.090  50.436  1.00 64.91  ?  332 GLN C C   1 
ATOM   12489 O  O   . GLN C  2  332 ? 85.648  46.385  51.190  1.00 74.66  ?  332 GLN C O   1 
ATOM   12490 C  CB  . GLN C  2  332 ? 85.705  44.843  48.447  1.00 62.96  ?  332 GLN C CB  1 
ATOM   12491 C  CG  . GLN C  2  332 ? 85.809  43.642  47.521  1.00 60.36  ?  332 GLN C CG  1 
ATOM   12492 C  CD  . GLN C  2  332 ? 84.652  43.583  46.556  1.00 74.47  ?  332 GLN C CD  1 
ATOM   12493 O  OE1 . GLN C  2  332 ? 84.112  44.612  46.127  1.00 64.06  ?  332 GLN C OE1 1 
ATOM   12494 N  NE2 . GLN C  2  332 ? 84.240  42.374  46.188  1.00 73.16  ?  332 GLN C NE2 1 
ATOM   12495 N  N   . CYS C  2  333 ? 87.603  46.909  50.173  1.00 59.64  ?  333 CYS C N   1 
ATOM   12496 C  CA  . CYS C  2  333 ? 87.791  48.258  50.714  1.00 56.04  ?  333 CYS C CA  1 
ATOM   12497 C  C   . CYS C  2  333 ? 87.871  48.350  52.247  1.00 65.98  ?  333 CYS C C   1 
ATOM   12498 O  O   . CYS C  2  333 ? 87.683  49.434  52.794  1.00 60.55  ?  333 CYS C O   1 
ATOM   12499 C  CB  . CYS C  2  333 ? 86.742  49.209  50.151  1.00 64.00  ?  333 CYS C CB  1 
ATOM   12500 S  SG  . CYS C  2  333 ? 86.608  49.162  48.342  1.00 56.17  ?  333 CYS C SG  1 
ATOM   12501 N  N   . ILE C  2  334 ? 88.194  47.238  52.928  1.00 66.22  ?  334 ILE C N   1 
ATOM   12502 C  CA  . ILE C  2  334 ? 88.368  47.196  54.382  1.00 55.51  ?  334 ILE C CA  1 
ATOM   12503 C  C   . ILE C  2  334 ? 89.877  47.319  54.638  1.00 61.97  ?  334 ILE C C   1 
ATOM   12504 O  O   . ILE C  2  334 ? 90.624  46.366  54.412  1.00 65.86  ?  334 ILE C O   1 
ATOM   12505 C  CB  . ILE C  2  334 ? 87.806  45.878  54.969  1.00 56.83  ?  334 ILE C CB  1 
ATOM   12506 C  CG1 . ILE C  2  334 ? 86.295  45.717  54.652  1.00 68.87  ?  334 ILE C CG1 1 
ATOM   12507 C  CG2 . ILE C  2  334 ? 88.048  45.815  56.469  1.00 51.98  ?  334 ILE C CG2 1 
ATOM   12508 C  CD1 . ILE C  2  334 ? 85.851  44.301  54.443  1.00 60.24  ?  334 ILE C CD1 1 
ATOM   12509 N  N   . MET C  2  335 ? 90.329  48.491  55.080  1.00 57.70  ?  335 MET C N   1 
ATOM   12510 C  CA  . MET C  2  335 ? 91.746  48.740  55.337  1.00 51.45  ?  335 MET C CA  1 
ATOM   12511 C  C   . MET C  2  335 ? 92.287  47.775  56.397  1.00 61.38  ?  335 MET C C   1 
ATOM   12512 O  O   . MET C  2  335 ? 91.771  47.772  57.515  1.00 67.62  ?  335 MET C O   1 
ATOM   12513 C  CB  . MET C  2  335 ? 91.945  50.182  55.821  1.00 62.01  ?  335 MET C CB  1 
ATOM   12514 C  CG  . MET C  2  335 ? 91.650  51.219  54.767  1.00 61.81  ?  335 MET C CG  1 
ATOM   12515 S  SD  . MET C  2  335 ? 92.031  52.880  55.353  1.00 69.11  ?  335 MET C SD  1 
ATOM   12516 C  CE  . MET C  2  335 ? 91.156  53.845  54.174  1.00 67.82  ?  335 MET C CE  1 
ATOM   12517 N  N   . PRO C  2  336 ? 93.324  46.959  56.102  1.00 56.07  ?  336 PRO C N   1 
ATOM   12518 C  CA  . PRO C  2  336 ? 93.840  46.045  57.139  1.00 57.35  ?  336 PRO C CA  1 
ATOM   12519 C  C   . PRO C  2  336 ? 94.308  46.736  58.423  1.00 67.80  ?  336 PRO C C   1 
ATOM   12520 O  O   . PRO C  2  336 ? 94.491  46.061  59.433  1.00 70.05  ?  336 PRO C O   1 
ATOM   12521 C  CB  . PRO C  2  336 ? 95.000  45.323  56.446  1.00 58.60  ?  336 PRO C CB  1 
ATOM   12522 C  CG  . PRO C  2  336 ? 94.796  45.529  55.003  1.00 62.77  ?  336 PRO C CG  1 
ATOM   12523 C  CD  . PRO C  2  336 ? 94.066  46.815  54.836  1.00 61.78  ?  336 PRO C CD  1 
ATOM   12524 N  N   . ALA C  2  337 ? 94.512  48.065  58.397  1.00 61.43  ?  337 ALA C N   1 
ATOM   12525 C  CA  . ALA C  2  337 ? 94.943  48.802  59.582  1.00 63.96  ?  337 ALA C CA  1 
ATOM   12526 C  C   . ALA C  2  337 ? 93.921  48.707  60.720  1.00 69.97  ?  337 ALA C C   1 
ATOM   12527 O  O   . ALA C  2  337 ? 94.295  48.852  61.884  1.00 69.12  ?  337 ALA C O   1 
ATOM   12528 C  CB  . ALA C  2  337 ? 95.171  50.262  59.234  1.00 61.13  ?  337 ALA C CB  1 
ATOM   12529 N  N   . LEU C  2  338 ? 92.636  48.473  60.391  1.00 63.75  ?  338 LEU C N   1 
ATOM   12530 C  CA  . LEU C  2  338 ? 91.571  48.378  61.389  1.00 75.11  ?  338 LEU C CA  1 
ATOM   12531 C  C   . LEU C  2  338 ? 91.839  47.307  62.448  1.00 78.32  ?  338 LEU C C   1 
ATOM   12532 O  O   . LEU C  2  338 ? 91.317  47.419  63.556  1.00 80.86  ?  338 LEU C O   1 
ATOM   12533 C  CB  . LEU C  2  338 ? 90.216  48.115  60.720  1.00 65.40  ?  338 LEU C CB  1 
ATOM   12534 C  CG  . LEU C  2  338 ? 89.672  49.217  59.817  1.00 60.93  ?  338 LEU C CG  1 
ATOM   12535 C  CD1 . LEU C  2  338 ? 88.508  48.708  59.007  1.00 59.88  ?  338 LEU C CD1 1 
ATOM   12536 C  CD2 . LEU C  2  338 ? 89.261  50.442  60.618  1.00 69.76  ?  338 LEU C CD2 1 
ATOM   12537 N  N   . ALA C  2  339 ? 92.632  46.278  62.126  1.00 65.36  ?  339 ALA C N   1 
ATOM   12538 C  CA  . ALA C  2  339 ? 92.948  45.237  63.099  1.00 69.86  ?  339 ALA C CA  1 
ATOM   12539 C  C   . ALA C  2  339 ? 93.890  45.803  64.179  1.00 78.51  ?  339 ALA C C   1 
ATOM   12540 O  O   . ALA C  2  339 ? 93.673  45.566  65.367  1.00 86.08  ?  339 ALA C O   1 
ATOM   12541 C  CB  . ALA C  2  339 ? 93.590  44.051  62.401  1.00 71.15  ?  339 ALA C CB  1 
ATOM   12542 N  N   . LYS C  2  340 ? 94.918  46.566  63.762  1.00 74.35  ?  340 LYS C N   1 
ATOM   12543 C  CA  . LYS C  2  340 ? 95.891  47.187  64.669  1.00 76.40  ?  340 LYS C CA  1 
ATOM   12544 C  C   . LYS C  2  340 ? 95.252  48.368  65.419  1.00 83.86  ?  340 LYS C C   1 
ATOM   12545 O  O   . LYS C  2  340 ? 95.518  48.575  66.604  1.00 88.37  ?  340 LYS C O   1 
ATOM   12546 C  CB  . LYS C  2  340 ? 97.111  47.666  63.858  1.00 71.30  ?  340 LYS C CB  1 
ATOM   12547 C  CG  . LYS C  2  340 ? 98.206  48.354  64.666  1.00 69.85  ?  340 LYS C CG  1 
ATOM   12548 C  CD  . LYS C  2  340 ? 99.356  48.809  63.763  1.00 73.89  ?  340 LYS C CD  1 
ATOM   12549 C  CE  . LYS C  2  340 ? 100.358 49.698  64.462  1.00 76.44  ?  340 LYS C CE  1 
ATOM   12550 N  NZ  . LYS C  2  340 ? 101.299 48.920  65.314  1.00 91.83  ?  340 LYS C NZ  1 
ATOM   12551 N  N   . LEU C  2  341 ? 94.416  49.143  64.723  1.00 77.86  ?  341 LEU C N   1 
ATOM   12552 C  CA  . LEU C  2  341 ? 93.743  50.295  65.315  1.00 79.52  ?  341 LEU C CA  1 
ATOM   12553 C  C   . LEU C  2  341 ? 92.769  49.852  66.411  1.00 78.30  ?  341 LEU C C   1 
ATOM   12554 O  O   . LEU C  2  341 ? 92.796  50.410  67.504  1.00 84.99  ?  341 LEU C O   1 
ATOM   12555 C  CB  . LEU C  2  341 ? 93.001  51.077  64.216  1.00 62.58  ?  341 LEU C CB  1 
ATOM   12556 C  CG  . LEU C  2  341 ? 92.283  52.357  64.639  1.00 63.53  ?  341 LEU C CG  1 
ATOM   12557 C  CD1 . LEU C  2  341 ? 93.265  53.477  64.913  1.00 64.85  ?  341 LEU C CD1 1 
ATOM   12558 C  CD2 . LEU C  2  341 ? 91.320  52.801  63.572  1.00 71.66  ?  341 LEU C CD2 1 
ATOM   12559 N  N   . SER C  2  342 ? 91.919  48.853  66.134  1.00 74.21  ?  342 SER C N   1 
ATOM   12560 C  CA  . SER C  2  342 ? 90.950  48.367  67.119  1.00 66.32  ?  342 SER C CA  1 
ATOM   12561 C  C   . SER C  2  342 ? 91.591  47.893  68.423  1.00 84.96  ?  342 SER C C   1 
ATOM   12562 O  O   . SER C  2  342 ? 90.880  47.733  69.413  1.00 99.72  ?  342 SER C O   1 
ATOM   12563 C  CB  . SER C  2  342 ? 90.114  47.236  66.533  1.00 75.49  ?  342 SER C CB  1 
ATOM   12564 O  OG  . SER C  2  342 ? 89.307  47.696  65.463  1.00 97.22  ?  342 SER C OG  1 
ATOM   12565 N  N   . LYS C  2  343 ? 92.911  47.659  68.438  1.00 78.31  ?  343 LYS C N   1 
ATOM   12566 C  CA  . LYS C  2  343 ? 93.587  47.218  69.650  1.00 83.16  ?  343 LYS C CA  1 
ATOM   12567 C  C   . LYS C  2  343 ? 93.699  48.368  70.656  1.00 87.99  ?  343 LYS C C   1 
ATOM   12568 O  O   . LYS C  2  343 ? 93.608  48.126  71.859  1.00 92.21  ?  343 LYS C O   1 
ATOM   12569 C  CB  . LYS C  2  343 ? 94.964  46.627  69.324  1.00 94.68  ?  343 LYS C CB  1 
ATOM   12570 C  CG  . LYS C  2  343 ? 94.870  45.313  68.558  1.00 91.72  ?  343 LYS C CG  1 
ATOM   12571 C  CD  . LYS C  2  343 ? 96.164  44.517  68.600  1.00 95.84  ?  343 LYS C CD  1 
ATOM   12572 C  CE  . LYS C  2  343 ? 95.984  43.132  68.026  1.00 109.63 ?  343 LYS C CE  1 
ATOM   12573 N  NZ  . LYS C  2  343 ? 95.302  42.209  68.976  1.00 103.61 ?  343 LYS C NZ  1 
ATOM   12574 N  N   . SER C  2  344 ? 93.866  49.615  70.178  1.00 88.12  ?  344 SER C N   1 
ATOM   12575 C  CA  . SER C  2  344 ? 93.962  50.783  71.061  1.00 89.66  ?  344 SER C CA  1 
ATOM   12576 C  C   . SER C  2  344 ? 92.601  51.216  71.643  1.00 93.09  ?  344 SER C C   1 
ATOM   12577 O  O   . SER C  2  344 ? 92.556  52.125  72.472  1.00 96.37  ?  344 SER C O   1 
ATOM   12578 C  CB  . SER C  2  344 ? 94.589  51.954  70.315  1.00 74.94  ?  344 SER C CB  1 
ATOM   12579 O  OG  . SER C  2  344 ? 95.794  51.549  69.688  1.00 96.65  ?  344 SER C OG  1 
ATOM   12580 N  N   . TYR C  2  345 ? 91.503  50.580  71.214  1.00 89.76  ?  345 TYR C N   1 
ATOM   12581 C  CA  . TYR C  2  345 ? 90.160  50.896  71.686  1.00 82.56  ?  345 TYR C CA  1 
ATOM   12582 C  C   . TYR C  2  345 ? 89.440  49.600  72.087  1.00 86.08  ?  345 TYR C C   1 
ATOM   12583 O  O   . TYR C  2  345 ? 89.952  48.505  71.844  1.00 85.00  ?  345 TYR C O   1 
ATOM   12584 C  CB  . TYR C  2  345 ? 89.380  51.628  70.576  1.00 82.63  ?  345 TYR C CB  1 
ATOM   12585 C  CG  . TYR C  2  345 ? 90.056  52.894  70.099  1.00 77.03  ?  345 TYR C CG  1 
ATOM   12586 C  CD1 . TYR C  2  345 ? 89.792  54.115  70.702  1.00 84.31  ?  345 TYR C CD1 1 
ATOM   12587 C  CD2 . TYR C  2  345 ? 90.959  52.871  69.045  1.00 83.54  ?  345 TYR C CD2 1 
ATOM   12588 C  CE1 . TYR C  2  345 ? 90.411  55.282  70.273  1.00 75.56  ?  345 TYR C CE1 1 
ATOM   12589 C  CE2 . TYR C  2  345 ? 91.591  54.030  68.612  1.00 93.88  ?  345 TYR C CE2 1 
ATOM   12590 C  CZ  . TYR C  2  345 ? 91.311  55.236  69.226  1.00 86.46  ?  345 TYR C CZ  1 
ATOM   12591 O  OH  . TYR C  2  345 ? 91.930  56.388  68.800  1.00 90.79  ?  345 TYR C OH  1 
ATOM   12592 N  N   . HIS C  2  346 ? 88.236  49.734  72.648  1.00 90.26  ?  346 HIS C N   1 
ATOM   12593 C  CA  . HIS C  2  346 ? 87.443  48.540  73.048  1.00 98.23  ?  346 HIS C CA  1 
ATOM   12594 C  C   . HIS C  2  346 ? 86.720  47.967  71.827  1.00 100.25 ?  346 HIS C C   1 
ATOM   12595 O  O   . HIS C  2  346 ? 86.079  46.904  71.954  1.00 102.93 ?  346 HIS C O   1 
ATOM   12596 C  CB  . HIS C  2  346 ? 86.433  48.909  74.139  1.00 97.60  ?  346 HIS C CB  1 
ATOM   12597 C  CG  . HIS C  2  346 ? 85.131  49.401  73.602  1.00 92.80  ?  346 HIS C CG  1 
ATOM   12598 N  ND1 . HIS C  2  346 ? 85.017  50.567  72.876  1.00 80.81  ?  346 HIS C ND1 1 
ATOM   12599 C  CD2 . HIS C  2  346 ? 83.897  48.889  73.678  1.00 99.52  ?  346 HIS C CD2 1 
ATOM   12600 C  CE1 . HIS C  2  346 ? 83.750  50.744  72.531  1.00 83.80  ?  346 HIS C CE1 1 
ATOM   12601 N  NE2 . HIS C  2  346 ? 83.054  49.737  73.009  1.00 98.22  ?  346 HIS C NE2 1 
ATOM   12602 N  N   . THR C  2  347 ? 86.828  48.637  70.676  1.00 100.66 ?  347 THR C N   1 
ATOM   12603 C  CA  . THR C  2  347 ? 86.087  48.197  69.462  1.00 79.88  ?  347 THR C CA  1 
ATOM   12604 C  C   . THR C  2  347 ? 86.425  46.739  69.134  1.00 90.56  ?  347 THR C C   1 
ATOM   12605 O  O   . THR C  2  347 ? 87.597  46.355  69.307  1.00 92.80  ?  347 THR C O   1 
ATOM   12606 C  CB  . THR C  2  347 ? 86.388  49.118  68.274  1.00 82.46  ?  347 THR C CB  1 
ATOM   12607 O  OG1 . THR C  2  347 ? 86.074  50.457  68.659  1.00 82.71  ?  347 THR C OG1 1 
ATOM   12608 C  CG2 . THR C  2  347 ? 85.611  48.747  67.030  1.00 93.12  ?  347 THR C CG2 1 
ATOM   12609 N  N   . LYS C  2  348 ? 85.433  45.967  68.680  1.00 91.15  ?  348 LYS C N   1 
ATOM   12610 C  CA  . LYS C  2  348 ? 85.666  44.550  68.292  1.00 86.17  ?  348 LYS C CA  1 
ATOM   12611 C  C   . LYS C  2  348 ? 85.638  44.439  66.764  1.00 96.00  ?  348 LYS C C   1 
ATOM   12612 O  O   . LYS C  2  348 ? 84.551  44.619  66.182  1.00 93.33  ?  348 LYS C O   1 
ATOM   12613 C  CB  . LYS C  2  348 ? 84.595  43.647  68.909  1.00 70.21  ?  348 LYS C CB  1 
ATOM   12614 C  CG  . LYS C  2  348 ? 85.033  42.847  70.128  1.00 99.68  ?  348 LYS C CG  1 
ATOM   12615 C  CD  . LYS C  2  348 ? 83.888  42.127  70.808  1.00 108.19 ?  348 LYS C CD  1 
ATOM   12616 C  CE  . LYS C  2  348 ? 84.094  40.630  70.897  1.00 97.93  ?  348 LYS C CE  1 
ATOM   12617 N  NZ  . LYS C  2  348 ? 82.828  39.919  71.196  1.00 100.77 ?  348 LYS C NZ  1 
ATOM   12618 N  N   . PHE C  2  349 ? 86.789  44.156  66.144  1.00 90.73  ?  349 PHE C N   1 
ATOM   12619 C  CA  . PHE C  2  349 ? 86.863  44.039  64.664  1.00 79.22  ?  349 PHE C CA  1 
ATOM   12620 C  C   . PHE C  2  349 ? 86.490  42.607  64.272  1.00 73.91  ?  349 PHE C C   1 
ATOM   12621 O  O   . PHE C  2  349 ? 87.320  41.701  64.473  1.00 75.65  ?  349 PHE C O   1 
ATOM   12622 C  CB  . PHE C  2  349 ? 88.266  44.405  64.177  1.00 70.19  ?  349 PHE C CB  1 
ATOM   12623 C  CG  . PHE C  2  349 ? 88.387  44.623  62.691  1.00 62.12  ?  349 PHE C CG  1 
ATOM   12624 C  CD1 . PHE C  2  349 ? 87.382  45.261  61.984  1.00 79.33  ?  349 PHE C CD1 1 
ATOM   12625 C  CD2 . PHE C  2  349 ? 89.508  44.194  62.000  1.00 65.37  ?  349 PHE C CD2 1 
ATOM   12626 C  CE1 . PHE C  2  349 ? 87.496  45.464  60.618  1.00 75.12  ?  349 PHE C CE1 1 
ATOM   12627 C  CE2 . PHE C  2  349 ? 89.620  44.396  60.633  1.00 60.39  ?  349 PHE C CE2 1 
ATOM   12628 C  CZ  . PHE C  2  349 ? 88.613  45.030  59.945  1.00 63.55  ?  349 PHE C CZ  1 
ATOM   12629 N  N   . ILE C  2  350 ? 85.286  42.405  63.734  1.00 69.20  ?  350 ILE C N   1 
ATOM   12630 C  CA  . ILE C  2  350 ? 84.821  41.019  63.430  1.00 71.25  ?  350 ILE C CA  1 
ATOM   12631 C  C   . ILE C  2  350 ? 84.832  40.781  61.916  1.00 69.88  ?  350 ILE C C   1 
ATOM   12632 O  O   . ILE C  2  350 ? 84.050  41.447  61.214  1.00 85.53  ?  350 ILE C O   1 
ATOM   12633 C  CB  . ILE C  2  350 ? 83.426  40.776  64.038  1.00 71.72  ?  350 ILE C CB  1 
ATOM   12634 C  CG1 . ILE C  2  350 ? 83.423  41.014  65.550  1.00 74.26  ?  350 ILE C CG1 1 
ATOM   12635 C  CG2 . ILE C  2  350 ? 82.917  39.388  63.682  1.00 72.62  ?  350 ILE C CG2 1 
ATOM   12636 C  CD1 . ILE C  2  350 ? 82.063  41.345  66.119  1.00 71.78  ?  350 ILE C CD1 1 
ATOM   12637 N  N   . THR C  2  351 ? 85.680  39.863  61.441  1.00 66.43  ?  351 THR C N   1 
ATOM   12638 C  CA  . THR C  2  351 ? 85.711  39.511  59.997  1.00 63.57  ?  351 THR C CA  1 
ATOM   12639 C  C   . THR C  2  351 ? 84.740  38.349  59.781  1.00 74.36  ?  351 THR C C   1 
ATOM   12640 O  O   . THR C  2  351 ? 84.684  37.472  60.663  1.00 79.01  ?  351 THR C O   1 
ATOM   12641 C  CB  . THR C  2  351 ? 87.134  39.161  59.547  1.00 57.22  ?  351 THR C CB  1 
ATOM   12642 O  OG1 . THR C  2  351 ? 87.656  38.194  60.458  1.00 76.64  ?  351 THR C OG1 1 
ATOM   12643 C  CG2 . THR C  2  351 ? 88.047  40.366  59.500  1.00 56.46  ?  351 THR C CG2 1 
ATOM   12644 N  N   . THR C  2  352 ? 84.020  38.305  58.655  1.00 75.78  ?  352 THR C N   1 
ATOM   12645 C  CA  . THR C  2  352 ? 82.973  37.255  58.498  1.00 73.04  ?  352 THR C CA  1 
ATOM   12646 C  C   . THR C  2  352 ? 83.136  36.435  57.213  1.00 70.14  ?  352 THR C C   1 
ATOM   12647 O  O   . THR C  2  352 ? 82.632  35.297  57.194  1.00 76.24  ?  352 THR C O   1 
ATOM   12648 C  CB  . THR C  2  352 ? 81.574  37.882  58.531  1.00 69.07  ?  352 THR C CB  1 
ATOM   12649 O  OG1 . THR C  2  352 ? 81.490  38.821  57.459  1.00 81.35  ?  352 THR C OG1 1 
ATOM   12650 C  CG2 . THR C  2  352 ? 81.269  38.574  59.842  1.00 81.04  ?  352 THR C CG2 1 
ATOM   12651 N  N   . SER C  2  353 ? 83.790  36.975  56.182  1.00 65.00  ?  353 SER C N   1 
ATOM   12652 C  CA  . SER C  2  353 ? 83.876  36.266  54.910  1.00 67.23  ?  353 SER C CA  1 
ATOM   12653 C  C   . SER C  2  353 ? 85.176  35.468  54.786  1.00 73.65  ?  353 SER C C   1 
ATOM   12654 O  O   . SER C  2  353 ? 86.248  36.031  55.007  1.00 74.91  ?  353 SER C O   1 
ATOM   12655 C  CB  . SER C  2  353 ? 83.786  37.259  53.757  1.00 75.69  ?  353 SER C CB  1 
ATOM   12656 O  OG  . SER C  2  353 ? 83.665  36.603  52.506  1.00 72.14  ?  353 SER C OG  1 
ATOM   12657 N  N   . PRO C  2  354 ? 85.126  34.172  54.401  1.00 71.21  ?  354 PRO C N   1 
ATOM   12658 C  CA  . PRO C  2  354 ? 86.382  33.426  54.227  1.00 69.95  ?  354 PRO C CA  1 
ATOM   12659 C  C   . PRO C  2  354 ? 87.229  33.956  53.058  1.00 81.35  ?  354 PRO C C   1 
ATOM   12660 O  O   . PRO C  2  354 ? 88.371  33.528  52.888  1.00 80.38  ?  354 PRO C O   1 
ATOM   12661 C  CB  . PRO C  2  354 ? 85.918  31.982  54.012  1.00 64.08  ?  354 PRO C CB  1 
ATOM   12662 C  CG  . PRO C  2  354 ? 84.541  32.082  53.518  1.00 59.49  ?  354 PRO C CG  1 
ATOM   12663 C  CD  . PRO C  2  354 ? 83.951  33.341  54.071  1.00 71.21  ?  354 PRO C CD  1 
ATOM   12664 N  N   . LYS C  2  355 ? 86.676  34.899  52.263  1.00 72.95  ?  355 LYS C N   1 
ATOM   12665 C  CA  . LYS C  2  355 ? 87.374  35.526  51.141  1.00 67.17  ?  355 LYS C CA  1 
ATOM   12666 C  C   . LYS C  2  355 ? 88.314  36.610  51.668  1.00 64.22  ?  355 LYS C C   1 
ATOM   12667 O  O   . LYS C  2  355 ? 89.373  36.834  51.092  1.00 72.65  ?  355 LYS C O   1 
ATOM   12668 C  CB  . LYS C  2  355 ? 86.374  36.181  50.178  1.00 55.03  ?  355 LYS C CB  1 
ATOM   12669 C  CG  . LYS C  2  355 ? 85.314  35.246  49.616  1.00 63.09  ?  355 LYS C CG  1 
ATOM   12670 C  CD  . LYS C  2  355 ? 84.331  36.022  48.750  1.00 66.44  ?  355 LYS C CD  1 
ATOM   12671 C  CE  . LYS C  2  355 ? 83.126  35.213  48.332  1.00 77.07  ?  355 LYS C CE  1 
ATOM   12672 N  NZ  . LYS C  2  355 ? 82.053  36.074  47.756  1.00 97.08  ?  355 LYS C NZ  1 
ATOM   12673 N  N   . ALA C  2  356 ? 87.919  37.301  52.747  1.00 57.82  ?  356 ALA C N   1 
ATOM   12674 C  CA  . ALA C  2  356 ? 88.724  38.360  53.336  1.00 71.28  ?  356 ALA C CA  1 
ATOM   12675 C  C   . ALA C  2  356 ? 89.024  38.088  54.807  1.00 72.50  ?  356 ALA C C   1 
ATOM   12676 O  O   . ALA C  2  356 ? 88.269  38.510  55.684  1.00 75.11  ?  356 ALA C O   1 
ATOM   12677 C  CB  . ALA C  2  356 ? 88.008  39.690  53.197  1.00 78.97  ?  356 ALA C CB  1 
ATOM   12678 N  N   . HIS C  2  357 ? 90.129  37.390  55.074  1.00 67.09  ?  357 HIS C N   1 
ATOM   12679 C  CA  . HIS C  2  357 ? 90.563  37.084  56.433  1.00 61.83  ?  357 HIS C CA  1 
ATOM   12680 C  C   . HIS C  2  357 ? 91.592  38.133  56.818  1.00 66.42  ?  357 HIS C C   1 
ATOM   12681 O  O   . HIS C  2  357 ? 92.543  38.331  56.070  1.00 78.39  ?  357 HIS C O   1 
ATOM   12682 C  CB  . HIS C  2  357 ? 91.239  35.701  56.493  1.00 69.15  ?  357 HIS C CB  1 
ATOM   12683 C  CG  . HIS C  2  357 ? 90.299  34.553  56.671  1.00 71.78  ?  357 HIS C CG  1 
ATOM   12684 N  ND1 . HIS C  2  357 ? 90.493  33.611  57.661  1.00 72.44  ?  357 HIS C ND1 1 
ATOM   12685 C  CD2 . HIS C  2  357 ? 89.194  34.222  55.966  1.00 90.31  ?  357 HIS C CD2 1 
ATOM   12686 C  CE1 . HIS C  2  357 ? 89.504  32.742  57.535  1.00 69.52  ?  357 HIS C CE1 1 
ATOM   12687 N  NE2 . HIS C  2  357 ? 88.697  33.069  56.527  1.00 84.73  ?  357 HIS C NE2 1 
ATOM   12688 N  N   . ILE C  2  358 ? 91.426  38.802  57.962  1.00 71.30  ?  358 ILE C N   1 
ATOM   12689 C  CA  . ILE C  2  358 ? 92.397  39.803  58.400  1.00 66.66  ?  358 ILE C CA  1 
ATOM   12690 C  C   . ILE C  2  358 ? 93.046  39.300  59.685  1.00 65.88  ?  358 ILE C C   1 
ATOM   12691 O  O   . ILE C  2  358 ? 92.342  38.910  60.615  1.00 69.34  ?  358 ILE C O   1 
ATOM   12692 C  CB  . ILE C  2  358 ? 91.747  41.198  58.558  1.00 62.20  ?  358 ILE C CB  1 
ATOM   12693 C  CG1 . ILE C  2  358 ? 91.150  41.670  57.210  1.00 60.47  ?  358 ILE C CG1 1 
ATOM   12694 C  CG2 . ILE C  2  358 ? 92.768  42.208  59.092  1.00 59.95  ?  358 ILE C CG2 1 
ATOM   12695 C  CD1 . ILE C  2  358 ? 90.067  42.697  57.314  1.00 55.25  ?  358 ILE C CD1 1 
ATOM   12696 N  N   . THR C  2  359 ? 94.388  39.273  59.723  1.00 70.64  ?  359 THR C N   1 
ATOM   12697 C  CA  . THR C  2  359 ? 95.132  38.797  60.893  1.00 71.46  ?  359 THR C CA  1 
ATOM   12698 C  C   . THR C  2  359 ? 94.817  39.654  62.117  1.00 71.09  ?  359 THR C C   1 
ATOM   12699 O  O   . THR C  2  359 ? 94.584  40.851  61.976  1.00 82.45  ?  359 THR C O   1 
ATOM   12700 C  CB  . THR C  2  359 ? 96.635  38.782  60.585  1.00 68.49  ?  359 THR C CB  1 
ATOM   12701 O  OG1 . THR C  2  359 ? 96.853  37.994  59.416  1.00 62.21  ?  359 THR C OG1 1 
ATOM   12702 C  CG2 . THR C  2  359 ? 97.464  38.237  61.735  1.00 63.38  ?  359 THR C CG2 1 
ATOM   12703 N  N   . ASP C  2  360 ? 94.807  39.035  63.311  1.00 78.17  ?  360 ASP C N   1 
ATOM   12704 C  CA  . ASP C  2  360 ? 94.524  39.701  64.587  1.00 80.00  ?  360 ASP C CA  1 
ATOM   12705 C  C   . ASP C  2  360 ? 93.149  40.357  64.597  1.00 73.40  ?  360 ASP C C   1 
ATOM   12706 O  O   . ASP C  2  360 ? 93.004  41.506  65.009  1.00 92.23  ?  360 ASP C O   1 
ATOM   12707 C  CB  . ASP C  2  360 ? 95.626  40.714  64.956  1.00 74.29  ?  360 ASP C CB  1 
ATOM   12708 C  CG  . ASP C  2  360 ? 96.965  40.085  65.295  1.00 97.13  ?  360 ASP C CG  1 
ATOM   12709 O  OD1 . ASP C  2  360 ? 97.093  38.845  65.165  1.00 102.01 ?  360 ASP C OD1 1 
ATOM   12710 O  OD2 . ASP C  2  360 ? 97.886  40.832  65.693  1.00 118.78 ?  360 ASP C OD2 1 
ATOM   12711 N  N   . SER C  2  361 ? 92.136  39.619  64.150  1.00 70.75  ?  361 SER C N   1 
ATOM   12712 C  CA  . SER C  2  361 ? 90.762  40.107  64.123  1.00 68.35  ?  361 SER C CA  1 
ATOM   12713 C  C   . SER C  2  361 ? 89.850  38.970  64.549  1.00 70.12  ?  361 SER C C   1 
ATOM   12714 O  O   . SER C  2  361 ? 90.174  37.802  64.324  1.00 75.16  ?  361 SER C O   1 
ATOM   12715 C  CB  . SER C  2  361 ? 90.383  40.604  62.730  1.00 63.87  ?  361 SER C CB  1 
ATOM   12716 O  OG  . SER C  2  361 ? 90.184  39.537  61.816  1.00 66.38  ?  361 SER C OG  1 
ATOM   12717 N  N   . ILE C  2  362 ? 88.719  39.298  65.165  1.00 69.62  ?  362 ILE C N   1 
ATOM   12718 C  CA  . ILE C  2  362 ? 87.781  38.277  65.614  1.00 65.85  ?  362 ILE C CA  1 
ATOM   12719 C  C   . ILE C  2  362 ? 87.151  37.731  64.340  1.00 68.88  ?  362 ILE C C   1 
ATOM   12720 O  O   . ILE C  2  362 ? 86.667  38.516  63.539  1.00 76.93  ?  362 ILE C O   1 
ATOM   12721 C  CB  . ILE C  2  362 ? 86.761  38.873  66.626  1.00 71.44  ?  362 ILE C CB  1 
ATOM   12722 C  CG1 . ILE C  2  362 ? 87.475  39.337  67.932  1.00 69.29  ?  362 ILE C CG1 1 
ATOM   12723 C  CG2 . ILE C  2  362 ? 85.660  37.858  66.936  1.00 68.64  ?  362 ILE C CG2 1 
ATOM   12724 C  CD1 . ILE C  2  362 ? 87.856  40.825  67.993  1.00 78.45  ?  362 ILE C CD1 1 
ATOM   12725 N  N   . TYR C  2  363 ? 87.187  36.412  64.122  1.00 64.89  ?  363 TYR C N   1 
ATOM   12726 C  CA  . TYR C  2  363 ? 86.617  35.837  62.909  1.00 65.89  ?  363 TYR C CA  1 
ATOM   12727 C  C   . TYR C  2  363 ? 85.362  35.047  63.227  1.00 73.62  ?  363 TYR C C   1 
ATOM   12728 O  O   . TYR C  2  363 ? 85.435  33.993  63.854  1.00 85.98  ?  363 TYR C O   1 
ATOM   12729 C  CB  . TYR C  2  363 ? 87.613  34.941  62.162  1.00 70.09  ?  363 TYR C CB  1 
ATOM   12730 C  CG  . TYR C  2  363 ? 87.029  34.335  60.903  1.00 72.20  ?  363 TYR C CG  1 
ATOM   12731 C  CD1 . TYR C  2  363 ? 86.855  35.097  59.758  1.00 77.56  ?  363 TYR C CD1 1 
ATOM   12732 C  CD2 . TYR C  2  363 ? 86.638  33.005  60.865  1.00 75.28  ?  363 TYR C CD2 1 
ATOM   12733 C  CE1 . TYR C  2  363 ? 86.311  34.549  58.603  1.00 80.84  ?  363 TYR C CE1 1 
ATOM   12734 C  CE2 . TYR C  2  363 ? 86.092  32.445  59.717  1.00 66.76  ?  363 TYR C CE2 1 
ATOM   12735 C  CZ  . TYR C  2  363 ? 85.927  33.222  58.587  1.00 71.76  ?  363 TYR C CZ  1 
ATOM   12736 O  OH  . TYR C  2  363 ? 85.386  32.681  57.447  1.00 72.86  ?  363 TYR C OH  1 
ATOM   12737 N  N   . MET C  2  364 ? 84.213  35.540  62.769  1.00 68.01  ?  364 MET C N   1 
ATOM   12738 C  CA  . MET C  2  364 ? 82.945  34.861  62.957  1.00 73.84  ?  364 MET C CA  1 
ATOM   12739 C  C   . MET C  2  364 ? 82.376  34.650  61.569  1.00 75.79  ?  364 MET C C   1 
ATOM   12740 O  O   . MET C  2  364 ? 81.737  35.545  61.027  1.00 76.54  ?  364 MET C O   1 
ATOM   12741 C  CB  . MET C  2  364 ? 81.990  35.708  63.796  1.00 73.06  ?  364 MET C CB  1 
ATOM   12742 C  CG  . MET C  2  364 ? 82.372  35.778  65.248  1.00 76.27  ?  364 MET C CG  1 
ATOM   12743 S  SD  . MET C  2  364 ? 81.137  36.693  66.209  1.00 91.68  ?  364 MET C SD  1 
ATOM   12744 C  CE  . MET C  2  364 ? 82.172  37.867  67.015  1.00 103.66 ?  364 MET C CE  1 
ATOM   12745 N  N   . GLU C  2  365 ? 82.626  33.481  60.977  1.00 80.49  ?  365 GLU C N   1 
ATOM   12746 C  CA  . GLU C  2  365 ? 82.151  33.173  59.630  1.00 83.90  ?  365 GLU C CA  1 
ATOM   12747 C  C   . GLU C  2  365 ? 80.636  33.307  59.521  1.00 74.96  ?  365 GLU C C   1 
ATOM   12748 O  O   . GLU C  2  365 ? 79.918  32.882  60.421  1.00 82.39  ?  365 GLU C O   1 
ATOM   12749 C  CB  . GLU C  2  365 ? 82.577  31.753  59.238  1.00 97.49  ?  365 GLU C CB  1 
ATOM   12750 C  CG  . GLU C  2  365 ? 82.359  31.429  57.775  1.00 85.96  ?  365 GLU C CG  1 
ATOM   12751 C  CD  . GLU C  2  365 ? 82.976  30.107  57.374  1.00 96.87  ?  365 GLU C CD  1 
ATOM   12752 O  OE1 . GLU C  2  365 ? 84.221  30.043  57.260  1.00 105.58 ?  365 GLU C OE1 1 
ATOM   12753 O  OE2 . GLU C  2  365 ? 82.215  29.131  57.180  1.00 120.16 ?  365 GLU C OE2 1 
ATOM   12754 N  N   . PHE C  2  366 ? 80.152  33.902  58.428  1.00 67.86  ?  366 PHE C N   1 
ATOM   12755 C  CA  . PHE C  2  366 ? 78.721  34.078  58.219  1.00 71.82  ?  366 PHE C CA  1 
ATOM   12756 C  C   . PHE C  2  366 ? 78.151  32.813  57.587  1.00 76.27  ?  366 PHE C C   1 
ATOM   12757 O  O   . PHE C  2  366 ? 78.392  32.563  56.409  1.00 85.86  ?  366 PHE C O   1 
ATOM   12758 C  CB  . PHE C  2  366 ? 78.467  35.302  57.322  1.00 68.10  ?  366 PHE C CB  1 
ATOM   12759 C  CG  . PHE C  2  366 ? 77.020  35.595  57.012  1.00 62.23  ?  366 PHE C CG  1 
ATOM   12760 C  CD1 . PHE C  2  366 ? 76.087  35.704  58.024  1.00 74.19  ?  366 PHE C CD1 1 
ATOM   12761 C  CD2 . PHE C  2  366 ? 76.605  35.809  55.713  1.00 61.39  ?  366 PHE C CD2 1 
ATOM   12762 C  CE1 . PHE C  2  366 ? 74.762  35.990  57.736  1.00 84.88  ?  366 PHE C CE1 1 
ATOM   12763 C  CE2 . PHE C  2  366 ? 75.280  36.098  55.429  1.00 62.16  ?  366 PHE C CE2 1 
ATOM   12764 C  CZ  . PHE C  2  366 ? 74.366  36.187  56.440  1.00 76.28  ?  366 PHE C CZ  1 
ATOM   12765 N  N   . ASP C  2  367 ? 77.421  32.000  58.365  1.00 77.42  ?  367 ASP C N   1 
ATOM   12766 C  CA  . ASP C  2  367 ? 76.841  30.763  57.847  1.00 78.99  ?  367 ASP C CA  1 
ATOM   12767 C  C   . ASP C  2  367 ? 75.716  31.095  56.878  1.00 83.11  ?  367 ASP C C   1 
ATOM   12768 O  O   . ASP C  2  367 ? 74.662  31.570  57.286  1.00 90.28  ?  367 ASP C O   1 
ATOM   12769 C  CB  . ASP C  2  367 ? 76.325  29.868  58.991  1.00 81.22  ?  367 ASP C CB  1 
ATOM   12770 C  CG  . ASP C  2  367 ? 75.837  28.498  58.551  1.00 96.21  ?  367 ASP C CG  1 
ATOM   12771 O  OD1 . ASP C  2  367 ? 76.170  28.083  57.421  1.00 93.24  ?  367 ASP C OD1 1 
ATOM   12772 O  OD2 . ASP C  2  367 ? 75.118  27.841  59.340  1.00 85.62  ?  367 ASP C OD2 1 
ATOM   12773 N  N   . GLU C  2  368 ? 75.923  30.805  55.594  1.00 92.56  ?  368 GLU C N   1 
ATOM   12774 C  CA  . GLU C  2  368 ? 74.898  31.123  54.565  1.00 77.78  ?  368 GLU C CA  1 
ATOM   12775 C  C   . GLU C  2  368 ? 73.743  30.118  54.646  1.00 91.61  ?  368 GLU C C   1 
ATOM   12776 O  O   . GLU C  2  368 ? 72.676  30.413  54.081  1.00 94.57  ?  368 GLU C O   1 
ATOM   12777 C  CB  . GLU C  2  368 ? 75.534  31.121  53.174  1.00 98.03  ?  368 GLU C CB  1 
ATOM   12778 C  CG  . GLU C  2  368 ? 76.227  29.815  52.831  1.00 120.37 ?  368 GLU C CG  1 
ATOM   12779 C  CD  . GLU C  2  368 ? 77.623  29.667  53.411  1.00 115.68 ?  368 GLU C CD  1 
ATOM   12780 O  OE1 . GLU C  2  368 ? 78.296  30.699  53.598  1.00 113.35 ?  368 GLU C OE1 1 
ATOM   12781 O  OE2 . GLU C  2  368 ? 78.032  28.519  53.676  1.00 109.00 ?  368 GLU C OE2 1 
ATOM   12782 N  N   . GLU C  2  369 ? 73.951  28.977  55.309  1.00 92.11  ?  369 GLU C N   1 
ATOM   12783 C  CA  . GLU C  2  369 ? 72.884  27.985  55.471  1.00 104.46 ?  369 GLU C CA  1 
ATOM   12784 C  C   . GLU C  2  369 ? 71.841  28.510  56.468  1.00 100.77 ?  369 GLU C C   1 
ATOM   12785 O  O   . GLU C  2  369 ? 70.645  28.423  56.202  1.00 110.63 ?  369 GLU C O   1 
ATOM   12786 C  CB  . GLU C  2  369 ? 73.455  26.648  55.968  1.00 122.76 ?  369 GLU C CB  1 
ATOM   12787 C  CG  . GLU C  2  369 ? 74.309  25.923  54.944  1.00 120.75 ?  369 GLU C CG  1 
ATOM   12788 C  CD  . GLU C  2  369 ? 74.896  24.618  55.443  1.00 122.64 ?  369 GLU C CD  1 
ATOM   12789 O  OE1 . GLU C  2  369 ? 75.005  24.443  56.679  1.00 120.82 ?  369 GLU C OE1 1 
ATOM   12790 O  OE2 . GLU C  2  369 ? 75.251  23.768  54.596  1.00 136.08 ?  369 GLU C OE2 1 
ATOM   12791 N  N   . ASN C  2  370 ? 72.297  29.054  57.611  1.00 96.30  ?  370 ASN C N   1 
ATOM   12792 C  CA  . ASN C  2  370 ? 71.441  29.642  58.649  1.00 93.98  ?  370 ASN C CA  1 
ATOM   12793 C  C   . ASN C  2  370 ? 71.863  31.115  58.731  1.00 91.44  ?  370 ASN C C   1 
ATOM   12794 O  O   . ASN C  2  370 ? 72.622  31.489  59.625  1.00 90.38  ?  370 ASN C O   1 
ATOM   12795 C  CB  . ASN C  2  370 ? 71.664  28.945  60.000  1.00 101.13 ?  370 ASN C CB  1 
ATOM   12796 C  CG  . ASN C  2  370 ? 71.382  27.462  59.985  1.00 123.65 ?  370 ASN C CG  1 
ATOM   12797 O  OD1 . ASN C  2  370 ? 70.555  26.970  59.210  1.00 133.63 ?  370 ASN C OD1 1 
ATOM   12798 N  ND2 . ASN C  2  370 ? 72.058  26.711  60.848  1.00 133.56 ?  370 ASN C ND2 1 
ATOM   12799 N  N   . PRO C  2  371 ? 71.445  31.962  57.770  1.00 89.48  ?  371 PRO C N   1 
ATOM   12800 C  CA  . PRO C  2  371 ? 71.909  33.357  57.779  1.00 82.39  ?  371 PRO C CA  1 
ATOM   12801 C  C   . PRO C  2  371 ? 71.429  34.226  58.940  1.00 88.74  ?  371 PRO C C   1 
ATOM   12802 O  O   . PRO C  2  371 ? 72.242  34.933  59.537  1.00 82.28  ?  371 PRO C O   1 
ATOM   12803 C  CB  . PRO C  2  371 ? 71.438  33.903  56.424  1.00 81.87  ?  371 PRO C CB  1 
ATOM   12804 C  CG  . PRO C  2  371 ? 70.978  32.738  55.639  1.00 86.90  ?  371 PRO C CG  1 
ATOM   12805 C  CD  . PRO C  2  371 ? 70.579  31.693  56.607  1.00 80.51  ?  371 PRO C CD  1 
ATOM   12806 N  N   . LEU C  2  372 ? 70.128  34.200  59.256  1.00 95.23  ?  372 LEU C N   1 
ATOM   12807 C  CA  . LEU C  2  372 ? 69.603  35.025  60.341  1.00 87.57  ?  372 LEU C CA  1 
ATOM   12808 C  C   . LEU C  2  372 ? 70.193  34.615  61.686  1.00 89.93  ?  372 LEU C C   1 
ATOM   12809 O  O   . LEU C  2  372 ? 70.557  35.485  62.476  1.00 91.92  ?  372 LEU C O   1 
ATOM   12810 C  CB  . LEU C  2  372 ? 68.068  34.972  60.370  1.00 94.47  ?  372 LEU C CB  1 
ATOM   12811 C  CG  . LEU C  2  372 ? 67.355  35.907  61.350  1.00 84.46  ?  372 LEU C CG  1 
ATOM   12812 C  CD1 . LEU C  2  372 ? 67.836  37.353  61.224  1.00 76.20  ?  372 LEU C CD1 1 
ATOM   12813 C  CD2 . LEU C  2  372 ? 65.860  35.844  61.142  1.00 89.76  ?  372 LEU C CD2 1 
ATOM   12814 N  N   . ASP C  2  373 ? 70.317  33.306  61.944  1.00 88.29  ?  373 ASP C N   1 
ATOM   12815 C  CA  . ASP C  2  373 ? 70.892  32.829  63.204  1.00 86.95  ?  373 ASP C CA  1 
ATOM   12816 C  C   . ASP C  2  373 ? 72.357  33.254  63.305  1.00 85.64  ?  373 ASP C C   1 
ATOM   12817 O  O   . ASP C  2  373 ? 72.806  33.661  64.374  1.00 87.24  ?  373 ASP C O   1 
ATOM   12818 C  CB  . ASP C  2  373 ? 70.793  31.299  63.310  1.00 99.37  ?  373 ASP C CB  1 
ATOM   12819 C  CG  . ASP C  2  373 ? 69.379  30.755  63.345  1.00 117.54 ?  373 ASP C CG  1 
ATOM   12820 O  OD1 . ASP C  2  373 ? 68.502  31.413  63.959  1.00 104.19 ?  373 ASP C OD1 1 
ATOM   12821 O  OD2 . ASP C  2  373 ? 69.147  29.667  62.767  1.00 126.13 ?  373 ASP C OD2 1 
ATOM   12822 N  N   . SER C  2  374 ? 73.100  33.164  62.193  1.00 82.15  ?  374 SER C N   1 
ATOM   12823 C  CA  . SER C  2  374 ? 74.506  33.554  62.163  1.00 76.35  ?  374 SER C CA  1 
ATOM   12824 C  C   . SER C  2  374 ? 74.650  35.052  62.426  1.00 84.59  ?  374 SER C C   1 
ATOM   12825 O  O   . SER C  2  374 ? 75.563  35.464  63.138  1.00 89.28  ?  374 SER C O   1 
ATOM   12826 C  CB  . SER C  2  374 ? 75.116  33.212  60.809  1.00 70.11  ?  374 SER C CB  1 
ATOM   12827 O  OG  . SER C  2  374 ? 76.532  33.221  60.856  1.00 77.52  ?  374 SER C OG  1 
ATOM   12828 N  N   . ALA C  2  375 ? 73.750  35.867  61.851  1.00 85.40  ?  375 ALA C N   1 
ATOM   12829 C  CA  . ALA C  2  375 ? 73.771  37.314  62.038  1.00 90.39  ?  375 ALA C CA  1 
ATOM   12830 C  C   . ALA C  2  375 ? 73.485  37.681  63.491  1.00 91.67  ?  375 ALA C C   1 
ATOM   12831 O  O   . ALA C  2  375 ? 74.095  38.611  64.018  1.00 95.97  ?  375 ALA C O   1 
ATOM   12832 C  CB  . ALA C  2  375 ? 72.744  37.968  61.133  1.00 87.97  ?  375 ALA C CB  1 
ATOM   12833 N  N   . LYS C  2  376 ? 72.562  36.959  64.140  1.00 79.59  ?  376 LYS C N   1 
ATOM   12834 C  CA  . LYS C  2  376 ? 72.224  37.218  65.539  1.00 87.37  ?  376 LYS C CA  1 
ATOM   12835 C  C   . LYS C  2  376 ? 73.420  36.908  66.453  1.00 94.88  ?  376 LYS C C   1 
ATOM   12836 O  O   . LYS C  2  376 ? 73.637  37.623  67.430  1.00 91.90  ?  376 LYS C O   1 
ATOM   12837 C  CB  . LYS C  2  376 ? 71.000  36.391  65.969  1.00 81.35  ?  376 LYS C CB  1 
ATOM   12838 C  CG  . LYS C  2  376 ? 69.685  36.853  65.349  1.00 85.56  ?  376 LYS C CG  1 
ATOM   12839 C  CD  . LYS C  2  376 ? 68.469  36.309  66.103  1.00 99.97  ?  376 LYS C CD  1 
ATOM   12840 C  CE  . LYS C  2  376 ? 67.258  36.106  65.221  1.00 93.28  ?  376 LYS C CE  1 
ATOM   12841 N  NZ  . LYS C  2  376 ? 67.204  34.729  64.659  1.00 104.79 ?  376 LYS C NZ  1 
ATOM   12842 N  N   . LYS C  2  377 ? 74.197  35.857  66.142  1.00 87.05  ?  377 LYS C N   1 
ATOM   12843 C  CA  . LYS C  2  377 ? 75.356  35.493  66.958  1.00 86.95  ?  377 LYS C CA  1 
ATOM   12844 C  C   . LYS C  2  377 ? 76.433  36.573  66.909  1.00 84.49  ?  377 LYS C C   1 
ATOM   12845 O  O   . LYS C  2  377 ? 77.087  36.834  67.919  1.00 92.33  ?  377 LYS C O   1 
ATOM   12846 C  CB  . LYS C  2  377 ? 75.952  34.152  66.499  1.00 76.55  ?  377 LYS C CB  1 
ATOM   12847 C  CG  . LYS C  2  377 ? 75.069  32.954  66.822  1.00 96.29  ?  377 LYS C CG  1 
ATOM   12848 C  CD  . LYS C  2  377 ? 75.845  31.636  66.767  1.00 106.38 ?  377 LYS C CD  1 
ATOM   12849 C  CE  . LYS C  2  377 ? 75.066  30.498  66.145  1.00 107.98 ?  377 LYS C CE  1 
ATOM   12850 N  NZ  . LYS C  2  377 ? 74.004  29.974  67.047  1.00 104.06 ?  377 LYS C NZ  1 
ATOM   12851 N  N   . ILE C  2  378 ? 76.620  37.199  65.742  1.00 88.50  ?  378 ILE C N   1 
ATOM   12852 C  CA  . ILE C  2  378 ? 77.626  38.244  65.575  1.00 90.47  ?  378 ILE C CA  1 
ATOM   12853 C  C   . ILE C  2  378 ? 77.147  39.526  66.248  1.00 83.69  ?  378 ILE C C   1 
ATOM   12854 O  O   . ILE C  2  378 ? 77.912  40.167  66.965  1.00 89.70  ?  378 ILE C O   1 
ATOM   12855 C  CB  . ILE C  2  378 ? 77.961  38.456  64.071  1.00 74.76  ?  378 ILE C CB  1 
ATOM   12856 C  CG1 . ILE C  2  378 ? 78.581  37.172  63.461  1.00 72.37  ?  378 ILE C CG1 1 
ATOM   12857 C  CG2 . ILE C  2  378 ? 78.914  39.641  63.897  1.00 67.78  ?  378 ILE C CG2 1 
ATOM   12858 C  CD1 . ILE C  2  378 ? 78.416  37.035  61.970  1.00 75.59  ?  378 ILE C CD1 1 
ATOM   12859 N  N   . LEU C  2  379 ? 75.882  39.893  66.033  1.00 81.57  ?  379 LEU C N   1 
ATOM   12860 C  CA  . LEU C  2  379 ? 75.324  41.098  66.637  1.00 82.76  ?  379 LEU C CA  1 
ATOM   12861 C  C   . LEU C  2  379 ? 75.315  41.010  68.171  1.00 94.17  ?  379 LEU C C   1 
ATOM   12862 O  O   . LEU C  2  379 ? 75.518  42.024  68.836  1.00 96.14  ?  379 LEU C O   1 
ATOM   12863 C  CB  . LEU C  2  379 ? 73.911  41.351  66.093  1.00 77.74  ?  379 LEU C CB  1 
ATOM   12864 C  CG  . LEU C  2  379 ? 73.181  42.575  66.632  1.00 89.35  ?  379 LEU C CG  1 
ATOM   12865 C  CD1 . LEU C  2  379 ? 73.965  43.854  66.382  1.00 75.82  ?  379 LEU C CD1 1 
ATOM   12866 C  CD2 . LEU C  2  379 ? 71.818  42.689  66.018  1.00 79.21  ?  379 LEU C CD2 1 
ATOM   12867 N  N   . LYS C  2  380 ? 75.100  39.809  68.733  1.00 92.43  ?  380 LYS C N   1 
ATOM   12868 C  CA  . LYS C  2  380 ? 75.101  39.623  70.184  1.00 89.76  ?  380 LYS C CA  1 
ATOM   12869 C  C   . LYS C  2  380 ? 76.470  39.974  70.768  1.00 96.07  ?  380 LYS C C   1 
ATOM   12870 O  O   . LYS C  2  380 ? 76.545  40.568  71.842  1.00 99.30  ?  380 LYS C O   1 
ATOM   12871 C  CB  . LYS C  2  380 ? 74.743  38.172  70.543  1.00 86.70  ?  380 LYS C CB  1 
ATOM   12872 C  CG  . LYS C  2  380 ? 74.756  37.899  72.043  1.00 85.91  ?  380 LYS C CG  1 
ATOM   12873 C  CD  . LYS C  2  380 ? 74.093  36.576  72.392  1.00 95.51  ?  380 LYS C CD  1 
ATOM   12874 C  CE  . LYS C  2  380 ? 74.203  36.251  73.865  1.00 110.56 ?  380 LYS C CE  1 
ATOM   12875 N  NZ  . LYS C  2  380 ? 73.017  35.503  74.360  1.00 117.54 ?  380 LYS C NZ  1 
ATOM   12876 N  N   . GLU C  2  381 ? 77.550  39.604  70.065  1.00 100.97 ?  381 GLU C N   1 
ATOM   12877 C  CA  . GLU C  2  381 ? 78.911  39.879  70.521  1.00 104.31 ?  381 GLU C CA  1 
ATOM   12878 C  C   . GLU C  2  381 ? 79.200  41.378  70.557  1.00 91.56  ?  381 GLU C C   1 
ATOM   12879 O  O   . GLU C  2  381 ? 79.931  41.837  71.434  1.00 91.03  ?  381 GLU C O   1 
ATOM   12880 C  CB  . GLU C  2  381 ? 79.928  39.166  69.622  1.00 88.67  ?  381 GLU C CB  1 
ATOM   12881 C  CG  . GLU C  2  381 ? 79.907  37.655  69.763  1.00 104.71 ?  381 GLU C CG  1 
ATOM   12882 C  CD  . GLU C  2  381 ? 80.359  37.154  71.119  1.00 117.72 ?  381 GLU C CD  1 
ATOM   12883 O  OE1 . GLU C  2  381 ? 79.499  37.013  72.018  1.00 115.58 ?  381 GLU C OE1 1 
ATOM   12884 O  OE2 . GLU C  2  381 ? 81.576  36.903  71.283  1.00 124.21 ?  381 GLU C OE2 1 
ATOM   12885 N  N   . ALA C  2  382 ? 78.638  42.139  69.611  1.00 78.83  ?  382 ALA C N   1 
ATOM   12886 C  CA  . ALA C  2  382 ? 78.829  43.584  69.568  1.00 88.20  ?  382 ALA C CA  1 
ATOM   12887 C  C   . ALA C  2  382 ? 78.086  44.246  70.732  1.00 97.06  ?  382 ALA C C   1 
ATOM   12888 O  O   . ALA C  2  382 ? 78.600  45.192  71.333  1.00 94.13  ?  382 ALA C O   1 
ATOM   12889 C  CB  . ALA C  2  382 ? 78.314  44.132  68.250  1.00 76.36  ?  382 ALA C CB  1 
ATOM   12890 N  N   . ILE C  2  383 ? 76.875  43.743  71.046  1.00 97.12  ?  383 ILE C N   1 
ATOM   12891 C  CA  . ILE C  2  383 ? 76.039  44.254  72.138  1.00 92.54  ?  383 ILE C CA  1 
ATOM   12892 C  C   . ILE C  2  383 ? 76.764  44.043  73.467  1.00 93.96  ?  383 ILE C C   1 
ATOM   12893 O  O   . ILE C  2  383 ? 76.909  44.983  74.248  1.00 99.31  ?  383 ILE C O   1 
ATOM   12894 C  CB  . ILE C  2  383 ? 74.632  43.577  72.131  1.00 89.88  ?  383 ILE C CB  1 
ATOM   12895 C  CG1 . ILE C  2  383 ? 73.783  44.083  70.943  1.00 92.40  ?  383 ILE C CG1 1 
ATOM   12896 C  CG2 . ILE C  2  383 ? 73.899  43.834  73.454  1.00 90.93  ?  383 ILE C CG2 1 
ATOM   12897 C  CD1 . ILE C  2  383 ? 72.695  43.170  70.509  1.00 89.60  ?  383 ILE C CD1 1 
ATOM   12898 N  N   . LEU C  2  384 ? 77.233  42.816  73.716  1.00 102.34 ?  384 LEU C N   1 
ATOM   12899 C  CA  . LEU C  2  384 ? 77.930  42.501  74.957  1.00 92.05  ?  384 LEU C CA  1 
ATOM   12900 C  C   . LEU C  2  384 ? 79.209  43.324  75.113  1.00 97.40  ?  384 LEU C C   1 
ATOM   12901 O  O   . LEU C  2  384 ? 79.610  43.595  76.242  1.00 105.27 ?  384 LEU C O   1 
ATOM   12902 C  CB  . LEU C  2  384 ? 78.248  40.998  75.037  1.00 94.63  ?  384 LEU C CB  1 
ATOM   12903 C  CG  . LEU C  2  384 ? 77.038  40.052  75.039  1.00 89.79  ?  384 LEU C CG  1 
ATOM   12904 C  CD1 . LEU C  2  384 ? 77.455  38.629  74.704  1.00 89.24  ?  384 LEU C CD1 1 
ATOM   12905 C  CD2 . LEU C  2  384 ? 76.302  40.093  76.370  1.00 93.95  ?  384 LEU C CD2 1 
ATOM   12906 N  N   . ASN C  2  385 ? 79.844  43.735  74.003  1.00 90.36  ?  385 ASN C N   1 
ATOM   12907 C  CA  . ASN C  2  385 ? 81.067  44.531  74.078  1.00 83.25  ?  385 ASN C CA  1 
ATOM   12908 C  C   . ASN C  2  385 ? 80.814  45.944  74.606  1.00 91.19  ?  385 ASN C C   1 
ATOM   12909 O  O   . ASN C  2  385 ? 81.759  46.589  75.055  1.00 102.33 ?  385 ASN C O   1 
ATOM   12910 C  CB  . ASN C  2  385 ? 81.770  44.589  72.724  1.00 94.22  ?  385 ASN C CB  1 
ATOM   12911 C  CG  . ASN C  2  385 ? 83.227  44.983  72.823  1.00 100.90 ?  385 ASN C CG  1 
ATOM   12912 O  OD1 . ASN C  2  385 ? 83.631  46.069  72.395  1.00 117.31 ?  385 ASN C OD1 1 
ATOM   12913 N  ND2 . ASN C  2  385 ? 84.049  44.115  73.399  1.00 95.11  ?  385 ASN C ND2 1 
ATOM   12914 N  N   . PHE C  2  386 ? 79.559  46.433  74.581  1.00 91.23  ?  386 PHE C N   1 
ATOM   12915 C  CA  . PHE C  2  386 ? 79.256  47.766  75.111  1.00 98.45  ?  386 PHE C CA  1 
ATOM   12916 C  C   . PHE C  2  386 ? 79.677  47.871  76.596  1.00 98.90  ?  386 PHE C C   1 
ATOM   12917 O  O   . PHE C  2  386 ? 79.941  48.971  77.079  1.00 105.94 ?  386 PHE C O   1 
ATOM   12918 C  CB  . PHE C  2  386 ? 77.761  48.097  74.921  1.00 98.78  ?  386 PHE C CB  1 
ATOM   12919 C  CG  . PHE C  2  386 ? 77.314  49.451  75.427  1.00 107.59 ?  386 PHE C CG  1 
ATOM   12920 C  CD1 . PHE C  2  386 ? 77.968  50.608  75.039  1.00 116.99 ?  386 PHE C CD1 1 
ATOM   12921 C  CD2 . PHE C  2  386 ? 76.203  49.572  76.241  1.00 115.58 ?  386 PHE C CD2 1 
ATOM   12922 C  CE1 . PHE C  2  386 ? 77.545  51.851  75.498  1.00 116.35 ?  386 PHE C CE1 1 
ATOM   12923 C  CE2 . PHE C  2  386 ? 75.784  50.817  76.695  1.00 105.27 ?  386 PHE C CE2 1 
ATOM   12924 C  CZ  . PHE C  2  386 ? 76.449  51.947  76.312  1.00 106.66 ?  386 PHE C CZ  1 
ATOM   12925 N  N   . LYS C  2  387 ? 79.782  46.716  77.299  1.00 103.86 ?  387 LYS C N   1 
ATOM   12926 C  CA  . LYS C  2  387 ? 80.207  46.645  78.701  1.00 109.42 ?  387 LYS C CA  1 
ATOM   12927 C  C   . LYS C  2  387 ? 81.628  47.205  78.885  1.00 114.01 ?  387 LYS C C   1 
ATOM   12928 O  O   . LYS C  2  387 ? 81.953  47.687  79.969  1.00 115.46 ?  387 LYS C O   1 
ATOM   12929 C  CB  . LYS C  2  387 ? 80.189  45.185  79.202  1.00 97.80  ?  387 LYS C CB  1 
ATOM   12930 C  CG  . LYS C  2  387 ? 78.801  44.604  79.437  1.00 99.52  ?  387 LYS C CG  1 
ATOM   12931 C  CD  . LYS C  2  387 ? 78.835  43.115  79.811  1.00 120.61 ?  387 LYS C CD  1 
ATOM   12932 C  CE  . LYS C  2  387 ? 77.875  42.756  80.925  1.00 111.82 ?  387 LYS C CE  1 
ATOM   12933 N  NZ  . LYS C  2  387 ? 77.440  41.334  80.854  1.00 105.49 ?  387 LYS C NZ  1 
ATOM   12934 N  N   . ASN C  2  388 ? 82.473  47.134  77.838  1.00 105.88 ?  388 ASN C N   1 
ATOM   12935 C  CA  . ASN C  2  388 ? 83.856  47.614  77.899  1.00 101.21 ?  388 ASN C CA  1 
ATOM   12936 C  C   . ASN C  2  388 ? 84.042  49.028  77.325  1.00 90.90  ?  388 ASN C C   1 
ATOM   12937 O  O   . ASN C  2  388 ? 85.174  49.451  77.107  1.00 90.27  ?  388 ASN C O   1 
ATOM   12938 C  CB  . ASN C  2  388 ? 84.771  46.624  77.182  1.00 97.13  ?  388 ASN C CB  1 
ATOM   12939 C  CG  . ASN C  2  388 ? 84.485  45.194  77.564  1.00 95.81  ?  388 ASN C CG  1 
ATOM   12940 O  OD1 . ASN C  2  388 ? 83.851  44.442  76.817  1.00 101.84 ?  388 ASN C OD1 1 
ATOM   12941 N  ND2 . ASN C  2  388 ? 84.928  44.790  78.747  1.00 99.53  ?  388 ASN C ND2 1 
ATOM   12942 N  N   . ARG C  2  389 ? 82.951  49.764  77.103  1.00 90.95  ?  389 ARG C N   1 
ATOM   12943 C  CA  . ARG C  2  389 ? 83.032  51.119  76.573  1.00 92.60  ?  389 ARG C CA  1 
ATOM   12944 C  C   . ARG C  2  389 ? 83.588  52.063  77.641  1.00 99.91  ?  389 ARG C C   1 
ATOM   12945 O  O   . ARG C  2  389 ? 83.139  52.022  78.786  1.00 112.57 ?  389 ARG C O   1 
ATOM   12946 C  CB  . ARG C  2  389 ? 81.629  51.588  76.130  1.00 93.93  ?  389 ARG C CB  1 
ATOM   12947 C  CG  . ARG C  2  389 ? 81.561  53.026  75.596  1.00 97.58  ?  389 ARG C CG  1 
ATOM   12948 C  CD  . ARG C  2  389 ? 81.611  53.093  74.084  1.00 90.01  ?  389 ARG C CD  1 
ATOM   12949 N  NE  . ARG C  2  389 ? 80.392  52.573  73.459  1.00 94.08  ?  389 ARG C NE  1 
ATOM   12950 C  CZ  . ARG C  2  389 ? 79.324  53.298  73.131  1.00 102.93 ?  389 ARG C CZ  1 
ATOM   12951 N  NH1 . ARG C  2  389 ? 79.298  54.605  73.369  1.00 106.08 ?  389 ARG C NH1 1 
ATOM   12952 N  NH2 . ARG C  2  389 ? 78.270  52.721  72.569  1.00 99.10  ?  389 ARG C NH2 1 
ATOM   12953 N  N   . ASP C  2  390 ? 84.562  52.911  77.270  1.00 92.24  ?  390 ASP C N   1 
ATOM   12954 C  CA  . ASP C  2  390 ? 85.139  53.896  78.187  1.00 107.60 ?  390 ASP C CA  1 
ATOM   12955 C  C   . ASP C  2  390 ? 84.475  55.232  77.845  1.00 115.79 ?  390 ASP C C   1 
ATOM   12956 O  O   . ASP C  2  390 ? 85.047  56.043  77.119  1.00 120.73 ?  390 ASP C O   1 
ATOM   12957 C  CB  . ASP C  2  390 ? 86.668  53.973  78.027  1.00 114.30 ?  390 ASP C CB  1 
ATOM   12958 C  CG  . ASP C  2  390 ? 87.367  54.743  79.131  1.00 122.93 ?  390 ASP C CG  1 
ATOM   12959 O  OD1 . ASP C  2  390 ? 86.864  55.825  79.513  1.00 109.77 ?  390 ASP C OD1 1 
ATOM   12960 O  OD2 . ASP C  2  390 ? 88.419  54.265  79.613  1.00 120.37 ?  390 ASP C OD2 1 
ATOM   12961 N  N   . GLN C  2  391 ? 83.257  55.444  78.359  1.00 113.78 ?  391 GLN C N   1 
ATOM   12962 C  CA  . GLN C  2  391 ? 82.462  56.642  78.085  1.00 112.62 ?  391 GLN C CA  1 
ATOM   12963 C  C   . GLN C  2  391 ? 83.194  57.976  78.271  1.00 116.25 ?  391 GLN C C   1 
ATOM   12964 O  O   . GLN C  2  391 ? 82.842  58.947  77.602  1.00 123.81 ?  391 GLN C O   1 
ATOM   12965 C  CB  . GLN C  2  391 ? 81.169  56.633  78.916  1.00 117.35 ?  391 GLN C CB  1 
ATOM   12966 C  CG  . GLN C  2  391 ? 80.170  55.547  78.515  1.00 114.26 ?  391 GLN C CG  1 
ATOM   12967 C  CD  . GLN C  2  391 ? 79.477  55.842  77.208  1.00 124.68 ?  391 GLN C CD  1 
ATOM   12968 O  OE1 . GLN C  2  391 ? 80.021  56.511  76.324  1.00 124.90 ?  391 GLN C OE1 1 
ATOM   12969 N  NE2 . GLN C  2  391 ? 78.255  55.343  77.049  1.00 129.99 ?  391 GLN C NE2 1 
ATOM   12970 N  N   . SER C  2  392 ? 84.192  58.040  79.160  1.00 118.01 ?  392 SER C N   1 
ATOM   12971 C  CA  . SER C  2  392 ? 84.930  59.282  79.386  1.00 113.31 ?  392 SER C CA  1 
ATOM   12972 C  C   . SER C  2  392 ? 85.779  59.670  78.175  1.00 115.60 ?  392 SER C C   1 
ATOM   12973 O  O   . SER C  2  392 ? 85.937  60.860  77.901  1.00 121.37 ?  392 SER C O   1 
ATOM   12974 C  CB  . SER C  2  392 ? 85.820  59.157  80.619  1.00 130.07 ?  392 SER C CB  1 
ATOM   12975 O  OG  . SER C  2  392 ? 86.909  58.275  80.394  1.00 141.40 ?  392 SER C OG  1 
ATOM   12976 N  N   . LYS C  2  393 ? 86.320  58.678  77.450  1.00 112.31 ?  393 LYS C N   1 
ATOM   12977 C  CA  . LYS C  2  393 ? 87.157  58.940  76.279  1.00 118.51 ?  393 LYS C CA  1 
ATOM   12978 C  C   . LYS C  2  393 ? 86.382  58.894  74.937  1.00 113.61 ?  393 LYS C C   1 
ATOM   12979 O  O   . LYS C  2  393 ? 87.003  58.958  73.875  1.00 113.21 ?  393 LYS C O   1 
ATOM   12980 C  CB  . LYS C  2  393 ? 88.349  57.970  76.268  1.00 122.03 ?  393 LYS C CB  1 
ATOM   12981 C  CG  . LYS C  2  393 ? 89.151  58.016  77.569  1.00 125.00 ?  393 LYS C CG  1 
ATOM   12982 C  CD  . LYS C  2  393 ? 90.550  57.409  77.434  1.00 144.05 ?  393 LYS C CD  1 
ATOM   12983 C  CE  . LYS C  2  393 ? 90.595  55.925  77.719  1.00 133.36 ?  393 LYS C CE  1 
ATOM   12984 N  NZ  . LYS C  2  393 ? 91.987  55.444  77.911  1.00 137.00 ?  393 LYS C NZ  1 
ATOM   12985 N  N   . VAL C  2  394 ? 85.039  58.815  74.979  1.00 95.51  ?  394 VAL C N   1 
ATOM   12986 C  CA  . VAL C  2  394 ? 84.227  58.783  73.762  1.00 88.40  ?  394 VAL C CA  1 
ATOM   12987 C  C   . VAL C  2  394 ? 84.106  60.205  73.225  1.00 93.05  ?  394 VAL C C   1 
ATOM   12988 O  O   . VAL C  2  394 ? 83.938  61.139  74.006  1.00 109.17 ?  394 VAL C O   1 
ATOM   12989 C  CB  . VAL C  2  394 ? 82.829  58.163  74.025  1.00 97.54  ?  394 VAL C CB  1 
ATOM   12990 C  CG1 . VAL C  2  394 ? 81.899  58.371  72.832  1.00 102.31 ?  394 VAL C CG1 1 
ATOM   12991 C  CG2 . VAL C  2  394 ? 82.943  56.682  74.362  1.00 105.68 ?  394 VAL C CG2 1 
ATOM   12992 N  N   . MET C  2  395 ? 84.193  60.376  71.900  1.00 85.29  ?  395 MET C N   1 
ATOM   12993 C  CA  . MET C  2  395 ? 84.085  61.695  71.288  1.00 88.55  ?  395 MET C CA  1 
ATOM   12994 C  C   . MET C  2  395 ? 83.477  61.581  69.898  1.00 81.48  ?  395 MET C C   1 
ATOM   12995 O  O   . MET C  2  395 ? 84.198  61.398  68.921  1.00 81.19  ?  395 MET C O   1 
ATOM   12996 C  CB  . MET C  2  395 ? 85.468  62.363  71.214  1.00 92.53  ?  395 MET C CB  1 
ATOM   12997 C  CG  . MET C  2  395 ? 85.414  63.855  70.960  1.00 86.18  ?  395 MET C CG  1 
ATOM   12998 S  SD  . MET C  2  395 ? 85.154  64.279  69.220  1.00 89.74  ?  395 MET C SD  1 
ATOM   12999 C  CE  . MET C  2  395 ? 86.764  64.913  68.802  1.00 106.34 ?  395 MET C CE  1 
ATOM   13000 N  N   . ILE C  2  396 ? 82.152  61.693  69.807  1.00 83.61  ?  396 ILE C N   1 
ATOM   13001 C  CA  . ILE C  2  396 ? 81.447  61.626  68.532  1.00 79.48  ?  396 ILE C CA  1 
ATOM   13002 C  C   . ILE C  2  396 ? 81.177  63.070  68.096  1.00 81.52  ?  396 ILE C C   1 
ATOM   13003 O  O   . ILE C  2  396 ? 80.352  63.727  68.731  1.00 95.05  ?  396 ILE C O   1 
ATOM   13004 C  CB  . ILE C  2  396 ? 80.117  60.841  68.678  1.00 79.67  ?  396 ILE C CB  1 
ATOM   13005 C  CG1 . ILE C  2  396 ? 80.361  59.394  69.160  1.00 79.04  ?  396 ILE C CG1 1 
ATOM   13006 C  CG2 . ILE C  2  396 ? 79.344  60.850  67.359  1.00 82.70  ?  396 ILE C CG2 1 
ATOM   13007 C  CD1 . ILE C  2  396 ? 79.134  58.732  69.773  1.00 80.54  ?  396 ILE C CD1 1 
ATOM   13008 N  N   . PRO C  2  397 ? 81.836  63.610  67.046  1.00 83.44  ?  397 PRO C N   1 
ATOM   13009 C  CA  . PRO C  2  397 ? 81.548  65.002  66.652  1.00 79.92  ?  397 PRO C CA  1 
ATOM   13010 C  C   . PRO C  2  397 ? 80.062  65.228  66.389  1.00 86.59  ?  397 PRO C C   1 
ATOM   13011 O  O   . PRO C  2  397 ? 79.449  64.419  65.700  1.00 93.82  ?  397 PRO C O   1 
ATOM   13012 C  CB  . PRO C  2  397 ? 82.375  65.193  65.376  1.00 82.92  ?  397 PRO C CB  1 
ATOM   13013 C  CG  . PRO C  2  397 ? 83.441  64.175  65.447  1.00 79.20  ?  397 PRO C CG  1 
ATOM   13014 C  CD  . PRO C  2  397 ? 82.855  63.002  66.170  1.00 81.02  ?  397 PRO C CD  1 
ATOM   13015 N  N   . GLU C  2  398 ? 79.475  66.296  66.953  1.00 84.43  ?  398 GLU C N   1 
ATOM   13016 C  CA  . GLU C  2  398 ? 78.053  66.576  66.751  1.00 93.34  ?  398 GLU C CA  1 
ATOM   13017 C  C   . GLU C  2  398 ? 77.912  67.212  65.370  1.00 96.76  ?  398 GLU C C   1 
ATOM   13018 O  O   . GLU C  2  398 ? 77.680  68.416  65.253  1.00 105.17 ?  398 GLU C O   1 
ATOM   13019 C  CB  . GLU C  2  398 ? 77.502  67.508  67.849  1.00 103.81 ?  398 GLU C CB  1 
ATOM   13020 C  CG  . GLU C  2  398 ? 77.391  66.861  69.223  1.00 119.70 ?  398 GLU C CG  1 
ATOM   13021 C  CD  . GLU C  2  398 ? 76.213  67.321  70.064  1.00 130.24 ?  398 GLU C CD  1 
ATOM   13022 O  OE1 . GLU C  2  398 ? 75.474  68.232  69.621  1.00 139.72 ?  398 GLU C OE1 1 
ATOM   13023 O  OE2 . GLU C  2  398 ? 76.028  66.766  71.171  1.00 147.61 ?  398 GLU C OE2 1 
ATOM   13024 N  N   . LEU C  2  399 ? 78.070  66.393  64.319  1.00 98.53  ?  399 LEU C N   1 
ATOM   13025 C  CA  . LEU C  2  399 ? 77.988  66.848  62.937  1.00 88.99  ?  399 LEU C CA  1 
ATOM   13026 C  C   . LEU C  2  399 ? 77.396  65.750  62.063  1.00 85.60  ?  399 LEU C C   1 
ATOM   13027 O  O   . LEU C  2  399 ? 78.079  64.788  61.729  1.00 77.89  ?  399 LEU C O   1 
ATOM   13028 C  CB  . LEU C  2  399 ? 79.372  67.251  62.412  1.00 76.96  ?  399 LEU C CB  1 
ATOM   13029 C  CG  . LEU C  2  399 ? 79.936  68.567  62.968  1.00 79.58  ?  399 LEU C CG  1 
ATOM   13030 C  CD1 . LEU C  2  399 ? 81.447  68.572  62.944  1.00 96.28  ?  399 LEU C CD1 1 
ATOM   13031 C  CD2 . LEU C  2  399 ? 79.410  69.755  62.198  1.00 83.71  ?  399 LEU C CD2 1 
ATOM   13032 N  N   . LYS C  2  400 ? 76.120  65.902  61.703  1.00 87.94  ?  400 LYS C N   1 
ATOM   13033 C  CA  . LYS C  2  400 ? 75.399  64.961  60.850  1.00 74.51  ?  400 LYS C CA  1 
ATOM   13034 C  C   . LYS C  2  400 ? 74.635  65.764  59.796  1.00 89.03  ?  400 LYS C C   1 
ATOM   13035 O  O   . LYS C  2  400 ? 74.472  66.977  59.946  1.00 95.41  ?  400 LYS C O   1 
ATOM   13036 C  CB  . LYS C  2  400 ? 74.451  64.064  61.673  1.00 81.04  ?  400 LYS C CB  1 
ATOM   13037 C  CG  . LYS C  2  400 ? 73.497  64.820  62.601  1.00 100.37 ?  400 LYS C CG  1 
ATOM   13038 C  CD  . LYS C  2  400 ? 72.272  63.990  63.008  1.00 84.47  ?  400 LYS C CD  1 
ATOM   13039 C  CE  . LYS C  2  400 ? 72.617  62.733  63.772  1.00 91.83  ?  400 LYS C CE  1 
ATOM   13040 N  NZ  . LYS C  2  400 ? 71.458  62.211  64.548  1.00 103.51 ?  400 LYS C NZ  1 
ATOM   13041 N  N   . CYS C  2  401 ? 74.181  65.105  58.727  1.00 89.73  ?  401 CYS C N   1 
ATOM   13042 C  CA  . CYS C  2  401 ? 73.466  65.793  57.656  1.00 81.27  ?  401 CYS C CA  1 
ATOM   13043 C  C   . CYS C  2  401 ? 72.352  64.918  57.098  1.00 86.05  ?  401 CYS C C   1 
ATOM   13044 O  O   . CYS C  2  401 ? 72.520  63.710  57.005  1.00 86.34  ?  401 CYS C O   1 
ATOM   13045 C  CB  . CYS C  2  401 ? 74.450  66.200  56.565  1.00 70.01  ?  401 CYS C CB  1 
ATOM   13046 S  SG  . CYS C  2  401 ? 73.783  67.381  55.370  1.00 97.49  ?  401 CYS C SG  1 
ATOM   13047 N  N   . LYS C  2  402 ? 71.221  65.515  56.715  1.00 87.69  ?  402 LYS C N   1 
ATOM   13048 C  CA  . LYS C  2  402 ? 70.100  64.746  56.169  1.00 83.00  ?  402 LYS C CA  1 
ATOM   13049 C  C   . LYS C  2  402 ? 70.338  64.432  54.696  1.00 79.55  ?  402 LYS C C   1 
ATOM   13050 O  O   . LYS C  2  402 ? 71.089  65.140  54.026  1.00 89.08  ?  402 LYS C O   1 
ATOM   13051 C  CB  . LYS C  2  402 ? 68.777  65.496  56.382  1.00 77.94  ?  402 LYS C CB  1 
ATOM   13052 C  CG  . LYS C  2  402 ? 68.503  65.746  57.862  1.00 91.19  ?  402 LYS C CG  1 
ATOM   13053 C  CD  . LYS C  2  402 ? 67.056  66.143  58.180  1.00 95.33  ?  402 LYS C CD  1 
ATOM   13054 C  CE  . LYS C  2  402 ? 66.402  65.291  59.254  1.00 114.21 ?  402 LYS C CE  1 
ATOM   13055 N  NZ  . LYS C  2  402 ? 67.262  65.083  60.460  1.00 100.04 ?  402 LYS C NZ  1 
ATOM   13056 N  N   . ALA C  2  403 ? 69.717  63.360  54.191  1.00 75.27  ?  403 ALA C N   1 
ATOM   13057 C  CA  . ALA C  2  403 ? 69.894  62.967  52.795  1.00 82.72  ?  403 ALA C CA  1 
ATOM   13058 C  C   . ALA C  2  403 ? 68.736  62.108  52.281  1.00 86.84  ?  403 ALA C C   1 
ATOM   13059 O  O   . ALA C  2  403 ? 68.034  61.479  53.073  1.00 93.81  ?  403 ALA C O   1 
ATOM   13060 C  CB  . ALA C  2  403 ? 71.204  62.209  52.639  1.00 75.10  ?  403 ALA C CB  1 
ATOM   13061 N  N   . ILE C  2  404 ? 68.500  62.185  50.971  1.00 75.14  ?  404 ILE C N   1 
ATOM   13062 C  CA  . ILE C  2  404 ? 67.411  61.386  50.343  1.00 76.38  ?  404 ILE C CA  1 
ATOM   13063 C  C   . ILE C  2  404 ? 68.063  60.477  49.303  1.00 73.74  ?  404 ILE C C   1 
ATOM   13064 O  O   . ILE C  2  404 ? 68.877  60.980  48.508  1.00 75.00  ?  404 ILE C O   1 
ATOM   13065 C  CB  . ILE C  2  404 ? 66.348  62.301  49.707  1.00 68.45  ?  404 ILE C CB  1 
ATOM   13066 C  CG1 . ILE C  2  404 ? 65.597  63.118  50.761  1.00 78.09  ?  404 ILE C CG1 1 
ATOM   13067 C  CG2 . ILE C  2  404 ? 65.398  61.496  48.834  1.00 69.56  ?  404 ILE C CG2 1 
ATOM   13068 C  CD1 . ILE C  2  404 ? 64.734  64.215  50.184  1.00 98.84  ?  404 ILE C CD1 1 
ATOM   13069 N  N   . LEU C  2  405 ? 67.726  59.188  49.338  1.00 65.11  ?  405 LEU C N   1 
ATOM   13070 C  CA  . LEU C  2  405 ? 68.314  58.212  48.387  1.00 73.00  ?  405 LEU C CA  1 
ATOM   13071 C  C   . LEU C  2  405 ? 67.237  57.194  48.011  1.00 73.26  ?  405 LEU C C   1 
ATOM   13072 O  O   . LEU C  2  405 ? 66.065  57.434  48.345  1.00 81.33  ?  405 LEU C O   1 
ATOM   13073 C  CB  . LEU C  2  405 ? 69.523  57.545  49.047  1.00 66.22  ?  405 LEU C CB  1 
ATOM   13074 C  CG  . LEU C  2  405 ? 69.239  56.639  50.242  1.00 66.04  ?  405 LEU C CG  1 
ATOM   13075 C  CD1 . LEU C  2  405 ? 70.437  55.744  50.508  1.00 84.28  ?  405 LEU C CD1 1 
ATOM   13076 C  CD2 . LEU C  2  405 ? 68.915  57.458  51.482  1.00 68.75  ?  405 LEU C CD2 1 
ATOM   13077 N  N   . GLY C  2  406 ? 67.621  56.108  47.341  1.00 68.90  ?  406 GLY C N   1 
ATOM   13078 C  CA  . GLY C  2  406 ? 66.622  55.125  46.881  1.00 75.08  ?  406 GLY C CA  1 
ATOM   13079 C  C   . GLY C  2  406 ? 66.234  55.416  45.448  1.00 73.65  ?  406 GLY C C   1 
ATOM   13080 O  O   . GLY C  2  406 ? 65.210  54.880  44.990  1.00 84.64  ?  406 GLY C O   1 
ATOM   13081 N  N   . TYR C  2  407 ? 67.035  56.233  44.766  1.00 69.25  ?  407 TYR C N   1 
ATOM   13082 C  CA  . TYR C  2  407 ? 66.735  56.620  43.400  1.00 63.35  ?  407 TYR C CA  1 
ATOM   13083 C  C   . TYR C  2  407 ? 67.163  55.574  42.394  1.00 70.36  ?  407 TYR C C   1 
ATOM   13084 O  O   . TYR C  2  407 ? 68.138  55.762  41.673  1.00 79.87  ?  407 TYR C O   1 
ATOM   13085 C  CB  . TYR C  2  407 ? 67.319  58.002  43.079  1.00 68.19  ?  407 TYR C CB  1 
ATOM   13086 C  CG  . TYR C  2  407 ? 66.609  59.109  43.826  1.00 74.26  ?  407 TYR C CG  1 
ATOM   13087 C  CD1 . TYR C  2  407 ? 65.276  59.396  43.578  1.00 60.34  ?  407 TYR C CD1 1 
ATOM   13088 C  CD2 . TYR C  2  407 ? 67.251  59.822  44.825  1.00 75.75  ?  407 TYR C CD2 1 
ATOM   13089 C  CE1 . TYR C  2  407 ? 64.607  60.384  44.286  1.00 80.27  ?  407 TYR C CE1 1 
ATOM   13090 C  CE2 . TYR C  2  407 ? 66.600  60.828  45.527  1.00 83.03  ?  407 TYR C CE2 1 
ATOM   13091 C  CZ  . TYR C  2  407 ? 65.273  61.102  45.259  1.00 86.59  ?  407 TYR C CZ  1 
ATOM   13092 O  OH  . TYR C  2  407 ? 64.606  62.087  45.949  1.00 72.87  ?  407 TYR C OH  1 
ATOM   13093 N  N   . SER C  2  408 ? 66.410  54.474  42.338  1.00 55.02  ?  408 SER C N   1 
ATOM   13094 C  CA  . SER C  2  408 ? 66.649  53.403  41.385  1.00 64.05  ?  408 SER C CA  1 
ATOM   13095 C  C   . SER C  2  408 ? 65.981  53.809  40.060  1.00 72.25  ?  408 SER C C   1 
ATOM   13096 O  O   . SER C  2  408 ? 65.261  54.807  40.030  1.00 69.41  ?  408 SER C O   1 
ATOM   13097 C  CB  . SER C  2  408 ? 66.051  52.097  41.902  1.00 71.20  ?  408 SER C CB  1 
ATOM   13098 O  OG  . SER C  2  408 ? 64.685  52.262  42.256  1.00 62.14  ?  408 SER C OG  1 
ATOM   13099 N  N   . VAL C  2  409 ? 66.195  53.055  38.970  1.00 67.81  ?  409 VAL C N   1 
ATOM   13100 C  CA  . VAL C  2  409 ? 65.578  53.403  37.686  1.00 62.21  ?  409 VAL C CA  1 
ATOM   13101 C  C   . VAL C  2  409 ? 64.052  53.348  37.808  1.00 74.80  ?  409 VAL C C   1 
ATOM   13102 O  O   . VAL C  2  409 ? 63.362  54.229  37.298  1.00 74.55  ?  409 VAL C O   1 
ATOM   13103 C  CB  . VAL C  2  409 ? 66.101  52.511  36.537  1.00 60.32  ?  409 VAL C CB  1 
ATOM   13104 C  CG1 . VAL C  2  409 ? 65.333  52.769  35.246  1.00 59.76  ?  409 VAL C CG1 1 
ATOM   13105 C  CG2 . VAL C  2  409 ? 67.592  52.735  36.327  1.00 72.36  ?  409 VAL C CG2 1 
ATOM   13106 N  N   . GLU C  2  410 ? 63.531  52.344  38.524  1.00 67.72  ?  410 GLU C N   1 
ATOM   13107 C  CA  . GLU C  2  410 ? 62.091  52.198  38.731  1.00 61.87  ?  410 GLU C CA  1 
ATOM   13108 C  C   . GLU C  2  410 ? 61.550  53.409  39.491  1.00 71.21  ?  410 GLU C C   1 
ATOM   13109 O  O   . GLU C  2  410 ? 60.505  53.942  39.132  1.00 80.65  ?  410 GLU C O   1 
ATOM   13110 C  CB  . GLU C  2  410 ? 61.786  50.908  39.517  1.00 63.49  ?  410 GLU C CB  1 
ATOM   13111 C  CG  . GLU C  2  410 ? 62.124  49.626  38.772  1.00 73.31  ?  410 GLU C CG  1 
ATOM   13112 C  CD  . GLU C  2  410 ? 63.554  49.126  38.893  1.00 91.85  ?  410 GLU C CD  1 
ATOM   13113 O  OE1 . GLU C  2  410 ? 64.404  49.847  39.466  1.00 76.83  ?  410 GLU C OE1 1 
ATOM   13114 O  OE2 . GLU C  2  410 ? 63.824  48.005  38.403  1.00 80.78  ?  410 GLU C OE2 1 
ATOM   13115 N  N   . GLU C  2  411 ? 62.267  53.851  40.528  1.00 67.98  ?  411 GLU C N   1 
ATOM   13116 C  CA  . GLU C  2  411 ? 61.846  54.996  41.328  1.00 66.32  ?  411 GLU C CA  1 
ATOM   13117 C  C   . GLU C  2  411 ? 61.931  56.288  40.537  1.00 69.69  ?  411 GLU C C   1 
ATOM   13118 O  O   . GLU C  2  411 ? 61.024  57.111  40.629  1.00 76.87  ?  411 GLU C O   1 
ATOM   13119 C  CB  . GLU C  2  411 ? 62.696  55.101  42.602  1.00 81.13  ?  411 GLU C CB  1 
ATOM   13120 C  CG  . GLU C  2  411 ? 62.377  56.306  43.473  1.00 85.33  ?  411 GLU C CG  1 
ATOM   13121 C  CD  . GLU C  2  411 ? 60.952  56.393  43.985  1.00 88.91  ?  411 GLU C CD  1 
ATOM   13122 O  OE1 . GLU C  2  411 ? 60.269  55.344  44.048  1.00 85.80  ?  411 GLU C OE1 1 
ATOM   13123 O  OE2 . GLU C  2  411 ? 60.523  57.515  44.341  1.00 98.81  ?  411 GLU C OE2 1 
ATOM   13124 N  N   . ILE C  2  412 ? 63.005  56.487  39.760  1.00 72.24  ?  412 ILE C N   1 
ATOM   13125 C  CA  . ILE C  2  412 ? 63.150  57.708  38.968  1.00 66.40  ?  412 ILE C CA  1 
ATOM   13126 C  C   . ILE C  2  412 ? 61.997  57.791  37.967  1.00 68.50  ?  412 ILE C C   1 
ATOM   13127 O  O   . ILE C  2  412 ? 61.375  58.840  37.840  1.00 68.12  ?  412 ILE C O   1 
ATOM   13128 C  CB  . ILE C  2  412 ? 64.544  57.787  38.287  1.00 60.34  ?  412 ILE C CB  1 
ATOM   13129 C  CG1 . ILE C  2  412 ? 65.636  58.087  39.337  1.00 56.55  ?  412 ILE C CG1 1 
ATOM   13130 C  CG2 . ILE C  2  412 ? 64.555  58.851  37.185  1.00 49.54  ?  412 ILE C CG2 1 
ATOM   13131 C  CD1 . ILE C  2  412 ? 67.019  57.740  38.913  1.00 66.52  ?  412 ILE C CD1 1 
ATOM   13132 N  N   . ILE C  2  413 ? 61.673  56.674  37.302  1.00 67.99  ?  413 ILE C N   1 
ATOM   13133 C  CA  . ILE C  2  413 ? 60.565  56.644  36.345  1.00 73.19  ?  413 ILE C CA  1 
ATOM   13134 C  C   . ILE C  2  413 ? 59.242  57.005  37.055  1.00 70.77  ?  413 ILE C C   1 
ATOM   13135 O  O   . ILE C  2  413 ? 58.464  57.804  36.532  1.00 73.73  ?  413 ILE C O   1 
ATOM   13136 C  CB  . ILE C  2  413 ? 60.499  55.270  35.617  1.00 64.51  ?  413 ILE C CB  1 
ATOM   13137 C  CG1 . ILE C  2  413 ? 61.652  55.139  34.602  1.00 68.06  ?  413 ILE C CG1 1 
ATOM   13138 C  CG2 . ILE C  2  413 ? 59.161  55.103  34.913  1.00 72.93  ?  413 ILE C CG2 1 
ATOM   13139 C  CD1 . ILE C  2  413 ? 61.941  53.712  34.136  1.00 70.06  ?  413 ILE C CD1 1 
ATOM   13140 N  N   . ASN C  2  414 ? 59.001  56.440  38.248  1.00 70.56  ?  414 ASN C N   1 
ATOM   13141 C  CA  . ASN C  2  414 ? 57.791  56.735  39.022  1.00 74.14  ?  414 ASN C CA  1 
ATOM   13142 C  C   . ASN C  2  414 ? 57.688  58.233  39.332  1.00 67.29  ?  414 ASN C C   1 
ATOM   13143 O  O   . ASN C  2  414 ? 56.605  58.799  39.220  1.00 73.92  ?  414 ASN C O   1 
ATOM   13144 C  CB  . ASN C  2  414 ? 57.777  55.941  40.336  1.00 73.00  ?  414 ASN C CB  1 
ATOM   13145 C  CG  . ASN C  2  414 ? 57.374  54.496  40.185  1.00 75.70  ?  414 ASN C CG  1 
ATOM   13146 O  OD1 . ASN C  2  414 ? 57.063  54.022  39.085  1.00 76.57  ?  414 ASN C OD1 1 
ATOM   13147 N  ND2 . ASN C  2  414 ? 57.370  53.761  41.290  1.00 75.94  ?  414 ASN C ND2 1 
ATOM   13148 N  N   . LYS C  2  415 ? 58.805  58.869  39.719  1.00 69.93  ?  415 LYS C N   1 
ATOM   13149 C  CA  . LYS C  2  415 ? 58.820  60.298  40.031  1.00 80.60  ?  415 LYS C CA  1 
ATOM   13150 C  C   . LYS C  2  415 ? 58.634  61.147  38.774  1.00 73.32  ?  415 LYS C C   1 
ATOM   13151 O  O   . LYS C  2  415 ? 57.977  62.183  38.832  1.00 76.78  ?  415 LYS C O   1 
ATOM   13152 C  CB  . LYS C  2  415 ? 60.119  60.686  40.750  1.00 63.46  ?  415 LYS C CB  1 
ATOM   13153 C  CG  . LYS C  2  415 ? 60.163  60.236  42.211  1.00 73.59  ?  415 LYS C CG  1 
ATOM   13154 C  CD  . LYS C  2  415 ? 60.781  61.284  43.115  1.00 91.53  ?  415 LYS C CD  1 
ATOM   13155 C  CE  . LYS C  2  415 ? 60.520  61.018  44.576  1.00 106.59 ?  415 LYS C CE  1 
ATOM   13156 N  NZ  . LYS C  2  415 ? 61.202  62.017  45.441  1.00 113.86 ?  415 LYS C NZ  1 
ATOM   13157 N  N   . LEU C  2  416 ? 59.196  60.712  37.641  1.00 64.89  ?  416 LEU C N   1 
ATOM   13158 C  CA  . LEU C  2  416 ? 59.046  61.443  36.386  1.00 70.92  ?  416 LEU C CA  1 
ATOM   13159 C  C   . LEU C  2  416 ? 57.589  61.396  35.894  1.00 78.15  ?  416 LEU C C   1 
ATOM   13160 O  O   . LEU C  2  416 ? 57.180  62.277  35.144  1.00 81.83  ?  416 LEU C O   1 
ATOM   13161 C  CB  . LEU C  2  416 ? 59.970  60.870  35.294  1.00 65.66  ?  416 LEU C CB  1 
ATOM   13162 C  CG  . LEU C  2  416 ? 61.479  61.028  35.480  1.00 67.04  ?  416 LEU C CG  1 
ATOM   13163 C  CD1 . LEU C  2  416 ? 62.229  60.262  34.408  1.00 64.98  ?  416 LEU C CD1 1 
ATOM   13164 C  CD2 . LEU C  2  416 ? 61.906  62.486  35.460  1.00 53.74  ?  416 LEU C CD2 1 
ATOM   13165 N  N   . ASP C  2  417 ? 56.808  60.376  36.299  1.00 71.70  ?  417 ASP C N   1 
ATOM   13166 C  CA  . ASP C  2  417 ? 55.403  60.266  35.894  1.00 71.98  ?  417 ASP C CA  1 
ATOM   13167 C  C   . ASP C  2  417 ? 54.573  61.459  36.386  1.00 78.09  ?  417 ASP C C   1 
ATOM   13168 O  O   . ASP C  2  417 ? 53.547  61.774  35.784  1.00 85.67  ?  417 ASP C O   1 
ATOM   13169 C  CB  . ASP C  2  417 ? 54.778  58.969  36.433  1.00 63.61  ?  417 ASP C CB  1 
ATOM   13170 C  CG  . ASP C  2  417 ? 54.936  57.772  35.526  1.00 80.18  ?  417 ASP C CG  1 
ATOM   13171 O  OD1 . ASP C  2  417 ? 55.836  57.799  34.655  1.00 92.88  ?  417 ASP C OD1 1 
ATOM   13172 O  OD2 . ASP C  2  417 ? 54.163  56.805  35.685  1.00 82.70  ?  417 ASP C OD2 1 
ATOM   13173 N  N   . LYS C  2  418 ? 55.012  62.118  37.472  1.00 76.16  ?  418 LYS C N   1 
ATOM   13174 C  CA  . LYS C  2  418 ? 54.317  63.273  38.037  1.00 79.23  ?  418 LYS C CA  1 
ATOM   13175 C  C   . LYS C  2  418 ? 54.254  64.442  37.041  1.00 80.82  ?  418 LYS C C   1 
ATOM   13176 O  O   . LYS C  2  418 ? 53.300  65.216  37.074  1.00 84.22  ?  418 LYS C O   1 
ATOM   13177 C  CB  . LYS C  2  418 ? 55.006  63.720  39.337  1.00 76.70  ?  418 LYS C CB  1 
ATOM   13178 C  CG  . LYS C  2  418 ? 54.915  62.686  40.452  1.00 98.48  ?  418 LYS C CG  1 
ATOM   13179 C  CD  . LYS C  2  418 ? 55.900  62.971  41.580  1.00 113.02 ?  418 LYS C CD  1 
ATOM   13180 C  CE  . LYS C  2  418 ? 55.488  62.296  42.867  1.00 132.36 ?  418 LYS C CE  1 
ATOM   13181 N  NZ  . LYS C  2  418 ? 56.397  62.636  43.992  1.00 109.76 ?  418 LYS C NZ  1 
ATOM   13182 N  N   . VAL C  2  419 ? 55.253  64.565  36.158  1.00 74.54  ?  419 VAL C N   1 
ATOM   13183 C  CA  . VAL C  2  419 ? 55.273  65.639  35.166  1.00 76.19  ?  419 VAL C CA  1 
ATOM   13184 C  C   . VAL C  2  419 ? 54.736  65.170  33.792  1.00 87.60  ?  419 VAL C C   1 
ATOM   13185 O  O   . VAL C  2  419 ? 55.033  65.801  32.775  1.00 89.77  ?  419 VAL C O   1 
ATOM   13186 C  CB  . VAL C  2  419 ? 56.671  66.302  35.059  1.00 71.71  ?  419 VAL C CB  1 
ATOM   13187 C  CG1 . VAL C  2  419 ? 57.152  66.778  36.424  1.00 59.58  ?  419 VAL C CG1 1 
ATOM   13188 C  CG2 . VAL C  2  419 ? 57.701  65.375  34.412  1.00 62.97  ?  419 VAL C CG2 1 
ATOM   13189 N  N   . VAL C  2  420 ? 53.956  64.085  33.787  1.00 81.17  ?  420 VAL C N   1 
ATOM   13190 C  CA  . VAL C  2  420 ? 53.387  63.552  32.513  1.00 70.43  ?  420 VAL C CA  1 
ATOM   13191 C  C   . VAL C  2  420 ? 51.892  63.885  32.460  1.00 79.78  ?  420 VAL C C   1 
ATOM   13192 O  O   . VAL C  2  420 ? 51.200  63.640  33.466  1.00 83.39  ?  420 VAL C O   1 
ATOM   13193 C  CB  . VAL C  2  420 ? 53.623  62.035  32.381  1.00 60.17  ?  420 VAL C CB  1 
ATOM   13194 C  CG1 . VAL C  2  420 ? 53.132  61.500  31.044  1.00 60.41  ?  420 VAL C CG1 1 
ATOM   13195 C  CG2 . VAL C  2  420 ? 55.082  61.670  32.603  1.00 79.78  ?  420 VAL C CG2 1 
ATOM   13196 N  N   . ASN C  2  421 ? 51.420  64.411  31.324  1.00 74.38  ?  421 ASN C N   1 
ATOM   13197 C  CA  . ASN C  2  421 ? 49.974  64.718  31.156  1.00 82.21  ?  421 ASN C CA  1 
ATOM   13198 C  C   . ASN C  2  421 ? 49.216  63.410  30.920  1.00 81.04  ?  421 ASN C C   1 
ATOM   13199 O  O   . ASN C  2  421 ? 49.670  62.612  30.078  1.00 82.88  ?  421 ASN C O   1 
ATOM   13200 C  CB  . ASN C  2  421 ? 49.721  65.719  30.026  1.00 81.91  ?  421 ASN C CB  1 
ATOM   13201 C  CG  . ASN C  2  421 ? 48.285  66.196  29.974  1.00 89.89  ?  421 ASN C CG  1 
ATOM   13202 O  OD1 . ASN C  2  421 ? 47.384  65.435  29.628  1.00 103.01 ?  421 ASN C OD1 1 
ATOM   13203 N  ND2 . ASN C  2  421 ? 48.062  67.455  30.314  1.00 84.85  ?  421 ASN C ND2 1 
ATOM   13204 N  N   . THR C  2  422 ? 48.100  63.208  31.622  1.00 73.03  ?  422 THR C N   1 
ATOM   13205 C  CA  . THR C  2  422 ? 47.344  61.931  31.515  1.00 84.17  ?  422 THR C CA  1 
ATOM   13206 C  C   . THR C  2  422 ? 46.730  61.779  30.121  1.00 93.02  ?  422 THR C C   1 
ATOM   13207 O  O   . THR C  2  422 ? 46.682  60.637  29.628  1.00 96.58  ?  422 THR C O   1 
ATOM   13208 C  CB  . THR C  2  422 ? 46.251  61.863  32.587  1.00 81.34  ?  422 THR C CB  1 
ATOM   13209 O  OG1 . THR C  2  422 ? 46.876  61.990  33.865  1.00 93.37  ?  422 THR C OG1 1 
ATOM   13210 C  CG2 . THR C  2  422 ? 45.448  60.582  32.531  1.00 108.82 ?  422 THR C CG2 1 
ATOM   13211 N  N   . GLN C  2  423 ? 46.289  62.879  29.508  1.00 89.22  ?  423 GLN C N   1 
ATOM   13212 C  CA  . GLN C  2  423 ? 45.580  62.796  28.201  1.00 91.77  ?  423 GLN C CA  1 
ATOM   13213 C  C   . GLN C  2  423 ? 46.561  62.680  27.030  1.00 92.60  ?  423 GLN C C   1 
ATOM   13214 O  O   . GLN C  2  423 ? 46.099  62.345  25.922  1.00 92.80  ?  423 GLN C O   1 
ATOM   13215 C  CB  . GLN C  2  423 ? 44.703  64.034  28.006  1.00 72.98  ?  423 GLN C CB  1 
ATOM   13216 C  CG  . GLN C  2  423 ? 43.662  64.223  29.098  1.00 74.80  ?  423 GLN C CG  1 
ATOM   13217 C  CD  . GLN C  2  423 ? 42.370  63.522  28.760  1.00 87.35  ?  423 GLN C CD  1 
ATOM   13218 O  OE1 . GLN C  2  423 ? 41.794  63.721  27.693  1.00 106.15 ?  423 GLN C OE1 1 
ATOM   13219 N  NE2 . GLN C  2  423 ? 41.905  62.685  29.673  1.00 103.97 ?  423 GLN C NE2 1 
ATOM   13220 N  N   . ILE C  2  424 ? 47.841  62.944  27.277  1.00 87.69  ?  424 ILE C N   1 
ATOM   13221 C  CA  . ILE C  2  424 ? 48.810  62.985  26.150  1.00 86.87  ?  424 ILE C CA  1 
ATOM   13222 C  C   . ILE C  2  424 ? 49.962  62.022  26.411  1.00 85.31  ?  424 ILE C C   1 
ATOM   13223 O  O   . ILE C  2  424 ? 49.955  60.913  25.844  1.00 86.51  ?  424 ILE C O   1 
ATOM   13224 C  CB  . ILE C  2  424 ? 49.359  64.417  26.029  1.00 84.20  ?  424 ILE C CB  1 
ATOM   13225 C  CG1 . ILE C  2  424 ? 48.292  65.478  26.309  1.00 127.09 ?  424 ILE C CG1 1 
ATOM   13226 C  CG2 . ILE C  2  424 ? 50.011  64.623  24.680  1.00 92.21  ?  424 ILE C CG2 1 
ATOM   13227 C  CD1 . ILE C  2  424 ? 48.848  66.879  26.403  1.00 122.57 ?  424 ILE C CD1 1 
ATOM   13228 N  N   . GLY C  2  425 ? 50.909  62.445  27.243  1.00 111.53 ?  425 GLY C N   1 
ATOM   13229 C  CA  . GLY C  2  425 ? 52.132  61.649  27.488  1.00 106.09 ?  425 GLY C CA  1 
ATOM   13230 C  C   . GLY C  2  425 ? 51.917  60.194  27.864  1.00 91.75  ?  425 GLY C C   1 
ATOM   13231 O  O   . GLY C  2  425 ? 50.897  59.891  28.510  1.00 94.16  ?  425 GLY C O   1 
ATOM   13232 N  N   . PRO C  2  426 ? 52.842  59.279  27.490  1.00 102.49 ?  426 PRO C N   1 
ATOM   13233 C  CA  . PRO C  2  426 ? 52.762  57.873  27.896  1.00 91.90  ?  426 PRO C CA  1 
ATOM   13234 C  C   . PRO C  2  426 ? 53.280  57.731  29.331  1.00 88.47  ?  426 PRO C C   1 
ATOM   13235 O  O   . PRO C  2  426 ? 53.890  58.666  29.813  1.00 99.31  ?  426 PRO C O   1 
ATOM   13236 C  CB  . PRO C  2  426 ? 53.756  57.186  26.955  1.00 59.14  ?  426 PRO C CB  1 
ATOM   13237 C  CG  . PRO C  2  426 ? 54.799  58.250  26.700  1.00 83.58  ?  426 PRO C CG  1 
ATOM   13238 C  CD  . PRO C  2  426 ? 54.021  59.549  26.662  1.00 96.81  ?  426 PRO C CD  1 
ATOM   13239 N  N   . MET C  2  427 ? 53.050  56.584  29.975  1.00 75.95  ?  427 MET C N   1 
ATOM   13240 C  CA  . MET C  2  427 ? 53.433  56.465  31.408  1.00 68.52  ?  427 MET C CA  1 
ATOM   13241 C  C   . MET C  2  427 ? 54.502  55.396  31.652  1.00 73.30  ?  427 MET C C   1 
ATOM   13242 O  O   . MET C  2  427 ? 54.660  54.510  30.791  1.00 74.92  ?  427 MET C O   1 
ATOM   13243 C  CB  . MET C  2  427 ? 52.185  56.126  32.230  1.00 71.82  ?  427 MET C CB  1 
ATOM   13244 C  CG  . MET C  2  427 ? 51.302  57.328  32.503  1.00 84.85  ?  427 MET C CG  1 
ATOM   13245 S  SD  . MET C  2  427 ? 52.195  58.678  33.314  1.00 89.97  ?  427 MET C SD  1 
ATOM   13246 C  CE  . MET C  2  427 ? 50.882  59.884  33.489  1.00 71.39  ?  427 MET C CE  1 
ATOM   13247 N  N   . GLN C  2  428 ? 55.199  55.484  32.788  1.00 71.70  ?  428 GLN C N   1 
ATOM   13248 C  CA  . GLN C  2  428 ? 56.227  54.515  33.156  1.00 66.40  ?  428 GLN C CA  1 
ATOM   13249 C  C   . GLN C  2  428 ? 57.331  54.368  32.101  1.00 69.16  ?  428 GLN C C   1 
ATOM   13250 O  O   . GLN C  2  428 ? 57.777  53.257  31.816  1.00 80.79  ?  428 GLN C O   1 
ATOM   13251 C  CB  . GLN C  2  428 ? 55.608  53.148  33.507  1.00 69.54  ?  428 GLN C CB  1 
ATOM   13252 C  CG  . GLN C  2  428 ? 54.809  53.152  34.798  1.00 62.39  ?  428 GLN C CG  1 
ATOM   13253 C  CD  . GLN C  2  428 ? 55.708  53.317  35.998  1.00 74.84  ?  428 GLN C CD  1 
ATOM   13254 O  OE1 . GLN C  2  428 ? 56.439  52.399  36.388  1.00 77.87  ?  428 GLN C OE1 1 
ATOM   13255 N  NE2 . GLN C  2  428 ? 55.686  54.491  36.613  1.00 75.21  ?  428 GLN C NE2 1 
ATOM   13256 N  N   . THR C  2  429 ? 57.782  55.491  31.538  1.00 68.22  ?  429 THR C N   1 
ATOM   13257 C  CA  . THR C  2  429 ? 58.862  55.507  30.555  1.00 57.22  ?  429 THR C CA  1 
ATOM   13258 C  C   . THR C  2  429 ? 59.818  56.638  30.939  1.00 74.53  ?  429 THR C C   1 
ATOM   13259 O  O   . THR C  2  429 ? 59.455  57.505  31.734  1.00 87.23  ?  429 THR C O   1 
ATOM   13260 C  CB  . THR C  2  429 ? 58.327  55.683  29.118  1.00 65.33  ?  429 THR C CB  1 
ATOM   13261 O  OG1 . THR C  2  429 ? 57.969  57.048  28.894  1.00 87.82  ?  429 THR C OG1 1 
ATOM   13262 C  CG2 . THR C  2  429 ? 57.150  54.773  28.807  1.00 70.30  ?  429 THR C CG2 1 
ATOM   13263 N  N   . VAL C  2  430 ? 61.030  56.637  30.381  1.00 78.34  ?  430 VAL C N   1 
ATOM   13264 C  CA  . VAL C  2  430 ? 62.000  57.697  30.675  1.00 64.69  ?  430 VAL C CA  1 
ATOM   13265 C  C   . VAL C  2  430 ? 61.764  58.940  29.802  1.00 68.21  ?  430 VAL C C   1 
ATOM   13266 O  O   . VAL C  2  430 ? 62.594  59.846  29.823  1.00 77.88  ?  430 VAL C O   1 
ATOM   13267 C  CB  . VAL C  2  430 ? 63.469  57.193  30.614  1.00 70.48  ?  430 VAL C CB  1 
ATOM   13268 C  CG1 . VAL C  2  430 ? 63.696  56.046  31.590  1.00 65.81  ?  430 VAL C CG1 1 
ATOM   13269 C  CG2 . VAL C  2  430 ? 63.879  56.791  29.194  1.00 69.94  ?  430 VAL C CG2 1 
ATOM   13270 N  N   . LYS C  2  431 ? 60.642  59.008  29.055  1.00 66.04  ?  431 LYS C N   1 
ATOM   13271 C  CA  . LYS C  2  431 ? 60.404  60.133  28.155  1.00 70.17  ?  431 LYS C CA  1 
ATOM   13272 C  C   . LYS C  2  431 ? 60.579  61.514  28.806  1.00 69.92  ?  431 LYS C C   1 
ATOM   13273 O  O   . LYS C  2  431 ? 61.281  62.344  28.232  1.00 80.68  ?  431 LYS C O   1 
ATOM   13274 C  CB  . LYS C  2  431 ? 59.042  60.026  27.440  1.00 64.45  ?  431 LYS C CB  1 
ATOM   13275 C  CG  . LYS C  2  431 ? 59.042  60.672  26.053  1.00 75.74  ?  431 LYS C CG  1 
ATOM   13276 C  CD  . LYS C  2  431 ? 57.677  60.621  25.370  1.00 76.54  ?  431 LYS C CD  1 
ATOM   13277 C  CE  . LYS C  2  431 ? 56.854  61.876  25.573  1.00 78.28  ?  431 LYS C CE  1 
ATOM   13278 N  NZ  . LYS C  2  431 ? 57.239  62.976  24.644  1.00 74.02  ?  431 LYS C NZ  1 
ATOM   13279 N  N   . PRO C  2  432 ? 60.008  61.815  29.992  1.00 62.34  ?  432 PRO C N   1 
ATOM   13280 C  CA  . PRO C  2  432 ? 60.222  63.151  30.574  1.00 68.22  ?  432 PRO C CA  1 
ATOM   13281 C  C   . PRO C  2  432 ? 61.694  63.533  30.677  1.00 71.14  ?  432 PRO C C   1 
ATOM   13282 O  O   . PRO C  2  432 ? 62.028  64.687  30.443  1.00 71.15  ?  432 PRO C O   1 
ATOM   13283 C  CB  . PRO C  2  432 ? 59.566  63.041  31.947  1.00 59.28  ?  432 PRO C CB  1 
ATOM   13284 C  CG  . PRO C  2  432 ? 58.525  62.022  31.762  1.00 70.77  ?  432 PRO C CG  1 
ATOM   13285 C  CD  . PRO C  2  432 ? 59.143  61.000  30.863  1.00 80.19  ?  432 PRO C CD  1 
ATOM   13286 N  N   . LEU C  2  433 ? 62.575  62.573  31.001  1.00 68.03  ?  433 LEU C N   1 
ATOM   13287 C  CA  . LEU C  2  433 ? 64.004  62.858  31.101  1.00 65.69  ?  433 LEU C CA  1 
ATOM   13288 C  C   . LEU C  2  433 ? 64.575  63.096  29.708  1.00 78.40  ?  433 LEU C C   1 
ATOM   13289 O  O   . LEU C  2  433 ? 65.329  64.048  29.512  1.00 88.26  ?  433 LEU C O   1 
ATOM   13290 C  CB  . LEU C  2  433 ? 64.747  61.706  31.801  1.00 65.59  ?  433 LEU C CB  1 
ATOM   13291 C  CG  . LEU C  2  433 ? 66.267  61.866  31.948  1.00 62.49  ?  433 LEU C CG  1 
ATOM   13292 C  CD1 . LEU C  2  433 ? 66.619  63.083  32.781  1.00 48.29  ?  433 LEU C CD1 1 
ATOM   13293 C  CD2 . LEU C  2  433 ? 66.880  60.629  32.574  1.00 60.82  ?  433 LEU C CD2 1 
ATOM   13294 N  N   . ALA C  2  434 ? 64.207  62.250  28.737  1.00 70.68  ?  434 ALA C N   1 
ATOM   13295 C  CA  . ALA C  2  434 ? 64.680  62.391  27.363  1.00 65.46  ?  434 ALA C CA  1 
ATOM   13296 C  C   . ALA C  2  434 ? 64.239  63.732  26.775  1.00 80.34  ?  434 ALA C C   1 
ATOM   13297 O  O   . ALA C  2  434 ? 65.027  64.392  26.100  1.00 84.37  ?  434 ALA C O   1 
ATOM   13298 C  CB  . ALA C  2  434 ? 64.145  61.251  26.513  1.00 59.15  ?  434 ALA C CB  1 
ATOM   13299 N  N   . ASP C  2  435 ? 62.981  64.135  27.046  1.00 76.70  ?  435 ASP C N   1 
ATOM   13300 C  CA  . ASP C  2  435 ? 62.397  65.389  26.563  1.00 68.49  ?  435 ASP C CA  1 
ATOM   13301 C  C   . ASP C  2  435 ? 63.158  66.609  27.079  1.00 71.80  ?  435 ASP C C   1 
ATOM   13302 O  O   . ASP C  2  435 ? 63.437  67.530  26.311  1.00 73.85  ?  435 ASP C O   1 
ATOM   13303 C  CB  . ASP C  2  435 ? 60.918  65.487  26.987  1.00 73.38  ?  435 ASP C CB  1 
ATOM   13304 C  CG  . ASP C  2  435 ? 59.973  64.580  26.219  1.00 92.26  ?  435 ASP C CG  1 
ATOM   13305 O  OD1 . ASP C  2  435 ? 60.459  63.784  25.379  1.00 91.37  ?  435 ASP C OD1 1 
ATOM   13306 O  OD2 . ASP C  2  435 ? 58.746  64.663  26.458  1.00 95.39  ?  435 ASP C OD2 1 
ATOM   13307 N  N   . VAL C  2  436 ? 63.497  66.612  28.375  1.00 65.05  ?  436 VAL C N   1 
ATOM   13308 C  CA  . VAL C  2  436 ? 64.220  67.717  29.006  1.00 73.60  ?  436 VAL C CA  1 
ATOM   13309 C  C   . VAL C  2  436 ? 65.647  67.831  28.439  1.00 83.36  ?  436 VAL C C   1 
ATOM   13310 O  O   . VAL C  2  436 ? 66.168  68.941  28.318  1.00 83.79  ?  436 VAL C O   1 
ATOM   13311 C  CB  . VAL C  2  436 ? 64.231  67.544  30.549  1.00 69.19  ?  436 VAL C CB  1 
ATOM   13312 C  CG1 . VAL C  2  436 ? 65.118  68.577  31.221  1.00 79.45  ?  436 VAL C CG1 1 
ATOM   13313 C  CG2 . VAL C  2  436 ? 62.823  67.629  31.124  1.00 75.89  ?  436 VAL C CG2 1 
ATOM   13314 N  N   . LEU C  2  437 ? 66.276  66.695  28.092  1.00 76.00  ?  437 LEU C N   1 
ATOM   13315 C  CA  . LEU C  2  437 ? 67.636  66.691  27.553  1.00 64.75  ?  437 LEU C CA  1 
ATOM   13316 C  C   . LEU C  2  437 ? 67.684  67.186  26.108  1.00 73.76  ?  437 LEU C C   1 
ATOM   13317 O  O   . LEU C  2  437 ? 68.567  67.971  25.770  1.00 74.04  ?  437 LEU C O   1 
ATOM   13318 C  CB  . LEU C  2  437 ? 68.247  65.283  27.649  1.00 56.74  ?  437 LEU C CB  1 
ATOM   13319 C  CG  . LEU C  2  437 ? 68.616  64.810  29.069  1.00 74.44  ?  437 LEU C CG  1 
ATOM   13320 C  CD1 . LEU C  2  437 ? 68.644  63.297  29.157  1.00 52.56  ?  437 LEU C CD1 1 
ATOM   13321 C  CD2 . LEU C  2  437 ? 69.954  65.381  29.514  1.00 62.96  ?  437 LEU C CD2 1 
ATOM   13322 N  N   . VAL C  2  438 ? 66.736  66.746  25.280  1.00 68.77  ?  438 VAL C N   1 
ATOM   13323 C  CA  . VAL C  2  438 ? 66.712  67.161  23.846  1.00 72.83  ?  438 VAL C CA  1 
ATOM   13324 C  C   . VAL C  2  438 ? 66.372  68.653  23.765  1.00 77.93  ?  438 VAL C C   1 
ATOM   13325 O  O   . VAL C  2  438 ? 67.006  69.355  22.954  1.00 81.61  ?  438 VAL C O   1 
ATOM   13326 C  CB  . VAL C  2  438 ? 65.710  66.313  23.040  1.00 63.77  ?  438 VAL C CB  1 
ATOM   13327 C  CG1 . VAL C  2  438 ? 65.155  67.073  21.845  1.00 74.70  ?  438 VAL C CG1 1 
ATOM   13328 C  CG2 . VAL C  2  438 ? 66.319  64.991  22.601  1.00 71.47  ?  438 VAL C CG2 1 
ATOM   13329 N  N   . SER C  2  439 ? 65.420  69.116  24.578  1.00 78.20  ?  439 SER C N   1 
ATOM   13330 C  CA  . SER C  2  439 ? 64.988  70.509  24.543  1.00 74.23  ?  439 SER C CA  1 
ATOM   13331 C  C   . SER C  2  439 ? 66.151  71.447  24.871  1.00 72.48  ?  439 SER C C   1 
ATOM   13332 O  O   . SER C  2  439 ? 66.276  72.511  24.265  1.00 84.15  ?  439 SER C O   1 
ATOM   13333 C  CB  . SER C  2  439 ? 63.842  70.735  25.524  1.00 68.87  ?  439 SER C CB  1 
ATOM   13334 O  OG  . SER C  2  439 ? 64.291  70.686  26.869  1.00 78.92  ?  439 SER C OG  1 
ATOM   13335 N  N   . GLY C  2  440 ? 66.990  71.043  25.816  1.00 66.21  ?  440 GLY C N   1 
ATOM   13336 C  CA  . GLY C  2  440 ? 68.136  71.837  26.224  1.00 65.50  ?  440 GLY C CA  1 
ATOM   13337 C  C   . GLY C  2  440 ? 67.989  72.452  27.598  1.00 73.04  ?  440 GLY C C   1 
ATOM   13338 O  O   . GLY C  2  440 ? 68.899  73.147  28.052  1.00 81.95  ?  440 GLY C O   1 
ATOM   13339 N  N   . VAL C  2  441 ? 66.856  72.193  28.294  1.00 76.58  ?  441 VAL C N   1 
ATOM   13340 C  CA  . VAL C  2  441 ? 66.619  72.718  29.647  1.00 76.69  ?  441 VAL C CA  1 
ATOM   13341 C  C   . VAL C  2  441 ? 67.741  72.191  30.544  1.00 69.93  ?  441 VAL C C   1 
ATOM   13342 O  O   . VAL C  2  441 ? 68.353  72.968  31.278  1.00 71.72  ?  441 VAL C O   1 
ATOM   13343 C  CB  . VAL C  2  441 ? 65.211  72.340  30.176  1.00 82.55  ?  441 VAL C CB  1 
ATOM   13344 C  CG1 . VAL C  2  441 ? 65.100  72.589  31.680  1.00 75.50  ?  441 VAL C CG1 1 
ATOM   13345 C  CG2 . VAL C  2  441 ? 64.121  73.099  29.421  1.00 57.02  ?  441 VAL C CG2 1 
ATOM   13346 N  N   . LEU C  2  442 ? 68.037  70.878  30.435  1.00 75.19  ?  442 LEU C N   1 
ATOM   13347 C  CA  . LEU C  2  442 ? 69.146  70.244  31.138  1.00 72.22  ?  442 LEU C CA  1 
ATOM   13348 C  C   . LEU C  2  442 ? 70.228  70.075  30.093  1.00 77.01  ?  442 LEU C C   1 
ATOM   13349 O  O   . LEU C  2  442 ? 70.006  69.398  29.090  1.00 74.38  ?  442 LEU C O   1 
ATOM   13350 C  CB  . LEU C  2  442 ? 68.797  68.857  31.693  1.00 58.46  ?  442 LEU C CB  1 
ATOM   13351 C  CG  . LEU C  2  442 ? 68.075  68.795  33.023  1.00 64.83  ?  442 LEU C CG  1 
ATOM   13352 C  CD1 . LEU C  2  442 ? 67.728  67.358  33.365  1.00 55.73  ?  442 LEU C CD1 1 
ATOM   13353 C  CD2 . LEU C  2  442 ? 68.907  69.382  34.142  1.00 83.63  ?  442 LEU C CD2 1 
ATOM   13354 N  N   . ARG C  2  443 ? 71.388  70.689  30.315  1.00 68.79  ?  443 ARG C N   1 
ATOM   13355 C  CA  . ARG C  2  443 ? 72.508  70.602  29.387  1.00 70.86  ?  443 ARG C CA  1 
ATOM   13356 C  C   . ARG C  2  443 ? 72.964  69.142  29.182  1.00 72.63  ?  443 ARG C C   1 
ATOM   13357 O  O   . ARG C  2  443 ? 73.416  68.787  28.093  1.00 71.53  ?  443 ARG C O   1 
ATOM   13358 C  CB  . ARG C  2  443 ? 73.673  71.472  29.890  1.00 70.42  ?  443 ARG C CB  1 
ATOM   13359 C  CG  . ARG C  2  443 ? 73.414  72.976  29.788  1.00 61.00  ?  443 ARG C CG  1 
ATOM   13360 C  CD  . ARG C  2  443 ? 73.595  73.493  28.374  1.00 76.72  ?  443 ARG C CD  1 
ATOM   13361 N  NE  . ARG C  2  443 ? 72.372  73.362  27.580  1.00 78.10  ?  443 ARG C NE  1 
ATOM   13362 C  CZ  . ARG C  2  443 ? 72.327  73.380  26.251  1.00 83.12  ?  443 ARG C CZ  1 
ATOM   13363 N  NH1 . ARG C  2  443 ? 73.441  73.525  25.541  1.00 92.93  ?  443 ARG C NH1 1 
ATOM   13364 N  NH2 . ARG C  2  443 ? 71.168  73.255  25.619  1.00 90.08  ?  443 ARG C NH2 1 
ATOM   13365 N  N   . GLY C  2  444 ? 72.832  68.316  30.216  1.00 70.55  ?  444 GLY C N   1 
ATOM   13366 C  CA  . GLY C  2  444 ? 73.205  66.911  30.139  1.00 65.83  ?  444 GLY C CA  1 
ATOM   13367 C  C   . GLY C  2  444 ? 73.035  66.179  31.452  1.00 59.94  ?  444 GLY C C   1 
ATOM   13368 O  O   . GLY C  2  444 ? 72.474  66.718  32.406  1.00 71.42  ?  444 GLY C O   1 
ATOM   13369 N  N   . ALA C  2  445 ? 73.519  64.939  31.511  1.00 63.58  ?  445 ALA C N   1 
ATOM   13370 C  CA  . ALA C  2  445 ? 73.441  64.132  32.724  1.00 61.55  ?  445 ALA C CA  1 
ATOM   13371 C  C   . ALA C  2  445 ? 74.815  63.534  32.992  1.00 66.69  ?  445 ALA C C   1 
ATOM   13372 O  O   . ALA C  2  445 ? 75.385  62.895  32.111  1.00 69.89  ?  445 ALA C O   1 
ATOM   13373 C  CB  . ALA C  2  445 ? 72.405  63.031  32.562  1.00 45.25  ?  445 ALA C CB  1 
ATOM   13374 N  N   . ALA C  2  446 ? 75.356  63.762  34.193  1.00 61.47  ?  446 ALA C N   1 
ATOM   13375 C  CA  . ALA C  2  446 ? 76.667  63.246  34.575  1.00 54.41  ?  446 ALA C CA  1 
ATOM   13376 C  C   . ALA C  2  446 ? 76.544  62.267  35.739  1.00 64.00  ?  446 ALA C C   1 
ATOM   13377 O  O   . ALA C  2  446 ? 75.616  62.368  36.540  1.00 65.40  ?  446 ALA C O   1 
ATOM   13378 C  CB  . ALA C  2  446 ? 77.584  64.394  34.961  1.00 59.17  ?  446 ALA C CB  1 
ATOM   13379 N  N   . ALA C  2  447 ? 77.487  61.323  35.832  1.00 60.65  ?  447 ALA C N   1 
ATOM   13380 C  CA  . ALA C  2  447 ? 77.508  60.324  36.895  1.00 61.67  ?  447 ALA C CA  1 
ATOM   13381 C  C   . ALA C  2  447 ? 78.806  60.448  37.674  1.00 61.93  ?  447 ALA C C   1 
ATOM   13382 O  O   . ALA C  2  447 ? 79.842  60.014  37.186  1.00 64.71  ?  447 ALA C O   1 
ATOM   13383 C  CB  . ALA C  2  447 ? 77.393  58.929  36.298  1.00 50.17  ?  447 ALA C CB  1 
ATOM   13384 N  N   . VAL C  2  448 ? 78.765  61.048  38.871  1.00 60.90  ?  448 VAL C N   1 
ATOM   13385 C  CA  . VAL C  2  448 ? 79.968  61.193  39.689  1.00 59.02  ?  448 VAL C CA  1 
ATOM   13386 C  C   . VAL C  2  448 ? 80.046  59.991  40.638  1.00 61.96  ?  448 VAL C C   1 
ATOM   13387 O  O   . VAL C  2  448 ? 79.266  59.877  41.581  1.00 65.14  ?  448 VAL C O   1 
ATOM   13388 C  CB  . VAL C  2  448 ? 80.023  62.543  40.440  1.00 66.82  ?  448 VAL C CB  1 
ATOM   13389 C  CG1 . VAL C  2  448 ? 81.295  62.642  41.275  1.00 61.93  ?  448 VAL C CG1 1 
ATOM   13390 C  CG2 . VAL C  2  448 ? 79.929  63.713  39.465  1.00 69.35  ?  448 VAL C CG2 1 
ATOM   13391 N  N   . VAL C  2  449 ? 80.993  59.098  40.360  1.00 73.41  ?  449 VAL C N   1 
ATOM   13392 C  CA  . VAL C  2  449 ? 81.175  57.887  41.206  1.00 73.21  ?  449 VAL C CA  1 
ATOM   13393 C  C   . VAL C  2  449 ? 82.646  57.903  41.620  1.00 67.45  ?  449 VAL C C   1 
ATOM   13394 O  O   . VAL C  2  449 ? 83.382  58.764  41.113  1.00 79.07  ?  449 VAL C O   1 
ATOM   13395 C  CB  . VAL C  2  449 ? 80.660  56.643  40.469  1.00 66.32  ?  449 VAL C CB  1 
ATOM   13396 C  CG1 . VAL C  2  449 ? 79.202  56.799  40.065  1.00 77.02  ?  449 VAL C CG1 1 
ATOM   13397 C  CG2 . VAL C  2  449 ? 81.516  56.365  39.247  1.00 42.09  ?  449 VAL C CG2 1 
ATOM   13398 N  N   . GLY C  2  450 ? 83.061  56.998  42.504  1.00 54.27  ?  450 GLY C N   1 
ATOM   13399 C  CA  . GLY C  2  450 ? 84.495  56.957  42.842  1.00 60.05  ?  450 GLY C CA  1 
ATOM   13400 C  C   . GLY C  2  450 ? 84.823  56.726  44.302  1.00 67.27  ?  450 GLY C C   1 
ATOM   13401 O  O   . GLY C  2  450 ? 83.882  56.591  45.107  1.00 73.35  ?  450 GLY C O   1 
ATOM   13402 N  N   . CYS C  2  451 ? 86.117  56.683  44.647  1.00 64.97  ?  451 CYS C N   1 
ATOM   13403 C  CA  . CYS C  2  451 ? 86.547  56.369  46.038  1.00 74.58  ?  451 CYS C CA  1 
ATOM   13404 C  C   . CYS C  2  451 ? 87.187  57.580  46.717  1.00 61.61  ?  451 CYS C C   1 
ATOM   13405 O  O   . CYS C  2  451 ? 86.852  58.716  46.342  1.00 62.52  ?  451 CYS C O   1 
ATOM   13406 C  CB  . CYS C  2  451 ? 87.589  55.255  46.034  1.00 70.60  ?  451 CYS C CB  1 
ATOM   13407 S  SG  . CYS C  2  451 ? 87.518  54.244  44.516  1.00 56.82  ?  451 CYS C SG  1 
ATOM   13408 N  N   . ASN C  2  452 ? 88.071  57.328  47.688  1.00 69.88  ?  452 ASN C N   1 
ATOM   13409 C  CA  . ASN C  2  452 ? 88.791  58.422  48.387  1.00 72.64  ?  452 ASN C CA  1 
ATOM   13410 C  C   . ASN C  2  452 ? 90.284  58.114  48.259  1.00 72.28  ?  452 ASN C C   1 
ATOM   13411 O  O   . ASN C  2  452 ? 90.662  56.954  48.503  1.00 89.68  ?  452 ASN C O   1 
ATOM   13412 C  CB  . ASN C  2  452 ? 88.348  58.581  49.843  1.00 73.93  ?  452 ASN C CB  1 
ATOM   13413 C  CG  . ASN C  2  452 ? 87.107  59.434  49.997  1.00 76.20  ?  452 ASN C CG  1 
ATOM   13414 O  OD1 . ASN C  2  452 ? 86.283  59.186  50.873  1.00 86.04  ?  452 ASN C OD1 1 
ATOM   13415 N  ND2 . ASN C  2  452 ? 86.966  60.440  49.150  1.00 82.51  ?  452 ASN C ND2 1 
ATOM   13416 N  N   . ASN C  2  453 ? 91.093  59.103  47.877  1.00 68.51  ?  453 ASN C N   1 
ATOM   13417 C  CA  . ASN C  2  453 ? 92.513  58.855  47.656  1.00 63.42  ?  453 ASN C CA  1 
ATOM   13418 C  C   . ASN C  2  453 ? 93.353  59.885  48.413  1.00 67.44  ?  453 ASN C C   1 
ATOM   13419 O  O   . ASN C  2  453 ? 93.074  61.074  48.280  1.00 85.30  ?  453 ASN C O   1 
ATOM   13420 C  CB  . ASN C  2  453 ? 92.833  58.906  46.165  1.00 69.99  ?  453 ASN C CB  1 
ATOM   13421 C  CG  . ASN C  2  453 ? 94.093  58.164  45.801  1.00 70.30  ?  453 ASN C CG  1 
ATOM   13422 O  OD1 . ASN C  2  453 ? 95.106  58.244  46.497  1.00 69.97  ?  453 ASN C OD1 1 
ATOM   13423 N  ND2 . ASN C  2  453 ? 94.065  57.421  44.706  1.00 61.47  ?  453 ASN C ND2 1 
ATOM   13424 N  N   . PRO C  2  454 ? 94.387  59.497  49.196  1.00 65.44  ?  454 PRO C N   1 
ATOM   13425 C  CA  . PRO C  2  454 ? 95.182  60.517  49.902  1.00 65.64  ?  454 PRO C CA  1 
ATOM   13426 C  C   . PRO C  2  454 ? 95.941  61.477  48.983  1.00 66.55  ?  454 PRO C C   1 
ATOM   13427 O  O   . PRO C  2  454 ? 96.548  62.430  49.465  1.00 76.62  ?  454 PRO C O   1 
ATOM   13428 C  CB  . PRO C  2  454 ? 96.138  59.701  50.775  1.00 68.47  ?  454 PRO C CB  1 
ATOM   13429 C  CG  . PRO C  2  454 ? 95.638  58.316  50.753  1.00 76.54  ?  454 PRO C CG  1 
ATOM   13430 C  CD  . PRO C  2  454 ? 94.885  58.143  49.486  1.00 74.04  ?  454 PRO C CD  1 
ATOM   13431 N  N   . LYS C  2  455 ? 95.909  61.243  47.667  1.00 65.31  ?  455 LYS C N   1 
ATOM   13432 C  CA  . LYS C  2  455 ? 96.558  62.140  46.709  1.00 70.46  ?  455 LYS C CA  1 
ATOM   13433 C  C   . LYS C  2  455 ? 95.656  63.390  46.495  1.00 75.63  ?  455 LYS C C   1 
ATOM   13434 O  O   . LYS C  2  455 ? 96.132  64.422  46.017  1.00 81.44  ?  455 LYS C O   1 
ATOM   13435 C  CB  . LYS C  2  455 ? 96.800  61.419  45.367  1.00 67.11  ?  455 LYS C CB  1 
ATOM   13436 C  CG  . LYS C  2  455 ? 97.439  60.036  45.504  1.00 77.09  ?  455 LYS C CG  1 
ATOM   13437 C  CD  . LYS C  2  455 ? 97.813  59.428  44.161  1.00 56.76  ?  455 LYS C CD  1 
ATOM   13438 C  CE  . LYS C  2  455 ? 98.912  58.401  44.299  1.00 62.87  ?  455 LYS C CE  1 
ATOM   13439 N  NZ  . LYS C  2  455 ? 98.978  57.478  43.137  1.00 75.75  ?  455 LYS C NZ  1 
ATOM   13440 N  N   . VAL C  2  456 ? 94.355  63.279  46.854  1.00 74.47  ?  456 VAL C N   1 
ATOM   13441 C  CA  . VAL C  2  456 ? 93.343  64.324  46.742  1.00 63.62  ?  456 VAL C CA  1 
ATOM   13442 C  C   . VAL C  2  456 ? 92.820  64.644  48.151  1.00 72.10  ?  456 VAL C C   1 
ATOM   13443 O  O   . VAL C  2  456 ? 92.680  63.733  48.970  1.00 68.36  ?  456 VAL C O   1 
ATOM   13444 C  CB  . VAL C  2  456 ? 92.178  63.831  45.846  1.00 53.71  ?  456 VAL C CB  1 
ATOM   13445 C  CG1 . VAL C  2  456 ? 91.162  64.941  45.607  1.00 66.40  ?  456 VAL C CG1 1 
ATOM   13446 C  CG2 . VAL C  2  456 ? 92.694  63.269  44.523  1.00 52.36  ?  456 VAL C CG2 1 
ATOM   13447 N  N   . VAL C  2  457 ? 92.511  65.919  48.413  1.00 79.82  ?  457 VAL C N   1 
ATOM   13448 C  CA  . VAL C  2  457 ? 91.893  66.277  49.724  1.00 65.57  ?  457 VAL C CA  1 
ATOM   13449 C  C   . VAL C  2  457 ? 90.574  65.507  49.821  1.00 75.36  ?  457 VAL C C   1 
ATOM   13450 O  O   . VAL C  2  457 ? 89.803  65.547  48.843  1.00 81.69  ?  457 VAL C O   1 
ATOM   13451 C  CB  . VAL C  2  457 ? 91.682  67.795  49.868  1.00 61.75  ?  457 VAL C CB  1 
ATOM   13452 C  CG1 . VAL C  2  457 ? 90.936  68.141  51.147  1.00 77.83  ?  457 VAL C CG1 1 
ATOM   13453 C  CG2 . VAL C  2  457 ? 92.998  68.553  49.794  1.00 63.34  ?  457 VAL C CG2 1 
ATOM   13454 N  N   . GLN C  2  458 ? 90.320  64.842  50.949  1.00 67.61  ?  458 GLN C N   1 
ATOM   13455 C  CA  . GLN C  2  458 ? 89.114  63.976  51.057  1.00 77.18  ?  458 GLN C CA  1 
ATOM   13456 C  C   . GLN C  2  458 ? 87.845  64.748  50.680  1.00 74.80  ?  458 GLN C C   1 
ATOM   13457 O  O   . GLN C  2  458 ? 87.615  65.818  51.274  1.00 72.83  ?  458 GLN C O   1 
ATOM   13458 C  CB  . GLN C  2  458 ? 89.004  63.395  52.468  1.00 77.08  ?  458 GLN C CB  1 
ATOM   13459 C  CG  . GLN C  2  458 ? 88.350  62.022  52.512  1.00 64.12  ?  458 GLN C CG  1 
ATOM   13460 C  CD  . GLN C  2  458 ? 87.019  62.052  53.222  1.00 90.07  ?  458 GLN C CD  1 
ATOM   13461 O  OE1 . GLN C  2  458 ? 86.800  62.839  54.140  1.00 90.57  ?  458 GLN C OE1 1 
ATOM   13462 N  NE2 . GLN C  2  458 ? 86.113  61.186  52.798  1.00 94.88  ?  458 GLN C NE2 1 
ATOM   13463 N  N   . ASP C  2  459 ? 87.066  64.228  49.725  1.00 64.54  ?  459 ASP C N   1 
ATOM   13464 C  CA  . ASP C  2  459 ? 85.757  64.836  49.354  1.00 71.88  ?  459 ASP C CA  1 
ATOM   13465 C  C   . ASP C  2  459 ? 85.930  66.148  48.577  1.00 75.90  ?  459 ASP C C   1 
ATOM   13466 O  O   . ASP C  2  459 ? 84.936  66.594  47.975  1.00 79.57  ?  459 ASP C O   1 
ATOM   13467 C  CB  . ASP C  2  459 ? 84.864  65.010  50.586  1.00 88.34  ?  459 ASP C CB  1 
ATOM   13468 C  CG  . ASP C  2  459 ? 84.672  63.724  51.371  1.00 90.43  ?  459 ASP C CG  1 
ATOM   13469 O  OD1 . ASP C  2  459 ? 84.785  62.643  50.760  1.00 76.73  ?  459 ASP C OD1 1 
ATOM   13470 O  OD2 . ASP C  2  459 ? 84.414  63.814  52.587  1.00 99.46  ?  459 ASP C OD2 1 
ATOM   13471 N  N   . SER C  2  460 ? 87.125  66.745  48.576  1.00 74.04  ?  460 SER C N   1 
ATOM   13472 C  CA  . SER C  2  460 ? 87.275  68.033  47.911  1.00 68.66  ?  460 SER C CA  1 
ATOM   13473 C  C   . SER C  2  460 ? 86.868  67.956  46.438  1.00 68.96  ?  460 SER C C   1 
ATOM   13474 O  O   . SER C  2  460 ? 85.997  68.710  46.007  1.00 73.03  ?  460 SER C O   1 
ATOM   13475 C  CB  . SER C  2  460 ? 88.713  68.529  48.029  1.00 71.20  ?  460 SER C CB  1 
ATOM   13476 O  OG  . SER C  2  460 ? 88.901  69.724  47.290  1.00 101.42 ?  460 SER C OG  1 
ATOM   13477 N  N   . ALA C  2  461 ? 87.482  67.048  45.670  1.00 68.33  ?  461 ALA C N   1 
ATOM   13478 C  CA  . ALA C  2  461 ? 87.173  66.920  44.252  1.00 68.97  ?  461 ALA C CA  1 
ATOM   13479 C  C   . ALA C  2  461 ? 85.753  66.436  44.005  1.00 69.44  ?  461 ALA C C   1 
ATOM   13480 O  O   . ALA C  2  461 ? 85.165  66.823  43.006  1.00 78.38  ?  461 ALA C O   1 
ATOM   13481 C  CB  . ALA C  2  461 ? 88.165  65.992  43.582  1.00 70.72  ?  461 ALA C CB  1 
ATOM   13482 N  N   . HIS C  2  462 ? 85.194  65.603  44.897  1.00 73.81  ?  462 HIS C N   1 
ATOM   13483 C  CA  . HIS C  2  462 ? 83.826  65.104  44.738  1.00 65.38  ?  462 HIS C CA  1 
ATOM   13484 C  C   . HIS C  2  462 ? 82.812  66.249  44.809  1.00 69.27  ?  462 HIS C C   1 
ATOM   13485 O  O   . HIS C  2  462 ? 81.945  66.363  43.945  1.00 59.81  ?  462 HIS C O   1 
ATOM   13486 C  CB  . HIS C  2  462 ? 83.483  64.071  45.829  1.00 71.74  ?  462 HIS C CB  1 
ATOM   13487 C  CG  . HIS C  2  462 ? 84.069  62.709  45.622  1.00 66.78  ?  462 HIS C CG  1 
ATOM   13488 N  ND1 . HIS C  2  462 ? 83.792  61.968  44.490  1.00 76.91  ?  462 HIS C ND1 1 
ATOM   13489 C  CD2 . HIS C  2  462 ? 84.862  61.979  46.440  1.00 62.61  ?  462 HIS C CD2 1 
ATOM   13490 C  CE1 . HIS C  2  462 ? 84.440  60.824  44.641  1.00 73.63  ?  462 HIS C CE1 1 
ATOM   13491 N  NE2 . HIS C  2  462 ? 85.095  60.786  45.802  1.00 65.16  ?  462 HIS C NE2 1 
ATOM   13492 N  N   . ILE C  2  463 ? 82.921  67.097  45.837  1.00 68.35  ?  463 ILE C N   1 
ATOM   13493 C  CA  . ILE C  2  463 ? 81.993  68.210  46.017  1.00 68.66  ?  463 ILE C CA  1 
ATOM   13494 C  C   . ILE C  2  463 ? 82.205  69.279  44.941  1.00 75.21  ?  463 ILE C C   1 
ATOM   13495 O  O   . ILE C  2  463 ? 81.239  69.717  44.322  1.00 81.11  ?  463 ILE C O   1 
ATOM   13496 C  CB  . ILE C  2  463 ? 82.113  68.791  47.452  1.00 58.38  ?  463 ILE C CB  1 
ATOM   13497 C  CG1 . ILE C  2  463 ? 81.770  67.727  48.528  1.00 70.64  ?  463 ILE C CG1 1 
ATOM   13498 C  CG2 . ILE C  2  463 ? 81.254  70.037  47.616  1.00 69.45  ?  463 ILE C CG2 1 
ATOM   13499 C  CD1 . ILE C  2  463 ? 80.444  66.941  48.345  1.00 64.77  ?  463 ILE C CD1 1 
ATOM   13500 N  N   . GLU C  2  464 ? 83.456  69.672  44.704  1.00 72.58  ?  464 GLU C N   1 
ATOM   13501 C  CA  . GLU C  2  464 ? 83.749  70.701  43.671  1.00 66.13  ?  464 GLU C CA  1 
ATOM   13502 C  C   . GLU C  2  464 ? 83.213  70.236  42.314  1.00 61.65  ?  464 GLU C C   1 
ATOM   13503 O  O   . GLU C  2  464 ? 82.663  71.077  41.582  1.00 64.34  ?  464 GLU C O   1 
ATOM   13504 C  CB  . GLU C  2  464 ? 85.253  70.965  43.598  1.00 71.90  ?  464 GLU C CB  1 
ATOM   13505 C  CG  . GLU C  2  464 ? 85.820  71.579  44.864  1.00 81.30  ?  464 GLU C CG  1 
ATOM   13506 C  CD  . GLU C  2  464 ? 85.180  72.896  45.267  1.00 107.42 ?  464 GLU C CD  1 
ATOM   13507 O  OE1 . GLU C  2  464 ? 84.903  73.715  44.369  1.00 112.30 ?  464 GLU C OE1 1 
ATOM   13508 O  OE2 . GLU C  2  464 ? 84.959  73.099  46.477  1.00 114.96 ?  464 GLU C OE2 1 
ATOM   13509 N  N   . THR C  2  465 ? 83.367  68.949  41.994  1.00 68.66  ?  465 THR C N   1 
ATOM   13510 C  CA  . THR C  2  465 ? 82.933  68.420  40.702  1.00 68.57  ?  465 THR C CA  1 
ATOM   13511 C  C   . THR C  2  465 ? 81.408  68.415  40.626  1.00 68.52  ?  465 THR C C   1 
ATOM   13512 O  O   . THR C  2  465 ? 80.843  68.935  39.667  1.00 65.28  ?  465 THR C O   1 
ATOM   13513 C  CB  . THR C  2  465 ? 83.501  67.010  40.482  1.00 63.74  ?  465 THR C CB  1 
ATOM   13514 O  OG1 . THR C  2  465 ? 84.922  67.090  40.387  1.00 70.14  ?  465 THR C OG1 1 
ATOM   13515 C  CG2 . THR C  2  465 ? 82.945  66.341  39.243  1.00 63.42  ?  465 THR C CG2 1 
ATOM   13516 N  N   . ILE C  2  466 ? 80.733  67.840  41.638  1.00 72.28  ?  466 ILE C N   1 
ATOM   13517 C  CA  . ILE C  2  466 ? 79.271  67.778  41.644  1.00 70.77  ?  466 ILE C CA  1 
ATOM   13518 C  C   . ILE C  2  466 ? 78.688  69.190  41.582  1.00 66.10  ?  466 ILE C C   1 
ATOM   13519 O  O   . ILE C  2  466 ? 77.837  69.468  40.741  1.00 81.85  ?  466 ILE C O   1 
ATOM   13520 C  CB  . ILE C  2  466 ? 78.739  66.989  42.871  1.00 64.79  ?  466 ILE C CB  1 
ATOM   13521 C  CG1 . ILE C  2  466 ? 79.175  65.509  42.801  1.00 57.76  ?  466 ILE C CG1 1 
ATOM   13522 C  CG2 . ILE C  2  466 ? 77.214  67.090  42.947  1.00 61.12  ?  466 ILE C CG2 1 
ATOM   13523 C  CD1 . ILE C  2  466 ? 79.013  64.729  44.098  1.00 66.51  ?  466 ILE C CD1 1 
ATOM   13524 N  N   . LYS C  2  467 ? 79.176  70.088  42.442  1.00 67.72  ?  467 LYS C N   1 
ATOM   13525 C  CA  . LYS C  2  467 ? 78.716  71.473  42.489  1.00 64.43  ?  467 LYS C CA  1 
ATOM   13526 C  C   . LYS C  2  467 ? 78.775  72.162  41.121  1.00 70.53  ?  467 LYS C C   1 
ATOM   13527 O  O   . LYS C  2  467 ? 77.791  72.757  40.693  1.00 86.18  ?  467 LYS C O   1 
ATOM   13528 C  CB  . LYS C  2  467 ? 79.556  72.282  43.491  1.00 65.82  ?  467 LYS C CB  1 
ATOM   13529 C  CG  . LYS C  2  467 ? 79.139  72.133  44.953  1.00 59.03  ?  467 LYS C CG  1 
ATOM   13530 C  CD  . LYS C  2  467 ? 79.374  73.434  45.710  1.00 73.32  ?  467 LYS C CD  1 
ATOM   13531 C  CE  . LYS C  2  467 ? 79.532  73.256  47.189  1.00 75.27  ?  467 LYS C CE  1 
ATOM   13532 N  NZ  . LYS C  2  467 ? 80.522  74.212  47.750  1.00 103.43 ?  467 LYS C NZ  1 
ATOM   13533 N  N   . GLY C  2  468 ? 79.922  72.082  40.457  1.00 68.64  ?  468 GLY C N   1 
ATOM   13534 C  CA  . GLY C  2  468 ? 80.117  72.711  39.159  1.00 64.76  ?  468 GLY C CA  1 
ATOM   13535 C  C   . GLY C  2  468 ? 79.221  72.170  38.067  1.00 60.41  ?  468 GLY C C   1 
ATOM   13536 O  O   . GLY C  2  468 ? 78.810  72.914  37.177  1.00 67.56  ?  468 GLY C O   1 
ATOM   13537 N  N   . LEU C  2  469 ? 78.917  70.874  38.115  1.00 68.55  ?  469 LEU C N   1 
ATOM   13538 C  CA  . LEU C  2  469 ? 78.067  70.256  37.105  1.00 65.46  ?  469 LEU C CA  1 
ATOM   13539 C  C   . LEU C  2  469 ? 76.610  70.677  37.309  1.00 67.76  ?  469 LEU C C   1 
ATOM   13540 O  O   . LEU C  2  469 ? 75.964  71.094  36.351  1.00 71.51  ?  469 LEU C O   1 
ATOM   13541 C  CB  . LEU C  2  469 ? 78.200  68.722  37.146  1.00 65.18  ?  469 LEU C CB  1 
ATOM   13542 C  CG  . LEU C  2  469 ? 79.570  68.141  36.755  1.00 61.39  ?  469 LEU C CG  1 
ATOM   13543 C  CD1 . LEU C  2  469 ? 79.730  66.726  37.276  1.00 65.46  ?  469 LEU C CD1 1 
ATOM   13544 C  CD2 . LEU C  2  469 ? 79.769  68.150  35.255  1.00 54.97  ?  469 LEU C CD2 1 
ATOM   13545 N  N   . ILE C  2  470 ? 76.093  70.587  38.548  1.00 67.12  ?  470 ILE C N   1 
ATOM   13546 C  CA  . ILE C  2  470 ? 74.704  70.980  38.814  1.00 71.59  ?  470 ILE C CA  1 
ATOM   13547 C  C   . ILE C  2  470 ? 74.494  72.476  38.544  1.00 72.81  ?  470 ILE C C   1 
ATOM   13548 O  O   . ILE C  2  470 ? 73.423  72.860  38.082  1.00 76.11  ?  470 ILE C O   1 
ATOM   13549 C  CB  . ILE C  2  470 ? 74.191  70.542  40.218  1.00 64.39  ?  470 ILE C CB  1 
ATOM   13550 C  CG1 . ILE C  2  470 ? 75.051  71.110  41.360  1.00 67.67  ?  470 ILE C CG1 1 
ATOM   13551 C  CG2 . ILE C  2  470 ? 74.099  69.015  40.306  1.00 69.17  ?  470 ILE C CG2 1 
ATOM   13552 C  CD1 . ILE C  2  470 ? 74.401  71.017  42.727  1.00 66.54  ?  470 ILE C CD1 1 
ATOM   13553 N  N   . LYS C  2  471 ? 75.512  73.312  38.794  1.00 72.47  ?  471 LYS C N   1 
ATOM   13554 C  CA  . LYS C  2  471 ? 75.411  74.746  38.529  1.00 65.34  ?  471 LYS C CA  1 
ATOM   13555 C  C   . LYS C  2  471 ? 75.254  75.006  37.019  1.00 67.38  ?  471 LYS C C   1 
ATOM   13556 O  O   . LYS C  2  471 ? 74.599  75.973  36.632  1.00 72.07  ?  471 LYS C O   1 
ATOM   13557 C  CB  . LYS C  2  471 ? 76.653  75.480  39.065  1.00 60.74  ?  471 LYS C CB  1 
ATOM   13558 C  CG  . LYS C  2  471 ? 76.650  76.987  38.787  1.00 72.29  ?  471 LYS C CG  1 
ATOM   13559 C  CD  . LYS C  2  471 ? 76.859  77.834  40.044  1.00 98.06  ?  471 LYS C CD  1 
ATOM   13560 C  CE  . LYS C  2  471 ? 76.339  79.255  39.915  1.00 95.57  ?  471 LYS C CE  1 
ATOM   13561 N  NZ  . LYS C  2  471 ? 75.363  79.591  40.989  1.00 90.60  ?  471 LYS C NZ  1 
ATOM   13562 N  N   . ASN C  2  472 ? 75.850  74.148  36.171  1.00 68.31  ?  472 ASN C N   1 
ATOM   13563 C  CA  . ASN C  2  472 ? 75.763  74.289  34.717  1.00 72.45  ?  472 ASN C CA  1 
ATOM   13564 C  C   . ASN C  2  472 ? 74.586  73.501  34.120  1.00 72.90  ?  472 ASN C C   1 
ATOM   13565 O  O   . ASN C  2  472 ? 74.646  73.109  32.955  1.00 79.12  ?  472 ASN C O   1 
ATOM   13566 C  CB  . ASN C  2  472 ? 77.077  73.854  34.060  1.00 54.69  ?  472 ASN C CB  1 
ATOM   13567 C  CG  . ASN C  2  472 ? 78.171  74.880  34.173  1.00 59.99  ?  472 ASN C CG  1 
ATOM   13568 O  OD1 . ASN C  2  472 ? 78.560  75.506  33.183  1.00 82.02  ?  472 ASN C OD1 1 
ATOM   13569 N  ND2 . ASN C  2  472 ? 78.694  75.081  35.373  1.00 64.78  ?  472 ASN C ND2 1 
ATOM   13570 N  N   . ASP C  2  473 ? 73.514  73.285  34.903  1.00 64.47  ?  473 ASP C N   1 
ATOM   13571 C  CA  . ASP C  2  473 ? 72.316  72.573  34.454  1.00 63.40  ?  473 ASP C CA  1 
ATOM   13572 C  C   . ASP C  2  473 ? 72.589  71.138  33.999  1.00 73.31  ?  473 ASP C C   1 
ATOM   13573 O  O   . ASP C  2  473 ? 72.007  70.675  33.020  1.00 71.16  ?  473 ASP C O   1 
ATOM   13574 C  CB  . ASP C  2  473 ? 71.590  73.361  33.345  1.00 69.90  ?  473 ASP C CB  1 
ATOM   13575 C  CG  . ASP C  2  473 ? 70.835  74.566  33.848  1.00 85.72  ?  473 ASP C CG  1 
ATOM   13576 O  OD1 . ASP C  2  473 ? 70.413  74.552  35.023  1.00 79.82  ?  473 ASP C OD1 1 
ATOM   13577 O  OD2 . ASP C  2  473 ? 70.640  75.517  33.058  1.00 93.72  ?  473 ASP C OD2 1 
ATOM   13578 N  N   . VAL C  2  474 ? 73.454  70.423  34.718  1.00 71.22  ?  474 VAL C N   1 
ATOM   13579 C  CA  . VAL C  2  474 ? 73.761  69.034  34.397  1.00 68.30  ?  474 VAL C CA  1 
ATOM   13580 C  C   . VAL C  2  474 ? 73.283  68.205  35.581  1.00 65.78  ?  474 VAL C C   1 
ATOM   13581 O  O   . VAL C  2  474 ? 73.861  68.307  36.662  1.00 69.14  ?  474 VAL C O   1 
ATOM   13582 C  CB  . VAL C  2  474 ? 75.268  68.832  34.129  1.00 65.21  ?  474 VAL C CB  1 
ATOM   13583 C  CG1 . VAL C  2  474 ? 75.584  67.365  33.867  1.00 64.49  ?  474 VAL C CG1 1 
ATOM   13584 C  CG2 . VAL C  2  474 ? 75.730  69.699  32.964  1.00 61.46  ?  474 VAL C CG2 1 
ATOM   13585 N  N   . ILE C  2  475 ? 72.212  67.409  35.407  1.00 64.44  ?  475 ILE C N   1 
ATOM   13586 C  CA  . ILE C  2  475 ? 71.708  66.579  36.506  1.00 63.93  ?  475 ILE C CA  1 
ATOM   13587 C  C   . ILE C  2  475 ? 72.792  65.556  36.864  1.00 66.48  ?  475 ILE C C   1 
ATOM   13588 O  O   . ILE C  2  475 ? 73.371  64.942  35.969  1.00 68.00  ?  475 ILE C O   1 
ATOM   13589 C  CB  . ILE C  2  475 ? 70.335  65.923  36.182  1.00 61.64  ?  475 ILE C CB  1 
ATOM   13590 C  CG1 . ILE C  2  475 ? 69.722  65.291  37.449  1.00 57.41  ?  475 ILE C CG1 1 
ATOM   13591 C  CG2 . ILE C  2  475 ? 70.447  64.892  35.063  1.00 60.58  ?  475 ILE C CG2 1 
ATOM   13592 C  CD1 . ILE C  2  475 ? 68.229  65.013  37.368  1.00 49.99  ?  475 ILE C CD1 1 
ATOM   13593 N  N   . VAL C  2  476 ? 73.113  65.425  38.152  1.00 60.57  ?  476 VAL C N   1 
ATOM   13594 C  CA  . VAL C  2  476 ? 74.165  64.516  38.587  1.00 55.58  ?  476 VAL C CA  1 
ATOM   13595 C  C   . VAL C  2  476 ? 73.621  63.320  39.358  1.00 63.08  ?  476 VAL C C   1 
ATOM   13596 O  O   . VAL C  2  476 ? 72.827  63.489  40.275  1.00 79.52  ?  476 VAL C O   1 
ATOM   13597 C  CB  . VAL C  2  476 ? 75.200  65.288  39.431  1.00 63.58  ?  476 VAL C CB  1 
ATOM   13598 C  CG1 . VAL C  2  476 ? 76.248  64.344  40.006  1.00 55.99  ?  476 VAL C CG1 1 
ATOM   13599 C  CG2 . VAL C  2  476 ? 75.857  66.389  38.608  1.00 64.80  ?  476 VAL C CG2 1 
ATOM   13600 N  N   . VAL C  2  477 ? 74.071  62.114  38.994  1.00 60.00  ?  477 VAL C N   1 
ATOM   13601 C  CA  . VAL C  2  477 ? 73.685  60.869  39.660  1.00 56.78  ?  477 VAL C CA  1 
ATOM   13602 C  C   . VAL C  2  477 ? 74.954  60.384  40.352  1.00 59.63  ?  477 VAL C C   1 
ATOM   13603 O  O   . VAL C  2  477 ? 76.040  60.521  39.795  1.00 69.53  ?  477 VAL C O   1 
ATOM   13604 C  CB  . VAL C  2  477 ? 73.069  59.811  38.709  1.00 55.38  ?  477 VAL C CB  1 
ATOM   13605 C  CG1 . VAL C  2  477 ? 71.735  60.291  38.151  1.00 45.89  ?  477 VAL C CG1 1 
ATOM   13606 C  CG2 . VAL C  2  477 ? 74.017  59.437  37.576  1.00 58.00  ?  477 VAL C CG2 1 
ATOM   13607 N  N   . VAL C  2  478 ? 74.838  59.866  41.577  1.00 64.90  ?  478 VAL C N   1 
ATOM   13608 C  CA  . VAL C  2  478 ? 76.010  59.438  42.342  1.00 56.76  ?  478 VAL C CA  1 
ATOM   13609 C  C   . VAL C  2  478 ? 75.848  58.047  42.917  1.00 65.65  ?  478 VAL C C   1 
ATOM   13610 O  O   . VAL C  2  478 ? 74.725  57.596  43.143  1.00 72.79  ?  478 VAL C O   1 
ATOM   13611 C  CB  . VAL C  2  478 ? 76.326  60.441  43.483  1.00 51.18  ?  478 VAL C CB  1 
ATOM   13612 C  CG1 . VAL C  2  478 ? 76.822  61.765  42.937  1.00 54.46  ?  478 VAL C CG1 1 
ATOM   13613 C  CG2 . VAL C  2  478 ? 75.116  60.654  44.388  1.00 61.83  ?  478 VAL C CG2 1 
ATOM   13614 N  N   . THR C  2  479 ? 76.997  57.396  43.154  1.00 56.83  ?  479 THR C N   1 
ATOM   13615 C  CA  . THR C  2  479 ? 77.017  56.041  43.761  1.00 59.25  ?  479 THR C CA  1 
ATOM   13616 C  C   . THR C  2  479 ? 78.299  55.879  44.587  1.00 66.68  ?  479 THR C C   1 
ATOM   13617 O  O   . THR C  2  479 ? 79.223  56.687  44.384  1.00 79.70  ?  479 THR C O   1 
ATOM   13618 C  CB  . THR C  2  479 ? 76.898  54.938  42.701  1.00 58.96  ?  479 THR C CB  1 
ATOM   13619 O  OG1 . THR C  2  479 ? 78.154  54.797  42.038  1.00 62.33  ?  479 THR C OG1 1 
ATOM   13620 C  CG2 . THR C  2  479 ? 75.812  55.192  41.679  1.00 62.81  ?  479 THR C CG2 1 
ATOM   13621 N  N   . GLY C  2  480 ? 78.353  54.892  45.483  1.00 63.69  ?  480 GLY C N   1 
ATOM   13622 C  CA  . GLY C  2  480 ? 79.503  54.601  46.330  1.00 76.29  ?  480 GLY C CA  1 
ATOM   13623 C  C   . GLY C  2  480 ? 79.953  55.720  47.241  1.00 59.74  ?  480 GLY C C   1 
ATOM   13624 O  O   . GLY C  2  480 ? 79.132  56.463  47.770  1.00 83.34  ?  480 GLY C O   1 
ATOM   13625 N  N   . CYS C  2  481 ? 81.266  55.835  47.445  1.00 56.57  ?  481 CYS C N   1 
ATOM   13626 C  CA  . CYS C  2  481 ? 81.834  56.856  48.318  1.00 68.05  ?  481 CYS C CA  1 
ATOM   13627 C  C   . CYS C  2  481 ? 81.583  58.260  47.815  1.00 72.78  ?  481 CYS C C   1 
ATOM   13628 O  O   . CYS C  2  481 ? 81.527  59.182  48.627  1.00 78.64  ?  481 CYS C O   1 
ATOM   13629 C  CB  . CYS C  2  481 ? 83.320  56.604  48.524  1.00 77.90  ?  481 CYS C CB  1 
ATOM   13630 S  SG  . CYS C  2  481 ? 83.688  55.090  49.451  1.00 72.50  ?  481 CYS C SG  1 
ATOM   13631 N  N   . ALA C  2  482 ? 81.439  58.444  46.494  1.00 64.47  ?  482 ALA C N   1 
ATOM   13632 C  CA  . ALA C  2  482 ? 81.160  59.765  45.942  1.00 65.81  ?  482 ALA C CA  1 
ATOM   13633 C  C   . ALA C  2  482 ? 79.763  60.209  46.409  1.00 73.45  ?  482 ALA C C   1 
ATOM   13634 O  O   . ALA C  2  482 ? 79.590  61.348  46.835  1.00 67.35  ?  482 ALA C O   1 
ATOM   13635 C  CB  . ALA C  2  482 ? 81.221  59.719  44.425  1.00 64.41  ?  482 ALA C CB  1 
ATOM   13636 N  N   . ALA C  2  483 ? 78.779  59.291  46.366  1.00 70.28  ?  483 ALA C N   1 
ATOM   13637 C  CA  . ALA C  2  483 ? 77.419  59.575  46.812  1.00 63.53  ?  483 ALA C CA  1 
ATOM   13638 C  C   . ALA C  2  483 ? 77.415  59.917  48.286  1.00 66.43  ?  483 ALA C C   1 
ATOM   13639 O  O   . ALA C  2  483 ? 76.716  60.836  48.699  1.00 81.22  ?  483 ALA C O   1 
ATOM   13640 C  CB  . ALA C  2  483 ? 76.524  58.370  46.563  1.00 61.14  ?  483 ALA C CB  1 
ATOM   13641 N  N   . GLN C  2  484 ? 78.194  59.190  49.082  1.00 71.53  ?  484 GLN C N   1 
ATOM   13642 C  CA  . GLN C  2  484 ? 78.265  59.436  50.512  1.00 75.53  ?  484 GLN C CA  1 
ATOM   13643 C  C   . GLN C  2  484 ? 78.902  60.807  50.744  1.00 68.17  ?  484 GLN C C   1 
ATOM   13644 O  O   . GLN C  2  484 ? 78.391  61.574  51.554  1.00 66.35  ?  484 GLN C O   1 
ATOM   13645 C  CB  . GLN C  2  484 ? 78.946  58.261  51.216  1.00 58.64  ?  484 GLN C CB  1 
ATOM   13646 C  CG  . GLN C  2  484 ? 78.132  56.973  51.095  1.00 67.03  ?  484 GLN C CG  1 
ATOM   13647 C  CD  . GLN C  2  484 ? 78.699  55.769  51.809  1.00 78.93  ?  484 GLN C CD  1 
ATOM   13648 O  OE1 . GLN C  2  484 ? 78.138  54.672  51.737  1.00 86.65  ?  484 GLN C OE1 1 
ATOM   13649 N  NE2 . GLN C  2  484 ? 79.803  55.910  52.521  1.00 83.16  ?  484 GLN C NE2 1 
ATOM   13650 N  N   . ALA C  2  485 ? 79.980  61.145  50.013  1.00 67.54  ?  485 ALA C N   1 
ATOM   13651 C  CA  . ALA C  2  485 ? 80.618  62.454  50.140  1.00 75.88  ?  485 ALA C CA  1 
ATOM   13652 C  C   . ALA C  2  485 ? 79.599  63.598  49.996  1.00 75.37  ?  485 ALA C C   1 
ATOM   13653 O  O   . ALA C  2  485 ? 79.634  64.559  50.765  1.00 66.32  ?  485 ALA C O   1 
ATOM   13654 C  CB  . ALA C  2  485 ? 81.720  62.606  49.103  1.00 78.80  ?  485 ALA C CB  1 
ATOM   13655 N  N   . ALA C  2  486 ? 78.680  63.470  49.013  1.00 77.29  ?  486 ALA C N   1 
ATOM   13656 C  CA  . ALA C  2  486 ? 77.619  64.442  48.754  1.00 68.80  ?  486 ALA C CA  1 
ATOM   13657 C  C   . ALA C  2  486 ? 76.617  64.432  49.908  1.00 61.51  ?  486 ALA C C   1 
ATOM   13658 O  O   . ALA C  2  486 ? 76.211  65.491  50.366  1.00 74.36  ?  486 ALA C O   1 
ATOM   13659 C  CB  . ALA C  2  486 ? 76.915  64.106  47.445  1.00 66.15  ?  486 ALA C CB  1 
ATOM   13660 N  N   . ALA C  2  487 ? 76.231  63.241  50.390  1.00 68.24  ?  487 ALA C N   1 
ATOM   13661 C  CA  . ALA C  2  487 ? 75.294  63.105  51.507  1.00 80.53  ?  487 ALA C CA  1 
ATOM   13662 C  C   . ALA C  2  487 ? 75.816  63.816  52.765  1.00 70.81  ?  487 ALA C C   1 
ATOM   13663 O  O   . ALA C  2  487 ? 75.033  64.414  53.501  1.00 80.70  ?  487 ALA C O   1 
ATOM   13664 C  CB  . ALA C  2  487 ? 75.064  61.631  51.814  1.00 56.78  ?  487 ALA C CB  1 
ATOM   13665 N  N   . LYS C  2  488 ? 77.133  63.742  53.006  1.00 71.53  ?  488 LYS C N   1 
ATOM   13666 C  CA  . LYS C  2  488 ? 77.774  64.367  54.166  1.00 75.63  ?  488 LYS C CA  1 
ATOM   13667 C  C   . LYS C  2  488 ? 77.780  65.885  54.046  1.00 62.41  ?  488 LYS C C   1 
ATOM   13668 O  O   . LYS C  2  488 ? 77.654  66.581  55.050  1.00 73.72  ?  488 LYS C O   1 
ATOM   13669 C  CB  . LYS C  2  488 ? 79.227  63.889  54.296  1.00 86.58  ?  488 LYS C CB  1 
ATOM   13670 C  CG  . LYS C  2  488 ? 79.392  62.401  54.585  1.00 68.12  ?  488 LYS C CG  1 
ATOM   13671 C  CD  . LYS C  2  488 ? 80.795  62.076  55.071  1.00 73.06  ?  488 LYS C CD  1 
ATOM   13672 C  CE  . LYS C  2  488 ? 81.864  62.285  54.026  1.00 68.99  ?  488 LYS C CE  1 
ATOM   13673 N  NZ  . LYS C  2  488 ? 83.225  62.007  54.552  1.00 73.00  ?  488 LYS C NZ  1 
ATOM   13674 N  N   . TYR C  2  489 ? 77.960  66.398  52.826  1.00 67.09  ?  489 TYR C N   1 
ATOM   13675 C  CA  . TYR C  2  489 ? 77.992  67.835  52.573  1.00 75.98  ?  489 TYR C CA  1 
ATOM   13676 C  C   . TYR C  2  489 ? 76.600  68.446  52.626  1.00 67.98  ?  489 TYR C C   1 
ATOM   13677 O  O   . TYR C  2  489 ? 76.447  69.574  53.089  1.00 84.51  ?  489 TYR C O   1 
ATOM   13678 C  CB  . TYR C  2  489 ? 78.618  68.106  51.207  1.00 77.66  ?  489 TYR C CB  1 
ATOM   13679 C  CG  . TYR C  2  489 ? 78.949  69.560  50.981  1.00 65.66  ?  489 TYR C CG  1 
ATOM   13680 C  CD1 . TYR C  2  489 ? 80.102  70.119  51.509  1.00 73.70  ?  489 TYR C CD1 1 
ATOM   13681 C  CD2 . TYR C  2  489 ? 78.119  70.374  50.227  1.00 70.75  ?  489 TYR C CD2 1 
ATOM   13682 C  CE1 . TYR C  2  489 ? 80.418  71.453  51.297  1.00 79.57  ?  489 TYR C CE1 1 
ATOM   13683 C  CE2 . TYR C  2  489 ? 78.422  71.709  50.008  1.00 89.26  ?  489 TYR C CE2 1 
ATOM   13684 C  CZ  . TYR C  2  489 ? 79.576  72.247  50.543  1.00 88.35  ?  489 TYR C CZ  1 
ATOM   13685 O  OH  . TYR C  2  489 ? 79.876  73.572  50.329  1.00 97.18  ?  489 TYR C OH  1 
ATOM   13686 N  N   . GLY C  2  490 ? 75.609  67.710  52.138  1.00 70.42  ?  490 GLY C N   1 
ATOM   13687 C  CA  . GLY C  2  490 ? 74.225  68.157  52.135  1.00 68.83  ?  490 GLY C CA  1 
ATOM   13688 C  C   . GLY C  2  490 ? 73.655  68.422  50.761  1.00 74.85  ?  490 GLY C C   1 
ATOM   13689 O  O   . GLY C  2  490 ? 72.653  69.133  50.643  1.00 90.01  ?  490 GLY C O   1 
ATOM   13690 N  N   . LEU C  2  491 ? 74.265  67.856  49.713  1.00 61.56  ?  491 LEU C N   1 
ATOM   13691 C  CA  . LEU C  2  491 ? 73.765  68.059  48.354  1.00 66.64  ?  491 LEU C CA  1 
ATOM   13692 C  C   . LEU C  2  491 ? 72.579  67.135  48.054  1.00 75.80  ?  491 LEU C C   1 
ATOM   13693 O  O   . LEU C  2  491 ? 71.812  67.415  47.135  1.00 88.12  ?  491 LEU C O   1 
ATOM   13694 C  CB  . LEU C  2  491 ? 74.871  67.842  47.316  1.00 65.03  ?  491 LEU C CB  1 
ATOM   13695 C  CG  . LEU C  2  491 ? 76.183  68.586  47.544  1.00 71.62  ?  491 LEU C CG  1 
ATOM   13696 C  CD1 . LEU C  2  491 ? 77.236  68.094  46.590  1.00 81.01  ?  491 LEU C CD1 1 
ATOM   13697 C  CD2 . LEU C  2  491 ? 76.009  70.083  47.384  1.00 67.13  ?  491 LEU C CD2 1 
ATOM   13698 N  N   . LEU C  2  492 ? 72.416  66.043  48.815  1.00 79.99  ?  492 LEU C N   1 
ATOM   13699 C  CA  . LEU C  2  492 ? 71.311  65.119  48.596  1.00 78.75  ?  492 LEU C CA  1 
ATOM   13700 C  C   . LEU C  2  492 ? 70.073  65.562  49.377  1.00 76.88  ?  492 LEU C C   1 
ATOM   13701 O  O   . LEU C  2  492 ? 69.506  64.801  50.158  1.00 78.49  ?  492 LEU C O   1 
ATOM   13702 C  CB  . LEU C  2  492 ? 71.743  63.688  48.971  1.00 71.88  ?  492 LEU C CB  1 
ATOM   13703 C  CG  . LEU C  2  492 ? 72.589  62.970  47.902  1.00 73.20  ?  492 LEU C CG  1 
ATOM   13704 C  CD1 . LEU C  2  492 ? 73.469  61.914  48.517  1.00 55.84  ?  492 LEU C CD1 1 
ATOM   13705 C  CD2 . LEU C  2  492 ? 71.704  62.364  46.827  1.00 84.92  ?  492 LEU C CD2 1 
ATOM   13706 N  N   . GLN C  2  493 ? 69.657  66.812  49.147  1.00 72.55  ?  493 GLN C N   1 
ATOM   13707 C  CA  . GLN C  2  493 ? 68.492  67.410  49.790  1.00 82.98  ?  493 GLN C CA  1 
ATOM   13708 C  C   . GLN C  2  493 ? 67.672  68.143  48.747  1.00 83.67  ?  493 GLN C C   1 
ATOM   13709 O  O   . GLN C  2  493 ? 68.219  68.638  47.763  1.00 82.76  ?  493 GLN C O   1 
ATOM   13710 C  CB  . GLN C  2  493 ? 68.924  68.401  50.868  1.00 75.02  ?  493 GLN C CB  1 
ATOM   13711 C  CG  . GLN C  2  493 ? 69.499  67.739  52.105  1.00 75.49  ?  493 GLN C CG  1 
ATOM   13712 C  CD  . GLN C  2  493 ? 70.109  68.735  53.059  1.00 84.27  ?  493 GLN C CD  1 
ATOM   13713 O  OE1 . GLN C  2  493 ? 70.317  69.915  52.735  1.00 90.37  ?  493 GLN C OE1 1 
ATOM   13714 N  NE2 . GLN C  2  493 ? 70.419  68.278  54.263  1.00 84.64  ?  493 GLN C NE2 1 
ATOM   13715 N  N   . LYS C  2  494 ? 66.365  68.252  48.977  1.00 77.83  ?  494 LYS C N   1 
ATOM   13716 C  CA  . LYS C  2  494 ? 65.485  68.935  48.027  1.00 63.08  ?  494 LYS C CA  1 
ATOM   13717 C  C   . LYS C  2  494 ? 65.869  70.417  47.943  1.00 65.76  ?  494 LYS C C   1 
ATOM   13718 O  O   . LYS C  2  494 ? 65.829  71.003  46.865  1.00 81.80  ?  494 LYS C O   1 
ATOM   13719 C  CB  . LYS C  2  494 ? 63.998  68.807  48.421  1.00 64.44  ?  494 LYS C CB  1 
ATOM   13720 C  CG  . LYS C  2  494 ? 63.514  67.432  48.915  1.00 70.69  ?  494 LYS C CG  1 
ATOM   13721 C  CD  . LYS C  2  494 ? 63.389  66.387  47.817  1.00 78.50  ?  494 LYS C CD  1 
ATOM   13722 C  CE  . LYS C  2  494 ? 62.029  66.365  47.164  1.00 79.94  ?  494 LYS C CE  1 
ATOM   13723 N  NZ  . LYS C  2  494 ? 60.974  65.796  48.047  1.00 79.34  ?  494 LYS C NZ  1 
ATOM   13724 N  N   . GLU C  2  495 ? 66.253  71.013  49.085  1.00 75.88  ?  495 GLU C N   1 
ATOM   13725 C  CA  . GLU C  2  495 ? 66.644  72.425  49.172  1.00 82.36  ?  495 GLU C CA  1 
ATOM   13726 C  C   . GLU C  2  495 ? 67.995  72.746  48.527  1.00 76.53  ?  495 GLU C C   1 
ATOM   13727 O  O   . GLU C  2  495 ? 68.328  73.923  48.386  1.00 90.57  ?  495 GLU C O   1 
ATOM   13728 C  CB  . GLU C  2  495 ? 66.608  72.937  50.626  1.00 73.74  ?  495 GLU C CB  1 
ATOM   13729 C  CG  . GLU C  2  495 ? 67.138  71.975  51.675  1.00 86.92  ?  495 GLU C CG  1 
ATOM   13730 C  CD  . GLU C  2  495 ? 66.052  71.137  52.320  1.00 99.35  ?  495 GLU C CD  1 
ATOM   13731 O  OE1 . GLU C  2  495 ? 65.356  71.655  53.223  1.00 101.18 ?  495 GLU C OE1 1 
ATOM   13732 O  OE2 . GLU C  2  495 ? 65.893  69.961  51.919  1.00 106.11 ?  495 GLU C OE2 1 
ATOM   13733 N  N   . ALA C  2  496 ? 68.770  71.728  48.128  1.00 76.86  ?  496 ALA C N   1 
ATOM   13734 C  CA  . ALA C  2  496 ? 70.057  71.972  47.478  1.00 79.23  ?  496 ALA C CA  1 
ATOM   13735 C  C   . ALA C  2  496 ? 69.872  72.478  46.041  1.00 78.99  ?  496 ALA C C   1 
ATOM   13736 O  O   . ALA C  2  496 ? 70.820  73.004  45.466  1.00 85.51  ?  496 ALA C O   1 
ATOM   13737 C  CB  . ALA C  2  496 ? 70.895  70.708  47.483  1.00 70.79  ?  496 ALA C CB  1 
ATOM   13738 N  N   . ALA C  2  497 ? 68.661  72.334  45.463  1.00 82.95  ?  497 ALA C N   1 
ATOM   13739 C  CA  . ALA C  2  497 ? 68.387  72.797  44.110  1.00 76.16  ?  497 ALA C CA  1 
ATOM   13740 C  C   . ALA C  2  497 ? 68.446  74.328  44.056  1.00 73.96  ?  497 ALA C C   1 
ATOM   13741 O  O   . ALA C  2  497 ? 69.169  74.869  43.223  1.00 83.37  ?  497 ALA C O   1 
ATOM   13742 C  CB  . ALA C  2  497 ? 67.028  72.290  43.639  1.00 68.18  ?  497 ALA C CB  1 
ATOM   13743 N  N   . GLU C  2  498 ? 67.724  75.034  44.943  1.00 71.04  ?  498 GLU C N   1 
ATOM   13744 C  CA  . GLU C  2  498 ? 67.762  76.499  44.941  1.00 83.41  ?  498 GLU C CA  1 
ATOM   13745 C  C   . GLU C  2  498 ? 69.156  76.996  45.322  1.00 83.02  ?  498 GLU C C   1 
ATOM   13746 O  O   . GLU C  2  498 ? 69.640  77.981  44.765  1.00 86.61  ?  498 GLU C O   1 
ATOM   13747 C  CB  . GLU C  2  498 ? 66.743  77.082  45.939  1.00 87.50  ?  498 GLU C CB  1 
ATOM   13748 C  CG  . GLU C  2  498 ? 65.366  77.363  45.365  1.00 109.30 ?  498 GLU C CG  1 
ATOM   13749 C  CD  . GLU C  2  498 ? 64.500  78.213  46.276  1.00 136.76 ?  498 GLU C CD  1 
ATOM   13750 O  OE1 . GLU C  2  498 ? 64.694  78.151  47.512  1.00 124.14 ?  498 GLU C OE1 1 
ATOM   13751 O  OE2 . GLU C  2  498 ? 63.625  78.941  45.752  1.00 150.94 ?  498 GLU C OE2 1 
ATOM   13752 N  N   . LYS C  2  499 ? 69.797  76.317  46.271  1.00 81.93  ?  499 LYS C N   1 
ATOM   13753 C  CA  . LYS C  2  499 ? 71.108  76.709  46.763  1.00 75.19  ?  499 LYS C CA  1 
ATOM   13754 C  C   . LYS C  2  499 ? 72.247  76.539  45.755  1.00 81.91  ?  499 LYS C C   1 
ATOM   13755 O  O   . LYS C  2  499 ? 73.136  77.390  45.717  1.00 86.34  ?  499 LYS C O   1 
ATOM   13756 C  CB  . LYS C  2  499 ? 71.435  75.910  48.043  1.00 78.49  ?  499 LYS C CB  1 
ATOM   13757 C  CG  . LYS C  2  499 ? 70.554  76.242  49.240  1.00 93.84  ?  499 LYS C CG  1 
ATOM   13758 C  CD  . LYS C  2  499 ? 70.907  75.404  50.469  1.00 91.39  ?  499 LYS C CD  1 
ATOM   13759 C  CE  . LYS C  2  499 ? 70.072  75.716  51.695  1.00 143.07 ?  499 LYS C CE  1 
ATOM   13760 N  NZ  . LYS C  2  499 ? 70.436  74.860  52.856  1.00 135.55 ?  499 LYS C NZ  1 
ATOM   13761 N  N   . TYR C  2  500 ? 72.254  75.451  44.962  1.00 74.38  ?  500 TYR C N   1 
ATOM   13762 C  CA  . TYR C  2  500 ? 73.361  75.203  44.032  1.00 82.18  ?  500 TYR C CA  1 
ATOM   13763 C  C   . TYR C  2  500 ? 73.003  74.947  42.563  1.00 73.80  ?  500 TYR C C   1 
ATOM   13764 O  O   . TYR C  2  500 ? 73.842  75.203  41.698  1.00 86.59  ?  500 TYR C O   1 
ATOM   13765 C  CB  . TYR C  2  500 ? 74.186  74.010  44.539  1.00 69.10  ?  500 TYR C CB  1 
ATOM   13766 C  CG  . TYR C  2  500 ? 74.609  74.109  45.989  1.00 69.03  ?  500 TYR C CG  1 
ATOM   13767 C  CD1 . TYR C  2  500 ? 75.712  74.862  46.362  1.00 71.34  ?  500 TYR C CD1 1 
ATOM   13768 C  CD2 . TYR C  2  500 ? 73.934  73.412  46.980  1.00 63.15  ?  500 TYR C CD2 1 
ATOM   13769 C  CE1 . TYR C  2  500 ? 76.123  74.935  47.686  1.00 74.75  ?  500 TYR C CE1 1 
ATOM   13770 C  CE2 . TYR C  2  500 ? 74.336  73.476  48.308  1.00 81.90  ?  500 TYR C CE2 1 
ATOM   13771 C  CZ  . TYR C  2  500 ? 75.432  74.239  48.658  1.00 84.52  ?  500 TYR C CZ  1 
ATOM   13772 O  OH  . TYR C  2  500 ? 75.833  74.315  49.972  1.00 85.90  ?  500 TYR C OH  1 
ATOM   13773 N  N   . ALA C  2  501 ? 71.811  74.416  42.266  1.00 72.82  ?  501 ALA C N   1 
ATOM   13774 C  CA  . ALA C  2  501 ? 71.437  74.111  40.882  1.00 78.88  ?  501 ALA C CA  1 
ATOM   13775 C  C   . ALA C  2  501 ? 71.274  75.336  39.990  1.00 75.03  ?  501 ALA C C   1 
ATOM   13776 O  O   . ALA C  2  501 ? 70.927  76.414  40.467  1.00 70.17  ?  501 ALA C O   1 
ATOM   13777 C  CB  . ALA C  2  501 ? 70.163  73.282  40.853  1.00 74.23  ?  501 ALA C CB  1 
ATOM   13778 N  N   . GLY C  2  502 ? 71.517  75.144  38.695  1.00 71.86  ?  502 GLY C N   1 
ATOM   13779 C  CA  . GLY C  2  502 ? 71.397  76.197  37.700  1.00 71.21  ?  502 GLY C CA  1 
ATOM   13780 C  C   . GLY C  2  502 ? 69.951  76.535  37.394  1.00 74.50  ?  502 GLY C C   1 
ATOM   13781 O  O   . GLY C  2  502 ? 69.041  76.023  38.047  1.00 87.72  ?  502 GLY C O   1 
ATOM   13782 N  N   . PRO C  2  503 ? 69.689  77.390  36.393  1.00 68.27  ?  503 PRO C N   1 
ATOM   13783 C  CA  . PRO C  2  503 ? 68.295  77.759  36.094  1.00 69.87  ?  503 PRO C CA  1 
ATOM   13784 C  C   . PRO C  2  503 ? 67.390  76.611  35.653  1.00 70.22  ?  503 PRO C C   1 
ATOM   13785 O  O   . PRO C  2  503 ? 66.289  76.465  36.179  1.00 71.63  ?  503 PRO C O   1 
ATOM   13786 C  CB  . PRO C  2  503 ? 68.429  78.829  35.003  1.00 67.89  ?  503 PRO C CB  1 
ATOM   13787 C  CG  . PRO C  2  503 ? 69.846  79.264  35.041  1.00 94.70  ?  503 PRO C CG  1 
ATOM   13788 C  CD  . PRO C  2  503 ? 70.638  78.101  35.519  1.00 84.99  ?  503 PRO C CD  1 
ATOM   13789 N  N   . GLY C  2  504 ? 67.849  75.816  34.697  1.00 74.14  ?  504 GLY C N   1 
ATOM   13790 C  CA  . GLY C  2  504 ? 67.088  74.688  34.174  1.00 77.63  ?  504 GLY C CA  1 
ATOM   13791 C  C   . GLY C  2  504 ? 66.949  73.536  35.147  1.00 76.20  ?  504 GLY C C   1 
ATOM   13792 O  O   . GLY C  2  504 ? 65.845  73.028  35.354  1.00 73.67  ?  504 GLY C O   1 
ATOM   13793 N  N   . LEU C  2  505 ? 68.065  73.111  35.754  1.00 75.81  ?  505 LEU C N   1 
ATOM   13794 C  CA  . LEU C  2  505 ? 68.038  72.000  36.697  1.00 73.95  ?  505 LEU C CA  1 
ATOM   13795 C  C   . LEU C  2  505 ? 67.182  72.334  37.910  1.00 77.19  ?  505 LEU C C   1 
ATOM   13796 O  O   . LEU C  2  505 ? 66.462  71.460  38.390  1.00 81.46  ?  505 LEU C O   1 
ATOM   13797 C  CB  . LEU C  2  505 ? 69.463  71.597  37.111  1.00 68.68  ?  505 LEU C CB  1 
ATOM   13798 C  CG  . LEU C  2  505 ? 69.598  70.533  38.208  1.00 73.63  ?  505 LEU C CG  1 
ATOM   13799 C  CD1 . LEU C  2  505 ? 69.073  69.177  37.762  1.00 59.11  ?  505 LEU C CD1 1 
ATOM   13800 C  CD2 . LEU C  2  505 ? 71.034  70.372  38.613  1.00 81.46  ?  505 LEU C CD2 1 
ATOM   13801 N  N   . ALA C  2  506 ? 67.227  73.586  38.398  1.00 75.27  ?  506 ALA C N   1 
ATOM   13802 C  CA  . ALA C  2  506 ? 66.403  73.974  39.545  1.00 74.38  ?  506 ALA C CA  1 
ATOM   13803 C  C   . ALA C  2  506 ? 64.914  73.860  39.192  1.00 75.56  ?  506 ALA C C   1 
ATOM   13804 O  O   . ALA C  2  506 ? 64.108  73.467  40.034  1.00 75.68  ?  506 ALA C O   1 
ATOM   13805 C  CB  . ALA C  2  506 ? 66.734  75.391  39.977  1.00 62.25  ?  506 ALA C CB  1 
ATOM   13806 N  N   . THR C  2  507 ? 64.558  74.191  37.943  1.00 66.69  ?  507 THR C N   1 
ATOM   13807 C  CA  . THR C  2  507 ? 63.179  74.102  37.468  1.00 66.52  ?  507 THR C CA  1 
ATOM   13808 C  C   . THR C  2  507 ? 62.737  72.635  37.443  1.00 77.36  ?  507 THR C C   1 
ATOM   13809 O  O   . THR C  2  507 ? 61.662  72.309  37.948  1.00 82.47  ?  507 THR C O   1 
ATOM   13810 C  CB  . THR C  2  507 ? 63.069  74.745  36.077  1.00 64.32  ?  507 THR C CB  1 
ATOM   13811 O  OG1 . THR C  2  507 ? 63.385  76.134  36.187  1.00 67.24  ?  507 THR C OG1 1 
ATOM   13812 C  CG2 . THR C  2  507 ? 61.695  74.565  35.454  1.00 61.81  ?  507 THR C CG2 1 
ATOM   13813 N  N   . VAL C  2  508 ? 63.579  71.750  36.872  1.00 77.36  ?  508 VAL C N   1 
ATOM   13814 C  CA  . VAL C  2  508 ? 63.282  70.317  36.778  1.00 72.94  ?  508 VAL C CA  1 
ATOM   13815 C  C   . VAL C  2  508 ? 63.188  69.709  38.179  1.00 79.67  ?  508 VAL C C   1 
ATOM   13816 O  O   . VAL C  2  508 ? 62.310  68.887  38.427  1.00 83.89  ?  508 VAL C O   1 
ATOM   13817 C  CB  . VAL C  2  508 ? 64.325  69.581  35.903  1.00 69.00  ?  508 VAL C CB  1 
ATOM   13818 C  CG1 . VAL C  2  508 ? 64.081  68.076  35.906  1.00 54.19  ?  508 VAL C CG1 1 
ATOM   13819 C  CG2 . VAL C  2  508 ? 64.312  70.115  34.476  1.00 74.15  ?  508 VAL C CG2 1 
ATOM   13820 N  N   . CYS C  2  509 ? 64.077  70.121  39.097  1.00 72.60  ?  509 CYS C N   1 
ATOM   13821 C  CA  . CYS C  2  509 ? 64.062  69.629  40.474  1.00 75.03  ?  509 CYS C CA  1 
ATOM   13822 C  C   . CYS C  2  509 ? 62.744  69.981  41.145  1.00 77.22  ?  509 CYS C C   1 
ATOM   13823 O  O   . CYS C  2  509 ? 62.193  69.168  41.877  1.00 83.55  ?  509 CYS C O   1 
ATOM   13824 C  CB  . CYS C  2  509 ? 65.235  70.200  41.264  1.00 65.31  ?  509 CYS C CB  1 
ATOM   13825 S  SG  . CYS C  2  509 ? 66.853  69.586  40.743  1.00 85.94  ?  509 CYS C SG  1 
ATOM   13826 N  N   . LYS C  2  510 ? 62.253  71.201  40.915  1.00 68.07  ?  510 LYS C N   1 
ATOM   13827 C  CA  . LYS C  2  510 ? 61.011  71.649  41.518  1.00 67.47  ?  510 LYS C CA  1 
ATOM   13828 C  C   . LYS C  2  510 ? 59.819  70.898  40.930  1.00 75.14  ?  510 LYS C C   1 
ATOM   13829 O  O   . LYS C  2  510 ? 58.946  70.466  41.681  1.00 87.91  ?  510 LYS C O   1 
ATOM   13830 C  CB  . LYS C  2  510 ? 60.845  73.166  41.315  1.00 66.58  ?  510 LYS C CB  1 
ATOM   13831 C  CG  . LYS C  2  510 ? 59.870  73.815  42.291  1.00 76.64  ?  510 LYS C CG  1 
ATOM   13832 C  CD  . LYS C  2  510 ? 59.771  75.326  42.088  1.00 76.58  ?  510 LYS C CD  1 
ATOM   13833 C  CE  . LYS C  2  510 ? 59.400  76.058  43.357  1.00 82.83  ?  510 LYS C CE  1 
ATOM   13834 N  NZ  . LYS C  2  510 ? 59.207  77.516  43.121  1.00 91.72  ?  510 LYS C NZ  1 
ATOM   13835 N  N   . LEU C  2  511 ? 59.782  70.733  39.597  1.00 77.39  ?  511 LEU C N   1 
ATOM   13836 C  CA  . LEU C  2  511 ? 58.672  70.049  38.923  1.00 74.02  ?  511 LEU C CA  1 
ATOM   13837 C  C   . LEU C  2  511 ? 58.593  68.562  39.291  1.00 76.15  ?  511 LEU C C   1 
ATOM   13838 O  O   . LEU C  2  511 ? 57.520  68.077  39.645  1.00 81.90  ?  511 LEU C O   1 
ATOM   13839 C  CB  . LEU C  2  511 ? 58.788  70.197  37.392  1.00 65.98  ?  511 LEU C CB  1 
ATOM   13840 C  CG  . LEU C  2  511 ? 58.645  71.615  36.823  1.00 62.57  ?  511 LEU C CG  1 
ATOM   13841 C  CD1 . LEU C  2  511 ? 59.215  71.702  35.420  1.00 60.89  ?  511 LEU C CD1 1 
ATOM   13842 C  CD2 . LEU C  2  511 ? 57.197  72.061  36.801  1.00 81.39  ?  511 LEU C CD2 1 
ATOM   13843 N  N   . VAL C  2  512 ? 59.721  67.846  39.211  1.00 73.80  ?  512 VAL C N   1 
ATOM   13844 C  CA  . VAL C  2  512 ? 59.769  66.415  39.519  1.00 71.43  ?  512 VAL C CA  1 
ATOM   13845 C  C   . VAL C  2  512 ? 59.852  66.148  41.041  1.00 75.53  ?  512 VAL C C   1 
ATOM   13846 O  O   . VAL C  2  512 ? 59.612  65.018  41.471  1.00 79.05  ?  512 VAL C O   1 
ATOM   13847 C  CB  . VAL C  2  512 ? 60.932  65.745  38.744  1.00 69.03  ?  512 VAL C CB  1 
ATOM   13848 C  CG1 . VAL C  2  512 ? 60.969  64.240  38.991  1.00 76.93  ?  512 VAL C CG1 1 
ATOM   13849 C  CG2 . VAL C  2  512 ? 60.825  66.032  37.249  1.00 62.74  ?  512 VAL C CG2 1 
ATOM   13850 N  N   . ASP C  2  513 ? 60.162  67.183  41.846  1.00 69.50  ?  513 ASP C N   1 
ATOM   13851 C  CA  . ASP C  2  513 ? 60.273  67.084  43.302  1.00 68.58  ?  513 ASP C CA  1 
ATOM   13852 C  C   . ASP C  2  513 ? 61.378  66.112  43.688  1.00 82.32  ?  513 ASP C C   1 
ATOM   13853 O  O   . ASP C  2  513 ? 61.110  65.035  44.225  1.00 87.11  ?  513 ASP C O   1 
ATOM   13854 C  CB  . ASP C  2  513 ? 58.935  66.687  43.939  1.00 74.16  ?  513 ASP C CB  1 
ATOM   13855 C  CG  . ASP C  2  513 ? 58.936  66.837  45.444  1.00 89.60  ?  513 ASP C CG  1 
ATOM   13856 O  OD1 . ASP C  2  513 ? 59.444  67.869  45.936  1.00 89.46  ?  513 ASP C OD1 1 
ATOM   13857 O  OD2 . ASP C  2  513 ? 58.430  65.922  46.132  1.00 108.19 ?  513 ASP C OD2 1 
ATOM   13858 N  N   . ILE C  2  514 ? 62.630  66.506  43.407  1.00 84.91  ?  514 ILE C N   1 
ATOM   13859 C  CA  . ILE C  2  514 ? 63.819  65.692  43.676  1.00 72.04  ?  514 ILE C CA  1 
ATOM   13860 C  C   . ILE C  2  514 ? 65.004  66.596  44.014  1.00 70.18  ?  514 ILE C C   1 
ATOM   13861 O  O   . ILE C  2  514 ? 64.990  67.774  43.649  1.00 80.78  ?  514 ILE C O   1 
ATOM   13862 C  CB  . ILE C  2  514 ? 64.190  64.838  42.410  1.00 75.95  ?  514 ILE C CB  1 
ATOM   13863 C  CG1 . ILE C  2  514 ? 64.223  65.727  41.133  1.00 65.17  ?  514 ILE C CG1 1 
ATOM   13864 C  CG2 . ILE C  2  514 ? 63.255  63.645  42.253  1.00 77.42  ?  514 ILE C CG2 1 
ATOM   13865 C  CD1 . ILE C  2  514 ? 64.648  65.058  39.846  1.00 65.43  ?  514 ILE C CD1 1 
ATOM   13866 N  N   . PRO C  2  515 ? 66.077  66.064  44.636  1.00 73.86  ?  515 PRO C N   1 
ATOM   13867 C  CA  . PRO C  2  515 ? 67.263  66.907  44.864  1.00 76.40  ?  515 PRO C CA  1 
ATOM   13868 C  C   . PRO C  2  515 ? 68.046  67.075  43.548  1.00 68.48  ?  515 PRO C C   1 
ATOM   13869 O  O   . PRO C  2  515 ? 67.755  66.372  42.577  1.00 67.82  ?  515 PRO C O   1 
ATOM   13870 C  CB  . PRO C  2  515 ? 68.078  66.112  45.898  1.00 73.75  ?  515 PRO C CB  1 
ATOM   13871 C  CG  . PRO C  2  515 ? 67.271  64.884  46.226  1.00 80.81  ?  515 PRO C CG  1 
ATOM   13872 C  CD  . PRO C  2  515 ? 66.307  64.688  45.113  1.00 70.97  ?  515 PRO C CD  1 
ATOM   13873 N  N   . PRO C  2  516 ? 69.041  67.977  43.462  1.00 69.02  ?  516 PRO C N   1 
ATOM   13874 C  CA  . PRO C  2  516 ? 69.800  68.098  42.202  1.00 70.40  ?  516 PRO C CA  1 
ATOM   13875 C  C   . PRO C  2  516 ? 70.785  66.938  41.976  1.00 71.11  ?  516 PRO C C   1 
ATOM   13876 O  O   . PRO C  2  516 ? 71.252  66.739  40.857  1.00 68.67  ?  516 PRO C O   1 
ATOM   13877 C  CB  . PRO C  2  516 ? 70.499  69.448  42.339  1.00 68.86  ?  516 PRO C CB  1 
ATOM   13878 C  CG  . PRO C  2  516 ? 70.668  69.638  43.802  1.00 79.85  ?  516 PRO C CG  1 
ATOM   13879 C  CD  . PRO C  2  516 ? 69.552  68.898  44.496  1.00 78.53  ?  516 PRO C CD  1 
ATOM   13880 N  N   . VAL C  2  517 ? 71.090  66.172  43.038  1.00 64.80  ?  517 VAL C N   1 
ATOM   13881 C  CA  . VAL C  2  517 ? 71.987  65.021  42.993  1.00 62.04  ?  517 VAL C CA  1 
ATOM   13882 C  C   . VAL C  2  517 ? 71.155  63.794  43.351  1.00 73.15  ?  517 VAL C C   1 
ATOM   13883 O  O   . VAL C  2  517 ? 70.456  63.813  44.361  1.00 84.17  ?  517 VAL C O   1 
ATOM   13884 C  CB  . VAL C  2  517 ? 73.150  65.194  43.989  1.00 67.54  ?  517 VAL C CB  1 
ATOM   13885 C  CG1 . VAL C  2  517 ? 74.161  64.070  43.838  1.00 63.19  ?  517 VAL C CG1 1 
ATOM   13886 C  CG2 . VAL C  2  517 ? 73.821  66.552  43.820  1.00 70.36  ?  517 VAL C CG2 1 
ATOM   13887 N  N   . LEU C  2  518 ? 71.215  62.737  42.541  1.00 68.15  ?  518 LEU C N   1 
ATOM   13888 C  CA  . LEU C  2  518 ? 70.420  61.533  42.787  1.00 73.30  ?  518 LEU C CA  1 
ATOM   13889 C  C   . LEU C  2  518 ? 71.282  60.346  43.209  1.00 76.15  ?  518 LEU C C   1 
ATOM   13890 O  O   . LEU C  2  518 ? 72.101  59.870  42.425  1.00 78.88  ?  518 LEU C O   1 
ATOM   13891 C  CB  . LEU C  2  518 ? 69.633  61.172  41.510  1.00 70.15  ?  518 LEU C CB  1 
ATOM   13892 C  CG  . LEU C  2  518 ? 68.176  61.640  41.420  1.00 73.43  ?  518 LEU C CG  1 
ATOM   13893 C  CD1 . LEU C  2  518 ? 68.060  63.146  41.578  1.00 77.44  ?  518 LEU C CD1 1 
ATOM   13894 C  CD2 . LEU C  2  518 ? 67.559  61.230  40.098  1.00 52.82  ?  518 LEU C CD2 1 
ATOM   13895 N  N   . HIS C  2  519 ? 71.090  59.853  44.440  1.00 79.66  ?  519 HIS C N   1 
ATOM   13896 C  CA  . HIS C  2  519 ? 71.849  58.709  44.933  1.00 66.34  ?  519 HIS C CA  1 
ATOM   13897 C  C   . HIS C  2  519 ? 71.241  57.451  44.331  1.00 68.90  ?  519 HIS C C   1 
ATOM   13898 O  O   . HIS C  2  519 ? 70.093  57.120  44.622  1.00 65.50  ?  519 HIS C O   1 
ATOM   13899 C  CB  . HIS C  2  519 ? 71.801  58.656  46.462  1.00 62.21  ?  519 HIS C CB  1 
ATOM   13900 C  CG  . HIS C  2  519 ? 72.818  57.756  47.082  1.00 65.70  ?  519 HIS C CG  1 
ATOM   13901 N  ND1 . HIS C  2  519 ? 73.091  56.508  46.562  1.00 71.86  ?  519 HIS C ND1 1 
ATOM   13902 C  CD2 . HIS C  2  519 ? 73.577  57.946  48.185  1.00 69.52  ?  519 HIS C CD2 1 
ATOM   13903 C  CE1 . HIS C  2  519 ? 74.013  55.982  47.351  1.00 76.37  ?  519 HIS C CE1 1 
ATOM   13904 N  NE2 . HIS C  2  519 ? 74.338  56.814  48.341  1.00 73.76  ?  519 HIS C NE2 1 
ATOM   13905 N  N   . MET C  2  520 ? 71.998  56.772  43.464  1.00 65.53  ?  520 MET C N   1 
ATOM   13906 C  CA  . MET C  2  520 ? 71.432  55.596  42.748  1.00 65.48  ?  520 MET C CA  1 
ATOM   13907 C  C   . MET C  2  520 ? 71.871  54.291  43.420  1.00 75.53  ?  520 MET C C   1 
ATOM   13908 O  O   . MET C  2  520 ? 71.413  53.224  42.968  1.00 77.53  ?  520 MET C O   1 
ATOM   13909 C  CB  . MET C  2  520 ? 71.865  55.600  41.278  1.00 61.14  ?  520 MET C CB  1 
ATOM   13910 C  CG  . MET C  2  520 ? 71.413  56.840  40.530  1.00 57.09  ?  520 MET C CG  1 
ATOM   13911 S  SD  . MET C  2  520 ? 71.259  56.579  38.746  1.00 90.93  ?  520 MET C SD  1 
ATOM   13912 C  CE  . MET C  2  520 ? 69.915  55.395  38.694  1.00 75.32  ?  520 MET C CE  1 
ATOM   13913 N  N   . GLY C  2  521 ? 72.721  54.363  44.448  1.00 69.13  ?  521 GLY C N   1 
ATOM   13914 C  CA  . GLY C  2  521 ? 73.075  53.137  45.190  1.00 67.57  ?  521 GLY C CA  1 
ATOM   13915 C  C   . GLY C  2  521 ? 74.570  52.909  45.317  1.00 72.18  ?  521 GLY C C   1 
ATOM   13916 O  O   . GLY C  2  521 ? 75.323  53.900  45.297  1.00 72.73  ?  521 GLY C O   1 
ATOM   13917 N  N   . SER C  2  522 ? 74.959  51.636  45.420  1.00 67.69  ?  522 SER C N   1 
ATOM   13918 C  CA  . SER C  2  522 ? 76.379  51.251  45.597  1.00 57.91  ?  522 SER C CA  1 
ATOM   13919 C  C   . SER C  2  522 ? 77.115  51.287  44.255  1.00 64.10  ?  522 SER C C   1 
ATOM   13920 O  O   . SER C  2  522 ? 76.479  51.640  43.245  1.00 74.81  ?  522 SER C O   1 
ATOM   13921 C  CB  . SER C  2  522 ? 76.411  49.878  46.197  1.00 81.17  ?  522 SER C CB  1 
ATOM   13922 O  OG  . SER C  2  522 ? 75.706  48.957  45.379  1.00 85.24  ?  522 SER C OG  1 
ATOM   13923 N  N   . CYS C  2  523 ? 78.400  50.928  44.245  1.00 67.73  ?  523 CYS C N   1 
ATOM   13924 C  CA  . CYS C  2  523 ? 79.164  50.888  42.969  1.00 78.24  ?  523 CYS C CA  1 
ATOM   13925 C  C   . CYS C  2  523 ? 78.590  49.778  42.081  1.00 65.49  ?  523 CYS C C   1 
ATOM   13926 O  O   . CYS C  2  523 ? 78.526  49.986  40.858  1.00 67.44  ?  523 CYS C O   1 
ATOM   13927 C  CB  . CYS C  2  523 ? 80.656  50.720  43.228  1.00 56.12  ?  523 CYS C CB  1 
ATOM   13928 S  SG  . CYS C  2  523 ? 81.560  52.283  43.062  1.00 120.46 ?  523 CYS C SG  1 
ATOM   13929 N  N   . VAL C  2  524 ? 78.188  48.649  42.667  1.00 65.17  ?  524 VAL C N   1 
ATOM   13930 C  CA  . VAL C  2  524 ? 77.504  47.594  41.864  1.00 63.53  ?  524 VAL C CA  1 
ATOM   13931 C  C   . VAL C  2  524 ? 76.248  48.225  41.260  1.00 72.03  ?  524 VAL C C   1 
ATOM   13932 O  O   . VAL C  2  524 ? 75.881  47.853  40.129  1.00 67.25  ?  524 VAL C O   1 
ATOM   13933 C  CB  . VAL C  2  524 ? 77.165  46.362  42.723  1.00 68.52  ?  524 VAL C CB  1 
ATOM   13934 C  CG1 . VAL C  2  524 ? 76.222  45.409  42.006  1.00 62.79  ?  524 VAL C CG1 1 
ATOM   13935 C  CG2 . VAL C  2  524 ? 78.418  45.633  43.182  1.00 68.90  ?  524 VAL C CG2 1 
ATOM   13936 N  N   . ASP C  2  525 ? 75.626  49.156  41.989  1.00 75.35  ?  525 ASP C N   1 
ATOM   13937 C  CA  . ASP C  2  525 ? 74.433  49.831  41.481  1.00 72.17  ?  525 ASP C CA  1 
ATOM   13938 C  C   . ASP C  2  525 ? 74.742  50.835  40.351  1.00 63.61  ?  525 ASP C C   1 
ATOM   13939 O  O   . ASP C  2  525 ? 73.821  51.492  39.866  1.00 66.70  ?  525 ASP C O   1 
ATOM   13940 C  CB  . ASP C  2  525 ? 73.648  50.501  42.626  1.00 78.60  ?  525 ASP C CB  1 
ATOM   13941 C  CG  . ASP C  2  525 ? 73.036  49.526  43.622  1.00 90.07  ?  525 ASP C CG  1 
ATOM   13942 O  OD1 . ASP C  2  525 ? 72.832  48.349  43.253  1.00 85.68  ?  525 ASP C OD1 1 
ATOM   13943 O  OD2 . ASP C  2  525 ? 72.756  49.944  44.771  1.00 92.64  ?  525 ASP C OD2 1 
ATOM   13944 N  N   . ILE C  2  526 ? 76.014  50.938  39.899  1.00 67.69  ?  526 ILE C N   1 
ATOM   13945 C  CA  . ILE C  2  526 ? 76.352  51.798  38.752  1.00 66.47  ?  526 ILE C CA  1 
ATOM   13946 C  C   . ILE C  2  526 ? 75.668  51.192  37.502  1.00 60.91  ?  526 ILE C C   1 
ATOM   13947 O  O   . ILE C  2  526 ? 75.465  51.893  36.516  1.00 61.72  ?  526 ILE C O   1 
ATOM   13948 C  CB  . ILE C  2  526 ? 77.887  51.955  38.562  1.00 56.62  ?  526 ILE C CB  1 
ATOM   13949 C  CG1 . ILE C  2  526 ? 78.467  52.859  39.668  1.00 57.75  ?  526 ILE C CG1 1 
ATOM   13950 C  CG2 . ILE C  2  526 ? 78.218  52.517  37.175  1.00 40.92  ?  526 ILE C CG2 1 
ATOM   13951 C  CD1 . ILE C  2  526 ? 79.963  52.883  39.770  1.00 49.57  ?  526 ILE C CD1 1 
ATOM   13952 N  N   . SER C  2  527 ? 75.292  49.894  37.559  1.00 55.12  ?  527 SER C N   1 
ATOM   13953 C  CA  . SER C  2  527 ? 74.572  49.216  36.489  1.00 60.90  ?  527 SER C CA  1 
ATOM   13954 C  C   . SER C  2  527 ? 73.224  49.919  36.268  1.00 60.63  ?  527 SER C C   1 
ATOM   13955 O  O   . SER C  2  527 ? 72.716  49.891  35.149  1.00 74.66  ?  527 SER C O   1 
ATOM   13956 C  CB  . SER C  2  527 ? 74.342  47.749  36.840  1.00 60.51  ?  527 SER C CB  1 
ATOM   13957 O  OG  . SER C  2  527 ? 73.824  47.609  38.153  1.00 71.25  ?  527 SER C OG  1 
ATOM   13958 N  N   . ARG C  2  528 ? 72.654  50.562  37.324  1.00 56.41  ?  528 ARG C N   1 
ATOM   13959 C  CA  . ARG C  2  528 ? 71.399  51.313  37.216  1.00 64.29  ?  528 ARG C CA  1 
ATOM   13960 C  C   . ARG C  2  528 ? 71.632  52.530  36.320  1.00 64.22  ?  528 ARG C C   1 
ATOM   13961 O  O   . ARG C  2  528 ? 70.752  52.897  35.553  1.00 72.22  ?  528 ARG C O   1 
ATOM   13962 C  CB  . ARG C  2  528 ? 70.915  51.816  38.582  1.00 60.79  ?  528 ARG C CB  1 
ATOM   13963 C  CG  . ARG C  2  528 ? 70.528  50.748  39.599  1.00 72.65  ?  528 ARG C CG  1 
ATOM   13964 C  CD  . ARG C  2  528 ? 69.756  51.377  40.748  1.00 63.87  ?  528 ARG C CD  1 
ATOM   13965 N  NE  . ARG C  2  528 ? 70.015  50.732  42.034  1.00 57.57  ?  528 ARG C NE  1 
ATOM   13966 C  CZ  . ARG C  2  528 ? 69.357  49.673  42.498  1.00 73.31  ?  528 ARG C CZ  1 
ATOM   13967 N  NH1 . ARG C  2  528 ? 68.390  49.112  41.781  1.00 63.35  ?  528 ARG C NH1 1 
ATOM   13968 N  NH2 . ARG C  2  528 ? 69.666  49.162  43.684  1.00 75.88  ?  528 ARG C NH2 1 
ATOM   13969 N  N   . ILE C  2  529 ? 72.820  53.157  36.415  1.00 60.93  ?  529 ILE C N   1 
ATOM   13970 C  CA  . ILE C  2  529 ? 73.174  54.307  35.592  1.00 49.38  ?  529 ILE C CA  1 
ATOM   13971 C  C   . ILE C  2  529 ? 73.264  53.840  34.143  1.00 55.21  ?  529 ILE C C   1 
ATOM   13972 O  O   . ILE C  2  529 ? 72.716  54.498  33.260  1.00 61.24  ?  529 ILE C O   1 
ATOM   13973 C  CB  . ILE C  2  529 ? 74.483  54.964  36.086  1.00 53.72  ?  529 ILE C CB  1 
ATOM   13974 C  CG1 . ILE C  2  529 ? 74.277  55.534  37.504  1.00 43.76  ?  529 ILE C CG1 1 
ATOM   13975 C  CG2 . ILE C  2  529 ? 74.937  56.064  35.115  1.00 42.56  ?  529 ILE C CG2 1 
ATOM   13976 C  CD1 . ILE C  2  529 ? 75.507  55.937  38.206  1.00 55.58  ?  529 ILE C CD1 1 
ATOM   13977 N  N   . LEU C  2  530 ? 73.907  52.687  33.885  1.00 48.35  ?  530 LEU C N   1 
ATOM   13978 C  CA  . LEU C  2  530 ? 73.977  52.158  32.520  1.00 55.71  ?  530 LEU C CA  1 
ATOM   13979 C  C   . LEU C  2  530 ? 72.553  51.888  32.015  1.00 64.38  ?  530 LEU C C   1 
ATOM   13980 O  O   . LEU C  2  530 ? 72.238  52.191  30.869  1.00 66.77  ?  530 LEU C O   1 
ATOM   13981 C  CB  . LEU C  2  530 ? 74.773  50.840  32.459  1.00 60.77  ?  530 LEU C CB  1 
ATOM   13982 C  CG  . LEU C  2  530 ? 76.293  50.916  32.588  1.00 59.53  ?  530 LEU C CG  1 
ATOM   13983 C  CD1 . LEU C  2  530 ? 76.883  49.523  32.766  1.00 57.65  ?  530 LEU C CD1 1 
ATOM   13984 C  CD2 . LEU C  2  530 ? 76.925  51.596  31.374  1.00 59.42  ?  530 LEU C CD2 1 
ATOM   13985 N  N   . ASP C  2  531 ? 71.696  51.332  32.887  1.00 58.69  ?  531 ASP C N   1 
ATOM   13986 C  CA  . ASP C  2  531 ? 70.307  51.017  32.564  1.00 57.99  ?  531 ASP C CA  1 
ATOM   13987 C  C   . ASP C  2  531 ? 69.524  52.279  32.222  1.00 66.93  ?  531 ASP C C   1 
ATOM   13988 O  O   . ASP C  2  531 ? 68.761  52.274  31.261  1.00 76.77  ?  531 ASP C O   1 
ATOM   13989 C  CB  . ASP C  2  531 ? 69.646  50.280  33.743  1.00 59.03  ?  531 ASP C CB  1 
ATOM   13990 C  CG  . ASP C  2  531 ? 68.242  49.781  33.468  1.00 74.23  ?  531 ASP C CG  1 
ATOM   13991 O  OD1 . ASP C  2  531 ? 67.995  49.290  32.348  1.00 69.95  ?  531 ASP C OD1 1 
ATOM   13992 O  OD2 . ASP C  2  531 ? 67.393  49.868  34.381  1.00 77.48  ?  531 ASP C OD2 1 
ATOM   13993 N  N   . LEU C  2  532 ? 69.709  53.359  32.988  1.00 71.21  ?  532 LEU C N   1 
ATOM   13994 C  CA  . LEU C  2  532 ? 69.009  54.613  32.736  1.00 59.82  ?  532 LEU C CA  1 
ATOM   13995 C  C   . LEU C  2  532 ? 69.486  55.222  31.416  1.00 64.10  ?  532 LEU C C   1 
ATOM   13996 O  O   . LEU C  2  532 ? 68.666  55.525  30.551  1.00 76.00  ?  532 LEU C O   1 
ATOM   13997 C  CB  . LEU C  2  532 ? 69.252  55.587  33.904  1.00 56.22  ?  532 LEU C CB  1 
ATOM   13998 C  CG  . LEU C  2  532 ? 68.502  56.920  33.866  1.00 58.53  ?  532 LEU C CG  1 
ATOM   13999 C  CD1 . LEU C  2  532 ? 67.015  56.725  34.121  1.00 64.10  ?  532 LEU C CD1 1 
ATOM   14000 C  CD2 . LEU C  2  532 ? 69.076  57.893  34.888  1.00 45.25  ?  532 LEU C CD2 1 
ATOM   14001 N  N   . VAL C  2  533 ? 70.807  55.375  31.244  1.00 58.14  ?  533 VAL C N   1 
ATOM   14002 C  CA  . VAL C  2  533 ? 71.355  55.952  30.017  1.00 60.58  ?  533 VAL C CA  1 
ATOM   14003 C  C   . VAL C  2  533 ? 70.971  55.102  28.787  1.00 69.94  ?  533 VAL C C   1 
ATOM   14004 O  O   . VAL C  2  533 ? 70.803  55.644  27.695  1.00 72.03  ?  533 VAL C O   1 
ATOM   14005 C  CB  . VAL C  2  533 ? 72.886  56.174  30.133  1.00 55.27  ?  533 VAL C CB  1 
ATOM   14006 C  CG1 . VAL C  2  533 ? 73.478  56.674  28.821  1.00 47.66  ?  533 VAL C CG1 1 
ATOM   14007 C  CG2 . VAL C  2  533 ? 73.204  57.157  31.253  1.00 46.64  ?  533 VAL C CG2 1 
ATOM   14008 N  N   . GLY C  2  534 ? 70.816  53.795  28.977  1.00 62.67  ?  534 GLY C N   1 
ATOM   14009 C  CA  . GLY C  2  534 ? 70.437  52.896  27.898  1.00 65.39  ?  534 GLY C CA  1 
ATOM   14010 C  C   . GLY C  2  534 ? 69.004  53.108  27.457  1.00 64.84  ?  534 GLY C C   1 
ATOM   14011 O  O   . GLY C  2  534 ? 68.723  53.151  26.257  1.00 62.53  ?  534 GLY C O   1 
ATOM   14012 N  N   . ARG C  2  535 ? 68.086  53.252  28.428  1.00 67.45  ?  535 ARG C N   1 
ATOM   14013 C  CA  . ARG C  2  535 ? 66.664  53.468  28.143  1.00 60.71  ?  535 ARG C CA  1 
ATOM   14014 C  C   . ARG C  2  535 ? 66.472  54.779  27.383  1.00 69.53  ?  535 ARG C C   1 
ATOM   14015 O  O   . ARG C  2  535 ? 65.673  54.831  26.451  1.00 71.91  ?  535 ARG C O   1 
ATOM   14016 C  CB  . ARG C  2  535 ? 65.843  53.509  29.441  1.00 70.99  ?  535 ARG C CB  1 
ATOM   14017 C  CG  . ARG C  2  535 ? 65.664  52.159  30.129  1.00 56.61  ?  535 ARG C CG  1 
ATOM   14018 C  CD  . ARG C  2  535 ? 65.332  52.366  31.591  1.00 70.95  ?  535 ARG C CD  1 
ATOM   14019 N  NE  . ARG C  2  535 ? 65.136  51.112  32.319  1.00 90.35  ?  535 ARG C NE  1 
ATOM   14020 C  CZ  . ARG C  2  535 ? 63.978  50.472  32.455  1.00 89.57  ?  535 ARG C CZ  1 
ATOM   14021 N  NH1 . ARG C  2  535 ? 62.870  50.956  31.897  1.00 57.71  ?  535 ARG C NH1 1 
ATOM   14022 N  NH2 . ARG C  2  535 ? 63.915  49.341  33.148  1.00 93.40  ?  535 ARG C NH2 1 
ATOM   14023 N  N   . VAL C  2  536 ? 67.204  55.836  27.779  1.00 60.02  ?  536 VAL C N   1 
ATOM   14024 C  CA  . VAL C  2  536 ? 67.128  57.140  27.118  1.00 59.90  ?  536 VAL C CA  1 
ATOM   14025 C  C   . VAL C  2  536 ? 67.612  56.992  25.671  1.00 66.98  ?  536 VAL C C   1 
ATOM   14026 O  O   . VAL C  2  536 ? 66.988  57.519  24.752  1.00 69.33  ?  536 VAL C O   1 
ATOM   14027 C  CB  . VAL C  2  536 ? 67.964  58.192  27.882  1.00 54.27  ?  536 VAL C CB  1 
ATOM   14028 C  CG1 . VAL C  2  536 ? 68.118  59.475  27.071  1.00 57.13  ?  536 VAL C CG1 1 
ATOM   14029 C  CG2 . VAL C  2  536 ? 67.350  58.485  29.247  1.00 61.20  ?  536 VAL C CG2 1 
ATOM   14030 N  N   . ALA C  2  537 ? 68.715  56.262  25.467  1.00 63.02  ?  537 ALA C N   1 
ATOM   14031 C  CA  . ALA C  2  537 ? 69.249  56.043  24.134  1.00 55.95  ?  537 ALA C CA  1 
ATOM   14032 C  C   . ALA C  2  537 ? 68.233  55.270  23.281  1.00 57.79  ?  537 ALA C C   1 
ATOM   14033 O  O   . ALA C  2  537 ? 67.917  55.708  22.178  1.00 65.31  ?  537 ALA C O   1 
ATOM   14034 C  CB  . ALA C  2  537 ? 70.571  55.283  24.216  1.00 55.87  ?  537 ALA C CB  1 
ATOM   14035 N  N   . ASN C  2  538 ? 67.699  54.152  23.797  1.00 51.04  ?  538 ASN C N   1 
ATOM   14036 C  CA  . ASN C  2  538 ? 66.732  53.336  23.065  1.00 66.42  ?  538 ASN C CA  1 
ATOM   14037 C  C   . ASN C  2  538 ? 65.462  54.107  22.736  1.00 61.27  ?  538 ASN C C   1 
ATOM   14038 O  O   . ASN C  2  538 ? 64.923  53.960  21.640  1.00 69.96  ?  538 ASN C O   1 
ATOM   14039 C  CB  . ASN C  2  538 ? 66.358  52.092  23.870  1.00 63.59  ?  538 ASN C CB  1 
ATOM   14040 C  CG  . ASN C  2  538 ? 67.344  50.959  23.767  1.00 67.61  ?  538 ASN C CG  1 
ATOM   14041 O  OD1 . ASN C  2  538 ? 67.942  50.713  22.710  1.00 77.73  ?  538 ASN C OD1 1 
ATOM   14042 N  ND2 . ASN C  2  538 ? 67.522  50.230  24.863  1.00 71.18  ?  538 ASN C ND2 1 
ATOM   14043 N  N   . LEU C  2  539 ? 64.975  54.915  23.681  1.00 59.44  ?  539 LEU C N   1 
ATOM   14044 C  CA  . LEU C  2  539 ? 63.761  55.700  23.483  1.00 72.14  ?  539 LEU C CA  1 
ATOM   14045 C  C   . LEU C  2  539 ? 63.947  56.740  22.380  1.00 66.10  ?  539 LEU C C   1 
ATOM   14046 O  O   . LEU C  2  539 ? 63.006  57.014  21.639  1.00 68.72  ?  539 LEU C O   1 
ATOM   14047 C  CB  . LEU C  2  539 ? 63.360  56.378  24.802  1.00 66.33  ?  539 LEU C CB  1 
ATOM   14048 C  CG  . LEU C  2  539 ? 62.000  57.062  24.852  1.00 50.40  ?  539 LEU C CG  1 
ATOM   14049 C  CD1 . LEU C  2  539 ? 60.858  56.069  24.654  1.00 67.44  ?  539 LEU C CD1 1 
ATOM   14050 C  CD2 . LEU C  2  539 ? 61.830  57.760  26.156  1.00 55.22  ?  539 LEU C CD2 1 
ATOM   14051 N  N   . LEU C  2  540 ? 65.155  57.309  22.262  1.00 69.11  ?  540 LEU C N   1 
ATOM   14052 C  CA  . LEU C  2  540 ? 65.451  58.297  21.226  1.00 58.15  ?  540 LEU C CA  1 
ATOM   14053 C  C   . LEU C  2  540 ? 65.947  57.660  19.908  1.00 65.10  ?  540 LEU C C   1 
ATOM   14054 O  O   . LEU C  2  540 ? 66.165  58.380  18.937  1.00 71.23  ?  540 LEU C O   1 
ATOM   14055 C  CB  . LEU C  2  540 ? 66.485  59.307  21.746  1.00 55.29  ?  540 LEU C CB  1 
ATOM   14056 C  CG  . LEU C  2  540 ? 66.025  60.187  22.911  1.00 53.17  ?  540 LEU C CG  1 
ATOM   14057 C  CD1 . LEU C  2  540 ? 67.207  60.781  23.642  1.00 49.46  ?  540 LEU C CD1 1 
ATOM   14058 C  CD2 . LEU C  2  540 ? 65.112  61.302  22.432  1.00 70.05  ?  540 LEU C CD2 1 
ATOM   14059 N  N   . GLY C  2  541 ? 66.112  56.337  19.882  1.00 59.57  ?  541 GLY C N   1 
ATOM   14060 C  CA  . GLY C  2  541 ? 66.568  55.615  18.700  1.00 60.81  ?  541 GLY C CA  1 
ATOM   14061 C  C   . GLY C  2  541 ? 68.015  55.873  18.328  1.00 63.05  ?  541 GLY C C   1 
ATOM   14062 O  O   . GLY C  2  541 ? 68.384  55.781  17.155  1.00 69.32  ?  541 GLY C O   1 
ATOM   14063 N  N   . VAL C  2  542 ? 68.852  56.179  19.326  1.00 56.02  ?  542 VAL C N   1 
ATOM   14064 C  CA  . VAL C  2  542 ? 70.269  56.473  19.108  1.00 54.45  ?  542 VAL C CA  1 
ATOM   14065 C  C   . VAL C  2  542 ? 71.142  55.531  19.958  1.00 61.26  ?  542 VAL C C   1 
ATOM   14066 O  O   . VAL C  2  542 ? 70.609  54.719  20.719  1.00 65.57  ?  542 VAL C O   1 
ATOM   14067 C  CB  . VAL C  2  542 ? 70.559  57.971  19.428  1.00 55.34  ?  542 VAL C CB  1 
ATOM   14068 C  CG1 . VAL C  2  542 ? 69.689  58.894  18.585  1.00 63.42  ?  542 VAL C CG1 1 
ATOM   14069 C  CG2 . VAL C  2  542 ? 70.385  58.270  20.915  1.00 57.77  ?  542 VAL C CG2 1 
ATOM   14070 N  N   . ASP C  2  543 ? 72.478  55.627  19.818  1.00 58.28  ?  543 ASP C N   1 
ATOM   14071 C  CA  . ASP C  2  543 ? 73.419  54.838  20.609  1.00 61.50  ?  543 ASP C CA  1 
ATOM   14072 C  C   . ASP C  2  543 ? 73.763  55.650  21.877  1.00 63.45  ?  543 ASP C C   1 
ATOM   14073 O  O   . ASP C  2  543 ? 73.508  56.857  21.924  1.00 67.27  ?  543 ASP C O   1 
ATOM   14074 C  CB  . ASP C  2  543 ? 74.693  54.551  19.796  1.00 68.88  ?  543 ASP C CB  1 
ATOM   14075 C  CG  . ASP C  2  543 ? 75.509  53.374  20.297  1.00 70.59  ?  543 ASP C CG  1 
ATOM   14076 O  OD1 . ASP C  2  543 ? 75.268  52.926  21.441  1.00 68.63  ?  543 ASP C OD1 1 
ATOM   14077 O  OD2 . ASP C  2  543 ? 76.393  52.902  19.547  1.00 73.75  ?  543 ASP C OD2 1 
ATOM   14078 N  N   . MET C  2  544 ? 74.335  55.004  22.899  1.00 58.24  ?  544 MET C N   1 
ATOM   14079 C  CA  . MET C  2  544 ? 74.680  55.698  24.142  1.00 59.55  ?  544 MET C CA  1 
ATOM   14080 C  C   . MET C  2  544 ? 75.765  56.756  23.945  1.00 62.65  ?  544 MET C C   1 
ATOM   14081 O  O   . MET C  2  544 ? 75.843  57.706  24.720  1.00 58.64  ?  544 MET C O   1 
ATOM   14082 C  CB  . MET C  2  544 ? 75.083  54.686  25.221  1.00 55.89  ?  544 MET C CB  1 
ATOM   14083 C  CG  . MET C  2  544 ? 73.904  53.864  25.702  1.00 58.59  ?  544 MET C CG  1 
ATOM   14084 S  SD  . MET C  2  544 ? 74.342  52.391  26.636  1.00 71.98  ?  544 MET C SD  1 
ATOM   14085 C  CE  . MET C  2  544 ? 75.057  53.127  28.105  1.00 69.13  ?  544 MET C CE  1 
ATOM   14086 N  N   . SER C  2  545 ? 76.587  56.611  22.904  1.00 65.40  ?  545 SER C N   1 
ATOM   14087 C  CA  . SER C  2  545 ? 77.641  57.573  22.613  1.00 64.26  ?  545 SER C CA  1 
ATOM   14088 C  C   . SER C  2  545 ? 77.095  58.890  22.032  1.00 79.09  ?  545 SER C C   1 
ATOM   14089 O  O   . SER C  2  545 ? 77.805  59.892  22.038  1.00 81.87  ?  545 SER C O   1 
ATOM   14090 C  CB  . SER C  2  545 ? 78.645  56.962  21.643  1.00 56.73  ?  545 SER C CB  1 
ATOM   14091 O  OG  . SER C  2  545 ? 77.989  56.317  20.564  1.00 63.40  ?  545 SER C OG  1 
ATOM   14092 N  N   . ASP C  2  546 ? 75.850  58.895  21.528  1.00 73.43  ?  546 ASP C N   1 
ATOM   14093 C  CA  . ASP C  2  546 ? 75.254  60.093  20.935  1.00 71.98  ?  546 ASP C CA  1 
ATOM   14094 C  C   . ASP C  2  546 ? 74.614  61.034  21.966  1.00 71.79  ?  546 ASP C C   1 
ATOM   14095 O  O   . ASP C  2  546 ? 74.331  62.183  21.637  1.00 72.57  ?  546 ASP C O   1 
ATOM   14096 C  CB  . ASP C  2  546 ? 74.201  59.682  19.893  1.00 66.30  ?  546 ASP C CB  1 
ATOM   14097 C  CG  . ASP C  2  546 ? 74.714  58.701  18.859  1.00 75.88  ?  546 ASP C CG  1 
ATOM   14098 O  OD1 . ASP C  2  546 ? 75.792  58.958  18.280  1.00 94.66  ?  546 ASP C OD1 1 
ATOM   14099 O  OD2 . ASP C  2  546 ? 74.040  57.678  18.630  1.00 82.82  ?  546 ASP C OD2 1 
ATOM   14100 N  N   . LEU C  2  547 ? 74.381  60.565  23.198  1.00 69.49  ?  547 LEU C N   1 
ATOM   14101 C  CA  . LEU C  2  547 ? 73.742  61.384  24.226  1.00 56.97  ?  547 LEU C CA  1 
ATOM   14102 C  C   . LEU C  2  547 ? 74.729  62.297  24.949  1.00 62.05  ?  547 LEU C C   1 
ATOM   14103 O  O   . LEU C  2  547 ? 75.897  61.934  25.091  1.00 67.42  ?  547 LEU C O   1 
ATOM   14104 C  CB  . LEU C  2  547 ? 73.076  60.474  25.273  1.00 55.29  ?  547 LEU C CB  1 
ATOM   14105 C  CG  . LEU C  2  547 ? 72.024  59.489  24.780  1.00 63.97  ?  547 LEU C CG  1 
ATOM   14106 C  CD1 . LEU C  2  547 ? 71.693  58.468  25.866  1.00 58.15  ?  547 LEU C CD1 1 
ATOM   14107 C  CD2 . LEU C  2  547 ? 70.768  60.209  24.328  1.00 50.71  ?  547 LEU C CD2 1 
ATOM   14108 N  N   . PRO C  2  548 ? 74.283  63.467  25.466  1.00 61.17  ?  548 PRO C N   1 
ATOM   14109 C  CA  . PRO C  2  548 ? 75.209  64.324  26.224  1.00 61.34  ?  548 PRO C CA  1 
ATOM   14110 C  C   . PRO C  2  548 ? 75.342  63.793  27.657  1.00 65.56  ?  548 PRO C C   1 
ATOM   14111 O  O   . PRO C  2  548 ? 74.751  64.328  28.599  1.00 70.41  ?  548 PRO C O   1 
ATOM   14112 C  CB  . PRO C  2  548 ? 74.536  65.693  26.167  1.00 55.13  ?  548 PRO C CB  1 
ATOM   14113 C  CG  . PRO C  2  548 ? 73.089  65.388  26.091  1.00 55.87  ?  548 PRO C CG  1 
ATOM   14114 C  CD  . PRO C  2  548 ? 72.926  64.053  25.418  1.00 45.83  ?  548 PRO C CD  1 
ATOM   14115 N  N   . VAL C  2  549 ? 76.093  62.702  27.807  1.00 58.02  ?  549 VAL C N   1 
ATOM   14116 C  CA  . VAL C  2  549 ? 76.294  62.056  29.100  1.00 57.97  ?  549 VAL C CA  1 
ATOM   14117 C  C   . VAL C  2  549 ? 77.782  61.903  29.382  1.00 69.26  ?  549 VAL C C   1 
ATOM   14118 O  O   . VAL C  2  549 ? 78.591  61.863  28.456  1.00 70.80  ?  549 VAL C O   1 
ATOM   14119 C  CB  . VAL C  2  549 ? 75.558  60.693  29.175  1.00 55.40  ?  549 VAL C CB  1 
ATOM   14120 C  CG1 . VAL C  2  549 ? 74.049  60.888  29.161  1.00 59.64  ?  549 VAL C CG1 1 
ATOM   14121 C  CG2 . VAL C  2  549 ? 75.982  59.763  28.044  1.00 64.29  ?  549 VAL C CG2 1 
ATOM   14122 N  N   . ALA C  2  550 ? 78.142  61.830  30.665  1.00 67.24  ?  550 ALA C N   1 
ATOM   14123 C  CA  . ALA C  2  550 ? 79.535  61.681  31.075  1.00 63.25  ?  550 ALA C CA  1 
ATOM   14124 C  C   . ALA C  2  550 ? 79.621  61.011  32.449  1.00 69.78  ?  550 ALA C C   1 
ATOM   14125 O  O   . ALA C  2  550 ? 78.659  61.039  33.216  1.00 75.24  ?  550 ALA C O   1 
ATOM   14126 C  CB  . ALA C  2  550 ? 80.215  63.047  31.118  1.00 43.52  ?  550 ALA C CB  1 
ATOM   14127 N  N   . GLY C  2  551 ? 80.767  60.405  32.733  1.00 59.02  ?  551 GLY C N   1 
ATOM   14128 C  CA  . GLY C  2  551 ? 81.044  59.755  34.006  1.00 54.41  ?  551 GLY C CA  1 
ATOM   14129 C  C   . GLY C  2  551 ? 82.267  60.399  34.623  1.00 53.73  ?  551 GLY C C   1 
ATOM   14130 O  O   . GLY C  2  551 ? 83.168  60.814  33.892  1.00 55.56  ?  551 GLY C O   1 
ATOM   14131 N  N   . VAL C  2  552 ? 82.310  60.527  35.958  1.00 43.86  ?  552 VAL C N   1 
ATOM   14132 C  CA  . VAL C  2  552 ? 83.458  61.154  36.619  1.00 53.57  ?  552 VAL C CA  1 
ATOM   14133 C  C   . VAL C  2  552 ? 83.893  60.364  37.851  1.00 58.61  ?  552 VAL C C   1 
ATOM   14134 O  O   . VAL C  2  552 ? 83.059  59.928  38.635  1.00 72.15  ?  552 VAL C O   1 
ATOM   14135 C  CB  . VAL C  2  552 ? 83.193  62.639  37.012  1.00 61.51  ?  552 VAL C CB  1 
ATOM   14136 C  CG1 . VAL C  2  552 ? 84.506  63.381  37.262  1.00 67.14  ?  552 VAL C CG1 1 
ATOM   14137 C  CG2 . VAL C  2  552 ? 82.356  63.370  35.963  1.00 62.33  ?  552 VAL C CG2 1 
ATOM   14138 N  N   . ALA C  2  553 ? 85.210  60.213  38.031  1.00 60.23  ?  553 ALA C N   1 
ATOM   14139 C  CA  . ALA C  2  553 ? 85.803  59.528  39.175  1.00 63.82  ?  553 ALA C CA  1 
ATOM   14140 C  C   . ALA C  2  553 ? 86.789  60.537  39.784  1.00 62.21  ?  553 ALA C C   1 
ATOM   14141 O  O   . ALA C  2  553 ? 87.994  60.443  39.560  1.00 58.15  ?  553 ALA C O   1 
ATOM   14142 C  CB  . ALA C  2  553 ? 86.526  58.274  38.712  1.00 55.64  ?  553 ALA C CB  1 
ATOM   14143 N  N   . PRO C  2  554 ? 86.278  61.555  40.506  1.00 55.76  ?  554 PRO C N   1 
ATOM   14144 C  CA  . PRO C  2  554 ? 87.168  62.592  41.058  1.00 60.15  ?  554 PRO C CA  1 
ATOM   14145 C  C   . PRO C  2  554 ? 88.282  62.081  41.958  1.00 65.36  ?  554 PRO C C   1 
ATOM   14146 O  O   . PRO C  2  554 ? 89.389  62.619  41.947  1.00 66.29  ?  554 PRO C O   1 
ATOM   14147 C  CB  . PRO C  2  554 ? 86.207  63.516  41.816  1.00 63.70  ?  554 PRO C CB  1 
ATOM   14148 C  CG  . PRO C  2  554 ? 84.881  63.269  41.212  1.00 65.43  ?  554 PRO C CG  1 
ATOM   14149 C  CD  . PRO C  2  554 ? 84.867  61.832  40.833  1.00 70.24  ?  554 PRO C CD  1 
ATOM   14150 N  N   . GLU C  2  555 ? 87.981  61.067  42.759  1.00 67.60  ?  555 GLU C N   1 
ATOM   14151 C  CA  . GLU C  2  555 ? 88.952  60.466  43.665  1.00 60.82  ?  555 GLU C CA  1 
ATOM   14152 C  C   . GLU C  2  555 ? 88.703  58.986  43.494  1.00 71.06  ?  555 GLU C C   1 
ATOM   14153 O  O   . GLU C  2  555 ? 87.558  58.558  43.625  1.00 83.58  ?  555 GLU C O   1 
ATOM   14154 C  CB  . GLU C  2  555 ? 88.734  60.945  45.112  1.00 55.24  ?  555 GLU C CB  1 
ATOM   14155 C  CG  . GLU C  2  555 ? 88.198  62.362  45.208  1.00 60.21  ?  555 GLU C CG  1 
ATOM   14156 C  CD  . GLU C  2  555 ? 88.042  62.929  46.602  1.00 74.58  ?  555 GLU C CD  1 
ATOM   14157 O  OE1 . GLU C  2  555 ? 88.538  62.308  47.571  1.00 81.22  ?  555 GLU C OE1 1 
ATOM   14158 O  OE2 . GLU C  2  555 ? 87.417  64.005  46.723  1.00 62.09  ?  555 GLU C OE2 1 
ATOM   14159 N  N   . TRP C  2  556 ? 89.727  58.211  43.139  1.00 57.32  ?  556 TRP C N   1 
ATOM   14160 C  CA  . TRP C  2  556 ? 89.543  56.778  42.946  1.00 61.24  ?  556 TRP C CA  1 
ATOM   14161 C  C   . TRP C  2  556 ? 90.834  56.051  43.254  1.00 65.33  ?  556 TRP C C   1 
ATOM   14162 O  O   . TRP C  2  556 ? 91.915  56.622  43.110  1.00 74.46  ?  556 TRP C O   1 
ATOM   14163 C  CB  . TRP C  2  556 ? 89.044  56.419  41.536  1.00 58.78  ?  556 TRP C CB  1 
ATOM   14164 C  CG  . TRP C  2  556 ? 90.064  56.653  40.465  1.00 58.09  ?  556 TRP C CG  1 
ATOM   14165 C  CD1 . TRP C  2  556 ? 90.265  57.801  39.761  1.00 53.00  ?  556 TRP C CD1 1 
ATOM   14166 C  CD2 . TRP C  2  556 ? 91.066  55.728  40.021  1.00 57.14  ?  556 TRP C CD2 1 
ATOM   14167 N  NE1 . TRP C  2  556 ? 91.321  57.646  38.896  1.00 56.57  ?  556 TRP C NE1 1 
ATOM   14168 C  CE2 . TRP C  2  556 ? 91.834  56.384  39.040  1.00 53.46  ?  556 TRP C CE2 1 
ATOM   14169 C  CE3 . TRP C  2  556 ? 91.385  54.407  40.355  1.00 55.22  ?  556 TRP C CE3 1 
ATOM   14170 C  CZ2 . TRP C  2  556 ? 92.903  55.766  38.396  1.00 60.03  ?  556 TRP C CZ2 1 
ATOM   14171 C  CZ3 . TRP C  2  556 ? 92.442  53.799  39.717  1.00 56.06  ?  556 TRP C CZ3 1 
ATOM   14172 C  CH2 . TRP C  2  556 ? 93.181  54.470  38.742  1.00 57.95  ?  556 TRP C CH2 1 
ATOM   14173 N  N   . MET C  2  557 ? 90.729  54.787  43.669  1.00 54.67  ?  557 MET C N   1 
ATOM   14174 C  CA  . MET C  2  557 ? 91.910  53.991  43.974  1.00 66.65  ?  557 MET C CA  1 
ATOM   14175 C  C   . MET C  2  557 ? 91.635  52.567  43.502  1.00 56.47  ?  557 MET C C   1 
ATOM   14176 O  O   . MET C  2  557 ? 92.383  52.041  42.686  1.00 62.79  ?  557 MET C O   1 
ATOM   14177 C  CB  . MET C  2  557 ? 92.363  54.171  45.440  1.00 61.46  ?  557 MET C CB  1 
ATOM   14178 C  CG  . MET C  2  557 ? 91.239  54.151  46.466  1.00 63.00  ?  557 MET C CG  1 
ATOM   14179 S  SD  . MET C  2  557 ? 90.557  52.513  46.830  1.00 74.23  ?  557 MET C SD  1 
ATOM   14180 C  CE  . MET C  2  557 ? 91.808  51.864  47.827  1.00 61.29  ?  557 MET C CE  1 
ATOM   14181 N  N   . SER C  2  558 ? 90.574  51.944  44.004  1.00 59.95  ?  558 SER C N   1 
ATOM   14182 C  CA  . SER C  2  558 ? 90.306  50.535  43.755  1.00 56.70  ?  558 SER C CA  1 
ATOM   14183 C  C   . SER C  2  558 ? 90.402  50.152  42.291  1.00 61.45  ?  558 SER C C   1 
ATOM   14184 O  O   . SER C  2  558 ? 90.004  50.923  41.422  1.00 65.20  ?  558 SER C O   1 
ATOM   14185 C  CB  . SER C  2  558 ? 88.912  50.171  44.257  1.00 68.02  ?  558 SER C CB  1 
ATOM   14186 O  OG  . SER C  2  558 ? 87.916  50.859  43.520  1.00 64.60  ?  558 SER C OG  1 
ATOM   14187 N  N   . GLU C  2  559 ? 90.921  48.945  42.016  1.00 65.21  ?  559 GLU C N   1 
ATOM   14188 C  CA  . GLU C  2  559 ? 90.977  48.402  40.665  1.00 53.83  ?  559 GLU C CA  1 
ATOM   14189 C  C   . GLU C  2  559 ? 89.529  48.296  40.106  1.00 58.91  ?  559 GLU C C   1 
ATOM   14190 O  O   . GLU C  2  559 ? 89.346  48.239  38.890  1.00 60.77  ?  559 GLU C O   1 
ATOM   14191 C  CB  . GLU C  2  559 ? 91.667  47.026  40.667  1.00 50.90  ?  559 GLU C CB  1 
ATOM   14192 C  CG  . GLU C  2  559 ? 93.177  47.105  40.824  1.00 74.89  ?  559 GLU C CG  1 
ATOM   14193 C  CD  . GLU C  2  559 ? 93.852  45.809  41.231  1.00 84.97  ?  559 GLU C CD  1 
ATOM   14194 O  OE1 . GLU C  2  559 ? 93.327  45.132  42.143  1.00 84.15  ?  559 GLU C OE1 1 
ATOM   14195 O  OE2 . GLU C  2  559 ? 94.909  45.474  40.648  1.00 59.21  ?  559 GLU C OE2 1 
ATOM   14196 N  N   . LYS C  2  560 ? 88.504  48.303  40.996  1.00 57.73  ?  560 LYS C N   1 
ATOM   14197 C  CA  . LYS C  2  560 ? 87.100  48.276  40.600  1.00 60.74  ?  560 LYS C CA  1 
ATOM   14198 C  C   . LYS C  2  560 ? 86.780  49.564  39.848  1.00 60.31  ?  560 LYS C C   1 
ATOM   14199 O  O   . LYS C  2  560 ? 86.055  49.526  38.862  1.00 67.99  ?  560 LYS C O   1 
ATOM   14200 C  CB  . LYS C  2  560 ? 86.189  48.184  41.827  1.00 50.56  ?  560 LYS C CB  1 
ATOM   14201 C  CG  . LYS C  2  560 ? 86.126  46.804  42.453  1.00 69.76  ?  560 LYS C CG  1 
ATOM   14202 C  CD  . LYS C  2  560 ? 85.096  46.742  43.579  1.00 62.65  ?  560 LYS C CD  1 
ATOM   14203 C  CE  . LYS C  2  560 ? 85.443  47.641  44.745  1.00 66.93  ?  560 LYS C CE  1 
ATOM   14204 N  NZ  . LYS C  2  560 ? 84.693  47.273  45.965  1.00 71.36  ?  560 LYS C NZ  1 
ATOM   14205 N  N   . ALA C  2  561 ? 87.312  50.705  40.315  1.00 54.22  ?  561 ALA C N   1 
ATOM   14206 C  CA  . ALA C  2  561 ? 87.098  51.994  39.663  1.00 60.20  ?  561 ALA C CA  1 
ATOM   14207 C  C   . ALA C  2  561 ? 87.672  51.981  38.236  1.00 58.71  ?  561 ALA C C   1 
ATOM   14208 O  O   . ALA C  2  561 ? 87.113  52.630  37.349  1.00 56.49  ?  561 ALA C O   1 
ATOM   14209 C  CB  . ALA C  2  561 ? 87.748  53.104  40.476  1.00 58.60  ?  561 ALA C CB  1 
ATOM   14210 N  N   . VAL C  2  562 ? 88.777  51.232  38.015  1.00 58.25  ?  562 VAL C N   1 
ATOM   14211 C  CA  . VAL C  2  562 ? 89.404  51.121  36.697  1.00 44.72  ?  562 VAL C CA  1 
ATOM   14212 C  C   . VAL C  2  562 ? 88.476  50.318  35.792  1.00 56.03  ?  562 VAL C C   1 
ATOM   14213 O  O   . VAL C  2  562 ? 88.187  50.746  34.676  1.00 62.84  ?  562 VAL C O   1 
ATOM   14214 C  CB  . VAL C  2  562 ? 90.811  50.483  36.762  1.00 45.45  ?  562 VAL C CB  1 
ATOM   14215 C  CG1 . VAL C  2  562 ? 91.416  50.366  35.370  1.00 50.04  ?  562 VAL C CG1 1 
ATOM   14216 C  CG2 . VAL C  2  562 ? 91.734  51.282  37.670  1.00 55.37  ?  562 VAL C CG2 1 
ATOM   14217 N  N   . ALA C  2  563 ? 87.993  49.160  36.266  1.00 57.71  ?  563 ALA C N   1 
ATOM   14218 C  CA  . ALA C  2  563 ? 87.075  48.328  35.487  1.00 57.30  ?  563 ALA C CA  1 
ATOM   14219 C  C   . ALA C  2  563 ? 85.790  49.105  35.188  1.00 63.79  ?  563 ALA C C   1 
ATOM   14220 O  O   . ALA C  2  563 ? 85.273  49.025  34.074  1.00 57.15  ?  563 ALA C O   1 
ATOM   14221 C  CB  . ALA C  2  563 ? 86.745  47.058  36.255  1.00 52.90  ?  563 ALA C CB  1 
ATOM   14222 N  N   . ILE C  2  564 ? 85.294  49.874  36.184  1.00 66.84  ?  564 ILE C N   1 
ATOM   14223 C  CA  . ILE C  2  564 ? 84.088  50.695  36.055  1.00 55.41  ?  564 ILE C CA  1 
ATOM   14224 C  C   . ILE C  2  564 ? 84.317  51.725  34.949  1.00 63.55  ?  564 ILE C C   1 
ATOM   14225 O  O   . ILE C  2  564 ? 83.559  51.772  33.979  1.00 65.97  ?  564 ILE C O   1 
ATOM   14226 C  CB  . ILE C  2  564 ? 83.681  51.337  37.421  1.00 52.23  ?  564 ILE C CB  1 
ATOM   14227 C  CG1 . ILE C  2  564 ? 82.973  50.286  38.322  1.00 54.77  ?  564 ILE C CG1 1 
ATOM   14228 C  CG2 . ILE C  2  564 ? 82.783  52.566  37.212  1.00 50.94  ?  564 ILE C CG2 1 
ATOM   14229 C  CD1 . ILE C  2  564 ? 83.023  50.555  39.818  1.00 51.31  ?  564 ILE C CD1 1 
ATOM   14230 N  N   . GLY C  2  565 ? 85.389  52.500  35.060  1.00 50.31  ?  565 GLY C N   1 
ATOM   14231 C  CA  . GLY C  2  565 ? 85.726  53.490  34.045  1.00 53.89  ?  565 GLY C CA  1 
ATOM   14232 C  C   . GLY C  2  565 ? 85.799  52.860  32.666  1.00 55.49  ?  565 GLY C C   1 
ATOM   14233 O  O   . GLY C  2  565 ? 85.176  53.346  31.726  1.00 61.06  ?  565 GLY C O   1 
ATOM   14234 N  N   . THR C  2  566 ? 86.523  51.737  32.552  1.00 54.11  ?  566 THR C N   1 
ATOM   14235 C  CA  . THR C  2  566 ? 86.675  51.036  31.279  1.00 55.73  ?  566 THR C CA  1 
ATOM   14236 C  C   . THR C  2  566 ? 85.339  50.611  30.666  1.00 61.67  ?  566 THR C C   1 
ATOM   14237 O  O   . THR C  2  566 ? 85.130  50.848  29.473  1.00 55.47  ?  566 THR C O   1 
ATOM   14238 C  CB  . THR C  2  566 ? 87.620  49.843  31.436  1.00 47.38  ?  566 THR C CB  1 
ATOM   14239 O  OG1 . THR C  2  566 ? 88.832  50.290  32.041  1.00 57.71  ?  566 THR C OG1 1 
ATOM   14240 C  CG2 . THR C  2  566 ? 87.947  49.195  30.113  1.00 39.30  ?  566 THR C CG2 1 
ATOM   14241 N  N   . TYR C  2  567 ? 84.432  49.980  31.454  1.00 61.10  ?  567 TYR C N   1 
ATOM   14242 C  CA  . TYR C  2  567 ? 83.143  49.566  30.883  1.00 64.85  ?  567 TYR C CA  1 
ATOM   14243 C  C   . TYR C  2  567 ? 82.237  50.760  30.606  1.00 59.37  ?  567 TYR C C   1 
ATOM   14244 O  O   . TYR C  2  567 ? 81.400  50.682  29.708  1.00 48.88  ?  567 TYR C O   1 
ATOM   14245 C  CB  . TYR C  2  567 ? 82.435  48.453  31.685  1.00 59.51  ?  567 TYR C CB  1 
ATOM   14246 C  CG  . TYR C  2  567 ? 81.841  48.800  33.036  1.00 66.69  ?  567 TYR C CG  1 
ATOM   14247 C  CD1 . TYR C  2  567 ? 80.753  49.657  33.140  1.00 61.74  ?  567 TYR C CD1 1 
ATOM   14248 C  CD2 . TYR C  2  567 ? 82.229  48.116  34.180  1.00 64.36  ?  567 TYR C CD2 1 
ATOM   14249 C  CE1 . TYR C  2  567 ? 80.152  49.919  34.366  1.00 59.74  ?  567 TYR C CE1 1 
ATOM   14250 C  CE2 . TYR C  2  567 ? 81.622  48.352  35.407  1.00 62.95  ?  567 TYR C CE2 1 
ATOM   14251 C  CZ  . TYR C  2  567 ? 80.590  49.264  35.501  1.00 60.18  ?  567 TYR C CZ  1 
ATOM   14252 O  OH  . TYR C  2  567 ? 79.997  49.504  36.721  1.00 60.37  ?  567 TYR C OH  1 
ATOM   14253 N  N   . VAL C  2  568 ? 82.426  51.874  31.327  1.00 54.61  ?  568 VAL C N   1 
ATOM   14254 C  CA  . VAL C  2  568 ? 81.630  53.069  31.090  1.00 56.52  ?  568 VAL C CA  1 
ATOM   14255 C  C   . VAL C  2  568 ? 82.067  53.645  29.733  1.00 57.77  ?  568 VAL C C   1 
ATOM   14256 O  O   . VAL C  2  568 ? 81.216  53.935  28.898  1.00 61.07  ?  568 VAL C O   1 
ATOM   14257 C  CB  . VAL C  2  568 ? 81.772  54.076  32.264  1.00 52.98  ?  568 VAL C CB  1 
ATOM   14258 C  CG1 . VAL C  2  568 ? 81.196  55.437  31.907  1.00 47.62  ?  568 VAL C CG1 1 
ATOM   14259 C  CG2 . VAL C  2  568 ? 81.088  53.538  33.518  1.00 50.98  ?  568 VAL C CG2 1 
ATOM   14260 N  N   . VAL C  2  569 ? 83.383  53.743  29.480  1.00 59.71  ?  569 VAL C N   1 
ATOM   14261 C  CA  . VAL C  2  569 ? 83.881  54.264  28.205  1.00 51.83  ?  569 VAL C CA  1 
ATOM   14262 C  C   . VAL C  2  569 ? 83.552  53.307  27.062  1.00 52.51  ?  569 VAL C C   1 
ATOM   14263 O  O   . VAL C  2  569 ? 83.179  53.764  25.986  1.00 58.75  ?  569 VAL C O   1 
ATOM   14264 C  CB  . VAL C  2  569 ? 85.391  54.579  28.238  1.00 52.47  ?  569 VAL C CB  1 
ATOM   14265 C  CG1 . VAL C  2  569 ? 85.828  55.215  26.927  1.00 62.15  ?  569 VAL C CG1 1 
ATOM   14266 C  CG2 . VAL C  2  569 ? 85.734  55.500  29.400  1.00 56.21  ?  569 VAL C CG2 1 
ATOM   14267 N  N   . THR C  2  570 ? 83.680  51.991  27.281  1.00 54.52  ?  570 THR C N   1 
ATOM   14268 C  CA  . THR C  2  570 ? 83.357  50.993  26.251  1.00 55.92  ?  570 THR C CA  1 
ATOM   14269 C  C   . THR C  2  570 ? 81.846  51.015  25.940  1.00 60.70  ?  570 THR C C   1 
ATOM   14270 O  O   . THR C  2  570 ? 81.451  50.726  24.812  1.00 57.03  ?  570 THR C O   1 
ATOM   14271 C  CB  . THR C  2  570 ? 83.816  49.592  26.689  1.00 54.11  ?  570 THR C CB  1 
ATOM   14272 O  OG1 . THR C  2  570 ? 85.159  49.667  27.172  1.00 64.59  ?  570 THR C OG1 1 
ATOM   14273 C  CG2 . THR C  2  570 ? 83.739  48.572  25.563  1.00 40.12  ?  570 THR C CG2 1 
ATOM   14274 N  N   . SER C  2  571 ? 81.002  51.359  26.931  1.00 54.37  ?  571 SER C N   1 
ATOM   14275 C  CA  . SER C  2  571 ? 79.558  51.440  26.716  1.00 51.64  ?  571 SER C CA  1 
ATOM   14276 C  C   . SER C  2  571 ? 79.162  52.689  25.892  1.00 62.09  ?  571 SER C C   1 
ATOM   14277 O  O   . SER C  2  571 ? 78.016  52.787  25.458  1.00 68.35  ?  571 SER C O   1 
ATOM   14278 C  CB  . SER C  2  571 ? 78.818  51.426  28.049  1.00 61.22  ?  571 SER C CB  1 
ATOM   14279 O  OG  . SER C  2  571 ? 78.994  50.188  28.723  1.00 55.02  ?  571 SER C OG  1 
ATOM   14280 N  N   . GLY C  2  572 ? 80.103  53.611  25.680  1.00 60.90  ?  572 GLY C N   1 
ATOM   14281 C  CA  . GLY C  2  572 ? 79.885  54.827  24.908  1.00 53.58  ?  572 GLY C CA  1 
ATOM   14282 C  C   . GLY C  2  572 ? 79.809  56.092  25.742  1.00 59.50  ?  572 GLY C C   1 
ATOM   14283 O  O   . GLY C  2  572 ? 79.460  57.148  25.215  1.00 79.52  ?  572 GLY C O   1 
ATOM   14284 N  N   . ILE C  2  573 ? 80.141  56.023  27.040  1.00 56.24  ?  573 ILE C N   1 
ATOM   14285 C  CA  . ILE C  2  573 ? 80.074  57.195  27.919  1.00 56.00  ?  573 ILE C CA  1 
ATOM   14286 C  C   . ILE C  2  573 ? 81.477  57.694  28.275  1.00 63.20  ?  573 ILE C C   1 
ATOM   14287 O  O   . ILE C  2  573 ? 82.245  56.947  28.879  1.00 63.22  ?  573 ILE C O   1 
ATOM   14288 C  CB  . ILE C  2  573 ? 79.286  56.828  29.204  1.00 46.33  ?  573 ILE C CB  1 
ATOM   14289 C  CG1 . ILE C  2  573 ? 77.831  56.423  28.881  1.00 57.65  ?  573 ILE C CG1 1 
ATOM   14290 C  CG2 . ILE C  2  573 ? 79.316  57.977  30.212  1.00 53.50  ?  573 ILE C CG2 1 
ATOM   14291 C  CD1 . ILE C  2  573 ? 77.202  55.470  29.889  1.00 53.90  ?  573 ILE C CD1 1 
ATOM   14292 N  N   . ASP C  2  574 ? 81.806  58.962  27.943  1.00 52.50  ?  574 ASP C N   1 
ATOM   14293 C  CA  . ASP C  2  574 ? 83.121  59.539  28.262  1.00 48.59  ?  574 ASP C CA  1 
ATOM   14294 C  C   . ASP C  2  574 ? 83.350  59.512  29.769  1.00 58.87  ?  574 ASP C C   1 
ATOM   14295 O  O   . ASP C  2  574 ? 82.396  59.676  30.527  1.00 65.39  ?  574 ASP C O   1 
ATOM   14296 C  CB  . ASP C  2  574 ? 83.211  60.993  27.779  1.00 54.19  ?  574 ASP C CB  1 
ATOM   14297 C  CG  . ASP C  2  574 ? 83.063  61.154  26.287  1.00 66.93  ?  574 ASP C CG  1 
ATOM   14298 O  OD1 . ASP C  2  574 ? 84.026  60.841  25.560  1.00 70.12  ?  574 ASP C OD1 1 
ATOM   14299 O  OD2 . ASP C  2  574 ? 81.981  61.595  25.844  1.00 66.46  ?  574 ASP C OD2 1 
ATOM   14300 N  N   . THR C  2  575 ? 84.597  59.310  30.211  1.00 57.52  ?  575 THR C N   1 
ATOM   14301 C  CA  . THR C  2  575 ? 84.886  59.261  31.640  1.00 52.78  ?  575 THR C CA  1 
ATOM   14302 C  C   . THR C  2  575 ? 86.056  60.144  32.012  1.00 52.59  ?  575 THR C C   1 
ATOM   14303 O  O   . THR C  2  575 ? 87.101  60.098  31.371  1.00 60.55  ?  575 THR C O   1 
ATOM   14304 C  CB  . THR C  2  575 ? 85.142  57.822  32.066  1.00 54.67  ?  575 THR C CB  1 
ATOM   14305 O  OG1 . THR C  2  575 ? 84.013  57.037  31.688  1.00 56.96  ?  575 THR C OG1 1 
ATOM   14306 C  CG2 . THR C  2  575 ? 85.378  57.687  33.561  1.00 60.26  ?  575 THR C CG2 1 
ATOM   14307 N  N   . TRP C  2  576 ? 85.883  60.941  33.064  1.00 61.33  ?  576 TRP C N   1 
ATOM   14308 C  CA  . TRP C  2  576 ? 86.931  61.818  33.557  1.00 62.89  ?  576 TRP C CA  1 
ATOM   14309 C  C   . TRP C  2  576 ? 87.522  61.185  34.805  1.00 62.54  ?  576 TRP C C   1 
ATOM   14310 O  O   . TRP C  2  576 ? 86.778  60.704  35.659  1.00 67.61  ?  576 TRP C O   1 
ATOM   14311 C  CB  . TRP C  2  576 ? 86.375  63.216  33.886  1.00 52.25  ?  576 TRP C CB  1 
ATOM   14312 C  CG  . TRP C  2  576 ? 86.459  64.194  32.752  1.00 57.23  ?  576 TRP C CG  1 
ATOM   14313 C  CD1 . TRP C  2  576 ? 87.377  65.189  32.591  1.00 59.15  ?  576 TRP C CD1 1 
ATOM   14314 C  CD2 . TRP C  2  576 ? 85.586  64.265  31.619  1.00 68.60  ?  576 TRP C CD2 1 
ATOM   14315 N  NE1 . TRP C  2  576 ? 87.127  65.879  31.427  1.00 57.07  ?  576 TRP C NE1 1 
ATOM   14316 C  CE2 . TRP C  2  576 ? 86.023  65.339  30.818  1.00 64.24  ?  576 TRP C CE2 1 
ATOM   14317 C  CE3 . TRP C  2  576 ? 84.464  63.531  31.210  1.00 59.15  ?  576 TRP C CE3 1 
ATOM   14318 C  CZ2 . TRP C  2  576 ? 85.388  65.685  29.628  1.00 61.14  ?  576 TRP C CZ2 1 
ATOM   14319 C  CZ3 . TRP C  2  576 ? 83.834  63.882  30.034  1.00 58.94  ?  576 TRP C CZ3 1 
ATOM   14320 C  CH2 . TRP C  2  576 ? 84.299  64.944  29.255  1.00 66.51  ?  576 TRP C CH2 1 
ATOM   14321 N  N   . LEU C  2  577 ? 88.855  61.172  34.909  1.00 61.46  ?  577 LEU C N   1 
ATOM   14322 C  CA  . LEU C  2  577 ? 89.545  60.598  36.057  1.00 52.97  ?  577 LEU C CA  1 
ATOM   14323 C  C   . LEU C  2  577 ? 90.273  61.694  36.847  1.00 67.81  ?  577 LEU C C   1 
ATOM   14324 O  O   . LEU C  2  577 ? 91.069  62.440  36.276  1.00 70.72  ?  577 LEU C O   1 
ATOM   14325 C  CB  . LEU C  2  577 ? 90.538  59.526  35.586  1.00 51.95  ?  577 LEU C CB  1 
ATOM   14326 C  CG  . LEU C  2  577 ? 89.954  58.378  34.764  1.00 56.32  ?  577 LEU C CG  1 
ATOM   14327 C  CD1 . LEU C  2  577 ? 91.048  57.425  34.327  1.00 42.49  ?  577 LEU C CD1 1 
ATOM   14328 C  CD2 . LEU C  2  577 ? 88.874  57.624  35.531  1.00 42.11  ?  577 LEU C CD2 1 
ATOM   14329 N  N   . GLY C  2  578 ? 89.971  61.788  38.141  1.00 57.39  ?  578 GLY C N   1 
ATOM   14330 C  CA  . GLY C  2  578 ? 90.573  62.762  39.047  1.00 60.51  ?  578 GLY C CA  1 
ATOM   14331 C  C   . GLY C  2  578 ? 91.953  62.347  39.514  1.00 63.38  ?  578 GLY C C   1 
ATOM   14332 O  O   . GLY C  2  578 ? 92.781  63.196  39.848  1.00 69.71  ?  578 GLY C O   1 
ATOM   14333 N  N   . VAL C  2  579 ? 92.201  61.026  39.554  1.00 55.04  ?  579 VAL C N   1 
ATOM   14334 C  CA  . VAL C  2  579 ? 93.487  60.435  39.930  1.00 68.11  ?  579 VAL C CA  1 
ATOM   14335 C  C   . VAL C  2  579 ? 94.061  59.867  38.632  1.00 67.23  ?  579 VAL C C   1 
ATOM   14336 O  O   . VAL C  2  579 ? 93.355  59.160  37.914  1.00 68.08  ?  579 VAL C O   1 
ATOM   14337 C  CB  . VAL C  2  579 ? 93.320  59.335  41.016  1.00 54.23  ?  579 VAL C CB  1 
ATOM   14338 C  CG1 . VAL C  2  579 ? 94.646  58.639  41.314  1.00 57.29  ?  579 VAL C CG1 1 
ATOM   14339 C  CG2 . VAL C  2  579 ? 92.730  59.922  42.289  1.00 58.47  ?  579 VAL C CG2 1 
ATOM   14340 N  N   . ALA C  2  580 ? 95.314  60.190  38.309  1.00 65.30  ?  580 ALA C N   1 
ATOM   14341 C  CA  . ALA C  2  580 ? 95.926  59.707  37.078  1.00 61.01  ?  580 ALA C CA  1 
ATOM   14342 C  C   . ALA C  2  580 ? 96.294  58.228  37.174  1.00 58.47  ?  580 ALA C C   1 
ATOM   14343 O  O   . ALA C  2  580 ? 97.025  57.852  38.089  1.00 70.73  ?  580 ALA C O   1 
ATOM   14344 C  CB  . ALA C  2  580 ? 97.172  60.520  36.774  1.00 75.18  ?  580 ALA C CB  1 
ATOM   14345 N  N   . PRO C  2  581 ? 95.835  57.368  36.243  1.00 64.49  ?  581 PRO C N   1 
ATOM   14346 C  CA  . PRO C  2  581 ? 96.236  55.952  36.311  1.00 60.21  ?  581 PRO C CA  1 
ATOM   14347 C  C   . PRO C  2  581 ? 97.715  55.769  35.921  1.00 66.27  ?  581 PRO C C   1 
ATOM   14348 O  O   . PRO C  2  581 ? 98.321  56.688  35.359  1.00 65.00  ?  581 PRO C O   1 
ATOM   14349 C  CB  . PRO C  2  581 ? 95.285  55.262  35.327  1.00 52.26  ?  581 PRO C CB  1 
ATOM   14350 C  CG  . PRO C  2  581 ? 94.892  56.307  34.373  1.00 58.83  ?  581 PRO C CG  1 
ATOM   14351 C  CD  . PRO C  2  581 ? 94.974  57.634  35.074  1.00 70.38  ?  581 PRO C CD  1 
ATOM   14352 N  N   . PRO C  2  582 ? 98.336  54.608  36.213  1.00 64.45  ?  582 PRO C N   1 
ATOM   14353 C  CA  . PRO C  2  582 ? 99.754  54.434  35.848  1.00 63.86  ?  582 PRO C CA  1 
ATOM   14354 C  C   . PRO C  2  582 ? 99.953  54.157  34.353  1.00 70.38  ?  582 PRO C C   1 
ATOM   14355 O  O   . PRO C  2  582 ? 100.296 53.040  33.954  1.00 64.44  ?  582 PRO C O   1 
ATOM   14356 C  CB  . PRO C  2  582 ? 100.200 53.271  36.736  1.00 60.40  ?  582 PRO C CB  1 
ATOM   14357 C  CG  . PRO C  2  582 ? 98.964  52.472  36.954  1.00 54.70  ?  582 PRO C CG  1 
ATOM   14358 C  CD  . PRO C  2  582 ? 97.792  53.409  36.881  1.00 51.50  ?  582 PRO C CD  1 
ATOM   14359 N  N   . VAL C  2  583 ? 99.726  55.186  33.521  1.00 63.73  ?  583 VAL C N   1 
ATOM   14360 C  CA  . VAL C  2  583 ? 99.859  55.076  32.069  1.00 46.18  ?  583 VAL C CA  1 
ATOM   14361 C  C   . VAL C  2  583 ? 100.835 56.086  31.466  1.00 55.66  ?  583 VAL C C   1 
ATOM   14362 O  O   . VAL C  2  583 ? 101.214 55.931  30.312  1.00 67.34  ?  583 VAL C O   1 
ATOM   14363 C  CB  . VAL C  2  583 ? 98.484  55.142  31.354  1.00 45.21  ?  583 VAL C CB  1 
ATOM   14364 C  CG1 . VAL C  2  583 ? 97.595  53.973  31.760  1.00 59.64  ?  583 VAL C CG1 1 
ATOM   14365 C  CG2 . VAL C  2  583 ? 97.779  56.468  31.609  1.00 53.61  ?  583 VAL C CG2 1 
ATOM   14366 N  N   . THR C  2  584 ? 101.242 57.103  32.230  1.00 57.02  ?  584 THR C N   1 
ATOM   14367 C  CA  . THR C  2  584 ? 102.155 58.159  31.782  1.00 51.41  ?  584 THR C CA  1 
ATOM   14368 C  C   . THR C  2  584 ? 103.343 57.686  30.925  1.00 65.08  ?  584 THR C C   1 
ATOM   14369 O  O   . THR C  2  584 ? 103.648 58.308  29.908  1.00 66.11  ?  584 THR C O   1 
ATOM   14370 C  CB  . THR C  2  584 ? 102.671 58.941  33.003  1.00 65.81  ?  584 THR C CB  1 
ATOM   14371 O  OG1 . THR C  2  584 ? 101.566 59.254  33.857  1.00 74.63  ?  584 THR C OG1 1 
ATOM   14372 C  CG2 . THR C  2  584 ? 103.405 60.217  32.616  1.00 77.21  ?  584 THR C CG2 1 
ATOM   14373 N  N   . GLY C  2  585 ? 104.005 56.614  31.343  1.00 63.19  ?  585 GLY C N   1 
ATOM   14374 C  CA  . GLY C  2  585 ? 105.172 56.092  30.642  1.00 51.61  ?  585 GLY C CA  1 
ATOM   14375 C  C   . GLY C  2  585 ? 104.920 55.431  29.301  1.00 56.91  ?  585 GLY C C   1 
ATOM   14376 O  O   . GLY C  2  585 ? 105.871 55.172  28.559  1.00 61.31  ?  585 GLY C O   1 
ATOM   14377 N  N   . GLY C  2  586 ? 103.659 55.151  28.991  1.00 57.16  ?  586 GLY C N   1 
ATOM   14378 C  CA  . GLY C  2  586 ? 103.271 54.512  27.737  1.00 60.71  ?  586 GLY C CA  1 
ATOM   14379 C  C   . GLY C  2  586 ? 102.623 55.482  26.767  1.00 54.07  ?  586 GLY C C   1 
ATOM   14380 O  O   . GLY C  2  586 ? 101.403 55.648  26.794  1.00 56.36  ?  586 GLY C O   1 
ATOM   14381 N  N   . PRO C  2  587 ? 103.398 56.138  25.880  1.00 56.02  ?  587 PRO C N   1 
ATOM   14382 C  CA  . PRO C  2  587 ? 102.785 57.097  24.941  1.00 51.23  ?  587 PRO C CA  1 
ATOM   14383 C  C   . PRO C  2  587 ? 101.659 56.528  24.081  1.00 59.65  ?  587 PRO C C   1 
ATOM   14384 O  O   . PRO C  2  587 ? 100.650 57.201  23.878  1.00 66.30  ?  587 PRO C O   1 
ATOM   14385 C  CB  . PRO C  2  587 ? 103.964 57.561  24.085  1.00 53.04  ?  587 PRO C CB  1 
ATOM   14386 C  CG  . PRO C  2  587 ? 105.167 57.277  24.890  1.00 53.77  ?  587 PRO C CG  1 
ATOM   14387 C  CD  . PRO C  2  587 ? 104.861 56.071  25.706  1.00 57.11  ?  587 PRO C CD  1 
ATOM   14388 N  N   . GLU C  2  588 ? 101.821 55.300  23.572  1.00 59.87  ?  588 GLU C N   1 
ATOM   14389 C  CA  . GLU C  2  588 ? 100.790 54.669  22.753  1.00 57.19  ?  588 GLU C CA  1 
ATOM   14390 C  C   . GLU C  2  588 ? 99.548  54.419  23.604  1.00 53.69  ?  588 GLU C C   1 
ATOM   14391 O  O   . GLU C  2  588 ? 98.438  54.664  23.144  1.00 55.86  ?  588 GLU C O   1 
ATOM   14392 C  CB  . GLU C  2  588 ? 101.308 53.349  22.157  1.00 66.04  ?  588 GLU C CB  1 
ATOM   14393 C  CG  . GLU C  2  588 ? 100.412 52.755  21.083  1.00 73.31  ?  588 GLU C CG  1 
ATOM   14394 C  CD  . GLU C  2  588 ? 100.892 51.429  20.521  1.00 80.59  ?  588 GLU C CD  1 
ATOM   14395 O  OE1 . GLU C  2  588 ? 102.083 51.096  20.720  1.00 77.65  ?  588 GLU C OE1 1 
ATOM   14396 O  OE2 . GLU C  2  588 ? 100.078 50.722  19.883  1.00 73.70  ?  588 GLU C OE2 1 
ATOM   14397 N  N   . VAL C  2  589 ? 99.731  53.960  24.851  1.00 57.58  ?  589 VAL C N   1 
ATOM   14398 C  CA  . VAL C  2  589 ? 98.604  53.690  25.743  1.00 52.98  ?  589 VAL C CA  1 
ATOM   14399 C  C   . VAL C  2  589 ? 97.860  54.985  26.069  1.00 59.70  ?  589 VAL C C   1 
ATOM   14400 O  O   . VAL C  2  589 ? 96.632  54.988  26.114  1.00 62.32  ?  589 VAL C O   1 
ATOM   14401 C  CB  . VAL C  2  589 ? 99.042  52.936  27.021  1.00 47.19  ?  589 VAL C CB  1 
ATOM   14402 C  CG1 . VAL C  2  589 ? 97.851  52.704  27.946  1.00 44.24  ?  589 VAL C CG1 1 
ATOM   14403 C  CG2 . VAL C  2  589 ? 99.709  51.609  26.661  1.00 49.67  ?  589 VAL C CG2 1 
ATOM   14404 N  N   . VAL C  2  590 ? 98.588  56.093  26.264  1.00 63.91  ?  590 VAL C N   1 
ATOM   14405 C  CA  . VAL C  2  590 ? 97.956  57.381  26.555  1.00 57.11  ?  590 VAL C CA  1 
ATOM   14406 C  C   . VAL C  2  590 ? 97.124  57.810  25.342  1.00 60.72  ?  590 VAL C C   1 
ATOM   14407 O  O   . VAL C  2  590 ? 95.995  58.266  25.505  1.00 61.33  ?  590 VAL C O   1 
ATOM   14408 C  CB  . VAL C  2  590 ? 99.003  58.454  26.928  1.00 48.14  ?  590 VAL C CB  1 
ATOM   14409 C  CG1 . VAL C  2  590 ? 98.372  59.838  26.969  1.00 53.31  ?  590 VAL C CG1 1 
ATOM   14410 C  CG2 . VAL C  2  590 ? 99.660  58.131  28.262  1.00 48.16  ?  590 VAL C CG2 1 
ATOM   14411 N  N   . ASP C  2  591 ? 97.671  57.643  24.129  1.00 56.68  ?  591 ASP C N   1 
ATOM   14412 C  CA  . ASP C  2  591 ? 96.950  58.001  22.915  1.00 52.11  ?  591 ASP C CA  1 
ATOM   14413 C  C   . ASP C  2  591 ? 95.705  57.138  22.754  1.00 60.34  ?  591 ASP C C   1 
ATOM   14414 O  O   . ASP C  2  591 ? 94.651  57.654  22.403  1.00 64.56  ?  591 ASP C O   1 
ATOM   14415 C  CB  . ASP C  2  591 ? 97.845  57.843  21.683  1.00 48.98  ?  591 ASP C CB  1 
ATOM   14416 C  CG  . ASP C  2  591 ? 97.196  58.365  20.419  1.00 65.65  ?  591 ASP C CG  1 
ATOM   14417 O  OD1 . ASP C  2  591 ? 96.677  59.501  20.445  1.00 69.91  ?  591 ASP C OD1 1 
ATOM   14418 O  OD2 . ASP C  2  591 ? 97.204  57.638  19.404  1.00 73.99  ?  591 ASP C OD2 1 
ATOM   14419 N  N   . ILE C  2  592 ? 95.816  55.831  23.017  1.00 60.54  ?  592 ILE C N   1 
ATOM   14420 C  CA  . ILE C  2  592 ? 94.676  54.927  22.889  1.00 56.99  ?  592 ILE C CA  1 
ATOM   14421 C  C   . ILE C  2  592 ? 93.594  55.350  23.893  1.00 57.12  ?  592 ILE C C   1 
ATOM   14422 O  O   . ILE C  2  592 ? 92.484  55.680  23.487  1.00 61.29  ?  592 ILE C O   1 
ATOM   14423 C  CB  . ILE C  2  592 ? 95.099  53.431  23.051  1.00 44.56  ?  592 ILE C CB  1 
ATOM   14424 C  CG1 . ILE C  2  592 ? 95.967  52.959  21.867  1.00 49.35  ?  592 ILE C CG1 1 
ATOM   14425 C  CG2 . ILE C  2  592 ? 93.865  52.528  23.194  1.00 53.90  ?  592 ILE C CG2 1 
ATOM   14426 C  CD1 . ILE C  2  592 ? 96.909  51.803  22.193  1.00 56.34  ?  592 ILE C CD1 1 
ATOM   14427 N  N   . LEU C  2  593 ? 93.912  55.340  25.191  1.00 60.10  ?  593 LEU C N   1 
ATOM   14428 C  CA  . LEU C  2  593 ? 92.932  55.671  26.223  1.00 60.57  ?  593 LEU C CA  1 
ATOM   14429 C  C   . LEU C  2  593 ? 92.296  57.051  26.094  1.00 56.78  ?  593 LEU C C   1 
ATOM   14430 O  O   . LEU C  2  593 ? 91.076  57.176  26.219  1.00 62.95  ?  593 LEU C O   1 
ATOM   14431 C  CB  . LEU C  2  593 ? 93.558  55.532  27.625  1.00 53.07  ?  593 LEU C CB  1 
ATOM   14432 C  CG  . LEU C  2  593 ? 93.966  54.125  28.065  1.00 52.75  ?  593 LEU C CG  1 
ATOM   14433 C  CD1 . LEU C  2  593 ? 94.754  54.178  29.352  1.00 45.07  ?  593 LEU C CD1 1 
ATOM   14434 C  CD2 . LEU C  2  593 ? 92.755  53.211  28.227  1.00 55.02  ?  593 LEU C CD2 1 
ATOM   14435 N  N   . THR C  2  594 ? 93.109  58.085  25.850  1.00 60.70  ?  594 THR C N   1 
ATOM   14436 C  CA  . THR C  2  594 ? 92.607  59.457  25.765  1.00 67.71  ?  594 THR C CA  1 
ATOM   14437 C  C   . THR C  2  594 ? 92.431  60.013  24.345  1.00 60.52  ?  594 THR C C   1 
ATOM   14438 O  O   . THR C  2  594 ? 92.355  61.233  24.211  1.00 67.90  ?  594 THR C O   1 
ATOM   14439 C  CB  . THR C  2  594 ? 93.523  60.389  26.576  1.00 62.08  ?  594 THR C CB  1 
ATOM   14440 O  OG1 . THR C  2  594 ? 94.754  60.565  25.869  1.00 53.76  ?  594 THR C OG1 1 
ATOM   14441 C  CG2 . THR C  2  594 ? 93.790  59.872  27.992  1.00 45.29  ?  594 THR C CG2 1 
ATOM   14442 N  N   . ASN C  2  595 ? 92.363  59.166  23.296  1.00 63.88  ?  595 ASN C N   1 
ATOM   14443 C  CA  . ASN C  2  595 ? 92.177  59.678  21.931  1.00 57.43  ?  595 ASN C CA  1 
ATOM   14444 C  C   . ASN C  2  595 ? 91.668  58.615  20.925  1.00 66.16  ?  595 ASN C C   1 
ATOM   14445 O  O   . ASN C  2  595 ? 90.499  58.663  20.542  1.00 63.98  ?  595 ASN C O   1 
ATOM   14446 C  CB  . ASN C  2  595 ? 93.460  60.349  21.409  1.00 55.08  ?  595 ASN C CB  1 
ATOM   14447 C  CG  . ASN C  2  595 ? 93.349  60.823  19.977  1.00 64.28  ?  595 ASN C CG  1 
ATOM   14448 O  OD1 . ASN C  2  595 ? 92.319  61.364  19.554  1.00 71.09  ?  595 ASN C OD1 1 
ATOM   14449 N  ND2 . ASN C  2  595 ? 94.403  60.627  19.193  1.00 80.18  ?  595 ASN C ND2 1 
ATOM   14450 N  N   . LYS C  2  596 ? 92.529  57.677  20.483  1.00 67.03  ?  596 LYS C N   1 
ATOM   14451 C  CA  . LYS C  2  596 ? 92.138  56.670  19.493  1.00 56.46  ?  596 LYS C CA  1 
ATOM   14452 C  C   . LYS C  2  596 ? 90.872  55.904  19.884  1.00 61.78  ?  596 LYS C C   1 
ATOM   14453 O  O   . LYS C  2  596 ? 90.059  55.596  19.016  1.00 66.82  ?  596 LYS C O   1 
ATOM   14454 C  CB  . LYS C  2  596 ? 93.293  55.691  19.222  1.00 46.58  ?  596 LYS C CB  1 
ATOM   14455 C  CG  . LYS C  2  596 ? 93.283  55.108  17.819  1.00 51.39  ?  596 LYS C CG  1 
ATOM   14456 C  CD  . LYS C  2  596 ? 94.552  54.312  17.516  1.00 63.28  ?  596 LYS C CD  1 
ATOM   14457 C  CE  . LYS C  2  596 ? 94.720  53.986  16.043  1.00 73.67  ?  596 LYS C CE  1 
ATOM   14458 N  NZ  . LYS C  2  596 ? 94.268  52.605  15.715  1.00 62.93  ?  596 LYS C NZ  1 
ATOM   14459 N  N   . MET C  2  597 ? 90.695  55.621  21.184  1.00 56.53  ?  597 MET C N   1 
ATOM   14460 C  CA  . MET C  2  597 ? 89.531  54.898  21.711  1.00 63.56  ?  597 MET C CA  1 
ATOM   14461 C  C   . MET C  2  597 ? 88.207  55.474  21.206  1.00 66.50  ?  597 MET C C   1 
ATOM   14462 O  O   . MET C  2  597 ? 87.277  54.723  20.917  1.00 64.47  ?  597 MET C O   1 
ATOM   14463 C  CB  . MET C  2  597 ? 89.542  54.959  23.242  1.00 62.01  ?  597 MET C CB  1 
ATOM   14464 C  CG  . MET C  2  597 ? 88.678  53.931  23.891  1.00 48.50  ?  597 MET C CG  1 
ATOM   14465 S  SD  . MET C  2  597 ? 89.040  53.856  25.648  1.00 85.16  ?  597 MET C SD  1 
ATOM   14466 C  CE  . MET C  2  597 ? 87.911  52.570  26.151  1.00 88.00  ?  597 MET C CE  1 
ATOM   14467 N  N   . GLU C  2  598 ? 88.127  56.809  21.103  1.00 62.84  ?  598 GLU C N   1 
ATOM   14468 C  CA  . GLU C  2  598 ? 86.941  57.518  20.615  1.00 55.22  ?  598 GLU C CA  1 
ATOM   14469 C  C   . GLU C  2  598 ? 86.498  56.967  19.253  1.00 66.05  ?  598 GLU C C   1 
ATOM   14470 O  O   . GLU C  2  598 ? 85.303  56.839  19.001  1.00 68.03  ?  598 GLU C O   1 
ATOM   14471 C  CB  . GLU C  2  598 ? 87.263  59.011  20.485  1.00 63.38  ?  598 GLU C CB  1 
ATOM   14472 C  CG  . GLU C  2  598 ? 86.094  59.888  20.091  1.00 72.29  ?  598 GLU C CG  1 
ATOM   14473 C  CD  . GLU C  2  598 ? 86.461  61.355  19.983  1.00 91.65  ?  598 GLU C CD  1 
ATOM   14474 O  OE1 . GLU C  2  598 ? 87.665  61.660  19.811  1.00 98.02  ?  598 GLU C OE1 1 
ATOM   14475 O  OE2 . GLU C  2  598 ? 85.543  62.202  20.067  1.00 94.32  ?  598 GLU C OE2 1 
ATOM   14476 N  N   . ASP C  2  599 ? 87.464  56.630  18.382  1.00 65.56  ?  599 ASP C N   1 
ATOM   14477 C  CA  . ASP C  2  599 ? 87.169  56.085  17.061  1.00 49.34  ?  599 ASP C CA  1 
ATOM   14478 C  C   . ASP C  2  599 ? 86.618  54.657  17.127  1.00 53.83  ?  599 ASP C C   1 
ATOM   14479 O  O   . ASP C  2  599 ? 86.007  54.205  16.164  1.00 63.20  ?  599 ASP C O   1 
ATOM   14480 C  CB  . ASP C  2  599 ? 88.433  56.099  16.187  1.00 58.93  ?  599 ASP C CB  1 
ATOM   14481 C  CG  . ASP C  2  599 ? 88.959  57.484  15.872  1.00 75.66  ?  599 ASP C CG  1 
ATOM   14482 O  OD1 . ASP C  2  599 ? 88.163  58.446  15.912  1.00 79.96  ?  599 ASP C OD1 1 
ATOM   14483 O  OD2 . ASP C  2  599 ? 90.168  57.605  15.577  1.00 79.86  ?  599 ASP C OD2 1 
ATOM   14484 N  N   . TRP C  2  600 ? 86.829  53.943  18.238  1.00 52.97  ?  600 TRP C N   1 
ATOM   14485 C  CA  . TRP C  2  600 ? 86.355  52.571  18.379  1.00 60.37  ?  600 TRP C CA  1 
ATOM   14486 C  C   . TRP C  2  600 ? 85.004  52.477  19.082  1.00 64.63  ?  600 TRP C C   1 
ATOM   14487 O  O   . TRP C  2  600 ? 84.142  51.731  18.630  1.00 73.48  ?  600 TRP C O   1 
ATOM   14488 C  CB  . TRP C  2  600 ? 87.359  51.727  19.188  1.00 63.84  ?  600 TRP C CB  1 
ATOM   14489 C  CG  . TRP C  2  600 ? 88.783  51.753  18.712  1.00 61.31  ?  600 TRP C CG  1 
ATOM   14490 C  CD1 . TRP C  2  600 ? 89.246  52.163  17.495  1.00 70.03  ?  600 TRP C CD1 1 
ATOM   14491 C  CD2 . TRP C  2  600 ? 89.927  51.320  19.451  1.00 46.31  ?  600 TRP C CD2 1 
ATOM   14492 N  NE1 . TRP C  2  600 ? 90.613  52.034  17.444  1.00 59.87  ?  600 TRP C NE1 1 
ATOM   14493 C  CE2 . TRP C  2  600 ? 91.056  51.520  18.634  1.00 45.80  ?  600 TRP C CE2 1 
ATOM   14494 C  CE3 . TRP C  2  600 ? 90.108  50.790  20.730  1.00 48.89  ?  600 TRP C CE3 1 
ATOM   14495 C  CZ2 . TRP C  2  600 ? 92.344  51.208  19.058  1.00 62.36  ?  600 TRP C CZ2 1 
ATOM   14496 C  CZ3 . TRP C  2  600 ? 91.384  50.480  21.149  1.00 43.91  ?  600 TRP C CZ3 1 
ATOM   14497 C  CH2 . TRP C  2  600 ? 92.485  50.688  20.319  1.00 56.44  ?  600 TRP C CH2 1 
ATOM   14498 N  N   . VAL C  2  601 ? 84.826  53.191  20.203  1.00 55.92  ?  601 VAL C N   1 
ATOM   14499 C  CA  . VAL C  2  601 ? 83.592  53.098  20.987  1.00 52.80  ?  601 VAL C CA  1 
ATOM   14500 C  C   . VAL C  2  601 ? 82.777  54.398  21.090  1.00 64.50  ?  601 VAL C C   1 
ATOM   14501 O  O   . VAL C  2  601 ? 81.748  54.404  21.762  1.00 64.78  ?  601 VAL C O   1 
ATOM   14502 C  CB  . VAL C  2  601 ? 83.901  52.535  22.397  1.00 57.80  ?  601 VAL C CB  1 
ATOM   14503 C  CG1 . VAL C  2  601 ? 84.658  51.213  22.298  1.00 55.79  ?  601 VAL C CG1 1 
ATOM   14504 C  CG2 . VAL C  2  601 ? 84.673  53.540  23.248  1.00 53.10  ?  601 VAL C CG2 1 
ATOM   14505 N  N   . GLY C  2  602 ? 83.216  55.471  20.445  1.00 61.10  ?  602 GLY C N   1 
ATOM   14506 C  CA  . GLY C  2  602 ? 82.494  56.740  20.488  1.00 56.22  ?  602 GLY C CA  1 
ATOM   14507 C  C   . GLY C  2  602 ? 82.666  57.541  21.767  1.00 58.60  ?  602 GLY C C   1 
ATOM   14508 O  O   . GLY C  2  602 ? 82.001  58.564  21.951  1.00 68.55  ?  602 GLY C O   1 
ATOM   14509 N  N   . ALA C  2  603 ? 83.560  57.097  22.655  1.00 61.70  ?  603 ALA C N   1 
ATOM   14510 C  CA  . ALA C  2  603 ? 83.839  57.766  23.923  1.00 53.94  ?  603 ALA C CA  1 
ATOM   14511 C  C   . ALA C  2  603 ? 85.330  57.601  24.254  1.00 62.29  ?  603 ALA C C   1 
ATOM   14512 O  O   . ALA C  2  603 ? 85.998  56.741  23.674  1.00 68.77  ?  603 ALA C O   1 
ATOM   14513 C  CB  . ALA C  2  603 ? 82.980  57.166  25.024  1.00 48.95  ?  603 ALA C CB  1 
ATOM   14514 N  N   . LYS C  2  604 ? 85.859  58.418  25.164  1.00 52.22  ?  604 LYS C N   1 
ATOM   14515 C  CA  . LYS C  2  604 ? 87.275  58.345  25.516  1.00 59.76  ?  604 LYS C CA  1 
ATOM   14516 C  C   . LYS C  2  604 ? 87.500  58.696  26.991  1.00 63.64  ?  604 LYS C C   1 
ATOM   14517 O  O   . LYS C  2  604 ? 86.571  59.098  27.692  1.00 58.76  ?  604 LYS C O   1 
ATOM   14518 C  CB  . LYS C  2  604 ? 88.104  59.271  24.589  1.00 53.96  ?  604 LYS C CB  1 
ATOM   14519 C  CG  . LYS C  2  604 ? 87.501  60.667  24.396  1.00 66.49  ?  604 LYS C CG  1 
ATOM   14520 C  CD  . LYS C  2  604 ? 88.375  61.591  23.546  1.00 68.45  ?  604 LYS C CD  1 
ATOM   14521 C  CE  . LYS C  2  604 ? 89.271  62.492  24.365  1.00 81.04  ?  604 LYS C CE  1 
ATOM   14522 N  NZ  . LYS C  2  604 ? 89.988  63.480  23.512  1.00 75.76  ?  604 LYS C NZ  1 
ATOM   14523 N  N   . PHE C  2  605 ? 88.732  58.514  27.466  1.00 54.62  ?  605 PHE C N   1 
ATOM   14524 C  CA  . PHE C  2  605 ? 89.082  58.849  28.834  1.00 51.36  ?  605 PHE C CA  1 
ATOM   14525 C  C   . PHE C  2  605 ? 89.614  60.282  28.854  1.00 60.41  ?  605 PHE C C   1 
ATOM   14526 O  O   . PHE C  2  605 ? 90.140  60.766  27.851  1.00 70.47  ?  605 PHE C O   1 
ATOM   14527 C  CB  . PHE C  2  605 ? 90.164  57.893  29.366  1.00 52.15  ?  605 PHE C CB  1 
ATOM   14528 C  CG  . PHE C  2  605 ? 89.652  56.603  29.959  1.00 51.58  ?  605 PHE C CG  1 
ATOM   14529 C  CD1 . PHE C  2  605 ? 89.095  56.577  31.223  1.00 46.14  ?  605 PHE C CD1 1 
ATOM   14530 C  CD2 . PHE C  2  605 ? 89.775  55.409  29.271  1.00 48.41  ?  605 PHE C CD2 1 
ATOM   14531 C  CE1 . PHE C  2  605 ? 88.640  55.387  31.773  1.00 53.60  ?  605 PHE C CE1 1 
ATOM   14532 C  CE2 . PHE C  2  605 ? 89.326  54.220  29.826  1.00 46.02  ?  605 PHE C CE2 1 
ATOM   14533 C  CZ  . PHE C  2  605 ? 88.762  54.215  31.073  1.00 54.78  ?  605 PHE C CZ  1 
ATOM   14534 N  N   . PHE C  2  606 ? 89.475  60.957  29.992  1.00 55.18  ?  606 PHE C N   1 
ATOM   14535 C  CA  . PHE C  2  606 ? 89.969  62.318  30.173  1.00 57.86  ?  606 PHE C CA  1 
ATOM   14536 C  C   . PHE C  2  606 ? 90.602  62.359  31.549  1.00 59.21  ?  606 PHE C C   1 
ATOM   14537 O  O   . PHE C  2  606 ? 89.907  62.111  32.527  1.00 58.35  ?  606 PHE C O   1 
ATOM   14538 C  CB  . PHE C  2  606 ? 88.825  63.341  30.127  1.00 66.98  ?  606 PHE C CB  1 
ATOM   14539 C  CG  . PHE C  2  606 ? 88.150  63.559  28.793  1.00 67.26  ?  606 PHE C CG  1 
ATOM   14540 C  CD1 . PHE C  2  606 ? 87.143  62.713  28.363  1.00 73.62  ?  606 PHE C CD1 1 
ATOM   14541 C  CD2 . PHE C  2  606 ? 88.437  64.674  28.029  1.00 52.04  ?  606 PHE C CD2 1 
ATOM   14542 C  CE1 . PHE C  2  606 ? 86.487  62.942  27.162  1.00 64.80  ?  606 PHE C CE1 1 
ATOM   14543 C  CE2 . PHE C  2  606 ? 87.779  64.901  26.831  1.00 51.83  ?  606 PHE C CE2 1 
ATOM   14544 C  CZ  . PHE C  2  606 ? 86.804  64.037  26.407  1.00 61.10  ?  606 PHE C CZ  1 
ATOM   14545 N  N   . ILE C  2  607 ? 91.902  62.645  31.645  1.00 65.78  ?  607 ILE C N   1 
ATOM   14546 C  CA  . ILE C  2  607 ? 92.567  62.706  32.946  1.00 57.80  ?  607 ILE C CA  1 
ATOM   14547 C  C   . ILE C  2  607 ? 92.673  64.170  33.361  1.00 71.97  ?  607 ILE C C   1 
ATOM   14548 O  O   . ILE C  2  607 ? 93.314  64.960  32.667  1.00 81.57  ?  607 ILE C O   1 
ATOM   14549 C  CB  . ILE C  2  607 ? 93.946  62.001  32.909  1.00 59.04  ?  607 ILE C CB  1 
ATOM   14550 C  CG1 . ILE C  2  607 ? 93.776  60.496  32.591  1.00 51.01  ?  607 ILE C CG1 1 
ATOM   14551 C  CG2 . ILE C  2  607 ? 94.672  62.188  34.249  1.00 64.29  ?  607 ILE C CG2 1 
ATOM   14552 C  CD1 . ILE C  2  607 ? 94.992  59.831  32.011  1.00 45.72  ?  607 ILE C CD1 1 
ATOM   14553 N  N   . GLU C  2  608 ? 92.022  64.544  34.469  1.00 66.29  ?  608 GLU C N   1 
ATOM   14554 C  CA  . GLU C  2  608 ? 92.060  65.920  34.954  1.00 67.97  ?  608 GLU C CA  1 
ATOM   14555 C  C   . GLU C  2  608 ? 91.974  65.932  36.473  1.00 75.79  ?  608 GLU C C   1 
ATOM   14556 O  O   . GLU C  2  608 ? 90.951  65.553  37.044  1.00 79.38  ?  608 GLU C O   1 
ATOM   14557 C  CB  . GLU C  2  608 ? 90.925  66.758  34.340  1.00 49.89  ?  608 GLU C CB  1 
ATOM   14558 C  CG  . GLU C  2  608 ? 90.990  68.234  34.696  1.00 60.68  ?  608 GLU C CG  1 
ATOM   14559 C  CD  . GLU C  2  608 ? 92.303  68.925  34.380  1.00 75.63  ?  608 GLU C CD  1 
ATOM   14560 O  OE1 . GLU C  2  608 ? 92.536  69.252  33.195  1.00 74.10  ?  608 GLU C OE1 1 
ATOM   14561 O  OE2 . GLU C  2  608 ? 93.099  69.145  35.320  1.00 90.39  ?  608 GLU C OE2 1 
ATOM   14562 N  N   . THR C  2  609 ? 93.055  66.362  37.127  1.00 72.60  ?  609 THR C N   1 
ATOM   14563 C  CA  . THR C  2  609 ? 93.116  66.422  38.583  1.00 64.21  ?  609 THR C CA  1 
ATOM   14564 C  C   . THR C  2  609 ? 92.376  67.664  39.113  1.00 73.54  ?  609 THR C C   1 
ATOM   14565 O  O   . THR C  2  609 ? 91.819  67.613  40.207  1.00 91.34  ?  609 THR C O   1 
ATOM   14566 C  CB  . THR C  2  609 ? 94.579  66.377  39.042  1.00 60.92  ?  609 THR C CB  1 
ATOM   14567 O  OG1 . THR C  2  609 ? 95.251  67.551  38.588  1.00 78.13  ?  609 THR C OG1 1 
ATOM   14568 C  CG2 . THR C  2  609 ? 95.308  65.138  38.543  1.00 55.76  ?  609 THR C CG2 1 
ATOM   14569 N  N   . ASP C  2  610 ? 92.357  68.771  38.347  1.00 72.66  ?  610 ASP C N   1 
ATOM   14570 C  CA  . ASP C  2  610 ? 91.674  70.000  38.752  1.00 72.56  ?  610 ASP C CA  1 
ATOM   14571 C  C   . ASP C  2  610 ? 90.166  69.840  38.494  1.00 75.49  ?  610 ASP C C   1 
ATOM   14572 O  O   . ASP C  2  610 ? 89.768  69.728  37.335  1.00 72.83  ?  610 ASP C O   1 
ATOM   14573 C  CB  . ASP C  2  610 ? 92.235  71.189  37.957  1.00 78.78  ?  610 ASP C CB  1 
ATOM   14574 C  CG  . ASP C  2  610 ? 91.666  72.538  38.347  1.00 76.18  ?  610 ASP C CG  1 
ATOM   14575 O  OD1 . ASP C  2  610 ? 90.521  72.578  38.844  1.00 82.04  ?  610 ASP C OD1 1 
ATOM   14576 O  OD2 . ASP C  2  610 ? 92.366  73.556  38.154  1.00 79.83  ?  610 ASP C OD2 1 
ATOM   14577 N  N   . PRO C  2  611 ? 89.301  69.820  39.534  1.00 76.96  ?  611 PRO C N   1 
ATOM   14578 C  CA  . PRO C  2  611 ? 87.864  69.636  39.275  1.00 72.23  ?  611 PRO C CA  1 
ATOM   14579 C  C   . PRO C  2  611 ? 87.202  70.792  38.535  1.00 72.77  ?  611 PRO C C   1 
ATOM   14580 O  O   . PRO C  2  611 ? 86.219  70.576  37.829  1.00 66.91  ?  611 PRO C O   1 
ATOM   14581 C  CB  . PRO C  2  611 ? 87.273  69.430  40.671  1.00 67.25  ?  611 PRO C CB  1 
ATOM   14582 C  CG  . PRO C  2  611 ? 88.213  70.093  41.584  1.00 77.67  ?  611 PRO C CG  1 
ATOM   14583 C  CD  . PRO C  2  611 ? 89.574  69.934  40.980  1.00 64.38  ?  611 PRO C CD  1 
ATOM   14584 N  N   . HIS C  2  612 ? 87.733  72.010  38.678  1.00 79.46  ?  612 HIS C N   1 
ATOM   14585 C  CA  . HIS C  2  612 ? 87.169  73.175  37.997  1.00 74.02  ?  612 HIS C CA  1 
ATOM   14586 C  C   . HIS C  2  612 ? 87.418  73.081  36.494  1.00 75.97  ?  612 HIS C C   1 
ATOM   14587 O  O   . HIS C  2  612 ? 86.563  73.484  35.706  1.00 79.36  ?  612 HIS C O   1 
ATOM   14588 C  CB  . HIS C  2  612 ? 87.742  74.472  38.577  1.00 82.15  ?  612 HIS C CB  1 
ATOM   14589 C  CG  . HIS C  2  612 ? 87.477  74.618  40.041  1.00 92.99  ?  612 HIS C CG  1 
ATOM   14590 N  ND1 . HIS C  2  612 ? 88.417  74.242  40.986  1.00 111.67 ?  612 HIS C ND1 1 
ATOM   14591 C  CD2 . HIS C  2  612 ? 86.367  75.057  40.679  1.00 103.52 ?  612 HIS C CD2 1 
ATOM   14592 C  CE1 . HIS C  2  612 ? 87.861  74.481  42.164  1.00 117.81 ?  612 HIS C CE1 1 
ATOM   14593 N  NE2 . HIS C  2  612 ? 86.626  74.972  42.027  1.00 122.60 ?  612 HIS C NE2 1 
ATOM   14594 N  N   . LYS C  2  613 ? 88.577  72.543  36.093  1.00 72.11  ?  613 LYS C N   1 
ATOM   14595 C  CA  . LYS C  2  613 ? 88.873  72.373  34.677  1.00 70.34  ?  613 LYS C CA  1 
ATOM   14596 C  C   . LYS C  2  613 ? 88.052  71.185  34.147  1.00 66.35  ?  613 LYS C C   1 
ATOM   14597 O  O   . LYS C  2  613 ? 87.590  71.222  33.009  1.00 73.53  ?  613 LYS C O   1 
ATOM   14598 C  CB  . LYS C  2  613 ? 90.377  72.153  34.447  1.00 67.65  ?  613 LYS C CB  1 
ATOM   14599 C  CG  . LYS C  2  613 ? 91.220  73.401  34.710  1.00 65.57  ?  613 LYS C CG  1 
ATOM   14600 C  CD  . LYS C  2  613 ? 92.724  73.130  34.681  1.00 73.88  ?  613 LYS C CD  1 
ATOM   14601 C  CE  . LYS C  2  613 ? 93.313  73.129  33.289  1.00 93.50  ?  613 LYS C CE  1 
ATOM   14602 N  NZ  . LYS C  2  613 ? 93.543  74.504  32.765  1.00 84.53  ?  613 LYS C NZ  1 
ATOM   14603 N  N   . ALA C  2  614 ? 87.854  70.144  34.976  1.00 63.50  ?  614 ALA C N   1 
ATOM   14604 C  CA  . ALA C  2  614 ? 87.087  68.967  34.586  1.00 66.78  ?  614 ALA C CA  1 
ATOM   14605 C  C   . ALA C  2  614 ? 85.644  69.319  34.219  1.00 63.86  ?  614 ALA C C   1 
ATOM   14606 O  O   . ALA C  2  614 ? 85.157  68.849  33.195  1.00 69.08  ?  614 ALA C O   1 
ATOM   14607 C  CB  . ALA C  2  614 ? 87.105  67.937  35.704  1.00 49.89  ?  614 ALA C CB  1 
ATOM   14608 N  N   . VAL C  2  615 ? 84.961  70.145  35.033  1.00 64.27  ?  615 VAL C N   1 
ATOM   14609 C  CA  . VAL C  2  615 ? 83.574  70.519  34.723  1.00 68.44  ?  615 VAL C CA  1 
ATOM   14610 C  C   . VAL C  2  615 ? 83.520  71.339  33.434  1.00 71.69  ?  615 VAL C C   1 
ATOM   14611 O  O   . VAL C  2  615 ? 82.563  71.203  32.677  1.00 69.86  ?  615 VAL C O   1 
ATOM   14612 C  CB  . VAL C  2  615 ? 82.805  71.197  35.891  1.00 54.48  ?  615 VAL C CB  1 
ATOM   14613 C  CG1 . VAL C  2  615 ? 82.779  70.300  37.124  1.00 69.64  ?  615 VAL C CG1 1 
ATOM   14614 C  CG2 . VAL C  2  615 ? 83.375  72.572  36.228  1.00 73.79  ?  615 VAL C CG2 1 
ATOM   14615 N  N   . GLU C  2  616 ? 84.550  72.163  33.158  1.00 68.82  ?  616 GLU C N   1 
ATOM   14616 C  CA  . GLU C  2  616 ? 84.593  72.950  31.925  1.00 67.59  ?  616 GLU C CA  1 
ATOM   14617 C  C   . GLU C  2  616 ? 84.658  72.007  30.725  1.00 67.28  ?  616 GLU C C   1 
ATOM   14618 O  O   . GLU C  2  616 ? 83.959  72.214  29.737  1.00 71.62  ?  616 GLU C O   1 
ATOM   14619 C  CB  . GLU C  2  616 ? 85.817  73.881  31.905  1.00 61.29  ?  616 GLU C CB  1 
ATOM   14620 C  CG  . GLU C  2  616 ? 85.686  75.101  32.799  1.00 89.13  ?  616 GLU C CG  1 
ATOM   14621 C  CD  . GLU C  2  616 ? 86.794  76.124  32.630  1.00 115.75 ?  616 GLU C CD  1 
ATOM   14622 O  OE1 . GLU C  2  616 ? 87.827  75.792  32.003  1.00 98.66  ?  616 GLU C OE1 1 
ATOM   14623 O  OE2 . GLU C  2  616 ? 86.630  77.262  33.129  1.00 117.29 ?  616 GLU C OE2 1 
ATOM   14624 N  N   . GLN C  2  617 ? 85.490  70.960  30.827  1.00 65.12  ?  617 GLN C N   1 
ATOM   14625 C  CA  . GLN C  2  617 ? 85.670  69.975  29.766  1.00 66.00  ?  617 GLN C CA  1 
ATOM   14626 C  C   . GLN C  2  617 ? 84.423  69.120  29.570  1.00 63.92  ?  617 GLN C C   1 
ATOM   14627 O  O   . GLN C  2  617 ? 84.072  68.820  28.434  1.00 69.43  ?  617 GLN C O   1 
ATOM   14628 C  CB  . GLN C  2  617 ? 86.864  69.071  30.083  1.00 57.59  ?  617 GLN C CB  1 
ATOM   14629 C  CG  . GLN C  2  617 ? 88.195  69.802  30.085  1.00 59.04  ?  617 GLN C CG  1 
ATOM   14630 C  CD  . GLN C  2  617 ? 89.250  69.040  30.848  1.00 67.03  ?  617 GLN C CD  1 
ATOM   14631 O  OE1 . GLN C  2  617 ? 89.226  67.806  30.931  1.00 72.36  ?  617 GLN C OE1 1 
ATOM   14632 N  NE2 . GLN C  2  617 ? 90.207  69.759  31.421  1.00 68.60  ?  617 GLN C NE2 1 
ATOM   14633 N  N   . ILE C  2  618 ? 83.756  68.721  30.665  1.00 68.34  ?  618 ILE C N   1 
ATOM   14634 C  CA  . ILE C  2  618 ? 82.546  67.897  30.582  1.00 63.13  ?  618 ILE C CA  1 
ATOM   14635 C  C   . ILE C  2  618 ? 81.462  68.675  29.842  1.00 70.07  ?  618 ILE C C   1 
ATOM   14636 O  O   . ILE C  2  618 ? 80.836  68.146  28.926  1.00 67.83  ?  618 ILE C O   1 
ATOM   14637 C  CB  . ILE C  2  618 ? 82.055  67.446  31.993  1.00 58.45  ?  618 ILE C CB  1 
ATOM   14638 C  CG1 . ILE C  2  618 ? 83.053  66.464  32.640  1.00 53.82  ?  618 ILE C CG1 1 
ATOM   14639 C  CG2 . ILE C  2  618 ? 80.663  66.805  31.904  1.00 46.59  ?  618 ILE C CG2 1 
ATOM   14640 C  CD1 . ILE C  2  618 ? 82.972  66.348  34.141  1.00 46.82  ?  618 ILE C CD1 1 
ATOM   14641 N  N   . VAL C  2  619 ? 81.256  69.940  30.226  1.00 65.33  ?  619 VAL C N   1 
ATOM   14642 C  CA  . VAL C  2  619 ? 80.245  70.787  29.597  1.00 61.74  ?  619 VAL C CA  1 
ATOM   14643 C  C   . VAL C  2  619 ? 80.569  70.984  28.108  1.00 73.45  ?  619 VAL C C   1 
ATOM   14644 O  O   . VAL C  2  619 ? 79.687  70.804  27.271  1.00 74.76  ?  619 VAL C O   1 
ATOM   14645 C  CB  . VAL C  2  619 ? 80.096  72.137  30.344  1.00 62.11  ?  619 VAL C CB  1 
ATOM   14646 C  CG1 . VAL C  2  619 ? 79.197  73.098  29.574  1.00 72.70  ?  619 VAL C CG1 1 
ATOM   14647 C  CG2 . VAL C  2  619 ? 79.559  71.922  31.759  1.00 59.86  ?  619 VAL C CG2 1 
ATOM   14648 N  N   . ASN C  2  620 ? 81.825  71.328  27.775  1.00 70.64  ?  620 ASN C N   1 
ATOM   14649 C  CA  . ASN C  2  620 ? 82.222  71.526  26.378  1.00 65.56  ?  620 ASN C CA  1 
ATOM   14650 C  C   . ASN C  2  620 ? 82.031  70.253  25.558  1.00 72.09  ?  620 ASN C C   1 
ATOM   14651 O  O   . ASN C  2  620 ? 81.548  70.328  24.429  1.00 68.30  ?  620 ASN C O   1 
ATOM   14652 C  CB  . ASN C  2  620 ? 83.679  71.970  26.285  1.00 57.85  ?  620 ASN C CB  1 
ATOM   14653 C  CG  . ASN C  2  620 ? 83.911  73.395  26.704  1.00 78.74  ?  620 ASN C CG  1 
ATOM   14654 O  OD1 . ASN C  2  620 ? 83.077  74.281  26.478  1.00 85.64  ?  620 ASN C OD1 1 
ATOM   14655 N  ND2 . ASN C  2  620 ? 85.055  73.651  27.326  1.00 87.84  ?  620 ASN C ND2 1 
ATOM   14656 N  N   . ARG C  2  621 ? 82.417  69.092  26.118  1.00 66.50  ?  621 ARG C N   1 
ATOM   14657 C  CA  . ARG C  2  621 ? 82.282  67.803  25.438  1.00 60.58  ?  621 ARG C CA  1 
ATOM   14658 C  C   . ARG C  2  621 ? 80.808  67.474  25.208  1.00 67.90  ?  621 ARG C C   1 
ATOM   14659 O  O   . ARG C  2  621 ? 80.439  67.063  24.107  1.00 66.81  ?  621 ARG C O   1 
ATOM   14660 C  CB  . ARG C  2  621 ? 82.954  66.688  26.261  1.00 60.42  ?  621 ARG C CB  1 
ATOM   14661 C  CG  . ARG C  2  621 ? 82.745  65.280  25.714  1.00 54.66  ?  621 ARG C CG  1 
ATOM   14662 C  CD  . ARG C  2  621 ? 83.401  65.087  24.364  1.00 58.80  ?  621 ARG C CD  1 
ATOM   14663 N  NE  . ARG C  2  621 ? 83.478  63.672  24.012  1.00 63.19  ?  621 ARG C NE  1 
ATOM   14664 C  CZ  . ARG C  2  621 ? 84.176  63.188  22.991  1.00 69.72  ?  621 ARG C CZ  1 
ATOM   14665 N  NH1 . ARG C  2  621 ? 84.868  64.002  22.201  1.00 81.17  ?  621 ARG C NH1 1 
ATOM   14666 N  NH2 . ARG C  2  621 ? 84.187  61.883  22.748  1.00 75.99  ?  621 ARG C NH2 1 
ATOM   14667 N  N   . MET C  2  622 ? 79.959  67.658  26.242  1.00 55.27  ?  622 MET C N   1 
ATOM   14668 C  CA  . MET C  2  622 ? 78.525  67.389  26.131  1.00 53.22  ?  622 MET C CA  1 
ATOM   14669 C  C   . MET C  2  622 ? 77.945  68.234  25.002  1.00 61.85  ?  622 MET C C   1 
ATOM   14670 O  O   . MET C  2  622 ? 77.229  67.709  24.156  1.00 64.69  ?  622 MET C O   1 
ATOM   14671 C  CB  . MET C  2  622 ? 77.805  67.682  27.457  1.00 56.24  ?  622 MET C CB  1 
ATOM   14672 C  CG  . MET C  2  622 ? 77.856  66.547  28.449  1.00 67.02  ?  622 MET C CG  1 
ATOM   14673 S  SD  . MET C  2  622 ? 77.251  67.061  30.071  1.00 62.07  ?  622 MET C SD  1 
ATOM   14674 C  CE  . MET C  2  622 ? 77.171  65.495  30.895  1.00 65.51  ?  622 MET C CE  1 
ATOM   14675 N  N   . ASN C  2  623 ? 78.274  69.531  24.971  1.00 60.10  ?  623 ASN C N   1 
ATOM   14676 C  CA  . ASN C  2  623 ? 77.787  70.422  23.923  1.00 66.40  ?  623 ASN C CA  1 
ATOM   14677 C  C   . ASN C  2  623 ? 78.204  69.900  22.551  1.00 72.26  ?  623 ASN C C   1 
ATOM   14678 O  O   . ASN C  2  623 ? 77.375  69.874  21.644  1.00 65.06  ?  623 ASN C O   1 
ATOM   14679 C  CB  . ASN C  2  623 ? 78.199  71.861  24.204  1.00 72.26  ?  623 ASN C CB  1 
ATOM   14680 C  CG  . ASN C  2  623 ? 77.484  72.444  25.396  1.00 76.01  ?  623 ASN C CG  1 
ATOM   14681 O  OD1 . ASN C  2  623 ? 76.260  72.329  25.532  1.00 80.67  ?  623 ASN C OD1 1 
ATOM   14682 N  ND2 . ASN C  2  623 ? 78.223  73.079  26.295  1.00 86.52  ?  623 ASN C ND2 1 
ATOM   14683 N  N   . GLU C  2  624 ? 79.466  69.464  22.393  1.00 69.21  ?  624 GLU C N   1 
ATOM   14684 C  CA  . GLU C  2  624 ? 79.931  68.906  21.124  1.00 63.38  ?  624 GLU C CA  1 
ATOM   14685 C  C   . GLU C  2  624 ? 79.030  67.762  20.663  1.00 58.23  ?  624 GLU C C   1 
ATOM   14686 O  O   . GLU C  2  624 ? 78.635  67.720  19.501  1.00 69.21  ?  624 GLU C O   1 
ATOM   14687 C  CB  . GLU C  2  624 ? 81.377  68.404  21.232  1.00 59.46  ?  624 GLU C CB  1 
ATOM   14688 C  CG  . GLU C  2  624 ? 82.411  69.506  21.349  1.00 81.43  ?  624 GLU C CG  1 
ATOM   14689 C  CD  . GLU C  2  624 ? 83.787  69.003  21.746  1.00 108.11 ?  624 GLU C CD  1 
ATOM   14690 O  OE1 . GLU C  2  624 ? 84.095  67.821  21.466  1.00 88.43  ?  624 GLU C OE1 1 
ATOM   14691 O  OE2 . GLU C  2  624 ? 84.557  69.793  22.339  1.00 106.51 ?  624 GLU C OE2 1 
ATOM   14692 N  N   . LYS C  2  625 ? 78.691  66.844  21.584  1.00 55.86  ?  625 LYS C N   1 
ATOM   14693 C  CA  . LYS C  2  625 ? 77.817  65.714  21.276  1.00 63.89  ?  625 LYS C CA  1 
ATOM   14694 C  C   . LYS C  2  625 ? 76.376  66.183  21.006  1.00 72.27  ?  625 LYS C C   1 
ATOM   14695 O  O   . LYS C  2  625 ? 75.659  65.530  20.244  1.00 68.65  ?  625 LYS C O   1 
ATOM   14696 C  CB  . LYS C  2  625 ? 77.852  64.675  22.407  1.00 58.61  ?  625 LYS C CB  1 
ATOM   14697 C  CG  . LYS C  2  625 ? 79.170  63.908  22.473  1.00 63.17  ?  625 LYS C CG  1 
ATOM   14698 C  CD  . LYS C  2  625 ? 79.060  62.640  23.302  1.00 73.31  ?  625 LYS C CD  1 
ATOM   14699 C  CE  . LYS C  2  625 ? 80.218  61.703  23.074  1.00 59.29  ?  625 LYS C CE  1 
ATOM   14700 N  NZ  . LYS C  2  625 ? 80.047  60.431  23.824  1.00 73.68  ?  625 LYS C NZ  1 
ATOM   14701 N  N   . ARG C  2  626 ? 75.953  67.311  21.623  1.00 72.83  ?  626 ARG C N   1 
ATOM   14702 C  CA  . ARG C  2  626 ? 74.622  67.880  21.410  1.00 60.42  ?  626 ARG C CA  1 
ATOM   14703 C  C   . ARG C  2  626 ? 74.581  68.449  20.000  1.00 65.01  ?  626 ARG C C   1 
ATOM   14704 O  O   . ARG C  2  626 ? 73.620  68.211  19.281  1.00 69.14  ?  626 ARG C O   1 
ATOM   14705 C  CB  . ARG C  2  626 ? 74.332  69.021  22.399  1.00 69.33  ?  626 ARG C CB  1 
ATOM   14706 C  CG  . ARG C  2  626 ? 74.150  68.601  23.846  1.00 55.57  ?  626 ARG C CG  1 
ATOM   14707 C  CD  . ARG C  2  626 ? 73.673  69.767  24.691  1.00 61.75  ?  626 ARG C CD  1 
ATOM   14708 N  NE  . ARG C  2  626 ? 72.307  70.153  24.338  1.00 73.29  ?  626 ARG C NE  1 
ATOM   14709 C  CZ  . ARG C  2  626 ? 71.201  69.603  24.836  1.00 75.53  ?  626 ARG C CZ  1 
ATOM   14710 N  NH1 . ARG C  2  626 ? 71.279  68.631  25.739  1.00 56.57  ?  626 ARG C NH1 1 
ATOM   14711 N  NH2 . ARG C  2  626 ? 70.008  70.025  24.438  1.00 76.92  ?  626 ARG C NH2 1 
ATOM   14712 N  N   . LYS C  2  627 ? 75.628  69.180  19.609  1.00 60.70  ?  627 LYS C N   1 
ATOM   14713 C  CA  . LYS C  2  627 ? 75.643  69.823  18.266  1.00 67.25  ?  627 LYS C CA  1 
ATOM   14714 C  C   . LYS C  2  627 ? 75.638  68.735  17.182  1.00 60.59  ?  627 LYS C C   1 
ATOM   14715 O  O   . LYS C  2  627 ? 74.888  68.898  16.202  1.00 78.29  ?  627 LYS C O   1 
ATOM   14716 C  CB  . LYS C  2  627 ? 76.826  70.793  18.147  1.00 61.71  ?  627 LYS C CB  1 
ATOM   14717 C  CG  . LYS C  2  627 ? 77.017  71.743  19.327  1.00 91.66  ?  627 LYS C CG  1 
ATOM   14718 C  CD  . LYS C  2  627 ? 76.657  73.196  19.060  1.00 89.97  ?  627 LYS C CD  1 
ATOM   14719 C  CE  . LYS C  2  627 ? 76.883  74.112  20.250  1.00 94.23  ?  627 LYS C CE  1 
ATOM   14720 N  NZ  . LYS C  2  627 ? 76.512  73.453  21.525  1.00 99.21  ?  627 LYS C NZ  1 
ATOM   14721 N  N   . LYS C  2  628 ? 76.425  67.666  17.352  1.00 57.26  ?  628 LYS C N   1 
ATOM   14722 C  CA  . LYS C  2  628 ? 76.445  66.568  16.389  1.00 58.58  ?  628 LYS C CA  1 
ATOM   14723 C  C   . LYS C  2  628 ? 75.057  65.934  16.245  1.00 57.93  ?  628 LYS C C   1 
ATOM   14724 O  O   . LYS C  2  628 ? 74.639  65.599  15.141  1.00 63.56  ?  628 LYS C O   1 
ATOM   14725 C  CB  . LYS C  2  628 ? 77.480  65.517  16.826  1.00 59.89  ?  628 LYS C CB  1 
ATOM   14726 C  CG  . LYS C  2  628 ? 77.627  64.343  15.871  1.00 74.42  ?  628 LYS C CG  1 
ATOM   14727 C  CD  . LYS C  2  628 ? 78.714  63.378  16.325  1.00 76.36  ?  628 LYS C CD  1 
ATOM   14728 C  CE  . LYS C  2  628 ? 78.815  62.192  15.398  1.00 88.49  ?  628 LYS C CE  1 
ATOM   14729 N  NZ  . LYS C  2  628 ? 79.898  61.260  15.805  1.00 89.51  ?  628 LYS C NZ  1 
ATOM   14730 N  N   . LEU C  2  629 ? 74.340  65.780  17.354  1.00 67.28  ?  629 LEU C N   1 
ATOM   14731 C  CA  . LEU C  2  629 ? 73.008  65.182  17.346  1.00 58.83  ?  629 LEU C CA  1 
ATOM   14732 C  C   . LEU C  2  629 ? 71.905  66.159  16.890  1.00 64.33  ?  629 LEU C C   1 
ATOM   14733 O  O   . LEU C  2  629 ? 70.840  65.719  16.460  1.00 73.79  ?  629 LEU C O   1 
ATOM   14734 C  CB  . LEU C  2  629 ? 72.711  64.649  18.759  1.00 58.37  ?  629 LEU C CB  1 
ATOM   14735 C  CG  . LEU C  2  629 ? 71.470  63.781  18.939  1.00 59.29  ?  629 LEU C CG  1 
ATOM   14736 C  CD1 . LEU C  2  629 ? 71.541  62.532  18.080  1.00 59.76  ?  629 LEU C CD1 1 
ATOM   14737 C  CD2 . LEU C  2  629 ? 71.295  63.400  20.396  1.00 49.17  ?  629 LEU C CD2 1 
ATOM   14738 N  N   . GLY C  2  630 ? 72.166  67.459  16.982  1.00 75.20  ?  630 GLY C N   1 
ATOM   14739 C  CA  . GLY C  2  630 ? 71.214  68.491  16.594  1.00 68.72  ?  630 GLY C CA  1 
ATOM   14740 C  C   . GLY C  2  630 ? 70.272  68.872  17.717  1.00 69.58  ?  630 GLY C C   1 
ATOM   14741 O  O   . GLY C  2  630 ? 69.112  69.197  17.462  1.00 74.74  ?  630 GLY C O   1 
ATOM   14742 N  N   . ILE C  2  631 ? 70.758  68.838  18.973  1.00 77.50  ?  631 ILE C N   1 
ATOM   14743 C  CA  . ILE C  2  631 ? 69.947  69.178  20.147  1.00 72.19  ?  631 ILE C CA  1 
ATOM   14744 C  C   . ILE C  2  631 ? 70.639  70.259  20.986  1.00 76.98  ?  631 ILE C C   1 
ATOM   14745 O  O   . ILE C  2  631 ? 71.424  71.050  20.461  1.00 85.41  ?  631 ILE C O   1 
ATOM   14746 C  CB  . ILE C  2  631 ? 69.622  67.918  20.999  1.00 60.12  ?  631 ILE C CB  1 
ATOM   14747 C  CG1 . ILE C  2  631 ? 70.889  67.334  21.659  1.00 64.18  ?  631 ILE C CG1 1 
ATOM   14748 C  CG2 . ILE C  2  631 ? 68.914  66.866  20.151  1.00 57.31  ?  631 ILE C CG2 1 
ATOM   14749 C  CD1 . ILE C  2  631 ? 70.621  66.435  22.865  1.00 61.57  ?  631 ILE C CD1 1 
ATOM   14750 N  N   . MET D  1  1   ? 66.806  72.826  13.635  1.00 92.98  ?  1   MET D N   1 
ATOM   14751 C  CA  . MET D  1  1   ? 67.615  73.367  14.725  1.00 85.01  ?  1   MET D CA  1 
ATOM   14752 C  C   . MET D  1  1   ? 66.926  73.149  16.072  1.00 85.60  ?  1   MET D C   1 
ATOM   14753 O  O   . MET D  1  1   ? 65.704  73.003  16.128  1.00 82.51  ?  1   MET D O   1 
ATOM   14754 C  CB  . MET D  1  1   ? 67.918  74.863  14.509  1.00 70.92  ?  1   MET D CB  1 
ATOM   14755 C  CG  . MET D  1  1   ? 66.711  75.686  14.094  1.00 84.95  ?  1   MET D CG  1 
ATOM   14756 S  SD  . MET D  1  1   ? 66.916  77.472  14.324  1.00 108.73 ?  1   MET D SD  1 
ATOM   14757 C  CE  . MET D  1  1   ? 68.278  77.802  13.214  1.00 81.16  ?  1   MET D CE  1 
ATOM   14758 N  N   . ASN D  1  2   ? 67.713  73.123  17.159  1.00 85.51  ?  2   ASN D N   1 
ATOM   14759 C  CA  . ASN D  1  2   ? 67.190  72.912  18.511  1.00 83.57  ?  2   ASN D CA  1 
ATOM   14760 C  C   . ASN D  1  2   ? 66.272  74.053  18.991  1.00 81.96  ?  2   ASN D C   1 
ATOM   14761 O  O   . ASN D  1  2   ? 66.238  75.127  18.388  1.00 73.26  ?  2   ASN D O   1 
ATOM   14762 C  CB  . ASN D  1  2   ? 68.342  72.686  19.500  1.00 82.40  ?  2   ASN D CB  1 
ATOM   14763 C  CG  . ASN D  1  2   ? 69.246  73.879  19.678  1.00 91.70  ?  2   ASN D CG  1 
ATOM   14764 O  OD1 . ASN D  1  2   ? 69.236  74.821  18.882  1.00 91.26  ?  2   ASN D OD1 1 
ATOM   14765 N  ND2 . ASN D  1  2   ? 70.052  73.863  20.728  1.00 106.51 ?  2   ASN D ND2 1 
ATOM   14766 N  N   . LEU D  1  3   ? 65.525  73.802  20.078  1.00 81.94  ?  3   LEU D N   1 
ATOM   14767 C  CA  . LEU D  1  3   ? 64.585  74.764  20.653  1.00 69.54  ?  3   LEU D CA  1 
ATOM   14768 C  C   . LEU D  1  3   ? 65.223  76.117  20.942  1.00 78.56  ?  3   LEU D C   1 
ATOM   14769 O  O   . LEU D  1  3   ? 64.600  77.144  20.685  1.00 83.64  ?  3   LEU D O   1 
ATOM   14770 C  CB  . LEU D  1  3   ? 63.981  74.193  21.949  1.00 67.55  ?  3   LEU D CB  1 
ATOM   14771 C  CG  . LEU D  1  3   ? 62.836  74.973  22.591  1.00 64.74  ?  3   LEU D CG  1 
ATOM   14772 C  CD1 . LEU D  1  3   ? 61.668  75.151  21.624  1.00 56.14  ?  3   LEU D CD1 1 
ATOM   14773 C  CD2 . LEU D  1  3   ? 62.366  74.279  23.861  1.00 58.94  ?  3   LEU D CD2 1 
ATOM   14774 N  N   . PHE D  1  4   ? 66.447  76.132  21.477  1.00 71.71  ?  4   PHE D N   1 
ATOM   14775 C  CA  . PHE D  1  4   ? 67.114  77.386  21.805  1.00 62.25  ?  4   PHE D CA  1 
ATOM   14776 C  C   . PHE D  1  4   ? 67.351  78.251  20.573  1.00 78.95  ?  4   PHE D C   1 
ATOM   14777 O  O   . PHE D  1  4   ? 66.876  79.389  20.523  1.00 76.32  ?  4   PHE D O   1 
ATOM   14778 C  CB  . PHE D  1  4   ? 68.438  77.128  22.541  1.00 79.53  ?  4   PHE D CB  1 
ATOM   14779 C  CG  . PHE D  1  4   ? 68.260  76.885  24.019  1.00 82.93  ?  4   PHE D CG  1 
ATOM   14780 C  CD1 . PHE D  1  4   ? 67.887  75.640  24.492  1.00 83.63  ?  4   PHE D CD1 1 
ATOM   14781 C  CD2 . PHE D  1  4   ? 68.413  77.914  24.927  1.00 75.50  ?  4   PHE D CD2 1 
ATOM   14782 C  CE1 . PHE D  1  4   ? 67.699  75.425  25.849  1.00 69.25  ?  4   PHE D CE1 1 
ATOM   14783 C  CE2 . PHE D  1  4   ? 68.226  77.695  26.280  1.00 71.09  ?  4   PHE D CE2 1 
ATOM   14784 C  CZ  . PHE D  1  4   ? 67.874  76.452  26.734  1.00 71.55  ?  4   PHE D CZ  1 
ATOM   14785 N  N   . GLN D  1  5   ? 68.058  77.722  19.565  1.00 80.79  ?  5   GLN D N   1 
ATOM   14786 C  CA  . GLN D  1  5   ? 68.324  78.506  18.359  1.00 75.92  ?  5   GLN D CA  1 
ATOM   14787 C  C   . GLN D  1  5   ? 67.029  78.888  17.638  1.00 71.25  ?  5   GLN D C   1 
ATOM   14788 O  O   . GLN D  1  5   ? 66.991  79.930  16.992  1.00 72.95  ?  5   GLN D O   1 
ATOM   14789 C  CB  . GLN D  1  5   ? 69.314  77.790  17.428  1.00 71.04  ?  5   GLN D CB  1 
ATOM   14790 C  CG  . GLN D  1  5   ? 70.695  77.541  18.053  1.00 78.34  ?  5   GLN D CG  1 
ATOM   14791 C  CD  . GLN D  1  5   ? 71.305  78.749  18.742  1.00 92.09  ?  5   GLN D CD  1 
ATOM   14792 O  OE1 . GLN D  1  5   ? 71.244  79.883  18.246  1.00 83.49  ?  5   GLN D OE1 1 
ATOM   14793 N  NE2 . GLN D  1  5   ? 71.914  78.535  19.906  1.00 91.12  ?  5   GLN D NE2 1 
ATOM   14794 N  N   . THR D  1  6   ? 65.963  78.080  17.769  1.00 72.79  ?  6   THR D N   1 
ATOM   14795 C  CA  . THR D  1  6   ? 64.674  78.392  17.152  1.00 74.54  ?  6   THR D CA  1 
ATOM   14796 C  C   . THR D  1  6   ? 64.064  79.614  17.845  1.00 72.98  ?  6   THR D C   1 
ATOM   14797 O  O   . THR D  1  6   ? 63.468  80.459  17.178  1.00 77.85  ?  6   THR D O   1 
ATOM   14798 C  CB  . THR D  1  6   ? 63.741  77.184  17.226  1.00 74.53  ?  6   THR D CB  1 
ATOM   14799 O  OG1 . THR D  1  6   ? 64.414  76.047  16.683  1.00 87.44  ?  6   THR D OG1 1 
ATOM   14800 C  CG2 . THR D  1  6   ? 62.440  77.411  16.479  1.00 58.52  ?  6   THR D CG2 1 
ATOM   14801 N  N   . VAL D  1  7   ? 64.216  79.716  19.174  1.00 67.95  ?  7   VAL D N   1 
ATOM   14802 C  CA  . VAL D  1  7   ? 63.694  80.860  19.917  1.00 70.53  ?  7   VAL D CA  1 
ATOM   14803 C  C   . VAL D  1  7   ? 64.550  82.087  19.576  1.00 74.44  ?  7   VAL D C   1 
ATOM   14804 O  O   . VAL D  1  7   ? 64.003  83.139  19.245  1.00 76.22  ?  7   VAL D O   1 
ATOM   14805 C  CB  . VAL D  1  7   ? 63.643  80.584  21.445  1.00 69.87  ?  7   VAL D CB  1 
ATOM   14806 C  CG1 . VAL D  1  7   ? 63.428  81.871  22.236  1.00 76.42  ?  7   VAL D CG1 1 
ATOM   14807 C  CG2 . VAL D  1  7   ? 62.555  79.568  21.778  1.00 64.29  ?  7   VAL D CG2 1 
ATOM   14808 N  N   . PHE D  1  8   ? 65.887  81.956  19.619  1.00 66.53  ?  8   PHE D N   1 
ATOM   14809 C  CA  . PHE D  1  8   ? 66.768  83.082  19.296  1.00 68.97  ?  8   PHE D CA  1 
ATOM   14810 C  C   . PHE D  1  8   ? 66.516  83.602  17.873  1.00 76.33  ?  8   PHE D C   1 
ATOM   14811 O  O   . PHE D  1  8   ? 66.564  84.810  17.657  1.00 91.20  ?  8   PHE D O   1 
ATOM   14812 C  CB  . PHE D  1  8   ? 68.253  82.708  19.471  1.00 65.35  ?  8   PHE D CB  1 
ATOM   14813 C  CG  . PHE D  1  8   ? 68.677  82.270  20.858  1.00 73.95  ?  8   PHE D CG  1 
ATOM   14814 C  CD1 . PHE D  1  8   ? 68.204  82.919  21.985  1.00 64.29  ?  8   PHE D CD1 1 
ATOM   14815 C  CD2 . PHE D  1  8   ? 69.580  81.234  21.029  1.00 76.62  ?  8   PHE D CD2 1 
ATOM   14816 C  CE1 . PHE D  1  8   ? 68.606  82.521  23.255  1.00 65.16  ?  8   PHE D CE1 1 
ATOM   14817 C  CE2 . PHE D  1  8   ? 69.979  80.839  22.300  1.00 69.10  ?  8   PHE D CE2 1 
ATOM   14818 C  CZ  . PHE D  1  8   ? 69.492  81.488  23.403  1.00 68.91  ?  8   PHE D CZ  1 
ATOM   14819 N  N   . THR D  1  9   ? 66.229  82.709  16.914  1.00 68.04  ?  9   THR D N   1 
ATOM   14820 C  CA  . THR D  1  9   ? 65.970  83.122  15.535  1.00 69.91  ?  9   THR D CA  1 
ATOM   14821 C  C   . THR D  1  9   ? 64.702  83.975  15.447  1.00 79.71  ?  9   THR D C   1 
ATOM   14822 O  O   . THR D  1  9   ? 64.731  85.055  14.860  1.00 90.43  ?  9   THR D O   1 
ATOM   14823 C  CB  . THR D  1  9   ? 65.888  81.899  14.613  1.00 72.14  ?  9   THR D CB  1 
ATOM   14824 O  OG1 . THR D  1  9   ? 67.158  81.245  14.591  1.00 73.35  ?  9   THR D OG1 1 
ATOM   14825 C  CG2 . THR D  1  9   ? 65.476  82.266  13.197  1.00 78.50  ?  9   THR D CG2 1 
ATOM   14826 N  N   . GLY D  1  10  ? 63.612  83.492  16.031  1.00 68.47  ?  10  GLY D N   1 
ATOM   14827 C  CA  . GLY D  1  10  ? 62.346  84.210  16.020  1.00 71.51  ?  10  GLY D CA  1 
ATOM   14828 C  C   . GLY D  1  10  ? 62.404  85.524  16.772  1.00 77.18  ?  10  GLY D C   1 
ATOM   14829 O  O   . GLY D  1  10  ? 61.720  86.477  16.397  1.00 79.22  ?  10  GLY D O   1 
ATOM   14830 N  N   . SER D  1  11  ? 63.209  85.587  17.850  1.00 78.15  ?  11  SER D N   1 
ATOM   14831 C  CA  . SER D  1  11  ? 63.358  86.813  18.640  1.00 72.60  ?  11  SER D CA  1 
ATOM   14832 C  C   . SER D  1  11  ? 64.132  87.840  17.823  1.00 80.05  ?  11  SER D C   1 
ATOM   14833 O  O   . SER D  1  11  ? 63.765  89.013  17.821  1.00 80.43  ?  11  SER D O   1 
ATOM   14834 C  CB  . SER D  1  11  ? 64.074  86.534  19.959  1.00 64.85  ?  11  SER D CB  1 
ATOM   14835 O  OG  . SER D  1  11  ? 63.235  85.820  20.854  1.00 77.81  ?  11  SER D OG  1 
ATOM   14836 N  N   . LYS D  1  12  ? 65.188  87.408  17.113  1.00 76.80  ?  12  LYS D N   1 
ATOM   14837 C  CA  . LYS D  1  12  ? 65.957  88.316  16.260  1.00 82.74  ?  12  LYS D CA  1 
ATOM   14838 C  C   . LYS D  1  12  ? 65.057  88.818  15.120  1.00 79.46  ?  12  LYS D C   1 
ATOM   14839 O  O   . LYS D  1  12  ? 65.156  89.981  14.731  1.00 72.96  ?  12  LYS D O   1 
ATOM   14840 C  CB  . LYS D  1  12  ? 67.205  87.616  15.695  1.00 85.93  ?  12  LYS D CB  1 
ATOM   14841 C  CG  . LYS D  1  12  ? 68.457  87.771  16.567  1.00 84.30  ?  12  LYS D CG  1 
ATOM   14842 C  CD  . LYS D  1  12  ? 69.238  86.475  16.742  1.00 81.11  ?  12  LYS D CD  1 
ATOM   14843 C  CE  . LYS D  1  12  ? 70.017  86.060  15.514  1.00 83.60  ?  12  LYS D CE  1 
ATOM   14844 N  NZ  . LYS D  1  12  ? 70.658  84.723  15.677  1.00 105.82 ?  12  LYS D NZ  1 
ATOM   14845 N  N   . GLN D  1  13  ? 64.165  87.946  14.609  1.00 79.70  ?  13  GLN D N   1 
ATOM   14846 C  CA  . GLN D  1  13  ? 63.209  88.303  13.561  1.00 84.29  ?  13  GLN D CA  1 
ATOM   14847 C  C   . GLN D  1  13  ? 62.248  89.359  14.121  1.00 75.47  ?  13  GLN D C   1 
ATOM   14848 O  O   . GLN D  1  13  ? 61.945  90.337  13.441  1.00 69.34  ?  13  GLN D O   1 
ATOM   14849 C  CB  . GLN D  1  13  ? 62.411  87.065  13.099  1.00 72.31  ?  13  GLN D CB  1 
ATOM   14850 C  CG  . GLN D  1  13  ? 63.222  86.060  12.282  1.00 84.83  ?  13  GLN D CG  1 
ATOM   14851 C  CD  . GLN D  1  13  ? 62.426  84.832  11.890  1.00 100.55 ?  13  GLN D CD  1 
ATOM   14852 O  OE1 . GLN D  1  13  ? 61.245  84.675  12.236  1.00 88.27  ?  13  GLN D OE1 1 
ATOM   14853 N  NE2 . GLN D  1  13  ? 63.060  83.925  11.152  1.00 98.94  ?  13  GLN D NE2 1 
ATOM   14854 N  N   . ALA D  1  14  ? 61.775  89.164  15.364  1.00 74.93  ?  14  ALA D N   1 
ATOM   14855 C  CA  . ALA D  1  14  ? 60.872  90.105  16.017  1.00 67.85  ?  14  ALA D CA  1 
ATOM   14856 C  C   . ALA D  1  14  ? 61.564  91.449  16.222  1.00 80.17  ?  14  ALA D C   1 
ATOM   14857 O  O   . ALA D  1  14  ? 60.909  92.482  16.105  1.00 79.94  ?  14  ALA D O   1 
ATOM   14858 C  CB  . ALA D  1  14  ? 60.405  89.547  17.352  1.00 65.06  ?  14  ALA D CB  1 
ATOM   14859 N  N   . LEU D  1  15  ? 62.876  91.451  16.523  1.00 77.25  ?  15  LEU D N   1 
ATOM   14860 C  CA  . LEU D  1  15  ? 63.606  92.703  16.701  1.00 65.87  ?  15  LEU D CA  1 
ATOM   14861 C  C   . LEU D  1  15  ? 63.689  93.413  15.349  1.00 67.03  ?  15  LEU D C   1 
ATOM   14862 O  O   . LEU D  1  15  ? 63.411  94.607  15.272  1.00 77.08  ?  15  LEU D O   1 
ATOM   14863 C  CB  . LEU D  1  15  ? 65.013  92.452  17.271  1.00 62.96  ?  15  LEU D CB  1 
ATOM   14864 C  CG  . LEU D  1  15  ? 65.961  93.659  17.281  1.00 64.50  ?  15  LEU D CG  1 
ATOM   14865 C  CD1 . LEU D  1  15  ? 65.550  94.680  18.309  1.00 78.23  ?  15  LEU D CD1 1 
ATOM   14866 C  CD2 . LEU D  1  15  ? 67.379  93.234  17.556  1.00 66.72  ?  15  LEU D CD2 1 
ATOM   14867 N  N   . ALA D  1  16  ? 64.055  92.675  14.286  1.00 73.77  ?  16  ALA D N   1 
ATOM   14868 C  CA  . ALA D  1  16  ? 64.166  93.226  12.933  1.00 80.01  ?  16  ALA D CA  1 
ATOM   14869 C  C   . ALA D  1  16  ? 62.843  93.848  12.473  1.00 81.51  ?  16  ALA D C   1 
ATOM   14870 O  O   . ALA D  1  16  ? 62.847  94.923  11.867  1.00 70.90  ?  16  ALA D O   1 
ATOM   14871 C  CB  . ALA D  1  16  ? 64.589  92.134  11.964  1.00 67.08  ?  16  ALA D CB  1 
ATOM   14872 N  N   . ALA D  1  17  ? 61.716  93.180  12.761  1.00 74.27  ?  17  ALA D N   1 
ATOM   14873 C  CA  . ALA D  1  17  ? 60.396  93.672  12.381  1.00 75.54  ?  17  ALA D CA  1 
ATOM   14874 C  C   . ALA D  1  17  ? 60.071  94.958  13.135  1.00 77.31  ?  17  ALA D C   1 
ATOM   14875 O  O   . ALA D  1  17  ? 59.540  95.899  12.543  1.00 71.85  ?  17  ALA D O   1 
ATOM   14876 C  CB  . ALA D  1  17  ? 59.344  92.612  12.669  1.00 67.47  ?  17  ALA D CB  1 
ATOM   14877 N  N   . ALA D  1  18  ? 60.391  95.005  14.437  1.00 78.76  ?  18  ALA D N   1 
ATOM   14878 C  CA  . ALA D  1  18  ? 60.146  96.190  15.257  1.00 74.63  ?  18  ALA D CA  1 
ATOM   14879 C  C   . ALA D  1  18  ? 61.047  97.346  14.812  1.00 82.56  ?  18  ALA D C   1 
ATOM   14880 O  O   . ALA D  1  18  ? 60.641  98.500  14.896  1.00 90.42  ?  18  ALA D O   1 
ATOM   14881 C  CB  . ALA D  1  18  ? 60.390  95.870  16.722  1.00 64.73  ?  18  ALA D CB  1 
ATOM   14882 N  N   . GLU D  1  19  ? 62.264  97.040  14.339  1.00 77.71  ?  19  GLU D N   1 
ATOM   14883 C  CA  . GLU D  1  19  ? 63.192  98.057  13.860  1.00 70.22  ?  19  GLU D CA  1 
ATOM   14884 C  C   . GLU D  1  19  ? 62.710  98.701  12.560  1.00 82.76  ?  19  GLU D C   1 
ATOM   14885 O  O   . GLU D  1  19  ? 62.960  99.882  12.330  1.00 87.26  ?  19  GLU D O   1 
ATOM   14886 C  CB  . GLU D  1  19  ? 64.559  97.432  13.536  1.00 85.52  ?  19  GLU D CB  1 
ATOM   14887 C  CG  . GLU D  1  19  ? 65.431  97.138  14.745  1.00 86.21  ?  19  GLU D CG  1 
ATOM   14888 C  CD  . GLU D  1  19  ? 66.710  96.384  14.425  1.00 96.65  ?  19  GLU D CD  1 
ATOM   14889 O  OE1 . GLU D  1  19  ? 66.936  96.057  13.236  1.00 105.26 ?  19  GLU D OE1 1 
ATOM   14890 O  OE2 . GLU D  1  19  ? 67.492  96.122  15.367  1.00 103.69 ?  19  GLU D OE2 1 
ATOM   14891 N  N   . GLY D  1  20  ? 62.032  97.917  11.724  1.00 81.09  ?  20  GLY D N   1 
ATOM   14892 C  CA  . GLY D  1  20  ? 61.521  98.384  10.441  1.00 90.63  ?  20  GLY D CA  1 
ATOM   14893 C  C   . GLY D  1  20  ? 60.324  99.299  10.596  1.00 80.72  ?  20  GLY D C   1 
ATOM   14894 O  O   . GLY D  1  20  ? 60.285  100.371 9.991   1.00 90.42  ?  20  GLY D O   1 
ATOM   14895 N  N   . ILE D  1  21  ? 59.333  98.882  11.393  1.00 84.37  ?  21  ILE D N   1 
ATOM   14896 C  CA  . ILE D  1  21  ? 58.128  99.686  11.607  1.00 87.21  ?  21  ILE D CA  1 
ATOM   14897 C  C   . ILE D  1  21  ? 58.433  100.948 12.426  1.00 81.07  ?  21  ILE D C   1 
ATOM   14898 O  O   . ILE D  1  21  ? 57.797  101.975 12.199  1.00 89.87  ?  21  ILE D O   1 
ATOM   14899 C  CB  . ILE D  1  21  ? 56.973  98.845  12.224  1.00 82.30  ?  21  ILE D CB  1 
ATOM   14900 C  CG1 . ILE D  1  21  ? 55.616  99.566  12.056  1.00 73.50  ?  21  ILE D CG1 1 
ATOM   14901 C  CG2 . ILE D  1  21  ? 57.244  98.511  13.692  1.00 83.74  ?  21  ILE D CG2 1 
ATOM   14902 C  CD1 . ILE D  1  21  ? 54.413  98.705  12.305  1.00 82.50  ?  21  ILE D CD1 1 
ATOM   14903 N  N   . VAL D  1  22  ? 59.405  100.871 13.339  1.00 85.51  ?  22  VAL D N   1 
ATOM   14904 C  CA  . VAL D  1  22  ? 59.780  102.060 14.162  1.00 81.25  ?  22  VAL D CA  1 
ATOM   14905 C  C   . VAL D  1  22  ? 60.414  103.114 13.246  1.00 87.17  ?  22  VAL D C   1 
ATOM   14906 O  O   . VAL D  1  22  ? 60.137  104.311 13.451  1.00 92.68  ?  22  VAL D O   1 
ATOM   14907 C  CB  . VAL D  1  22  ? 60.706  101.684 15.335  1.00 89.77  ?  22  VAL D CB  1 
ATOM   14908 C  CG1 . VAL D  1  22  ? 62.158  101.558 14.903  1.00 123.08 ?  22  VAL D CG1 1 
ATOM   14909 C  CG2 . VAL D  1  22  ? 60.574  102.661 16.493  1.00 74.99  ?  22  VAL D CG2 1 
ATOM   14910 N  N   . LYS D  1  23  ? 61.225  102.686 12.274  1.00 83.59  ?  23  LYS D N   1 
ATOM   14911 C  CA  . LYS D  1  23  ? 61.840  103.618 11.334  1.00 100.50 ?  23  LYS D CA  1 
ATOM   14912 C  C   . LYS D  1  23  ? 60.757  104.303 10.494  1.00 99.97  ?  23  LYS D C   1 
ATOM   14913 O  O   . LYS D  1  23  ? 60.837  105.503 10.246  1.00 91.19  ?  23  LYS D O   1 
ATOM   14914 C  CB  . LYS D  1  23  ? 62.845  102.885 10.428  1.00 94.36  ?  23  LYS D CB  1 
ATOM   14915 C  CG  . LYS D  1  23  ? 63.754  103.792 9.574   1.00 108.14 ?  23  LYS D CG  1 
ATOM   14916 C  CD  . LYS D  1  23  ? 64.499  104.934 10.326  1.00 120.34 ?  23  LYS D CD  1 
ATOM   14917 C  CE  . LYS D  1  23  ? 65.375  104.509 11.495  1.00 127.99 ?  23  LYS D CE  1 
ATOM   14918 N  NZ  . LYS D  1  23  ? 64.970  105.163 12.773  1.00 105.41 ?  23  LYS D NZ  1 
ATOM   14919 N  N   . GLN D  1  24  ? 59.727  103.548 10.095  1.00 86.57  ?  24  GLN D N   1 
ATOM   14920 C  CA  . GLN D  1  24  ? 58.616  104.081 9.316   1.00 82.96  ?  24  GLN D CA  1 
ATOM   14921 C  C   . GLN D  1  24  ? 57.906  105.194 10.097  1.00 90.90  ?  24  GLN D C   1 
ATOM   14922 O  O   . GLN D  1  24  ? 57.527  106.202 9.509   1.00 103.10 ?  24  GLN D O   1 
ATOM   14923 C  CB  . GLN D  1  24  ? 57.634  102.954 8.965   1.00 84.95  ?  24  GLN D CB  1 
ATOM   14924 C  CG  . GLN D  1  24  ? 56.602  103.337 7.914   1.00 102.75 ?  24  GLN D CG  1 
ATOM   14925 C  CD  . GLN D  1  24  ? 55.734  102.170 7.499   1.00 113.34 ?  24  GLN D CD  1 
ATOM   14926 O  OE1 . GLN D  1  24  ? 56.072  100.994 7.713   1.00 111.86 ?  24  GLN D OE1 1 
ATOM   14927 N  NE2 . GLN D  1  24  ? 54.592  102.471 6.889   1.00 85.01  ?  24  GLN D NE2 1 
ATOM   14928 N  N   . ALA D  1  25  ? 57.741  105.021 11.418  1.00 92.09  ?  25  ALA D N   1 
ATOM   14929 C  CA  . ALA D  1  25  ? 57.097  106.027 12.268  1.00 94.38  ?  25  ALA D CA  1 
ATOM   14930 C  C   . ALA D  1  25  ? 57.989  107.262 12.423  1.00 100.21 ?  25  ALA D C   1 
ATOM   14931 O  O   . ALA D  1  25  ? 57.482  108.380 12.479  1.00 93.66  ?  25  ALA D O   1 
ATOM   14932 C  CB  . ALA D  1  25  ? 56.787  105.435 13.634  1.00 80.25  ?  25  ALA D CB  1 
ATOM   14933 N  N   . VAL D  1  26  ? 59.311  107.065 12.490  1.00 98.09  ?  26  VAL D N   1 
ATOM   14934 C  CA  . VAL D  1  26  ? 60.255  108.173 12.617  1.00 93.06  ?  26  VAL D CA  1 
ATOM   14935 C  C   . VAL D  1  26  ? 60.213  108.999 11.328  1.00 97.50  ?  26  VAL D C   1 
ATOM   14936 O  O   . VAL D  1  26  ? 60.120  110.224 11.383  1.00 102.38 ?  26  VAL D O   1 
ATOM   14937 C  CB  . VAL D  1  26  ? 61.691  107.654 12.916  1.00 85.06  ?  26  VAL D CB  1 
ATOM   14938 C  CG1 . VAL D  1  26  ? 62.745  108.730 12.661  1.00 87.59  ?  26  VAL D CG1 1 
ATOM   14939 C  CG2 . VAL D  1  26  ? 61.796  107.128 14.344  1.00 89.21  ?  26  VAL D CG2 1 
ATOM   14940 N  N   . ASP D  1  27  ? 60.261  108.324 10.174  1.00 96.79  ?  27  ASP D N   1 
ATOM   14941 C  CA  . ASP D  1  27  ? 60.253  108.989 8.872   1.00 106.48 ?  27  ASP D CA  1 
ATOM   14942 C  C   . ASP D  1  27  ? 58.912  109.636 8.496   1.00 103.08 ?  27  ASP D C   1 
ATOM   14943 O  O   . ASP D  1  27  ? 58.921  110.656 7.809   1.00 105.95 ?  27  ASP D O   1 
ATOM   14944 C  CB  . ASP D  1  27  ? 60.677  108.000 7.771   1.00 117.38 ?  27  ASP D CB  1 
ATOM   14945 C  CG  . ASP D  1  27  ? 62.054  107.391 7.970   1.00 114.02 ?  27  ASP D CG  1 
ATOM   14946 O  OD1 . ASP D  1  27  ? 62.811  107.896 8.828   1.00 117.77 ?  27  ASP D OD1 1 
ATOM   14947 O  OD2 . ASP D  1  27  ? 62.372  106.404 7.270   1.00 109.29 ?  27  ASP D OD2 1 
ATOM   14948 N  N   . GLU D  1  28  ? 57.771  109.062 8.918   1.00 92.30  ?  28  GLU D N   1 
ATOM   14949 C  CA  . GLU D  1  28  ? 56.463  109.616 8.560   1.00 94.12  ?  28  GLU D CA  1 
ATOM   14950 C  C   . GLU D  1  28  ? 55.878  110.566 9.599   1.00 94.72  ?  28  GLU D C   1 
ATOM   14951 O  O   . GLU D  1  28  ? 55.371  111.625 9.234   1.00 113.25 ?  28  GLU D O   1 
ATOM   14952 C  CB  . GLU D  1  28  ? 55.451  108.487 8.297   1.00 92.60  ?  28  GLU D CB  1 
ATOM   14953 C  CG  . GLU D  1  28  ? 55.711  107.720 7.015   1.00 112.27 ?  28  GLU D CG  1 
ATOM   14954 C  CD  . GLU D  1  28  ? 54.720  106.605 6.746   1.00 122.81 ?  28  GLU D CD  1 
ATOM   14955 O  OE1 . GLU D  1  28  ? 53.581  106.683 7.261   1.00 122.03 ?  28  GLU D OE1 1 
ATOM   14956 O  OE2 . GLU D  1  28  ? 55.084  105.654 6.017   1.00 113.38 ?  28  GLU D OE2 1 
ATOM   14957 N  N   . LYS D  1  29  ? 55.907  110.185 10.879  1.00 92.28  ?  29  LYS D N   1 
ATOM   14958 C  CA  . LYS D  1  29  ? 55.320  111.001 11.942  1.00 92.84  ?  29  LYS D CA  1 
ATOM   14959 C  C   . LYS D  1  29  ? 56.335  111.798 12.786  1.00 94.29  ?  29  LYS D C   1 
ATOM   14960 O  O   . LYS D  1  29  ? 55.926  112.659 13.564  1.00 94.49  ?  29  LYS D O   1 
ATOM   14961 C  CB  . LYS D  1  29  ? 54.459  110.110 12.856  1.00 90.27  ?  29  LYS D CB  1 
ATOM   14962 C  CG  . LYS D  1  29  ? 53.344  109.348 12.134  1.00 89.98  ?  29  LYS D CG  1 
ATOM   14963 C  CD  . LYS D  1  29  ? 52.119  110.215 11.884  1.00 92.58  ?  29  LYS D CD  1 
ATOM   14964 C  CE  . LYS D  1  29  ? 50.952  109.433 11.333  1.00 96.76  ?  29  LYS D CE  1 
ATOM   14965 N  NZ  . LYS D  1  29  ? 49.689  110.220 11.372  1.00 98.45  ?  29  LYS D NZ  1 
ATOM   14966 N  N   . GLY D  1  30  ? 57.626  111.516 12.638  1.00 92.71  ?  30  GLY D N   1 
ATOM   14967 C  CA  . GLY D  1  30  ? 58.660  112.215 13.395  1.00 93.37  ?  30  GLY D CA  1 
ATOM   14968 C  C   . GLY D  1  30  ? 58.884  111.624 14.774  1.00 100.24 ?  30  GLY D C   1 
ATOM   14969 O  O   . GLY D  1  30  ? 58.029  110.895 15.282  1.00 105.35 ?  30  GLY D O   1 
ATOM   14970 N  N   . ARG D  1  31  ? 60.027  111.943 15.407  1.00 97.28  ?  31  ARG D N   1 
ATOM   14971 C  CA  . ARG D  1  31  ? 60.356  111.415 16.738  1.00 98.31  ?  31  ARG D CA  1 
ATOM   14972 C  C   . ARG D  1  31  ? 59.541  112.051 17.882  1.00 100.68 ?  31  ARG D C   1 
ATOM   14973 O  O   . ARG D  1  31  ? 59.612  111.564 19.009  1.00 91.37  ?  31  ARG D O   1 
ATOM   14974 C  CB  . ARG D  1  31  ? 61.861  111.564 17.020  1.00 89.49  ?  31  ARG D CB  1 
ATOM   14975 C  CG  . ARG D  1  31  ? 62.746  110.881 15.981  1.00 95.93  ?  31  ARG D CG  1 
ATOM   14976 C  CD  . ARG D  1  31  ? 63.711  109.879 16.575  1.00 90.72  ?  31  ARG D CD  1 
ATOM   14977 N  NE  . ARG D  1  31  ? 64.461  109.173 15.534  1.00 94.56  ?  31  ARG D NE  1 
ATOM   14978 C  CZ  . ARG D  1  31  ? 65.570  109.620 14.950  1.00 100.16 ?  31  ARG D CZ  1 
ATOM   14979 N  NH1 . ARG D  1  31  ? 66.086  110.796 15.293  1.00 110.14 ?  31  ARG D NH1 1 
ATOM   14980 N  NH2 . ARG D  1  31  ? 66.172  108.896 14.015  1.00 100.02 ?  31  ARG D NH2 1 
ATOM   14981 N  N   . ASP D  1  32  ? 58.780  113.123 17.613  1.00 101.20 ?  32  ASP D N   1 
ATOM   14982 C  CA  . ASP D  1  32  ? 57.985  113.781 18.652  1.00 94.09  ?  32  ASP D CA  1 
ATOM   14983 C  C   . ASP D  1  32  ? 56.505  113.378 18.632  1.00 95.28  ?  32  ASP D C   1 
ATOM   14984 O  O   . ASP D  1  32  ? 55.766  113.778 19.531  1.00 92.68  ?  32  ASP D O   1 
ATOM   14985 C  CB  . ASP D  1  32  ? 58.120  115.306 18.531  1.00 98.02  ?  32  ASP D CB  1 
ATOM   14986 C  CG  . ASP D  1  32  ? 59.553  115.789 18.629  1.00 120.75 ?  32  ASP D CG  1 
ATOM   14987 O  OD1 . ASP D  1  32  ? 60.357  115.124 19.316  1.00 122.95 ?  32  ASP D OD1 1 
ATOM   14988 O  OD2 . ASP D  1  32  ? 59.870  116.834 18.018  1.00 116.86 ?  32  ASP D OD2 1 
ATOM   14989 N  N   . TYR D  1  33  ? 56.066  112.585 17.634  1.00 104.89 ?  33  TYR D N   1 
ATOM   14990 C  CA  . TYR D  1  33  ? 54.673  112.145 17.546  1.00 91.12  ?  33  TYR D CA  1 
ATOM   14991 C  C   . TYR D  1  33  ? 54.337  111.293 18.769  1.00 95.28  ?  33  TYR D C   1 
ATOM   14992 O  O   . TYR D  1  33  ? 55.123  110.430 19.153  1.00 98.63  ?  33  TYR D O   1 
ATOM   14993 C  CB  . TYR D  1  33  ? 54.444  111.355 16.248  1.00 89.69  ?  33  TYR D CB  1 
ATOM   14994 C  CG  . TYR D  1  33  ? 52.990  111.074 15.933  1.00 89.87  ?  33  TYR D CG  1 
ATOM   14995 C  CD1 . TYR D  1  33  ? 52.222  111.988 15.226  1.00 92.76  ?  33  TYR D CD1 1 
ATOM   14996 C  CD2 . TYR D  1  33  ? 52.401  109.870 16.288  1.00 97.23  ?  33  TYR D CD2 1 
ATOM   14997 C  CE1 . TYR D  1  33  ? 50.893  111.727 14.913  1.00 93.19  ?  33  TYR D CE1 1 
ATOM   14998 C  CE2 . TYR D  1  33  ? 51.075  109.595 15.979  1.00 90.58  ?  33  TYR D CE2 1 
ATOM   14999 C  CZ  . TYR D  1  33  ? 50.323  110.525 15.287  1.00 92.34  ?  33  TYR D CZ  1 
ATOM   15000 O  OH  . TYR D  1  33  ? 49.009  110.260 14.978  1.00 100.22 ?  33  TYR D OH  1 
ATOM   15001 N  N   . LYS D  1  34  ? 53.183  111.548 19.391  1.00 105.05 ?  34  LYS D N   1 
ATOM   15002 C  CA  . LYS D  1  34  ? 52.782  110.827 20.595  1.00 93.80  ?  34  LYS D CA  1 
ATOM   15003 C  C   . LYS D  1  34  ? 52.331  109.391 20.317  1.00 85.03  ?  34  LYS D C   1 
ATOM   15004 O  O   . LYS D  1  34  ? 51.540  109.147 19.406  1.00 84.22  ?  34  LYS D O   1 
ATOM   15005 C  CB  . LYS D  1  34  ? 51.683  111.601 21.352  1.00 99.18  ?  34  LYS D CB  1 
ATOM   15006 C  CG  . LYS D  1  34  ? 52.098  113.006 21.813  1.00 105.95 ?  34  LYS D CG  1 
ATOM   15007 C  CD  . LYS D  1  34  ? 52.938  113.002 23.102  1.00 118.03 ?  34  LYS D CD  1 
ATOM   15008 C  CE  . LYS D  1  34  ? 53.792  114.246 23.273  1.00 117.08 ?  34  LYS D CE  1 
ATOM   15009 N  NZ  . LYS D  1  34  ? 55.234  113.919 23.456  1.00 112.03 ?  34  LYS D NZ  1 
ATOM   15010 N  N   . VAL D  1  35  ? 52.840  108.444 21.120  1.00 88.42  ?  35  VAL D N   1 
ATOM   15011 C  CA  . VAL D  1  35  ? 52.492  107.027 21.014  1.00 83.54  ?  35  VAL D CA  1 
ATOM   15012 C  C   . VAL D  1  35  ? 51.724  106.654 22.281  1.00 79.35  ?  35  VAL D C   1 
ATOM   15013 O  O   . VAL D  1  35  ? 52.147  107.000 23.384  1.00 78.42  ?  35  VAL D O   1 
ATOM   15014 C  CB  . VAL D  1  35  ? 53.732  106.119 20.779  1.00 80.76  ?  35  VAL D CB  1 
ATOM   15015 C  CG1 . VAL D  1  35  ? 54.629  106.692 19.689  1.00 94.10  ?  35  VAL D CG1 1 
ATOM   15016 C  CG2 . VAL D  1  35  ? 54.529  105.901 22.060  1.00 82.04  ?  35  VAL D CG2 1 
ATOM   15017 N  N   . ALA D  1  36  ? 50.571  105.996 22.128  1.00 85.61  ?  36  ALA D N   1 
ATOM   15018 C  CA  . ALA D  1  36  ? 49.741  105.601 23.267  1.00 78.50  ?  36  ALA D CA  1 
ATOM   15019 C  C   . ALA D  1  36  ? 48.716  104.556 22.850  1.00 83.86  ?  36  ALA D C   1 
ATOM   15020 O  O   . ALA D  1  36  ? 48.357  104.472 21.676  1.00 76.51  ?  36  ALA D O   1 
ATOM   15021 C  CB  . ALA D  1  36  ? 49.026  106.815 23.847  1.00 79.53  ?  36  ALA D CB  1 
ATOM   15022 N  N   . PHE D  1  37  ? 48.240  103.762 23.814  1.00 89.08  ?  37  PHE D N   1 
ATOM   15023 C  CA  . PHE D  1  37  ? 47.247  102.732 23.539  1.00 78.74  ?  37  PHE D CA  1 
ATOM   15024 C  C   . PHE D  1  37  ? 45.852  103.214 24.006  1.00 91.30  ?  37  PHE D C   1 
ATOM   15025 O  O   . PHE D  1  37  ? 45.764  104.004 24.947  1.00 80.74  ?  37  PHE D O   1 
ATOM   15026 C  CB  . PHE D  1  37  ? 47.641  101.404 24.220  1.00 78.25  ?  37  PHE D CB  1 
ATOM   15027 C  CG  . PHE D  1  37  ? 48.541  100.486 23.414  1.00 84.97  ?  37  PHE D CG  1 
ATOM   15028 C  CD1 . PHE D  1  37  ? 48.202  100.109 22.126  1.00 84.61  ?  37  PHE D CD1 1 
ATOM   15029 C  CD2 . PHE D  1  37  ? 49.685  99.942  23.973  1.00 82.87  ?  37  PHE D CD2 1 
ATOM   15030 C  CE1 . PHE D  1  37  ? 49.017  99.253  21.397  1.00 84.97  ?  37  PHE D CE1 1 
ATOM   15031 C  CE2 . PHE D  1  37  ? 50.494  99.079  23.241  1.00 66.81  ?  37  PHE D CE2 1 
ATOM   15032 C  CZ  . PHE D  1  37  ? 50.156  98.743  21.960  1.00 68.25  ?  37  PHE D CZ  1 
ATOM   15033 N  N   . PRO D  1  38  ? 44.750  102.773 23.359  1.00 97.72  ?  38  PRO D N   1 
ATOM   15034 C  CA  . PRO D  1  38  ? 43.417  103.250 23.775  1.00 91.29  ?  38  PRO D CA  1 
ATOM   15035 C  C   . PRO D  1  38  ? 43.014  103.004 25.230  1.00 94.96  ?  38  PRO D C   1 
ATOM   15036 O  O   . PRO D  1  38  ? 42.739  101.867 25.615  1.00 86.39  ?  38  PRO D O   1 
ATOM   15037 C  CB  . PRO D  1  38  ? 42.454  102.519 22.827  1.00 80.77  ?  38  PRO D CB  1 
ATOM   15038 C  CG  . PRO D  1  38  ? 43.269  102.030 21.714  1.00 81.53  ?  38  PRO D CG  1 
ATOM   15039 C  CD  . PRO D  1  38  ? 44.662  101.855 22.206  1.00 95.30  ?  38  PRO D CD  1 
ATOM   15040 N  N   . ASP D  1  39  ? 42.943  104.084 26.027  1.00 101.89 ?  39  ASP D N   1 
ATOM   15041 C  CA  . ASP D  1  39  ? 42.521  104.033 27.427  1.00 92.28  ?  39  ASP D CA  1 
ATOM   15042 C  C   . ASP D  1  39  ? 43.343  103.069 28.297  1.00 92.36  ?  39  ASP D C   1 
ATOM   15043 O  O   . ASP D  1  39  ? 42.911  101.946 28.552  1.00 88.02  ?  39  ASP D O   1 
ATOM   15044 C  CB  . ASP D  1  39  ? 41.017  103.691 27.485  1.00 91.70  ?  39  ASP D CB  1 
ATOM   15045 C  CG  . ASP D  1  39  ? 40.372  103.753 28.857  1.00 113.59 ?  39  ASP D CG  1 
ATOM   15046 O  OD1 . ASP D  1  39  ? 41.044  104.207 29.813  1.00 118.55 ?  39  ASP D OD1 1 
ATOM   15047 O  OD2 . ASP D  1  39  ? 39.193  103.353 28.975  1.00 112.73 ?  39  ASP D OD2 1 
ATOM   15048 N  N   . THR D  1  40  ? 44.524  103.520 28.766  1.00 94.61  ?  40  THR D N   1 
ATOM   15049 C  CA  . THR D  1  40  ? 45.390  102.722 29.642  1.00 86.65  ?  40  THR D CA  1 
ATOM   15050 C  C   . THR D  1  40  ? 46.278  103.639 30.481  1.00 98.03  ?  40  THR D C   1 
ATOM   15051 O  O   . THR D  1  40  ? 46.926  104.544 29.952  1.00 91.59  ?  40  THR D O   1 
ATOM   15052 C  CB  . THR D  1  40  ? 46.221  101.679 28.861  1.00 80.67  ?  40  THR D CB  1 
ATOM   15053 O  OG1 . THR D  1  40  ? 46.896  100.827 29.792  1.00 71.44  ?  40  THR D OG1 1 
ATOM   15054 C  CG2 . THR D  1  40  ? 47.232  102.310 27.914  1.00 101.33 ?  40  THR D CG2 1 
ATOM   15055 N  N   . ALA D  1  41  ? 46.302  103.401 31.796  1.00 92.72  ?  41  ALA D N   1 
ATOM   15056 C  CA  . ALA D  1  41  ? 47.104  104.198 32.721  1.00 99.21  ?  41  ALA D CA  1 
ATOM   15057 C  C   . ALA D  1  41  ? 48.534  103.664 32.882  1.00 89.81  ?  41  ALA D C   1 
ATOM   15058 O  O   . ALA D  1  41  ? 49.283  104.197 33.701  1.00 93.76  ?  41  ALA D O   1 
ATOM   15059 C  CB  . ALA D  1  41  ? 46.420  104.235 34.078  1.00 108.64 ?  41  ALA D CB  1 
ATOM   15060 N  N   . TYR D  1  42  ? 48.917  102.624 32.117  1.00 90.67  ?  42  TYR D N   1 
ATOM   15061 C  CA  . TYR D  1  42  ? 50.245  102.029 32.219  1.00 90.05  ?  42  TYR D CA  1 
ATOM   15062 C  C   . TYR D  1  42  ? 51.061  102.174 30.932  1.00 86.65  ?  42  TYR D C   1 
ATOM   15063 O  O   . TYR D  1  42  ? 51.980  101.390 30.716  1.00 85.12  ?  42  TYR D O   1 
ATOM   15064 C  CB  . TYR D  1  42  ? 50.109  100.552 32.628  1.00 80.31  ?  42  TYR D CB  1 
ATOM   15065 C  CG  . TYR D  1  42  ? 49.359  100.386 33.933  1.00 88.90  ?  42  TYR D CG  1 
ATOM   15066 C  CD1 . TYR D  1  42  ? 47.979  100.239 33.949  1.00 98.30  ?  42  TYR D CD1 1 
ATOM   15067 C  CD2 . TYR D  1  42  ? 50.019  100.452 35.152  1.00 79.71  ?  42  TYR D CD2 1 
ATOM   15068 C  CE1 . TYR D  1  42  ? 47.279  100.132 35.145  1.00 93.17  ?  42  TYR D CE1 1 
ATOM   15069 C  CE2 . TYR D  1  42  ? 49.332  100.343 36.354  1.00 85.33  ?  42  TYR D CE2 1 
ATOM   15070 C  CZ  . TYR D  1  42  ? 47.959  100.181 36.348  1.00 86.27  ?  42  TYR D CZ  1 
ATOM   15071 O  OH  . TYR D  1  42  ? 47.264  100.074 37.531  1.00 80.08  ?  42  TYR D OH  1 
ATOM   15072 N  N   . SER D  1  43  ? 50.746  103.180 30.087  1.00 96.91  ?  43  SER D N   1 
ATOM   15073 C  CA  . SER D  1  43  ? 51.457  103.435 28.828  1.00 87.68  ?  43  SER D CA  1 
ATOM   15074 C  C   . SER D  1  43  ? 51.598  102.082 28.077  1.00 86.69  ?  43  SER D C   1 
ATOM   15075 O  O   . SER D  1  43  ? 50.572  101.520 27.698  1.00 93.94  ?  43  SER D O   1 
ATOM   15076 C  CB  . SER D  1  43  ? 52.788  104.133 29.110  1.00 84.37  ?  43  SER D CB  1 
ATOM   15077 O  OG  . SER D  1  43  ? 53.493  104.419 27.911  1.00 105.98 ?  43  SER D OG  1 
ATOM   15078 N  N   . LEU D  1  44  ? 52.826  101.545 27.890  1.00 87.80  ?  44  LEU D N   1 
ATOM   15079 C  CA  . LEU D  1  44  ? 53.040  100.292 27.171  1.00 81.15  ?  44  LEU D CA  1 
ATOM   15080 C  C   . LEU D  1  44  ? 53.250  99.271  28.296  1.00 93.26  ?  44  LEU D C   1 
ATOM   15081 O  O   . LEU D  1  44  ? 54.332  99.212  28.874  1.00 88.53  ?  44  LEU D O   1 
ATOM   15082 C  CB  . LEU D  1  44  ? 54.265  100.380 26.249  1.00 82.24  ?  44  LEU D CB  1 
ATOM   15083 C  CG  . LEU D  1  44  ? 54.217  101.410 25.104  1.00 68.45  ?  44  LEU D CG  1 
ATOM   15084 C  CD1 . LEU D  1  44  ? 55.375  101.198 24.157  1.00 72.01  ?  44  LEU D CD1 1 
ATOM   15085 C  CD2 . LEU D  1  44  ? 52.917  101.346 24.321  1.00 68.74  ?  44  LEU D CD2 1 
ATOM   15086 N  N   . PRO D  1  45  ? 52.217  98.486  28.680  1.00 93.07  ?  45  PRO D N   1 
ATOM   15087 C  CA  . PRO D  1  45  ? 52.325  97.579  29.834  1.00 91.92  ?  45  PRO D CA  1 
ATOM   15088 C  C   . PRO D  1  45  ? 53.599  96.729  29.910  1.00 85.96  ?  45  PRO D C   1 
ATOM   15089 O  O   . PRO D  1  45  ? 54.204  96.701  30.964  1.00 92.86  ?  45  PRO D O   1 
ATOM   15090 C  CB  . PRO D  1  45  ? 51.125  96.642  29.627  1.00 94.46  ?  45  PRO D CB  1 
ATOM   15091 C  CG  . PRO D  1  45  ? 50.090  97.523  28.975  1.00 90.40  ?  45  PRO D CG  1 
ATOM   15092 C  CD  . PRO D  1  45  ? 50.891  98.411  28.047  1.00 90.99  ?  45  PRO D CD  1 
ATOM   15093 N  N   . VAL D  1  46  ? 53.980  96.068  28.815  1.00 80.74  ?  46  VAL D N   1 
ATOM   15094 C  CA  . VAL D  1  46  ? 55.116  95.146  28.889  1.00 92.81  ?  46  VAL D CA  1 
ATOM   15095 C  C   . VAL D  1  46  ? 56.381  95.923  29.246  1.00 90.07  ?  46  VAL D C   1 
ATOM   15096 O  O   . VAL D  1  46  ? 57.109  95.530  30.158  1.00 80.29  ?  46  VAL D O   1 
ATOM   15097 C  CB  . VAL D  1  46  ? 55.306  94.317  27.598  1.00 86.22  ?  46  VAL D CB  1 
ATOM   15098 C  CG1 . VAL D  1  46  ? 56.407  93.280  27.780  1.00 59.00  ?  46  VAL D CG1 1 
ATOM   15099 C  CG2 . VAL D  1  46  ? 54.001  93.643  27.183  1.00 80.62  ?  46  VAL D CG2 1 
ATOM   15100 N  N   . ILE D  1  47  ? 56.635  97.033  28.546  1.00 81.72  ?  47  ILE D N   1 
ATOM   15101 C  CA  . ILE D  1  47  ? 57.819  97.850  28.812  1.00 76.78  ?  47  ILE D CA  1 
ATOM   15102 C  C   . ILE D  1  47  ? 57.727  98.472  30.199  1.00 75.51  ?  47  ILE D C   1 
ATOM   15103 O  O   . ILE D  1  47  ? 58.732  98.538  30.904  1.00 86.39  ?  47  ILE D O   1 
ATOM   15104 C  CB  . ILE D  1  47  ? 58.030  98.906  27.693  1.00 71.48  ?  47  ILE D CB  1 
ATOM   15105 C  CG1 . ILE D  1  47  ? 58.459  98.205  26.379  1.00 71.77  ?  47  ILE D CG1 1 
ATOM   15106 C  CG2 . ILE D  1  47  ? 59.076  99.954  28.110  1.00 77.27  ?  47  ILE D CG2 1 
ATOM   15107 C  CD1 . ILE D  1  47  ? 58.120  98.933  25.128  1.00 85.43  ?  47  ILE D CD1 1 
ATOM   15108 N  N   . PHE D  1  48  ? 56.532  98.913  30.603  1.00 80.49  ?  48  PHE D N   1 
ATOM   15109 C  CA  . PHE D  1  48  ? 56.351  99.500  31.922  1.00 84.60  ?  48  PHE D CA  1 
ATOM   15110 C  C   . PHE D  1  48  ? 56.569  98.451  33.021  1.00 83.24  ?  48  PHE D C   1 
ATOM   15111 O  O   . PHE D  1  48  ? 57.038  98.798  34.102  1.00 93.04  ?  48  PHE D O   1 
ATOM   15112 C  CB  . PHE D  1  48  ? 54.959  100.136 32.048  1.00 82.34  ?  48  PHE D CB  1 
ATOM   15113 C  CG  . PHE D  1  48  ? 54.722  100.765 33.399  1.00 84.54  ?  48  PHE D CG  1 
ATOM   15114 C  CD1 . PHE D  1  48  ? 55.459  101.863 33.808  1.00 80.72  ?  48  PHE D CD1 1 
ATOM   15115 C  CD2 . PHE D  1  48  ? 53.792  100.233 34.276  1.00 81.97  ?  48  PHE D CD2 1 
ATOM   15116 C  CE1 . PHE D  1  48  ? 55.259  102.425 35.062  1.00 76.46  ?  48  PHE D CE1 1 
ATOM   15117 C  CE2 . PHE D  1  48  ? 53.593  100.799 35.527  1.00 79.16  ?  48  PHE D CE2 1 
ATOM   15118 C  CZ  . PHE D  1  48  ? 54.326  101.892 35.912  1.00 84.26  ?  48  PHE D CZ  1 
ATOM   15119 N  N   . ALA D  1  49  ? 56.246  97.179  32.757  1.00 82.64  ?  49  ALA D N   1 
ATOM   15120 C  CA  . ALA D  1  49  ? 56.441  96.126  33.747  1.00 77.86  ?  49  ALA D CA  1 
ATOM   15121 C  C   . ALA D  1  49  ? 57.926  95.778  33.876  1.00 81.16  ?  49  ALA D C   1 
ATOM   15122 O  O   . ALA D  1  49  ? 58.428  95.647  34.987  1.00 87.65  ?  49  ALA D O   1 
ATOM   15123 C  CB  . ALA D  1  49  ? 55.644  94.888  33.362  1.00 72.15  ?  49  ALA D CB  1 
ATOM   15124 N  N   . ALA D  1  50  ? 58.629  95.643  32.745  1.00 82.23  ?  50  ALA D N   1 
ATOM   15125 C  CA  . ALA D  1  50  ? 60.043  95.286  32.741  1.00 76.75  ?  50  ALA D CA  1 
ATOM   15126 C  C   . ALA D  1  50  ? 60.981  96.412  33.184  1.00 85.89  ?  50  ALA D C   1 
ATOM   15127 O  O   . ALA D  1  50  ? 61.912  96.160  33.947  1.00 103.45 ?  50  ALA D O   1 
ATOM   15128 C  CB  . ALA D  1  50  ? 60.442  94.802  31.354  1.00 62.57  ?  50  ALA D CB  1 
ATOM   15129 N  N   . THR D  1  51  ? 60.754  97.638  32.706  1.00 81.10  ?  51  THR D N   1 
ATOM   15130 C  CA  . THR D  1  51  ? 61.618  98.776  33.021  1.00 85.39  ?  51  THR D CA  1 
ATOM   15131 C  C   . THR D  1  51  ? 61.047  99.738  34.050  1.00 84.50  ?  51  THR D C   1 
ATOM   15132 O  O   . THR D  1  51  ? 61.804  100.432 34.727  1.00 89.61  ?  51  THR D O   1 
ATOM   15133 C  CB  . THR D  1  51  ? 61.903  99.565  31.734  1.00 100.48 ?  51  THR D CB  1 
ATOM   15134 O  OG1 . THR D  1  51  ? 60.702  100.207 31.286  1.00 85.92  ?  51  THR D OG1 1 
ATOM   15135 C  CG2 . THR D  1  51  ? 62.476  98.688  30.628  1.00 79.65  ?  51  THR D CG2 1 
ATOM   15136 N  N   . GLY D  1  52  ? 59.729  99.809  34.132  1.00 85.09  ?  52  GLY D N   1 
ATOM   15137 C  CA  . GLY D  1  52  ? 59.058  100.743 35.025  1.00 88.70  ?  52  GLY D CA  1 
ATOM   15138 C  C   . GLY D  1  52  ? 59.052  102.145 34.442  1.00 91.12  ?  52  GLY D C   1 
ATOM   15139 O  O   . GLY D  1  52  ? 58.854  103.120 35.168  1.00 89.81  ?  52  GLY D O   1 
ATOM   15140 N  N   . LYS D  1  53  ? 59.264  102.253 33.118  1.00 92.88  ?  53  LYS D N   1 
ATOM   15141 C  CA  . LYS D  1  53  ? 59.316  103.520 32.409  1.00 102.30 ?  53  LYS D CA  1 
ATOM   15142 C  C   . LYS D  1  53  ? 58.154  103.608 31.428  1.00 97.37  ?  53  LYS D C   1 
ATOM   15143 O  O   . LYS D  1  53  ? 57.769  102.602 30.832  1.00 86.79  ?  53  LYS D O   1 
ATOM   15144 C  CB  . LYS D  1  53  ? 60.654  103.643 31.651  1.00 105.86 ?  53  LYS D CB  1 
ATOM   15145 C  CG  . LYS D  1  53  ? 61.899  103.331 32.492  1.00 110.04 ?  53  LYS D CG  1 
ATOM   15146 C  CD  . LYS D  1  53  ? 62.253  104.459 33.470  1.00 132.11 ?  53  LYS D CD  1 
ATOM   15147 C  CE  . LYS D  1  53  ? 63.271  104.042 34.509  1.00 125.57 ?  53  LYS D CE  1 
ATOM   15148 N  NZ  . LYS D  1  53  ? 63.204  104.905 35.720  1.00 106.73 ?  53  LYS D NZ  1 
ATOM   15149 N  N   . LYS D  1  54  ? 57.599  104.808 31.257  1.00 99.14  ?  54  LYS D N   1 
ATOM   15150 C  CA  . LYS D  1  54  ? 56.485  105.010 30.343  1.00 94.75  ?  54  LYS D CA  1 
ATOM   15151 C  C   . LYS D  1  54  ? 56.982  105.599 29.030  1.00 98.60  ?  54  LYS D C   1 
ATOM   15152 O  O   . LYS D  1  54  ? 57.786  106.530 29.039  1.00 95.43  ?  54  LYS D O   1 
ATOM   15153 C  CB  . LYS D  1  54  ? 55.436  105.924 30.982  1.00 78.03  ?  54  LYS D CB  1 
ATOM   15154 C  CG  . LYS D  1  54  ? 54.766  105.286 32.190  1.00 96.08  ?  54  LYS D CG  1 
ATOM   15155 C  CD  . LYS D  1  54  ? 53.606  106.115 32.734  1.00 85.46  ?  54  LYS D CD  1 
ATOM   15156 C  CE  . LYS D  1  54  ? 52.411  105.266 33.083  1.00 93.37  ?  54  LYS D CE  1 
ATOM   15157 N  NZ  . LYS D  1  54  ? 51.377  106.038 33.818  1.00 113.41 ?  54  LYS D NZ  1 
ATOM   15158 N  N   . ILE D  1  55  ? 56.513  105.043 27.901  1.00 101.58 ?  55  ILE D N   1 
ATOM   15159 C  CA  . ILE D  1  55  ? 56.880  105.502 26.562  1.00 88.41  ?  55  ILE D CA  1 
ATOM   15160 C  C   . ILE D  1  55  ? 55.764  106.438 26.076  1.00 96.40  ?  55  ILE D C   1 
ATOM   15161 O  O   . ILE D  1  55  ? 54.613  106.013 25.984  1.00 101.90 ?  55  ILE D O   1 
ATOM   15162 C  CB  . ILE D  1  55  ? 57.073  104.287 25.622  1.00 72.66  ?  55  ILE D CB  1 
ATOM   15163 C  CG1 . ILE D  1  55  ? 58.157  103.314 26.149  1.00 76.07  ?  55  ILE D CG1 1 
ATOM   15164 C  CG2 . ILE D  1  55  ? 57.366  104.732 24.202  1.00 78.40  ?  55  ILE D CG2 1 
ATOM   15165 C  CD1 . ILE D  1  55  ? 59.577  103.901 26.385  1.00 82.18  ?  55  ILE D CD1 1 
ATOM   15166 N  N   . THR D  1  56  ? 56.098  107.713 25.790  1.00 83.55  ?  56  THR D N   1 
ATOM   15167 C  CA  . THR D  1  56  ? 55.116  108.715 25.371  1.00 82.66  ?  56  THR D CA  1 
ATOM   15168 C  C   . THR D  1  56  ? 55.270  109.236 23.933  1.00 92.37  ?  56  THR D C   1 
ATOM   15169 O  O   . THR D  1  56  ? 54.294  109.747 23.386  1.00 98.43  ?  56  THR D O   1 
ATOM   15170 C  CB  . THR D  1  56  ? 55.150  109.891 26.346  1.00 101.86 ?  56  THR D CB  1 
ATOM   15171 O  OG1 . THR D  1  56  ? 56.428  110.528 26.266  1.00 105.53 ?  56  THR D OG1 1 
ATOM   15172 C  CG2 . THR D  1  56  ? 54.859  109.466 27.779  1.00 98.36  ?  56  THR D CG2 1 
ATOM   15173 N  N   . ASN D  1  57  ? 56.463  109.137 23.327  1.00 86.09  ?  57  ASN D N   1 
ATOM   15174 C  CA  . ASN D  1  57  ? 56.664  109.620 21.956  1.00 85.58  ?  57  ASN D CA  1 
ATOM   15175 C  C   . ASN D  1  57  ? 57.413  108.604 21.088  1.00 88.20  ?  57  ASN D C   1 
ATOM   15176 O  O   . ASN D  1  57  ? 57.946  107.626 21.607  1.00 99.19  ?  57  ASN D O   1 
ATOM   15177 C  CB  . ASN D  1  57  ? 57.382  110.981 21.953  1.00 101.63 ?  57  ASN D CB  1 
ATOM   15178 C  CG  . ASN D  1  57  ? 58.660  111.017 22.753  1.00 96.63  ?  57  ASN D CG  1 
ATOM   15179 O  OD1 . ASN D  1  57  ? 58.635  110.986 23.982  1.00 115.95 ?  57  ASN D OD1 1 
ATOM   15180 N  ND2 . ASN D  1  57  ? 59.807  111.108 22.088  1.00 85.98  ?  57  ASN D ND2 1 
ATOM   15181 N  N   . VAL D  1  58  ? 57.443  108.830 19.764  1.00 89.78  ?  58  VAL D N   1 
ATOM   15182 C  CA  . VAL D  1  58  ? 58.120  107.934 18.823  1.00 99.59  ?  58  VAL D CA  1 
ATOM   15183 C  C   . VAL D  1  58  ? 59.617  107.800 19.172  1.00 102.97 ?  58  VAL D C   1 
ATOM   15184 O  O   . VAL D  1  58  ? 60.184  106.717 19.035  1.00 102.93 ?  58  VAL D O   1 
ATOM   15185 C  CB  . VAL D  1  58  ? 57.890  108.388 17.352  1.00 87.04  ?  58  VAL D CB  1 
ATOM   15186 C  CG1 . VAL D  1  58  ? 58.845  107.685 16.393  1.00 81.75  ?  58  VAL D CG1 1 
ATOM   15187 C  CG2 . VAL D  1  58  ? 56.442  108.155 16.925  1.00 82.36  ?  58  VAL D CG2 1 
ATOM   15188 N  N   . GLY D  1  59  ? 60.234  108.884 19.629  1.00 90.94  ?  59  GLY D N   1 
ATOM   15189 C  CA  . GLY D  1  59  ? 61.637  108.874 20.022  1.00 94.87  ?  59  GLY D CA  1 
ATOM   15190 C  C   . GLY D  1  59  ? 61.885  107.934 21.186  1.00 97.14  ?  59  GLY D C   1 
ATOM   15191 O  O   . GLY D  1  59  ? 62.880  107.202 21.196  1.00 89.05  ?  59  GLY D O   1 
ATOM   15192 N  N   . GLU D  1  60  ? 60.966  107.932 22.172  1.00 90.23  ?  60  GLU D N   1 
ATOM   15193 C  CA  . GLU D  1  60  ? 61.061  107.045 23.337  1.00 90.62  ?  60  GLU D CA  1 
ATOM   15194 C  C   . GLU D  1  60  ? 60.802  105.589 22.911  1.00 91.34  ?  60  GLU D C   1 
ATOM   15195 O  O   . GLU D  1  60  ? 61.424  104.674 23.452  1.00 81.74  ?  60  GLU D O   1 
ATOM   15196 C  CB  . GLU D  1  60  ? 60.077  107.473 24.439  1.00 83.86  ?  60  GLU D CB  1 
ATOM   15197 C  CG  . GLU D  1  60  ? 60.509  108.725 25.185  1.00 81.11  ?  60  GLU D CG  1 
ATOM   15198 C  CD  . GLU D  1  60  ? 59.566  109.173 26.283  1.00 98.44  ?  60  GLU D CD  1 
ATOM   15199 O  OE1 . GLU D  1  60  ? 58.674  108.381 26.663  1.00 110.36 ?  60  GLU D OE1 1 
ATOM   15200 O  OE2 . GLU D  1  60  ? 59.717  110.319 26.766  1.00 90.90  ?  60  GLU D OE2 1 
ATOM   15201 N  N   . LEU D  1  61  ? 59.894  105.382 21.934  1.00 91.86  ?  61  LEU D N   1 
ATOM   15202 C  CA  . LEU D  1  61  ? 59.582  104.060 21.382  1.00 82.83  ?  61  LEU D CA  1 
ATOM   15203 C  C   . LEU D  1  61  ? 60.823  103.508 20.666  1.00 88.81  ?  61  LEU D C   1 
ATOM   15204 O  O   . LEU D  1  61  ? 61.053  102.300 20.675  1.00 93.07  ?  61  LEU D O   1 
ATOM   15205 C  CB  . LEU D  1  61  ? 58.401  104.165 20.397  1.00 80.81  ?  61  LEU D CB  1 
ATOM   15206 C  CG  . LEU D  1  61  ? 57.847  102.848 19.840  1.00 81.56  ?  61  LEU D CG  1 
ATOM   15207 C  CD1 . LEU D  1  61  ? 56.984  102.137 20.864  1.00 88.24  ?  61  LEU D CD1 1 
ATOM   15208 C  CD2 . LEU D  1  61  ? 57.032  103.084 18.578  1.00 75.44  ?  61  LEU D CD2 1 
ATOM   15209 N  N   . GLU D  1  62  ? 61.624  104.393 20.054  1.00 89.57  ?  62  GLU D N   1 
ATOM   15210 C  CA  . GLU D  1  62  ? 62.853  104.004 19.377  1.00 87.57  ?  62  GLU D CA  1 
ATOM   15211 C  C   . GLU D  1  62  ? 63.857  103.488 20.415  1.00 90.00  ?  62  GLU D C   1 
ATOM   15212 O  O   . GLU D  1  62  ? 64.535  102.490 20.174  1.00 92.97  ?  62  GLU D O   1 
ATOM   15213 C  CB  . GLU D  1  62  ? 63.436  105.203 18.606  1.00 83.53  ?  62  GLU D CB  1 
ATOM   15214 C  CG  . GLU D  1  62  ? 64.431  104.814 17.528  1.00 90.21  ?  62  GLU D CG  1 
ATOM   15215 C  CD  . GLU D  1  62  ? 65.073  105.985 16.811  1.00 98.81  ?  62  GLU D CD  1 
ATOM   15216 O  OE1 . GLU D  1  62  ? 65.412  106.983 17.485  1.00 91.27  ?  62  GLU D OE1 1 
ATOM   15217 O  OE2 . GLU D  1  62  ? 65.242  105.902 15.572  1.00 97.91  ?  62  GLU D OE2 1 
ATOM   15218 N  N   . GLY D  1  63  ? 63.934  104.166 21.558  1.00 85.45  ?  63  GLY D N   1 
ATOM   15219 C  CA  . GLY D  1  63  ? 64.822  103.781 22.646  1.00 80.86  ?  63  GLY D CA  1 
ATOM   15220 C  C   . GLY D  1  63  ? 64.451  102.443 23.252  1.00 85.73  ?  63  GLY D C   1 
ATOM   15221 O  O   . GLY D  1  63  ? 65.329  101.696 23.689  1.00 95.00  ?  63  GLY D O   1 
ATOM   15222 N  N   . ALA D  1  64  ? 63.144  102.123 23.283  1.00 79.74  ?  64  ALA D N   1 
ATOM   15223 C  CA  . ALA D  1  64  ? 62.664  100.847 23.815  1.00 77.75  ?  64  ALA D CA  1 
ATOM   15224 C  C   . ALA D  1  64  ? 63.216  99.650  23.017  1.00 91.14  ?  64  ALA D C   1 
ATOM   15225 O  O   . ALA D  1  64  ? 63.207  98.531  23.526  1.00 98.49  ?  64  ALA D O   1 
ATOM   15226 C  CB  . ALA D  1  64  ? 61.146  100.817 23.809  1.00 79.69  ?  64  ALA D CB  1 
ATOM   15227 N  N   . LEU D  1  65  ? 63.723  99.904  21.810  1.00 85.60  ?  65  LEU D N   1 
ATOM   15228 C  CA  . LEU D  1  65  ? 64.299  98.812  20.979  1.00 90.69  ?  65  LEU D CA  1 
ATOM   15229 C  C   . LEU D  1  65  ? 65.510  98.207  21.698  1.00 95.66  ?  65  LEU D C   1 
ATOM   15230 O  O   . LEU D  1  65  ? 65.752  96.998  21.522  1.00 94.94  ?  65  LEU D O   1 
ATOM   15231 C  CB  . LEU D  1  65  ? 64.688  99.386  19.615  1.00 89.48  ?  65  LEU D CB  1 
ATOM   15232 C  CG  . LEU D  1  65  ? 63.608  99.286  18.540  1.00 75.99  ?  65  LEU D CG  1 
ATOM   15233 C  CD1 . LEU D  1  65  ? 64.201  99.494  17.155  1.00 97.70  ?  65  LEU D CD1 1 
ATOM   15234 C  CD2 . LEU D  1  65  ? 62.900  97.944  18.621  1.00 73.35  ?  65  LEU D CD2 1 
ATOM   15235 N  N   . ASP D  1  66  ? 66.235  99.014  22.478  1.00 96.11  ?  66  ASP D N   1 
ATOM   15236 C  CA  . ASP D  1  66  ? 67.418  98.532  23.195  1.00 98.72  ?  66  ASP D CA  1 
ATOM   15237 C  C   . ASP D  1  66  ? 67.029  97.509  24.280  1.00 93.33  ?  66  ASP D C   1 
ATOM   15238 O  O   . ASP D  1  66  ? 67.852  96.668  24.643  1.00 99.09  ?  66  ASP D O   1 
ATOM   15239 C  CB  . ASP D  1  66  ? 68.200  99.700  23.810  1.00 93.81  ?  66  ASP D CB  1 
ATOM   15240 C  CG  . ASP D  1  66  ? 69.009  100.472 22.789  1.00 103.46 ?  66  ASP D CG  1 
ATOM   15241 O  OD1 . ASP D  1  66  ? 69.938  99.878  22.196  1.00 98.03  ?  66  ASP D OD1 1 
ATOM   15242 O  OD2 . ASP D  1  66  ? 68.714  101.670 22.582  1.00 121.51 ?  66  ASP D OD2 1 
ATOM   15243 N  N   . ILE D  1  67  ? 65.780  97.562  24.778  1.00 81.44  ?  67  ILE D N   1 
ATOM   15244 C  CA  . ILE D  1  67  ? 65.286  96.609  25.769  1.00 73.60  ?  67  ILE D CA  1 
ATOM   15245 C  C   . ILE D  1  67  ? 65.186  95.230  25.087  1.00 82.97  ?  67  ILE D C   1 
ATOM   15246 O  O   . ILE D  1  67  ? 65.567  94.223  25.680  1.00 85.33  ?  67  ILE D O   1 
ATOM   15247 C  CB  . ILE D  1  67  ? 63.910  97.060  26.334  1.00 79.29  ?  67  ILE D CB  1 
ATOM   15248 C  CG1 . ILE D  1  67  ? 63.966  98.477  26.963  1.00 91.21  ?  67  ILE D CG1 1 
ATOM   15249 C  CG2 . ILE D  1  67  ? 63.364  96.039  27.331  1.00 85.99  ?  67  ILE D CG2 1 
ATOM   15250 C  CD1 . ILE D  1  67  ? 65.061  98.715  28.026  1.00 104.52 ?  67  ILE D CD1 1 
ATOM   15251 N  N   . VAL D  1  68  ? 64.696  95.195  23.831  1.00 87.97  ?  68  VAL D N   1 
ATOM   15252 C  CA  . VAL D  1  68  ? 64.570  93.956  23.054  1.00 83.00  ?  68  VAL D CA  1 
ATOM   15253 C  C   . VAL D  1  68  ? 65.979  93.382  22.835  1.00 86.31  ?  68  VAL D C   1 
ATOM   15254 O  O   . VAL D  1  68  ? 66.189  92.182  23.016  1.00 81.53  ?  68  VAL D O   1 
ATOM   15255 C  CB  . VAL D  1  68  ? 63.848  94.193  21.693  1.00 77.02  ?  68  VAL D CB  1 
ATOM   15256 C  CG1 . VAL D  1  68  ? 63.781  92.911  20.867  1.00 66.93  ?  68  VAL D CG1 1 
ATOM   15257 C  CG2 . VAL D  1  68  ? 62.445  94.750  21.893  1.00 70.66  ?  68  VAL D CG2 1 
ATOM   15258 N  N   . ARG D  1  69  ? 66.943  94.244  22.465  1.00 77.55  ?  69  ARG D N   1 
ATOM   15259 C  CA  . ARG D  1  69  ? 68.329  93.837  22.226  1.00 80.17  ?  69  ARG D CA  1 
ATOM   15260 C  C   . ARG D  1  69  ? 68.979  93.264  23.484  1.00 83.02  ?  69  ARG D C   1 
ATOM   15261 O  O   . ARG D  1  69  ? 69.656  92.238  23.415  1.00 90.69  ?  69  ARG D O   1 
ATOM   15262 C  CB  . ARG D  1  69  ? 69.167  95.032  21.746  1.00 84.74  ?  69  ARG D CB  1 
ATOM   15263 C  CG  . ARG D  1  69  ? 68.801  95.559  20.366  1.00 87.39  ?  69  ARG D CG  1 
ATOM   15264 C  CD  . ARG D  1  69  ? 69.678  96.742  19.974  1.00 93.22  ?  69  ARG D CD  1 
ATOM   15265 N  NE  . ARG D  1  69  ? 68.891  97.929  19.642  1.00 87.30  ?  69  ARG D NE  1 
ATOM   15266 C  CZ  . ARG D  1  69  ? 68.321  98.158  18.462  1.00 91.03  ?  69  ARG D CZ  1 
ATOM   15267 N  NH1 . ARG D  1  69  ? 68.438  97.275  17.475  1.00 100.46 ?  69  ARG D NH1 1 
ATOM   15268 N  NH2 . ARG D  1  69  ? 67.627  99.270  18.258  1.00 90.32  ?  69  ARG D NH2 1 
ATOM   15269 N  N   . SER D  1  70  ? 68.792  93.934  24.627  1.00 69.12  ?  70  SER D N   1 
ATOM   15270 C  CA  . SER D  1  70  ? 69.374  93.501  25.894  1.00 79.44  ?  70  SER D CA  1 
ATOM   15271 C  C   . SER D  1  70  ? 68.835  92.143  26.362  1.00 82.09  ?  70  SER D C   1 
ATOM   15272 O  O   . SER D  1  70  ? 69.589  91.356  26.934  1.00 85.81  ?  70  SER D O   1 
ATOM   15273 C  CB  . SER D  1  70  ? 69.127  94.552  26.971  1.00 74.29  ?  70  SER D CB  1 
ATOM   15274 O  OG  . SER D  1  70  ? 67.768  94.567  27.379  1.00 92.48  ?  70  SER D OG  1 
ATOM   15275 N  N   . LEU D  1  71  ? 67.545  91.868  26.129  1.00 73.33  ?  71  LEU D N   1 
ATOM   15276 C  CA  . LEU D  1  71  ? 66.944  90.602  26.551  1.00 77.81  ?  71  LEU D CA  1 
ATOM   15277 C  C   . LEU D  1  71  ? 67.387  89.412  25.684  1.00 86.88  ?  71  LEU D C   1 
ATOM   15278 O  O   . LEU D  1  71  ? 67.230  88.272  26.121  1.00 86.22  ?  71  LEU D O   1 
ATOM   15279 C  CB  . LEU D  1  71  ? 65.405  90.700  26.573  1.00 76.64  ?  71  LEU D CB  1 
ATOM   15280 C  CG  . LEU D  1  71  ? 64.720  91.144  27.878  1.00 75.77  ?  71  LEU D CG  1 
ATOM   15281 C  CD1 . LEU D  1  71  ? 65.341  92.408  28.455  1.00 82.84  ?  71  LEU D CD1 1 
ATOM   15282 C  CD2 . LEU D  1  71  ? 63.237  91.355  27.652  1.00 68.89  ?  71  LEU D CD2 1 
ATOM   15283 N  N   . ILE D  1  72  ? 67.942  89.650  24.477  1.00 84.05  ?  72  ILE D N   1 
ATOM   15284 C  CA  . ILE D  1  72  ? 68.404  88.547  23.627  1.00 77.01  ?  72  ILE D CA  1 
ATOM   15285 C  C   . ILE D  1  72  ? 69.885  88.269  23.885  1.00 73.91  ?  72  ILE D C   1 
ATOM   15286 O  O   . ILE D  1  72  ? 70.749  89.013  23.422  1.00 75.27  ?  72  ILE D O   1 
ATOM   15287 C  CB  . ILE D  1  72  ? 68.138  88.795  22.119  1.00 74.65  ?  72  ILE D CB  1 
ATOM   15288 C  CG1 . ILE D  1  72  ? 66.628  88.887  21.845  1.00 82.39  ?  72  ILE D CG1 1 
ATOM   15289 C  CG2 . ILE D  1  72  ? 68.758  87.670  21.275  1.00 65.60  ?  72  ILE D CG2 1 
ATOM   15290 C  CD1 . ILE D  1  72  ? 66.266  89.484  20.512  1.00 75.86  ?  72  ILE D CD1 1 
ATOM   15291 N  N   . VAL D  1  73  ? 70.166  87.192  24.635  1.00 71.49  ?  73  VAL D N   1 
ATOM   15292 C  CA  . VAL D  1  73  ? 71.516  86.736  24.960  1.00 69.26  ?  73  VAL D CA  1 
ATOM   15293 C  C   . VAL D  1  73  ? 71.584  85.322  24.390  1.00 74.86  ?  73  VAL D C   1 
ATOM   15294 O  O   . VAL D  1  73  ? 70.960  84.417  24.939  1.00 80.84  ?  73  VAL D O   1 
ATOM   15295 C  CB  . VAL D  1  73  ? 71.768  86.744  26.487  1.00 70.71  ?  73  VAL D CB  1 
ATOM   15296 C  CG1 . VAL D  1  73  ? 73.177  86.257  26.809  1.00 73.22  ?  73  VAL D CG1 1 
ATOM   15297 C  CG2 . VAL D  1  73  ? 71.532  88.132  27.070  1.00 71.25  ?  73  VAL D CG2 1 
ATOM   15298 N  N   . GLU D  1  74  ? 72.300  85.131  23.278  1.00 63.41  ?  74  GLU D N   1 
ATOM   15299 C  CA  . GLU D  1  74  ? 72.371  83.824  22.630  1.00 63.24  ?  74  GLU D CA  1 
ATOM   15300 C  C   . GLU D  1  74  ? 73.293  82.817  23.330  1.00 78.82  ?  74  GLU D C   1 
ATOM   15301 O  O   . GLU D  1  74  ? 74.339  82.450  22.799  1.00 82.85  ?  74  GLU D O   1 
ATOM   15302 C  CB  . GLU D  1  74  ? 72.754  83.990  21.154  1.00 79.22  ?  74  GLU D CB  1 
ATOM   15303 C  CG  . GLU D  1  74  ? 71.713  84.753  20.353  1.00 72.18  ?  74  GLU D CG  1 
ATOM   15304 C  CD  . GLU D  1  74  ? 71.984  84.783  18.864  1.00 93.22  ?  74  GLU D CD  1 
ATOM   15305 O  OE1 . GLU D  1  74  ? 71.985  83.699  18.237  1.00 105.28 ?  74  GLU D OE1 1 
ATOM   15306 O  OE2 . GLU D  1  74  ? 72.195  85.893  18.322  1.00 93.04  ?  74  GLU D OE2 1 
ATOM   15307 N  N   . GLU D  1  75  ? 72.879  82.352  24.516  1.00 79.24  ?  75  GLU D N   1 
ATOM   15308 C  CA  . GLU D  1  75  ? 73.606  81.363  25.311  1.00 75.82  ?  75  GLU D CA  1 
ATOM   15309 C  C   . GLU D  1  75  ? 72.610  80.271  25.676  1.00 69.75  ?  75  GLU D C   1 
ATOM   15310 O  O   . GLU D  1  75  ? 71.507  80.577  26.121  1.00 74.20  ?  75  GLU D O   1 
ATOM   15311 C  CB  . GLU D  1  75  ? 74.194  81.999  26.573  1.00 74.19  ?  75  GLU D CB  1 
ATOM   15312 C  CG  . GLU D  1  75  ? 75.348  82.936  26.281  1.00 73.83  ?  75  GLU D CG  1 
ATOM   15313 C  CD  . GLU D  1  75  ? 75.982  83.541  27.515  1.00 95.51  ?  75  GLU D CD  1 
ATOM   15314 O  OE1 . GLU D  1  75  ? 75.882  82.925  28.601  1.00 95.97  ?  75  GLU D OE1 1 
ATOM   15315 O  OE2 . GLU D  1  75  ? 76.580  84.635  27.396  1.00 103.07 ?  75  GLU D OE2 1 
ATOM   15316 N  N   . GLU D  1  76  ? 72.979  79.008  25.481  1.00 75.23  ?  76  GLU D N   1 
ATOM   15317 C  CA  . GLU D  1  76  ? 72.064  77.904  25.749  1.00 79.36  ?  76  GLU D CA  1 
ATOM   15318 C  C   . GLU D  1  76  ? 71.921  77.537  27.237  1.00 84.15  ?  76  GLU D C   1 
ATOM   15319 O  O   . GLU D  1  76  ? 72.543  76.589  27.714  1.00 79.36  ?  76  GLU D O   1 
ATOM   15320 C  CB  . GLU D  1  76  ? 72.445  76.685  24.903  1.00 91.03  ?  76  GLU D CB  1 
ATOM   15321 C  CG  . GLU D  1  76  ? 72.488  76.997  23.414  1.00 89.02  ?  76  GLU D CG  1 
ATOM   15322 C  CD  . GLU D  1  76  ? 72.160  75.839  22.495  1.00 94.21  ?  76  GLU D CD  1 
ATOM   15323 O  OE1 . GLU D  1  76  ? 72.125  74.682  22.975  1.00 103.55 ?  76  GLU D OE1 1 
ATOM   15324 O  OE2 . GLU D  1  76  ? 71.938  76.090  21.289  1.00 90.76  ?  76  GLU D OE2 1 
ATOM   15325 N  N   . MET D  1  77  ? 71.076  78.305  27.953  1.00 73.97  ?  77  MET D N   1 
ATOM   15326 C  CA  . MET D  1  77  ? 70.726  78.118  29.371  1.00 71.80  ?  77  MET D CA  1 
ATOM   15327 C  C   . MET D  1  77  ? 69.257  78.559  29.509  1.00 72.02  ?  77  MET D C   1 
ATOM   15328 O  O   . MET D  1  77  ? 68.875  79.548  28.887  1.00 69.47  ?  77  MET D O   1 
ATOM   15329 C  CB  . MET D  1  77  ? 71.634  78.957  30.288  1.00 71.22  ?  77  MET D CB  1 
ATOM   15330 C  CG  . MET D  1  77  ? 73.026  78.380  30.468  1.00 75.67  ?  77  MET D CG  1 
ATOM   15331 S  SD  . MET D  1  77  ? 73.067  76.843  31.427  1.00 91.67  ?  77  MET D SD  1 
ATOM   15332 C  CE  . MET D  1  77  ? 73.603  77.461  33.014  1.00 86.63  ?  77  MET D CE  1 
ATOM   15333 N  N   . LEU D  1  78  ? 68.426  77.840  30.284  1.00 77.38  ?  78  LEU D N   1 
ATOM   15334 C  CA  . LEU D  1  78  ? 66.998  78.180  30.405  1.00 72.77  ?  78  LEU D CA  1 
ATOM   15335 C  C   . LEU D  1  78  ? 66.701  79.673  30.636  1.00 71.29  ?  78  LEU D C   1 
ATOM   15336 O  O   . LEU D  1  78  ? 65.835  80.226  29.961  1.00 82.63  ?  78  LEU D O   1 
ATOM   15337 C  CB  . LEU D  1  78  ? 66.308  77.327  31.489  1.00 80.56  ?  78  LEU D CB  1 
ATOM   15338 C  CG  . LEU D  1  78  ? 64.812  77.613  31.739  1.00 58.42  ?  78  LEU D CG  1 
ATOM   15339 C  CD1 . LEU D  1  78  ? 63.976  77.376  30.486  1.00 57.22  ?  78  LEU D CD1 1 
ATOM   15340 C  CD2 . LEU D  1  78  ? 64.281  76.768  32.872  1.00 58.96  ?  78  LEU D CD2 1 
ATOM   15341 N  N   . ASP D  1  79  ? 67.396  80.319  31.580  1.00 69.95  ?  79  ASP D N   1 
ATOM   15342 C  CA  . ASP D  1  79  ? 67.156  81.736  31.870  1.00 77.30  ?  79  ASP D CA  1 
ATOM   15343 C  C   . ASP D  1  79  ? 67.327  82.642  30.644  1.00 71.36  ?  79  ASP D C   1 
ATOM   15344 O  O   . ASP D  1  79  ? 66.678  83.684  30.560  1.00 77.86  ?  79  ASP D O   1 
ATOM   15345 C  CB  . ASP D  1  79  ? 68.061  82.220  33.021  1.00 72.23  ?  79  ASP D CB  1 
ATOM   15346 C  CG  . ASP D  1  79  ? 69.531  82.335  32.667  1.00 82.93  ?  79  ASP D CG  1 
ATOM   15347 O  OD1 . ASP D  1  79  ? 70.127  81.312  32.270  1.00 99.15  ?  79  ASP D OD1 1 
ATOM   15348 O  OD2 . ASP D  1  79  ? 70.086  83.446  32.797  1.00 80.20  ?  79  ASP D OD2 1 
ATOM   15349 N  N   . LYS D  1  80  ? 68.172  82.238  29.690  1.00 73.30  ?  80  LYS D N   1 
ATOM   15350 C  CA  . LYS D  1  80  ? 68.433  83.025  28.483  1.00 73.62  ?  80  LYS D CA  1 
ATOM   15351 C  C   . LYS D  1  80  ? 67.289  82.846  27.485  1.00 68.71  ?  80  LYS D C   1 
ATOM   15352 O  O   . LYS D  1  80  ? 66.893  83.809  26.833  1.00 78.85  ?  80  LYS D O   1 
ATOM   15353 C  CB  . LYS D  1  80  ? 69.768  82.617  27.829  1.00 69.58  ?  80  LYS D CB  1 
ATOM   15354 C  CG  . LYS D  1  80  ? 70.943  82.393  28.791  1.00 70.74  ?  80  LYS D CG  1 
ATOM   15355 C  CD  . LYS D  1  80  ? 71.676  83.670  29.146  1.00 80.58  ?  80  LYS D CD  1 
ATOM   15356 C  CE  . LYS D  1  80  ? 72.814  83.420  30.113  1.00 84.85  ?  80  LYS D CE  1 
ATOM   15357 N  NZ  . LYS D  1  80  ? 72.706  84.267  31.327  1.00 95.36  ?  80  LYS D NZ  1 
ATOM   15358 N  N   . LEU D  1  81  ? 66.770  81.618  27.347  1.00 62.60  ?  81  LEU D N   1 
ATOM   15359 C  CA  . LEU D  1  81  ? 65.614  81.377  26.438  1.00 70.51  ?  81  LEU D CA  1 
ATOM   15360 C  C   . LEU D  1  81  ? 64.438  82.217  26.921  1.00 78.35  ?  81  LEU D C   1 
ATOM   15361 O  O   . LEU D  1  81  ? 63.821  82.912  26.093  1.00 81.69  ?  81  LEU D O   1 
ATOM   15362 C  CB  . LEU D  1  81  ? 65.196  79.902  26.460  1.00 59.05  ?  81  LEU D CB  1 
ATOM   15363 C  CG  . LEU D  1  81  ? 64.011  79.539  25.557  1.00 71.26  ?  81  LEU D CG  1 
ATOM   15364 C  CD1 . LEU D  1  81  ? 64.266  78.227  24.833  1.00 67.64  ?  81  LEU D CD1 1 
ATOM   15365 C  CD2 . LEU D  1  81  ? 62.672  79.489  26.306  1.00 77.66  ?  81  LEU D CD2 1 
ATOM   15366 N  N   . LEU D  1  82  ? 64.143  82.137  28.215  1.00 78.46  ?  82  LEU D N   1 
ATOM   15367 C  CA  . LEU D  1  82  ? 62.965  82.828  28.743  1.00 67.63  ?  82  LEU D CA  1 
ATOM   15368 C  C   . LEU D  1  82  ? 63.100  84.335  28.531  1.00 75.82  ?  82  LEU D C   1 
ATOM   15369 O  O   . LEU D  1  82  ? 62.115  84.991  28.200  1.00 77.99  ?  82  LEU D O   1 
ATOM   15370 C  CB  . LEU D  1  82  ? 62.757  82.500  30.230  1.00 71.41  ?  82  LEU D CB  1 
ATOM   15371 C  CG  . LEU D  1  82  ? 62.572  81.017  30.557  1.00 72.02  ?  82  LEU D CG  1 
ATOM   15372 C  CD1 . LEU D  1  82  ? 62.672  80.771  32.050  1.00 64.09  ?  82  LEU D CD1 1 
ATOM   15373 C  CD2 . LEU D  1  82  ? 61.253  80.491  30.017  1.00 60.77  ?  82  LEU D CD2 1 
ATOM   15374 N  N   . ASN D  1  83  ? 64.317  84.883  28.697  1.00 78.09  ?  83  ASN D N   1 
ATOM   15375 C  CA  . ASN D  1  83  ? 64.567  86.307  28.465  1.00 70.66  ?  83  ASN D CA  1 
ATOM   15376 C  C   . ASN D  1  83  ? 64.392  86.601  26.974  1.00 75.86  ?  83  ASN D C   1 
ATOM   15377 O  O   . ASN D  1  83  ? 63.839  87.638  26.613  1.00 74.54  ?  83  ASN D O   1 
ATOM   15378 C  CB  . ASN D  1  83  ? 65.980  86.696  28.909  1.00 81.47  ?  83  ASN D CB  1 
ATOM   15379 C  CG  . ASN D  1  83  ? 66.127  86.888  30.398  1.00 77.41  ?  83  ASN D CG  1 
ATOM   15380 O  OD1 . ASN D  1  83  ? 65.145  87.060  31.130  1.00 76.07  ?  83  ASN D OD1 1 
ATOM   15381 N  ND2 . ASN D  1  83  ? 67.366  86.869  30.878  1.00 77.96  ?  83  ASN D ND2 1 
ATOM   15382 N  N   . SER D  1  84  ? 64.850  85.684  26.103  1.00 80.57  ?  84  SER D N   1 
ATOM   15383 C  CA  . SER D  1  84  ? 64.692  85.838  24.659  1.00 75.26  ?  84  SER D CA  1 
ATOM   15384 C  C   . SER D  1  84  ? 63.195  85.844  24.300  1.00 77.00  ?  84  SER D C   1 
ATOM   15385 O  O   . SER D  1  84  ? 62.782  86.583  23.408  1.00 75.28  ?  84  SER D O   1 
ATOM   15386 C  CB  . SER D  1  84  ? 65.407  84.712  23.920  1.00 71.36  ?  84  SER D CB  1 
ATOM   15387 O  OG  . SER D  1  84  ? 65.556  85.007  22.541  1.00 74.84  ?  84  SER D OG  1 
ATOM   15388 N  N   . GLY D  1  85  ? 62.401  85.037  25.004  1.00 75.00  ?  85  GLY D N   1 
ATOM   15389 C  CA  . GLY D  1  85  ? 60.961  84.984  24.802  1.00 68.68  ?  85  GLY D CA  1 
ATOM   15390 C  C   . GLY D  1  85  ? 60.314  86.304  25.173  1.00 69.83  ?  85  GLY D C   1 
ATOM   15391 O  O   . GLY D  1  85  ? 59.379  86.743  24.504  1.00 74.63  ?  85  GLY D O   1 
ATOM   15392 N  N   . LEU D  1  86  ? 60.813  86.955  26.245  1.00 75.01  ?  86  LEU D N   1 
ATOM   15393 C  CA  . LEU D  1  86  ? 60.310  88.259  26.686  1.00 67.06  ?  86  LEU D CA  1 
ATOM   15394 C  C   . LEU D  1  86  ? 60.735  89.350  25.695  1.00 75.34  ?  86  LEU D C   1 
ATOM   15395 O  O   . LEU D  1  86  ? 60.014  90.332  25.541  1.00 72.28  ?  86  LEU D O   1 
ATOM   15396 C  CB  . LEU D  1  86  ? 60.811  88.615  28.093  1.00 59.63  ?  86  LEU D CB  1 
ATOM   15397 C  CG  . LEU D  1  86  ? 60.235  87.802  29.247  1.00 71.73  ?  86  LEU D CG  1 
ATOM   15398 C  CD1 . LEU D  1  86  ? 61.033  88.032  30.515  1.00 78.42  ?  86  LEU D CD1 1 
ATOM   15399 C  CD2 . LEU D  1  86  ? 58.771  88.137  29.492  1.00 63.34  ?  86  LEU D CD2 1 
ATOM   15400 N  N   . ALA D  1  87  ? 61.891  89.187  25.017  1.00 75.96  ?  87  ALA D N   1 
ATOM   15401 C  CA  . ALA D  1  87  ? 62.342  90.142  24.002  1.00 68.90  ?  87  ALA D CA  1 
ATOM   15402 C  C   . ALA D  1  87  ? 61.322  90.144  22.856  1.00 70.00  ?  87  ALA D C   1 
ATOM   15403 O  O   . ALA D  1  87  ? 61.007  91.199  22.316  1.00 75.33  ?  87  ALA D O   1 
ATOM   15404 C  CB  . ALA D  1  87  ? 63.705  89.737  23.469  1.00 71.58  ?  87  ALA D CB  1 
ATOM   15405 N  N   . THR D  1  88  ? 60.804  88.953  22.498  1.00 64.57  ?  88  THR D N   1 
ATOM   15406 C  CA  . THR D  1  88  ? 59.785  88.788  21.459  1.00 66.84  ?  88  THR D CA  1 
ATOM   15407 C  C   . THR D  1  88  ? 58.527  89.539  21.890  1.00 74.05  ?  88  THR D C   1 
ATOM   15408 O  O   . THR D  1  88  ? 57.911  90.218  21.074  1.00 74.80  ?  88  THR D O   1 
ATOM   15409 C  CB  . THR D  1  88  ? 59.480  87.294  21.251  1.00 66.02  ?  88  THR D CB  1 
ATOM   15410 O  OG1 . THR D  1  88  ? 60.672  86.638  20.813  1.00 79.42  ?  88  THR D OG1 1 
ATOM   15411 C  CG2 . THR D  1  88  ? 58.361  87.053  20.253  1.00 56.00  ?  88  THR D CG2 1 
ATOM   15412 N  N   . ALA D  1  89  ? 58.151  89.421  23.175  1.00 70.93  ?  89  ALA D N   1 
ATOM   15413 C  CA  . ALA D  1  89  ? 56.983  90.100  23.729  1.00 64.44  ?  89  ALA D CA  1 
ATOM   15414 C  C   . ALA D  1  89  ? 57.168  91.623  23.693  1.00 70.54  ?  89  ALA D C   1 
ATOM   15415 O  O   . ALA D  1  89  ? 56.264  92.330  23.258  1.00 78.31  ?  89  ALA D O   1 
ATOM   15416 C  CB  . ALA D  1  89  ? 56.733  89.630  25.154  1.00 56.17  ?  89  ALA D CB  1 
ATOM   15417 N  N   . VAL D  1  90  ? 58.335  92.136  24.113  1.00 71.02  ?  90  VAL D N   1 
ATOM   15418 C  CA  . VAL D  1  90  ? 58.589  93.581  24.087  1.00 70.76  ?  90  VAL D CA  1 
ATOM   15419 C  C   . VAL D  1  90  ? 58.555  94.078  22.635  1.00 70.67  ?  90  VAL D C   1 
ATOM   15420 O  O   . VAL D  1  90  ? 57.985  95.135  22.362  1.00 73.74  ?  90  VAL D O   1 
ATOM   15421 C  CB  . VAL D  1  90  ? 59.921  93.944  24.787  1.00 74.95  ?  90  VAL D CB  1 
ATOM   15422 C  CG1 . VAL D  1  90  ? 60.266  95.416  24.575  1.00 71.42  ?  90  VAL D CG1 1 
ATOM   15423 C  CG2 . VAL D  1  90  ? 59.857  93.628  26.278  1.00 66.91  ?  90  VAL D CG2 1 
ATOM   15424 N  N   . ALA D  1  91  ? 59.143  93.309  21.706  1.00 69.61  ?  91  ALA D N   1 
ATOM   15425 C  CA  . ALA D  1  91  ? 59.147  93.658  20.290  1.00 75.08  ?  91  ALA D CA  1 
ATOM   15426 C  C   . ALA D  1  91  ? 57.712  93.682  19.757  1.00 77.11  ?  91  ALA D C   1 
ATOM   15427 O  O   . ALA D  1  91  ? 57.349  94.609  19.037  1.00 76.77  ?  91  ALA D O   1 
ATOM   15428 C  CB  . ALA D  1  91  ? 59.983  92.657  19.507  1.00 60.03  ?  91  ALA D CB  1 
ATOM   15429 N  N   . ALA D  1  92  ? 56.886  92.687  20.127  1.00 70.87  ?  92  ALA D N   1 
ATOM   15430 C  CA  . ALA D  1  92  ? 55.490  92.625  19.689  1.00 77.26  ?  92  ALA D CA  1 
ATOM   15431 C  C   . ALA D  1  92  ? 54.723  93.859  20.158  1.00 78.39  ?  92  ALA D C   1 
ATOM   15432 O  O   . ALA D  1  92  ? 53.892  94.373  19.415  1.00 81.10  ?  92  ALA D O   1 
ATOM   15433 C  CB  . ALA D  1  92  ? 54.824  91.366  20.222  1.00 63.49  ?  92  ALA D CB  1 
ATOM   15434 N  N   . GLU D  1  93  ? 55.004  94.341  21.382  1.00 73.43  ?  93  GLU D N   1 
ATOM   15435 C  CA  . GLU D  1  93  ? 54.350  95.535  21.902  1.00 79.23  ?  93  GLU D CA  1 
ATOM   15436 C  C   . GLU D  1  93  ? 54.820  96.760  21.119  1.00 90.76  ?  93  GLU D C   1 
ATOM   15437 O  O   . GLU D  1  93  ? 54.015  97.635  20.819  1.00 94.09  ?  93  GLU D O   1 
ATOM   15438 C  CB  . GLU D  1  93  ? 54.662  95.734  23.387  1.00 73.93  ?  93  GLU D CB  1 
ATOM   15439 C  CG  . GLU D  1  93  ? 53.896  96.905  23.975  1.00 90.54  ?  93  GLU D CG  1 
ATOM   15440 C  CD  . GLU D  1  93  ? 53.917  96.974  25.485  1.00 104.32 ?  93  GLU D CD  1 
ATOM   15441 O  OE1 . GLU D  1  93  ? 55.012  97.182  26.055  1.00 101.04 ?  93  GLU D OE1 1 
ATOM   15442 O  OE2 . GLU D  1  93  ? 52.836  96.822  26.100  1.00 104.60 ?  93  GLU D OE2 1 
ATOM   15443 N  N   . ILE D  1  94  ? 56.118  96.832  20.788  1.00 85.14  ?  94  ILE D N   1 
ATOM   15444 C  CA  . ILE D  1  94  ? 56.663  97.955  20.024  1.00 78.43  ?  94  ILE D CA  1 
ATOM   15445 C  C   . ILE D  1  94  ? 56.007  97.999  18.639  1.00 81.72  ?  94  ILE D C   1 
ATOM   15446 O  O   . ILE D  1  94  ? 55.617  99.073  18.180  1.00 76.24  ?  94  ILE D O   1 
ATOM   15447 C  CB  . ILE D  1  94  ? 58.218  97.873  19.957  1.00 69.09  ?  94  ILE D CB  1 
ATOM   15448 C  CG1 . ILE D  1  94  ? 58.826  98.285  21.314  1.00 73.62  ?  94  ILE D CG1 1 
ATOM   15449 C  CG2 . ILE D  1  94  ? 58.772  98.751  18.833  1.00 71.95  ?  94  ILE D CG2 1 
ATOM   15450 C  CD1 . ILE D  1  94  ? 60.204  97.783  21.574  1.00 81.53  ?  94  ILE D CD1 1 
ATOM   15451 N  N   . ILE D  1  95  ? 55.855  96.832  17.993  1.00 77.54  ?  95  ILE D N   1 
ATOM   15452 C  CA  . ILE D  1  95  ? 55.228  96.742  16.671  1.00 75.40  ?  95  ILE D CA  1 
ATOM   15453 C  C   . ILE D  1  95  ? 53.760  97.165  16.765  1.00 85.44  ?  95  ILE D C   1 
ATOM   15454 O  O   . ILE D  1  95  ? 53.287  97.930  15.926  1.00 81.54  ?  95  ILE D O   1 
ATOM   15455 C  CB  . ILE D  1  95  ? 55.373  95.308  16.086  1.00 70.93  ?  95  ILE D CB  1 
ATOM   15456 C  CG1 . ILE D  1  95  ? 56.850  95.003  15.744  1.00 69.79  ?  95  ILE D CG1 1 
ATOM   15457 C  CG2 . ILE D  1  95  ? 54.486  95.129  14.851  1.00 81.94  ?  95  ILE D CG2 1 
ATOM   15458 C  CD1 . ILE D  1  95  ? 57.205  93.542  15.740  1.00 64.54  ?  95  ILE D CD1 1 
ATOM   15459 N  N   . GLU D  1  96  ? 53.044  96.672  17.785  1.00 83.06  ?  96  GLU D N   1 
ATOM   15460 C  CA  . GLU D  1  96  ? 51.636  97.016  17.977  1.00 72.69  ?  96  GLU D CA  1 
ATOM   15461 C  C   . GLU D  1  96  ? 51.468  98.492  18.340  1.00 78.25  ?  96  GLU D C   1 
ATOM   15462 O  O   . GLU D  1  96  ? 50.457  99.091  17.979  1.00 88.79  ?  96  GLU D O   1 
ATOM   15463 C  CB  . GLU D  1  96  ? 50.979  96.113  19.038  1.00 74.15  ?  96  GLU D CB  1 
ATOM   15464 C  CG  . GLU D  1  96  ? 50.740  94.686  18.568  1.00 82.24  ?  96  GLU D CG  1 
ATOM   15465 C  CD  . GLU D  1  96  ? 49.831  94.557  17.362  1.00 82.65  ?  96  GLU D CD  1 
ATOM   15466 O  OE1 . GLU D  1  96  ? 48.838  95.315  17.284  1.00 81.79  ?  96  GLU D OE1 1 
ATOM   15467 O  OE2 . GLU D  1  96  ? 50.107  93.698  16.496  1.00 84.85  ?  96  GLU D OE2 1 
ATOM   15468 N  N   . ALA D  1  97  ? 52.445  99.085  19.041  1.00 79.27  ?  97  ALA D N   1 
ATOM   15469 C  CA  . ALA D  1  97  ? 52.382  100.499 19.403  1.00 78.23  ?  97  ALA D CA  1 
ATOM   15470 C  C   . ALA D  1  97  ? 52.568  101.341 18.139  1.00 82.53  ?  97  ALA D C   1 
ATOM   15471 O  O   . ALA D  1  97  ? 51.850  102.320 17.947  1.00 82.69  ?  97  ALA D O   1 
ATOM   15472 C  CB  . ALA D  1  97  ? 53.462  100.830 20.421  1.00 86.16  ?  97  ALA D CB  1 
ATOM   15473 N  N   . ALA D  1  98  ? 53.518  100.948 17.268  1.00 81.44  ?  98  ALA D N   1 
ATOM   15474 C  CA  . ALA D  1  98  ? 53.770  101.651 16.015  1.00 78.50  ?  98  ALA D CA  1 
ATOM   15475 C  C   . ALA D  1  98  ? 52.602  101.481 15.036  1.00 82.08  ?  98  ALA D C   1 
ATOM   15476 O  O   . ALA D  1  98  ? 52.391  102.348 14.193  1.00 86.07  ?  98  ALA D O   1 
ATOM   15477 C  CB  . ALA D  1  98  ? 55.052  101.146 15.384  1.00 82.97  ?  98  ALA D CB  1 
ATOM   15478 N  N   . LYS D  1  99  ? 51.851  100.387 15.166  1.00 75.74  ?  99  LYS D N   1 
ATOM   15479 C  CA  . LYS D  1  99  ? 50.675  100.157 14.285  1.00 80.15  ?  99  LYS D CA  1 
ATOM   15480 C  C   . LYS D  1  99  ? 49.644  101.260 14.539  1.00 85.19  ?  99  LYS D C   1 
ATOM   15481 O  O   . LYS D  1  99  ? 49.074  101.769 13.557  1.00 97.13  ?  99  LYS D O   1 
ATOM   15482 C  CB  . LYS D  1  99  ? 50.072  98.777  14.564  1.00 88.60  ?  99  LYS D CB  1 
ATOM   15483 C  CG  . LYS D  1  99  ? 50.459  97.675  13.587  1.00 80.23  ?  99  LYS D CG  1 
ATOM   15484 C  CD  . LYS D  1  99  ? 49.337  96.691  13.325  1.00 92.72  ?  99  LYS D CD  1 
ATOM   15485 C  CE  . LYS D  1  99  ? 49.624  95.299  13.847  1.00 82.61  ?  99  LYS D CE  1 
ATOM   15486 N  NZ  . LYS D  1  99  ? 48.520  94.354  13.548  1.00 106.16 ?  99  LYS D NZ  1 
ATOM   15487 N  N   . TYR D  1  100 ? 49.416  101.607 15.807  1.00 84.44  ?  100 TYR D N   1 
ATOM   15488 C  CA  . TYR D  1  100 ? 48.452  102.651 16.179  1.00 93.91  ?  100 TYR D CA  1 
ATOM   15489 C  C   . TYR D  1  100 ? 48.946  104.053 15.795  1.00 87.13  ?  100 TYR D C   1 
ATOM   15490 O  O   . TYR D  1  100 ? 48.135  104.968 15.655  1.00 104.72 ?  100 TYR D O   1 
ATOM   15491 C  CB  . TYR D  1  100 ? 48.152  102.604 17.694  1.00 91.89  ?  100 TYR D CB  1 
ATOM   15492 C  CG  . TYR D  1  100 ? 47.123  101.567 18.089  1.00 84.29  ?  100 TYR D CG  1 
ATOM   15493 C  CD1 . TYR D  1  100 ? 47.476  100.234 18.243  1.00 82.23  ?  100 TYR D CD1 1 
ATOM   15494 C  CD2 . TYR D  1  100 ? 45.800  101.918 18.309  1.00 83.47  ?  100 TYR D CD2 1 
ATOM   15495 C  CE1 . TYR D  1  100 ? 46.536  99.275  18.598  1.00 94.93  ?  100 TYR D CE1 1 
ATOM   15496 C  CE2 . TYR D  1  100 ? 44.850  100.969 18.663  1.00 88.87  ?  100 TYR D CE2 1 
ATOM   15497 C  CZ  . TYR D  1  100 ? 45.223  99.646  18.812  1.00 98.86  ?  100 TYR D CZ  1 
ATOM   15498 O  OH  . TYR D  1  100 ? 44.288  98.699  19.160  1.00 96.96  ?  100 TYR D OH  1 
ATOM   15499 N  N   . VAL D  1  101 ? 50.263  104.225 15.628  1.00 87.07  ?  101 VAL D N   1 
ATOM   15500 C  CA  . VAL D  1  101 ? 50.861  105.506 15.257  1.00 103.83 ?  101 VAL D CA  1 
ATOM   15501 C  C   . VAL D  1  101 ? 50.664  105.758 13.758  1.00 100.52 ?  101 VAL D C   1 
ATOM   15502 O  O   . VAL D  1  101 ? 50.187  106.824 13.370  1.00 85.54  ?  101 VAL D O   1 
ATOM   15503 C  CB  . VAL D  1  101 ? 52.369  105.526 15.646  1.00 90.71  ?  101 VAL D CB  1 
ATOM   15504 C  CG1 . VAL D  1  101 ? 53.106  106.685 14.983  1.00 84.33  ?  101 VAL D CG1 1 
ATOM   15505 C  CG2 . VAL D  1  101 ? 52.541  105.573 17.159  1.00 92.38  ?  101 VAL D CG2 1 
ATOM   15506 N  N   . LEU D  1  102 ? 51.014  104.766 12.926  1.00 96.21  ?  102 LEU D N   1 
ATOM   15507 C  CA  . LEU D  1  102 ? 50.925  104.870 11.469  1.00 101.11 ?  102 LEU D CA  1 
ATOM   15508 C  C   . LEU D  1  102 ? 49.518  104.665 10.879  1.00 99.25  ?  102 LEU D C   1 
ATOM   15509 O  O   . LEU D  1  102 ? 49.376  104.711 9.656   1.00 102.10 ?  102 LEU D O   1 
ATOM   15510 C  CB  . LEU D  1  102 ? 51.907  103.869 10.834  1.00 89.80  ?  102 LEU D CB  1 
ATOM   15511 C  CG  . LEU D  1  102 ? 53.395  104.140 11.093  1.00 81.96  ?  102 LEU D CG  1 
ATOM   15512 C  CD1 . LEU D  1  102 ? 54.223  102.887 10.889  1.00 79.96  ?  102 LEU D CD1 1 
ATOM   15513 C  CD2 . LEU D  1  102 ? 53.910  105.270 10.211  1.00 95.93  ?  102 LEU D CD2 1 
ATOM   15514 N  N   . SER D  1  103 ? 48.486  104.455 11.709  1.00 88.26  ?  103 SER D N   1 
ATOM   15515 C  CA  . SER D  1  103 ? 47.133  104.259 11.193  1.00 92.85  ?  103 SER D CA  1 
ATOM   15516 C  C   . SER D  1  103 ? 46.085  104.817 12.144  1.00 102.09 ?  103 SER D C   1 
ATOM   15517 O  O   . SER D  1  103 ? 46.189  104.624 13.352  1.00 110.68 ?  103 SER D O   1 
ATOM   15518 C  CB  . SER D  1  103 ? 46.870  102.778 10.949  1.00 85.25  ?  103 SER D CB  1 
ATOM   15519 O  OG  . SER D  1  103 ? 45.567  102.576 10.429  1.00 96.46  ?  103 SER D OG  1 
ATOM   15520 N  N   . ASP D  1  104 ? 45.070  105.503 11.600  1.00 91.48  ?  104 ASP D N   1 
ATOM   15521 C  CA  . ASP D  1  104 ? 43.998  106.075 12.415  1.00 90.79  ?  104 ASP D CA  1 
ATOM   15522 C  C   . ASP D  1  104 ? 43.198  104.936 13.046  1.00 100.87 ?  104 ASP D C   1 
ATOM   15523 O  O   . ASP D  1  104 ? 42.892  104.985 14.235  1.00 116.32 ?  104 ASP D O   1 
ATOM   15524 C  CB  . ASP D  1  104 ? 43.071  106.961 11.563  1.00 94.55  ?  104 ASP D CB  1 
ATOM   15525 C  CG  . ASP D  1  104 ? 43.755  108.138 10.896  1.00 111.20 ?  104 ASP D CG  1 
ATOM   15526 O  OD1 . ASP D  1  104 ? 44.578  108.801 11.561  1.00 132.22 ?  104 ASP D OD1 1 
ATOM   15527 O  OD2 . ASP D  1  104 ? 43.458  108.402 9.711   1.00 116.69 ?  104 ASP D OD2 1 
ATOM   15528 N  N   . ALA D  1  105 ? 42.871  103.908 12.241  1.00 98.46  ?  105 ALA D N   1 
ATOM   15529 C  CA  . ALA D  1  105 ? 42.132  102.723 12.680  1.00 99.59  ?  105 ALA D CA  1 
ATOM   15530 C  C   . ALA D  1  105 ? 42.937  101.479 12.275  1.00 90.62  ?  105 ALA D C   1 
ATOM   15531 O  O   . ALA D  1  105 ? 42.715  100.941 11.191  1.00 89.36  ?  105 ALA D O   1 
ATOM   15532 C  CB  . ALA D  1  105 ? 40.761  102.692 12.022  1.00 104.88 ?  105 ALA D CB  1 
ATOM   15533 N  N   . PRO D  1  106 ? 43.897  101.016 13.102  1.00 91.57  ?  106 PRO D N   1 
ATOM   15534 C  CA  . PRO D  1  106 ? 44.700  99.850  12.701  1.00 96.04  ?  106 PRO D CA  1 
ATOM   15535 C  C   . PRO D  1  106 ? 43.954  98.521  12.704  1.00 93.49  ?  106 PRO D C   1 
ATOM   15536 O  O   . PRO D  1  106 ? 44.354  97.601  11.993  1.00 90.10  ?  106 PRO D O   1 
ATOM   15537 C  CB  . PRO D  1  106 ? 45.834  99.844  13.729  1.00 89.37  ?  106 PRO D CB  1 
ATOM   15538 C  CG  . PRO D  1  106 ? 45.230  100.445 14.936  1.00 94.06  ?  106 PRO D CG  1 
ATOM   15539 C  CD  . PRO D  1  106 ? 44.324  101.528 14.420  1.00 94.82  ?  106 PRO D CD  1 
ATOM   15540 N  N   . TYR D  1  107 ? 42.884  98.405  13.503  1.00 97.16  ?  107 TYR D N   1 
ATOM   15541 C  CA  . TYR D  1  107 ? 42.130  97.160  13.597  1.00 90.47  ?  107 TYR D CA  1 
ATOM   15542 C  C   . TYR D  1  107 ? 40.755  97.231  12.941  1.00 105.04 ?  107 TYR D C   1 
ATOM   15543 O  O   . TYR D  1  107 ? 40.028  98.209  13.109  1.00 96.00  ?  107 TYR D O   1 
ATOM   15544 C  CB  . TYR D  1  107 ? 42.003  96.736  15.070  1.00 84.35  ?  107 TYR D CB  1 
ATOM   15545 C  CG  . TYR D  1  107 ? 43.230  96.006  15.565  1.00 86.89  ?  107 TYR D CG  1 
ATOM   15546 C  CD1 . TYR D  1  107 ? 43.425  94.666  15.272  1.00 104.75 ?  107 TYR D CD1 1 
ATOM   15547 C  CD2 . TYR D  1  107 ? 44.238  96.677  16.239  1.00 92.85  ?  107 TYR D CD2 1 
ATOM   15548 C  CE1 . TYR D  1  107 ? 44.574  94.001  15.673  1.00 104.58 ?  107 TYR D CE1 1 
ATOM   15549 C  CE2 . TYR D  1  107 ? 45.389  96.020  16.654  1.00 96.37  ?  107 TYR D CE2 1 
ATOM   15550 C  CZ  . TYR D  1  107 ? 45.551  94.677  16.372  1.00 98.25  ?  107 TYR D CZ  1 
ATOM   15551 O  OH  . TYR D  1  107 ? 46.673  93.996  16.778  1.00 97.88  ?  107 TYR D OH  1 
ATOM   15552 N  N   . ALA D  1  108 ? 40.407  96.168  12.196  1.00 125.77 ?  108 ALA D N   1 
ATOM   15553 C  CA  . ALA D  1  108 ? 39.133  96.035  11.497  1.00 132.67 ?  108 ALA D CA  1 
ATOM   15554 C  C   . ALA D  1  108 ? 38.310  94.926  12.152  1.00 133.39 ?  108 ALA D C   1 
ATOM   15555 O  O   . ALA D  1  108 ? 38.874  93.969  12.683  1.00 117.50 ?  108 ALA D O   1 
ATOM   15556 C  CB  . ALA D  1  108 ? 39.378  95.698  10.035  1.00 136.43 ?  108 ALA D CB  1 
ATOM   15557 N  N   . GLU D  1  109 ? 36.978  95.045  12.105  1.00 132.31 ?  109 GLU D N   1 
ATOM   15558 C  CA  . GLU D  1  109 ? 36.097  94.050  12.711  1.00 127.48 ?  109 GLU D CA  1 
ATOM   15559 C  C   . GLU D  1  109 ? 36.297  92.654  12.100  1.00 132.29 ?  109 GLU D C   1 
ATOM   15560 O  O   . GLU D  1  109 ? 36.667  92.538  10.930  1.00 135.88 ?  109 GLU D O   1 
ATOM   15561 C  CB  . GLU D  1  109 ? 34.623  94.479  12.576  1.00 127.79 ?  109 GLU D CB  1 
ATOM   15562 C  CG  . GLU D  1  109 ? 34.160  95.440  13.658  1.00 141.09 ?  109 GLU D CG  1 
ATOM   15563 C  CD  . GLU D  1  109 ? 33.984  94.809  15.027  1.00 151.40 ?  109 GLU D CD  1 
ATOM   15564 O  OE1 . GLU D  1  109 ? 33.185  93.851  15.145  1.00 157.69 ?  109 GLU D OE1 1 
ATOM   15565 O  OE2 . GLU D  1  109 ? 34.645  95.273  15.984  1.00 135.79 ?  109 GLU D OE2 1 
ATOM   15566 N  N   . PRO D  1  110 ? 36.064  91.574  12.873  1.00 129.60 ?  110 PRO D N   1 
ATOM   15567 C  CA  . PRO D  1  110 ? 35.633  91.540  14.283  1.00 110.04 ?  110 PRO D CA  1 
ATOM   15568 C  C   . PRO D  1  110 ? 36.765  91.720  15.301  1.00 112.75 ?  110 PRO D C   1 
ATOM   15569 O  O   . PRO D  1  110 ? 36.505  91.686  16.501  1.00 121.61 ?  110 PRO D O   1 
ATOM   15570 C  CB  . PRO D  1  110 ? 34.953  90.165  14.411  1.00 104.60 ?  110 PRO D CB  1 
ATOM   15571 C  CG  . PRO D  1  110 ? 35.276  89.386  13.136  1.00 120.66 ?  110 PRO D CG  1 
ATOM   15572 C  CD  . PRO D  1  110 ? 36.247  90.214  12.339  1.00 119.02 ?  110 PRO D CD  1 
ATOM   15573 N  N   . CYS D  1  111 ? 38.011  91.919  14.831  1.00 115.03 ?  111 CYS D N   1 
ATOM   15574 C  CA  . CYS D  1  111 ? 39.178  92.083  15.698  1.00 101.76 ?  111 CYS D CA  1 
ATOM   15575 C  C   . CYS D  1  111 ? 39.039  93.259  16.654  1.00 94.27  ?  111 CYS D C   1 
ATOM   15576 O  O   . CYS D  1  111 ? 38.479  94.293  16.293  1.00 109.51 ?  111 CYS D O   1 
ATOM   15577 C  CB  . CYS D  1  111 ? 40.449  92.193  14.864  1.00 92.63  ?  111 CYS D CB  1 
ATOM   15578 S  SG  . CYS D  1  111 ? 40.729  90.784  13.765  1.00 121.75 ?  111 CYS D SG  1 
ATOM   15579 N  N   . VAL D  1  112 ? 39.563  93.094  17.876  1.00 88.58  ?  112 VAL D N   1 
ATOM   15580 C  CA  . VAL D  1  112 ? 39.494  94.109  18.924  1.00 98.30  ?  112 VAL D CA  1 
ATOM   15581 C  C   . VAL D  1  112 ? 40.813  94.866  19.066  1.00 91.36  ?  112 VAL D C   1 
ATOM   15582 O  O   . VAL D  1  112 ? 40.809  96.091  19.192  1.00 99.69  ?  112 VAL D O   1 
ATOM   15583 C  CB  . VAL D  1  112 ? 39.079  93.458  20.265  1.00 83.07  ?  112 VAL D CB  1 
ATOM   15584 C  CG1 . VAL D  1  112 ? 38.953  94.507  21.366  1.00 103.20 ?  112 VAL D CG1 1 
ATOM   15585 C  CG2 . VAL D  1  112 ? 37.774  92.683  20.107  1.00 99.92  ?  112 VAL D CG2 1 
ATOM   15586 N  N   . GLY D  1  113 ? 41.923  94.144  19.060  1.00 79.74  ?  113 GLY D N   1 
ATOM   15587 C  CA  . GLY D  1  113 ? 43.232  94.760  19.210  1.00 93.12  ?  113 GLY D CA  1 
ATOM   15588 C  C   . GLY D  1  113 ? 43.535  95.018  20.669  1.00 95.42  ?  113 GLY D C   1 
ATOM   15589 O  O   . GLY D  1  113 ? 43.367  94.118  21.494  1.00 99.81  ?  113 GLY D O   1 
ATOM   15590 N  N   . PHE D  1  114 ? 43.970  96.240  21.013  1.00 93.13  ?  114 PHE D N   1 
ATOM   15591 C  CA  . PHE D  1  114 ? 44.288  96.568  22.404  1.00 89.08  ?  114 PHE D CA  1 
ATOM   15592 C  C   . PHE D  1  114 ? 43.056  96.486  23.294  1.00 71.88  ?  114 PHE D C   1 
ATOM   15593 O  O   . PHE D  1  114 ? 41.990  96.956  22.908  1.00 92.33  ?  114 PHE D O   1 
ATOM   15594 C  CB  . PHE D  1  114 ? 44.902  97.967  22.511  1.00 78.16  ?  114 PHE D CB  1 
ATOM   15595 C  CG  . PHE D  1  114 ? 45.390  98.295  23.903  1.00 79.02  ?  114 PHE D CG  1 
ATOM   15596 C  CD1 . PHE D  1  114 ? 46.565  97.751  24.390  1.00 86.82  ?  114 PHE D CD1 1 
ATOM   15597 C  CD2 . PHE D  1  114 ? 44.660  99.125  24.734  1.00 70.76  ?  114 PHE D CD2 1 
ATOM   15598 C  CE1 . PHE D  1  114 ? 47.010  98.049  25.672  1.00 78.59  ?  114 PHE D CE1 1 
ATOM   15599 C  CE2 . PHE D  1  114 ? 45.106  99.419  26.016  1.00 72.10  ?  114 PHE D CE2 1 
ATOM   15600 C  CZ  . PHE D  1  114 ? 46.276  98.877  26.478  1.00 77.51  ?  114 PHE D CZ  1 
ATOM   15601 N  N   . ILE D  1  115 ? 43.207  95.904  24.491  1.00 82.13  ?  115 ILE D N   1 
ATOM   15602 C  CA  . ILE D  1  115 ? 42.113  95.758  25.449  1.00 84.57  ?  115 ILE D CA  1 
ATOM   15603 C  C   . ILE D  1  115 ? 42.212  96.889  26.482  1.00 83.87  ?  115 ILE D C   1 
ATOM   15604 O  O   . ILE D  1  115 ? 43.246  97.026  27.127  1.00 76.63  ?  115 ILE D O   1 
ATOM   15605 C  CB  . ILE D  1  115 ? 42.184  94.354  26.105  1.00 77.92  ?  115 ILE D CB  1 
ATOM   15606 C  CG1 . ILE D  1  115 ? 42.184  93.219  25.045  1.00 74.27  ?  115 ILE D CG1 1 
ATOM   15607 C  CG2 . ILE D  1  115 ? 41.059  94.165  27.110  1.00 89.11  ?  115 ILE D CG2 1 
ATOM   15608 C  CD1 . ILE D  1  115 ? 40.956  93.135  24.098  1.00 68.12  ?  115 ILE D CD1 1 
ATOM   15609 N  N   . SER D  1  116 ? 41.151  97.702  26.632  1.00 83.88  ?  116 SER D N   1 
ATOM   15610 C  CA  . SER D  1  116 ? 41.145  98.836  27.564  1.00 84.05  ?  116 SER D CA  1 
ATOM   15611 C  C   . SER D  1  116 ? 41.223  98.434  29.040  1.00 86.08  ?  116 SER D C   1 
ATOM   15612 O  O   . SER D  1  116 ? 40.745  97.367  29.417  1.00 90.92  ?  116 SER D O   1 
ATOM   15613 C  CB  . SER D  1  116 ? 39.905  99.693  27.337  1.00 95.32  ?  116 SER D CB  1 
ATOM   15614 O  OG  . SER D  1  116 ? 38.754  99.139  27.956  1.00 95.93  ?  116 SER D OG  1 
ATOM   15615 N  N   . ASP D  1  117 ? 41.799  99.310  29.881  1.00 83.63  ?  117 ASP D N   1 
ATOM   15616 C  CA  . ASP D  1  117 ? 41.934  99.051  31.317  1.00 86.83  ?  117 ASP D CA  1 
ATOM   15617 C  C   . ASP D  1  117 ? 40.593  98.703  31.986  1.00 89.46  ?  117 ASP D C   1 
ATOM   15618 O  O   . ASP D  1  117 ? 40.555  97.754  32.769  1.00 89.39  ?  117 ASP D O   1 
ATOM   15619 C  CB  . ASP D  1  117 ? 42.598  100.235 32.043  1.00 92.20  ?  117 ASP D CB  1 
ATOM   15620 C  CG  . ASP D  1  117 ? 44.109  100.247 31.949  1.00 93.66  ?  117 ASP D CG  1 
ATOM   15621 O  OD1 . ASP D  1  117 ? 44.648  99.638  31.001  1.00 95.43  ?  117 ASP D OD1 1 
ATOM   15622 O  OD2 . ASP D  1  117 ? 44.752  100.869 32.822  1.00 94.83  ?  117 ASP D OD2 1 
ATOM   15623 N  N   . PRO D  1  118 ? 39.474  99.414  31.710  1.00 91.77  ?  118 PRO D N   1 
ATOM   15624 C  CA  . PRO D  1  118 ? 38.201  99.031  32.346  1.00 91.67  ?  118 PRO D CA  1 
ATOM   15625 C  C   . PRO D  1  118 ? 37.792  97.583  32.055  1.00 100.15 ?  118 PRO D C   1 
ATOM   15626 O  O   . PRO D  1  118 ? 37.159  96.955  32.903  1.00 103.98 ?  118 PRO D O   1 
ATOM   15627 C  CB  . PRO D  1  118 ? 37.192  100.025 31.762  1.00 81.05  ?  118 PRO D CB  1 
ATOM   15628 C  CG  . PRO D  1  118 ? 37.996  101.151 31.260  1.00 89.00  ?  118 PRO D CG  1 
ATOM   15629 C  CD  . PRO D  1  118 ? 39.292  100.572 30.815  1.00 82.87  ?  118 PRO D CD  1 
ATOM   15630 N  N   . ILE D  1  119 ? 38.149  97.043  30.870  1.00 92.69  ?  119 ILE D N   1 
ATOM   15631 C  CA  . ILE D  1  119 ? 37.813  95.657  30.539  1.00 82.41  ?  119 ILE D CA  1 
ATOM   15632 C  C   . ILE D  1  119 ? 38.628  94.715  31.445  1.00 93.05  ?  119 ILE D C   1 
ATOM   15633 O  O   . ILE D  1  119 ? 38.104  93.702  31.904  1.00 98.62  ?  119 ILE D O   1 
ATOM   15634 C  CB  . ILE D  1  119 ? 38.026  95.351  29.034  1.00 87.18  ?  119 ILE D CB  1 
ATOM   15635 C  CG1 . ILE D  1  119 ? 37.010  96.126  28.171  1.00 91.45  ?  119 ILE D CG1 1 
ATOM   15636 C  CG2 . ILE D  1  119 ? 37.903  93.846  28.775  1.00 92.12  ?  119 ILE D CG2 1 
ATOM   15637 C  CD1 . ILE D  1  119 ? 37.411  96.282  26.721  1.00 96.93  ?  119 ILE D CD1 1 
ATOM   15638 N  N   . ILE D  1  120 ? 39.900  95.070  31.724  1.00 92.24  ?  120 ILE D N   1 
ATOM   15639 C  CA  . ILE D  1  120 ? 40.784  94.291  32.605  1.00 84.18  ?  120 ILE D CA  1 
ATOM   15640 C  C   . ILE D  1  120 ? 40.159  94.254  34.007  1.00 89.50  ?  120 ILE D C   1 
ATOM   15641 O  O   . ILE D  1  120 ? 40.159  93.209  34.653  1.00 91.64  ?  120 ILE D O   1 
ATOM   15642 C  CB  . ILE D  1  120 ? 42.221  94.899  32.668  1.00 77.56  ?  120 ILE D CB  1 
ATOM   15643 C  CG1 . ILE D  1  120 ? 42.857  95.125  31.267  1.00 87.58  ?  120 ILE D CG1 1 
ATOM   15644 C  CG2 . ILE D  1  120 ? 43.134  94.053  33.555  1.00 79.13  ?  120 ILE D CG2 1 
ATOM   15645 C  CD1 . ILE D  1  120 ? 42.846  93.974  30.340  1.00 87.18  ?  120 ILE D CD1 1 
ATOM   15646 N  N   . ARG D  1  121 ? 39.620  95.401  34.464  1.00 83.66  ?  121 ARG D N   1 
ATOM   15647 C  CA  . ARG D  1  121 ? 38.966  95.525  35.768  1.00 83.59  ?  121 ARG D CA  1 
ATOM   15648 C  C   . ARG D  1  121 ? 37.674  94.693  35.792  1.00 102.66 ?  121 ARG D C   1 
ATOM   15649 O  O   . ARG D  1  121 ? 37.335  94.104  36.820  1.00 111.59 ?  121 ARG D O   1 
ATOM   15650 C  CB  . ARG D  1  121 ? 38.639  96.996  36.071  1.00 96.61  ?  121 ARG D CB  1 
ATOM   15651 C  CG  . ARG D  1  121 ? 39.828  97.942  35.933  1.00 101.27 ?  121 ARG D CG  1 
ATOM   15652 C  CD  . ARG D  1  121 ? 39.593  99.260  36.645  1.00 105.93 ?  121 ARG D CD  1 
ATOM   15653 N  NE  . ARG D  1  121 ? 40.337  99.320  37.904  1.00 111.99 ?  121 ARG D NE  1 
ATOM   15654 C  CZ  . ARG D  1  121 ? 41.575  99.785  38.044  1.00 104.53 ?  121 ARG D CZ  1 
ATOM   15655 N  NH1 . ARG D  1  121 ? 42.249  100.241 36.993  1.00 91.31  ?  121 ARG D NH1 1 
ATOM   15656 N  NH2 . ARG D  1  121 ? 42.156  99.790  39.238  1.00 91.47  ?  121 ARG D NH2 1 
ATOM   15657 N  N   . SER D  1  122 ? 36.957  94.656  34.654  1.00 102.57 ?  122 SER D N   1 
ATOM   15658 C  CA  . SER D  1  122 ? 35.708  93.909  34.490  1.00 101.55 ?  122 SER D CA  1 
ATOM   15659 C  C   . SER D  1  122 ? 35.941  92.408  34.630  1.00 90.53  ?  122 SER D C   1 
ATOM   15660 O  O   . SER D  1  122 ? 35.118  91.715  35.225  1.00 100.35 ?  122 SER D O   1 
ATOM   15661 C  CB  . SER D  1  122 ? 35.094  94.200  33.121  1.00 92.95  ?  122 SER D CB  1 
ATOM   15662 O  OG  . SER D  1  122 ? 34.079  93.273  32.771  1.00 106.13 ?  122 SER D OG  1 
ATOM   15663 N  N   . LEU D  1  123 ? 37.050  91.907  34.068  1.00 98.47  ?  123 LEU D N   1 
ATOM   15664 C  CA  . LEU D  1  123 ? 37.380  90.481  34.120  1.00 110.96 ?  123 LEU D CA  1 
ATOM   15665 C  C   . LEU D  1  123 ? 38.146  90.073  35.393  1.00 98.83  ?  123 LEU D C   1 
ATOM   15666 O  O   . LEU D  1  123 ? 38.284  88.884  35.659  1.00 90.79  ?  123 LEU D O   1 
ATOM   15667 C  CB  . LEU D  1  123 ? 38.190  90.080  32.874  1.00 80.97  ?  123 LEU D CB  1 
ATOM   15668 C  CG  . LEU D  1  123 ? 37.534  90.380  31.522  1.00 100.73 ?  123 LEU D CG  1 
ATOM   15669 C  CD1 . LEU D  1  123 ? 38.539  90.276  30.395  1.00 94.61  ?  123 LEU D CD1 1 
ATOM   15670 C  CD2 . LEU D  1  123 ? 36.344  89.461  31.260  1.00 118.02 ?  123 LEU D CD2 1 
ATOM   15671 N  N   . GLY D  1  124 ? 38.624  91.043  36.164  1.00 95.47  ?  124 GLY D N   1 
ATOM   15672 C  CA  . GLY D  1  124 ? 39.376  90.773  37.379  1.00 82.00  ?  124 GLY D CA  1 
ATOM   15673 C  C   . GLY D  1  124 ? 38.598  90.075  38.467  1.00 88.14  ?  124 GLY D C   1 
ATOM   15674 O  O   . GLY D  1  124 ? 39.097  89.121  39.067  1.00 97.77  ?  124 GLY D O   1 
ATOM   15675 N  N   . VAL D  1  125 ? 37.382  90.545  38.747  1.00 93.78  ?  125 VAL D N   1 
ATOM   15676 C  CA  . VAL D  1  125 ? 36.568  89.934  39.799  1.00 93.28  ?  125 VAL D CA  1 
ATOM   15677 C  C   . VAL D  1  125 ? 36.177  88.491  39.406  1.00 94.73  ?  125 VAL D C   1 
ATOM   15678 O  O   . VAL D  1  125 ? 36.434  87.572  40.186  1.00 102.74 ?  125 VAL D O   1 
ATOM   15679 C  CB  . VAL D  1  125 ? 35.344  90.800  40.187  1.00 96.10  ?  125 VAL D CB  1 
ATOM   15680 C  CG1 . VAL D  1  125 ? 34.563  90.150  41.326  1.00 81.23  ?  125 VAL D CG1 1 
ATOM   15681 C  CG2 . VAL D  1  125 ? 35.777  92.215  40.573  1.00 94.85  ?  125 VAL D CG2 1 
ATOM   15682 N  N   . PRO D  1  126 ? 35.601  88.242  38.207  1.00 92.47  ?  126 PRO D N   1 
ATOM   15683 C  CA  . PRO D  1  126 ? 35.254  86.857  37.843  1.00 95.50  ?  126 PRO D CA  1 
ATOM   15684 C  C   . PRO D  1  126 ? 36.452  85.904  37.820  1.00 97.64  ?  126 PRO D C   1 
ATOM   15685 O  O   . PRO D  1  126 ? 36.259  84.702  37.977  1.00 108.73 ?  126 PRO D O   1 
ATOM   15686 C  CB  . PRO D  1  126 ? 34.586  86.997  36.472  1.00 98.26  ?  126 PRO D CB  1 
ATOM   15687 C  CG  . PRO D  1  126 ? 35.023  88.297  35.956  1.00 96.44  ?  126 PRO D CG  1 
ATOM   15688 C  CD  . PRO D  1  126 ? 35.218  89.183  37.139  1.00 105.12 ?  126 PRO D CD  1 
ATOM   15689 N  N   . LEU D  1  127 ? 37.684  86.420  37.637  1.00 90.33  ?  127 LEU D N   1 
ATOM   15690 C  CA  . LEU D  1  127 ? 38.878  85.569  37.648  1.00 94.40  ?  127 LEU D CA  1 
ATOM   15691 C  C   . LEU D  1  127 ? 39.157  85.106  39.080  1.00 96.35  ?  127 LEU D C   1 
ATOM   15692 O  O   . LEU D  1  127 ? 39.477  83.937  39.303  1.00 87.54  ?  127 LEU D O   1 
ATOM   15693 C  CB  . LEU D  1  127 ? 40.114  86.324  37.118  1.00 75.12  ?  127 LEU D CB  1 
ATOM   15694 C  CG  . LEU D  1  127 ? 40.315  86.350  35.601  1.00 78.53  ?  127 LEU D CG  1 
ATOM   15695 C  CD1 . LEU D  1  127 ? 41.365  87.370  35.217  1.00 65.56  ?  127 LEU D CD1 1 
ATOM   15696 C  CD2 . LEU D  1  127 ? 40.720  84.982  35.066  1.00 77.39  ?  127 LEU D CD2 1 
ATOM   15697 N  N   . VAL D  1  128 ? 39.027  86.028  40.050  1.00 97.63  ?  128 VAL D N   1 
ATOM   15698 C  CA  . VAL D  1  128 ? 39.267  85.743  41.464  1.00 94.58  ?  128 VAL D CA  1 
ATOM   15699 C  C   . VAL D  1  128 ? 38.235  84.743  42.004  1.00 89.23  ?  128 VAL D C   1 
ATOM   15700 O  O   . VAL D  1  128 ? 38.616  83.737  42.601  1.00 88.97  ?  128 VAL D O   1 
ATOM   15701 C  CB  . VAL D  1  128 ? 39.283  87.051  42.295  1.00 90.09  ?  128 VAL D CB  1 
ATOM   15702 C  CG1 . VAL D  1  128 ? 39.349  86.752  43.789  1.00 76.11  ?  128 VAL D CG1 1 
ATOM   15703 C  CG2 . VAL D  1  128 ? 40.444  87.952  41.876  1.00 86.51  ?  128 VAL D CG2 1 
ATOM   15704 N  N   . THR D  1  129 ? 36.936  85.010  41.793  1.00 92.90  ?  129 THR D N   1 
ATOM   15705 C  CA  . THR D  1  129 ? 35.884  84.104  42.276  1.00 101.19 ?  129 THR D CA  1 
ATOM   15706 C  C   . THR D  1  129 ? 35.865  82.742  41.543  1.00 105.97 ?  129 THR D C   1 
ATOM   15707 O  O   . THR D  1  129 ? 35.218  81.808  42.018  1.00 100.42 ?  129 THR D O   1 
ATOM   15708 C  CB  . THR D  1  129 ? 34.493  84.782  42.271  1.00 99.66  ?  129 THR D CB  1 
ATOM   15709 O  OG1 . THR D  1  129 ? 33.499  83.837  42.678  1.00 133.45 ?  129 THR D OG1 1 
ATOM   15710 C  CG2 . THR D  1  129 ? 34.114  85.363  40.926  1.00 98.15  ?  129 THR D CG2 1 
ATOM   15711 N  N   . GLY D  1  130 ? 36.567  82.633  40.421  1.00 96.64  ?  130 GLY D N   1 
ATOM   15712 C  CA  . GLY D  1  130 ? 36.619  81.387  39.670  1.00 84.04  ?  130 GLY D CA  1 
ATOM   15713 C  C   . GLY D  1  130 ? 35.563  81.256  38.592  1.00 99.75  ?  130 GLY D C   1 
ATOM   15714 O  O   . GLY D  1  130 ? 35.437  80.188  37.992  1.00 106.66 ?  130 GLY D O   1 
ATOM   15715 N  N   . ASP D  1  131 ? 34.802  82.331  38.313  1.00 108.54 ?  131 ASP D N   1 
ATOM   15716 C  CA  . ASP D  1  131 ? 33.775  82.311  37.265  1.00 109.44 ?  131 ASP D CA  1 
ATOM   15717 C  C   . ASP D  1  131 ? 34.460  82.095  35.915  1.00 106.22 ?  131 ASP D C   1 
ATOM   15718 O  O   . ASP D  1  131 ? 33.933  81.375  35.068  1.00 110.49 ?  131 ASP D O   1 
ATOM   15719 C  CB  . ASP D  1  131 ? 32.962  83.617  37.259  1.00 112.74 ?  131 ASP D CB  1 
ATOM   15720 C  CG  . ASP D  1  131 ? 32.126  83.841  38.506  1.00 135.65 ?  131 ASP D CG  1 
ATOM   15721 O  OD1 . ASP D  1  131 ? 32.092  82.935  39.375  1.00 135.08 ?  131 ASP D OD1 1 
ATOM   15722 O  OD2 . ASP D  1  131 ? 31.509  84.924  38.619  1.00 152.61 ?  131 ASP D OD2 1 
ATOM   15723 N  N   . ILE D  1  132 ? 35.641  82.715  35.727  1.00 92.32  ?  132 ILE D N   1 
ATOM   15724 C  CA  . ILE D  1  132 ? 36.467  82.540  34.541  1.00 83.85  ?  132 ILE D CA  1 
ATOM   15725 C  C   . ILE D  1  132 ? 37.565  81.589  35.037  1.00 87.63  ?  132 ILE D C   1 
ATOM   15726 O  O   . ILE D  1  132 ? 38.512  82.051  35.675  1.00 90.85  ?  132 ILE D O   1 
ATOM   15727 C  CB  . ILE D  1  132 ? 37.046  83.879  34.019  1.00 84.10  ?  132 ILE D CB  1 
ATOM   15728 C  CG1 . ILE D  1  132 ? 35.921  84.759  33.435  1.00 80.97  ?  132 ILE D CG1 1 
ATOM   15729 C  CG2 . ILE D  1  132 ? 38.115  83.615  32.949  1.00 81.46  ?  132 ILE D CG2 1 
ATOM   15730 C  CD1 . ILE D  1  132 ? 36.287  86.193  33.232  1.00 70.12  ?  132 ILE D CD1 1 
ATOM   15731 N  N   . PRO D  1  133 ? 37.438  80.259  34.837  1.00 80.15  ?  133 PRO D N   1 
ATOM   15732 C  CA  . PRO D  1  133 ? 38.474  79.347  35.350  1.00 72.83  ?  133 PRO D CA  1 
ATOM   15733 C  C   . PRO D  1  133 ? 39.828  79.453  34.652  1.00 71.10  ?  133 PRO D C   1 
ATOM   15734 O  O   . PRO D  1  133 ? 40.851  79.183  35.271  1.00 78.48  ?  133 PRO D O   1 
ATOM   15735 C  CB  . PRO D  1  133 ? 37.864  77.953  35.151  1.00 80.92  ?  133 PRO D CB  1 
ATOM   15736 C  CG  . PRO D  1  133 ? 36.444  78.169  34.755  1.00 74.01  ?  133 PRO D CG  1 
ATOM   15737 C  CD  . PRO D  1  133 ? 36.372  79.516  34.141  1.00 78.66  ?  133 PRO D CD  1 
ATOM   15738 N  N   . GLY D  1  134 ? 39.824  79.836  33.379  1.00 69.41  ?  134 GLY D N   1 
ATOM   15739 C  CA  . GLY D  1  134 ? 41.048  79.963  32.602  1.00 76.52  ?  134 GLY D CA  1 
ATOM   15740 C  C   . GLY D  1  134 ? 40.926  80.883  31.409  1.00 75.92  ?  134 GLY D C   1 
ATOM   15741 O  O   . GLY D  1  134 ? 39.821  81.277  31.028  1.00 80.31  ?  134 GLY D O   1 
ATOM   15742 N  N   . VAL D  1  135 ? 42.079  81.286  30.860  1.00 76.35  ?  135 VAL D N   1 
ATOM   15743 C  CA  . VAL D  1  135 ? 42.057  82.101  29.607  1.00 76.49  ?  135 VAL D CA  1 
ATOM   15744 C  C   . VAL D  1  135 ? 42.803  81.315  28.522  1.00 76.32  ?  135 VAL D C   1 
ATOM   15745 O  O   . VAL D  1  135 ? 44.039  81.186  28.609  1.00 72.21  ?  135 VAL D O   1 
ATOM   15746 C  CB  . VAL D  1  135 ? 42.548  83.554  29.789  1.00 60.64  ?  135 VAL D CB  1 
ATOM   15747 C  CG1 . VAL D  1  135 ? 42.089  84.156  31.105  1.00 66.68  ?  135 VAL D CG1 1 
ATOM   15748 C  CG2 . VAL D  1  135 ? 44.041  83.737  29.590  1.00 73.59  ?  135 VAL D CG2 1 
ATOM   15749 N  N   . ALA D  1  136 ? 42.057  80.750  27.579  1.00 76.95  ?  136 ALA D N   1 
ATOM   15750 C  CA  . ALA D  1  136 ? 42.598  79.966  26.472  1.00 70.95  ?  136 ALA D CA  1 
ATOM   15751 C  C   . ALA D  1  136 ? 43.065  80.887  25.356  1.00 70.31  ?  136 ALA D C   1 
ATOM   15752 O  O   . ALA D  1  136 ? 42.236  81.527  24.717  1.00 91.25  ?  136 ALA D O   1 
ATOM   15753 C  CB  . ALA D  1  136 ? 41.534  79.019  25.939  1.00 71.35  ?  136 ALA D CB  1 
ATOM   15754 N  N   . VAL D  1  137 ? 44.375  80.957  25.108  1.00 58.63  ?  137 VAL D N   1 
ATOM   15755 C  CA  . VAL D  1  137 ? 44.910  81.807  24.048  1.00 67.65  ?  137 VAL D CA  1 
ATOM   15756 C  C   . VAL D  1  137 ? 45.148  80.939  22.822  1.00 68.96  ?  137 VAL D C   1 
ATOM   15757 O  O   . VAL D  1  137 ? 46.191  80.302  22.712  1.00 80.64  ?  137 VAL D O   1 
ATOM   15758 C  CB  . VAL D  1  137 ? 46.197  82.522  24.506  1.00 77.68  ?  137 VAL D CB  1 
ATOM   15759 C  CG1 . VAL D  1  137 ? 46.700  83.483  23.433  1.00 62.82  ?  137 VAL D CG1 1 
ATOM   15760 C  CG2 . VAL D  1  137 ? 45.964  83.249  25.827  1.00 75.00  ?  137 VAL D CG2 1 
ATOM   15761 N  N   . ILE D  1  138 ? 44.176  80.894  21.910  1.00 65.22  ?  138 ILE D N   1 
ATOM   15762 C  CA  . ILE D  1  138 ? 44.286  80.069  20.713  1.00 71.35  ?  138 ILE D CA  1 
ATOM   15763 C  C   . ILE D  1  138 ? 44.942  80.853  19.590  1.00 74.57  ?  138 ILE D C   1 
ATOM   15764 O  O   . ILE D  1  138 ? 44.482  81.935  19.239  1.00 78.20  ?  138 ILE D O   1 
ATOM   15765 C  CB  . ILE D  1  138 ? 42.904  79.490  20.333  1.00 69.39  ?  138 ILE D CB  1 
ATOM   15766 C  CG1 . ILE D  1  138 ? 42.429  78.528  21.448  1.00 77.17  ?  138 ILE D CG1 1 
ATOM   15767 C  CG2 . ILE D  1  138 ? 42.976  78.769  18.987  1.00 63.14  ?  138 ILE D CG2 1 
ATOM   15768 C  CD1 . ILE D  1  138 ? 41.018  78.155  21.420  1.00 78.06  ?  138 ILE D CD1 1 
ATOM   15769 N  N   . LEU D  1  139 ? 46.022  80.301  19.029  1.00 79.79  ?  139 LEU D N   1 
ATOM   15770 C  CA  . LEU D  1  139 ? 46.790  80.941  17.970  1.00 79.46  ?  139 LEU D CA  1 
ATOM   15771 C  C   . LEU D  1  139 ? 47.078  79.955  16.839  1.00 77.91  ?  139 LEU D C   1 
ATOM   15772 O  O   . LEU D  1  139 ? 47.336  78.787  17.104  1.00 80.66  ?  139 LEU D O   1 
ATOM   15773 C  CB  . LEU D  1  139 ? 48.109  81.430  18.597  1.00 67.14  ?  139 LEU D CB  1 
ATOM   15774 C  CG  . LEU D  1  139 ? 49.077  82.205  17.692  1.00 79.16  ?  139 LEU D CG  1 
ATOM   15775 C  CD1 . LEU D  1  139 ? 49.813  83.274  18.470  1.00 80.75  ?  139 LEU D CD1 1 
ATOM   15776 C  CD2 . LEU D  1  139 ? 50.093  81.278  17.038  1.00 68.76  ?  139 LEU D CD2 1 
ATOM   15777 N  N   . GLY D  1  140 ? 47.035  80.427  15.597  1.00 74.90  ?  140 GLY D N   1 
ATOM   15778 C  CA  . GLY D  1  140 ? 47.328  79.589  14.440  1.00 92.39  ?  140 GLY D CA  1 
ATOM   15779 C  C   . GLY D  1  140 ? 46.154  79.252  13.542  1.00 96.85  ?  140 GLY D C   1 
ATOM   15780 O  O   . GLY D  1  140 ? 45.249  80.066  13.355  1.00 81.13  ?  140 GLY D O   1 
ATOM   15781 N  N   . GLU D  1  141 ? 46.184  78.040  12.955  1.00 91.01  ?  141 GLU D N   1 
ATOM   15782 C  CA  . GLU D  1  141 ? 45.155  77.552  12.038  1.00 88.52  ?  141 GLU D CA  1 
ATOM   15783 C  C   . GLU D  1  141 ? 44.879  76.061  12.284  1.00 86.67  ?  141 GLU D C   1 
ATOM   15784 O  O   . GLU D  1  141 ? 45.810  75.266  12.380  1.00 98.11  ?  141 GLU D O   1 
ATOM   15785 C  CB  . GLU D  1  141 ? 45.627  77.757  10.588  1.00 93.92  ?  141 GLU D CB  1 
ATOM   15786 C  CG  . GLU D  1  141 ? 44.550  77.546  9.536   1.00 109.18 ?  141 GLU D CG  1 
ATOM   15787 C  CD  . GLU D  1  141 ? 45.070  77.464  8.113   1.00 121.43 ?  141 GLU D CD  1 
ATOM   15788 O  OE1 . GLU D  1  141 ? 46.167  76.893  7.908   1.00 119.55 ?  141 GLU D OE1 1 
ATOM   15789 O  OE2 . GLU D  1  141 ? 44.376  77.966  7.199   1.00 118.83 ?  141 GLU D OE2 1 
ATOM   15790 N  N   . CYS D  1  142 ? 43.598  75.687  12.364  1.00 89.48  ?  142 CYS D N   1 
ATOM   15791 C  CA  . CYS D  1  142 ? 43.166  74.302  12.581  1.00 94.27  ?  142 CYS D CA  1 
ATOM   15792 C  C   . CYS D  1  142 ? 43.055  73.568  11.226  1.00 100.85 ?  142 CYS D C   1 
ATOM   15793 O  O   . CYS D  1  142 ? 42.951  74.232  10.193  1.00 97.71  ?  142 CYS D O   1 
ATOM   15794 C  CB  . CYS D  1  142 ? 41.825  74.297  13.315  1.00 90.87  ?  142 CYS D CB  1 
ATOM   15795 S  SG  . CYS D  1  142 ? 41.951  74.512  15.111  1.00 96.82  ?  142 CYS D SG  1 
ATOM   15796 N  N   . PRO D  1  143 ? 43.038  72.215  11.182  1.00 93.71  ?  143 PRO D N   1 
ATOM   15797 C  CA  . PRO D  1  143 ? 42.900  71.533  9.879   1.00 100.85 ?  143 PRO D CA  1 
ATOM   15798 C  C   . PRO D  1  143 ? 41.612  71.912  9.138   1.00 108.04 ?  143 PRO D C   1 
ATOM   15799 O  O   . PRO D  1  143 ? 41.608  71.981  7.910   1.00 109.98 ?  143 PRO D O   1 
ATOM   15800 C  CB  . PRO D  1  143 ? 42.923  70.045  10.248  1.00 92.83  ?  143 PRO D CB  1 
ATOM   15801 C  CG  . PRO D  1  143 ? 42.581  69.995  11.688  1.00 90.06  ?  143 PRO D CG  1 
ATOM   15802 C  CD  . PRO D  1  143 ? 43.145  71.240  12.283  1.00 86.71  ?  143 PRO D CD  1 
ATOM   15803 N  N   . ASP D  1  144 ? 40.551  72.185  9.909   1.00 106.98 ?  144 ASP D N   1 
ATOM   15804 C  CA  . ASP D  1  144 ? 39.235  72.562  9.328   1.00 114.41 ?  144 ASP D CA  1 
ATOM   15805 C  C   . ASP D  1  144 ? 38.502  73.470  10.322  1.00 114.49 ?  144 ASP D C   1 
ATOM   15806 O  O   . ASP D  1  144 ? 38.892  73.474  11.505  1.00 116.25 ?  144 ASP D O   1 
ATOM   15807 C  CB  . ASP D  1  144 ? 38.402  71.318  9.021   1.00 121.17 ?  144 ASP D CB  1 
ATOM   15808 C  CG  . ASP D  1  144 ? 38.224  70.413  10.228  1.00 119.34 ?  144 ASP D CG  1 
ATOM   15809 O  OD1 . ASP D  1  144 ? 37.486  70.807  11.151  1.00 127.32 ?  144 ASP D OD1 1 
ATOM   15810 O  OD2 . ASP D  1  144 ? 38.829  69.324  10.235  1.00 119.33 ?  144 ASP D OD2 1 
ATOM   15811 N  N   . SER D  1  145 ? 37.474  74.196  9.867   1.00 103.35 ?  145 SER D N   1 
ATOM   15812 C  CA  . SER D  1  145 ? 36.714  75.076  10.758  1.00 98.47  ?  145 SER D CA  1 
ATOM   15813 C  C   . SER D  1  145 ? 35.827  74.321  11.758  1.00 107.56 ?  145 SER D C   1 
ATOM   15814 O  O   . SER D  1  145 ? 35.435  74.902  12.769  1.00 112.51 ?  145 SER D O   1 
ATOM   15815 C  CB  . SER D  1  145 ? 35.885  76.076  9.955   1.00 104.16 ?  145 SER D CB  1 
ATOM   15816 O  OG  . SER D  1  145 ? 34.682  75.506  9.465   1.00 124.60 ?  145 SER D OG  1 
ATOM   15817 N  N   . GLU D  1  146 ? 35.508  73.044  11.492  1.00 110.80 ?  146 GLU D N   1 
ATOM   15818 C  CA  . GLU D  1  146 ? 34.669  72.261  12.402  1.00 102.33 ?  146 GLU D CA  1 
ATOM   15819 C  C   . GLU D  1  146 ? 35.416  72.019  13.712  1.00 97.91  ?  146 GLU D C   1 
ATOM   15820 O  O   . GLU D  1  146 ? 34.840  72.191  14.784  1.00 86.91  ?  146 GLU D O   1 
ATOM   15821 C  CB  . GLU D  1  146 ? 34.266  70.918  11.765  1.00 109.29 ?  146 GLU D CB  1 
ATOM   15822 C  CG  . GLU D  1  146 ? 33.293  71.055  10.605  1.00 114.73 ?  146 GLU D CG  1 
ATOM   15823 C  CD  . GLU D  1  146 ? 32.975  69.769  9.866   1.00 136.77 ?  146 GLU D CD  1 
ATOM   15824 O  OE1 . GLU D  1  146 ? 33.614  68.732  10.161  1.00 138.19 ?  146 GLU D OE1 1 
ATOM   15825 O  OE2 . GLU D  1  146 ? 32.084  69.799  8.985   1.00 135.31 ?  146 GLU D OE2 1 
ATOM   15826 N  N   . THR D  1  147 ? 36.702  71.634  13.625  1.00 109.70 ?  147 THR D N   1 
ATOM   15827 C  CA  . THR D  1  147 ? 37.520  71.375  14.812  1.00 109.29 ?  147 THR D CA  1 
ATOM   15828 C  C   . THR D  1  147 ? 37.763  72.665  15.591  1.00 99.36  ?  147 THR D C   1 
ATOM   15829 O  O   . THR D  1  147 ? 37.739  72.638  16.819  1.00 101.10 ?  147 THR D O   1 
ATOM   15830 C  CB  . THR D  1  147 ? 38.854  70.689  14.442  1.00 93.75  ?  147 THR D CB  1 
ATOM   15831 O  OG1 . THR D  1  147 ? 39.580  71.446  13.461  1.00 103.87 ?  147 THR D OG1 1 
ATOM   15832 C  CG2 . THR D  1  147 ? 38.662  69.257  13.956  1.00 85.73  ?  147 THR D CG2 1 
ATOM   15833 N  N   . ALA D  1  148 ? 37.991  73.792  14.897  1.00 91.90  ?  148 ALA D N   1 
ATOM   15834 C  CA  . ALA D  1  148 ? 38.220  75.061  15.582  1.00 84.46  ?  148 ALA D CA  1 
ATOM   15835 C  C   . ALA D  1  148 ? 36.989  75.457  16.408  1.00 92.51  ?  148 ALA D C   1 
ATOM   15836 O  O   . ALA D  1  148 ? 37.129  75.775  17.583  1.00 87.32  ?  148 ALA D O   1 
ATOM   15837 C  CB  . ALA D  1  148 ? 38.563  76.153  14.578  1.00 79.48  ?  148 ALA D CB  1 
ATOM   15838 N  N   . ALA D  1  149 ? 35.786  75.399  15.810  1.00 88.56  ?  149 ALA D N   1 
ATOM   15839 C  CA  . ALA D  1  149 ? 34.552  75.757  16.506  1.00 90.11  ?  149 ALA D CA  1 
ATOM   15840 C  C   . ALA D  1  149 ? 34.240  74.819  17.670  1.00 104.98 ?  149 ALA D C   1 
ATOM   15841 O  O   . ALA D  1  149 ? 33.725  75.278  18.687  1.00 100.28 ?  149 ALA D O   1 
ATOM   15842 C  CB  . ALA D  1  149 ? 33.388  75.777  15.529  1.00 81.16  ?  149 ALA D CB  1 
ATOM   15843 N  N   . LYS D  1  150 ? 34.538  73.517  17.535  1.00 94.96  ?  150 LYS D N   1 
ATOM   15844 C  CA  . LYS D  1  150 ? 34.273  72.564  18.614  1.00 86.81  ?  150 LYS D CA  1 
ATOM   15845 C  C   . LYS D  1  150 ? 35.125  72.908  19.841  1.00 90.75  ?  150 LYS D C   1 
ATOM   15846 O  O   . LYS D  1  150 ? 34.626  72.869  20.965  1.00 78.38  ?  150 LYS D O   1 
ATOM   15847 C  CB  . LYS D  1  150 ? 34.557  71.123  18.158  1.00 86.62  ?  150 LYS D CB  1 
ATOM   15848 C  CG  . LYS D  1  150 ? 33.510  70.551  17.205  1.00 90.32  ?  150 LYS D CG  1 
ATOM   15849 C  CD  . LYS D  1  150 ? 33.525  69.015  17.175  1.00 118.94 ?  150 LYS D CD  1 
ATOM   15850 C  CE  . LYS D  1  150 ? 32.491  68.401  18.089  1.00 113.52 ?  150 LYS D CE  1 
ATOM   15851 N  NZ  . LYS D  1  150 ? 32.571  66.915  18.106  1.00 104.22 ?  150 LYS D NZ  1 
ATOM   15852 N  N   . ILE D  1  151 ? 36.405  73.256  19.621  1.00 83.99  ?  151 ILE D N   1 
ATOM   15853 C  CA  . ILE D  1  151 ? 37.331  73.610  20.701  1.00 81.84  ?  151 ILE D CA  1 
ATOM   15854 C  C   . ILE D  1  151 ? 36.917  74.939  21.335  1.00 90.13  ?  151 ILE D C   1 
ATOM   15855 O  O   . ILE D  1  151 ? 36.899  75.054  22.561  1.00 87.10  ?  151 ILE D O   1 
ATOM   15856 C  CB  . ILE D  1  151 ? 38.799  73.661  20.174  1.00 70.87  ?  151 ILE D CB  1 
ATOM   15857 C  CG1 . ILE D  1  151 ? 39.311  72.242  19.837  1.00 69.19  ?  151 ILE D CG1 1 
ATOM   15858 C  CG2 . ILE D  1  151 ? 39.725  74.334  21.194  1.00 66.65  ?  151 ILE D CG2 1 
ATOM   15859 C  CD1 . ILE D  1  151 ? 40.479  72.199  18.876  1.00 68.48  ?  151 ILE D CD1 1 
ATOM   15860 N  N   . ILE D  1  152 ? 36.627  75.952  20.521  1.00 87.59  ?  152 ILE D N   1 
ATOM   15861 C  CA  . ILE D  1  152 ? 36.180  77.247  21.108  1.00 82.66  ?  152 ILE D CA  1 
ATOM   15862 C  C   . ILE D  1  152 ? 34.907  77.012  21.920  1.00 87.32  ?  152 ILE D C   1 
ATOM   15863 O  O   . ILE D  1  152 ? 34.902  77.343  23.120  1.00 86.85  ?  152 ILE D O   1 
ATOM   15864 C  CB  . ILE D  1  152 ? 35.955  78.315  20.025  1.00 78.89  ?  152 ILE D CB  1 
ATOM   15865 C  CG1 . ILE D  1  152 ? 37.281  78.874  19.514  1.00 70.02  ?  152 ILE D CG1 1 
ATOM   15866 C  CG2 . ILE D  1  152 ? 35.047  79.416  20.544  1.00 92.13  ?  152 ILE D CG2 1 
ATOM   15867 C  CD1 . ILE D  1  152 ? 37.325  78.989  18.024  1.00 71.22  ?  152 ILE D CD1 1 
ATOM   15868 N  N   . LYS D  1  153 ? 33.876  76.457  21.285  1.00 86.88  ?  153 LYS D N   1 
ATOM   15869 C  CA  . LYS D  1  153 ? 32.603  76.290  21.977  1.00 89.82  ?  153 LYS D CA  1 
ATOM   15870 C  C   . LYS D  1  153 ? 32.750  75.476  23.258  1.00 90.73  ?  153 LYS D C   1 
ATOM   15871 O  O   . LYS D  1  153 ? 31.992  75.702  24.197  1.00 96.59  ?  153 LYS D O   1 
ATOM   15872 C  CB  . LYS D  1  153 ? 31.548  75.668  21.044  1.00 97.48  ?  153 LYS D CB  1 
ATOM   15873 C  CG  . LYS D  1  153 ? 31.162  76.586  19.883  1.00 93.59  ?  153 LYS D CG  1 
ATOM   15874 C  CD  . LYS D  1  153 ? 29.840  76.211  19.221  1.00 116.48 ?  153 LYS D CD  1 
ATOM   15875 C  CE  . LYS D  1  153 ? 29.944  75.016  18.301  1.00 117.47 ?  153 LYS D CE  1 
ATOM   15876 N  NZ  . LYS D  1  153 ? 28.887  75.032  17.254  1.00 118.01 ?  153 LYS D NZ  1 
ATOM   15877 N  N   . ASP D  1  154 ? 33.716  74.546  23.314  1.00 91.16  ?  154 ASP D N   1 
ATOM   15878 C  CA  . ASP D  1  154 ? 33.926  73.747  24.518  1.00 94.26  ?  154 ASP D CA  1 
ATOM   15879 C  C   . ASP D  1  154 ? 34.560  74.610  25.610  1.00 90.64  ?  154 ASP D C   1 
ATOM   15880 O  O   . ASP D  1  154 ? 34.110  74.560  26.754  1.00 95.49  ?  154 ASP D O   1 
ATOM   15881 C  CB  . ASP D  1  154 ? 34.802  72.524  24.220  1.00 88.54  ?  154 ASP D CB  1 
ATOM   15882 C  CG  . ASP D  1  154 ? 34.810  71.484  25.326  1.00 85.48  ?  154 ASP D CG  1 
ATOM   15883 O  OD1 . ASP D  1  154 ? 33.910  71.528  26.191  1.00 98.09  ?  154 ASP D OD1 1 
ATOM   15884 O  OD2 . ASP D  1  154 ? 35.709  70.620  25.321  1.00 82.64  ?  154 ASP D OD2 1 
ATOM   15885 N  N   . TYR D  1  155 ? 35.585  75.417  25.267  1.00 81.72  ?  155 TYR D N   1 
ATOM   15886 C  CA  . TYR D  1  155 ? 36.223  76.298  26.252  1.00 77.77  ?  155 TYR D CA  1 
ATOM   15887 C  C   . TYR D  1  155 ? 35.189  77.320  26.752  1.00 91.94  ?  155 TYR D C   1 
ATOM   15888 O  O   . TYR D  1  155 ? 35.092  77.563  27.952  1.00 96.43  ?  155 TYR D O   1 
ATOM   15889 C  CB  . TYR D  1  155 ? 37.427  77.051  25.646  1.00 75.38  ?  155 TYR D CB  1 
ATOM   15890 C  CG  . TYR D  1  155 ? 38.701  76.243  25.501  1.00 77.57  ?  155 TYR D CG  1 
ATOM   15891 C  CD1 . TYR D  1  155 ? 39.215  75.513  26.566  1.00 83.92  ?  155 TYR D CD1 1 
ATOM   15892 C  CD2 . TYR D  1  155 ? 39.456  76.305  24.339  1.00 79.57  ?  155 TYR D CD2 1 
ATOM   15893 C  CE1 . TYR D  1  155 ? 40.401  74.801  26.451  1.00 81.55  ?  155 TYR D CE1 1 
ATOM   15894 C  CE2 . TYR D  1  155 ? 40.650  75.604  24.215  1.00 81.27  ?  155 TYR D CE2 1 
ATOM   15895 C  CZ  . TYR D  1  155 ? 41.120  74.851  25.273  1.00 80.25  ?  155 TYR D CZ  1 
ATOM   15896 O  OH  . TYR D  1  155 ? 42.297  74.155  25.151  1.00 70.66  ?  155 TYR D OH  1 
ATOM   15897 N  N   . GLN D  1  156 ? 34.449  77.912  25.815  1.00 93.46  ?  156 GLN D N   1 
ATOM   15898 C  CA  . GLN D  1  156 ? 33.403  78.891  26.201  1.00 85.26  ?  156 GLN D CA  1 
ATOM   15899 C  C   . GLN D  1  156 ? 32.408  78.198  27.135  1.00 94.19  ?  156 GLN D C   1 
ATOM   15900 O  O   . GLN D  1  156 ? 31.989  78.828  28.124  1.00 107.74 ?  156 GLN D O   1 
ATOM   15901 C  CB  . GLN D  1  156 ? 32.713  79.431  24.951  1.00 96.82  ?  156 GLN D CB  1 
ATOM   15902 C  CG  . GLN D  1  156 ? 31.308  79.937  25.220  1.00 103.73 ?  156 GLN D CG  1 
ATOM   15903 C  CD  . GLN D  1  156 ? 30.752  80.711  24.051  1.00 107.67 ?  156 GLN D CD  1 
ATOM   15904 O  OE1 . GLN D  1  156 ? 30.772  80.251  22.911  1.00 84.85  ?  156 GLN D OE1 1 
ATOM   15905 N  NE2 . GLN D  1  156 ? 30.248  81.903  24.327  1.00 119.50 ?  156 GLN D NE2 1 
ATOM   15906 N  N   . SER D  1  157 ? 32.057  76.944  26.832  1.00 89.14  ?  157 SER D N   1 
ATOM   15907 C  CA  . SER D  1  157 ? 31.108  76.185  27.687  1.00 82.57  ?  157 SER D CA  1 
ATOM   15908 C  C   . SER D  1  157 ? 31.670  76.090  29.109  1.00 92.16  ?  157 SER D C   1 
ATOM   15909 O  O   . SER D  1  157 ? 30.882  76.225  30.065  1.00 91.23  ?  157 SER D O   1 
ATOM   15910 C  CB  . SER D  1  157 ? 30.834  74.820  27.113  1.00 78.70  ?  157 SER D CB  1 
ATOM   15911 O  OG  . SER D  1  157 ? 31.778  73.873  27.588  1.00 119.02 ?  157 SER D OG  1 
ATOM   15912 N  N   . LYS D  1  158 ? 32.983  75.887  29.238  1.00 97.78  ?  158 LYS D N   1 
ATOM   15913 C  CA  . LYS D  1  158 ? 33.617  75.785  30.580  1.00 89.95  ?  158 LYS D CA  1 
ATOM   15914 C  C   . LYS D  1  158 ? 33.695  77.180  31.207  1.00 91.80  ?  158 LYS D C   1 
ATOM   15915 O  O   . LYS D  1  158 ? 34.042  77.269  32.400  1.00 93.50  ?  158 LYS D O   1 
ATOM   15916 C  CB  . LYS D  1  158 ? 35.007  75.150  30.471  1.00 97.72  ?  158 LYS D CB  1 
ATOM   15917 C  CG  . LYS D  1  158 ? 35.121  73.996  29.486  1.00 85.25  ?  158 LYS D CG  1 
ATOM   15918 C  CD  . LYS D  1  158 ? 35.394  72.665  30.150  1.00 72.71  ?  158 LYS D CD  1 
ATOM   15919 C  CE  . LYS D  1  158 ? 35.229  71.492  29.209  1.00 75.62  ?  158 LYS D CE  1 
ATOM   15920 N  NZ  . LYS D  1  158 ? 34.010  70.708  29.518  1.00 104.91 ?  158 LYS D NZ  1 
ATOM   15921 N  N   . GLY D  1  159 ? 33.388  78.224  30.431  1.00 93.37  ?  159 GLY D N   1 
ATOM   15922 C  CA  . GLY D  1  159 ? 33.398  79.601  30.962  1.00 88.30  ?  159 GLY D CA  1 
ATOM   15923 C  C   . GLY D  1  159 ? 34.785  80.212  30.888  1.00 79.56  ?  159 GLY D C   1 
ATOM   15924 O  O   . GLY D  1  159 ? 34.924  81.402  31.235  1.00 90.65  ?  159 GLY D O   1 
ATOM   15925 N  N   . LEU D  1  160 ? 35.757  79.429  30.409  1.00 89.01  ?  160 LEU D N   1 
ATOM   15926 C  CA  . LEU D  1  160 ? 37.137  79.937  30.209  1.00 85.09  ?  160 LEU D CA  1 
ATOM   15927 C  C   . LEU D  1  160 ? 37.091  81.028  29.138  1.00 83.69  ?  160 LEU D C   1 
ATOM   15928 O  O   . LEU D  1  160 ? 36.414  80.812  28.115  1.00 77.13  ?  160 LEU D O   1 
ATOM   15929 C  CB  . LEU D  1  160 ? 38.010  78.777  29.721  1.00 70.11  ?  160 LEU D CB  1 
ATOM   15930 C  CG  . LEU D  1  160 ? 38.772  77.992  30.788  1.00 80.52  ?  160 LEU D CG  1 
ATOM   15931 C  CD1 . LEU D  1  160 ? 37.905  76.892  31.376  1.00 71.12  ?  160 LEU D CD1 1 
ATOM   15932 C  CD2 . LEU D  1  160 ? 40.056  77.413  30.215  1.00 85.60  ?  160 LEU D CD2 1 
ATOM   15933 N  N   . LEU D  1  161 ? 37.780  82.148  29.358  1.00 72.83  ?  161 LEU D N   1 
ATOM   15934 C  CA  . LEU D  1  161 ? 37.856  83.189  28.297  1.00 70.18  ?  161 LEU D CA  1 
ATOM   15935 C  C   . LEU D  1  161 ? 38.694  82.662  27.127  1.00 81.49  ?  161 LEU D C   1 
ATOM   15936 O  O   . LEU D  1  161 ? 39.768  82.090  27.386  1.00 84.94  ?  161 LEU D O   1 
ATOM   15937 C  CB  . LEU D  1  161 ? 38.474  84.458  28.889  1.00 75.95  ?  161 LEU D CB  1 
ATOM   15938 C  CG  . LEU D  1  161 ? 38.875  85.527  27.873  1.00 90.20  ?  161 LEU D CG  1 
ATOM   15939 C  CD1 . LEU D  1  161 ? 37.683  85.947  27.029  1.00 85.56  ?  161 LEU D CD1 1 
ATOM   15940 C  CD2 . LEU D  1  161 ? 39.485  86.733  28.570  1.00 65.01  ?  161 LEU D CD2 1 
ATOM   15941 N  N   . THR D  1  162 ? 38.238  82.870  25.896  1.00 78.94  ?  162 THR D N   1 
ATOM   15942 C  CA  . THR D  1  162 ? 39.003  82.338  24.743  1.00 79.23  ?  162 THR D CA  1 
ATOM   15943 C  C   . THR D  1  162 ? 39.408  83.513  23.846  1.00 84.09  ?  162 THR D C   1 
ATOM   15944 O  O   . THR D  1  162 ? 38.506  84.235  23.383  1.00 97.40  ?  162 THR D O   1 
ATOM   15945 C  CB  . THR D  1  162 ? 38.250  81.176  24.083  1.00 87.57  ?  162 THR D CB  1 
ATOM   15946 O  OG1 . THR D  1  162 ? 38.124  80.171  25.083  1.00 113.13 ?  162 THR D OG1 1 
ATOM   15947 C  CG2 . THR D  1  162 ? 38.937  80.634  22.851  1.00 91.50  ?  162 THR D CG2 1 
ATOM   15948 N  N   . CYS D  1  163 ? 40.711  83.696  23.624  1.00 79.55  ?  163 CYS D N   1 
ATOM   15949 C  CA  . CYS D  1  163 ? 41.223  84.833  22.861  1.00 79.38  ?  163 CYS D CA  1 
ATOM   15950 C  C   . CYS D  1  163 ? 41.833  84.267  21.604  1.00 78.86  ?  163 CYS D C   1 
ATOM   15951 O  O   . CYS D  1  163 ? 42.690  83.392  21.692  1.00 87.07  ?  163 CYS D O   1 
ATOM   15952 C  CB  . CYS D  1  163 ? 42.245  85.615  23.675  1.00 62.08  ?  163 CYS D CB  1 
ATOM   15953 S  SG  . CYS D  1  163 ? 41.629  86.181  25.279  1.00 91.21  ?  163 CYS D SG  1 
ATOM   15954 N  N   . LEU D  1  164 ? 41.389  84.733  20.437  1.00 70.81  ?  164 LEU D N   1 
ATOM   15955 C  CA  . LEU D  1  164 ? 41.889  84.197  19.175  1.00 74.25  ?  164 LEU D CA  1 
ATOM   15956 C  C   . LEU D  1  164 ? 42.798  85.130  18.401  1.00 70.88  ?  164 LEU D C   1 
ATOM   15957 O  O   . LEU D  1  164 ? 42.539  86.325  18.314  1.00 79.54  ?  164 LEU D O   1 
ATOM   15958 C  CB  . LEU D  1  164 ? 40.726  83.877  18.221  1.00 75.13  ?  164 LEU D CB  1 
ATOM   15959 C  CG  . LEU D  1  164 ? 39.433  83.317  18.831  1.00 78.16  ?  164 LEU D CG  1 
ATOM   15960 C  CD1 . LEU D  1  164 ? 38.419  83.017  17.751  1.00 80.07  ?  164 LEU D CD1 1 
ATOM   15961 C  CD2 . LEU D  1  164 ? 39.685  82.066  19.653  1.00 80.32  ?  164 LEU D CD2 1 
ATOM   15962 N  N   . VAL D  1  165 ? 43.853  84.538  17.837  1.00 79.66  ?  165 VAL D N   1 
ATOM   15963 C  CA  . VAL D  1  165 ? 44.839  85.334  17.059  1.00 81.69  ?  165 VAL D CA  1 
ATOM   15964 C  C   . VAL D  1  165 ? 45.316  84.496  15.869  1.00 77.28  ?  165 VAL D C   1 
ATOM   15965 O  O   . VAL D  1  165 ? 45.841  83.393  16.102  1.00 75.40  ?  165 VAL D O   1 
ATOM   15966 C  CB  . VAL D  1  165 ? 45.997  85.793  17.961  1.00 64.15  ?  165 VAL D CB  1 
ATOM   15967 C  CG1 . VAL D  1  165 ? 46.600  84.646  18.754  1.00 81.58  ?  165 VAL D CG1 1 
ATOM   15968 C  CG2 . VAL D  1  165 ? 47.053  86.521  17.161  1.00 71.09  ?  165 VAL D CG2 1 
ATOM   15969 N  N   . GLY D  1  166 ? 45.120  84.992  14.648  1.00 69.96  ?  166 GLY D N   1 
ATOM   15970 C  CA  . GLY D  1  166 ? 45.502  84.300  13.425  1.00 76.89  ?  166 GLY D CA  1 
ATOM   15971 C  C   . GLY D  1  166 ? 44.309  83.872  12.596  1.00 82.65  ?  166 GLY D C   1 
ATOM   15972 O  O   . GLY D  1  166 ? 43.226  84.446  12.723  1.00 85.61  ?  166 GLY D O   1 
ATOM   15973 N  N   . LYS D  1  167 ? 44.498  82.849  11.741  1.00 83.53  ?  167 LYS D N   1 
ATOM   15974 C  CA  . LYS D  1  167 ? 43.425  82.342  10.880  1.00 90.56  ?  167 LYS D CA  1 
ATOM   15975 C  C   . LYS D  1  167 ? 42.280  81.690  11.666  1.00 85.15  ?  167 LYS D C   1 
ATOM   15976 O  O   . LYS D  1  167 ? 41.192  81.520  11.118  1.00 76.94  ?  167 LYS D O   1 
ATOM   15977 C  CB  . LYS D  1  167 ? 43.973  81.361  9.835   1.00 96.49  ?  167 LYS D CB  1 
ATOM   15978 C  CG  . LYS D  1  167 ? 44.871  82.012  8.776   1.00 108.55 ?  167 LYS D CG  1 
ATOM   15979 C  CD  . LYS D  1  167 ? 44.601  81.481  7.360   1.00 121.51 ?  167 LYS D CD  1 
ATOM   15980 C  CE  . LYS D  1  167 ? 45.854  81.346  6.528   1.00 125.84 ?  167 LYS D CE  1 
ATOM   15981 N  NZ  . LYS D  1  167 ? 45.571  80.734  5.205   1.00 120.90 ?  167 LYS D NZ  1 
ATOM   15982 N  N   . VAL D  1  168 ? 42.506  81.329  12.941  1.00 79.41  ?  168 VAL D N   1 
ATOM   15983 C  CA  . VAL D  1  168 ? 41.441  80.739  13.761  1.00 77.88  ?  168 VAL D CA  1 
ATOM   15984 C  C   . VAL D  1  168 ? 40.238  81.696  13.863  1.00 85.93  ?  168 VAL D C   1 
ATOM   15985 O  O   . VAL D  1  168 ? 39.127  81.242  14.118  1.00 93.07  ?  168 VAL D O   1 
ATOM   15986 C  CB  . VAL D  1  168 ? 41.924  80.296  15.173  1.00 70.68  ?  168 VAL D CB  1 
ATOM   15987 C  CG1 . VAL D  1  168 ? 42.753  79.015  15.101  1.00 73.65  ?  168 VAL D CG1 1 
ATOM   15988 C  CG2 . VAL D  1  168 ? 42.695  81.411  15.879  1.00 78.99  ?  168 VAL D CG2 1 
ATOM   15989 N  N   . ILE D  1  169 ? 40.448  83.007  13.650  1.00 79.88  ?  169 ILE D N   1 
ATOM   15990 C  CA  . ILE D  1  169 ? 39.363  83.979  13.710  1.00 76.17  ?  169 ILE D CA  1 
ATOM   15991 C  C   . ILE D  1  169 ? 38.417  83.715  12.539  1.00 92.33  ?  169 ILE D C   1 
ATOM   15992 O  O   . ILE D  1  169 ? 37.204  83.649  12.733  1.00 95.95  ?  169 ILE D O   1 
ATOM   15993 C  CB  . ILE D  1  169 ? 39.916  85.427  13.689  1.00 73.97  ?  169 ILE D CB  1 
ATOM   15994 C  CG1 . ILE D  1  169 ? 40.720  85.723  14.973  1.00 80.76  ?  169 ILE D CG1 1 
ATOM   15995 C  CG2 . ILE D  1  169 ? 38.775  86.430  13.531  1.00 93.81  ?  169 ILE D CG2 1 
ATOM   15996 C  CD1 . ILE D  1  169 ? 41.679  86.857  14.860  1.00 78.93  ?  169 ILE D CD1 1 
ATOM   15997 N  N   . ASP D  1  170 ? 38.975  83.544  11.328  1.00 90.72  ?  170 ASP D N   1 
ATOM   15998 C  CA  . ASP D  1  170 ? 38.191  83.272  10.119  1.00 89.59  ?  170 ASP D CA  1 
ATOM   15999 C  C   . ASP D  1  170 ? 37.482  81.920  10.213  1.00 99.30  ?  170 ASP D C   1 
ATOM   16000 O  O   . ASP D  1  170 ? 36.353  81.784  9.745   1.00 104.38 ?  170 ASP D O   1 
ATOM   16001 C  CB  . ASP D  1  170 ? 39.099  83.281  8.876   1.00 90.39  ?  170 ASP D CB  1 
ATOM   16002 C  CG  . ASP D  1  170 ? 39.731  84.622  8.560   1.00 96.00  ?  170 ASP D CG  1 
ATOM   16003 O  OD1 . ASP D  1  170 ? 39.036  85.652  8.691   1.00 98.10  ?  170 ASP D OD1 1 
ATOM   16004 O  OD2 . ASP D  1  170 ? 40.916  84.639  8.166   1.00 114.44 ?  170 ASP D OD2 1 
ATOM   16005 N  N   . GLN D  1  171 ? 38.148  80.919  10.802  1.00 91.20  ?  171 GLN D N   1 
ATOM   16006 C  CA  . GLN D  1  171 ? 37.585  79.579  10.958  1.00 103.19 ?  171 GLN D CA  1 
ATOM   16007 C  C   . GLN D  1  171 ? 36.418  79.565  11.945  1.00 100.52 ?  171 GLN D C   1 
ATOM   16008 O  O   . GLN D  1  171 ? 35.421  78.887  11.707  1.00 104.15 ?  171 GLN D O   1 
ATOM   16009 C  CB  . GLN D  1  171 ? 38.671  78.606  11.430  1.00 91.67  ?  171 GLN D CB  1 
ATOM   16010 C  CG  . GLN D  1  171 ? 39.684  78.274  10.352  1.00 95.73  ?  171 GLN D CG  1 
ATOM   16011 C  CD  . GLN D  1  171 ? 40.676  77.251  10.822  1.00 84.89  ?  171 GLN D CD  1 
ATOM   16012 O  OE1 . GLN D  1  171 ? 41.263  77.376  11.900  1.00 94.69  ?  171 GLN D OE1 1 
ATOM   16013 N  NE2 . GLN D  1  171 ? 40.892  76.214  10.025  1.00 98.80  ?  171 GLN D NE2 1 
ATOM   16014 N  N   . ALA D  1  172 ? 36.546  80.302  13.056  1.00 101.70 ?  172 ALA D N   1 
ATOM   16015 C  CA  . ALA D  1  172 ? 35.500  80.380  14.073  1.00 89.83  ?  172 ALA D CA  1 
ATOM   16016 C  C   . ALA D  1  172 ? 34.251  81.053  13.492  1.00 96.33  ?  172 ALA D C   1 
ATOM   16017 O  O   . ALA D  1  172 ? 33.135  80.631  13.788  1.00 96.96  ?  172 ALA D O   1 
ATOM   16018 C  CB  . ALA D  1  172 ? 36.031  81.092  15.302  1.00 78.44  ?  172 ALA D CB  1 
ATOM   16019 N  N   . ILE D  1  173 ? 34.435  82.095  12.668  1.00 98.42  ?  173 ILE D N   1 
ATOM   16020 C  CA  . ILE D  1  173 ? 33.322  82.795  12.029  1.00 93.09  ?  173 ILE D CA  1 
ATOM   16021 C  C   . ILE D  1  173 ? 32.526  81.815  11.165  1.00 101.24 ?  173 ILE D C   1 
ATOM   16022 O  O   . ILE D  1  173 ? 31.303  81.749  11.278  1.00 102.29 ?  173 ILE D O   1 
ATOM   16023 C  CB  . ILE D  1  173 ? 33.839  84.013  11.199  1.00 88.37  ?  173 ILE D CB  1 
ATOM   16024 C  CG1 . ILE D  1  173 ? 34.353  85.152  12.121  1.00 83.81  ?  173 ILE D CG1 1 
ATOM   16025 C  CG2 . ILE D  1  173 ? 32.774  84.518  10.215  1.00 93.92  ?  173 ILE D CG2 1 
ATOM   16026 C  CD1 . ILE D  1  173 ? 33.274  86.017  12.866  1.00 97.90  ?  173 ILE D CD1 1 
ATOM   16027 N  N   . GLU D  1  174 ? 33.231  81.046  10.316  1.00 112.61 ?  174 GLU D N   1 
ATOM   16028 C  CA  . GLU D  1  174 ? 32.616  80.058  9.423   1.00 118.42 ?  174 GLU D CA  1 
ATOM   16029 C  C   . GLU D  1  174 ? 31.925  78.947  10.213  1.00 121.87 ?  174 GLU D C   1 
ATOM   16030 O  O   . GLU D  1  174 ? 30.840  78.513  9.839   1.00 134.64 ?  174 GLU D O   1 
ATOM   16031 C  CB  . GLU D  1  174 ? 33.667  79.441  8.491   1.00 121.22 ?  174 GLU D CB  1 
ATOM   16032 C  CG  . GLU D  1  174 ? 34.210  80.407  7.453   1.00 144.06 ?  174 GLU D CG  1 
ATOM   16033 C  CD  . GLU D  1  174 ? 35.349  79.855  6.616   1.00 163.70 ?  174 GLU D CD  1 
ATOM   16034 O  OE1 . GLU D  1  174 ? 35.896  78.786  6.972   1.00 137.62 ?  174 GLU D OE1 1 
ATOM   16035 O  OE2 . GLU D  1  174 ? 35.698  80.500  5.600   1.00 174.12 ?  174 GLU D OE2 1 
ATOM   16036 N  N   . GLY D  1  175 ? 32.548  78.506  11.300  1.00 110.29 ?  175 GLY D N   1 
ATOM   16037 C  CA  . GLY D  1  175 ? 31.987  77.461  12.147  1.00 101.77 ?  175 GLY D CA  1 
ATOM   16038 C  C   . GLY D  1  175 ? 30.912  77.949  13.103  1.00 107.21 ?  175 GLY D C   1 
ATOM   16039 O  O   . GLY D  1  175 ? 30.604  77.268  14.084  1.00 109.81 ?  175 GLY D O   1 
ATOM   16040 N  N   . LYS D  1  176 ? 30.332  79.135  12.831  1.00 109.27 ?  176 LYS D N   1 
ATOM   16041 C  CA  . LYS D  1  176 ? 29.271  79.737  13.634  1.00 102.11 ?  176 LYS D CA  1 
ATOM   16042 C  C   . LYS D  1  176 ? 29.426  79.921  15.136  1.00 106.24 ?  176 LYS D C   1 
ATOM   16043 O  O   . LYS D  1  176 ? 28.576  79.487  15.912  1.00 112.70 ?  176 LYS D O   1 
ATOM   16044 C  CB  . LYS D  1  176 ? 27.922  79.045  13.364  1.00 102.55 ?  176 LYS D CB  1 
ATOM   16045 C  CG  . LYS D  1  176 ? 27.557  78.923  11.883  1.00 120.73 ?  176 LYS D CG  1 
ATOM   16046 C  CD  . LYS D  1  176 ? 27.288  80.268  11.202  1.00 122.62 ?  176 LYS D CD  1 
ATOM   16047 C  CE  . LYS D  1  176 ? 26.867  80.104  9.761   1.00 137.03 ?  176 LYS D CE  1 
ATOM   16048 N  NZ  . LYS D  1  176 ? 27.336  81.234  8.917   1.00 134.01 ?  176 LYS D NZ  1 
ATOM   16049 N  N   . VAL D  1  177 ? 30.537  80.544  15.545  1.00 99.55  ?  177 VAL D N   1 
ATOM   16050 C  CA  . VAL D  1  177 ? 30.745  80.807  17.000  1.00 94.23  ?  177 VAL D CA  1 
ATOM   16051 C  C   . VAL D  1  177 ? 30.219  82.199  17.346  1.00 98.57  ?  177 VAL D C   1 
ATOM   16052 O  O   . VAL D  1  177 ? 30.306  83.102  16.491  1.00 98.76  ?  177 VAL D O   1 
ATOM   16053 C  CB  . VAL D  1  177 ? 32.209  80.657  17.462  1.00 80.42  ?  177 VAL D CB  1 
ATOM   16054 C  CG1 . VAL D  1  177 ? 32.830  79.366  16.952  1.00 79.83  ?  177 VAL D CG1 1 
ATOM   16055 C  CG2 . VAL D  1  177 ? 33.055  81.855  17.062  1.00 87.35  ?  177 VAL D CG2 1 
ATOM   16056 N  N   . LYS D  1  178 ? 29.694  82.345  18.556  1.00 88.20  ?  178 LYS D N   1 
ATOM   16057 C  CA  . LYS D  1  178 ? 29.195  83.628  19.043  1.00 95.72  ?  178 LYS D CA  1 
ATOM   16058 C  C   . LYS D  1  178 ? 30.328  84.399  19.718  1.00 97.32  ?  178 LYS D C   1 
ATOM   16059 O  O   . LYS D  1  178 ? 30.709  84.064  20.838  1.00 108.71 ?  178 LYS D O   1 
ATOM   16060 C  CB  . LYS D  1  178 ? 28.027  83.408  20.016  1.00 95.22  ?  178 LYS D CB  1 
ATOM   16061 C  CG  . LYS D  1  178 ? 26.813  82.750  19.367  1.00 90.09  ?  178 LYS D CG  1 
ATOM   16062 C  CD  . LYS D  1  178 ? 25.587  82.783  20.284  1.00 101.00 ?  178 LYS D CD  1 
ATOM   16063 C  CE  . LYS D  1  178 ? 24.270  82.716  19.541  1.00 118.19 ?  178 LYS D CE  1 
ATOM   16064 N  NZ  . LYS D  1  178 ? 23.229  83.574  20.176  1.00 123.40 ?  178 LYS D NZ  1 
ATOM   16065 N  N   . MET D  1  179 ? 30.870  85.429  19.046  1.00 87.51  ?  179 MET D N   1 
ATOM   16066 C  CA  . MET D  1  179 ? 31.978  86.211  19.596  1.00 88.05  ?  179 MET D CA  1 
ATOM   16067 C  C   . MET D  1  179 ? 31.544  87.503  20.279  1.00 97.33  ?  179 MET D C   1 
ATOM   16068 O  O   . MET D  1  179 ? 30.571  88.130  19.869  1.00 106.67 ?  179 MET D O   1 
ATOM   16069 C  CB  . MET D  1  179 ? 32.990  86.535  18.495  1.00 97.64  ?  179 MET D CB  1 
ATOM   16070 C  CG  . MET D  1  179 ? 33.613  85.311  17.888  1.00 96.24  ?  179 MET D CG  1 
ATOM   16071 S  SD  . MET D  1  179 ? 35.101  85.706  16.953  1.00 103.12 ?  179 MET D SD  1 
ATOM   16072 C  CE  . MET D  1  179 ? 35.044  84.455  15.740  1.00 103.29 ?  179 MET D CE  1 
ATOM   16073 N  N   . GLY D  1  180 ? 32.297  87.896  21.300  1.00 91.13  ?  180 GLY D N   1 
ATOM   16074 C  CA  . GLY D  1  180 ? 32.040  89.106  22.070  1.00 86.95  ?  180 GLY D CA  1 
ATOM   16075 C  C   . GLY D  1  180 ? 32.679  89.038  23.440  1.00 92.90  ?  180 GLY D C   1 
ATOM   16076 O  O   . GLY D  1  180 ? 32.939  87.947  23.947  1.00 87.56  ?  180 GLY D O   1 
ATOM   16077 N  N   . LEU D  1  181 ? 32.932  90.196  24.063  1.00 104.17 ?  181 LEU D N   1 
ATOM   16078 C  CA  . LEU D  1  181 ? 33.545  90.236  25.391  1.00 77.17  ?  181 LEU D CA  1 
ATOM   16079 C  C   . LEU D  1  181 ? 32.669  89.515  26.417  1.00 93.70  ?  181 LEU D C   1 
ATOM   16080 O  O   . LEU D  1  181 ? 33.192  88.781  27.253  1.00 91.77  ?  181 LEU D O   1 
ATOM   16081 C  CB  . LEU D  1  181 ? 33.801  91.693  25.824  1.00 104.28 ?  181 LEU D CB  1 
ATOM   16082 C  CG  . LEU D  1  181 ? 34.280  91.915  27.269  1.00 92.32  ?  181 LEU D CG  1 
ATOM   16083 C  CD1 . LEU D  1  181 ? 35.631  91.266  27.518  1.00 73.20  ?  181 LEU D CD1 1 
ATOM   16084 C  CD2 . LEU D  1  181 ? 34.359  93.396  27.596  1.00 99.11  ?  181 LEU D CD2 1 
ATOM   16085 N  N   . ASP D  1  182 ? 31.343  89.710  26.353  1.00 100.31 ?  182 ASP D N   1 
ATOM   16086 C  CA  . ASP D  1  182 ? 30.435  89.039  27.285  1.00 95.73  ?  182 ASP D CA  1 
ATOM   16087 C  C   . ASP D  1  182 ? 30.358  87.543  26.965  1.00 90.04  ?  182 ASP D C   1 
ATOM   16088 O  O   . ASP D  1  182 ? 30.268  86.729  27.883  1.00 91.40  ?  182 ASP D O   1 
ATOM   16089 C  CB  . ASP D  1  182 ? 29.032  89.673  27.254  1.00 101.00 ?  182 ASP D CB  1 
ATOM   16090 C  CG  . ASP D  1  182 ? 28.869  90.844  28.204  1.00 127.25 ?  182 ASP D CG  1 
ATOM   16091 O  OD1 . ASP D  1  182 ? 28.820  90.610  29.435  1.00 125.03 ?  182 ASP D OD1 1 
ATOM   16092 O  OD2 . ASP D  1  182 ? 28.792  91.994  27.718  1.00 157.11 ?  182 ASP D OD2 1 
ATOM   16093 N  N   . LEU D  1  183 ? 30.414  87.179  25.672  1.00 85.93  ?  183 LEU D N   1 
ATOM   16094 C  CA  . LEU D  1  183 ? 30.391  85.774  25.259  1.00 85.61  ?  183 LEU D CA  1 
ATOM   16095 C  C   . LEU D  1  183 ? 31.720  85.047  25.558  1.00 87.00  ?  183 LEU D C   1 
ATOM   16096 O  O   . LEU D  1  183 ? 31.848  83.864  25.249  1.00 91.89  ?  183 LEU D O   1 
ATOM   16097 C  CB  . LEU D  1  183 ? 30.054  85.669  23.765  1.00 86.96  ?  183 LEU D CB  1 
ATOM   16098 C  CG  . LEU D  1  183 ? 28.594  85.961  23.397  1.00 88.88  ?  183 LEU D CG  1 
ATOM   16099 C  CD1 . LEU D  1  183 ? 28.492  86.513  21.994  1.00 93.34  ?  183 LEU D CD1 1 
ATOM   16100 C  CD2 . LEU D  1  183 ? 27.727  84.718  23.558  1.00 85.50  ?  183 LEU D CD2 1 
ATOM   16101 N  N   . ARG D  1  184 ? 32.699  85.753  26.156  1.00 78.65  ?  184 ARG D N   1 
ATOM   16102 C  CA  . ARG D  1  184 ? 33.992  85.210  26.551  1.00 76.17  ?  184 ARG D CA  1 
ATOM   16103 C  C   . ARG D  1  184 ? 34.838  84.674  25.385  1.00 86.78  ?  184 ARG D C   1 
ATOM   16104 O  O   . ARG D  1  184 ? 35.623  83.752  25.583  1.00 108.78 ?  184 ARG D O   1 
ATOM   16105 C  CB  . ARG D  1  184 ? 33.796  84.143  27.646  1.00 92.59  ?  184 ARG D CB  1 
ATOM   16106 C  CG  . ARG D  1  184 ? 32.925  84.636  28.798  1.00 92.46  ?  184 ARG D CG  1 
ATOM   16107 C  CD  . ARG D  1  184 ? 33.102  83.837  30.076  1.00 87.75  ?  184 ARG D CD  1 
ATOM   16108 N  NE  . ARG D  1  184 ? 32.526  84.536  31.224  1.00 92.80  ?  184 ARG D NE  1 
ATOM   16109 C  CZ  . ARG D  1  184 ? 32.515  84.064  32.468  1.00 96.26  ?  184 ARG D CZ  1 
ATOM   16110 N  NH1 . ARG D  1  184 ? 33.051  82.882  32.743  1.00 88.90  ?  184 ARG D NH1 1 
ATOM   16111 N  NH2 . ARG D  1  184 ? 31.968  84.773  33.449  1.00 108.21 ?  184 ARG D NH2 1 
ATOM   16112 N  N   . VAL D  1  185 ? 34.652  85.252  24.194  1.00 79.71  ?  185 VAL D N   1 
ATOM   16113 C  CA  . VAL D  1  185 ? 35.464  84.859  23.003  1.00 90.97  ?  185 VAL D CA  1 
ATOM   16114 C  C   . VAL D  1  185 ? 35.881  86.152  22.299  1.00 86.24  ?  185 VAL D C   1 
ATOM   16115 O  O   . VAL D  1  185 ? 35.021  86.752  21.626  1.00 88.87  ?  185 VAL D O   1 
ATOM   16116 C  CB  . VAL D  1  185 ? 34.680  83.931  22.057  1.00 93.27  ?  185 VAL D CB  1 
ATOM   16117 C  CG1 . VAL D  1  185 ? 35.475  83.606  20.802  1.00 72.15  ?  185 VAL D CG1 1 
ATOM   16118 C  CG2 . VAL D  1  185 ? 34.234  82.656  22.757  1.00 93.33  ?  185 VAL D CG2 1 
ATOM   16119 N  N   . ILE D  1  186 ? 37.140  86.571  22.456  1.00 78.86  ?  186 ILE D N   1 
ATOM   16120 C  CA  . ILE D  1  186 ? 37.573  87.883  21.887  1.00 81.19  ?  186 ILE D CA  1 
ATOM   16121 C  C   . ILE D  1  186 ? 38.614  87.665  20.786  1.00 78.12  ?  186 ILE D C   1 
ATOM   16122 O  O   . ILE D  1  186 ? 39.703  87.149  21.099  1.00 83.04  ?  186 ILE D O   1 
ATOM   16123 C  CB  . ILE D  1  186 ? 38.122  88.794  23.001  1.00 73.21  ?  186 ILE D CB  1 
ATOM   16124 C  CG1 . ILE D  1  186 ? 37.067  89.078  24.072  1.00 96.40  ?  186 ILE D CG1 1 
ATOM   16125 C  CG2 . ILE D  1  186 ? 38.694  90.076  22.416  1.00 77.21  ?  186 ILE D CG2 1 
ATOM   16126 C  CD1 . ILE D  1  186 ? 37.634  89.221  25.464  1.00 71.42  ?  186 ILE D CD1 1 
ATOM   16127 N  N   . PRO D  1  187 ? 38.334  88.039  19.519  1.00 78.45  ?  187 PRO D N   1 
ATOM   16128 C  CA  . PRO D  1  187 ? 39.334  87.949  18.455  1.00 79.18  ?  187 PRO D CA  1 
ATOM   16129 C  C   . PRO D  1  187 ? 40.258  89.172  18.525  1.00 83.03  ?  187 PRO D C   1 
ATOM   16130 O  O   . PRO D  1  187 ? 39.762  90.277  18.417  1.00 92.73  ?  187 PRO D O   1 
ATOM   16131 C  CB  . PRO D  1  187 ? 38.480  87.981  17.182  1.00 72.25  ?  187 PRO D CB  1 
ATOM   16132 C  CG  . PRO D  1  187 ? 37.266  88.800  17.567  1.00 91.89  ?  187 PRO D CG  1 
ATOM   16133 C  CD  . PRO D  1  187 ? 37.043  88.535  19.042  1.00 77.70  ?  187 PRO D CD  1 
ATOM   16134 N  N   . LEU D  1  188 ? 41.563  88.965  18.710  1.00 67.25  ?  188 LEU D N   1 
ATOM   16135 C  CA  . LEU D  1  188 ? 42.487  90.120  18.871  1.00 67.56  ?  188 LEU D CA  1 
ATOM   16136 C  C   . LEU D  1  188 ? 42.931  90.623  17.495  1.00 84.43  ?  188 LEU D C   1 
ATOM   16137 O  O   . LEU D  1  188 ? 42.745  91.825  17.225  1.00 100.78 ?  188 LEU D O   1 
ATOM   16138 C  CB  . LEU D  1  188 ? 43.695  89.682  19.704  1.00 73.02  ?  188 LEU D CB  1 
ATOM   16139 C  CG  . LEU D  1  188 ? 43.377  89.197  21.116  1.00 69.17  ?  188 LEU D CG  1 
ATOM   16140 C  CD1 . LEU D  1  188 ? 44.072  87.875  21.391  1.00 83.40  ?  188 LEU D CD1 1 
ATOM   16141 C  CD2 . LEU D  1  188 ? 43.784  90.237  22.148  1.00 86.43  ?  188 LEU D CD2 1 
ATOM   16142 N  N   . GLY D  1  189 ? 43.496  89.742  16.666  1.00 87.40  ?  189 GLY D N   1 
ATOM   16143 C  CA  . GLY D  1  189 ? 44.002  90.152  15.363  1.00 91.01  ?  189 GLY D CA  1 
ATOM   16144 C  C   . GLY D  1  189 ? 44.589  89.011  14.566  1.00 89.77  ?  189 GLY D C   1 
ATOM   16145 O  O   . GLY D  1  189 ? 44.853  87.941  15.111  1.00 94.52  ?  189 GLY D O   1 
ATOM   16146 N  N   . TYR D  1  190 ? 44.813  89.233  13.272  1.00 86.56  ?  190 TYR D N   1 
ATOM   16147 C  CA  . TYR D  1  190 ? 45.369  88.204  12.399  1.00 81.05  ?  190 TYR D CA  1 
ATOM   16148 C  C   . TYR D  1  190 ? 46.890  88.114  12.491  1.00 95.38  ?  190 TYR D C   1 
ATOM   16149 O  O   . TYR D  1  190 ? 47.443  87.034  12.271  1.00 102.12 ?  190 TYR D O   1 
ATOM   16150 C  CB  . TYR D  1  190 ? 44.924  88.445  10.953  1.00 90.82  ?  190 TYR D CB  1 
ATOM   16151 C  CG  . TYR D  1  190 ? 43.426  88.337  10.795  1.00 89.67  ?  190 TYR D CG  1 
ATOM   16152 C  CD1 . TYR D  1  190 ? 42.807  87.102  10.675  1.00 96.89  ?  190 TYR D CD1 1 
ATOM   16153 C  CD2 . TYR D  1  190 ? 42.622  89.467  10.823  1.00 80.82  ?  190 TYR D CD2 1 
ATOM   16154 C  CE1 . TYR D  1  190 ? 41.428  86.992  10.561  1.00 91.18  ?  190 TYR D CE1 1 
ATOM   16155 C  CE2 . TYR D  1  190 ? 41.241  89.371  10.705  1.00 105.61 ?  190 TYR D CE2 1 
ATOM   16156 C  CZ  . TYR D  1  190 ? 40.646  88.131  10.576  1.00 95.11  ?  190 TYR D CZ  1 
ATOM   16157 O  OH  . TYR D  1  190 ? 39.278  88.038  10.456  1.00 101.24 ?  190 TYR D OH  1 
ATOM   16158 N  N   . ASP D  1  191 ? 47.573  89.226  12.812  1.00 91.85  ?  191 ASP D N   1 
ATOM   16159 C  CA  . ASP D  1  191 ? 49.033  89.213  12.933  1.00 98.89  ?  191 ASP D CA  1 
ATOM   16160 C  C   . ASP D  1  191 ? 49.452  88.463  14.194  1.00 91.55  ?  191 ASP D C   1 
ATOM   16161 O  O   . ASP D  1  191 ? 48.705  88.433  15.170  1.00 84.63  ?  191 ASP D O   1 
ATOM   16162 C  CB  . ASP D  1  191 ? 49.595  90.645  12.969  1.00 87.38  ?  191 ASP D CB  1 
ATOM   16163 C  CG  . ASP D  1  191 ? 49.546  91.370  11.639  1.00 99.05  ?  191 ASP D CG  1 
ATOM   16164 O  OD1 . ASP D  1  191 ? 49.355  90.697  10.599  1.00 101.96 ?  191 ASP D OD1 1 
ATOM   16165 O  OD2 . ASP D  1  191 ? 49.704  92.610  11.636  1.00 112.77 ?  191 ASP D OD2 1 
ATOM   16166 N  N   . VAL D  1  192 ? 50.649  87.863  14.185  1.00 90.06  ?  192 VAL D N   1 
ATOM   16167 C  CA  . VAL D  1  192 ? 51.142  87.119  15.346  1.00 90.30  ?  192 VAL D CA  1 
ATOM   16168 C  C   . VAL D  1  192 ? 51.296  88.063  16.542  1.00 86.94  ?  192 VAL D C   1 
ATOM   16169 O  O   . VAL D  1  192 ? 50.914  87.711  17.657  1.00 83.47  ?  192 VAL D O   1 
ATOM   16170 C  CB  . VAL D  1  192 ? 52.469  86.386  15.021  1.00 77.61  ?  192 VAL D CB  1 
ATOM   16171 C  CG1 . VAL D  1  192 ? 53.096  85.796  16.280  1.00 62.21  ?  192 VAL D CG1 1 
ATOM   16172 C  CG2 . VAL D  1  192 ? 52.246  85.296  13.978  1.00 82.21  ?  192 VAL D CG2 1 
ATOM   16173 N  N   . THR D  1  193 ? 51.822  89.273  16.301  1.00 85.08  ?  193 THR D N   1 
ATOM   16174 C  CA  . THR D  1  193 ? 52.031  90.267  17.356  1.00 81.64  ?  193 THR D CA  1 
ATOM   16175 C  C   . THR D  1  193 ? 50.754  90.597  18.151  1.00 78.39  ?  193 THR D C   1 
ATOM   16176 O  O   . THR D  1  193 ? 50.868  91.066  19.280  1.00 80.28  ?  193 THR D O   1 
ATOM   16177 C  CB  . THR D  1  193 ? 52.672  91.536  16.768  1.00 84.66  ?  193 THR D CB  1 
ATOM   16178 O  OG1 . THR D  1  193 ? 51.896  91.974  15.653  1.00 82.08  ?  193 THR D OG1 1 
ATOM   16179 C  CG2 . THR D  1  193 ? 54.115  91.318  16.334  1.00 72.74  ?  193 THR D CG2 1 
ATOM   16180 N  N   . SER D  1  194 ? 49.552  90.353  17.592  1.00 76.29  ?  194 SER D N   1 
ATOM   16181 C  CA  . SER D  1  194 ? 48.298  90.638  18.304  1.00 84.07  ?  194 SER D CA  1 
ATOM   16182 C  C   . SER D  1  194 ? 48.184  89.848  19.616  1.00 83.78  ?  194 SER D C   1 
ATOM   16183 O  O   . SER D  1  194 ? 47.432  90.252  20.505  1.00 80.65  ?  194 SER D O   1 
ATOM   16184 C  CB  . SER D  1  194 ? 47.094  90.332  17.419  1.00 80.65  ?  194 SER D CB  1 
ATOM   16185 O  OG  . SER D  1  194 ? 47.194  90.978  16.161  1.00 95.83  ?  194 SER D OG  1 
ATOM   16186 N  N   . VAL D  1  195 ? 48.976  88.786  19.760  1.00 75.63  ?  195 VAL D N   1 
ATOM   16187 C  CA  . VAL D  1  195 ? 48.930  87.956  21.001  1.00 75.75  ?  195 VAL D CA  1 
ATOM   16188 C  C   . VAL D  1  195 ? 49.469  88.772  22.181  1.00 82.35  ?  195 VAL D C   1 
ATOM   16189 O  O   . VAL D  1  195 ? 49.242  88.355  23.332  1.00 76.56  ?  195 VAL D O   1 
ATOM   16190 C  CB  . VAL D  1  195 ? 49.721  86.647  20.819  1.00 70.16  ?  195 VAL D CB  1 
ATOM   16191 C  CG1 . VAL D  1  195 ? 51.217  86.868  20.973  1.00 62.96  ?  195 VAL D CG1 1 
ATOM   16192 C  CG2 . VAL D  1  195 ? 49.236  85.558  21.762  1.00 65.71  ?  195 VAL D CG2 1 
ATOM   16193 N  N   . ILE D  1  196 ? 50.144  89.892  21.911  1.00 89.64  ?  196 ILE D N   1 
ATOM   16194 C  CA  . ILE D  1  196 ? 50.775  90.699  23.000  1.00 80.92  ?  196 ILE D CA  1 
ATOM   16195 C  C   . ILE D  1  196 ? 49.687  91.333  23.870  1.00 78.12  ?  196 ILE D C   1 
ATOM   16196 O  O   . ILE D  1  196 ? 49.943  91.540  25.069  1.00 83.51  ?  196 ILE D O   1 
ATOM   16197 C  CB  . ILE D  1  196 ? 51.714  91.772  22.414  1.00 73.20  ?  196 ILE D CB  1 
ATOM   16198 C  CG1 . ILE D  1  196 ? 52.686  92.310  23.467  1.00 76.66  ?  196 ILE D CG1 1 
ATOM   16199 C  CG2 . ILE D  1  196 ? 50.918  92.891  21.762  1.00 64.75  ?  196 ILE D CG2 1 
ATOM   16200 C  CD1 . ILE D  1  196 ? 53.287  91.242  24.348  1.00 78.46  ?  196 ILE D CD1 1 
ATOM   16201 N  N   . HIS D  1  197 ? 48.525  91.629  23.290  1.00 72.60  ?  197 HIS D N   1 
ATOM   16202 C  CA  . HIS D  1  197 ? 47.472  92.349  24.058  1.00 88.32  ?  197 HIS D CA  1 
ATOM   16203 C  C   . HIS D  1  197 ? 46.876  91.435  25.135  1.00 87.31  ?  197 HIS D C   1 
ATOM   16204 O  O   . HIS D  1  197 ? 46.324  91.968  26.120  1.00 102.47 ?  197 HIS D O   1 
ATOM   16205 C  CB  . HIS D  1  197 ? 46.422  92.932  23.109  1.00 85.98  ?  197 HIS D CB  1 
ATOM   16206 C  CG  . HIS D  1  197 ? 46.971  93.733  21.977  1.00 82.23  ?  197 HIS D CG  1 
ATOM   16207 N  ND1 . HIS D  1  197 ? 47.902  94.735  22.145  1.00 91.92  ?  197 HIS D ND1 1 
ATOM   16208 C  CD2 . HIS D  1  197 ? 46.710  93.686  20.665  1.00 74.33  ?  197 HIS D CD2 1 
ATOM   16209 C  CE1 . HIS D  1  197 ? 48.189  95.265  20.965  1.00 83.83  ?  197 HIS D CE1 1 
ATOM   16210 N  NE2 . HIS D  1  197 ? 47.476  94.643  20.053  1.00 89.59  ?  197 HIS D NE2 1 
ATOM   16211 N  N   . VAL D  1  198 ? 46.955  90.114  24.958  1.00 81.21  ?  198 VAL D N   1 
ATOM   16212 C  CA  . VAL D  1  198 ? 46.493  89.192  26.039  1.00 80.18  ?  198 VAL D CA  1 
ATOM   16213 C  C   . VAL D  1  198 ? 47.596  89.161  27.097  1.00 81.50  ?  198 VAL D C   1 
ATOM   16214 O  O   . VAL D  1  198 ? 47.272  89.199  28.295  1.00 74.51  ?  198 VAL D O   1 
ATOM   16215 C  CB  . VAL D  1  198 ? 46.188  87.784  25.498  1.00 67.62  ?  198 VAL D CB  1 
ATOM   16216 C  CG1 . VAL D  1  198 ? 46.167  86.748  26.610  1.00 63.58  ?  198 VAL D CG1 1 
ATOM   16217 C  CG2 . VAL D  1  198 ? 44.884  87.756  24.719  1.00 76.85  ?  198 VAL D CG2 1 
ATOM   16218 N  N   . VAL D  1  199 ? 48.851  89.103  26.657  1.00 73.34  ?  199 VAL D N   1 
ATOM   16219 C  CA  . VAL D  1  199 ? 49.994  89.127  27.572  1.00 73.24  ?  199 VAL D CA  1 
ATOM   16220 C  C   . VAL D  1  199 ? 49.863  90.377  28.473  1.00 80.73  ?  199 VAL D C   1 
ATOM   16221 O  O   . VAL D  1  199 ? 50.126  90.299  29.675  1.00 81.72  ?  199 VAL D O   1 
ATOM   16222 C  CB  . VAL D  1  199 ? 51.322  89.131  26.773  1.00 72.92  ?  199 VAL D CB  1 
ATOM   16223 C  CG1 . VAL D  1  199 ? 52.506  89.524  27.650  1.00 65.15  ?  199 VAL D CG1 1 
ATOM   16224 C  CG2 . VAL D  1  199 ? 51.560  87.779  26.107  1.00 55.85  ?  199 VAL D CG2 1 
ATOM   16225 N  N   . THR D  1  200 ? 49.414  91.515  27.893  1.00 75.82  ?  200 THR D N   1 
ATOM   16226 C  CA  . THR D  1  200 ? 49.211  92.758  28.640  1.00 77.27  ?  200 THR D CA  1 
ATOM   16227 C  C   . THR D  1  200 ? 48.042  92.615  29.630  1.00 83.35  ?  200 THR D C   1 
ATOM   16228 O  O   . THR D  1  200 ? 48.036  93.301  30.646  1.00 88.68  ?  200 THR D O   1 
ATOM   16229 C  CB  . THR D  1  200 ? 49.006  93.942  27.689  1.00 87.82  ?  200 THR D CB  1 
ATOM   16230 O  OG1 . THR D  1  200 ? 47.911  93.661  26.817  1.00 106.28 ?  200 THR D OG1 1 
ATOM   16231 C  CG2 . THR D  1  200 ? 50.256  94.266  26.878  1.00 71.52  ?  200 THR D CG2 1 
ATOM   16232 N  N   . ILE D  1  201 ? 47.062  91.727  29.354  1.00 81.68  ?  201 ILE D N   1 
ATOM   16233 C  CA  . ILE D  1  201 ? 45.939  91.494  30.270  1.00 78.33  ?  201 ILE D CA  1 
ATOM   16234 C  C   . ILE D  1  201 ? 46.513  90.905  31.564  1.00 77.26  ?  201 ILE D C   1 
ATOM   16235 O  O   . ILE D  1  201 ? 46.158  91.344  32.656  1.00 74.88  ?  201 ILE D O   1 
ATOM   16236 C  CB  . ILE D  1  201 ? 44.888  90.525  29.655  1.00 68.91  ?  201 ILE D CB  1 
ATOM   16237 C  CG1 . ILE D  1  201 ? 44.160  91.168  28.465  1.00 70.36  ?  201 ILE D CG1 1 
ATOM   16238 C  CG2 . ILE D  1  201 ? 43.890  90.025  30.720  1.00 62.61  ?  201 ILE D CG2 1 
ATOM   16239 C  CD1 . ILE D  1  201 ? 43.289  90.213  27.689  1.00 71.24  ?  201 ILE D CD1 1 
ATOM   16240 N  N   . ALA D  1  202 ? 47.408  89.912  31.433  1.00 69.41  ?  202 ALA D N   1 
ATOM   16241 C  CA  . ALA D  1  202 ? 48.034  89.263  32.578  1.00 72.74  ?  202 ALA D CA  1 
ATOM   16242 C  C   . ALA D  1  202 ? 48.991  90.208  33.303  1.00 79.90  ?  202 ALA D C   1 
ATOM   16243 O  O   . ALA D  1  202 ? 49.011  90.219  34.531  1.00 88.65  ?  202 ALA D O   1 
ATOM   16244 C  CB  . ALA D  1  202 ? 48.775  88.018  32.125  1.00 58.54  ?  202 ALA D CB  1 
ATOM   16245 N  N   . ILE D  1  203 ? 49.777  91.000  32.562  1.00 71.08  ?  203 ILE D N   1 
ATOM   16246 C  CA  . ILE D  1  203 ? 50.716  91.934  33.182  1.00 68.07  ?  203 ILE D CA  1 
ATOM   16247 C  C   . ILE D  1  203 ? 49.949  93.039  33.910  1.00 81.18  ?  203 ILE D C   1 
ATOM   16248 O  O   . ILE D  1  203 ? 50.269  93.352  35.057  1.00 88.45  ?  203 ILE D O   1 
ATOM   16249 C  CB  . ILE D  1  203 ? 51.714  92.492  32.135  1.00 60.52  ?  203 ILE D CB  1 
ATOM   16250 C  CG1 . ILE D  1  203 ? 52.739  91.401  31.748  1.00 65.52  ?  203 ILE D CG1 1 
ATOM   16251 C  CG2 . ILE D  1  203 ? 52.425  93.736  32.661  1.00 67.80  ?  203 ILE D CG2 1 
ATOM   16252 C  CD1 . ILE D  1  203 ? 53.401  91.606  30.429  1.00 81.58  ?  203 ILE D CD1 1 
ATOM   16253 N  N   . ARG D  1  204 ? 48.932  93.621  33.263  1.00 70.97  ?  204 ARG D N   1 
ATOM   16254 C  CA  . ARG D  1  204 ? 48.138  94.663  33.906  1.00 77.57  ?  204 ARG D CA  1 
ATOM   16255 C  C   . ARG D  1  204 ? 47.387  94.112  35.111  1.00 83.67  ?  204 ARG D C   1 
ATOM   16256 O  O   . ARG D  1  204 ? 47.181  94.852  36.064  1.00 83.82  ?  204 ARG D O   1 
ATOM   16257 C  CB  . ARG D  1  204 ? 47.173  95.328  32.918  1.00 72.87  ?  204 ARG D CB  1 
ATOM   16258 C  CG  . ARG D  1  204 ? 47.853  96.383  32.063  1.00 82.81  ?  204 ARG D CG  1 
ATOM   16259 C  CD  . ARG D  1  204 ? 46.905  96.984  31.061  1.00 89.81  ?  204 ARG D CD  1 
ATOM   16260 N  NE  . ARG D  1  204 ? 46.688  96.087  29.929  1.00 93.94  ?  204 ARG D NE  1 
ATOM   16261 C  CZ  . ARG D  1  204 ? 45.776  96.279  28.984  1.00 91.07  ?  204 ARG D CZ  1 
ATOM   16262 N  NH1 . ARG D  1  204 ? 44.980  97.343  29.024  1.00 70.60  ?  204 ARG D NH1 1 
ATOM   16263 N  NH2 . ARG D  1  204 ? 45.650  95.410  27.988  1.00 89.08  ?  204 ARG D NH2 1 
ATOM   16264 N  N   . ALA D  1  205 ? 47.002  92.824  35.102  1.00 75.91  ?  205 ALA D N   1 
ATOM   16265 C  CA  . ALA D  1  205 ? 46.320  92.231  36.250  1.00 76.35  ?  205 ALA D CA  1 
ATOM   16266 C  C   . ALA D  1  205 ? 47.247  92.241  37.473  1.00 89.24  ?  205 ALA D C   1 
ATOM   16267 O  O   . ALA D  1  205 ? 46.779  92.425  38.593  1.00 90.82  ?  205 ALA D O   1 
ATOM   16268 C  CB  . ALA D  1  205 ? 45.894  90.809  35.932  1.00 64.45  ?  205 ALA D CB  1 
ATOM   16269 N  N   . ALA D  1  206 ? 48.562  92.055  37.258  1.00 76.24  ?  206 ALA D N   1 
ATOM   16270 C  CA  . ALA D  1  206 ? 49.542  92.074  38.339  1.00 76.20  ?  206 ALA D CA  1 
ATOM   16271 C  C   . ALA D  1  206 ? 49.737  93.497  38.868  1.00 91.00  ?  206 ALA D C   1 
ATOM   16272 O  O   . ALA D  1  206 ? 49.923  93.683  40.066  1.00 98.68  ?  206 ALA D O   1 
ATOM   16273 C  CB  . ALA D  1  206 ? 50.869  91.520  37.847  1.00 75.48  ?  206 ALA D CB  1 
ATOM   16274 N  N   . LEU D  1  207 ? 49.696  94.500  37.985  1.00 94.56  ?  207 LEU D N   1 
ATOM   16275 C  CA  . LEU D  1  207 ? 49.867  95.891  38.393  1.00 94.22  ?  207 LEU D CA  1 
ATOM   16276 C  C   . LEU D  1  207 ? 48.594  96.412  39.069  1.00 91.39  ?  207 LEU D C   1 
ATOM   16277 O  O   . LEU D  1  207 ? 48.670  97.080  40.100  1.00 99.07  ?  207 LEU D O   1 
ATOM   16278 C  CB  . LEU D  1  207 ? 50.198  96.767  37.173  1.00 84.85  ?  207 LEU D CB  1 
ATOM   16279 C  CG  . LEU D  1  207 ? 51.506  96.455  36.445  1.00 67.64  ?  207 LEU D CG  1 
ATOM   16280 C  CD1 . LEU D  1  207 ? 51.513  97.064  35.064  1.00 71.49  ?  207 LEU D CD1 1 
ATOM   16281 C  CD2 . LEU D  1  207 ? 52.703  96.972  37.212  1.00 88.21  ?  207 LEU D CD2 1 
ATOM   16282 N  N   . ILE D  1  208 ? 47.426  96.102  38.489  1.00 82.61  ?  208 ILE D N   1 
ATOM   16283 C  CA  . ILE D  1  208 ? 46.133  96.550  39.005  1.00 86.66  ?  208 ILE D CA  1 
ATOM   16284 C  C   . ILE D  1  208 ? 45.709  95.784  40.276  1.00 85.88  ?  208 ILE D C   1 
ATOM   16285 O  O   . ILE D  1  208 ? 45.583  96.394  41.337  1.00 102.37 ?  208 ILE D O   1 
ATOM   16286 C  CB  . ILE D  1  208 ? 45.039  96.476  37.886  1.00 79.51  ?  208 ILE D CB  1 
ATOM   16287 C  CG1 . ILE D  1  208 ? 45.289  97.544  36.801  1.00 78.59  ?  208 ILE D CG1 1 
ATOM   16288 C  CG2 . ILE D  1  208 ? 43.630  96.630  38.476  1.00 74.05  ?  208 ILE D CG2 1 
ATOM   16289 C  CD1 . ILE D  1  208 ? 44.632  97.263  35.471  1.00 83.77  ?  208 ILE D CD1 1 
ATOM   16290 N  N   . PHE D  1  209 ? 45.481  94.463  40.175  1.00 87.46  ?  209 PHE D N   1 
ATOM   16291 C  CA  . PHE D  1  209 ? 45.017  93.666  41.309  1.00 83.67  ?  209 PHE D CA  1 
ATOM   16292 C  C   . PHE D  1  209 ? 46.146  93.264  42.240  1.00 87.63  ?  209 PHE D C   1 
ATOM   16293 O  O   . PHE D  1  209 ? 46.013  93.386  43.458  1.00 98.17  ?  209 PHE D O   1 
ATOM   16294 C  CB  . PHE D  1  209 ? 44.255  92.422  40.826  1.00 84.29  ?  209 PHE D CB  1 
ATOM   16295 C  CG  . PHE D  1  209 ? 43.247  92.725  39.745  1.00 89.38  ?  209 PHE D CG  1 
ATOM   16296 C  CD1 . PHE D  1  209 ? 42.073  93.392  40.039  1.00 87.82  ?  209 PHE D CD1 1 
ATOM   16297 C  CD2 . PHE D  1  209 ? 43.498  92.387  38.428  1.00 91.00  ?  209 PHE D CD2 1 
ATOM   16298 C  CE1 . PHE D  1  209 ? 41.155  93.683  39.040  1.00 80.69  ?  209 PHE D CE1 1 
ATOM   16299 C  CE2 . PHE D  1  209 ? 42.583  92.686  37.431  1.00 77.60  ?  209 PHE D CE2 1 
ATOM   16300 C  CZ  . PHE D  1  209 ? 41.429  93.347  37.740  1.00 78.18  ?  209 PHE D CZ  1 
ATOM   16301 N  N   . GLY D  1  210 ? 47.242  92.781  41.674  1.00 78.43  ?  210 GLY D N   1 
ATOM   16302 C  CA  . GLY D  1  210 ? 48.386  92.366  42.472  1.00 79.92  ?  210 GLY D CA  1 
ATOM   16303 C  C   . GLY D  1  210 ? 49.026  93.501  43.243  1.00 84.56  ?  210 GLY D C   1 
ATOM   16304 O  O   . GLY D  1  210 ? 49.647  93.273  44.282  1.00 85.04  ?  210 GLY D O   1 
ATOM   16305 N  N   . GLY D  1  211 ? 48.881  94.719  42.736  1.00 75.68  ?  211 GLY D N   1 
ATOM   16306 C  CA  . GLY D  1  211 ? 49.460  95.888  43.374  1.00 80.89  ?  211 GLY D CA  1 
ATOM   16307 C  C   . GLY D  1  211 ? 50.969  95.909  43.255  1.00 84.39  ?  211 GLY D C   1 
ATOM   16308 O  O   . GLY D  1  211 ? 51.650  96.479  44.109  1.00 97.48  ?  211 GLY D O   1 
ATOM   16309 N  N   . ILE D  1  212 ? 51.507  95.293  42.192  1.00 78.91  ?  212 ILE D N   1 
ATOM   16310 C  CA  . ILE D  1  212 ? 52.950  95.255  41.967  1.00 78.34  ?  212 ILE D CA  1 
ATOM   16311 C  C   . ILE D  1  212 ? 53.330  96.564  41.271  1.00 92.18  ?  212 ILE D C   1 
ATOM   16312 O  O   . ILE D  1  212 ? 52.532  97.106  40.503  1.00 103.23 ?  212 ILE D O   1 
ATOM   16313 C  CB  . ILE D  1  212 ? 53.385  94.008  41.132  1.00 89.67  ?  212 ILE D CB  1 
ATOM   16314 C  CG1 . ILE D  1  212 ? 52.701  92.693  41.606  1.00 76.17  ?  212 ILE D CG1 1 
ATOM   16315 C  CG2 . ILE D  1  212 ? 54.909  93.862  41.131  1.00 93.88  ?  212 ILE D CG2 1 
ATOM   16316 C  CD1 . ILE D  1  212 ? 52.986  92.246  43.052  1.00 93.29  ?  212 ILE D CD1 1 
ATOM   16317 N  N   . LYS D  1  213 ? 54.530  97.082  41.549  1.00 91.67  ?  213 LYS D N   1 
ATOM   16318 C  CA  . LYS D  1  213 ? 54.986  98.336  40.950  1.00 97.40  ?  213 LYS D CA  1 
ATOM   16319 C  C   . LYS D  1  213 ? 55.784  98.059  39.680  1.00 90.01  ?  213 LYS D C   1 
ATOM   16320 O  O   . LYS D  1  213 ? 56.374  96.987  39.544  1.00 89.43  ?  213 LYS D O   1 
ATOM   16321 C  CB  . LYS D  1  213 ? 55.842  99.128  41.952  1.00 88.77  ?  213 LYS D CB  1 
ATOM   16322 C  CG  . LYS D  1  213 ? 55.149  99.392  43.290  1.00 101.33 ?  213 LYS D CG  1 
ATOM   16323 C  CD  . LYS D  1  213 ? 54.345  100.692 43.300  1.00 112.85 ?  213 LYS D CD  1 
ATOM   16324 C  CE  . LYS D  1  213 ? 53.477  100.832 44.532  1.00 104.66 ?  213 LYS D CE  1 
ATOM   16325 N  NZ  . LYS D  1  213 ? 52.112  100.277 44.326  1.00 114.54 ?  213 LYS D NZ  1 
ATOM   16326 N  N   . GLY D  1  214 ? 55.797  99.025  38.764  1.00 86.21  ?  214 GLY D N   1 
ATOM   16327 C  CA  . GLY D  1  214 ? 56.528  98.899  37.509  1.00 83.27  ?  214 GLY D CA  1 
ATOM   16328 C  C   . GLY D  1  214 ? 58.013  98.730  37.753  1.00 88.60  ?  214 GLY D C   1 
ATOM   16329 O  O   . GLY D  1  214 ? 58.562  99.343  38.671  1.00 87.34  ?  214 GLY D O   1 
ATOM   16330 N  N   . GLY D  1  215 ? 58.657  97.888  36.955  1.00 77.81  ?  215 GLY D N   1 
ATOM   16331 C  CA  . GLY D  1  215 ? 60.081  97.618  37.107  1.00 83.18  ?  215 GLY D CA  1 
ATOM   16332 C  C   . GLY D  1  215 ? 60.352  96.327  37.857  1.00 89.87  ?  215 GLY D C   1 
ATOM   16333 O  O   . GLY D  1  215 ? 61.408  95.715  37.674  1.00 89.19  ?  215 GLY D O   1 
ATOM   16334 N  N   . GLN D  1  216 ? 59.400  95.894  38.711  1.00 86.97  ?  216 GLN D N   1 
ATOM   16335 C  CA  . GLN D  1  216 ? 59.534  94.650  39.475  1.00 95.33  ?  216 GLN D CA  1 
ATOM   16336 C  C   . GLN D  1  216 ? 59.112  93.503  38.556  1.00 88.91  ?  216 GLN D C   1 
ATOM   16337 O  O   . GLN D  1  216 ? 58.035  92.936  38.725  1.00 92.67  ?  216 GLN D O   1 
ATOM   16338 C  CB  . GLN D  1  216 ? 58.659  94.685  40.748  1.00 86.32  ?  216 GLN D CB  1 
ATOM   16339 C  CG  . GLN D  1  216 ? 58.932  95.869  41.677  1.00 92.84  ?  216 GLN D CG  1 
ATOM   16340 C  CD  . GLN D  1  216 ? 60.390  96.001  42.051  1.00 105.83 ?  216 GLN D CD  1 
ATOM   16341 O  OE1 . GLN D  1  216 ? 61.013  95.057  42.549  1.00 118.78 ?  216 GLN D OE1 1 
ATOM   16342 N  NE2 . GLN D  1  216 ? 60.976  97.172  41.817  1.00 98.37  ?  216 GLN D NE2 1 
ATOM   16343 N  N   . LEU D  1  217 ? 59.961  93.182  37.571  1.00 80.92  ?  217 LEU D N   1 
ATOM   16344 C  CA  . LEU D  1  217 ? 59.677  92.142  36.587  1.00 81.84  ?  217 LEU D CA  1 
ATOM   16345 C  C   . LEU D  1  217 ? 59.531  90.762  37.220  1.00 94.42  ?  217 LEU D C   1 
ATOM   16346 O  O   . LEU D  1  217 ? 58.582  90.046  36.900  1.00 87.68  ?  217 LEU D O   1 
ATOM   16347 C  CB  . LEU D  1  217 ? 60.778  92.128  35.513  1.00 76.34  ?  217 LEU D CB  1 
ATOM   16348 C  CG  . LEU D  1  217 ? 60.590  91.188  34.319  1.00 75.12  ?  217 LEU D CG  1 
ATOM   16349 C  CD1 . LEU D  1  217 ? 59.253  91.409  33.618  1.00 60.66  ?  217 LEU D CD1 1 
ATOM   16350 C  CD2 . LEU D  1  217 ? 61.728  91.349  33.330  1.00 85.18  ?  217 LEU D CD2 1 
ATOM   16351 N  N   . ASN D  1  218 ? 60.447  90.385  38.118  1.00 80.61  ?  218 ASN D N   1 
ATOM   16352 C  CA  . ASN D  1  218 ? 60.376  89.079  38.766  1.00 83.83  ?  218 ASN D CA  1 
ATOM   16353 C  C   . ASN D  1  218 ? 59.077  88.903  39.549  1.00 92.27  ?  218 ASN D C   1 
ATOM   16354 O  O   . ASN D  1  218 ? 58.508  87.812  39.548  1.00 96.87  ?  218 ASN D O   1 
ATOM   16355 C  CB  . ASN D  1  218 ? 61.577  88.868  39.675  1.00 92.74  ?  218 ASN D CB  1 
ATOM   16356 C  CG  . ASN D  1  218 ? 62.880  88.744  38.925  1.00 107.66 ?  218 ASN D CG  1 
ATOM   16357 O  OD1 . ASN D  1  218 ? 62.912  88.573  37.699  1.00 107.58 ?  218 ASN D OD1 1 
ATOM   16358 N  ND2 . ASN D  1  218 ? 63.991  88.830  39.645  1.00 129.00 ?  218 ASN D ND2 1 
ATOM   16359 N  N   . ASP D  1  219 ? 58.598  89.966  40.202  1.00 89.16  ?  219 ASP D N   1 
ATOM   16360 C  CA  . ASP D  1  219 ? 57.360  89.897  40.971  1.00 88.61  ?  219 ASP D CA  1 
ATOM   16361 C  C   . ASP D  1  219 ? 56.127  89.850  40.059  1.00 85.24  ?  219 ASP D C   1 
ATOM   16362 O  O   . ASP D  1  219 ? 55.144  89.196  40.405  1.00 93.55  ?  219 ASP D O   1 
ATOM   16363 C  CB  . ASP D  1  219 ? 57.272  91.074  41.950  1.00 96.93  ?  219 ASP D CB  1 
ATOM   16364 C  CG  . ASP D  1  219 ? 58.388  91.069  42.975  1.00 111.69 ?  219 ASP D CG  1 
ATOM   16365 O  OD1 . ASP D  1  219 ? 58.354  90.212  43.884  1.00 112.19 ?  219 ASP D OD1 1 
ATOM   16366 O  OD2 . ASP D  1  219 ? 59.301  91.919  42.863  1.00 114.34 ?  219 ASP D OD2 1 
ATOM   16367 N  N   . ILE D  1  220 ? 56.175  90.525  38.898  1.00 87.03  ?  220 ILE D N   1 
ATOM   16368 C  CA  . ILE D  1  220 ? 55.055  90.523  37.953  1.00 79.82  ?  220 ILE D CA  1 
ATOM   16369 C  C   . ILE D  1  220 ? 54.963  89.144  37.286  1.00 84.83  ?  220 ILE D C   1 
ATOM   16370 O  O   . ILE D  1  220 ? 53.868  88.593  37.161  1.00 74.39  ?  220 ILE D O   1 
ATOM   16371 C  CB  . ILE D  1  220 ? 55.198  91.674  36.915  1.00 63.29  ?  220 ILE D CB  1 
ATOM   16372 C  CG1 . ILE D  1  220 ? 54.959  93.040  37.592  1.00 79.08  ?  220 ILE D CG1 1 
ATOM   16373 C  CG2 . ILE D  1  220 ? 54.232  91.482  35.741  1.00 68.56  ?  220 ILE D CG2 1 
ATOM   16374 C  CD1 . ILE D  1  220 ? 55.536  94.221  36.869  1.00 90.31  ?  220 ILE D CD1 1 
ATOM   16375 N  N   . LEU D  1  221 ? 56.113  88.576  36.885  1.00 80.47  ?  221 LEU D N   1 
ATOM   16376 C  CA  . LEU D  1  221 ? 56.144  87.252  36.259  1.00 74.55  ?  221 LEU D CA  1 
ATOM   16377 C  C   . LEU D  1  221 ? 55.697  86.165  37.241  1.00 84.66  ?  221 LEU D C   1 
ATOM   16378 O  O   . LEU D  1  221 ? 55.188  85.133  36.808  1.00 88.79  ?  221 LEU D O   1 
ATOM   16379 C  CB  . LEU D  1  221 ? 57.540  86.931  35.718  1.00 70.94  ?  221 LEU D CB  1 
ATOM   16380 C  CG  . LEU D  1  221 ? 58.060  87.855  34.621  1.00 63.88  ?  221 LEU D CG  1 
ATOM   16381 C  CD1 . LEU D  1  221 ? 59.534  87.627  34.390  1.00 79.41  ?  221 LEU D CD1 1 
ATOM   16382 C  CD2 . LEU D  1  221 ? 57.288  87.679  33.329  1.00 57.61  ?  221 LEU D CD2 1 
ATOM   16383 N  N   . LYS D  1  222 ? 55.884  86.388  38.550  1.00 84.84  ?  222 LYS D N   1 
ATOM   16384 C  CA  . LYS D  1  222 ? 55.445  85.447  39.578  1.00 82.40  ?  222 LYS D CA  1 
ATOM   16385 C  C   . LYS D  1  222 ? 53.914  85.499  39.668  1.00 87.11  ?  222 LYS D C   1 
ATOM   16386 O  O   . LYS D  1  222 ? 53.270  84.456  39.780  1.00 80.43  ?  222 LYS D O   1 
ATOM   16387 C  CB  . LYS D  1  222 ? 56.027  85.831  40.947  1.00 79.94  ?  222 LYS D CB  1 
ATOM   16388 C  CG  . LYS D  1  222 ? 57.323  85.125  41.324  1.00 86.59  ?  222 LYS D CG  1 
ATOM   16389 C  CD  . LYS D  1  222 ? 57.546  85.110  42.841  1.00 120.55 ?  222 LYS D CD  1 
ATOM   16390 C  CE  . LYS D  1  222 ? 57.817  86.471  43.454  1.00 114.08 ?  222 LYS D CE  1 
ATOM   16391 N  NZ  . LYS D  1  222 ? 59.215  86.927  43.228  1.00 108.54 ?  222 LYS D NZ  1 
ATOM   16392 N  N   . TYR D  1  223 ? 53.334  86.716  39.631  1.00 80.93  ?  223 TYR D N   1 
ATOM   16393 C  CA  . TYR D  1  223 ? 51.891  86.895  39.709  1.00 70.82  ?  223 TYR D CA  1 
ATOM   16394 C  C   . TYR D  1  223 ? 51.198  86.218  38.533  1.00 78.12  ?  223 TYR D C   1 
ATOM   16395 O  O   . TYR D  1  223 ? 50.246  85.477  38.739  1.00 83.04  ?  223 TYR D O   1 
ATOM   16396 C  CB  . TYR D  1  223 ? 51.525  88.391  39.742  1.00 72.83  ?  223 TYR D CB  1 
ATOM   16397 C  CG  . TYR D  1  223 ? 50.044  88.641  39.939  1.00 70.70  ?  223 TYR D CG  1 
ATOM   16398 C  CD1 . TYR D  1  223 ? 49.170  88.650  38.862  1.00 73.11  ?  223 TYR D CD1 1 
ATOM   16399 C  CD2 . TYR D  1  223 ? 49.517  88.845  41.205  1.00 70.51  ?  223 TYR D CD2 1 
ATOM   16400 C  CE1 . TYR D  1  223 ? 47.809  88.868  39.038  1.00 77.89  ?  223 TYR D CE1 1 
ATOM   16401 C  CE2 . TYR D  1  223 ? 48.157  89.056  41.395  1.00 78.19  ?  223 TYR D CE2 1 
ATOM   16402 C  CZ  . TYR D  1  223 ? 47.305  89.072  40.308  1.00 80.96  ?  223 TYR D CZ  1 
ATOM   16403 O  OH  . TYR D  1  223 ? 45.957  89.283  40.485  1.00 80.98  ?  223 TYR D OH  1 
ATOM   16404 N  N   . THR D  1  224 ? 51.663  86.462  37.300  1.00 79.55  ?  224 THR D N   1 
ATOM   16405 C  CA  . THR D  1  224 ? 51.039  85.860  36.119  1.00 74.02  ?  224 THR D CA  1 
ATOM   16406 C  C   . THR D  1  224 ? 51.124  84.339  36.178  1.00 77.62  ?  224 THR D C   1 
ATOM   16407 O  O   . THR D  1  224 ? 50.151  83.652  35.867  1.00 71.65  ?  224 THR D O   1 
ATOM   16408 C  CB  . THR D  1  224 ? 51.684  86.394  34.835  1.00 63.42  ?  224 THR D CB  1 
ATOM   16409 O  OG1 . THR D  1  224 ? 53.088  86.139  34.868  1.00 72.45  ?  224 THR D OG1 1 
ATOM   16410 C  CG2 . THR D  1  224 ? 51.447  87.877  34.646  1.00 66.27  ?  224 THR D CG2 1 
ATOM   16411 N  N   . ALA D  1  225 ? 52.285  83.816  36.591  1.00 74.62  ?  225 ALA D N   1 
ATOM   16412 C  CA  . ALA D  1  225 ? 52.515  82.379  36.680  1.00 65.93  ?  225 ALA D CA  1 
ATOM   16413 C  C   . ALA D  1  225 ? 51.660  81.693  37.737  1.00 74.36  ?  225 ALA D C   1 
ATOM   16414 O  O   . ALA D  1  225 ? 51.208  80.575  37.506  1.00 87.05  ?  225 ALA D O   1 
ATOM   16415 C  CB  . ALA D  1  225 ? 53.984  82.107  36.957  1.00 67.25  ?  225 ALA D CB  1 
ATOM   16416 N  N   . GLU D  1  226 ? 51.440  82.338  38.889  1.00 69.58  ?  226 GLU D N   1 
ATOM   16417 C  CA  . GLU D  1  226 ? 50.669  81.734  39.975  1.00 72.75  ?  226 GLU D CA  1 
ATOM   16418 C  C   . GLU D  1  226 ? 49.196  82.136  40.023  1.00 73.75  ?  226 GLU D C   1 
ATOM   16419 O  O   . GLU D  1  226 ? 48.384  81.365  40.530  1.00 81.13  ?  226 GLU D O   1 
ATOM   16420 C  CB  . GLU D  1  226 ? 51.301  82.102  41.324  1.00 71.06  ?  226 GLU D CB  1 
ATOM   16421 C  CG  . GLU D  1  226 ? 52.761  81.710  41.471  1.00 87.87  ?  226 GLU D CG  1 
ATOM   16422 C  CD  . GLU D  1  226 ? 53.383  82.122  42.793  1.00 106.53 ?  226 GLU D CD  1 
ATOM   16423 O  OE1 . GLU D  1  226 ? 52.761  82.925  43.527  1.00 113.95 ?  226 GLU D OE1 1 
ATOM   16424 O  OE2 . GLU D  1  226 ? 54.500  81.643  43.092  1.00 122.75 ?  226 GLU D OE2 1 
ATOM   16425 N  N   . ARG D  1  227 ? 48.846  83.334  39.544  1.00 70.27  ?  227 ARG D N   1 
ATOM   16426 C  CA  . ARG D  1  227 ? 47.473  83.820  39.632  1.00 71.78  ?  227 ARG D CA  1 
ATOM   16427 C  C   . ARG D  1  227 ? 46.686  83.881  38.320  1.00 73.89  ?  227 ARG D C   1 
ATOM   16428 O  O   . ARG D  1  227 ? 45.480  83.650  38.344  1.00 89.99  ?  227 ARG D O   1 
ATOM   16429 C  CB  . ARG D  1  227 ? 47.455  85.231  40.247  1.00 75.78  ?  227 ARG D CB  1 
ATOM   16430 C  CG  . ARG D  1  227 ? 48.277  85.382  41.526  1.00 78.05  ?  227 ARG D CG  1 
ATOM   16431 C  CD  . ARG D  1  227 ? 47.523  84.945  42.763  1.00 89.90  ?  227 ARG D CD  1 
ATOM   16432 N  NE  . ARG D  1  227 ? 48.436  84.682  43.875  1.00 110.38 ?  227 ARG D NE  1 
ATOM   16433 C  CZ  . ARG D  1  227 ? 48.086  84.105  45.021  1.00 122.32 ?  227 ARG D CZ  1 
ATOM   16434 N  NH1 . ARG D  1  227 ? 46.829  83.721  45.225  1.00 122.11 ?  227 ARG D NH1 1 
ATOM   16435 N  NH2 . ARG D  1  227 ? 48.990  83.906  45.974  1.00 110.10 ?  227 ARG D NH2 1 
ATOM   16436 N  N   . VAL D  1  228 ? 47.326  84.222  37.191  1.00 72.52  ?  228 VAL D N   1 
ATOM   16437 C  CA  . VAL D  1  228 ? 46.600  84.324  35.919  1.00 62.07  ?  228 VAL D CA  1 
ATOM   16438 C  C   . VAL D  1  228 ? 46.522  82.931  35.298  1.00 64.78  ?  228 VAL D C   1 
ATOM   16439 O  O   . VAL D  1  228 ? 47.531  82.435  34.813  1.00 70.64  ?  228 VAL D O   1 
ATOM   16440 C  CB  . VAL D  1  228 ? 47.227  85.345  34.947  1.00 67.25  ?  228 VAL D CB  1 
ATOM   16441 C  CG1 . VAL D  1  228 ? 46.449  85.385  33.635  1.00 61.20  ?  228 VAL D CG1 1 
ATOM   16442 C  CG2 . VAL D  1  228 ? 47.277  86.736  35.577  1.00 67.77  ?  228 VAL D CG2 1 
ATOM   16443 N  N   . PRO D  1  229 ? 45.330  82.290  35.237  1.00 65.39  ?  229 PRO D N   1 
ATOM   16444 C  CA  . PRO D  1  229 ? 45.208  80.928  34.711  1.00 68.84  ?  229 PRO D CA  1 
ATOM   16445 C  C   . PRO D  1  229 ? 45.160  80.895  33.177  1.00 71.02  ?  229 PRO D C   1 
ATOM   16446 O  O   . PRO D  1  229 ? 44.157  80.469  32.637  1.00 75.88  ?  229 PRO D O   1 
ATOM   16447 C  CB  . PRO D  1  229 ? 43.854  80.474  35.269  1.00 63.38  ?  229 PRO D CB  1 
ATOM   16448 C  CG  . PRO D  1  229 ? 43.033  81.741  35.284  1.00 67.83  ?  229 PRO D CG  1 
ATOM   16449 C  CD  . PRO D  1  229 ? 44.023  82.829  35.644  1.00 69.27  ?  229 PRO D CD  1 
ATOM   16450 N  N   . ALA D  1  230 ? 46.279  81.264  32.548  1.00 69.10  ?  230 ALA D N   1 
ATOM   16451 C  CA  . ALA D  1  230 ? 46.328  81.324  31.071  1.00 68.87  ?  230 ALA D CA  1 
ATOM   16452 C  C   . ALA D  1  230 ? 47.163  80.189  30.485  1.00 72.72  ?  230 ALA D C   1 
ATOM   16453 O  O   . ALA D  1  230 ? 48.047  79.669  31.192  1.00 69.76  ?  230 ALA D O   1 
ATOM   16454 C  CB  . ALA D  1  230 ? 46.899  82.647  30.635  1.00 59.02  ?  230 ALA D CB  1 
ATOM   16455 N  N   . PHE D  1  231 ? 46.886  79.839  29.233  1.00 68.24  ?  231 PHE D N   1 
ATOM   16456 C  CA  . PHE D  1  231 ? 47.644  78.825  28.502  1.00 66.42  ?  231 PHE D CA  1 
ATOM   16457 C  C   . PHE D  1  231 ? 47.497  79.085  27.005  1.00 66.11  ?  231 PHE D C   1 
ATOM   16458 O  O   . PHE D  1  231 ? 46.529  79.716  26.587  1.00 72.48  ?  231 PHE D O   1 
ATOM   16459 C  CB  . PHE D  1  231 ? 47.177  77.409  28.859  1.00 62.66  ?  231 PHE D CB  1 
ATOM   16460 C  CG  . PHE D  1  231 ? 45.721  77.125  28.583  1.00 65.94  ?  231 PHE D CG  1 
ATOM   16461 C  CD1 . PHE D  1  231 ? 45.285  76.840  27.301  1.00 70.35  ?  231 PHE D CD1 1 
ATOM   16462 C  CD2 . PHE D  1  231 ? 44.801  77.078  29.614  1.00 71.88  ?  231 PHE D CD2 1 
ATOM   16463 C  CE1 . PHE D  1  231 ? 43.948  76.569  27.049  1.00 78.43  ?  231 PHE D CE1 1 
ATOM   16464 C  CE2 . PHE D  1  231 ? 43.466  76.793  29.362  1.00 75.57  ?  231 PHE D CE2 1 
ATOM   16465 C  CZ  . PHE D  1  231 ? 43.048  76.536  28.082  1.00 79.00  ?  231 PHE D CZ  1 
ATOM   16466 N  N   . VAL D  1  232 ? 48.447  78.614  26.200  1.00 65.41  ?  232 VAL D N   1 
ATOM   16467 C  CA  . VAL D  1  232 ? 48.398  78.829  24.758  1.00 66.03  ?  232 VAL D CA  1 
ATOM   16468 C  C   . VAL D  1  232 ? 48.073  77.530  24.035  1.00 74.27  ?  232 VAL D C   1 
ATOM   16469 O  O   . VAL D  1  232 ? 48.440  76.451  24.492  1.00 70.56  ?  232 VAL D O   1 
ATOM   16470 C  CB  . VAL D  1  232 ? 49.724  79.437  24.246  1.00 56.81  ?  232 VAL D CB  1 
ATOM   16471 C  CG1 . VAL D  1  232 ? 49.645  79.760  22.757  1.00 57.99  ?  232 VAL D CG1 1 
ATOM   16472 C  CG2 . VAL D  1  232 ? 50.096  80.679  25.045  1.00 61.02  ?  232 VAL D CG2 1 
ATOM   16473 N  N   . ASN D  1  233 ? 47.342  77.650  22.922  1.00 67.49  ?  233 ASN D N   1 
ATOM   16474 C  CA  . ASN D  1  233 ? 46.996  76.468  22.090  1.00 65.64  ?  233 ASN D CA  1 
ATOM   16475 C  C   . ASN D  1  233 ? 47.376  76.799  20.645  1.00 77.89  ?  233 ASN D C   1 
ATOM   16476 O  O   . ASN D  1  233 ? 46.530  77.371  19.936  1.00 85.55  ?  233 ASN D O   1 
ATOM   16477 C  CB  . ASN D  1  233 ? 45.522  76.081  22.226  1.00 64.46  ?  233 ASN D CB  1 
ATOM   16478 C  CG  . ASN D  1  233 ? 45.246  75.184  23.413  1.00 76.02  ?  233 ASN D CG  1 
ATOM   16479 O  OD1 . ASN D  1  233 ? 45.956  75.233  24.415  1.00 90.32  ?  233 ASN D OD1 1 
ATOM   16480 N  ND2 . ASN D  1  233 ? 44.215  74.363  23.312  1.00 60.60  ?  233 ASN D ND2 1 
ATOM   16481 N  N   . ALA D  1  234 ? 48.600  76.462  20.234  1.00 72.67  ?  234 ALA D N   1 
ATOM   16482 C  CA  . ALA D  1  234 ? 49.096  76.788  18.899  1.00 66.91  ?  234 ALA D CA  1 
ATOM   16483 C  C   . ALA D  1  234 ? 48.774  75.687  17.894  1.00 75.28  ?  234 ALA D C   1 
ATOM   16484 O  O   . ALA D  1  234 ? 49.279  74.575  18.019  1.00 82.52  ?  234 ALA D O   1 
ATOM   16485 C  CB  . ALA D  1  234 ? 50.593  77.031  18.944  1.00 67.52  ?  234 ALA D CB  1 
ATOM   16486 N  N   . PHE D  1  235 ? 47.938  76.000  16.889  1.00 75.07  ?  235 PHE D N   1 
ATOM   16487 C  CA  . PHE D  1  235 ? 47.536  75.041  15.858  1.00 83.03  ?  235 PHE D CA  1 
ATOM   16488 C  C   . PHE D  1  235 ? 48.199  75.336  14.514  1.00 82.63  ?  235 PHE D C   1 
ATOM   16489 O  O   . PHE D  1  235 ? 48.530  76.483  14.222  1.00 77.88  ?  235 PHE D O   1 
ATOM   16490 C  CB  . PHE D  1  235 ? 46.010  75.051  15.694  1.00 84.86  ?  235 PHE D CB  1 
ATOM   16491 C  CG  . PHE D  1  235 ? 45.259  74.625  16.932  1.00 85.33  ?  235 PHE D CG  1 
ATOM   16492 C  CD1 . PHE D  1  235 ? 45.326  73.321  17.389  1.00 77.80  ?  235 PHE D CD1 1 
ATOM   16493 C  CD2 . PHE D  1  235 ? 44.480  75.528  17.635  1.00 91.36  ?  235 PHE D CD2 1 
ATOM   16494 C  CE1 . PHE D  1  235 ? 44.637  72.933  18.529  1.00 86.85  ?  235 PHE D CE1 1 
ATOM   16495 C  CE2 . PHE D  1  235 ? 43.790  75.136  18.774  1.00 77.76  ?  235 PHE D CE2 1 
ATOM   16496 C  CZ  . PHE D  1  235 ? 43.873  73.842  19.214  1.00 80.61  ?  235 PHE D CZ  1 
ATOM   16497 N  N   . GLY D  1  236 ? 48.367  74.295  13.703  1.00 79.54  ?  236 GLY D N   1 
ATOM   16498 C  CA  . GLY D  1  236 ? 48.984  74.415  12.388  1.00 80.04  ?  236 GLY D CA  1 
ATOM   16499 C  C   . GLY D  1  236 ? 50.480  74.653  12.461  1.00 77.00  ?  236 GLY D C   1 
ATOM   16500 O  O   . GLY D  1  236 ? 51.029  74.796  13.554  1.00 83.25  ?  236 GLY D O   1 
ATOM   16501 N  N   . PRO D  1  237 ? 51.184  74.716  11.313  1.00 77.34  ?  237 PRO D N   1 
ATOM   16502 C  CA  . PRO D  1  237 ? 52.642  74.942  11.358  1.00 82.55  ?  237 PRO D CA  1 
ATOM   16503 C  C   . PRO D  1  237 ? 53.074  76.135  12.212  1.00 74.88  ?  237 PRO D C   1 
ATOM   16504 O  O   . PRO D  1  237 ? 52.433  77.186  12.204  1.00 85.08  ?  237 PRO D O   1 
ATOM   16505 C  CB  . PRO D  1  237 ? 53.017  75.136  9.888   1.00 77.04  ?  237 PRO D CB  1 
ATOM   16506 C  CG  . PRO D  1  237 ? 51.965  74.431  9.131   1.00 77.34  ?  237 PRO D CG  1 
ATOM   16507 C  CD  . PRO D  1  237 ? 50.703  74.564  9.927   1.00 69.05  ?  237 PRO D CD  1 
ATOM   16508 N  N   . LEU D  1  238 ? 54.170  75.961  12.954  1.00 72.13  ?  238 LEU D N   1 
ATOM   16509 C  CA  . LEU D  1  238 ? 54.700  76.996  13.837  1.00 80.40  ?  238 LEU D CA  1 
ATOM   16510 C  C   . LEU D  1  238 ? 55.955  77.620  13.235  1.00 77.45  ?  238 LEU D C   1 
ATOM   16511 O  O   . LEU D  1  238 ? 56.911  76.905  12.939  1.00 92.73  ?  238 LEU D O   1 
ATOM   16512 C  CB  . LEU D  1  238 ? 55.055  76.372  15.202  1.00 82.61  ?  238 LEU D CB  1 
ATOM   16513 C  CG  . LEU D  1  238 ? 54.008  76.444  16.319  1.00 90.20  ?  238 LEU D CG  1 
ATOM   16514 C  CD1 . LEU D  1  238 ? 52.711  75.767  15.930  1.00 79.13  ?  238 LEU D CD1 1 
ATOM   16515 C  CD2 . LEU D  1  238 ? 54.538  75.800  17.588  1.00 73.37  ?  238 LEU D CD2 1 
ATOM   16516 N  N   . SER D  1  239 ? 55.967  78.943  13.062  1.00 67.66  ?  239 SER D N   1 
ATOM   16517 C  CA  . SER D  1  239 ? 57.138  79.631  12.525  1.00 69.21  ?  239 SER D CA  1 
ATOM   16518 C  C   . SER D  1  239 ? 58.124  79.900  13.673  1.00 84.20  ?  239 SER D C   1 
ATOM   16519 O  O   . SER D  1  239 ? 57.759  79.729  14.840  1.00 88.67  ?  239 SER D O   1 
ATOM   16520 C  CB  . SER D  1  239 ? 56.721  80.947  11.877  1.00 76.47  ?  239 SER D CB  1 
ATOM   16521 O  OG  . SER D  1  239 ? 56.213  81.853  12.842  1.00 77.00  ?  239 SER D OG  1 
ATOM   16522 N  N   . GLU D  1  240 ? 59.361  80.337  13.363  1.00 83.23  ?  240 GLU D N   1 
ATOM   16523 C  CA  . GLU D  1  240 ? 60.346  80.637  14.412  1.00 77.94  ?  240 GLU D CA  1 
ATOM   16524 C  C   . GLU D  1  240 ? 59.823  81.763  15.321  1.00 78.60  ?  240 GLU D C   1 
ATOM   16525 O  O   . GLU D  1  240 ? 60.011  81.714  16.537  1.00 63.10  ?  240 GLU D O   1 
ATOM   16526 C  CB  . GLU D  1  240 ? 61.700  81.046  13.808  1.00 78.03  ?  240 GLU D CB  1 
ATOM   16527 C  CG  . GLU D  1  240 ? 62.371  79.960  12.986  1.00 71.33  ?  240 GLU D CG  1 
ATOM   16528 C  CD  . GLU D  1  240 ? 62.165  80.053  11.486  1.00 91.53  ?  240 GLU D CD  1 
ATOM   16529 O  OE1 . GLU D  1  240 ? 61.392  80.931  11.035  1.00 97.35  ?  240 GLU D OE1 1 
ATOM   16530 O  OE2 . GLU D  1  240 ? 62.781  79.241  10.758  1.00 96.67  ?  240 GLU D OE2 1 
ATOM   16531 N  N   . LEU D  1  241 ? 59.157  82.763  14.724  1.00 70.01  ?  241 LEU D N   1 
ATOM   16532 C  CA  . LEU D  1  241 ? 58.587  83.891  15.459  1.00 67.99  ?  241 LEU D CA  1 
ATOM   16533 C  C   . LEU D  1  241 ? 57.531  83.404  16.449  1.00 73.91  ?  241 LEU D C   1 
ATOM   16534 O  O   . LEU D  1  241 ? 57.500  83.860  17.592  1.00 80.38  ?  241 LEU D O   1 
ATOM   16535 C  CB  . LEU D  1  241 ? 57.947  84.874  14.472  1.00 65.95  ?  241 LEU D CB  1 
ATOM   16536 C  CG  . LEU D  1  241 ? 57.422  86.179  15.065  1.00 59.24  ?  241 LEU D CG  1 
ATOM   16537 C  CD1 . LEU D  1  241 ? 58.535  87.188  15.223  1.00 71.29  ?  241 LEU D CD1 1 
ATOM   16538 C  CD2 . LEU D  1  241 ? 56.334  86.763  14.198  1.00 66.35  ?  241 LEU D CD2 1 
ATOM   16539 N  N   . VAL D  1  242 ? 56.667  82.475  16.008  1.00 76.58  ?  242 VAL D N   1 
ATOM   16540 C  CA  . VAL D  1  242 ? 55.613  81.921  16.857  1.00 72.70  ?  242 VAL D CA  1 
ATOM   16541 C  C   . VAL D  1  242 ? 56.231  81.139  18.016  1.00 71.35  ?  242 VAL D C   1 
ATOM   16542 O  O   . VAL D  1  242 ? 55.747  81.244  19.140  1.00 69.34  ?  242 VAL D O   1 
ATOM   16543 C  CB  . VAL D  1  242 ? 54.622  81.054  16.038  1.00 69.96  ?  242 VAL D CB  1 
ATOM   16544 C  CG1 . VAL D  1  242 ? 53.712  80.239  16.952  1.00 64.18  ?  242 VAL D CG1 1 
ATOM   16545 C  CG2 . VAL D  1  242 ? 53.789  81.921  15.097  1.00 75.04  ?  242 VAL D CG2 1 
ATOM   16546 N  N   . VAL D  1  243 ? 57.303  80.373  17.762  1.00 74.27  ?  243 VAL D N   1 
ATOM   16547 C  CA  . VAL D  1  243 ? 57.959  79.612  18.827  1.00 67.39  ?  243 VAL D CA  1 
ATOM   16548 C  C   . VAL D  1  243 ? 58.558  80.582  19.865  1.00 74.60  ?  243 VAL D C   1 
ATOM   16549 O  O   . VAL D  1  243 ? 58.526  80.287  21.057  1.00 80.43  ?  243 VAL D O   1 
ATOM   16550 C  CB  . VAL D  1  243 ? 59.008  78.622  18.266  1.00 62.47  ?  243 VAL D CB  1 
ATOM   16551 C  CG1 . VAL D  1  243 ? 59.808  77.973  19.391  1.00 55.71  ?  243 VAL D CG1 1 
ATOM   16552 C  CG2 . VAL D  1  243 ? 58.339  77.555  17.405  1.00 56.88  ?  243 VAL D CG2 1 
ATOM   16553 N  N   . SER D  1  244 ? 59.071  81.746  19.426  1.00 70.30  ?  244 SER D N   1 
ATOM   16554 C  CA  . SER D  1  244 ? 59.617  82.750  20.341  1.00 65.82  ?  244 SER D CA  1 
ATOM   16555 C  C   . SER D  1  244 ? 58.504  83.316  21.213  1.00 78.06  ?  244 SER D C   1 
ATOM   16556 O  O   . SER D  1  244 ? 58.708  83.541  22.406  1.00 70.58  ?  244 SER D O   1 
ATOM   16557 C  CB  . SER D  1  244 ? 60.276  83.873  19.557  1.00 60.59  ?  244 SER D CB  1 
ATOM   16558 O  OG  . SER D  1  244 ? 61.391  83.352  18.857  1.00 90.62  ?  244 SER D OG  1 
ATOM   16559 N  N   . ALA D  1  245 ? 57.318  83.535  20.623  1.00 71.97  ?  245 ALA D N   1 
ATOM   16560 C  CA  . ALA D  1  245 ? 56.160  84.014  21.370  1.00 69.28  ?  245 ALA D CA  1 
ATOM   16561 C  C   . ALA D  1  245 ? 55.774  82.946  22.419  1.00 69.95  ?  245 ALA D C   1 
ATOM   16562 O  O   . ALA D  1  245 ? 55.418  83.287  23.543  1.00 69.76  ?  245 ALA D O   1 
ATOM   16563 C  CB  . ALA D  1  245 ? 55.002  84.271  20.423  1.00 55.12  ?  245 ALA D CB  1 
ATOM   16564 N  N   . GLY D  1  246 ? 55.888  81.669  22.050  1.00 66.02  ?  246 GLY D N   1 
ATOM   16565 C  CA  . GLY D  1  246 ? 55.618  80.552  22.946  1.00 68.51  ?  246 GLY D CA  1 
ATOM   16566 C  C   . GLY D  1  246 ? 56.564  80.578  24.130  1.00 74.29  ?  246 GLY D C   1 
ATOM   16567 O  O   . GLY D  1  246 ? 56.158  80.281  25.255  1.00 79.60  ?  246 GLY D O   1 
ATOM   16568 N  N   . ALA D  1  247 ? 57.834  80.958  23.889  1.00 69.75  ?  247 ALA D N   1 
ATOM   16569 C  CA  . ALA D  1  247 ? 58.831  81.091  24.949  1.00 69.18  ?  247 ALA D CA  1 
ATOM   16570 C  C   . ALA D  1  247 ? 58.436  82.272  25.864  1.00 71.68  ?  247 ALA D C   1 
ATOM   16571 O  O   . ALA D  1  247 ? 58.610  82.189  27.078  1.00 74.87  ?  247 ALA D O   1 
ATOM   16572 C  CB  . ALA D  1  247 ? 60.209  81.320  24.350  1.00 61.06  ?  247 ALA D CB  1 
ATOM   16573 N  N   . GLY D  1  248 ? 57.893  83.341  25.278  1.00 63.40  ?  248 GLY D N   1 
ATOM   16574 C  CA  . GLY D  1  248 ? 57.431  84.498  26.032  1.00 64.00  ?  248 GLY D CA  1 
ATOM   16575 C  C   . GLY D  1  248 ? 56.263  84.124  26.921  1.00 63.60  ?  248 GLY D C   1 
ATOM   16576 O  O   . GLY D  1  248 ? 56.195  84.543  28.078  1.00 66.50  ?  248 GLY D O   1 
ATOM   16577 N  N   . ALA D  1  249 ? 55.341  83.309  26.393  1.00 58.21  ?  249 ALA D N   1 
ATOM   16578 C  CA  . ALA D  1  249 ? 54.193  82.830  27.156  1.00 57.86  ?  249 ALA D CA  1 
ATOM   16579 C  C   . ALA D  1  249 ? 54.696  81.938  28.297  1.00 71.60  ?  249 ALA D C   1 
ATOM   16580 O  O   . ALA D  1  249 ? 54.198  82.040  29.413  1.00 75.84  ?  249 ALA D O   1 
ATOM   16581 C  CB  . ALA D  1  249 ? 53.257  82.048  26.250  1.00 53.62  ?  249 ALA D CB  1 
ATOM   16582 N  N   . ILE D  1  250 ? 55.696  81.081  28.020  1.00 68.57  ?  250 ILE D N   1 
ATOM   16583 C  CA  . ILE D  1  250 ? 56.297  80.204  29.027  1.00 68.64  ?  250 ILE D CA  1 
ATOM   16584 C  C   . ILE D  1  250 ? 56.965  81.062  30.120  1.00 70.90  ?  250 ILE D C   1 
ATOM   16585 O  O   . ILE D  1  250 ? 56.909  80.697  31.293  1.00 67.85  ?  250 ILE D O   1 
ATOM   16586 C  CB  . ILE D  1  250 ? 57.286  79.189  28.365  1.00 68.59  ?  250 ILE D CB  1 
ATOM   16587 C  CG1 . ILE D  1  250 ? 56.500  78.094  27.604  1.00 72.53  ?  250 ILE D CG1 1 
ATOM   16588 C  CG2 . ILE D  1  250 ? 58.214  78.556  29.411  1.00 54.14  ?  250 ILE D CG2 1 
ATOM   16589 C  CD1 . ILE D  1  250 ? 57.304  77.266  26.639  1.00 54.96  ?  250 ILE D CD1 1 
ATOM   16590 N  N   . ALA D  1  251 ? 57.580  82.204  29.743  1.00 67.89  ?  251 ALA D N   1 
ATOM   16591 C  CA  . ALA D  1  251 ? 58.216  83.117  30.699  1.00 64.02  ?  251 ALA D CA  1 
ATOM   16592 C  C   . ALA D  1  251 ? 57.183  83.664  31.695  1.00 67.28  ?  251 ALA D C   1 
ATOM   16593 O  O   . ALA D  1  251 ? 57.518  83.902  32.855  1.00 72.77  ?  251 ALA D O   1 
ATOM   16594 C  CB  . ALA D  1  251 ? 58.889  84.263  29.960  1.00 62.10  ?  251 ALA D CB  1 
ATOM   16595 N  N   . LEU D  1  252 ? 55.927  83.850  31.254  1.00 69.67  ?  252 LEU D N   1 
ATOM   16596 C  CA  . LEU D  1  252 ? 54.856  84.322  32.136  1.00 73.40  ?  252 LEU D CA  1 
ATOM   16597 C  C   . LEU D  1  252 ? 54.236  83.162  32.942  1.00 65.87  ?  252 LEU D C   1 
ATOM   16598 O  O   . LEU D  1  252 ? 53.269  83.382  33.660  1.00 69.54  ?  252 LEU D O   1 
ATOM   16599 C  CB  . LEU D  1  252 ? 53.737  84.998  31.323  1.00 71.52  ?  252 LEU D CB  1 
ATOM   16600 C  CG  . LEU D  1  252 ? 54.148  86.059  30.304  1.00 72.81  ?  252 LEU D CG  1 
ATOM   16601 C  CD1 . LEU D  1  252 ? 52.990  86.405  29.391  1.00 66.52  ?  252 LEU D CD1 1 
ATOM   16602 C  CD2 . LEU D  1  252 ? 54.666  87.311  30.988  1.00 63.20  ?  252 LEU D CD2 1 
ATOM   16603 N  N   . GLY D  1  253 ? 54.772  81.953  32.806  1.00 68.21  ?  253 GLY D N   1 
ATOM   16604 C  CA  . GLY D  1  253 ? 54.275  80.774  33.499  1.00 70.51  ?  253 GLY D CA  1 
ATOM   16605 C  C   . GLY D  1  253 ? 53.099  80.111  32.810  1.00 68.04  ?  253 GLY D C   1 
ATOM   16606 O  O   . GLY D  1  253 ? 52.439  79.262  33.409  1.00 75.09  ?  253 GLY D O   1 
ATOM   16607 N  N   . PHE D  1  254 ? 52.828  80.469  31.548  1.00 70.95  ?  254 PHE D N   1 
ATOM   16608 C  CA  . PHE D  1  254 ? 51.710  79.889  30.811  1.00 70.67  ?  254 PHE D CA  1 
ATOM   16609 C  C   . PHE D  1  254 ? 52.178  78.710  29.951  1.00 66.32  ?  254 PHE D C   1 
ATOM   16610 O  O   . PHE D  1  254 ? 53.014  78.909  29.066  1.00 59.28  ?  254 PHE D O   1 
ATOM   16611 C  CB  . PHE D  1  254 ? 51.057  80.942  29.900  1.00 61.92  ?  254 PHE D CB  1 
ATOM   16612 C  CG  . PHE D  1  254 ? 50.616  82.223  30.570  1.00 64.19  ?  254 PHE D CG  1 
ATOM   16613 C  CD1 . PHE D  1  254 ? 50.266  82.243  31.911  1.00 72.71  ?  254 PHE D CD1 1 
ATOM   16614 C  CD2 . PHE D  1  254 ? 50.501  83.396  29.845  1.00 59.08  ?  254 PHE D CD2 1 
ATOM   16615 C  CE1 . PHE D  1  254 ? 49.847  83.420  32.517  1.00 75.34  ?  254 PHE D CE1 1 
ATOM   16616 C  CE2 . PHE D  1  254 ? 50.075  84.568  30.454  1.00 59.55  ?  254 PHE D CE2 1 
ATOM   16617 C  CZ  . PHE D  1  254 ? 49.754  84.574  31.785  1.00 67.02  ?  254 PHE D CZ  1 
ATOM   16618 N  N   . PRO D  1  255 ? 51.655  77.482  30.157  1.00 66.07  ?  255 PRO D N   1 
ATOM   16619 C  CA  . PRO D  1  255 ? 52.079  76.373  29.289  1.00 54.75  ?  255 PRO D CA  1 
ATOM   16620 C  C   . PRO D  1  255 ? 51.618  76.591  27.851  1.00 54.59  ?  255 PRO D C   1 
ATOM   16621 O  O   . PRO D  1  255 ? 50.609  77.249  27.619  1.00 70.41  ?  255 PRO D O   1 
ATOM   16622 C  CB  . PRO D  1  255 ? 51.420  75.129  29.904  1.00 62.02  ?  255 PRO D CB  1 
ATOM   16623 C  CG  . PRO D  1  255 ? 50.747  75.567  31.136  1.00 69.67  ?  255 PRO D CG  1 
ATOM   16624 C  CD  . PRO D  1  255 ? 50.644  77.052  31.142  1.00 71.84  ?  255 PRO D CD  1 
ATOM   16625 N  N   . VAL D  1  256 ? 52.365  76.043  26.890  1.00 65.15  ?  256 VAL D N   1 
ATOM   16626 C  CA  . VAL D  1  256 ? 52.057  76.153  25.468  1.00 63.76  ?  256 VAL D CA  1 
ATOM   16627 C  C   . VAL D  1  256 ? 51.815  74.754  24.920  1.00 64.30  ?  256 VAL D C   1 
ATOM   16628 O  O   . VAL D  1  256 ? 52.723  73.931  24.958  1.00 83.60  ?  256 VAL D O   1 
ATOM   16629 C  CB  . VAL D  1  256 ? 53.220  76.820  24.705  1.00 57.84  ?  256 VAL D CB  1 
ATOM   16630 C  CG1 . VAL D  1  256 ? 52.927  76.868  23.215  1.00 65.35  ?  256 VAL D CG1 1 
ATOM   16631 C  CG2 . VAL D  1  256 ? 53.510  78.215  25.246  1.00 59.09  ?  256 VAL D CG2 1 
ATOM   16632 N  N   . LEU D  1  257 ? 50.611  74.473  24.417  1.00 67.05  ?  257 LEU D N   1 
ATOM   16633 C  CA  . LEU D  1  257 ? 50.301  73.158  23.860  1.00 63.71  ?  257 LEU D CA  1 
ATOM   16634 C  C   . LEU D  1  257 ? 50.071  73.298  22.364  1.00 76.14  ?  257 LEU D C   1 
ATOM   16635 O  O   . LEU D  1  257 ? 49.383  74.221  21.934  1.00 85.56  ?  257 LEU D O   1 
ATOM   16636 C  CB  . LEU D  1  257 ? 49.069  72.569  24.539  1.00 57.57  ?  257 LEU D CB  1 
ATOM   16637 C  CG  . LEU D  1  257 ? 49.114  72.501  26.083  1.00 63.80  ?  257 LEU D CG  1 
ATOM   16638 C  CD1 . LEU D  1  257 ? 48.319  73.638  26.707  1.00 62.76  ?  257 LEU D CD1 1 
ATOM   16639 C  CD2 . LEU D  1  257 ? 48.584  71.168  26.595  1.00 67.70  ?  257 LEU D CD2 1 
ATOM   16640 N  N   . THR D  1  258 ? 50.649  72.394  21.566  1.00 68.41  ?  258 THR D N   1 
ATOM   16641 C  CA  . THR D  1  258 ? 50.537  72.467  20.112  1.00 77.14  ?  258 THR D CA  1 
ATOM   16642 C  C   . THR D  1  258 ? 50.241  71.120  19.472  1.00 78.29  ?  258 THR D C   1 
ATOM   16643 O  O   . THR D  1  258 ? 50.554  70.083  20.034  1.00 75.07  ?  258 THR D O   1 
ATOM   16644 C  CB  . THR D  1  258 ? 51.841  73.050  19.524  1.00 75.19  ?  258 THR D CB  1 
ATOM   16645 O  OG1 . THR D  1  258 ? 51.792  72.998  18.096  1.00 84.75  ?  258 THR D OG1 1 
ATOM   16646 C  CG2 . THR D  1  258 ? 53.085  72.319  20.004  1.00 57.93  ?  258 THR D CG2 1 
ATOM   16647 N  N   . ASP D  1  259 ? 49.651  71.145  18.279  1.00 79.61  ?  259 ASP D N   1 
ATOM   16648 C  CA  . ASP D  1  259 ? 49.363  69.922  17.528  1.00 73.47  ?  259 ASP D CA  1 
ATOM   16649 C  C   . ASP D  1  259 ? 50.585  69.506  16.677  1.00 79.99  ?  259 ASP D C   1 
ATOM   16650 O  O   . ASP D  1  259 ? 50.609  68.389  16.160  1.00 92.52  ?  259 ASP D O   1 
ATOM   16651 C  CB  . ASP D  1  259 ? 48.113  70.101  16.638  1.00 82.87  ?  259 ASP D CB  1 
ATOM   16652 C  CG  . ASP D  1  259 ? 48.172  71.251  15.645  1.00 83.65  ?  259 ASP D CG  1 
ATOM   16653 O  OD1 . ASP D  1  259 ? 49.161  72.014  15.676  1.00 89.79  ?  259 ASP D OD1 1 
ATOM   16654 O  OD2 . ASP D  1  259 ? 47.223  71.395  14.844  1.00 79.30  ?  259 ASP D OD2 1 
ATOM   16655 N  N   . GLN D  1  260 ? 51.597  70.398  16.539  1.00 70.24  ?  260 GLN D N   1 
ATOM   16656 C  CA  . GLN D  1  260 ? 52.801  70.146  15.749  1.00 83.66  ?  260 GLN D CA  1 
ATOM   16657 C  C   . GLN D  1  260 ? 53.888  69.487  16.589  1.00 84.43  ?  260 GLN D C   1 
ATOM   16658 O  O   . GLN D  1  260 ? 53.926  69.668  17.803  1.00 77.88  ?  260 GLN D O   1 
ATOM   16659 C  CB  . GLN D  1  260 ? 53.340  71.466  15.171  1.00 70.67  ?  260 GLN D CB  1 
ATOM   16660 C  CG  . GLN D  1  260 ? 52.351  72.212  14.288  1.00 65.98  ?  260 GLN D CG  1 
ATOM   16661 C  CD  . GLN D  1  260 ? 52.130  71.540  12.959  1.00 85.63  ?  260 GLN D CD  1 
ATOM   16662 O  OE1 . GLN D  1  260 ? 53.068  71.329  12.183  1.00 105.26 ?  260 GLN D OE1 1 
ATOM   16663 N  NE2 . GLN D  1  260 ? 50.883  71.195  12.652  1.00 96.92  ?  260 GLN D NE2 1 
ATOM   16664 N  N   . VAL D  1  261 ? 54.789  68.739  15.937  1.00 87.22  ?  261 VAL D N   1 
ATOM   16665 C  CA  . VAL D  1  261 ? 55.886  68.066  16.629  1.00 78.65  ?  261 VAL D CA  1 
ATOM   16666 C  C   . VAL D  1  261 ? 56.960  69.094  16.979  1.00 81.50  ?  261 VAL D C   1 
ATOM   16667 O  O   . VAL D  1  261 ? 57.508  69.742  16.086  1.00 81.58  ?  261 VAL D O   1 
ATOM   16668 C  CB  . VAL D  1  261 ? 56.470  66.915  15.777  1.00 64.86  ?  261 VAL D CB  1 
ATOM   16669 C  CG1 . VAL D  1  261 ? 57.770  66.391  16.378  1.00 73.31  ?  261 VAL D CG1 1 
ATOM   16670 C  CG2 . VAL D  1  261 ? 55.456  65.785  15.623  1.00 75.32  ?  261 VAL D CG2 1 
ATOM   16671 N  N   . VAL D  1  262 ? 57.255  69.248  18.279  1.00 78.38  ?  262 VAL D N   1 
ATOM   16672 C  CA  . VAL D  1  262 ? 58.261  70.198  18.757  1.00 82.72  ?  262 VAL D CA  1 
ATOM   16673 C  C   . VAL D  1  262 ? 59.097  69.556  19.881  1.00 79.40  ?  262 VAL D C   1 
ATOM   16674 O  O   . VAL D  1  262 ? 58.664  68.550  20.445  1.00 79.99  ?  262 VAL D O   1 
ATOM   16675 C  CB  . VAL D  1  262 ? 57.606  71.519  19.265  1.00 70.51  ?  262 VAL D CB  1 
ATOM   16676 C  CG1 . VAL D  1  262 ? 56.826  72.226  18.162  1.00 83.93  ?  262 VAL D CG1 1 
ATOM   16677 C  CG2 . VAL D  1  262 ? 56.719  71.276  20.483  1.00 57.81  ?  262 VAL D CG2 1 
ATOM   16678 N  N   . PRO D  1  263 ? 60.275  70.114  20.252  1.00 76.48  ?  263 PRO D N   1 
ATOM   16679 C  CA  . PRO D  1  263 ? 61.036  69.526  21.370  1.00 80.54  ?  263 PRO D CA  1 
ATOM   16680 C  C   . PRO D  1  263 ? 60.295  69.838  22.672  1.00 80.80  ?  263 PRO D C   1 
ATOM   16681 O  O   . PRO D  1  263 ? 60.383  70.945  23.199  1.00 79.52  ?  263 PRO D O   1 
ATOM   16682 C  CB  . PRO D  1  263 ? 62.409  70.222  21.284  1.00 73.14  ?  263 PRO D CB  1 
ATOM   16683 C  CG  . PRO D  1  263 ? 62.398  70.982  19.980  1.00 75.26  ?  263 PRO D CG  1 
ATOM   16684 C  CD  . PRO D  1  263 ? 60.966  71.304  19.723  1.00 71.64  ?  263 PRO D CD  1 
ATOM   16685 N  N   . GLU D  1  264 ? 59.524  68.873  23.161  1.00 81.38  ?  264 GLU D N   1 
ATOM   16686 C  CA  . GLU D  1  264 ? 58.715  69.047  24.360  1.00 67.42  ?  264 GLU D CA  1 
ATOM   16687 C  C   . GLU D  1  264 ? 59.519  69.330  25.624  1.00 76.82  ?  264 GLU D C   1 
ATOM   16688 O  O   . GLU D  1  264 ? 60.671  68.919  25.744  1.00 78.03  ?  264 GLU D O   1 
ATOM   16689 C  CB  . GLU D  1  264 ? 57.842  67.803  24.589  1.00 80.24  ?  264 GLU D CB  1 
ATOM   16690 C  CG  . GLU D  1  264 ? 56.703  67.652  23.600  1.00 78.83  ?  264 GLU D CG  1 
ATOM   16691 C  CD  . GLU D  1  264 ? 55.861  66.420  23.853  1.00 84.08  ?  264 GLU D CD  1 
ATOM   16692 O  OE1 . GLU D  1  264 ? 54.920  66.499  24.675  1.00 89.00  ?  264 GLU D OE1 1 
ATOM   16693 O  OE2 . GLU D  1  264 ? 56.139  65.373  23.226  1.00 93.28  ?  264 GLU D OE2 1 
ATOM   16694 N  N   . VAL D  1  265 ? 58.883  70.044  26.568  1.00 80.77  ?  265 VAL D N   1 
ATOM   16695 C  CA  . VAL D  1  265 ? 59.429  70.396  27.878  1.00 70.66  ?  265 VAL D CA  1 
ATOM   16696 C  C   . VAL D  1  265 ? 58.294  70.092  28.865  1.00 68.60  ?  265 VAL D C   1 
ATOM   16697 O  O   . VAL D  1  265 ? 57.299  70.814  28.861  1.00 72.59  ?  265 VAL D O   1 
ATOM   16698 C  CB  . VAL D  1  265 ? 59.841  71.887  27.967  1.00 64.42  ?  265 VAL D CB  1 
ATOM   16699 C  CG1 . VAL D  1  265 ? 60.270  72.245  29.385  1.00 56.99  ?  265 VAL D CG1 1 
ATOM   16700 C  CG2 . VAL D  1  265 ? 60.953  72.211  26.979  1.00 58.93  ?  265 VAL D CG2 1 
ATOM   16701 N  N   . PRO D  1  266 ? 58.394  69.038  29.710  1.00 66.10  ?  266 PRO D N   1 
ATOM   16702 C  CA  . PRO D  1  266 ? 57.293  68.654  30.609  1.00 70.07  ?  266 PRO D CA  1 
ATOM   16703 C  C   . PRO D  1  266 ? 56.627  69.834  31.333  1.00 78.60  ?  266 PRO D C   1 
ATOM   16704 O  O   . PRO D  1  266 ? 57.333  70.740  31.738  1.00 78.23  ?  266 PRO D O   1 
ATOM   16705 C  CB  . PRO D  1  266 ? 57.997  67.759  31.639  1.00 64.19  ?  266 PRO D CB  1 
ATOM   16706 C  CG  . PRO D  1  266 ? 59.086  67.085  30.839  1.00 64.77  ?  266 PRO D CG  1 
ATOM   16707 C  CD  . PRO D  1  266 ? 59.552  68.145  29.861  1.00 74.70  ?  266 PRO D CD  1 
ATOM   16708 N  N   . THR D  1  267 ? 55.294  69.790  31.441  1.00 83.14  ?  267 THR D N   1 
ATOM   16709 C  CA  . THR D  1  267 ? 54.506  70.832  32.159  1.00 77.25  ?  267 THR D CA  1 
ATOM   16710 C  C   . THR D  1  267 ? 54.799  72.237  31.620  1.00 68.50  ?  267 THR D C   1 
ATOM   16711 O  O   . THR D  1  267 ? 54.487  73.205  32.334  1.00 83.87  ?  267 THR D O   1 
ATOM   16712 C  CB  . THR D  1  267 ? 54.655  70.669  33.675  1.00 82.53  ?  267 THR D CB  1 
ATOM   16713 O  OG1 . THR D  1  267 ? 55.859  71.331  34.062  1.00 70.13  ?  267 THR D OG1 1 
ATOM   16714 C  CG2 . THR D  1  267 ? 54.700  69.222  34.112  1.00 104.65 ?  267 THR D CG2 1 
ATOM   16715 N  N   . LEU D  1  268 ? 55.365  72.345  30.417  1.00 75.41  ?  268 LEU D N   1 
ATOM   16716 C  CA  . LEU D  1  268 ? 55.554  73.674  29.773  1.00 71.30  ?  268 LEU D CA  1 
ATOM   16717 C  C   . LEU D  1  268 ? 55.164  73.620  28.291  1.00 71.95  ?  268 LEU D C   1 
ATOM   16718 O  O   . LEU D  1  268 ? 54.128  74.211  27.935  1.00 79.10  ?  268 LEU D O   1 
ATOM   16719 C  CB  . LEU D  1  268 ? 57.017  74.089  29.951  1.00 76.99  ?  268 LEU D CB  1 
ATOM   16720 C  CG  . LEU D  1  268 ? 57.370  74.637  31.332  1.00 66.89  ?  268 LEU D CG  1 
ATOM   16721 C  CD1 . LEU D  1  268 ? 58.782  75.200  31.344  1.00 63.98  ?  268 LEU D CD1 1 
ATOM   16722 C  CD2 . LEU D  1  268 ? 56.371  75.700  31.762  1.00 61.55  ?  268 LEU D CD2 1 
ATOM   16723 N  N   . LEU D  1  269 ? 55.969  72.947  27.465  1.00 82.24  ?  269 LEU D N   1 
ATOM   16724 C  CA  . LEU D  1  269 ? 55.665  72.829  26.014  1.00 69.67  ?  269 LEU D CA  1 
ATOM   16725 C  C   . LEU D  1  269 ? 55.227  71.394  25.710  1.00 67.42  ?  269 LEU D C   1 
ATOM   16726 O  O   . LEU D  1  269 ? 56.081  70.492  25.785  1.00 76.77  ?  269 LEU D O   1 
ATOM   16727 C  CB  . LEU D  1  269 ? 56.914  73.204  25.212  1.00 63.16  ?  269 LEU D CB  1 
ATOM   16728 C  CG  . LEU D  1  269 ? 56.804  73.007  23.701  1.00 69.71  ?  269 LEU D CG  1 
ATOM   16729 C  CD1 . LEU D  1  269 ? 55.570  73.707  23.153  1.00 59.62  ?  269 LEU D CD1 1 
ATOM   16730 C  CD2 . LEU D  1  269 ? 58.057  73.505  22.999  1.00 55.59  ?  269 LEU D CD2 1 
ATOM   16731 N  N   . LEU D  1  270 ? 53.946  71.196  25.385  1.00 60.97  ?  270 LEU D N   1 
ATOM   16732 C  CA  . LEU D  1  270 ? 53.447  69.855  25.091  1.00 74.24  ?  270 LEU D CA  1 
ATOM   16733 C  C   . LEU D  1  270 ? 52.841  69.736  23.702  1.00 72.49  ?  270 LEU D C   1 
ATOM   16734 O  O   . LEU D  1  270 ? 52.424  70.730  23.118  1.00 75.10  ?  270 LEU D O   1 
ATOM   16735 C  CB  . LEU D  1  270 ? 52.384  69.469  26.135  1.00 71.45  ?  270 LEU D CB  1 
ATOM   16736 C  CG  . LEU D  1  270 ? 52.755  69.705  27.602  1.00 57.79  ?  270 LEU D CG  1 
ATOM   16737 C  CD1 . LEU D  1  270 ? 51.525  69.698  28.476  1.00 67.98  ?  270 LEU D CD1 1 
ATOM   16738 C  CD2 . LEU D  1  270 ? 53.750  68.666  28.090  1.00 79.82  ?  270 LEU D CD2 1 
ATOM   16739 N  N   . THR D  1  271 ? 52.775  68.501  23.186  1.00 67.87  ?  271 THR D N   1 
ATOM   16740 C  CA  . THR D  1  271 ? 52.212  68.220  21.869  1.00 78.49  ?  271 THR D CA  1 
ATOM   16741 C  C   . THR D  1  271 ? 51.027  67.260  21.772  1.00 78.52  ?  271 THR D C   1 
ATOM   16742 O  O   . THR D  1  271 ? 51.202  66.050  21.897  1.00 88.71  ?  271 THR D O   1 
ATOM   16743 C  CB  . THR D  1  271 ? 53.245  67.513  20.982  1.00 66.83  ?  271 THR D CB  1 
ATOM   16744 O  OG1 . THR D  1  271 ? 53.687  66.330  21.646  1.00 120.96 ?  271 THR D OG1 1 
ATOM   16745 C  CG2 . THR D  1  271 ? 54.436  68.391  20.654  1.00 60.15  ?  271 THR D CG2 1 
ATOM   16746 N  N   . GLN D  1  272 ? 49.826  67.813  21.573  1.00 72.75  ?  272 GLN D N   1 
ATOM   16747 C  CA  . GLN D  1  272 ? 48.612  66.968  21.414  1.00 77.00  ?  272 GLN D CA  1 
ATOM   16748 C  C   . GLN D  1  272 ? 48.021  66.935  20.002  1.00 80.68  ?  272 GLN D C   1 
ATOM   16749 O  O   . GLN D  1  272 ? 47.450  67.957  19.578  1.00 85.85  ?  272 GLN D O   1 
ATOM   16750 C  CB  . GLN D  1  272 ? 47.616  67.536  22.426  1.00 75.10  ?  272 GLN D CB  1 
ATOM   16751 C  CG  . GLN D  1  272 ? 46.254  66.854  22.389  1.00 88.94  ?  272 GLN D CG  1 
ATOM   16752 C  CD  . GLN D  1  272 ? 46.352  65.348  22.352  1.00 79.08  ?  272 GLN D CD  1 
ATOM   16753 O  OE1 . GLN D  1  272 ? 46.565  64.743  21.305  1.00 95.20  ?  272 GLN D OE1 1 
ATOM   16754 N  NE2 . GLN D  1  272 ? 46.187  64.725  23.506  1.00 73.69  ?  272 GLN D NE2 1 
ATOM   16755 N  N   . LYS D  1  273 ? 48.159  65.804  19.308  1.00 75.47  ?  273 LYS D N   1 
ATOM   16756 C  CA  . LYS D  1  273 ? 47.660  65.667  17.945  1.00 77.58  ?  273 LYS D CA  1 
ATOM   16757 C  C   . LYS D  1  273 ? 46.150  65.409  17.916  1.00 89.73  ?  273 LYS D C   1 
ATOM   16758 O  O   . LYS D  1  273 ? 45.487  65.788  16.951  1.00 105.43 ?  273 LYS D O   1 
ATOM   16759 C  CB  . LYS D  1  273 ? 48.421  64.561  17.204  1.00 74.17  ?  273 LYS D CB  1 
ATOM   16760 C  CG  . LYS D  1  273 ? 49.932  64.794  17.178  1.00 85.45  ?  273 LYS D CG  1 
ATOM   16761 C  CD  . LYS D  1  273 ? 50.565  64.432  15.842  1.00 91.96  ?  273 LYS D CD  1 
ATOM   16762 C  CE  . LYS D  1  273 ? 52.068  64.299  15.937  1.00 109.70 ?  273 LYS D CE  1 
ATOM   16763 N  NZ  . LYS D  1  273 ? 52.488  62.938  16.371  1.00 98.41  ?  273 LYS D NZ  1 
ATOM   16764 N  N   . ASP D  1  274 ? 45.600  64.777  18.964  1.00 87.22  ?  274 ASP D N   1 
ATOM   16765 C  CA  . ASP D  1  274 ? 44.169  64.506  19.025  1.00 81.51  ?  274 ASP D CA  1 
ATOM   16766 C  C   . ASP D  1  274 ? 43.437  65.774  19.468  1.00 87.85  ?  274 ASP D C   1 
ATOM   16767 O  O   . ASP D  1  274 ? 43.586  66.216  20.608  1.00 87.78  ?  274 ASP D O   1 
ATOM   16768 C  CB  . ASP D  1  274 ? 43.880  63.337  19.982  1.00 83.54  ?  274 ASP D CB  1 
ATOM   16769 C  CG  . ASP D  1  274 ? 42.486  62.746  19.859  1.00 87.35  ?  274 ASP D CG  1 
ATOM   16770 O  OD1 . ASP D  1  274 ? 41.646  63.341  19.147  1.00 100.26 ?  274 ASP D OD1 1 
ATOM   16771 O  OD2 . ASP D  1  274 ? 42.236  61.688  20.471  1.00 82.44  ?  274 ASP D OD2 1 
ATOM   16772 N  N   . TYR D  1  275 ? 42.654  66.362  18.559  1.00 93.57  ?  275 TYR D N   1 
ATOM   16773 C  CA  . TYR D  1  275 ? 41.900  67.580  18.842  1.00 83.02  ?  275 TYR D CA  1 
ATOM   16774 C  C   . TYR D  1  275 ? 40.762  67.318  19.834  1.00 81.94  ?  275 TYR D C   1 
ATOM   16775 O  O   . TYR D  1  275 ? 40.407  68.211  20.602  1.00 89.70  ?  275 TYR D O   1 
ATOM   16776 C  CB  . TYR D  1  275 ? 41.365  68.177  17.536  1.00 77.54  ?  275 TYR D CB  1 
ATOM   16777 C  CG  . TYR D  1  275 ? 42.467  68.573  16.578  1.00 86.49  ?  275 TYR D CG  1 
ATOM   16778 C  CD1 . TYR D  1  275 ? 43.210  69.727  16.781  1.00 88.20  ?  275 TYR D CD1 1 
ATOM   16779 C  CD2 . TYR D  1  275 ? 42.786  67.779  15.486  1.00 95.12  ?  275 TYR D CD2 1 
ATOM   16780 C  CE1 . TYR D  1  275 ? 44.227  70.094  15.908  1.00 90.02  ?  275 TYR D CE1 1 
ATOM   16781 C  CE2 . TYR D  1  275 ? 43.802  68.133  14.608  1.00 85.37  ?  275 TYR D CE2 1 
ATOM   16782 C  CZ  . TYR D  1  275 ? 44.522  69.291  14.822  1.00 82.21  ?  275 TYR D CZ  1 
ATOM   16783 O  OH  . TYR D  1  275 ? 45.523  69.639  13.946  1.00 86.24  ?  275 TYR D OH  1 
ATOM   16784 N  N   . ASP D  1  276 ? 40.203  66.095  19.837  1.00 76.74  ?  276 ASP D N   1 
ATOM   16785 C  CA  . ASP D  1  276 ? 39.128  65.727  20.763  1.00 89.08  ?  276 ASP D CA  1 
ATOM   16786 C  C   . ASP D  1  276 ? 39.618  65.625  22.223  1.00 86.20  ?  276 ASP D C   1 
ATOM   16787 O  O   . ASP D  1  276 ? 38.798  65.484  23.131  1.00 84.22  ?  276 ASP D O   1 
ATOM   16788 C  CB  . ASP D  1  276 ? 38.487  64.399  20.333  1.00 85.27  ?  276 ASP D CB  1 
ATOM   16789 C  CG  . ASP D  1  276 ? 37.817  64.467  18.977  1.00 94.59  ?  276 ASP D CG  1 
ATOM   16790 O  OD1 . ASP D  1  276 ? 36.911  65.313  18.804  1.00 105.75 ?  276 ASP D OD1 1 
ATOM   16791 O  OD2 . ASP D  1  276 ? 38.198  63.675  18.087  1.00 108.55 ?  276 ASP D OD2 1 
ATOM   16792 N  N   . LYS D  1  277 ? 40.942  65.691  22.448  1.00 85.84  ?  277 LYS D N   1 
ATOM   16793 C  CA  . LYS D  1  277 ? 41.536  65.635  23.781  1.00 80.81  ?  277 LYS D CA  1 
ATOM   16794 C  C   . LYS D  1  277 ? 42.167  66.993  24.147  1.00 79.90  ?  277 LYS D C   1 
ATOM   16795 O  O   . LYS D  1  277 ? 42.381  67.255  25.330  1.00 85.59  ?  277 LYS D O   1 
ATOM   16796 C  CB  . LYS D  1  277 ? 42.431  64.390  23.899  1.00 78.83  ?  277 LYS D CB  1 
ATOM   16797 C  CG  . LYS D  1  277 ? 41.686  63.118  24.268  1.00 82.98  ?  277 LYS D CG  1 
ATOM   16798 C  CD  . LYS D  1  277 ? 42.632  62.011  24.727  1.00 89.51  ?  277 LYS D CD  1 
ATOM   16799 C  CE  . LYS D  1  277 ? 43.419  61.384  23.600  1.00 98.66  ?  277 LYS D CE  1 
ATOM   16800 N  NZ  . LYS D  1  277 ? 43.958  60.048  23.972  1.00 99.23  ?  277 LYS D NZ  1 
ATOM   16801 N  N   . MET D  1  278 ? 42.439  67.837  23.149  1.00 78.23  ?  278 MET D N   1 
ATOM   16802 C  CA  . MET D  1  278 ? 43.093  69.146  23.423  1.00 74.38  ?  278 MET D CA  1 
ATOM   16803 C  C   . MET D  1  278 ? 42.563  69.930  24.629  1.00 76.47  ?  278 MET D C   1 
ATOM   16804 O  O   . MET D  1  278 ? 43.392  70.390  25.437  1.00 68.27  ?  278 MET D O   1 
ATOM   16805 C  CB  . MET D  1  278 ? 43.060  70.038  22.178  1.00 69.42  ?  278 MET D CB  1 
ATOM   16806 C  CG  . MET D  1  278 ? 43.749  71.377  22.372  1.00 93.75  ?  278 MET D CG  1 
ATOM   16807 S  SD  . MET D  1  278 ? 45.438  71.237  23.018  1.00 75.42  ?  278 MET D SD  1 
ATOM   16808 C  CE  . MET D  1  278 ? 46.377  71.259  21.492  1.00 67.76  ?  278 MET D CE  1 
ATOM   16809 N  N   . VAL D  1  279 ? 41.238  70.069  24.750  1.00 71.92  ?  279 VAL D N   1 
ATOM   16810 C  CA  . VAL D  1  279 ? 40.663  70.855  25.838  1.00 74.49  ?  279 VAL D CA  1 
ATOM   16811 C  C   . VAL D  1  279 ? 41.036  70.236  27.186  1.00 77.35  ?  279 VAL D C   1 
ATOM   16812 O  O   . VAL D  1  279 ? 41.548  70.936  28.058  1.00 73.62  ?  279 VAL D O   1 
ATOM   16813 C  CB  . VAL D  1  279 ? 39.135  71.010  25.673  1.00 83.82  ?  279 VAL D CB  1 
ATOM   16814 C  CG1 . VAL D  1  279 ? 38.522  71.715  26.879  1.00 69.19  ?  279 VAL D CG1 1 
ATOM   16815 C  CG2 . VAL D  1  279 ? 38.806  71.765  24.388  1.00 76.24  ?  279 VAL D CG2 1 
ATOM   16816 N  N   . LYS D  1  280 ? 40.811  68.921  27.346  1.00 77.82  ?  280 LYS D N   1 
ATOM   16817 C  CA  . LYS D  1  280 ? 41.132  68.229  28.595  1.00 69.24  ?  280 LYS D CA  1 
ATOM   16818 C  C   . LYS D  1  280 ? 42.624  68.334  28.955  1.00 77.99  ?  280 LYS D C   1 
ATOM   16819 O  O   . LYS D  1  280 ? 42.947  68.475  30.134  1.00 82.42  ?  280 LYS D O   1 
ATOM   16820 C  CB  . LYS D  1  280 ? 40.702  66.754  28.529  1.00 72.60  ?  280 LYS D CB  1 
ATOM   16821 C  CG  . LYS D  1  280 ? 39.194  66.548  28.562  1.00 70.26  ?  280 LYS D CG  1 
ATOM   16822 C  CD  . LYS D  1  280 ? 38.831  65.096  28.855  1.00 84.84  ?  280 LYS D CD  1 
ATOM   16823 C  CE  . LYS D  1  280 ? 37.339  64.864  28.843  1.00 115.31 ?  280 LYS D CE  1 
ATOM   16824 N  NZ  . LYS D  1  280 ? 36.989  63.418  28.861  1.00 105.91 ?  280 LYS D NZ  1 
ATOM   16825 N  N   . THR D  1  281 ? 43.496  68.266  27.945  1.00 82.41  ?  281 THR D N   1 
ATOM   16826 C  CA  . THR D  1  281 ? 44.959  68.378  28.185  1.00 83.03  ?  281 THR D CA  1 
ATOM   16827 C  C   . THR D  1  281 ? 45.283  69.794  28.665  1.00 81.55  ?  281 THR D C   1 
ATOM   16828 O  O   . THR D  1  281 ? 46.001  69.920  29.675  1.00 80.35  ?  281 THR D O   1 
ATOM   16829 C  CB  . THR D  1  281 ? 45.752  68.040  26.915  1.00 64.21  ?  281 THR D CB  1 
ATOM   16830 O  OG1 . THR D  1  281 ? 45.853  69.228  26.129  1.00 107.17 ?  281 THR D OG1 1 
ATOM   16831 C  CG2 . THR D  1  281 ? 45.126  66.940  26.086  1.00 64.11  ?  281 THR D CG2 1 
ATOM   16832 N  N   . SER D  1  282 ? 44.765  70.812  27.973  1.00 65.72  ?  282 SER D N   1 
ATOM   16833 C  CA  . SER D  1  282 ? 45.041  72.199  28.319  1.00 68.70  ?  282 SER D CA  1 
ATOM   16834 C  C   . SER D  1  282 ? 44.625  72.531  29.740  1.00 71.64  ?  282 SER D C   1 
ATOM   16835 O  O   . SER D  1  282 ? 45.376  73.192  30.455  1.00 79.62  ?  282 SER D O   1 
ATOM   16836 C  CB  . SER D  1  282 ? 44.332  73.134  27.351  1.00 69.49  ?  282 SER D CB  1 
ATOM   16837 O  OG  . SER D  1  282 ? 44.833  72.972  26.035  1.00 73.14  ?  282 SER D OG  1 
ATOM   16838 N  N   . LEU D  1  283 ? 43.443  72.073  30.161  1.00 67.25  ?  283 LEU D N   1 
ATOM   16839 C  CA  . LEU D  1  283 ? 42.969  72.354  31.511  1.00 72.79  ?  283 LEU D CA  1 
ATOM   16840 C  C   . LEU D  1  283 ? 43.872  71.663  32.523  1.00 76.42  ?  283 LEU D C   1 
ATOM   16841 O  O   . LEU D  1  283 ? 44.258  72.276  33.514  1.00 78.70  ?  283 LEU D O   1 
ATOM   16842 C  CB  . LEU D  1  283 ? 41.510  71.913  31.692  1.00 64.68  ?  283 LEU D CB  1 
ATOM   16843 C  CG  . LEU D  1  283 ? 40.487  72.560  30.750  1.00 67.54  ?  283 LEU D CG  1 
ATOM   16844 C  CD1 . LEU D  1  283 ? 39.135  71.898  30.889  1.00 66.50  ?  283 LEU D CD1 1 
ATOM   16845 C  CD2 . LEU D  1  283 ? 40.365  74.058  30.993  1.00 65.07  ?  283 LEU D CD2 1 
ATOM   16846 N  N   . GLU D  1  284 ? 44.243  70.404  32.265  1.00 73.77  ?  284 GLU D N   1 
ATOM   16847 C  CA  . GLU D  1  284 ? 45.126  69.675  33.166  1.00 69.20  ?  284 GLU D CA  1 
ATOM   16848 C  C   . GLU D  1  284 ? 46.497  70.350  33.241  1.00 71.85  ?  284 GLU D C   1 
ATOM   16849 O  O   . GLU D  1  284 ? 47.073  70.447  34.321  1.00 74.42  ?  284 GLU D O   1 
ATOM   16850 C  CB  . GLU D  1  284 ? 45.279  68.221  32.712  1.00 63.71  ?  284 GLU D CB  1 
ATOM   16851 C  CG  . GLU D  1  284 ? 46.096  67.392  33.684  1.00 75.31  ?  284 GLU D CG  1 
ATOM   16852 C  CD  . GLU D  1  284 ? 46.235  65.936  33.301  1.00 90.15  ?  284 GLU D CD  1 
ATOM   16853 O  OE1 . GLU D  1  284 ? 45.236  65.346  32.829  1.00 103.93 ?  284 GLU D OE1 1 
ATOM   16854 O  OE2 . GLU D  1  284 ? 47.345  65.384  33.474  1.00 91.54  ?  284 GLU D OE2 1 
ATOM   16855 N  N   . ALA D  1  285 ? 47.013  70.823  32.101  1.00 75.62  ?  285 ALA D N   1 
ATOM   16856 C  CA  . ALA D  1  285 ? 48.313  71.485  32.038  1.00 73.45  ?  285 ALA D CA  1 
ATOM   16857 C  C   . ALA D  1  285 ? 48.366  72.756  32.880  1.00 62.16  ?  285 ALA D C   1 
ATOM   16858 O  O   . ALA D  1  285 ? 49.440  73.116  33.358  1.00 82.04  ?  285 ALA D O   1 
ATOM   16859 C  CB  . ALA D  1  285 ? 48.660  71.813  30.594  1.00 69.47  ?  285 ALA D CB  1 
ATOM   16860 N  N   . ARG D  1  286 ? 47.228  73.443  33.057  1.00 67.50  ?  286 ARG D N   1 
ATOM   16861 C  CA  . ARG D  1  286 ? 47.190  74.672  33.844  1.00 73.38  ?  286 ARG D CA  1 
ATOM   16862 C  C   . ARG D  1  286 ? 46.363  74.517  35.131  1.00 77.32  ?  286 ARG D C   1 
ATOM   16863 O  O   . ARG D  1  286 ? 45.846  75.501  35.652  1.00 79.01  ?  286 ARG D O   1 
ATOM   16864 C  CB  . ARG D  1  286 ? 46.653  75.817  32.966  1.00 58.63  ?  286 ARG D CB  1 
ATOM   16865 C  CG  . ARG D  1  286 ? 46.852  77.228  33.511  1.00 67.16  ?  286 ARG D CG  1 
ATOM   16866 C  CD  . ARG D  1  286 ? 48.245  77.496  34.044  1.00 65.64  ?  286 ARG D CD  1 
ATOM   16867 N  NE  . ARG D  1  286 ? 48.512  78.925  34.163  1.00 62.84  ?  286 ARG D NE  1 
ATOM   16868 C  CZ  . ARG D  1  286 ? 49.453  79.458  34.932  1.00 65.71  ?  286 ARG D CZ  1 
ATOM   16869 N  NH1 . ARG D  1  286 ? 50.245  78.680  35.661  1.00 72.21  ?  286 ARG D NH1 1 
ATOM   16870 N  NH2 . ARG D  1  286 ? 49.617  80.772  34.976  1.00 79.38  ?  286 ARG D NH2 1 
ATOM   16871 N  N   . ASN D  1  287 ? 46.259  73.281  35.648  1.00 78.32  ?  287 ASN D N   1 
ATOM   16872 C  CA  . ASN D  1  287 ? 45.525  72.952  36.869  1.00 72.43  ?  287 ASN D CA  1 
ATOM   16873 C  C   . ASN D  1  287 ? 44.143  73.616  36.968  1.00 81.93  ?  287 ASN D C   1 
ATOM   16874 O  O   . ASN D  1  287 ? 43.759  74.090  38.036  1.00 97.65  ?  287 ASN D O   1 
ATOM   16875 C  CB  . ASN D  1  287 ? 46.382  73.282  38.098  1.00 72.34  ?  287 ASN D CB  1 
ATOM   16876 C  CG  . ASN D  1  287 ? 46.043  72.446  39.308  1.00 100.73 ?  287 ASN D CG  1 
ATOM   16877 O  OD1 . ASN D  1  287 ? 46.086  71.213  39.263  1.00 115.25 ?  287 ASN D OD1 1 
ATOM   16878 N  ND2 . ASN D  1  287 ? 45.694  73.088  40.419  1.00 124.96 ?  287 ASN D ND2 1 
ATOM   16879 N  N   . ILE D  1  288 ? 43.391  73.636  35.863  1.00 81.10  ?  288 ILE D N   1 
ATOM   16880 C  CA  . ILE D  1  288 ? 42.054  74.223  35.847  1.00 80.43  ?  288 ILE D CA  1 
ATOM   16881 C  C   . ILE D  1  288 ? 41.038  73.113  36.101  1.00 91.46  ?  288 ILE D C   1 
ATOM   16882 O  O   . ILE D  1  288 ? 40.856  72.237  35.255  1.00 84.72  ?  288 ILE D O   1 
ATOM   16883 C  CB  . ILE D  1  288 ? 41.784  74.943  34.507  1.00 69.33  ?  288 ILE D CB  1 
ATOM   16884 C  CG1 . ILE D  1  288 ? 42.739  76.144  34.329  1.00 74.66  ?  288 ILE D CG1 1 
ATOM   16885 C  CG2 . ILE D  1  288 ? 40.326  75.391  34.436  1.00 73.12  ?  288 ILE D CG2 1 
ATOM   16886 C  CD1 . ILE D  1  288 ? 42.974  76.543  32.889  1.00 84.21  ?  288 ILE D CD1 1 
ATOM   16887 N  N   . LYS D  1  289 ? 40.385  73.139  37.269  1.00 99.61  ?  289 LYS D N   1 
ATOM   16888 C  CA  . LYS D  1  289 ? 39.393  72.132  37.630  1.00 101.74 ?  289 LYS D CA  1 
ATOM   16889 C  C   . LYS D  1  289 ? 37.992  72.706  37.422  1.00 106.46 ?  289 LYS D C   1 
ATOM   16890 O  O   . LYS D  1  289 ? 37.614  73.672  38.086  1.00 91.50  ?  289 LYS D O   1 
ATOM   16891 C  CB  . LYS D  1  289 ? 39.601  71.680  39.082  1.00 103.63 ?  289 LYS D CB  1 
ATOM   16892 C  CG  . LYS D  1  289 ? 40.995  71.107  39.323  1.00 106.28 ?  289 LYS D CG  1 
ATOM   16893 C  CD  . LYS D  1  289 ? 41.163  70.539  40.718  1.00 128.76 ?  289 LYS D CD  1 
ATOM   16894 C  CE  . LYS D  1  289 ? 42.582  70.090  40.973  1.00 130.09 ?  289 LYS D CE  1 
ATOM   16895 N  NZ  . LYS D  1  289 ? 42.755  69.550  42.349  1.00 160.34 ?  289 LYS D NZ  1 
ATOM   16896 N  N   . ILE D  1  290 ? 37.232  72.121  36.481  1.00 108.59 ?  290 ILE D N   1 
ATOM   16897 C  CA  . ILE D  1  290 ? 35.883  72.581  36.158  1.00 110.83 ?  290 ILE D CA  1 
ATOM   16898 C  C   . ILE D  1  290 ? 34.837  71.867  37.006  1.00 121.04 ?  290 ILE D C   1 
ATOM   16899 O  O   . ILE D  1  290 ? 34.692  70.648  36.907  1.00 114.72 ?  290 ILE D O   1 
ATOM   16900 C  CB  . ILE D  1  290 ? 35.581  72.376  34.649  1.00 95.08  ?  290 ILE D CB  1 
ATOM   16901 C  CG1 . ILE D  1  290 ? 36.647  73.039  33.739  1.00 92.70  ?  290 ILE D CG1 1 
ATOM   16902 C  CG2 . ILE D  1  290 ? 34.173  72.864  34.310  1.00 113.03 ?  290 ILE D CG2 1 
ATOM   16903 C  CD1 . ILE D  1  290 ? 36.828  74.547  33.879  1.00 98.00  ?  290 ILE D CD1 1 
ATOM   16904 N  N   . LYS D  1  291 ? 34.091  72.629  37.822  1.00 134.48 ?  291 LYS D N   1 
ATOM   16905 C  CA  . LYS D  1  291 ? 33.032  72.069  38.660  1.00 140.32 ?  291 LYS D CA  1 
ATOM   16906 C  C   . LYS D  1  291 ? 31.801  71.861  37.776  1.00 137.00 ?  291 LYS D C   1 
ATOM   16907 O  O   . LYS D  1  291 ? 30.976  72.763  37.622  1.00 131.01 ?  291 LYS D O   1 
ATOM   16908 C  CB  . LYS D  1  291 ? 32.717  72.996  39.847  1.00 145.64 ?  291 LYS D CB  1 
ATOM   16909 C  CG  . LYS D  1  291 ? 33.832  73.032  40.888  1.00 143.87 ?  291 LYS D CG  1 
ATOM   16910 C  CD  . LYS D  1  291 ? 33.484  73.916  42.076  1.00 148.09 ?  291 LYS D CD  1 
ATOM   16911 C  CE  . LYS D  1  291 ? 34.532  73.843  43.158  1.00 150.66 ?  291 LYS D CE  1 
ATOM   16912 N  NZ  . LYS D  1  291 ? 34.165  74.664  44.341  1.00 144.79 ?  291 LYS D NZ  1 
ATOM   16913 N  N   . ILE D  1  292 ? 31.701  70.665  37.181  1.00 133.58 ?  292 ILE D N   1 
ATOM   16914 C  CA  . ILE D  1  292 ? 30.605  70.322  36.281  1.00 145.90 ?  292 ILE D CA  1 
ATOM   16915 C  C   . ILE D  1  292 ? 29.332  70.027  37.070  1.00 162.08 ?  292 ILE D C   1 
ATOM   16916 O  O   . ILE D  1  292 ? 29.363  69.242  38.019  1.00 160.29 ?  292 ILE D O   1 
ATOM   16917 C  CB  . ILE D  1  292 ? 30.989  69.119  35.375  1.00 134.62 ?  292 ILE D CB  1 
ATOM   16918 C  CG1 . ILE D  1  292 ? 32.309  69.390  34.613  1.00 135.97 ?  292 ILE D CG1 1 
ATOM   16919 C  CG2 . ILE D  1  292 ? 29.856  68.816  34.391  1.00 137.44 ?  292 ILE D CG2 1 
ATOM   16920 C  CD1 . ILE D  1  292 ? 33.014  68.144  34.116  1.00 121.66 ?  292 ILE D CD1 1 
ATOM   16921 N  N   . THR D  1  293 ? 28.210  70.648  36.669  1.00 172.21 ?  293 THR D N   1 
ATOM   16922 C  CA  . THR D  1  293 ? 26.913  70.443  37.319  1.00 170.31 ?  293 THR D CA  1 
ATOM   16923 C  C   . THR D  1  293 ? 26.136  69.307  36.622  1.00 166.75 ?  293 THR D C   1 
ATOM   16924 O  O   . THR D  1  293 ? 25.346  68.624  37.276  1.00 171.43 ?  293 THR D O   1 
ATOM   16925 C  CB  . THR D  1  293 ? 26.108  71.758  37.333  1.00 163.22 ?  293 THR D CB  1 
ATOM   16926 O  OG1 . THR D  1  293 ? 26.964  72.840  37.719  1.00 155.25 ?  293 THR D OG1 1 
ATOM   16927 C  CG2 . THR D  1  293 ? 24.907  71.696  38.274  1.00 162.86 ?  293 THR D CG2 1 
ATOM   16928 N  N   . GLU D  1  294 ? 26.365  69.105  35.305  1.00 150.72 ?  294 GLU D N   1 
ATOM   16929 C  CA  . GLU D  1  294 ? 25.710  68.061  34.511  1.00 156.81 ?  294 GLU D CA  1 
ATOM   16930 C  C   . GLU D  1  294 ? 24.185  68.051  34.443  1.00 147.35 ?  294 GLU D C   1 
ATOM   16931 O  O   . GLU D  1  294 ? 23.555  67.028  34.716  1.00 142.83 ?  294 GLU D O   1 
ATOM   16932 C  CB  . GLU D  1  294 ? 26.206  66.655  34.919  1.00 163.66 ?  294 GLU D CB  1 
ATOM   16933 C  CG  . GLU D  1  294 ? 27.300  66.082  34.033  1.00 159.78 ?  294 GLU D CG  1 
ATOM   16934 C  CD  . GLU D  1  294 ? 28.012  64.881  34.625  1.00 169.01 ?  294 GLU D CD  1 
ATOM   16935 O  OE1 . GLU D  1  294 ? 27.454  64.252  35.553  1.00 164.88 ?  294 GLU D OE1 1 
ATOM   16936 O  OE2 . GLU D  1  294 ? 29.130  64.566  34.156  1.00 176.36 ?  294 GLU D OE2 1 
ATOM   16937 N  N   . ILE D  1  295 ? 23.595  69.189  34.075  1.00 134.60 ?  295 ILE D N   1 
ATOM   16938 C  CA  . ILE D  1  295 ? 22.145  69.291  33.962  1.00 137.75 ?  295 ILE D CA  1 
ATOM   16939 C  C   . ILE D  1  295 ? 21.580  68.570  32.725  1.00 131.95 ?  295 ILE D C   1 
ATOM   16940 O  O   . ILE D  1  295 ? 22.109  68.763  31.630  1.00 120.19 ?  295 ILE D O   1 
ATOM   16941 C  CB  . ILE D  1  295 ? 21.750  70.794  33.986  1.00 131.91 ?  295 ILE D CB  1 
ATOM   16942 C  CG1 . ILE D  1  295 ? 22.485  71.551  35.120  1.00 133.13 ?  295 ILE D CG1 1 
ATOM   16943 C  CG2 . ILE D  1  295 ? 20.241  70.936  34.147  1.00 112.21 ?  295 ILE D CG2 1 
ATOM   16944 C  CD1 . ILE D  1  295 ? 22.423  73.066  35.014  1.00 103.17 ?  295 ILE D CD1 1 
ATOM   16945 N  N   . PRO D  1  296 ? 20.531  67.728  32.860  1.00 126.83 ?  296 PRO D N   1 
ATOM   16946 C  CA  . PRO D  1  296 ? 20.003  67.031  31.673  1.00 127.85 ?  296 PRO D CA  1 
ATOM   16947 C  C   . PRO D  1  296 ? 19.196  67.949  30.752  1.00 125.68 ?  296 PRO D C   1 
ATOM   16948 O  O   . PRO D  1  296 ? 17.970  67.997  30.838  1.00 118.20 ?  296 PRO D O   1 
ATOM   16949 C  CB  . PRO D  1  296 ? 19.152  65.910  32.274  1.00 124.61 ?  296 PRO D CB  1 
ATOM   16950 C  CG  . PRO D  1  296 ? 18.715  66.432  33.589  1.00 111.01 ?  296 PRO D CG  1 
ATOM   16951 C  CD  . PRO D  1  296 ? 19.784  67.365  34.082  1.00 107.47 ?  296 PRO D CD  1 
ATOM   16952 N  N   . ILE D  1  297 ? 19.891  68.674  29.863  1.00 126.91 ?  297 ILE D N   1 
ATOM   16953 C  CA  . ILE D  1  297 ? 19.266  69.619  28.933  1.00 128.51 ?  297 ILE D CA  1 
ATOM   16954 C  C   . ILE D  1  297 ? 19.926  69.518  27.542  1.00 119.20 ?  297 ILE D C   1 
ATOM   16955 O  O   . ILE D  1  297 ? 21.120  69.232  27.451  1.00 111.00 ?  297 ILE D O   1 
ATOM   16956 C  CB  . ILE D  1  297 ? 19.335  71.077  29.499  1.00 126.65 ?  297 ILE D CB  1 
ATOM   16957 C  CG1 . ILE D  1  297 ? 20.754  71.406  30.024  1.00 129.34 ?  297 ILE D CG1 1 
ATOM   16958 C  CG2 . ILE D  1  297 ? 18.284  71.304  30.597  1.00 117.44 ?  297 ILE D CG2 1 
ATOM   16959 C  CD1 . ILE D  1  297 ? 21.012  72.844  30.333  1.00 114.42 ?  297 ILE D CD1 1 
ATOM   16960 N  N   . PRO D  1  298 ? 19.179  69.754  26.445  1.00 112.13 ?  298 PRO D N   1 
ATOM   16961 C  CA  . PRO D  1  298 ? 19.782  69.647  25.105  1.00 126.40 ?  298 PRO D CA  1 
ATOM   16962 C  C   . PRO D  1  298 ? 20.554  70.881  24.630  1.00 136.47 ?  298 PRO D C   1 
ATOM   16963 O  O   . PRO D  1  298 ? 21.139  70.841  23.550  1.00 142.85 ?  298 PRO D O   1 
ATOM   16964 C  CB  . PRO D  1  298 ? 18.567  69.398  24.214  1.00 112.72 ?  298 PRO D CB  1 
ATOM   16965 C  CG  . PRO D  1  298 ? 17.486  70.153  24.874  1.00 118.42 ?  298 PRO D CG  1 
ATOM   16966 C  CD  . PRO D  1  298 ? 17.747  70.101  26.355  1.00 120.56 ?  298 PRO D CD  1 
ATOM   16967 N  N   . VAL D  1  299 ? 20.547  71.976  25.407  1.00 130.70 ?  299 VAL D N   1 
ATOM   16968 C  CA  . VAL D  1  299 ? 21.250  73.207  25.028  1.00 117.43 ?  299 VAL D CA  1 
ATOM   16969 C  C   . VAL D  1  299 ? 22.361  73.503  26.050  1.00 119.39 ?  299 VAL D C   1 
ATOM   16970 O  O   . VAL D  1  299 ? 22.310  73.008  27.175  1.00 124.10 ?  299 VAL D O   1 
ATOM   16971 C  CB  . VAL D  1  299 ? 20.273  74.413  24.890  1.00 116.38 ?  299 VAL D CB  1 
ATOM   16972 C  CG1 . VAL D  1  299 ? 20.917  75.558  24.114  1.00 125.02 ?  299 VAL D CG1 1 
ATOM   16973 C  CG2 . VAL D  1  299 ? 18.958  73.998  24.231  1.00 118.01 ?  299 VAL D CG2 1 
ATOM   16974 N  N   . SER D  1  300 ? 23.365  74.301  25.658  1.00 109.98 ?  300 SER D N   1 
ATOM   16975 C  CA  . SER D  1  300 ? 24.483  74.645  26.538  1.00 104.82 ?  300 SER D CA  1 
ATOM   16976 C  C   . SER D  1  300 ? 24.050  75.484  27.752  1.00 106.69 ?  300 SER D C   1 
ATOM   16977 O  O   . SER D  1  300 ? 22.955  76.042  27.762  1.00 119.81 ?  300 SER D O   1 
ATOM   16978 C  CB  . SER D  1  300 ? 25.567  75.375  25.748  1.00 114.52 ?  300 SER D CB  1 
ATOM   16979 O  OG  . SER D  1  300 ? 26.778  75.447  26.482  1.00 123.23 ?  300 SER D OG  1 
ATOM   16980 N  N   . PHE D  1  301 ? 24.912  75.564  28.777  1.00 95.50  ?  301 PHE D N   1 
ATOM   16981 C  CA  . PHE D  1  301 ? 24.627  76.305  30.006  1.00 90.60  ?  301 PHE D CA  1 
ATOM   16982 C  C   . PHE D  1  301 ? 25.938  76.844  30.575  1.00 92.00  ?  301 PHE D C   1 
ATOM   16983 O  O   . PHE D  1  301 ? 26.732  76.074  31.110  1.00 100.18 ?  301 PHE D O   1 
ATOM   16984 C  CB  . PHE D  1  301 ? 23.948  75.357  31.004  1.00 92.12  ?  301 PHE D CB  1 
ATOM   16985 C  CG  . PHE D  1  301 ? 23.398  75.969  32.270  1.00 102.39 ?  301 PHE D CG  1 
ATOM   16986 C  CD1 . PHE D  1  301 ? 24.209  76.168  33.372  1.00 92.48  ?  301 PHE D CD1 1 
ATOM   16987 C  CD2 . PHE D  1  301 ? 22.048  76.244  32.393  1.00 100.57 ?  301 PHE D CD2 1 
ATOM   16988 C  CE1 . PHE D  1  301 ? 23.691  76.686  34.552  1.00 93.12  ?  301 PHE D CE1 1 
ATOM   16989 C  CE2 . PHE D  1  301 ? 21.533  76.756  33.574  1.00 98.04  ?  301 PHE D CE2 1 
ATOM   16990 C  CZ  . PHE D  1  301 ? 22.357  76.973  34.646  1.00 96.29  ?  301 PHE D CZ  1 
ATOM   16991 N  N   . ALA D  1  302 ? 26.174  78.157  30.457  1.00 96.35  ?  302 ALA D N   1 
ATOM   16992 C  CA  . ALA D  1  302 ? 27.414  78.766  30.940  1.00 97.05  ?  302 ALA D CA  1 
ATOM   16993 C  C   . ALA D  1  302 ? 27.254  80.269  31.197  1.00 106.53 ?  302 ALA D C   1 
ATOM   16994 O  O   . ALA D  1  302 ? 26.330  80.890  30.677  1.00 100.31 ?  302 ALA D O   1 
ATOM   16995 C  CB  . ALA D  1  302 ? 28.522  78.534  29.920  1.00 81.43  ?  302 ALA D CB  1 
ATOM   16996 N  N   . ALA D  1  303 ? 28.166  80.854  31.994  1.00 103.83 ?  303 ALA D N   1 
ATOM   16997 C  CA  . ALA D  1  303 ? 28.148  82.283  32.311  1.00 95.88  ?  303 ALA D CA  1 
ATOM   16998 C  C   . ALA D  1  303 ? 28.341  83.162  31.070  1.00 98.10  ?  303 ALA D C   1 
ATOM   16999 O  O   . ALA D  1  303 ? 28.018  84.347  31.116  1.00 114.72 ?  303 ALA D O   1 
ATOM   17000 C  CB  . ALA D  1  303 ? 29.231  82.599  33.330  1.00 91.27  ?  303 ALA D CB  1 
ATOM   17001 N  N   . ALA D  1  304 ? 28.872  82.605  29.975  1.00 94.48  ?  304 ALA D N   1 
ATOM   17002 C  CA  . ALA D  1  304 ? 29.077  83.365  28.749  1.00 103.42 ?  304 ALA D CA  1 
ATOM   17003 C  C   . ALA D  1  304 ? 27.743  83.767  28.105  1.00 107.65 ?  304 ALA D C   1 
ATOM   17004 O  O   . ALA D  1  304 ? 27.685  84.784  27.417  1.00 105.72 ?  304 ALA D O   1 
ATOM   17005 C  CB  . ALA D  1  304 ? 29.901  82.547  27.766  1.00 101.02 ?  304 ALA D CB  1 
ATOM   17006 N  N   . PHE D  1  305 ? 26.677  82.978  28.326  1.00 107.03 ?  305 PHE D N   1 
ATOM   17007 C  CA  . PHE D  1  305 ? 25.360  83.270  27.757  1.00 114.21 ?  305 PHE D CA  1 
ATOM   17008 C  C   . PHE D  1  305 ? 24.505  84.180  28.658  1.00 116.98 ?  305 PHE D C   1 
ATOM   17009 O  O   . PHE D  1  305 ? 23.288  84.240  28.489  1.00 117.85 ?  305 PHE D O   1 
ATOM   17010 C  CB  . PHE D  1  305 ? 24.615  81.964  27.446  1.00 111.25 ?  305 PHE D CB  1 
ATOM   17011 C  CG  . PHE D  1  305 ? 25.450  80.963  26.684  1.00 111.13 ?  305 PHE D CG  1 
ATOM   17012 C  CD1 . PHE D  1  305 ? 25.874  81.229  25.395  1.00 109.11 ?  305 PHE D CD1 1 
ATOM   17013 C  CD2 . PHE D  1  305 ? 25.836  79.772  27.269  1.00 104.30 ?  305 PHE D CD2 1 
ATOM   17014 C  CE1 . PHE D  1  305 ? 26.655  80.315  24.701  1.00 91.38  ?  305 PHE D CE1 1 
ATOM   17015 C  CE2 . PHE D  1  305 ? 26.612  78.857  26.572  1.00 103.66 ?  305 PHE D CE2 1 
ATOM   17016 C  CZ  . PHE D  1  305 ? 27.014  79.132  25.291  1.00 99.19  ?  305 PHE D CZ  1 
ATOM   17017 N  N   . GLU D  1  306 ? 25.168  84.849  29.603  1.00 120.16 ?  306 GLU D N   1 
ATOM   17018 C  CA  . GLU D  1  306 ? 24.450  85.808  30.476  1.00 115.77 ?  306 GLU D CA  1 
ATOM   17019 C  C   . GLU D  1  306 ? 24.235  87.093  29.678  1.00 120.62 ?  306 GLU D C   1 
ATOM   17020 O  O   . GLU D  1  306 ? 25.089  87.409  28.827  1.00 124.44 ?  306 GLU D O   1 
ATOM   17021 C  CB  . GLU D  1  306 ? 25.258  86.084  31.744  1.00 117.55 ?  306 GLU D CB  1 
ATOM   17022 C  CG  . GLU D  1  306 ? 24.872  85.195  32.911  1.00 124.59 ?  306 GLU D CG  1 
ATOM   17023 C  CD  . GLU D  1  306 ? 25.457  85.628  34.245  1.00 136.83 ?  306 GLU D CD  1 
ATOM   17024 O  OE1 . GLU D  1  306 ? 26.659  85.956  34.282  1.00 121.50 ?  306 GLU D OE1 1 
ATOM   17025 O  OE2 . GLU D  1  306 ? 24.709  85.636  35.242  1.00 149.33 ?  306 GLU D OE2 1 
ATOM   17026 N  N   . GLY D  1  307 ? 23.133  87.793  29.936  1.00 121.09 ?  307 GLY D N   1 
ATOM   17027 C  CA  . GLY D  1  307 ? 22.838  89.042  29.249  1.00 136.94 ?  307 GLY D CA  1 
ATOM   17028 C  C   . GLY D  1  307 ? 22.654  88.825  27.762  1.00 124.73 ?  307 GLY D C   1 
ATOM   17029 O  O   . GLY D  1  307 ? 23.052  89.664  26.951  1.00 129.38 ?  307 GLY D O   1 
ATOM   17030 N  N   . GLU D  1  308 ? 22.077  87.670  27.418  1.00 125.29 ?  308 GLU D N   1 
ATOM   17031 C  CA  . GLU D  1  308 ? 21.838  87.333  25.992  1.00 133.68 ?  308 GLU D CA  1 
ATOM   17032 C  C   . GLU D  1  308 ? 20.813  88.311  25.417  1.00 139.10 ?  308 GLU D C   1 
ATOM   17033 O  O   . GLU D  1  308 ? 19.831  88.621  26.119  1.00 142.07 ?  308 GLU D O   1 
ATOM   17034 C  CB  . GLU D  1  308 ? 21.341  85.892  25.865  1.00 134.83 ?  308 GLU D CB  1 
ATOM   17035 C  CG  . GLU D  1  308 ? 22.405  84.922  25.384  1.00 134.20 ?  308 GLU D CG  1 
ATOM   17036 C  CD  . GLU D  1  308 ? 21.888  83.532  25.056  1.00 140.29 ?  308 GLU D CD  1 
ATOM   17037 O  OE1 . GLU D  1  308 ? 21.764  82.714  25.987  1.00 144.31 ?  308 GLU D OE1 1 
ATOM   17038 O  OE2 . GLU D  1  308 ? 21.612  83.270  23.869  1.00 140.54 ?  308 GLU D OE2 1 
ATOM   17039 N  N   . ARG D  1  309 ? 21.030  88.762  24.177  1.00 142.23 ?  309 ARG D N   1 
ATOM   17040 C  CA  . ARG D  1  309 ? 20.105  89.729  23.528  1.00 155.95 ?  309 ARG D CA  1 
ATOM   17041 C  C   . ARG D  1  309 ? 19.182  88.978  22.564  1.00 154.34 ?  309 ARG D C   1 
ATOM   17042 O  O   . ARG D  1  309 ? 19.382  89.100  21.341  1.00 162.92 ?  309 ARG D O   1 
ATOM   17043 C  CB  . ARG D  1  309 ? 20.905  90.817  22.809  1.00 172.03 ?  309 ARG D CB  1 
ATOM   17044 C  CG  . ARG D  1  309 ? 21.755  91.663  23.745  1.00 178.67 ?  309 ARG D CG  1 
ATOM   17045 C  CD  . ARG D  1  309 ? 20.895  92.486  24.685  1.00 179.76 ?  309 ARG D CD  1 
ATOM   17046 N  NE  . ARG D  1  309 ? 21.698  93.319  25.566  1.00 181.63 ?  309 ARG D NE  1 
ATOM   17047 C  CZ  . ARG D  1  309 ? 21.174  94.051  26.535  1.00 163.77 ?  309 ARG D CZ  1 
ATOM   17048 N  NH1 . ARG D  1  309 ? 19.863  94.082  26.672  1.00 161.50 ?  309 ARG D NH1 1 
ATOM   17049 N  NH2 . ARG D  1  309 ? 21.950  94.738  27.357  1.00 161.90 ?  309 ARG D NH2 1 
ATOM   17050 N  N   . ILE D  1  310 ? 18.213  88.234  23.101  1.00 132.19 ?  310 ILE D N   1 
ATOM   17051 C  CA  . ILE D  1  310 ? 17.273  87.481  22.277  1.00 128.32 ?  310 ILE D CA  1 
ATOM   17052 C  C   . ILE D  1  310 ? 16.311  88.503  21.674  1.00 142.99 ?  310 ILE D C   1 
ATOM   17053 O  O   . ILE D  1  310 ? 15.388  88.957  22.347  1.00 141.56 ?  310 ILE D O   1 
ATOM   17054 C  CB  . ILE D  1  310 ? 16.548  86.391  23.115  1.00 115.53 ?  310 ILE D CB  1 
ATOM   17055 C  CG1 . ILE D  1  310 ? 17.558  85.466  23.843  1.00 111.63 ?  310 ILE D CG1 1 
ATOM   17056 C  CG2 . ILE D  1  310 ? 15.587  85.579  22.248  1.00 118.77 ?  310 ILE D CG2 1 
ATOM   17057 C  CD1 . ILE D  1  310 ? 18.618  84.776  22.968  1.00 125.99 ?  310 ILE D CD1 1 
ATOM   17058 N  N   . ARG D  1  311 ? 16.553  88.880  20.415  1.00 154.38 ?  311 ARG D N   1 
ATOM   17059 C  CA  . ARG D  1  311 ? 15.723  89.939  19.778  1.00 161.96 ?  311 ARG D CA  1 
ATOM   17060 C  C   . ARG D  1  311 ? 14.511  89.325  19.067  1.00 163.84 ?  311 ARG D C   1 
ATOM   17061 O  O   . ARG D  1  311 ? 14.495  88.092  18.890  1.00 161.25 ?  311 ARG D O   1 
ATOM   17062 C  CB  . ARG D  1  311 ? 16.567  90.747  18.785  1.00 166.57 ?  311 ARG D CB  1 
ATOM   17063 C  CG  . ARG D  1  311 ? 17.843  91.331  19.376  1.00 163.43 ?  311 ARG D CG  1 
ATOM   17064 C  CD  . ARG D  1  311 ? 17.606  92.415  20.415  1.00 187.54 ?  311 ARG D CD  1 
ATOM   17065 N  NE  . ARG D  1  311 ? 18.641  93.438  20.462  1.00 191.95 ?  311 ARG D NE  1 
ATOM   17066 C  CZ  . ARG D  1  311 ? 19.009  94.099  21.554  1.00 191.98 ?  311 ARG D CZ  1 
ATOM   17067 N  NH1 . ARG D  1  311 ? 18.335  93.959  22.681  1.00 210.92 ?  311 ARG D NH1 1 
ATOM   17068 N  NH2 . ARG D  1  311 ? 20.065  94.891  21.508  1.00 166.98 ?  311 ARG D NH2 1 
ATOM   17069 N  N   . LYS D  1  312 ? 13.546  90.157  18.666  1.00 159.89 ?  312 LYS D N   1 
ATOM   17070 C  CA  . LYS D  1  312 ? 12.289  89.676  18.033  1.00 164.30 ?  312 LYS D CA  1 
ATOM   17071 C  C   . LYS D  1  312 ? 12.535  88.648  16.924  1.00 162.00 ?  312 LYS D C   1 
ATOM   17072 O  O   . LYS D  1  312 ? 11.994  87.531  17.039  1.00 160.48 ?  312 LYS D O   1 
ATOM   17073 C  CB  . LYS D  1  312 ? 11.491  90.863  17.483  1.00 175.58 ?  312 LYS D CB  1 
ATOM   17074 C  CG  . LYS D  1  312 ? 12.330  92.015  16.947  1.00 180.29 ?  312 LYS D CG  1 
ATOM   17075 C  CD  . LYS D  1  312 ? 12.520  93.133  17.948  1.00 180.86 ?  312 LYS D CD  1 
ATOM   17076 C  CE  . LYS D  1  312 ? 13.144  94.372  17.342  1.00 188.77 ?  312 LYS D CE  1 
ATOM   17077 N  NZ  . LYS D  1  312 ? 12.704  95.604  18.038  1.00 185.12 ?  312 LYS D NZ  1 
ATOM   17078 N  N   . ASN D  1  313 ? 13.308  88.996  15.890  1.00 166.53 ?  313 ASN D N   1 
ATOM   17079 C  CA  . ASN D  1  313 ? 13.435  88.066  14.769  1.00 175.86 ?  313 ASN D CA  1 
ATOM   17080 C  C   . ASN D  1  313 ? 14.050  86.728  15.188  1.00 172.73 ?  313 ASN D C   1 
ATOM   17081 O  O   . ASN D  1  313 ? 13.547  85.675  14.788  1.00 163.61 ?  313 ASN D O   1 
ATOM   17082 C  CB  . ASN D  1  313 ? 14.238  88.703  13.633  1.00 179.61 ?  313 ASN D CB  1 
ATOM   17083 C  CG  . ASN D  1  313 ? 14.072  87.998  12.308  1.00 185.16 ?  313 ASN D CG  1 
ATOM   17084 O  OD1 . ASN D  1  313 ? 13.158  87.189  12.114  1.00 175.69 ?  313 ASN D OD1 1 
ATOM   17085 N  ND2 . ASN D  1  313 ? 14.954  88.289  11.361  1.00 192.99 ?  313 ASN D ND2 1 
ATOM   17086 N  N   . ASP D  1  314 ? 15.124  86.758  15.992  1.00 166.31 ?  314 ASP D N   1 
ATOM   17087 C  CA  . ASP D  1  314 ? 15.789  85.534  16.453  1.00 165.02 ?  314 ASP D CA  1 
ATOM   17088 C  C   . ASP D  1  314 ? 15.016  84.802  17.567  1.00 158.08 ?  314 ASP D C   1 
ATOM   17089 O  O   . ASP D  1  314 ? 15.483  83.766  18.038  1.00 143.52 ?  314 ASP D O   1 
ATOM   17090 C  CB  . ASP D  1  314 ? 17.211  85.856  16.949  1.00 164.65 ?  314 ASP D CB  1 
ATOM   17091 C  CG  . ASP D  1  314 ? 18.160  86.319  15.863  1.00 172.08 ?  314 ASP D CG  1 
ATOM   17092 O  OD1 . ASP D  1  314 ? 18.095  85.767  14.742  1.00 188.22 ?  314 ASP D OD1 1 
ATOM   17093 O  OD2 . ASP D  1  314 ? 18.975  87.226  16.137  1.00 164.46 ?  314 ASP D OD2 1 
ATOM   17094 N  N   . MET D  1  315 ? 13.830  85.303  17.906  1.00 166.24 ?  315 MET D N   1 
ATOM   17095 C  CA  . MET D  1  315 ? 13.092  84.681  19.033  1.00 150.21 ?  315 MET D CA  1 
ATOM   17096 C  C   . MET D  1  315 ? 11.893  83.882  18.518  1.00 137.27 ?  315 MET D C   1 
ATOM   17097 O  O   . MET D  1  315 ? 11.386  84.209  17.427  1.00 140.72 ?  315 MET D O   1 
ATOM   17098 C  CB  . MET D  1  315 ? 12.636  85.744  20.035  1.00 152.78 ?  315 MET D CB  1 
ATOM   17099 C  CG  . MET D  1  315 ? 11.181  86.099  19.927  1.00 157.23 ?  315 MET D CG  1 
ATOM   17100 S  SD  . MET D  1  315 ? 10.809  87.264  21.242  1.00 140.48 ?  315 MET D SD  1 
ATOM   17101 C  CE  . MET D  1  315 ? 9.219   87.903  20.710  1.00 134.65 ?  315 MET D CE  1 
ATOM   17102 N  N   . LEU D  1  316 ? 11.474  82.870  19.276  1.00 123.15 ?  316 LEU D N   1 
ATOM   17103 C  CA  . LEU D  1  316 ? 10.359  82.008  18.909  1.00 121.88 ?  316 LEU D CA  1 
ATOM   17104 C  C   . LEU D  1  316 ? 9.183   82.233  19.859  1.00 131.14 ?  316 LEU D C   1 
ATOM   17105 O  O   . LEU D  1  316 ? 8.061   82.421  19.395  1.00 143.99 ?  316 LEU D O   1 
ATOM   17106 C  CB  . LEU D  1  316 ? 10.793  80.532  18.942  1.00 120.96 ?  316 LEU D CB  1 
ATOM   17107 C  CG  . LEU D  1  316 ? 9.701   79.499  18.653  1.00 125.28 ?  316 LEU D CG  1 
ATOM   17108 C  CD1 . LEU D  1  316 ? 9.179   79.629  17.229  1.00 146.91 ?  316 LEU D CD1 1 
ATOM   17109 C  CD2 . LEU D  1  316 ? 10.215  78.095  18.878  1.00 127.75 ?  316 LEU D CD2 1 
ATOM   17110 N  N   . ALA D  1  317 ? 9.431   82.218  21.180  1.00 126.86 ?  317 ALA D N   1 
ATOM   17111 C  CA  . ALA D  1  317 ? 8.371   82.412  22.169  1.00 124.97 ?  317 ALA D CA  1 
ATOM   17112 C  C   . ALA D  1  317 ? 8.670   83.554  23.132  1.00 115.89 ?  317 ALA D C   1 
ATOM   17113 O  O   . ALA D  1  317 ? 9.820   83.760  23.513  1.00 115.06 ?  317 ALA D O   1 
ATOM   17114 C  CB  . ALA D  1  317 ? 8.152   81.131  22.952  1.00 120.81 ?  317 ALA D CB  1 
ATOM   17115 N  N   . GLU D  1  318 ? 7.598   84.247  23.527  1.00 112.84 ?  318 GLU D N   1 
ATOM   17116 C  CA  . GLU D  1  318 ? 7.728   85.391  24.461  1.00 94.81  ?  318 GLU D CA  1 
ATOM   17117 C  C   . GLU D  1  318 ? 6.764   85.182  25.629  1.00 96.71  ?  318 GLU D C   1 
ATOM   17118 O  O   . GLU D  1  318 ? 5.653   84.671  25.391  1.00 100.56 ?  318 GLU D O   1 
ATOM   17119 C  CB  . GLU D  1  318 ? 7.404   86.685  23.719  1.00 89.66  ?  318 GLU D CB  1 
ATOM   17120 C  CG  . GLU D  1  318 ? 7.580   87.932  24.556  1.00 87.98  ?  318 GLU D CG  1 
ATOM   17121 C  CD  . GLU D  1  318 ? 7.556   89.196  23.716  1.00 107.33 ?  318 GLU D CD  1 
ATOM   17122 O  OE1 . GLU D  1  318 ? 6.873   89.199  22.677  1.00 117.93 ?  318 GLU D OE1 1 
ATOM   17123 O  OE2 . GLU D  1  318 ? 8.228   90.163  24.096  1.00 105.41 ?  318 GLU D OE2 1 
ATOM   17124 N  N   . PHE D  1  319 ? 7.179   85.553  26.837  1.00 93.70  ?  319 PHE D N   1 
ATOM   17125 C  CA  . PHE D  1  319 ? 6.355   85.421  28.040  1.00 91.99  ?  319 PHE D CA  1 
ATOM   17126 C  C   . PHE D  1  319 ? 6.615   86.635  28.921  1.00 87.87  ?  319 PHE D C   1 
ATOM   17127 O  O   . PHE D  1  319 ? 7.741   87.109  28.992  1.00 90.76  ?  319 PHE D O   1 
ATOM   17128 C  CB  . PHE D  1  319 ? 6.687   84.142  28.826  1.00 82.79  ?  319 PHE D CB  1 
ATOM   17129 C  CG  . PHE D  1  319 ? 6.984   82.913  27.999  1.00 95.77  ?  319 PHE D CG  1 
ATOM   17130 C  CD1 . PHE D  1  319 ? 8.258   82.671  27.520  1.00 103.65 ?  319 PHE D CD1 1 
ATOM   17131 C  CD2 . PHE D  1  319 ? 5.996   81.983  27.731  1.00 98.97  ?  319 PHE D CD2 1 
ATOM   17132 C  CE1 . PHE D  1  319 ? 8.529   81.543  26.761  1.00 107.77 ?  319 PHE D CE1 1 
ATOM   17133 C  CE2 . PHE D  1  319 ? 6.271   80.854  26.975  1.00 89.32  ?  319 PHE D CE2 1 
ATOM   17134 C  CZ  . PHE D  1  319 ? 7.536   80.638  26.499  1.00 89.77  ?  319 PHE D CZ  1 
ATOM   17135 N  N   . GLY D  1  320 ? 5.571   87.083  29.621  1.00 82.46  ?  320 GLY D N   1 
ATOM   17136 C  CA  . GLY D  1  320 ? 5.708   88.258  30.498  1.00 90.93  ?  320 GLY D CA  1 
ATOM   17137 C  C   . GLY D  1  320 ? 5.718   89.535  29.683  1.00 87.23  ?  320 GLY D C   1 
ATOM   17138 O  O   . GLY D  1  320 ? 5.303   89.493  28.509  1.00 87.94  ?  320 GLY D O   1 
ATOM   17139 N  N   . GLY D  1  321 ? 6.173   90.631  30.288  1.00 88.25  ?  321 GLY D N   1 
ATOM   17140 C  CA  . GLY D  1  321 ? 6.227   91.917  29.574  1.00 84.08  ?  321 GLY D CA  1 
ATOM   17141 C  C   . GLY D  1  321 ? 4.839   92.489  29.359  1.00 106.67 ?  321 GLY D C   1 
ATOM   17142 O  O   . GLY D  1  321 ? 3.866   91.873  29.835  1.00 110.84 ?  321 GLY D O   1 
ATOM   17143 N  N   . ASN D  1  322 ? 4.750   93.627  28.668  1.00 115.17 ?  322 ASN D N   1 
ATOM   17144 C  CA  . ASN D  1  322 ? 3.426   94.220  28.352  1.00 130.70 ?  322 ASN D CA  1 
ATOM   17145 C  C   . ASN D  1  322 ? 2.872   93.389  27.192  1.00 132.47 ?  322 ASN D C   1 
ATOM   17146 O  O   . ASN D  1  322 ? 2.486   93.989  26.169  1.00 136.08 ?  322 ASN D O   1 
ATOM   17147 C  CB  . ASN D  1  322 ? 3.546   95.692  27.952  1.00 153.80 ?  322 ASN D CB  1 
ATOM   17148 C  CG  . ASN D  1  322 ? 2.283   96.480  28.226  1.00 185.54 ?  322 ASN D CG  1 
ATOM   17149 O  OD1 . ASN D  1  322 ? 1.855   96.598  29.372  1.00 177.04 ?  322 ASN D OD1 1 
ATOM   17150 N  ND2 . ASN D  1  322 ? 1.678   97.021  27.181  1.00 181.69 ?  322 ASN D ND2 1 
ATOM   17151 N  N   . LYS D  1  323 ? 2.845   92.062  27.344  1.00 110.83 ?  323 LYS D N   1 
ATOM   17152 C  CA  . LYS D  1  323 ? 2.374   91.202  26.259  1.00 102.41 ?  323 LYS D CA  1 
ATOM   17153 C  C   . LYS D  1  323 ? 1.460   90.128  26.862  1.00 104.20 ?  323 LYS D C   1 
ATOM   17154 O  O   . LYS D  1  323 ? 0.325   89.975  26.412  1.00 114.64 ?  323 LYS D O   1 
ATOM   17155 C  CB  . LYS D  1  323 ? 3.497   90.537  25.445  1.00 93.15  ?  323 LYS D CB  1 
ATOM   17156 C  CG  . LYS D  1  323 ? 4.422   91.510  24.718  1.00 112.90 ?  323 LYS D CG  1 
ATOM   17157 C  CD  . LYS D  1  323 ? 3.696   92.321  23.650  1.00 127.21 ?  323 LYS D CD  1 
ATOM   17158 C  CE  . LYS D  1  323 ? 4.630   93.230  22.884  1.00 130.94 ?  323 LYS D CE  1 
ATOM   17159 N  NZ  . LYS D  1  323 ? 3.920   94.042  21.855  1.00 139.00 ?  323 LYS D NZ  1 
ATOM   17160 N  N   . THR D  1  324 ? 1.946   89.383  27.869  1.00 95.34  ?  324 THR D N   1 
ATOM   17161 C  CA  . THR D  1  324 ? 1.155   88.339  28.523  1.00 93.54  ?  324 THR D CA  1 
ATOM   17162 C  C   . THR D  1  324 ? 1.478   88.263  30.018  1.00 90.75  ?  324 THR D C   1 
ATOM   17163 O  O   . THR D  1  324 ? 2.501   88.780  30.457  1.00 100.43 ?  324 THR D O   1 
ATOM   17164 C  CB  . THR D  1  324 ? 1.339   86.991  27.812  1.00 92.09  ?  324 THR D CB  1 
ATOM   17165 O  OG1 . THR D  1  324 ? 0.432   86.044  28.379  1.00 121.75 ?  324 THR D OG1 1 
ATOM   17166 C  CG2 . THR D  1  324 ? 2.742   86.460  27.923  1.00 83.43  ?  324 THR D CG2 1 
ATOM   17167 N  N   . LYS D  1  325 ? 0.601   87.632  30.802  1.00 90.21  ?  325 LYS D N   1 
ATOM   17168 C  CA  . LYS D  1  325 ? 0.797   87.524  32.244  1.00 77.05  ?  325 LYS D CA  1 
ATOM   17169 C  C   . LYS D  1  325 ? 1.805   86.431  32.583  1.00 88.23  ?  325 LYS D C   1 
ATOM   17170 O  O   . LYS D  1  325 ? 1.632   85.287  32.171  1.00 100.70 ?  325 LYS D O   1 
ATOM   17171 C  CB  . LYS D  1  325 ? -0.544  87.259  32.946  1.00 96.28  ?  325 LYS D CB  1 
ATOM   17172 C  CG  . LYS D  1  325 ? -1.538  88.410  32.799  1.00 108.56 ?  325 LYS D CG  1 
ATOM   17173 C  CD  . LYS D  1  325 ? -2.904  88.082  33.391  1.00 126.30 ?  325 LYS D CD  1 
ATOM   17174 C  CE  . LYS D  1  325 ? -3.876  89.231  33.237  1.00 141.93 ?  325 LYS D CE  1 
ATOM   17175 N  NZ  . LYS D  1  325 ? -5.202  88.933  33.844  1.00 111.99 ?  325 LYS D NZ  1 
ATOM   17176 N  N   . ALA D  1  326 ? 2.864   86.782  33.330  1.00 95.47  ?  326 ALA D N   1 
ATOM   17177 C  CA  . ALA D  1  326 ? 3.898   85.827  33.728  1.00 90.88  ?  326 ALA D CA  1 
ATOM   17178 C  C   . ALA D  1  326 ? 4.346   86.074  35.161  1.00 92.07  ?  326 ALA D C   1 
ATOM   17179 O  O   . ALA D  1  326 ? 4.348   87.214  35.619  1.00 84.75  ?  326 ALA D O   1 
ATOM   17180 C  CB  . ALA D  1  326 ? 5.089   85.924  32.795  1.00 81.93  ?  326 ALA D CB  1 
ATOM   17181 N  N   . TRP D  1  327 ? 4.737   85.005  35.868  1.00 86.30  ?  327 TRP D N   1 
ATOM   17182 C  CA  . TRP D  1  327 ? 5.169   85.124  37.254  1.00 82.29  ?  327 TRP D CA  1 
ATOM   17183 C  C   . TRP D  1  327 ? 6.096   83.986  37.683  1.00 99.20  ?  327 TRP D C   1 
ATOM   17184 O  O   . TRP D  1  327 ? 6.246   83.001  36.964  1.00 110.18 ?  327 TRP D O   1 
ATOM   17185 C  CB  . TRP D  1  327 ? 3.938   85.187  38.180  1.00 97.53  ?  327 TRP D CB  1 
ATOM   17186 C  CG  . TRP D  1  327 ? 2.995   84.024  38.053  1.00 104.81 ?  327 TRP D CG  1 
ATOM   17187 C  CD1 . TRP D  1  327 ? 1.897   83.945  37.249  1.00 100.88 ?  327 TRP D CD1 1 
ATOM   17188 C  CD2 . TRP D  1  327 ? 3.016   82.814  38.823  1.00 112.03 ?  327 TRP D CD2 1 
ATOM   17189 N  NE1 . TRP D  1  327 ? 1.255   82.744  37.442  1.00 99.67  ?  327 TRP D NE1 1 
ATOM   17190 C  CE2 . TRP D  1  327 ? 1.922   82.032  38.405  1.00 102.03 ?  327 TRP D CE2 1 
ATOM   17191 C  CE3 . TRP D  1  327 ? 3.864   82.310  39.817  1.00 114.58 ?  327 TRP D CE3 1 
ATOM   17192 C  CZ2 . TRP D  1  327 ? 1.657   80.775  38.943  1.00 104.02 ?  327 TRP D CZ2 1 
ATOM   17193 C  CZ3 . TRP D  1  327 ? 3.601   81.062  40.345  1.00 104.99 ?  327 TRP D CZ3 1 
ATOM   17194 C  CH2 . TRP D  1  327 ? 2.508   80.310  39.910  1.00 105.67 ?  327 TRP D CH2 1 
ATOM   17195 N  N   . GLU D  1  328 ? 6.726   84.135  38.859  1.00 88.91  ?  328 GLU D N   1 
ATOM   17196 C  CA  . GLU D  1  328 ? 7.624   83.134  39.431  1.00 86.30  ?  328 GLU D CA  1 
ATOM   17197 C  C   . GLU D  1  328 ? 7.456   83.121  40.956  1.00 94.20  ?  328 GLU D C   1 
ATOM   17198 O  O   . GLU D  1  328 ? 7.068   84.137  41.531  1.00 99.02  ?  328 GLU D O   1 
ATOM   17199 C  CB  . GLU D  1  328 ? 9.084   83.406  39.023  1.00 83.35  ?  328 GLU D CB  1 
ATOM   17200 C  CG  . GLU D  1  328 ? 9.673   84.690  39.584  1.00 100.34 ?  328 GLU D CG  1 
ATOM   17201 C  CD  . GLU D  1  328 ? 11.067  85.010  39.078  1.00 99.14  ?  328 GLU D CD  1 
ATOM   17202 O  OE1 . GLU D  1  328 ? 11.446  84.486  38.006  1.00 86.68  ?  328 GLU D OE1 1 
ATOM   17203 O  OE2 . GLU D  1  328 ? 11.779  85.789  39.753  1.00 97.55  ?  328 GLU D OE2 1 
ATOM   17204 N  N   . LEU D  1  329 ? 7.727   81.979  41.611  1.00 97.83  ?  329 LEU D N   1 
ATOM   17205 C  CA  . LEU D  1  329 ? 7.573   81.871  43.064  1.00 90.31  ?  329 LEU D CA  1 
ATOM   17206 C  C   . LEU D  1  329 ? 8.282   80.640  43.636  1.00 98.03  ?  329 LEU D C   1 
ATOM   17207 O  O   . LEU D  1  329 ? 8.370   79.615  42.968  1.00 112.75 ?  329 LEU D O   1 
ATOM   17208 C  CB  . LEU D  1  329 ? 6.068   81.799  43.398  1.00 94.11  ?  329 LEU D CB  1 
ATOM   17209 C  CG  . LEU D  1  329 ? 5.676   81.463  44.845  1.00 106.85 ?  329 LEU D CG  1 
ATOM   17210 C  CD1 . LEU D  1  329 ? 5.866   82.657  45.758  1.00 101.40 ?  329 LEU D CD1 1 
ATOM   17211 C  CD2 . LEU D  1  329 ? 4.250   80.947  44.914  1.00 118.04 ?  329 LEU D CD2 1 
ATOM   17212 N  N   . VAL D  1  330 ? 8.769   80.743  44.882  1.00 99.53  ?  330 VAL D N   1 
ATOM   17213 C  CA  . VAL D  1  330 ? 9.420   79.644  45.595  1.00 108.62 ?  330 VAL D CA  1 
ATOM   17214 C  C   . VAL D  1  330 ? 8.678   79.494  46.927  1.00 124.42 ?  330 VAL D C   1 
ATOM   17215 O  O   . VAL D  1  330 ? 8.522   80.477  47.650  1.00 121.21 ?  330 VAL D O   1 
ATOM   17216 C  CB  . VAL D  1  330 ? 10.932  79.881  45.805  1.00 111.70 ?  330 VAL D CB  1 
ATOM   17217 C  CG1 . VAL D  1  330 ? 11.506  78.874  46.799  1.00 112.98 ?  330 VAL D CG1 1 
ATOM   17218 C  CG2 . VAL D  1  330 ? 11.682  79.813  44.479  1.00 115.64 ?  330 VAL D CG2 1 
ATOM   17219 N  N   . MET D  1  331 ? 8.208   78.274  47.240  1.00 130.97 ?  331 MET D N   1 
ATOM   17220 C  CA  . MET D  1  331 ? 7.449   77.997  48.459  1.00 129.22 ?  331 MET D CA  1 
ATOM   17221 C  C   . MET D  1  331 ? 8.145   77.028  49.406  1.00 138.58 ?  331 MET D C   1 
ATOM   17222 O  O   . MET D  1  331 ? 8.906   76.164  48.974  1.00 137.93 ?  331 MET D O   1 
ATOM   17223 C  CB  . MET D  1  331 ? 6.085   77.395  48.093  1.00 120.39 ?  331 MET D CB  1 
ATOM   17224 C  CG  . MET D  1  331 ? 5.137   78.376  47.454  1.00 119.24 ?  331 MET D CG  1 
ATOM   17225 S  SD  . MET D  1  331 ? 3.576   77.611  46.964  1.00 145.09 ?  331 MET D SD  1 
ATOM   17226 C  CE  . MET D  1  331 ? 2.859   77.308  48.548  1.00 151.08 ?  331 MET D CE  1 
ATOM   17227 N  N   . CYS D  1  332 ? 7.848   77.169  50.704  1.00 141.79 ?  332 CYS D N   1 
ATOM   17228 C  CA  . CYS D  1  332 ? 8.366   76.323  51.771  1.00 136.80 ?  332 CYS D CA  1 
ATOM   17229 C  C   . CYS D  1  332 ? 7.247   75.337  52.098  1.00 134.96 ?  332 CYS D C   1 
ATOM   17230 O  O   . CYS D  1  332 ? 6.127   75.761  52.375  1.00 134.08 ?  332 CYS D O   1 
ATOM   17231 C  CB  . CYS D  1  332 ? 8.737   77.173  52.985  1.00 141.48 ?  332 CYS D CB  1 
ATOM   17232 S  SG  . CYS D  1  332 ? 9.666   76.287  54.262  1.00 159.63 ?  332 CYS D SG  1 
ATOM   17233 N  N   . ALA D  1  333 ? 7.527   74.032  52.039  1.00 155.46 ?  333 ALA D N   1 
ATOM   17234 C  CA  . ALA D  1  333 ? 6.511   73.012  52.302  1.00 164.57 ?  333 ALA D CA  1 
ATOM   17235 C  C   . ALA D  1  333 ? 7.109   71.765  52.977  1.00 172.33 ?  333 ALA D C   1 
ATOM   17236 O  O   . ALA D  1  333 ? 8.325   71.585  52.971  1.00 179.30 ?  333 ALA D O   1 
ATOM   17237 C  CB  . ALA D  1  333 ? 5.835   72.629  50.991  1.00 171.04 ?  333 ALA D CB  1 
ATOM   17238 N  N   . ASP D  1  334 ? 6.255   70.908  53.562  1.00 172.94 ?  334 ASP D N   1 
ATOM   17239 C  CA  . ASP D  1  334 ? 6.704   69.688  54.235  1.00 167.36 ?  334 ASP D CA  1 
ATOM   17240 C  C   . ASP D  1  334 ? 7.078   68.598  53.210  1.00 172.00 ?  334 ASP D C   1 
ATOM   17241 O  O   . ASP D  1  334 ? 6.745   68.719  52.032  1.00 171.52 ?  334 ASP D O   1 
ATOM   17242 C  CB  . ASP D  1  334 ? 5.601   69.185  55.188  1.00 170.89 ?  334 ASP D CB  1 
ATOM   17243 C  CG  . ASP D  1  334 ? 6.105   68.427  56.401  1.00 178.06 ?  334 ASP D CG  1 
ATOM   17244 O  OD1 . ASP D  1  334 ? 7.202   68.761  56.898  1.00 180.74 ?  334 ASP D OD1 1 
ATOM   17245 O  OD2 . ASP D  1  334 ? 5.395   67.503  56.860  1.00 160.24 ?  334 ASP D OD2 1 
ATOM   17246 N  N   . GLN D  1  335 ? 7.770   67.536  53.660  1.00 190.27 ?  335 GLN D N   1 
ATOM   17247 C  CA  . GLN D  1  335 ? 8.200   66.440  52.784  1.00 191.38 ?  335 GLN D CA  1 
ATOM   17248 C  C   . GLN D  1  335 ? 7.049   65.738  52.036  1.00 190.21 ?  335 GLN D C   1 
ATOM   17249 O  O   . GLN D  1  335 ? 7.293   65.087  51.021  1.00 189.30 ?  335 GLN D O   1 
ATOM   17250 C  CB  . GLN D  1  335 ? 9.058   65.414  53.558  1.00 196.21 ?  335 GLN D CB  1 
ATOM   17251 C  CG  . GLN D  1  335 ? 10.424  65.916  54.042  1.00 196.48 ?  335 GLN D CG  1 
ATOM   17252 C  CD  . GLN D  1  335 ? 11.186  64.895  54.852  1.00 209.10 ?  335 GLN D CD  1 
ATOM   17253 O  OE1 . GLN D  1  335 ? 10.600  63.995  55.463  1.00 203.42 ?  335 GLN D OE1 1 
ATOM   17254 N  NE2 . GLN D  1  335 ? 12.510  64.999  54.868  1.00 222.34 ?  335 GLN D NE2 1 
ATOM   17255 N  N   . GLY D  1  336 ? 5.823   65.873  52.532  1.00 186.84 ?  336 GLY D N   1 
ATOM   17256 C  CA  . GLY D  1  336 ? 4.656   65.255  51.915  1.00 182.41 ?  336 GLY D CA  1 
ATOM   17257 C  C   . GLY D  1  336 ? 4.205   65.940  50.640  1.00 184.43 ?  336 GLY D C   1 
ATOM   17258 O  O   . GLY D  1  336 ? 3.764   65.273  49.702  1.00 184.71 ?  336 GLY D O   1 
ATOM   17259 N  N   . GLU D  1  337 ? 4.302   67.275  50.592  1.00 175.42 ?  337 GLU D N   1 
ATOM   17260 C  CA  . GLU D  1  337 ? 3.890   68.040  49.416  1.00 177.95 ?  337 GLU D CA  1 
ATOM   17261 C  C   . GLU D  1  337 ? 4.918   67.931  48.285  1.00 175.45 ?  337 GLU D C   1 
ATOM   17262 O  O   . GLU D  1  337 ? 4.544   67.924  47.113  1.00 171.35 ?  337 GLU D O   1 
ATOM   17263 C  CB  . GLU D  1  337 ? 3.696   69.521  49.781  1.00 185.35 ?  337 GLU D CB  1 
ATOM   17264 C  CG  . GLU D  1  337 ? 2.618   69.772  50.823  1.00 188.56 ?  337 GLU D CG  1 
ATOM   17265 C  CD  . GLU D  1  337 ? 2.286   71.235  51.049  1.00 196.68 ?  337 GLU D CD  1 
ATOM   17266 O  OE1 . GLU D  1  337 ? 2.590   72.061  50.159  1.00 188.21 ?  337 GLU D OE1 1 
ATOM   17267 O  OE2 . GLU D  1  337 ? 1.718   71.555  52.118  1.00 197.21 ?  337 GLU D OE2 1 
ATOM   17268 N  N   . VAL D  1  338 ? 6.208   67.853  48.636  1.00 164.34 ?  338 VAL D N   1 
ATOM   17269 C  CA  . VAL D  1  338 ? 7.296   67.776  47.660  1.00 160.07 ?  338 VAL D CA  1 
ATOM   17270 C  C   . VAL D  1  338 ? 7.643   66.326  47.306  1.00 167.56 ?  338 VAL D C   1 
ATOM   17271 O  O   . VAL D  1  338 ? 7.920   65.524  48.196  1.00 169.98 ?  338 VAL D O   1 
ATOM   17272 C  CB  . VAL D  1  338 ? 8.534   68.529  48.198  1.00 153.68 ?  338 VAL D CB  1 
ATOM   17273 C  CG1 . VAL D  1  338 ? 9.697   68.453  47.214  1.00 152.61 ?  338 VAL D CG1 1 
ATOM   17274 C  CG2 . VAL D  1  338 ? 8.192   69.980  48.526  1.00 154.24 ?  338 VAL D CG2 1 
ATOM   17275 N  N   . GLU D  1  339 ? 7.641   65.999  46.003  1.00 177.24 ?  339 GLU D N   1 
ATOM   17276 C  CA  . GLU D  1  339 ? 7.961   64.661  45.510  1.00 186.33 ?  339 GLU D CA  1 
ATOM   17277 C  C   . GLU D  1  339 ? 9.326   64.681  44.805  1.00 183.89 ?  339 GLU D C   1 
ATOM   17278 O  O   . GLU D  1  339 ? 9.448   64.203  43.677  1.00 187.73 ?  339 GLU D O   1 
ATOM   17279 C  CB  . GLU D  1  339 ? 6.863   64.178  44.542  1.00 189.34 ?  339 GLU D CB  1 
ATOM   17280 C  CG  . GLU D  1  339 ? 5.477   64.116  45.156  1.00 200.90 ?  339 GLU D CG  1 
ATOM   17281 C  CD  . GLU D  1  339 ? 4.447   63.450  44.265  1.00 208.18 ?  339 GLU D CD  1 
ATOM   17282 O  OE1 . GLU D  1  339 ? 4.577   63.556  43.024  1.00 197.93 ?  339 GLU D OE1 1 
ATOM   17283 O  OE2 . GLU D  1  339 ? 3.508   62.824  44.807  1.00 201.39 ?  339 GLU D OE2 1 
ATOM   17284 N  N   . ASP D  1  340 ? 10.355  65.241  45.471  1.00 165.74 ?  340 ASP D N   1 
ATOM   17285 C  CA  . ASP D  1  340 ? 11.726  65.357  44.948  1.00 158.10 ?  340 ASP D CA  1 
ATOM   17286 C  C   . ASP D  1  340 ? 11.773  65.751  43.442  1.00 159.54 ?  340 ASP D C   1 
ATOM   17287 O  O   . ASP D  1  340 ? 11.047  66.668  43.065  1.00 166.73 ?  340 ASP D O   1 
ATOM   17288 C  CB  . ASP D  1  340 ? 12.531  64.080  45.267  1.00 162.34 ?  340 ASP D CB  1 
ATOM   17289 C  CG  . ASP D  1  340 ? 14.029  64.310  45.290  1.00 154.86 ?  340 ASP D CG  1 
ATOM   17290 O  OD1 . ASP D  1  340 ? 14.512  64.971  46.233  1.00 144.24 ?  340 ASP D OD1 1 
ATOM   17291 O  OD2 . ASP D  1  340 ? 14.715  63.836  44.360  1.00 159.56 ?  340 ASP D OD2 1 
ATOM   17292 N  N   . HIS D  1  341 ? 12.601  65.100  42.589  1.00 154.53 ?  341 HIS D N   1 
ATOM   17293 C  CA  . HIS D  1  341 ? 12.664  65.451  41.170  1.00 148.55 ?  341 HIS D CA  1 
ATOM   17294 C  C   . HIS D  1  341 ? 11.310  65.169  40.519  1.00 145.14 ?  341 HIS D C   1 
ATOM   17295 O  O   . HIS D  1  341 ? 10.956  64.014  40.294  1.00 149.29 ?  341 HIS D O   1 
ATOM   17296 C  CB  . HIS D  1  341 ? 13.787  64.674  40.463  1.00 145.46 ?  341 HIS D CB  1 
ATOM   17297 C  CG  . HIS D  1  341 ? 14.069  65.150  39.070  1.00 139.05 ?  341 HIS D CG  1 
ATOM   17298 N  ND1 . HIS D  1  341 ? 13.925  66.478  38.718  1.00 146.33 ?  341 HIS D ND1 1 
ATOM   17299 C  CD2 . HIS D  1  341 ? 14.494  64.457  37.989  1.00 135.98 ?  341 HIS D CD2 1 
ATOM   17300 C  CE1 . HIS D  1  341 ? 14.253  66.551  37.438  1.00 146.62 ?  341 HIS D CE1 1 
ATOM   17301 N  NE2 . HIS D  1  341 ? 14.603  65.359  36.957  1.00 137.26 ?  341 HIS D NE2 1 
ATOM   17302 N  N   . LYS D  1  342 ? 10.546  66.228  40.249  1.00 138.85 ?  342 LYS D N   1 
ATOM   17303 C  CA  . LYS D  1  342 ? 9.217   66.119  39.660  1.00 143.50 ?  342 LYS D CA  1 
ATOM   17304 C  C   . LYS D  1  342 ? 8.993   67.324  38.743  1.00 141.30 ?  342 LYS D C   1 
ATOM   17305 O  O   . LYS D  1  342 ? 8.977   68.458  39.217  1.00 139.42 ?  342 LYS D O   1 
ATOM   17306 C  CB  . LYS D  1  342 ? 8.172   66.047  40.797  1.00 141.53 ?  342 LYS D CB  1 
ATOM   17307 C  CG  . LYS D  1  342 ? 6.745   66.469  40.445  1.00 142.75 ?  342 LYS D CG  1 
ATOM   17308 C  CD  . LYS D  1  342 ? 5.884   65.304  39.989  1.00 144.00 ?  342 LYS D CD  1 
ATOM   17309 C  CE  . LYS D  1  342 ? 4.506   65.754  39.571  1.00 135.30 ?  342 LYS D CE  1 
ATOM   17310 N  NZ  . LYS D  1  342 ? 3.688   66.228  40.719  1.00 134.94 ?  342 LYS D NZ  1 
ATOM   17311 N  N   . ILE D  1  343 ? 8.844   67.081  37.432  1.00 147.31 ?  343 ILE D N   1 
ATOM   17312 C  CA  . ILE D  1  343 ? 8.631   68.147  36.454  1.00 148.92 ?  343 ILE D CA  1 
ATOM   17313 C  C   . ILE D  1  343 ? 7.266   67.966  35.799  1.00 149.37 ?  343 ILE D C   1 
ATOM   17314 O  O   . ILE D  1  343 ? 7.060   67.001  35.066  1.00 157.97 ?  343 ILE D O   1 
ATOM   17315 C  CB  . ILE D  1  343 ? 9.758   68.157  35.385  1.00 154.57 ?  343 ILE D CB  1 
ATOM   17316 C  CG1 . ILE D  1  343 ? 11.173  68.068  36.017  1.00 147.38 ?  343 ILE D CG1 1 
ATOM   17317 C  CG2 . ILE D  1  343 ? 9.628   69.376  34.467  1.00 142.02 ?  343 ILE D CG2 1 
ATOM   17318 C  CD1 . ILE D  1  343 ? 11.583  69.204  36.970  1.00 133.66 ?  343 ILE D CD1 1 
ATOM   17319 N  N   . GLU D  1  344 ? 6.338   68.892  36.060  1.00 153.28 ?  344 GLU D N   1 
ATOM   17320 C  CA  . GLU D  1  344 ? 4.992   68.841  35.495  1.00 155.97 ?  344 GLU D CA  1 
ATOM   17321 C  C   . GLU D  1  344 ? 4.740   70.122  34.706  1.00 148.94 ?  344 GLU D C   1 
ATOM   17322 O  O   . GLU D  1  344 ? 4.673   71.199  35.293  1.00 145.59 ?  344 GLU D O   1 
ATOM   17323 C  CB  . GLU D  1  344 ? 3.955   68.659  36.622  1.00 160.86 ?  344 GLU D CB  1 
ATOM   17324 C  CG  . GLU D  1  344 ? 2.509   68.942  36.245  1.00 159.05 ?  344 GLU D CG  1 
ATOM   17325 C  CD  . GLU D  1  344 ? 1.929   68.051  35.165  1.00 172.36 ?  344 GLU D CD  1 
ATOM   17326 O  OE1 . GLU D  1  344 ? 1.945   66.811  35.340  1.00 169.82 ?  344 GLU D OE1 1 
ATOM   17327 O  OE2 . GLU D  1  344 ? 1.448   68.592  34.144  1.00 174.93 ?  344 GLU D OE2 1 
ATOM   17328 N  N   . VAL D  1  345 ? 4.610   70.006  33.376  1.00 135.50 ?  345 VAL D N   1 
ATOM   17329 C  CA  . VAL D  1  345 ? 4.366   71.158  32.515  1.00 130.56 ?  345 VAL D CA  1 
ATOM   17330 C  C   . VAL D  1  345 ? 2.878   71.285  32.210  1.00 137.32 ?  345 VAL D C   1 
ATOM   17331 O  O   . VAL D  1  345 ? 2.410   70.815  31.174  1.00 146.67 ?  345 VAL D O   1 
ATOM   17332 C  CB  . VAL D  1  345 ? 5.207   71.079  31.221  1.00 141.06 ?  345 VAL D CB  1 
ATOM   17333 C  CG1 . VAL D  1  345 ? 4.913   72.261  30.299  1.00 135.80 ?  345 VAL D CG1 1 
ATOM   17334 C  CG2 . VAL D  1  345 ? 6.695   71.014  31.551  1.00 134.16 ?  345 VAL D CG2 1 
ATOM   17335 N  N   . ILE D  1  346 ? 2.135   71.921  33.117  1.00 142.00 ?  346 ILE D N   1 
ATOM   17336 C  CA  . ILE D  1  346 ? 0.701   72.144  32.941  1.00 142.28 ?  346 ILE D CA  1 
ATOM   17337 C  C   . ILE D  1  346 ? 0.529   73.188  31.834  1.00 139.27 ?  346 ILE D C   1 
ATOM   17338 O  O   . ILE D  1  346 ? 1.255   74.176  31.804  1.00 136.65 ?  346 ILE D O   1 
ATOM   17339 C  CB  . ILE D  1  346 ? 0.034   72.581  34.286  1.00 129.53 ?  346 ILE D CB  1 
ATOM   17340 C  CG1 . ILE D  1  346 ? -0.219  71.348  35.198  1.00 125.22 ?  346 ILE D CG1 1 
ATOM   17341 C  CG2 . ILE D  1  346 ? -1.274  73.336  34.041  1.00 119.86 ?  346 ILE D CG2 1 
ATOM   17342 C  CD1 . ILE D  1  346 ? -0.086  71.600  36.697  1.00 120.04 ?  346 ILE D CD1 1 
ATOM   17343 N  N   . GLY D  1  347 ? -0.414  72.952  30.933  1.00 136.06 ?  347 GLY D N   1 
ATOM   17344 C  CA  . GLY D  1  347 ? -0.671  73.858  29.824  1.00 139.20 ?  347 GLY D CA  1 
ATOM   17345 C  C   . GLY D  1  347 ? 0.075   73.453  28.567  1.00 147.70 ?  347 GLY D C   1 
ATOM   17346 O  O   . GLY D  1  347 ? 0.803   72.457  28.568  1.00 149.73 ?  347 GLY D O   1 
ATOM   17347 N  N   . PRO D  1  348 ? -0.078  74.204  27.460  1.00 155.50 ?  348 PRO D N   1 
ATOM   17348 C  CA  . PRO D  1  348 ? 0.624   73.824  26.221  1.00 151.35 ?  348 PRO D CA  1 
ATOM   17349 C  C   . PRO D  1  348 ? 2.147   73.940  26.305  1.00 153.97 ?  348 PRO D C   1 
ATOM   17350 O  O   . PRO D  1  348 ? 2.672   74.547  27.235  1.00 154.64 ?  348 PRO D O   1 
ATOM   17351 C  CB  . PRO D  1  348 ? 0.048   74.785  25.169  1.00 145.57 ?  348 PRO D CB  1 
ATOM   17352 C  CG  . PRO D  1  348 ? -1.149  75.417  25.800  1.00 151.58 ?  348 PRO D CG  1 
ATOM   17353 C  CD  . PRO D  1  348 ? -0.904  75.410  27.266  1.00 154.05 ?  348 PRO D CD  1 
ATOM   17354 N  N   . ASP D  1  349 ? 2.858   73.355  25.332  1.00 140.43 ?  349 ASP D N   1 
ATOM   17355 C  CA  . ASP D  1  349 ? 4.320   73.403  25.288  1.00 128.05 ?  349 ASP D CA  1 
ATOM   17356 C  C   . ASP D  1  349 ? 4.777   74.153  24.028  1.00 128.03 ?  349 ASP D C   1 
ATOM   17357 O  O   . ASP D  1  349 ? 3.960   74.449  23.157  1.00 142.37 ?  349 ASP D O   1 
ATOM   17358 C  CB  . ASP D  1  349 ? 4.901   71.975  25.313  1.00 135.63 ?  349 ASP D CB  1 
ATOM   17359 C  CG  . ASP D  1  349 ? 6.288   71.883  25.921  1.00 141.38 ?  349 ASP D CG  1 
ATOM   17360 O  OD1 . ASP D  1  349 ? 7.259   72.268  25.241  1.00 141.65 ?  349 ASP D OD1 1 
ATOM   17361 O  OD2 . ASP D  1  349 ? 6.400   71.422  27.076  1.00 151.79 ?  349 ASP D OD2 1 
ATOM   17362 N  N   . ILE D  1  350 ? 6.075   74.469  23.935  1.00 120.96 ?  350 ILE D N   1 
ATOM   17363 C  CA  . ILE D  1  350 ? 6.633   75.185  22.788  1.00 134.77 ?  350 ILE D CA  1 
ATOM   17364 C  C   . ILE D  1  350 ? 6.386   74.452  21.452  1.00 151.55 ?  350 ILE D C   1 
ATOM   17365 O  O   . ILE D  1  350 ? 6.448   75.086  20.403  1.00 154.04 ?  350 ILE D O   1 
ATOM   17366 C  CB  . ILE D  1  350 ? 8.139   75.518  23.018  1.00 128.65 ?  350 ILE D CB  1 
ATOM   17367 C  CG1 . ILE D  1  350 ? 8.693   76.455  21.923  1.00 133.36 ?  350 ILE D CG1 1 
ATOM   17368 C  CG2 . ILE D  1  350 ? 8.998   74.259  23.114  1.00 142.01 ?  350 ILE D CG2 1 
ATOM   17369 C  CD1 . ILE D  1  350 ? 8.181   77.848  21.973  1.00 124.67 ?  350 ILE D CD1 1 
ATOM   17370 N  N   . ASP D  1  351 ? 6.094   73.143  21.476  1.00 143.62 ?  351 ASP D N   1 
ATOM   17371 C  CA  . ASP D  1  351 ? 5.822   72.398  20.245  1.00 144.80 ?  351 ASP D CA  1 
ATOM   17372 C  C   . ASP D  1  351 ? 4.526   72.899  19.593  1.00 151.02 ?  351 ASP D C   1 
ATOM   17373 O  O   . ASP D  1  351 ? 4.444   72.970  18.368  1.00 155.39 ?  351 ASP D O   1 
ATOM   17374 C  CB  . ASP D  1  351 ? 5.712   70.896  20.535  1.00 161.34 ?  351 ASP D CB  1 
ATOM   17375 C  CG  . ASP D  1  351 ? 6.978   70.293  21.100  1.00 168.84 ?  351 ASP D CG  1 
ATOM   17376 O  OD1 . ASP D  1  351 ? 8.000   70.279  20.382  1.00 171.50 ?  351 ASP D OD1 1 
ATOM   17377 O  OD2 . ASP D  1  351 ? 6.948   69.834  22.262  1.00 168.75 ?  351 ASP D OD2 1 
ATOM   17378 N  N   . THR D  1  352 ? 3.518   73.253  20.416  1.00 160.37 ?  352 THR D N   1 
ATOM   17379 C  CA  . THR D  1  352 ? 2.217   73.759  19.950  1.00 157.95 ?  352 THR D CA  1 
ATOM   17380 C  C   . THR D  1  352 ? 2.350   75.058  19.125  1.00 151.63 ?  352 THR D C   1 
ATOM   17381 O  O   . THR D  1  352 ? 1.444   75.394  18.364  1.00 145.00 ?  352 THR D O   1 
ATOM   17382 C  CB  . THR D  1  352 ? 1.273   73.981  21.156  1.00 134.66 ?  352 THR D CB  1 
ATOM   17383 O  OG1 . THR D  1  352 ? 1.341   72.850  22.028  1.00 135.51 ?  352 THR D OG1 1 
ATOM   17384 C  CG2 . THR D  1  352 ? -0.173  74.213  20.739  1.00 130.40 ?  352 THR D CG2 1 
ATOM   17385 N  N   . ILE D  1  353 ? 3.468   75.785  19.276  1.00 152.36 ?  353 ILE D N   1 
ATOM   17386 C  CA  . ILE D  1  353 ? 3.703   77.039  18.553  1.00 145.03 ?  353 ILE D CA  1 
ATOM   17387 C  C   . ILE D  1  353 ? 3.843   76.772  17.043  1.00 147.96 ?  353 ILE D C   1 
ATOM   17388 O  O   . ILE D  1  353 ? 4.262   75.685  16.644  1.00 148.13 ?  353 ILE D O   1 
ATOM   17389 C  CB  . ILE D  1  353 ? 4.956   77.796  19.137  1.00 139.82 ?  353 ILE D CB  1 
ATOM   17390 C  CG1 . ILE D  1  353 ? 4.794   79.333  19.043  1.00 136.81 ?  353 ILE D CG1 1 
ATOM   17391 C  CG2 . ILE D  1  353 ? 6.256   77.353  18.444  1.00 152.95 ?  353 ILE D CG2 1 
ATOM   17392 C  CD1 . ILE D  1  353 ? 5.666   80.126  20.057  1.00 122.46 ?  353 ILE D CD1 1 
ATOM   17393 N  N   . ASP D  1  354 ? 3.490   77.764  16.214  1.00 158.64 ?  354 ASP D N   1 
ATOM   17394 C  CA  . ASP D  1  354 ? 3.589   77.650  14.755  1.00 166.02 ?  354 ASP D CA  1 
ATOM   17395 C  C   . ASP D  1  354 ? 4.103   78.963  14.151  1.00 169.80 ?  354 ASP D C   1 
ATOM   17396 O  O   . ASP D  1  354 ? 5.021   78.944  13.331  1.00 164.55 ?  354 ASP D O   1 
ATOM   17397 C  CB  . ASP D  1  354 ? 2.231   77.272  14.142  1.00 151.61 ?  354 ASP D CB  1 
ATOM   17398 C  CG  . ASP D  1  354 ? 2.289   77.046  12.645  1.00 168.13 ?  354 ASP D CG  1 
ATOM   17399 O  OD1 . ASP D  1  354 ? 3.272   76.434  12.175  1.00 173.29 ?  354 ASP D OD1 1 
ATOM   17400 O  OD2 . ASP D  1  354 ? 1.349   77.477  11.944  1.00 176.47 ?  354 ASP D OD2 1 
ATOM   17401 N  N   . LYS D  1  355 ? 3.514   80.098  14.558  1.00 174.14 ?  355 LYS D N   1 
ATOM   17402 C  CA  . LYS D  1  355 ? 3.916   81.420  14.080  1.00 176.17 ?  355 LYS D CA  1 
ATOM   17403 C  C   . LYS D  1  355 ? 5.267   81.787  14.714  1.00 173.14 ?  355 LYS D C   1 
ATOM   17404 O  O   . LYS D  1  355 ? 5.555   81.341  15.825  1.00 168.70 ?  355 LYS D O   1 
ATOM   17405 C  CB  . LYS D  1  355 ? 2.847   82.454  14.468  1.00 177.31 ?  355 LYS D CB  1 
ATOM   17406 C  CG  . LYS D  1  355 ? 2.841   83.716  13.617  1.00 172.80 ?  355 LYS D CG  1 
ATOM   17407 C  CD  . LYS D  1  355 ? 2.133   84.855  14.342  1.00 172.25 ?  355 LYS D CD  1 
ATOM   17408 C  CE  . LYS D  1  355 ? 2.328   86.192  13.679  1.00 173.83 ?  355 LYS D CE  1 
ATOM   17409 N  NZ  . LYS D  1  355 ? 1.651   87.270  14.442  1.00 182.27 ?  355 LYS D NZ  1 
ATOM   17410 N  N   . ALA D  1  356 ? 6.097   82.584  14.020  1.00 166.27 ?  356 ALA D N   1 
ATOM   17411 C  CA  . ALA D  1  356 ? 7.410   82.953  14.555  1.00 154.15 ?  356 ALA D CA  1 
ATOM   17412 C  C   . ALA D  1  356 ? 7.349   83.737  15.898  1.00 164.09 ?  356 ALA D C   1 
ATOM   17413 O  O   . ALA D  1  356 ? 7.974   83.287  16.861  1.00 168.45 ?  356 ALA D O   1 
ATOM   17414 C  CB  . ALA D  1  356 ? 8.234   83.703  13.512  1.00 133.48 ?  356 ALA D CB  1 
ATOM   17415 N  N   . PRO D  1  357 ? 6.613   84.870  16.039  1.00 165.44 ?  357 PRO D N   1 
ATOM   17416 C  CA  . PRO D  1  357 ? 6.590   85.567  17.338  1.00 158.25 ?  357 PRO D CA  1 
ATOM   17417 C  C   . PRO D  1  357 ? 5.399   85.179  18.226  1.00 164.22 ?  357 PRO D C   1 
ATOM   17418 O  O   . PRO D  1  357 ? 4.675   86.052  18.701  1.00 173.35 ?  357 PRO D O   1 
ATOM   17419 C  CB  . PRO D  1  357 ? 6.522   87.037  16.919  1.00 163.21 ?  357 PRO D CB  1 
ATOM   17420 C  CG  . PRO D  1  357 ? 5.777   87.021  15.597  1.00 168.55 ?  357 PRO D CG  1 
ATOM   17421 C  CD  . PRO D  1  357 ? 5.797   85.604  15.051  1.00 168.02 ?  357 PRO D CD  1 
ATOM   17422 N  N   . GLY D  1  358 ? 5.201   83.881  18.439  1.00 141.07 ?  358 GLY D N   1 
ATOM   17423 C  CA  . GLY D  1  358 ? 4.105   83.389  19.267  1.00 136.64 ?  358 GLY D CA  1 
ATOM   17424 C  C   . GLY D  1  358 ? 4.334   83.688  20.734  1.00 137.79 ?  358 GLY D C   1 
ATOM   17425 O  O   . GLY D  1  358 ? 5.445   83.518  21.236  1.00 123.49 ?  358 GLY D O   1 
ATOM   17426 N  N   . ARG D  1  359 ? 3.273   84.132  21.416  1.00 143.34 ?  359 ARG D N   1 
ATOM   17427 C  CA  . ARG D  1  359 ? 3.396   84.509  22.849  1.00 117.03 ?  359 ARG D CA  1 
ATOM   17428 C  C   . ARG D  1  359 ? 2.389   83.716  23.686  1.00 115.98 ?  359 ARG D C   1 
ATOM   17429 O  O   . ARG D  1  359 ? 1.248   83.538  23.220  1.00 119.72 ?  359 ARG D O   1 
ATOM   17430 C  CB  . ARG D  1  359 ? 3.180   86.016  23.017  1.00 90.18  ?  359 ARG D CB  1 
ATOM   17431 C  CG  . ARG D  1  359 ? 3.712   86.852  21.862  1.00 103.26 ?  359 ARG D CG  1 
ATOM   17432 C  CD  . ARG D  1  359 ? 3.485   88.324  22.115  1.00 113.46 ?  359 ARG D CD  1 
ATOM   17433 N  NE  . ARG D  1  359 ? 4.597   89.146  21.665  1.00 131.83 ?  359 ARG D NE  1 
ATOM   17434 C  CZ  . ARG D  1  359 ? 4.886   89.393  20.393  1.00 141.90 ?  359 ARG D CZ  1 
ATOM   17435 N  NH1 . ARG D  1  359 ? 4.165   88.849  19.429  1.00 139.50 ?  359 ARG D NH1 1 
ATOM   17436 N  NH2 . ARG D  1  359 ? 5.900   90.184  20.093  1.00 135.24 ?  359 ARG D NH2 1 
ATOM   17437 N  N   . MET D  1  360 ? 2.801   83.266  24.873  1.00 110.22 ?  360 MET D N   1 
ATOM   17438 C  CA  . MET D  1  360 ? 1.929   82.504  25.774  1.00 117.14 ?  360 MET D CA  1 
ATOM   17439 C  C   . MET D  1  360 ? 2.189   82.873  27.256  1.00 110.17 ?  360 MET D C   1 
ATOM   17440 O  O   . MET D  1  360 ? 3.280   83.345  27.568  1.00 110.80 ?  360 MET D O   1 
ATOM   17441 C  CB  . MET D  1  360 ? 2.176   80.991  25.585  1.00 112.81 ?  360 MET D CB  1 
ATOM   17442 C  CG  . MET D  1  360 ? 1.662   80.429  24.268  1.00 133.73 ?  360 MET D CG  1 
ATOM   17443 S  SD  . MET D  1  360 ? -0.132  80.586  24.024  1.00 195.82 ?  360 MET D SD  1 
ATOM   17444 C  CE  . MET D  1  360 ? -0.726  79.335  25.144  1.00 152.86 ?  360 MET D CE  1 
ATOM   17445 N  N   . PRO D  1  361 ? 1.238   82.653  28.198  1.00 111.57 ?  361 PRO D N   1 
ATOM   17446 C  CA  . PRO D  1  361 ? 1.531   82.974  29.610  1.00 104.05 ?  361 PRO D CA  1 
ATOM   17447 C  C   . PRO D  1  361 ? 2.560   82.016  30.212  1.00 110.15 ?  361 PRO D C   1 
ATOM   17448 O  O   . PRO D  1  361 ? 2.806   80.953  29.643  1.00 121.14 ?  361 PRO D O   1 
ATOM   17449 C  CB  . PRO D  1  361 ? 0.171   82.833  30.312  1.00 104.74 ?  361 PRO D CB  1 
ATOM   17450 C  CG  . PRO D  1  361 ? -0.833  82.604  29.241  1.00 120.02 ?  361 PRO D CG  1 
ATOM   17451 C  CD  . PRO D  1  361 ? -0.114  82.084  28.049  1.00 129.64 ?  361 PRO D CD  1 
ATOM   17452 N  N   . LEU D  1  362 ? 3.153   82.372  31.360  1.00 102.70 ?  362 LEU D N   1 
ATOM   17453 C  CA  . LEU D  1  362 ? 4.153   81.508  31.983  1.00 96.56  ?  362 LEU D CA  1 
ATOM   17454 C  C   . LEU D  1  362 ? 4.236   81.698  33.494  1.00 96.36  ?  362 LEU D C   1 
ATOM   17455 O  O   . LEU D  1  362 ? 4.552   82.783  33.965  1.00 92.16  ?  362 LEU D O   1 
ATOM   17456 C  CB  . LEU D  1  362 ? 5.524   81.777  31.346  1.00 85.01  ?  362 LEU D CB  1 
ATOM   17457 C  CG  . LEU D  1  362 ? 6.695   80.940  31.854  1.00 89.84  ?  362 LEU D CG  1 
ATOM   17458 C  CD1 . LEU D  1  362 ? 6.546   79.477  31.463  1.00 91.44  ?  362 LEU D CD1 1 
ATOM   17459 C  CD2 . LEU D  1  362 ? 8.007   81.481  31.322  1.00 84.88  ?  362 LEU D CD2 1 
ATOM   17460 N  N   . GLY D  1  363 ? 3.971   80.631  34.234  1.00 92.93  ?  363 GLY D N   1 
ATOM   17461 C  CA  . GLY D  1  363 ? 4.033   80.635  35.688  1.00 97.75  ?  363 GLY D CA  1 
ATOM   17462 C  C   . GLY D  1  363 ? 5.051   79.618  36.156  1.00 110.40 ?  363 GLY D C   1 
ATOM   17463 O  O   . GLY D  1  363 ? 5.110   78.518  35.607  1.00 116.39 ?  363 GLY D O   1 
ATOM   17464 N  N   . MET D  1  364 ? 5.875   79.972  37.152  1.00 110.22 ?  364 MET D N   1 
ATOM   17465 C  CA  . MET D  1  364 ? 6.903   79.060  37.660  1.00 110.55 ?  364 MET D CA  1 
ATOM   17466 C  C   . MET D  1  364 ? 6.776   78.866  39.167  1.00 104.22 ?  364 MET D C   1 
ATOM   17467 O  O   . MET D  1  364 ? 7.339   79.645  39.932  1.00 97.85  ?  364 MET D O   1 
ATOM   17468 C  CB  . MET D  1  364 ? 8.306   79.588  37.311  1.00 101.32 ?  364 MET D CB  1 
ATOM   17469 C  CG  . MET D  1  364 ? 8.570   79.635  35.821  1.00 94.20  ?  364 MET D CG  1 
ATOM   17470 S  SD  . MET D  1  364 ? 10.311  79.888  35.394  1.00 108.70 ?  364 MET D SD  1 
ATOM   17471 C  CE  . MET D  1  364 ? 10.280  81.611  34.933  1.00 122.51 ?  364 MET D CE  1 
ATOM   17472 N  N   . LEU D  1  365 ? 6.048   77.825  39.593  1.00 105.69 ?  365 LEU D N   1 
ATOM   17473 C  CA  . LEU D  1  365 ? 5.872   77.531  41.014  1.00 114.48 ?  365 LEU D CA  1 
ATOM   17474 C  C   . LEU D  1  365 ? 6.851   76.434  41.421  1.00 116.49 ?  365 LEU D C   1 
ATOM   17475 O  O   . LEU D  1  365 ? 6.891   75.383  40.786  1.00 116.66 ?  365 LEU D O   1 
ATOM   17476 C  CB  . LEU D  1  365 ? 4.426   77.093  41.302  1.00 113.35 ?  365 LEU D CB  1 
ATOM   17477 C  CG  . LEU D  1  365 ? 4.009   77.078  42.788  1.00 103.57 ?  365 LEU D CG  1 
ATOM   17478 C  CD1 . LEU D  1  365 ? 2.537   77.398  42.952  1.00 110.90 ?  365 LEU D CD1 1 
ATOM   17479 C  CD2 . LEU D  1  365 ? 4.308   75.734  43.434  1.00 117.43 ?  365 LEU D CD2 1 
ATOM   17480 N  N   . ILE D  1  366 ? 7.641   76.679  42.476  1.00 124.20 ?  366 ILE D N   1 
ATOM   17481 C  CA  . ILE D  1  366 ? 8.642   75.730  42.963  1.00 129.22 ?  366 ILE D CA  1 
ATOM   17482 C  C   . ILE D  1  366 ? 8.443   75.456  44.452  1.00 128.36 ?  366 ILE D C   1 
ATOM   17483 O  O   . ILE D  1  366 ? 8.417   76.394  45.238  1.00 126.64 ?  366 ILE D O   1 
ATOM   17484 C  CB  . ILE D  1  366 ? 10.057  76.309  42.686  1.00 112.67 ?  366 ILE D CB  1 
ATOM   17485 C  CG1 . ILE D  1  366 ? 10.313  76.445  41.152  1.00 102.72 ?  366 ILE D CG1 1 
ATOM   17486 C  CG2 . ILE D  1  366 ? 11.132  75.453  43.354  1.00 119.88 ?  366 ILE D CG2 1 
ATOM   17487 C  CD1 . ILE D  1  366 ? 10.254  77.859  40.595  1.00 84.23  ?  366 ILE D CD1 1 
ATOM   17488 N  N   . LYS D  1  367 ? 8.315   74.183  44.845  1.00 122.27 ?  367 LYS D N   1 
ATOM   17489 C  CA  . LYS D  1  367 ? 8.134   73.827  46.251  1.00 128.44 ?  367 LYS D CA  1 
ATOM   17490 C  C   . LYS D  1  367 ? 9.445   73.278  46.816  1.00 133.58 ?  367 LYS D C   1 
ATOM   17491 O  O   . LYS D  1  367 ? 10.205  72.637  46.096  1.00 133.23 ?  367 LYS D O   1 
ATOM   17492 C  CB  . LYS D  1  367 ? 7.001   72.806  46.408  1.00 147.26 ?  367 LYS D CB  1 
ATOM   17493 C  CG  . LYS D  1  367 ? 5.667   73.307  45.869  1.00 139.72 ?  367 LYS D CG  1 
ATOM   17494 C  CD  . LYS D  1  367 ? 4.528   72.340  46.152  1.00 148.60 ?  367 LYS D CD  1 
ATOM   17495 C  CE  . LYS D  1  367 ? 3.241   72.788  45.508  1.00 131.23 ?  367 LYS D CE  1 
ATOM   17496 N  NZ  . LYS D  1  367 ? 2.155   71.792  45.690  1.00 154.55 ?  367 LYS D NZ  1 
ATOM   17497 N  N   . VAL D  1  368 ? 9.683   73.533  48.106  1.00 139.96 ?  368 VAL D N   1 
ATOM   17498 C  CA  . VAL D  1  368 ? 10.932  73.051  48.765  1.00 152.95 ?  368 VAL D CA  1 
ATOM   17499 C  C   . VAL D  1  368 ? 10.556  72.258  50.020  1.00 163.12 ?  368 VAL D C   1 
ATOM   17500 O  O   . VAL D  1  368 ? 9.498   72.555  50.607  1.00 166.32 ?  368 VAL D O   1 
ATOM   17501 C  CB  . VAL D  1  368 ? 11.875  74.222  49.103  1.00 151.85 ?  368 VAL D CB  1 
ATOM   17502 C  CG1 . VAL D  1  368 ? 13.244  73.731  49.545  1.00 158.20 ?  368 VAL D CG1 1 
ATOM   17503 C  CG2 . VAL D  1  368 ? 12.003  75.196  47.942  1.00 142.12 ?  368 VAL D CG2 1 
ATOM   17504 N  N   . SER D  1  369 ? 11.392  71.293  50.411  1.00 162.06 ?  369 SER D N   1 
ATOM   17505 C  CA  . SER D  1  369 ? 11.130  70.467  51.599  1.00 159.73 ?  369 SER D CA  1 
ATOM   17506 C  C   . SER D  1  369 ? 11.754  71.038  52.874  1.00 168.81 ?  369 SER D C   1 
ATOM   17507 O  O   . SER D  1  369 ? 12.766  71.736  52.820  1.00 159.96 ?  369 SER D O   1 
ATOM   17508 C  CB  . SER D  1  369 ? 11.634  69.039  51.392  1.00 160.96 ?  369 SER D CB  1 
ATOM   17509 O  OG  . SER D  1  369 ? 10.711  68.214  50.699  1.00 159.19 ?  369 SER D OG  1 
ATOM   17510 N  N   . GLY D  1  370 ? 11.143  70.711  54.010  1.00 187.09 ?  370 GLY D N   1 
ATOM   17511 C  CA  . GLY D  1  370 ? 11.583  71.173  55.319  1.00 197.95 ?  370 GLY D CA  1 
ATOM   17512 C  C   . GLY D  1  370 ? 12.855  70.523  55.827  1.00 211.78 ?  370 GLY D C   1 
ATOM   17513 O  O   . GLY D  1  370 ? 12.861  69.341  56.181  1.00 212.02 ?  370 GLY D O   1 
ATOM   17514 N  N   . THR D  1  371 ? 13.933  71.325  55.840  1.00 219.44 ?  371 THR D N   1 
ATOM   17515 C  CA  . THR D  1  371 ? 15.262  70.869  56.329  1.00 221.80 ?  371 THR D CA  1 
ATOM   17516 C  C   . THR D  1  371 ? 16.031  72.112  56.796  1.00 219.95 ?  371 THR D C   1 
ATOM   17517 O  O   . THR D  1  371 ? 16.776  72.676  55.972  1.00 218.40 ?  371 THR D O   1 
ATOM   17518 C  CB  . THR D  1  371 ? 16.032  70.114  55.239  1.00 219.74 ?  371 THR D CB  1 
ATOM   17519 O  OG1 . THR D  1  371 ? 15.275  68.961  54.870  1.00 220.83 ?  371 THR D OG1 1 
ATOM   17520 C  CG2 . THR D  1  371 ? 17.417  69.695  55.682  1.00 221.31 ?  371 THR D CG2 1 
ATOM   17521 N  N   . ASN D  1  372 ? 15.840  72.539  58.049  1.00 193.47 ?  372 ASN D N   1 
ATOM   17522 C  CA  . ASN D  1  372 ? 16.479  73.744  58.600  1.00 191.12 ?  372 ASN D CA  1 
ATOM   17523 C  C   . ASN D  1  372 ? 16.315  74.945  57.644  1.00 192.10 ?  372 ASN D C   1 
ATOM   17524 O  O   . ASN D  1  372 ? 17.222  75.765  57.499  1.00 182.44 ?  372 ASN D O   1 
ATOM   17525 C  CB  . ASN D  1  372 ? 17.952  73.497  59.006  1.00 177.87 ?  372 ASN D CB  1 
ATOM   17526 C  CG  . ASN D  1  372 ? 18.895  73.074  57.900  1.00 181.23 ?  372 ASN D CG  1 
ATOM   17527 O  OD1 . ASN D  1  372 ? 19.347  73.891  57.093  1.00 180.05 ?  372 ASN D OD1 1 
ATOM   17528 N  ND2 . ASN D  1  372 ? 19.229  71.789  57.842  1.00 180.12 ?  372 ASN D ND2 1 
ATOM   17529 N  N   . MET D  1  373 ? 15.140  74.994  57.005  1.00 189.12 ?  373 MET D N   1 
ATOM   17530 C  CA  . MET D  1  373 ? 14.826  76.101  56.066  1.00 175.03 ?  373 MET D CA  1 
ATOM   17531 C  C   . MET D  1  373 ? 13.538  76.786  56.529  1.00 165.13 ?  373 MET D C   1 
ATOM   17532 O  O   . MET D  1  373 ? 12.601  76.068  56.928  1.00 162.30 ?  373 MET D O   1 
ATOM   17533 C  CB  . MET D  1  373 ? 14.649  75.571  54.640  1.00 173.17 ?  373 MET D CB  1 
ATOM   17534 C  CG  . MET D  1  373 ? 14.326  76.644  53.619  1.00 166.63 ?  373 MET D CG  1 
ATOM   17535 S  SD  . MET D  1  373 ? 14.382  76.022  51.921  1.00 178.87 ?  373 MET D SD  1 
ATOM   17536 C  CE  . MET D  1  373 ? 13.787  77.457  51.027  1.00 160.53 ?  373 MET D CE  1 
ATOM   17537 N  N   . GLN D  1  374 ? 13.500  78.116  56.493  1.00 168.63 ?  374 GLN D N   1 
ATOM   17538 C  CA  . GLN D  1  374 ? 12.346  78.910  56.917  1.00 170.83 ?  374 GLN D CA  1 
ATOM   17539 C  C   . GLN D  1  374 ? 11.748  79.704  55.752  1.00 156.56 ?  374 GLN D C   1 
ATOM   17540 O  O   . GLN D  1  374 ? 12.386  79.849  54.711  1.00 154.67 ?  374 GLN D O   1 
ATOM   17541 C  CB  . GLN D  1  374 ? 12.774  79.890  58.024  1.00 163.31 ?  374 GLN D CB  1 
ATOM   17542 C  CG  . GLN D  1  374 ? 13.354  79.214  59.254  1.00 176.35 ?  374 GLN D CG  1 
ATOM   17543 C  CD  . GLN D  1  374 ? 13.685  80.215  60.331  1.00 181.90 ?  374 GLN D CD  1 
ATOM   17544 O  OE1 . GLN D  1  374 ? 14.196  81.308  60.058  1.00 154.81 ?  374 GLN D OE1 1 
ATOM   17545 N  NE2 . GLN D  1  374 ? 13.406  79.868  61.582  1.00 193.15 ?  374 GLN D NE2 1 
ATOM   17546 N  N   . LYS D  1  375 ? 10.527  80.237  55.934  1.00 143.54 ?  375 LYS D N   1 
ATOM   17547 C  CA  . LYS D  1  375 ? 9.880   81.050  54.902  1.00 136.28 ?  375 LYS D CA  1 
ATOM   17548 C  C   . LYS D  1  375 ? 10.724  82.297  54.585  1.00 134.59 ?  375 LYS D C   1 
ATOM   17549 O  O   . LYS D  1  375 ? 10.632  82.826  53.480  1.00 140.71 ?  375 LYS D O   1 
ATOM   17550 C  CB  . LYS D  1  375 ? 8.472   81.485  55.346  1.00 133.92 ?  375 LYS D CB  1 
ATOM   17551 C  CG  . LYS D  1  375 ? 7.405   80.412  55.192  1.00 130.40 ?  375 LYS D CG  1 
ATOM   17552 C  CD  . LYS D  1  375 ? 6.022   80.976  55.470  1.00 136.91 ?  375 LYS D CD  1 
ATOM   17553 C  CE  . LYS D  1  375 ? 4.956   79.913  55.458  1.00 138.56 ?  375 LYS D CE  1 
ATOM   17554 N  NZ  . LYS D  1  375 ? 3.621   80.475  55.787  1.00 141.54 ?  375 LYS D NZ  1 
ATOM   17555 N  N   . ASP D  1  376 ? 11.540  82.763  55.545  1.00 134.15 ?  376 ASP D N   1 
ATOM   17556 C  CA  . ASP D  1  376 ? 12.398  83.925  55.340  1.00 129.70 ?  376 ASP D CA  1 
ATOM   17557 C  C   . ASP D  1  376 ? 13.513  83.651  54.313  1.00 127.16 ?  376 ASP D C   1 
ATOM   17558 O  O   . ASP D  1  376 ? 14.151  84.599  53.859  1.00 130.72 ?  376 ASP D O   1 
ATOM   17559 C  CB  . ASP D  1  376 ? 13.010  84.379  56.675  1.00 137.90 ?  376 ASP D CB  1 
ATOM   17560 C  CG  . ASP D  1  376 ? 11.989  84.825  57.705  1.00 147.99 ?  376 ASP D CG  1 
ATOM   17561 O  OD1 . ASP D  1  376 ? 10.832  85.104  57.315  1.00 146.75 ?  376 ASP D OD1 1 
ATOM   17562 O  OD2 . ASP D  1  376 ? 12.344  84.894  58.900  1.00 149.56 ?  376 ASP D OD2 1 
ATOM   17563 N  N   . PHE D  1  377 ? 13.750  82.374  53.944  1.00 128.88 ?  377 PHE D N   1 
ATOM   17564 C  CA  . PHE D  1  377 ? 14.769  82.016  52.956  1.00 124.73 ?  377 PHE D CA  1 
ATOM   17565 C  C   . PHE D  1  377 ? 14.190  81.967  51.533  1.00 127.20 ?  377 PHE D C   1 
ATOM   17566 O  O   . PHE D  1  377 ? 14.955  82.054  50.580  1.00 122.26 ?  377 PHE D O   1 
ATOM   17567 C  CB  . PHE D  1  377 ? 15.398  80.648  53.280  1.00 127.15 ?  377 PHE D CB  1 
ATOM   17568 C  CG  . PHE D  1  377 ? 16.115  80.503  54.604  1.00 140.50 ?  377 PHE D CG  1 
ATOM   17569 C  CD1 . PHE D  1  377 ? 16.472  81.615  55.349  1.00 143.40 ?  377 PHE D CD1 1 
ATOM   17570 C  CD2 . PHE D  1  377 ? 16.468  79.255  55.083  1.00 158.40 ?  377 PHE D CD2 1 
ATOM   17571 C  CE1 . PHE D  1  377 ? 17.138  81.473  56.559  1.00 151.75 ?  377 PHE D CE1 1 
ATOM   17572 C  CE2 . PHE D  1  377 ? 17.133  79.118  56.292  1.00 162.65 ?  377 PHE D CE2 1 
ATOM   17573 C  CZ  . PHE D  1  377 ? 17.466  80.227  57.022  1.00 155.28 ?  377 PHE D CZ  1 
ATOM   17574 N  N   . GLU D  1  378 ? 12.858  81.840  51.378  1.00 120.25 ?  378 GLU D N   1 
ATOM   17575 C  CA  . GLU D  1  378 ? 12.235  81.772  50.049  1.00 116.85 ?  378 GLU D CA  1 
ATOM   17576 C  C   . GLU D  1  378 ? 12.641  82.946  49.134  1.00 117.40 ?  378 GLU D C   1 
ATOM   17577 O  O   . GLU D  1  378 ? 12.897  82.708  47.955  1.00 114.86 ?  378 GLU D O   1 
ATOM   17578 C  CB  . GLU D  1  378 ? 10.694  81.708  50.128  1.00 132.36 ?  378 GLU D CB  1 
ATOM   17579 C  CG  . GLU D  1  378 ? 10.090  80.568  50.932  1.00 142.81 ?  378 GLU D CG  1 
ATOM   17580 C  CD  . GLU D  1  378 ? 8.657   80.839  51.351  1.00 146.80 ?  378 GLU D CD  1 
ATOM   17581 O  OE1 . GLU D  1  378 ? 8.364   81.982  51.772  1.00 146.32 ?  378 GLU D OE1 1 
ATOM   17582 O  OE2 . GLU D  1  378 ? 7.825   79.910  51.257  1.00 140.55 ?  378 GLU D OE2 1 
ATOM   17583 N  N   . PRO D  1  379 ? 12.701  84.212  49.614  1.00 121.54 ?  379 PRO D N   1 
ATOM   17584 C  CA  . PRO D  1  379 ? 13.081  85.309  48.707  1.00 114.34 ?  379 PRO D CA  1 
ATOM   17585 C  C   . PRO D  1  379 ? 14.453  85.164  48.061  1.00 107.17 ?  379 PRO D C   1 
ATOM   17586 O  O   . PRO D  1  379 ? 14.620  85.612  46.931  1.00 119.14 ?  379 PRO D O   1 
ATOM   17587 C  CB  . PRO D  1  379 ? 13.028  86.555  49.599  1.00 117.92 ?  379 PRO D CB  1 
ATOM   17588 C  CG  . PRO D  1  379 ? 12.189  86.179  50.747  1.00 115.61 ?  379 PRO D CG  1 
ATOM   17589 C  CD  . PRO D  1  379 ? 12.428  84.724  50.971  1.00 128.75 ?  379 PRO D CD  1 
ATOM   17590 N  N   . VAL D  1  380 ? 15.402  84.550  48.769  1.00 92.87  ?  380 VAL D N   1 
ATOM   17591 C  CA  . VAL D  1  380 ? 16.780  84.362  48.226  1.00 113.81 ?  380 VAL D CA  1 
ATOM   17592 C  C   . VAL D  1  380 ? 16.719  83.337  47.094  1.00 110.89 ?  380 VAL D C   1 
ATOM   17593 O  O   . VAL D  1  380 ? 17.361  83.569  46.052  1.00 102.71 ?  380 VAL D O   1 
ATOM   17594 C  CB  . VAL D  1  380 ? 17.740  83.901  49.338  1.00 100.37 ?  380 VAL D CB  1 
ATOM   17595 C  CG1 . VAL D  1  380 ? 19.147  83.667  48.812  1.00 114.12 ?  380 VAL D CG1 1 
ATOM   17596 C  CG2 . VAL D  1  380 ? 17.755  84.869  50.511  1.00 96.47  ?  380 VAL D CG2 1 
ATOM   17597 N  N   . LEU D  1  381 ? 15.966  82.257  47.291  1.00 108.28 ?  381 LEU D N   1 
ATOM   17598 C  CA  . LEU D  1  381 ? 15.853  81.182  46.309  1.00 110.59 ?  381 LEU D CA  1 
ATOM   17599 C  C   . LEU D  1  381 ? 15.133  81.702  45.066  1.00 106.62 ?  381 LEU D C   1 
ATOM   17600 O  O   . LEU D  1  381 ? 15.560  81.429  43.946  1.00 110.96 ?  381 LEU D O   1 
ATOM   17601 C  CB  . LEU D  1  381 ? 15.052  79.990  46.881  1.00 119.22 ?  381 LEU D CB  1 
ATOM   17602 C  CG  . LEU D  1  381 ? 15.748  79.000  47.834  1.00 127.88 ?  381 LEU D CG  1 
ATOM   17603 C  CD1 . LEU D  1  381 ? 17.044  78.486  47.268  1.00 134.26 ?  381 LEU D CD1 1 
ATOM   17604 C  CD2 . LEU D  1  381 ? 15.961  79.588  49.204  1.00 130.94 ?  381 LEU D CD2 1 
ATOM   17605 N  N   . GLU D  1  382 ? 14.040  82.450  45.265  1.00 102.57 ?  382 GLU D N   1 
ATOM   17606 C  CA  . GLU D  1  382 ? 13.249  82.994  44.168  1.00 97.93  ?  382 GLU D CA  1 
ATOM   17607 C  C   . GLU D  1  382 ? 14.039  84.014  43.349  1.00 102.64 ?  382 GLU D C   1 
ATOM   17608 O  O   . GLU D  1  382 ? 13.917  84.042  42.124  1.00 102.23 ?  382 GLU D O   1 
ATOM   17609 C  CB  . GLU D  1  382 ? 11.953  83.629  44.712  1.00 107.34 ?  382 GLU D CB  1 
ATOM   17610 C  CG  . GLU D  1  382 ? 10.833  83.725  43.691  1.00 105.74 ?  382 GLU D CG  1 
ATOM   17611 C  CD  . GLU D  1  382 ? 9.748   84.722  44.043  1.00 111.97 ?  382 GLU D CD  1 
ATOM   17612 O  OE1 . GLU D  1  382 ? 9.337   84.761  45.225  1.00 109.42 ?  382 GLU D OE1 1 
ATOM   17613 O  OE2 . GLU D  1  382 ? 9.305   85.463  43.137  1.00 114.90 ?  382 GLU D OE2 1 
ATOM   17614 N  N   . ARG D  1  383 ? 14.847  84.850  44.013  1.00 97.01  ?  383 ARG D N   1 
ATOM   17615 C  CA  . ARG D  1  383 ? 15.634  85.865  43.319  1.00 89.40  ?  383 ARG D CA  1 
ATOM   17616 C  C   . ARG D  1  383 ? 16.678  85.233  42.397  1.00 90.50  ?  383 ARG D C   1 
ATOM   17617 O  O   . ARG D  1  383 ? 16.899  85.734  41.297  1.00 97.38  ?  383 ARG D O   1 
ATOM   17618 C  CB  . ARG D  1  383 ? 16.307  86.817  44.332  1.00 87.17  ?  383 ARG D CB  1 
ATOM   17619 C  CG  . ARG D  1  383 ? 17.271  87.850  43.729  1.00 86.55  ?  383 ARG D CG  1 
ATOM   17620 C  CD  . ARG D  1  383 ? 16.581  88.944  42.930  1.00 81.10  ?  383 ARG D CD  1 
ATOM   17621 N  NE  . ARG D  1  383 ? 16.129  88.475  41.619  1.00 78.01  ?  383 ARG D NE  1 
ATOM   17622 C  CZ  . ARG D  1  383 ? 15.597  89.253  40.682  1.00 85.18  ?  383 ARG D CZ  1 
ATOM   17623 N  NH1 . ARG D  1  383 ? 15.447  90.554  40.893  1.00 91.78  ?  383 ARG D NH1 1 
ATOM   17624 N  NH2 . ARG D  1  383 ? 15.212  88.734  39.524  1.00 83.28  ?  383 ARG D NH2 1 
ATOM   17625 N  N   . ARG D  1  384 ? 17.314  84.139  42.834  1.00 91.74  ?  384 ARG D N   1 
ATOM   17626 C  CA  . ARG D  1  384 ? 18.344  83.479  42.032  1.00 96.49  ?  384 ARG D CA  1 
ATOM   17627 C  C   . ARG D  1  384 ? 17.828  82.822  40.749  1.00 92.99  ?  384 ARG D C   1 
ATOM   17628 O  O   . ARG D  1  384 ? 18.648  82.464  39.905  1.00 89.85  ?  384 ARG D O   1 
ATOM   17629 C  CB  . ARG D  1  384 ? 19.119  82.441  42.870  1.00 103.72 ?  384 ARG D CB  1 
ATOM   17630 C  CG  . ARG D  1  384 ? 20.391  82.961  43.548  1.00 98.20  ?  384 ARG D CG  1 
ATOM   17631 C  CD  . ARG D  1  384 ? 21.432  83.454  42.559  1.00 88.16  ?  384 ARG D CD  1 
ATOM   17632 N  NE  . ARG D  1  384 ? 22.799  83.291  43.054  1.00 121.20 ?  384 ARG D NE  1 
ATOM   17633 C  CZ  . ARG D  1  384 ? 23.875  83.835  42.488  1.00 129.60 ?  384 ARG D CZ  1 
ATOM   17634 N  NH1 . ARG D  1  384 ? 23.756  84.591  41.402  1.00 118.70 ?  384 ARG D NH1 1 
ATOM   17635 N  NH2 . ARG D  1  384 ? 25.079  83.627  43.006  1.00 134.71 ?  384 ARG D NH2 1 
ATOM   17636 N  N   . LEU D  1  385 ? 16.512  82.676  40.591  1.00 93.49  ?  385 LEU D N   1 
ATOM   17637 C  CA  . LEU D  1  385 ? 15.949  82.062  39.356  1.00 86.81  ?  385 LEU D CA  1 
ATOM   17638 C  C   . LEU D  1  385 ? 16.478  82.804  38.122  1.00 89.59  ?  385 LEU D C   1 
ATOM   17639 O  O   . LEU D  1  385 ? 16.784  82.127  37.123  1.00 91.81  ?  385 LEU D O   1 
ATOM   17640 C  CB  . LEU D  1  385 ? 14.421  82.123  39.423  1.00 91.69  ?  385 LEU D CB  1 
ATOM   17641 C  CG  . LEU D  1  385 ? 13.784  81.320  40.557  1.00 98.46  ?  385 LEU D CG  1 
ATOM   17642 C  CD1 . LEU D  1  385 ? 12.275  81.509  40.574  1.00 90.77  ?  385 LEU D CD1 1 
ATOM   17643 C  CD2 . LEU D  1  385 ? 14.137  79.846  40.441  1.00 86.70  ?  385 LEU D CD2 1 
ATOM   17644 N  N   . HIS D  1  386 ? 16.589  84.132  38.190  1.00 83.77  ?  386 HIS D N   1 
ATOM   17645 C  CA  . HIS D  1  386 ? 17.046  84.960  37.075  1.00 76.32  ?  386 HIS D CA  1 
ATOM   17646 C  C   . HIS D  1  386 ? 18.463  84.551  36.674  1.00 93.03  ?  386 HIS D C   1 
ATOM   17647 O  O   . HIS D  1  386 ? 18.738  84.320  35.497  1.00 97.99  ?  386 HIS D O   1 
ATOM   17648 C  CB  . HIS D  1  386 ? 17.030  86.452  37.452  1.00 65.91  ?  386 HIS D CB  1 
ATOM   17649 C  CG  . HIS D  1  386 ? 17.656  87.355  36.441  1.00 77.02  ?  386 HIS D CG  1 
ATOM   17650 N  ND1 . HIS D  1  386 ? 16.914  88.291  35.746  1.00 89.70  ?  386 HIS D ND1 1 
ATOM   17651 C  CD2 . HIS D  1  386 ? 18.944  87.434  36.039  1.00 95.98  ?  386 HIS D CD2 1 
ATOM   17652 C  CE1 . HIS D  1  386 ? 17.773  88.926  34.966  1.00 98.58  ?  386 HIS D CE1 1 
ATOM   17653 N  NE2 . HIS D  1  386 ? 19.007  88.440  35.106  1.00 103.25 ?  386 HIS D NE2 1 
ATOM   17654 N  N   . TYR D  1  387 ? 19.355  84.457  37.663  1.00 91.37  ?  387 TYR D N   1 
ATOM   17655 C  CA  . TYR D  1  387 ? 20.752  84.075  37.456  1.00 84.47  ?  387 TYR D CA  1 
ATOM   17656 C  C   . TYR D  1  387 ? 20.845  82.680  36.838  1.00 90.58  ?  387 TYR D C   1 
ATOM   17657 O  O   . TYR D  1  387 ? 21.598  82.493  35.889  1.00 98.43  ?  387 TYR D O   1 
ATOM   17658 C  CB  . TYR D  1  387 ? 21.498  84.143  38.801  1.00 79.14  ?  387 TYR D CB  1 
ATOM   17659 C  CG  . TYR D  1  387 ? 22.896  83.566  38.815  1.00 107.00 ?  387 TYR D CG  1 
ATOM   17660 C  CD1 . TYR D  1  387 ? 23.983  84.319  38.397  1.00 114.13 ?  387 TYR D CD1 1 
ATOM   17661 C  CD2 . TYR D  1  387 ? 23.146  82.313  39.359  1.00 125.55 ?  387 TYR D CD2 1 
ATOM   17662 C  CE1 . TYR D  1  387 ? 25.277  83.812  38.452  1.00 120.22 ?  387 TYR D CE1 1 
ATOM   17663 C  CE2 . TYR D  1  387 ? 24.434  81.792  39.413  1.00 118.44 ?  387 TYR D CE2 1 
ATOM   17664 C  CZ  . TYR D  1  387 ? 25.500  82.547  38.961  1.00 115.60 ?  387 TYR D CZ  1 
ATOM   17665 O  OH  . TYR D  1  387 ? 26.781  82.048  39.005  1.00 121.27 ?  387 TYR D OH  1 
ATOM   17666 N  N   . PHE D  1  388 ? 20.068  81.710  37.354  1.00 92.42  ?  388 PHE D N   1 
ATOM   17667 C  CA  . PHE D  1  388 ? 20.094  80.336  36.845  1.00 91.72  ?  388 PHE D CA  1 
ATOM   17668 C  C   . PHE D  1  388 ? 19.520  80.212  35.433  1.00 93.80  ?  388 PHE D C   1 
ATOM   17669 O  O   . PHE D  1  388 ? 20.123  79.553  34.589  1.00 99.69  ?  388 PHE D O   1 
ATOM   17670 C  CB  . PHE D  1  388 ? 19.321  79.375  37.778  1.00 93.08  ?  388 PHE D CB  1 
ATOM   17671 C  CG  . PHE D  1  388 ? 19.776  79.306  39.219  1.00 102.02 ?  388 PHE D CG  1 
ATOM   17672 C  CD1 . PHE D  1  388 ? 21.118  79.397  39.547  1.00 111.67 ?  388 PHE D CD1 1 
ATOM   17673 C  CD2 . PHE D  1  388 ? 18.864  79.110  40.240  1.00 94.91  ?  388 PHE D CD2 1 
ATOM   17674 C  CE1 . PHE D  1  388 ? 21.533  79.328  40.870  1.00 114.06 ?  388 PHE D CE1 1 
ATOM   17675 C  CE2 . PHE D  1  388 ? 19.282  79.036  41.562  1.00 107.99 ?  388 PHE D CE2 1 
ATOM   17676 C  CZ  . PHE D  1  388 ? 20.613  79.146  41.868  1.00 110.50 ?  388 PHE D CZ  1 
ATOM   17677 N  N   . LEU D  1  389 ? 18.386  80.863  35.175  1.00 86.65  ?  389 LEU D N   1 
ATOM   17678 C  CA  . LEU D  1  389 ? 17.723  80.707  33.852  1.00 86.94  ?  389 LEU D CA  1 
ATOM   17679 C  C   . LEU D  1  389 ? 18.517  81.438  32.764  1.00 82.53  ?  389 LEU D C   1 
ATOM   17680 O  O   . LEU D  1  389 ? 18.552  80.931  31.630  1.00 87.83  ?  389 LEU D O   1 
ATOM   17681 C  CB  . LEU D  1  389 ? 16.296  81.252  33.953  1.00 94.67  ?  389 LEU D CB  1 
ATOM   17682 C  CG  . LEU D  1  389 ? 15.340  80.424  34.810  1.00 93.25  ?  389 LEU D CG  1 
ATOM   17683 C  CD1 . LEU D  1  389 ? 13.915  80.939  34.680  1.00 92.97  ?  389 LEU D CD1 1 
ATOM   17684 C  CD2 . LEU D  1  389 ? 15.412  78.954  34.431  1.00 92.09  ?  389 LEU D CD2 1 
ATOM   17685 N  N   . ASN D  1  390 ? 19.129  82.579  33.089  1.00 81.33  ?  390 ASN D N   1 
ATOM   17686 C  CA  . ASN D  1  390 ? 19.827  83.380  32.047  1.00 93.41  ?  390 ASN D CA  1 
ATOM   17687 C  C   . ASN D  1  390 ? 21.077  82.628  31.569  1.00 94.96  ?  390 ASN D C   1 
ATOM   17688 O  O   . ASN D  1  390 ? 21.526  82.902  30.440  1.00 95.43  ?  390 ASN D O   1 
ATOM   17689 C  CB  . ASN D  1  390 ? 20.142  84.792  32.543  1.00 82.09  ?  390 ASN D CB  1 
ATOM   17690 C  CG  . ASN D  1  390 ? 19.284  85.847  31.877  1.00 81.86  ?  390 ASN D CG  1 
ATOM   17691 O  OD1 . ASN D  1  390 ? 18.939  85.724  30.705  1.00 95.68  ?  390 ASN D OD1 1 
ATOM   17692 N  ND2 . ASN D  1  390 ? 18.934  86.885  32.617  1.00 92.77  ?  390 ASN D ND2 1 
ATOM   17693 N  N   . TYR D  1  391 ? 21.614  81.720  32.388  1.00 82.36  ?  391 TYR D N   1 
ATOM   17694 C  CA  . TYR D  1  391 ? 22.802  80.935  32.032  1.00 89.04  ?  391 TYR D CA  1 
ATOM   17695 C  C   . TYR D  1  391 ? 22.520  80.006  30.833  1.00 92.25  ?  391 TYR D C   1 
ATOM   17696 O  O   . TYR D  1  391 ? 23.457  79.600  30.149  1.00 91.60  ?  391 TYR D O   1 
ATOM   17697 C  CB  . TYR D  1  391 ? 23.267  80.081  33.234  1.00 93.09  ?  391 TYR D CB  1 
ATOM   17698 C  CG  . TYR D  1  391 ? 24.421  80.649  34.038  1.00 94.47  ?  391 TYR D CG  1 
ATOM   17699 C  CD1 . TYR D  1  391 ? 24.443  81.984  34.414  1.00 104.92 ?  391 TYR D CD1 1 
ATOM   17700 C  CD2 . TYR D  1  391 ? 25.464  79.838  34.461  1.00 87.44  ?  391 TYR D CD2 1 
ATOM   17701 C  CE1 . TYR D  1  391 ? 25.490  82.505  35.164  1.00 100.85 ?  391 TYR D CE1 1 
ATOM   17702 C  CE2 . TYR D  1  391 ? 26.516  80.348  35.212  1.00 88.56  ?  391 TYR D CE2 1 
ATOM   17703 C  CZ  . TYR D  1  391 ? 26.523  81.683  35.566  1.00 97.34  ?  391 TYR D CZ  1 
ATOM   17704 O  OH  . TYR D  1  391 ? 27.561  82.200  36.306  1.00 105.43 ?  391 TYR D OH  1 
ATOM   17705 N  N   . ILE D  1  392 ? 21.244  79.660  30.584  1.00 92.67  ?  392 ILE D N   1 
ATOM   17706 C  CA  . ILE D  1  392 ? 20.871  78.797  29.468  1.00 86.58  ?  392 ILE D CA  1 
ATOM   17707 C  C   . ILE D  1  392 ? 21.087  79.570  28.172  1.00 94.32  ?  392 ILE D C   1 
ATOM   17708 O  O   . ILE D  1  392 ? 20.647  80.715  28.065  1.00 105.59 ?  392 ILE D O   1 
ATOM   17709 C  CB  . ILE D  1  392 ? 19.381  78.363  29.554  1.00 87.10  ?  392 ILE D CB  1 
ATOM   17710 C  CG1 . ILE D  1  392 ? 19.052  77.591  30.847  1.00 90.95  ?  392 ILE D CG1 1 
ATOM   17711 C  CG2 . ILE D  1  392 ? 18.987  77.544  28.322  1.00 93.54  ?  392 ILE D CG2 1 
ATOM   17712 C  CD1 . ILE D  1  392 ? 17.532  77.674  31.253  1.00 87.47  ?  392 ILE D CD1 1 
ATOM   17713 N  N   . GLU D  1  393 ? 21.737  78.948  27.181  1.00 94.61  ?  393 GLU D N   1 
ATOM   17714 C  CA  . GLU D  1  393 ? 21.951  79.593  25.887  1.00 108.89 ?  393 GLU D CA  1 
ATOM   17715 C  C   . GLU D  1  393 ? 20.628  79.559  25.117  1.00 124.76 ?  393 GLU D C   1 
ATOM   17716 O  O   . GLU D  1  393 ? 19.943  78.537  25.114  1.00 133.62 ?  393 GLU D O   1 
ATOM   17717 C  CB  . GLU D  1  393 ? 23.065  78.877  25.095  1.00 122.18 ?  393 GLU D CB  1 
ATOM   17718 C  CG  . GLU D  1  393 ? 23.115  79.234  23.616  1.00 118.66 ?  393 GLU D CG  1 
ATOM   17719 C  CD  . GLU D  1  393 ? 24.301  78.662  22.867  1.00 120.34 ?  393 GLU D CD  1 
ATOM   17720 O  OE1 . GLU D  1  393 ? 24.755  77.551  23.227  1.00 116.31 ?  393 GLU D OE1 1 
ATOM   17721 O  OE2 . GLU D  1  393 ? 24.775  79.326  21.915  1.00 120.67 ?  393 GLU D OE2 1 
ATOM   17722 N  N   . GLY D  1  394 ? 20.280  80.669  24.480  1.00 134.08 ?  394 GLY D N   1 
ATOM   17723 C  CA  . GLY D  1  394 ? 19.050  80.778  23.712  1.00 130.70 ?  394 GLY D CA  1 
ATOM   17724 C  C   . GLY D  1  394 ? 17.923  81.458  24.463  1.00 121.65 ?  394 GLY D C   1 
ATOM   17725 O  O   . GLY D  1  394 ? 17.094  82.123  23.842  1.00 123.43 ?  394 GLY D O   1 
ATOM   17726 N  N   . VAL D  1  395 ? 17.867  81.309  25.799  1.00 100.69 ?  395 VAL D N   1 
ATOM   17727 C  CA  . VAL D  1  395 ? 16.799  81.942  26.582  1.00 104.64 ?  395 VAL D CA  1 
ATOM   17728 C  C   . VAL D  1  395 ? 17.334  83.168  27.332  1.00 107.90 ?  395 VAL D C   1 
ATOM   17729 O  O   . VAL D  1  395 ? 18.536  83.275  27.588  1.00 112.88 ?  395 VAL D O   1 
ATOM   17730 C  CB  . VAL D  1  395 ? 16.056  80.950  27.533  1.00 112.33 ?  395 VAL D CB  1 
ATOM   17731 C  CG1 . VAL D  1  395 ? 15.889  79.572  26.891  1.00 105.70 ?  395 VAL D CG1 1 
ATOM   17732 C  CG2 . VAL D  1  395 ? 16.743  80.849  28.892  1.00 98.78  ?  395 VAL D CG2 1 
ATOM   17733 N  N   . MET D  1  396 ? 16.408  84.078  27.656  1.00 97.65  ?  396 MET D N   1 
ATOM   17734 C  CA  . MET D  1  396 ? 16.772  85.317  28.388  1.00 90.56  ?  396 MET D CA  1 
ATOM   17735 C  C   . MET D  1  396 ? 15.664  85.639  29.395  1.00 85.43  ?  396 MET D C   1 
ATOM   17736 O  O   . MET D  1  396 ? 14.531  85.899  28.953  1.00 90.74  ?  396 MET D O   1 
ATOM   17737 C  CB  . MET D  1  396 ? 16.938  86.486  27.417  1.00 92.83  ?  396 MET D CB  1 
ATOM   17738 C  CG  . MET D  1  396 ? 17.087  87.821  28.108  1.00 113.89 ?  396 MET D CG  1 
ATOM   17739 S  SD  . MET D  1  396 ? 16.192  89.105  27.212  1.00 91.74  ?  396 MET D SD  1 
ATOM   17740 C  CE  . MET D  1  396 ? 14.539  88.874  27.864  1.00 86.95  ?  396 MET D CE  1 
ATOM   17741 N  N   . HIS D  1  397 ? 15.978  85.603  30.689  1.00 73.95  ?  397 HIS D N   1 
ATOM   17742 C  CA  . HIS D  1  397 ? 15.026  85.891  31.759  1.00 74.86  ?  397 HIS D CA  1 
ATOM   17743 C  C   . HIS D  1  397 ? 15.322  87.272  32.335  1.00 83.03  ?  397 HIS D C   1 
ATOM   17744 O  O   . HIS D  1  397 ? 16.464  87.551  32.699  1.00 80.58  ?  397 HIS D O   1 
ATOM   17745 C  CB  . HIS D  1  397 ? 15.121  84.827  32.866  1.00 77.63  ?  397 HIS D CB  1 
ATOM   17746 C  CG  . HIS D  1  397 ? 14.253  85.112  34.054  1.00 79.49  ?  397 HIS D CG  1 
ATOM   17747 N  ND1 . HIS D  1  397 ? 14.573  86.109  34.960  1.00 69.86  ?  397 HIS D ND1 1 
ATOM   17748 C  CD2 . HIS D  1  397 ? 13.106  84.513  34.451  1.00 88.54  ?  397 HIS D CD2 1 
ATOM   17749 C  CE1 . HIS D  1  397 ? 13.614  86.091  35.872  1.00 77.68  ?  397 HIS D CE1 1 
ATOM   17750 N  NE2 . HIS D  1  397 ? 12.710  85.144  35.608  1.00 91.74  ?  397 HIS D NE2 1 
ATOM   17751 N  N   . VAL D  1  398 ? 14.298  88.134  32.420  1.00 86.22  ?  398 VAL D N   1 
ATOM   17752 C  CA  . VAL D  1  398 ? 14.440  89.489  32.950  1.00 75.04  ?  398 VAL D CA  1 
ATOM   17753 C  C   . VAL D  1  398 ? 13.236  89.803  33.827  1.00 71.80  ?  398 VAL D C   1 
ATOM   17754 O  O   . VAL D  1  398 ? 12.113  89.588  33.401  1.00 79.60  ?  398 VAL D O   1 
ATOM   17755 C  CB  . VAL D  1  398 ? 14.537  90.521  31.801  1.00 60.02  ?  398 VAL D CB  1 
ATOM   17756 C  CG1 . VAL D  1  398 ? 14.631  91.939  32.353  1.00 69.08  ?  398 VAL D CG1 1 
ATOM   17757 C  CG2 . VAL D  1  398 ? 15.715  90.217  30.885  1.00 93.02  ?  398 VAL D CG2 1 
ATOM   17758 N  N   . GLY D  1  399 ? 13.471  90.305  35.029  1.00 65.14  ?  399 GLY D N   1 
ATOM   17759 C  CA  . GLY D  1  399 ? 12.402  90.675  35.946  1.00 70.76  ?  399 GLY D CA  1 
ATOM   17760 C  C   . GLY D  1  399 ? 12.337  89.828  37.198  1.00 76.43  ?  399 GLY D C   1 
ATOM   17761 O  O   . GLY D  1  399 ? 13.245  89.044  37.469  1.00 81.27  ?  399 GLY D O   1 
ATOM   17762 N  N   . GLN D  1  400 ? 11.256  89.989  37.975  1.00 77.69  ?  400 GLN D N   1 
ATOM   17763 C  CA  . GLN D  1  400 ? 11.062  89.258  39.228  1.00 75.85  ?  400 GLN D CA  1 
ATOM   17764 C  C   . GLN D  1  400 ? 9.577   89.195  39.621  1.00 79.30  ?  400 GLN D C   1 
ATOM   17765 O  O   . GLN D  1  400 ? 8.773   89.975  39.115  1.00 82.04  ?  400 GLN D O   1 
ATOM   17766 C  CB  . GLN D  1  400 ? 11.864  89.939  40.352  1.00 66.50  ?  400 GLN D CB  1 
ATOM   17767 C  CG  . GLN D  1  400 ? 11.550  91.429  40.531  1.00 75.72  ?  400 GLN D CG  1 
ATOM   17768 C  CD  . GLN D  1  400 ? 12.286  92.317  39.552  1.00 76.57  ?  400 GLN D CD  1 
ATOM   17769 O  OE1 . GLN D  1  400 ? 13.429  92.048  39.168  1.00 76.14  ?  400 GLN D OE1 1 
ATOM   17770 N  NE2 . GLN D  1  400 ? 11.651  93.405  39.128  1.00 78.57  ?  400 GLN D NE2 1 
ATOM   17771 N  N   . ARG D  1  401 ? 9.224   88.276  40.536  1.00 69.08  ?  401 ARG D N   1 
ATOM   17772 C  CA  . ARG D  1  401 ? 7.856   88.105  41.036  1.00 81.71  ?  401 ARG D CA  1 
ATOM   17773 C  C   . ARG D  1  401 ? 6.802   88.023  39.899  1.00 84.03  ?  401 ARG D C   1 
ATOM   17774 O  O   . ARG D  1  401 ? 6.935   87.144  39.054  1.00 85.74  ?  401 ARG D O   1 
ATOM   17775 C  CB  . ARG D  1  401 ? 7.521   89.191  42.082  1.00 85.81  ?  401 ARG D CB  1 
ATOM   17776 C  CG  . ARG D  1  401 ? 8.341   89.099  43.359  1.00 92.12  ?  401 ARG D CG  1 
ATOM   17777 C  CD  . ARG D  1  401 ? 7.871   90.120  44.370  1.00 78.94  ?  401 ARG D CD  1 
ATOM   17778 N  NE  . ARG D  1  401 ? 8.506   89.943  45.675  1.00 81.76  ?  401 ARG D NE  1 
ATOM   17779 C  CZ  . ARG D  1  401 ? 8.263   90.711  46.733  1.00 89.43  ?  401 ARG D CZ  1 
ATOM   17780 N  NH1 . ARG D  1  401 ? 7.396   91.716  46.651  1.00 74.09  ?  401 ARG D NH1 1 
ATOM   17781 N  NH2 . ARG D  1  401 ? 8.888   90.483  47.882  1.00 99.90  ?  401 ARG D NH2 1 
ATOM   17782 N  N   . ASN D  1  402 ? 5.771   88.899  39.865  1.00 84.20  ?  402 ASN D N   1 
ATOM   17783 C  CA  . ASN D  1  402 ? 4.751   88.834  38.820  1.00 80.62  ?  402 ASN D CA  1 
ATOM   17784 C  C   . ASN D  1  402 ? 5.016   89.805  37.666  1.00 75.74  ?  402 ASN D C   1 
ATOM   17785 O  O   . ASN D  1  402 ? 4.090   90.144  36.931  1.00 85.94  ?  402 ASN D O   1 
ATOM   17786 C  CB  . ASN D  1  402 ? 3.351   89.039  39.412  1.00 82.27  ?  402 ASN D CB  1 
ATOM   17787 C  CG  . ASN D  1  402 ? 3.038   90.463  39.788  1.00 93.90  ?  402 ASN D CG  1 
ATOM   17788 O  OD1 . ASN D  1  402 ? 2.384   91.195  39.038  1.00 117.28 ?  402 ASN D OD1 1 
ATOM   17789 N  ND2 . ASN D  1  402 ? 3.499   90.890  40.954  1.00 108.37 ?  402 ASN D ND2 1 
ATOM   17790 N  N   . LEU D  1  403 ? 6.274   90.232  37.490  1.00 76.04  ?  403 LEU D N   1 
ATOM   17791 C  CA  . LEU D  1  403 ? 6.651   91.135  36.405  1.00 84.85  ?  403 LEU D CA  1 
ATOM   17792 C  C   . LEU D  1  403 ? 7.897   90.582  35.710  1.00 81.43  ?  403 LEU D C   1 
ATOM   17793 O  O   . LEU D  1  403 ? 8.861   91.311  35.469  1.00 67.70  ?  403 LEU D O   1 
ATOM   17794 C  CB  . LEU D  1  403 ? 6.899   92.556  36.935  1.00 72.51  ?  403 LEU D CB  1 
ATOM   17795 C  CG  . LEU D  1  403 ? 5.666   93.301  37.449  1.00 65.22  ?  403 LEU D CG  1 
ATOM   17796 C  CD1 . LEU D  1  403 ? 6.070   94.471  38.285  1.00 77.93  ?  403 LEU D CD1 1 
ATOM   17797 C  CD2 . LEU D  1  403 ? 4.797   93.800  36.305  1.00 82.86  ?  403 LEU D CD2 1 
ATOM   17798 N  N   . THR D  1  404 ? 7.856   89.278  35.381  1.00 78.28  ?  404 THR D N   1 
ATOM   17799 C  CA  . THR D  1  404 ? 8.955   88.586  34.709  1.00 64.41  ?  404 THR D CA  1 
ATOM   17800 C  C   . THR D  1  404 ? 8.805   88.716  33.197  1.00 69.53  ?  404 THR D C   1 
ATOM   17801 O  O   . THR D  1  404 ? 7.749   89.114  32.712  1.00 84.15  ?  404 THR D O   1 
ATOM   17802 C  CB  . THR D  1  404 ? 9.017   87.113  35.145  1.00 72.81  ?  404 THR D CB  1 
ATOM   17803 O  OG1 . THR D  1  404 ? 7.798   86.465  34.793  1.00 76.57  ?  404 THR D OG1 1 
ATOM   17804 C  CG2 . THR D  1  404 ? 9.293   86.958  36.629  1.00 88.45  ?  404 THR D CG2 1 
ATOM   17805 N  N   . TRP D  1  405 ? 9.868   88.397  32.455  1.00 80.36  ?  405 TRP D N   1 
ATOM   17806 C  CA  . TRP D  1  405 ? 9.876   88.475  31.002  1.00 79.85  ?  405 TRP D CA  1 
ATOM   17807 C  C   . TRP D  1  405 ? 10.867  87.456  30.453  1.00 82.86  ?  405 TRP D C   1 
ATOM   17808 O  O   . TRP D  1  405 ? 12.073  87.676  30.516  1.00 90.10  ?  405 TRP D O   1 
ATOM   17809 C  CB  . TRP D  1  405 ? 10.238  89.899  30.542  1.00 67.55  ?  405 TRP D CB  1 
ATOM   17810 C  CG  . TRP D  1  405 ? 10.171  90.116  29.058  1.00 82.47  ?  405 TRP D CG  1 
ATOM   17811 C  CD1 . TRP D  1  405 ? 9.383   89.458  28.161  1.00 84.97  ?  405 TRP D CD1 1 
ATOM   17812 C  CD2 . TRP D  1  405 ? 10.889  91.103  28.310  1.00 99.79  ?  405 TRP D CD2 1 
ATOM   17813 N  NE1 . TRP D  1  405 ? 9.595   89.947  26.897  1.00 85.12  ?  405 TRP D NE1 1 
ATOM   17814 C  CE2 . TRP D  1  405 ? 10.511  90.964  26.960  1.00 94.54  ?  405 TRP D CE2 1 
ATOM   17815 C  CE3 . TRP D  1  405 ? 11.830  92.084  28.647  1.00 105.21 ?  405 TRP D CE3 1 
ATOM   17816 C  CZ2 . TRP D  1  405 ? 11.032  91.771  25.953  1.00 116.57 ?  405 TRP D CZ2 1 
ATOM   17817 C  CZ3 . TRP D  1  405 ? 12.358  92.871  27.643  1.00 115.96 ?  405 TRP D CZ3 1 
ATOM   17818 C  CH2 . TRP D  1  405 ? 11.961  92.709  26.315  1.00 136.17 ?  405 TRP D CH2 1 
ATOM   17819 N  N   . VAL D  1  406 ? 10.357  86.334  29.937  1.00 75.83  ?  406 VAL D N   1 
ATOM   17820 C  CA  . VAL D  1  406 ? 11.187  85.270  29.379  1.00 89.54  ?  406 VAL D CA  1 
ATOM   17821 C  C   . VAL D  1  406 ? 11.102  85.309  27.843  1.00 103.38 ?  406 VAL D C   1 
ATOM   17822 O  O   . VAL D  1  406 ? 10.032  85.553  27.286  1.00 89.73  ?  406 VAL D O   1 
ATOM   17823 C  CB  . VAL D  1  406 ? 10.753  83.898  29.960  1.00 82.74  ?  406 VAL D CB  1 
ATOM   17824 C  CG1 . VAL D  1  406 ? 11.559  82.752  29.351  1.00 96.60  ?  406 VAL D CG1 1 
ATOM   17825 C  CG2 . VAL D  1  406 ? 10.868  83.893  31.481  1.00 67.48  ?  406 VAL D CG2 1 
ATOM   17826 N  N   . ARG D  1  407 ? 12.238  85.092  27.165  1.00 106.72 ?  407 ARG D N   1 
ATOM   17827 C  CA  . ARG D  1  407 ? 12.314  85.097  25.707  1.00 95.75  ?  407 ARG D CA  1 
ATOM   17828 C  C   . ARG D  1  407 ? 13.124  83.885  25.262  1.00 106.42 ?  407 ARG D C   1 
ATOM   17829 O  O   . ARG D  1  407 ? 14.315  83.822  25.555  1.00 121.34 ?  407 ARG D O   1 
ATOM   17830 C  CB  . ARG D  1  407 ? 13.005  86.377  25.212  1.00 94.32  ?  407 ARG D CB  1 
ATOM   17831 C  CG  . ARG D  1  407 ? 12.183  87.642  25.414  1.00 110.18 ?  407 ARG D CG  1 
ATOM   17832 C  CD  . ARG D  1  407 ? 12.792  88.848  24.708  1.00 122.69 ?  407 ARG D CD  1 
ATOM   17833 N  NE  . ARG D  1  407 ? 11.893  89.425  23.707  1.00 121.56 ?  407 ARG D NE  1 
ATOM   17834 C  CZ  . ARG D  1  407 ? 12.175  90.491  22.965  1.00 132.58 ?  407 ARG D CZ  1 
ATOM   17835 N  NH1 . ARG D  1  407 ? 13.343  91.111  23.096  1.00 150.19 ?  407 ARG D NH1 1 
ATOM   17836 N  NH2 . ARG D  1  407 ? 11.294  90.945  22.082  1.00 130.31 ?  407 ARG D NH2 1 
ATOM   17837 N  N   . ILE D  1  408 ? 12.497  82.925  24.567  1.00 109.06 ?  408 ILE D N   1 
ATOM   17838 C  CA  . ILE D  1  408 ? 13.206  81.733  24.098  1.00 104.80 ?  408 ILE D CA  1 
ATOM   17839 C  C   . ILE D  1  408 ? 13.622  81.925  22.634  1.00 102.85 ?  408 ILE D C   1 
ATOM   17840 O  O   . ILE D  1  408 ? 12.851  82.450  21.834  1.00 118.00 ?  408 ILE D O   1 
ATOM   17841 C  CB  . ILE D  1  408 ? 12.348  80.460  24.318  1.00 105.02 ?  408 ILE D CB  1 
ATOM   17842 C  CG1 . ILE D  1  408 ? 12.100  80.243  25.826  1.00 108.53 ?  408 ILE D CG1 1 
ATOM   17843 C  CG2 . ILE D  1  408 ? 13.031  79.231  23.704  1.00 101.27 ?  408 ILE D CG2 1 
ATOM   17844 C  CD1 . ILE D  1  408 ? 11.080  79.198  26.150  1.00 100.98 ?  408 ILE D CD1 1 
ATOM   17845 N  N   . GLY D  1  409 ? 14.842  81.510  22.308  1.00 118.60 ?  409 GLY D N   1 
ATOM   17846 C  CA  . GLY D  1  409 ? 15.404  81.635  20.969  1.00 133.83 ?  409 GLY D CA  1 
ATOM   17847 C  C   . GLY D  1  409 ? 14.986  80.539  20.012  1.00 134.51 ?  409 GLY D C   1 
ATOM   17848 O  O   . GLY D  1  409 ? 14.597  79.450  20.437  1.00 134.22 ?  409 GLY D O   1 
ATOM   17849 N  N   . LYS D  1  410 ? 15.082  80.814  18.704  1.00 130.49 ?  410 LYS D N   1 
ATOM   17850 C  CA  . LYS D  1  410 ? 14.716  79.837  17.676  1.00 138.07 ?  410 LYS D CA  1 
ATOM   17851 C  C   . LYS D  1  410 ? 15.715  78.678  17.672  1.00 141.99 ?  410 LYS D C   1 
ATOM   17852 O  O   . LYS D  1  410 ? 15.326  77.534  17.441  1.00 136.02 ?  410 LYS D O   1 
ATOM   17853 C  CB  . LYS D  1  410 ? 14.681  80.488  16.282  1.00 143.37 ?  410 LYS D CB  1 
ATOM   17854 C  CG  . LYS D  1  410 ? 13.737  81.682  16.167  1.00 134.43 ?  410 LYS D CG  1 
ATOM   17855 C  CD  . LYS D  1  410 ? 13.651  82.221  14.734  1.00 130.28 ?  410 LYS D CD  1 
ATOM   17856 C  CE  . LYS D  1  410 ? 12.459  81.702  13.955  1.00 116.15 ?  410 LYS D CE  1 
ATOM   17857 N  NZ  . LYS D  1  410 ? 11.737  82.798  13.255  1.00 128.26 ?  410 LYS D NZ  1 
ATOM   17858 N  N   . GLU D  1  411 ? 16.997  78.975  17.928  1.00 142.74 ?  411 GLU D N   1 
ATOM   17859 C  CA  . GLU D  1  411 ? 18.048  77.962  17.955  1.00 150.46 ?  411 GLU D CA  1 
ATOM   17860 C  C   . GLU D  1  411 ? 17.820  76.950  19.077  1.00 152.04 ?  411 GLU D C   1 
ATOM   17861 O  O   . GLU D  1  411 ? 18.107  75.768  18.893  1.00 153.48 ?  411 GLU D O   1 
ATOM   17862 C  CB  . GLU D  1  411 ? 19.427  78.622  18.127  1.00 163.78 ?  411 GLU D CB  1 
ATOM   17863 C  CG  . GLU D  1  411 ? 19.837  79.509  16.963  1.00 168.97 ?  411 GLU D CG  1 
ATOM   17864 C  CD  . GLU D  1  411 ? 21.248  80.058  17.046  1.00 173.77 ?  411 GLU D CD  1 
ATOM   17865 O  OE1 . GLU D  1  411 ? 22.101  79.422  17.707  1.00 172.31 ?  411 GLU D OE1 1 
ATOM   17866 O  OE2 . GLU D  1  411 ? 21.503  81.127  16.445  1.00 170.74 ?  411 GLU D OE2 1 
ATOM   17867 N  N   . ALA D  1  412 ? 17.314  77.404  20.236  1.00 143.35 ?  412 ALA D N   1 
ATOM   17868 C  CA  . ALA D  1  412 ? 17.064  76.517  21.372  1.00 119.91 ?  412 ALA D CA  1 
ATOM   17869 C  C   . ALA D  1  412 ? 16.011  75.460  21.056  1.00 125.68 ?  412 ALA D C   1 
ATOM   17870 O  O   . ALA D  1  412 ? 16.184  74.301  21.425  1.00 131.94 ?  412 ALA D O   1 
ATOM   17871 C  CB  . ALA D  1  412 ? 16.634  77.327  22.582  1.00 121.49 ?  412 ALA D CB  1 
ATOM   17872 N  N   . PHE D  1  413 ? 14.924  75.845  20.376  1.00 125.38 ?  413 PHE D N   1 
ATOM   17873 C  CA  . PHE D  1  413 ? 13.869  74.901  20.024  1.00 124.74 ?  413 PHE D CA  1 
ATOM   17874 C  C   . PHE D  1  413 ? 14.403  73.826  19.073  1.00 139.13 ?  413 PHE D C   1 
ATOM   17875 O  O   . PHE D  1  413 ? 14.051  72.656  19.215  1.00 142.65 ?  413 PHE D O   1 
ATOM   17876 C  CB  . PHE D  1  413 ? 12.682  75.645  19.397  1.00 127.88 ?  413 PHE D CB  1 
ATOM   17877 C  CG  . PHE D  1  413 ? 11.512  74.767  19.015  1.00 131.53 ?  413 PHE D CG  1 
ATOM   17878 C  CD1 . PHE D  1  413 ? 10.830  74.036  19.972  1.00 129.35 ?  413 PHE D CD1 1 
ATOM   17879 C  CD2 . PHE D  1  413 ? 11.070  74.705  17.706  1.00 128.91 ?  413 PHE D CD2 1 
ATOM   17880 C  CE1 . PHE D  1  413 ? 9.746   73.242  19.620  1.00 132.14 ?  413 PHE D CE1 1 
ATOM   17881 C  CE2 . PHE D  1  413 ? 9.986   73.909  17.358  1.00 136.27 ?  413 PHE D CE2 1 
ATOM   17882 C  CZ  . PHE D  1  413 ? 9.331   73.183  18.316  1.00 139.64 ?  413 PHE D CZ  1 
ATOM   17883 N  N   . GLU D  1  414 ? 15.262  74.216  18.118  1.00 139.61 ?  414 GLU D N   1 
ATOM   17884 C  CA  . GLU D  1  414 ? 15.849  73.266  17.172  1.00 136.22 ?  414 GLU D CA  1 
ATOM   17885 C  C   . GLU D  1  414 ? 16.750  72.271  17.911  1.00 137.08 ?  414 GLU D C   1 
ATOM   17886 O  O   . GLU D  1  414 ? 16.749  71.087  17.579  1.00 135.87 ?  414 GLU D O   1 
ATOM   17887 C  CB  . GLU D  1  414 ? 16.645  74.006  16.081  1.00 145.32 ?  414 GLU D CB  1 
ATOM   17888 C  CG  . GLU D  1  414 ? 15.795  74.521  14.928  1.00 151.24 ?  414 GLU D CG  1 
ATOM   17889 C  CD  . GLU D  1  414 ? 16.135  75.919  14.452  1.00 163.65 ?  414 GLU D CD  1 
ATOM   17890 O  OE1 . GLU D  1  414 ? 17.327  76.298  14.508  1.00 171.63 ?  414 GLU D OE1 1 
ATOM   17891 O  OE2 . GLU D  1  414 ? 15.205  76.636  14.017  1.00 158.66 ?  414 GLU D OE2 1 
ATOM   17892 N  N   . LYS D  1  415 ? 17.504  72.739  18.921  1.00 136.88 ?  415 LYS D N   1 
ATOM   17893 C  CA  . LYS D  1  415 ? 18.380  71.864  19.712  1.00 122.93 ?  415 LYS D CA  1 
ATOM   17894 C  C   . LYS D  1  415 ? 17.581  70.834  20.534  1.00 127.66 ?  415 LYS D C   1 
ATOM   17895 O  O   . LYS D  1  415 ? 18.135  69.808  20.923  1.00 142.27 ?  415 LYS D O   1 
ATOM   17896 C  CB  . LYS D  1  415 ? 19.271  72.690  20.657  1.00 118.48 ?  415 LYS D CB  1 
ATOM   17897 C  CG  . LYS D  1  415 ? 20.415  73.432  19.960  1.00 123.39 ?  415 LYS D CG  1 
ATOM   17898 C  CD  . LYS D  1  415 ? 21.763  73.225  20.649  1.00 119.57 ?  415 LYS D CD  1 
ATOM   17899 C  CE  . LYS D  1  415 ? 22.766  74.308  20.321  1.00 119.77 ?  415 LYS D CE  1 
ATOM   17900 N  NZ  . LYS D  1  415 ? 23.001  74.449  18.858  1.00 128.87 ?  415 LYS D NZ  1 
ATOM   17901 N  N   . GLY D  1  416 ? 16.306  71.121  20.792  1.00 134.41 ?  416 GLY D N   1 
ATOM   17902 C  CA  . GLY D  1  416 ? 15.421  70.242  21.544  1.00 133.43 ?  416 GLY D CA  1 
ATOM   17903 C  C   . GLY D  1  416 ? 14.946  70.824  22.860  1.00 127.88 ?  416 GLY D C   1 
ATOM   17904 O  O   . GLY D  1  416 ? 14.489  70.076  23.726  1.00 131.80 ?  416 GLY D O   1 
ATOM   17905 N  N   . PHE D  1  417 ? 15.031  72.155  23.029  1.00 127.39 ?  417 PHE D N   1 
ATOM   17906 C  CA  . PHE D  1  417 ? 14.607  72.800  24.270  1.00 120.63 ?  417 PHE D CA  1 
ATOM   17907 C  C   . PHE D  1  417 ? 13.089  72.892  24.369  1.00 124.36 ?  417 PHE D C   1 
ATOM   17908 O  O   . PHE D  1  417 ? 12.429  73.334  23.430  1.00 123.38 ?  417 PHE D O   1 
ATOM   17909 C  CB  . PHE D  1  417 ? 15.215  74.202  24.388  1.00 95.43  ?  417 PHE D CB  1 
ATOM   17910 C  CG  . PHE D  1  417 ? 15.046  74.828  25.751  1.00 100.47 ?  417 PHE D CG  1 
ATOM   17911 C  CD1 . PHE D  1  417 ? 15.892  74.497  26.794  1.00 106.23 ?  417 PHE D CD1 1 
ATOM   17912 C  CD2 . PHE D  1  417 ? 14.046  75.755  25.987  1.00 105.54 ?  417 PHE D CD2 1 
ATOM   17913 C  CE1 . PHE D  1  417 ? 15.740  75.079  28.045  1.00 103.00 ?  417 PHE D CE1 1 
ATOM   17914 C  CE2 . PHE D  1  417 ? 13.892  76.331  27.241  1.00 110.15 ?  417 PHE D CE2 1 
ATOM   17915 C  CZ  . PHE D  1  417 ? 14.738  75.988  28.262  1.00 113.44 ?  417 PHE D CZ  1 
ATOM   17916 N  N   . ARG D  1  418 ? 12.543  72.475  25.513  1.00 122.52 ?  418 ARG D N   1 
ATOM   17917 C  CA  . ARG D  1  418 ? 11.108  72.502  25.790  1.00 126.33 ?  418 ARG D CA  1 
ATOM   17918 C  C   . ARG D  1  418 ? 10.907  73.025  27.222  1.00 133.17 ?  418 ARG D C   1 
ATOM   17919 O  O   . ARG D  1  418 ? 11.879  73.148  27.967  1.00 122.14 ?  418 ARG D O   1 
ATOM   17920 C  CB  . ARG D  1  418 ? 10.500  71.094  25.629  1.00 121.86 ?  418 ARG D CB  1 
ATOM   17921 C  CG  . ARG D  1  418 ? 10.883  70.373  24.330  1.00 128.47 ?  418 ARG D CG  1 
ATOM   17922 C  CD  . ARG D  1  418 ? 10.081  70.840  23.128  1.00 127.50 ?  418 ARG D CD  1 
ATOM   17923 N  NE  . ARG D  1  418 ? 10.467  70.137  21.900  1.00 141.64 ?  418 ARG D NE  1 
ATOM   17924 C  CZ  . ARG D  1  418 ? 11.400  70.540  21.038  1.00 141.48 ?  418 ARG D CZ  1 
ATOM   17925 N  NH1 . ARG D  1  418 ? 12.072  71.667  21.250  1.00 130.72 ?  418 ARG D NH1 1 
ATOM   17926 N  NH2 . ARG D  1  418 ? 11.666  69.821  19.955  1.00 138.19 ?  418 ARG D NH2 1 
ATOM   17927 N  N   . LEU D  1  419 ? 9.662   73.337  27.613  1.00 137.58 ?  419 LEU D N   1 
ATOM   17928 C  CA  . LEU D  1  419 ? 9.394   73.851  28.962  1.00 133.68 ?  419 LEU D CA  1 
ATOM   17929 C  C   . LEU D  1  419 ? 9.864   72.881  30.055  1.00 132.10 ?  419 LEU D C   1 
ATOM   17930 O  O   . LEU D  1  419 ? 10.178  73.323  31.159  1.00 130.04 ?  419 LEU D O   1 
ATOM   17931 C  CB  . LEU D  1  419 ? 7.899   74.168  29.156  1.00 125.48 ?  419 LEU D CB  1 
ATOM   17932 C  CG  . LEU D  1  419 ? 7.343   75.450  28.516  1.00 107.62 ?  419 LEU D CG  1 
ATOM   17933 C  CD1 . LEU D  1  419 ? 8.060   76.685  29.010  1.00 99.18  ?  419 LEU D CD1 1 
ATOM   17934 C  CD2 . LEU D  1  419 ? 7.378   75.380  27.014  1.00 113.98 ?  419 LEU D CD2 1 
ATOM   17935 N  N   . LYS D  1  420 ? 9.926   71.573  29.755  1.00 136.89 ?  420 LYS D N   1 
ATOM   17936 C  CA  . LYS D  1  420 ? 10.380  70.564  30.721  1.00 145.12 ?  420 LYS D CA  1 
ATOM   17937 C  C   . LYS D  1  420 ? 11.807  70.869  31.202  1.00 143.26 ?  420 LYS D C   1 
ATOM   17938 O  O   . LYS D  1  420 ? 12.147  70.585  32.350  1.00 141.49 ?  420 LYS D O   1 
ATOM   17939 C  CB  . LYS D  1  420 ? 10.371  69.159  30.083  1.00 143.19 ?  420 LYS D CB  1 
ATOM   17940 C  CG  . LYS D  1  420 ? 9.000   68.653  29.628  1.00 150.15 ?  420 LYS D CG  1 
ATOM   17941 C  CD  . LYS D  1  420 ? 8.362   67.689  30.620  1.00 155.75 ?  420 LYS D CD  1 
ATOM   17942 C  CE  . LYS D  1  420 ? 6.941   67.359  30.234  1.00 154.16 ?  420 LYS D CE  1 
ATOM   17943 N  NZ  . LYS D  1  420 ? 6.262   66.534  31.265  1.00 148.59 ?  420 LYS D NZ  1 
ATOM   17944 N  N   . HIS D  1  421 ? 12.631  71.447  30.327  1.00 144.58 ?  421 HIS D N   1 
ATOM   17945 C  CA  . HIS D  1  421 ? 14.055  71.684  30.693  1.00 137.28 ?  421 HIS D CA  1 
ATOM   17946 C  C   . HIS D  1  421 ? 14.161  72.858  31.674  1.00 129.72 ?  421 HIS D C   1 
ATOM   17947 O  O   . HIS D  1  421 ? 15.098  72.869  32.502  1.00 128.71 ?  421 HIS D O   1 
ATOM   17948 C  CB  . HIS D  1  421 ? 14.891  71.878  29.425  1.00 131.91 ?  421 HIS D CB  1 
ATOM   17949 C  CG  . HIS D  1  421 ? 14.688  70.782  28.434  1.00 133.11 ?  421 HIS D CG  1 
ATOM   17950 N  ND1 . HIS D  1  421 ? 14.010  70.962  27.249  1.00 129.12 ?  421 HIS D ND1 1 
ATOM   17951 C  CD2 . HIS D  1  421 ? 15.068  69.499  28.453  1.00 132.66 ?  421 HIS D CD2 1 
ATOM   17952 C  CE1 . HIS D  1  421 ? 13.988  69.818  26.581  1.00 128.13 ?  421 HIS D CE1 1 
ATOM   17953 N  NE2 . HIS D  1  421 ? 14.626  68.916  27.294  1.00 131.02 ?  421 HIS D NE2 1 
ATOM   17954 N  N   . PHE D  1  422 ? 13.231  73.813  31.590  1.00 127.97 ?  422 PHE D N   1 
ATOM   17955 C  CA  . PHE D  1  422 ? 13.298  75.011  32.466  1.00 129.04 ?  422 PHE D CA  1 
ATOM   17956 C  C   . PHE D  1  422 ? 13.444  74.554  33.920  1.00 132.45 ?  422 PHE D C   1 
ATOM   17957 O  O   . PHE D  1  422 ? 14.308  75.090  34.638  1.00 129.06 ?  422 PHE D O   1 
ATOM   17958 C  CB  . PHE D  1  422 ? 12.057  75.887  32.284  1.00 117.55 ?  422 PHE D CB  1 
ATOM   17959 C  CG  . PHE D  1  422 ? 12.288  77.141  31.480  1.00 113.52 ?  422 PHE D CG  1 
ATOM   17960 C  CD1 . PHE D  1  422 ? 12.963  78.222  32.025  1.00 122.95 ?  422 PHE D CD1 1 
ATOM   17961 C  CD2 . PHE D  1  422 ? 11.831  77.240  30.176  1.00 109.52 ?  422 PHE D CD2 1 
ATOM   17962 C  CE1 . PHE D  1  422 ? 13.174  79.372  31.282  1.00 125.76 ?  422 PHE D CE1 1 
ATOM   17963 C  CE2 . PHE D  1  422 ? 12.043  78.391  29.434  1.00 93.89  ?  422 PHE D CE2 1 
ATOM   17964 C  CZ  . PHE D  1  422 ? 12.714  79.455  29.988  1.00 114.51 ?  422 PHE D CZ  1 
ATOM   17965 N  N   . GLY D  1  423 ? 12.625  73.584  34.332  1.00 158.66 ?  423 GLY D N   1 
ATOM   17966 C  CA  . GLY D  1  423 ? 12.670  73.092  35.722  1.00 160.75 ?  423 GLY D CA  1 
ATOM   17967 C  C   . GLY D  1  423 ? 13.939  72.306  35.994  1.00 161.38 ?  423 GLY D C   1 
ATOM   17968 O  O   . GLY D  1  423 ? 14.460  72.400  37.122  1.00 162.34 ?  423 GLY D O   1 
ATOM   17969 N  N   . GLU D  1  424 ? 14.424  71.560  34.997  1.00 138.75 ?  424 GLU D N   1 
ATOM   17970 C  CA  . GLU D  1  424 ? 15.613  70.736  35.191  1.00 137.86 ?  424 GLU D CA  1 
ATOM   17971 C  C   . GLU D  1  424 ? 16.778  71.606  35.660  1.00 139.07 ?  424 GLU D C   1 
ATOM   17972 O  O   . GLU D  1  424 ? 17.539  71.171  36.521  1.00 137.55 ?  424 GLU D O   1 
ATOM   17973 C  CB  . GLU D  1  424 ? 15.987  69.984  33.899  1.00 145.45 ?  424 GLU D CB  1 
ATOM   17974 C  CG  . GLU D  1  424 ? 15.083  68.801  33.588  1.00 153.82 ?  424 GLU D CG  1 
ATOM   17975 C  CD  . GLU D  1  424 ? 15.332  67.550  34.409  1.00 148.58 ?  424 GLU D CD  1 
ATOM   17976 O  OE1 . GLU D  1  424 ? 16.153  67.602  35.353  1.00 141.12 ?  424 GLU D OE1 1 
ATOM   17977 O  OE2 . GLU D  1  424 ? 14.701  66.511  34.108  1.00 143.78 ?  424 GLU D OE2 1 
ATOM   17978 N  N   . VAL D  1  425 ? 16.913  72.834  35.120  1.00 134.25 ?  425 VAL D N   1 
ATOM   17979 C  CA  . VAL D  1  425 ? 18.004  73.720  35.539  1.00 122.09 ?  425 VAL D CA  1 
ATOM   17980 C  C   . VAL D  1  425 ? 17.730  74.232  36.951  1.00 120.26 ?  425 VAL D C   1 
ATOM   17981 O  O   . VAL D  1  425 ? 18.657  74.346  37.749  1.00 125.90 ?  425 VAL D O   1 
ATOM   17982 C  CB  . VAL D  1  425 ? 18.302  74.899  34.560  1.00 108.57 ?  425 VAL D CB  1 
ATOM   17983 C  CG1 . VAL D  1  425 ? 18.259  74.452  33.102  1.00 113.50 ?  425 VAL D CG1 1 
ATOM   17984 C  CG2 . VAL D  1  425 ? 17.370  76.089  34.789  1.00 107.51 ?  425 VAL D CG2 1 
ATOM   17985 N  N   . ILE D  1  426 ? 16.463  74.543  37.263  1.00 122.54 ?  426 ILE D N   1 
ATOM   17986 C  CA  . ILE D  1  426 ? 16.102  75.051  38.581  1.00 130.54 ?  426 ILE D CA  1 
ATOM   17987 C  C   . ILE D  1  426 ? 16.370  73.971  39.633  1.00 133.68 ?  426 ILE D C   1 
ATOM   17988 O  O   . ILE D  1  426 ? 17.091  74.224  40.592  1.00 130.79 ?  426 ILE D O   1 
ATOM   17989 C  CB  . ILE D  1  426 ? 14.634  75.557  38.614  1.00 112.77 ?  426 ILE D CB  1 
ATOM   17990 C  CG1 . ILE D  1  426 ? 14.458  76.804  37.711  1.00 106.03 ?  426 ILE D CG1 1 
ATOM   17991 C  CG2 . ILE D  1  426 ? 14.208  75.870  40.052  1.00 112.28 ?  426 ILE D CG2 1 
ATOM   17992 C  CD1 . ILE D  1  426 ? 13.033  77.028  37.208  1.00 113.43 ?  426 ILE D CD1 1 
ATOM   17993 N  N   . TYR D  1  427 ? 15.829  72.760  39.443  1.00 134.74 ?  427 TYR D N   1 
ATOM   17994 C  CA  . TYR D  1  427 ? 16.037  71.667  40.395  1.00 125.94 ?  427 TYR D CA  1 
ATOM   17995 C  C   . TYR D  1  427 ? 17.523  71.355  40.581  1.00 125.83 ?  427 TYR D C   1 
ATOM   17996 O  O   . TYR D  1  427 ? 17.958  71.131  41.709  1.00 131.26 ?  427 TYR D O   1 
ATOM   17997 C  CB  . TYR D  1  427 ? 15.275  70.409  39.939  1.00 128.90 ?  427 TYR D CB  1 
ATOM   17998 C  CG  . TYR D  1  427 ? 15.543  69.180  40.783  1.00 145.45 ?  427 TYR D CG  1 
ATOM   17999 C  CD1 . TYR D  1  427 ? 15.117  69.109  42.102  1.00 144.73 ?  427 TYR D CD1 1 
ATOM   18000 C  CD2 . TYR D  1  427 ? 16.198  68.078  40.252  1.00 142.51 ?  427 TYR D CD2 1 
ATOM   18001 C  CE1 . TYR D  1  427 ? 15.348  67.978  42.877  1.00 140.27 ?  427 TYR D CE1 1 
ATOM   18002 C  CE2 . TYR D  1  427 ? 16.442  66.945  41.019  1.00 139.56 ?  427 TYR D CE2 1 
ATOM   18003 C  CZ  . TYR D  1  427 ? 16.012  66.896  42.330  1.00 147.16 ?  427 TYR D CZ  1 
ATOM   18004 O  OH  . TYR D  1  427 ? 16.243  65.772  43.086  1.00 149.39 ?  427 TYR D OH  1 
ATOM   18005 N  N   . ALA D  1  428 ? 18.300  71.349  39.493  1.00 125.25 ?  428 ALA D N   1 
ATOM   18006 C  CA  . ALA D  1  428 ? 19.727  71.055  39.578  1.00 128.99 ?  428 ALA D CA  1 
ATOM   18007 C  C   . ALA D  1  428 ? 20.507  72.152  40.307  1.00 135.20 ?  428 ALA D C   1 
ATOM   18008 O  O   . ALA D  1  428 ? 21.344  71.837  41.151  1.00 141.93 ?  428 ALA D O   1 
ATOM   18009 C  CB  . ALA D  1  428 ? 20.302  70.843  38.186  1.00 120.40 ?  428 ALA D CB  1 
ATOM   18010 N  N   . LYS D  1  429 ? 20.247  73.430  39.991  1.00 130.45 ?  429 LYS D N   1 
ATOM   18011 C  CA  . LYS D  1  429 ? 20.964  74.533  40.633  1.00 135.50 ?  429 LYS D CA  1 
ATOM   18012 C  C   . LYS D  1  429 ? 20.474  74.799  42.059  1.00 137.70 ?  429 LYS D C   1 
ATOM   18013 O  O   . LYS D  1  429 ? 21.241  75.310  42.872  1.00 142.56 ?  429 LYS D O   1 
ATOM   18014 C  CB  . LYS D  1  429 ? 20.882  75.815  39.784  1.00 122.37 ?  429 LYS D CB  1 
ATOM   18015 C  CG  . LYS D  1  429 ? 21.563  75.734  38.406  1.00 108.27 ?  429 LYS D CG  1 
ATOM   18016 C  CD  . LYS D  1  429 ? 23.087  75.517  38.428  1.00 110.71 ?  429 LYS D CD  1 
ATOM   18017 C  CE  . LYS D  1  429 ? 23.867  76.604  39.124  1.00 104.80 ?  429 LYS D CE  1 
ATOM   18018 N  NZ  . LYS D  1  429 ? 25.329  76.417  38.947  1.00 121.67 ?  429 LYS D NZ  1 
ATOM   18019 N  N   . MET D  1  430 ? 19.221  74.452  42.376  1.00 129.83 ?  430 MET D N   1 
ATOM   18020 C  CA  . MET D  1  430 ? 18.689  74.659  43.725  1.00 136.71 ?  430 MET D CA  1 
ATOM   18021 C  C   . MET D  1  430 ? 19.398  73.769  44.750  1.00 145.60 ?  430 MET D C   1 
ATOM   18022 O  O   . MET D  1  430 ? 19.439  74.121  45.927  1.00 155.42 ?  430 MET D O   1 
ATOM   18023 C  CB  . MET D  1  430 ? 17.177  74.391  43.767  1.00 130.47 ?  430 MET D CB  1 
ATOM   18024 C  CG  . MET D  1  430 ? 16.348  75.501  43.157  1.00 140.33 ?  430 MET D CG  1 
ATOM   18025 S  SD  . MET D  1  430 ? 16.141  76.916  44.258  1.00 134.79 ?  430 MET D SD  1 
ATOM   18026 C  CE  . MET D  1  430 ? 14.765  76.347  45.239  1.00 148.75 ?  430 MET D CE  1 
ATOM   18027 N  N   . LEU D  1  431 ? 19.951  72.625  44.316  1.00 148.89 ?  431 LEU D N   1 
ATOM   18028 C  CA  . LEU D  1  431 ? 20.666  71.716  45.207  1.00 152.48 ?  431 LEU D CA  1 
ATOM   18029 C  C   . LEU D  1  431 ? 22.176  71.974  45.136  1.00 156.50 ?  431 LEU D C   1 
ATOM   18030 O  O   . LEU D  1  431 ? 22.862  71.861  46.148  1.00 161.91 ?  431 LEU D O   1 
ATOM   18031 C  CB  . LEU D  1  431 ? 20.369  70.252  44.840  1.00 143.00 ?  431 LEU D CB  1 
ATOM   18032 C  CG  . LEU D  1  431 ? 18.895  69.860  44.724  1.00 143.02 ?  431 LEU D CG  1 
ATOM   18033 C  CD1 . LEU D  1  431 ? 18.757  68.440  44.229  1.00 144.26 ?  431 LEU D CD1 1 
ATOM   18034 C  CD2 . LEU D  1  431 ? 18.176  70.016  46.047  1.00 141.69 ?  431 LEU D CD2 1 
ATOM   18035 N  N   . ASP D  1  432 ? 22.697  72.316  43.949  1.00 150.98 ?  432 ASP D N   1 
ATOM   18036 C  CA  . ASP D  1  432 ? 24.122  72.578  43.776  1.00 151.37 ?  432 ASP D CA  1 
ATOM   18037 C  C   . ASP D  1  432 ? 24.551  73.872  44.472  1.00 149.09 ?  432 ASP D C   1 
ATOM   18038 O  O   . ASP D  1  432 ? 25.658  73.939  45.001  1.00 153.20 ?  432 ASP D O   1 
ATOM   18039 C  CB  . ASP D  1  432 ? 24.463  72.647  42.278  1.00 148.77 ?  432 ASP D CB  1 
ATOM   18040 C  CG  . ASP D  1  432 ? 25.942  72.788  41.985  1.00 164.83 ?  432 ASP D CG  1 
ATOM   18041 O  OD1 . ASP D  1  432 ? 26.755  72.233  42.756  1.00 165.76 ?  432 ASP D OD1 1 
ATOM   18042 O  OD2 . ASP D  1  432 ? 26.287  73.447  40.981  1.00 162.98 ?  432 ASP D OD2 1 
ATOM   18043 N  N   . GLU D  1  433 ? 23.684  74.895  44.475  1.00 146.00 ?  433 GLU D N   1 
ATOM   18044 C  CA  . GLU D  1  433 ? 23.997  76.181  45.095  1.00 151.71 ?  433 GLU D CA  1 
ATOM   18045 C  C   . GLU D  1  433 ? 23.429  76.297  46.512  1.00 148.72 ?  433 GLU D C   1 
ATOM   18046 O  O   . GLU D  1  433 ? 24.120  76.792  47.400  1.00 144.63 ?  433 GLU D O   1 
ATOM   18047 C  CB  . GLU D  1  433 ? 23.443  77.327  44.224  1.00 154.73 ?  433 GLU D CB  1 
ATOM   18048 C  CG  . GLU D  1  433 ? 24.116  78.678  44.437  1.00 153.00 ?  433 GLU D CG  1 
ATOM   18049 C  CD  . GLU D  1  433 ? 25.144  79.076  43.395  1.00 154.12 ?  433 GLU D CD  1 
ATOM   18050 O  OE1 . GLU D  1  433 ? 25.260  78.375  42.364  1.00 141.06 ?  433 GLU D OE1 1 
ATOM   18051 O  OE2 . GLU D  1  433 ? 25.833  80.099  43.610  1.00 157.82 ?  433 GLU D OE2 1 
ATOM   18052 N  N   . PHE D  1  434 ? 22.181  75.858  46.727  1.00 166.11 ?  434 PHE D N   1 
ATOM   18053 C  CA  . PHE D  1  434 ? 21.541  75.965  48.036  1.00 169.53 ?  434 PHE D CA  1 
ATOM   18054 C  C   . PHE D  1  434 ? 21.238  74.616  48.688  1.00 171.64 ?  434 PHE D C   1 
ATOM   18055 O  O   . PHE D  1  434 ? 20.188  74.449  49.309  1.00 171.33 ?  434 PHE D O   1 
ATOM   18056 C  CB  . PHE D  1  434 ? 20.260  76.801  47.909  1.00 167.62 ?  434 PHE D CB  1 
ATOM   18057 C  CG  . PHE D  1  434 ? 20.520  78.195  47.395  1.00 171.60 ?  434 PHE D CG  1 
ATOM   18058 C  CD1 . PHE D  1  434 ? 21.016  79.176  48.232  1.00 183.10 ?  434 PHE D CD1 1 
ATOM   18059 C  CD2 . PHE D  1  434 ? 20.279  78.520  46.072  1.00 168.58 ?  434 PHE D CD2 1 
ATOM   18060 C  CE1 . PHE D  1  434 ? 21.260  80.456  47.759  1.00 184.88 ?  434 PHE D CE1 1 
ATOM   18061 C  CE2 . PHE D  1  434 ? 20.518  79.804  45.603  1.00 171.18 ?  434 PHE D CE2 1 
ATOM   18062 C  CZ  . PHE D  1  434 ? 21.009  80.762  46.450  1.00 182.82 ?  434 PHE D CZ  1 
ATOM   18063 N  N   . GLY D  1  435 ? 22.163  73.675  48.570  1.00 154.74 ?  435 GLY D N   1 
ATOM   18064 C  CA  . GLY D  1  435 ? 21.996  72.361  49.177  1.00 148.69 ?  435 GLY D CA  1 
ATOM   18065 C  C   . GLY D  1  435 ? 22.109  72.399  50.690  1.00 156.48 ?  435 GLY D C   1 
ATOM   18066 O  O   . GLY D  1  435 ? 21.674  71.465  51.367  1.00 162.59 ?  435 GLY D O   1 
ATOM   18067 N  N   . SER D  1  436 ? 22.694  73.482  51.234  1.00 158.97 ?  436 SER D N   1 
ATOM   18068 C  CA  . SER D  1  436 ? 22.875  73.660  52.672  1.00 163.46 ?  436 SER D CA  1 
ATOM   18069 C  C   . SER D  1  436 ? 21.540  73.695  53.424  1.00 166.18 ?  436 SER D C   1 
ATOM   18070 O  O   . SER D  1  436 ? 21.477  73.239  54.563  1.00 179.56 ?  436 SER D O   1 
ATOM   18071 C  CB  . SER D  1  436 ? 23.657  74.941  52.952  1.00 145.93 ?  436 SER D CB  1 
ATOM   18072 O  OG  . SER D  1  436 ? 23.798  75.171  54.344  1.00 154.29 ?  436 SER D OG  1 
ATOM   18073 N  N   . VAL D  1  437 ? 20.479  74.237  52.802  1.00 166.33 ?  437 VAL D N   1 
ATOM   18074 C  CA  . VAL D  1  437 ? 19.161  74.312  53.445  1.00 169.82 ?  437 VAL D CA  1 
ATOM   18075 C  C   . VAL D  1  437 ? 18.046  73.660  52.605  1.00 171.04 ?  437 VAL D C   1 
ATOM   18076 O  O   . VAL D  1  437 ? 16.875  73.834  52.931  1.00 176.44 ?  437 VAL D O   1 
ATOM   18077 C  CB  . VAL D  1  437 ? 18.792  75.771  53.824  1.00 164.68 ?  437 VAL D CB  1 
ATOM   18078 C  CG1 . VAL D  1  437 ? 19.824  76.366  54.776  1.00 161.21 ?  437 VAL D CG1 1 
ATOM   18079 C  CG2 . VAL D  1  437 ? 18.629  76.647  52.585  1.00 157.62 ?  437 VAL D CG2 1 
ATOM   18080 N  N   . VAL D  1  438 ? 18.394  72.909  51.543  1.00 164.34 ?  438 VAL D N   1 
ATOM   18081 C  CA  . VAL D  1  438 ? 17.395  72.249  50.697  1.00 164.47 ?  438 VAL D CA  1 
ATOM   18082 C  C   . VAL D  1  438 ? 17.770  70.781  50.487  1.00 174.74 ?  438 VAL D C   1 
ATOM   18083 O  O   . VAL D  1  438 ? 18.922  70.478  50.180  1.00 170.87 ?  438 VAL D O   1 
ATOM   18084 C  CB  . VAL D  1  438 ? 17.230  72.970  49.337  1.00 157.06 ?  438 VAL D CB  1 
ATOM   18085 C  CG1 . VAL D  1  438 ? 16.273  72.202  48.428  1.00 146.55 ?  438 VAL D CG1 1 
ATOM   18086 C  CG2 . VAL D  1  438 ? 16.753  74.406  49.531  1.00 154.60 ?  438 VAL D CG2 1 
ATOM   18087 N  N   . ASP D  1  439 ? 16.791  69.875  50.649  1.00 182.25 ?  439 ASP D N   1 
ATOM   18088 C  CA  . ASP D  1  439 ? 16.987  68.437  50.469  1.00 171.73 ?  439 ASP D CA  1 
ATOM   18089 C  C   . ASP D  1  439 ? 16.182  67.958  49.254  1.00 165.95 ?  439 ASP D C   1 
ATOM   18090 O  O   . ASP D  1  439 ? 16.724  67.272  48.390  1.00 164.01 ?  439 ASP D O   1 
ATOM   18091 C  CB  . ASP D  1  439 ? 16.552  67.670  51.732  1.00 174.12 ?  439 ASP D CB  1 
ATOM   18092 C  CG  . ASP D  1  439 ? 17.557  67.703  52.868  1.00 184.87 ?  439 ASP D CG  1 
ATOM   18093 O  OD1 . ASP D  1  439 ? 18.483  68.541  52.820  1.00 178.85 ?  439 ASP D OD1 1 
ATOM   18094 O  OD2 . ASP D  1  439 ? 17.412  66.895  53.810  1.00 190.34 ?  439 ASP D OD2 1 
ATOM   18095 N  N   . LYS D  1  440 ? 14.893  68.332  49.188  1.00 164.97 ?  440 LYS D N   1 
ATOM   18096 C  CA  . LYS D  1  440 ? 13.998  67.955  48.091  1.00 163.08 ?  440 LYS D CA  1 
ATOM   18097 C  C   . LYS D  1  440 ? 13.381  69.206  47.461  1.00 154.96 ?  440 LYS D C   1 
ATOM   18098 O  O   . LYS D  1  440 ? 13.219  70.220  48.140  1.00 153.65 ?  440 LYS D O   1 
ATOM   18099 C  CB  . LYS D  1  440 ? 12.870  67.033  48.590  1.00 169.75 ?  440 LYS D CB  1 
ATOM   18100 C  CG  . LYS D  1  440 ? 13.278  66.043  49.679  1.00 157.15 ?  440 LYS D CG  1 
ATOM   18101 C  CD  . LYS D  1  440 ? 12.109  65.167  50.144  1.00 155.22 ?  440 LYS D CD  1 
ATOM   18102 C  CE  . LYS D  1  440 ? 11.665  64.114  49.150  1.00 160.05 ?  440 LYS D CE  1 
ATOM   18103 N  NZ  . LYS D  1  440 ? 12.777  63.223  48.721  1.00 164.20 ?  440 LYS D NZ  1 
ATOM   18104 N  N   . CYS D  1  441 ? 13.024  69.131  46.170  1.00 151.84 ?  441 CYS D N   1 
ATOM   18105 C  CA  . CYS D  1  441 ? 12.432  70.265  45.458  1.00 152.12 ?  441 CYS D CA  1 
ATOM   18106 C  C   . CYS D  1  441 ? 11.704  69.789  44.195  1.00 138.54 ?  441 CYS D C   1 
ATOM   18107 O  O   . CYS D  1  441 ? 12.138  68.829  43.568  1.00 143.84 ?  441 CYS D O   1 
ATOM   18108 C  CB  . CYS D  1  441 ? 13.512  71.294  45.125  1.00 157.07 ?  441 CYS D CB  1 
ATOM   18109 S  SG  . CYS D  1  441 ? 13.016  72.538  43.906  1.00 148.96 ?  441 CYS D SG  1 
ATOM   18110 N  N   . GLU D  1  442 ? 10.602  70.460  43.819  1.00 137.11 ?  442 GLU D N   1 
ATOM   18111 C  CA  . GLU D  1  442 ? 9.842   70.104  42.618  1.00 133.53 ?  442 GLU D CA  1 
ATOM   18112 C  C   . GLU D  1  442 ? 9.370   71.363  41.889  1.00 138.93 ?  442 GLU D C   1 
ATOM   18113 O  O   . GLU D  1  442 ? 9.016   72.350  42.532  1.00 142.99 ?  442 GLU D O   1 
ATOM   18114 C  CB  . GLU D  1  442 ? 8.656   69.179  42.947  1.00 144.59 ?  442 GLU D CB  1 
ATOM   18115 C  CG  . GLU D  1  442 ? 7.599   69.777  43.863  1.00 141.89 ?  442 GLU D CG  1 
ATOM   18116 C  CD  . GLU D  1  442 ? 6.383   68.894  44.072  1.00 161.69 ?  442 GLU D CD  1 
ATOM   18117 O  OE1 . GLU D  1  442 ? 6.450   67.690  43.733  1.00 171.21 ?  442 GLU D OE1 1 
ATOM   18118 O  OE2 . GLU D  1  442 ? 5.360   69.409  44.578  1.00 153.55 ?  442 GLU D OE2 1 
ATOM   18119 N  N   . VAL D  1  443 ? 9.376   71.330  40.547  1.00 131.61 ?  443 VAL D N   1 
ATOM   18120 C  CA  . VAL D  1  443 ? 8.971   72.468  39.722  1.00 119.41 ?  443 VAL D CA  1 
ATOM   18121 C  C   . VAL D  1  443 ? 7.661   72.177  38.992  1.00 122.31 ?  443 VAL D C   1 
ATOM   18122 O  O   . VAL D  1  443 ? 7.430   71.046  38.571  1.00 127.60 ?  443 VAL D O   1 
ATOM   18123 C  CB  . VAL D  1  443 ? 10.089  72.831  38.715  1.00 114.74 ?  443 VAL D CB  1 
ATOM   18124 C  CG1 . VAL D  1  443 ? 9.702   74.053  37.887  1.00 116.92 ?  443 VAL D CG1 1 
ATOM   18125 C  CG2 . VAL D  1  443 ? 11.416  73.062  39.431  1.00 116.08 ?  443 VAL D CG2 1 
ATOM   18126 N  N   . THR D  1  444 ? 6.813   73.204  38.835  1.00 129.28 ?  444 THR D N   1 
ATOM   18127 C  CA  . THR D  1  444 ? 5.530   73.079  38.147  1.00 124.67 ?  444 THR D CA  1 
ATOM   18128 C  C   . THR D  1  444 ? 5.368   74.266  37.192  1.00 126.78 ?  444 THR D C   1 
ATOM   18129 O  O   . THR D  1  444 ? 5.021   75.360  37.628  1.00 128.87 ?  444 THR D O   1 
ATOM   18130 C  CB  . THR D  1  444 ? 4.374   73.024  39.166  1.00 115.81 ?  444 THR D CB  1 
ATOM   18131 O  OG1 . THR D  1  444 ? 4.735   72.174  40.257  1.00 130.74 ?  444 THR D OG1 1 
ATOM   18132 C  CG2 . THR D  1  444 ? 3.073   72.533  38.545  1.00 120.26 ?  444 THR D CG2 1 
ATOM   18133 N  N   . ILE D  1  445 ? 5.627   74.056  35.896  1.00 120.96 ?  445 ILE D N   1 
ATOM   18134 C  CA  . ILE D  1  445 ? 5.506   75.121  34.896  1.00 118.32 ?  445 ILE D CA  1 
ATOM   18135 C  C   . ILE D  1  445 ? 4.041   75.233  34.462  1.00 121.57 ?  445 ILE D C   1 
ATOM   18136 O  O   . ILE D  1  445 ? 3.380   74.212  34.306  1.00 127.41 ?  445 ILE D O   1 
ATOM   18137 C  CB  . ILE D  1  445 ? 6.436   74.833  33.685  1.00 107.39 ?  445 ILE D CB  1 
ATOM   18138 C  CG1 . ILE D  1  445 ? 7.917   74.636  34.116  1.00 95.01  ?  445 ILE D CG1 1 
ATOM   18139 C  CG2 . ILE D  1  445 ? 6.307   75.922  32.624  1.00 96.61  ?  445 ILE D CG2 1 
ATOM   18140 C  CD1 . ILE D  1  445 ? 8.613   75.838  34.793  1.00 102.08 ?  445 ILE D CD1 1 
ATOM   18141 N  N   . ILE D  1  446 ? 3.527   76.462  34.279  1.00 112.13 ?  446 ILE D N   1 
ATOM   18142 C  CA  . ILE D  1  446 ? 2.133   76.668  33.874  1.00 120.06 ?  446 ILE D CA  1 
ATOM   18143 C  C   . ILE D  1  446 ? 2.038   77.572  32.644  1.00 116.52 ?  446 ILE D C   1 
ATOM   18144 O  O   . ILE D  1  446 ? 2.438   78.731  32.702  1.00 114.65 ?  446 ILE D O   1 
ATOM   18145 C  CB  . ILE D  1  446 ? 1.298   77.262  35.041  1.00 125.24 ?  446 ILE D CB  1 
ATOM   18146 C  CG1 . ILE D  1  446 ? 1.446   76.419  36.349  1.00 116.02 ?  446 ILE D CG1 1 
ATOM   18147 C  CG2 . ILE D  1  446 ? -0.172  77.377  34.635  1.00 120.62 ?  446 ILE D CG2 1 
ATOM   18148 C  CD1 . ILE D  1  446 ? 2.061   77.161  37.546  1.00 109.57 ?  446 ILE D CD1 1 
ATOM   18149 N  N   . THR D  1  447 ? 1.490   77.049  31.540  1.00 124.01 ?  447 THR D N   1 
ATOM   18150 C  CA  . THR D  1  447 ? 1.305   77.810  30.299  1.00 132.85 ?  447 THR D CA  1 
ATOM   18151 C  C   . THR D  1  447 ? -0.198  78.045  30.002  1.00 139.61 ?  447 THR D C   1 
ATOM   18152 O  O   . THR D  1  447 ? -0.525  78.781  29.073  1.00 136.94 ?  447 THR D O   1 
ATOM   18153 C  CB  . THR D  1  447 ? 2.025   77.103  29.140  1.00 135.99 ?  447 THR D CB  1 
ATOM   18154 O  OG1 . THR D  1  447 ? 3.357   76.787  29.545  1.00 142.39 ?  447 THR D OG1 1 
ATOM   18155 C  CG2 . THR D  1  447 ? 2.077   77.950  27.872  1.00 122.65 ?  447 THR D CG2 1 
ATOM   18156 N  N   . ASP D  1  448 ? -1.108  77.437  30.788  1.00 137.61 ?  448 ASP D N   1 
ATOM   18157 C  CA  . ASP D  1  448 ? -2.546  77.613  30.604  1.00 144.39 ?  448 ASP D CA  1 
ATOM   18158 C  C   . ASP D  1  448 ? -2.967  78.976  31.186  1.00 150.62 ?  448 ASP D C   1 
ATOM   18159 O  O   . ASP D  1  448 ? -2.704  79.217  32.362  1.00 152.16 ?  448 ASP D O   1 
ATOM   18160 C  CB  . ASP D  1  448 ? -3.308  76.483  31.319  1.00 154.01 ?  448 ASP D CB  1 
ATOM   18161 C  CG  . ASP D  1  448 ? -4.816  76.607  31.225  1.00 155.27 ?  448 ASP D CG  1 
ATOM   18162 O  OD1 . ASP D  1  448 ? -5.356  76.439  30.110  1.00 156.84 ?  448 ASP D OD1 1 
ATOM   18163 O  OD2 . ASP D  1  448 ? -5.455  76.874  32.266  1.00 149.41 ?  448 ASP D OD2 1 
ATOM   18164 N  N   . PRO D  1  449 ? -3.619  79.878  30.420  1.00 146.70 ?  449 PRO D N   1 
ATOM   18165 C  CA  . PRO D  1  449 ? -4.009  81.179  31.001  1.00 148.54 ?  449 PRO D CA  1 
ATOM   18166 C  C   . PRO D  1  449 ? -4.904  81.098  32.237  1.00 141.17 ?  449 PRO D C   1 
ATOM   18167 O  O   . PRO D  1  449 ? -4.775  81.919  33.144  1.00 132.63 ?  449 PRO D O   1 
ATOM   18168 C  CB  . PRO D  1  449 ? -4.734  81.891  29.851  1.00 126.85 ?  449 PRO D CB  1 
ATOM   18169 C  CG  . PRO D  1  449 ? -4.333  81.184  28.624  1.00 124.07 ?  449 PRO D CG  1 
ATOM   18170 C  CD  . PRO D  1  449 ? -4.013  79.778  29.001  1.00 137.87 ?  449 PRO D CD  1 
ATOM   18171 N  N   . GLY D  1  450 ? -5.807  80.126  32.259  1.00 133.48 ?  450 GLY D N   1 
ATOM   18172 C  CA  . GLY D  1  450 ? -6.727  79.943  33.372  1.00 140.03 ?  450 GLY D CA  1 
ATOM   18173 C  C   . GLY D  1  450 ? -6.060  79.537  34.671  1.00 138.82 ?  450 GLY D C   1 
ATOM   18174 O  O   . GLY D  1  450 ? -6.250  80.195  35.694  1.00 134.99 ?  450 GLY D O   1 
ATOM   18175 N  N   . LYS D  1  451 ? -5.273  78.451  34.646  1.00 136.86 ?  451 LYS D N   1 
ATOM   18176 C  CA  . LYS D  1  451 ? -4.593  77.961  35.847  1.00 130.76 ?  451 LYS D CA  1 
ATOM   18177 C  C   . LYS D  1  451 ? -3.506  78.918  36.349  1.00 133.21 ?  451 LYS D C   1 
ATOM   18178 O  O   . LYS D  1  451 ? -3.306  79.014  37.558  1.00 134.58 ?  451 LYS D O   1 
ATOM   18179 C  CB  . LYS D  1  451 ? -4.009  76.560  35.609  1.00 123.30 ?  451 LYS D CB  1 
ATOM   18180 C  CG  . LYS D  1  451 ? -5.072  75.468  35.520  1.00 133.76 ?  451 LYS D CG  1 
ATOM   18181 C  CD  . LYS D  1  451 ? -4.468  74.124  35.152  1.00 153.40 ?  451 LYS D CD  1 
ATOM   18182 C  CE  . LYS D  1  451 ? -5.500  73.069  34.831  1.00 125.19 ?  451 LYS D CE  1 
ATOM   18183 N  NZ  . LYS D  1  451 ? -4.871  71.831  34.295  1.00 120.51 ?  451 LYS D NZ  1 
ATOM   18184 N  N   . ALA D  1  452 ? -2.814  79.627  35.446  1.00 127.30 ?  452 ALA D N   1 
ATOM   18185 C  CA  . ALA D  1  452 ? -1.776  80.575  35.853  1.00 120.46 ?  452 ALA D CA  1 
ATOM   18186 C  C   . ALA D  1  452 ? -2.390  81.716  36.664  1.00 117.95 ?  452 ALA D C   1 
ATOM   18187 O  O   . ALA D  1  452 ? -1.806  82.150  37.654  1.00 115.34 ?  452 ALA D O   1 
ATOM   18188 C  CB  . ALA D  1  452 ? -1.070  81.134  34.627  1.00 112.39 ?  452 ALA D CB  1 
ATOM   18189 N  N   . GLU D  1  453 ? -3.567  82.195  36.247  1.00 114.36 ?  453 GLU D N   1 
ATOM   18190 C  CA  . GLU D  1  453 ? -4.269  83.274  36.933  1.00 109.15 ?  453 GLU D CA  1 
ATOM   18191 C  C   . GLU D  1  453 ? -4.714  82.834  38.330  1.00 114.19 ?  453 GLU D C   1 
ATOM   18192 O  O   . GLU D  1  453 ? -4.587  83.602  39.281  1.00 114.22 ?  453 GLU D O   1 
ATOM   18193 C  CB  . GLU D  1  453 ? -5.486  83.710  36.100  1.00 110.61 ?  453 GLU D CB  1 
ATOM   18194 C  CG  . GLU D  1  453 ? -6.304  84.831  36.715  1.00 125.52 ?  453 GLU D CG  1 
ATOM   18195 C  CD  . GLU D  1  453 ? -7.462  85.306  35.858  1.00 157.44 ?  453 GLU D CD  1 
ATOM   18196 O  OE1 . GLU D  1  453 ? -7.755  84.654  34.830  1.00 146.21 ?  453 GLU D OE1 1 
ATOM   18197 O  OE2 . GLU D  1  453 ? -8.082  86.332  36.221  1.00 172.68 ?  453 GLU D OE2 1 
ATOM   18198 N  N   . GLU D  1  454 ? -5.231  81.602  38.455  1.00 128.69 ?  454 GLU D N   1 
ATOM   18199 C  CA  . GLU D  1  454 ? -5.697  81.078  39.743  1.00 117.85 ?  454 GLU D CA  1 
ATOM   18200 C  C   . GLU D  1  454 ? -4.520  80.868  40.698  1.00 118.36 ?  454 GLU D C   1 
ATOM   18201 O  O   . GLU D  1  454 ? -4.549  81.365  41.821  1.00 125.53 ?  454 GLU D O   1 
ATOM   18202 C  CB  . GLU D  1  454 ? -6.458  79.749  39.564  1.00 122.87 ?  454 GLU D CB  1 
ATOM   18203 C  CG  . GLU D  1  454 ? -7.673  79.808  38.654  1.00 131.84 ?  454 GLU D CG  1 
ATOM   18204 C  CD  . GLU D  1  454 ? -8.161  78.439  38.227  1.00 158.38 ?  454 GLU D CD  1 
ATOM   18205 O  OE1 . GLU D  1  454 ? -7.990  77.477  39.010  1.00 149.66 ?  454 GLU D OE1 1 
ATOM   18206 O  OE2 . GLU D  1  454 ? -8.708  78.325  37.107  1.00 169.39 ?  454 GLU D OE2 1 
ATOM   18207 N  N   . LEU D  1  455 ? -3.485  80.135  40.252  1.00 117.15 ?  455 LEU D N   1 
ATOM   18208 C  CA  . LEU D  1  455 ? -2.304  79.857  41.069  1.00 114.40 ?  455 LEU D CA  1 
ATOM   18209 C  C   . LEU D  1  455 ? -1.583  81.136  41.505  1.00 126.90 ?  455 LEU D C   1 
ATOM   18210 O  O   . LEU D  1  455 ? -0.954  81.146  42.562  1.00 133.23 ?  455 LEU D O   1 
ATOM   18211 C  CB  . LEU D  1  455 ? -1.335  78.939  40.302  1.00 118.06 ?  455 LEU D CB  1 
ATOM   18212 C  CG  . LEU D  1  455 ? -1.713  77.442  40.258  1.00 118.91 ?  455 LEU D CG  1 
ATOM   18213 C  CD1 . LEU D  1  455 ? -1.301  76.805  38.945  1.00 124.06 ?  455 LEU D CD1 1 
ATOM   18214 C  CD2 . LEU D  1  455 ? -1.083  76.684  41.410  1.00 113.74 ?  455 LEU D CD2 1 
ATOM   18215 N  N   . GLU D  1  456 ? -1.672  82.211  40.705  1.00 125.23 ?  456 GLU D N   1 
ATOM   18216 C  CA  . GLU D  1  456 ? -1.037  83.482  41.043  1.00 117.63 ?  456 GLU D CA  1 
ATOM   18217 C  C   . GLU D  1  456 ? -1.666  84.062  42.315  1.00 121.42 ?  456 GLU D C   1 
ATOM   18218 O  O   . GLU D  1  456 ? -0.951  84.470  43.221  1.00 125.70 ?  456 GLU D O   1 
ATOM   18219 C  CB  . GLU D  1  456 ? -1.171  84.480  39.878  1.00 117.56 ?  456 GLU D CB  1 
ATOM   18220 C  CG  . GLU D  1  456 ? -0.269  85.695  39.999  1.00 109.50 ?  456 GLU D CG  1 
ATOM   18221 C  CD  . GLU D  1  456 ? -0.624  86.828  39.057  1.00 120.32 ?  456 GLU D CD  1 
ATOM   18222 O  OE1 . GLU D  1  456 ? -1.184  86.546  37.974  1.00 135.14 ?  456 GLU D OE1 1 
ATOM   18223 O  OE2 . GLU D  1  456 ? -0.340  87.998  39.401  1.00 103.31 ?  456 GLU D OE2 1 
ATOM   18224 N  N   . GLY D  1  457 ? -2.992  84.085  42.374  1.00 125.01 ?  457 GLY D N   1 
ATOM   18225 C  CA  . GLY D  1  457 ? -3.707  84.609  43.530  1.00 119.33 ?  457 GLY D CA  1 
ATOM   18226 C  C   . GLY D  1  457 ? -3.734  83.671  44.722  1.00 123.25 ?  457 GLY D C   1 
ATOM   18227 O  O   . GLY D  1  457 ? -3.944  84.119  45.850  1.00 138.16 ?  457 GLY D O   1 
ATOM   18228 N  N   . LYS D  1  458 ? -3.531  82.363  44.494  1.00 122.82 ?  458 LYS D N   1 
ATOM   18229 C  CA  . LYS D  1  458 ? -3.552  81.377  45.577  1.00 129.86 ?  458 LYS D CA  1 
ATOM   18230 C  C   . LYS D  1  458 ? -2.349  81.512  46.525  1.00 136.30 ?  458 LYS D C   1 
ATOM   18231 O  O   . LYS D  1  458 ? -2.541  81.708  47.724  1.00 137.95 ?  458 LYS D O   1 
ATOM   18232 C  CB  . LYS D  1  458 ? -3.600  79.940  45.017  1.00 140.92 ?  458 LYS D CB  1 
ATOM   18233 C  CG  . LYS D  1  458 ? -4.943  79.527  44.433  1.00 140.41 ?  458 LYS D CG  1 
ATOM   18234 C  CD  . LYS D  1  458 ? -4.930  78.066  43.994  1.00 144.67 ?  458 LYS D CD  1 
ATOM   18235 C  CE  . LYS D  1  458 ? -6.224  77.650  43.337  1.00 137.63 ?  458 LYS D CE  1 
ATOM   18236 N  NZ  . LYS D  1  458 ? -6.100  76.334  42.655  1.00 126.16 ?  458 LYS D NZ  1 
ATOM   18237 N  N   . TYR D  1  459 ? -1.113  81.393  46.000  1.00 132.54 ?  459 TYR D N   1 
ATOM   18238 C  CA  . TYR D  1  459 ? 0.088   81.465  46.833  1.00 132.65 ?  459 TYR D CA  1 
ATOM   18239 C  C   . TYR D  1  459 ? 1.087   82.555  46.449  1.00 127.69 ?  459 TYR D C   1 
ATOM   18240 O  O   . TYR D  1  459 ? 1.815   83.014  47.323  1.00 132.54 ?  459 TYR D O   1 
ATOM   18241 C  CB  . TYR D  1  459 ? 0.811   80.111  46.827  1.00 140.50 ?  459 TYR D CB  1 
ATOM   18242 C  CG  . TYR D  1  459 ? 0.010   78.980  47.434  1.00 168.98 ?  459 TYR D CG  1 
ATOM   18243 C  CD1 . TYR D  1  459 ? -0.204  78.910  48.803  1.00 177.06 ?  459 TYR D CD1 1 
ATOM   18244 C  CD2 . TYR D  1  459 ? -0.478  77.947  46.646  1.00 158.31 ?  459 TYR D CD2 1 
ATOM   18245 C  CE1 . TYR D  1  459 ? -0.910  77.856  49.372  1.00 169.69 ?  459 TYR D CE1 1 
ATOM   18246 C  CE2 . TYR D  1  459 ? -1.188  76.889  47.202  1.00 159.11 ?  459 TYR D CE2 1 
ATOM   18247 C  CZ  . TYR D  1  459 ? -1.405  76.847  48.568  1.00 172.03 ?  459 TYR D CZ  1 
ATOM   18248 O  OH  . TYR D  1  459 ? -2.103  75.806  49.135  1.00 173.48 ?  459 TYR D OH  1 
ATOM   18249 N  N   . ALA D  1  460 ? 1.154   82.962  45.172  1.00 114.22 ?  460 ALA D N   1 
ATOM   18250 C  CA  . ALA D  1  460 ? 2.120   83.982  44.764  1.00 108.61 ?  460 ALA D CA  1 
ATOM   18251 C  C   . ALA D  1  460 ? 1.821   85.395  45.329  1.00 111.17 ?  460 ALA D C   1 
ATOM   18252 O  O   . ALA D  1  460 ? 2.668   85.947  46.029  1.00 114.11 ?  460 ALA D O   1 
ATOM   18253 C  CB  . ALA D  1  460 ? 2.248   84.014  43.246  1.00 98.10  ?  460 ALA D CB  1 
ATOM   18254 N  N   . VAL D  1  461 ? 0.633   85.970  45.062  1.00 114.31 ?  461 VAL D N   1 
ATOM   18255 C  CA  . VAL D  1  461 ? 0.313   87.317  45.549  1.00 99.82  ?  461 VAL D CA  1 
ATOM   18256 C  C   . VAL D  1  461 ? 0.328   87.402  47.092  1.00 113.25 ?  461 VAL D C   1 
ATOM   18257 O  O   . VAL D  1  461 ? 0.927   88.339  47.627  1.00 111.25 ?  461 VAL D O   1 
ATOM   18258 C  CB  . VAL D  1  461 ? -0.998  87.879  44.944  1.00 107.31 ?  461 VAL D CB  1 
ATOM   18259 C  CG1 . VAL D  1  461 ? -1.284  89.281  45.472  1.00 103.68 ?  461 VAL D CG1 1 
ATOM   18260 C  CG2 . VAL D  1  461 ? -0.930  87.889  43.422  1.00 98.83  ?  461 VAL D CG2 1 
ATOM   18261 N  N   . PRO D  1  462 ? -0.283  86.458  47.843  1.00 115.27 ?  462 PRO D N   1 
ATOM   18262 C  CA  . PRO D  1  462 ? -0.232  86.565  49.312  1.00 118.25 ?  462 PRO D CA  1 
ATOM   18263 C  C   . PRO D  1  462 ? 1.188   86.466  49.879  1.00 120.56 ?  462 PRO D C   1 
ATOM   18264 O  O   . PRO D  1  462 ? 1.459   87.044  50.932  1.00 121.04 ?  462 PRO D O   1 
ATOM   18265 C  CB  . PRO D  1  462 ? -1.117  85.406  49.794  1.00 104.90 ?  462 PRO D CB  1 
ATOM   18266 C  CG  . PRO D  1  462 ? -1.901  84.977  48.606  1.00 107.04 ?  462 PRO D CG  1 
ATOM   18267 C  CD  . PRO D  1  462 ? -1.042  85.264  47.424  1.00 114.81 ?  462 PRO D CD  1 
ATOM   18268 N  N   . ARG D  1  463 ? 2.094   85.744  49.193  1.00 100.37 ?  463 ARG D N   1 
ATOM   18269 C  CA  . ARG D  1  463 ? 3.475   85.600  49.660  1.00 105.69 ?  463 ARG D CA  1 
ATOM   18270 C  C   . ARG D  1  463 ? 4.238   86.913  49.519  1.00 110.88 ?  463 ARG D C   1 
ATOM   18271 O  O   . ARG D  1  463 ? 4.932   87.313  50.451  1.00 110.90 ?  463 ARG D O   1 
ATOM   18272 C  CB  . ARG D  1  463 ? 4.211   84.494  48.886  1.00 116.14 ?  463 ARG D CB  1 
ATOM   18273 C  CG  . ARG D  1  463 ? 3.979   83.088  49.433  1.00 123.96 ?  463 ARG D CG  1 
ATOM   18274 C  CD  . ARG D  1  463 ? 4.977   82.687  50.508  1.00 124.49 ?  463 ARG D CD  1 
ATOM   18275 N  NE  . ARG D  1  463 ? 5.220   81.245  50.507  1.00 139.78 ?  463 ARG D NE  1 
ATOM   18276 C  CZ  . ARG D  1  463 ? 4.402   80.332  51.028  1.00 133.93 ?  463 ARG D CZ  1 
ATOM   18277 N  NH1 . ARG D  1  463 ? 3.266   80.700  51.610  1.00 114.23 ?  463 ARG D NH1 1 
ATOM   18278 N  NH2 . ARG D  1  463 ? 4.716   79.046  50.973  1.00 140.85 ?  463 ARG D NH2 1 
ATOM   18279 N  N   . TYR D  1  464 ? 4.108   87.599  48.371  1.00 110.02 ?  464 TYR D N   1 
ATOM   18280 C  CA  . TYR D  1  464 ? 4.802   88.874  48.165  1.00 110.47 ?  464 TYR D CA  1 
ATOM   18281 C  C   . TYR D  1  464 ? 4.365   89.893  49.225  1.00 111.97 ?  464 TYR D C   1 
ATOM   18282 O  O   . TYR D  1  464 ? 5.188   90.667  49.702  1.00 106.90 ?  464 TYR D O   1 
ATOM   18283 C  CB  . TYR D  1  464 ? 4.544   89.449  46.756  1.00 107.40 ?  464 TYR D CB  1 
ATOM   18284 C  CG  . TYR D  1  464 ? 4.786   88.502  45.597  1.00 94.67  ?  464 TYR D CG  1 
ATOM   18285 C  CD1 . TYR D  1  464 ? 5.756   87.512  45.668  1.00 94.90  ?  464 TYR D CD1 1 
ATOM   18286 C  CD2 . TYR D  1  464 ? 4.061   88.615  44.420  1.00 92.89  ?  464 TYR D CD2 1 
ATOM   18287 C  CE1 . TYR D  1  464 ? 5.982   86.646  44.605  1.00 98.77  ?  464 TYR D CE1 1 
ATOM   18288 C  CE2 . TYR D  1  464 ? 4.279   87.757  43.351  1.00 90.04  ?  464 TYR D CE2 1 
ATOM   18289 C  CZ  . TYR D  1  464 ? 5.240   86.771  43.447  1.00 96.06  ?  464 TYR D CZ  1 
ATOM   18290 O  OH  . TYR D  1  464 ? 5.454   85.923  42.387  1.00 96.87  ?  464 TYR D OH  1 
ATOM   18291 N  N   . LYS D  1  465 ? 3.079   89.875  49.604  1.00 110.33 ?  465 LYS D N   1 
ATOM   18292 C  CA  . LYS D  1  465 ? 2.552   90.784  50.617  1.00 110.26 ?  465 LYS D CA  1 
ATOM   18293 C  C   . LYS D  1  465 ? 3.116   90.424  51.993  1.00 113.75 ?  465 LYS D C   1 
ATOM   18294 O  O   . LYS D  1  465 ? 3.469   91.315  52.762  1.00 122.91 ?  465 LYS D O   1 
ATOM   18295 C  CB  . LYS D  1  465 ? 1.018   90.735  50.638  1.00 96.20  ?  465 LYS D CB  1 
ATOM   18296 C  CG  . LYS D  1  465 ? 0.390   91.255  49.353  1.00 121.28 ?  465 LYS D CG  1 
ATOM   18297 C  CD  . LYS D  1  465 ? -1.124  91.265  49.418  1.00 117.81 ?  465 LYS D CD  1 
ATOM   18298 C  CE  . LYS D  1  465 ? -1.731  91.869  48.177  1.00 110.49 ?  465 LYS D CE  1 
ATOM   18299 N  NZ  . LYS D  1  465 ? -3.187  91.588  48.078  1.00 121.78 ?  465 LYS D NZ  1 
ATOM   18300 N  N   . GLU D  1  466 ? 3.206   89.117  52.296  1.00 116.22 ?  466 GLU D N   1 
ATOM   18301 C  CA  . GLU D  1  466 ? 3.735   88.616  53.567  1.00 123.60 ?  466 GLU D CA  1 
ATOM   18302 C  C   . GLU D  1  466 ? 5.208   89.006  53.730  1.00 115.04 ?  466 GLU D C   1 
ATOM   18303 O  O   . GLU D  1  466 ? 5.611   89.457  54.800  1.00 112.81 ?  466 GLU D O   1 
ATOM   18304 C  CB  . GLU D  1  466 ? 3.580   87.079  53.630  1.00 119.97 ?  466 GLU D CB  1 
ATOM   18305 C  CG  . GLU D  1  466 ? 4.158   86.427  54.878  1.00 128.37 ?  466 GLU D CG  1 
ATOM   18306 C  CD  . GLU D  1  466 ? 3.994   84.919  54.944  1.00 144.91 ?  466 GLU D CD  1 
ATOM   18307 O  OE1 . GLU D  1  466 ? 3.921   84.277  53.871  1.00 143.67 ?  466 GLU D OE1 1 
ATOM   18308 O  OE2 . GLU D  1  466 ? 3.947   84.376  56.072  1.00 142.55 ?  466 GLU D OE2 1 
ATOM   18309 N  N   . ARG D  1  467 ? 5.991   88.839  52.662  1.00 114.79 ?  467 ARG D N   1 
ATOM   18310 C  CA  . ARG D  1  467 ? 7.441   89.164  52.723  1.00 109.61 ?  467 ARG D CA  1 
ATOM   18311 C  C   . ARG D  1  467 ? 7.620   90.677  52.867  1.00 108.02 ?  467 ARG D C   1 
ATOM   18312 O  O   . ARG D  1  467 ? 8.404   91.095  53.740  1.00 116.26 ?  467 ARG D O   1 
ATOM   18313 C  CB  . ARG D  1  467 ? 8.148   88.654  51.464  1.00 99.94  ?  467 ARG D CB  1 
ATOM   18314 C  CG  . ARG D  1  467 ? 7.982   87.161  51.222  1.00 114.28 ?  467 ARG D CG  1 
ATOM   18315 C  CD  . ARG D  1  467 ? 7.969   86.821  49.744  1.00 114.30 ?  467 ARG D CD  1 
ATOM   18316 N  NE  . ARG D  1  467 ? 8.671   85.578  49.460  1.00 119.51 ?  467 ARG D NE  1 
ATOM   18317 C  CZ  . ARG D  1  467 ? 8.526   84.873  48.345  1.00 123.40 ?  467 ARG D CZ  1 
ATOM   18318 N  NH1 . ARG D  1  467 ? 7.750   85.342  47.385  1.00 129.68 ?  467 ARG D NH1 1 
ATOM   18319 N  NH2 . ARG D  1  467 ? 9.126   83.722  48.171  1.00 130.55 ?  467 ARG D NH2 1 
ATOM   18320 N  N   . ASP D  1  468 ? 6.920   91.463  52.046  1.00 108.29 ?  468 ASP D N   1 
ATOM   18321 C  CA  . ASP D  1  468 ? 7.086   92.915  52.074  1.00 112.43 ?  468 ASP D CA  1 
ATOM   18322 C  C   . ASP D  1  468 ? 6.724   93.507  53.433  1.00 114.48 ?  468 ASP D C   1 
ATOM   18323 O  O   . ASP D  1  468 ? 7.303   94.518  53.826  1.00 134.11 ?  468 ASP D O   1 
ATOM   18324 C  CB  . ASP D  1  468 ? 6.246   93.584  50.974  1.00 106.31 ?  468 ASP D CB  1 
ATOM   18325 C  CG  . ASP D  1  468 ? 6.825   93.456  49.579  1.00 108.51 ?  468 ASP D CG  1 
ATOM   18326 O  OD1 . ASP D  1  468 ? 8.006   93.059  49.456  1.00 96.99  ?  468 ASP D OD1 1 
ATOM   18327 O  OD2 . ASP D  1  468 ? 6.100   93.755  48.608  1.00 112.08 ?  468 ASP D OD2 1 
ATOM   18328 N  N   . ALA D  1  469 ? 5.778   92.892  54.153  1.00 112.25 ?  469 ALA D N   1 
ATOM   18329 C  CA  . ALA D  1  469 ? 5.372   93.391  55.464  1.00 110.87 ?  469 ALA D CA  1 
ATOM   18330 C  C   . ALA D  1  469 ? 6.081   92.650  56.598  1.00 111.76 ?  469 ALA D C   1 
ATOM   18331 O  O   . ALA D  1  469 ? 5.532   92.569  57.693  1.00 140.26 ?  469 ALA D O   1 
ATOM   18332 C  CB  . ALA D  1  469 ? 3.867   93.250  55.621  1.00 111.49 ?  469 ALA D CB  1 
ATOM   18333 N  N   . ARG D  1  470 ? 7.291   92.115  56.357  1.00 112.72 ?  470 ARG D N   1 
ATOM   18334 C  CA  . ARG D  1  470 ? 8.015   91.390  57.396  1.00 126.62 ?  470 ARG D CA  1 
ATOM   18335 C  C   . ARG D  1  470 ? 8.397   92.326  58.547  1.00 144.65 ?  470 ARG D C   1 
ATOM   18336 O  O   . ARG D  1  470 ? 8.287   91.930  59.706  1.00 163.01 ?  470 ARG D O   1 
ATOM   18337 C  CB  . ARG D  1  470 ? 9.250   90.669  56.811  1.00 113.31 ?  470 ARG D CB  1 
ATOM   18338 C  CG  . ARG D  1  470 ? 10.116  89.905  57.827  1.00 140.28 ?  470 ARG D CG  1 
ATOM   18339 C  CD  . ARG D  1  470 ? 9.396   88.767  58.545  1.00 162.89 ?  470 ARG D CD  1 
ATOM   18340 N  NE  . ARG D  1  470 ? 10.294  88.044  59.451  1.00 162.83 ?  470 ARG D NE  1 
ATOM   18341 C  CZ  . ARG D  1  470 ? 9.895   87.208  60.408  1.00 167.54 ?  470 ARG D CZ  1 
ATOM   18342 N  NH1 . ARG D  1  470 ? 8.600   86.971  60.598  1.00 173.37 ?  470 ARG D NH1 1 
ATOM   18343 N  NH2 . ARG D  1  470 ? 10.786  86.601  61.181  1.00 174.87 ?  470 ARG D NH2 1 
ATOM   18344 N  N   . LEU D  1  471 ? 8.816   93.565  58.244  1.00 121.85 ?  471 LEU D N   1 
ATOM   18345 C  CA  . LEU D  1  471 ? 9.189   94.508  59.295  1.00 131.42 ?  471 LEU D CA  1 
ATOM   18346 C  C   . LEU D  1  471 ? 8.975   95.951  58.834  1.00 138.98 ?  471 LEU D C   1 
ATOM   18347 O  O   . LEU D  1  471 ? 9.877   96.572  58.273  1.00 141.07 ?  471 LEU D O   1 
ATOM   18348 C  CB  . LEU D  1  471 ? 10.650  94.259  59.708  1.00 120.50 ?  471 LEU D CB  1 
ATOM   18349 C  CG  . LEU D  1  471 ? 11.173  94.991  60.943  1.00 133.95 ?  471 LEU D CG  1 
ATOM   18350 C  CD1 . LEU D  1  471 ? 10.276  94.769  62.164  1.00 131.02 ?  471 LEU D CD1 1 
ATOM   18351 C  CD2 . LEU D  1  471 ? 12.590  94.544  61.251  1.00 114.01 ?  471 LEU D CD2 1 
ATOM   18352 N  N   . GLU D  1  472 ? 7.792   96.505  59.111  1.00 137.04 ?  472 GLU D N   1 
ATOM   18353 C  CA  . GLU D  1  472 ? 7.483   97.881  58.633  1.00 128.43 ?  472 GLU D CA  1 
ATOM   18354 C  C   . GLU D  1  472 ? 7.698   98.892  59.764  1.00 132.90 ?  472 GLU D C   1 
ATOM   18355 O  O   . GLU D  1  472 ? 7.080   99.972  59.706  1.00 148.19 ?  472 GLU D O   1 
ATOM   18356 C  CB  . GLU D  1  472 ? 6.059   97.938  58.082  1.00 123.67 ?  472 GLU D CB  1 
ATOM   18357 C  CG  . GLU D  1  472 ? 5.009   97.642  59.135  1.00 151.02 ?  472 GLU D CG  1 
ATOM   18358 C  CD  . GLU D  1  472 ? 3.603   97.578  58.570  1.00 162.09 ?  472 GLU D CD  1 
ATOM   18359 O  OE1 . GLU D  1  472 ? 3.388   98.087  57.453  1.00 145.79 ?  472 GLU D OE1 1 
ATOM   18360 O  OE2 . GLU D  1  472 ? 2.734   97.005  59.248  1.00 182.10 ?  472 GLU D OE2 1 
ATOM   18361 N  N   . SER D  1  473 ? 8.538   98.558  60.746  1.00 130.90 ?  473 SER D N   1 
ATOM   18362 C  CA  . SER D  1  473 ? 8.852   99.488  61.829  1.00 132.79 ?  473 SER D CA  1 
ATOM   18363 C  C   . SER D  1  473 ? 10.347  99.806  61.939  1.00 133.97 ?  473 SER D C   1 
ATOM   18364 O  O   . SER D  1  473 ? 10.704  100.758 62.632  1.00 133.54 ?  473 SER D O   1 
ATOM   18365 C  CB  . SER D  1  473 ? 8.349   98.932  63.157  1.00 128.06 ?  473 SER D CB  1 
ATOM   18366 O  OG  . SER D  1  473 ? 8.870   97.636  63.400  1.00 132.93 ?  473 SER D OG  1 
ATOM   18367 N  N   . LEU D  1  474 ? 11.220  99.030  61.276  1.00 121.84 ?  474 LEU D N   1 
ATOM   18368 C  CA  . LEU D  1  474 ? 12.653  99.275  61.346  1.00 102.61 ?  474 LEU D CA  1 
ATOM   18369 C  C   . LEU D  1  474 ? 13.034  100.488 60.510  1.00 110.39 ?  474 LEU D C   1 
ATOM   18370 O  O   . LEU D  1  474 ? 12.529  100.658 59.402  1.00 110.92 ?  474 LEU D O   1 
ATOM   18371 C  CB  . LEU D  1  474 ? 13.422  98.035  60.871  1.00 86.32  ?  474 LEU D CB  1 
ATOM   18372 C  CG  . LEU D  1  474 ? 14.940  98.059  61.030  1.00 89.67  ?  474 LEU D CG  1 
ATOM   18373 C  CD1 . LEU D  1  474 ? 15.340  98.193  62.492  1.00 91.03  ?  474 LEU D CD1 1 
ATOM   18374 C  CD2 . LEU D  1  474 ? 15.554  96.806  60.437  1.00 85.61  ?  474 LEU D CD2 1 
ATOM   18375 N  N   . VAL D  1  475 ? 13.921  101.332 61.049  1.00 112.90 ?  475 VAL D N   1 
ATOM   18376 C  CA  . VAL D  1  475 ? 14.393  102.532 60.359  1.00 110.98 ?  475 VAL D CA  1 
ATOM   18377 C  C   . VAL D  1  475 ? 15.908  102.450 60.166  1.00 110.40 ?  475 VAL D C   1 
ATOM   18378 O  O   . VAL D  1  475 ? 16.588  101.732 60.899  1.00 110.17 ?  475 VAL D O   1 
ATOM   18379 C  CB  . VAL D  1  475 ? 13.976  103.842 61.078  1.00 102.86 ?  475 VAL D CB  1 
ATOM   18380 C  CG1 . VAL D  1  475 ? 12.459  103.989 61.117  1.00 93.37  ?  475 VAL D CG1 1 
ATOM   18381 C  CG2 . VAL D  1  475 ? 14.569  103.930 62.482  1.00 105.79 ?  475 VAL D CG2 1 
ATOM   18382 N  N   . ASP D  1  476 ? 16.435  103.186 59.182  1.00 103.49 ?  476 ASP D N   1 
ATOM   18383 C  CA  . ASP D  1  476 ? 17.872  103.186 58.898  1.00 99.23  ?  476 ASP D CA  1 
ATOM   18384 C  C   . ASP D  1  476 ? 18.702  103.759 60.057  1.00 103.29 ?  476 ASP D C   1 
ATOM   18385 O  O   . ASP D  1  476 ? 19.906  103.529 60.106  1.00 102.81 ?  476 ASP D O   1 
ATOM   18386 C  CB  . ASP D  1  476 ? 18.170  103.982 57.615  1.00 92.70  ?  476 ASP D CB  1 
ATOM   18387 C  CG  . ASP D  1  476 ? 17.458  103.478 56.375  1.00 100.04 ?  476 ASP D CG  1 
ATOM   18388 O  OD1 . ASP D  1  476 ? 16.820  102.409 56.451  1.00 119.22 ?  476 ASP D OD1 1 
ATOM   18389 O  OD2 . ASP D  1  476 ? 17.551  104.147 55.326  1.00 93.41  ?  476 ASP D OD2 1 
ATOM   18390 N  N   . GLU D  1  477 ? 18.069  104.497 60.979  1.00 107.65 ?  477 GLU D N   1 
ATOM   18391 C  CA  . GLU D  1  477 ? 18.757  105.102 62.116  1.00 106.41 ?  477 GLU D CA  1 
ATOM   18392 C  C   . GLU D  1  477 ? 19.049  104.085 63.227  1.00 109.11 ?  477 GLU D C   1 
ATOM   18393 O  O   . GLU D  1  477 ? 20.027  104.254 63.954  1.00 105.33 ?  477 GLU D O   1 
ATOM   18394 C  CB  . GLU D  1  477 ? 17.926  106.271 62.678  1.00 105.19 ?  477 GLU D CB  1 
ATOM   18395 C  CG  . GLU D  1  477 ? 17.596  107.351 61.658  1.00 106.53 ?  477 GLU D CG  1 
ATOM   18396 C  CD  . GLU D  1  477 ? 16.252  107.190 60.973  1.00 115.83 ?  477 GLU D CD  1 
ATOM   18397 O  OE1 . GLU D  1  477 ? 16.152  106.355 60.047  1.00 106.38 ?  477 GLU D OE1 1 
ATOM   18398 O  OE2 . GLU D  1  477 ? 15.298  107.904 61.360  1.00 137.13 ?  477 GLU D OE2 1 
ATOM   18399 N  N   . LYS D  1  478 ? 18.216  103.035 63.361  1.00 109.81 ?  478 LYS D N   1 
ATOM   18400 C  CA  . LYS D  1  478 ? 18.390  102.017 64.400  1.00 99.99  ?  478 LYS D CA  1 
ATOM   18401 C  C   . LYS D  1  478 ? 19.135  100.771 63.907  1.00 102.72 ?  478 LYS D C   1 
ATOM   18402 O  O   . LYS D  1  478 ? 18.983  99.705  64.503  1.00 106.71 ?  478 LYS D O   1 
ATOM   18403 C  CB  . LYS D  1  478 ? 17.019  101.606 64.968  1.00 101.03 ?  478 LYS D CB  1 
ATOM   18404 C  CG  . LYS D  1  478 ? 16.245  102.747 65.633  1.00 102.05 ?  478 LYS D CG  1 
ATOM   18405 C  CD  . LYS D  1  478 ? 16.625  102.963 67.102  1.00 105.55 ?  478 LYS D CD  1 
ATOM   18406 C  CE  . LYS D  1  478 ? 15.991  101.954 68.036  1.00 119.50 ?  478 LYS D CE  1 
ATOM   18407 N  NZ  . LYS D  1  478 ? 16.041  102.398 69.456  1.00 114.47 ?  478 LYS D NZ  1 
ATOM   18408 N  N   . VAL D  1  479 ? 19.939  100.892 62.836  1.00 105.93 ?  479 VAL D N   1 
ATOM   18409 C  CA  . VAL D  1  479 ? 20.698  99.761  62.287  1.00 97.71  ?  479 VAL D CA  1 
ATOM   18410 C  C   . VAL D  1  479 ? 22.172  100.148 62.116  1.00 108.15 ?  479 VAL D C   1 
ATOM   18411 O  O   . VAL D  1  479 ? 22.472  101.317 61.888  1.00 117.06 ?  479 VAL D O   1 
ATOM   18412 C  CB  . VAL D  1  479 ? 20.080  99.287  60.951  1.00 99.23  ?  479 VAL D CB  1 
ATOM   18413 C  CG1 . VAL D  1  479 ? 20.875  98.131  60.359  1.00 110.23 ?  479 VAL D CG1 1 
ATOM   18414 C  CG2 . VAL D  1  479 ? 18.627  98.886  61.138  1.00 103.07 ?  479 VAL D CG2 1 
ATOM   18415 N  N   . ASP D  1  480 ? 23.089  99.170  62.229  1.00 119.70 ?  480 ASP D N   1 
ATOM   18416 C  CA  . ASP D  1  480 ? 24.531  99.413  62.091  1.00 121.95 ?  480 ASP D CA  1 
ATOM   18417 C  C   . ASP D  1  480 ? 25.137  98.799  60.813  1.00 114.35 ?  480 ASP D C   1 
ATOM   18418 O  O   . ASP D  1  480 ? 26.231  99.197  60.413  1.00 106.93 ?  480 ASP D O   1 
ATOM   18419 C  CB  . ASP D  1  480 ? 25.292  98.916  63.341  1.00 126.34 ?  480 ASP D CB  1 
ATOM   18420 C  CG  . ASP D  1  480 ? 25.219  97.421  63.602  1.00 132.73 ?  480 ASP D CG  1 
ATOM   18421 O  OD1 . ASP D  1  480 ? 24.278  96.770  63.091  1.00 130.20 ?  480 ASP D OD1 1 
ATOM   18422 O  OD2 . ASP D  1  480 ? 26.098  96.902  64.328  1.00 120.22 ?  480 ASP D OD2 1 
ATOM   18423 N  N   . THR D  1  481 ? 24.448  97.836  60.180  1.00 117.18 ?  481 THR D N   1 
ATOM   18424 C  CA  . THR D  1  481 ? 24.955  97.193  58.968  1.00 110.24 ?  481 THR D CA  1 
ATOM   18425 C  C   . THR D  1  481 ? 23.985  97.315  57.787  1.00 110.94 ?  481 THR D C   1 
ATOM   18426 O  O   . THR D  1  481 ? 22.825  96.921  57.887  1.00 110.89 ?  481 THR D O   1 
ATOM   18427 C  CB  . THR D  1  481 ? 25.240  95.707  59.247  1.00 113.39 ?  481 THR D CB  1 
ATOM   18428 O  OG1 . THR D  1  481 ? 25.994  95.590  60.456  1.00 121.72 ?  481 THR D OG1 1 
ATOM   18429 C  CG2 . THR D  1  481 ? 25.987  95.030  58.100  1.00 108.41 ?  481 THR D CG2 1 
ATOM   18430 N  N   . PHE D  1  482 ? 24.475  97.848  56.663  1.00 104.49 ?  482 PHE D N   1 
ATOM   18431 C  CA  . PHE D  1  482 ? 23.705  97.978  55.427  1.00 93.60  ?  482 PHE D CA  1 
ATOM   18432 C  C   . PHE D  1  482 ? 24.175  96.841  54.505  1.00 100.91 ?  482 PHE D C   1 
ATOM   18433 O  O   . PHE D  1  482 ? 25.082  96.100  54.887  1.00 107.74 ?  482 PHE D O   1 
ATOM   18434 C  CB  . PHE D  1  482 ? 23.952  99.354  54.776  1.00 83.32  ?  482 PHE D CB  1 
ATOM   18435 C  CG  . PHE D  1  482 ? 23.309  100.561 55.432  1.00 91.86  ?  482 PHE D CG  1 
ATOM   18436 C  CD1 . PHE D  1  482 ? 22.476  100.419 56.532  1.00 105.82 ?  482 PHE D CD1 1 
ATOM   18437 C  CD2 . PHE D  1  482 ? 23.522  101.833 54.934  1.00 85.75  ?  482 PHE D CD2 1 
ATOM   18438 C  CE1 . PHE D  1  482 ? 21.890  101.529 57.126  1.00 110.71 ?  482 PHE D CE1 1 
ATOM   18439 C  CE2 . PHE D  1  482 ? 22.927  102.939 55.528  1.00 90.74  ?  482 PHE D CE2 1 
ATOM   18440 C  CZ  . PHE D  1  482 ? 22.112  102.779 56.616  1.00 99.97  ?  482 PHE D CZ  1 
ATOM   18441 N  N   . TYR D  1  483 ? 23.569  96.672  53.316  1.00 101.79 ?  483 TYR D N   1 
ATOM   18442 C  CA  . TYR D  1  483 ? 23.983  95.599  52.405  1.00 92.66  ?  483 TYR D CA  1 
ATOM   18443 C  C   . TYR D  1  483 ? 24.159  96.092  50.978  1.00 95.66  ?  483 TYR D C   1 
ATOM   18444 O  O   . TYR D  1  483 ? 23.580  97.100  50.590  1.00 89.56  ?  483 TYR D O   1 
ATOM   18445 C  CB  . TYR D  1  483 ? 22.995  94.423  52.462  1.00 85.84  ?  483 TYR D CB  1 
ATOM   18446 C  CG  . TYR D  1  483 ? 23.022  93.716  53.796  1.00 92.39  ?  483 TYR D CG  1 
ATOM   18447 C  CD1 . TYR D  1  483 ? 24.002  92.779  54.087  1.00 96.00  ?  483 TYR D CD1 1 
ATOM   18448 C  CD2 . TYR D  1  483 ? 22.124  94.050  54.799  1.00 102.89 ?  483 TYR D CD2 1 
ATOM   18449 C  CE1 . TYR D  1  483 ? 24.059  92.155  55.327  1.00 116.65 ?  483 TYR D CE1 1 
ATOM   18450 C  CE2 . TYR D  1  483 ? 22.173  93.437  56.045  1.00 115.37 ?  483 TYR D CE2 1 
ATOM   18451 C  CZ  . TYR D  1  483 ? 23.145  92.490  56.307  1.00 128.24 ?  483 TYR D CZ  1 
ATOM   18452 O  OH  . TYR D  1  483 ? 23.202  91.874  57.535  1.00 117.17 ?  483 TYR D OH  1 
ATOM   18453 N  N   . SER D  1  484 ? 24.982  95.385  50.203  1.00 81.86  ?  484 SER D N   1 
ATOM   18454 C  CA  . SER D  1  484 ? 25.247  95.747  48.820  1.00 74.06  ?  484 SER D CA  1 
ATOM   18455 C  C   . SER D  1  484 ? 25.022  94.538  47.928  1.00 90.89  ?  484 SER D C   1 
ATOM   18456 O  O   . SER D  1  484 ? 25.515  93.455  48.234  1.00 97.53  ?  484 SER D O   1 
ATOM   18457 C  CB  . SER D  1  484 ? 26.674  96.265  48.660  1.00 88.47  ?  484 SER D CB  1 
ATOM   18458 O  OG  . SER D  1  484 ? 27.643  95.286  48.997  1.00 87.61  ?  484 SER D OG  1 
ATOM   18459 N  N   . CYS D  1  485 ? 24.270  94.713  46.833  1.00 82.43  ?  485 CYS D N   1 
ATOM   18460 C  CA  . CYS D  1  485 ? 23.987  93.632  45.897  1.00 74.30  ?  485 CYS D CA  1 
ATOM   18461 C  C   . CYS D  1  485 ? 24.575  93.962  44.529  1.00 85.01  ?  485 CYS D C   1 
ATOM   18462 O  O   . CYS D  1  485 ? 24.374  95.064  44.021  1.00 92.15  ?  485 CYS D O   1 
ATOM   18463 C  CB  . CYS D  1  485 ? 22.484  93.388  45.807  1.00 79.46  ?  485 CYS D CB  1 
ATOM   18464 S  SG  . CYS D  1  485 ? 22.021  92.032  44.700  1.00 82.78  ?  485 CYS D SG  1 
ATOM   18465 N  N   . ASN D  1  486 ? 25.303  93.008  43.933  1.00 79.63  ?  486 ASN D N   1 
ATOM   18466 C  CA  . ASN D  1  486 ? 25.920  93.189  42.616  1.00 74.21  ?  486 ASN D CA  1 
ATOM   18467 C  C   . ASN D  1  486 ? 25.324  92.242  41.565  1.00 74.38  ?  486 ASN D C   1 
ATOM   18468 O  O   . ASN D  1  486 ? 25.938  92.034  40.524  1.00 85.76  ?  486 ASN D O   1 
ATOM   18469 C  CB  . ASN D  1  486 ? 27.440  92.985  42.712  1.00 70.63  ?  486 ASN D CB  1 
ATOM   18470 C  CG  . ASN D  1  486 ? 27.884  91.569  43.009  1.00 84.32  ?  486 ASN D CG  1 
ATOM   18471 O  OD1 . ASN D  1  486 ? 27.081  90.682  43.313  1.00 85.41  ?  486 ASN D OD1 1 
ATOM   18472 N  ND2 . ASN D  1  486 ? 29.186  91.325  42.927  1.00 88.68  ?  486 ASN D ND2 1 
ATOM   18473 N  N   . LEU D  1  487 ? 24.140  91.673  41.825  1.00 73.96  ?  487 LEU D N   1 
ATOM   18474 C  CA  . LEU D  1  487 ? 23.501  90.743  40.897  1.00 66.82  ?  487 LEU D CA  1 
ATOM   18475 C  C   . LEU D  1  487 ? 23.252  91.388  39.538  1.00 69.26  ?  487 LEU D C   1 
ATOM   18476 O  O   . LEU D  1  487 ? 23.533  90.775  38.509  1.00 68.07  ?  487 LEU D O   1 
ATOM   18477 C  CB  . LEU D  1  487 ? 22.175  90.242  41.496  1.00 71.45  ?  487 LEU D CB  1 
ATOM   18478 C  CG  . LEU D  1  487 ? 21.437  89.150  40.721  1.00 63.10  ?  487 LEU D CG  1 
ATOM   18479 C  CD1 . LEU D  1  487 ? 22.139  87.813  40.862  1.00 72.20  ?  487 LEU D CD1 1 
ATOM   18480 C  CD2 . LEU D  1  487 ? 20.002  89.022  41.199  1.00 78.40  ?  487 LEU D CD2 1 
ATOM   18481 N  N   . CYS D  1  488 ? 22.747  92.626  39.525  1.00 70.51  ?  488 CYS D N   1 
ATOM   18482 C  CA  . CYS D  1  488 ? 22.454  93.317  38.277  1.00 66.53  ?  488 CYS D CA  1 
ATOM   18483 C  C   . CYS D  1  488 ? 23.690  93.865  37.557  1.00 76.88  ?  488 CYS D C   1 
ATOM   18484 O  O   . CYS D  1  488 ? 23.534  94.631  36.607  1.00 88.38  ?  488 CYS D O   1 
ATOM   18485 C  CB  . CYS D  1  488 ? 21.411  94.403  38.506  1.00 52.80  ?  488 CYS D CB  1 
ATOM   18486 S  SG  . CYS D  1  488 ? 19.817  93.770  39.079  1.00 78.17  ?  488 CYS D SG  1 
ATOM   18487 N  N   . GLN D  1  489 ? 24.908  93.470  37.969  1.00 72.18  ?  489 GLN D N   1 
ATOM   18488 C  CA  . GLN D  1  489 ? 26.115  93.932  37.283  1.00 72.15  ?  489 GLN D CA  1 
ATOM   18489 C  C   . GLN D  1  489 ? 26.279  93.246  35.915  1.00 82.53  ?  489 GLN D C   1 
ATOM   18490 O  O   . GLN D  1  489 ? 27.042  93.736  35.083  1.00 82.92  ?  489 GLN D O   1 
ATOM   18491 C  CB  . GLN D  1  489 ? 27.365  93.735  38.151  1.00 74.51  ?  489 GLN D CB  1 
ATOM   18492 C  CG  . GLN D  1  489 ? 27.504  94.778  39.253  1.00 80.06  ?  489 GLN D CG  1 
ATOM   18493 C  CD  . GLN D  1  489 ? 28.922  94.882  39.755  1.00 91.65  ?  489 GLN D CD  1 
ATOM   18494 O  OE1 . GLN D  1  489 ? 29.518  93.896  40.205  1.00 92.14  ?  489 GLN D OE1 1 
ATOM   18495 N  NE2 . GLN D  1  489 ? 29.498  96.076  39.692  1.00 95.36  ?  489 GLN D NE2 1 
ATOM   18496 N  N   . SER D  1  490 ? 25.560  92.130  35.670  1.00 86.51  ?  490 SER D N   1 
ATOM   18497 C  CA  . SER D  1  490 ? 25.617  91.424  34.391  1.00 92.82  ?  490 SER D CA  1 
ATOM   18498 C  C   . SER D  1  490 ? 25.133  92.348  33.272  1.00 100.75 ?  490 SER D C   1 
ATOM   18499 O  O   . SER D  1  490 ? 25.715  92.362  32.186  1.00 116.38 ?  490 SER D O   1 
ATOM   18500 C  CB  . SER D  1  490 ? 24.752  90.167  34.437  1.00 88.83  ?  490 SER D CB  1 
ATOM   18501 O  OG  . SER D  1  490 ? 25.073  89.373  35.568  1.00 109.44 ?  490 SER D OG  1 
ATOM   18502 N  N   . PHE D  1  491 ? 24.078  93.132  33.545  1.00 99.57  ?  491 PHE D N   1 
ATOM   18503 C  CA  . PHE D  1  491 ? 23.541  94.077  32.577  1.00 88.96  ?  491 PHE D CA  1 
ATOM   18504 C  C   . PHE D  1  491 ? 24.259  95.437  32.738  1.00 94.51  ?  491 PHE D C   1 
ATOM   18505 O  O   . PHE D  1  491 ? 24.915  95.889  31.800  1.00 112.03 ?  491 PHE D O   1 
ATOM   18506 C  CB  . PHE D  1  491 ? 22.008  94.196  32.727  1.00 83.76  ?  491 PHE D CB  1 
ATOM   18507 C  CG  . PHE D  1  491 ? 21.260  92.920  32.423  1.00 141.77 ?  491 PHE D CG  1 
ATOM   18508 C  CD1 . PHE D  1  491 ? 20.948  92.574  31.117  1.00 144.33 ?  491 PHE D CD1 1 
ATOM   18509 C  CD2 . PHE D  1  491 ? 20.826  92.091  33.443  1.00 139.13 ?  491 PHE D CD2 1 
ATOM   18510 C  CE1 . PHE D  1  491 ? 20.217  91.424  30.841  1.00 111.33 ?  491 PHE D CE1 1 
ATOM   18511 C  CE2 . PHE D  1  491 ? 20.110  90.937  33.161  1.00 117.77 ?  491 PHE D CE2 1 
ATOM   18512 C  CZ  . PHE D  1  491 ? 19.805  90.611  31.864  1.00 102.02 ?  491 PHE D CZ  1 
ATOM   18513 N  N   . ALA D  1  492 ? 24.142  96.078  33.918  1.00 89.42  ?  492 ALA D N   1 
ATOM   18514 C  CA  . ALA D  1  492 ? 24.771  97.372  34.193  1.00 73.13  ?  492 ALA D CA  1 
ATOM   18515 C  C   . ALA D  1  492 ? 26.064  97.186  34.977  1.00 80.60  ?  492 ALA D C   1 
ATOM   18516 O  O   . ALA D  1  492 ? 26.005  97.024  36.192  1.00 85.79  ?  492 ALA D O   1 
ATOM   18517 C  CB  . ALA D  1  492 ? 23.836  98.240  35.016  1.00 74.80  ?  492 ALA D CB  1 
ATOM   18518 N  N   . PRO D  1  493 ? 27.242  97.171  34.328  1.00 80.67  ?  493 PRO D N   1 
ATOM   18519 C  CA  . PRO D  1  493 ? 28.481  96.932  35.087  1.00 88.83  ?  493 PRO D CA  1 
ATOM   18520 C  C   . PRO D  1  493 ? 28.813  97.860  36.248  1.00 89.74  ?  493 PRO D C   1 
ATOM   18521 O  O   . PRO D  1  493 ? 29.451  97.415  37.200  1.00 90.93  ?  493 PRO D O   1 
ATOM   18522 C  CB  . PRO D  1  493 ? 29.564  96.974  34.006  1.00 92.20  ?  493 PRO D CB  1 
ATOM   18523 C  CG  . PRO D  1  493 ? 29.009  97.834  32.942  1.00 98.81  ?  493 PRO D CG  1 
ATOM   18524 C  CD  . PRO D  1  493 ? 27.533  97.612  32.948  1.00 81.66  ?  493 PRO D CD  1 
ATOM   18525 N  N   . ALA D  1  494 ? 28.402  99.134  36.184  1.00 74.48  ?  494 ALA D N   1 
ATOM   18526 C  CA  . ALA D  1  494 ? 28.708  100.085 37.251  1.00 72.51  ?  494 ALA D CA  1 
ATOM   18527 C  C   . ALA D  1  494 ? 27.651  100.152 38.352  1.00 71.42  ?  494 ALA D C   1 
ATOM   18528 O  O   . ALA D  1  494 ? 27.892  100.801 39.369  1.00 76.25  ?  494 ALA D O   1 
ATOM   18529 C  CB  . ALA D  1  494 ? 28.919  101.465 36.660  1.00 72.28  ?  494 ALA D CB  1 
ATOM   18530 N  N   . HIS D  1  495 ? 26.496  99.498  38.172  1.00 74.11  ?  495 HIS D N   1 
ATOM   18531 C  CA  . HIS D  1  495 ? 25.438  99.541  39.175  1.00 75.49  ?  495 HIS D CA  1 
ATOM   18532 C  C   . HIS D  1  495 ? 25.747  98.732  40.433  1.00 76.68  ?  495 HIS D C   1 
ATOM   18533 O  O   . HIS D  1  495 ? 26.186  97.583  40.354  1.00 70.56  ?  495 HIS D O   1 
ATOM   18534 C  CB  . HIS D  1  495 ? 24.109  99.063  38.581  1.00 60.01  ?  495 HIS D CB  1 
ATOM   18535 C  CG  . HIS D  1  495 ? 23.013  98.994  39.595  1.00 69.22  ?  495 HIS D CG  1 
ATOM   18536 N  ND1 . HIS D  1  495 ? 22.457  100.137 40.132  1.00 74.48  ?  495 HIS D ND1 1 
ATOM   18537 C  CD2 . HIS D  1  495 ? 22.438  97.914  40.170  1.00 85.04  ?  495 HIS D CD2 1 
ATOM   18538 C  CE1 . HIS D  1  495 ? 21.549  99.721  40.999  1.00 77.83  ?  495 HIS D CE1 1 
ATOM   18539 N  NE2 . HIS D  1  495 ? 21.499  98.389  41.051  1.00 76.65  ?  495 HIS D NE2 1 
ATOM   18540 N  N   . VAL D  1  496 ? 25.479  99.342  41.600  1.00 81.24  ?  496 VAL D N   1 
ATOM   18541 C  CA  . VAL D  1  496 ? 25.655  98.729  42.915  1.00 77.95  ?  496 VAL D CA  1 
ATOM   18542 C  C   . VAL D  1  496 ? 24.417  99.102  43.723  1.00 87.97  ?  496 VAL D C   1 
ATOM   18543 O  O   . VAL D  1  496 ? 24.073  100.282 43.795  1.00 90.89  ?  496 VAL D O   1 
ATOM   18544 C  CB  . VAL D  1  496 ? 26.932  99.226  43.632  1.00 69.59  ?  496 VAL D CB  1 
ATOM   18545 C  CG1 . VAL D  1  496 ? 27.183  98.430  44.910  1.00 75.94  ?  496 VAL D CG1 1 
ATOM   18546 C  CG2 . VAL D  1  496 ? 28.141  99.165  42.710  1.00 74.00  ?  496 VAL D CG2 1 
ATOM   18547 N  N   . CYS D  1  497 ? 23.738  98.117  44.316  1.00 82.41  ?  497 CYS D N   1 
ATOM   18548 C  CA  . CYS D  1  497 ? 22.541  98.382  45.113  1.00 65.66  ?  497 CYS D CA  1 
ATOM   18549 C  C   . CYS D  1  497 ? 22.802  98.404  46.609  1.00 76.35  ?  497 CYS D C   1 
ATOM   18550 O  O   . CYS D  1  497 ? 23.153  97.375  47.172  1.00 97.02  ?  497 CYS D O   1 
ATOM   18551 C  CB  . CYS D  1  497 ? 21.502  97.276  44.913  1.00 71.08  ?  497 CYS D CB  1 
ATOM   18552 S  SG  . CYS D  1  497 ? 20.083  97.738  43.880  1.00 74.18  ?  497 CYS D SG  1 
ATOM   18553 N  N   . ILE D  1  498 ? 22.624  99.558  47.255  1.00 76.22  ?  498 ILE D N   1 
ATOM   18554 C  CA  . ILE D  1  498 ? 22.802  99.686  48.701  1.00 73.10  ?  498 ILE D CA  1 
ATOM   18555 C  C   . ILE D  1  498 ? 21.451  99.542  49.390  1.00 79.87  ?  498 ILE D C   1 
ATOM   18556 O  O   . ILE D  1  498 ? 20.659  100.484 49.440  1.00 77.64  ?  498 ILE D O   1 
ATOM   18557 C  CB  . ILE D  1  498 ? 23.502  101.032 49.004  1.00 71.34  ?  498 ILE D CB  1 
ATOM   18558 C  CG1 . ILE D  1  498 ? 24.832  101.163 48.219  1.00 72.39  ?  498 ILE D CG1 1 
ATOM   18559 C  CG2 . ILE D  1  498 ? 23.725  101.207 50.507  1.00 65.28  ?  498 ILE D CG2 1 
ATOM   18560 C  CD1 . ILE D  1  498 ? 25.897  100.101 48.491  1.00 72.80  ?  498 ILE D CD1 1 
ATOM   18561 N  N   . VAL D  1  499 ? 21.196  98.350  49.937  1.00 65.66  ?  499 VAL D N   1 
ATOM   18562 C  CA  . VAL D  1  499 ? 19.864  98.052  50.543  1.00 73.15  ?  499 VAL D CA  1 
ATOM   18563 C  C   . VAL D  1  499 ? 19.849  98.436  52.027  1.00 88.03  ?  499 VAL D C   1 
ATOM   18564 O  O   . VAL D  1  499 ? 20.678  97.890  52.781  1.00 91.11  ?  499 VAL D O   1 
ATOM   18565 C  CB  . VAL D  1  499 ? 19.541  96.560  50.335  1.00 73.91  ?  499 VAL D CB  1 
ATOM   18566 C  CG1 . VAL D  1  499 ? 18.242  96.137  50.997  1.00 89.46  ?  499 VAL D CG1 1 
ATOM   18567 C  CG2 . VAL D  1  499 ? 19.536  96.188  48.860  1.00 77.37  ?  499 VAL D CG2 1 
ATOM   18568 N  N   . THR D  1  500 ? 18.942  99.336  52.429  1.00 84.72  ?  500 THR D N   1 
ATOM   18569 C  CA  . THR D  1  500 ? 18.803  99.705  53.862  1.00 81.28  ?  500 THR D CA  1 
ATOM   18570 C  C   . THR D  1  500 ? 17.359  99.399  54.270  1.00 91.02  ?  500 THR D C   1 
ATOM   18571 O  O   . THR D  1  500 ? 16.541  99.223  53.363  1.00 88.55  ?  500 THR D O   1 
ATOM   18572 C  CB  . THR D  1  500 ? 19.156  101.178 54.091  1.00 82.55  ?  500 THR D CB  1 
ATOM   18573 O  OG1 . THR D  1  500 ? 17.994  101.953 53.794  1.00 92.80  ?  500 THR D OG1 1 
ATOM   18574 C  CG2 . THR D  1  500 ? 20.316  101.646 53.241  1.00 97.92  ?  500 THR D CG2 1 
ATOM   18575 N  N   . PRO D  1  501 ? 17.011  99.293  55.571  1.00 93.46  ?  501 PRO D N   1 
ATOM   18576 C  CA  . PRO D  1  501 ? 15.649  98.920  55.975  1.00 97.49  ?  501 PRO D CA  1 
ATOM   18577 C  C   . PRO D  1  501 ? 14.557  99.693  55.220  1.00 89.34  ?  501 PRO D C   1 
ATOM   18578 O  O   . PRO D  1  501 ? 13.564  99.086  54.871  1.00 95.10  ?  501 PRO D O   1 
ATOM   18579 C  CB  . PRO D  1  501 ? 15.630  99.328  57.454  1.00 93.80  ?  501 PRO D CB  1 
ATOM   18580 C  CG  . PRO D  1  501 ? 17.055  99.116  57.909  1.00 98.15  ?  501 PRO D CG  1 
ATOM   18581 C  CD  . PRO D  1  501 ? 17.904  99.500  56.714  1.00 96.27  ?  501 PRO D CD  1 
ATOM   18582 N  N   . GLU D  1  502 ? 14.760  100.991 54.989  1.00 93.44  ?  502 GLU D N   1 
ATOM   18583 C  CA  . GLU D  1  502 ? 13.774  101.837 54.318  1.00 95.58  ?  502 GLU D CA  1 
ATOM   18584 C  C   . GLU D  1  502 ? 13.970  101.891 52.796  1.00 97.35  ?  502 GLU D C   1 
ATOM   18585 O  O   . GLU D  1  502 ? 12.985  101.989 52.065  1.00 97.41  ?  502 GLU D O   1 
ATOM   18586 C  CB  . GLU D  1  502 ? 13.791  103.242 54.934  1.00 99.48  ?  502 GLU D CB  1 
ATOM   18587 C  CG  . GLU D  1  502 ? 13.461  103.225 56.418  1.00 106.75 ?  502 GLU D CG  1 
ATOM   18588 C  CD  . GLU D  1  502 ? 13.351  104.587 57.072  1.00 109.41 ?  502 GLU D CD  1 
ATOM   18589 O  OE1 . GLU D  1  502 ? 12.277  105.219 56.951  1.00 115.77 ?  502 GLU D OE1 1 
ATOM   18590 O  OE2 . GLU D  1  502 ? 14.337  105.019 57.714  1.00 102.52 ?  502 GLU D OE2 1 
ATOM   18591 N  N   . ARG D  1  503 ? 15.221  101.806 52.316  1.00 90.01  ?  503 ARG D N   1 
ATOM   18592 C  CA  . ARG D  1  503 ? 15.516  101.827 50.881  1.00 76.12  ?  503 ARG D CA  1 
ATOM   18593 C  C   . ARG D  1  503 ? 15.886  100.417 50.418  1.00 85.93  ?  503 ARG D C   1 
ATOM   18594 O  O   . ARG D  1  503 ? 17.062  100.059 50.369  1.00 89.92  ?  503 ARG D O   1 
ATOM   18595 C  CB  . ARG D  1  503 ? 16.643  102.823 50.566  1.00 85.94  ?  503 ARG D CB  1 
ATOM   18596 C  CG  . ARG D  1  503 ? 16.963  102.982 49.079  1.00 88.75  ?  503 ARG D CG  1 
ATOM   18597 C  CD  . ARG D  1  503 ? 18.319  103.643 48.852  1.00 94.19  ?  503 ARG D CD  1 
ATOM   18598 N  NE  . ARG D  1  503 ? 18.229  104.778 47.929  1.00 95.92  ?  503 ARG D NE  1 
ATOM   18599 C  CZ  . ARG D  1  503 ? 18.517  104.751 46.628  1.00 99.06  ?  503 ARG D CZ  1 
ATOM   18600 N  NH1 . ARG D  1  503 ? 18.934  103.627 46.053  1.00 83.98  ?  503 ARG D NH1 1 
ATOM   18601 N  NH2 . ARG D  1  503 ? 18.396  105.850 45.894  1.00 100.48 ?  503 ARG D NH2 1 
ATOM   18602 N  N   . LEU D  1  504 ? 14.869  99.643  50.051  1.00 91.54  ?  504 LEU D N   1 
ATOM   18603 C  CA  . LEU D  1  504 ? 15.117  98.244  49.630  1.00 82.33  ?  504 LEU D CA  1 
ATOM   18604 C  C   . LEU D  1  504 ? 15.631  98.215  48.191  1.00 73.99  ?  504 LEU D C   1 
ATOM   18605 O  O   . LEU D  1  504 ? 15.731  99.291  47.576  1.00 83.23  ?  504 LEU D O   1 
ATOM   18606 C  CB  . LEU D  1  504 ? 13.811  97.459  49.767  1.00 73.58  ?  504 LEU D CB  1 
ATOM   18607 C  CG  . LEU D  1  504 ? 12.835  97.578  48.600  1.00 69.84  ?  504 LEU D CG  1 
ATOM   18608 C  CD1 . LEU D  1  504 ? 11.743  96.534  48.733  1.00 75.08  ?  504 LEU D CD1 1 
ATOM   18609 C  CD2 . LEU D  1  504 ? 12.229  98.971  48.535  1.00 78.67  ?  504 LEU D CD2 1 
ATOM   18610 N  N   . GLY D  1  505 ? 15.938  97.023  47.686  1.00 71.49  ?  505 GLY D N   1 
ATOM   18611 C  CA  . GLY D  1  505 ? 16.455  96.856  46.334  1.00 73.06  ?  505 GLY D CA  1 
ATOM   18612 C  C   . GLY D  1  505 ? 15.534  97.445  45.283  1.00 75.05  ?  505 GLY D C   1 
ATOM   18613 O  O   . GLY D  1  505 ? 14.328  97.561  45.507  1.00 73.23  ?  505 GLY D O   1 
ATOM   18614 N  N   . LEU D  1  506 ? 16.095  97.827  44.131  1.00 82.79  ?  506 LEU D N   1 
ATOM   18615 C  CA  . LEU D  1  506 ? 15.314  98.430  43.042  1.00 72.25  ?  506 LEU D CA  1 
ATOM   18616 C  C   . LEU D  1  506 ? 14.374  97.403  42.401  1.00 75.80  ?  506 LEU D C   1 
ATOM   18617 O  O   . LEU D  1  506 ? 13.279  97.755  41.960  1.00 61.96  ?  506 LEU D O   1 
ATOM   18618 C  CB  . LEU D  1  506 ? 16.241  99.051  41.980  1.00 71.74  ?  506 LEU D CB  1 
ATOM   18619 C  CG  . LEU D  1  506 ? 17.403  99.923  42.482  1.00 63.32  ?  506 LEU D CG  1 
ATOM   18620 C  CD1 . LEU D  1  506 ? 18.131  100.551 41.330  1.00 74.46  ?  506 LEU D CD1 1 
ATOM   18621 C  CD2 . LEU D  1  506 ? 16.932  101.014 43.439  1.00 77.37  ?  506 LEU D CD2 1 
ATOM   18622 N  N   . CYS D  1  507 ? 14.796  96.133  42.367  1.00 78.22  ?  507 CYS D N   1 
ATOM   18623 C  CA  . CYS D  1  507 ? 13.989  95.049  41.819  1.00 73.48  ?  507 CYS D CA  1 
ATOM   18624 C  C   . CYS D  1  507 ? 12.695  94.875  42.621  1.00 65.87  ?  507 CYS D C   1 
ATOM   18625 O  O   . CYS D  1  507 ? 11.666  94.511  42.054  1.00 88.29  ?  507 CYS D O   1 
ATOM   18626 C  CB  . CYS D  1  507 ? 14.796  93.754  41.793  1.00 72.46  ?  507 CYS D CB  1 
ATOM   18627 S  SG  . CYS D  1  507 ? 15.557  93.320  43.379  1.00 75.93  ?  507 CYS D SG  1 
ATOM   18628 N  N   . GLY D  1  508 ? 12.758  95.125  43.924  1.00 64.83  ?  508 GLY D N   1 
ATOM   18629 C  CA  . GLY D  1  508 ? 11.606  94.984  44.802  1.00 81.60  ?  508 GLY D CA  1 
ATOM   18630 C  C   . GLY D  1  508 ? 11.551  93.640  45.499  1.00 83.98  ?  508 GLY D C   1 
ATOM   18631 O  O   . GLY D  1  508 ? 10.690  93.430  46.353  1.00 89.93  ?  508 GLY D O   1 
ATOM   18632 N  N   . ALA D  1  509 ? 12.464  92.716  45.147  1.00 67.61  ?  509 ALA D N   1 
ATOM   18633 C  CA  . ALA D  1  509 ? 12.509  91.383  45.739  1.00 76.38  ?  509 ALA D CA  1 
ATOM   18634 C  C   . ALA D  1  509 ? 13.698  91.184  46.697  1.00 98.28  ?  509 ALA D C   1 
ATOM   18635 O  O   . ALA D  1  509 ? 13.941  90.051  47.114  1.00 99.68  ?  509 ALA D O   1 
ATOM   18636 C  CB  . ALA D  1  509 ? 12.563  90.341  44.634  1.00 93.30  ?  509 ALA D CB  1 
ATOM   18637 N  N   . VAL D  1  510 ? 14.436  92.262  47.051  1.00 88.77  ?  510 VAL D N   1 
ATOM   18638 C  CA  . VAL D  1  510 ? 15.581  92.169  47.963  1.00 72.07  ?  510 VAL D CA  1 
ATOM   18639 C  C   . VAL D  1  510 ? 15.500  93.262  49.034  1.00 87.77  ?  510 VAL D C   1 
ATOM   18640 O  O   . VAL D  1  510 ? 15.983  94.372  48.817  1.00 81.96  ?  510 VAL D O   1 
ATOM   18641 C  CB  . VAL D  1  510 ? 16.930  92.244  47.206  1.00 62.95  ?  510 VAL D CB  1 
ATOM   18642 C  CG1 . VAL D  1  510 ? 18.106  92.192  48.178  1.00 74.28  ?  510 VAL D CG1 1 
ATOM   18643 C  CG2 . VAL D  1  510 ? 17.044  91.126  46.173  1.00 95.10  ?  510 VAL D CG2 1 
ATOM   18644 N  N   . SER D  1  511 ? 14.897  92.943  50.189  1.00 89.56  ?  511 SER D N   1 
ATOM   18645 C  CA  . SER D  1  511 ? 14.776  93.878  51.309  1.00 79.47  ?  511 SER D CA  1 
ATOM   18646 C  C   . SER D  1  511 ? 16.022  93.768  52.196  1.00 93.15  ?  511 SER D C   1 
ATOM   18647 O  O   . SER D  1  511 ? 16.860  92.899  51.957  1.00 103.56 ?  511 SER D O   1 
ATOM   18648 C  CB  . SER D  1  511 ? 13.527  93.559  52.128  1.00 90.58  ?  511 SER D CB  1 
ATOM   18649 O  OG  . SER D  1  511 ? 13.736  92.455  52.994  1.00 93.72  ?  511 SER D OG  1 
ATOM   18650 N  N   . TRP D  1  512 ? 16.152  94.627  53.224  1.00 98.95  ?  512 TRP D N   1 
ATOM   18651 C  CA  . TRP D  1  512 ? 17.306  94.560  54.125  1.00 105.08 ?  512 TRP D CA  1 
ATOM   18652 C  C   . TRP D  1  512 ? 17.366  93.197  54.839  1.00 104.75 ?  512 TRP D C   1 
ATOM   18653 O  O   . TRP D  1  512 ? 18.451  92.706  55.147  1.00 97.68  ?  512 TRP D O   1 
ATOM   18654 C  CB  . TRP D  1  512 ? 17.255  95.704  55.151  1.00 90.26  ?  512 TRP D CB  1 
ATOM   18655 C  CG  . TRP D  1  512 ? 18.410  95.700  56.105  1.00 101.49 ?  512 TRP D CG  1 
ATOM   18656 C  CD1 . TRP D  1  512 ? 19.628  96.281  55.920  1.00 109.48 ?  512 TRP D CD1 1 
ATOM   18657 C  CD2 . TRP D  1  512 ? 18.463  95.052  57.381  1.00 101.98 ?  512 TRP D CD2 1 
ATOM   18658 N  NE1 . TRP D  1  512 ? 20.431  96.053  57.012  1.00 108.84 ?  512 TRP D NE1 1 
ATOM   18659 C  CE2 . TRP D  1  512 ? 19.742  95.293  57.921  1.00 103.50 ?  512 TRP D CE2 1 
ATOM   18660 C  CE3 . TRP D  1  512 ? 17.552  94.292  58.123  1.00 98.93  ?  512 TRP D CE3 1 
ATOM   18661 C  CZ2 . TRP D  1  512 ? 20.130  94.800  59.165  1.00 107.69 ?  512 TRP D CZ2 1 
ATOM   18662 C  CZ3 . TRP D  1  512 ? 17.940  93.804  59.353  1.00 99.37  ?  512 TRP D CZ3 1 
ATOM   18663 C  CH2 . TRP D  1  512 ? 19.215  94.060  59.863  1.00 110.06 ?  512 TRP D CH2 1 
ATOM   18664 N  N   . LEU D  1  513 ? 16.199  92.585  55.076  1.00 101.42 ?  513 LEU D N   1 
ATOM   18665 C  CA  . LEU D  1  513 ? 16.103  91.291  55.738  1.00 111.15 ?  513 LEU D CA  1 
ATOM   18666 C  C   . LEU D  1  513 ? 16.519  90.177  54.773  1.00 112.35 ?  513 LEU D C   1 
ATOM   18667 O  O   . LEU D  1  513 ? 17.235  89.259  55.166  1.00 109.39 ?  513 LEU D O   1 
ATOM   18668 C  CB  . LEU D  1  513 ? 14.661  91.060  56.229  1.00 108.84 ?  513 LEU D CB  1 
ATOM   18669 C  CG  . LEU D  1  513 ? 14.061  92.152  57.160  1.00 113.47 ?  513 LEU D CG  1 
ATOM   18670 C  CD1 . LEU D  1  513 ? 12.997  92.988  56.438  1.00 107.75 ?  513 LEU D CD1 1 
ATOM   18671 C  CD2 . LEU D  1  513 ? 13.459  91.536  58.414  1.00 103.69 ?  513 LEU D CD2 1 
ATOM   18672 N  N   . ASP D  1  514 ? 16.076  90.267  53.508  1.00 110.74 ?  514 ASP D N   1 
ATOM   18673 C  CA  . ASP D  1  514 ? 16.404  89.273  52.485  1.00 97.60  ?  514 ASP D CA  1 
ATOM   18674 C  C   . ASP D  1  514 ? 17.889  89.327  52.119  1.00 99.28  ?  514 ASP D C   1 
ATOM   18675 O  O   . ASP D  1  514 ? 18.479  88.295  51.807  1.00 104.13 ?  514 ASP D O   1 
ATOM   18676 C  CB  . ASP D  1  514 ? 15.550  89.489  51.227  1.00 90.89  ?  514 ASP D CB  1 
ATOM   18677 C  CG  . ASP D  1  514 ? 14.061  89.550  51.500  1.00 106.74 ?  514 ASP D CG  1 
ATOM   18678 O  OD1 . ASP D  1  514 ? 13.594  88.827  52.407  1.00 119.75 ?  514 ASP D OD1 1 
ATOM   18679 O  OD2 . ASP D  1  514 ? 13.363  90.328  50.813  1.00 80.26  ?  514 ASP D OD2 1 
ATOM   18680 N  N   . ALA D  1  515 ? 18.491  90.525  52.150  1.00 94.66  ?  515 ALA D N   1 
ATOM   18681 C  CA  . ALA D  1  515 ? 19.906  90.684  51.836  1.00 95.13  ?  515 ALA D CA  1 
ATOM   18682 C  C   . ALA D  1  515 ? 20.765  90.039  52.923  1.00 111.09 ?  515 ALA D C   1 
ATOM   18683 O  O   . ALA D  1  515 ? 21.775  89.410  52.612  1.00 104.51 ?  515 ALA D O   1 
ATOM   18684 C  CB  . ALA D  1  515 ? 20.248  92.158  51.707  1.00 97.10  ?  515 ALA D CB  1 
ATOM   18685 N  N   . LYS D  1  516 ? 20.363  90.187  54.196  1.00 116.90 ?  516 LYS D N   1 
ATOM   18686 C  CA  . LYS D  1  516 ? 21.087  89.596  55.317  1.00 109.67 ?  516 LYS D CA  1 
ATOM   18687 C  C   . LYS D  1  516 ? 21.012  88.071  55.212  1.00 114.72 ?  516 LYS D C   1 
ATOM   18688 O  O   . LYS D  1  516 ? 22.024  87.396  55.389  1.00 117.05 ?  516 LYS D O   1 
ATOM   18689 C  CB  . LYS D  1  516 ? 20.481  90.073  56.649  1.00 112.42 ?  516 LYS D CB  1 
ATOM   18690 C  CG  . LYS D  1  516 ? 21.189  89.527  57.896  1.00 121.91 ?  516 LYS D CG  1 
ATOM   18691 C  CD  . LYS D  1  516 ? 20.217  89.130  59.012  1.00 116.04 ?  516 LYS D CD  1 
ATOM   18692 C  CE  . LYS D  1  516 ? 19.834  90.283  59.912  1.00 106.70 ?  516 LYS D CE  1 
ATOM   18693 N  NZ  . LYS D  1  516 ? 20.727  90.378  61.098  1.00 111.87 ?  516 LYS D NZ  1 
ATOM   18694 N  N   . ALA D  1  517 ? 19.817  87.534  54.914  1.00 117.05 ?  517 ALA D N   1 
ATOM   18695 C  CA  . ALA D  1  517 ? 19.612  86.094  54.772  1.00 111.94 ?  517 ALA D CA  1 
ATOM   18696 C  C   . ALA D  1  517 ? 20.467  85.523  53.640  1.00 118.93 ?  517 ALA D C   1 
ATOM   18697 O  O   . ALA D  1  517 ? 20.965  84.404  53.759  1.00 116.07 ?  517 ALA D O   1 
ATOM   18698 C  CB  . ALA D  1  517 ? 18.143  85.803  54.510  1.00 103.44 ?  517 ALA D CB  1 
ATOM   18699 N  N   . THR D  1  518 ? 20.643  86.291  52.546  1.00 115.15 ?  518 THR D N   1 
ATOM   18700 C  CA  . THR D  1  518 ? 21.455  85.866  51.404  1.00 108.86 ?  518 THR D CA  1 
ATOM   18701 C  C   . THR D  1  518 ? 22.903  85.655  51.849  1.00 119.11 ?  518 THR D C   1 
ATOM   18702 O  O   . THR D  1  518 ? 23.511  84.642  51.506  1.00 128.98 ?  518 THR D O   1 
ATOM   18703 C  CB  . THR D  1  518 ? 21.387  86.918  50.282  1.00 100.55 ?  518 THR D CB  1 
ATOM   18704 O  OG1 . THR D  1  518 ? 20.026  87.124  49.906  1.00 109.85 ?  518 THR D OG1 1 
ATOM   18705 C  CG2 . THR D  1  518 ? 22.202  86.524  49.061  1.00 98.09  ?  518 THR D CG2 1 
ATOM   18706 N  N   . LEU D  1  519 ? 23.451  86.608  52.618  1.00 111.85 ?  519 LEU D N   1 
ATOM   18707 C  CA  . LEU D  1  519 ? 24.824  86.532  53.112  1.00 115.03 ?  519 LEU D CA  1 
ATOM   18708 C  C   . LEU D  1  519 ? 25.010  85.344  54.065  1.00 123.85 ?  519 LEU D C   1 
ATOM   18709 O  O   . LEU D  1  519 ? 26.076  84.729  54.075  1.00 120.28 ?  519 LEU D O   1 
ATOM   18710 C  CB  . LEU D  1  519 ? 25.192  87.852  53.814  1.00 99.61  ?  519 LEU D CB  1 
ATOM   18711 C  CG  . LEU D  1  519 ? 26.597  87.963  54.397  1.00 100.92 ?  519 LEU D CG  1 
ATOM   18712 C  CD1 . LEU D  1  519 ? 27.654  87.891  53.313  1.00 122.93 ?  519 LEU D CD1 1 
ATOM   18713 C  CD2 . LEU D  1  519 ? 26.748  89.250  55.174  1.00 96.30  ?  519 LEU D CD2 1 
ATOM   18714 N  N   . GLU D  1  520 ? 23.978  85.013  54.855  1.00 126.51 ?  520 GLU D N   1 
ATOM   18715 C  CA  . GLU D  1  520 ? 24.050  83.891  55.790  1.00 131.04 ?  520 GLU D CA  1 
ATOM   18716 C  C   . GLU D  1  520 ? 24.134  82.569  55.025  1.00 130.49 ?  520 GLU D C   1 
ATOM   18717 O  O   . GLU D  1  520 ? 24.965  81.719  55.347  1.00 127.17 ?  520 GLU D O   1 
ATOM   18718 C  CB  . GLU D  1  520 ? 22.812  83.863  56.712  1.00 127.98 ?  520 GLU D CB  1 
ATOM   18719 C  CG  . GLU D  1  520 ? 22.729  85.015  57.699  1.00 128.48 ?  520 GLU D CG  1 
ATOM   18720 C  CD  . GLU D  1  520 ? 23.802  85.020  58.769  1.00 152.25 ?  520 GLU D CD  1 
ATOM   18721 O  OE1 . GLU D  1  520 ? 24.165  83.925  59.257  1.00 159.50 ?  520 GLU D OE1 1 
ATOM   18722 O  OE2 . GLU D  1  520 ? 24.277  86.123  59.124  1.00 155.21 ?  520 GLU D OE2 1 
ATOM   18723 N  N   . LEU D  1  521 ? 23.280  82.400  54.012  1.00 126.91 ?  521 LEU D N   1 
ATOM   18724 C  CA  . LEU D  1  521 ? 23.229  81.173  53.225  1.00 123.34 ?  521 LEU D CA  1 
ATOM   18725 C  C   . LEU D  1  521 ? 24.387  81.046  52.232  1.00 130.80 ?  521 LEU D C   1 
ATOM   18726 O  O   . LEU D  1  521 ? 24.747  79.929  51.870  1.00 147.81 ?  521 LEU D O   1 
ATOM   18727 C  CB  . LEU D  1  521 ? 21.874  81.074  52.504  1.00 118.58 ?  521 LEU D CB  1 
ATOM   18728 C  CG  . LEU D  1  521 ? 20.633  81.111  53.417  1.00 131.12 ?  521 LEU D CG  1 
ATOM   18729 C  CD1 . LEU D  1  521 ? 19.389  81.485  52.641  1.00 128.37 ?  521 LEU D CD1 1 
ATOM   18730 C  CD2 . LEU D  1  521 ? 20.436  79.788  54.136  1.00 139.15 ?  521 LEU D CD2 1 
ATOM   18731 N  N   . ASN D  1  522 ? 24.974  82.167  51.795  1.00 131.81 ?  522 ASN D N   1 
ATOM   18732 C  CA  . ASN D  1  522 ? 26.095  82.124  50.860  1.00 129.61 ?  522 ASN D CA  1 
ATOM   18733 C  C   . ASN D  1  522 ? 27.076  83.251  51.180  1.00 132.68 ?  522 ASN D C   1 
ATOM   18734 O  O   . ASN D  1  522 ? 26.880  84.383  50.735  1.00 133.69 ?  522 ASN D O   1 
ATOM   18735 C  CB  . ASN D  1  522 ? 25.608  82.229  49.415  1.00 127.12 ?  522 ASN D CB  1 
ATOM   18736 C  CG  . ASN D  1  522 ? 26.679  81.923  48.392  1.00 144.74 ?  522 ASN D CG  1 
ATOM   18737 O  OD1 . ASN D  1  522 ? 27.813  81.552  48.725  1.00 142.91 ?  522 ASN D OD1 1 
ATOM   18738 N  ND2 . ASN D  1  522 ? 26.346  82.072  47.116  1.00 149.53 ?  522 ASN D ND2 1 
ATOM   18739 N  N   . PRO D  1  523 ? 28.139  82.975  51.958  1.00 129.16 ?  523 PRO D N   1 
ATOM   18740 C  CA  . PRO D  1  523 ? 29.100  84.045  52.283  1.00 128.30 ?  523 PRO D CA  1 
ATOM   18741 C  C   . PRO D  1  523 ? 29.718  84.696  51.045  1.00 121.93 ?  523 PRO D C   1 
ATOM   18742 O  O   . PRO D  1  523 ? 30.023  85.886  51.067  1.00 109.99 ?  523 PRO D O   1 
ATOM   18743 C  CB  . PRO D  1  523 ? 30.156  83.335  53.138  1.00 134.47 ?  523 PRO D CB  1 
ATOM   18744 C  CG  . PRO D  1  523 ? 29.498  82.097  53.633  1.00 134.30 ?  523 PRO D CG  1 
ATOM   18745 C  CD  . PRO D  1  523 ? 28.525  81.692  52.578  1.00 127.39 ?  523 PRO D CD  1 
ATOM   18746 N  N   . THR D  1  524 ? 29.892  83.916  49.967  1.00 124.45 ?  524 THR D N   1 
ATOM   18747 C  CA  . THR D  1  524 ? 30.453  84.403  48.707  1.00 125.64 ?  524 THR D CA  1 
ATOM   18748 C  C   . THR D  1  524 ? 29.311  84.646  47.708  1.00 131.61 ?  524 THR D C   1 
ATOM   18749 O  O   . THR D  1  524 ? 29.408  84.257  46.543  1.00 127.94 ?  524 THR D O   1 
ATOM   18750 C  CB  . THR D  1  524 ? 31.459  83.379  48.164  1.00 125.84 ?  524 THR D CB  1 
ATOM   18751 O  OG1 . THR D  1  524 ? 30.760  82.178  47.810  1.00 115.06 ?  524 THR D OG1 1 
ATOM   18752 C  CG2 . THR D  1  524 ? 32.555  83.055  49.170  1.00 122.07 ?  524 THR D CG2 1 
ATOM   18753 N  N   . GLY D  1  525 ? 28.241  85.280  48.180  1.00 125.11 ?  525 GLY D N   1 
ATOM   18754 C  CA  . GLY D  1  525 ? 27.069  85.564  47.365  1.00 114.99 ?  525 GLY D CA  1 
ATOM   18755 C  C   . GLY D  1  525 ? 27.039  86.979  46.828  1.00 106.57 ?  525 GLY D C   1 
ATOM   18756 O  O   . GLY D  1  525 ? 27.995  87.737  47.003  1.00 108.57 ?  525 GLY D O   1 
ATOM   18757 N  N   . PRO D  1  526 ? 25.943  87.372  46.158  1.00 87.78  ?  526 PRO D N   1 
ATOM   18758 C  CA  . PRO D  1  526 ? 25.872  88.740  45.623  1.00 93.70  ?  526 PRO D CA  1 
ATOM   18759 C  C   . PRO D  1  526 ? 25.725  89.807  46.705  1.00 104.99 ?  526 PRO D C   1 
ATOM   18760 O  O   . PRO D  1  526 ? 26.204  90.926  46.528  1.00 108.95 ?  526 PRO D O   1 
ATOM   18761 C  CB  . PRO D  1  526 ? 24.643  88.710  44.701  1.00 100.46 ?  526 PRO D CB  1 
ATOM   18762 C  CG  . PRO D  1  526 ? 24.200  87.282  44.636  1.00 103.62 ?  526 PRO D CG  1 
ATOM   18763 C  CD  . PRO D  1  526 ? 24.720  86.609  45.854  1.00 87.73  ?  526 PRO D CD  1 
ATOM   18764 N  N   . CYS D  1  527 ? 25.059  89.469  47.820  1.00 102.96 ?  527 CYS D N   1 
ATOM   18765 C  CA  . CYS D  1  527 ? 24.854  90.410  48.916  1.00 92.59  ?  527 CYS D CA  1 
ATOM   18766 C  C   . CYS D  1  527 ? 26.001  90.336  49.921  1.00 108.58 ?  527 CYS D C   1 
ATOM   18767 O  O   . CYS D  1  527 ? 26.328  89.252  50.399  1.00 98.92  ?  527 CYS D O   1 
ATOM   18768 C  CB  . CYS D  1  527 ? 23.513  90.152  49.593  1.00 77.05  ?  527 CYS D CB  1 
ATOM   18769 S  SG  . CYS D  1  527 ? 22.093  90.223  48.473  1.00 95.59  ?  527 CYS D SG  1 
ATOM   18770 N  N   . GLN D  1  528 ? 26.604  91.495  50.241  1.00 104.29 ?  528 GLN D N   1 
ATOM   18771 C  CA  . GLN D  1  528 ? 27.704  91.603  51.203  1.00 103.90 ?  528 GLN D CA  1 
ATOM   18772 C  C   . GLN D  1  528 ? 27.392  92.706  52.215  1.00 107.96 ?  528 GLN D C   1 
ATOM   18773 O  O   . GLN D  1  528 ? 26.659  93.640  51.901  1.00 107.67 ?  528 GLN D O   1 
ATOM   18774 C  CB  . GLN D  1  528 ? 29.037  91.895  50.491  1.00 109.19 ?  528 GLN D CB  1 
ATOM   18775 C  CG  . GLN D  1  528 ? 29.521  90.769  49.576  1.00 120.18 ?  528 GLN D CG  1 
ATOM   18776 C  CD  . GLN D  1  528 ? 29.676  89.445  50.288  1.00 118.06 ?  528 GLN D CD  1 
ATOM   18777 O  OE1 . GLN D  1  528 ? 28.947  88.481  50.021  1.00 116.64 ?  528 GLN D OE1 1 
ATOM   18778 N  NE2 . GLN D  1  528 ? 30.628  89.359  51.208  1.00 115.81 ?  528 GLN D NE2 1 
ATOM   18779 N  N   . ALA D  1  529 ? 27.938  92.594  53.433  1.00 114.36 ?  529 ALA D N   1 
ATOM   18780 C  CA  . ALA D  1  529 ? 27.694  93.574  54.490  1.00 98.52  ?  529 ALA D CA  1 
ATOM   18781 C  C   . ALA D  1  529 ? 28.478  94.866  54.286  1.00 88.93  ?  529 ALA D C   1 
ATOM   18782 O  O   . ALA D  1  529 ? 29.578  94.850  53.737  1.00 99.71  ?  529 ALA D O   1 
ATOM   18783 C  CB  . ALA D  1  529 ? 28.037  92.974  55.842  1.00 95.06  ?  529 ALA D CB  1 
ATOM   18784 N  N   . VAL D  1  530 ? 27.900  95.986  54.740  1.00 96.22  ?  530 VAL D N   1 
ATOM   18785 C  CA  . VAL D  1  530 ? 28.491  97.319  54.645  1.00 102.42 ?  530 VAL D CA  1 
ATOM   18786 C  C   . VAL D  1  530 ? 28.288  98.012  56.001  1.00 103.27 ?  530 VAL D C   1 
ATOM   18787 O  O   . VAL D  1  530 ? 27.168  98.429  56.292  1.00 105.06 ?  530 VAL D O   1 
ATOM   18788 C  CB  . VAL D  1  530 ? 27.835  98.150  53.507  1.00 99.61  ?  530 VAL D CB  1 
ATOM   18789 C  CG1 . VAL D  1  530 ? 28.501  99.519  53.371  1.00 94.88  ?  530 VAL D CG1 1 
ATOM   18790 C  CG2 . VAL D  1  530 ? 27.874  97.398  52.181  1.00 91.54  ?  530 VAL D CG2 1 
ATOM   18791 N  N   . PRO D  1  531 ? 29.322  98.150  56.855  1.00 96.32  ?  531 PRO D N   1 
ATOM   18792 C  CA  . PRO D  1  531 ? 29.098  98.821  58.147  1.00 101.99 ?  531 PRO D CA  1 
ATOM   18793 C  C   . PRO D  1  531 ? 28.858  100.320 57.967  1.00 107.32 ?  531 PRO D C   1 
ATOM   18794 O  O   . PRO D  1  531 ? 29.571  100.970 57.209  1.00 117.34 ?  531 PRO D O   1 
ATOM   18795 C  CB  . PRO D  1  531 ? 30.364  98.500  58.945  1.00 115.49 ?  531 PRO D CB  1 
ATOM   18796 C  CG  . PRO D  1  531 ? 31.409  98.233  57.930  1.00 102.85 ?  531 PRO D CG  1 
ATOM   18797 C  CD  . PRO D  1  531 ? 30.727  97.724  56.692  1.00 95.99  ?  531 PRO D CD  1 
ATOM   18798 N  N   . LYS D  1  532 ? 27.839  100.862 58.647  1.00 107.75 ?  532 LYS D N   1 
ATOM   18799 C  CA  . LYS D  1  532 ? 27.469  102.275 58.550  1.00 91.05  ?  532 LYS D CA  1 
ATOM   18800 C  C   . LYS D  1  532 ? 28.474  103.165 59.301  1.00 111.76 ?  532 LYS D C   1 
ATOM   18801 O  O   . LYS D  1  532 ? 28.164  103.679 60.376  1.00 120.79 ?  532 LYS D O   1 
ATOM   18802 C  CB  . LYS D  1  532 ? 26.046  102.459 59.113  1.00 85.99  ?  532 LYS D CB  1 
ATOM   18803 C  CG  . LYS D  1  532 ? 25.257  103.598 58.482  1.00 84.04  ?  532 LYS D CG  1 
ATOM   18804 C  CD  . LYS D  1  532 ? 24.364  104.321 59.477  1.00 108.82 ?  532 LYS D CD  1 
ATOM   18805 C  CE  . LYS D  1  532 ? 23.217  103.480 59.980  1.00 98.51  ?  532 LYS D CE  1 
ATOM   18806 N  NZ  . LYS D  1  532 ? 22.414  104.185 61.019  1.00 111.41 ?  532 LYS D NZ  1 
ATOM   18807 N  N   . GLU D  1  533 ? 29.672  103.358 58.722  1.00 122.95 ?  533 GLU D N   1 
ATOM   18808 C  CA  . GLU D  1  533 ? 30.741  104.151 59.341  1.00 128.71 ?  533 GLU D CA  1 
ATOM   18809 C  C   . GLU D  1  533 ? 31.096  105.379 58.501  1.00 118.76 ?  533 GLU D C   1 
ATOM   18810 O  O   . GLU D  1  533 ? 30.941  105.366 57.282  1.00 113.79 ?  533 GLU D O   1 
ATOM   18811 C  CB  . GLU D  1  533 ? 32.005  103.288 59.552  1.00 127.73 ?  533 GLU D CB  1 
ATOM   18812 C  CG  . GLU D  1  533 ? 31.726  101.807 59.756  1.00 130.29 ?  533 GLU D CG  1 
ATOM   18813 C  CD  . GLU D  1  533 ? 32.938  100.938 60.025  1.00 145.52 ?  533 GLU D CD  1 
ATOM   18814 O  OE1 . GLU D  1  533 ? 34.027  101.246 59.489  1.00 157.64 ?  533 GLU D OE1 1 
ATOM   18815 O  OE2 . GLU D  1  533 ? 32.793  99.937  60.764  1.00 135.63 ?  533 GLU D OE2 1 
ATOM   18816 N  N   . GLY D  1  534 ? 31.581  106.421 59.166  1.00 119.88 ?  534 GLY D N   1 
ATOM   18817 C  CA  . GLY D  1  534 ? 31.974  107.661 58.513  1.00 106.85 ?  534 GLY D CA  1 
ATOM   18818 C  C   . GLY D  1  534 ? 30.792  108.516 58.116  1.00 104.72 ?  534 GLY D C   1 
ATOM   18819 O  O   . GLY D  1  534 ? 30.670  108.913 56.958  1.00 116.97 ?  534 GLY D O   1 
ATOM   18820 N  N   . VAL D  1  535 ? 29.877  108.717 59.065  1.00 106.10 ?  535 VAL D N   1 
ATOM   18821 C  CA  . VAL D  1  535 ? 28.644  109.492 58.755  1.00 96.20  ?  535 VAL D CA  1 
ATOM   18822 C  C   . VAL D  1  535 ? 29.050  110.932 58.447  1.00 105.92 ?  535 VAL D C   1 
ATOM   18823 O  O   . VAL D  1  535 ? 29.880  111.486 59.189  1.00 123.85 ?  535 VAL D O   1 
ATOM   18824 C  CB  . VAL D  1  535 ? 27.626  109.427 59.907  1.00 92.77  ?  535 VAL D CB  1 
ATOM   18825 C  CG1 . VAL D  1  535 ? 28.166  110.081 61.168  1.00 97.66  ?  535 VAL D CG1 1 
ATOM   18826 C  CG2 . VAL D  1  535 ? 26.295  110.045 59.511  1.00 100.59 ?  535 VAL D CG2 1 
ATOM   18827 N  N   . VAL D  1  536 ? 28.445  111.524 57.421  1.00 105.28 ?  536 VAL D N   1 
ATOM   18828 C  CA  . VAL D  1  536 ? 28.748  112.944 57.093  1.00 119.04 ?  536 VAL D CA  1 
ATOM   18829 C  C   . VAL D  1  536 ? 27.434  113.713 57.003  1.00 113.59 ?  536 VAL D C   1 
ATOM   18830 O  O   . VAL D  1  536 ? 27.385  114.857 57.495  1.00 123.87 ?  536 VAL D O   1 
ATOM   18831 C  CB  . VAL D  1  536 ? 29.565  113.034 55.798  1.00 104.61 ?  536 VAL D CB  1 
ATOM   18832 C  CG1 . VAL D  1  536 ? 29.746  114.484 55.435  1.00 117.46 ?  536 VAL D CG1 1 
ATOM   18833 C  CG2 . VAL D  1  536 ? 30.931  112.413 55.979  1.00 118.39 ?  536 VAL D CG2 1 
ATOM   18834 N  N   . ASP D  1  537 ? 26.416  113.108 56.397  1.00 89.06  ?  537 ASP D N   1 
ATOM   18835 C  CA  . ASP D  1  537 ? 25.112  113.771 56.402  1.00 100.86 ?  537 ASP D CA  1 
ATOM   18836 C  C   . ASP D  1  537 ? 24.018  112.709 56.472  1.00 83.74  ?  537 ASP D C   1 
ATOM   18837 O  O   . ASP D  1  537 ? 23.888  111.922 55.545  1.00 93.34  ?  537 ASP D O   1 
ATOM   18838 C  CB  . ASP D  1  537 ? 24.945  114.631 55.136  1.00 93.02  ?  537 ASP D CB  1 
ATOM   18839 C  CG  . ASP D  1  537 ? 23.820  115.645 55.205  1.00 106.02 ?  537 ASP D CG  1 
ATOM   18840 O  OD1 . ASP D  1  537 ? 22.766  115.326 55.798  1.00 111.19 ?  537 ASP D OD1 1 
ATOM   18841 O  OD2 . ASP D  1  537 ? 23.988  116.753 54.654  1.00 108.35 ?  537 ASP D OD2 1 
ATOM   18842 N  N   . GLU D  1  538 ? 23.240  112.667 57.563  1.00 87.75  ?  538 GLU D N   1 
ATOM   18843 C  CA  . GLU D  1  538 ? 22.168  111.675 57.692  1.00 87.24  ?  538 GLU D CA  1 
ATOM   18844 C  C   . GLU D  1  538 ? 20.873  112.113 57.002  1.00 90.42  ?  538 GLU D C   1 
ATOM   18845 O  O   . GLU D  1  538 ? 20.000  111.276 56.785  1.00 88.57  ?  538 GLU D O   1 
ATOM   18846 C  CB  . GLU D  1  538 ? 21.909  111.321 59.164  1.00 103.67 ?  538 GLU D CB  1 
ATOM   18847 C  CG  . GLU D  1  538 ? 22.941  110.367 59.737  1.00 105.77 ?  538 GLU D CG  1 
ATOM   18848 C  CD  . GLU D  1  538 ? 22.656  109.879 61.143  1.00 128.73 ?  538 GLU D CD  1 
ATOM   18849 O  OE1 . GLU D  1  538 ? 21.747  110.437 61.800  1.00 129.92 ?  538 GLU D OE1 1 
ATOM   18850 O  OE2 . GLU D  1  538 ? 23.344  108.931 61.588  1.00 133.83 ?  538 GLU D OE2 1 
ATOM   18851 N  N   . ASN D  1  539 ? 20.737  113.404 56.654  1.00 100.57 ?  539 ASN D N   1 
ATOM   18852 C  CA  . ASN D  1  539 ? 19.544  113.880 55.954  1.00 102.17 ?  539 ASN D CA  1 
ATOM   18853 C  C   . ASN D  1  539 ? 19.665  113.507 54.478  1.00 99.24  ?  539 ASN D C   1 
ATOM   18854 O  O   . ASN D  1  539 ? 18.699  113.024 53.887  1.00 90.49  ?  539 ASN D O   1 
ATOM   18855 C  CB  . ASN D  1  539 ? 19.378  115.385 56.113  1.00 99.17  ?  539 ASN D CB  1 
ATOM   18856 C  CG  . ASN D  1  539 ? 18.931  115.782 57.495  1.00 122.39 ?  539 ASN D CG  1 
ATOM   18857 O  OD1 . ASN D  1  539 ? 18.131  115.090 58.139  1.00 124.34 ?  539 ASN D OD1 1 
ATOM   18858 N  ND2 . ASN D  1  539 ? 19.431  116.909 57.988  1.00 147.58 ?  539 ASN D ND2 1 
ATOM   18859 N  N   . LEU D  1  540 ? 20.856  113.719 53.887  1.00 90.55  ?  540 LEU D N   1 
ATOM   18860 C  CA  . LEU D  1  540 ? 21.120  113.371 52.489  1.00 83.13  ?  540 LEU D CA  1 
ATOM   18861 C  C   . LEU D  1  540 ? 21.443  111.882 52.366  1.00 83.57  ?  540 LEU D C   1 
ATOM   18862 O  O   . LEU D  1  540 ? 21.108  111.266 51.357  1.00 87.09  ?  540 LEU D O   1 
ATOM   18863 C  CB  . LEU D  1  540 ? 22.305  114.182 51.929  1.00 86.03  ?  540 LEU D CB  1 
ATOM   18864 C  CG  . LEU D  1  540 ? 21.995  115.565 51.347  1.00 85.14  ?  540 LEU D CG  1 
ATOM   18865 C  CD1 . LEU D  1  540 ? 23.253  116.407 51.231  1.00 92.87  ?  540 LEU D CD1 1 
ATOM   18866 C  CD2 . LEU D  1  540 ? 21.355  115.458 49.983  1.00 81.87  ?  540 LEU D CD2 1 
ATOM   18867 N  N   . GLY D  1  541 ? 22.105  111.324 53.374  1.00 77.43  ?  541 GLY D N   1 
ATOM   18868 C  CA  . GLY D  1  541 ? 22.481  109.920 53.381  1.00 75.13  ?  541 GLY D CA  1 
ATOM   18869 C  C   . GLY D  1  541 ? 23.858  109.715 52.792  1.00 74.02  ?  541 GLY D C   1 
ATOM   18870 O  O   . GLY D  1  541 ? 23.997  109.110 51.730  1.00 82.77  ?  541 GLY D O   1 
ATOM   18871 N  N   . ILE D  1  542 ? 24.887  110.226 53.478  1.00 79.30  ?  542 ILE D N   1 
ATOM   18872 C  CA  . ILE D  1  542 ? 26.272  110.115 53.027  1.00 82.16  ?  542 ILE D CA  1 
ATOM   18873 C  C   . ILE D  1  542 ? 27.132  109.446 54.103  1.00 92.84  ?  542 ILE D C   1 
ATOM   18874 O  O   . ILE D  1  542 ? 27.246  109.969 55.211  1.00 87.98  ?  542 ILE D O   1 
ATOM   18875 C  CB  . ILE D  1  542 ? 26.841  111.510 52.660  1.00 78.72  ?  542 ILE D CB  1 
ATOM   18876 C  CG1 . ILE D  1  542 ? 25.953  112.223 51.623  1.00 74.39  ?  542 ILE D CG1 1 
ATOM   18877 C  CG2 . ILE D  1  542 ? 28.275  111.371 52.136  1.00 83.81  ?  542 ILE D CG2 1 
ATOM   18878 C  CD1 . ILE D  1  542 ? 26.157  113.715 51.522  1.00 76.27  ?  542 ILE D CD1 1 
ATOM   18879 N  N   . TRP D  1  543 ? 27.740  108.299 53.768  1.00 93.19  ?  543 TRP D N   1 
ATOM   18880 C  CA  . TRP D  1  543 ? 28.621  107.555 54.668  1.00 87.88  ?  543 TRP D CA  1 
ATOM   18881 C  C   . TRP D  1  543 ? 29.885  107.226 53.902  1.00 93.27  ?  543 TRP D C   1 
ATOM   18882 O  O   . TRP D  1  543 ? 29.802  106.772 52.762  1.00 96.22  ?  543 TRP D O   1 
ATOM   18883 C  CB  . TRP D  1  543 ? 27.965  106.257 55.143  1.00 86.28  ?  543 TRP D CB  1 
ATOM   18884 C  CG  . TRP D  1  543 ? 26.823  106.466 56.079  1.00 87.28  ?  543 TRP D CG  1 
ATOM   18885 C  CD1 . TRP D  1  543 ? 26.877  106.529 57.438  1.00 86.68  ?  543 TRP D CD1 1 
ATOM   18886 C  CD2 . TRP D  1  543 ? 25.447  106.631 55.721  1.00 77.69  ?  543 TRP D CD2 1 
ATOM   18887 N  NE1 . TRP D  1  543 ? 25.616  106.723 57.950  1.00 102.05 ?  543 TRP D NE1 1 
ATOM   18888 C  CE2 . TRP D  1  543 ? 24.720  106.790 56.915  1.00 86.45  ?  543 TRP D CE2 1 
ATOM   18889 C  CE3 . TRP D  1  543 ? 24.757  106.664 54.506  1.00 74.28  ?  543 TRP D CE3 1 
ATOM   18890 C  CZ2 . TRP D  1  543 ? 23.341  106.982 56.927  1.00 90.95  ?  543 TRP D CZ2 1 
ATOM   18891 C  CZ3 . TRP D  1  543 ? 23.390  106.844 54.522  1.00 78.86  ?  543 TRP D CZ3 1 
ATOM   18892 C  CH2 . TRP D  1  543 ? 22.699  107.013 55.720  1.00 79.54  ?  543 TRP D CH2 1 
ATOM   18893 N  N   . GLU D  1  544 ? 31.053  107.434 54.513  1.00 93.19  ?  544 GLU D N   1 
ATOM   18894 C  CA  . GLU D  1  544 ? 32.320  107.163 53.838  1.00 98.73  ?  544 GLU D CA  1 
ATOM   18895 C  C   . GLU D  1  544 ? 32.455  105.690 53.468  1.00 95.42  ?  544 GLU D C   1 
ATOM   18896 O  O   . GLU D  1  544 ? 32.899  105.390 52.364  1.00 107.41 ?  544 GLU D O   1 
ATOM   18897 C  CB  . GLU D  1  544 ? 33.517  107.609 54.690  1.00 98.61  ?  544 GLU D CB  1 
ATOM   18898 C  CG  . GLU D  1  544 ? 33.523  109.095 55.011  1.00 105.22 ?  544 GLU D CG  1 
ATOM   18899 C  CD  . GLU D  1  544 ? 34.675  109.554 55.883  1.00 134.71 ?  544 GLU D CD  1 
ATOM   18900 O  OE1 . GLU D  1  544 ? 35.506  108.703 56.277  1.00 136.74 ?  544 GLU D OE1 1 
ATOM   18901 O  OE2 . GLU D  1  544 ? 34.744  110.770 56.177  1.00 148.54 ?  544 GLU D OE2 1 
ATOM   18902 N  N   . LYS D  1  545 ? 32.074  104.773 54.369  1.00 93.54  ?  545 LYS D N   1 
ATOM   18903 C  CA  . LYS D  1  545 ? 32.175  103.344 54.080  1.00 100.03 ?  545 LYS D CA  1 
ATOM   18904 C  C   . LYS D  1  545 ? 31.253  102.954 52.922  1.00 99.35  ?  545 LYS D C   1 
ATOM   18905 O  O   . LYS D  1  545 ? 31.622  102.099 52.116  1.00 100.15 ?  545 LYS D O   1 
ATOM   18906 C  CB  . LYS D  1  545 ? 31.879  102.504 55.336  1.00 95.77  ?  545 LYS D CB  1 
ATOM   18907 C  CG  . LYS D  1  545 ? 31.982  100.991 55.119  1.00 98.39  ?  545 LYS D CG  1 
ATOM   18908 C  CD  . LYS D  1  545 ? 33.430  100.478 55.096  1.00 109.36 ?  545 LYS D CD  1 
ATOM   18909 C  CE  . LYS D  1  545 ? 33.590  99.172  54.342  1.00 121.37 ?  545 LYS D CE  1 
ATOM   18910 N  NZ  . LYS D  1  545 ? 34.846  99.141  53.543  1.00 129.30 ?  545 LYS D NZ  1 
ATOM   18911 N  N   . VAL D  1  546 ? 30.070  103.585 52.821  1.00 93.41  ?  546 VAL D N   1 
ATOM   18912 C  CA  . VAL D  1  546 ? 29.136  103.298 51.729  1.00 99.49  ?  546 VAL D CA  1 
ATOM   18913 C  C   . VAL D  1  546 ? 29.776  103.773 50.421  1.00 86.73  ?  546 VAL D C   1 
ATOM   18914 O  O   . VAL D  1  546 ? 29.837  103.020 49.454  1.00 91.32  ?  546 VAL D O   1 
ATOM   18915 C  CB  . VAL D  1  546 ? 27.755  103.965 51.959  1.00 86.94  ?  546 VAL D CB  1 
ATOM   18916 C  CG1 . VAL D  1  546 ? 26.891  103.892 50.704  1.00 88.45  ?  546 VAL D CG1 1 
ATOM   18917 C  CG2 . VAL D  1  546 ? 27.031  103.330 53.145  1.00 87.62  ?  546 VAL D CG2 1 
ATOM   18918 N  N   . ASN D  1  547 ? 30.281  105.013 50.416  1.00 85.38  ?  547 ASN D N   1 
ATOM   18919 C  CA  . ASN D  1  547 ? 30.945  105.577 49.208  1.00 86.08  ?  547 ASN D CA  1 
ATOM   18920 C  C   . ASN D  1  547 ? 32.121  104.682 48.801  1.00 87.39  ?  547 ASN D C   1 
ATOM   18921 O  O   . ASN D  1  547 ? 32.336  104.522 47.586  1.00 88.32  ?  547 ASN D O   1 
ATOM   18922 C  CB  . ASN D  1  547 ? 31.427  107.015 49.439  1.00 77.08  ?  547 ASN D CB  1 
ATOM   18923 C  CG  . ASN D  1  547 ? 30.330  108.062 49.407  1.00 82.44  ?  547 ASN D CG  1 
ATOM   18924 O  OD1 . ASN D  1  547 ? 29.150  107.729 49.483  1.00 92.52  ?  547 ASN D OD1 1 
ATOM   18925 N  ND2 . ASN D  1  547 ? 30.707  109.330 49.307  1.00 88.61  ?  547 ASN D ND2 1 
ATOM   18926 N  N   . GLU D  1  548 ? 32.850  104.122 49.771  1.00 84.32  ?  548 GLU D N   1 
ATOM   18927 C  CA  . GLU D  1  548 ? 34.024  103.301 49.493  1.00 77.41  ?  548 GLU D CA  1 
ATOM   18928 C  C   . GLU D  1  548 ? 33.633  101.956 48.895  1.00 83.68  ?  548 GLU D C   1 
ATOM   18929 O  O   . GLU D  1  548 ? 34.273  101.512 47.943  1.00 93.55  ?  548 GLU D O   1 
ATOM   18930 C  CB  . GLU D  1  548 ? 34.847  103.075 50.771  1.00 92.63  ?  548 GLU D CB  1 
ATOM   18931 C  CG  . GLU D  1  548 ? 35.619  104.296 51.238  1.00 108.22 ?  548 GLU D CG  1 
ATOM   18932 C  CD  . GLU D  1  548 ? 36.072  104.214 52.682  1.00 127.03 ?  548 GLU D CD  1 
ATOM   18933 O  OE1 . GLU D  1  548 ? 36.512  103.120 53.106  1.00 127.04 ?  548 GLU D OE1 1 
ATOM   18934 O  OE2 . GLU D  1  548 ? 35.985  105.243 53.393  1.00 123.66 ?  548 GLU D OE2 1 
ATOM   18935 N  N   . THR D  1  549 ? 32.604  101.294 49.444  1.00 81.38  ?  549 THR D N   1 
ATOM   18936 C  CA  . THR D  1  549 ? 32.172  99.997  48.917  1.00 77.68  ?  549 THR D CA  1 
ATOM   18937 C  C   . THR D  1  549 ? 31.610  100.165 47.502  1.00 80.66  ?  549 THR D C   1 
ATOM   18938 O  O   . THR D  1  549 ? 31.797  99.287  46.660  1.00 76.87  ?  549 THR D O   1 
ATOM   18939 C  CB  . THR D  1  549 ? 31.160  99.328  49.857  1.00 81.27  ?  549 THR D CB  1 
ATOM   18940 O  OG1 . THR D  1  549 ? 31.621  99.435  51.208  1.00 100.58 ?  549 THR D OG1 1 
ATOM   18941 C  CG2 . THR D  1  549 ? 30.935  97.858  49.515  1.00 76.95  ?  549 THR D CG2 1 
ATOM   18942 N  N   . VAL D  1  550 ? 30.938  101.297 47.234  1.00 86.97  ?  550 VAL D N   1 
ATOM   18943 C  CA  . VAL D  1  550 ? 30.391  101.579 45.909  1.00 86.05  ?  550 VAL D CA  1 
ATOM   18944 C  C   . VAL D  1  550 ? 31.562  101.789 44.938  1.00 88.44  ?  550 VAL D C   1 
ATOM   18945 O  O   . VAL D  1  550 ? 31.537  101.254 43.835  1.00 86.62  ?  550 VAL D O   1 
ATOM   18946 C  CB  . VAL D  1  550 ? 29.428  102.795 45.943  1.00 63.86  ?  550 VAL D CB  1 
ATOM   18947 C  CG1 . VAL D  1  550 ? 29.134  103.308 44.538  1.00 67.79  ?  550 VAL D CG1 1 
ATOM   18948 C  CG2 . VAL D  1  550 ? 28.129  102.440 46.659  1.00 72.06  ?  550 VAL D CG2 1 
ATOM   18949 N  N   . SER D  1  551 ? 32.594  102.540 45.345  1.00 80.98  ?  551 SER D N   1 
ATOM   18950 C  CA  . SER D  1  551 ? 33.762  102.770 44.492  1.00 83.57  ?  551 SER D CA  1 
ATOM   18951 C  C   . SER D  1  551 ? 34.496  101.458 44.205  1.00 89.38  ?  551 SER D C   1 
ATOM   18952 O  O   . SER D  1  551 ? 35.042  101.286 43.117  1.00 91.03  ?  551 SER D O   1 
ATOM   18953 C  CB  . SER D  1  551 ? 34.722  103.752 45.155  1.00 81.46  ?  551 SER D CB  1 
ATOM   18954 O  OG  . SER D  1  551 ? 34.036  104.890 45.651  1.00 105.91 ?  551 SER D OG  1 
ATOM   18955 N  N   . LYS D  1  552 ? 34.515  100.537 45.176  1.00 87.57  ?  552 LYS D N   1 
ATOM   18956 C  CA  . LYS D  1  552 ? 35.178  99.249  45.012  1.00 82.48  ?  552 LYS D CA  1 
ATOM   18957 C  C   . LYS D  1  552 ? 34.415  98.353  44.027  1.00 77.02  ?  552 LYS D C   1 
ATOM   18958 O  O   . LYS D  1  552 ? 35.016  97.835  43.087  1.00 87.33  ?  552 LYS D O   1 
ATOM   18959 C  CB  . LYS D  1  552 ? 35.321  98.550  46.378  1.00 84.12  ?  552 LYS D CB  1 
ATOM   18960 C  CG  . LYS D  1  552 ? 35.907  97.146  46.289  1.00 86.10  ?  552 LYS D CG  1 
ATOM   18961 C  CD  . LYS D  1  552 ? 36.157  96.534  47.655  1.00 99.34  ?  552 LYS D CD  1 
ATOM   18962 C  CE  . LYS D  1  552 ? 37.034  95.307  47.556  1.00 131.94 ?  552 LYS D CE  1 
ATOM   18963 N  NZ  . LYS D  1  552 ? 37.343  94.728  48.892  1.00 142.15 ?  552 LYS D NZ  1 
ATOM   18964 N  N   . ILE D  1  553 ? 33.102  98.170  44.239  1.00 74.55  ?  553 ILE D N   1 
ATOM   18965 C  CA  . ILE D  1  553 ? 32.292  97.309  43.377  1.00 82.49  ?  553 ILE D CA  1 
ATOM   18966 C  C   . ILE D  1  553 ? 32.111  97.919  41.979  1.00 84.24  ?  553 ILE D C   1 
ATOM   18967 O  O   . ILE D  1  553 ? 32.149  97.188  40.991  1.00 85.72  ?  553 ILE D O   1 
ATOM   18968 C  CB  . ILE D  1  553 ? 30.939  96.958  44.055  1.00 73.69  ?  553 ILE D CB  1 
ATOM   18969 C  CG1 . ILE D  1  553 ? 31.173  96.229  45.396  1.00 66.92  ?  553 ILE D CG1 1 
ATOM   18970 C  CG2 . ILE D  1  553 ? 30.080  96.091  43.126  1.00 81.39  ?  553 ILE D CG2 1 
ATOM   18971 C  CD1 . ILE D  1  553 ? 29.970  96.160  46.298  1.00 70.91  ?  553 ILE D CD1 1 
ATOM   18972 N  N   . SER D  1  554 ? 31.934  99.246  41.884  1.00 81.16  ?  554 SER D N   1 
ATOM   18973 C  CA  . SER D  1  554 ? 31.776  99.912  40.587  1.00 78.68  ?  554 SER D CA  1 
ATOM   18974 C  C   . SER D  1  554 ? 33.076  99.960  39.790  1.00 91.67  ?  554 SER D C   1 
ATOM   18975 O  O   . SER D  1  554 ? 33.057  100.434 38.657  1.00 99.36  ?  554 SER D O   1 
ATOM   18976 C  CB  . SER D  1  554 ? 31.322  101.356 40.772  1.00 71.68  ?  554 SER D CB  1 
ATOM   18977 O  OG  . SER D  1  554 ? 30.303  101.494 41.747  1.00 112.15 ?  554 SER D OG  1 
ATOM   18978 N  N   . GLN D  1  555 ? 34.204  99.520  40.373  1.00 93.94  ?  555 GLN D N   1 
ATOM   18979 C  CA  . GLN D  1  555 ? 35.505  99.574  39.715  1.00 93.65  ?  555 GLN D CA  1 
ATOM   18980 C  C   . GLN D  1  555 ? 35.875  101.034 39.425  1.00 96.49  ?  555 GLN D C   1 
ATOM   18981 O  O   . GLN D  1  555 ? 36.429  101.338 38.368  1.00 100.72 ?  555 GLN D O   1 
ATOM   18982 C  CB  . GLN D  1  555 ? 35.527  98.722  38.434  1.00 103.20 ?  555 GLN D CB  1 
ATOM   18983 C  CG  . GLN D  1  555 ? 35.329  97.232  38.693  1.00 98.05  ?  555 GLN D CG  1 
ATOM   18984 C  CD  . GLN D  1  555 ? 36.464  96.630  39.491  1.00 117.35 ?  555 GLN D CD  1 
ATOM   18985 O  OE1 . GLN D  1  555 ? 37.621  97.059  39.403  1.00 119.96 ?  555 GLN D OE1 1 
ATOM   18986 N  NE2 . GLN D  1  555 ? 36.162  95.615  40.290  1.00 118.40 ?  555 GLN D NE2 1 
ATOM   18987 N  N   . GLY D  1  556 ? 35.555  101.918 40.372  1.00 87.14  ?  556 GLY D N   1 
ATOM   18988 C  CA  . GLY D  1  556 ? 35.846  103.341 40.279  1.00 82.14  ?  556 GLY D CA  1 
ATOM   18989 C  C   . GLY D  1  556 ? 34.910  104.173 39.427  1.00 76.91  ?  556 GLY D C   1 
ATOM   18990 O  O   . GLY D  1  556 ? 35.164  105.366 39.252  1.00 90.50  ?  556 GLY D O   1 
ATOM   18991 N  N   . ALA D  1  557 ? 33.828  103.584 38.888  1.00 77.35  ?  557 ALA D N   1 
ATOM   18992 C  CA  . ALA D  1  557 ? 32.901  104.343 38.043  1.00 69.85  ?  557 ALA D CA  1 
ATOM   18993 C  C   . ALA D  1  557 ? 32.062  105.317 38.867  1.00 77.97  ?  557 ALA D C   1 
ATOM   18994 O  O   . ALA D  1  557 ? 31.878  106.466 38.462  1.00 86.88  ?  557 ALA D O   1 
ATOM   18995 C  CB  . ALA D  1  557 ? 32.002  103.400 37.259  1.00 76.41  ?  557 ALA D CB  1 
ATOM   18996 N  N   . VAL D  1  558 ? 31.559  104.863 40.022  1.00 84.70  ?  558 VAL D N   1 
ATOM   18997 C  CA  . VAL D  1  558 ? 30.754  105.690 40.915  1.00 84.52  ?  558 VAL D CA  1 
ATOM   18998 C  C   . VAL D  1  558 ? 31.538  105.866 42.214  1.00 86.55  ?  558 VAL D C   1 
ATOM   18999 O  O   . VAL D  1  558 ? 31.898  104.870 42.838  1.00 90.61  ?  558 VAL D O   1 
ATOM   19000 C  CB  . VAL D  1  558 ? 29.381  105.036 41.175  1.00 65.54  ?  558 VAL D CB  1 
ATOM   19001 C  CG1 . VAL D  1  558 ? 28.509  105.937 42.035  1.00 67.94  ?  558 VAL D CG1 1 
ATOM   19002 C  CG2 . VAL D  1  558 ? 28.678  104.698 39.864  1.00 71.56  ?  558 VAL D CG2 1 
ATOM   19003 N  N   . THR D  1  559 ? 31.818  107.118 42.613  1.00 89.54  ?  559 THR D N   1 
ATOM   19004 C  CA  . THR D  1  559 ? 32.582  107.383 43.834  1.00 98.03  ?  559 THR D CA  1 
ATOM   19005 C  C   . THR D  1  559 ? 31.717  108.015 44.944  1.00 97.86  ?  559 THR D C   1 
ATOM   19006 O  O   . THR D  1  559 ? 31.670  107.486 46.054  1.00 101.35 ?  559 THR D O   1 
ATOM   19007 C  CB  . THR D  1  559 ? 33.828  108.232 43.515  1.00 79.64  ?  559 THR D CB  1 
ATOM   19008 O  OG1 . THR D  1  559 ? 33.428  109.497 42.987  1.00 101.68 ?  559 THR D OG1 1 
ATOM   19009 C  CG2 . THR D  1  559 ? 34.766  107.540 42.543  1.00 72.36  ?  559 THR D CG2 1 
ATOM   19010 N  N   . SER D  1  560 ? 31.041  109.137 44.652  1.00 96.87  ?  560 SER D N   1 
ATOM   19011 C  CA  . SER D  1  560 ? 30.201  109.817 45.640  1.00 90.81  ?  560 SER D CA  1 
ATOM   19012 C  C   . SER D  1  560 ? 28.733  109.459 45.446  1.00 86.91  ?  560 SER D C   1 
ATOM   19013 O  O   . SER D  1  560 ? 28.245  109.477 44.319  1.00 93.60  ?  560 SER D O   1 
ATOM   19014 C  CB  . SER D  1  560 ? 30.381  111.328 45.543  1.00 94.00  ?  560 SER D CB  1 
ATOM   19015 O  OG  . SER D  1  560 ? 30.215  111.783 44.210  1.00 128.45 ?  560 SER D OG  1 
ATOM   19016 N  N   . VAL D  1  561 ? 28.051  109.164 46.565  1.00 81.99  ?  561 VAL D N   1 
ATOM   19017 C  CA  . VAL D  1  561 ? 26.630  108.708 46.509  1.00 80.71  ?  561 VAL D CA  1 
ATOM   19018 C  C   . VAL D  1  561 ? 25.816  109.286 47.673  1.00 84.65  ?  561 VAL D C   1 
ATOM   19019 O  O   . VAL D  1  561 ? 26.418  109.544 48.731  1.00 84.96  ?  561 VAL D O   1 
ATOM   19020 C  CB  . VAL D  1  561 ? 26.572  107.167 46.532  1.00 65.02  ?  561 VAL D CB  1 
ATOM   19021 C  CG1 . VAL D  1  561 ? 25.229  106.646 47.016  1.00 89.96  ?  561 VAL D CG1 1 
ATOM   19022 C  CG2 . VAL D  1  561 ? 26.937  106.548 45.193  1.00 73.70  ?  561 VAL D CG2 1 
ATOM   19023 N  N   . THR D  1  562 ? 24.506  109.479 47.490  1.00 68.36  ?  562 THR D N   1 
ATOM   19024 C  CA  . THR D  1  562 ? 23.574  109.948 48.510  1.00 66.04  ?  562 THR D CA  1 
ATOM   19025 C  C   . THR D  1  562 ? 22.433  108.938 48.482  1.00 78.69  ?  562 THR D C   1 
ATOM   19026 O  O   . THR D  1  562 ? 21.815  108.752 47.435  1.00 90.46  ?  562 THR D O   1 
ATOM   19027 C  CB  . THR D  1  562 ? 23.083  111.378 48.220  1.00 73.48  ?  562 THR D CB  1 
ATOM   19028 O  OG1 . THR D  1  562 ? 22.579  111.443 46.884  1.00 99.12  ?  562 THR D OG1 1 
ATOM   19029 C  CG2 . THR D  1  562 ? 24.170  112.421 48.437  1.00 77.87  ?  562 THR D CG2 1 
ATOM   19030 N  N   . LEU D  1  563 ? 22.172  108.258 49.605  1.00 83.26  ?  563 LEU D N   1 
ATOM   19031 C  CA  . LEU D  1  563 ? 21.109  107.255 49.646  1.00 83.39  ?  563 LEU D CA  1 
ATOM   19032 C  C   . LEU D  1  563 ? 19.707  107.863 49.700  1.00 77.80  ?  563 LEU D C   1 
ATOM   19033 O  O   . LEU D  1  563 ? 18.748  107.154 49.401  1.00 85.65  ?  563 LEU D O   1 
ATOM   19034 C  CB  . LEU D  1  563 ? 21.293  106.297 50.841  1.00 78.26  ?  563 LEU D CB  1 
ATOM   19035 C  CG  . LEU D  1  563 ? 22.617  105.530 50.945  1.00 65.00  ?  563 LEU D CG  1 
ATOM   19036 C  CD1 . LEU D  1  563 ? 22.531  104.470 52.018  1.00 66.51  ?  563 LEU D CD1 1 
ATOM   19037 C  CD2 . LEU D  1  563 ? 23.006  104.871 49.622  1.00 69.05  ?  563 LEU D CD2 1 
ATOM   19038 N  N   . TYR D  1  564 ? 19.566  109.145 50.085  1.00 64.12  ?  564 TYR D N   1 
ATOM   19039 C  CA  . TYR D  1  564 ? 18.240  109.757 50.188  1.00 69.33  ?  564 TYR D CA  1 
ATOM   19040 C  C   . TYR D  1  564 ? 18.060  111.011 49.320  1.00 75.22  ?  564 TYR D C   1 
ATOM   19041 O  O   . TYR D  1  564 ? 17.319  111.914 49.710  1.00 80.45  ?  564 TYR D O   1 
ATOM   19042 C  CB  . TYR D  1  564 ? 17.923  110.094 51.659  1.00 86.66  ?  564 TYR D CB  1 
ATOM   19043 C  CG  . TYR D  1  564 ? 18.358  109.054 52.672  1.00 85.39  ?  564 TYR D CG  1 
ATOM   19044 C  CD1 . TYR D  1  564 ? 18.065  107.710 52.491  1.00 84.62  ?  564 TYR D CD1 1 
ATOM   19045 C  CD2 . TYR D  1  564 ? 19.012  109.422 53.838  1.00 84.34  ?  564 TYR D CD2 1 
ATOM   19046 C  CE1 . TYR D  1  564 ? 18.451  106.755 53.420  1.00 85.86  ?  564 TYR D CE1 1 
ATOM   19047 C  CE2 . TYR D  1  564 ? 19.402  108.476 54.777  1.00 91.44  ?  564 TYR D CE2 1 
ATOM   19048 C  CZ  . TYR D  1  564 ? 19.116  107.142 54.567  1.00 90.99  ?  564 TYR D CZ  1 
ATOM   19049 O  OH  . TYR D  1  564 ? 19.491  106.204 55.500  1.00 74.30  ?  564 TYR D OH  1 
ATOM   19050 N  N   . SER D  1  565 ? 18.700  111.069 48.144  1.00 75.51  ?  565 SER D N   1 
ATOM   19051 C  CA  . SER D  1  565 ? 18.566  112.232 47.264  1.00 63.21  ?  565 SER D CA  1 
ATOM   19052 C  C   . SER D  1  565 ? 18.606  111.835 45.792  1.00 74.05  ?  565 SER D C   1 
ATOM   19053 O  O   . SER D  1  565 ? 19.297  110.885 45.420  1.00 82.28  ?  565 SER D O   1 
ATOM   19054 C  CB  . SER D  1  565 ? 19.664  113.247 47.561  1.00 76.55  ?  565 SER D CB  1 
ATOM   19055 O  OG  . SER D  1  565 ? 19.758  114.260 46.571  1.00 65.19  ?  565 SER D OG  1 
ATOM   19056 N  N   . ILE D  1  566 ? 17.866  112.577 44.955  1.00 70.39  ?  566 ILE D N   1 
ATOM   19057 C  CA  . ILE D  1  566 ? 17.822  112.333 43.512  1.00 75.06  ?  566 ILE D CA  1 
ATOM   19058 C  C   . ILE D  1  566 ? 18.624  113.380 42.728  1.00 71.80  ?  566 ILE D C   1 
ATOM   19059 O  O   . ILE D  1  566 ? 18.845  113.177 41.539  1.00 81.88  ?  566 ILE D O   1 
ATOM   19060 C  CB  . ILE D  1  566 ? 16.371  112.224 42.987  1.00 61.58  ?  566 ILE D CB  1 
ATOM   19061 C  CG1 . ILE D  1  566 ? 15.662  113.588 43.004  1.00 74.79  ?  566 ILE D CG1 1 
ATOM   19062 C  CG2 . ILE D  1  566 ? 15.601  111.195 43.796  1.00 77.98  ?  566 ILE D CG2 1 
ATOM   19063 C  CD1 . ILE D  1  566 ? 14.319  113.601 42.346  1.00 95.20  ?  566 ILE D CD1 1 
ATOM   19064 N  N   . LEU D  1  567 ? 19.051  114.486 43.371  1.00 66.27  ?  567 LEU D N   1 
ATOM   19065 C  CA  . LEU D  1  567 ? 19.816  115.535 42.701  1.00 67.66  ?  567 LEU D CA  1 
ATOM   19066 C  C   . LEU D  1  567 ? 21.316  115.464 43.022  1.00 88.67  ?  567 LEU D C   1 
ATOM   19067 O  O   . LEU D  1  567 ? 22.135  115.411 42.103  1.00 82.76  ?  567 LEU D O   1 
ATOM   19068 C  CB  . LEU D  1  567 ? 19.283  116.916 43.102  1.00 66.17  ?  567 LEU D CB  1 
ATOM   19069 C  CG  . LEU D  1  567 ? 17.894  117.276 42.596  1.00 75.89  ?  567 LEU D CG  1 
ATOM   19070 C  CD1 . LEU D  1  567 ? 17.330  118.439 43.373  1.00 89.61  ?  567 LEU D CD1 1 
ATOM   19071 C  CD2 . LEU D  1  567 ? 17.917  117.608 41.116  1.00 79.35  ?  567 LEU D CD2 1 
ATOM   19072 N  N   . GLN D  1  568 ? 21.682  115.487 44.317  1.00 88.01  ?  568 GLN D N   1 
ATOM   19073 C  CA  . GLN D  1  568 ? 23.090  115.451 44.706  1.00 94.03  ?  568 GLN D CA  1 
ATOM   19074 C  C   . GLN D  1  568 ? 23.633  114.035 44.648  1.00 90.23  ?  568 GLN D C   1 
ATOM   19075 O  O   . GLN D  1  568 ? 23.164  113.182 45.397  1.00 87.67  ?  568 GLN D O   1 
ATOM   19076 C  CB  . GLN D  1  568 ? 23.278  116.022 46.123  1.00 95.84  ?  568 GLN D CB  1 
ATOM   19077 C  CG  . GLN D  1  568 ? 24.735  115.989 46.598  1.00 103.53 ?  568 GLN D CG  1 
ATOM   19078 C  CD  . GLN D  1  568 ? 24.955  116.750 47.879  1.00 101.76 ?  568 GLN D CD  1 
ATOM   19079 O  OE1 . GLN D  1  568 ? 24.247  117.715 48.187  1.00 121.23 ?  568 GLN D OE1 1 
ATOM   19080 N  NE2 . GLN D  1  568 ? 25.950  116.335 48.656  1.00 111.16 ?  568 GLN D NE2 1 
ATOM   19081 N  N   . ASP D  1  569 ? 24.620  113.777 43.757  1.00 85.18  ?  569 ASP D N   1 
ATOM   19082 C  CA  . ASP D  1  569 ? 25.272  112.466 43.582  1.00 67.20  ?  569 ASP D CA  1 
ATOM   19083 C  C   . ASP D  1  569 ? 24.310  111.292 43.828  1.00 78.27  ?  569 ASP D C   1 
ATOM   19084 O  O   . ASP D  1  569 ? 24.503  110.517 44.763  1.00 80.71  ?  569 ASP D O   1 
ATOM   19085 C  CB  . ASP D  1  569 ? 26.488  112.371 44.515  1.00 67.50  ?  569 ASP D CB  1 
ATOM   19086 C  CG  . ASP D  1  569 ? 27.389  113.582 44.431  1.00 98.52  ?  569 ASP D CG  1 
ATOM   19087 O  OD1 . ASP D  1  569 ? 27.814  113.928 43.308  1.00 93.39  ?  569 ASP D OD1 1 
ATOM   19088 O  OD2 . ASP D  1  569 ? 27.666  114.190 45.489  1.00 111.18 ?  569 ASP D OD2 1 
ATOM   19089 N  N   . PRO D  1  570 ? 23.234  111.170 43.035  1.00 78.29  ?  570 PRO D N   1 
ATOM   19090 C  CA  . PRO D  1  570 ? 22.269  110.097 43.291  1.00 73.92  ?  570 PRO D CA  1 
ATOM   19091 C  C   . PRO D  1  570 ? 22.793  108.694 43.071  1.00 77.63  ?  570 PRO D C   1 
ATOM   19092 O  O   . PRO D  1  570 ? 23.792  108.486 42.391  1.00 79.86  ?  570 PRO D O   1 
ATOM   19093 C  CB  . PRO D  1  570 ? 21.140  110.415 42.313  1.00 77.69  ?  570 PRO D CB  1 
ATOM   19094 C  CG  . PRO D  1  570 ? 21.813  111.103 41.202  1.00 79.76  ?  570 PRO D CG  1 
ATOM   19095 C  CD  . PRO D  1  570 ? 22.812  111.990 41.883  1.00 65.15  ?  570 PRO D CD  1 
ATOM   19096 N  N   . MET D  1  571 ? 22.094  107.727 43.649  1.00 83.91  ?  571 MET D N   1 
ATOM   19097 C  CA  . MET D  1  571 ? 22.438  106.320 43.509  1.00 85.75  ?  571 MET D CA  1 
ATOM   19098 C  C   . MET D  1  571 ? 22.120  105.873 42.077  1.00 90.11  ?  571 MET D C   1 
ATOM   19099 O  O   . MET D  1  571 ? 21.175  106.383 41.474  1.00 103.13 ?  571 MET D O   1 
ATOM   19100 C  CB  . MET D  1  571 ? 21.604  105.490 44.499  1.00 97.86  ?  571 MET D CB  1 
ATOM   19101 C  CG  . MET D  1  571 ? 22.314  105.187 45.793  1.00 89.13  ?  571 MET D CG  1 
ATOM   19102 S  SD  . MET D  1  571 ? 23.470  103.824 45.589  1.00 110.01 ?  571 MET D SD  1 
ATOM   19103 C  CE  . MET D  1  571 ? 22.345  102.436 45.659  1.00 99.16  ?  571 MET D CE  1 
ATOM   19104 N  N   . THR D  1  572 ? 22.895  104.927 41.529  1.00 83.14  ?  572 THR D N   1 
ATOM   19105 C  CA  . THR D  1  572 ? 22.655  104.449 40.166  1.00 74.32  ?  572 THR D CA  1 
ATOM   19106 C  C   . THR D  1  572 ? 21.472  103.481 40.114  1.00 72.65  ?  572 THR D C   1 
ATOM   19107 O  O   . THR D  1  572 ? 21.145  102.849 41.117  1.00 76.57  ?  572 THR D O   1 
ATOM   19108 C  CB  . THR D  1  572 ? 23.919  103.793 39.593  1.00 69.99  ?  572 THR D CB  1 
ATOM   19109 O  OG1 . THR D  1  572 ? 24.383  102.769 40.479  1.00 82.19  ?  572 THR D OG1 1 
ATOM   19110 C  CG2 . THR D  1  572 ? 25.024  104.792 39.333  1.00 58.75  ?  572 THR D CG2 1 
ATOM   19111 N  N   . SER D  1  573 ? 20.827  103.372 38.946  1.00 79.01  ?  573 SER D N   1 
ATOM   19112 C  CA  . SER D  1  573 ? 19.695  102.459 38.759  1.00 74.83  ?  573 SER D CA  1 
ATOM   19113 C  C   . SER D  1  573 ? 20.032  101.493 37.619  1.00 84.04  ?  573 SER D C   1 
ATOM   19114 O  O   . SER D  1  573 ? 20.666  101.897 36.645  1.00 78.57  ?  573 SER D O   1 
ATOM   19115 C  CB  . SER D  1  573 ? 18.396  103.214 38.464  1.00 75.42  ?  573 SER D CB  1 
ATOM   19116 O  OG  . SER D  1  573 ? 17.940  104.027 39.533  1.00 80.47  ?  573 SER D OG  1 
ATOM   19117 N  N   . CYS D  1  574 ? 19.634  100.218 37.746  1.00 70.24  ?  574 CYS D N   1 
ATOM   19118 C  CA  . CYS D  1  574 ? 19.923  99.209  36.729  1.00 60.81  ?  574 CYS D CA  1 
ATOM   19119 C  C   . CYS D  1  574 ? 18.834  99.174  35.639  1.00 65.63  ?  574 CYS D C   1 
ATOM   19120 O  O   . CYS D  1  574 ? 18.914  99.961  34.699  1.00 80.67  ?  574 CYS D O   1 
ATOM   19121 C  CB  . CYS D  1  574 ? 20.138  97.841  37.370  1.00 50.31  ?  574 CYS D CB  1 
ATOM   19122 S  SG  . CYS D  1  574 ? 18.856  97.379  38.561  1.00 71.47  ?  574 CYS D SG  1 
ATOM   19123 N  N   . GLY D  1  575 ? 17.853  98.279  35.740  1.00 49.63  ?  575 GLY D N   1 
ATOM   19124 C  CA  . GLY D  1  575 ? 16.807  98.190  34.729  1.00 61.31  ?  575 GLY D CA  1 
ATOM   19125 C  C   . GLY D  1  575 ? 15.612  97.343  35.107  1.00 67.97  ?  575 GLY D C   1 
ATOM   19126 O  O   . GLY D  1  575 ? 14.682  97.202  34.312  1.00 77.23  ?  575 GLY D O   1 
ATOM   19127 N  N   . CYS D  1  576 ? 15.617  96.774  36.314  1.00 57.31  ?  576 CYS D N   1 
ATOM   19128 C  CA  . CYS D  1  576 ? 14.519  95.937  36.797  1.00 50.82  ?  576 CYS D CA  1 
ATOM   19129 C  C   . CYS D  1  576 ? 13.490  96.731  37.603  1.00 66.68  ?  576 CYS D C   1 
ATOM   19130 O  O   . CYS D  1  576 ? 12.389  96.230  37.828  1.00 80.36  ?  576 CYS D O   1 
ATOM   19131 C  CB  . CYS D  1  576 ? 15.069  94.774  37.611  1.00 58.99  ?  576 CYS D CB  1 
ATOM   19132 S  SG  . CYS D  1  576 ? 16.317  95.255  38.830  1.00 76.69  ?  576 CYS D SG  1 
ATOM   19133 N  N   . PHE D  1  577 ? 13.834  97.955  38.051  1.00 62.64  ?  577 PHE D N   1 
ATOM   19134 C  CA  . PHE D  1  577 ? 12.942  98.814  38.837  1.00 60.34  ?  577 PHE D CA  1 
ATOM   19135 C  C   . PHE D  1  577 ? 11.503  98.898  38.347  1.00 64.57  ?  577 PHE D C   1 
ATOM   19136 O  O   . PHE D  1  577 ? 11.259  99.036  37.153  1.00 64.85  ?  577 PHE D O   1 
ATOM   19137 C  CB  . PHE D  1  577 ? 13.464  100.261 38.881  1.00 71.38  ?  577 PHE D CB  1 
ATOM   19138 C  CG  . PHE D  1  577 ? 14.128  100.764 37.621  1.00 66.77  ?  577 PHE D CG  1 
ATOM   19139 C  CD1 . PHE D  1  577 ? 13.375  101.195 36.546  1.00 58.06  ?  577 PHE D CD1 1 
ATOM   19140 C  CD2 . PHE D  1  577 ? 15.507  100.827 37.525  1.00 72.49  ?  577 PHE D CD2 1 
ATOM   19141 C  CE1 . PHE D  1  577 ? 13.987  101.656 35.392  1.00 62.64  ?  577 PHE D CE1 1 
ATOM   19142 C  CE2 . PHE D  1  577 ? 16.116  101.298 36.374  1.00 75.85  ?  577 PHE D CE2 1 
ATOM   19143 C  CZ  . PHE D  1  577 ? 15.353  101.701 35.311  1.00 74.17  ?  577 PHE D CZ  1 
ATOM   19144 N  N   . GLU D  1  578 ? 10.548  98.830  39.276  1.00 74.82  ?  578 GLU D N   1 
ATOM   19145 C  CA  . GLU D  1  578 ? 9.113   98.911  38.893  1.00 83.30  ?  578 GLU D CA  1 
ATOM   19146 C  C   . GLU D  1  578 ? 8.665   100.358 38.678  1.00 80.75  ?  578 GLU D C   1 
ATOM   19147 O  O   . GLU D  1  578 ? 7.796   100.579 37.817  1.00 84.91  ?  578 GLU D O   1 
ATOM   19148 C  CB  . GLU D  1  578 ? 8.251   98.240  39.962  1.00 79.14  ?  578 GLU D CB  1 
ATOM   19149 C  CG  . GLU D  1  578 ? 6.948   97.690  39.410  1.00 95.24  ?  578 GLU D CG  1 
ATOM   19150 C  CD  . GLU D  1  578 ? 5.755   97.782  40.346  1.00 109.33 ?  578 GLU D CD  1 
ATOM   19151 O  OE1 . GLU D  1  578 ? 5.895   97.384  41.518  1.00 110.47 ?  578 GLU D OE1 1 
ATOM   19152 O  OE2 . GLU D  1  578 ? 4.689   98.246  39.897  1.00 96.88  ?  578 GLU D OE2 1 
ATOM   19153 N  N   . CYS D  1  579 ? 9.235   101.297 39.436  1.00 69.72  ?  579 CYS D N   1 
ATOM   19154 C  CA  . CYS D  1  579 ? 8.840   102.693 39.321  1.00 70.76  ?  579 CYS D CA  1 
ATOM   19155 C  C   . CYS D  1  579 ? 10.011  103.593 38.951  1.00 72.57  ?  579 CYS D C   1 
ATOM   19156 O  O   . CYS D  1  579 ? 11.170  103.226 39.132  1.00 73.40  ?  579 CYS D O   1 
ATOM   19157 C  CB  . CYS D  1  579 ? 8.184   103.162 40.616  1.00 72.23  ?  579 CYS D CB  1 
ATOM   19158 S  SG  . CYS D  1  579 ? 6.853   102.087 41.206  1.00 87.72  ?  579 CYS D SG  1 
ATOM   19159 N  N   . ILE D  1  580 ? 9.689   104.786 38.433  1.00 62.76  ?  580 ILE D N   1 
ATOM   19160 C  CA  . ILE D  1  580 ? 10.665  105.806 38.061  1.00 66.85  ?  580 ILE D CA  1 
ATOM   19161 C  C   . ILE D  1  580 ? 10.111  107.144 38.535  1.00 74.44  ?  580 ILE D C   1 
ATOM   19162 O  O   . ILE D  1  580 ? 8.949   107.450 38.268  1.00 73.29  ?  580 ILE D O   1 
ATOM   19163 C  CB  . ILE D  1  580 ? 10.940  105.846 36.537  1.00 66.29  ?  580 ILE D CB  1 
ATOM   19164 C  CG1 . ILE D  1  580 ? 11.597  104.539 36.051  1.00 73.56  ?  580 ILE D CG1 1 
ATOM   19165 C  CG2 . ILE D  1  580 ? 11.825  107.056 36.198  1.00 72.40  ?  580 ILE D CG2 1 
ATOM   19166 C  CD1 . ILE D  1  580 ? 11.471  104.304 34.597  1.00 69.91  ?  580 ILE D CD1 1 
ATOM   19167 N  N   . THR D  1  581 ? 10.930  107.942 39.231  1.00 72.69  ?  581 THR D N   1 
ATOM   19168 C  CA  . THR D  1  581 ? 10.499  109.247 39.725  1.00 76.87  ?  581 THR D CA  1 
ATOM   19169 C  C   . THR D  1  581 ? 11.338  110.358 39.089  1.00 76.28  ?  581 THR D C   1 
ATOM   19170 O  O   . THR D  1  581 ? 12.519  110.499 39.404  1.00 79.47  ?  581 THR D O   1 
ATOM   19171 C  CB  . THR D  1  581 ? 10.566  109.292 41.256  1.00 68.42  ?  581 THR D CB  1 
ATOM   19172 O  OG1 . THR D  1  581 ? 9.880   108.162 41.794  1.00 75.74  ?  581 THR D OG1 1 
ATOM   19173 C  CG2 . THR D  1  581 ? 9.962   110.556 41.810  1.00 65.45  ?  581 THR D CG2 1 
ATOM   19174 N  N   . GLY D  1  582 ? 10.722  111.127 38.196  1.00 73.50  ?  582 GLY D N   1 
ATOM   19175 C  CA  . GLY D  1  582 ? 11.380  112.222 37.494  1.00 78.36  ?  582 GLY D CA  1 
ATOM   19176 C  C   . GLY D  1  582 ? 10.998  113.588 38.020  1.00 76.45  ?  582 GLY D C   1 
ATOM   19177 O  O   . GLY D  1  582 ? 9.876   113.784 38.488  1.00 78.01  ?  582 GLY D O   1 
ATOM   19178 N  N   . ILE D  1  583 ? 11.928  114.538 37.882  1.00 76.60  ?  583 ILE D N   1 
ATOM   19179 C  CA  . ILE D  1  583 ? 11.701  115.919 38.396  1.00 78.56  ?  583 ILE D CA  1 
ATOM   19180 C  C   . ILE D  1  583 ? 10.825  116.706 37.421  1.00 88.00  ?  583 ILE D C   1 
ATOM   19181 O  O   . ILE D  1  583 ? 11.059  116.604 36.203  1.00 99.64  ?  583 ILE D O   1 
ATOM   19182 C  CB  . ILE D  1  583 ? 13.048  116.630 38.637  1.00 69.65  ?  583 ILE D CB  1 
ATOM   19183 C  CG1 . ILE D  1  583 ? 12.867  118.132 38.864  1.00 80.86  ?  583 ILE D CG1 1 
ATOM   19184 C  CG2 . ILE D  1  583 ? 14.014  116.348 37.498  1.00 98.49  ?  583 ILE D CG2 1 
ATOM   19185 C  CD1 . ILE D  1  583 ? 12.054  118.469 40.088  1.00 109.39 ?  583 ILE D CD1 1 
ATOM   19186 N  N   . MET D  1  584 ? 9.858   117.458 37.945  1.00 85.20  ?  584 MET D N   1 
ATOM   19187 C  CA  . MET D  1  584 ? 8.984   118.304 37.141  1.00 85.76  ?  584 MET D CA  1 
ATOM   19188 C  C   . MET D  1  584 ? 9.182   119.733 37.657  1.00 91.42  ?  584 MET D C   1 
ATOM   19189 O  O   . MET D  1  584 ? 8.525   120.132 38.620  1.00 91.25  ?  584 MET D O   1 
ATOM   19190 C  CB  . MET D  1  584 ? 7.519   117.861 37.288  1.00 87.35  ?  584 MET D CB  1 
ATOM   19191 C  CG  . MET D  1  584 ? 6.571   118.570 36.336  1.00 103.06 ?  584 MET D CG  1 
ATOM   19192 S  SD  . MET D  1  584 ? 4.854   118.008 36.480  1.00 105.75 ?  584 MET D SD  1 
ATOM   19193 C  CE  . MET D  1  584 ? 4.007   119.359 35.673  1.00 102.81 ?  584 MET D CE  1 
ATOM   19194 N  N   . PRO D  1  585 ? 10.116  120.508 37.071  1.00 79.17  ?  585 PRO D N   1 
ATOM   19195 C  CA  . PRO D  1  585 ? 10.340  121.877 37.566  1.00 76.30  ?  585 PRO D CA  1 
ATOM   19196 C  C   . PRO D  1  585 ? 9.094   122.755 37.534  1.00 79.27  ?  585 PRO D C   1 
ATOM   19197 O  O   . PRO D  1  585 ? 8.976   123.674 38.339  1.00 83.37  ?  585 PRO D O   1 
ATOM   19198 C  CB  . PRO D  1  585 ? 11.435  122.419 36.640  1.00 77.11  ?  585 PRO D CB  1 
ATOM   19199 C  CG  . PRO D  1  585 ? 12.056  121.231 36.026  1.00 74.18  ?  585 PRO D CG  1 
ATOM   19200 C  CD  . PRO D  1  585 ? 10.995  120.200 35.927  1.00 72.49  ?  585 PRO D CD  1 
ATOM   19201 N  N   . GLU D  1  586 ? 8.166   122.465 36.615  1.00 89.53  ?  586 GLU D N   1 
ATOM   19202 C  CA  . GLU D  1  586 ? 6.932   123.230 36.471  1.00 91.05  ?  586 GLU D CA  1 
ATOM   19203 C  C   . GLU D  1  586 ? 6.099   123.157 37.744  1.00 95.74  ?  586 GLU D C   1 
ATOM   19204 O  O   . GLU D  1  586 ? 5.527   124.164 38.156  1.00 97.45  ?  586 GLU D O   1 
ATOM   19205 C  CB  . GLU D  1  586 ? 6.110   122.706 35.279  1.00 88.72  ?  586 GLU D CB  1 
ATOM   19206 C  CG  . GLU D  1  586 ? 6.834   122.761 33.943  1.00 89.59  ?  586 GLU D CG  1 
ATOM   19207 C  CD  . GLU D  1  586 ? 7.425   121.438 33.495  1.00 103.26 ?  586 GLU D CD  1 
ATOM   19208 O  OE1 . GLU D  1  586 ? 8.234   120.862 34.255  1.00 107.01 ?  586 GLU D OE1 1 
ATOM   19209 O  OE2 . GLU D  1  586 ? 7.084   120.977 32.382  1.00 115.30 ?  586 GLU D OE2 1 
ATOM   19210 N  N   . ALA D  1  587 ? 6.038   121.973 38.370  1.00 97.02  ?  587 ALA D N   1 
ATOM   19211 C  CA  . ALA D  1  587 ? 5.257   121.759 39.589  1.00 99.02  ?  587 ALA D CA  1 
ATOM   19212 C  C   . ALA D  1  587 ? 6.100   121.736 40.880  1.00 99.69  ?  587 ALA D C   1 
ATOM   19213 O  O   . ALA D  1  587 ? 5.575   121.376 41.933  1.00 95.93  ?  587 ALA D O   1 
ATOM   19214 C  CB  . ALA D  1  587 ? 4.484   120.457 39.462  1.00 90.33  ?  587 ALA D CB  1 
ATOM   19215 N  N   . ASN D  1  588 ? 7.396   122.108 40.808  1.00 101.07 ?  588 ASN D N   1 
ATOM   19216 C  CA  . ASN D  1  588 ? 8.303   122.121 41.965  1.00 94.30  ?  588 ASN D CA  1 
ATOM   19217 C  C   . ASN D  1  588 ? 8.235   120.813 42.768  1.00 100.57 ?  588 ASN D C   1 
ATOM   19218 O  O   . ASN D  1  588 ? 8.316   120.823 43.999  1.00 105.16 ?  588 ASN D O   1 
ATOM   19219 C  CB  . ASN D  1  588 ? 8.008   123.325 42.866  1.00 99.91  ?  588 ASN D CB  1 
ATOM   19220 C  CG  . ASN D  1  588 ? 9.188   123.737 43.714  1.00 111.35 ?  588 ASN D CG  1 
ATOM   19221 O  OD1 . ASN D  1  588 ? 10.255  124.102 43.200  1.00 101.05 ?  588 ASN D OD1 1 
ATOM   19222 N  ND2 . ASN D  1  588 ? 9.035   123.677 45.031  1.00 112.61 ?  588 ASN D ND2 1 
ATOM   19223 N  N   . GLY D  1  589 ? 8.087   119.706 42.052  1.00 101.03 ?  589 GLY D N   1 
ATOM   19224 C  CA  . GLY D  1  589 ? 7.984   118.386 42.651  1.00 98.52  ?  589 GLY D CA  1 
ATOM   19225 C  C   . GLY D  1  589 ? 8.196   117.321 41.599  1.00 86.82  ?  589 GLY D C   1 
ATOM   19226 O  O   . GLY D  1  589 ? 8.475   117.634 40.439  1.00 88.16  ?  589 GLY D O   1 
ATOM   19227 N  N   . VAL D  1  590 ? 8.056   116.049 42.000  1.00 78.65  ?  590 VAL D N   1 
ATOM   19228 C  CA  . VAL D  1  590 ? 8.272   114.903 41.122  1.00 77.44  ?  590 VAL D CA  1 
ATOM   19229 C  C   . VAL D  1  590 ? 7.058   114.079 40.682  1.00 73.80  ?  590 VAL D C   1 
ATOM   19230 O  O   . VAL D  1  590 ? 6.071   114.013 41.413  1.00 83.40  ?  590 VAL D O   1 
ATOM   19231 C  CB  . VAL D  1  590 ? 9.233   114.015 41.954  1.00 72.71  ?  590 VAL D CB  1 
ATOM   19232 C  CG1 . VAL D  1  590 ? 10.479  114.787 42.370  1.00 78.94  ?  590 VAL D CG1 1 
ATOM   19233 C  CG2 . VAL D  1  590 ? 8.538   113.430 43.183  1.00 66.35  ?  590 VAL D CG2 1 
ATOM   19234 N  N   . VAL D  1  591 ? 7.141   113.429 39.501  1.00 66.77  ?  591 VAL D N   1 
ATOM   19235 C  CA  . VAL D  1  591 ? 6.069   112.560 38.998  1.00 65.21  ?  591 VAL D CA  1 
ATOM   19236 C  C   . VAL D  1  591 ? 6.554   111.112 39.115  1.00 75.54  ?  591 VAL D C   1 
ATOM   19237 O  O   . VAL D  1  591 ? 7.755   110.861 39.036  1.00 78.59  ?  591 VAL D O   1 
ATOM   19238 C  CB  . VAL D  1  591 ? 5.593   112.889 37.550  1.00 64.10  ?  591 VAL D CB  1 
ATOM   19239 C  CG1 . VAL D  1  591 ? 5.435   114.387 37.350  1.00 72.73  ?  591 VAL D CG1 1 
ATOM   19240 C  CG2 . VAL D  1  591 ? 6.513   112.292 36.492  1.00 62.44  ?  591 VAL D CG2 1 
ATOM   19241 N  N   . MET D  1  592 ? 5.634   110.162 39.309  1.00 69.05  ?  592 MET D N   1 
ATOM   19242 C  CA  . MET D  1  592 ? 6.002   108.756 39.440  1.00 69.22  ?  592 MET D CA  1 
ATOM   19243 C  C   . MET D  1  592 ? 5.276   107.917 38.406  1.00 78.78  ?  592 MET D C   1 
ATOM   19244 O  O   . MET D  1  592 ? 4.142   108.230 38.052  1.00 85.91  ?  592 MET D O   1 
ATOM   19245 C  CB  . MET D  1  592 ? 5.672   108.255 40.847  1.00 68.26  ?  592 MET D CB  1 
ATOM   19246 C  CG  . MET D  1  592 ? 6.592   107.151 41.316  1.00 68.14  ?  592 MET D CG  1 
ATOM   19247 S  SD  . MET D  1  592 ? 6.240   106.595 42.990  1.00 85.95  ?  592 MET D SD  1 
ATOM   19248 C  CE  . MET D  1  592 ? 6.591   108.065 43.900  1.00 86.01  ?  592 MET D CE  1 
ATOM   19249 N  N   . VAL D  1  593 ? 5.935   106.867 37.911  1.00 71.09  ?  593 VAL D N   1 
ATOM   19250 C  CA  . VAL D  1  593 ? 5.310   105.999 36.869  1.00 60.76  ?  593 VAL D CA  1 
ATOM   19251 C  C   . VAL D  1  593 ? 5.720   104.544 37.110  1.00 77.59  ?  593 VAL D C   1 
ATOM   19252 O  O   . VAL D  1  593 ? 6.898   104.310 37.433  1.00 82.04  ?  593 VAL D O   1 
ATOM   19253 C  CB  . VAL D  1  593 ? 5.675   106.467 35.448  1.00 58.01  ?  593 VAL D CB  1 
ATOM   19254 C  CG1 . VAL D  1  593 ? 7.179   106.479 35.223  1.00 90.02  ?  593 VAL D CG1 1 
ATOM   19255 C  CG2 . VAL D  1  593 ? 4.978   105.634 34.383  1.00 73.95  ?  593 VAL D CG2 1 
ATOM   19256 N  N   . ASN D  1  594 ? 4.775   103.612 36.965  1.00 68.45  ?  594 ASN D N   1 
ATOM   19257 C  CA  . ASN D  1  594 ? 5.062   102.192 37.152  1.00 72.50  ?  594 ASN D CA  1 
ATOM   19258 C  C   . ASN D  1  594 ? 5.193   101.540 35.770  1.00 78.35  ?  594 ASN D C   1 
ATOM   19259 O  O   . ASN D  1  594 ? 4.729   102.098 34.777  1.00 78.02  ?  594 ASN D O   1 
ATOM   19260 C  CB  . ASN D  1  594 ? 4.013   101.495 38.030  1.00 71.45  ?  594 ASN D CB  1 
ATOM   19261 C  CG  . ASN D  1  594 ? 2.590   101.635 37.559  1.00 83.97  ?  594 ASN D CG  1 
ATOM   19262 O  OD1 . ASN D  1  594 ? 2.074   100.791 36.819  1.00 110.57 ?  594 ASN D OD1 1 
ATOM   19263 N  ND2 . ASN D  1  594 ? 1.914   102.695 37.984  1.00 77.76  ?  594 ASN D ND2 1 
ATOM   19264 N  N   . ARG D  1  595 ? 5.856   100.384 35.704  1.00 77.04  ?  595 ARG D N   1 
ATOM   19265 C  CA  . ARG D  1  595 ? 6.091   99.678  34.444  1.00 65.94  ?  595 ARG D CA  1 
ATOM   19266 C  C   . ARG D  1  595 ? 4.803   99.359  33.661  1.00 76.00  ?  595 ARG D C   1 
ATOM   19267 O  O   . ARG D  1  595 ? 4.803   99.436  32.435  1.00 74.04  ?  595 ARG D O   1 
ATOM   19268 C  CB  . ARG D  1  595 ? 6.892   98.388  34.714  1.00 69.80  ?  595 ARG D CB  1 
ATOM   19269 C  CG  . ARG D  1  595 ? 7.716   97.897  33.523  1.00 85.93  ?  595 ARG D CG  1 
ATOM   19270 C  CD  . ARG D  1  595 ? 8.731   96.834  33.921  1.00 89.57  ?  595 ARG D CD  1 
ATOM   19271 N  NE  . ARG D  1  595 ? 9.927   97.404  34.548  1.00 78.10  ?  595 ARG D NE  1 
ATOM   19272 C  CZ  . ARG D  1  595 ? 10.952  97.939  33.889  1.00 82.76  ?  595 ARG D CZ  1 
ATOM   19273 N  NH1 . ARG D  1  595 ? 10.943  97.997  32.560  1.00 91.33  ?  595 ARG D NH1 1 
ATOM   19274 N  NH2 . ARG D  1  595 ? 11.989  98.432  34.552  1.00 75.76  ?  595 ARG D NH2 1 
ATOM   19275 N  N   . GLU D  1  596 ? 3.716   99.011  34.357  1.00 77.60  ?  596 GLU D N   1 
ATOM   19276 C  CA  . GLU D  1  596 ? 2.448   98.671  33.707  1.00 73.53  ?  596 GLU D CA  1 
ATOM   19277 C  C   . GLU D  1  596 ? 1.782   99.863  33.000  1.00 93.96  ?  596 GLU D C   1 
ATOM   19278 O  O   . GLU D  1  596 ? 1.106   99.669  31.990  1.00 108.32 ?  596 GLU D O   1 
ATOM   19279 C  CB  . GLU D  1  596 ? 1.475   98.064  34.731  1.00 90.97  ?  596 GLU D CB  1 
ATOM   19280 C  CG  . GLU D  1  596 ? 1.951   96.755  35.346  1.00 99.68  ?  596 GLU D CG  1 
ATOM   19281 C  CD  . GLU D  1  596 ? 2.397   96.856  36.792  1.00 114.55 ?  596 GLU D CD  1 
ATOM   19282 O  OE1 . GLU D  1  596 ? 3.068   97.852  37.147  1.00 108.54 ?  596 GLU D OE1 1 
ATOM   19283 O  OE2 . GLU D  1  596 ? 2.076   95.931  37.571  1.00 125.17 ?  596 GLU D OE2 1 
ATOM   19284 N  N   . PHE D  1  597 ? 1.963   101.084 33.527  1.00 91.83  ?  597 PHE D N   1 
ATOM   19285 C  CA  . PHE D  1  597 ? 1.372   102.295 32.949  1.00 90.34  ?  597 PHE D CA  1 
ATOM   19286 C  C   . PHE D  1  597 ? 1.972   102.605 31.574  1.00 87.78  ?  597 PHE D C   1 
ATOM   19287 O  O   . PHE D  1  597 ? 3.125   103.030 31.485  1.00 89.56  ?  597 PHE D O   1 
ATOM   19288 C  CB  . PHE D  1  597 ? 1.591   103.484 33.895  1.00 93.33  ?  597 PHE D CB  1 
ATOM   19289 C  CG  . PHE D  1  597 ? 0.741   104.687 33.575  1.00 91.50  ?  597 PHE D CG  1 
ATOM   19290 C  CD1 . PHE D  1  597 ? -0.587  104.737 33.956  1.00 93.12  ?  597 PHE D CD1 1 
ATOM   19291 C  CD2 . PHE D  1  597 ? 1.272   105.771 32.900  1.00 93.29  ?  597 PHE D CD2 1 
ATOM   19292 C  CE1 . PHE D  1  597 ? -1.367  105.847 33.668  1.00 89.59  ?  597 PHE D CE1 1 
ATOM   19293 C  CE2 . PHE D  1  597 ? 0.489   106.882 32.615  1.00 94.43  ?  597 PHE D CE2 1 
ATOM   19294 C  CZ  . PHE D  1  597 ? -0.826  106.911 32.997  1.00 99.11  ?  597 PHE D CZ  1 
ATOM   19295 N  N   . GLY D  1  598 ? 1.183   102.405 30.523  1.00 90.31  ?  598 GLY D N   1 
ATOM   19296 C  CA  . GLY D  1  598 ? 1.628   102.624 29.151  1.00 96.83  ?  598 GLY D CA  1 
ATOM   19297 C  C   . GLY D  1  598 ? 1.370   103.997 28.561  1.00 99.36  ?  598 GLY D C   1 
ATOM   19298 O  O   . GLY D  1  598 ? 1.884   104.303 27.481  1.00 102.20 ?  598 GLY D O   1 
ATOM   19299 N  N   . ALA D  1  599 ? 0.576   104.834 29.239  1.00 98.56  ?  599 ALA D N   1 
ATOM   19300 C  CA  . ALA D  1  599 ? 0.254   106.174 28.741  1.00 90.01  ?  599 ALA D CA  1 
ATOM   19301 C  C   . ALA D  1  599 ? 1.378   107.190 29.028  1.00 89.63  ?  599 ALA D C   1 
ATOM   19302 O  O   . ALA D  1  599 ? 2.280   106.902 29.814  1.00 98.67  ?  599 ALA D O   1 
ATOM   19303 C  CB  . ALA D  1  599 ? -1.059  106.641 29.360  1.00 94.36  ?  599 ALA D CB  1 
ATOM   19304 N  N   . THR D  1  600 ? 1.331   108.370 28.375  1.00 96.72  ?  600 THR D N   1 
ATOM   19305 C  CA  . THR D  1  600 ? 2.325   109.427 28.571  1.00 90.84  ?  600 THR D CA  1 
ATOM   19306 C  C   . THR D  1  600 ? 2.134   110.073 29.953  1.00 90.10  ?  600 THR D C   1 
ATOM   19307 O  O   . THR D  1  600 ? 1.068   109.950 30.561  1.00 87.80  ?  600 THR D O   1 
ATOM   19308 C  CB  . THR D  1  600 ? 2.248   110.439 27.405  1.00 87.51  ?  600 THR D CB  1 
ATOM   19309 O  OG1 . THR D  1  600 ? 2.605   109.768 26.195  1.00 112.67 ?  600 THR D OG1 1 
ATOM   19310 C  CG2 . THR D  1  600 ? 3.163   111.646 27.597  1.00 86.53  ?  600 THR D CG2 1 
ATOM   19311 N  N   . THR D  1  601 ? 3.180   110.742 30.452  1.00 88.50  ?  601 THR D N   1 
ATOM   19312 C  CA  . THR D  1  601 ? 3.166   111.387 31.766  1.00 89.51  ?  601 THR D CA  1 
ATOM   19313 C  C   . THR D  1  601 ? 3.305   112.914 31.636  1.00 90.27  ?  601 THR D C   1 
ATOM   19314 O  O   . THR D  1  601 ? 3.506   113.413 30.527  1.00 94.65  ?  601 THR D O   1 
ATOM   19315 C  CB  . THR D  1  601 ? 4.284   110.781 32.622  1.00 80.38  ?  601 THR D CB  1 
ATOM   19316 O  OG1 . THR D  1  601 ? 5.551   111.190 32.106  1.00 85.89  ?  601 THR D OG1 1 
ATOM   19317 C  CG2 . THR D  1  601 ? 4.206   109.266 32.685  1.00 95.58  ?  601 THR D CG2 1 
ATOM   19318 N  N   . PRO D  1  602 ? 3.207   113.690 32.738  1.00 82.96  ?  602 PRO D N   1 
ATOM   19319 C  CA  . PRO D  1  602 ? 3.336   115.150 32.609  1.00 91.08  ?  602 PRO D CA  1 
ATOM   19320 C  C   . PRO D  1  602 ? 4.687   115.627 32.084  1.00 94.10  ?  602 PRO D C   1 
ATOM   19321 O  O   . PRO D  1  602 ? 4.809   116.788 31.696  1.00 92.61  ?  602 PRO D O   1 
ATOM   19322 C  CB  . PRO D  1  602 ? 3.063   115.658 34.028  1.00 103.03 ?  602 PRO D CB  1 
ATOM   19323 C  CG  . PRO D  1  602 ? 2.362   114.542 34.709  1.00 92.45  ?  602 PRO D CG  1 
ATOM   19324 C  CD  . PRO D  1  602 ? 2.967   113.311 34.141  1.00 85.76  ?  602 PRO D CD  1 
ATOM   19325 N  N   . LEU D  1  603 ? 5.699   114.745 32.063  1.00 85.79  ?  603 LEU D N   1 
ATOM   19326 C  CA  . LEU D  1  603 ? 7.011   115.105 31.536  1.00 77.57  ?  603 LEU D CA  1 
ATOM   19327 C  C   . LEU D  1  603 ? 7.102   114.829 30.021  1.00 81.81  ?  603 LEU D C   1 
ATOM   19328 O  O   . LEU D  1  603 ? 8.185   114.944 29.450  1.00 86.07  ?  603 LEU D O   1 
ATOM   19329 C  CB  . LEU D  1  603 ? 8.115   114.335 32.277  1.00 67.47  ?  603 LEU D CB  1 
ATOM   19330 C  CG  . LEU D  1  603 ? 8.174   114.522 33.792  1.00 78.33  ?  603 LEU D CG  1 
ATOM   19331 C  CD1 . LEU D  1  603 ? 9.203   113.596 34.402  1.00 65.11  ?  603 LEU D CD1 1 
ATOM   19332 C  CD2 . LEU D  1  603 ? 8.481   115.960 34.162  1.00 91.36  ?  603 LEU D CD2 1 
ATOM   19333 N  N   . GLY D  1  604 ? 5.982   114.483 29.385  1.00 75.71  ?  604 GLY D N   1 
ATOM   19334 C  CA  . GLY D  1  604 ? 5.946   114.193 27.958  1.00 92.07  ?  604 GLY D CA  1 
ATOM   19335 C  C   . GLY D  1  604 ? 6.687   112.924 27.595  1.00 84.70  ?  604 GLY D C   1 
ATOM   19336 O  O   . GLY D  1  604 ? 7.260   112.828 26.508  1.00 93.38  ?  604 GLY D O   1 
ATOM   19337 N  N   . MET D  1  605 ? 6.683   111.938 28.499  1.00 89.29  ?  605 MET D N   1 
ATOM   19338 C  CA  . MET D  1  605 ? 7.373   110.672 28.278  1.00 88.60  ?  605 MET D CA  1 
ATOM   19339 C  C   . MET D  1  605 ? 6.612   109.514 28.902  1.00 90.87  ?  605 MET D C   1 
ATOM   19340 O  O   . MET D  1  605 ? 5.908   109.690 29.894  1.00 85.74  ?  605 MET D O   1 
ATOM   19341 C  CB  . MET D  1  605 ? 8.761   110.714 28.934  1.00 87.22  ?  605 MET D CB  1 
ATOM   19342 C  CG  . MET D  1  605 ? 9.800   111.451 28.137  1.00 89.43  ?  605 MET D CG  1 
ATOM   19343 S  SD  . MET D  1  605 ? 11.345  111.579 29.056  1.00 81.36  ?  605 MET D SD  1 
ATOM   19344 C  CE  . MET D  1  605 ? 10.987  113.016 30.059  1.00 65.80  ?  605 MET D CE  1 
ATOM   19345 N  N   . THR D  1  606 ? 6.787   108.321 28.336  1.00 91.46  ?  606 THR D N   1 
ATOM   19346 C  CA  . THR D  1  606 ? 6.172   107.102 28.848  1.00 92.92  ?  606 THR D CA  1 
ATOM   19347 C  C   . THR D  1  606 ? 7.207   106.413 29.746  1.00 86.85  ?  606 THR D C   1 
ATOM   19348 O  O   . THR D  1  606 ? 8.377   106.797 29.728  1.00 85.68  ?  606 THR D O   1 
ATOM   19349 C  CB  . THR D  1  606 ? 5.774   106.200 27.681  1.00 85.78  ?  606 THR D CB  1 
ATOM   19350 O  OG1 . THR D  1  606 ? 6.937   105.939 26.891  1.00 75.54  ?  606 THR D OG1 1 
ATOM   19351 C  CG2 . THR D  1  606 ? 4.675   106.812 26.825  1.00 81.33  ?  606 THR D CG2 1 
ATOM   19352 N  N   . PHE D  1  607 ? 6.803   105.391 30.520  1.00 86.51  ?  607 PHE D N   1 
ATOM   19353 C  CA  . PHE D  1  607 ? 7.737   104.679 31.397  1.00 78.19  ?  607 PHE D CA  1 
ATOM   19354 C  C   . PHE D  1  607 ? 8.959   104.159 30.628  1.00 74.83  ?  607 PHE D C   1 
ATOM   19355 O  O   . PHE D  1  607 ? 10.073  104.238 31.133  1.00 86.01  ?  607 PHE D O   1 
ATOM   19356 C  CB  . PHE D  1  607 ? 7.033   103.515 32.107  1.00 80.75  ?  607 PHE D CB  1 
ATOM   19357 C  CG  . PHE D  1  607 ? 7.927   102.729 33.036  1.00 67.58  ?  607 PHE D CG  1 
ATOM   19358 C  CD1 . PHE D  1  607 ? 8.713   101.695 32.559  1.00 54.13  ?  607 PHE D CD1 1 
ATOM   19359 C  CD2 . PHE D  1  607 ? 7.969   103.015 34.387  1.00 63.94  ?  607 PHE D CD2 1 
ATOM   19360 C  CE1 . PHE D  1  607 ? 9.538   100.981 33.411  1.00 54.57  ?  607 PHE D CE1 1 
ATOM   19361 C  CE2 . PHE D  1  607 ? 8.777   102.281 35.242  1.00 77.33  ?  607 PHE D CE2 1 
ATOM   19362 C  CZ  . PHE D  1  607 ? 9.556   101.268 34.749  1.00 75.69  ?  607 PHE D CZ  1 
ATOM   19363 N  N   . GLY D  1  608 ? 8.745   103.647 29.424  1.00 68.24  ?  608 GLY D N   1 
ATOM   19364 C  CA  . GLY D  1  608 ? 9.833   103.136 28.604  1.00 77.41  ?  608 GLY D CA  1 
ATOM   19365 C  C   . GLY D  1  608 ? 10.828  104.212 28.217  1.00 77.98  ?  608 GLY D C   1 
ATOM   19366 O  O   . GLY D  1  608 ? 12.036  103.965 28.200  1.00 87.04  ?  608 GLY D O   1 
ATOM   19367 N  N   . GLU D  1  609 ? 10.325  105.417 27.905  1.00 82.56  ?  609 GLU D N   1 
ATOM   19368 C  CA  . GLU D  1  609 ? 11.169  106.552 27.524  1.00 87.98  ?  609 GLU D CA  1 
ATOM   19369 C  C   . GLU D  1  609 ? 11.981  107.030 28.729  1.00 78.73  ?  609 GLU D C   1 
ATOM   19370 O  O   . GLU D  1  609 ? 13.163  107.341 28.593  1.00 77.04  ?  609 GLU D O   1 
ATOM   19371 C  CB  . GLU D  1  609 ? 10.309  107.702 26.971  1.00 83.28  ?  609 GLU D CB  1 
ATOM   19372 C  CG  . GLU D  1  609 ? 9.685   107.397 25.621  1.00 91.05  ?  609 GLU D CG  1 
ATOM   19373 C  CD  . GLU D  1  609 ? 8.956   108.563 24.982  1.00 104.15 ?  609 GLU D CD  1 
ATOM   19374 O  OE1 . GLU D  1  609 ? 7.828   108.878 25.426  1.00 100.86 ?  609 GLU D OE1 1 
ATOM   19375 O  OE2 . GLU D  1  609 ? 9.510   109.157 24.029  1.00 105.56 ?  609 GLU D OE2 1 
ATOM   19376 N  N   . LEU D  1  610 ? 11.347  107.083 29.906  1.00 82.23  ?  610 LEU D N   1 
ATOM   19377 C  CA  . LEU D  1  610 ? 12.011  107.496 31.138  1.00 77.01  ?  610 LEU D CA  1 
ATOM   19378 C  C   . LEU D  1  610 ? 13.056  106.460 31.563  1.00 74.56  ?  610 LEU D C   1 
ATOM   19379 O  O   . LEU D  1  610 ? 14.113  106.838 32.062  1.00 75.13  ?  610 LEU D O   1 
ATOM   19380 C  CB  . LEU D  1  610 ? 10.974  107.671 32.265  1.00 62.92  ?  610 LEU D CB  1 
ATOM   19381 C  CG  . LEU D  1  610 ? 10.240  109.021 32.318  1.00 72.64  ?  610 LEU D CG  1 
ATOM   19382 C  CD1 . LEU D  1  610 ? 8.882   108.882 32.966  1.00 75.61  ?  610 LEU D CD1 1 
ATOM   19383 C  CD2 . LEU D  1  610 ? 11.050  110.061 33.077  1.00 68.47  ?  610 LEU D CD2 1 
ATOM   19384 N  N   . ALA D  1  611 ? 12.771  105.162 31.360  1.00 68.81  ?  611 ALA D N   1 
ATOM   19385 C  CA  . ALA D  1  611 ? 13.687  104.081 31.727  1.00 62.32  ?  611 ALA D CA  1 
ATOM   19386 C  C   . ALA D  1  611 ? 15.014  104.178 30.988  1.00 74.36  ?  611 ALA D C   1 
ATOM   19387 O  O   . ALA D  1  611 ? 16.054  103.833 31.548  1.00 72.52  ?  611 ALA D O   1 
ATOM   19388 C  CB  . ALA D  1  611 ? 13.042  102.734 31.458  1.00 72.86  ?  611 ALA D CB  1 
ATOM   19389 N  N   . SER D  1  612 ? 14.990  104.639 29.738  1.00 73.84  ?  612 SER D N   1 
ATOM   19390 C  CA  . SER D  1  612 ? 16.215  104.807 28.962  1.00 79.17  ?  612 SER D CA  1 
ATOM   19391 C  C   . SER D  1  612 ? 17.091  105.929 29.565  1.00 85.62  ?  612 SER D C   1 
ATOM   19392 O  O   . SER D  1  612 ? 18.307  105.902 29.395  1.00 84.87  ?  612 SER D O   1 
ATOM   19393 C  CB  . SER D  1  612 ? 15.873  105.137 27.513  1.00 71.42  ?  612 SER D CB  1 
ATOM   19394 O  OG  . SER D  1  612 ? 15.152  106.355 27.420  1.00 91.98  ?  612 SER D OG  1 
ATOM   19395 N  N   . MET D  1  613 ? 16.476  106.896 30.274  1.00 85.15  ?  613 MET D N   1 
ATOM   19396 C  CA  . MET D  1  613 ? 17.183  108.014 30.897  1.00 80.49  ?  613 MET D CA  1 
ATOM   19397 C  C   . MET D  1  613 ? 17.620  107.741 32.337  1.00 88.41  ?  613 MET D C   1 
ATOM   19398 O  O   . MET D  1  613 ? 18.355  108.559 32.889  1.00 84.63  ?  613 MET D O   1 
ATOM   19399 C  CB  . MET D  1  613 ? 16.274  109.243 30.958  1.00 68.24  ?  613 MET D CB  1 
ATOM   19400 C  CG  . MET D  1  613 ? 15.615  109.597 29.655  1.00 83.85  ?  613 MET D CG  1 
ATOM   19401 S  SD  . MET D  1  613 ? 15.257  111.364 29.514  1.00 82.32  ?  613 MET D SD  1 
ATOM   19402 C  CE  . MET D  1  613 ? 14.317  111.635 30.995  1.00 70.22  ?  613 MET D CE  1 
ATOM   19403 N  N   . THR D  1  614 ? 17.150  106.654 32.973  1.00 66.03  ?  614 THR D N   1 
ATOM   19404 C  CA  . THR D  1  614 ? 17.500  106.385 34.369  1.00 68.54  ?  614 THR D CA  1 
ATOM   19405 C  C   . THR D  1  614 ? 18.395  105.162 34.564  1.00 76.12  ?  614 THR D C   1 
ATOM   19406 O  O   . THR D  1  614 ? 19.324  105.199 35.372  1.00 84.08  ?  614 THR D O   1 
ATOM   19407 C  CB  . THR D  1  614 ? 16.217  106.237 35.192  1.00 68.97  ?  614 THR D CB  1 
ATOM   19408 O  OG1 . THR D  1  614 ? 15.522  105.071 34.758  1.00 92.97  ?  614 THR D OG1 1 
ATOM   19409 C  CG2 . THR D  1  614 ? 15.302  107.426 35.053  1.00 58.33  ?  614 THR D CG2 1 
ATOM   19410 N  N   . GLY D  1  615 ? 18.094  104.084 33.854  1.00 69.58  ?  615 GLY D N   1 
ATOM   19411 C  CA  . GLY D  1  615 ? 18.848  102.845 33.975  1.00 66.41  ?  615 GLY D CA  1 
ATOM   19412 C  C   . GLY D  1  615 ? 20.190  102.856 33.281  1.00 64.07  ?  615 GLY D C   1 
ATOM   19413 O  O   . GLY D  1  615 ? 20.533  103.819 32.594  1.00 74.28  ?  615 GLY D O   1 
ATOM   19414 N  N   . GLY D  1  616 ? 20.941  101.774 33.474  1.00 63.72  ?  616 GLY D N   1 
ATOM   19415 C  CA  . GLY D  1  616 ? 22.256  101.586 32.872  1.00 75.96  ?  616 GLY D CA  1 
ATOM   19416 C  C   . GLY D  1  616 ? 23.449  101.713 33.800  1.00 65.43  ?  616 GLY D C   1 
ATOM   19417 O  O   . GLY D  1  616 ? 24.590  101.647 33.339  1.00 77.89  ?  616 GLY D O   1 
ATOM   19418 N  N   . GLY D  1  617 ? 23.209  101.888 35.093  1.00 61.83  ?  617 GLY D N   1 
ATOM   19419 C  CA  . GLY D  1  617 ? 24.292  102.036 36.058  1.00 64.32  ?  617 GLY D CA  1 
ATOM   19420 C  C   . GLY D  1  617 ? 24.989  103.381 35.959  1.00 71.34  ?  617 GLY D C   1 
ATOM   19421 O  O   . GLY D  1  617 ? 26.202  103.468 36.154  1.00 70.67  ?  617 GLY D O   1 
ATOM   19422 N  N   . VAL D  1  618 ? 24.231  104.442 35.646  1.00 84.47  ?  618 VAL D N   1 
ATOM   19423 C  CA  . VAL D  1  618 ? 24.768  105.797 35.499  1.00 69.45  ?  618 VAL D CA  1 
ATOM   19424 C  C   . VAL D  1  618 ? 24.080  106.720 36.502  1.00 78.41  ?  618 VAL D C   1 
ATOM   19425 O  O   . VAL D  1  618 ? 22.866  106.617 36.683  1.00 86.76  ?  618 VAL D O   1 
ATOM   19426 C  CB  . VAL D  1  618 ? 24.546  106.304 34.050  1.00 61.90  ?  618 VAL D CB  1 
ATOM   19427 C  CG1 . VAL D  1  618 ? 25.125  107.703 33.859  1.00 87.28  ?  618 VAL D CG1 1 
ATOM   19428 C  CG2 . VAL D  1  618 ? 25.136  105.332 33.033  1.00 67.83  ?  618 VAL D CG2 1 
ATOM   19429 N  N   . GLN D  1  619 ? 24.844  107.619 37.155  1.00 85.28  ?  619 GLN D N   1 
ATOM   19430 C  CA  . GLN D  1  619 ? 24.274  108.559 38.126  1.00 79.90  ?  619 GLN D CA  1 
ATOM   19431 C  C   . GLN D  1  619 ? 23.474  109.582 37.335  1.00 78.30  ?  619 GLN D C   1 
ATOM   19432 O  O   . GLN D  1  619 ? 24.054  110.375 36.594  1.00 76.80  ?  619 GLN D O   1 
ATOM   19433 C  CB  . GLN D  1  619 ? 25.372  109.240 38.962  1.00 68.59  ?  619 GLN D CB  1 
ATOM   19434 C  CG  . GLN D  1  619 ? 26.064  108.291 39.934  1.00 57.78  ?  619 GLN D CG  1 
ATOM   19435 C  CD  . GLN D  1  619 ? 26.973  109.002 40.907  1.00 64.36  ?  619 GLN D CD  1 
ATOM   19436 O  OE1 . GLN D  1  619 ? 28.174  109.169 40.669  1.00 73.15  ?  619 GLN D OE1 1 
ATOM   19437 N  NE2 . GLN D  1  619 ? 26.430  109.428 42.036  1.00 81.39  ?  619 GLN D NE2 1 
ATOM   19438 N  N   . THR D  1  620 ? 22.143  109.539 37.468  1.00 68.08  ?  620 THR D N   1 
ATOM   19439 C  CA  . THR D  1  620 ? 21.246  110.415 36.722  1.00 65.53  ?  620 THR D CA  1 
ATOM   19440 C  C   . THR D  1  620 ? 20.524  111.448 37.590  1.00 67.81  ?  620 THR D C   1 
ATOM   19441 O  O   . THR D  1  620 ? 19.407  111.192 38.031  1.00 78.41  ?  620 THR D O   1 
ATOM   19442 C  CB  . THR D  1  620 ? 20.226  109.545 35.967  1.00 76.96  ?  620 THR D CB  1 
ATOM   19443 O  OG1 . THR D  1  620 ? 19.623  108.623 36.885  1.00 77.47  ?  620 THR D OG1 1 
ATOM   19444 C  CG2 . THR D  1  620 ? 20.861  108.775 34.821  1.00 78.49  ?  620 THR D CG2 1 
ATOM   19445 N  N   . PRO D  1  621 ? 21.105  112.642 37.813  1.00 67.14  ?  621 PRO D N   1 
ATOM   19446 C  CA  . PRO D  1  621 ? 20.402  113.658 38.611  1.00 63.93  ?  621 PRO D CA  1 
ATOM   19447 C  C   . PRO D  1  621 ? 19.011  113.973 38.074  1.00 61.86  ?  621 PRO D C   1 
ATOM   19448 O  O   . PRO D  1  621 ? 18.835  114.124 36.869  1.00 74.56  ?  621 PRO D O   1 
ATOM   19449 C  CB  . PRO D  1  621 ? 21.320  114.878 38.515  1.00 61.81  ?  621 PRO D CB  1 
ATOM   19450 C  CG  . PRO D  1  621 ? 22.652  114.330 38.229  1.00 64.66  ?  621 PRO D CG  1 
ATOM   19451 C  CD  . PRO D  1  621 ? 22.419  113.135 37.363  1.00 79.44  ?  621 PRO D CD  1 
ATOM   19452 N  N   . GLY D  1  622 ? 18.041  114.048 38.974  1.00 67.99  ?  622 GLY D N   1 
ATOM   19453 C  CA  . GLY D  1  622 ? 16.664  114.363 38.627  1.00 68.17  ?  622 GLY D CA  1 
ATOM   19454 C  C   . GLY D  1  622 ? 15.759  113.175 38.393  1.00 72.14  ?  622 GLY D C   1 
ATOM   19455 O  O   . GLY D  1  622 ? 14.537  113.320 38.446  1.00 76.46  ?  622 GLY D O   1 
ATOM   19456 N  N   . PHE D  1  623 ? 16.333  112.001 38.113  1.00 72.40  ?  623 PHE D N   1 
ATOM   19457 C  CA  . PHE D  1  623 ? 15.532  110.811 37.844  1.00 74.37  ?  623 PHE D CA  1 
ATOM   19458 C  C   . PHE D  1  623 ? 16.073  109.604 38.603  1.00 71.88  ?  623 PHE D C   1 
ATOM   19459 O  O   . PHE D  1  623 ? 17.287  109.427 38.676  1.00 77.43  ?  623 PHE D O   1 
ATOM   19460 C  CB  . PHE D  1  623 ? 15.524  110.519 36.339  1.00 62.48  ?  623 PHE D CB  1 
ATOM   19461 C  CG  . PHE D  1  623 ? 15.129  111.673 35.446  1.00 73.24  ?  623 PHE D CG  1 
ATOM   19462 C  CD1 . PHE D  1  623 ? 16.082  112.536 34.937  1.00 68.07  ?  623 PHE D CD1 1 
ATOM   19463 C  CD2 . PHE D  1  623 ? 13.811  111.860 35.073  1.00 81.06  ?  623 PHE D CD2 1 
ATOM   19464 C  CE1 . PHE D  1  623 ? 15.715  113.592 34.112  1.00 73.77  ?  623 PHE D CE1 1 
ATOM   19465 C  CE2 . PHE D  1  623 ? 13.447  112.916 34.248  1.00 85.01  ?  623 PHE D CE2 1 
ATOM   19466 C  CZ  . PHE D  1  623 ? 14.401  113.776 33.774  1.00 82.30  ?  623 PHE D CZ  1 
ATOM   19467 N  N   . MET D  1  624 ? 15.180  108.769 39.165  1.00 73.65  ?  624 MET D N   1 
ATOM   19468 C  CA  . MET D  1  624 ? 15.604  107.586 39.917  1.00 74.82  ?  624 MET D CA  1 
ATOM   19469 C  C   . MET D  1  624 ? 14.647  106.401 39.729  1.00 75.89  ?  624 MET D C   1 
ATOM   19470 O  O   . MET D  1  624 ? 13.450  106.597 39.529  1.00 71.54  ?  624 MET D O   1 
ATOM   19471 C  CB  . MET D  1  624 ? 15.746  107.926 41.417  1.00 73.05  ?  624 MET D CB  1 
ATOM   19472 C  CG  . MET D  1  624 ? 14.412  107.980 42.182  1.00 80.01  ?  624 MET D CG  1 
ATOM   19473 S  SD  . MET D  1  624 ? 14.543  108.022 43.994  1.00 83.21  ?  624 MET D SD  1 
ATOM   19474 C  CE  . MET D  1  624 ? 15.310  106.439 44.308  1.00 89.59  ?  624 MET D CE  1 
ATOM   19475 N  N   . GLY D  1  625 ? 15.190  105.190 39.814  1.00 76.75  ?  625 GLY D N   1 
ATOM   19476 C  CA  . GLY D  1  625 ? 14.425  103.953 39.701  1.00 75.36  ?  625 GLY D CA  1 
ATOM   19477 C  C   . GLY D  1  625 ? 14.295  103.302 41.063  1.00 73.22  ?  625 GLY D C   1 
ATOM   19478 O  O   . GLY D  1  625 ? 15.202  103.434 41.889  1.00 74.04  ?  625 GLY D O   1 
ATOM   19479 N  N   . HIS D  1  626 ? 13.176  102.610 41.328  1.00 74.86  ?  626 HIS D N   1 
ATOM   19480 C  CA  . HIS D  1  626 ? 12.955  101.975 42.633  1.00 77.71  ?  626 HIS D CA  1 
ATOM   19481 C  C   . HIS D  1  626 ? 11.707  101.084 42.638  1.00 77.24  ?  626 HIS D C   1 
ATOM   19482 O  O   . HIS D  1  626 ? 10.882  101.166 41.730  1.00 80.72  ?  626 HIS D O   1 
ATOM   19483 C  CB  . HIS D  1  626 ? 12.781  103.068 43.708  1.00 73.68  ?  626 HIS D CB  1 
ATOM   19484 C  CG  . HIS D  1  626 ? 11.677  104.025 43.391  1.00 63.32  ?  626 HIS D CG  1 
ATOM   19485 N  ND1 . HIS D  1  626 ? 10.429  103.897 43.960  1.00 79.05  ?  626 HIS D ND1 1 
ATOM   19486 C  CD2 . HIS D  1  626 ? 11.664  105.084 42.552  1.00 75.08  ?  626 HIS D CD2 1 
ATOM   19487 C  CE1 . HIS D  1  626 ? 9.699   104.882 43.463  1.00 73.40  ?  626 HIS D CE1 1 
ATOM   19488 N  NE2 . HIS D  1  626 ? 10.401  105.623 42.611  1.00 74.62  ?  626 HIS D NE2 1 
ATOM   19489 N  N   . GLY D  1  627 ? 11.571  100.259 43.674  1.00 78.38  ?  627 GLY D N   1 
ATOM   19490 C  CA  . GLY D  1  627 ? 10.410  99.392  43.836  1.00 86.24  ?  627 GLY D CA  1 
ATOM   19491 C  C   . GLY D  1  627 ? 9.209   100.179 44.330  1.00 96.02  ?  627 GLY D C   1 
ATOM   19492 O  O   . GLY D  1  627 ? 9.353   101.343 44.713  1.00 98.42  ?  627 GLY D O   1 
ATOM   19493 N  N   . ARG D  1  628 ? 8.011   99.570  44.341  1.00 87.57  ?  628 ARG D N   1 
ATOM   19494 C  CA  . ARG D  1  628 ? 6.807   100.280 44.794  1.00 76.37  ?  628 ARG D CA  1 
ATOM   19495 C  C   . ARG D  1  628 ? 6.700   100.401 46.330  1.00 84.93  ?  628 ARG D C   1 
ATOM   19496 O  O   . ARG D  1  628 ? 5.898   101.193 46.823  1.00 95.40  ?  628 ARG D O   1 
ATOM   19497 C  CB  . ARG D  1  628 ? 5.537   99.652  44.182  1.00 75.12  ?  628 ARG D CB  1 
ATOM   19498 C  CG  . ARG D  1  628 ? 4.900   98.526  44.999  1.00 101.84 ?  628 ARG D CG  1 
ATOM   19499 C  CD  . ARG D  1  628 ? 4.088   97.569  44.139  1.00 116.48 ?  628 ARG D CD  1 
ATOM   19500 N  NE  . ARG D  1  628 ? 3.081   98.256  43.323  1.00 121.23 ?  628 ARG D NE  1 
ATOM   19501 C  CZ  . ARG D  1  628 ? 2.491   97.736  42.248  1.00 124.75 ?  628 ARG D CZ  1 
ATOM   19502 N  NH1 . ARG D  1  628 ? 2.803   96.511  41.834  1.00 128.03 ?  628 ARG D NH1 1 
ATOM   19503 N  NH2 . ARG D  1  628 ? 1.591   98.439  41.573  1.00 120.79 ?  628 ARG D NH2 1 
ATOM   19504 N  N   . GLN D  1  629 ? 7.504   99.640  47.080  1.00 82.97  ?  629 GLN D N   1 
ATOM   19505 C  CA  . GLN D  1  629 ? 7.465   99.684  48.543  1.00 93.46  ?  629 GLN D CA  1 
ATOM   19506 C  C   . GLN D  1  629 ? 8.242   100.890 49.104  1.00 85.26  ?  629 GLN D C   1 
ATOM   19507 O  O   . GLN D  1  629 ? 7.962   101.331 50.216  1.00 94.23  ?  629 GLN D O   1 
ATOM   19508 C  CB  . GLN D  1  629 ? 8.002   98.368  49.134  1.00 94.14  ?  629 GLN D CB  1 
ATOM   19509 C  CG  . GLN D  1  629 ? 7.450   97.095  48.481  1.00 106.40 ?  629 GLN D CG  1 
ATOM   19510 C  CD  . GLN D  1  629 ? 8.420   96.493  47.478  1.00 105.37 ?  629 GLN D CD  1 
ATOM   19511 O  OE1 . GLN D  1  629 ? 8.710   97.075  46.425  1.00 99.44  ?  629 GLN D OE1 1 
ATOM   19512 N  NE2 . GLN D  1  629 ? 8.948   95.309  47.778  1.00 93.05  ?  629 GLN D NE2 1 
ATOM   19513 N  N   . PHE D  1  630 ? 9.205   101.425 48.340  1.00 87.61  ?  630 PHE D N   1 
ATOM   19514 C  CA  . PHE D  1  630 ? 10.004  102.584 48.754  1.00 93.18  ?  630 PHE D CA  1 
ATOM   19515 C  C   . PHE D  1  630 ? 9.227   103.918 48.625  1.00 87.11  ?  630 PHE D C   1 
ATOM   19516 O  O   . PHE D  1  630 ? 9.717   104.952 49.074  1.00 84.50  ?  630 PHE D O   1 
ATOM   19517 C  CB  . PHE D  1  630 ? 11.289  102.636 47.902  1.00 95.19  ?  630 PHE D CB  1 
ATOM   19518 C  CG  . PHE D  1  630 ? 12.237  103.785 48.175  1.00 86.87  ?  630 PHE D CG  1 
ATOM   19519 C  CD1 . PHE D  1  630 ? 12.899  103.886 49.385  1.00 93.02  ?  630 PHE D CD1 1 
ATOM   19520 C  CD2 . PHE D  1  630 ? 12.519  104.720 47.194  1.00 80.04  ?  630 PHE D CD2 1 
ATOM   19521 C  CE1 . PHE D  1  630 ? 13.791  104.924 49.624  1.00 86.75  ?  630 PHE D CE1 1 
ATOM   19522 C  CE2 . PHE D  1  630 ? 13.414  105.754 47.436  1.00 78.90  ?  630 PHE D CE2 1 
ATOM   19523 C  CZ  . PHE D  1  630 ? 14.040  105.854 48.650  1.00 87.71  ?  630 PHE D CZ  1 
ATOM   19524 N  N   . ILE D  1  631 ? 8.024   103.899 48.026  1.00 89.20  ?  631 ILE D N   1 
ATOM   19525 C  CA  . ILE D  1  631 ? 7.233   105.115 47.836  1.00 80.93  ?  631 ILE D CA  1 
ATOM   19526 C  C   . ILE D  1  631 ? 6.843   105.770 49.166  1.00 84.32  ?  631 ILE D C   1 
ATOM   19527 O  O   . ILE D  1  631 ? 7.016   106.978 49.327  1.00 89.77  ?  631 ILE D O   1 
ATOM   19528 C  CB  . ILE D  1  631 ? 5.987   104.827 46.956  1.00 81.33  ?  631 ILE D CB  1 
ATOM   19529 C  CG1 . ILE D  1  631 ? 6.409   104.403 45.533  1.00 75.20  ?  631 ILE D CG1 1 
ATOM   19530 C  CG2 . ILE D  1  631 ? 5.069   106.060 46.906  1.00 77.91  ?  631 ILE D CG2 1 
ATOM   19531 C  CD1 . ILE D  1  631 ? 5.354   103.647 44.763  1.00 94.62  ?  631 ILE D CD1 1 
ATOM   19532 N  N   . ALA D  1  632 ? 6.309   104.988 50.110  1.00 88.34  ?  632 ALA D N   1 
ATOM   19533 C  CA  . ALA D  1  632 ? 5.884   105.517 51.408  1.00 89.81  ?  632 ALA D CA  1 
ATOM   19534 C  C   . ALA D  1  632 ? 7.029   105.719 52.401  1.00 94.39  ?  632 ALA D C   1 
ATOM   19535 O  O   . ALA D  1  632 ? 6.822   106.363 53.428  1.00 93.26  ?  632 ALA D O   1 
ATOM   19536 C  CB  . ALA D  1  632 ? 4.851   104.591 52.018  1.00 85.92  ?  632 ALA D CB  1 
ATOM   19537 N  N   . SER D  1  633 ? 8.224   105.169 52.114  1.00 104.14 ?  633 SER D N   1 
ATOM   19538 C  CA  . SER D  1  633 ? 9.399   105.270 52.986  1.00 100.80 ?  633 SER D CA  1 
ATOM   19539 C  C   . SER D  1  633 ? 9.673   106.690 53.478  1.00 87.11  ?  633 SER D C   1 
ATOM   19540 O  O   . SER D  1  633 ? 9.511   107.656 52.734  1.00 81.26  ?  633 SER D O   1 
ATOM   19541 C  CB  . SER D  1  633 ? 10.636  104.735 52.266  1.00 99.74  ?  633 SER D CB  1 
ATOM   19542 O  OG  . SER D  1  633 ? 11.828  104.959 53.001  1.00 95.19  ?  633 SER D OG  1 
ATOM   19543 N  N   . LYS D  1  634 ? 10.115  106.808 54.734  1.00 88.78  ?  634 LYS D N   1 
ATOM   19544 C  CA  . LYS D  1  634 ? 10.439  108.116 55.311  1.00 82.42  ?  634 LYS D CA  1 
ATOM   19545 C  C   . LYS D  1  634 ? 11.730  108.662 54.676  1.00 83.23  ?  634 LYS D C   1 
ATOM   19546 O  O   . LYS D  1  634 ? 11.992  109.860 54.764  1.00 87.70  ?  634 LYS D O   1 
ATOM   19547 C  CB  . LYS D  1  634 ? 10.599  108.043 56.845  1.00 85.84  ?  634 LYS D CB  1 
ATOM   19548 C  CG  . LYS D  1  634 ? 9.597   107.132 57.547  1.00 108.03 ?  634 LYS D CG  1 
ATOM   19549 C  CD  . LYS D  1  634 ? 9.532   107.377 59.053  1.00 114.34 ?  634 LYS D CD  1 
ATOM   19550 C  CE  . LYS D  1  634 ? 8.533   106.474 59.748  1.00 125.31 ?  634 LYS D CE  1 
ATOM   19551 N  NZ  . LYS D  1  634 ? 8.735   105.029 59.434  1.00 119.89 ?  634 LYS D NZ  1 
ATOM   19552 N  N   . LYS D  1  635 ? 12.532  107.782 54.042  1.00 79.56  ?  635 LYS D N   1 
ATOM   19553 C  CA  . LYS D  1  635 ? 13.777  108.155 53.388  1.00 85.13  ?  635 LYS D CA  1 
ATOM   19554 C  C   . LYS D  1  635 ? 13.601  108.477 51.894  1.00 86.96  ?  635 LYS D C   1 
ATOM   19555 O  O   . LYS D  1  635 ? 14.587  108.748 51.211  1.00 77.92  ?  635 LYS D O   1 
ATOM   19556 C  CB  . LYS D  1  635 ? 14.808  107.034 53.570  1.00 73.03  ?  635 LYS D CB  1 
ATOM   19557 C  CG  . LYS D  1  635 ? 15.140  106.719 55.026  1.00 95.10  ?  635 LYS D CG  1 
ATOM   19558 C  CD  . LYS D  1  635 ? 15.604  107.944 55.824  1.00 94.24  ?  635 LYS D CD  1 
ATOM   19559 C  CE  . LYS D  1  635 ? 16.382  107.587 57.070  1.00 96.95  ?  635 LYS D CE  1 
ATOM   19560 N  NZ  . LYS D  1  635 ? 15.979  108.399 58.247  1.00 79.56  ?  635 LYS D NZ  1 
ATOM   19561 N  N   . PHE D  1  636 ? 12.362  108.465 51.388  1.00 84.17  ?  636 PHE D N   1 
ATOM   19562 C  CA  . PHE D  1  636 ? 12.097  108.770 49.991  1.00 81.27  ?  636 PHE D CA  1 
ATOM   19563 C  C   . PHE D  1  636 ? 12.296  110.266 49.766  1.00 86.91  ?  636 PHE D C   1 
ATOM   19564 O  O   . PHE D  1  636 ? 11.500  111.061 50.259  1.00 100.54 ?  636 PHE D O   1 
ATOM   19565 C  CB  . PHE D  1  636 ? 10.660  108.360 49.635  1.00 84.62  ?  636 PHE D CB  1 
ATOM   19566 C  CG  . PHE D  1  636 ? 10.276  108.586 48.193  1.00 83.66  ?  636 PHE D CG  1 
ATOM   19567 C  CD1 . PHE D  1  636 ? 10.604  107.661 47.220  1.00 84.32  ?  636 PHE D CD1 1 
ATOM   19568 C  CD2 . PHE D  1  636 ? 9.554   109.703 47.819  1.00 83.73  ?  636 PHE D CD2 1 
ATOM   19569 C  CE1 . PHE D  1  636 ? 10.241  107.863 45.896  1.00 88.31  ?  636 PHE D CE1 1 
ATOM   19570 C  CE2 . PHE D  1  636 ? 9.186   109.901 46.496  1.00 84.41  ?  636 PHE D CE2 1 
ATOM   19571 C  CZ  . PHE D  1  636 ? 9.532   108.978 45.543  1.00 91.13  ?  636 PHE D CZ  1 
ATOM   19572 N  N   . MET D  1  637 ? 13.377  110.641 49.080  1.00 80.49  ?  637 MET D N   1 
ATOM   19573 C  CA  . MET D  1  637 ? 13.645  112.073 48.774  1.00 78.57  ?  637 MET D CA  1 
ATOM   19574 C  C   . MET D  1  637 ? 13.823  112.870 50.072  1.00 85.41  ?  637 MET D C   1 
ATOM   19575 O  O   . MET D  1  637 ? 13.412  114.043 50.100  1.00 96.95  ?  637 MET D O   1 
ATOM   19576 C  CB  . MET D  1  637 ? 12.496  112.680 47.962  1.00 76.97  ?  637 MET D CB  1 
ATOM   19577 C  CG  . MET D  1  637 ? 12.070  111.827 46.786  1.00 87.44  ?  637 MET D CG  1 
ATOM   19578 S  SD  . MET D  1  637 ? 11.607  112.838 45.360  1.00 79.32  ?  637 MET D SD  1 
ATOM   19579 C  CE  . MET D  1  637 ? 12.908  114.067 45.410  1.00 86.51  ?  637 MET D CE  1 
ATOM   19580 N  N   . LYS D  1  638 ? 14.433  112.264 51.094  1.00 84.09  ?  638 LYS D N   1 
ATOM   19581 C  CA  . LYS D  1  638 ? 14.668  112.967 52.363  1.00 89.92  ?  638 LYS D CA  1 
ATOM   19582 C  C   . LYS D  1  638 ? 15.435  114.286 52.194  1.00 87.10  ?  638 LYS D C   1 
ATOM   19583 O  O   . LYS D  1  638 ? 15.068  115.291 52.800  1.00 87.20  ?  638 LYS D O   1 
ATOM   19584 C  CB  . LYS D  1  638 ? 15.411  112.061 53.362  1.00 78.33  ?  638 LYS D CB  1 
ATOM   19585 C  CG  . LYS D  1  638 ? 15.304  112.525 54.811  1.00 91.15  ?  638 LYS D CG  1 
ATOM   19586 C  CD  . LYS D  1  638 ? 16.112  111.646 55.748  1.00 95.50  ?  638 LYS D CD  1 
ATOM   19587 C  CE  . LYS D  1  638 ? 16.189  112.208 57.149  1.00 86.37  ?  638 LYS D CE  1 
ATOM   19588 N  NZ  . LYS D  1  638 ? 17.222  111.522 57.975  1.00 94.13  ?  638 LYS D NZ  1 
ATOM   19589 N  N   . GLY D  1  639 ? 16.483  114.270 51.379  1.00 82.41  ?  639 GLY D N   1 
ATOM   19590 C  CA  . GLY D  1  639 ? 17.302  115.450 51.135  1.00 89.15  ?  639 GLY D CA  1 
ATOM   19591 C  C   . GLY D  1  639 ? 16.603  116.580 50.404  1.00 90.29  ?  639 GLY D C   1 
ATOM   19592 O  O   . GLY D  1  639 ? 17.091  117.711 50.405  1.00 95.66  ?  639 GLY D O   1 
ATOM   19593 N  N   . GLU D  1  640 ? 15.461  116.292 49.771  1.00 79.38  ?  640 GLU D N   1 
ATOM   19594 C  CA  . GLU D  1  640 ? 14.706  117.299 49.028  1.00 86.78  ?  640 GLU D CA  1 
ATOM   19595 C  C   . GLU D  1  640 ? 13.409  117.732 49.738  1.00 99.90  ?  640 GLU D C   1 
ATOM   19596 O  O   . GLU D  1  640 ? 12.722  118.623 49.244  1.00 106.79 ?  640 GLU D O   1 
ATOM   19597 C  CB  . GLU D  1  640 ? 14.375  116.765 47.627  1.00 70.15  ?  640 GLU D CB  1 
ATOM   19598 C  CG  . GLU D  1  640 ? 15.537  116.800 46.646  1.00 89.25  ?  640 GLU D CG  1 
ATOM   19599 C  CD  . GLU D  1  640 ? 16.483  115.616 46.697  1.00 94.59  ?  640 GLU D CD  1 
ATOM   19600 O  OE1 . GLU D  1  640 ? 16.016  114.472 46.495  1.00 90.25  ?  640 GLU D OE1 1 
ATOM   19601 O  OE2 . GLU D  1  640 ? 17.695  115.832 46.926  1.00 88.00  ?  640 GLU D OE2 1 
ATOM   19602 N  N   . GLY D  1  641 ? 13.089  117.124 50.877  1.00 92.30  ?  641 GLY D N   1 
ATOM   19603 C  CA  . GLY D  1  641 ? 11.883  117.466 51.621  1.00 97.42  ?  641 GLY D CA  1 
ATOM   19604 C  C   . GLY D  1  641 ? 10.878  116.338 51.737  1.00 93.31  ?  641 GLY D C   1 
ATOM   19605 O  O   . GLY D  1  641 ? 9.687   116.586 51.939  1.00 101.70 ?  641 GLY D O   1 
ATOM   19606 N  N   . GLY D  1  642 ? 11.349  115.103 51.613  1.00 87.84  ?  642 GLY D N   1 
ATOM   19607 C  CA  . GLY D  1  642 ? 10.495  113.931 51.730  1.00 97.61  ?  642 GLY D CA  1 
ATOM   19608 C  C   . GLY D  1  642 ? 9.507   113.747 50.599  1.00 94.09  ?  642 GLY D C   1 
ATOM   19609 O  O   . GLY D  1  642 ? 9.475   114.529 49.644  1.00 82.83  ?  642 GLY D O   1 
ATOM   19610 N  N   . LEU D  1  643 ? 8.686   112.693 50.715  1.00 92.16  ?  643 LEU D N   1 
ATOM   19611 C  CA  . LEU D  1  643 ? 7.669   112.339 49.721  1.00 93.66  ?  643 LEU D CA  1 
ATOM   19612 C  C   . LEU D  1  643 ? 6.683   113.474 49.389  1.00 94.28  ?  643 LEU D C   1 
ATOM   19613 O  O   . LEU D  1  643 ? 5.974   113.379 48.385  1.00 90.55  ?  643 LEU D O   1 
ATOM   19614 C  CB  . LEU D  1  643 ? 6.998   110.995 50.071  1.00 83.06  ?  643 LEU D CB  1 
ATOM   19615 C  CG  . LEU D  1  643 ? 6.289   110.881 51.429  1.00 89.64  ?  643 LEU D CG  1 
ATOM   19616 C  CD1 . LEU D  1  643 ? 4.901   111.499 51.384  1.00 91.67  ?  643 LEU D CD1 1 
ATOM   19617 C  CD2 . LEU D  1  643 ? 6.216   109.428 51.883  1.00 96.98  ?  643 LEU D CD2 1 
ATOM   19618 N  N   . GLY D  1  644 ? 6.655   114.535 50.191  1.00 86.76  ?  644 GLY D N   1 
ATOM   19619 C  CA  . GLY D  1  644 ? 5.730   115.639 49.966  1.00 88.99  ?  644 GLY D CA  1 
ATOM   19620 C  C   . GLY D  1  644 ? 5.869   116.248 48.581  1.00 104.13 ?  644 GLY D C   1 
ATOM   19621 O  O   . GLY D  1  644 ? 5.039   117.070 48.185  1.00 105.41 ?  644 GLY D O   1 
ATOM   19622 N  N   . ARG D  1  645 ? 6.926   115.853 47.832  1.00 95.08  ?  645 ARG D N   1 
ATOM   19623 C  CA  . ARG D  1  645 ? 7.186   116.335 46.478  1.00 89.04  ?  645 ARG D CA  1 
ATOM   19624 C  C   . ARG D  1  645 ? 6.417   115.552 45.412  1.00 87.96  ?  645 ARG D C   1 
ATOM   19625 O  O   . ARG D  1  645 ? 6.404   115.984 44.266  1.00 83.36  ?  645 ARG D O   1 
ATOM   19626 C  CB  . ARG D  1  645 ? 8.683   116.243 46.160  1.00 79.26  ?  645 ARG D CB  1 
ATOM   19627 C  CG  . ARG D  1  645 ? 9.564   117.081 47.069  1.00 87.91  ?  645 ARG D CG  1 
ATOM   19628 C  CD  . ARG D  1  645 ? 9.627   118.535 46.644  1.00 75.02  ?  645 ARG D CD  1 
ATOM   19629 N  NE  . ARG D  1  645 ? 10.712  119.226 47.339  1.00 86.13  ?  645 ARG D NE  1 
ATOM   19630 C  CZ  . ARG D  1  645 ? 10.909  120.540 47.319  1.00 90.18  ?  645 ARG D CZ  1 
ATOM   19631 N  NH1 . ARG D  1  645 ? 10.093  121.332 46.632  1.00 94.39  ?  645 ARG D NH1 1 
ATOM   19632 N  NH2 . ARG D  1  645 ? 11.927  121.074 47.982  1.00 84.46  ?  645 ARG D NH2 1 
ATOM   19633 N  N   . ILE D  1  646 ? 5.785   114.411 45.759  1.00 93.20  ?  646 ILE D N   1 
ATOM   19634 C  CA  . ILE D  1  646 ? 5.042   113.627 44.770  1.00 84.10  ?  646 ILE D CA  1 
ATOM   19635 C  C   . ILE D  1  646 ? 3.836   114.442 44.324  1.00 81.96  ?  646 ILE D C   1 
ATOM   19636 O  O   . ILE D  1  646 ? 2.966   114.720 45.137  1.00 89.35  ?  646 ILE D O   1 
ATOM   19637 C  CB  . ILE D  1  646 ? 4.608   112.248 45.324  1.00 72.20  ?  646 ILE D CB  1 
ATOM   19638 C  CG1 . ILE D  1  646 ? 5.830   111.417 45.768  1.00 66.96  ?  646 ILE D CG1 1 
ATOM   19639 C  CG2 . ILE D  1  646 ? 3.804   111.495 44.261  1.00 80.50  ?  646 ILE D CG2 1 
ATOM   19640 C  CD1 . ILE D  1  646 ? 5.510   110.288 46.708  1.00 81.41  ?  646 ILE D CD1 1 
ATOM   19641 N  N   . VAL D  1  647 ? 3.789   114.841 43.049  1.00 79.41  ?  647 VAL D N   1 
ATOM   19642 C  CA  . VAL D  1  647 ? 2.683   115.654 42.533  1.00 86.53  ?  647 VAL D CA  1 
ATOM   19643 C  C   . VAL D  1  647 ? 1.821   114.924 41.502  1.00 87.82  ?  647 VAL D C   1 
ATOM   19644 O  O   . VAL D  1  647 ? 0.734   115.404 41.184  1.00 98.85  ?  647 VAL D O   1 
ATOM   19645 C  CB  . VAL D  1  647 ? 3.174   117.010 41.967  1.00 85.12  ?  647 VAL D CB  1 
ATOM   19646 C  CG1 . VAL D  1  647 ? 3.892   117.829 43.033  1.00 81.22  ?  647 VAL D CG1 1 
ATOM   19647 C  CG2 . VAL D  1  647 ? 4.052   116.828 40.732  1.00 87.91  ?  647 VAL D CG2 1 
ATOM   19648 N  N   . TRP D  1  648 ? 2.289   113.792 40.967  1.00 84.94  ?  648 TRP D N   1 
ATOM   19649 C  CA  . TRP D  1  648 ? 1.526   113.047 39.971  1.00 86.08  ?  648 TRP D CA  1 
ATOM   19650 C  C   . TRP D  1  648 ? 1.972   111.600 39.962  1.00 86.19  ?  648 TRP D C   1 
ATOM   19651 O  O   . TRP D  1  648 ? 3.166   111.329 40.010  1.00 83.67  ?  648 TRP D O   1 
ATOM   19652 C  CB  . TRP D  1  648 ? 1.744   113.662 38.576  1.00 82.37  ?  648 TRP D CB  1 
ATOM   19653 C  CG  . TRP D  1  648 ? 0.869   113.105 37.493  1.00 74.38  ?  648 TRP D CG  1 
ATOM   19654 C  CD1 . TRP D  1  648 ? -0.258  113.674 36.983  1.00 86.56  ?  648 TRP D CD1 1 
ATOM   19655 C  CD2 . TRP D  1  648 ? 1.103   111.918 36.720  1.00 75.59  ?  648 TRP D CD2 1 
ATOM   19656 N  NE1 . TRP D  1  648 ? -0.760  112.901 35.964  1.00 97.89  ?  648 TRP D NE1 1 
ATOM   19657 C  CE2 . TRP D  1  648 ? 0.059   111.818 35.780  1.00 90.34  ?  648 TRP D CE2 1 
ATOM   19658 C  CE3 . TRP D  1  648 ? 2.099   110.934 36.724  1.00 82.58  ?  648 TRP D CE3 1 
ATOM   19659 C  CZ2 . TRP D  1  648 ? -0.032  110.760 34.875  1.00 89.27  ?  648 TRP D CZ2 1 
ATOM   19660 C  CZ3 . TRP D  1  648 ? 1.998   109.880 35.838  1.00 87.25  ?  648 TRP D CZ3 1 
ATOM   19661 C  CH2 . TRP D  1  648 ? 0.948   109.806 34.920  1.00 81.33  ?  648 TRP D CH2 1 
ATOM   19662 N  N   . MET D  1  649 ? 1.024   110.671 39.904  1.00 81.58  ?  649 MET D N   1 
ATOM   19663 C  CA  . MET D  1  649 ? 1.332   109.243 39.840  1.00 87.82  ?  649 MET D CA  1 
ATOM   19664 C  C   . MET D  1  649 ? 0.089   108.506 39.335  1.00 83.35  ?  649 MET D C   1 
ATOM   19665 O  O   . MET D  1  649 ? -1.020  108.972 39.596  1.00 89.90  ?  649 MET D O   1 
ATOM   19666 C  CB  . MET D  1  649 ? 1.805   108.696 41.198  1.00 79.93  ?  649 MET D CB  1 
ATOM   19667 C  CG  . MET D  1  649 ? 0.706   108.546 42.213  1.00 84.29  ?  649 MET D CG  1 
ATOM   19668 S  SD  . MET D  1  649 ? 1.342   108.433 43.897  1.00 110.08 ?  649 MET D SD  1 
ATOM   19669 C  CE  . MET D  1  649 ? 1.917   106.763 43.908  1.00 98.38  ?  649 MET D CE  1 
ATOM   19670 N  N   . PRO D  1  650 ? 0.214   107.384 38.601  1.00 81.42  ?  650 PRO D N   1 
ATOM   19671 C  CA  . PRO D  1  650 ? -0.996  106.706 38.113  1.00 80.79  ?  650 PRO D CA  1 
ATOM   19672 C  C   . PRO D  1  650 ? -2.009  106.393 39.210  1.00 99.09  ?  650 PRO D C   1 
ATOM   19673 O  O   . PRO D  1  650 ? -1.628  106.134 40.348  1.00 105.05 ?  650 PRO D O   1 
ATOM   19674 C  CB  . PRO D  1  650 ? -0.454  105.425 37.477  1.00 89.35  ?  650 PRO D CB  1 
ATOM   19675 C  CG  . PRO D  1  650 ? 0.933   105.740 37.118  1.00 83.70  ?  650 PRO D CG  1 
ATOM   19676 C  CD  . PRO D  1  650 ? 1.432   106.674 38.170  1.00 85.72  ?  650 PRO D CD  1 
ATOM   19677 N  N   . LYS D  1  651 ? -3.307  106.418 38.864  1.00 110.89 ?  651 LYS D N   1 
ATOM   19678 C  CA  . LYS D  1  651 ? -4.387  106.119 39.805  1.00 104.02 ?  651 LYS D CA  1 
ATOM   19679 C  C   . LYS D  1  651 ? -4.186  104.710 40.372  1.00 106.80 ?  651 LYS D C   1 
ATOM   19680 O  O   . LYS D  1  651 ? -4.386  104.499 41.564  1.00 112.89 ?  651 LYS D O   1 
ATOM   19681 C  CB  . LYS D  1  651 ? -5.751  106.240 39.094  1.00 110.16 ?  651 LYS D CB  1 
ATOM   19682 C  CG  . LYS D  1  651 ? -6.965  105.772 39.906  1.00 122.37 ?  651 LYS D CG  1 
ATOM   19683 C  CD  . LYS D  1  651 ? -7.427  106.785 40.952  1.00 130.02 ?  651 LYS D CD  1 
ATOM   19684 C  CE  . LYS D  1  651 ? -8.884  106.618 41.340  1.00 120.53 ?  651 LYS D CE  1 
ATOM   19685 N  NZ  . LYS D  1  651 ? -9.230  105.220 41.718  1.00 124.44 ?  651 LYS D NZ  1 
ATOM   19686 N  N   . GLU D  1  652 ? -3.745  103.759 39.530  1.00 96.30  ?  652 GLU D N   1 
ATOM   19687 C  CA  . GLU D  1  652 ? -3.500  102.385 39.961  1.00 106.09 ?  652 GLU D CA  1 
ATOM   19688 C  C   . GLU D  1  652 ? -2.496  102.340 41.117  1.00 106.99 ?  652 GLU D C   1 
ATOM   19689 O  O   . GLU D  1  652 ? -2.767  101.723 42.145  1.00 114.76 ?  652 GLU D O   1 
ATOM   19690 C  CB  . GLU D  1  652 ? -2.964  101.544 38.792  1.00 122.61 ?  652 GLU D CB  1 
ATOM   19691 C  CG  . GLU D  1  652 ? -3.962  101.317 37.676  1.00 137.37 ?  652 GLU D CG  1 
ATOM   19692 C  CD  . GLU D  1  652 ? -3.447  100.379 36.603  1.00 171.49 ?  652 GLU D CD  1 
ATOM   19693 O  OE1 . GLU D  1  652 ? -2.276  100.539 36.185  1.00 132.71 ?  652 GLU D OE1 1 
ATOM   19694 O  OE2 . GLU D  1  652 ? -4.212  99.480  36.183  1.00 182.46 ?  652 GLU D OE2 1 
ATOM   19695 N  N   . LEU D  1  653 ? -1.345  103.000 40.949  1.00 95.75  ?  653 LEU D N   1 
ATOM   19696 C  CA  . LEU D  1  653 ? -0.306  103.025 41.971  1.00 89.43  ?  653 LEU D CA  1 
ATOM   19697 C  C   . LEU D  1  653 ? -0.757  103.829 43.190  1.00 98.52  ?  653 LEU D C   1 
ATOM   19698 O  O   . LEU D  1  653 ? -0.515  103.411 44.319  1.00 99.24  ?  653 LEU D O   1 
ATOM   19699 C  CB  . LEU D  1  653 ? 0.983   103.614 41.374  1.00 83.06  ?  653 LEU D CB  1 
ATOM   19700 C  CG  . LEU D  1  653 ? 2.279   103.383 42.150  1.00 79.18  ?  653 LEU D CG  1 
ATOM   19701 C  CD1 . LEU D  1  653 ? 2.705   101.914 42.113  1.00 99.99  ?  653 LEU D CD1 1 
ATOM   19702 C  CD2 . LEU D  1  653 ? 3.393   104.241 41.587  1.00 78.67  ?  653 LEU D CD2 1 
ATOM   19703 N  N   . LYS D  1  654 ? -1.431  104.965 42.971  1.00 96.27  ?  654 LYS D N   1 
ATOM   19704 C  CA  . LYS D  1  654 ? -1.921  105.809 44.060  1.00 89.37  ?  654 LYS D CA  1 
ATOM   19705 C  C   . LYS D  1  654 ? -2.849  105.023 44.994  1.00 112.37 ?  654 LYS D C   1 
ATOM   19706 O  O   . LYS D  1  654 ? -2.700  105.101 46.212  1.00 117.58 ?  654 LYS D O   1 
ATOM   19707 C  CB  . LYS D  1  654 ? -2.657  107.032 43.490  1.00 93.62  ?  654 LYS D CB  1 
ATOM   19708 C  CG  . LYS D  1  654 ? -3.172  108.000 44.558  1.00 100.49 ?  654 LYS D CG  1 
ATOM   19709 C  CD  . LYS D  1  654 ? -2.956  109.468 44.194  1.00 102.71 ?  654 LYS D CD  1 
ATOM   19710 C  CE  . LYS D  1  654 ? -3.949  109.991 43.181  1.00 111.51 ?  654 LYS D CE  1 
ATOM   19711 N  NZ  . LYS D  1  654 ? -5.153  110.582 43.826  1.00 100.84 ?  654 LYS D NZ  1 
ATOM   19712 N  N   . ASP D  1  655 ? -3.797  104.261 44.426  1.00 119.88 ?  655 ASP D N   1 
ATOM   19713 C  CA  . ASP D  1  655 ? -4.730  103.461 45.219  1.00 117.34 ?  655 ASP D CA  1 
ATOM   19714 C  C   . ASP D  1  655 ? -3.977  102.378 45.983  1.00 114.24 ?  655 ASP D C   1 
ATOM   19715 O  O   . ASP D  1  655 ? -4.246  102.162 47.163  1.00 133.33 ?  655 ASP D O   1 
ATOM   19716 C  CB  . ASP D  1  655 ? -5.795  102.799 44.318  1.00 125.61 ?  655 ASP D CB  1 
ATOM   19717 C  CG  . ASP D  1  655 ? -6.822  103.746 43.737  1.00 122.49 ?  655 ASP D CG  1 
ATOM   19718 O  OD1 . ASP D  1  655 ? -7.022  104.835 44.319  1.00 115.23 ?  655 ASP D OD1 1 
ATOM   19719 O  OD2 . ASP D  1  655 ? -7.432  103.396 42.701  1.00 123.57 ?  655 ASP D OD2 1 
ATOM   19720 N  N   . PHE D  1  656 ? -3.036  101.697 45.317  1.00 92.81  ?  656 PHE D N   1 
ATOM   19721 C  CA  . PHE D  1  656 ? -2.256  100.634 45.940  1.00 87.47  ?  656 PHE D CA  1 
ATOM   19722 C  C   . PHE D  1  656 ? -1.494  101.145 47.163  1.00 92.71  ?  656 PHE D C   1 
ATOM   19723 O  O   . PHE D  1  656 ? -1.555  100.527 48.225  1.00 108.43 ?  656 PHE D O   1 
ATOM   19724 C  CB  . PHE D  1  656 ? -1.283  100.034 44.917  1.00 100.38 ?  656 PHE D CB  1 
ATOM   19725 C  CG  . PHE D  1  656 ? -0.549  98.807  45.397  1.00 110.26 ?  656 PHE D CG  1 
ATOM   19726 C  CD1 . PHE D  1  656 ? 0.561   98.920  46.215  1.00 102.52 ?  656 PHE D CD1 1 
ATOM   19727 C  CD2 . PHE D  1  656 ? -0.942  97.544  44.995  1.00 115.09 ?  656 PHE D CD2 1 
ATOM   19728 C  CE1 . PHE D  1  656 ? 1.242   97.794  46.647  1.00 109.25 ?  656 PHE D CE1 1 
ATOM   19729 C  CE2 . PHE D  1  656 ? -0.256  96.418  45.425  1.00 130.02 ?  656 PHE D CE2 1 
ATOM   19730 C  CZ  . PHE D  1  656 ? 0.832   96.549  46.247  1.00 135.04 ?  656 PHE D CZ  1 
ATOM   19731 N  N   . VAL D  1  657 ? -0.794  102.275 47.022  1.00 92.21  ?  657 VAL D N   1 
ATOM   19732 C  CA  . VAL D  1  657 ? -0.024  102.835 48.132  1.00 93.45  ?  657 VAL D CA  1 
ATOM   19733 C  C   . VAL D  1  657 ? -0.768  103.913 48.928  1.00 90.88  ?  657 VAL D C   1 
ATOM   19734 O  O   . VAL D  1  657 ? -0.123  104.697 49.617  1.00 94.55  ?  657 VAL D O   1 
ATOM   19735 C  CB  . VAL D  1  657 ? 1.405   103.266 47.697  1.00 92.28  ?  657 VAL D CB  1 
ATOM   19736 C  CG1 . VAL D  1  657 ? 2.145   102.115 47.022  1.00 81.75  ?  657 VAL D CG1 1 
ATOM   19737 C  CG2 . VAL D  1  657 ? 1.383   104.500 46.797  1.00 92.64  ?  657 VAL D CG2 1 
ATOM   19738 N  N   . ALA D  1  658 ? -2.097  103.945 48.833  1.00 92.31  ?  658 ALA D N   1 
ATOM   19739 C  CA  . ALA D  1  658 ? -2.868  105.022 49.498  1.00 97.75  ?  658 ALA D CA  1 
ATOM   19740 C  C   . ALA D  1  658 ? -2.540  105.103 50.994  1.00 110.78 ?  658 ALA D C   1 
ATOM   19741 O  O   . ALA D  1  658 ? -2.020  106.152 51.422  1.00 110.83 ?  658 ALA D O   1 
ATOM   19742 C  CB  . ALA D  1  658 ? -4.343  104.796 49.276  1.00 105.86 ?  658 ALA D CB  1 
ATOM   19743 N  N   . GLU D  1  659 ? -2.831  104.048 51.760  1.00 125.69 ?  659 GLU D N   1 
ATOM   19744 C  CA  . GLU D  1  659 ? -2.658  104.105 53.239  1.00 132.90 ?  659 GLU D CA  1 
ATOM   19745 C  C   . GLU D  1  659 ? -1.182  104.150 53.649  1.00 136.83 ?  659 GLU D C   1 
ATOM   19746 O  O   . GLU D  1  659 ? -0.831  105.040 54.448  1.00 134.61 ?  659 GLU D O   1 
ATOM   19747 C  CB  . GLU D  1  659 ? -3.333  102.895 53.888  1.00 126.90 ?  659 GLU D CB  1 
ATOM   19748 C  CG  . GLU D  1  659 ? -4.674  102.550 53.268  1.00 138.91 ?  659 GLU D CG  1 
ATOM   19749 C  CD  . GLU D  1  659 ? -5.693  101.995 54.249  1.00 163.06 ?  659 GLU D CD  1 
ATOM   19750 O  OE1 . GLU D  1  659 ? -5.273  101.436 55.281  1.00 170.80 ?  659 GLU D OE1 1 
ATOM   19751 O  OE2 . GLU D  1  659 ? -6.903  102.125 53.977  1.00 170.54 ?  659 GLU D OE2 1 
ATOM   19752 N  N   . LYS D  1  660 ? -0.353  103.232 53.152  1.00 120.82 ?  660 LYS D N   1 
ATOM   19753 C  CA  . LYS D  1  660 ? 1.060   103.184 53.620  1.00 106.35 ?  660 LYS D CA  1 
ATOM   19754 C  C   . LYS D  1  660 ? 1.678   104.587 53.554  1.00 114.91 ?  660 LYS D C   1 
ATOM   19755 O  O   . LYS D  1  660 ? 2.541   104.883 54.401  1.00 117.10 ?  660 LYS D O   1 
ATOM   19756 C  CB  . LYS D  1  660 ? 1.859   102.167 52.799  1.00 94.96  ?  660 LYS D CB  1 
ATOM   19757 C  CG  . LYS D  1  660 ? 1.802   100.731 53.306  1.00 106.12 ?  660 LYS D CG  1 
ATOM   19758 C  CD  . LYS D  1  660 ? 3.167   100.091 53.468  1.00 126.88 ?  660 LYS D CD  1 
ATOM   19759 C  CE  . LYS D  1  660 ? 3.150   98.583  53.321  1.00 111.49 ?  660 LYS D CE  1 
ATOM   19760 N  NZ  . LYS D  1  660 ? 2.501   97.927  54.480  1.00 117.17 ?  660 LYS D NZ  1 
ATOM   19761 N  N   . LEU D  1  661 ? 1.255   105.427 52.600  1.00 112.47 ?  661 LEU D N   1 
ATOM   19762 C  CA  . LEU D  1  661 ? 1.879   106.772 52.427  1.00 114.13 ?  661 LEU D CA  1 
ATOM   19763 C  C   . LEU D  1  661 ? 1.191   107.849 53.278  1.00 125.71 ?  661 LEU D C   1 
ATOM   19764 O  O   . LEU D  1  661 ? 1.913   108.574 53.989  1.00 131.38 ?  661 LEU D O   1 
ATOM   19765 C  CB  . LEU D  1  661 ? 1.824   107.180 50.947  1.00 101.01 ?  661 LEU D CB  1 
ATOM   19766 C  CG  . LEU D  1  661 ? 2.659   108.406 50.562  1.00 113.73 ?  661 LEU D CG  1 
ATOM   19767 C  CD1 . LEU D  1  661 ? 3.257   108.284 49.159  1.00 110.20 ?  661 LEU D CD1 1 
ATOM   19768 C  CD2 . LEU D  1  661 ? 1.832   109.676 50.678  1.00 115.29 ?  661 LEU D CD2 1 
ATOM   19769 N  N   . ASN D  1  662 ? -0.139  107.962 53.202  1.00 124.25 ?  662 ASN D N   1 
ATOM   19770 C  CA  . ASN D  1  662 ? -0.882  108.965 53.958  1.00 128.24 ?  662 ASN D CA  1 
ATOM   19771 C  C   . ASN D  1  662 ? -0.445  108.883 55.423  1.00 131.33 ?  662 ASN D C   1 
ATOM   19772 O  O   . ASN D  1  662 ? -0.360  109.909 56.092  1.00 137.15 ?  662 ASN D O   1 
ATOM   19773 C  CB  . ASN D  1  662 ? -2.381  108.725 53.821  1.00 121.08 ?  662 ASN D CB  1 
ATOM   19774 C  CG  . ASN D  1  662 ? -2.894  109.018 52.434  1.00 118.30 ?  662 ASN D CG  1 
ATOM   19775 O  OD1 . ASN D  1  662 ? -2.362  109.873 51.723  1.00 112.56 ?  662 ASN D OD1 1 
ATOM   19776 N  ND2 . ASN D  1  662 ? -3.936  108.318 52.009  1.00 123.16 ?  662 ASN D ND2 1 
ATOM   19777 N  N   . LYS D  1  663 ? -0.090  107.673 55.886  1.00 120.10 ?  663 LYS D N   1 
ATOM   19778 C  CA  . LYS D  1  663 ? 0.314   107.438 57.305  1.00 128.80 ?  663 LYS D CA  1 
ATOM   19779 C  C   . LYS D  1  663 ? 1.703   108.030 57.579  1.00 130.79 ?  663 LYS D C   1 
ATOM   19780 O  O   . LYS D  1  663 ? 2.051   108.208 58.751  1.00 129.05 ?  663 LYS D O   1 
ATOM   19781 C  CB  . LYS D  1  663 ? 0.263   105.932 57.594  1.00 124.30 ?  663 LYS D CB  1 
ATOM   19782 C  CG  . LYS D  1  663 ? 0.646   105.483 59.001  1.00 134.28 ?  663 LYS D CG  1 
ATOM   19783 C  CD  . LYS D  1  663 ? 1.322   104.130 59.047  1.00 130.27 ?  663 LYS D CD  1 
ATOM   19784 C  CE  . LYS D  1  663 ? 1.806   103.770 60.436  1.00 142.58 ?  663 LYS D CE  1 
ATOM   19785 N  NZ  . LYS D  1  663 ? 1.874   102.299 60.637  1.00 160.80 ?  663 LYS D NZ  1 
ATOM   19786 N  N   . THR D  1  664 ? 2.485   108.305 56.542  1.00 132.22 ?  664 THR D N   1 
ATOM   19787 C  CA  . THR D  1  664 ? 3.828   108.849 56.709  1.00 124.84 ?  664 THR D CA  1 
ATOM   19788 C  C   . THR D  1  664 ? 3.848   110.156 55.912  1.00 129.35 ?  664 THR D C   1 
ATOM   19789 O  O   . THR D  1  664 ? 4.910   110.557 55.449  1.00 140.17 ?  664 THR D O   1 
ATOM   19790 C  CB  . THR D  1  664 ? 4.971   107.919 56.275  1.00 108.36 ?  664 THR D CB  1 
ATOM   19791 O  OG1 . THR D  1  664 ? 4.846   107.632 54.882  1.00 114.95 ?  664 THR D OG1 1 
ATOM   19792 C  CG2 . THR D  1  664 ? 5.011   106.623 57.076  1.00 110.54 ?  664 THR D CG2 1 
ATOM   19793 N  N   . ALA D  1  665 ? 2.694   110.824 55.748  1.00 127.96 ?  665 ALA D N   1 
ATOM   19794 C  CA  . ALA D  1  665 ? 2.645   112.090 55.012  1.00 131.18 ?  665 ALA D CA  1 
ATOM   19795 C  C   . ALA D  1  665 ? 3.114   113.203 55.945  1.00 153.00 ?  665 ALA D C   1 
ATOM   19796 O  O   . ALA D  1  665 ? 2.289   113.832 56.610  1.00 158.72 ?  665 ALA D O   1 
ATOM   19797 C  CB  . ALA D  1  665 ? 1.230   112.367 54.529  1.00 128.01 ?  665 ALA D CB  1 
ATOM   19798 N  N   . LYS D  1  666 ? 4.448   113.418 56.022  1.00 157.26 ?  666 LYS D N   1 
ATOM   19799 C  CA  . LYS D  1  666 ? 5.077   114.414 56.905  1.00 143.65 ?  666 LYS D CA  1 
ATOM   19800 C  C   . LYS D  1  666 ? 4.693   114.076 58.354  1.00 149.43 ?  666 LYS D C   1 
ATOM   19801 O  O   . LYS D  1  666 ? 4.362   114.966 59.134  1.00 154.46 ?  666 LYS D O   1 
ATOM   19802 C  CB  . LYS D  1  666 ? 4.635   115.848 56.553  1.00 121.56 ?  666 LYS D CB  1 
ATOM   19803 C  CG  . LYS D  1  666 ? 4.757   116.232 55.077  1.00 121.73 ?  666 LYS D CG  1 
ATOM   19804 C  CD  . LYS D  1  666 ? 6.187   116.591 54.649  1.00 104.17 ?  666 LYS D CD  1 
ATOM   19805 C  CE  . LYS D  1  666 ? 6.710   115.707 53.542  1.00 87.73  ?  666 LYS D CE  1 
ATOM   19806 N  NZ  . LYS D  1  666 ? 7.058   114.343 54.018  1.00 103.15 ?  666 LYS D NZ  1 
ATOM   19807 N  N   . GLU D  1  667 ? 4.728   112.773 58.695  1.00 149.44 ?  667 GLU D N   1 
ATOM   19808 C  CA  . GLU D  1  667 ? 4.350   112.237 60.002  1.00 123.42 ?  667 GLU D CA  1 
ATOM   19809 C  C   . GLU D  1  667 ? 2.824   112.266 60.219  1.00 145.11 ?  667 GLU D C   1 
ATOM   19810 O  O   . GLU D  1  667 ? 2.377   112.156 61.356  1.00 182.52 ?  667 GLU D O   1 
ATOM   19811 C  CB  . GLU D  1  667 ? 5.094   112.953 61.144  1.00 123.35 ?  667 GLU D CB  1 
ATOM   19812 C  CG  . GLU D  1  667 ? 6.593   112.715 61.126  1.00 149.19 ?  667 GLU D CG  1 
ATOM   19813 C  CD  . GLU D  1  667 ? 6.995   111.261 61.280  1.00 169.82 ?  667 GLU D CD  1 
ATOM   19814 O  OE1 . GLU D  1  667 ? 6.340   110.543 62.070  1.00 144.32 ?  667 GLU D OE1 1 
ATOM   19815 O  OE2 . GLU D  1  667 ? 7.963   110.838 60.607  1.00 174.75 ?  667 GLU D OE2 1 
ATOM   19816 N  N   . LEU D  1  668 ? 2.065   112.421 59.124  1.00 147.36 ?  668 LEU D N   1 
ATOM   19817 C  CA  . LEU D  1  668 ? 0.571   112.412 59.170  1.00 167.04 ?  668 LEU D CA  1 
ATOM   19818 C  C   . LEU D  1  668 ? 0.066   113.693 59.858  1.00 197.51 ?  668 LEU D C   1 
ATOM   19819 O  O   . LEU D  1  668 ? -0.909  114.277 59.347  1.00 215.20 ?  668 LEU D O   1 
ATOM   19820 C  CB  . LEU D  1  668 ? 0.071   111.091 59.774  1.00 174.38 ?  668 LEU D CB  1 
ATOM   19821 C  CG  . LEU D  1  668 ? -1.443  110.978 59.946  1.00 179.07 ?  668 LEU D CG  1 
ATOM   19822 C  CD1 . LEU D  1  668 ? -2.150  111.035 58.601  1.00 178.49 ?  668 LEU D CD1 1 
ATOM   19823 C  CD2 . LEU D  1  668 ? -1.809  109.701 60.687  1.00 166.77 ?  668 LEU D CD2 1 
ATOM   19824 N  N   . TYR D  1  669 ? 0.699   114.122 60.956  1.00 203.95 ?  669 TYR D N   1 
ATOM   19825 C  CA  . TYR D  1  669 ? 0.274   115.372 61.640  1.00 208.92 ?  669 TYR D CA  1 
ATOM   19826 C  C   . TYR D  1  669 ? 0.256   116.583 60.702  1.00 205.84 ?  669 TYR D C   1 
ATOM   19827 O  O   . TYR D  1  669 ? -0.728  117.348 60.736  1.00 183.29 ?  669 TYR D O   1 
ATOM   19828 C  CB  . TYR D  1  669 ? 1.159   115.636 62.860  1.00 203.51 ?  669 TYR D CB  1 
ATOM   19829 C  CG  . TYR D  1  669 ? 2.411   116.421 62.564  1.00 206.68 ?  669 TYR D CG  1 
ATOM   19830 C  CD1 . TYR D  1  669 ? 3.533   115.805 62.037  1.00 194.47 ?  669 TYR D CD1 1 
ATOM   19831 C  CD2 . TYR D  1  669 ? 2.473   117.784 62.801  1.00 199.03 ?  669 TYR D CD2 1 
ATOM   19832 C  CE1 . TYR D  1  669 ? 4.686   116.519 61.758  1.00 183.82 ?  669 TYR D CE1 1 
ATOM   19833 C  CE2 . TYR D  1  669 ? 3.618   118.514 62.527  1.00 193.77 ?  669 TYR D CE2 1 
ATOM   19834 C  CZ  . TYR D  1  669 ? 4.729   117.879 62.003  1.00 176.58 ?  669 TYR D CZ  1 
ATOM   19835 O  OH  . TYR D  1  669 ? 5.869   118.596 61.730  1.00 155.77 ?  669 TYR D OH  1 
ATOM   19836 N  N   . ASN D  1  670 ? 1.300   116.774 59.887  1.00 212.94 ?  670 ASN D N   1 
ATOM   19837 C  CA  . ASN D  1  670 ? 1.344   118.000 59.039  1.00 203.18 ?  670 ASN D CA  1 
ATOM   19838 C  C   . ASN D  1  670 ? 0.202   117.935 58.013  1.00 194.32 ?  670 ASN D C   1 
ATOM   19839 O  O   . ASN D  1  670 ? -0.518  118.944 57.885  1.00 182.71 ?  670 ASN D O   1 
ATOM   19840 C  CB  . ASN D  1  670 ? 2.722   118.257 58.414  1.00 193.67 ?  670 ASN D CB  1 
ATOM   19841 C  CG  . ASN D  1  670 ? 2.755   119.470 57.510  1.00 194.92 ?  670 ASN D CG  1 
ATOM   19842 O  OD1 . ASN D  1  670 ? 1.947   120.385 57.656  1.00 198.15 ?  670 ASN D OD1 1 
ATOM   19843 N  ND2 . ASN D  1  670 ? 3.691   119.489 56.575  1.00 178.96 ?  670 ASN D ND2 1 
ATOM   19844 N  N   . ILE D  1  671 ? 0.035   116.803 57.317  1.00 169.48 ?  671 ILE D N   1 
ATOM   19845 C  CA  . ILE D  1  671 ? -1.017  116.739 56.258  1.00 155.90 ?  671 ILE D CA  1 
ATOM   19846 C  C   . ILE D  1  671 ? -1.696  115.367 56.301  1.00 152.74 ?  671 ILE D C   1 
ATOM   19847 O  O   . ILE D  1  671 ? -0.992  114.367 56.543  1.00 132.94 ?  671 ILE D O   1 
ATOM   19848 C  CB  . ILE D  1  671 ? -0.415  117.035 54.870  1.00 141.65 ?  671 ILE D CB  1 
ATOM   19849 C  CG1 . ILE D  1  671 ? -0.105  118.523 54.690  1.00 139.73 ?  671 ILE D CG1 1 
ATOM   19850 C  CG2 . ILE D  1  671 ? -1.317  116.511 53.763  1.00 113.75 ?  671 ILE D CG2 1 
ATOM   19851 C  CD1 . ILE D  1  671 ? 1.353   118.817 54.427  1.00 138.83 ?  671 ILE D CD1 1 
ATOM   19852 N  N   . ASP D  1  672 ? -3.011  115.330 56.068  1.00 154.78 ?  672 ASP D N   1 
ATOM   19853 C  CA  . ASP D  1  672 ? -3.767  114.049 56.075  1.00 154.09 ?  672 ASP D CA  1 
ATOM   19854 C  C   . ASP D  1  672 ? -4.417  113.851 54.702  1.00 142.47 ?  672 ASP D C   1 
ATOM   19855 O  O   . ASP D  1  672 ? -4.699  114.864 54.033  1.00 134.71 ?  672 ASP D O   1 
ATOM   19856 C  CB  . ASP D  1  672 ? -4.794  114.018 57.209  1.00 159.62 ?  672 ASP D CB  1 
ATOM   19857 C  CG  . ASP D  1  672 ? -4.227  114.461 58.547  1.00 161.77 ?  672 ASP D CG  1 
ATOM   19858 O  OD1 . ASP D  1  672 ? -3.772  115.619 58.636  1.00 162.22 ?  672 ASP D OD1 1 
ATOM   19859 O  OD2 . ASP D  1  672 ? -4.244  113.645 59.489  1.00 141.37 ?  672 ASP D OD2 1 
ATOM   19860 N  N   . ASN D  1  673 ? -4.636  112.595 54.301  1.00 169.15 ?  673 ASN D N   1 
ATOM   19861 C  CA  . ASN D  1  673 ? -5.228  112.302 52.969  1.00 168.81 ?  673 ASN D CA  1 
ATOM   19862 C  C   . ASN D  1  673 ? -4.383  112.977 51.883  1.00 166.41 ?  673 ASN D C   1 
ATOM   19863 O  O   . ASN D  1  673 ? -4.972  113.615 50.989  1.00 171.41 ?  673 ASN D O   1 
ATOM   19864 C  CB  . ASN D  1  673 ? -6.695  112.731 52.889  1.00 172.80 ?  673 ASN D CB  1 
ATOM   19865 C  CG  . ASN D  1  673 ? -7.565  111.709 52.191  1.00 184.52 ?  673 ASN D CG  1 
ATOM   19866 O  OD1 . ASN D  1  673 ? -7.062  110.741 51.625  1.00 183.79 ?  673 ASN D OD1 1 
ATOM   19867 N  ND2 . ASN D  1  673 ? -8.872  111.913 52.226  1.00 187.37 ?  673 ASN D ND2 1 
ATOM   19868 N  N   . PHE D  1  674 ? -3.057  112.832 51.961  1.00 135.61 ?  674 PHE D N   1 
ATOM   19869 C  CA  . PHE D  1  674 ? -2.151  113.457 50.963  1.00 129.70 ?  674 PHE D CA  1 
ATOM   19870 C  C   . PHE D  1  674 ? -2.533  112.966 49.564  1.00 121.45 ?  674 PHE D C   1 
ATOM   19871 O  O   . PHE D  1  674 ? -2.516  113.774 48.617  1.00 126.55 ?  674 PHE D O   1 
ATOM   19872 C  CB  . PHE D  1  674 ? -0.693  113.125 51.290  1.00 121.65 ?  674 PHE D CB  1 
ATOM   19873 C  CG  . PHE D  1  674 ? 0.315   113.638 50.293  1.00 109.73 ?  674 PHE D CG  1 
ATOM   19874 C  CD1 . PHE D  1  674 ? 0.190   114.903 49.742  1.00 119.01 ?  674 PHE D CD1 1 
ATOM   19875 C  CD2 . PHE D  1  674 ? 1.394   112.858 49.909  1.00 108.37 ?  674 PHE D CD2 1 
ATOM   19876 C  CE1 . PHE D  1  674 ? 1.118   115.374 48.827  1.00 121.53 ?  674 PHE D CE1 1 
ATOM   19877 C  CE2 . PHE D  1  674 ? 2.323   113.330 48.995  1.00 111.97 ?  674 PHE D CE2 1 
ATOM   19878 C  CZ  . PHE D  1  674 ? 2.183   114.587 48.455  1.00 116.47 ?  674 PHE D CZ  1 
ATOM   19879 N  N   . ALA D  1  675 ? -2.867  111.680 49.446  1.00 109.01 ?  675 ALA D N   1 
ATOM   19880 C  CA  . ALA D  1  675 ? -3.239  111.105 48.134  1.00 105.59 ?  675 ALA D CA  1 
ATOM   19881 C  C   . ALA D  1  675 ? -4.242  112.027 47.434  1.00 116.71 ?  675 ALA D C   1 
ATOM   19882 O  O   . ALA D  1  675 ? -4.023  112.342 46.248  1.00 118.76 ?  675 ALA D O   1 
ATOM   19883 C  CB  . ALA D  1  675 ? -3.808  109.723 48.327  1.00 97.04  ?  675 ALA D CB  1 
ATOM   19884 N  N   . ASP D  1  676 ? -5.297  112.438 48.142  1.00 126.37 ?  676 ASP D N   1 
ATOM   19885 C  CA  . ASP D  1  676 ? -6.332  113.280 47.534  1.00 138.49 ?  676 ASP D CA  1 
ATOM   19886 C  C   . ASP D  1  676 ? -5.746  114.553 46.885  1.00 135.08 ?  676 ASP D C   1 
ATOM   19887 O  O   . ASP D  1  676 ? -6.431  115.192 46.090  1.00 140.36 ?  676 ASP D O   1 
ATOM   19888 C  CB  . ASP D  1  676 ? -7.394  113.669 48.580  1.00 158.86 ?  676 ASP D CB  1 
ATOM   19889 C  CG  . ASP D  1  676 ? -8.230  112.511 49.092  1.00 171.74 ?  676 ASP D CG  1 
ATOM   19890 O  OD1 . ASP D  1  676 ? -7.763  111.354 49.002  1.00 162.29 ?  676 ASP D OD1 1 
ATOM   19891 O  OD2 . ASP D  1  676 ? -9.351  112.763 49.588  1.00 167.03 ?  676 ASP D OD2 1 
ATOM   19892 N  N   . MET D  1  677 ? -4.495  114.918 47.222  1.00 123.69 ?  677 MET D N   1 
ATOM   19893 C  CA  . MET D  1  677 ? -3.829  116.099 46.668  1.00 113.75 ?  677 MET D CA  1 
ATOM   19894 C  C   . MET D  1  677 ? -2.964  115.743 45.447  1.00 108.88 ?  677 MET D C   1 
ATOM   19895 O  O   . MET D  1  677 ? -2.675  116.622 44.640  1.00 115.73 ?  677 MET D O   1 
ATOM   19896 C  CB  . MET D  1  677 ? -2.937  116.765 47.730  1.00 113.53 ?  677 MET D CB  1 
ATOM   19897 C  CG  . MET D  1  677 ? -3.656  117.091 49.017  1.00 126.46 ?  677 MET D CG  1 
ATOM   19898 S  SD  . MET D  1  677 ? -2.635  118.088 50.127  1.00 131.99 ?  677 MET D SD  1 
ATOM   19899 C  CE  . MET D  1  677 ? -3.131  119.680 49.644  1.00 110.66 ?  677 MET D CE  1 
ATOM   19900 N  N   . ILE D  1  678 ? -2.534  114.474 45.317  1.00 110.82 ?  678 ILE D N   1 
ATOM   19901 C  CA  . ILE D  1  678 ? -1.697  114.044 44.195  1.00 104.18 ?  678 ILE D CA  1 
ATOM   19902 C  C   . ILE D  1  678 ? -2.561  113.878 42.945  1.00 105.82 ?  678 ILE D C   1 
ATOM   19903 O  O   . ILE D  1  678 ? -3.684  113.389 43.038  1.00 116.58 ?  678 ILE D O   1 
ATOM   19904 C  CB  . ILE D  1  678 ? -0.936  112.736 44.552  1.00 87.16  ?  678 ILE D CB  1 
ATOM   19905 C  CG1 . ILE D  1  678 ? 0.012   112.965 45.748  1.00 84.17  ?  678 ILE D CG1 1 
ATOM   19906 C  CG2 . ILE D  1  678 ? -0.155  112.213 43.344  1.00 83.86  ?  678 ILE D CG2 1 
ATOM   19907 C  CD1 . ILE D  1  678 ? 0.481   111.704 46.428  1.00 84.40  ?  678 ILE D CD1 1 
ATOM   19908 N  N   . CYS D  1  679 ? -2.046  114.290 41.781  1.00 88.01  ?  679 CYS D N   1 
ATOM   19909 C  CA  . CYS D  1  679 ? -2.779  114.190 40.519  1.00 103.32 ?  679 CYS D CA  1 
ATOM   19910 C  C   . CYS D  1  679 ? -2.568  112.815 39.861  1.00 105.09 ?  679 CYS D C   1 
ATOM   19911 O  O   . CYS D  1  679 ? -1.645  112.092 40.228  1.00 101.64 ?  679 CYS D O   1 
ATOM   19912 C  CB  . CYS D  1  679 ? -2.363  115.326 39.588  1.00 97.95  ?  679 CYS D CB  1 
ATOM   19913 S  SG  . CYS D  1  679 ? -3.370  115.471 38.088  1.00 104.26 ?  679 CYS D SG  1 
ATOM   19914 N  N   . ASP D  1  680 ? -3.434  112.450 38.898  1.00 112.23 ?  680 ASP D N   1 
ATOM   19915 C  CA  . ASP D  1  680 ? -3.334  111.172 38.183  1.00 108.17 ?  680 ASP D CA  1 
ATOM   19916 C  C   . ASP D  1  680 ? -3.910  111.286 36.760  1.00 108.27 ?  680 ASP D C   1 
ATOM   19917 O  O   . ASP D  1  680 ? -4.461  112.326 36.405  1.00 111.65 ?  680 ASP D O   1 
ATOM   19918 C  CB  . ASP D  1  680 ? -4.005  110.036 38.983  1.00 107.02 ?  680 ASP D CB  1 
ATOM   19919 C  CG  . ASP D  1  680 ? -5.468  110.254 39.292  1.00 121.37 ?  680 ASP D CG  1 
ATOM   19920 O  OD1 . ASP D  1  680 ? -6.141  110.959 38.513  1.00 122.17 ?  680 ASP D OD1 1 
ATOM   19921 O  OD2 . ASP D  1  680 ? -5.945  109.709 40.309  1.00 131.44 ?  680 ASP D OD2 1 
ATOM   19922 N  N   . GLU D  1  681 ? -3.771  110.233 35.941  1.00 97.87  ?  681 GLU D N   1 
ATOM   19923 C  CA  . GLU D  1  681 ? -4.262  110.249 34.562  1.00 100.04 ?  681 GLU D CA  1 
ATOM   19924 C  C   . GLU D  1  681 ? -5.764  110.536 34.440  1.00 107.08 ?  681 GLU D C   1 
ATOM   19925 O  O   . GLU D  1  681 ? -6.201  111.012 33.393  1.00 102.10 ?  681 GLU D O   1 
ATOM   19926 C  CB  . GLU D  1  681 ? -3.884  108.944 33.826  1.00 85.38  ?  681 GLU D CB  1 
ATOM   19927 C  CG  . GLU D  1  681 ? -4.769  107.737 34.109  1.00 106.00 ?  681 GLU D CG  1 
ATOM   19928 C  CD  . GLU D  1  681 ? -4.344  106.874 35.280  1.00 109.62 ?  681 GLU D CD  1 
ATOM   19929 O  OE1 . GLU D  1  681 ? -3.919  107.438 36.313  1.00 112.07 ?  681 GLU D OE1 1 
ATOM   19930 O  OE2 . GLU D  1  681 ? -4.445  105.631 35.170  1.00 102.94 ?  681 GLU D OE2 1 
ATOM   19931 N  N   . THR D  1  682 ? -6.553  110.258 35.492  1.00 105.30 ?  682 THR D N   1 
ATOM   19932 C  CA  . THR D  1  682 ? -7.997  110.501 35.446  1.00 112.50 ?  682 THR D CA  1 
ATOM   19933 C  C   . THR D  1  682 ? -8.308  111.990 35.628  1.00 125.76 ?  682 THR D C   1 
ATOM   19934 O  O   . THR D  1  682 ? -9.284  112.478 35.059  1.00 129.08 ?  682 THR D O   1 
ATOM   19935 C  CB  . THR D  1  682 ? -8.741  109.641 36.475  1.00 101.34 ?  682 THR D CB  1 
ATOM   19936 O  OG1 . THR D  1  682 ? -8.474  110.126 37.789  1.00 110.56 ?  682 THR D OG1 1 
ATOM   19937 C  CG2 . THR D  1  682 ? -8.387  108.166 36.373  1.00 106.93 ?  682 THR D CG2 1 
ATOM   19938 N  N   . ILE D  1  683 ? -7.491  112.713 36.413  1.00 116.75 ?  683 ILE D N   1 
ATOM   19939 C  CA  . ILE D  1  683 ? -7.699  114.144 36.630  1.00 113.73 ?  683 ILE D CA  1 
ATOM   19940 C  C   . ILE D  1  683 ? -7.149  114.912 35.415  1.00 117.87 ?  683 ILE D C   1 
ATOM   19941 O  O   . ILE D  1  683 ? -7.901  115.638 34.767  1.00 113.26 ?  683 ILE D O   1 
ATOM   19942 C  CB  . ILE D  1  683 ? -7.053  114.612 37.964  1.00 105.96 ?  683 ILE D CB  1 
ATOM   19943 C  CG1 . ILE D  1  683 ? -7.769  113.980 39.179  1.00 101.56 ?  683 ILE D CG1 1 
ATOM   19944 C  CG2 . ILE D  1  683 ? -7.068  116.141 38.054  1.00 99.65  ?  683 ILE D CG2 1 
ATOM   19945 C  CD1 . ILE D  1  683 ? -6.911  113.862 40.430  1.00 108.34 ?  683 ILE D CD1 1 
ATOM   19946 N  N   . ALA D  1  684 ? -5.842  114.742 35.104  1.00 120.62 ?  684 ALA D N   1 
ATOM   19947 C  CA  . ALA D  1  684 ? -5.176  115.400 33.968  1.00 121.90 ?  684 ALA D CA  1 
ATOM   19948 C  C   . ALA D  1  684 ? -3.724  114.930 33.830  1.00 123.88 ?  684 ALA D C   1 
ATOM   19949 O  O   . ALA D  1  684 ? -3.115  114.519 34.816  1.00 127.22 ?  684 ALA D O   1 
ATOM   19950 C  CB  . ALA D  1  684 ? -5.200  116.915 34.135  1.00 125.42 ?  684 ALA D CB  1 
ATOM   19951 N  N   . THR D  1  685 ? -3.168  115.001 32.611  1.00 125.61 ?  685 THR D N   1 
ATOM   19952 C  CA  . THR D  1  685 ? -1.783  114.596 32.359  1.00 119.07 ?  685 THR D CA  1 
ATOM   19953 C  C   . THR D  1  685 ? -0.922  115.768 31.867  1.00 121.35 ?  685 THR D C   1 
ATOM   19954 O  O   . THR D  1  685 ? 0.272   115.789 32.148  1.00 113.78 ?  685 THR D O   1 
ATOM   19955 C  CB  . THR D  1  685 ? -1.731  113.441 31.356  1.00 113.87 ?  685 THR D CB  1 
ATOM   19956 O  OG1 . THR D  1  685 ? -2.354  113.850 30.139  1.00 150.27 ?  685 THR D OG1 1 
ATOM   19957 C  CG2 . THR D  1  685 ? -2.395  112.185 31.880  1.00 106.35 ?  685 THR D CG2 1 
ATOM   19958 N  N   . GLU D  1  686 ? -1.503  116.728 31.129  1.00 126.25 ?  686 GLU D N   1 
ATOM   19959 C  CA  . GLU D  1  686 ? -0.746  117.876 30.618  1.00 117.91 ?  686 GLU D CA  1 
ATOM   19960 C  C   . GLU D  1  686 ? -0.224  118.746 31.757  1.00 114.37 ?  686 GLU D C   1 
ATOM   19961 O  O   . GLU D  1  686 ? -0.952  119.011 32.708  1.00 116.83 ?  686 GLU D O   1 
ATOM   19962 C  CB  . GLU D  1  686 ? -1.612  118.728 29.676  1.00 122.77 ?  686 GLU D CB  1 
ATOM   19963 C  CG  . GLU D  1  686 ? -1.766  118.161 28.274  1.00 137.24 ?  686 GLU D CG  1 
ATOM   19964 C  CD  . GLU D  1  686 ? -1.133  118.997 27.179  1.00 139.43 ?  686 GLU D CD  1 
ATOM   19965 O  OE1 . GLU D  1  686 ? -1.150  120.245 27.293  1.00 134.64 ?  686 GLU D OE1 1 
ATOM   19966 O  OE2 . GLU D  1  686 ? -0.626  118.402 26.201  1.00 125.33 ?  686 GLU D OE2 1 
ATOM   19967 N  N   . SER D  1  687 ? 1.033   119.194 31.653  1.00 112.05 ?  687 SER D N   1 
ATOM   19968 C  CA  . SER D  1  687 ? 1.676   120.017 32.677  1.00 112.58 ?  687 SER D CA  1 
ATOM   19969 C  C   . SER D  1  687 ? 0.864   121.247 33.072  1.00 112.69 ?  687 SER D C   1 
ATOM   19970 O  O   . SER D  1  687 ? 0.793   121.566 34.255  1.00 110.34 ?  687 SER D O   1 
ATOM   19971 C  CB  . SER D  1  687 ? 3.063   120.452 32.213  1.00 108.81 ?  687 SER D CB  1 
ATOM   19972 O  OG  . SER D  1  687 ? 3.975   119.365 32.171  1.00 123.33 ?  687 SER D OG  1 
ATOM   19973 N  N   . GLU D  1  688 ? 0.262   121.943 32.101  1.00 109.70 ?  688 GLU D N   1 
ATOM   19974 C  CA  . GLU D  1  688 ? -0.532  123.135 32.405  1.00 129.09 ?  688 GLU D CA  1 
ATOM   19975 C  C   . GLU D  1  688 ? -1.759  122.789 33.247  1.00 132.34 ?  688 GLU D C   1 
ATOM   19976 O  O   . GLU D  1  688 ? -2.082  123.513 34.186  1.00 135.41 ?  688 GLU D O   1 
ATOM   19977 C  CB  . GLU D  1  688 ? -0.971  123.844 31.113  1.00 145.65 ?  688 GLU D CB  1 
ATOM   19978 C  CG  . GLU D  1  688 ? 0.121   124.679 30.468  1.00 149.42 ?  688 GLU D CG  1 
ATOM   19979 C  CD  . GLU D  1  688 ? -0.260  125.264 29.124  1.00 165.91 ?  688 GLU D CD  1 
ATOM   19980 O  OE1 . GLU D  1  688 ? -1.475  125.430 28.870  1.00 171.19 ?  688 GLU D OE1 1 
ATOM   19981 O  OE2 . GLU D  1  688 ? 0.658   125.559 28.324  1.00 172.84 ?  688 GLU D OE2 1 
ATOM   19982 N  N   . GLU D  1  689 ? -2.424  121.682 32.919  1.00 135.67 ?  689 GLU D N   1 
ATOM   19983 C  CA  . GLU D  1  689 ? -3.637  121.278 33.675  1.00 128.33 ?  689 GLU D CA  1 
ATOM   19984 C  C   . GLU D  1  689 ? -3.218  120.780 35.060  1.00 123.09 ?  689 GLU D C   1 
ATOM   19985 O  O   . GLU D  1  689 ? -3.913  121.108 36.039  1.00 129.32 ?  689 GLU D O   1 
ATOM   19986 C  CB  . GLU D  1  689 ? -4.397  120.197 32.906  1.00 134.71 ?  689 GLU D CB  1 
ATOM   19987 C  CG  . GLU D  1  689 ? -5.070  120.716 31.650  1.00 143.91 ?  689 GLU D CG  1 
ATOM   19988 C  CD  . GLU D  1  689 ? -4.192  120.710 30.411  1.00 159.40 ?  689 GLU D CD  1 
ATOM   19989 O  OE1 . GLU D  1  689 ? -3.193  121.455 30.391  1.00 165.22 ?  689 GLU D OE1 1 
ATOM   19990 O  OE2 . GLU D  1  689 ? -4.510  119.959 29.468  1.00 163.27 ?  689 GLU D OE2 1 
ATOM   19991 N  N   . VAL D  1  690 ? -2.117  120.031 35.135  1.00 118.59 ?  690 VAL D N   1 
ATOM   19992 C  CA  . VAL D  1  690 ? -1.670  119.453 36.403  1.00 112.94 ?  690 VAL D CA  1 
ATOM   19993 C  C   . VAL D  1  690 ? -1.280  120.563 37.386  1.00 113.56 ?  690 VAL D C   1 
ATOM   19994 O  O   . VAL D  1  690 ? -1.652  120.488 38.558  1.00 113.20 ?  690 VAL D O   1 
ATOM   19995 C  CB  . VAL D  1  690 ? -0.522  118.426 36.192  1.00 97.59  ?  690 VAL D CB  1 
ATOM   19996 C  CG1 . VAL D  1  690 ? 0.103   118.015 37.522  1.00 99.27  ?  690 VAL D CG1 1 
ATOM   19997 C  CG2 . VAL D  1  690 ? -1.020  117.197 35.437  1.00 92.47  ?  690 VAL D CG2 1 
ATOM   19998 N  N   . VAL D  1  691 ? -0.554  121.598 36.925  1.00 104.55 ?  691 VAL D N   1 
ATOM   19999 C  CA  . VAL D  1  691 ? -0.168  122.692 37.825  1.00 100.22 ?  691 VAL D CA  1 
ATOM   20000 C  C   . VAL D  1  691 ? -1.405  123.427 38.350  1.00 121.24 ?  691 VAL D C   1 
ATOM   20001 O  O   . VAL D  1  691 ? -1.381  123.911 39.479  1.00 130.38 ?  691 VAL D O   1 
ATOM   20002 C  CB  . VAL D  1  691 ? 0.884   123.664 37.239  1.00 100.19 ?  691 VAL D CB  1 
ATOM   20003 C  CG1 . VAL D  1  691 ? 2.167   122.927 36.870  1.00 106.59 ?  691 VAL D CG1 1 
ATOM   20004 C  CG2 . VAL D  1  691 ? 0.336   124.447 36.052  1.00 108.52 ?  691 VAL D CG2 1 
ATOM   20005 N  N   . LYS D  1  692 ? -2.489  123.496 37.555  1.00 126.65 ?  692 LYS D N   1 
ATOM   20006 C  CA  . LYS D  1  692 ? -3.721  124.155 37.989  1.00 128.93 ?  692 LYS D CA  1 
ATOM   20007 C  C   . LYS D  1  692 ? -4.373  123.337 39.102  1.00 126.39 ?  692 LYS D C   1 
ATOM   20008 O  O   . LYS D  1  692 ? -4.808  123.905 40.101  1.00 127.55 ?  692 LYS D O   1 
ATOM   20009 C  CB  . LYS D  1  692 ? -4.706  124.316 36.819  1.00 130.64 ?  692 LYS D CB  1 
ATOM   20010 C  CG  . LYS D  1  692 ? -4.363  125.454 35.869  1.00 138.33 ?  692 LYS D CG  1 
ATOM   20011 C  CD  . LYS D  1  692 ? -5.393  125.574 34.755  1.00 150.97 ?  692 LYS D CD  1 
ATOM   20012 C  CE  . LYS D  1  692 ? -4.944  126.515 33.666  1.00 166.55 ?  692 LYS D CE  1 
ATOM   20013 N  NZ  . LYS D  1  692 ? -5.947  126.613 32.573  1.00 176.12 ?  692 LYS D NZ  1 
ATOM   20014 N  N   . PHE D  1  693 ? -4.436  122.006 38.935  1.00 124.55 ?  693 PHE D N   1 
ATOM   20015 C  CA  . PHE D  1  693 ? -5.019  121.114 39.938  1.00 125.15 ?  693 PHE D CA  1 
ATOM   20016 C  C   . PHE D  1  693 ? -4.228  121.192 41.246  1.00 117.33 ?  693 PHE D C   1 
ATOM   20017 O  O   . PHE D  1  693 ? -4.822  121.155 42.322  1.00 124.78 ?  693 PHE D O   1 
ATOM   20018 C  CB  . PHE D  1  693 ? -5.047  119.664 39.416  1.00 115.54 ?  693 PHE D CB  1 
ATOM   20019 C  CG  . PHE D  1  693 ? -5.363  118.626 40.468  1.00 119.40 ?  693 PHE D CG  1 
ATOM   20020 C  CD1 . PHE D  1  693 ? -6.668  118.368 40.840  1.00 117.52 ?  693 PHE D CD1 1 
ATOM   20021 C  CD2 . PHE D  1  693 ? -4.352  117.917 41.091  1.00 127.81 ?  693 PHE D CD2 1 
ATOM   20022 C  CE1 . PHE D  1  693 ? -6.957  117.414 41.808  1.00 109.19 ?  693 PHE D CE1 1 
ATOM   20023 C  CE2 . PHE D  1  693 ? -4.643  116.967 42.060  1.00 126.09 ?  693 PHE D CE2 1 
ATOM   20024 C  CZ  . PHE D  1  693 ? -5.943  116.723 42.415  1.00 102.25 ?  693 PHE D CZ  1 
ATOM   20025 N  N   . LEU D  1  694 ? -2.895  121.294 41.155  1.00 111.99 ?  694 LEU D N   1 
ATOM   20026 C  CA  . LEU D  1  694 ? -2.046  121.381 42.342  1.00 106.29 ?  694 LEU D CA  1 
ATOM   20027 C  C   . LEU D  1  694 ? -2.222  122.732 43.033  1.00 113.55 ?  694 LEU D C   1 
ATOM   20028 O  O   . LEU D  1  694 ? -2.191  122.791 44.261  1.00 121.63 ?  694 LEU D O   1 
ATOM   20029 C  CB  . LEU D  1  694 ? -0.572  121.140 41.975  1.00 93.09  ?  694 LEU D CB  1 
ATOM   20030 C  CG  . LEU D  1  694 ? -0.250  119.743 41.421  1.00 93.12  ?  694 LEU D CG  1 
ATOM   20031 C  CD1 . LEU D  1  694 ? 1.059   119.739 40.681  1.00 95.04  ?  694 LEU D CD1 1 
ATOM   20032 C  CD2 . LEU D  1  694 ? -0.206  118.701 42.528  1.00 101.27 ?  694 LEU D CD2 1 
ATOM   20033 N  N   . GLU D  1  695 ? -2.417  123.810 42.258  1.00 113.58 ?  695 GLU D N   1 
ATOM   20034 C  CA  . GLU D  1  695 ? -2.643  125.142 42.822  1.00 117.00 ?  695 GLU D CA  1 
ATOM   20035 C  C   . GLU D  1  695 ? -4.000  125.163 43.532  1.00 121.69 ?  695 GLU D C   1 
ATOM   20036 O  O   . GLU D  1  695 ? -4.125  125.767 44.597  1.00 119.39 ?  695 GLU D O   1 
ATOM   20037 C  CB  . GLU D  1  695 ? -2.626  126.218 41.722  1.00 113.66 ?  695 GLU D CB  1 
ATOM   20038 C  CG  . GLU D  1  695 ? -1.235  126.642 41.285  1.00 120.69 ?  695 GLU D CG  1 
ATOM   20039 C  CD  . GLU D  1  695 ? -1.216  127.679 40.180  1.00 135.05 ?  695 GLU D CD  1 
ATOM   20040 O  OE1 . GLU D  1  695 ? -2.153  127.682 39.350  1.00 130.93 ?  695 GLU D OE1 1 
ATOM   20041 O  OE2 . GLU D  1  695 ? -0.261  128.488 40.142  1.00 147.90 ?  695 GLU D OE2 1 
ATOM   20042 N  N   . GLU D  1  696 ? -5.012  124.503 42.940  1.00 129.18 ?  696 GLU D N   1 
ATOM   20043 C  CA  . GLU D  1  696 ? -6.356  124.433 43.510  1.00 135.17 ?  696 GLU D CA  1 
ATOM   20044 C  C   . GLU D  1  696 ? -6.317  123.750 44.876  1.00 123.85 ?  696 GLU D C   1 
ATOM   20045 O  O   . GLU D  1  696 ? -6.802  124.312 45.857  1.00 135.58 ?  696 GLU D O   1 
ATOM   20046 C  CB  . GLU D  1  696 ? -7.308  123.650 42.580  1.00 141.85 ?  696 GLU D CB  1 
ATOM   20047 C  CG  . GLU D  1  696 ? -7.724  124.385 41.319  1.00 151.56 ?  696 GLU D CG  1 
ATOM   20048 C  CD  . GLU D  1  696 ? -8.497  123.525 40.337  1.00 156.16 ?  696 GLU D CD  1 
ATOM   20049 O  OE1 . GLU D  1  696 ? -9.077  122.501 40.767  1.00 152.77 ?  696 GLU D OE1 1 
ATOM   20050 O  OE2 . GLU D  1  696 ? -8.525  123.876 39.136  1.00 166.32 ?  696 GLU D OE2 1 
ATOM   20051 N  N   . LYS D  1  697 ? -5.736  122.544 44.943  1.00 110.91 ?  697 LYS D N   1 
ATOM   20052 C  CA  . LYS D  1  697 ? -5.662  121.787 46.190  1.00 110.98 ?  697 LYS D CA  1 
ATOM   20053 C  C   . LYS D  1  697 ? -4.639  122.347 47.185  1.00 115.83 ?  697 LYS D C   1 
ATOM   20054 O  O   . LYS D  1  697 ? -4.693  121.996 48.360  1.00 112.99 ?  697 LYS D O   1 
ATOM   20055 C  CB  . LYS D  1  697 ? -5.352  120.306 45.906  1.00 98.19  ?  697 LYS D CB  1 
ATOM   20056 C  CG  . LYS D  1  697 ? -6.377  119.602 45.020  1.00 102.69 ?  697 LYS D CG  1 
ATOM   20057 C  CD  . LYS D  1  697 ? -7.599  119.129 45.795  1.00 121.98 ?  697 LYS D CD  1 
ATOM   20058 C  CE  . LYS D  1  697 ? -8.744  118.768 44.882  1.00 118.20 ?  697 LYS D CE  1 
ATOM   20059 N  NZ  . LYS D  1  697 ? -10.015 118.589 45.631  1.00 123.35 ?  697 LYS D NZ  1 
ATOM   20060 N  N   . GLY D  1  698 ? -3.727  123.198 46.728  1.00 118.03 ?  698 GLY D N   1 
ATOM   20061 C  CA  . GLY D  1  698 ? -2.707  123.766 47.598  1.00 111.59 ?  698 GLY D CA  1 
ATOM   20062 C  C   . GLY D  1  698 ? -1.734  122.691 48.027  1.00 106.88 ?  698 GLY D C   1 
ATOM   20063 O  O   . GLY D  1  698 ? -1.502  122.489 49.222  1.00 104.17 ?  698 GLY D O   1 
ATOM   20064 N  N   . HIS D  1  699 ? -1.168  121.987 47.036  1.00 94.14  ?  699 HIS D N   1 
ATOM   20065 C  CA  . HIS D  1  699 ? -0.231  120.896 47.265  1.00 90.39  ?  699 HIS D CA  1 
ATOM   20066 C  C   . HIS D  1  699 ? 0.971   121.361 48.083  1.00 103.76 ?  699 HIS D C   1 
ATOM   20067 O  O   . HIS D  1  699 ? 1.507   122.437 47.816  1.00 105.41 ?  699 HIS D O   1 
ATOM   20068 C  CB  . HIS D  1  699 ? 0.249   120.320 45.921  1.00 96.22  ?  699 HIS D CB  1 
ATOM   20069 C  CG  . HIS D  1  699 ? 0.782   118.924 46.018  1.00 102.82 ?  699 HIS D CG  1 
ATOM   20070 N  ND1 . HIS D  1  699 ? 2.056   118.667 46.491  1.00 109.53 ?  699 HIS D ND1 1 
ATOM   20071 C  CD2 . HIS D  1  699 ? 0.189   117.752 45.699  1.00 88.56  ?  699 HIS D CD2 1 
ATOM   20072 C  CE1 . HIS D  1  699 ? 2.196   117.351 46.453  1.00 108.88 ?  699 HIS D CE1 1 
ATOM   20073 N  NE2 . HIS D  1  699 ? 1.097   116.760 45.980  1.00 105.08 ?  699 HIS D NE2 1 
ATOM   20074 N  N   . PRO D  1  700 ? 1.423   120.575 49.079  1.00 106.51 ?  700 PRO D N   1 
ATOM   20075 C  CA  . PRO D  1  700 ? 2.584   121.014 49.871  1.00 107.52 ?  700 PRO D CA  1 
ATOM   20076 C  C   . PRO D  1  700 ? 3.860   121.228 49.049  1.00 119.55 ?  700 PRO D C   1 
ATOM   20077 O  O   . PRO D  1  700 ? 4.759   121.936 49.502  1.00 113.19 ?  700 PRO D O   1 
ATOM   20078 C  CB  . PRO D  1  700 ? 2.762   119.895 50.904  1.00 114.10 ?  700 PRO D CB  1 
ATOM   20079 C  CG  . PRO D  1  700 ? 2.003   118.734 50.382  1.00 104.42 ?  700 PRO D CG  1 
ATOM   20080 C  CD  . PRO D  1  700 ? 0.905   119.271 49.540  1.00 105.66 ?  700 PRO D CD  1 
ATOM   20081 N  N   . ALA D  1  701 ? 3.944   120.621 47.847  1.00 124.93 ?  701 ALA D N   1 
ATOM   20082 C  CA  . ALA D  1  701 ? 5.110   120.742 46.969  1.00 131.59 ?  701 ALA D CA  1 
ATOM   20083 C  C   . ALA D  1  701 ? 5.300   122.159 46.443  1.00 132.57 ?  701 ALA D C   1 
ATOM   20084 O  O   . ALA D  1  701 ? 6.436   122.615 46.311  1.00 128.69 ?  701 ALA D O   1 
ATOM   20085 C  CB  . ALA D  1  701 ? 4.982   119.775 45.803  1.00 123.35 ?  701 ALA D CB  1 
ATOM   20086 N  N   . LEU D  1  702 ? 4.198   122.854 46.137  1.00 111.43 ?  702 LEU D N   1 
ATOM   20087 C  CA  . LEU D  1  702 ? 4.276   124.219 45.624  1.00 105.82 ?  702 LEU D CA  1 
ATOM   20088 C  C   . LEU D  1  702 ? 4.781   125.171 46.707  1.00 106.23 ?  702 LEU D C   1 
ATOM   20089 O  O   . LEU D  1  702 ? 5.531   126.094 46.395  1.00 116.90 ?  702 LEU D O   1 
ATOM   20090 C  CB  . LEU D  1  702 ? 2.912   124.692 45.092  1.00 103.70 ?  702 LEU D CB  1 
ATOM   20091 C  CG  . LEU D  1  702 ? 2.229   123.812 44.037  1.00 104.49 ?  702 LEU D CG  1 
ATOM   20092 C  CD1 . LEU D  1  702 ? 0.879   124.378 43.670  1.00 94.01  ?  702 LEU D CD1 1 
ATOM   20093 C  CD2 . LEU D  1  702 ? 3.079   123.673 42.786  1.00 91.84  ?  702 LEU D CD2 1 
ATOM   20094 N  N   . LYS D  1  703 ? 4.389   124.952 47.973  1.00 108.30 ?  703 LYS D N   1 
ATOM   20095 C  CA  . LYS D  1  703 ? 4.832   125.806 49.075  1.00 116.57 ?  703 LYS D CA  1 
ATOM   20096 C  C   . LYS D  1  703 ? 5.983   125.147 49.840  1.00 117.65 ?  703 LYS D C   1 
ATOM   20097 O  O   . LYS D  1  703 ? 5.895   124.924 51.047  1.00 127.25 ?  703 LYS D O   1 
ATOM   20098 C  CB  . LYS D  1  703 ? 3.657   126.140 50.006  1.00 118.33 ?  703 LYS D CB  1 
ATOM   20099 C  CG  . LYS D  1  703 ? 2.587   126.981 49.318  1.00 112.63 ?  703 LYS D CG  1 
ATOM   20100 C  CD  . LYS D  1  703 ? 1.731   127.780 50.301  1.00 115.90 ?  703 LYS D CD  1 
ATOM   20101 C  CE  . LYS D  1  703 ? 1.414   129.168 49.799  1.00 122.05 ?  703 LYS D CE  1 
ATOM   20102 N  NZ  . LYS D  1  703 ? 0.161   129.697 50.395  1.00 132.81 ?  703 LYS D NZ  1 
ATOM   20103 N  N   . MET D  1  704 ? 7.057   124.846 49.098  1.00 114.61 ?  704 MET D N   1 
ATOM   20104 C  CA  . MET D  1  704 ? 8.260   124.209 49.694  1.00 104.86 ?  704 MET D CA  1 
ATOM   20105 C  C   . MET D  1  704 ? 9.498   124.767 48.983  1.00 104.44 ?  704 MET D C   1 
ATOM   20106 O  O   . MET D  1  704 ? 9.355   125.218 47.832  1.00 114.09 ?  704 MET D O   1 
ATOM   20107 C  CB  . MET D  1  704 ? 8.212   122.692 49.499  1.00 94.03  ?  704 MET D CB  1 
ATOM   20108 C  CG  . MET D  1  704 ? 8.134   121.911 50.793  1.00 103.31 ?  704 MET D CG  1 
ATOM   20109 S  SD  . MET D  1  704 ? 8.489   120.153 50.550  1.00 112.68 ?  704 MET D SD  1 
ATOM   20110 C  CE  . MET D  1  704 ? 7.100   119.672 49.526  1.00 81.06  ?  704 MET D CE  1 
ATOM   20111 N  N   . ASP D  1  705 ? 10.654  124.785 49.650  1.00 98.56  ?  705 ASP D N   1 
ATOM   20112 C  CA  . ASP D  1  705 ? 11.855  125.410 49.031  1.00 111.73 ?  705 ASP D CA  1 
ATOM   20113 C  C   . ASP D  1  705 ? 12.080  124.806 47.642  1.00 113.63 ?  705 ASP D C   1 
ATOM   20114 O  O   . ASP D  1  705 ? 11.878  123.588 47.487  1.00 116.56 ?  705 ASP D O   1 
ATOM   20115 C  CB  . ASP D  1  705 ? 13.098  125.259 49.908  1.00 120.44 ?  705 ASP D CB  1 
ATOM   20116 C  CG  . ASP D  1  705 ? 13.241  123.884 50.531  1.00 143.30 ?  705 ASP D CG  1 
ATOM   20117 O  OD1 . ASP D  1  705 ? 13.111  122.886 49.795  1.00 142.91 ?  705 ASP D OD1 1 
ATOM   20118 O  OD2 . ASP D  1  705 ? 13.487  123.826 51.746  1.00 151.39 ?  705 ASP D OD2 1 
ATOM   20119 N  N   . PRO D  1  706 ? 12.400  125.668 46.640  1.00 110.88 ?  706 PRO D N   1 
ATOM   20120 C  CA  . PRO D  1  706 ? 12.624  125.229 45.268  1.00 108.58 ?  706 PRO D CA  1 
ATOM   20121 C  C   . PRO D  1  706 ? 13.510  123.987 45.271  1.00 101.67 ?  706 PRO D C   1 
ATOM   20122 O  O   . PRO D  1  706 ? 14.559  124.003 45.887  1.00 117.09 ?  706 PRO D O   1 
ATOM   20123 C  CB  . PRO D  1  706 ? 13.369  126.406 44.629  1.00 104.39 ?  706 PRO D CB  1 
ATOM   20124 C  CG  . PRO D  1  706 ? 12.803  127.607 45.341  1.00 97.50  ?  706 PRO D CG  1 
ATOM   20125 C  CD  . PRO D  1  706 ? 12.566  127.126 46.758  1.00 105.90 ?  706 PRO D CD  1 
ATOM   20126 N  N   . ILE D  1  707 ? 13.065  122.971 44.556  1.00 85.05  ?  707 ILE D N   1 
ATOM   20127 C  CA  . ILE D  1  707 ? 13.845  121.717 44.612  1.00 96.90  ?  707 ILE D CA  1 
ATOM   20128 C  C   . ILE D  1  707 ? 15.124  121.881 43.786  1.00 100.23 ?  707 ILE D C   1 
ATOM   20129 O  O   . ILE D  1  707 ? 16.184  121.410 44.239  1.00 105.33 ?  707 ILE D O   1 
ATOM   20130 C  CB  . ILE D  1  707 ? 12.991  120.552 44.112  1.00 94.06  ?  707 ILE D CB  1 
ATOM   20131 C  CG1 . ILE D  1  707 ? 13.865  119.315 44.167  1.00 89.32  ?  707 ILE D CG1 1 
ATOM   20132 C  CG2 . ILE D  1  707 ? 12.441  120.818 42.722  1.00 73.81  ?  707 ILE D CG2 1 
ATOM   20133 C  CD1 . ILE D  1  707 ? 13.092  118.018 44.105  1.00 85.30  ?  707 ILE D CD1 1 
ATOM   20134 N  N   . MET D  1  708 ? 15.023  122.518 42.616  1.00 108.76 ?  708 MET D N   1 
ATOM   20135 C  CA  . MET D  1  708 ? 16.205  122.714 41.735  1.00 95.51  ?  708 MET D CA  1 
ATOM   20136 C  C   . MET D  1  708 ? 16.606  124.193 41.755  1.00 94.41  ?  708 MET D C   1 
ATOM   20137 O  O   . MET D  1  708 ? 15.736  125.020 41.419  1.00 107.28 ?  708 MET D O   1 
ATOM   20138 C  CB  . MET D  1  708 ? 15.889  122.298 40.296  1.00 82.22  ?  708 MET D CB  1 
ATOM   20139 C  CG  . MET D  1  708 ? 15.784  120.798 40.107  1.00 79.69  ?  708 MET D CG  1 
ATOM   20140 S  SD  . MET D  1  708 ? 16.054  120.319 38.383  1.00 102.19 ?  708 MET D SD  1 
ATOM   20141 C  CE  . MET D  1  708 ? 17.601  121.159 38.047  1.00 90.37  ?  708 MET D CE  1 
HETATM 20142 FE FE1 . SF4 E  3  .   ? 104.566 -19.014 2.234   1.00 149.05 ?  801 SF4 A FE1 1 
HETATM 20143 FE FE2 . SF4 E  3  .   ? 103.869 -19.141 -0.281  1.00 169.73 ?  801 SF4 A FE2 1 
HETATM 20144 FE FE3 . SF4 E  3  .   ? 102.032 -19.383 1.607   1.00 102.41 ?  801 SF4 A FE3 1 
HETATM 20145 FE FE4 . SF4 E  3  .   ? 103.818 -21.300 1.224   1.00 161.80 ?  801 SF4 A FE4 1 
HETATM 20146 S  S1  . SF4 E  3  .   ? 102.176 -20.687 -0.274  1.00 181.32 ?  801 SF4 A S1  1 
HETATM 20147 S  S2  . SF4 E  3  .   ? 103.156 -20.506 3.273   1.00 172.59 ?  801 SF4 A S2  1 
HETATM 20148 S  S3  . SF4 E  3  .   ? 105.723 -20.172 0.623   1.00 99.01  ?  801 SF4 A S3  1 
HETATM 20149 S  S4  . SF4 E  3  .   ? 103.219 -17.476 1.163   1.00 148.78 ?  801 SF4 A S4  1 
HETATM 20150 NI NI  . NI  F  4  .   ? 101.348 -25.238 -2.173  1.00 117.14 ?  802 NI  A NI  1 
HETATM 20151 NI NI  . NI  G  4  .   ? 102.470 -23.584 -0.478  1.00 183.31 ?  803 NI  A NI  1 
HETATM 20152 C  C1  . EDO H  5  .   ? 101.170 -15.507 42.204  1.00 94.00  ?  804 EDO A C1  1 
HETATM 20153 O  O1  . EDO H  5  .   ? 101.651 -14.526 43.085  1.00 82.75  ?  804 EDO A O1  1 
HETATM 20154 C  C2  . EDO H  5  .   ? 100.443 -14.938 41.042  1.00 92.95  ?  804 EDO A C2  1 
HETATM 20155 O  O2  . EDO H  5  .   ? 100.353 -15.829 39.955  1.00 80.74  ?  804 EDO A O2  1 
HETATM 20156 O  O5  . PE4 I  6  .   ? 108.220 -27.660 59.746  1.00 106.62 ?  805 PE4 A O5  1 
HETATM 20157 C  C9  . PE4 I  6  .   ? 108.012 -27.507 61.125  1.00 118.89 ?  805 PE4 A C9  1 
HETATM 20158 C  C10 . PE4 I  6  .   ? 109.284 -26.975 61.788  1.00 112.92 ?  805 PE4 A C10 1 
HETATM 20159 O  O6  . PE4 I  6  .   ? 110.213 -28.018 61.967  1.00 121.66 ?  805 PE4 A O6  1 
HETATM 20160 C  C11 . PE4 I  6  .   ? 110.190 -28.749 63.169  1.00 110.51 ?  805 PE4 A C11 1 
HETATM 20161 C  C12 . PE4 I  6  .   ? 110.113 -30.244 62.854  1.00 102.70 ?  805 PE4 A C12 1 
HETATM 20162 O  O7  . PE4 I  6  .   ? 111.139 -30.602 61.956  1.00 120.44 ?  805 PE4 A O7  1 
HETATM 20163 C  C13 . PE4 I  6  .   ? 110.828 -31.492 60.909  1.00 112.87 ?  805 PE4 A C13 1 
HETATM 20164 C  C14 . PE4 I  6  .   ? 110.427 -30.708 59.657  1.00 101.75 ?  805 PE4 A C14 1 
HETATM 20165 O  O8  . PE4 I  6  .   ? 109.035 -30.628 59.559  1.00 94.05  ?  805 PE4 A O8  1 
HETATM 20166 C  C1  . EDO J  5  .   ? 113.810 -9.869  57.912  1.00 102.79 ?  806 EDO A C1  1 
HETATM 20167 O  O1  . EDO J  5  .   ? 114.056 -9.812  59.314  1.00 106.85 ?  806 EDO A O1  1 
HETATM 20168 C  C2  . EDO J  5  .   ? 113.025 -8.651  57.448  1.00 96.87  ?  806 EDO A C2  1 
HETATM 20169 O  O2  . EDO J  5  .   ? 111.674 -8.975  57.151  1.00 91.34  ?  806 EDO A O2  1 
HETATM 20170 C  C1  . GOL K  7  .   ? 75.206  -31.183 -19.397 1.00 121.74 ?  807 GOL A C1  1 
HETATM 20171 O  O1  . GOL K  7  .   ? 75.145  -32.136 -18.344 1.00 132.65 ?  807 GOL A O1  1 
HETATM 20172 C  C2  . GOL K  7  .   ? 76.075  -31.677 -20.532 1.00 126.47 ?  807 GOL A C2  1 
HETATM 20173 O  O2  . GOL K  7  .   ? 77.393  -31.951 -20.048 1.00 134.04 ?  807 GOL A O2  1 
HETATM 20174 C  C3  . GOL K  7  .   ? 75.507  -32.909 -21.199 1.00 134.76 ?  807 GOL A C3  1 
HETATM 20175 O  O3  . GOL K  7  .   ? 76.349  -33.351 -22.256 1.00 137.85 ?  807 GOL A O3  1 
HETATM 20176 C  C1  . PEG L  8  .   ? 133.606 -7.045  43.646  1.00 99.21  ?  808 PEG A C1  1 
HETATM 20177 O  O1  . PEG L  8  .   ? 134.290 -5.811  43.499  1.00 110.49 ?  808 PEG A O1  1 
HETATM 20178 C  C2  . PEG L  8  .   ? 132.778 -7.374  42.437  1.00 110.52 ?  808 PEG A C2  1 
HETATM 20179 O  O2  . PEG L  8  .   ? 131.532 -6.690  42.512  1.00 130.06 ?  808 PEG A O2  1 
HETATM 20180 C  C3  . PEG L  8  .   ? 130.597 -7.044  41.496  1.00 103.49 ?  808 PEG A C3  1 
HETATM 20181 C  C4  . PEG L  8  .   ? 129.209 -6.978  42.061  1.00 94.11  ?  808 PEG A C4  1 
HETATM 20182 O  O4  . PEG L  8  .   ? 128.913 -5.688  42.576  1.00 83.12  ?  808 PEG A O4  1 
HETATM 20183 CA CA  . CA  M  9  .   ? 142.198 -36.378 40.003  1.00 125.21 2  809 CA  A CA  1 
HETATM 20184 CA CA  . CA  N  9  .   ? 103.090 -38.648 53.518  1.00 136.67 ?  810 CA  A CA  1 
HETATM 20185 CA CA  . CA  O  9  .   ? 107.078 -25.055 55.805  1.00 118.18 ?  811 CA  A CA  1 
HETATM 20186 CA CA  . CA  P  9  .   ? 131.557 4.147   49.404  1.00 124.39 ?  812 CA  A CA  1 
HETATM 20187 CL CL  . CL  Q  10 .   ? 118.238 -13.985 34.256  1.00 94.46  ?  813 CL  A CL  1 
HETATM 20188 CL CL  . CL  R  10 .   ? 125.751 -36.483 31.085  1.00 105.60 ?  814 CL  A CL  1 
HETATM 20189 C  C1  . EDO S  5  .   ? 142.561 -19.399 27.610  1.00 99.81  ?  815 EDO A C1  1 
HETATM 20190 O  O1  . EDO S  5  .   ? 142.486 -20.638 28.310  1.00 118.33 ?  815 EDO A O1  1 
HETATM 20191 C  C2  . EDO S  5  .   ? 141.454 -19.343 26.583  1.00 104.27 ?  815 EDO A C2  1 
HETATM 20192 O  O2  . EDO S  5  .   ? 141.552 -20.449 25.697  1.00 120.53 ?  815 EDO A O2  1 
HETATM 20193 C  C1  . EDO T  5  .   ? 121.382 -30.178 20.843  1.00 74.74  ?  816 EDO A C1  1 
HETATM 20194 O  O1  . EDO T  5  .   ? 122.495 -31.013 21.114  1.00 85.15  ?  816 EDO A O1  1 
HETATM 20195 C  C2  . EDO T  5  .   ? 120.812 -30.523 19.489  1.00 100.03 ?  816 EDO A C2  1 
HETATM 20196 O  O2  . EDO T  5  .   ? 121.717 -30.126 18.470  1.00 72.75  ?  816 EDO A O2  1 
HETATM 20197 C  C1  . EDO U  5  .   ? 90.983  -35.696 -26.731 1.00 108.29 ?  817 EDO A C1  1 
HETATM 20198 O  O1  . EDO U  5  .   ? 91.599  -35.308 -25.512 1.00 124.25 ?  817 EDO A O1  1 
HETATM 20199 C  C2  . EDO U  5  .   ? 91.427  -37.085 -27.132 1.00 91.62  ?  817 EDO A C2  1 
HETATM 20200 O  O2  . EDO U  5  .   ? 90.862  -38.050 -26.259 1.00 88.59  ?  817 EDO A O2  1 
HETATM 20201 C  C1  . EDO V  5  .   ? 137.158 -8.907  47.858  1.00 93.20  ?  818 EDO A C1  1 
HETATM 20202 O  O1  . EDO V  5  .   ? 137.768 -8.083  48.839  1.00 97.50  ?  818 EDO A O1  1 
HETATM 20203 C  C2  . EDO V  5  .   ? 136.735 -8.097  46.635  1.00 100.85 ?  818 EDO A C2  1 
HETATM 20204 O  O2  . EDO V  5  .   ? 137.529 -8.421  45.501  1.00 86.11  ?  818 EDO A O2  1 
HETATM 20205 C  C1  . EDO W  5  .   ? 124.758 -10.828 63.546  1.00 100.99 ?  819 EDO A C1  1 
HETATM 20206 O  O1  . EDO W  5  .   ? 126.153 -10.730 63.342  1.00 96.72  ?  819 EDO A O1  1 
HETATM 20207 C  C2  . EDO W  5  .   ? 124.019 -9.612  63.132  1.00 97.24  ?  819 EDO A C2  1 
HETATM 20208 O  O2  . EDO W  5  .   ? 123.251 -9.798  61.960  1.00 83.89  ?  819 EDO A O2  1 
HETATM 20209 C  C1  . EDO X  5  .   ? 123.356 -22.153 58.789  1.00 117.14 ?  820 EDO A C1  1 
HETATM 20210 O  O1  . EDO X  5  .   ? 124.336 -22.785 57.990  1.00 92.70  ?  820 EDO A O1  1 
HETATM 20211 C  C2  . EDO X  5  .   ? 121.978 -22.328 58.271  1.00 107.72 ?  820 EDO A C2  1 
HETATM 20212 O  O2  . EDO X  5  .   ? 121.633 -23.680 58.047  1.00 99.32  ?  820 EDO A O2  1 
HETATM 20213 C  C1  . GOL Y  7  .   ? 115.185 16.510  5.972   1.00 87.38  ?  701 GOL B C1  1 
HETATM 20214 O  O1  . GOL Y  7  .   ? 114.647 17.295  7.033   1.00 79.20  ?  701 GOL B O1  1 
HETATM 20215 C  C2  . GOL Y  7  .   ? 114.242 16.470  4.789   1.00 110.42 ?  701 GOL B C2  1 
HETATM 20216 O  O2  . GOL Y  7  .   ? 112.962 15.981  5.202   1.00 114.24 ?  701 GOL B O2  1 
HETATM 20217 C  C3  . GOL Y  7  .   ? 114.086 17.820  4.123   1.00 88.25  ?  701 GOL B C3  1 
HETATM 20218 O  O3  . GOL Y  7  .   ? 115.317 18.269  3.575   1.00 80.90  ?  701 GOL B O3  1 
HETATM 20219 FE FE1 . SF4 Z  3  .   ? 99.267  50.698  48.804  1.00 55.28  ?  702 SF4 B FE1 1 
HETATM 20220 FE FE2 . SF4 Z  3  .   ? 97.947  48.738  50.028  1.00 54.11  ?  702 SF4 B FE2 1 
HETATM 20221 FE FE3 . SF4 Z  3  .   ? 99.362  48.241  47.823  1.00 62.91  ?  702 SF4 B FE3 1 
HETATM 20222 FE FE4 . SF4 Z  3  .   ? 97.161  49.618  47.629  1.00 55.65  ?  702 SF4 B FE4 1 
HETATM 20223 S  S1  . SF4 Z  3  .   ? 97.270  47.407  48.271  1.00 53.68  ?  702 SF4 B S1  1 
HETATM 20224 S  S2  . SF4 Z  3  .   ? 99.108  50.141  46.564  1.00 69.10  ?  702 SF4 B S2  1 
HETATM 20225 S  S3  . SF4 Z  3  .   ? 97.122  50.856  49.577  1.00 74.49  ?  702 SF4 B S3  1 
HETATM 20226 S  S4  . SF4 Z  3  .   ? 100.227 48.876  49.876  1.00 72.03  ?  702 SF4 B S4  1 
HETATM 20227 C  C1  . PEG AA 8  .   ? 105.271 0.123   51.747  1.00 85.03  ?  703 PEG B C1  1 
HETATM 20228 O  O1  . PEG AA 8  .   ? 105.153 -1.000  50.886  1.00 83.14  ?  703 PEG B O1  1 
HETATM 20229 C  C2  . PEG AA 8  .   ? 103.929 0.657   52.159  1.00 87.42  ?  703 PEG B C2  1 
HETATM 20230 O  O2  . PEG AA 8  .   ? 103.826 0.619   53.584  1.00 108.79 ?  703 PEG B O2  1 
HETATM 20231 C  C3  . PEG AA 8  .   ? 102.510 0.407   54.106  1.00 116.37 ?  703 PEG B C3  1 
HETATM 20232 C  C4  . PEG AA 8  .   ? 101.865 1.725   54.435  1.00 104.72 ?  703 PEG B C4  1 
HETATM 20233 O  O4  . PEG AA 8  .   ? 100.489 1.747   54.075  1.00 96.28  ?  703 PEG B O4  1 
HETATM 20234 C  C1  . GOL BA 7  .   ? 123.806 45.947  25.517  1.00 95.83  ?  704 GOL B C1  1 
HETATM 20235 O  O1  . GOL BA 7  .   ? 124.177 46.907  26.498  1.00 96.04  ?  704 GOL B O1  1 
HETATM 20236 C  C2  . GOL BA 7  .   ? 123.683 46.574  24.145  1.00 97.36  ?  704 GOL B C2  1 
HETATM 20237 O  O2  . GOL BA 7  .   ? 122.465 47.320  24.064  1.00 104.90 ?  704 GOL B O2  1 
HETATM 20238 C  C3  . GOL BA 7  .   ? 123.735 45.545  23.037  1.00 90.32  ?  704 GOL B C3  1 
HETATM 20239 O  O3  . GOL BA 7  .   ? 123.509 46.142  21.767  1.00 98.20  ?  704 GOL B O3  1 
HETATM 20240 FE FE1 . XCC CA 11 .   ? 107.627 28.867  28.798  1.00 64.91  ?  705 XCC B FE1 1 
HETATM 20241 FE FE2 . XCC CA 11 .   ? 106.542 25.584  27.934  1.00 75.70  ?  705 XCC B FE2 1 
HETATM 20242 FE FE3 . XCC CA 11 .   ? 109.182 27.648  31.288  1.00 69.28  ?  705 XCC B FE3 1 
HETATM 20243 FE FE4 . XCC CA 11 .   ? 109.926 26.587  28.307  1.00 60.60  ?  705 XCC B FE4 1 
HETATM 20244 S  S1  . XCC CA 11 .   ? 109.250 25.846  30.193  1.00 62.29  ?  705 XCC B S1  1 
HETATM 20245 S  S2  . XCC CA 11 .   ? 109.559 28.353  29.373  1.00 45.79  ?  705 XCC B S2  1 
HETATM 20246 S  S4  . XCC CA 11 .   ? 107.033 27.756  30.662  1.00 52.97  ?  705 XCC B S4  1 
HETATM 20247 S  S3  . XCC CA 11 .   ? 107.980 27.123  27.621  1.00 55.55  ?  705 XCC B S3  1 
HETATM 20248 NI NI  . XCC CA 11 .   ? 107.102 25.075  30.397  1.00 88.03  ?  705 XCC B NI  1 
HETATM 20249 C  C1  . GOL DA 7  .   ? 96.307  -1.916  48.200  1.00 88.65  ?  706 GOL B C1  1 
HETATM 20250 O  O1  . GOL DA 7  .   ? 95.420  -0.825  47.970  1.00 93.98  ?  706 GOL B O1  1 
HETATM 20251 C  C2  . GOL DA 7  .   ? 97.084  -1.738  49.488  1.00 96.69  ?  706 GOL B C2  1 
HETATM 20252 O  O2  . GOL DA 7  .   ? 96.249  -2.015  50.611  1.00 107.73 ?  706 GOL B O2  1 
HETATM 20253 C  C3  . GOL DA 7  .   ? 98.344  -2.575  49.552  1.00 96.02  ?  706 GOL B C3  1 
HETATM 20254 O  O3  . GOL DA 7  .   ? 99.069  -2.339  50.756  1.00 103.77 ?  706 GOL B O3  1 
HETATM 20255 C  C1  . GOL EA 7  .   ? 120.813 30.053  50.797  1.00 118.79 ?  707 GOL B C1  1 
HETATM 20256 O  O1  . GOL EA 7  .   ? 121.342 29.247  51.846  1.00 114.25 ?  707 GOL B O1  1 
HETATM 20257 C  C2  . GOL EA 7  .   ? 121.001 29.397  49.445  1.00 116.50 ?  707 GOL B C2  1 
HETATM 20258 O  O2  . GOL EA 7  .   ? 120.718 30.328  48.401  1.00 103.87 ?  707 GOL B O2  1 
HETATM 20259 C  C3  . GOL EA 7  .   ? 122.375 28.792  49.252  1.00 93.82  ?  707 GOL B C3  1 
HETATM 20260 O  O3  . GOL EA 7  .   ? 122.698 28.650  47.871  1.00 79.61  ?  707 GOL B O3  1 
HETATM 20261 CA CA  . CA  FA 9  .   ? 92.549  9.000   32.289  1.00 122.27 ?  708 CA  B CA  1 
HETATM 20262 CL CL  . CL  GA 10 .   ? 98.494  1.017   37.908  1.00 68.11  ?  709 CL  B CL  1 
HETATM 20263 CL CL  . CL  HA 10 .   ? 119.509 35.707  5.981   1.00 78.56  ?  710 CL  B CL  1 
HETATM 20264 CL CL  . CL  IA 10 .   ? 118.124 43.883  17.412  1.00 96.97  ?  711 CL  B CL  1 
HETATM 20265 CL CL  . CL  JA 10 .   ? 129.273 19.451  31.746  1.00 122.12 ?  712 CL  B CL  1 
HETATM 20266 CL CL  . CL  KA 10 .   ? 129.423 36.949  25.040  1.00 98.17  ?  713 CL  B CL  1 
HETATM 20267 C  C1  . EDO LA 5  .   ? 95.756  -6.633  31.941  1.00 88.31  ?  714 EDO B C1  1 
HETATM 20268 O  O1  . EDO LA 5  .   ? 96.126  -7.774  31.181  1.00 87.81  ?  714 EDO B O1  1 
HETATM 20269 C  C2  . EDO LA 5  .   ? 95.520  -7.027  33.385  1.00 120.86 ?  714 EDO B C2  1 
HETATM 20270 O  O2  . EDO LA 5  .   ? 95.760  -5.928  34.254  1.00 93.12  ?  714 EDO B O2  1 
HETATM 20271 C  C1  . EDO MA 5  .   ? 96.306  3.460   23.948  1.00 91.30  ?  715 EDO B C1  1 
HETATM 20272 O  O1  . EDO MA 5  .   ? 97.142  4.525   24.375  1.00 74.89  ?  715 EDO B O1  1 
HETATM 20273 C  C2  . EDO MA 5  .   ? 96.581  3.126   22.494  1.00 100.11 ?  715 EDO B C2  1 
HETATM 20274 O  O2  . EDO MA 5  .   ? 95.466  2.464   21.912  1.00 94.11  ?  715 EDO B O2  1 
HETATM 20275 C  C1  . EDO NA 5  .   ? 112.867 4.184   20.433  1.00 63.06  ?  716 EDO B C1  1 
HETATM 20276 O  O1  . EDO NA 5  .   ? 114.148 4.523   19.929  1.00 80.77  ?  716 EDO B O1  1 
HETATM 20277 C  C2  . EDO NA 5  .   ? 111.841 4.301   19.333  1.00 72.87  ?  716 EDO B C2  1 
HETATM 20278 O  O2  . EDO NA 5  .   ? 112.053 3.294   18.358  1.00 77.42  ?  716 EDO B O2  1 
HETATM 20279 C  C1  . EDO OA 5  .   ? 108.002 21.919  61.830  1.00 86.17  ?  717 EDO B C1  1 
HETATM 20280 O  O1  . EDO OA 5  .   ? 106.696 21.501  61.469  1.00 78.20  ?  717 EDO B O1  1 
HETATM 20281 C  C2  . EDO OA 5  .   ? 108.996 21.145  61.021  1.00 73.85  ?  717 EDO B C2  1 
HETATM 20282 O  O2  . EDO OA 5  .   ? 108.659 21.289  59.654  1.00 94.30  ?  717 EDO B O2  1 
HETATM 20283 C  C1  . EDO PA 5  .   ? 118.520 43.291  6.669   1.00 92.04  ?  718 EDO B C1  1 
HETATM 20284 O  O1  . EDO PA 5  .   ? 119.209 42.058  6.709   1.00 108.68 ?  718 EDO B O1  1 
HETATM 20285 C  C2  . EDO PA 5  .   ? 117.062 43.142  6.442   1.00 94.12  ?  718 EDO B C2  1 
HETATM 20286 O  O2  . EDO PA 5  .   ? 116.741 42.129  5.510   1.00 100.89 ?  718 EDO B O2  1 
HETATM 20287 C  C1  . EDO QA 5  .   ? 123.514 42.151  9.863   1.00 104.11 ?  719 EDO B C1  1 
HETATM 20288 O  O1  . EDO QA 5  .   ? 122.457 43.081  9.759   1.00 106.53 ?  719 EDO B O1  1 
HETATM 20289 C  C2  . EDO QA 5  .   ? 123.088 40.752  9.621   1.00 97.40  ?  719 EDO B C2  1 
HETATM 20290 O  O2  . EDO QA 5  .   ? 121.875 40.650  8.902   1.00 108.08 ?  719 EDO B O2  1 
HETATM 20291 C  C1  . EDO RA 5  .   ? 94.780  31.911  7.165   1.00 72.05  ?  720 EDO B C1  1 
HETATM 20292 O  O1  . EDO RA 5  .   ? 95.470  32.811  8.008   1.00 56.59  ?  720 EDO B O1  1 
HETATM 20293 C  C2  . EDO RA 5  .   ? 93.306  31.993  7.306   1.00 80.23  ?  720 EDO B C2  1 
HETATM 20294 O  O2  . EDO RA 5  .   ? 92.615  31.074  6.484   1.00 88.43  ?  720 EDO B O2  1 
HETATM 20295 C  C1  . EDO SA 5  .   ? 106.309 13.701  55.783  1.00 102.85 ?  721 EDO B C1  1 
HETATM 20296 O  O1  . EDO SA 5  .   ? 107.555 13.049  55.634  1.00 99.83  ?  721 EDO B O1  1 
HETATM 20297 C  C2  . EDO SA 5  .   ? 105.234 13.106  54.953  1.00 105.19 ?  721 EDO B C2  1 
HETATM 20298 O  O2  . EDO SA 5  .   ? 105.220 11.693  54.988  1.00 122.25 ?  721 EDO B O2  1 
HETATM 20299 C  C1  . EDO TA 5  .   ? 98.650  9.957   30.640  1.00 93.06  ?  722 EDO B C1  1 
HETATM 20300 O  O1  . EDO TA 5  .   ? 99.871  10.050  29.927  1.00 75.73  ?  722 EDO B O1  1 
HETATM 20301 C  C2  . EDO TA 5  .   ? 98.245  11.237  31.259  1.00 71.80  ?  722 EDO B C2  1 
HETATM 20302 O  O2  . EDO TA 5  .   ? 98.216  11.171  32.670  1.00 75.98  ?  722 EDO B O2  1 
HETATM 20303 C  C1  . EDO UA 5  .   ? 88.348  6.755   41.376  1.00 108.20 ?  723 EDO B C1  1 
HETATM 20304 O  O1  . EDO UA 5  .   ? 88.348  8.088   41.847  1.00 106.68 ?  723 EDO B O1  1 
HETATM 20305 C  C2  . EDO UA 5  .   ? 89.628  6.046   41.594  1.00 97.22  ?  723 EDO B C2  1 
HETATM 20306 O  O2  . EDO UA 5  .   ? 90.054  6.075   42.939  1.00 98.87  ?  723 EDO B O2  1 
HETATM 20307 C  C1  . EDO VA 5  .   ? 87.243  20.733  9.219   1.00 89.12  ?  724 EDO B C1  1 
HETATM 20308 O  O1  . EDO VA 5  .   ? 87.558  19.710  8.294   1.00 112.98 ?  724 EDO B O1  1 
HETATM 20309 C  C2  . EDO VA 5  .   ? 86.720  20.221  10.509  1.00 100.65 ?  724 EDO B C2  1 
HETATM 20310 O  O2  . EDO VA 5  .   ? 87.735  19.891  11.437  1.00 96.13  ?  724 EDO B O2  1 
HETATM 20311 C  C1  . EDO WA 5  .   ? 91.752  3.378   16.706  1.00 110.84 ?  725 EDO B C1  1 
HETATM 20312 O  O1  . EDO WA 5  .   ? 92.576  4.187   17.524  1.00 82.13  ?  725 EDO B O1  1 
HETATM 20313 C  C2  . EDO WA 5  .   ? 91.130  4.123   15.585  1.00 105.96 ?  725 EDO B C2  1 
HETATM 20314 O  O2  . EDO WA 5  .   ? 92.075  4.696   14.703  1.00 89.30  ?  725 EDO B O2  1 
HETATM 20315 C  C1  . EDO XA 5  .   ? 75.999  25.871  36.225  1.00 93.04  ?  726 EDO B C1  1 
HETATM 20316 O  O1  . EDO XA 5  .   ? 76.615  26.831  37.060  1.00 89.27  ?  726 EDO B O1  1 
HETATM 20317 C  C2  . EDO XA 5  .   ? 76.494  24.492  36.455  1.00 93.49  ?  726 EDO B C2  1 
HETATM 20318 O  O2  . EDO XA 5  .   ? 75.837  23.522  35.663  1.00 113.78 ?  726 EDO B O2  1 
HETATM 20319 C  C1  . EDO YA 5  .   ? 100.195 8.545   17.194  1.00 101.42 ?  727 EDO B C1  1 
HETATM 20320 O  O1  . EDO YA 5  .   ? 101.335 9.167   17.752  1.00 66.20  ?  727 EDO B O1  1 
HETATM 20321 C  C2  . EDO YA 5  .   ? 99.629  9.288   16.042  1.00 91.23  ?  727 EDO B C2  1 
HETATM 20322 O  O2  . EDO YA 5  .   ? 98.663  8.549   15.322  1.00 92.32  ?  727 EDO B O2  1 
HETATM 20323 C  C1  . EDO ZA 5  .   ? 90.461  14.812  34.010  1.00 89.24  ?  728 EDO B C1  1 
HETATM 20324 O  O1  . EDO ZA 5  .   ? 89.903  15.759  34.900  1.00 83.96  ?  728 EDO B O1  1 
HETATM 20325 C  C2  . EDO ZA 5  .   ? 90.080  13.414  34.326  1.00 73.87  ?  728 EDO B C2  1 
HETATM 20326 O  O2  . EDO ZA 5  .   ? 88.932  12.976  33.629  1.00 72.25  ?  728 EDO B O2  1 
HETATM 20327 FE FE1 . SF4 AB 3  .   ? 110.683 48.564  42.391  1.00 44.09  ?  701 SF4 C FE1 1 
HETATM 20328 FE FE2 . SF4 AB 3  .   ? 108.909 48.516  40.456  1.00 53.47  ?  701 SF4 C FE2 1 
HETATM 20329 FE FE3 . SF4 AB 3  .   ? 109.381 50.770  41.747  1.00 49.04  ?  701 SF4 C FE3 1 
HETATM 20330 FE FE4 . SF4 AB 3  .   ? 108.139 48.754  42.923  1.00 53.72  ?  701 SF4 C FE4 1 
HETATM 20331 S  S1  . SF4 AB 3  .   ? 107.302 49.981  41.162  1.00 56.12  ?  701 SF4 C S1  1 
HETATM 20332 S  S2  . SF4 AB 3  .   ? 109.779 50.019  43.902  1.00 58.87  ?  701 SF4 C S2  1 
HETATM 20333 S  S3  . SF4 AB 3  .   ? 109.141 46.892  42.079  1.00 59.67  ?  701 SF4 C S3  1 
HETATM 20334 S  S4  . SF4 AB 3  .   ? 110.885 49.711  40.386  1.00 60.60  ?  701 SF4 C S4  1 
HETATM 20335 FE FE1 . SF4 BB 3  .   ? 109.563 39.434  32.592  1.00 57.33  ?  702 SF4 C FE1 1 
HETATM 20336 FE FE2 . SF4 BB 3  .   ? 109.460 40.910  30.358  1.00 43.29  ?  702 SF4 C FE2 1 
HETATM 20337 FE FE3 . SF4 BB 3  .   ? 110.755 41.781  32.549  1.00 50.12  ?  702 SF4 C FE3 1 
HETATM 20338 FE FE4 . SF4 BB 3  .   ? 108.129 41.614  32.562  1.00 43.00  ?  702 SF4 C FE4 1 
HETATM 20339 S  S1  . SF4 BB 3  .   ? 109.344 43.037  31.218  1.00 66.72  ?  702 SF4 C S1  1 
HETATM 20340 S  S2  . SF4 BB 3  .   ? 109.470 40.964  34.285  1.00 58.90  ?  702 SF4 C S2  1 
HETATM 20341 S  S3  . SF4 BB 3  .   ? 107.690 39.771  31.296  1.00 52.91  ?  702 SF4 C S3  1 
HETATM 20342 S  S4  . SF4 BB 3  .   ? 111.374 39.972  31.255  1.00 71.76  ?  702 SF4 C S4  1 
HETATM 20343 C  C1  . EDO CB 5  .   ? 81.722  63.075  19.444  1.00 96.84  ?  703 EDO C C1  1 
HETATM 20344 O  O1  . EDO CB 5  .   ? 82.178  61.848  18.892  1.00 93.11  ?  703 EDO C O1  1 
HETATM 20345 C  C2  . EDO CB 5  .   ? 82.320  64.253  18.700  1.00 94.67  ?  703 EDO C C2  1 
HETATM 20346 O  O2  . EDO CB 5  .   ? 82.431  65.381  19.558  1.00 91.69  ?  703 EDO C O2  1 
HETATM 20347 FE FE1 . XCC DB 11 .   ? 85.481  50.401  46.401  1.00 123.92 ?  704 XCC C FE1 1 
HETATM 20348 FE FE2 . XCC DB 11 .   ? 82.227  50.341  47.763  1.00 126.45 ?  704 XCC C FE2 1 
HETATM 20349 FE FE3 . XCC DB 11 .   ? 85.375  53.590  45.310  1.00 119.24 ?  704 XCC C FE3 1 
HETATM 20350 FE FE4 . XCC DB 11 .   ? 84.541  52.813  48.540  1.00 81.30  ?  704 XCC C FE4 1 
HETATM 20351 S  S1  . XCC DB 11 .   ? 83.788  53.562  46.751  1.00 107.05 ?  704 XCC C S1  1 
HETATM 20352 S  S2  . XCC DB 11 .   ? 85.925  52.454  46.962  1.00 55.75  ?  704 XCC C S2  1 
HETATM 20353 S  S4  . XCC DB 11 .   ? 84.562  51.482  44.741  1.00 65.28  ?  704 XCC C S4  1 
HETATM 20354 S  S3  . XCC DB 11 .   ? 84.138  50.662  48.117  1.00 74.15  ?  704 XCC C S3  1 
HETATM 20355 NI NI  . XCC DB 11 .   ? 82.377  52.087  45.798  1.00 128.89 ?  704 XCC C NI  1 
HETATM 20356 CA CA  . CA  EB 9  .   ? 78.574  32.801  63.125  1.00 103.08 2  705 CA  C CA  1 
HETATM 20357 CA CA  . CA  FB 9  .   ? 61.464  61.362  50.903  1.00 123.14 ?  706 CA  C CA  1 
HETATM 20358 CA CA  . CA  GB 9  .   ? 70.210  40.884  33.348  1.00 123.48 ?  707 CA  C CA  1 
HETATM 20359 CL CL  . CL  HB 10 .   ? 61.863  53.679  28.902  1.00 83.58  ?  708 CL  C CL  1 
HETATM 20360 C  C1  . EDO IB 5  .   ? 62.621  47.314  51.455  1.00 104.51 ?  709 EDO C C1  1 
HETATM 20361 O  O1  . EDO IB 5  .   ? 61.990  46.042  51.441  1.00 98.77  ?  709 EDO C O1  1 
HETATM 20362 C  C2  . EDO IB 5  .   ? 62.507  47.973  50.094  1.00 90.75  ?  709 EDO C C2  1 
HETATM 20363 O  O2  . EDO IB 5  .   ? 62.580  49.387  50.215  1.00 84.50  ?  709 EDO C O2  1 
HETATM 20364 C  C1  . EDO JB 5  .   ? 83.654  77.249  27.822  1.00 105.29 ?  710 EDO C C1  1 
HETATM 20365 O  O1  . EDO JB 5  .   ? 83.991  76.691  29.082  1.00 111.87 ?  710 EDO C O1  1 
HETATM 20366 C  C2  . EDO JB 5  .   ? 82.153  77.395  27.692  1.00 121.50 ?  710 EDO C C2  1 
HETATM 20367 O  O2  . EDO JB 5  .   ? 81.525  76.123  27.674  1.00 108.15 ?  710 EDO C O2  1 
HETATM 20368 C  C1  . EDO KB 5  .   ? 90.778  62.390  17.184  1.00 80.74  ?  711 EDO C C1  1 
HETATM 20369 O  O1  . EDO KB 5  .   ? 92.036  61.782  16.938  1.00 74.63  ?  711 EDO C O1  1 
HETATM 20370 C  C2  . EDO KB 5  .   ? 89.709  61.330  17.263  1.00 81.20  ?  711 EDO C C2  1 
HETATM 20371 O  O2  . EDO KB 5  .   ? 89.280  60.991  15.956  1.00 85.29  ?  711 EDO C O2  1 
HETATM 20372 C  C1  . EDO LB 5  .   ? 64.989  44.304  33.286  1.00 100.70 ?  712 EDO C C1  1 
HETATM 20373 O  O1  . EDO LB 5  .   ? 66.086  45.189  33.478  1.00 98.08  ?  712 EDO C O1  1 
HETATM 20374 C  C2  . EDO LB 5  .   ? 65.480  42.925  32.877  1.00 108.55 ?  712 EDO C C2  1 
HETATM 20375 O  O2  . EDO LB 5  .   ? 64.526  42.268  32.050  1.00 111.11 ?  712 EDO C O2  1 
HETATM 20376 C  C1  . EDO MB 5  .   ? 119.669 55.281  25.615  1.00 101.57 ?  713 EDO C C1  1 
HETATM 20377 O  O1  . EDO MB 5  .   ? 119.927 56.579  26.112  1.00 110.84 ?  713 EDO C O1  1 
HETATM 20378 C  C2  . EDO MB 5  .   ? 118.387 55.181  24.878  1.00 100.92 ?  713 EDO C C2  1 
HETATM 20379 O  O2  . EDO MB 5  .   ? 118.147 53.894  24.345  1.00 111.71 ?  713 EDO C O2  1 
HETATM 20380 C  C1  . EDO NB 5  .   ? 79.929  24.586  29.409  1.00 83.08  ?  714 EDO C C1  1 
HETATM 20381 O  O1  . EDO NB 5  .   ? 80.196  23.199  29.482  1.00 82.65  ?  714 EDO C O1  1 
HETATM 20382 C  C2  . EDO NB 5  .   ? 79.049  24.952  28.274  1.00 81.04  ?  714 EDO C C2  1 
HETATM 20383 O  O2  . EDO NB 5  .   ? 78.271  26.107  28.521  1.00 83.61  ?  714 EDO C O2  1 
HETATM 20384 FE FE1 . SF4 OB 3  .   ? 20.264  93.015  43.574  1.00 70.39  ?  801 SF4 D FE1 1 
HETATM 20385 FE FE2 . SF4 OB 3  .   ? 19.784  95.621  43.247  1.00 72.03  ?  801 SF4 D FE2 1 
HETATM 20386 FE FE3 . SF4 OB 3  .   ? 17.761  93.880  43.270  1.00 73.55  ?  801 SF4 D FE3 1 
HETATM 20387 FE FE4 . SF4 OB 3  .   ? 19.450  93.937  41.240  1.00 72.23  ?  801 SF4 D FE4 1 
HETATM 20388 S  S1  . SF4 OB 3  .   ? 18.003  95.633  41.792  1.00 81.33  ?  801 SF4 D S1  1 
HETATM 20389 S  S2  . SF4 OB 3  .   ? 18.685  92.019  42.248  1.00 93.96  ?  801 SF4 D S2  1 
HETATM 20390 S  S3  . SF4 OB 3  .   ? 21.471  94.444  42.219  1.00 85.18  ?  801 SF4 D S3  1 
HETATM 20391 S  S4  . SF4 OB 3  .   ? 19.108  94.357  45.062  1.00 94.13  ?  801 SF4 D S4  1 
HETATM 20392 NI NI  . NI  PB 4  .   ? 18.504  95.197  39.064  1.00 75.38  ?  802 NI  D NI  1 
HETATM 20393 NI NI  . NI  QB 4  .   ? 17.092  97.070  37.420  1.00 53.46  ?  803 NI  D NI  1 
HETATM 20394 C  C1  . PEG RB 8  .   ? 65.668  90.201  34.588  1.00 111.77 ?  804 PEG D C1  1 
HETATM 20395 O  O1  . PEG RB 8  .   ? 67.043  90.532  34.490  1.00 103.74 ?  804 PEG D O1  1 
HETATM 20396 C  C2  . PEG RB 8  .   ? 65.469  88.957  35.401  1.00 118.43 ?  804 PEG D C2  1 
HETATM 20397 O  O2  . PEG RB 8  .   ? 64.165  88.423  35.168  1.00 121.63 ?  804 PEG D O2  1 
HETATM 20398 C  C3  . PEG RB 8  .   ? 64.073  87.503  34.079  1.00 120.61 ?  804 PEG D C3  1 
HETATM 20399 C  C4  . PEG RB 8  .   ? 64.413  86.114  34.537  1.00 118.01 ?  804 PEG D C4  1 
HETATM 20400 O  O4  . PEG RB 8  .   ? 64.160  85.158  33.520  1.00 94.53  ?  804 PEG D O4  1 
HETATM 20401 N  N1A . ACO SB 12 .   ? 10.496  94.828  30.536  1.00 131.69 ?  805 ACO D N1A 1 
HETATM 20402 C  C2A . ACO SB 12 .   ? 11.116  95.853  29.906  1.00 149.31 ?  805 ACO D C2A 1 
HETATM 20403 N  N3A . ACO SB 12 .   ? 10.920  96.047  28.584  1.00 157.86 ?  805 ACO D N3A 1 
HETATM 20404 C  C4A . ACO SB 12 .   ? 10.110  95.222  27.897  1.00 160.31 ?  805 ACO D C4A 1 
HETATM 20405 C  C5A . ACO SB 12 .   ? 9.493   94.206  28.511  1.00 151.92 ?  805 ACO D C5A 1 
HETATM 20406 C  C6A . ACO SB 12 .   ? 9.699   94.017  29.860  1.00 143.43 ?  805 ACO D C6A 1 
HETATM 20407 N  N6A . ACO SB 12 .   ? 9.080   92.946  30.618  1.00 134.53 ?  805 ACO D N6A 1 
HETATM 20408 N  N7A . ACO SB 12 .   ? 8.744   93.531  27.604  1.00 145.32 ?  805 ACO D N7A 1 
HETATM 20409 C  C8A . ACO SB 12 .   ? 8.865   94.103  26.395  1.00 148.45 ?  805 ACO D C8A 1 
HETATM 20410 N  N9A . ACO SB 12 .   ? 9.702   95.100  26.635  1.00 168.22 ?  805 ACO D N9A 1 
HETATM 20411 C  C1B . ACO SB 12 .   ? 9.993   95.858  25.584  1.00 181.27 ?  805 ACO D C1B 1 
HETATM 20412 C  C2B . ACO SB 12 .   ? 11.224  96.755  25.812  1.00 190.22 ?  805 ACO D C2B 1 
HETATM 20413 O  O2B . ACO SB 12 .   ? 10.832  97.997  26.514  1.00 197.84 ?  805 ACO D O2B 1 
HETATM 20414 C  C3B . ACO SB 12 .   ? 11.704  97.060  24.401  1.00 204.73 ?  805 ACO D C3B 1 
HETATM 20415 O  O3B . ACO SB 12 .   ? 11.295  98.369  23.998  1.00 219.66 ?  805 ACO D O3B 1 
HETATM 20416 P  P3B . ACO SB 12 .   ? 12.375  99.597  24.177  1.00 219.98 ?  805 ACO D P3B 1 
HETATM 20417 O  O7A . ACO SB 12 .   ? 13.632  99.266  23.410  1.00 208.80 ?  805 ACO D O7A 1 
HETATM 20418 O  O8A . ACO SB 12 .   ? 11.777  100.877 23.645  1.00 208.53 ?  805 ACO D O8A 1 
HETATM 20419 O  O9A . ACO SB 12 .   ? 12.707  99.765  25.641  1.00 193.75 ?  805 ACO D O9A 1 
HETATM 20420 C  C4B . ACO SB 12 .   ? 10.953  95.935  23.491  1.00 187.43 ?  805 ACO D C4B 1 
HETATM 20421 O  O4B . ACO SB 12 .   ? 10.357  95.070  24.451  1.00 178.01 ?  805 ACO D O4B 1 
HETATM 20422 C  C5B . ACO SB 12 .   ? 11.960  95.222  22.629  1.00 192.82 ?  805 ACO D C5B 1 
HETATM 20423 O  O5B . ACO SB 12 .   ? 13.190  95.891  22.721  1.00 213.48 ?  805 ACO D O5B 1 
HETATM 20424 P  P1A . ACO SB 12 .   ? 14.359  95.620  21.587  1.00 209.71 ?  805 ACO D P1A 1 
HETATM 20425 O  O1A . ACO SB 12 .   ? 14.873  96.944  21.073  1.00 184.66 ?  805 ACO D O1A 1 
HETATM 20426 O  O2A . ACO SB 12 .   ? 13.790  94.822  20.444  1.00 195.68 ?  805 ACO D O2A 1 
HETATM 20427 O  O3A . ACO SB 12 .   ? 15.606  94.759  22.236  1.00 214.09 ?  805 ACO D O3A 1 
HETATM 20428 P  P2A . ACO SB 12 .   ? 15.452  93.836  23.593  1.00 232.11 ?  805 ACO D P2A 1 
HETATM 20429 O  O4A . ACO SB 12 .   ? 16.095  92.486  23.383  1.00 206.18 ?  805 ACO D O4A 1 
HETATM 20430 O  O5A . ACO SB 12 .   ? 13.990  93.631  23.909  1.00 209.11 ?  805 ACO D O5A 1 
HETATM 20431 O  O6A . ACO SB 12 .   ? 16.169  94.623  24.852  1.00 189.31 ?  805 ACO D O6A 1 
HETATM 20432 C  CBP . ACO SB 12 .   ? 16.460  96.970  25.246  1.00 171.92 ?  805 ACO D CBP 1 
HETATM 20433 C  CCP . ACO SB 12 .   ? 15.520  95.767  25.337  1.00 174.09 ?  805 ACO D CCP 1 
HETATM 20434 C  CDP . ACO SB 12 .   ? 16.876  97.198  23.797  1.00 187.81 ?  805 ACO D CDP 1 
HETATM 20435 C  CEP . ACO SB 12 .   ? 15.714  98.199  25.756  1.00 158.61 ?  805 ACO D CEP 1 
HETATM 20436 C  CAP . ACO SB 12 .   ? 17.696  96.689  26.107  1.00 156.10 ?  805 ACO D CAP 1 
HETATM 20437 O  OAP . ACO SB 12 .   ? 18.777  96.347  25.286  1.00 158.30 ?  805 ACO D OAP 1 
HETATM 20438 C  C9P . ACO SB 12 .   ? 18.054  97.926  26.934  1.00 149.85 ?  805 ACO D C9P 1 
HETATM 20439 O  O9P . ACO SB 12 .   ? 18.579  98.857  26.420  1.00 140.89 ?  805 ACO D O9P 1 
HETATM 20440 N  N8P . ACO SB 12 .   ? 17.746  97.959  28.359  1.00 160.21 ?  805 ACO D N8P 1 
HETATM 20441 C  C7P . ACO SB 12 .   ? 17.107  96.816  29.001  1.00 123.38 ?  805 ACO D C7P 1 
HETATM 20442 C  C6P . ACO SB 12 .   ? 18.186  95.847  29.509  1.00 112.11 ?  805 ACO D C6P 1 
HETATM 20443 C  C5P . ACO SB 12 .   ? 17.651  94.966  30.650  1.00 94.78  ?  805 ACO D C5P 1 
HETATM 20444 O  O5P . ACO SB 12 .   ? 17.485  93.808  30.466  1.00 105.26 ?  805 ACO D O5P 1 
HETATM 20445 N  N4P . ACO SB 12 .   ? 17.350  95.557  31.948  1.00 96.62  ?  805 ACO D N4P 1 
HETATM 20446 C  C3P . ACO SB 12 .   ? 16.850  94.711  33.022  1.00 85.03  ?  805 ACO D C3P 1 
HETATM 20447 C  C2P . ACO SB 12 .   ? 17.977  93.765  33.439  1.00 92.97  ?  805 ACO D C2P 1 
HETATM 20448 S  S1P . ACO SB 12 .   ? 18.079  93.671  35.248  1.00 105.86 ?  805 ACO D S1P 1 
HETATM 20449 C  C   . ACO SB 12 .   ? 16.944  92.366  35.810  1.00 90.74  ?  805 ACO D C   1 
HETATM 20450 O  O   . ACO SB 12 .   ? 15.936  92.166  35.220  1.00 86.25  ?  805 ACO D O   1 
HETATM 20451 C  CH3 . ACO SB 12 .   ? 17.280  91.523  37.037  1.00 53.02  ?  805 ACO D CH3 1 
HETATM 20452 C  C1  . GOL TB 7  .   ? 30.666  88.254  33.517  1.00 116.62 ?  806 GOL D C1  1 
HETATM 20453 O  O1  . GOL TB 7  .   ? 29.523  88.130  34.359  1.00 93.21  ?  806 GOL D O1  1 
HETATM 20454 C  C2  . GOL TB 7  .   ? 30.354  87.845  32.093  1.00 119.96 ?  806 GOL D C2  1 
HETATM 20455 O  O2  . GOL TB 7  .   ? 29.231  88.577  31.604  1.00 100.42 ?  806 GOL D O2  1 
HETATM 20456 C  C3  . GOL TB 7  .   ? 31.529  87.996  31.150  1.00 117.27 ?  806 GOL D C3  1 
HETATM 20457 O  O3  . GOL TB 7  .   ? 32.300  89.156  31.453  1.00 115.33 ?  806 GOL D O3  1 
HETATM 20458 C  C   . TRS UB 13 .   ? 21.472  105.175 29.014  1.00 90.25  ?  807 TRS D C   1 
HETATM 20459 C  C1  . TRS UB 13 .   ? 21.256  105.973 30.297  1.00 74.97  ?  807 TRS D C1  1 
HETATM 20460 C  C2  . TRS UB 13 .   ? 21.316  106.075 27.791  1.00 85.62  ?  807 TRS D C2  1 
HETATM 20461 C  C3  . TRS UB 13 .   ? 20.508  103.995 28.940  1.00 60.05  ?  807 TRS D C3  1 
HETATM 20462 N  N   . TRS UB 13 .   ? 22.871  104.631 29.023  1.00 103.76 ?  807 TRS D N   1 
HETATM 20463 O  O1  . TRS UB 13 .   ? 22.067  105.498 31.360  1.00 101.85 ?  807 TRS D O1  1 
HETATM 20464 O  O2  . TRS UB 13 .   ? 19.952  106.313 27.479  1.00 82.50  ?  807 TRS D O2  1 
HETATM 20465 O  O3  . TRS UB 13 .   ? 19.740  103.860 30.126  1.00 102.66 ?  807 TRS D O3  1 
HETATM 20466 CA CA  . CA  VB 9  .   ? 15.356  122.078 48.472  1.00 126.75 ?  808 CA  D CA  1 
HETATM 20467 CA CA  . CA  WB 9  .   ? 26.471  93.164  29.676  1.00 163.41 ?  809 CA  D CA  1 
HETATM 20468 C  C1  . EDO XB 5  .   ? 10.127  99.900  54.545  1.00 100.41 ?  810 EDO D C1  1 
HETATM 20469 O  O1  . EDO XB 5  .   ? 10.771  99.121  53.548  1.00 80.24  ?  810 EDO D O1  1 
HETATM 20470 C  C2  . EDO XB 5  .   ? 10.384  99.318  55.919  1.00 110.20 ?  810 EDO D C2  1 
HETATM 20471 O  O2  . EDO XB 5  .   ? 10.374  100.345 56.900  1.00 104.57 ?  810 EDO D O2  1 
HETATM 20472 C  C1  . EDO YB 5  .   ? 4.478   121.828 54.158  1.00 109.54 ?  811 EDO D C1  1 
HETATM 20473 O  O1  . EDO YB 5  .   ? 5.419   121.491 55.166  1.00 109.20 ?  811 EDO D O1  1 
HETATM 20474 C  C2  . EDO YB 5  .   ? 5.168   121.862 52.821  1.00 101.17 ?  811 EDO D C2  1 
HETATM 20475 O  O2  . EDO YB 5  .   ? 5.830   123.104 52.699  1.00 120.68 ?  811 EDO D O2  1 
HETATM 20476 C  C1  . EDO ZB 5  .   ? 46.190  73.541  7.357   1.00 116.78 ?  812 EDO D C1  1 
HETATM 20477 O  O1  . EDO ZB 5  .   ? 46.501  73.469  8.740   1.00 99.25  ?  812 EDO D O1  1 
HETATM 20478 C  C2  . EDO ZB 5  .   ? 44.723  73.248  7.133   1.00 119.59 ?  812 EDO D C2  1 
HETATM 20479 O  O2  . EDO ZB 5  .   ? 44.264  73.877  5.946   1.00 111.02 ?  812 EDO D O2  1 
HETATM 20480 C  C1  . EDO AC 5  .   ? 51.625  68.685  36.144  1.00 121.50 ?  813 EDO D C1  1 
HETATM 20481 O  O1  . EDO AC 5  .   ? 51.262  70.020  36.435  1.00 101.04 ?  813 EDO D O1  1 
HETATM 20482 C  C2  . EDO AC 5  .   ? 50.460  67.775  36.023  1.00 117.70 ?  813 EDO D C2  1 
HETATM 20483 O  O2  . EDO AC 5  .   ? 50.017  67.611  34.690  1.00 87.50  ?  813 EDO D O2  1 
HETATM 20484 O  O   . HOH BC 14 .   ? 128.412 -4.721  50.363  1.00 66.02  ?  901 HOH A O   1 
HETATM 20485 O  O   . HOH BC 14 .   ? 142.078 -33.440 39.655  1.00 88.84  ?  902 HOH A O   1 
HETATM 20486 O  O   . HOH CC 14 .   ? 126.967 12.896  26.737  1.00 62.16  ?  801 HOH B O   1 
HETATM 20487 O  O   . HOH CC 14 .   ? 96.972  6.804   32.365  1.00 59.95  ?  802 HOH B O   1 
HETATM 20488 O  O   . HOH CC 14 .   ? 103.311 47.650  20.734  1.00 57.86  ?  803 HOH B O   1 
HETATM 20489 O  O   . HOH CC 14 .   ? 117.323 33.382  42.361  1.00 63.09  ?  804 HOH B O   1 
HETATM 20490 O  O   . HOH CC 14 .   ? 82.002  23.582  42.130  1.00 61.53  ?  805 HOH B O   1 
HETATM 20491 O  O   . HOH DC 14 .   ? 90.055  56.099  57.791  1.00 67.34  ?  801 HOH C O   1 
HETATM 20492 O  O   . HOH DC 14 .   ? 104.346 35.823  32.937  1.00 46.68  ?  802 HOH C O   1 
HETATM 20493 O  O   . HOH DC 14 .   ? 105.538 39.579  26.944  1.00 65.55  ?  803 HOH C O   1 
HETATM 20494 O  O   . HOH DC 14 .   ? 80.160  32.120  25.222  1.00 51.57  ?  804 HOH C O   1 
HETATM 20495 O  O   . HOH DC 14 .   ? 88.990  39.016  23.988  1.00 60.85  ?  805 HOH C O   1 
HETATM 20496 O  O   . HOH EC 14 .   ? 20.858  83.295  28.168  1.00 98.54  ?  901 HOH D O   1 
HETATM 20497 O  O   . HOH EC 14 .   ? 62.517  92.720  38.006  1.00 78.68  ?  902 HOH D 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   . MET A 1   ? 1.2341 0.6472 0.8335 0.1401  0.1324  -0.0095 1   MET A N   
2     C CA  . MET A 1   ? 1.1154 0.5142 0.7230 0.1267  0.0994  -0.0067 1   MET A CA  
3     C C   . MET A 1   ? 1.1665 0.6054 0.8398 0.1257  0.0925  0.0103  1   MET A C   
4     O O   . MET A 1   ? 1.3541 0.8382 1.0623 0.1274  0.1043  0.0227  1   MET A O   
5     C CB  . MET A 1   ? 1.1665 0.5658 0.7491 0.1066  0.0772  -0.0014 1   MET A CB  
6     C CG  . MET A 1   ? 1.1969 0.5574 0.7097 0.1047  0.0777  -0.0154 1   MET A CG  
7     S SD  . MET A 1   ? 1.4997 0.8754 0.9953 0.0853  0.0556  -0.0029 1   MET A SD  
8     C CE  . MET A 1   ? 1.3052 0.6578 0.7998 0.0706  0.0167  -0.0075 1   MET A CE  
9     N N   . ASN A 2   ? 1.1320 0.5539 0.8203 0.1212  0.0722  0.0116  2   ASN A N   
10    C CA  . ASN A 2   ? 1.1891 0.6452 0.9328 0.1193  0.0639  0.0290  2   ASN A CA  
11    C C   . ASN A 2   ? 1.0991 0.5881 0.8560 0.1001  0.0474  0.0429  2   ASN A C   
12    O O   . ASN A 2   ? 0.9965 0.4769 0.7213 0.0892  0.0400  0.0388  2   ASN A O   
13    C CB  . ASN A 2   ? 1.1868 0.6097 0.9386 0.1200  0.0495  0.0274  2   ASN A CB  
14    C CG  . ASN A 2   ? 1.1643 0.5440 0.8791 0.1043  0.0282  0.0169  2   ASN A CG  
15    O OD1 . ASN A 2   ? 1.0723 0.4650 0.7854 0.0857  0.0103  0.0231  2   ASN A OD1 
16    N ND2 . ASN A 2   ? 1.4211 0.7483 1.1066 0.1116  0.0290  -0.0001 2   ASN A ND2 
17    N N   . LEU A 3   ? 1.0243 0.5497 0.8262 0.0970  0.0416  0.0591  3   LEU A N   
18    C CA  . LEU A 3   ? 0.8759 0.4318 0.6914 0.0812  0.0283  0.0710  3   LEU A CA  
19    C C   . LEU A 3   ? 1.0715 0.6043 0.8662 0.0652  0.0061  0.0681  3   LEU A C   
20    O O   . LEU A 3   ? 1.1149 0.6587 0.8988 0.0551  -0.0017 0.0701  3   LEU A O   
21    C CB  . LEU A 3   ? 0.8015 0.3924 0.6628 0.0813  0.0245  0.0869  3   LEU A CB  
22    C CG  . LEU A 3   ? 0.8040 0.4298 0.6822 0.0681  0.0148  0.0986  3   LEU A CG  
23    C CD1 . LEU A 3   ? 0.7350 0.3786 0.6027 0.0662  0.0241  0.0967  3   LEU A CD1 
24    C CD2 . LEU A 3   ? 0.6682 0.3252 0.5839 0.0707  0.0137  0.1122  3   LEU A CD2 
25    N N   . PHE A 4   ? 1.0916 0.5919 0.8826 0.0629  -0.0048 0.0636  4   PHE A N   
26    C CA  . PHE A 4   ? 0.9503 0.4306 0.7281 0.0459  -0.0274 0.0608  4   PHE A CA  
27    C C   . PHE A 4   ? 0.9961 0.4535 0.7277 0.0419  -0.0327 0.0471  4   PHE A C   
28    O O   . PHE A 4   ? 1.0519 0.5240 0.7808 0.0300  -0.0468 0.0511  4   PHE A O   
29    C CB  . PHE A 4   ? 1.0563 0.4995 0.8371 0.0437  -0.0363 0.0573  4   PHE A CB  
30    C CG  . PHE A 4   ? 0.9614 0.4268 0.7851 0.0388  -0.0408 0.0754  4   PHE A CG  
31    C CD1 . PHE A 4   ? 1.0440 0.5270 0.8924 0.0534  -0.0269 0.0850  4   PHE A CD1 
32    C CD2 . PHE A 4   ? 1.0212 0.4949 0.8612 0.0196  -0.0586 0.0842  4   PHE A CD2 
33    C CE1 . PHE A 4   ? 1.0272 0.5301 0.9087 0.0491  -0.0316 0.1030  4   PHE A CE1 
34    C CE2 . PHE A 4   ? 0.9968 0.4916 0.8720 0.0150  -0.0600 0.1022  4   PHE A CE2 
35    C CZ  . PHE A 4   ? 1.0466 0.5539 0.9390 0.0298  -0.0468 0.1116  4   PHE A CZ  
36    N N   . GLN A 5   ? 1.1258 0.5474 0.8199 0.0530  -0.0213 0.0311  5   GLN A N   
37    C CA  . GLN A 5   ? 1.0956 0.4900 0.7366 0.0502  -0.0260 0.0173  5   GLN A CA  
38    C C   . GLN A 5   ? 1.1706 0.5958 0.8047 0.0497  -0.0191 0.0254  5   GLN A C   
39    O O   . GLN A 5   ? 1.3331 0.7498 0.9375 0.0407  -0.0342 0.0230  5   GLN A O   
40    C CB  . GLN A 5   ? 1.1033 0.4535 0.7031 0.0649  -0.0098 -0.0019 5   GLN A CB  
41    C CG  . GLN A 5   ? 1.2356 0.5434 0.8341 0.0649  -0.0190 -0.0126 5   GLN A CG  
42    C CD  . GLN A 5   ? 1.3639 0.6519 0.9557 0.0433  -0.0513 -0.0154 5   GLN A CD  
43    O OE1 . GLN A 5   ? 1.3527 0.6345 0.9122 0.0326  -0.0671 -0.0209 5   GLN A OE1 
44    N NE2 . GLN A 5   ? 1.3346 0.6132 0.9582 0.0359  -0.0625 -0.0105 5   GLN A NE2 
45    N N   . THR A 6   ? 1.1702 0.6310 0.8335 0.0584  0.0013  0.0358  6   THR A N   
46    C CA  . THR A 6   ? 1.1024 0.5904 0.7628 0.0566  0.0086  0.0445  6   THR A CA  
47    C C   . THR A 6   ? 1.0600 0.5689 0.7379 0.0424  -0.0145 0.0553  6   THR A C   
48    O O   . THR A 6   ? 1.1754 0.6811 0.8274 0.0375  -0.0224 0.0564  6   THR A O   
49    C CB  . THR A 6   ? 1.0565 0.5798 0.7528 0.0661  0.0320  0.0531  6   THR A CB  
50    O OG1 . THR A 6   ? 1.1359 0.6428 0.8201 0.0809  0.0540  0.0429  6   THR A OG1 
51    C CG2 . THR A 6   ? 0.9450 0.4932 0.6404 0.0624  0.0400  0.0621  6   THR A CG2 
52    N N   . VAL A 7   ? 1.0124 0.5415 0.7333 0.0369  -0.0248 0.0637  7   VAL A N   
53    C CA  . VAL A 7   ? 0.9531 0.5058 0.6966 0.0249  -0.0437 0.0738  7   VAL A CA  
54    C C   . VAL A 7   ? 1.0316 0.5598 0.7485 0.0147  -0.0677 0.0667  7   VAL A C   
55    O O   . VAL A 7   ? 1.0727 0.6124 0.7850 0.0096  -0.0800 0.0713  7   VAL A O   
56    C CB  . VAL A 7   ? 0.8396 0.4169 0.6307 0.0214  -0.0465 0.0842  7   VAL A CB  
57    C CG1 . VAL A 7   ? 0.9401 0.5376 0.7533 0.0087  -0.0656 0.0923  7   VAL A CG1 
58    C CG2 . VAL A 7   ? 1.0351 0.6435 0.8526 0.0298  -0.0283 0.0927  7   VAL A CG2 
59    N N   . PHE A 8   ? 0.9740 0.4675 0.6739 0.0120  -0.0758 0.0552  8   PHE A N   
60    C CA  . PHE A 8   ? 1.0864 0.5555 0.7613 0.0004  -0.1016 0.0467  8   PHE A CA  
61    C C   . PHE A 8   ? 1.1133 0.5684 0.7389 0.0041  -0.1031 0.0413  8   PHE A C   
62    O O   . PHE A 8   ? 1.1578 0.6213 0.7789 -0.0035 -0.1237 0.0451  8   PHE A O   
63    C CB  . PHE A 8   ? 1.0882 0.5153 0.7479 -0.0028 -0.1079 0.0328  8   PHE A CB  
64    C CG  . PHE A 8   ? 1.0639 0.4995 0.7695 -0.0082 -0.1086 0.0405  8   PHE A CG  
65    C CD1 . PHE A 8   ? 0.9707 0.4441 0.7227 -0.0196 -0.1190 0.0559  8   PHE A CD1 
66    C CD2 . PHE A 8   ? 1.1737 0.5783 0.8748 -0.0008 -0.0978 0.0331  8   PHE A CD2 
67    C CE1 . PHE A 8   ? 1.0946 0.5741 0.8841 -0.0251 -0.1180 0.0649  8   PHE A CE1 
68    C CE2 . PHE A 8   ? 1.1351 0.5443 0.8755 -0.0054 -0.0987 0.0428  8   PHE A CE2 
69    C CZ  . PHE A 8   ? 1.1095 0.5558 0.8921 -0.0184 -0.1087 0.0592  8   PHE A CZ  
70    N N   . THR A 9   ? 1.1304 0.5653 0.7200 0.0165  -0.0807 0.0337  9   THR A N   
71    C CA  . THR A 9   ? 1.2429 0.6611 0.7795 0.0206  -0.0777 0.0300  9   THR A CA  
72    C C   . THR A 9   ? 1.2632 0.7127 0.8127 0.0183  -0.0823 0.0457  9   THR A C   
73    O O   . THR A 9   ? 1.3903 0.8284 0.9079 0.0143  -0.1007 0.0460  9   THR A O   
74    C CB  . THR A 9   ? 1.1519 0.5535 0.6598 0.0348  -0.0458 0.0226  9   THR A CB  
75    O OG1 . THR A 9   ? 1.2580 0.6244 0.7490 0.0387  -0.0436 0.0061  9   THR A OG1 
76    C CG2 . THR A 9   ? 1.3090 0.6928 0.7590 0.0385  -0.0384 0.0211  9   THR A CG2 
77    N N   . GLY A 10  ? 1.1335 0.6196 0.7278 0.0214  -0.0670 0.0582  10  GLY A N   
78    C CA  . GLY A 10  ? 1.1569 0.6700 0.7663 0.0203  -0.0693 0.0721  10  GLY A CA  
79    C C   . GLY A 10  ? 1.1783 0.7073 0.8115 0.0115  -0.0980 0.0778  10  GLY A C   
80    O O   . GLY A 10  ? 1.1987 0.7340 0.8238 0.0115  -0.1083 0.0854  10  GLY A O   
81    N N   . SER A 11  ? 1.1314 0.6671 0.7957 0.0041  -0.1107 0.0752  11  SER A N   
82    C CA  . SER A 11  ? 0.9876 0.5431 0.6816 -0.0055 -0.1367 0.0806  11  SER A CA  
83    C C   . SER A 11  ? 1.0289 0.5590 0.6828 -0.0103 -0.1623 0.0735  11  SER A C   
84    O O   . SER A 11  ? 1.0474 0.5944 0.7121 -0.0126 -0.1817 0.0807  11  SER A O   
85    C CB  . SER A 11  ? 0.9494 0.5148 0.6835 -0.0143 -0.1416 0.0800  11  SER A CB  
86    O OG  . SER A 11  ? 1.0445 0.6384 0.8185 -0.0108 -0.1230 0.0892  11  SER A OG  
87    N N   . LYS A 12  ? 1.0555 0.5445 0.6620 -0.0106 -0.1632 0.0590  12  LYS A N   
88    C CA  . LYS A 12  ? 1.1923 0.6522 0.7510 -0.0152 -0.1887 0.0504  12  LYS A CA  
89    C C   . LYS A 12  ? 1.1717 0.6286 0.6935 -0.0065 -0.1867 0.0582  12  LYS A C   
90    O O   . LYS A 12  ? 1.0881 0.5451 0.5970 -0.0097 -0.2135 0.0616  12  LYS A O   
91    C CB  . LYS A 12  ? 1.3481 0.7600 0.8577 -0.0156 -0.1859 0.0310  12  LYS A CB  
92    C CG  . LYS A 12  ? 1.2459 0.6487 0.7807 -0.0289 -0.2034 0.0217  12  LYS A CG  
93    C CD  . LYS A 12  ? 1.1868 0.5649 0.7191 -0.0242 -0.1811 0.0113  12  LYS A CD  
94    C CE  . LYS A 12  ? 1.3068 0.6325 0.7682 -0.0166 -0.1733 -0.0079 12  LYS A CE  
95    N NZ  . LYS A 12  ? 1.4017 0.7035 0.8656 -0.0094 -0.1518 -0.0182 12  LYS A NZ  
96    N N   . GLN A 13  ? 1.2281 0.6840 0.7369 0.0038  -0.1556 0.0627  13  GLN A N   
97    C CA  . GLN A 13  ? 1.1463 0.5975 0.6224 0.0109  -0.1492 0.0726  13  GLN A CA  
98    C C   . GLN A 13  ? 1.2643 0.7503 0.7837 0.0104  -0.1642 0.0882  13  GLN A C   
99    O O   . GLN A 13  ? 1.2233 0.7015 0.7166 0.0130  -0.1803 0.0954  13  GLN A O   
100   C CB  . GLN A 13  ? 1.1483 0.5999 0.6190 0.0190  -0.1111 0.0756  13  GLN A CB  
101   C CG  . GLN A 13  ? 1.2062 0.6228 0.6273 0.0235  -0.0918 0.0615  13  GLN A CG  
102   C CD  . GLN A 13  ? 1.3774 0.8041 0.8086 0.0310  -0.0538 0.0647  13  GLN A CD  
103   O OE1 . GLN A 13  ? 1.2571 0.7135 0.7257 0.0315  -0.0425 0.0777  13  GLN A OE1 
104   N NE2 . GLN A 13  ? 1.3495 0.7521 0.7487 0.0370  -0.0332 0.0521  13  GLN A NE2 
105   N N   . ALA A 14  ? 1.2150 0.7379 0.7985 0.0084  -0.1585 0.0934  14  ALA A N   
106   C CA  . ALA A 14  ? 0.9831 0.5406 0.6117 0.0095  -0.1691 0.1060  14  ALA A CA  
107   C C   . ALA A 14  ? 1.1288 0.6913 0.7632 0.0042  -0.2050 0.1061  14  ALA A C   
108   O O   . ALA A 14  ? 1.1661 0.7383 0.8041 0.0093  -0.2193 0.1159  14  ALA A O   
109   C CB  . ALA A 14  ? 0.8507 0.4431 0.5395 0.0075  -0.1556 0.1088  14  ALA A CB  
110   N N   . LEU A 15  ? 1.1177 0.6726 0.7541 -0.0061 -0.2205 0.0953  15  LEU A N   
111   C CA  . LEU A 15  ? 1.0855 0.6466 0.7304 -0.0140 -0.2569 0.0940  15  LEU A CA  
112   C C   . LEU A 15  ? 1.2213 0.7508 0.8027 -0.0094 -0.2756 0.0932  15  LEU A C   
113   O O   . LEU A 15  ? 1.3075 0.8516 0.8987 -0.0074 -0.3015 0.1014  15  LEU A O   
114   C CB  . LEU A 15  ? 1.0573 0.6084 0.7111 -0.0283 -0.2677 0.0809  15  LEU A CB  
115   C CG  . LEU A 15  ? 0.9567 0.5068 0.6116 -0.0403 -0.3076 0.0757  15  LEU A CG  
116   C CD1 . LEU A 15  ? 0.9796 0.5816 0.7043 -0.0438 -0.3240 0.0881  15  LEU A CD1 
117   C CD2 . LEU A 15  ? 1.1496 0.6752 0.7984 -0.0548 -0.3143 0.0602  15  LEU A CD2 
118   N N   . ALA A 16  ? 1.1902 0.6772 0.7062 -0.0064 -0.2618 0.0843  16  ALA A N   
119   C CA  . ALA A 16  ? 1.2595 0.7113 0.7043 -0.0019 -0.2760 0.0839  16  ALA A CA  
120   C C   . ALA A 16  ? 1.3880 0.8505 0.8318 0.0092  -0.2749 0.1024  16  ALA A C   
121   O O   . ALA A 16  ? 1.4184 0.8699 0.8314 0.0121  -0.3019 0.1082  16  ALA A O   
122   C CB  . ALA A 16  ? 1.1805 0.5891 0.5600 0.0012  -0.2510 0.0723  16  ALA A CB  
123   N N   . ALA A 17  ? 1.3734 0.8553 0.8500 0.0153  -0.2452 0.1116  17  ALA A N   
124   C CA  . ALA A 17  ? 1.2424 0.7310 0.7218 0.0254  -0.2414 0.1286  17  ALA A CA  
125   C C   . ALA A 17  ? 1.2212 0.7451 0.7541 0.0278  -0.2694 0.1375  17  ALA A C   
126   O O   . ALA A 17  ? 1.2543 0.7737 0.7742 0.0367  -0.2844 0.1498  17  ALA A O   
127   C CB  . ALA A 17  ? 1.1196 0.6204 0.6247 0.0288  -0.2042 0.1331  17  ALA A CB  
128   N N   . ALA A 18  ? 1.2226 0.7817 0.8167 0.0205  -0.2754 0.1322  18  ALA A N   
129   C CA  . ALA A 18  ? 1.1105 0.7094 0.7632 0.0224  -0.2985 0.1397  18  ALA A CA  
130   C C   . ALA A 18  ? 1.1579 0.7531 0.7959 0.0185  -0.3401 0.1381  18  ALA A C   
131   O O   . ALA A 18  ? 1.2174 0.8403 0.8916 0.0245  -0.3627 0.1475  18  ALA A O   
132   C CB  . ALA A 18  ? 1.0094 0.6455 0.7274 0.0134  -0.2903 0.1348  18  ALA A CB  
133   N N   . GLU A 19  ? 1.0157 0.5770 0.6013 0.0091  -0.3510 0.1255  19  GLU A N   
134   C CA  . GLU A 19  ? 1.1690 0.7227 0.7335 0.0036  -0.3934 0.1218  19  GLU A CA  
135   C C   . GLU A 19  ? 1.4151 0.9419 0.9218 0.0171  -0.4062 0.1335  19  GLU A C   
136   O O   . GLU A 19  ? 1.4584 1.0016 0.9786 0.0208  -0.4382 0.1400  19  GLU A O   
137   C CB  . GLU A 19  ? 1.3011 0.8207 0.8218 -0.0107 -0.4000 0.1023  19  GLU A CB  
138   C CG  . GLU A 19  ? 1.3179 0.8627 0.8978 -0.0263 -0.4006 0.0926  19  GLU A CG  
139   C CD  . GLU A 19  ? 1.4532 0.9588 0.9929 -0.0383 -0.3959 0.0728  19  GLU A CD  
140   O OE1 . GLU A 19  ? 1.4576 0.9240 0.9375 -0.0315 -0.3713 0.0666  19  GLU A OE1 
141   O OE2 . GLU A 19  ? 1.5586 1.0724 1.1286 -0.0545 -0.4157 0.0634  19  GLU A OE2 
142   N N   . GLY A 20  ? 1.4695 0.9601 0.9194 0.0238  -0.3772 0.1358  20  GLY A N   
143   C CA  . GLY A 20  ? 1.3992 0.8676 0.8005 0.0342  -0.3752 0.1446  20  GLY A CA  
144   C C   . GLY A 20  ? 1.2997 0.7996 0.7494 0.0468  -0.3731 0.1603  20  GLY A C   
145   O O   . GLY A 20  ? 1.4322 0.9303 0.8666 0.0537  -0.3896 0.1668  20  GLY A O   
146   N N   . ILE A 21  ? 1.3457 0.8726 0.8517 0.0505  -0.3532 0.1659  21  ILE A N   
147   C CA  . ILE A 21  ? 1.3875 0.9419 0.9399 0.0639  -0.3483 0.1789  21  ILE A CA  
148   C C   . ILE A 21  ? 1.2791 0.8740 0.8872 0.0666  -0.3827 0.1811  21  ILE A C   
149   O O   . ILE A 21  ? 1.1974 0.8035 0.8178 0.0789  -0.3930 0.1906  21  ILE A O   
150   C CB  . ILE A 21  ? 1.2693 0.8377 0.8608 0.0663  -0.3157 0.1815  21  ILE A CB  
151   C CG1 . ILE A 21  ? 1.0902 0.6739 0.7135 0.0806  -0.3057 0.1929  21  ILE A CG1 
152   C CG2 . ILE A 21  ? 1.5021 1.1008 1.1472 0.0589  -0.3214 0.1761  21  ILE A CG2 
153   C CD1 . ILE A 21  ? 1.2780 0.8526 0.9030 0.0814  -0.2686 0.1946  21  ILE A CD1 
154   N N   . VAL A 22  ? 1.2131 0.8298 0.8557 0.0553  -0.3992 0.1732  22  VAL A N   
155   C CA  . VAL A 22  ? 1.0231 0.6855 0.7285 0.0552  -0.4301 0.1749  22  VAL A CA  
156   C C   . VAL A 22  ? 1.2040 0.8557 0.8752 0.0557  -0.4616 0.1741  22  VAL A C   
157   O O   . VAL A 22  ? 1.2851 0.9689 0.9969 0.0651  -0.4803 0.1815  22  VAL A O   
158   C CB  . VAL A 22  ? 1.0872 0.7747 0.8376 0.0389  -0.4408 0.1671  22  VAL A CB  
159   C CG1 . VAL A 22  ? 1.1632 0.8897 0.9616 0.0321  -0.4783 0.1653  22  VAL A CG1 
160   C CG2 . VAL A 22  ? 1.0861 0.8060 0.8969 0.0414  -0.4079 0.1693  22  VAL A CG2 
161   N N   . LYS A 23  ? 1.2124 0.8191 0.8083 0.0471  -0.4666 0.1653  23  LYS A N   
162   C CA  . LYS A 23  ? 1.2753 0.8675 0.8306 0.0473  -0.4957 0.1639  23  LYS A CA  
163   C C   . LYS A 23  ? 1.4102 1.0015 0.9571 0.0660  -0.4914 0.1796  23  LYS A C   
164   O O   . LYS A 23  ? 1.4796 1.0895 1.0417 0.0721  -0.5195 0.1850  23  LYS A O   
165   C CB  . LYS A 23  ? 1.2727 0.8108 0.7402 0.0372  -0.4933 0.1514  23  LYS A CB  
166   C CG  . LYS A 23  ? 1.3497 0.8725 0.7741 0.0344  -0.5267 0.1469  23  LYS A CG  
167   C CD  . LYS A 23  ? 1.5235 0.9889 0.8540 0.0282  -0.5172 0.1352  23  LYS A CD  
168   C CE  . LYS A 23  ? 1.5035 0.9510 0.7855 0.0266  -0.5484 0.1313  23  LYS A CE  
169   N NZ  . LYS A 23  ? 1.6995 1.0926 0.8933 0.0188  -0.5401 0.1156  23  LYS A NZ  
170   N N   . GLN A 24  ? 1.4326 1.0033 0.9588 0.0748  -0.4565 0.1873  24  GLN A N   
171   C CA  . GLN A 24  ? 1.3047 0.8702 0.8231 0.0913  -0.4501 0.2028  24  GLN A CA  
172   C C   . GLN A 24  ? 1.3265 0.9401 0.9224 0.1045  -0.4637 0.2119  24  GLN A C   
173   O O   . GLN A 24  ? 1.3690 0.9862 0.9637 0.1172  -0.4796 0.2227  24  GLN A O   
174   C CB  . GLN A 24  ? 1.2622 0.8026 0.7585 0.0951  -0.4086 0.2082  24  GLN A CB  
175   C CG  . GLN A 24  ? 1.6639 1.1573 1.0822 0.0856  -0.3905 0.2021  24  GLN A CG  
176   C CD  . GLN A 24  ? 1.8672 1.3411 1.2705 0.0891  -0.3511 0.2098  24  GLN A CD  
177   O OE1 . GLN A 24  ? 1.7331 1.2111 1.1541 0.1003  -0.3441 0.2231  24  GLN A OE1 
178   N NE2 . GLN A 24  ? 1.8605 1.3127 1.2323 0.0794  -0.3246 0.2014  24  GLN A NE2 
179   N N   . ALA A 25  ? 1.2447 0.8949 0.9071 0.1025  -0.4566 0.2080  25  ALA A N   
180   C CA  . ALA A 25  ? 1.1834 0.8822 0.9227 0.1157  -0.4654 0.2152  25  ALA A CA  
181   C C   . ALA A 25  ? 1.3004 1.0321 1.0698 0.1137  -0.5057 0.2139  25  ALA A C   
182   O O   . ALA A 25  ? 1.4533 1.2140 1.2630 0.1296  -0.5182 0.2234  25  ALA A O   
183   C CB  . ALA A 25  ? 1.0397 0.7685 0.8383 0.1124  -0.4457 0.2108  25  ALA A CB  
184   N N   . VAL A 26  ? 1.1558 0.8831 0.9074 0.0946  -0.5263 0.2019  26  VAL A N   
185   C CA  . VAL A 26  ? 1.1839 0.9429 0.9656 0.0897  -0.5657 0.1995  26  VAL A CA  
186   C C   . VAL A 26  ? 1.3966 1.1303 1.1234 0.0989  -0.5863 0.2064  26  VAL A C   
187   O O   . VAL A 26  ? 1.5535 1.3196 1.3161 0.1084  -0.6122 0.2134  26  VAL A O   
188   C CB  . VAL A 26  ? 1.3201 1.0828 1.1051 0.0646  -0.5833 0.1837  26  VAL A CB  
189   C CG1 . VAL A 26  ? 1.2607 1.0428 1.0928 0.0550  -0.5612 0.1790  26  VAL A CG1 
190   C CG2 . VAL A 26  ? 1.3605 1.0649 1.0524 0.0530  -0.5885 0.1735  26  VAL A CG2 
191   N N   . ASP A 27  ? 1.3809 1.0584 1.0219 0.0967  -0.5739 0.2054  27  ASP A N   
192   C CA  . ASP A 27  ? 1.4986 1.1469 1.0787 0.1042  -0.5906 0.2128  27  ASP A CA  
193   C C   . ASP A 27  ? 1.4795 1.1294 1.0686 0.1275  -0.5804 0.2322  27  ASP A C   
194   O O   . ASP A 27  ? 1.6575 1.3015 1.2230 0.1372  -0.6027 0.2420  27  ASP A O   
195   C CB  . ASP A 27  ? 1.5551 1.1432 1.0409 0.0940  -0.5756 0.2054  27  ASP A CB  
196   C CG  . ASP A 27  ? 1.7779 1.3526 1.2373 0.0729  -0.5895 0.1857  27  ASP A CG  
197   O OD1 . ASP A 27  ? 1.8774 1.4860 1.3823 0.0641  -0.6200 0.1785  27  ASP A OD1 
198   O OD2 . ASP A 27  ? 1.7277 1.2578 1.1221 0.0649  -0.5691 0.1771  27  ASP A OD2 
199   N N   . GLU A 28  ? 1.4341 1.0895 1.0549 0.1363  -0.5478 0.2377  28  GLU A N   
200   C CA  . GLU A 28  ? 1.3425 0.9931 0.9700 0.1574  -0.5350 0.2549  28  GLU A CA  
201   C C   . GLU A 28  ? 1.3033 1.0054 1.0173 0.1743  -0.5407 0.2614  28  GLU A C   
202   O O   . GLU A 28  ? 1.4841 1.1884 1.2054 0.1936  -0.5480 0.2759  28  GLU A O   
203   C CB  . GLU A 28  ? 1.3184 0.9336 0.9157 0.1560  -0.4926 0.2563  28  GLU A CB  
204   C CG  . GLU A 28  ? 1.5512 1.1375 1.1205 0.1712  -0.4786 0.2736  28  GLU A CG  
205   C CD  . GLU A 28  ? 1.9113 1.4678 1.4599 0.1669  -0.4370 0.2738  28  GLU A CD  
206   O OE1 . GLU A 28  ? 1.9462 1.4735 1.4430 0.1515  -0.4225 0.2658  28  GLU A OE1 
207   O OE2 . GLU A 28  ? 1.9494 1.5120 1.5343 0.1789  -0.4187 0.2811  28  GLU A OE2 
208   N N   . LYS A 29  ? 1.2389 0.9813 1.0174 0.1682  -0.5359 0.2517  29  LYS A N   
209   C CA  . LYS A 29  ? 1.2816 1.0754 1.1439 0.1848  -0.5371 0.2568  29  LYS A CA  
210   C C   . LYS A 29  ? 1.2649 1.1155 1.1921 0.1776  -0.5660 0.2499  29  LYS A C   
211   O O   . LYS A 29  ? 1.3347 1.2329 1.3335 0.1920  -0.5688 0.2542  29  LYS A O   
212   C CB  . LYS A 29  ? 1.1367 0.9342 1.0300 0.1878  -0.4995 0.2539  29  LYS A CB  
213   C CG  . LYS A 29  ? 1.2587 1.0061 1.1012 0.1945  -0.4689 0.2607  29  LYS A CG  
214   C CD  . LYS A 29  ? 1.2693 1.0163 1.1298 0.2202  -0.4656 0.2751  29  LYS A CD  
215   C CE  . LYS A 29  ? 1.4111 1.1156 1.2400 0.2245  -0.4312 0.2801  29  LYS A CE  
216   N NZ  . LYS A 29  ? 1.5025 1.1544 1.2509 0.2143  -0.4271 0.2852  29  LYS A NZ  
217   N N   . GLY A 30  ? 1.2016 1.0474 1.1054 0.1553  -0.5858 0.2389  30  GLY A N   
218   C CA  . GLY A 30  ? 1.1910 1.0885 1.1558 0.1440  -0.6136 0.2318  30  GLY A CA  
219   C C   . GLY A 30  ? 1.3141 1.2439 1.3374 0.1309  -0.5962 0.2228  30  GLY A C   
220   O O   . GLY A 30  ? 1.4079 1.3303 1.4387 0.1369  -0.5630 0.2240  30  GLY A O   
221   N N   . ARG A 31  ? 1.3532 1.3193 1.4195 0.1121  -0.6185 0.2142  31  ARG A N   
222   C CA  . ARG A 31  ? 1.3066 1.3053 1.4308 0.0965  -0.6039 0.2070  31  ARG A CA  
223   C C   . ARG A 31  ? 1.1790 1.2408 1.3970 0.1108  -0.5908 0.2136  31  ARG A C   
224   O O   . ARG A 31  ? 1.1847 1.2784 1.4556 0.0983  -0.5772 0.2095  31  ARG A O   
225   C CB  . ARG A 31  ? 1.4891 1.4985 1.6220 0.0679  -0.6312 0.1953  31  ARG A CB  
226   C CG  . ARG A 31  ? 1.3333 1.2786 1.3729 0.0523  -0.6408 0.1852  31  ARG A CG  
227   C CD  . ARG A 31  ? 1.0953 1.0343 1.1385 0.0240  -0.6410 0.1717  31  ARG A CD  
228   N NE  . ARG A 31  ? 1.2236 1.0982 1.1740 0.0120  -0.6477 0.1605  31  ARG A NE  
229   C CZ  . ARG A 31  ? 1.4872 1.3435 1.3990 0.0011  -0.6795 0.1520  31  ARG A CZ  
230   N NH1 . ARG A 31  ? 1.6405 1.5397 1.6007 -0.0005 -0.7101 0.1540  31  ARG A NH1 
231   N NH2 . ARG A 31  ? 1.5167 1.3119 1.3408 -0.0077 -0.6801 0.1408  31  ARG A NH2 
232   N N   . ASP A 32  ? 1.1714 1.2507 1.4097 0.1371  -0.5933 0.2240  32  ASP A N   
233   C CA  . ASP A 32  ? 1.1031 1.2405 1.4273 0.1539  -0.5787 0.2291  32  ASP A CA  
234   C C   . ASP A 32  ? 1.1353 1.2511 1.4476 0.1789  -0.5448 0.2353  32  ASP A C   
235   O O   . ASP A 32  ? 0.9363 1.0932 1.3128 0.1937  -0.5265 0.2373  32  ASP A O   
236   C CB  . ASP A 32  ? 1.2423 1.4264 1.6142 0.1665  -0.6080 0.2352  32  ASP A CB  
237   C CG  . ASP A 32  ? 1.4485 1.6764 1.8668 0.1420  -0.6354 0.2284  32  ASP A CG  
238   O OD1 . ASP A 32  ? 1.3123 1.5558 1.7595 0.1192  -0.6238 0.2207  32  ASP A OD1 
239   O OD2 . ASP A 32  ? 1.4328 1.6793 1.8592 0.1449  -0.6688 0.2313  32  ASP A OD2 
240   N N   . TYR A 33  ? 1.2244 1.2754 1.4551 0.1827  -0.5351 0.2375  33  TYR A N   
241   C CA  . TYR A 33  ? 1.0897 1.1120 1.3015 0.2031  -0.5039 0.2428  33  TYR A CA  
242   C C   . TYR A 33  ? 0.9079 0.9468 1.1574 0.1988  -0.4716 0.2365  33  TYR A C   
243   O O   . TYR A 33  ? 1.0428 1.0828 1.2909 0.1756  -0.4684 0.2289  33  TYR A O   
244   C CB  . TYR A 33  ? 1.1759 1.1269 1.2931 0.1997  -0.4982 0.2451  33  TYR A CB  
245   C CG  . TYR A 33  ? 1.1672 1.0844 1.2607 0.2202  -0.4712 0.2526  33  TYR A CG  
246   C CD1 . TYR A 33  ? 1.0617 0.9682 1.1452 0.2425  -0.4803 0.2649  33  TYR A CD1 
247   C CD2 . TYR A 33  ? 1.1460 1.0382 1.2238 0.2160  -0.4376 0.2479  33  TYR A CD2 
248   C CE1 . TYR A 33  ? 1.0713 0.9425 1.1326 0.2594  -0.4559 0.2720  33  TYR A CE1 
249   C CE2 . TYR A 33  ? 1.2142 1.0729 1.2701 0.2321  -0.4136 0.2538  33  TYR A CE2 
250   C CZ  . TYR A 33  ? 1.2385 1.0855 1.2863 0.2532  -0.4225 0.2658  33  TYR A CZ  
251   O OH  . TYR A 33  ? 1.3187 1.1294 1.3460 0.2674  -0.3991 0.2719  33  TYR A OH  
252   N N   . LYS A 34  ? 1.0455 1.0963 1.3278 0.2216  -0.4484 0.2396  34  LYS A N   
253   C CA  . LYS A 34  ? 0.8341 0.9020 1.1528 0.2205  -0.4170 0.2339  34  LYS A CA  
254   C C   . LYS A 34  ? 0.8596 0.8735 1.1176 0.2092  -0.3938 0.2300  34  LYS A C   
255   O O   . LYS A 34  ? 0.9828 0.9458 1.1831 0.2175  -0.3855 0.2335  34  LYS A O   
256   C CB  . LYS A 34  ? 0.9624 1.0515 1.3251 0.2505  -0.3989 0.2367  34  LYS A CB  
257   C CG  . LYS A 34  ? 1.0378 1.1499 1.4427 0.2520  -0.3661 0.2301  34  LYS A CG  
258   C CD  . LYS A 34  ? 0.7869 0.8963 1.2092 0.2832  -0.3451 0.2306  34  LYS A CD  
259   C CE  . LYS A 34  ? 1.1461 1.2868 1.6171 0.2867  -0.3136 0.2231  34  LYS A CE  
260   N NZ  . LYS A 34  ? 1.1279 1.2678 1.6185 0.3188  -0.2946 0.2209  34  LYS A NZ  
261   N N   . VAL A 35  ? 0.7754 0.8026 1.0498 0.1899  -0.3821 0.2238  35  VAL A N   
262   C CA  . VAL A 35  ? 0.9901 0.9734 1.2153 0.1788  -0.3593 0.2198  35  VAL A CA  
263   C C   . VAL A 35  ? 0.9550 0.9628 1.2264 0.1860  -0.3295 0.2173  35  VAL A C   
264   O O   . VAL A 35  ? 0.9366 0.9983 1.2737 0.1820  -0.3277 0.2167  35  VAL A O   
265   C CB  . VAL A 35  ? 0.9537 0.9213 1.1463 0.1509  -0.3702 0.2152  35  VAL A CB  
266   C CG1 . VAL A 35  ? 1.0478 1.0699 1.3049 0.1354  -0.3815 0.2133  35  VAL A CG1 
267   C CG2 . VAL A 35  ? 0.8074 0.7335 0.9539 0.1421  -0.3440 0.2115  35  VAL A CG2 
268   N N   . ALA A 36  ? 0.9187 0.8880 1.1569 0.1963  -0.3052 0.2161  36  ALA A N   
269   C CA  . ALA A 36  ? 0.9533 0.9386 1.2245 0.2036  -0.2746 0.2114  36  ALA A CA  
270   C C   . ALA A 36  ? 0.9349 0.8646 1.1485 0.2045  -0.2507 0.2071  36  ALA A C   
271   O O   . ALA A 36  ? 0.8760 0.7584 1.0375 0.2081  -0.2587 0.2116  36  ALA A O   
272   C CB  . ALA A 36  ? 0.8541 0.8779 1.1852 0.2298  -0.2722 0.2132  36  ALA A CB  
273   N N   . PHE A 37  ? 0.8452 0.7827 1.0659 0.1988  -0.2187 0.1970  37  PHE A N   
274   C CA  . PHE A 37  ? 0.8344 0.7253 1.0082 0.1977  -0.1962 0.1915  37  PHE A CA  
275   C C   . PHE A 37  ? 0.8540 0.7431 1.0497 0.2223  -0.1813 0.1883  37  PHE A C   
276   O O   . PHE A 37  ? 0.9432 0.8772 1.1939 0.2358  -0.1780 0.1868  37  PHE A O   
277   C CB  . PHE A 37  ? 0.7869 0.6833 0.9487 0.1756  -0.1731 0.1819  37  PHE A CB  
278   C CG  . PHE A 37  ? 0.7708 0.6427 0.8885 0.1537  -0.1806 0.1827  37  PHE A CG  
279   C CD1 . PHE A 37  ? 0.9337 0.7545 0.9959 0.1516  -0.1828 0.1857  37  PHE A CD1 
280   C CD2 . PHE A 37  ? 0.8908 0.7893 1.0222 0.1354  -0.1826 0.1802  37  PHE A CD2 
281   C CE1 . PHE A 37  ? 0.9179 0.7175 0.9398 0.1334  -0.1861 0.1852  37  PHE A CE1 
282   C CE2 . PHE A 37  ? 0.7788 0.6518 0.8688 0.1176  -0.1877 0.1791  37  PHE A CE2 
283   C CZ  . PHE A 37  ? 0.6813 0.5065 0.7170 0.1175  -0.1886 0.1811  37  PHE A CZ  
284   N N   . PRO A 38  ? 0.7720 0.6099 0.9276 0.2289  -0.1716 0.1869  38  PRO A N   
285   C CA  . PRO A 38  ? 0.8154 0.6459 0.9899 0.2532  -0.1587 0.1822  38  PRO A CA  
286   C C   . PRO A 38  ? 0.9222 0.7845 1.1270 0.2552  -0.1304 0.1679  38  PRO A C   
287   O O   . PRO A 38  ? 0.8284 0.6818 1.0092 0.2381  -0.1114 0.1586  38  PRO A O   
288   C CB  . PRO A 38  ? 0.9086 0.6720 1.0275 0.2524  -0.1539 0.1833  38  PRO A CB  
289   C CG  . PRO A 38  ? 1.0015 0.7415 1.0767 0.2325  -0.1673 0.1918  38  PRO A CG  
290   C CD  . PRO A 38  ? 0.8717 0.6558 0.9648 0.2147  -0.1712 0.1895  38  PRO A CD  
291   N N   . ASP A 39  ? 0.9536 0.8529 1.2105 0.2777  -0.1275 0.1664  39  ASP A N   
292   C CA  . ASP A 39  ? 1.0239 0.9540 1.3094 0.2843  -0.0993 0.1531  39  ASP A CA  
293   C C   . ASP A 39  ? 0.9312 0.8898 1.2142 0.2583  -0.0838 0.1476  39  ASP A C   
294   O O   . ASP A 39  ? 0.8405 0.7752 1.0880 0.2466  -0.0659 0.1379  39  ASP A O   
295   C CB  . ASP A 39  ? 1.0790 0.9610 1.3354 0.2982  -0.0817 0.1416  39  ASP A CB  
296   C CG  . ASP A 39  ? 1.2083 1.1140 1.4890 0.3120  -0.0533 0.1263  39  ASP A CG  
297   O OD1 . ASP A 39  ? 1.2388 1.2035 1.5658 0.3142  -0.0454 0.1264  39  ASP A OD1 
298   O OD2 . ASP A 39  ? 1.2476 1.1120 1.5001 0.3200  -0.0387 0.1139  39  ASP A OD2 
299   N N   . THR A 40  ? 0.9178 0.9275 1.2403 0.2493  -0.0920 0.1545  40  THR A N   
300   C CA  . THR A 40  ? 0.7146 0.7530 1.0403 0.2256  -0.0791 0.1521  40  THR A CA  
301   C C   . THR A 40  ? 0.7443 0.8483 1.1347 0.2271  -0.0793 0.1575  40  THR A C   
302   O O   . THR A 40  ? 0.8065 0.9319 1.2315 0.2344  -0.1025 0.1667  40  THR A O   
303   C CB  . THR A 40  ? 0.6216 0.6338 0.9063 0.1998  -0.0933 0.1567  40  THR A CB  
304   O OG1 . THR A 40  ? 0.6767 0.7124 0.9641 0.1793  -0.0791 0.1543  40  THR A OG1 
305   C CG2 . THR A 40  ? 0.7587 0.7760 1.0535 0.1964  -0.1250 0.1682  40  THR A CG2 
306   N N   . ALA A 41  ? 0.6770 0.8138 1.0844 0.2197  -0.0540 0.1527  41  ALA A N   
307   C CA  . ALA A 41  ? 0.6608 0.8622 1.1316 0.2184  -0.0494 0.1587  41  ALA A CA  
308   C C   . ALA A 41  ? 0.6480 0.8673 1.1234 0.1878  -0.0589 0.1667  41  ALA A C   
309   O O   . ALA A 41  ? 0.8696 1.1409 1.3948 0.1805  -0.0519 0.1722  41  ALA A O   
310   C CB  . ALA A 41  ? 0.7695 0.9972 1.2562 0.2287  -0.0137 0.1503  41  ALA A CB  
311   N N   . TYR A 42  ? 0.6165 0.7926 1.0419 0.1705  -0.0737 0.1672  42  TYR A N   
312   C CA  . TYR A 42  ? 0.7421 0.9267 1.1656 0.1421  -0.0817 0.1729  42  TYR A CA  
313   C C   . TYR A 42  ? 0.7730 0.9322 1.1779 0.1335  -0.1156 0.1776  42  TYR A C   
314   O O   . TYR A 42  ? 0.7860 0.9265 1.1634 0.1118  -0.1223 0.1783  42  TYR A O   
315   C CB  . TYR A 42  ? 0.5614 0.7202 0.9395 0.1277  -0.0614 0.1677  42  TYR A CB  
316   C CG  . TYR A 42  ? 0.7078 0.8879 1.0945 0.1347  -0.0292 0.1628  42  TYR A CG  
317   C CD1 . TYR A 42  ? 0.5957 0.8203 1.0185 0.1242  -0.0138 0.1687  42  TYR A CD1 
318   C CD2 . TYR A 42  ? 0.8071 0.9611 1.1637 0.1512  -0.0138 0.1522  42  TYR A CD2 
319   C CE1 . TYR A 42  ? 0.5680 0.8112 0.9928 0.1309  0.0171  0.1646  42  TYR A CE1 
320   C CE2 . TYR A 42  ? 0.7080 0.8787 1.0661 0.1581  0.0152  0.1459  42  TYR A CE2 
321   C CZ  . TYR A 42  ? 0.6831 0.8989 1.0735 0.1486  0.0313  0.1523  42  TYR A CZ  
322   O OH  . TYR A 42  ? 0.8498 1.0812 1.2360 0.1556  0.0613  0.1465  42  TYR A OH  
323   N N   . SER A 43  ? 0.7639 0.9210 1.1812 0.1511  -0.1364 0.1806  43  SER A N   
324   C CA  . SER A 43  ? 0.7671 0.9002 1.1628 0.1441  -0.1707 0.1856  43  SER A CA  
325   C C   . SER A 43  ? 0.8192 0.8988 1.1468 0.1283  -0.1701 0.1817  43  SER A C   
326   O O   . SER A 43  ? 0.8809 0.9222 1.1678 0.1371  -0.1577 0.1773  43  SER A O   
327   C CB  . SER A 43  ? 0.7939 0.9694 1.2364 0.1293  -0.1913 0.1918  43  SER A CB  
328   O OG  . SER A 43  ? 1.1241 1.2741 1.5400 0.1227  -0.2255 0.1948  43  SER A OG  
329   N N   . LEU A 44  ? 0.7428 0.8198 1.0608 0.1059  -0.1828 0.1827  44  LEU A N   
330   C CA  . LEU A 44  ? 0.7111 0.7412 0.9687 0.0916  -0.1789 0.1783  44  LEU A CA  
331   C C   . LEU A 44  ? 0.8317 0.8749 1.0957 0.0786  -0.1528 0.1751  44  LEU A C   
332   O O   . LEU A 44  ? 0.8911 0.9567 1.1793 0.0617  -0.1567 0.1776  44  LEU A O   
333   C CB  . LEU A 44  ? 0.7940 0.8087 1.0330 0.0768  -0.2073 0.1797  44  LEU A CB  
334   C CG  . LEU A 44  ? 0.8004 0.7743 0.9936 0.0859  -0.2279 0.1814  44  LEU A CG  
335   C CD1 . LEU A 44  ? 0.6204 0.6091 0.8401 0.1088  -0.2393 0.1877  44  LEU A CD1 
336   C CD2 . LEU A 44  ? 0.8237 0.7834 0.9956 0.0706  -0.2560 0.1810  44  LEU A CD2 
337   N N   . PRO A 45  ? 0.6905 0.7192 0.9328 0.0849  -0.1279 0.1702  45  PRO A N   
338   C CA  . PRO A 45  ? 0.7191 0.7625 0.9668 0.0749  -0.1043 0.1685  45  PRO A CA  
339   C C   . PRO A 45  ? 0.7355 0.7706 0.9710 0.0527  -0.1088 0.1703  45  PRO A C   
340   O O   . PRO A 45  ? 0.8083 0.8723 1.0739 0.0420  -0.1014 0.1745  45  PRO A O   
341   C CB  . PRO A 45  ? 0.8201 0.8324 1.0281 0.0828  -0.0869 0.1616  45  PRO A CB  
342   C CG  . PRO A 45  ? 0.7385 0.7374 0.9439 0.1024  -0.0944 0.1604  45  PRO A CG  
343   C CD  . PRO A 45  ? 0.6237 0.6195 0.8339 0.1007  -0.1228 0.1665  45  PRO A CD  
344   N N   . VAL A 46  ? 0.6460 0.6408 0.8379 0.0468  -0.1192 0.1673  46  VAL A N   
345   C CA  . VAL A 46  ? 0.6978 0.6782 0.8742 0.0281  -0.1221 0.1672  46  VAL A CA  
346   C C   . VAL A 46  ? 0.7707 0.7773 0.9855 0.0155  -0.1385 0.1719  46  VAL A C   
347   O O   . VAL A 46  ? 0.7761 0.7997 1.0118 0.0026  -0.1291 0.1756  46  VAL A O   
348   C CB  . VAL A 46  ? 0.7977 0.7322 0.9230 0.0263  -0.1312 0.1624  46  VAL A CB  
349   C CG1 . VAL A 46  ? 0.6333 0.5503 0.7420 0.0105  -0.1315 0.1605  46  VAL A CG1 
350   C CG2 . VAL A 46  ? 0.9508 0.8626 1.0446 0.0373  -0.1163 0.1588  46  VAL A CG2 
351   N N   . ILE A 47  ? 0.6588 0.6675 0.8820 0.0183  -0.1633 0.1724  47  ILE A N   
352   C CA  . ILE A 47  ? 0.6360 0.6712 0.8990 0.0043  -0.1835 0.1761  47  ILE A CA  
353   C C   . ILE A 47  ? 0.7076 0.7955 1.0307 0.0033  -0.1683 0.1829  47  ILE A C   
354   O O   . ILE A 47  ? 0.7398 0.8466 1.0923 -0.0153 -0.1698 0.1870  47  ILE A O   
355   C CB  . ILE A 47  ? 0.6119 0.6450 0.8752 0.0110  -0.2144 0.1760  47  ILE A CB  
356   C CG1 . ILE A 47  ? 0.5712 0.5502 0.7681 0.0136  -0.2251 0.1702  47  ILE A CG1 
357   C CG2 . ILE A 47  ? 0.6773 0.7386 0.9831 -0.0054 -0.2385 0.1787  47  ILE A CG2 
358   C CD1 . ILE A 47  ? 0.7965 0.7645 0.9821 0.0088  -0.2602 0.1690  47  ILE A CD1 
359   N N   . PHE A 48  ? 0.7097 0.8183 1.0489 0.0225  -0.1528 0.1839  48  PHE A N   
360   C CA  . PHE A 48  ? 0.5930 0.7529 0.9873 0.0245  -0.1351 0.1896  48  PHE A CA  
361   C C   . PHE A 48  ? 0.6165 0.7780 1.0050 0.0109  -0.1101 0.1923  48  PHE A C   
362   O O   . PHE A 48  ? 0.7120 0.9120 1.1444 0.0008  -0.1003 0.1997  48  PHE A O   
363   C CB  . PHE A 48  ? 0.4731 0.6467 0.8771 0.0505  -0.1217 0.1875  48  PHE A CB  
364   C CG  . PHE A 48  ? 0.5683 0.7956 1.0274 0.0551  -0.1003 0.1921  48  PHE A CG  
365   C CD1 . PHE A 48  ? 0.5538 0.8303 1.0767 0.0531  -0.1117 0.1987  48  PHE A CD1 
366   C CD2 . PHE A 48  ? 0.6354 0.8657 1.0824 0.0604  -0.0685 0.1899  48  PHE A CD2 
367   C CE1 . PHE A 48  ? 0.6078 0.9367 1.1834 0.0572  -0.0884 0.2035  48  PHE A CE1 
368   C CE2 . PHE A 48  ? 0.5018 0.7807 0.9947 0.0649  -0.0459 0.1940  48  PHE A CE2 
369   C CZ  . PHE A 48  ? 0.4975 0.8263 1.0556 0.0636  -0.0543 0.2011  48  PHE A CZ  
370   N N   . ALA A 49  ? 0.5810 0.7021 0.9170 0.0105  -0.0998 0.1876  49  ALA A N   
371   C CA  . ALA A 49  ? 0.5706 0.6896 0.8965 -0.0006 -0.0789 0.1913  49  ALA A CA  
372   C C   . ALA A 49  ? 0.6871 0.7981 1.0192 -0.0241 -0.0903 0.1964  49  ALA A C   
373   O O   . ALA A 49  ? 0.7114 0.8418 1.0657 -0.0367 -0.0771 0.2050  49  ALA A O   
374   C CB  . ALA A 49  ? 0.6101 0.6909 0.8825 0.0067  -0.0681 0.1848  49  ALA A CB  
375   N N   . ALA A 50  ? 0.7423 0.8220 1.0525 -0.0301 -0.1143 0.1911  50  ALA A N   
376   C CA  . ALA A 50  ? 0.7447 0.8080 1.0550 -0.0518 -0.1271 0.1929  50  ALA A CA  
377   C C   . ALA A 50  ? 0.7804 0.8797 1.1464 -0.0672 -0.1419 0.1991  50  ALA A C   
378   O O   . ALA A 50  ? 0.7761 0.8803 1.1615 -0.0867 -0.1383 0.2059  50  ALA A O   
379   C CB  . ALA A 50  ? 0.6513 0.6664 0.9139 -0.0516 -0.1463 0.1830  50  ALA A CB  
380   N N   . THR A 51  ? 0.6469 0.7711 1.0402 -0.0591 -0.1593 0.1975  51  THR A N   
381   C CA  . THR A 51  ? 0.6469 0.8100 1.0982 -0.0732 -0.1775 0.2026  51  THR A CA  
382   C C   . THR A 51  ? 0.7060 0.9315 1.2201 -0.0655 -0.1621 0.2113  51  THR A C   
383   O O   . THR A 51  ? 0.6600 0.9255 1.2314 -0.0811 -0.1691 0.2183  51  THR A O   
384   C CB  . THR A 51  ? 0.8088 0.9589 1.2503 -0.0700 -0.2132 0.1954  51  THR A CB  
385   O OG1 . THR A 51  ? 0.7673 0.9269 1.2048 -0.0439 -0.2125 0.1939  51  THR A OG1 
386   C CG2 . THR A 51  ? 0.8443 0.9329 1.2220 -0.0771 -0.2280 0.1855  51  THR A CG2 
387   N N   . GLY A 52  ? 0.5799 0.8137 1.0849 -0.0419 -0.1416 0.2099  52  GLY A N   
388   C CA  . GLY A 52  ? 0.6352 0.9255 1.1956 -0.0301 -0.1243 0.2159  52  GLY A CA  
389   C C   . GLY A 52  ? 0.7856 1.1077 1.3888 -0.0184 -0.1486 0.2154  52  GLY A C   
390   O O   . GLY A 52  ? 0.6982 1.0716 1.3556 -0.0067 -0.1368 0.2200  52  GLY A O   
391   N N   . LYS A 53  ? 0.7610 1.0526 1.3389 -0.0202 -0.1827 0.2099  53  LYS A N   
392   C CA  . LYS A 53  ? 0.6548 0.9697 1.2650 -0.0093 -0.2123 0.2102  53  LYS A CA  
393   C C   . LYS A 53  ? 0.6757 0.9590 1.2421 0.0188  -0.2149 0.2046  53  LYS A C   
394   O O   . LYS A 53  ? 0.6909 0.9243 1.1939 0.0222  -0.2040 0.1988  53  LYS A O   
395   C CB  . LYS A 53  ? 0.7573 1.0544 1.3603 -0.0305 -0.2509 0.2078  53  LYS A CB  
396   C CG  . LYS A 53  ? 0.9665 1.2785 1.6008 -0.0627 -0.2511 0.2118  53  LYS A CG  
397   C CD  . LYS A 53  ? 1.2689 1.5472 1.8788 -0.0834 -0.2889 0.2053  53  LYS A CD  
398   C CE  . LYS A 53  ? 1.4298 1.6960 2.0444 -0.1149 -0.2848 0.2065  53  LYS A CE  
399   N NZ  . LYS A 53  ? 1.4063 1.6135 1.9644 -0.1291 -0.3118 0.1954  53  LYS A NZ  
400   N N   . LYS A 54  ? 0.7929 1.1048 1.3950 0.0384  -0.2303 0.2073  54  LYS A N   
401   C CA  . LYS A 54  ? 0.7127 0.9935 1.2771 0.0655  -0.2346 0.2041  54  LYS A CA  
402   C C   . LYS A 54  ? 0.6980 0.9557 1.2405 0.0662  -0.2766 0.2044  54  LYS A C   
403   O O   . LYS A 54  ? 0.7139 1.0057 1.3011 0.0572  -0.3044 0.2085  54  LYS A O   
404   C CB  . LYS A 54  ? 0.6336 0.9569 1.2484 0.0923  -0.2184 0.2070  54  LYS A CB  
405   C CG  . LYS A 54  ? 0.6030 0.9420 1.2262 0.0943  -0.1752 0.2050  54  LYS A CG  
406   C CD  . LYS A 54  ? 0.6764 1.0485 1.3388 0.1243  -0.1560 0.2048  54  LYS A CD  
407   C CE  . LYS A 54  ? 0.8633 1.2047 1.4814 0.1369  -0.1220 0.1967  54  LYS A CE  
408   N NZ  . LYS A 54  ? 0.8878 1.2617 1.5448 0.1650  -0.1002 0.1944  54  LYS A NZ  
409   N N   . ILE A 55  ? 0.7917 0.9918 1.2644 0.0757  -0.2813 0.2006  55  ILE A N   
410   C CA  . ILE A 55  ? 0.7792 0.9490 1.2164 0.0779  -0.3184 0.2014  55  ILE A CA  
411   C C   . ILE A 55  ? 0.8973 1.0733 1.3473 0.1086  -0.3271 0.2074  55  ILE A C   
412   O O   . ILE A 55  ? 1.0037 1.1524 1.4246 0.1260  -0.3051 0.2061  55  ILE A O   
413   C CB  . ILE A 55  ? 0.8113 0.9135 1.1627 0.0694  -0.3146 0.1949  55  ILE A CB  
414   C CG1 . ILE A 55  ? 0.6747 0.7685 1.0152 0.0418  -0.3045 0.1888  55  ILE A CG1 
415   C CG2 . ILE A 55  ? 0.9258 0.9922 1.2309 0.0733  -0.3494 0.1962  55  ILE A CG2 
416   C CD1 . ILE A 55  ? 0.9191 1.0351 1.2906 0.0193  -0.3327 0.1884  55  ILE A CD1 
417   N N   . THR A 56  ? 0.7704 0.9818 1.2658 0.1153  -0.3599 0.2141  56  THR A N   
418   C CA  . THR A 56  ? 0.6704 0.8887 1.1785 0.1452  -0.3665 0.2185  56  THR A CA  
419   C C   . THR A 56  ? 0.8995 1.0782 1.3511 0.1498  -0.3969 0.2188  56  THR A C   
420   O O   . THR A 56  ? 1.0433 1.1982 1.4696 0.1734  -0.3933 0.2214  56  THR A O   
421   C CB  . THR A 56  ? 0.8051 1.0965 1.4013 0.1525  -0.3645 0.2206  56  THR A CB  
422   O OG1 . THR A 56  ? 0.9756 1.2933 1.5950 0.1343  -0.3966 0.2206  56  THR A OG1 
423   C CG2 . THR A 56  ? 0.6709 1.0055 1.3230 0.1471  -0.3310 0.2212  56  THR A CG2 
424   N N   . ASN A 57  ? 0.8001 0.9704 1.2309 0.1279  -0.4259 0.2164  57  ASN A N   
425   C CA  . ASN A 57  ? 0.8144 0.9480 1.1883 0.1318  -0.4540 0.2169  57  ASN A CA  
426   C C   . ASN A 57  ? 0.8461 0.9214 1.1405 0.1121  -0.4629 0.2115  57  ASN A C   
427   O O   . ASN A 57  ? 0.9547 1.0253 1.2478 0.0923  -0.4546 0.2069  57  ASN A O   
428   C CB  . ASN A 57  ? 0.9062 1.0858 1.3273 0.1299  -0.4855 0.2182  57  ASN A CB  
429   C CG  . ASN A 57  ? 1.0150 1.2306 1.4795 0.1006  -0.4996 0.2133  57  ASN A CG  
430   O OD1 . ASN A 57  ? 1.0897 1.2745 1.5109 0.0784  -0.5192 0.2072  57  ASN A OD1 
431   N ND2 . ASN A 57  ? 1.0743 1.3544 1.6243 0.0995  -0.4888 0.2153  57  ASN A ND2 
432   N N   . VAL A 58  ? 1.0521 1.0829 1.2797 0.1183  -0.4785 0.2125  58  VAL A N   
433   C CA  . VAL A 58  ? 0.9691 0.9425 1.1151 0.1025  -0.4849 0.2066  58  VAL A CA  
434   C C   . VAL A 58  ? 1.1023 1.0868 1.2578 0.0748  -0.5079 0.1979  58  VAL A C   
435   O O   . VAL A 58  ? 1.1604 1.1073 1.2686 0.0587  -0.5034 0.1909  58  VAL A O   
436   C CB  . VAL A 58  ? 1.0752 1.0072 1.1547 0.1145  -0.4984 0.2108  58  VAL A CB  
437   C CG1 . VAL A 58  ? 0.9770 0.8570 0.9764 0.0969  -0.5087 0.2032  58  VAL A CG1 
438   C CG2 . VAL A 58  ? 1.1089 1.0151 1.1654 0.1367  -0.4713 0.2186  58  VAL A CG2 
439   N N   . GLY A 59  ? 1.0133 1.0480 1.2297 0.0692  -0.5315 0.1979  59  GLY A N   
440   C CA  . GLY A 59  ? 0.8918 0.9390 1.1245 0.0410  -0.5536 0.1892  59  GLY A CA  
441   C C   . GLY A 59  ? 0.9965 1.0574 1.2631 0.0244  -0.5323 0.1868  59  GLY A C   
442   O O   . GLY A 59  ? 1.0821 1.1163 1.3193 0.0018  -0.5393 0.1783  59  GLY A O   
443   N N   . GLU A 60  ? 0.8457 0.9465 1.1721 0.0366  -0.5052 0.1943  60  GLU A N   
444   C CA  . GLU A 60  ? 0.8518 0.9694 1.2127 0.0234  -0.4794 0.1943  60  GLU A CA  
445   C C   . GLU A 60  ? 0.9151 0.9701 1.1967 0.0219  -0.4498 0.1871  60  GLU A C   
446   O O   . GLU A 60  ? 0.9018 0.9435 1.1725 0.0018  -0.4338 0.1792  60  GLU A O   
447   C CB  . GLU A 60  ? 0.7798 0.9526 1.2151 0.0397  -0.4521 0.2023  60  GLU A CB  
448   C CG  . GLU A 60  ? 0.7007 0.9421 1.2214 0.0348  -0.4661 0.2054  60  GLU A CG  
449   C CD  . GLU A 60  ? 0.8084 1.1064 1.4025 0.0514  -0.4368 0.2122  60  GLU A CD  
450   O OE1 . GLU A 60  ? 0.8950 1.1776 1.4734 0.0699  -0.4086 0.2148  60  GLU A OE1 
451   O OE2 . GLU A 60  ? 0.7641 1.1209 1.4299 0.0459  -0.4410 0.2141  60  GLU A OE2 
452   N N   . LEU A 61  ? 1.0376 1.0541 1.2653 0.0427  -0.4432 0.1904  61  LEU A N   
453   C CA  . LEU A 61  ? 0.8902 0.8499 1.0449 0.0421  -0.4166 0.1846  61  LEU A CA  
454   C C   . LEU A 61  ? 1.0582 0.9758 1.1541 0.0224  -0.4335 0.1743  61  LEU A C   
455   O O   . LEU A 61  ? 1.2681 1.1552 1.3285 0.0123  -0.4097 0.1662  61  LEU A O   
456   C CB  . LEU A 61  ? 0.9465 0.8739 1.0578 0.0662  -0.4127 0.1920  61  LEU A CB  
457   C CG  . LEU A 61  ? 0.9815 0.8568 1.0266 0.0672  -0.3821 0.1880  61  LEU A CG  
458   C CD1 . LEU A 61  ? 0.9809 0.8734 1.0570 0.0696  -0.3426 0.1863  61  LEU A CD1 
459   C CD2 . LEU A 61  ? 0.8386 0.6739 0.8306 0.0856  -0.3883 0.1965  61  LEU A CD2 
460   N N   . GLU A 62  ? 1.0830 0.9984 1.1680 0.0178  -0.4751 0.1739  62  GLU A N   
461   C CA  . GLU A 62  ? 1.1250 0.9991 1.1521 -0.0007 -0.4942 0.1619  62  GLU A CA  
462   C C   . GLU A 62  ? 1.1956 1.0856 1.2592 -0.0259 -0.4867 0.1522  62  GLU A C   
463   O O   . GLU A 62  ? 1.0452 0.8937 1.0609 -0.0386 -0.4758 0.1408  62  GLU A O   
464   C CB  . GLU A 62  ? 1.0447 0.9196 1.0590 -0.0007 -0.5391 0.1622  62  GLU A CB  
465   C CG  . GLU A 62  ? 1.1602 0.9808 1.0947 -0.0147 -0.5577 0.1487  62  GLU A CG  
466   C CD  . GLU A 62  ? 1.3653 1.1905 1.2908 -0.0180 -0.5933 0.1446  62  GLU A CD  
467   O OE1 . GLU A 62  ? 1.2418 1.1198 1.2402 -0.0239 -0.6119 0.1469  62  GLU A OE1 
468   O OE2 . GLU A 62  ? 1.2261 1.0033 1.0720 -0.0147 -0.6014 0.1395  62  GLU A OE2 
469   N N   . GLY A 63  ? 1.0682 1.0176 1.2169 -0.0323 -0.4910 0.1577  63  GLY A N   
470   C CA  . GLY A 63  ? 0.9750 0.9434 1.1660 -0.0570 -0.4832 0.1521  63  GLY A CA  
471   C C   . GLY A 63  ? 0.9805 0.9316 1.1592 -0.0582 -0.4383 0.1500  63  GLY A C   
472   O O   . GLY A 63  ? 1.0027 0.9363 1.1751 -0.0780 -0.4313 0.1422  63  GLY A O   
473   N N   . ALA A 64  ? 0.9731 0.9272 1.1475 -0.0369 -0.4088 0.1570  64  ALA A N   
474   C CA  . ALA A 64  ? 0.9475 0.8870 1.1087 -0.0356 -0.3678 0.1557  64  ALA A CA  
475   C C   . ALA A 64  ? 1.0559 0.9346 1.1426 -0.0421 -0.3611 0.1446  64  ALA A C   
476   O O   . ALA A 64  ? 1.0043 0.8708 1.0840 -0.0463 -0.3329 0.1421  64  ALA A O   
477   C CB  . ALA A 64  ? 0.8413 0.7897 1.0045 -0.0117 -0.3440 0.1633  64  ALA A CB  
478   N N   . LEU A 65  ? 1.0769 0.9177 1.1072 -0.0416 -0.3864 0.1383  65  LEU A N   
479   C CA  . LEU A 65  ? 1.0385 0.8220 0.9971 -0.0464 -0.3788 0.1265  65  LEU A CA  
480   C C   . LEU A 65  ? 1.1501 0.9249 1.1203 -0.0685 -0.3784 0.1169  65  LEU A C   
481   O O   . LEU A 65  ? 1.2121 0.9498 1.1432 -0.0704 -0.3582 0.1090  65  LEU A O   
482   C CB  . LEU A 65  ? 0.9555 0.7017 0.8502 -0.0429 -0.4079 0.1213  65  LEU A CB  
483   C CG  . LEU A 65  ? 1.0466 0.7722 0.8955 -0.0215 -0.3992 0.1288  65  LEU A CG  
484   C CD1 . LEU A 65  ? 1.0945 0.7982 0.8973 -0.0180 -0.4357 0.1288  65  LEU A CD1 
485   C CD2 . LEU A 65  ? 0.9504 0.6344 0.7446 -0.0173 -0.3656 0.1234  65  LEU A CD2 
486   N N   . ASP A 66  ? 1.0958 0.9046 1.1222 -0.0851 -0.3999 0.1182  66  ASP A N   
487   C CA  . ASP A 66  ? 1.0638 0.8630 1.1058 -0.1082 -0.4007 0.1108  66  ASP A CA  
488   C C   . ASP A 66  ? 1.0740 0.8832 1.1421 -0.1083 -0.3619 0.1168  66  ASP A C   
489   O O   . ASP A 66  ? 0.9844 0.7657 1.0410 -0.1214 -0.3538 0.1101  66  ASP A O   
490   C CB  . ASP A 66  ? 1.1018 0.9400 1.2046 -0.1276 -0.4326 0.1128  66  ASP A CB  
491   C CG  . ASP A 66  ? 1.3174 1.1356 1.3870 -0.1338 -0.4764 0.1031  66  ASP A CG  
492   O OD1 . ASP A 66  ? 1.2853 1.0455 1.2819 -0.1355 -0.4825 0.0888  66  ASP A OD1 
493   O OD2 . ASP A 66  ? 1.5423 1.4036 1.6586 -0.1362 -0.5048 0.1095  66  ASP A OD2 
494   N N   . ILE A 67  ? 1.0282 0.8736 1.1276 -0.0929 -0.3389 0.1289  67  ILE A N   
495   C CA  . ILE A 67  ? 0.9119 0.7672 1.0299 -0.0911 -0.3033 0.1351  67  ILE A CA  
496   C C   . ILE A 67  ? 0.9146 0.7192 0.9693 -0.0831 -0.2844 0.1270  67  ILE A C   
497   O O   . ILE A 67  ? 1.0146 0.8034 1.0666 -0.0901 -0.2674 0.1256  67  ILE A O   
498   C CB  . ILE A 67  ? 0.7532 0.6532 0.9088 -0.0744 -0.2847 0.1469  67  ILE A CB  
499   C CG1 . ILE A 67  ? 0.8858 0.8422 1.1121 -0.0804 -0.2990 0.1555  67  ILE A CG1 
500   C CG2 . ILE A 67  ? 0.6084 0.5114 0.7688 -0.0710 -0.2490 0.1516  67  ILE A CG2 
501   C CD1 . ILE A 67  ? 0.7474 0.7418 1.0021 -0.0589 -0.2893 0.1639  67  ILE A CD1 
502   N N   . VAL A 68  ? 0.8946 0.6740 0.8994 -0.0685 -0.2875 0.1226  68  VAL A N   
503   C CA  . VAL A 68  ? 0.9479 0.6832 0.8947 -0.0602 -0.2688 0.1152  68  VAL A CA  
504   C C   . VAL A 68  ? 0.9836 0.6777 0.8999 -0.0737 -0.2771 0.1023  68  VAL A C   
505   O O   . VAL A 68  ? 1.1112 0.7830 1.0122 -0.0728 -0.2560 0.0986  68  VAL A O   
506   C CB  . VAL A 68  ? 0.8702 0.5857 0.7687 -0.0447 -0.2729 0.1142  68  VAL A CB  
507   C CG1 . VAL A 68  ? 0.8581 0.5305 0.6993 -0.0380 -0.2521 0.1065  68  VAL A CG1 
508   C CG2 . VAL A 68  ? 0.7776 0.5268 0.7040 -0.0303 -0.2636 0.1263  68  VAL A CG2 
509   N N   . ARG A 69  ? 0.9914 0.6749 0.8999 -0.0857 -0.3092 0.0949  69  ARG A N   
510   C CA  . ARG A 69  ? 1.0496 0.6890 0.9259 -0.0995 -0.3210 0.0799  69  ARG A CA  
511   C C   . ARG A 69  ? 0.9691 0.6136 0.8862 -0.1143 -0.3105 0.0822  69  ARG A C   
512   O O   . ARG A 69  ? 1.0590 0.6629 0.9472 -0.1164 -0.2997 0.0729  69  ARG A O   
513   C CB  . ARG A 69  ? 0.9616 0.5942 0.8270 -0.1115 -0.3619 0.0720  69  ARG A CB  
514   C CG  . ARG A 69  ? 0.9985 0.6205 0.8161 -0.0968 -0.3751 0.0713  69  ARG A CG  
515   C CD  . ARG A 69  ? 1.2846 0.8841 1.0695 -0.1078 -0.4159 0.0596  69  ARG A CD  
516   N NE  . ARG A 69  ? 1.2530 0.8456 0.9940 -0.0927 -0.4294 0.0629  69  ARG A NE  
517   C CZ  . ARG A 69  ? 1.2472 0.8787 1.0205 -0.0875 -0.4509 0.0752  69  ARG A CZ  
518   N NH1 . ARG A 69  ? 1.2000 0.8849 1.0538 -0.0961 -0.4603 0.0844  69  ARG A NH1 
519   N NH2 . ARG A 69  ? 1.3973 1.0143 1.1231 -0.0729 -0.4620 0.0792  69  ARG A NH2 
520   N N   . SER A 70  ? 0.8508 0.5444 0.8347 -0.1234 -0.3122 0.0953  70  SER A N   
521   C CA  . SER A 70  ? 0.9983 0.6997 1.0233 -0.1390 -0.3018 0.1011  70  SER A CA  
522   C C   . SER A 70  ? 0.9759 0.6678 0.9925 -0.1274 -0.2666 0.1066  70  SER A C   
523   O O   . SER A 70  ? 1.0197 0.6907 1.0413 -0.1372 -0.2584 0.1067  70  SER A O   
524   C CB  . SER A 70  ? 0.8749 0.6361 0.9726 -0.1495 -0.3078 0.1155  70  SER A CB  
525   O OG  . SER A 70  ? 1.0700 0.8710 1.1912 -0.1328 -0.2844 0.1283  70  SER A OG  
526   N N   . LEU A 71  ? 0.9665 0.6726 0.9711 -0.1072 -0.2475 0.1115  71  LEU A N   
527   C CA  . LEU A 71  ? 0.8891 0.5906 0.8870 -0.0959 -0.2171 0.1165  71  LEU A CA  
528   C C   . LEU A 71  ? 0.9953 0.6449 0.9386 -0.0879 -0.2087 0.1038  71  LEU A C   
529   O O   . LEU A 71  ? 1.0855 0.7270 1.0269 -0.0812 -0.1871 0.1071  71  LEU A O   
530   C CB  . LEU A 71  ? 0.7310 0.4670 0.7389 -0.0792 -0.2011 0.1253  71  LEU A CB  
531   C CG  . LEU A 71  ? 0.7073 0.4959 0.7722 -0.0829 -0.1969 0.1390  71  LEU A CG  
532   C CD1 . LEU A 71  ? 0.7083 0.5236 0.7770 -0.0666 -0.1916 0.1428  71  LEU A CD1 
533   C CD2 . LEU A 71  ? 0.9086 0.7068 0.9939 -0.0856 -0.1743 0.1486  71  LEU A CD2 
534   N N   . ILE A 72  ? 0.9798 0.5949 0.8787 -0.0878 -0.2254 0.0895  72  ILE A N   
535   C CA  . ILE A 72  ? 0.9992 0.5654 0.8456 -0.0791 -0.2150 0.0762  72  ILE A CA  
536   C C   . ILE A 72  ? 1.0206 0.5474 0.8598 -0.0935 -0.2264 0.0656  72  ILE A C   
537   O O   . ILE A 72  ? 1.0993 0.6073 0.9241 -0.1062 -0.2527 0.0551  72  ILE A O   
538   C CB  . ILE A 72  ? 0.9043 0.4491 0.6959 -0.0684 -0.2208 0.0661  72  ILE A CB  
539   C CG1 . ILE A 72  ? 0.9290 0.5079 0.7282 -0.0551 -0.2093 0.0775  72  ILE A CG1 
540   C CG2 . ILE A 72  ? 0.8857 0.3834 0.6258 -0.0581 -0.2045 0.0524  72  ILE A CG2 
541   C CD1 . ILE A 72  ? 0.8408 0.4037 0.5926 -0.0476 -0.2198 0.0725  72  ILE A CD1 
542   N N   . VAL A 73  ? 1.0153 0.5280 0.8642 -0.0915 -0.2083 0.0684  73  VAL A N   
543   C CA  . VAL A 73  ? 1.0197 0.4885 0.8611 -0.1031 -0.2157 0.0592  73  VAL A CA  
544   C C   . VAL A 73  ? 1.1744 0.6068 0.9809 -0.0846 -0.1930 0.0512  73  VAL A C   
545   O O   . VAL A 73  ? 1.1086 0.5549 0.9362 -0.0750 -0.1719 0.0627  73  VAL A O   
546   C CB  . VAL A 73  ? 0.8848 0.3728 0.7804 -0.1199 -0.2168 0.0743  73  VAL A CB  
547   C CG1 . VAL A 73  ? 0.9389 0.3743 0.8247 -0.1324 -0.2247 0.0650  73  VAL A CG1 
548   C CG2 . VAL A 73  ? 1.0741 0.6073 1.0116 -0.1365 -0.2359 0.0832  73  VAL A CG2 
549   N N   . GLU A 74  ? 1.2533 0.6397 1.0058 -0.0791 -0.1979 0.0310  74  GLU A N   
550   C CA  . GLU A 74  ? 1.1215 0.4738 0.8383 -0.0588 -0.1744 0.0209  74  GLU A CA  
551   C C   . GLU A 74  ? 1.2105 0.5285 0.9390 -0.0602 -0.1687 0.0194  74  GLU A C   
552   O O   . GLU A 74  ? 1.1233 0.3868 0.8161 -0.0618 -0.1760 0.0005  74  GLU A O   
553   C CB  . GLU A 74  ? 1.3978 0.7111 1.0503 -0.0526 -0.1798 -0.0005 74  GLU A CB  
554   C CG  . GLU A 74  ? 1.1758 0.5184 0.8108 -0.0463 -0.1796 0.0037  74  GLU A CG  
555   C CD  . GLU A 74  ? 1.4266 0.7333 0.9939 -0.0333 -0.1717 -0.0133 74  GLU A CD  
556   O OE1 . GLU A 74  ? 1.5352 0.8292 1.0868 -0.0159 -0.1439 -0.0173 74  GLU A OE1 
557   O OE2 . GLU A 74  ? 1.2425 0.5354 0.7730 -0.0405 -0.1934 -0.0218 74  GLU A OE2 
558   N N   . GLU A 75  ? 1.1875 0.5334 0.9608 -0.0589 -0.1564 0.0385  75  GLU A N   
559   C CA  . GLU A 75  ? 1.1939 0.5100 0.9811 -0.0578 -0.1494 0.0421  75  GLU A CA  
560   C C   . GLU A 75  ? 1.0460 0.3937 0.8545 -0.0385 -0.1246 0.0575  75  GLU A C   
561   O O   . GLU A 75  ? 1.1302 0.5291 0.9666 -0.0400 -0.1207 0.0731  75  GLU A O   
562   C CB  . GLU A 75  ? 1.0025 0.3219 0.8274 -0.0833 -0.1667 0.0538  75  GLU A CB  
563   C CG  . GLU A 75  ? 1.0528 0.3395 0.8599 -0.1044 -0.1941 0.0373  75  GLU A CG  
564   C CD  . GLU A 75  ? 1.2777 0.5681 1.1262 -0.1325 -0.2112 0.0485  75  GLU A CD  
565   O OE1 . GLU A 75  ? 1.4512 0.7552 1.3352 -0.1347 -0.1992 0.0683  75  GLU A OE1 
566   O OE2 . GLU A 75  ? 1.2573 0.5378 1.1027 -0.1532 -0.2369 0.0379  75  GLU A OE2 
567   N N   . GLU A 76  ? 1.0714 0.3898 0.8667 -0.0196 -0.1085 0.0523  76  GLU A N   
568   C CA  . GLU A 76  ? 1.0832 0.4331 0.8989 -0.0005 -0.0873 0.0656  76  GLU A CA  
569   C C   . GLU A 76  ? 1.0527 0.4218 0.9095 -0.0056 -0.0865 0.0887  76  GLU A C   
570   O O   . GLU A 76  ? 1.1296 0.4700 0.9913 0.0029  -0.0813 0.0927  76  GLU A O   
571   C CB  . GLU A 76  ? 1.2174 0.5354 1.0082 0.0239  -0.0698 0.0519  76  GLU A CB  
572   C CG  . GLU A 76  ? 1.1899 0.4924 0.9358 0.0299  -0.0663 0.0307  76  GLU A CG  
573   C CD  . GLU A 76  ? 1.3127 0.6062 1.0401 0.0559  -0.0418 0.0204  76  GLU A CD  
574   O OE1 . GLU A 76  ? 1.3227 0.6165 1.0731 0.0719  -0.0288 0.0274  76  GLU A OE1 
575   O OE2 . GLU A 76  ? 1.3749 0.6623 1.0651 0.0607  -0.0353 0.0062  76  GLU A OE2 
576   N N   . MET A 77  ? 0.8576 0.2746 0.7409 -0.0179 -0.0907 0.1038  77  MET A N   
577   C CA  . MET A 77  ? 0.8720 0.3141 0.7902 -0.0230 -0.0878 0.1273  77  MET A CA  
578   C C   . MET A 77  ? 0.8444 0.3456 0.7792 -0.0226 -0.0825 0.1369  77  MET A C   
579   O O   . MET A 77  ? 0.9265 0.4434 0.8545 -0.0296 -0.0895 0.1288  77  MET A O   
580   C CB  . MET A 77  ? 0.9830 0.4098 0.9176 -0.0477 -0.1026 0.1348  77  MET A CB  
581   C CG  . MET A 77  ? 1.0206 0.3897 0.9447 -0.0490 -0.1062 0.1290  77  MET A CG  
582   S SD  . MET A 77  ? 1.1818 0.5538 1.1220 -0.0318 -0.0880 0.1463  77  MET A SD  
583   C CE  . MET A 77  ? 1.1263 0.5254 1.0981 -0.0567 -0.0909 0.1685  77  MET A CE  
584   N N   . LEU A 78  ? 0.8560 0.3867 0.8095 -0.0143 -0.0719 0.1531  78  LEU A N   
585   C CA  . LEU A 78  ? 0.7538 0.3363 0.7187 -0.0119 -0.0658 0.1594  78  LEU A CA  
586   C C   . LEU A 78  ? 0.8429 0.4483 0.8175 -0.0291 -0.0757 0.1594  78  LEU A C   
587   O O   . LEU A 78  ? 0.9485 0.5688 0.9129 -0.0260 -0.0765 0.1498  78  LEU A O   
588   C CB  . LEU A 78  ? 0.8474 0.4540 0.8313 -0.0075 -0.0582 0.1789  78  LEU A CB  
589   C CG  . LEU A 78  ? 0.7003 0.3546 0.6921 -0.0024 -0.0511 0.1835  78  LEU A CG  
590   C CD1 . LEU A 78  ? 0.6137 0.2733 0.5913 0.0097  -0.0457 0.1685  78  LEU A CD1 
591   C CD2 . LEU A 78  ? 0.7069 0.3777 0.7087 0.0053  -0.0449 0.1999  78  LEU A CD2 
592   N N   . ASP A 79  ? 0.7198 0.3291 0.7152 -0.0461 -0.0824 0.1708  79  ASP A N   
593   C CA  . ASP A 79  ? 0.7170 0.3561 0.7307 -0.0615 -0.0909 0.1727  79  ASP A CA  
594   C C   . ASP A 79  ? 0.8330 0.4623 0.8283 -0.0622 -0.1027 0.1547  79  ASP A C   
595   O O   . ASP A 79  ? 0.8897 0.5515 0.8927 -0.0626 -0.1051 0.1541  79  ASP A O   
596   C CB  . ASP A 79  ? 0.6895 0.3224 0.7269 -0.0826 -0.0984 0.1837  79  ASP A CB  
597   C CG  . ASP A 79  ? 0.9352 0.5163 0.9595 -0.0919 -0.1115 0.1731  79  ASP A CG  
598   O OD1 . ASP A 79  ? 1.1281 0.6715 1.1283 -0.0789 -0.1074 0.1660  79  ASP A OD1 
599   O OD2 . ASP A 79  ? 1.0913 0.6704 1.1305 -0.1119 -0.1260 0.1714  79  ASP A OD2 
600   N N   . LYS A 80  ? 0.9332 0.5173 0.9025 -0.0614 -0.1099 0.1405  80  LYS A N   
601   C CA  . LYS A 80  ? 0.9676 0.5363 0.9116 -0.0631 -0.1230 0.1233  80  LYS A CA  
602   C C   . LYS A 80  ? 0.8226 0.4083 0.7474 -0.0462 -0.1125 0.1181  80  LYS A C   
603   O O   . LYS A 80  ? 0.8955 0.4948 0.8132 -0.0481 -0.1213 0.1135  80  LYS A O   
604   C CB  . LYS A 80  ? 0.8458 0.3571 0.7587 -0.0638 -0.1302 0.1074  80  LYS A CB  
605   C CG  . LYS A 80  ? 0.8397 0.3219 0.7678 -0.0780 -0.1367 0.1126  80  LYS A CG  
606   C CD  . LYS A 80  ? 0.9734 0.4578 0.9201 -0.1032 -0.1585 0.1123  80  LYS A CD  
607   C CE  . LYS A 80  ? 0.8698 0.3273 0.8361 -0.1196 -0.1626 0.1207  80  LYS A CE  
608   N NZ  . LYS A 80  ? 1.2297 0.7294 1.2428 -0.1393 -0.1660 0.1393  80  LYS A NZ  
609   N N   . LEU A 81  ? 0.7586 0.3431 0.6767 -0.0302 -0.0948 0.1199  81  LEU A N   
610   C CA  . LEU A 81  ? 0.8044 0.4055 0.7080 -0.0158 -0.0827 0.1161  81  LEU A CA  
611   C C   . LEU A 81  ? 0.8522 0.4979 0.7780 -0.0190 -0.0830 0.1260  81  LEU A C   
612   O O   . LEU A 81  ? 0.9317 0.5851 0.8438 -0.0163 -0.0851 0.1209  81  LEU A O   
613   C CB  . LEU A 81  ? 0.7557 0.3555 0.6610 -0.0005 -0.0651 0.1191  81  LEU A CB  
614   C CG  . LEU A 81  ? 0.9425 0.5504 0.8316 0.0137  -0.0510 0.1128  81  LEU A CG  
615   C CD1 . LEU A 81  ? 1.0715 0.6570 0.9516 0.0284  -0.0380 0.1071  81  LEU A CD1 
616   C CD2 . LEU A 81  ? 0.6163 0.2674 0.5272 0.0160  -0.0437 0.1235  81  LEU A CD2 
617   N N   . LEU A 82  ? 0.8022 0.4736 0.7585 -0.0238 -0.0800 0.1399  82  LEU A N   
618   C CA  . LEU A 82  ? 0.8609 0.5732 0.8369 -0.0247 -0.0776 0.1478  82  LEU A CA  
619   C C   . LEU A 82  ? 0.8479 0.5694 0.8307 -0.0345 -0.0928 0.1450  82  LEU A C   
620   O O   . LEU A 82  ? 0.8949 0.6358 0.8772 -0.0295 -0.0927 0.1440  82  LEU A O   
621   C CB  . LEU A 82  ? 0.8190 0.5545 0.8211 -0.0279 -0.0702 0.1628  82  LEU A CB  
622   C CG  . LEU A 82  ? 0.7220 0.4514 0.7197 -0.0176 -0.0585 0.1678  82  LEU A CG  
623   C CD1 . LEU A 82  ? 0.6625 0.4059 0.6794 -0.0233 -0.0548 0.1840  82  LEU A CD1 
624   C CD2 . LEU A 82  ? 0.5325 0.2801 0.5230 -0.0050 -0.0486 0.1646  82  LEU A CD2 
625   N N   . ASN A 83  ? 0.8594 0.5659 0.8491 -0.0482 -0.1073 0.1437  83  ASN A N   
626   C CA  . ASN A 83  ? 0.8244 0.5420 0.8241 -0.0578 -0.1253 0.1409  83  ASN A CA  
627   C C   . ASN A 83  ? 0.8636 0.5624 0.8276 -0.0501 -0.1333 0.1284  83  ASN A C   
628   O O   . ASN A 83  ? 0.9069 0.6249 0.8762 -0.0493 -0.1427 0.1288  83  ASN A O   
629   C CB  . ASN A 83  ? 0.7443 0.4467 0.7581 -0.0762 -0.1409 0.1406  83  ASN A CB  
630   C CG  . ASN A 83  ? 0.8001 0.5310 0.8563 -0.0879 -0.1359 0.1561  83  ASN A CG  
631   O OD1 . ASN A 83  ? 0.8813 0.6479 0.9569 -0.0820 -0.1222 0.1664  83  ASN A OD1 
632   N ND2 . ASN A 83  ? 0.9002 0.6142 0.9700 -0.1055 -0.1461 0.1580  83  ASN A ND2 
633   N N   . SER A 84  ? 0.8667 0.5281 0.7936 -0.0433 -0.1285 0.1181  84  SER A N   
634   C CA  . SER A 84  ? 0.8197 0.4604 0.7058 -0.0355 -0.1320 0.1071  84  SER A CA  
635   C C   . SER A 84  ? 0.8880 0.5544 0.7751 -0.0240 -0.1199 0.1128  84  SER A C   
636   O O   . SER A 84  ? 0.9278 0.5924 0.7961 -0.0210 -0.1277 0.1102  84  SER A O   
637   C CB  . SER A 84  ? 0.9384 0.5383 0.7881 -0.0282 -0.1222 0.0959  84  SER A CB  
638   O OG  . SER A 84  ? 1.0144 0.5882 0.8192 -0.0238 -0.1274 0.0843  84  SER A OG  
639   N N   . GLY A 85  ? 0.8553 0.5431 0.7629 -0.0183 -0.1023 0.1206  85  GLY A N   
640   C CA  . GLY A 85  ? 0.7955 0.5063 0.7072 -0.0096 -0.0912 0.1252  85  GLY A CA  
641   C C   . GLY A 85  ? 0.8841 0.6227 0.8191 -0.0126 -0.1015 0.1312  85  GLY A C   
642   O O   . GLY A 85  ? 1.0263 0.7694 0.9516 -0.0062 -0.1018 0.1312  85  GLY A O   
643   N N   . LEU A 86  ? 0.7825 0.5398 0.7499 -0.0221 -0.1093 0.1370  86  LEU A N   
644   C CA  . LEU A 86  ? 0.7144 0.5030 0.7109 -0.0241 -0.1183 0.1426  86  LEU A CA  
645   C C   . LEU A 86  ? 0.8593 0.6359 0.8414 -0.0258 -0.1398 0.1373  86  LEU A C   
646   O O   . LEU A 86  ? 0.8098 0.6058 0.8043 -0.0207 -0.1468 0.1405  86  LEU A O   
647   C CB  . LEU A 86  ? 0.6255 0.4388 0.6621 -0.0354 -0.1195 0.1508  86  LEU A CB  
648   C CG  . LEU A 86  ? 0.7703 0.6003 0.8218 -0.0337 -0.0998 0.1589  86  LEU A CG  
649   C CD1 . LEU A 86  ? 0.6402 0.4886 0.7258 -0.0472 -0.1008 0.1684  86  LEU A CD1 
650   C CD2 . LEU A 86  ? 0.6043 0.4592 0.6615 -0.0221 -0.0875 0.1612  86  LEU A CD2 
651   N N   . ALA A 87  ? 0.8185 0.5613 0.7719 -0.0318 -0.1512 0.1288  87  ALA A N   
652   C CA  . ALA A 87  ? 0.8167 0.5436 0.7473 -0.0336 -0.1738 0.1229  87  ALA A CA  
653   C C   . ALA A 87  ? 0.7574 0.4743 0.6553 -0.0198 -0.1679 0.1225  87  ALA A C   
654   O O   . ALA A 87  ? 0.9116 0.6355 0.8080 -0.0162 -0.1830 0.1251  87  ALA A O   
655   C CB  . ALA A 87  ? 0.8554 0.5419 0.7531 -0.0416 -0.1836 0.1115  87  ALA A CB  
656   N N   . THR A 88  ? 0.7233 0.4251 0.5980 -0.0122 -0.1461 0.1205  88  THR A N   
657   C CA  . THR A 88  ? 0.8562 0.5476 0.7018 -0.0015 -0.1371 0.1214  88  THR A CA  
658   C C   . THR A 88  ? 0.8497 0.5715 0.7250 0.0046  -0.1350 0.1303  88  THR A C   
659   O O   . THR A 88  ? 0.8740 0.5890 0.7325 0.0114  -0.1410 0.1332  88  THR A O   
660   C CB  . THR A 88  ? 0.9317 0.6081 0.7580 0.0031  -0.1129 0.1179  88  THR A CB  
661   O OG1 . THR A 88  ? 0.9814 0.6259 0.7765 0.0004  -0.1144 0.1082  88  THR A OG1 
662   C CG2 . THR A 88  ? 0.7237 0.3928 0.5266 0.0114  -0.1004 0.1205  88  THR A CG2 
663   N N   . ALA A 89  ? 0.7387 0.4911 0.6550 0.0031  -0.1265 0.1349  89  ALA A N   
664   C CA  . ALA A 89  ? 0.7540 0.5342 0.6980 0.0101  -0.1228 0.1412  89  ALA A CA  
665   C C   . ALA A 89  ? 0.9331 0.7270 0.8942 0.0112  -0.1447 0.1445  89  ALA A C   
666   O O   . ALA A 89  ? 0.9741 0.7703 0.9339 0.0212  -0.1476 0.1479  89  ALA A O   
667   C CB  . ALA A 89  ? 0.6302 0.4388 0.6092 0.0076  -0.1092 0.1445  89  ALA A CB  
668   N N   . VAL A 90  ? 0.8367 0.6386 0.8151 0.0008  -0.1612 0.1438  90  VAL A N   
669   C CA  . VAL A 90  ? 0.8657 0.6856 0.8664 0.0008  -0.1848 0.1470  90  VAL A CA  
670   C C   . VAL A 90  ? 0.9085 0.6981 0.8655 0.0069  -0.2019 0.1451  90  VAL A C   
671   O O   . VAL A 90  ? 1.0143 0.8149 0.9809 0.0161  -0.2153 0.1504  90  VAL A O   
672   C CB  . VAL A 90  ? 0.7942 0.6292 0.8250 -0.0151 -0.1998 0.1463  90  VAL A CB  
673   C CG1 . VAL A 90  ? 0.6785 0.5316 0.7310 -0.0161 -0.2285 0.1488  90  VAL A CG1 
674   C CG2 . VAL A 90  ? 0.6509 0.5190 0.7266 -0.0204 -0.1824 0.1519  90  VAL A CG2 
675   N N   . ALA A 91  ? 0.8565 0.6073 0.7641 0.0032  -0.2007 0.1381  91  ALA A N   
676   C CA  . ALA A 91  ? 0.8798 0.5980 0.7371 0.0084  -0.2140 0.1368  91  ALA A CA  
677   C C   . ALA A 91  ? 0.9636 0.6771 0.8084 0.0223  -0.2021 0.1441  91  ALA A C   
678   O O   . ALA A 91  ? 1.0453 0.7497 0.8732 0.0299  -0.2186 0.1495  91  ALA A O   
679   C CB  . ALA A 91  ? 0.8527 0.5312 0.6594 0.0031  -0.2069 0.1271  91  ALA A CB  
680   N N   . ALA A 92  ? 0.8334 0.5515 0.6864 0.0254  -0.1749 0.1447  92  ALA A N   
681   C CA  . ALA A 92  ? 0.8671 0.5783 0.7104 0.0360  -0.1620 0.1504  92  ALA A CA  
682   C C   . ALA A 92  ? 0.9657 0.7016 0.8447 0.0458  -0.1728 0.1574  92  ALA A C   
683   O O   . ALA A 92  ? 0.9829 0.7033 0.8449 0.0559  -0.1766 0.1636  92  ALA A O   
684   C CB  . ALA A 92  ? 0.7110 0.4275 0.5633 0.0348  -0.1343 0.1480  92  ALA A CB  
685   N N   . GLU A 93  ? 0.8203 0.5938 0.7493 0.0434  -0.1766 0.1572  93  GLU A N   
686   C CA  . GLU A 93  ? 0.7556 0.5582 0.7251 0.0541  -0.1847 0.1629  93  GLU A CA  
687   C C   . GLU A 93  ? 0.7187 0.5157 0.6802 0.0592  -0.2145 0.1678  93  GLU A C   
688   O O   . GLU A 93  ? 0.8330 0.6291 0.7985 0.0736  -0.2211 0.1744  93  GLU A O   
689   C CB  . GLU A 93  ? 0.7707 0.6167 0.7946 0.0484  -0.1809 0.1622  93  GLU A CB  
690   C CG  . GLU A 93  ? 0.7755 0.6556 0.8450 0.0612  -0.1858 0.1674  93  GLU A CG  
691   C CD  . GLU A 93  ? 1.0287 0.9510 1.1479 0.0582  -0.1708 0.1672  93  GLU A CD  
692   O OE1 . GLU A 93  ? 1.0025 0.9493 1.1511 0.0461  -0.1797 0.1684  93  GLU A OE1 
693   O OE2 . GLU A 93  ? 1.1262 1.0556 1.2533 0.0672  -0.1498 0.1659  93  GLU A OE2 
694   N N   . ILE A 94  ? 0.8319 0.6230 0.7808 0.0477  -0.2340 0.1645  94  ILE A N   
695   C CA  . ILE A 94  ? 0.9745 0.7599 0.9118 0.0506  -0.2667 0.1683  94  ILE A CA  
696   C C   . ILE A 94  ? 0.9857 0.7282 0.8648 0.0612  -0.2685 0.1735  94  ILE A C   
697   O O   . ILE A 94  ? 1.0163 0.7593 0.8977 0.0743  -0.2860 0.1823  94  ILE A O   
698   C CB  . ILE A 94  ? 0.8527 0.6328 0.7792 0.0335  -0.2863 0.1607  94  ILE A CB  
699   C CG1 . ILE A 94  ? 0.9381 0.7637 0.9298 0.0226  -0.2894 0.1593  94  ILE A CG1 
700   C CG2 . ILE A 94  ? 0.9370 0.6995 0.8320 0.0358  -0.3210 0.1630  94  ILE A CG2 
701   C CD1 . ILE A 94  ? 0.9061 0.7203 0.8888 0.0025  -0.2945 0.1500  94  ILE A CD1 
702   N N   . ILE A 95  ? 0.8747 0.5814 0.7045 0.0562  -0.2490 0.1693  95  ILE A N   
703   C CA  . ILE A 95  ? 1.0453 0.7104 0.8184 0.0638  -0.2459 0.1754  95  ILE A CA  
704   C C   . ILE A 95  ? 1.0925 0.7605 0.8835 0.0789  -0.2376 0.1853  95  ILE A C   
705   O O   . ILE A 95  ? 1.0277 0.6785 0.7954 0.0884  -0.2477 0.1928  95  ILE A O   
706   C CB  . ILE A 95  ? 0.9553 0.5902 0.6843 0.0553  -0.2200 0.1689  95  ILE A CB  
707   C CG1 . ILE A 95  ? 1.0308 0.6508 0.7292 0.0437  -0.2308 0.1588  95  ILE A CG1 
708   C CG2 . ILE A 95  ? 0.9210 0.5174 0.5994 0.0620  -0.2096 0.1775  95  ILE A CG2 
709   C CD1 . ILE A 95  ? 1.0519 0.6590 0.7333 0.0358  -0.2038 0.1494  95  ILE A CD1 
710   N N   . GLU A 96  ? 0.9742 0.6668 0.8075 0.0804  -0.2162 0.1823  96  GLU A N   
711   C CA  . GLU A 96  ? 0.8629 0.5558 0.7137 0.0944  -0.2066 0.1884  96  GLU A CA  
712   C C   . GLU A 96  ? 0.9861 0.7043 0.8766 0.1091  -0.2287 0.1948  96  GLU A C   
713   O O   . GLU A 96  ? 0.8991 0.6045 0.7849 0.1231  -0.2296 0.2013  96  GLU A O   
714   C CB  . GLU A 96  ? 0.7644 0.4752 0.6439 0.0909  -0.1783 0.1811  96  GLU A CB  
715   C CG  . GLU A 96  ? 0.8786 0.5643 0.7229 0.0801  -0.1557 0.1768  96  GLU A CG  
716   C CD  . GLU A 96  ? 1.0389 0.6840 0.8424 0.0840  -0.1483 0.1838  96  GLU A CD  
717   O OE1 . GLU A 96  ? 1.0120 0.6507 0.8253 0.0960  -0.1503 0.1895  96  GLU A OE1 
718   O OE2 . GLU A 96  ? 1.0418 0.6612 0.8045 0.0752  -0.1388 0.1837  96  GLU A OE2 
719   N N   . ALA A 97  ? 0.9261 0.6847 0.8598 0.1050  -0.2428 0.1915  97  ALA A N   
720   C CA  . ALA A 97  ? 0.7267 0.5174 0.7065 0.1187  -0.2642 0.1977  97  ALA A CA  
721   C C   . ALA A 97  ? 0.9126 0.6810 0.8579 0.1254  -0.2912 0.2051  97  ALA A C   
722   O O   . ALA A 97  ? 0.9003 0.6767 0.8619 0.1421  -0.2977 0.2108  97  ALA A O   
723   C CB  . ALA A 97  ? 0.6977 0.5366 0.7292 0.1081  -0.2726 0.1928  97  ALA A CB  
724   N N   . ALA A 98  ? 0.8922 0.6343 0.7874 0.1119  -0.3013 0.2022  98  ALA A N   
725   C CA  . ALA A 98  ? 1.0185 0.7400 0.8729 0.1149  -0.3211 0.2059  98  ALA A CA  
726   C C   . ALA A 98  ? 0.9796 0.6682 0.7983 0.1259  -0.3034 0.2126  98  ALA A C   
727   O O   . ALA A 98  ? 1.0562 0.7409 0.8675 0.1374  -0.3178 0.2203  98  ALA A O   
728   C CB  . ALA A 98  ? 0.9556 0.6507 0.7582 0.0982  -0.3309 0.1995  98  ALA A CB  
729   N N   . LYS A 99  ? 0.9469 0.6135 0.7473 0.1219  -0.2727 0.2104  99  LYS A N   
730   C CA  . LYS A 99  ? 0.9190 0.5552 0.6915 0.1286  -0.2538 0.2168  99  LYS A CA  
731   C C   . LYS A 99  ? 1.0212 0.6717 0.8322 0.1484  -0.2584 0.2239  99  LYS A C   
732   O O   . LYS A 99  ? 1.1109 0.7396 0.8998 0.1573  -0.2607 0.2331  99  LYS A O   
733   C CB  . LYS A 99  ? 0.8657 0.4881 0.6314 0.1200  -0.2215 0.2116  99  LYS A CB  
734   C CG  . LYS A 99  ? 0.9211 0.5199 0.6397 0.1037  -0.2097 0.2067  99  LYS A CG  
735   C CD  . LYS A 99  ? 0.9500 0.5411 0.6702 0.0963  -0.1785 0.2024  99  LYS A CD  
736   C CE  . LYS A 99  ? 1.1390 0.6997 0.8093 0.0854  -0.1608 0.2026  99  LYS A CE  
737   N NZ  . LYS A 99  ? 1.1922 0.7492 0.8718 0.0789  -0.1324 0.1998  99  LYS A NZ  
738   N N   . TYR A 100 ? 1.0616 0.7480 0.9303 0.1558  -0.2587 0.2201  100 TYR A N   
739   C CA  . TYR A 100 ? 0.9243 0.6278 0.8351 0.1769  -0.2613 0.2248  100 TYR A CA  
740   C C   . TYR A 100 ? 1.0510 0.7761 0.9788 0.1883  -0.2918 0.2318  100 TYR A C   
741   O O   . TYR A 100 ? 1.1255 0.8572 1.0774 0.2081  -0.2952 0.2380  100 TYR A O   
742   C CB  . TYR A 100 ? 0.9171 0.6544 0.8839 0.1811  -0.2499 0.2175  100 TYR A CB  
743   C CG  . TYR A 100 ? 0.8627 0.5760 0.8178 0.1781  -0.2204 0.2123  100 TYR A CG  
744   C CD1 . TYR A 100 ? 0.7717 0.4705 0.6992 0.1588  -0.2061 0.2067  100 TYR A CD1 
745   C CD2 . TYR A 100 ? 0.9520 0.6549 0.9220 0.1944  -0.2075 0.2126  100 TYR A CD2 
746   C CE1 . TYR A 100 ? 0.9007 0.5790 0.8181 0.1548  -0.1811 0.2018  100 TYR A CE1 
747   C CE2 . TYR A 100 ? 0.7881 0.4661 0.7452 0.1898  -0.1831 0.2066  100 TYR A CE2 
748   C CZ  . TYR A 100 ? 0.8188 0.4866 0.7508 0.1694  -0.1707 0.2013  100 TYR A CZ  
749   O OH  . TYR A 100 ? 0.9932 0.6388 0.9142 0.1639  -0.1486 0.1950  100 TYR A OH  
750   N N   . VAL A 101 ? 0.9929 0.7274 0.9077 0.1761  -0.3144 0.2303  101 VAL A N   
751   C CA  . VAL A 101 ? 1.1191 0.8741 1.0470 0.1839  -0.3464 0.2360  101 VAL A CA  
752   C C   . VAL A 101 ? 1.1565 0.8693 1.0241 0.1876  -0.3524 0.2456  101 VAL A C   
753   O O   . VAL A 101 ? 1.1179 0.8331 0.9957 0.2053  -0.3635 0.2555  101 VAL A O   
754   C CB  . VAL A 101 ? 1.0960 0.8767 1.0353 0.1669  -0.3698 0.2290  101 VAL A CB  
755   C CG1 . VAL A 101 ? 1.0162 0.8045 0.9471 0.1700  -0.4045 0.2340  101 VAL A CG1 
756   C CG2 . VAL A 101 ? 1.1023 0.9340 1.1146 0.1655  -0.3679 0.2237  101 VAL A CG2 
757   N N   . LEU A 102 ? 1.1454 0.8201 0.9514 0.1716  -0.3437 0.2432  102 LEU A N   
758   C CA  . LEU A 102 ? 1.2400 0.8741 0.9853 0.1726  -0.3466 0.2526  102 LEU A CA  
759   C C   . LEU A 102 ? 1.2588 0.8664 0.9966 0.1843  -0.3248 0.2626  102 LEU A C   
760   O O   . LEU A 102 ? 1.3715 0.9486 1.0677 0.1879  -0.3287 0.2738  102 LEU A O   
761   C CB  . LEU A 102 ? 1.1482 0.7509 0.8323 0.1528  -0.3387 0.2461  102 LEU A CB  
762   C CG  . LEU A 102 ? 1.1155 0.7311 0.7912 0.1402  -0.3633 0.2365  102 LEU A CG  
763   C CD1 . LEU A 102 ? 1.1545 0.7398 0.7779 0.1226  -0.3474 0.2274  102 LEU A CD1 
764   C CD2 . LEU A 102 ? 1.3140 0.9283 0.9687 0.1455  -0.3971 0.2427  102 LEU A CD2 
765   N N   . SER A 103 ? 1.1683 0.7852 0.9446 0.1894  -0.3029 0.2588  103 SER A N   
766   C CA  . SER A 103 ? 1.1028 0.6931 0.8762 0.1990  -0.2828 0.2663  103 SER A CA  
767   C C   . SER A 103 ? 1.1016 0.7174 0.9346 0.2122  -0.2725 0.2608  103 SER A C   
768   O O   . SER A 103 ? 1.2114 0.8473 1.0677 0.2042  -0.2620 0.2493  103 SER A O   
769   C CB  . SER A 103 ? 1.0953 0.6493 0.8250 0.1816  -0.2560 0.2642  103 SER A CB  
770   O OG  . SER A 103 ? 1.4020 0.9277 1.1285 0.1877  -0.2386 0.2716  103 SER A OG  
771   N N   . ASP A 104 ? 1.1040 0.7184 0.9609 0.2334  -0.2754 0.2689  104 ASP A N   
772   C CA  . ASP A 104 ? 1.0093 0.6464 0.9211 0.2491  -0.2651 0.2628  104 ASP A CA  
773   C C   . ASP A 104 ? 1.1275 0.7467 1.0361 0.2386  -0.2354 0.2525  104 ASP A C   
774   O O   . ASP A 104 ? 1.1142 0.7610 1.0566 0.2378  -0.2277 0.2412  104 ASP A O   
775   C CB  . ASP A 104 ? 1.0508 0.6791 0.9804 0.2744  -0.2704 0.2737  104 ASP A CB  
776   C CG  . ASP A 104 ? 1.4302 1.0865 1.3769 0.2887  -0.3012 0.2830  104 ASP A CG  
777   O OD1 . ASP A 104 ? 1.6005 1.3001 1.5743 0.2845  -0.3175 0.2767  104 ASP A OD1 
778   O OD2 . ASP A 104 ? 1.4905 1.1260 1.4256 0.3034  -0.3101 0.2968  104 ASP A OD2 
779   N N   . ALA A 105 ? 1.0415 0.6161 0.9103 0.2294  -0.2196 0.2567  105 ALA A N   
780   C CA  . ALA A 105 ? 1.0889 0.6446 0.9521 0.2169  -0.1932 0.2472  105 ALA A CA  
781   C C   . ALA A 105 ? 1.0591 0.5941 0.8738 0.1926  -0.1853 0.2479  105 ALA A C   
782   O O   . ALA A 105 ? 1.0729 0.5719 0.8547 0.1862  -0.1769 0.2557  105 ALA A O   
783   C CB  . ALA A 105 ? 1.2891 0.8107 1.1547 0.2268  -0.1809 0.2505  105 ALA A CB  
784   N N   . PRO A 106 ? 0.9648 0.5215 0.7747 0.1793  -0.1877 0.2404  106 PRO A N   
785   C CA  . PRO A 106 ? 0.9560 0.4932 0.7200 0.1588  -0.1788 0.2406  106 PRO A CA  
786   C C   . PRO A 106 ? 1.0515 0.5663 0.8045 0.1452  -0.1518 0.2362  106 PRO A C   
787   O O   . PRO A 106 ? 1.1124 0.6033 0.8274 0.1322  -0.1421 0.2407  106 PRO A O   
788   C CB  . PRO A 106 ? 0.9632 0.5296 0.7326 0.1505  -0.1882 0.2322  106 PRO A CB  
789   C CG  . PRO A 106 ? 0.9483 0.5487 0.7704 0.1613  -0.1928 0.2257  106 PRO A CG  
790   C CD  . PRO A 106 ? 0.9657 0.5648 0.8125 0.1823  -0.1983 0.2321  106 PRO A CD  
791   N N   . TYR A 107 ? 0.9763 0.4988 0.7619 0.1482  -0.1400 0.2272  107 TYR A N   
792   C CA  . TYR A 107 ? 0.9057 0.4090 0.6841 0.1344  -0.1171 0.2215  107 TYR A CA  
793   C C   . TYR A 107 ? 0.9396 0.4111 0.7197 0.1402  -0.1100 0.2256  107 TYR A C   
794   O O   . TYR A 107 ? 1.1353 0.6037 0.9315 0.1587  -0.1209 0.2304  107 TYR A O   
795   C CB  . TYR A 107 ? 0.9201 0.4468 0.7260 0.1312  -0.1087 0.2078  107 TYR A CB  
796   C CG  . TYR A 107 ? 0.9927 0.5409 0.7901 0.1188  -0.1093 0.2037  107 TYR A CG  
797   C CD1 . TYR A 107 ? 0.9444 0.5210 0.7564 0.1253  -0.1271 0.2033  107 TYR A CD1 
798   C CD2 . TYR A 107 ? 1.0271 0.5671 0.8042 0.1005  -0.0927 0.2003  107 TYR A CD2 
799   C CE1 . TYR A 107 ? 0.8959 0.4874 0.6994 0.1134  -0.1286 0.1991  107 TYR A CE1 
800   C CE2 . TYR A 107 ? 1.0545 0.6113 0.8239 0.0908  -0.0925 0.1963  107 TYR A CE2 
801   C CZ  . TYR A 107 ? 1.0241 0.6041 0.8049 0.0971  -0.1106 0.1955  107 TYR A CZ  
802   O OH  . TYR A 107 ? 1.0045 0.5956 0.7760 0.0869  -0.1108 0.1911  107 TYR A OH  
803   N N   . ALA A 108 ? 1.0858 0.5339 0.8508 0.1241  -0.0920 0.2237  108 ALA A N   
804   C CA  . ALA A 108 ? 0.9820 0.3951 0.7464 0.1247  -0.0840 0.2264  108 ALA A CA  
805   C C   . ALA A 108 ? 1.0384 0.4412 0.8010 0.1051  -0.0645 0.2170  108 ALA A C   
806   O O   . ALA A 108 ? 1.2307 0.6481 0.9827 0.0897  -0.0565 0.2144  108 ALA A O   
807   C CB  . ALA A 108 ? 1.0355 0.4211 0.7690 0.1232  -0.0877 0.2433  108 ALA A CB  
808   N N   . GLU A 109 ? 1.0503 0.4274 0.8234 0.1054  -0.0574 0.2114  109 GLU A N   
809   C CA  . GLU A 109 ? 1.1938 0.5599 0.9668 0.0858  -0.0409 0.2018  109 GLU A CA  
810   C C   . GLU A 109 ? 1.1503 0.5121 0.8993 0.0635  -0.0297 0.2108  109 GLU A C   
811   O O   . GLU A 109 ? 1.2235 0.5708 0.9509 0.0633  -0.0323 0.2255  109 GLU A O   
812   C CB  . GLU A 109 ? 1.3442 0.6734 1.1246 0.0880  -0.0370 0.1969  109 GLU A CB  
813   C CG  . GLU A 109 ? 1.5690 0.9017 1.3731 0.1055  -0.0404 0.1810  109 GLU A CG  
814   C CD  . GLU A 109 ? 1.9999 1.2918 1.8080 0.1080  -0.0362 0.1735  109 GLU A CD  
815   O OE1 . GLU A 109 ? 2.1954 1.4721 2.0015 0.0909  -0.0258 0.1619  109 GLU A OE1 
816   O OE2 . GLU A 109 ? 2.0986 1.3729 1.9124 0.1268  -0.0440 0.1791  109 GLU A OE2 
817   N N   . PRO A 110 ? 1.0393 0.4145 0.7909 0.0455  -0.0169 0.2029  110 PRO A N   
818   C CA  . PRO A 110 ? 1.0234 0.4142 0.7952 0.0428  -0.0128 0.1865  110 PRO A CA  
819   C C   . PRO A 110 ? 1.1017 0.5271 0.8844 0.0560  -0.0218 0.1809  110 PRO A C   
820   O O   . PRO A 110 ? 1.2390 0.6710 1.0387 0.0646  -0.0238 0.1691  110 PRO A O   
821   C CB  . PRO A 110 ? 1.0175 0.4116 0.7852 0.0180  0.0032  0.1857  110 PRO A CB  
822   C CG  . PRO A 110 ? 1.0379 0.4358 0.7834 0.0127  0.0064  0.2001  110 PRO A CG  
823   C CD  . PRO A 110 ? 0.9669 0.3409 0.6993 0.0259  -0.0041 0.2115  110 PRO A CD  
824   N N   . CYS A 111 ? 1.0273 0.4729 0.7989 0.0573  -0.0270 0.1886  111 CYS A N   
825   C CA  . CYS A 111 ? 0.9587 0.4365 0.7418 0.0672  -0.0364 0.1841  111 CYS A CA  
826   C C   . CYS A 111 ? 0.8745 0.3587 0.6784 0.0890  -0.0498 0.1809  111 CYS A C   
827   O O   . CYS A 111 ? 1.0700 0.5370 0.8743 0.1009  -0.0569 0.1867  111 CYS A O   
828   C CB  . CYS A 111 ? 1.0487 0.5396 0.8124 0.0644  -0.0412 0.1923  111 CYS A CB  
829   S SG  . CYS A 111 ? 1.1662 0.6559 0.9090 0.0419  -0.0222 0.1939  111 CYS A SG  
830   N N   . VAL A 112 ? 1.0172 0.5269 0.8397 0.0950  -0.0522 0.1723  112 VAL A N   
831   C CA  . VAL A 112 ? 0.9444 0.4693 0.7934 0.1157  -0.0615 0.1674  112 VAL A CA  
832   C C   . VAL A 112 ? 0.9025 0.4591 0.7635 0.1249  -0.0775 0.1732  112 VAL A C   
833   O O   . VAL A 112 ? 1.0036 0.5631 0.8794 0.1438  -0.0908 0.1777  112 VAL A O   
834   C CB  . VAL A 112 ? 0.9074 0.4611 0.7822 0.1115  -0.0488 0.1495  112 VAL A CB  
835   C CG1 . VAL A 112 ? 1.0441 0.6246 0.9509 0.1316  -0.0531 0.1426  112 VAL A CG1 
836   C CG2 . VAL A 112 ? 0.9122 0.4334 0.7761 0.1017  -0.0365 0.1420  112 VAL A CG2 
837   N N   . GLY A 113 ? 0.8885 0.4697 0.7462 0.1118  -0.0766 0.1723  113 GLY A N   
838   C CA  . GLY A 113 ? 0.9122 0.5226 0.7815 0.1166  -0.0924 0.1760  113 GLY A CA  
839   C C   . GLY A 113 ? 0.9721 0.6280 0.8848 0.1221  -0.0905 0.1661  113 GLY A C   
840   O O   . GLY A 113 ? 0.9799 0.6528 0.9032 0.1131  -0.0755 0.1559  113 GLY A O   
841   N N   . PHE A 114 ? 0.9722 0.6499 0.9111 0.1367  -0.1055 0.1697  114 PHE A N   
842   C CA  . PHE A 114 ? 0.8239 0.5478 0.8065 0.1418  -0.1019 0.1622  114 PHE A CA  
843   C C   . PHE A 114 ? 0.9192 0.6432 0.9160 0.1498  -0.0845 0.1515  114 PHE A C   
844   O O   . PHE A 114 ? 1.0292 0.7209 1.0159 0.1611  -0.0833 0.1518  114 PHE A O   
845   C CB  . PHE A 114 ? 0.8590 0.6074 0.8715 0.1563  -0.1220 0.1693  114 PHE A CB  
846   C CG  . PHE A 114 ? 0.8452 0.6460 0.9058 0.1588  -0.1171 0.1636  114 PHE A CG  
847   C CD1 . PHE A 114 ? 0.8782 0.7076 0.9486 0.1426  -0.1175 0.1625  114 PHE A CD1 
848   C CD2 . PHE A 114 ? 0.7699 0.5892 0.8648 0.1773  -0.1099 0.1594  114 PHE A CD2 
849   C CE1 . PHE A 114 ? 0.7992 0.6754 0.9132 0.1431  -0.1113 0.1594  114 PHE A CE1 
850   C CE2 . PHE A 114 ? 0.7594 0.6286 0.8980 0.1790  -0.1020 0.1553  114 PHE A CE2 
851   C CZ  . PHE A 114 ? 0.6801 0.5776 0.8280 0.1608  -0.1028 0.1563  114 PHE A CZ  
852   N N   . ILE A 115 ? 0.9519 0.7093 0.9689 0.1440  -0.0712 0.1421  115 ILE A N   
853   C CA  . ILE A 115 ? 0.9497 0.7099 0.9760 0.1508  -0.0542 0.1299  115 ILE A CA  
854   C C   . ILE A 115 ? 0.8857 0.6847 0.9538 0.1679  -0.0532 0.1281  115 ILE A C   
855   O O   . ILE A 115 ? 0.8588 0.6979 0.9505 0.1621  -0.0534 0.1304  115 ILE A O   
856   C CB  . ILE A 115 ? 0.8255 0.5960 0.8414 0.1332  -0.0399 0.1214  115 ILE A CB  
857   C CG1 . ILE A 115 ? 0.7494 0.4905 0.7320 0.1158  -0.0405 0.1242  115 ILE A CG1 
858   C CG2 . ILE A 115 ? 0.7400 0.5093 0.7580 0.1397  -0.0245 0.1076  115 ILE A CG2 
859   C CD1 . ILE A 115 ? 0.8574 0.5520 0.8152 0.1163  -0.0381 0.1228  115 ILE A CD1 
860   N N   . SER A 116 ? 0.9405 0.7273 1.0194 0.1889  -0.0511 0.1246  116 SER A N   
861   C CA  . SER A 116 ? 0.8625 0.6877 0.9852 0.2083  -0.0480 0.1229  116 SER A CA  
862   C C   . SER A 116 ? 0.8385 0.6974 0.9755 0.2056  -0.0263 0.1115  116 SER A C   
863   O O   . SER A 116 ? 0.9234 0.7654 1.0324 0.1948  -0.0136 0.1016  116 SER A O   
864   C CB  . SER A 116 ? 1.1290 0.9271 1.2569 0.2338  -0.0499 0.1211  116 SER A CB  
865   O OG  . SER A 116 ? 1.2897 1.0532 1.3997 0.2365  -0.0703 0.1339  116 SER A OG  
866   N N   . ASP A 117 ? 0.7837 0.6918 0.9647 0.2152  -0.0224 0.1136  117 ASP A N   
867   C CA  . ASP A 117 ? 0.7854 0.7292 0.9804 0.2133  -0.0001 0.1054  117 ASP A CA  
868   C C   . ASP A 117 ? 0.7675 0.6870 0.9390 0.2234  0.0198  0.0882  117 ASP A C   
869   O O   . ASP A 117 ? 0.7595 0.6836 0.9106 0.2110  0.0338  0.0807  117 ASP A O   
870   C CB  . ASP A 117 ? 0.7551 0.7545 1.0063 0.2252  0.0028  0.1112  117 ASP A CB  
871   C CG  . ASP A 117 ? 0.7731 0.8065 1.0471 0.2070  -0.0107 0.1247  117 ASP A CG  
872   O OD1 . ASP A 117 ? 0.7232 0.7322 0.9711 0.1909  -0.0277 0.1306  117 ASP A OD1 
873   O OD2 . ASP A 117 ? 0.8270 0.9105 1.1452 0.2084  -0.0033 0.1288  117 ASP A OD2 
874   N N   . PRO A 118 ? 0.6971 0.5876 0.8676 0.2454  0.0207  0.0812  118 PRO A N   
875   C CA  . PRO A 118 ? 0.7419 0.6042 0.8856 0.2531  0.0388  0.0623  118 PRO A CA  
876   C C   . PRO A 118 ? 0.7855 0.6141 0.8818 0.2297  0.0388  0.0557  118 PRO A C   
877   O O   . PRO A 118 ? 0.9864 0.8119 1.0618 0.2267  0.0542  0.0411  118 PRO A O   
878   C CB  . PRO A 118 ? 0.7731 0.5979 0.9202 0.2775  0.0327  0.0595  118 PRO A CB  
879   C CG  . PRO A 118 ? 0.8977 0.7541 1.0893 0.2904  0.0182  0.0754  118 PRO A CG  
880   C CD  . PRO A 118 ? 0.8480 0.7263 1.0391 0.2648  0.0041  0.0897  118 PRO A CD  
881   N N   . ILE A 119 ? 0.7394 0.5450 0.8189 0.2132  0.0218  0.0663  119 ILE A N   
882   C CA  . ILE A 119 ? 0.7255 0.5054 0.7676 0.1907  0.0218  0.0614  119 ILE A CA  
883   C C   . ILE A 119 ? 0.7753 0.5938 0.8179 0.1747  0.0293  0.0621  119 ILE A C   
884   O O   . ILE A 119 ? 0.9150 0.7258 0.9329 0.1646  0.0372  0.0513  119 ILE A O   
885   C CB  . ILE A 119 ? 0.7741 0.5230 0.8003 0.1783  0.0050  0.0735  119 ILE A CB  
886   C CG1 . ILE A 119 ? 0.7382 0.4376 0.7532 0.1915  -0.0002 0.0721  119 ILE A CG1 
887   C CG2 . ILE A 119 ? 0.6439 0.3835 0.6430 0.1532  0.0058  0.0715  119 ILE A CG2 
888   C CD1 . ILE A 119 ? 1.1981 0.8723 1.2033 0.1865  -0.0169 0.0887  119 ILE A CD1 
889   N N   . ILE A 120 ? 0.7194 0.5782 0.7900 0.1725  0.0257  0.0748  120 ILE A N   
890   C CA  . ILE A 120 ? 0.6983 0.5920 0.7717 0.1579  0.0324  0.0783  120 ILE A CA  
891   C C   . ILE A 120 ? 0.7648 0.6753 0.8345 0.1657  0.0530  0.0661  120 ILE A C   
892   O O   . ILE A 120 ? 0.5888 0.5065 0.6384 0.1531  0.0599  0.0631  120 ILE A O   
893   C CB  . ILE A 120 ? 0.6905 0.6224 0.7997 0.1556  0.0251  0.0935  120 ILE A CB  
894   C CG1 . ILE A 120 ? 0.7958 0.7102 0.9059 0.1508  0.0035  0.1045  120 ILE A CG1 
895   C CG2 . ILE A 120 ? 0.5175 0.4787 0.6274 0.1392  0.0320  0.0987  120 ILE A CG2 
896   C CD1 . ILE A 120 ? 0.7663 0.6494 0.8425 0.1344  -0.0037 0.1055  120 ILE A CD1 
897   N N   . ARG A 121 ? 0.7475 0.6640 0.8354 0.1878  0.0629  0.0591  121 ARG A N   
898   C CA  . ARG A 121 ? 0.6792 0.6097 0.7607 0.1982  0.0852  0.0458  121 ARG A CA  
899   C C   . ARG A 121 ? 0.8424 0.7306 0.8772 0.1941  0.0880  0.0282  121 ARG A C   
900   O O   . ARG A 121 ? 1.0062 0.9017 1.0161 0.1865  0.0987  0.0206  121 ARG A O   
901   C CB  . ARG A 121 ? 0.6515 0.5958 0.7659 0.2257  0.0954  0.0415  121 ARG A CB  
902   C CG  . ARG A 121 ? 0.8120 0.8000 0.9793 0.2301  0.0890  0.0588  121 ARG A CG  
903   C CD  . ARG A 121 ? 0.8903 0.9100 1.0973 0.2565  0.1057  0.0547  121 ARG A CD  
904   N NE  . ARG A 121 ? 0.8100 0.8834 1.0403 0.2517  0.1249  0.0601  121 ARG A NE  
905   C CZ  . ARG A 121 ? 0.9362 1.0546 1.2097 0.2424  0.1192  0.0773  121 ARG A CZ  
906   N NH1 . ARG A 121 ? 0.9154 1.0320 1.2113 0.2378  0.0931  0.0895  121 ARG A NH1 
907   N NH2 . ARG A 121 ? 0.9975 1.1614 1.2902 0.2367  0.1394  0.0825  121 ARG A NH2 
908   N N   . SER A 122 ? 0.8944 0.7377 0.9169 0.1977  0.0770  0.0226  122 SER A N   
909   C CA  . SER A 122 ? 0.8388 0.6378 0.8212 0.1916  0.0767  0.0057  122 SER A CA  
910   C C   . SER A 122 ? 0.8735 0.6729 0.8304 0.1656  0.0700  0.0074  122 SER A C   
911   O O   . SER A 122 ? 1.0456 0.8317 0.9717 0.1600  0.0749  -0.0078 122 SER A O   
912   C CB  . SER A 122 ? 0.8569 0.6082 0.8358 0.1961  0.0642  0.0053  122 SER A CB  
913   O OG  . SER A 122 ? 1.0934 0.8022 1.0368 0.1840  0.0614  -0.0088 122 SER A OG  
914   N N   . LEU A 123 ? 0.8392 0.6525 0.8081 0.1508  0.0580  0.0248  123 LEU A N   
915   C CA  . LEU A 123 ? 0.9174 0.7332 0.8681 0.1284  0.0512  0.0280  123 LEU A CA  
916   C C   . LEU A 123 ? 0.9206 0.7769 0.8740 0.1224  0.0581  0.0348  123 LEU A C   
917   O O   . LEU A 123 ? 1.0289 0.8875 0.9630 0.1079  0.0548  0.0341  123 LEU A O   
918   C CB  . LEU A 123 ? 0.7279 0.5342 0.6869 0.1164  0.0365  0.0425  123 LEU A CB  
919   C CG  . LEU A 123 ? 1.0530 0.8160 1.0046 0.1175  0.0287  0.0403  123 LEU A CG  
920   C CD1 . LEU A 123 ? 0.9017 0.6616 0.8611 0.1083  0.0172  0.0569  123 LEU A CD1 
921   C CD2 . LEU A 123 ? 1.2263 0.9585 1.1511 0.1062  0.0282  0.0259  123 LEU A CD2 
922   N N   . GLY A 124 ? 0.8558 0.7443 0.8351 0.1327  0.0668  0.0427  124 GLY A N   
923   C CA  . GLY A 124 ? 0.7949 0.7203 0.7786 0.1261  0.0747  0.0519  124 GLY A CA  
924   C C   . GLY A 124 ? 0.8081 0.7374 0.7608 0.1265  0.0879  0.0404  124 GLY A C   
925   O O   . GLY A 124 ? 0.8244 0.7675 0.7627 0.1140  0.0873  0.0471  124 GLY A O   
926   N N   . VAL A 125 ? 0.7182 0.6330 0.6574 0.1416  0.0992  0.0229  125 VAL A N   
927   C CA  . VAL A 125 ? 0.7988 0.7142 0.7015 0.1431  0.1121  0.0096  125 VAL A CA  
928   C C   . VAL A 125 ? 0.9408 0.8328 0.8070 0.1259  0.0975  0.0027  125 VAL A C   
929   O O   . VAL A 125 ? 0.9251 0.8332 0.7710 0.1163  0.0982  0.0075  125 VAL A O   
930   C CB  . VAL A 125 ? 0.8152 0.7170 0.7093 0.1648  0.1285  -0.0102 125 VAL A CB  
931   C CG1 . VAL A 125 ? 0.7669 0.6695 0.6167 0.1660  0.1427  -0.0245 125 VAL A CG1 
932   C CG2 . VAL A 125 ? 0.8156 0.7476 0.7541 0.1826  0.1422  -0.0018 125 VAL A CG2 
933   N N   . PRO A 126 ? 0.9708 0.8267 0.8304 0.1208  0.0834  -0.0066 126 PRO A N   
934   C CA  . PRO A 126 ? 0.9016 0.7421 0.7343 0.1029  0.0689  -0.0121 126 PRO A CA  
935   C C   . PRO A 126 ? 0.8948 0.7600 0.7388 0.0877  0.0589  0.0076  126 PRO A C   
936   O O   . PRO A 126 ? 0.9931 0.8610 0.8156 0.0759  0.0506  0.0061  126 PRO A O   
937   C CB  . PRO A 126 ? 0.7967 0.5976 0.6320 0.0996  0.0579  -0.0212 126 PRO A CB  
938   C CG  . PRO A 126 ? 0.9332 0.7322 0.7995 0.1132  0.0622  -0.0129 126 PRO A CG  
939   C CD  . PRO A 126 ? 0.9726 0.8005 0.8494 0.1303  0.0796  -0.0111 126 PRO A CD  
940   N N   . LEU A 127 ? 0.7456 0.6282 0.6229 0.0886  0.0588  0.0256  127 LEU A N   
941   C CA  . LEU A 127 ? 0.8383 0.7407 0.7263 0.0761  0.0508  0.0434  127 LEU A CA  
942   C C   . LEU A 127 ? 0.8229 0.7513 0.6963 0.0755  0.0595  0.0495  127 LEU A C   
943   O O   . LEU A 127 ? 1.0233 0.9576 0.8831 0.0650  0.0511  0.0554  127 LEU A O   
944   C CB  . LEU A 127 ? 0.6293 0.5418 0.5522 0.0778  0.0490  0.0590  127 LEU A CB  
945   C CG  . LEU A 127 ? 0.7594 0.6496 0.6928 0.0723  0.0365  0.0612  127 LEU A CG  
946   C CD1 . LEU A 127 ? 0.5801 0.4768 0.5416 0.0781  0.0352  0.0726  127 LEU A CD1 
947   C CD2 . LEU A 127 ? 0.9105 0.8014 0.8394 0.0573  0.0260  0.0679  127 LEU A CD2 
948   N N   . VAL A 128 ? 0.7715 0.7157 0.6479 0.0875  0.0769  0.0488  128 VAL A N   
949   C CA  . VAL A 128 ? 0.7961 0.7647 0.6568 0.0873  0.0893  0.0562  128 VAL A CA  
950   C C   . VAL A 128 ? 0.8201 0.7766 0.6330 0.0849  0.0876  0.0426  128 VAL A C   
951   O O   . VAL A 128 ? 0.9977 0.9653 0.7909 0.0768  0.0841  0.0523  128 VAL A O   
952   C CB  . VAL A 128 ? 0.8180 0.8085 0.6968 0.1011  0.1113  0.0578  128 VAL A CB  
953   C CG1 . VAL A 128 ? 0.7703 0.7839 0.6272 0.1002  0.1277  0.0653  128 VAL A CG1 
954   C CG2 . VAL A 128 ? 0.6213 0.6281 0.5490 0.1011  0.1090  0.0730  128 VAL A CG2 
955   N N   . THR A 129 ? 0.8613 0.7926 0.6541 0.0915  0.0881  0.0201  129 THR A N   
956   C CA  . THR A 129 ? 0.8077 0.7242 0.5523 0.0881  0.0836  0.0040  129 THR A CA  
957   C C   . THR A 129 ? 0.8562 0.7640 0.5934 0.0713  0.0591  0.0057  129 THR A C   
958   O O   . THR A 129 ? 1.0824 0.9830 0.7820 0.0659  0.0506  -0.0047 129 THR A O   
959   C CB  . THR A 129 ? 0.9226 0.8095 0.6481 0.0991  0.0899  -0.0226 129 THR A CB  
960   O OG1 . THR A 129 ? 1.0659 0.9265 0.8118 0.0946  0.0758  -0.0286 129 THR A OG1 
961   C CG2 . THR A 129 ? 0.8806 0.7777 0.6158 0.1189  0.1154  -0.0262 129 THR A CG2 
962   N N   . GLY A 130 ? 0.7912 0.7003 0.5636 0.0637  0.0478  0.0179  130 GLY A N   
963   C CA  . GLY A 130 ? 0.9056 0.8110 0.6791 0.0491  0.0271  0.0206  130 GLY A CA  
964   C C   . GLY A 130 ? 0.9647 0.8416 0.7361 0.0429  0.0160  0.0025  130 GLY A C   
965   O O   . GLY A 130 ? 0.9497 0.8258 0.7269 0.0299  -0.0004 0.0036  130 GLY A O   
966   N N   . ASP A 131 ? 0.8630 0.7158 0.6282 0.0520  0.0251  -0.0139 131 ASP A N   
967   C CA  . ASP A 131 ? 0.9234 0.7429 0.6860 0.0451  0.0155  -0.0308 131 ASP A CA  
968   C C   . ASP A 131 ? 0.9142 0.7297 0.7129 0.0362  0.0075  -0.0184 131 ASP A C   
969   O O   . ASP A 131 ? 1.0033 0.8001 0.8042 0.0234  -0.0040 -0.0259 131 ASP A O   
970   C CB  . ASP A 131 ? 0.9894 0.7806 0.7381 0.0595  0.0282  -0.0496 131 ASP A CB  
971   C CG  . ASP A 131 ? 1.3241 1.1147 1.0300 0.0672  0.0366  -0.0659 131 ASP A CG  
972   O OD1 . ASP A 131 ? 1.4212 1.2160 1.0988 0.0560  0.0244  -0.0715 131 ASP A OD1 
973   O OD2 . ASP A 131 ? 1.4290 1.2162 1.1295 0.0853  0.0554  -0.0727 131 ASP A OD2 
974   N N   . ILE A 132 ? 0.8146 0.6477 0.6401 0.0420  0.0139  0.0005  132 ILE A N   
975   C CA  . ILE A 132 ? 0.9110 0.7431 0.7652 0.0349  0.0080  0.0140  132 ILE A CA  
976   C C   . ILE A 132 ? 0.9551 0.8184 0.8162 0.0289  0.0031  0.0295  132 ILE A C   
977   O O   . ILE A 132 ? 0.8700 0.7527 0.7375 0.0362  0.0105  0.0415  132 ILE A O   
978   C CB  . ILE A 132 ? 0.8109 0.6370 0.6857 0.0464  0.0164  0.0223  132 ILE A CB  
979   C CG1 . ILE A 132 ? 0.8495 0.6403 0.7183 0.0533  0.0193  0.0082  132 ILE A CG1 
980   C CG2 . ILE A 132 ? 0.8731 0.7031 0.7705 0.0389  0.0104  0.0381  132 ILE A CG2 
981   C CD1 . ILE A 132 ? 0.7831 0.5702 0.6691 0.0692  0.0269  0.0145  132 ILE A CD1 
982   N N   . PRO A 133 ? 0.8200 0.6892 0.6804 0.0161  -0.0095 0.0295  133 PRO A N   
983   C CA  . PRO A 133 ? 0.6206 0.5172 0.4871 0.0133  -0.0148 0.0444  133 PRO A CA  
984   C C   . PRO A 133 ? 0.7546 0.6602 0.6480 0.0145  -0.0120 0.0620  133 PRO A C   
985   O O   . PRO A 133 ? 0.8682 0.7921 0.7645 0.0167  -0.0119 0.0751  133 PRO A O   
986   C CB  . PRO A 133 ? 0.6697 0.5703 0.5352 0.0004  -0.0303 0.0387  133 PRO A CB  
987   C CG  . PRO A 133 ? 0.8793 0.7546 0.7331 -0.0052 -0.0330 0.0191  133 PRO A CG  
988   C CD  . PRO A 133 ? 0.8206 0.6729 0.6782 0.0035  -0.0201 0.0164  133 PRO A CD  
989   N N   . GLY A 134 ? 0.6842 0.5739 0.5937 0.0127  -0.0103 0.0623  134 GLY A N   
990   C CA  . GLY A 134 ? 0.7159 0.6099 0.6453 0.0136  -0.0085 0.0765  134 GLY A CA  
991   C C   . GLY A 134 ? 0.7064 0.5788 0.6435 0.0154  -0.0044 0.0761  134 GLY A C   
992   O O   . GLY A 134 ? 0.7613 0.6129 0.6915 0.0145  -0.0037 0.0656  134 GLY A O   
993   N N   . VAL A 135 ? 0.5288 0.4030 0.4777 0.0181  -0.0027 0.0877  135 VAL A N   
994   C CA  . VAL A 135 ? 0.6527 0.5067 0.6053 0.0203  -0.0009 0.0899  135 VAL A CA  
995   C C   . VAL A 135 ? 0.7445 0.5961 0.7040 0.0135  -0.0021 0.0971  135 VAL A C   
996   O O   . VAL A 135 ? 0.8018 0.6635 0.7673 0.0151  -0.0026 0.1057  135 VAL A O   
997   C CB  . VAL A 135 ? 0.6534 0.5102 0.6111 0.0306  0.0012  0.0954  135 VAL A CB  
998   C CG1 . VAL A 135 ? 0.6728 0.5070 0.6309 0.0337  -0.0003 0.0980  135 VAL A CG1 
999   C CG2 . VAL A 135 ? 0.6469 0.5110 0.6007 0.0389  0.0060  0.0882  135 VAL A CG2 
1000  N N   . ALA A 136 ? 0.7854 0.6224 0.7439 0.0056  -0.0013 0.0933  136 ALA A N   
1001  C CA  . ALA A 136 ? 0.6453 0.4808 0.6103 -0.0008 0.0013  0.0993  136 ALA A CA  
1002  C C   . ALA A 136 ? 0.6666 0.4796 0.6231 0.0026  0.0045  0.1054  136 ALA A C   
1003  O O   . ALA A 136 ? 0.9066 0.6962 0.8546 0.0012  0.0060  0.1035  136 ALA A O   
1004  C CB  . ALA A 136 ? 0.7544 0.5874 0.7250 -0.0128 0.0021  0.0934  136 ALA A CB  
1005  N N   . VAL A 137 ? 0.6319 0.4489 0.5882 0.0069  0.0044  0.1127  137 VAL A N   
1006  C CA  . VAL A 137 ? 0.6924 0.4878 0.6357 0.0098  0.0049  0.1181  137 VAL A CA  
1007  C C   . VAL A 137 ? 0.7284 0.5165 0.6677 0.0030  0.0130  0.1211  137 VAL A C   
1008  O O   . VAL A 137 ? 0.8318 0.6295 0.7743 0.0039  0.0154  0.1236  137 VAL A O   
1009  C CB  . VAL A 137 ? 0.6722 0.4734 0.6153 0.0169  -0.0010 0.1227  137 VAL A CB  
1010  C CG1 . VAL A 137 ? 0.4900 0.2682 0.4160 0.0195  -0.0038 0.1275  137 VAL A CG1 
1011  C CG2 . VAL A 137 ? 0.5970 0.4113 0.5492 0.0230  -0.0058 0.1208  137 VAL A CG2 
1012  N N   . ILE A 138 ? 0.6561 0.4277 0.5902 -0.0040 0.0186  0.1205  138 ILE A N   
1013  C CA  . ILE A 138 ? 0.6575 0.4243 0.5898 -0.0119 0.0300  0.1242  138 ILE A CA  
1014  C C   . ILE A 138 ? 0.7623 0.5041 0.6682 -0.0074 0.0324  0.1312  138 ILE A C   
1015  O O   . ILE A 138 ? 0.7692 0.4879 0.6588 -0.0039 0.0269  0.1339  138 ILE A O   
1016  C CB  . ILE A 138 ? 0.7269 0.4869 0.6665 -0.0242 0.0356  0.1218  138 ILE A CB  
1017  C CG1 . ILE A 138 ? 0.5472 0.3343 0.5112 -0.0297 0.0308  0.1137  138 ILE A CG1 
1018  C CG2 . ILE A 138 ? 0.7668 0.5194 0.7032 -0.0328 0.0502  0.1280  138 ILE A CG2 
1019  C CD1 . ILE A 138 ? 0.8343 0.6124 0.8054 -0.0431 0.0316  0.1085  138 ILE A CD1 
1020  N N   . LEU A 139 ? 0.7293 0.4742 0.6295 -0.0064 0.0398  0.1337  139 LEU A N   
1021  C CA  . LEU A 139 ? 0.8048 0.5241 0.6730 -0.0017 0.0403  0.1388  139 LEU A CA  
1022  C C   . LEU A 139 ? 0.8384 0.5527 0.6958 -0.0060 0.0579  0.1415  139 LEU A C   
1023  O O   . LEU A 139 ? 0.9110 0.6486 0.7894 -0.0063 0.0658  0.1380  139 LEU A O   
1024  C CB  . LEU A 139 ? 0.7393 0.4645 0.6053 0.0070  0.0283  0.1367  139 LEU A CB  
1025  C CG  . LEU A 139 ? 0.8467 0.5502 0.6810 0.0111  0.0273  0.1388  139 LEU A CG  
1026  C CD1 . LEU A 139 ? 0.7974 0.4970 0.6264 0.0171  0.0085  0.1387  139 LEU A CD1 
1027  C CD2 . LEU A 139 ? 0.9951 0.7064 0.8309 0.0122  0.0381  0.1351  139 LEU A CD2 
1028  N N   . GLY A 140 ? 0.8206 0.5058 0.6462 -0.0082 0.0645  0.1481  140 GLY A N   
1029  C CA  . GLY A 140 ? 0.9340 0.6131 0.7440 -0.0114 0.0845  0.1511  140 GLY A CA  
1030  C C   . GLY A 140 ? 1.0172 0.6903 0.8308 -0.0240 0.1008  0.1576  140 GLY A C   
1031  O O   . GLY A 140 ? 0.9491 0.6041 0.7575 -0.0287 0.0941  0.1620  140 GLY A O   
1032  N N   . GLU A 141 ? 0.9195 0.6071 0.7436 -0.0291 0.1220  0.1583  141 GLU A N   
1033  C CA  . GLU A 141 ? 0.8922 0.5775 0.7240 -0.0438 0.1403  0.1655  141 GLU A CA  
1034  C C   . GLU A 141 ? 0.9238 0.6517 0.8061 -0.0507 0.1519  0.1610  141 GLU A C   
1035  O O   . GLU A 141 ? 0.9999 0.7513 0.8962 -0.0421 0.1576  0.1557  141 GLU A O   
1036  C CB  . GLU A 141 ? 0.9785 0.6363 0.7666 -0.0445 0.1597  0.1746  141 GLU A CB  
1037  C CG  . GLU A 141 ? 1.0760 0.7194 0.8610 -0.0610 0.1774  0.1862  141 GLU A CG  
1038  C CD  . GLU A 141 ? 1.4101 1.0211 1.1425 -0.0610 0.1960  0.1972  141 GLU A CD  
1039  O OE1 . GLU A 141 ? 1.4662 1.0796 1.1769 -0.0504 0.2048  0.1929  141 GLU A OE1 
1040  O OE2 . GLU A 141 ? 1.3482 0.9286 1.0580 -0.0714 0.2018  0.2101  141 GLU A OE2 
1041  N N   . CYS A 142 ? 0.8886 0.6253 0.7987 -0.0663 0.1544  0.1630  142 CYS A N   
1042  C CA  . CYS A 142 ? 0.8900 0.6696 0.8522 -0.0754 0.1622  0.1593  142 CYS A CA  
1043  C C   . CYS A 142 ? 0.9108 0.6968 0.8788 -0.0857 0.1918  0.1675  142 CYS A C   
1044  O O   . CYS A 142 ? 0.9228 0.6740 0.8512 -0.0894 0.2044  0.1770  142 CYS A O   
1045  C CB  . CYS A 142 ? 0.8105 0.5951 0.7988 -0.0887 0.1473  0.1555  142 CYS A CB  
1046  S SG  . CYS A 142 ? 0.8671 0.6647 0.8653 -0.0770 0.1179  0.1437  142 CYS A SG  
1047  N N   . PRO A 143 ? 0.9507 0.7817 0.9680 -0.0905 0.2039  0.1653  143 PRO A N   
1048  C CA  . PRO A 143 ? 0.8634 0.7044 0.8902 -0.1008 0.2354  0.1739  143 PRO A CA  
1049  C C   . PRO A 143 ? 0.8939 0.7095 0.9131 -0.1237 0.2435  0.1843  143 PRO A C   
1050  O O   . PRO A 143 ? 0.9798 0.7768 0.9741 -0.1301 0.2686  0.1955  143 PRO A O   
1051  C CB  . PRO A 143 ? 0.6677 0.5676 0.7607 -0.1021 0.2400  0.1686  143 PRO A CB  
1052  C CG  . PRO A 143 ? 0.7748 0.6898 0.8918 -0.1005 0.2086  0.1595  143 PRO A CG  
1053  C CD  . PRO A 143 ? 0.7701 0.6461 0.8370 -0.0864 0.1901  0.1562  143 PRO A CD  
1054  N N   . ASP A 144 ? 0.8897 0.7011 0.9268 -0.1358 0.2227  0.1807  144 ASP A N   
1055  C CA  . ASP A 144 ? 0.8631 0.6451 0.8947 -0.1579 0.2266  0.1891  144 ASP A CA  
1056  C C   . ASP A 144 ? 0.9020 0.6597 0.9267 -0.1593 0.1972  0.1815  144 ASP A C   
1057  O O   . ASP A 144 ? 0.8702 0.6471 0.9081 -0.1477 0.1760  0.1693  144 ASP A O   
1058  C CB  . ASP A 144 ? 1.0172 0.8371 1.1055 -0.1813 0.2436  0.1924  144 ASP A CB  
1059  C CG  . ASP A 144 ? 1.1072 0.9848 1.2573 -0.1815 0.2302  0.1802  144 ASP A CG  
1060  O OD1 . ASP A 144 ? 1.0148 0.8926 1.1676 -0.1756 0.2017  0.1690  144 ASP A OD1 
1061  O OD2 . ASP A 144 ? 1.1975 1.1211 1.3933 -0.1871 0.2485  0.1825  144 ASP A OD2 
1062  N N   . SER A 145 ? 1.0689 0.7825 1.0712 -0.1725 0.1970  0.1889  145 SER A N   
1063  C CA  . SER A 145 ? 1.0047 0.6909 0.9990 -0.1727 0.1719  0.1808  145 SER A CA  
1064  C C   . SER A 145 ? 1.0187 0.7401 1.0630 -0.1845 0.1571  0.1666  145 SER A C   
1065  O O   . SER A 145 ? 1.1340 0.8481 1.1743 -0.1773 0.1345  0.1548  145 SER A O   
1066  C CB  . SER A 145 ? 1.0807 0.7109 1.0454 -0.1856 0.1768  0.1924  145 SER A CB  
1067  O OG  . SER A 145 ? 1.2269 0.8631 1.2255 -0.2138 0.1888  0.1962  145 SER A OG  
1068  N N   . GLU A 146 ? 1.0633 0.8239 1.1542 -0.2024 0.1696  0.1678  146 GLU A N   
1069  C CA  . GLU A 146 ? 0.8753 0.6728 1.0154 -0.2153 0.1536  0.1549  146 GLU A CA  
1070  C C   . GLU A 146 ? 0.9260 0.7572 1.0744 -0.1943 0.1344  0.1427  146 GLU A C   
1071  O O   . GLU A 146 ? 1.0917 0.9268 1.2486 -0.1962 0.1116  0.1299  146 GLU A O   
1072  C CB  . GLU A 146 ? 0.9518 0.7923 1.1456 -0.2371 0.1716  0.1604  146 GLU A CB  
1073  C CG  . GLU A 146 ? 1.2514 1.0614 1.4469 -0.2651 0.1878  0.1715  146 GLU A CG  
1074  C CD  . GLU A 146 ? 1.2579 1.0394 1.4186 -0.2641 0.2182  0.1906  146 GLU A CD  
1075  O OE1 . GLU A 146 ? 1.1924 0.9923 1.3407 -0.2450 0.2325  0.1950  146 GLU A OE1 
1076  O OE2 . GLU A 146 ? 1.2819 1.0199 1.4251 -0.2827 0.2276  0.2014  146 GLU A OE2 
1077  N N   . THR A 147 ? 0.9889 0.8409 1.1315 -0.1744 0.1435  0.1464  147 THR A N   
1078  C CA  . THR A 147 ? 0.9813 0.8615 1.1305 -0.1546 0.1263  0.1372  147 THR A CA  
1079  C C   . THR A 147 ? 0.8637 0.7078 0.9688 -0.1389 0.1091  0.1322  147 THR A C   
1080  O O   . THR A 147 ? 0.7690 0.6279 0.8796 -0.1308 0.0897  0.1225  147 THR A O   
1081  C CB  . THR A 147 ? 0.8091 0.7193 0.9678 -0.1386 0.1415  0.1420  147 THR A CB  
1082  O OG1 . THR A 147 ? 1.1187 0.9955 1.2363 -0.1318 0.1609  0.1516  147 THR A OG1 
1083  C CG2 . THR A 147 ? 0.8137 0.7759 1.0304 -0.1492 0.1534  0.1437  147 THR A CG2 
1084  N N   . ALA A 148 ? 0.8733 0.6717 0.9355 -0.1345 0.1162  0.1395  148 ALA A N   
1085  C CA  . ALA A 148 ? 0.8782 0.6458 0.9042 -0.1192 0.1007  0.1357  148 ALA A CA  
1086  C C   . ALA A 148 ? 0.8977 0.6541 0.9304 -0.1283 0.0839  0.1250  148 ALA A C   
1087  O O   . ALA A 148 ? 0.8522 0.6221 0.8873 -0.1187 0.0675  0.1147  148 ALA A O   
1088  C CB  . ALA A 148 ? 0.9797 0.7034 0.9623 -0.1134 0.1104  0.1469  148 ALA A CB  
1089  N N   . ALA A 149 ? 0.7729 0.5026 0.8067 -0.1471 0.0886  0.1270  149 ALA A N   
1090  C CA  . ALA A 149 ? 0.8713 0.5839 0.9084 -0.1566 0.0732  0.1148  149 ALA A CA  
1091  C C   . ALA A 149 ? 0.8841 0.6391 0.9532 -0.1609 0.0582  0.1010  149 ALA A C   
1092  O O   . ALA A 149 ? 0.9050 0.6529 0.9636 -0.1548 0.0417  0.0884  149 ALA A O   
1093  C CB  . ALA A 149 ? 1.1187 0.8002 1.1597 -0.1802 0.0821  0.1198  149 ALA A CB  
1094  N N   . LYS A 150 ? 0.8128 0.6127 0.9199 -0.1699 0.0641  0.1038  150 LYS A N   
1095  C CA  . LYS A 150 ? 0.7732 0.6174 0.9129 -0.1735 0.0480  0.0930  150 LYS A CA  
1096  C C   . LYS A 150 ? 0.7627 0.6166 0.8832 -0.1502 0.0339  0.0869  150 LYS A C   
1097  O O   . LYS A 150 ? 0.7765 0.6350 0.8950 -0.1508 0.0156  0.0744  150 LYS A O   
1098  C CB  . LYS A 150 ? 0.6702 0.5638 0.8552 -0.1806 0.0592  0.1004  150 LYS A CB  
1099  C CG  . LYS A 150 ? 0.8334 0.7795 1.0519 -0.1761 0.0428  0.0936  150 LYS A CG  
1100  C CD  . LYS A 150 ? 1.0157 1.0037 1.2633 -0.1653 0.0569  0.1035  150 LYS A CD  
1101  C CE  . LYS A 150 ? 0.9971 1.0039 1.2820 -0.1830 0.0781  0.1121  150 LYS A CE  
1102  N NZ  . LYS A 150 ? 1.0068 1.0555 1.3208 -0.1694 0.0927  0.1196  150 LYS A NZ  
1103  N N   . ILE A 151 ? 0.7434 0.5978 0.8474 -0.1309 0.0427  0.0957  151 ILE A N   
1104  C CA  . ILE A 151 ? 0.6784 0.5415 0.7663 -0.1104 0.0321  0.0927  151 ILE A CA  
1105  C C   . ILE A 151 ? 0.7795 0.6068 0.8333 -0.1029 0.0233  0.0858  151 ILE A C   
1106  O O   . ILE A 151 ? 0.8028 0.6391 0.8515 -0.0975 0.0093  0.0764  151 ILE A O   
1107  C CB  . ILE A 151 ? 0.6506 0.5202 0.7313 -0.0943 0.0442  0.1035  151 ILE A CB  
1108  C CG1 . ILE A 151 ? 0.5859 0.4983 0.7035 -0.0954 0.0504  0.1075  151 ILE A CG1 
1109  C CG2 . ILE A 151 ? 0.6104 0.4763 0.6685 -0.0752 0.0346  0.1020  151 ILE A CG2 
1110  C CD1 . ILE A 151 ? 0.6786 0.5901 0.7892 -0.0841 0.0678  0.1168  151 ILE A CD1 
1111  N N   . ILE A 152 ? 0.7936 0.5808 0.8231 -0.1014 0.0318  0.0908  152 ILE A N   
1112  C CA  . ILE A 152 ? 0.7213 0.4759 0.7226 -0.0913 0.0246  0.0849  152 ILE A CA  
1113  C C   . ILE A 152 ? 0.7470 0.4933 0.7498 -0.1010 0.0128  0.0695  152 ILE A C   
1114  O O   . ILE A 152 ? 0.7971 0.5449 0.7873 -0.0901 0.0032  0.0600  152 ILE A O   
1115  C CB  . ILE A 152 ? 0.6379 0.3502 0.6154 -0.0881 0.0338  0.0944  152 ILE A CB  
1116  C CG1 . ILE A 152 ? 0.6214 0.3399 0.5887 -0.0757 0.0417  0.1069  152 ILE A CG1 
1117  C CG2 . ILE A 152 ? 0.7583 0.4388 0.7135 -0.0769 0.0257  0.0875  152 ILE A CG2 
1118  C CD1 . ILE A 152 ? 0.8083 0.4908 0.7531 -0.0765 0.0519  0.1189  152 ILE A CD1 
1119  N N   . LYS A 153 ? 0.7410 0.4796 0.7592 -0.1222 0.0139  0.0666  153 LYS A N   
1120  C CA  . LYS A 153 ? 0.7756 0.5027 0.7938 -0.1340 0.0011  0.0499  153 LYS A CA  
1121  C C   . LYS A 153 ? 0.9012 0.6680 0.9289 -0.1314 -0.0137 0.0395  153 LYS A C   
1122  O O   . LYS A 153 ? 1.0786 0.8340 1.0906 -0.1311 -0.0256 0.0241  153 LYS A O   
1123  C CB  . LYS A 153 ? 0.7593 0.4749 0.7980 -0.1609 0.0042  0.0497  153 LYS A CB  
1124  C CG  . LYS A 153 ? 0.7442 0.4095 0.7660 -0.1650 0.0169  0.0590  153 LYS A CG  
1125  C CD  . LYS A 153 ? 1.0266 0.6823 1.0717 -0.1944 0.0220  0.0611  153 LYS A CD  
1126  C CE  . LYS A 153 ? 1.3304 0.9306 1.3553 -0.1998 0.0344  0.0721  153 LYS A CE  
1127  N NZ  . LYS A 153 ? 1.4124 0.9692 1.4332 -0.2174 0.0263  0.0597  153 LYS A NZ  
1128  N N   . ASP A 154 ? 0.8637 0.6743 0.9140 -0.1286 -0.0129 0.0480  154 ASP A N   
1129  C CA  . ASP A 154 ? 0.8482 0.6964 0.9067 -0.1247 -0.0277 0.0418  154 ASP A CA  
1130  C C   . ASP A 154 ? 0.8526 0.6964 0.8813 -0.1029 -0.0303 0.0402  154 ASP A C   
1131  O O   . ASP A 154 ? 0.8709 0.7203 0.8858 -0.1006 -0.0430 0.0290  154 ASP A O   
1132  C CB  . ASP A 154 ? 0.7627 0.6558 0.8559 -0.1253 -0.0247 0.0531  154 ASP A CB  
1133  C CG  . ASP A 154 ? 0.9304 0.8639 1.0387 -0.1246 -0.0426 0.0485  154 ASP A CG  
1134  O OD1 . ASP A 154 ? 0.9849 0.9118 1.0741 -0.1265 -0.0581 0.0354  154 ASP A OD1 
1135  O OD2 . ASP A 154 ? 1.0191 0.9894 1.1566 -0.1212 -0.0412 0.0579  154 ASP A OD2 
1136  N N   . TYR A 155 ? 0.7838 0.6177 0.8016 -0.0878 -0.0185 0.0514  155 TYR A N   
1137  C CA  . TYR A 155 ? 0.7060 0.5382 0.7011 -0.0689 -0.0198 0.0512  155 TYR A CA  
1138  C C   . TYR A 155 ? 0.9203 0.7211 0.8903 -0.0661 -0.0227 0.0377  155 TYR A C   
1139  O O   . TYR A 155 ? 0.9194 0.7276 0.8739 -0.0580 -0.0288 0.0298  155 TYR A O   
1140  C CB  . TYR A 155 ? 0.5427 0.3676 0.5331 -0.0560 -0.0085 0.0646  155 TYR A CB  
1141  C CG  . TYR A 155 ? 0.7516 0.6063 0.7579 -0.0512 -0.0060 0.0758  155 TYR A CG  
1142  C CD1 . TYR A 155 ? 0.6771 0.5605 0.6880 -0.0454 -0.0142 0.0762  155 TYR A CD1 
1143  C CD2 . TYR A 155 ? 0.7927 0.6429 0.8052 -0.0509 0.0051  0.0862  155 TYR A CD2 
1144  C CE1 . TYR A 155 ? 0.5964 0.5023 0.6217 -0.0394 -0.0121 0.0863  155 TYR A CE1 
1145  C CE2 . TYR A 155 ? 0.8281 0.7013 0.8530 -0.0447 0.0084  0.0944  155 TYR A CE2 
1146  C CZ  . TYR A 155 ? 0.7492 0.6494 0.7821 -0.0387 -0.0005 0.0944  155 TYR A CZ  
1147  O OH  . TYR A 155 ? 0.7804 0.6987 0.8257 -0.0313 0.0025  0.1025  155 TYR A OH  
1148  N N   . GLN A 156 ? 0.9155 0.6797 0.8804 -0.0724 -0.0175 0.0353  156 GLN A N   
1149  C CA  . GLN A 156 ? 0.8730 0.6020 0.8151 -0.0681 -0.0193 0.0216  156 GLN A CA  
1150  C C   . GLN A 156 ? 0.7732 0.5050 0.7092 -0.0789 -0.0318 0.0032  156 GLN A C   
1151  O O   . GLN A 156 ? 0.9626 0.6778 0.8747 -0.0698 -0.0341 -0.0103 156 GLN A O   
1152  C CB  . GLN A 156 ? 0.7857 0.4707 0.7233 -0.0722 -0.0120 0.0249  156 GLN A CB  
1153  C CG  . GLN A 156 ? 0.8934 0.5522 0.8343 -0.0933 -0.0162 0.0143  156 GLN A CG  
1154  C CD  . GLN A 156 ? 1.0591 0.6712 0.9932 -0.0963 -0.0078 0.0213  156 GLN A CD  
1155  O OE1 . GLN A 156 ? 0.8688 0.4552 0.7859 -0.0785 -0.0034 0.0251  156 GLN A OE1 
1156  N NE2 . GLN A 156 ? 1.2205 0.8211 1.1691 -0.1192 -0.0057 0.0245  156 GLN A NE2 
1157  N N   . SER A 157 ? 0.8421 0.5964 0.7994 -0.0976 -0.0401 0.0022  157 SER A N   
1158  C CA  . SER A 157 ? 0.9569 0.7171 0.9092 -0.1100 -0.0561 -0.0153 157 SER A CA  
1159  C C   . SER A 157 ? 0.9208 0.7056 0.8536 -0.0964 -0.0637 -0.0199 157 SER A C   
1160  O O   . SER A 157 ? 1.0361 0.8132 0.9470 -0.0999 -0.0750 -0.0374 157 SER A O   
1161  C CB  . SER A 157 ? 0.8853 0.6744 0.8725 -0.1316 -0.0647 -0.0122 157 SER A CB  
1162  O OG  . SER A 157 ? 1.4040 1.1672 1.4067 -0.1500 -0.0592 -0.0118 157 SER A OG  
1163  N N   . LYS A 158 ? 0.8514 0.6637 0.7897 -0.0818 -0.0577 -0.0044 158 LYS A N   
1164  C CA  . LYS A 158 ? 0.8310 0.6657 0.7506 -0.0693 -0.0627 -0.0049 158 LYS A CA  
1165  C C   . LYS A 158 ? 0.9558 0.7723 0.8489 -0.0500 -0.0508 -0.0067 158 LYS A C   
1166  O O   . LYS A 158 ? 0.9725 0.8078 0.8517 -0.0386 -0.0500 -0.0029 158 LYS A O   
1167  C CB  . LYS A 158 ? 0.9627 0.8367 0.9050 -0.0656 -0.0639 0.0131  158 LYS A CB  
1168  C CG  . LYS A 158 ? 0.8429 0.7441 0.8140 -0.0815 -0.0772 0.0141  158 LYS A CG  
1169  C CD  . LYS A 158 ? 0.8265 0.7463 0.8334 -0.0823 -0.0685 0.0307  158 LYS A CD  
1170  C CE  . LYS A 158 ? 0.7649 0.7233 0.8039 -0.0915 -0.0812 0.0345  158 LYS A CE  
1171  N NZ  . LYS A 158 ? 0.7926 0.7513 0.8408 -0.1119 -0.0957 0.0200  158 LYS A NZ  
1172  N N   . GLY A 159 ? 0.9100 0.6911 0.7978 -0.0466 -0.0417 -0.0116 159 GLY A N   
1173  C CA  . GLY A 159 ? 0.8743 0.6402 0.7440 -0.0275 -0.0304 -0.0138 159 GLY A CA  
1174  C C   . GLY A 159 ? 0.8817 0.6646 0.7649 -0.0144 -0.0208 0.0050  159 GLY A C   
1175  O O   . GLY A 159 ? 1.0064 0.7900 0.8801 0.0013  -0.0126 0.0054  159 GLY A O   
1176  N N   . LEU A 160 ? 0.8726 0.6695 0.7786 -0.0209 -0.0213 0.0199  160 LEU A N   
1177  C CA  . LEU A 160 ? 0.8047 0.6146 0.7215 -0.0104 -0.0143 0.0363  160 LEU A CA  
1178  C C   . LEU A 160 ? 0.9460 0.7278 0.8640 -0.0039 -0.0073 0.0398  160 LEU A C   
1179  O O   . LEU A 160 ? 0.9417 0.6950 0.8578 -0.0112 -0.0075 0.0345  160 LEU A O   
1180  C CB  . LEU A 160 ? 0.5932 0.4257 0.5304 -0.0182 -0.0168 0.0492  160 LEU A CB  
1181  C CG  . LEU A 160 ? 0.6116 0.4771 0.5516 -0.0157 -0.0217 0.0555  160 LEU A CG  
1182  C CD1 . LEU A 160 ? 0.7074 0.5852 0.6427 -0.0250 -0.0333 0.0459  160 LEU A CD1 
1183  C CD2 . LEU A 160 ? 0.5121 0.3928 0.4721 -0.0162 -0.0200 0.0700  160 LEU A CD2 
1184  N N   . LEU A 161 ? 0.8215 0.6109 0.7432 0.0091  -0.0024 0.0496  161 LEU A N   
1185  C CA  . LEU A 161 ? 0.7117 0.4782 0.6350 0.0171  0.0012  0.0552  161 LEU A CA  
1186  C C   . LEU A 161 ? 0.7751 0.5437 0.7077 0.0105  0.0009  0.0689  161 LEU A C   
1187  O O   . LEU A 161 ? 0.8831 0.6743 0.8232 0.0127  0.0006  0.0778  161 LEU A O   
1188  C CB  . LEU A 161 ? 0.7419 0.5183 0.6675 0.0341  0.0049  0.0579  161 LEU A CB  
1189  C CG  . LEU A 161 ? 0.7888 0.5487 0.7198 0.0438  0.0048  0.0665  161 LEU A CG  
1190  C CD1 . LEU A 161 ? 0.7561 0.4763 0.6777 0.0451  0.0048  0.0605  161 LEU A CD1 
1191  C CD2 . LEU A 161 ? 0.5818 0.3604 0.5231 0.0592  0.0074  0.0692  161 LEU A CD2 
1192  N N   . THR A 162 ? 0.8347 0.5778 0.7649 0.0022  0.0021  0.0705  162 THR A N   
1193  C CA  . THR A 162 ? 0.7772 0.5195 0.7115 -0.0040 0.0048  0.0826  162 THR A CA  
1194  C C   . THR A 162 ? 0.8348 0.5551 0.7599 0.0061  0.0052  0.0916  162 THR A C   
1195  O O   . THR A 162 ? 0.8965 0.5893 0.8132 0.0115  0.0045  0.0889  162 THR A O   
1196  C CB  . THR A 162 ? 0.8144 0.5441 0.7520 -0.0210 0.0077  0.0809  162 THR A CB  
1197  O OG1 . THR A 162 ? 0.9581 0.7032 0.9031 -0.0298 0.0032  0.0694  162 THR A OG1 
1198  C CG2 . THR A 162 ? 0.7426 0.4820 0.6873 -0.0280 0.0137  0.0919  162 THR A CG2 
1199  N N   . CYS A 163 ? 0.7613 0.4917 0.6866 0.0092  0.0050  0.1018  163 CYS A N   
1200  C CA  . CYS A 163 ? 0.7530 0.4648 0.6673 0.0180  0.0021  0.1109  163 CYS A CA  
1201  C C   . CYS A 163 ? 0.6809 0.3832 0.5847 0.0098  0.0069  0.1196  163 CYS A C   
1202  O O   . CYS A 163 ? 0.8455 0.5686 0.7558 0.0054  0.0099  0.1207  163 CYS A O   
1203  C CB  . CYS A 163 ? 0.6415 0.3744 0.5637 0.0294  -0.0042 0.1132  163 CYS A CB  
1204  S SG  . CYS A 163 ? 0.8827 0.6296 0.8173 0.0409  -0.0054 0.1039  163 CYS A SG  
1205  N N   . LEU A 164 ? 0.6679 0.3377 0.5541 0.0086  0.0087  0.1263  164 LEU A N   
1206  C CA  . LEU A 164 ? 0.7407 0.3989 0.6121 0.0004  0.0166  0.1349  164 LEU A CA  
1207  C C   . LEU A 164 ? 0.9097 0.5516 0.7576 0.0091  0.0109  0.1446  164 LEU A C   
1208  O O   . LEU A 164 ? 0.9172 0.5406 0.7558 0.0190  0.0014  0.1483  164 LEU A O   
1209  C CB  . LEU A 164 ? 0.7561 0.3873 0.6209 -0.0116 0.0253  0.1373  164 LEU A CB  
1210  C CG  . LEU A 164 ? 0.7842 0.4235 0.6693 -0.0218 0.0273  0.1265  164 LEU A CG  
1211  C CD1 . LEU A 164 ? 0.8749 0.4813 0.7526 -0.0349 0.0345  0.1301  164 LEU A CD1 
1212  C CD2 . LEU A 164 ? 0.7370 0.4147 0.6442 -0.0298 0.0312  0.1212  164 LEU A CD2 
1213  N N   . VAL A 165 ? 0.7717 0.4213 0.6104 0.0062  0.0158  0.1478  165 VAL A N   
1214  C CA  . VAL A 165 ? 0.9582 0.5886 0.7671 0.0123  0.0099  0.1560  165 VAL A CA  
1215  C C   . VAL A 165 ? 0.9708 0.5904 0.7587 0.0037  0.0253  0.1608  165 VAL A C   
1216  O O   . VAL A 165 ? 1.0341 0.6761 0.8393 -0.0026 0.0366  0.1557  165 VAL A O   
1217  C CB  . VAL A 165 ? 0.8076 0.4564 0.6216 0.0207  -0.0030 0.1531  165 VAL A CB  
1218  C CG1 . VAL A 165 ? 0.8697 0.5503 0.7079 0.0173  0.0020  0.1455  165 VAL A CG1 
1219  C CG2 . VAL A 165 ? 0.9596 0.5879 0.7389 0.0234  -0.0081 0.1592  165 VAL A CG2 
1220  N N   . GLY A 166 ? 0.9106 0.4977 0.6621 0.0046  0.0261  0.1708  166 GLY A N   
1221  C CA  . GLY A 166 ? 1.0681 0.6413 0.7924 -0.0025 0.0430  0.1765  166 GLY A CA  
1222  C C   . GLY A 166 ? 1.0716 0.6270 0.7921 -0.0147 0.0599  0.1841  166 GLY A C   
1223  O O   . GLY A 166 ? 1.0990 0.6384 0.8255 -0.0164 0.0550  0.1872  166 GLY A O   
1224  N N   . LYS A 167 ? 1.0745 0.6318 0.7858 -0.0234 0.0811  0.1871  167 LYS A N   
1225  C CA  . LYS A 167 ? 0.9653 0.5088 0.6760 -0.0381 0.1004  0.1957  167 LYS A CA  
1226  C C   . LYS A 167 ? 1.0641 0.6302 0.8224 -0.0490 0.1024  0.1885  167 LYS A C   
1227  O O   . LYS A 167 ? 1.0958 0.6463 0.8580 -0.0626 0.1127  0.1949  167 LYS A O   
1228  C CB  . LYS A 167 ? 1.1262 0.6743 0.8217 -0.0442 0.1252  0.1995  167 LYS A CB  
1229  C CG  . LYS A 167 ? 1.2610 0.7868 0.9047 -0.0355 0.1238  0.2043  167 LYS A CG  
1230  C CD  . LYS A 167 ? 1.1426 0.6427 0.7604 -0.0386 0.1201  0.2149  167 LYS A CD  
1231  C CE  . LYS A 167 ? 1.3946 0.8777 0.9633 -0.0367 0.1316  0.2208  167 LYS A CE  
1232  N NZ  . LYS A 167 ? 1.4261 0.8842 0.9706 -0.0410 0.1310  0.2335  167 LYS A NZ  
1233  N N   . VAL A 168 ? 1.0872 0.6880 0.8797 -0.0441 0.0923  0.1757  168 VAL A N   
1234  C CA  . VAL A 168 ? 0.8657 0.4878 0.6985 -0.0536 0.0909  0.1675  168 VAL A CA  
1235  C C   . VAL A 168 ? 0.9540 0.5461 0.7822 -0.0553 0.0804  0.1684  168 VAL A C   
1236  O O   . VAL A 168 ? 1.0173 0.6132 0.8692 -0.0675 0.0819  0.1633  168 VAL A O   
1237  C CB  . VAL A 168 ? 0.7779 0.4396 0.6400 -0.0460 0.0807  0.1554  168 VAL A CB  
1238  C CG1 . VAL A 168 ? 1.0608 0.7168 0.9134 -0.0313 0.0615  0.1518  168 VAL A CG1 
1239  C CG2 . VAL A 168 ? 0.7481 0.4355 0.6488 -0.0572 0.0804  0.1471  168 VAL A CG2 
1240  N N   . ILE A 169 ? 1.0471 0.6086 0.8455 -0.0429 0.0689  0.1743  169 ILE A N   
1241  C CA  . ILE A 169 ? 1.0436 0.5732 0.8368 -0.0408 0.0595  0.1756  169 ILE A CA  
1242  C C   . ILE A 169 ? 1.0958 0.5925 0.8778 -0.0574 0.0738  0.1862  169 ILE A C   
1243  O O   . ILE A 169 ? 1.0949 0.5794 0.8929 -0.0673 0.0735  0.1816  169 ILE A O   
1244  C CB  . ILE A 169 ? 0.9661 0.4740 0.7331 -0.0219 0.0436  0.1816  169 ILE A CB  
1245  C CG1 . ILE A 169 ? 0.8967 0.4376 0.6821 -0.0080 0.0295  0.1709  169 ILE A CG1 
1246  C CG2 . ILE A 169 ? 1.2147 0.6943 0.9803 -0.0181 0.0355  0.1835  169 ILE A CG2 
1247  C CD1 . ILE A 169 ? 1.0211 0.5530 0.7860 0.0079  0.0148  0.1771  169 ILE A CD1 
1248  N N   . ASP A 170 ? 1.0879 0.5817 0.8486 -0.0604 0.0838  0.1969  170 ASP A N   
1249  C CA  . ASP A 170 ? 1.1006 0.5770 0.8561 -0.0759 0.0970  0.2068  170 ASP A CA  
1250  C C   . ASP A 170 ? 1.1805 0.6715 0.9687 -0.0979 0.1134  0.2031  170 ASP A C   
1251  O O   . ASP A 170 ? 1.2517 0.7262 1.0507 -0.1129 0.1171  0.2056  170 ASP A O   
1252  C CB  . ASP A 170 ? 1.1311 0.6054 0.8543 -0.0741 0.1073  0.2180  170 ASP A CB  
1253  C CG  . ASP A 170 ? 1.4229 0.8789 1.1131 -0.0561 0.0902  0.2234  170 ASP A CG  
1254  O OD1 . ASP A 170 ? 1.3672 0.8084 1.0622 -0.0468 0.0730  0.2220  170 ASP A OD1 
1255  O OD2 . ASP A 170 ? 1.4947 0.9507 1.1541 -0.0511 0.0942  0.2285  170 ASP A OD2 
1256  N N   . GLN A 171 ? 1.0834 0.6089 0.8918 -0.0997 0.1215  0.1965  171 GLN A N   
1257  C CA  . GLN A 171 ? 1.0738 0.6332 0.9264 -0.1180 0.1315  0.1896  171 GLN A CA  
1258  C C   . GLN A 171 ? 1.1710 0.7313 1.0506 -0.1238 0.1157  0.1763  171 GLN A C   
1259  O O   . GLN A 171 ? 1.2494 0.8117 1.1541 -0.1445 0.1217  0.1747  171 GLN A O   
1260  C CB  . GLN A 171 ? 0.9746 0.5844 0.8498 -0.1116 0.1360  0.1821  171 GLN A CB  
1261  C CG  . GLN A 171 ? 0.8897 0.5021 0.7459 -0.1116 0.1583  0.1929  171 GLN A CG  
1262  C CD  . GLN A 171 ? 0.9566 0.6159 0.8383 -0.1041 0.1634  0.1845  171 GLN A CD  
1263  O OE1 . GLN A 171 ? 1.0345 0.7142 0.9288 -0.0916 0.1465  0.1736  171 GLN A OE1 
1264  N NE2 . GLN A 171 ? 0.9884 0.6651 0.8784 -0.1109 0.1881  0.1901  171 GLN A NE2 
1265  N N   . ALA A 172 ? 1.1229 0.6820 0.9973 -0.1064 0.0962  0.1664  172 ALA A N   
1266  C CA  . ALA A 172 ? 1.0039 0.5605 0.8964 -0.1093 0.0821  0.1521  172 ALA A CA  
1267  C C   . ALA A 172 ? 1.1739 0.6784 1.0524 -0.1198 0.0833  0.1573  172 ALA A C   
1268  O O   . ALA A 172 ? 1.2408 0.7403 1.1391 -0.1355 0.0805  0.1480  172 ALA A O   
1269  C CB  . ALA A 172 ? 0.8618 0.4246 0.7469 -0.0869 0.0653  0.1431  172 ALA A CB  
1270  N N   . ILE A 173 ? 1.1750 0.6382 1.0175 -0.1117 0.0862  0.1725  173 ILE A N   
1271  C CA  . ILE A 173 ? 1.2091 0.6275 1.0399 -0.1178 0.0850  0.1789  173 ILE A CA  
1272  C C   . ILE A 173 ? 1.2878 0.7090 1.1364 -0.1456 0.1011  0.1855  173 ILE A C   
1273  O O   . ILE A 173 ? 1.2286 0.6302 1.0923 -0.1615 0.0990  0.1798  173 ILE A O   
1274  C CB  . ILE A 173 ? 1.0939 0.4953 0.8942 -0.0981 0.0787  0.1918  173 ILE A CB  
1275  C CG1 . ILE A 173 ? 1.0201 0.4199 0.8120 -0.0721 0.0608  0.1845  173 ILE A CG1 
1276  C CG2 . ILE A 173 ? 1.1082 0.4729 0.9013 -0.1054 0.0795  0.2013  173 ILE A CG2 
1277  C CD1 . ILE A 173 ? 1.3722 0.7747 1.1398 -0.0532 0.0538  0.1954  173 ILE A CD1 
1278  N N   A GLU A 174 ? 1.2369 0.6829 1.0843 -0.1514 0.1174  0.1965  174 GLU A N   
1279  N N   B GLU A 174 ? 1.2132 0.6591 1.0606 -0.1514 0.1175  0.1966  174 GLU A N   
1280  C CA  A GLU A 174 ? 1.2314 0.6882 1.0988 -0.1768 0.1357  0.2045  174 GLU A CA  
1281  C CA  B GLU A 174 ? 1.2257 0.6816 1.0930 -0.1770 0.1355  0.2046  174 GLU A CA  
1282  C C   A GLU A 174 ? 1.3068 0.7828 1.2182 -0.1996 0.1371  0.1914  174 GLU A C   
1283  C C   B GLU A 174 ? 1.3002 0.7771 1.2119 -0.1998 0.1376  0.1917  174 GLU A C   
1284  O O   A GLU A 174 ? 1.3827 0.8519 1.3146 -0.2225 0.1417  0.1936  174 GLU A O   
1285  O O   B GLU A 174 ? 1.3822 0.8545 1.3154 -0.2232 0.1432  0.1942  174 GLU A O   
1286  C CB  A GLU A 174 ? 1.2171 0.7044 1.0774 -0.1749 0.1545  0.2144  174 GLU A CB  
1287  C CB  B GLU A 174 ? 1.2172 0.6998 1.0744 -0.1752 0.1545  0.2160  174 GLU A CB  
1288  C CG  A GLU A 174 ? 1.2659 0.7705 1.1486 -0.1994 0.1766  0.2236  174 GLU A CG  
1289  C CG  B GLU A 174 ? 1.2900 0.7474 1.1025 -0.1611 0.1542  0.2303  174 GLU A CG  
1290  C CD  A GLU A 174 ? 1.3246 0.8587 1.1998 -0.1959 0.1983  0.2315  174 GLU A CD  
1291  C CD  B GLU A 174 ? 1.2252 0.7027 1.0143 -0.1490 0.1651  0.2350  174 GLU A CD  
1292  O OE1 A GLU A 174 ? 1.4088 0.9382 1.2487 -0.1742 0.1952  0.2329  174 GLU A OE1 
1293  O OE1 B GLU A 174 ? 1.3755 0.8848 1.1836 -0.1592 0.1851  0.2351  174 GLU A OE1 
1294  O OE2 A GLU A 174 ? 1.2841 0.8468 1.1901 -0.2148 0.2184  0.2355  174 GLU A OE2 
1295  O OE2 B GLU A 174 ? 1.0554 0.5171 0.8087 -0.1290 0.1534  0.2379  174 GLU A OE2 
1296  N N   . GLY A 175 ? 1.2162 0.7271 1.1464 -0.1907 0.1275  0.1763  175 GLY A N   
1297  C CA  . GLY A 175 ? 1.1812 0.7292 1.1571 -0.2062 0.1196  0.1601  175 GLY A CA  
1298  C C   . GLY A 175 ? 1.1826 0.7026 1.1586 -0.2091 0.1000  0.1442  175 GLY A C   
1299  O O   . GLY A 175 ? 1.2016 0.7515 1.2079 -0.2177 0.0881  0.1278  175 GLY A O   
1300  N N   . LYS A 176 ? 1.2208 0.6820 1.1612 -0.2008 0.0959  0.1487  176 LYS A N   
1301  C CA  . LYS A 176 ? 1.1738 0.5978 1.1079 -0.2003 0.0797  0.1336  176 LYS A CA  
1302  C C   . LYS A 176 ? 1.0415 0.4935 0.9803 -0.1816 0.0617  0.1127  176 LYS A C   
1303  O O   . LYS A 176 ? 1.0419 0.5019 0.9984 -0.1925 0.0506  0.0945  176 LYS A O   
1304  C CB  . LYS A 176 ? 1.1862 0.5948 1.1451 -0.2332 0.0811  0.1283  176 LYS A CB  
1305  C CG  . LYS A 176 ? 1.3197 0.7085 1.2797 -0.2504 0.0975  0.1492  176 LYS A CG  
1306  C CD  . LYS A 176 ? 1.4700 0.8092 1.3980 -0.2333 0.0930  0.1591  176 LYS A CD  
1307  C CE  . LYS A 176 ? 1.6853 0.9899 1.6255 -0.2533 0.0910  0.1596  176 LYS A CE  
1308  N NZ  . LYS A 176 ? 1.6484 0.9068 1.5594 -0.2358 0.0882  0.1717  176 LYS A NZ  
1309  N N   . VAL A 177 ? 1.0770 0.5420 0.9981 -0.1545 0.0585  0.1155  177 VAL A N   
1310  C CA  . VAL A 177 ? 1.1421 0.6329 1.0653 -0.1361 0.0442  0.0987  177 VAL A CA  
1311  C C   . VAL A 177 ? 1.2417 0.6872 1.1390 -0.1174 0.0360  0.0933  177 VAL A C   
1312  O O   . VAL A 177 ? 1.2738 0.6859 1.1487 -0.1059 0.0396  0.1075  177 VAL A O   
1313  C CB  . VAL A 177 ? 1.0298 0.5665 0.9556 -0.1197 0.0459  0.1045  177 VAL A CB  
1314  C CG1 . VAL A 177 ? 0.9206 0.4736 0.8413 -0.0981 0.0333  0.0921  177 VAL A CG1 
1315  C CG2 . VAL A 177 ? 1.0276 0.6132 0.9841 -0.1347 0.0519  0.1052  177 VAL A CG2 
1316  N N   . LYS A 178 ? 1.3786 0.8227 1.2781 -0.1132 0.0249  0.0727  178 LYS A N   
1317  C CA  . LYS A 178 ? 1.4039 0.8083 1.2824 -0.0930 0.0188  0.0648  178 LYS A CA  
1318  C C   . LYS A 178 ? 1.3032 0.7360 1.1763 -0.0653 0.0163  0.0679  178 LYS A C   
1319  O O   . LYS A 178 ? 1.2415 0.7162 1.1245 -0.0600 0.0120  0.0573  178 LYS A O   
1320  C CB  . LYS A 178 ? 1.6441 1.0379 1.5239 -0.0985 0.0098  0.0396  178 LYS A CB  
1321  C CG  . LYS A 178 ? 1.6649 1.0294 1.5524 -0.1285 0.0093  0.0338  178 LYS A CG  
1322  C CD  . LYS A 178 ? 1.5755 0.9213 1.4567 -0.1316 -0.0018 0.0065  178 LYS A CD  
1323  C CE  . LYS A 178 ? 1.8428 1.1538 1.7316 -0.1628 -0.0046 -0.0006 178 LYS A CE  
1324  N NZ  . LYS A 178 ? 1.8009 1.0959 1.6806 -0.1675 -0.0176 -0.0301 178 LYS A NZ  
1325  N N   . MET A 179 ? 1.2469 0.6576 1.1048 -0.0485 0.0179  0.0831  179 MET A N   
1326  C CA  . MET A 179 ? 1.2087 0.6471 1.0652 -0.0244 0.0141  0.0870  179 MET A CA  
1327  C C   . MET A 179 ? 1.2218 0.6377 1.0709 0.0004  0.0083  0.0802  179 MET A C   
1328  O O   . MET A 179 ? 1.4344 0.8006 1.2707 0.0055  0.0075  0.0835  179 MET A O   
1329  C CB  . MET A 179 ? 0.9685 0.4098 0.8158 -0.0224 0.0176  0.1086  179 MET A CB  
1330  C CG  . MET A 179 ? 1.0889 0.5583 0.9455 -0.0426 0.0260  0.1145  179 MET A CG  
1331  S SD  . MET A 179 ? 1.2539 0.7384 1.0971 -0.0353 0.0297  0.1338  179 MET A SD  
1332  C CE  . MET A 179 ? 1.4341 0.8574 1.2465 -0.0354 0.0327  0.1520  179 MET A CE  
1333  N N   . GLY A 180 ? 1.0666 0.5197 0.9251 0.0162  0.0053  0.0719  180 GLY A N   
1334  C CA  . GLY A 180 ? 1.0896 0.5334 0.9476 0.0415  0.0022  0.0647  180 GLY A CA  
1335  C C   . GLY A 180 ? 1.0561 0.5479 0.9267 0.0512  0.0027  0.0533  180 GLY A C   
1336  O O   . GLY A 180 ? 1.0620 0.5871 0.9384 0.0372  0.0038  0.0488  180 GLY A O   
1337  N N   . LEU A 181 ? 1.1524 0.6489 1.0286 0.0754  0.0023  0.0495  181 LEU A N   
1338  C CA  . LEU A 181 ? 0.9417 0.4832 0.8295 0.0850  0.0054  0.0404  181 LEU A CA  
1339  C C   . LEU A 181 ? 1.1236 0.6630 1.0017 0.0774  0.0094  0.0189  181 LEU A C   
1340  O O   . LEU A 181 ? 1.0827 0.6600 0.9634 0.0712  0.0110  0.0139  181 LEU A O   
1341  C CB  . LEU A 181 ? 0.9745 0.5214 0.8745 0.1128  0.0058  0.0419  181 LEU A CB  
1342  C CG  . LEU A 181 ? 0.9830 0.5843 0.9014 0.1221  0.0094  0.0417  181 LEU A CG  
1343  C CD1 . LEU A 181 ? 1.2947 0.9096 1.2333 0.1418  0.0048  0.0544  181 LEU A CD1 
1344  C CD2 . LEU A 181 ? 1.2107 0.8210 1.1256 0.1303  0.0195  0.0216  181 LEU A CD2 
1345  N N   . ASP A 182 ? 1.3394 0.8319 1.2038 0.0778  0.0100  0.0060  182 ASP A N   
1346  C CA  . ASP A 182 ? 1.3484 0.8322 1.1984 0.0692  0.0115  -0.0169 182 ASP A CA  
1347  C C   . ASP A 182 ? 1.2553 0.7522 1.1047 0.0397  0.0062  -0.0164 182 ASP A C   
1348  O O   . ASP A 182 ? 1.3280 0.8449 1.1706 0.0314  0.0046  -0.0302 182 ASP A O   
1349  C CB  . ASP A 182 ? 1.5162 0.9392 1.3508 0.0751  0.0122  -0.0314 182 ASP A CB  
1350  C CG  . ASP A 182 ? 1.5402 0.9544 1.3732 0.1056  0.0194  -0.0428 182 ASP A CG  
1351  O OD1 . ASP A 182 ? 1.5392 0.9964 1.3776 0.1176  0.0257  -0.0474 182 ASP A OD1 
1352  O OD2 . ASP A 182 ? 1.5962 0.9600 1.4232 0.1180  0.0198  -0.0465 182 ASP A OD2 
1353  N N   . LEU A 183 ? 1.2360 0.7233 1.0923 0.0248  0.0038  0.0003  183 LEU A N   
1354  C CA  . LEU A 183 ? 1.0501 0.5535 0.9130 -0.0020 0.0005  0.0032  183 LEU A CA  
1355  C C   . LEU A 183 ? 1.0765 0.6356 0.9535 -0.0035 0.0006  0.0146  183 LEU A C   
1356  O O   . LEU A 183 ? 1.0635 0.6418 0.9504 -0.0223 -0.0013 0.0189  183 LEU A O   
1357  C CB  . LEU A 183 ? 1.0646 0.5330 0.9285 -0.0165 0.0017  0.0167  183 LEU A CB  
1358  C CG  . LEU A 183 ? 1.0336 0.4403 0.8840 -0.0190 0.0012  0.0077  183 LEU A CG  
1359  C CD1 . LEU A 183 ? 1.1330 0.5030 0.9795 -0.0203 0.0044  0.0282  183 LEU A CD1 
1360  C CD2 . LEU A 183 ? 1.0771 0.4728 0.9274 -0.0448 -0.0035 -0.0087 183 LEU A CD2 
1361  N N   . ARG A 184 ? 0.9462 0.5304 0.8263 0.0163  0.0030  0.0195  184 ARG A N   
1362  C CA  . ARG A 184 ? 0.8846 0.5162 0.7765 0.0171  0.0030  0.0295  184 ARG A CA  
1363  C C   . ARG A 184 ? 0.9008 0.5412 0.8021 0.0065  0.0031  0.0471  184 ARG A C   
1364  O O   . ARG A 184 ? 0.9657 0.6400 0.8764 -0.0004 0.0023  0.0515  184 ARG A O   
1365  C CB  . ARG A 184 ? 1.0344 0.6953 0.9245 0.0092  0.0003  0.0179  184 ARG A CB  
1366  C CG  . ARG A 184 ? 1.0737 0.7268 0.9479 0.0199  0.0018  -0.0008 184 ARG A CG  
1367  C CD  . ARG A 184 ? 1.2304 0.9073 1.1072 0.0408  0.0086  0.0026  184 ARG A CD  
1368  N NE  . ARG A 184 ? 1.4828 1.1456 1.3440 0.0548  0.0144  -0.0150 184 ARG A NE  
1369  C CZ  . ARG A 184 ? 1.6390 1.3124 1.4819 0.0534  0.0153  -0.0298 184 ARG A CZ  
1370  N NH1 . ARG A 184 ? 1.3597 1.0590 1.1995 0.0383  0.0085  -0.0279 184 ARG A NH1 
1371  N NH2 . ARG A 184 ? 1.6886 1.3459 1.5144 0.0681  0.0231  -0.0467 184 ARG A NH2 
1372  N N   . VAL A 185 ? 0.8611 0.4688 0.7573 0.0063  0.0045  0.0568  185 VAL A N   
1373  C CA  . VAL A 185 ? 0.9960 0.6079 0.8947 -0.0021 0.0069  0.0736  185 VAL A CA  
1374  C C   . VAL A 185 ? 1.0441 0.6348 0.9333 0.0132  0.0055  0.0859  185 VAL A C   
1375  O O   . VAL A 185 ? 0.9556 0.5048 0.8334 0.0146  0.0056  0.0883  185 VAL A O   
1376  C CB  . VAL A 185 ? 0.8805 0.4734 0.7795 -0.0238 0.0108  0.0751  185 VAL A CB  
1377  C CG1 . VAL A 185 ? 0.9211 0.5175 0.8194 -0.0306 0.0170  0.0920  185 VAL A CG1 
1378  C CG2 . VAL A 185 ? 0.9095 0.5256 0.8213 -0.0391 0.0085  0.0623  185 VAL A CG2 
1379  N N   . ILE A 186 ? 0.8939 0.5103 0.7877 0.0238  0.0027  0.0937  186 ILE A N   
1380  C CA  . ILE A 186 ? 0.7550 0.3556 0.6417 0.0395  -0.0027 0.1047  186 ILE A CA  
1381  C C   . ILE A 186 ? 0.8180 0.4181 0.6940 0.0338  -0.0032 0.1195  186 ILE A C   
1382  O O   . ILE A 186 ? 0.9971 0.6287 0.8803 0.0310  -0.0031 0.1208  186 ILE A O   
1383  C CB  . ILE A 186 ? 0.6524 0.2810 0.5539 0.0570  -0.0073 0.1010  186 ILE A CB  
1384  C CG1 . ILE A 186 ? 1.0136 0.6398 0.9207 0.0651  -0.0041 0.0856  186 ILE A CG1 
1385  C CG2 . ILE A 186 ? 0.9114 0.5317 0.8113 0.0719  -0.0160 0.1129  186 ILE A CG2 
1386  C CD1 . ILE A 186 ? 0.8937 0.5585 0.8172 0.0767  -0.0031 0.0805  186 ILE A CD1 
1387  N N   . PRO A 187 ? 0.8119 0.3747 0.6678 0.0324  -0.0032 0.1307  187 PRO A N   
1388  C CA  . PRO A 187 ? 0.7632 0.3223 0.6015 0.0291  -0.0032 0.1443  187 PRO A CA  
1389  C C   . PRO A 187 ? 0.8415 0.4067 0.6769 0.0464  -0.0167 0.1507  187 PRO A C   
1390  O O   . PRO A 187 ? 0.9103 0.4524 0.7406 0.0592  -0.0247 0.1551  187 PRO A O   
1391  C CB  . PRO A 187 ? 0.7690 0.2825 0.5845 0.0213  0.0023  0.1542  187 PRO A CB  
1392  C CG  . PRO A 187 ? 0.9129 0.3994 0.7325 0.0305  -0.0022 0.1487  187 PRO A CG  
1393  C CD  . PRO A 187 ? 0.9421 0.4613 0.7877 0.0338  -0.0026 0.1310  187 PRO A CD  
1394  N N   . LEU A 188 ? 0.7879 0.3834 0.6285 0.0464  -0.0201 0.1510  188 LEU A N   
1395  C CA  . LEU A 188 ? 0.6743 0.2803 0.5176 0.0601  -0.0349 0.1556  188 LEU A CA  
1396  C C   . LEU A 188 ? 0.8396 0.4195 0.6514 0.0622  -0.0433 0.1688  188 LEU A C   
1397  O O   . LEU A 188 ? 1.0193 0.5893 0.8280 0.0757  -0.0579 0.1754  188 LEU A O   
1398  C CB  . LEU A 188 ? 0.7894 0.4363 0.6528 0.0584  -0.0366 0.1497  188 LEU A CB  
1399  C CG  . LEU A 188 ? 0.7809 0.4556 0.6710 0.0568  -0.0291 0.1382  188 LEU A CG  
1400  C CD1 . LEU A 188 ? 0.6914 0.3973 0.5925 0.0503  -0.0274 0.1356  188 LEU A CD1 
1401  C CD2 . LEU A 188 ? 0.9298 0.6143 0.8400 0.0718  -0.0343 0.1343  188 LEU A CD2 
1402  N N   . GLY A 189 ? 0.9603 0.5303 0.7484 0.0500  -0.0343 0.1728  189 GLY A N   
1403  C CA  . GLY A 189 ? 0.8756 0.4290 0.6330 0.0500  -0.0392 0.1822  189 GLY A CA  
1404  C C   . GLY A 189 ? 0.9385 0.4878 0.6738 0.0365  -0.0241 0.1833  189 GLY A C   
1405  O O   . GLY A 189 ? 0.8659 0.4264 0.6117 0.0283  -0.0118 0.1779  189 GLY A O   
1406  N N   . TYR A 190 ? 1.1500 0.6828 0.8534 0.0352  -0.0244 0.1908  190 TYR A N   
1407  C CA  . TYR A 190 ? 1.1034 0.6299 0.7815 0.0244  -0.0079 0.1922  190 TYR A CA  
1408  C C   . TYR A 190 ? 1.1166 0.6521 0.7800 0.0269  -0.0138 0.1876  190 TYR A C   
1409  O O   . TYR A 190 ? 0.9935 0.5307 0.6474 0.0201  0.0019  0.1848  190 TYR A O   
1410  C CB  . TYR A 190 ? 0.9817 0.4818 0.6268 0.0213  -0.0025 0.2028  190 TYR A CB  
1411  C CG  . TYR A 190 ? 0.8946 0.3814 0.5526 0.0147  0.0073  0.2075  190 TYR A CG  
1412  C CD1 . TYR A 190 ? 1.0176 0.5071 0.6884 0.0004  0.0279  0.2056  190 TYR A CD1 
1413  C CD2 . TYR A 190 ? 0.8935 0.3637 0.5523 0.0227  -0.0046 0.2138  190 TYR A CD2 
1414  C CE1 . TYR A 190 ? 1.0309 0.5054 0.7136 -0.0080 0.0354  0.2092  190 TYR A CE1 
1415  C CE2 . TYR A 190 ? 1.0674 0.5198 0.7362 0.0162  0.0038  0.2175  190 TYR A CE2 
1416  C CZ  . TYR A 190 ? 1.1673 0.6210 0.8474 -0.0002 0.0233  0.2148  190 TYR A CZ  
1417  O OH  . TYR A 190 ? 1.1855 0.6191 0.8756 -0.0086 0.0300  0.2179  190 TYR A OH  
1418  N N   . ASP A 191 ? 1.0656 0.6059 0.7280 0.0368  -0.0365 0.1869  191 ASP A N   
1419  C CA  . ASP A 191 ? 1.0110 0.5554 0.6589 0.0380  -0.0460 0.1819  191 ASP A CA  
1420  C C   . ASP A 191 ? 0.9876 0.5589 0.6706 0.0356  -0.0421 0.1727  191 ASP A C   
1421  O O   . ASP A 191 ? 1.0216 0.6132 0.7427 0.0364  -0.0403 0.1700  191 ASP A O   
1422  C CB  . ASP A 191 ? 1.1981 0.7436 0.8425 0.0474  -0.0740 0.1839  191 ASP A CB  
1423  C CG  . ASP A 191 ? 1.4804 1.0021 1.0858 0.0505  -0.0820 0.1920  191 ASP A CG  
1424  O OD1 . ASP A 191 ? 1.6101 1.1143 1.1956 0.0460  -0.0650 0.1977  191 ASP A OD1 
1425  O OD2 . ASP A 191 ? 1.5963 1.1172 1.1914 0.0569  -0.1060 0.1931  191 ASP A OD2 
1426  N N   . VAL A 192 ? 1.1257 0.7036 0.8008 0.0327  -0.0403 0.1653  192 VAL A N   
1427  C CA  . VAL A 192 ? 1.0150 0.6246 0.7286 0.0302  -0.0368 0.1556  192 VAL A CA  
1428  C C   . VAL A 192 ? 0.9633 0.5947 0.7087 0.0348  -0.0569 0.1542  192 VAL A C   
1429  O O   . VAL A 192 ? 1.0041 0.6626 0.7874 0.0340  -0.0531 0.1504  192 VAL A O   
1430  C CB  . VAL A 192 ? 0.8720 0.4774 0.5676 0.0276  -0.0307 0.1481  192 VAL A CB  
1431  C CG1 . VAL A 192 ? 0.9622 0.5967 0.6969 0.0259  -0.0279 0.1404  192 VAL A CG1 
1432  C CG2 . VAL A 192 ? 1.2388 0.8266 0.9056 0.0243  -0.0075 0.1496  192 VAL A CG2 
1433  N N   . THR A 193 ? 0.9442 0.5652 0.6744 0.0395  -0.0782 0.1579  193 THR A N   
1434  C CA  . THR A 193 ? 0.8012 0.4462 0.5655 0.0437  -0.0974 0.1576  193 THR A CA  
1435  C C   . THR A 193 ? 0.9377 0.6006 0.7373 0.0495  -0.0931 0.1601  193 THR A C   
1436  O O   . THR A 193 ? 0.9766 0.6687 0.8137 0.0517  -0.0995 0.1577  193 THR A O   
1437  C CB  . THR A 193 ? 0.9772 0.6076 0.7186 0.0483  -0.1226 0.1624  193 THR A CB  
1438  O OG1 . THR A 193 ? 1.1643 0.7639 0.8698 0.0534  -0.1216 0.1716  193 THR A OG1 
1439  C CG2 . THR A 193 ? 1.1131 0.7313 0.8264 0.0419  -0.1317 0.1560  193 THR A CG2 
1440  N N   . SER A 194 ? 0.9290 0.5746 0.7171 0.0510  -0.0805 0.1639  194 SER A N   
1441  C CA  . SER A 194 ? 0.8851 0.5416 0.7025 0.0575  -0.0776 0.1642  194 SER A CA  
1442  C C   . SER A 194 ? 0.8773 0.5631 0.7271 0.0525  -0.0643 0.1556  194 SER A C   
1443  O O   . SER A 194 ? 0.8888 0.5871 0.7628 0.0579  -0.0617 0.1531  194 SER A O   
1444  C CB  . SER A 194 ? 0.8184 0.4435 0.6146 0.0595  -0.0702 0.1704  194 SER A CB  
1445  O OG  . SER A 194 ? 1.0386 0.6445 0.8071 0.0491  -0.0543 0.1715  194 SER A OG  
1446  N N   . VAL A 195 ? 0.8655 0.5604 0.7138 0.0439  -0.0567 0.1512  195 VAL A N   
1447  C CA  . VAL A 195 ? 0.7576 0.4799 0.6341 0.0401  -0.0470 0.1451  195 VAL A CA  
1448  C C   . VAL A 195 ? 0.9048 0.6543 0.8119 0.0450  -0.0570 0.1445  195 VAL A C   
1449  O O   . VAL A 195 ? 0.8256 0.5956 0.7554 0.0460  -0.0499 0.1411  195 VAL A O   
1450  C CB  . VAL A 195 ? 0.6873 0.4124 0.5571 0.0323  -0.0388 0.1420  195 VAL A CB  
1451  C CG1 . VAL A 195 ? 0.7743 0.5027 0.6429 0.0315  -0.0509 0.1415  195 VAL A CG1 
1452  C CG2 . VAL A 195 ? 0.6398 0.3878 0.5332 0.0288  -0.0277 0.1377  195 VAL A CG2 
1453  N N   . ILE A 196 ? 0.8211 0.5719 0.7289 0.0476  -0.0734 0.1478  196 ILE A N   
1454  C CA  . ILE A 196 ? 0.7700 0.5503 0.7120 0.0508  -0.0823 0.1484  196 ILE A CA  
1455  C C   . ILE A 196 ? 0.8618 0.6557 0.8265 0.0611  -0.0777 0.1480  196 ILE A C   
1456  O O   . ILE A 196 ? 0.8312 0.6551 0.8270 0.0630  -0.0756 0.1470  196 ILE A O   
1457  C CB  . ILE A 196 ? 0.6786 0.4572 0.6188 0.0514  -0.1041 0.1522  196 ILE A CB  
1458  C CG1 . ILE A 196 ? 0.6864 0.4994 0.6653 0.0476  -0.1111 0.1524  196 ILE A CG1 
1459  C CG2 . ILE A 196 ? 0.9052 0.6718 0.8391 0.0630  -0.1163 0.1576  196 ILE A CG2 
1460  C CD1 . ILE A 196 ? 0.9402 0.7584 0.9212 0.0358  -0.1042 0.1495  196 ILE A CD1 
1461  N N   . HIS A 197 ? 0.8564 0.6266 0.8046 0.0676  -0.0744 0.1486  197 HIS A N   
1462  C CA  . HIS A 197 ? 0.8159 0.5915 0.7815 0.0790  -0.0697 0.1463  197 HIS A CA  
1463  C C   . HIS A 197 ? 0.8074 0.5989 0.7848 0.0758  -0.0530 0.1382  197 HIS A C   
1464  O O   . HIS A 197 ? 0.9639 0.7671 0.9591 0.0853  -0.0481 0.1341  197 HIS A O   
1465  C CB  . HIS A 197 ? 0.8152 0.5542 0.7569 0.0857  -0.0718 0.1497  197 HIS A CB  
1466  C CG  . HIS A 197 ? 0.9307 0.6559 0.8604 0.0919  -0.0907 0.1589  197 HIS A CG  
1467  N ND1 . HIS A 197 ? 0.8879 0.6383 0.8453 0.1005  -0.1062 0.1620  197 HIS A ND1 
1468  C CD2 . HIS A 197 ? 0.8913 0.5817 0.7839 0.0901  -0.0967 0.1660  197 HIS A CD2 
1469  C CE1 . HIS A 197 ? 0.7575 0.4873 0.6932 0.1041  -0.1238 0.1702  197 HIS A CE1 
1470  N NE2 . HIS A 197 ? 0.8611 0.5529 0.7544 0.0983  -0.1182 0.1732  197 HIS A NE2 
1471  N N   . VAL A 198 ? 0.6907 0.4833 0.6581 0.0637  -0.0450 0.1358  198 VAL A N   
1472  C CA  . VAL A 198 ? 0.6804 0.4908 0.6576 0.0605  -0.0324 0.1291  198 VAL A CA  
1473  C C   . VAL A 198 ? 0.8041 0.6451 0.8009 0.0569  -0.0329 0.1316  198 VAL A C   
1474  O O   . VAL A 198 ? 0.8581 0.7200 0.8680 0.0586  -0.0245 0.1284  198 VAL A O   
1475  C CB  . VAL A 198 ? 0.7581 0.5545 0.7174 0.0506  -0.0241 0.1256  198 VAL A CB  
1476  C CG1 . VAL A 198 ? 0.8074 0.6093 0.7624 0.0415  -0.0243 0.1289  198 VAL A CG1 
1477  C CG2 . VAL A 198 ? 0.7676 0.5739 0.7316 0.0498  -0.0149 0.1173  198 VAL A CG2 
1478  N N   . VAL A 199 ? 0.7634 0.6043 0.7595 0.0516  -0.0420 0.1370  199 VAL A N   
1479  C CA  . VAL A 199 ? 0.6048 0.4702 0.6206 0.0464  -0.0437 0.1405  199 VAL A CA  
1480  C C   . VAL A 199 ? 0.7056 0.5975 0.7512 0.0540  -0.0448 0.1422  199 VAL A C   
1481  O O   . VAL A 199 ? 0.7180 0.6350 0.7815 0.0515  -0.0368 0.1437  199 VAL A O   
1482  C CB  . VAL A 199 ? 0.7275 0.5813 0.7347 0.0393  -0.0557 0.1441  199 VAL A CB  
1483  C CG1 . VAL A 199 ? 0.5985 0.4750 0.6304 0.0330  -0.0607 0.1484  199 VAL A CG1 
1484  C CG2 . VAL A 199 ? 0.4663 0.2996 0.4485 0.0332  -0.0501 0.1418  199 VAL A CG2 
1485  N N   . THR A 200 ? 0.6452 0.5321 0.6964 0.0641  -0.0534 0.1429  200 THR A N   
1486  C CA  . THR A 200 ? 0.6806 0.5959 0.7655 0.0741  -0.0535 0.1443  200 THR A CA  
1487  C C   . THR A 200 ? 0.7484 0.6743 0.8379 0.0818  -0.0355 0.1377  200 THR A C   
1488  O O   . THR A 200 ? 0.8243 0.7808 0.9422 0.0874  -0.0285 0.1385  200 THR A O   
1489  C CB  . THR A 200 ? 0.7066 0.6138 0.7976 0.0856  -0.0687 0.1472  200 THR A CB  
1490  O OG1 . THR A 200 ? 0.9669 0.8428 1.0335 0.0945  -0.0655 0.1435  200 THR A OG1 
1491  C CG2 . THR A 200 ? 0.8919 0.7895 0.9750 0.0779  -0.0886 0.1528  200 THR A CG2 
1492  N N   . ILE A 201 ? 0.6934 0.5951 0.7554 0.0815  -0.0275 0.1309  201 ILE A N   
1493  C CA  . ILE A 201 ? 0.6992 0.6067 0.7590 0.0874  -0.0122 0.1223  201 ILE A CA  
1494  C C   . ILE A 201 ? 0.7133 0.6477 0.7797 0.0789  -0.0026 0.1244  201 ILE A C   
1495  O O   . ILE A 201 ? 0.6708 0.6275 0.7497 0.0851  0.0093  0.1220  201 ILE A O   
1496  C CB  . ILE A 201 ? 0.7254 0.6004 0.7546 0.0847  -0.0089 0.1143  201 ILE A CB  
1497  C CG1 . ILE A 201 ? 0.8507 0.6941 0.8704 0.0927  -0.0164 0.1138  201 ILE A CG1 
1498  C CG2 . ILE A 201 ? 0.4927 0.3731 0.5146 0.0875  0.0048  0.1036  201 ILE A CG2 
1499  C CD1 . ILE A 201 ? 0.6607 0.4707 0.6528 0.0855  -0.0137 0.1083  201 ILE A CD1 
1500  N N   . ALA A 202 ? 0.6401 0.5707 0.6965 0.0656  -0.0067 0.1295  202 ALA A N   
1501  C CA  . ALA A 202 ? 0.7071 0.6577 0.7669 0.0573  0.0006  0.1341  202 ALA A CA  
1502  C C   . ALA A 202 ? 0.7156 0.6957 0.8069 0.0564  0.0011  0.1425  202 ALA A C   
1503  O O   . ALA A 202 ? 0.7497 0.7529 0.8497 0.0563  0.0138  0.1449  202 ALA A O   
1504  C CB  . ALA A 202 ? 0.4282 0.3645 0.4728 0.0458  -0.0054 0.1379  202 ALA A CB  
1505  N N   . ILE A 203 ? 0.5569 0.5370 0.6651 0.0550  -0.0125 0.1472  203 ILE A N   
1506  C CA  . ILE A 203 ? 0.5895 0.6001 0.7335 0.0516  -0.0143 0.1553  203 ILE A CA  
1507  C C   . ILE A 203 ? 0.6734 0.7117 0.8428 0.0649  -0.0028 0.1531  203 ILE A C   
1508  O O   . ILE A 203 ? 0.7469 0.8166 0.9402 0.0619  0.0087  0.1587  203 ILE A O   
1509  C CB  . ILE A 203 ? 0.5165 0.5200 0.6711 0.0466  -0.0352 0.1592  203 ILE A CB  
1510  C CG1 . ILE A 203 ? 0.4965 0.4784 0.6309 0.0320  -0.0425 0.1618  203 ILE A CG1 
1511  C CG2 . ILE A 203 ? 0.5313 0.5710 0.7312 0.0452  -0.0394 0.1659  203 ILE A CG2 
1512  C CD1 . ILE A 203 ? 0.8258 0.7839 0.9476 0.0295  -0.0616 0.1605  203 ILE A CD1 
1513  N N   . ARG A 204 ? 0.6451 0.6711 0.8098 0.0800  -0.0044 0.1454  204 ARG A N   
1514  C CA  . ARG A 204 ? 0.6011 0.6503 0.7898 0.0962  0.0075  0.1415  204 ARG A CA  
1515  C C   . ARG A 204 ? 0.7109 0.7683 0.8849 0.0988  0.0303  0.1356  204 ARG A C   
1516  O O   . ARG A 204 ? 0.6297 0.7172 0.8276 0.1078  0.0454  0.1351  204 ARG A O   
1517  C CB  . ARG A 204 ? 0.6289 0.6560 0.8137 0.1130  -0.0009 0.1352  204 ARG A CB  
1518  C CG  . ARG A 204 ? 0.5783 0.6127 0.7899 0.1161  -0.0218 0.1427  204 ARG A CG  
1519  C CD  . ARG A 204 ? 0.5985 0.6062 0.8014 0.1332  -0.0311 0.1390  204 ARG A CD  
1520  N NE  . ARG A 204 ? 0.7411 0.7035 0.9007 0.1261  -0.0408 0.1378  204 ARG A NE  
1521  C CZ  . ARG A 204 ? 0.7883 0.7163 0.9280 0.1370  -0.0463 0.1352  204 ARG A CZ  
1522  N NH1 . ARG A 204 ? 0.7376 0.6681 0.8958 0.1574  -0.0446 0.1328  204 ARG A NH1 
1523  N NH2 . ARG A 204 ? 0.7993 0.6894 0.9011 0.1279  -0.0523 0.1356  204 ARG A NH2 
1524  N N   . ALA A 205 ? 0.5911 0.6245 0.7268 0.0909  0.0329  0.1313  205 ALA A N   
1525  C CA  . ALA A 205 ? 0.6168 0.6564 0.7326 0.0919  0.0512  0.1258  205 ALA A CA  
1526  C C   . ALA A 205 ? 0.7971 0.8711 0.9314 0.0831  0.0624  0.1377  205 ALA A C   
1527  O O   . ALA A 205 ? 0.8042 0.8979 0.9377 0.0888  0.0817  0.1358  205 ALA A O   
1528  C CB  . ALA A 205 ? 0.5452 0.5561 0.6216 0.0830  0.0468  0.1212  205 ALA A CB  
1529  N N   . ALA A 206 ? 0.6770 0.7554 0.8259 0.0689  0.0510  0.1499  206 ALA A N   
1530  C CA  . ALA A 206 ? 0.5554 0.6617 0.7246 0.0574  0.0594  0.1633  206 ALA A CA  
1531  C C   . ALA A 206 ? 0.6161 0.7613 0.8313 0.0642  0.0686  0.1669  206 ALA A C   
1532  O O   . ALA A 206 ? 0.6543 0.8282 0.8825 0.0613  0.0873  0.1739  206 ALA A O   
1533  C CB  . ALA A 206 ? 0.5766 0.6711 0.7504 0.0411  0.0423  0.1730  206 ALA A CB  
1534  N N   . LEU A 207 ? 0.6015 0.7490 0.8421 0.0736  0.0558  0.1631  207 LEU A N   
1535  C CA  . LEU A 207 ? 0.5159 0.7040 0.8073 0.0818  0.0617  0.1666  207 LEU A CA  
1536  C C   . LEU A 207 ? 0.6097 0.8127 0.9026 0.1024  0.0846  0.1568  207 LEU A C   
1537  O O   . LEU A 207 ? 0.6722 0.9166 1.0016 0.1064  0.1020  0.1616  207 LEU A O   
1538  C CB  . LEU A 207 ? 0.5151 0.6990 0.8307 0.0869  0.0369  0.1662  207 LEU A CB  
1539  C CG  . LEU A 207 ? 0.5412 0.7116 0.8576 0.0683  0.0131  0.1738  207 LEU A CG  
1540  C CD1 . LEU A 207 ? 0.5432 0.6985 0.8649 0.0762  -0.0117 0.1709  207 LEU A CD1 
1541  C CD2 . LEU A 207 ? 0.6363 0.8435 0.9952 0.0517  0.0142  0.1865  207 LEU A CD2 
1542  N N   . ILE A 208 ? 0.6087 0.7780 0.8634 0.1151  0.0855  0.1427  208 ILE A N   
1543  C CA  . ILE A 208 ? 0.7309 0.9059 0.9816 0.1359  0.1061  0.1302  208 ILE A CA  
1544  C C   . ILE A 208 ? 0.7837 0.9621 1.0005 0.1325  0.1300  0.1270  208 ILE A C   
1545  O O   . ILE A 208 ? 0.7916 1.0038 1.0266 0.1395  0.1535  0.1282  208 ILE A O   
1546  C CB  . ILE A 208 ? 0.6548 0.7879 0.8808 0.1508  0.0950  0.1159  208 ILE A CB  
1547  C CG1 . ILE A 208 ? 0.6471 0.7795 0.9063 0.1579  0.0731  0.1206  208 ILE A CG1 
1548  C CG2 . ILE A 208 ? 0.6564 0.7866 0.8702 0.1719  0.1167  0.1001  208 ILE A CG2 
1549  C CD1 . ILE A 208 ? 0.5065 0.5894 0.7343 0.1625  0.0558  0.1134  208 ILE A CD1 
1550  N N   . PHE A 209 ? 0.8129 0.9578 0.9806 0.1223  0.1242  0.1232  209 PHE A N   
1551  C CA  . PHE A 209 ? 0.6899 0.8336 0.8184 0.1193  0.1422  0.1200  209 PHE A CA  
1552  C C   . PHE A 209 ? 0.6751 0.8424 0.8097 0.1016  0.1488  0.1385  209 PHE A C   
1553  O O   . PHE A 209 ? 0.7859 0.9735 0.9108 0.1026  0.1717  0.1414  209 PHE A O   
1554  C CB  . PHE A 209 ? 0.7664 0.8673 0.8442 0.1157  0.1304  0.1087  209 PHE A CB  
1555  C CG  . PHE A 209 ? 0.8411 0.9128 0.9137 0.1295  0.1216  0.0926  209 PHE A CG  
1556  C CD1 . PHE A 209 ? 0.8068 0.8743 0.8711 0.1484  0.1369  0.0765  209 PHE A CD1 
1557  C CD2 . PHE A 209 ? 0.8177 0.8649 0.8946 0.1244  0.0992  0.0943  209 PHE A CD2 
1558  C CE1 . PHE A 209 ? 0.6758 0.7118 0.7360 0.1611  0.1286  0.0628  209 PHE A CE1 
1559  C CE2 . PHE A 209 ? 0.8973 0.9154 0.9692 0.1363  0.0919  0.0822  209 PHE A CE2 
1560  C CZ  . PHE A 209 ? 0.9491 0.9606 1.0136 0.1544  0.1059  0.0669  209 PHE A CZ  
1561  N N   . GLY A 210 ? 0.6926 0.8546 0.8408 0.0857  0.1299  0.1508  210 GLY A N   
1562  C CA  . GLY A 210 ? 0.6942 0.8721 0.8497 0.0677  0.1336  0.1694  210 GLY A CA  
1563  C C   . GLY A 210 ? 0.5741 0.7962 0.7798 0.0651  0.1482  0.1813  210 GLY A C   
1564  O O   . GLY A 210 ? 0.6268 0.8647 0.8383 0.0504  0.1577  0.1972  210 GLY A O   
1565  N N   . GLY A 211 ? 0.6166 0.8592 0.8613 0.0790  0.1493  0.1747  211 GLY A N   
1566  C CA  . GLY A 211 ? 0.6179 0.9091 0.9198 0.0781  0.1624  0.1849  211 GLY A CA  
1567  C C   . GLY A 211 ? 0.6018 0.9056 0.9394 0.0556  0.1475  0.2021  211 GLY A C   
1568  O O   . GLY A 211 ? 0.6269 0.9711 1.0064 0.0468  0.1615  0.2150  211 GLY A O   
1569  N N   . ILE A 212 ? 0.4787 0.7480 0.8006 0.0457  0.1200  0.2020  212 ILE A N   
1570  C CA  . ILE A 212 ? 0.5524 0.8258 0.9026 0.0243  0.1035  0.2154  212 ILE A CA  
1571  C C   . ILE A 212 ? 0.7043 0.9998 1.1063 0.0286  0.0862  0.2134  212 ILE A C   
1572  O O   . ILE A 212 ? 0.7446 1.0342 1.1458 0.0479  0.0795  0.2012  212 ILE A O   
1573  C CB  . ILE A 212 ? 0.4429 0.6690 0.7511 0.0128  0.0838  0.2156  212 ILE A CB  
1574  C CG1 . ILE A 212 ? 0.5207 0.7276 0.7789 0.0119  0.0987  0.2173  212 ILE A CG1 
1575  C CG2 . ILE A 212 ? 0.5659 0.7922 0.9001 -0.0095 0.0687  0.2282  212 ILE A CG2 
1576  C CD1 . ILE A 212 ? 0.5621 0.7258 0.7804 0.0063  0.0816  0.2153  212 ILE A CD1 
1577  N N   . LYS A 213 ? 0.6118 0.9322 1.0592 0.0104  0.0780  0.2258  213 LYS A N   
1578  C CA  . LYS A 213 ? 0.5507 0.8961 1.0506 0.0122  0.0580  0.2252  213 LYS A CA  
1579  C C   . LYS A 213 ? 0.5447 0.8550 1.0315 -0.0012 0.0243  0.2240  213 LYS A C   
1580  O O   . LYS A 213 ? 0.5891 0.8676 1.0439 -0.0172 0.0203  0.2280  213 LYS A O   
1581  C CB  . LYS A 213 ? 0.4285 0.8316 0.9954 0.0002  0.0703  0.2386  213 LYS A CB  
1582  C CG  . LYS A 213 ? 0.6310 1.0698 1.2077 0.0094  0.1094  0.2424  213 LYS A CG  
1583  C CD  . LYS A 213 ? 0.8033 1.2595 1.3891 0.0408  0.1209  0.2291  213 LYS A CD  
1584  C CE  . LYS A 213 ? 0.8121 1.2859 1.3819 0.0527  0.1606  0.2278  213 LYS A CE  
1585  N NZ  . LYS A 213 ? 1.1009 1.5335 1.6093 0.0742  0.1652  0.2105  213 LYS A NZ  
1586  N N   . GLY A 214 ? 0.5669 0.8824 1.0771 0.0065  0.0005  0.2188  214 GLY A N   
1587  C CA  . GLY A 214 ? 0.4553 0.7378 0.9502 -0.0043 -0.0322 0.2162  214 GLY A CA  
1588  C C   . GLY A 214 ? 0.5368 0.8211 1.0492 -0.0328 -0.0408 0.2259  214 GLY A C   
1589  O O   . GLY A 214 ? 0.5805 0.9063 1.1404 -0.0447 -0.0284 0.2366  214 GLY A O   
1590  N N   . GLY A 215 ? 0.5772 0.8155 1.0514 -0.0440 -0.0601 0.2222  215 GLY A N   
1591  C CA  . GLY A 215 ? 0.7112 0.9402 1.1953 -0.0708 -0.0698 0.2295  215 GLY A CA  
1592  C C   . GLY A 215 ? 0.5574 0.7630 1.0097 -0.0802 -0.0493 0.2362  215 GLY A C   
1593  O O   . GLY A 215 ? 0.8022 0.9789 1.2423 -0.0987 -0.0591 0.2394  215 GLY A O   
1594  N N   . GLN A 216 ? 0.5411 0.7564 0.9775 -0.0669 -0.0217 0.2383  216 GLN A N   
1595  C CA  . GLN A 216 ? 0.6842 0.8779 1.0867 -0.0734 -0.0036 0.2458  216 GLN A CA  
1596  C C   . GLN A 216 ? 0.7195 0.8636 1.0639 -0.0634 -0.0121 0.2351  216 GLN A C   
1597  O O   . GLN A 216 ? 0.6794 0.8152 0.9911 -0.0501 0.0028  0.2320  216 GLN A O   
1598  C CB  . GLN A 216 ? 0.6523 0.8777 1.0585 -0.0639 0.0282  0.2519  216 GLN A CB  
1599  C CG  . GLN A 216 ? 0.6880 0.9701 1.1553 -0.0691 0.0416  0.2610  216 GLN A CG  
1600  C CD  . GLN A 216 ? 0.7944 1.0865 1.2999 -0.0972 0.0345  0.2749  216 GLN A CD  
1601  O OE1 . GLN A 216 ? 1.0288 1.3349 1.5746 -0.1065 0.0125  0.2730  216 GLN A OE1 
1602  N NE2 . GLN A 216 ? 0.7857 1.0690 1.2784 -0.1122 0.0513  0.2894  216 GLN A NE2 
1603  N N   . LEU A 217 ? 0.5662 0.6781 0.8983 -0.0703 -0.0363 0.2290  217 LEU A N   
1604  C CA  . LEU A 217 ? 0.6086 0.6759 0.8907 -0.0615 -0.0443 0.2189  217 LEU A CA  
1605  C C   . LEU A 217 ? 0.7533 0.7990 1.0022 -0.0618 -0.0294 0.2241  217 LEU A C   
1606  O O   . LEU A 217 ? 0.8191 0.8510 1.0354 -0.0478 -0.0234 0.2175  217 LEU A O   
1607  C CB  . LEU A 217 ? 0.6130 0.6495 0.8875 -0.0715 -0.0699 0.2127  217 LEU A CB  
1608  C CG  . LEU A 217 ? 0.6144 0.6086 0.8410 -0.0611 -0.0783 0.2009  217 LEU A CG  
1609  C CD1 . LEU A 217 ? 0.7222 0.7232 0.9366 -0.0417 -0.0758 0.1929  217 LEU A CD1 
1610  C CD2 . LEU A 217 ? 0.8977 0.8635 1.1158 -0.0710 -0.1023 0.1941  217 LEU A CD2 
1611  N N   . ASN A 218 ? 0.6521 0.6946 0.9101 -0.0779 -0.0244 0.2369  218 ASN A N   
1612  C CA  . ASN A 218 ? 0.8049 0.8261 1.0314 -0.0773 -0.0125 0.2442  218 ASN A CA  
1613  C C   . ASN A 218 ? 0.8235 0.8675 1.0379 -0.0644 0.0086  0.2466  218 ASN A C   
1614  O O   . ASN A 218 ? 0.9113 0.9369 1.0903 -0.0552 0.0128  0.2445  218 ASN A O   
1615  C CB  . ASN A 218 ? 0.7662 0.7779 1.0059 -0.0972 -0.0111 0.2597  218 ASN A CB  
1616  C CG  . ASN A 218 ? 1.1194 1.0974 1.3606 -0.1092 -0.0329 0.2544  218 ASN A CG  
1617  O OD1 . ASN A 218 ? 1.0868 1.0408 1.3070 -0.1006 -0.0474 0.2396  218 ASN A OD1 
1618  N ND2 . ASN A 218 ? 1.2117 1.1850 1.4758 -0.1301 -0.0353 0.2660  218 ASN A ND2 
1619  N N   . ASP A 219 ? 0.6724 0.7568 0.9160 -0.0631 0.0214  0.2497  219 ASP A N   
1620  C CA  . ASP A 219 ? 0.7390 0.8434 0.9679 -0.0502 0.0425  0.2496  219 ASP A CA  
1621  C C   . ASP A 219 ? 0.7418 0.8366 0.9473 -0.0310 0.0377  0.2320  219 ASP A C   
1622  O O   . ASP A 219 ? 0.8333 0.9226 1.0072 -0.0211 0.0478  0.2284  219 ASP A O   
1623  C CB  . ASP A 219 ? 0.8588 1.0098 1.1277 -0.0527 0.0599  0.2568  219 ASP A CB  
1624  C CG  . ASP A 219 ? 1.0022 1.1652 1.2955 -0.0738 0.0686  0.2765  219 ASP A CG  
1625  O OD1 . ASP A 219 ? 1.0736 1.2074 1.3631 -0.0883 0.0546  0.2826  219 ASP A OD1 
1626  O OD2 . ASP A 219 ? 0.9960 1.1963 1.3120 -0.0759 0.0906  0.2857  219 ASP A OD2 
1627  N N   . ILE A 220 ? 0.7619 0.8527 0.9812 -0.0268 0.0213  0.2216  220 ILE A N   
1628  C CA  . ILE A 220 ? 0.6199 0.6975 0.8181 -0.0104 0.0160  0.2066  220 ILE A CA  
1629  C C   . ILE A 220 ? 0.7229 0.7627 0.8816 -0.0100 0.0084  0.2022  220 ILE A C   
1630  O O   . ILE A 220 ? 0.7849 0.8163 0.9172 0.0002  0.0141  0.1949  220 ILE A O   
1631  C CB  . ILE A 220 ? 0.4881 0.5707 0.7108 -0.0065 -0.0004 0.1999  220 ILE A CB  
1632  C CG1 . ILE A 220 ? 0.5849 0.7100 0.8475 0.0007  0.0099  0.2014  220 ILE A CG1 
1633  C CG2 . ILE A 220 ? 0.6523 0.7067 0.8453 0.0060  -0.0101 0.1871  220 ILE A CG2 
1634  C CD1 . ILE A 220 ? 0.5303 0.6755 0.8364 -0.0045 -0.0064 0.2039  220 ILE A CD1 
1635  N N   . LEU A 221 ? 0.6899 0.7075 0.8461 -0.0210 -0.0040 0.2062  221 LEU A N   
1636  C CA  . LEU A 221 ? 0.5849 0.5694 0.7088 -0.0193 -0.0097 0.2025  221 LEU A CA  
1637  C C   . LEU A 221 ? 0.7410 0.7257 0.8446 -0.0173 0.0028  0.2089  221 LEU A C   
1638  O O   . LEU A 221 ? 0.6805 0.6480 0.7593 -0.0110 0.0008  0.2037  221 LEU A O   
1639  C CB  . LEU A 221 ? 0.5887 0.5487 0.7145 -0.0305 -0.0232 0.2052  221 LEU A CB  
1640  C CG  . LEU A 221 ? 0.5398 0.4914 0.6746 -0.0326 -0.0400 0.1970  221 LEU A CG  
1641  C CD1 . LEU A 221 ? 0.7857 0.7134 0.9224 -0.0460 -0.0522 0.1994  221 LEU A CD1 
1642  C CD2 . LEU A 221 ? 0.5374 0.4709 0.6467 -0.0207 -0.0448 0.1848  221 LEU A CD2 
1643  N N   . LYS A 222 ? 0.6624 0.6680 0.7767 -0.0230 0.0153  0.2210  222 LYS A N   
1644  C CA  . LYS A 222 ? 0.6004 0.6075 0.6917 -0.0212 0.0267  0.2291  222 LYS A CA  
1645  C C   . LYS A 222 ? 0.7065 0.7271 0.7813 -0.0084 0.0357  0.2185  222 LYS A C   
1646  O O   . LYS A 222 ? 0.7868 0.7987 0.8333 -0.0031 0.0365  0.2166  222 LYS A O   
1647  C CB  . LYS A 222 ? 0.4777 0.5015 0.5838 -0.0326 0.0387  0.2467  222 LYS A CB  
1648  C CG  . LYS A 222 ? 0.8049 0.8269 0.8819 -0.0315 0.0494  0.2582  222 LYS A CG  
1649  C CD  . LYS A 222 ? 0.9292 0.9600 1.0180 -0.0454 0.0609  0.2792  222 LYS A CD  
1650  C CE  . LYS A 222 ? 0.8209 0.8620 0.8805 -0.0425 0.0775  0.2903  222 LYS A CE  
1651  N NZ  . LYS A 222 ? 0.8825 0.8971 0.9059 -0.0378 0.0686  0.2957  222 LYS A NZ  
1652  N N   . TYR A 223 ? 0.6826 0.7237 0.7757 -0.0030 0.0415  0.2112  223 TYR A N   
1653  C CA  . TYR A 223 ? 0.6138 0.6630 0.6914 0.0099  0.0503  0.1991  223 TYR A CA  
1654  C C   . TYR A 223 ? 0.6742 0.6989 0.7316 0.0164  0.0382  0.1858  223 TYR A C   
1655  O O   . TYR A 223 ? 0.7214 0.7405 0.7524 0.0215  0.0411  0.1795  223 TYR A O   
1656  C CB  . TYR A 223 ? 0.5396 0.6132 0.6460 0.0164  0.0577  0.1940  223 TYR A CB  
1657  C CG  . TYR A 223 ? 0.4793 0.5579 0.5694 0.0309  0.0687  0.1806  223 TYR A CG  
1658  C CD1 . TYR A 223 ? 0.6394 0.6988 0.7188 0.0403  0.0596  0.1658  223 TYR A CD1 
1659  C CD2 . TYR A 223 ? 0.5930 0.6932 0.6770 0.0351  0.0892  0.1825  223 TYR A CD2 
1660  C CE1 . TYR A 223 ? 0.7005 0.7591 0.7645 0.0531  0.0689  0.1523  223 TYR A CE1 
1661  C CE2 . TYR A 223 ? 0.7215 0.8220 0.7871 0.0492  0.0995  0.1677  223 TYR A CE2 
1662  C CZ  . TYR A 223 ? 0.7138 0.7924 0.7705 0.0580  0.0885  0.1521  223 TYR A CZ  
1663  O OH  . TYR A 223 ? 0.8224 0.8961 0.8605 0.0714  0.0979  0.1364  223 TYR A OH  
1664  N N   . THR A 224 ? 0.6702 0.6802 0.7387 0.0153  0.0247  0.1815  224 THR A N   
1665  C CA  . THR A 224 ? 0.5684 0.5555 0.6187 0.0202  0.0158  0.1705  224 THR A CA  
1666  C C   . THR A 224 ? 0.6401 0.6140 0.6694 0.0170  0.0129  0.1734  224 THR A C   
1667  O O   . THR A 224 ? 0.7282 0.6962 0.7395 0.0213  0.0127  0.1654  224 THR A O   
1668  C CB  . THR A 224 ? 0.5840 0.5567 0.6452 0.0191  0.0031  0.1674  224 THR A CB  
1669  O OG1 . THR A 224 ? 0.5463 0.5131 0.6166 0.0093  -0.0038 0.1763  224 THR A OG1 
1670  C CG2 . THR A 224 ? 0.6287 0.6140 0.7101 0.0254  0.0026  0.1637  224 THR A CG2 
1671  N N   . ALA A 225 ? 0.6936 0.6629 0.7272 0.0096  0.0098  0.1849  225 ALA A N   
1672  C CA  . ALA A 225 ? 0.5833 0.5406 0.6012 0.0088  0.0061  0.1894  225 ALA A CA  
1673  C C   . ALA A 225 ? 0.5884 0.5570 0.5872 0.0118  0.0123  0.1920  225 ALA A C   
1674  O O   . ALA A 225 ? 0.8756 0.8378 0.8606 0.0145  0.0068  0.1899  225 ALA A O   
1675  C CB  . ALA A 225 ? 0.5991 0.5463 0.6258 0.0012  0.0025  0.2021  225 ALA A CB  
1676  N N   . GLU A 226 ? 0.5920 0.5787 0.5898 0.0113  0.0236  0.1964  226 GLU A N   
1677  C CA  . GLU A 226 ? 0.6013 0.5969 0.5736 0.0141  0.0298  0.1988  226 GLU A CA  
1678  C C   . GLU A 226 ? 0.6211 0.6245 0.5794 0.0214  0.0359  0.1832  226 GLU A C   
1679  O O   . GLU A 226 ? 0.7345 0.7396 0.6658 0.0238  0.0363  0.1806  226 GLU A O   
1680  C CB  . GLU A 226 ? 0.6232 0.6316 0.5958 0.0087  0.0415  0.2154  226 GLU A CB  
1681  C CG  . GLU A 226 ? 0.8991 0.8955 0.8823 0.0003  0.0362  0.2323  226 GLU A CG  
1682  C CD  . GLU A 226 ? 1.0669 1.0739 1.0498 -0.0073 0.0490  0.2511  226 GLU A CD  
1683  O OE1 . GLU A 226 ? 0.9166 0.9454 0.9016 -0.0069 0.0644  0.2503  226 GLU A OE1 
1684  O OE2 . GLU A 226 ? 1.0718 1.0644 1.0526 -0.0134 0.0449  0.2671  226 GLU A OE2 
1685  N N   . ARG A 227 ? 0.6062 0.6128 0.5809 0.0253  0.0398  0.1730  227 ARG A N   
1686  C CA  . ARG A 227 ? 0.5868 0.5966 0.5488 0.0337  0.0469  0.1577  227 ARG A CA  
1687  C C   . ARG A 227 ? 0.7041 0.6974 0.6687 0.0380  0.0389  0.1423  227 ARG A C   
1688  O O   . ARG A 227 ? 0.6960 0.6845 0.6438 0.0437  0.0421  0.1287  227 ARG A O   
1689  C CB  . ARG A 227 ? 0.6052 0.6357 0.5825 0.0380  0.0632  0.1595  227 ARG A CB  
1690  C CG  . ARG A 227 ? 0.7008 0.7494 0.6794 0.0318  0.0748  0.1769  227 ARG A CG  
1691  C CD  . ARG A 227 ? 0.9967 1.0476 0.9361 0.0332  0.0828  0.1783  227 ARG A CD  
1692  N NE  . ARG A 227 ? 1.1530 1.2073 1.0735 0.0439  0.0936  0.1612  227 ARG A NE  
1693  C CZ  . ARG A 227 ? 1.4004 1.4740 1.3292 0.0507  0.1136  0.1591  227 ARG A CZ  
1694  N NH1 . ARG A 227 ? 1.2018 1.2975 1.1616 0.0458  0.1247  0.1744  227 ARG A NH1 
1695  N NH2 . ARG A 227 ? 1.5162 1.5874 1.4241 0.0622  0.1231  0.1411  227 ARG A NH2 
1696  N N   . VAL A 228 ? 0.6350 0.6169 0.6172 0.0352  0.0292  0.1440  228 VAL A N   
1697  C CA  . VAL A 228 ? 0.5523 0.5162 0.5342 0.0384  0.0228  0.1320  228 VAL A CA  
1698  C C   . VAL A 228 ? 0.6978 0.6485 0.6684 0.0328  0.0134  0.1304  228 VAL A C   
1699  O O   . VAL A 228 ? 0.7639 0.7105 0.7426 0.0284  0.0076  0.1385  228 VAL A O   
1700  C CB  . VAL A 228 ? 0.4397 0.3989 0.4437 0.0398  0.0185  0.1345  228 VAL A CB  
1701  C CG1 . VAL A 228 ? 0.5424 0.4796 0.5411 0.0428  0.0127  0.1247  228 VAL A CG1 
1702  C CG2 . VAL A 228 ? 0.5357 0.5144 0.5587 0.0457  0.0270  0.1367  228 VAL A CG2 
1703  N N   . PRO A 229 ? 0.7055 0.6502 0.6592 0.0328  0.0117  0.1197  229 PRO A N   
1704  C CA  . PRO A 229 ? 0.6756 0.6146 0.6257 0.0269  0.0027  0.1191  229 PRO A CA  
1705  C C   . PRO A 229 ? 0.7210 0.6435 0.6807 0.0243  -0.0012 0.1156  229 PRO A C   
1706  O O   . PRO A 229 ? 0.7860 0.7003 0.7412 0.0206  -0.0042 0.1070  229 PRO A O   
1707  C CB  . PRO A 229 ? 0.6717 0.6126 0.6016 0.0261  0.0012  0.1082  229 PRO A CB  
1708  C CG  . PRO A 229 ? 0.5926 0.5265 0.5160 0.0325  0.0094  0.0973  229 PRO A CG  
1709  C CD  . PRO A 229 ? 0.6840 0.6275 0.6220 0.0379  0.0177  0.1068  229 PRO A CD  
1710  N N   . ALA A 230 ? 0.6678 0.5847 0.6393 0.0250  -0.0013 0.1226  230 ALA A N   
1711  C CA  . ALA A 230 ? 0.6860 0.5854 0.6607 0.0231  -0.0036 0.1207  230 ALA A CA  
1712  C C   . ALA A 230 ? 0.6811 0.5802 0.6607 0.0195  -0.0062 0.1266  230 ALA A C   
1713  O O   . ALA A 230 ? 0.6514 0.5605 0.6347 0.0198  -0.0076 0.1342  230 ALA A O   
1714  C CB  . ALA A 230 ? 0.5405 0.4313 0.5205 0.0271  -0.0037 0.1231  230 ALA A CB  
1715  N N   . PHE A 231 ? 0.6187 0.5051 0.5981 0.0167  -0.0054 0.1235  231 PHE A N   
1716  C CA  . PHE A 231 ? 0.5942 0.4796 0.5791 0.0153  -0.0048 0.1274  231 PHE A CA  
1717  C C   . PHE A 231 ? 0.7095 0.5758 0.6890 0.0132  -0.0005 0.1250  231 PHE A C   
1718  O O   . PHE A 231 ? 0.7809 0.6362 0.7541 0.0113  0.0007  0.1205  231 PHE A O   
1719  C CB  . PHE A 231 ? 0.5707 0.4731 0.5639 0.0128  -0.0066 0.1266  231 PHE A CB  
1720  C CG  . PHE A 231 ? 0.7064 0.6101 0.6996 0.0066  -0.0069 0.1179  231 PHE A CG  
1721  C CD1 . PHE A 231 ? 0.7332 0.6286 0.7317 0.0012  -0.0021 0.1152  231 PHE A CD1 
1722  C CD2 . PHE A 231 ? 0.6847 0.5966 0.6714 0.0053  -0.0114 0.1124  231 PHE A CD2 
1723  C CE1 . PHE A 231 ? 0.7253 0.6196 0.7259 -0.0071 -0.0029 0.1075  231 PHE A CE1 
1724  C CE2 . PHE A 231 ? 0.6526 0.5617 0.6382 -0.0019 -0.0133 0.1026  231 PHE A CE2 
1725  C CZ  . PHE A 231 ? 0.7250 0.6252 0.7194 -0.0089 -0.0095 0.1005  231 PHE A CZ  
1726  N N   . VAL A 232 ? 0.6393 0.4986 0.6184 0.0143  0.0024  0.1282  232 VAL A N   
1727  C CA  . VAL A 232 ? 0.6766 0.5164 0.6447 0.0126  0.0083  0.1271  232 VAL A CA  
1728  C C   . VAL A 232 ? 0.6807 0.5278 0.6584 0.0092  0.0168  0.1261  232 VAL A C   
1729  O O   . VAL A 232 ? 0.6199 0.4832 0.6120 0.0118  0.0172  0.1277  232 VAL A O   
1730  C CB  . VAL A 232 ? 0.6690 0.4918 0.6237 0.0165  0.0063  0.1298  232 VAL A CB  
1731  C CG1 . VAL A 232 ? 0.5225 0.3231 0.4583 0.0152  0.0129  0.1292  232 VAL A CG1 
1732  C CG2 . VAL A 232 ? 0.5509 0.3718 0.5033 0.0186  -0.0030 0.1314  232 VAL A CG2 
1733  N N   . ASN A 233 ? 0.6692 0.5053 0.6414 0.0034  0.0236  0.1245  233 ASN A N   
1734  C CA  . ASN A 233 ? 0.5517 0.3970 0.5369 -0.0017 0.0345  0.1244  233 ASN A CA  
1735  C C   . ASN A 233 ? 0.6908 0.5122 0.6552 -0.0021 0.0456  0.1269  233 ASN A C   
1736  O O   . ASN A 233 ? 0.7226 0.5268 0.6749 -0.0084 0.0490  0.1279  233 ASN A O   
1737  C CB  . ASN A 233 ? 0.5463 0.4027 0.5464 -0.0119 0.0337  0.1208  233 ASN A CB  
1738  C CG  . ASN A 233 ? 0.7868 0.6719 0.8080 -0.0118 0.0244  0.1183  233 ASN A CG  
1739  O OD1 . ASN A 233 ? 0.9371 0.8302 0.9577 -0.0038 0.0175  0.1203  233 ASN A OD1 
1740  N ND2 . ASN A 233 ? 0.5423 0.4419 0.5811 -0.0218 0.0233  0.1144  233 ASN A ND2 
1741  N N   . ALA A 234 ? 0.6024 0.4192 0.5592 0.0049  0.0509  0.1279  234 ALA A N   
1742  C CA  . ALA A 234 ? 0.7859 0.5775 0.7149 0.0058  0.0612  0.1294  234 ALA A CA  
1743  C C   . ALA A 234 ? 0.7644 0.5653 0.7039 0.0018  0.0806  0.1303  234 ALA A C   
1744  O O   . ALA A 234 ? 0.8306 0.6526 0.7925 0.0066  0.0869  0.1287  234 ALA A O   
1745  C CB  . ALA A 234 ? 0.7239 0.5021 0.6354 0.0149  0.0570  0.1277  234 ALA A CB  
1746  N N   . PHE A 235 ? 0.6178 0.4037 0.5434 -0.0067 0.0905  0.1340  235 PHE A N   
1747  C CA  . PHE A 235 ? 0.6989 0.4951 0.6364 -0.0130 0.1116  0.1363  235 PHE A CA  
1748  C C   . PHE A 235 ? 0.9365 0.7048 0.8350 -0.0105 0.1276  0.1396  235 PHE A C   
1749  O O   . PHE A 235 ? 0.9205 0.6571 0.7801 -0.0079 0.1196  0.1415  235 PHE A O   
1750  C CB  . PHE A 235 ? 0.8076 0.6083 0.7614 -0.0281 0.1131  0.1392  235 PHE A CB  
1751  C CG  . PHE A 235 ? 0.6488 0.4773 0.6384 -0.0322 0.0989  0.1344  235 PHE A CG  
1752  C CD1 . PHE A 235 ? 0.6579 0.5241 0.6865 -0.0320 0.1014  0.1321  235 PHE A CD1 
1753  C CD2 . PHE A 235 ? 0.6777 0.4945 0.6608 -0.0356 0.0833  0.1322  235 PHE A CD2 
1754  C CE1 . PHE A 235 ? 0.7854 0.6758 0.8416 -0.0360 0.0863  0.1280  235 PHE A CE1 
1755  C CE2 . PHE A 235 ? 0.7613 0.6012 0.7706 -0.0394 0.0710  0.1266  235 PHE A CE2 
1756  C CZ  . PHE A 235 ? 0.7963 0.6722 0.8399 -0.0402 0.0715  0.1247  235 PHE A CZ  
1757  N N   . GLY A 236 ? 0.8812 0.6627 0.7902 -0.0108 0.1501  0.1402  236 GLY A N   
1758  C CA  . GLY A 236 ? 0.8340 0.5902 0.7029 -0.0082 0.1693  0.1428  236 GLY A CA  
1759  C C   . GLY A 236 ? 0.8578 0.5950 0.6951 0.0066  0.1651  0.1360  236 GLY A C   
1760  O O   . GLY A 236 ? 1.0024 0.7441 0.8497 0.0138  0.1462  0.1306  236 GLY A O   
1761  N N   . PRO A 237 ? 0.8198 0.5332 0.6161 0.0108  0.1829  0.1358  237 PRO A N   
1762  C CA  . PRO A 237 ? 0.8545 0.5452 0.6167 0.0241  0.1781  0.1268  237 PRO A CA  
1763  C C   . PRO A 237 ? 0.9623 0.6333 0.7061 0.0260  0.1473  0.1244  237 PRO A C   
1764  O O   . PRO A 237 ? 1.0722 0.7253 0.7941 0.0196  0.1347  0.1307  237 PRO A O   
1765  C CB  . PRO A 237 ? 0.8592 0.5202 0.5681 0.0245  0.1994  0.1287  237 PRO A CB  
1766  C CG  . PRO A 237 ? 1.0535 0.7357 0.7863 0.0144  0.2247  0.1375  237 PRO A CG  
1767  C CD  . PRO A 237 ? 0.8651 0.5696 0.6418 0.0028  0.2091  0.1436  237 PRO A CD  
1768  N N   . LEU A 238 ? 0.9684 0.6427 0.7231 0.0350  0.1356  0.1160  238 LEU A N   
1769  C CA  . LEU A 238 ? 1.0175 0.6778 0.7616 0.0355  0.1077  0.1140  238 LEU A CA  
1770  C C   . LEU A 238 ? 0.9929 0.6173 0.6885 0.0414  0.1024  0.1060  238 LEU A C   
1771  O O   . LEU A 238 ? 1.0187 0.6364 0.7082 0.0501  0.1133  0.0970  238 LEU A O   
1772  C CB  . LEU A 238 ? 0.8768 0.5629 0.6659 0.0383  0.0952  0.1118  238 LEU A CB  
1773  C CG  . LEU A 238 ? 0.9574 0.6808 0.7947 0.0338  0.0990  0.1171  238 LEU A CG  
1774  C CD1 . LEU A 238 ? 0.7574 0.5017 0.6296 0.0391  0.0885  0.1153  238 LEU A CD1 
1775  C CD2 . LEU A 238 ? 0.8334 0.5587 0.6726 0.0238  0.0890  0.1237  238 LEU A CD2 
1776  N N   . SER A 239 ? 0.9655 0.5662 0.6269 0.0375  0.0842  0.1085  239 SER A N   
1777  C CA  . SER A 239 ? 0.9945 0.5602 0.6073 0.0411  0.0737  0.1002  239 SER A CA  
1778  C C   . SER A 239 ? 1.0309 0.5991 0.6641 0.0426  0.0526  0.0931  239 SER A C   
1779  O O   . SER A 239 ? 1.0765 0.6729 0.7568 0.0407  0.0461  0.0970  239 SER A O   
1780  C CB  . SER A 239 ? 1.1805 0.7234 0.7536 0.0363  0.0582  0.1072  239 SER A CB  
1781  O OG  . SER A 239 ? 1.3493 0.9067 0.9509 0.0322  0.0337  0.1127  239 SER A OG  
1782  N N   . GLU A 240 ? 1.1014 0.6386 0.6975 0.0447  0.0415  0.0828  240 GLU A N   
1783  C CA  . GLU A 240 ? 1.0458 0.5814 0.6602 0.0433  0.0209  0.0767  240 GLU A CA  
1784  C C   . GLU A 240 ? 1.0902 0.6441 0.7304 0.0351  -0.0034 0.0858  240 GLU A C   
1785  O O   . GLU A 240 ? 1.0669 0.6395 0.7464 0.0326  -0.0131 0.0873  240 GLU A O   
1786  C CB  . GLU A 240 ? 1.2150 0.7093 0.7801 0.0447  0.0109  0.0629  240 GLU A CB  
1787  C CG  . GLU A 240 ? 1.2376 0.7112 0.7776 0.0552  0.0356  0.0508  240 GLU A CG  
1788  C CD  . GLU A 240 ? 1.4547 0.9038 0.9365 0.0590  0.0525  0.0479  240 GLU A CD  
1789  O OE1 . GLU A 240 ? 1.5813 1.0291 1.0414 0.0531  0.0456  0.0576  240 GLU A OE1 
1790  O OE2 . GLU A 240 ? 1.6267 1.0567 1.0834 0.0687  0.0740  0.0363  240 GLU A OE2 
1791  N N   . LEU A 241 ? 1.0515 0.6000 0.6699 0.0320  -0.0119 0.0928  241 LEU A N   
1792  C CA  . LEU A 241 ? 1.0224 0.5888 0.6656 0.0271  -0.0330 0.1013  241 LEU A CA  
1793  C C   . LEU A 241 ? 1.0315 0.6339 0.7259 0.0267  -0.0235 0.1089  241 LEU A C   
1794  O O   . LEU A 241 ? 1.0400 0.6633 0.7692 0.0239  -0.0364 0.1117  241 LEU A O   
1795  C CB  . LEU A 241 ? 0.9749 0.5254 0.5827 0.0271  -0.0406 0.1084  241 LEU A CB  
1796  C CG  . LEU A 241 ? 0.9076 0.4737 0.5382 0.0251  -0.0637 0.1167  241 LEU A CG  
1797  C CD1 . LEU A 241 ? 1.0914 0.6454 0.7071 0.0222  -0.0921 0.1120  241 LEU A CD1 
1798  C CD2 . LEU A 241 ? 1.0723 0.6309 0.6853 0.0275  -0.0607 0.1277  241 LEU A CD2 
1799  N N   . VAL A 242 ? 1.0098 0.6197 0.7081 0.0287  -0.0009 0.1120  242 VAL A N   
1800  C CA  . VAL A 242 ? 0.8839 0.5257 0.6264 0.0273  0.0068  0.1175  242 VAL A CA  
1801  C C   . VAL A 242 ? 0.9561 0.6164 0.7323 0.0288  0.0067  0.1139  242 VAL A C   
1802  O O   . VAL A 242 ? 0.9783 0.6627 0.7881 0.0267  0.0002  0.1180  242 VAL A O   
1803  C CB  . VAL A 242 ? 0.9392 0.5848 0.6799 0.0268  0.0299  0.1210  242 VAL A CB  
1804  C CG1 . VAL A 242 ? 0.7774 0.4563 0.5644 0.0248  0.0368  0.1235  242 VAL A CG1 
1805  C CG2 . VAL A 242 ? 1.1020 0.7296 0.8142 0.0240  0.0287  0.1284  242 VAL A CG2 
1806  N N   . VAL A 243 ? 1.0006 0.6475 0.7656 0.0332  0.0142  0.1064  243 VAL A N   
1807  C CA  . VAL A 243 ? 0.8203 0.4790 0.6146 0.0359  0.0134  0.1043  243 VAL A CA  
1808  C C   . VAL A 243 ? 0.8855 0.5441 0.6897 0.0303  -0.0086 0.1057  243 VAL A C   
1809  O O   . VAL A 243 ? 0.9135 0.5941 0.7509 0.0285  -0.0125 0.1109  243 VAL A O   
1810  C CB  . VAL A 243 ? 0.7623 0.4005 0.5402 0.0438  0.0257  0.0952  243 VAL A CB  
1811  C CG1 . VAL A 243 ? 0.6584 0.3010 0.4629 0.0470  0.0209  0.0944  243 VAL A CG1 
1812  C CG2 . VAL A 243 ? 0.9824 0.6304 0.7619 0.0497  0.0506  0.0952  243 VAL A CG2 
1813  N N   . SER A 244 ? 0.9036 0.5392 0.6792 0.0267  -0.0232 0.1018  244 SER A N   
1814  C CA  . SER A 244 ? 0.9199 0.5581 0.7081 0.0195  -0.0450 0.1033  244 SER A CA  
1815  C C   . SER A 244 ? 0.9120 0.5828 0.7331 0.0168  -0.0499 0.1131  244 SER A C   
1816  O O   . SER A 244 ? 0.9683 0.6568 0.8192 0.0125  -0.0574 0.1172  244 SER A O   
1817  C CB  . SER A 244 ? 0.9202 0.5310 0.6709 0.0163  -0.0614 0.0975  244 SER A CB  
1818  O OG  . SER A 244 ? 1.0610 0.6769 0.8287 0.0079  -0.0837 0.0984  244 SER A OG  
1819  N N   . ALA A 245 ? 0.8902 0.5668 0.7047 0.0193  -0.0441 0.1170  245 ALA A N   
1820  C CA  . ALA A 245 ? 0.9486 0.6513 0.7902 0.0188  -0.0466 0.1241  245 ALA A CA  
1821  C C   . ALA A 245 ? 0.8841 0.6121 0.7578 0.0192  -0.0357 0.1267  245 ALA A C   
1822  O O   . ALA A 245 ? 0.8543 0.6045 0.7539 0.0176  -0.0404 0.1310  245 ALA A O   
1823  C CB  . ALA A 245 ? 0.8343 0.5297 0.6581 0.0216  -0.0408 0.1270  245 ALA A CB  
1824  N N   . GLY A 246 ? 0.8416 0.5669 0.7126 0.0221  -0.0214 0.1243  246 GLY A N   
1825  C CA  . GLY A 246 ? 0.8300 0.5778 0.7280 0.0234  -0.0133 0.1270  246 GLY A CA  
1826  C C   . GLY A 246 ? 0.8227 0.5760 0.7374 0.0215  -0.0213 0.1297  246 GLY A C   
1827  O O   . GLY A 246 ? 0.7625 0.5379 0.6995 0.0208  -0.0206 0.1350  246 GLY A O   
1828  N N   . ALA A 247 ? 0.7933 0.5245 0.6949 0.0196  -0.0293 0.1261  247 ALA A N   
1829  C CA  . ALA A 247 ? 0.6985 0.4300 0.6157 0.0151  -0.0376 0.1295  247 ALA A CA  
1830  C C   . ALA A 247 ? 0.8274 0.5811 0.7648 0.0086  -0.0470 0.1360  247 ALA A C   
1831  O O   . ALA A 247 ? 0.8057 0.5742 0.7643 0.0052  -0.0474 0.1431  247 ALA A O   
1832  C CB  . ALA A 247 ? 0.6913 0.3904 0.5878 0.0125  -0.0460 0.1223  247 ALA A CB  
1833  N N   . GLY A 248 ? 0.7965 0.5525 0.7272 0.0080  -0.0534 0.1345  248 GLY A N   
1834  C CA  . GLY A 248 ? 0.7285 0.5078 0.6809 0.0048  -0.0607 0.1398  248 GLY A CA  
1835  C C   . GLY A 248 ? 0.8206 0.6255 0.7902 0.0083  -0.0496 0.1443  248 GLY A C   
1836  O O   . GLY A 248 ? 0.7463 0.5730 0.7381 0.0056  -0.0499 0.1499  248 GLY A O   
1837  N N   . ALA A 249 ? 0.7582 0.5609 0.7171 0.0136  -0.0392 0.1415  249 ALA A N   
1838  C CA  . ALA A 249 ? 0.5695 0.3934 0.5406 0.0160  -0.0305 0.1436  249 ALA A CA  
1839  C C   . ALA A 249 ? 0.6929 0.5272 0.6759 0.0144  -0.0274 0.1490  249 ALA A C   
1840  O O   . ALA A 249 ? 0.6822 0.5366 0.6774 0.0139  -0.0250 0.1534  249 ALA A O   
1841  C CB  . ALA A 249 ? 0.5797 0.3973 0.5388 0.0191  -0.0220 0.1392  249 ALA A CB  
1842  N N   . ILE A 250 ? 0.8078 0.6262 0.7851 0.0147  -0.0272 0.1489  250 ILE A N   
1843  C CA  . ILE A 250 ? 0.6415 0.4637 0.6283 0.0147  -0.0258 0.1557  250 ILE A CA  
1844  C C   . ILE A 250 ? 0.6446 0.4726 0.6439 0.0073  -0.0316 0.1631  250 ILE A C   
1845  O O   . ILE A 250 ? 0.7910 0.6327 0.7997 0.0061  -0.0286 0.1718  250 ILE A O   
1846  C CB  . ILE A 250 ? 0.5541 0.3531 0.5320 0.0189  -0.0240 0.1527  250 ILE A CB  
1847  C CG1 . ILE A 250 ? 0.5973 0.4018 0.5729 0.0263  -0.0148 0.1485  250 ILE A CG1 
1848  C CG2 . ILE A 250 ? 0.5320 0.3259 0.5189 0.0184  -0.0261 0.1611  250 ILE A CG2 
1849  C CD1 . ILE A 250 ? 0.5558 0.3394 0.5218 0.0326  -0.0095 0.1429  250 ILE A CD1 
1850  N N   . ALA A 251 ? 0.5945 0.4136 0.5941 0.0017  -0.0401 0.1605  251 ALA A N   
1851  C CA  . ALA A 251 ? 0.6292 0.4577 0.6470 -0.0076 -0.0458 0.1675  251 ALA A CA  
1852  C C   . ALA A 251 ? 0.6690 0.5298 0.7029 -0.0072 -0.0395 0.1732  251 ALA A C   
1853  O O   . ALA A 251 ? 0.6902 0.5647 0.7401 -0.0136 -0.0373 0.1826  251 ALA A O   
1854  C CB  . ALA A 251 ? 0.6885 0.5056 0.7053 -0.0132 -0.0587 0.1621  251 ALA A CB  
1855  N N   . LEU A 252 ? 0.6677 0.5386 0.6960 0.0002  -0.0352 0.1675  252 LEU A N   
1856  C CA  . LEU A 252 ? 0.6909 0.5884 0.7297 0.0029  -0.0278 0.1700  252 LEU A CA  
1857  C C   . LEU A 252 ? 0.6398 0.5448 0.6702 0.0060  -0.0188 0.1730  252 LEU A C   
1858  O O   . LEU A 252 ? 0.7944 0.7172 0.8254 0.0093  -0.0119 0.1724  252 LEU A O   
1859  C CB  . LEU A 252 ? 0.6079 0.5077 0.6430 0.0099  -0.0281 0.1617  252 LEU A CB  
1860  C CG  . LEU A 252 ? 0.7036 0.5926 0.7398 0.0097  -0.0395 0.1582  252 LEU A CG  
1861  C CD1 . LEU A 252 ? 0.7973 0.6814 0.8237 0.0180  -0.0390 0.1518  252 LEU A CD1 
1862  C CD2 . LEU A 252 ? 0.5576 0.4654 0.6203 0.0048  -0.0455 0.1636  252 LEU A CD2 
1863  N N   . GLY A 253 ? 0.6152 0.5063 0.6372 0.0060  -0.0198 0.1755  253 GLY A N   
1864  C CA  . GLY A 253 ? 0.6683 0.5665 0.6832 0.0096  -0.0154 0.1793  253 GLY A CA  
1865  C C   . GLY A 253 ? 0.7099 0.6098 0.7155 0.0153  -0.0139 0.1701  253 GLY A C   
1866  O O   . GLY A 253 ? 0.8975 0.8087 0.8982 0.0175  -0.0121 0.1715  253 GLY A O   
1867  N N   . PHE A 254 ? 0.7288 0.6170 0.7310 0.0166  -0.0152 0.1612  254 PHE A N   
1868  C CA  . PHE A 254 ? 0.6755 0.5640 0.6713 0.0194  -0.0127 0.1532  254 PHE A CA  
1869  C C   . PHE A 254 ? 0.6321 0.5105 0.6269 0.0215  -0.0121 0.1521  254 PHE A C   
1870  O O   . PHE A 254 ? 0.6243 0.4850 0.6149 0.0218  -0.0125 0.1505  254 PHE A O   
1871  C CB  . PHE A 254 ? 0.6129 0.4936 0.6043 0.0197  -0.0126 0.1460  254 PHE A CB  
1872  C CG  . PHE A 254 ? 0.6538 0.5451 0.6502 0.0207  -0.0123 0.1457  254 PHE A CG  
1873  C CD1 . PHE A 254 ? 0.6521 0.5617 0.6511 0.0213  -0.0082 0.1481  254 PHE A CD1 
1874  C CD2 . PHE A 254 ? 0.6567 0.5401 0.6539 0.0225  -0.0155 0.1430  254 PHE A CD2 
1875  C CE1 . PHE A 254 ? 0.7357 0.6568 0.7406 0.0240  -0.0048 0.1469  254 PHE A CE1 
1876  C CE2 . PHE A 254 ? 0.4663 0.3624 0.4731 0.0259  -0.0144 0.1426  254 PHE A CE2 
1877  C CZ  . PHE A 254 ? 0.7274 0.6429 0.7390 0.0269  -0.0076 0.1440  254 PHE A CZ  
1878  N N   . PRO A 255 ? 0.6102 0.5005 0.6090 0.0234  -0.0111 0.1522  255 PRO A N   
1879  C CA  . PRO A 255 ? 0.5917 0.4772 0.5957 0.0271  -0.0087 0.1512  255 PRO A CA  
1880  C C   . PRO A 255 ? 0.6038 0.4801 0.6037 0.0256  -0.0027 0.1432  255 PRO A C   
1881  O O   . PRO A 255 ? 0.7751 0.6550 0.7723 0.0216  -0.0016 0.1385  255 PRO A O   
1882  C CB  . PRO A 255 ? 0.6634 0.5699 0.6773 0.0292  -0.0116 0.1542  255 PRO A CB  
1883  C CG  . PRO A 255 ? 0.7247 0.6434 0.7318 0.0257  -0.0151 0.1545  255 PRO A CG  
1884  C CD  . PRO A 255 ? 0.7676 0.6771 0.7664 0.0228  -0.0128 0.1525  255 PRO A CD  
1885  N N   . VAL A 256 ? 0.6035 0.4654 0.6008 0.0291  0.0022  0.1419  256 VAL A N   
1886  C CA  . VAL A 256 ? 0.6859 0.5370 0.6752 0.0278  0.0106  0.1362  256 VAL A CA  
1887  C C   . VAL A 256 ? 0.6536 0.5191 0.6594 0.0309  0.0185  0.1354  256 VAL A C   
1888  O O   . VAL A 256 ? 0.7581 0.6246 0.7725 0.0384  0.0200  0.1376  256 VAL A O   
1889  C CB  . VAL A 256 ? 0.6386 0.4624 0.6084 0.0299  0.0117  0.1341  256 VAL A CB  
1890  C CG1 . VAL A 256 ? 0.5196 0.3304 0.4748 0.0289  0.0220  0.1296  256 VAL A CG1 
1891  C CG2 . VAL A 256 ? 0.6241 0.4388 0.5845 0.0264  0.0014  0.1355  256 VAL A CG2 
1892  N N   . LEU A 257 ? 0.6370 0.5139 0.6502 0.0250  0.0233  0.1326  257 LEU A N   
1893  C CA  . LEU A 257 ? 0.5871 0.4836 0.6229 0.0259  0.0311  0.1320  257 LEU A CA  
1894  C C   . LEU A 257 ? 0.6840 0.5686 0.7112 0.0218  0.0455  0.1290  257 LEU A C   
1895  O O   . LEU A 257 ? 0.7701 0.6437 0.7842 0.0135  0.0460  0.1276  257 LEU A O   
1896  C CB  . LEU A 257 ? 0.5166 0.4396 0.5717 0.0195  0.0234  0.1316  257 LEU A CB  
1897  C CG  . LEU A 257 ? 0.6245 0.5592 0.6820 0.0229  0.0093  0.1356  257 LEU A CG  
1898  C CD1 . LEU A 257 ? 0.7241 0.6496 0.7626 0.0174  0.0028  0.1335  257 LEU A CD1 
1899  C CD2 . LEU A 257 ? 0.5785 0.5439 0.6610 0.0224  0.0024  0.1367  257 LEU A CD2 
1900  N N   . THR A 258 ? 0.6975 0.5822 0.7302 0.0284  0.0584  0.1284  258 THR A N   
1901  C CA  . THR A 258 ? 0.6594 0.5320 0.6798 0.0251  0.0757  0.1266  258 THR A CA  
1902  C C   . THR A 258 ? 0.7384 0.6384 0.7907 0.0260  0.0906  0.1269  258 THR A C   
1903  O O   . THR A 258 ? 0.8157 0.7401 0.8975 0.0340  0.0877  0.1278  258 THR A O   
1904  C CB  . THR A 258 ? 0.6517 0.4915 0.6379 0.0327  0.0806  0.1242  258 THR A CB  
1905  O OG1 . THR A 258 ? 0.7471 0.5748 0.7164 0.0303  0.0990  0.1232  258 THR A OG1 
1906  C CG2 . THR A 258 ? 0.5255 0.3653 0.5196 0.0461  0.0806  0.1224  258 THR A CG2 
1907  N N   . ASP A 259 ? 0.6681 0.5646 0.7158 0.0179  0.1070  0.1272  259 ASP A N   
1908  C CA  . ASP A 259 ? 0.6953 0.6203 0.7763 0.0171  0.1249  0.1281  259 ASP A CA  
1909  C C   . ASP A 259 ? 0.8017 0.7155 0.8699 0.0307  0.1451  0.1257  259 ASP A C   
1910  O O   . ASP A 259 ? 0.8659 0.8039 0.9618 0.0329  0.1642  0.1261  259 ASP A O   
1911  C CB  . ASP A 259 ? 0.6924 0.6189 0.7760 -0.0007 0.1352  0.1309  259 ASP A CB  
1912  C CG  . ASP A 259 ? 0.7791 0.6655 0.8152 -0.0048 0.1464  0.1328  259 ASP A CG  
1913  O OD1 . ASP A 259 ? 0.8348 0.6919 0.8337 0.0050  0.1420  0.1307  259 ASP A OD1 
1914  O OD2 . ASP A 259 ? 0.7404 0.6236 0.7759 -0.0186 0.1581  0.1370  259 ASP A OD2 
1915  N N   . GLN A 260 ? 0.7494 0.6280 0.7778 0.0393  0.1403  0.1223  260 GLN A N   
1916  C CA  . GLN A 260 ? 0.8366 0.6961 0.8430 0.0522  0.1586  0.1173  260 GLN A CA  
1917  C C   . GLN A 260 ? 0.7490 0.6106 0.7694 0.0692  0.1518  0.1135  260 GLN A C   
1918  O O   . GLN A 260 ? 0.7357 0.6025 0.7677 0.0692  0.1301  0.1162  260 GLN A O   
1919  C CB  . GLN A 260 ? 0.7672 0.5815 0.7151 0.0492  0.1581  0.1151  260 GLN A CB  
1920  C CG  . GLN A 260 ? 1.0459 0.8433 0.9645 0.0530  0.1849  0.1121  260 GLN A CG  
1921  C CD  . GLN A 260 ? 1.0582 0.8575 0.9693 0.0383  0.1990  0.1194  260 GLN A CD  
1922  O OE1 . GLN A 260 ? 0.8703 0.6755 0.7915 0.0251  0.1864  0.1254  260 GLN A OE1 
1923  N NE2 . GLN A 260 ? 1.5616 1.3534 1.4532 0.0406  0.2268  0.1190  260 GLN A NE2 
1924  N N   . VAL A 261 ? 0.8156 0.6711 0.8329 0.0836  0.1709  0.1079  261 VAL A N   
1925  C CA  . VAL A 261 ? 0.7236 0.5755 0.7533 0.1018  0.1670  0.1040  261 VAL A CA  
1926  C C   . VAL A 261 ? 0.8174 0.6221 0.8006 0.1034  0.1526  0.0987  261 VAL A C   
1927  O O   . VAL A 261 ? 0.8725 0.6434 0.8114 0.1041  0.1621  0.0914  261 VAL A O   
1928  C CB  . VAL A 261 ? 0.6406 0.5022 0.6853 0.1183  0.1949  0.0984  261 VAL A CB  
1929  C CG1 . VAL A 261 ? 0.7721 0.6118 0.8135 0.1390  0.1921  0.0918  261 VAL A CG1 
1930  C CG2 . VAL A 261 ? 0.6895 0.6068 0.7954 0.1177  0.2042  0.1049  261 VAL A CG2 
1931  N N   . VAL A 262 ? 0.8234 0.6269 0.8164 0.1028  0.1292  0.1028  262 VAL A N   
1932  C CA  . VAL A 262 ? 0.8728 0.6371 0.8312 0.1015  0.1130  0.0993  262 VAL A CA  
1933  C C   . VAL A 262 ? 0.8583 0.6206 0.8378 0.1124  0.1012  0.1021  262 VAL A C   
1934  O O   . VAL A 262 ? 0.9758 0.7711 0.9954 0.1179  0.0997  0.1092  262 VAL A O   
1935  C CB  . VAL A 262 ? 0.8190 0.5820 0.7641 0.0844  0.0949  0.1047  262 VAL A CB  
1936  C CG1 . VAL A 262 ? 0.8320 0.5913 0.7538 0.0744  0.1047  0.1038  262 VAL A CG1 
1937  C CG2 . VAL A 262 ? 0.5639 0.3611 0.5458 0.0794  0.0817  0.1143  262 VAL A CG2 
1938  N N   . PRO A 263 ? 0.7578 0.4814 0.7115 0.1144  0.0910  0.0975  263 PRO A N   
1939  C CA  . PRO A 263 ? 0.8156 0.5335 0.7887 0.1232  0.0797  0.1027  263 PRO A CA  
1940  C C   . PRO A 263 ? 0.8739 0.6181 0.8693 0.1130  0.0615  0.1163  263 PRO A C   
1941  O O   . PRO A 263 ? 0.8895 0.6204 0.8696 0.1009  0.0471  0.1192  263 PRO A O   
1942  C CB  . PRO A 263 ? 0.7958 0.4631 0.7318 0.1220  0.0723  0.0940  263 PRO A CB  
1943  C CG  . PRO A 263 ? 0.8748 0.5227 0.7722 0.1181  0.0832  0.0821  263 PRO A CG  
1944  C CD  . PRO A 263 ? 0.8432 0.5256 0.7495 0.1078  0.0872  0.0884  263 PRO A CD  
1945  N N   . GLU A 264 ? 0.8762 0.6594 0.9081 0.1179  0.0625  0.1242  264 GLU A N   
1946  C CA  . GLU A 264 ? 0.6117 0.4213 0.6610 0.1093  0.0468  0.1359  264 GLU A CA  
1947  C C   . GLU A 264 ? 0.7111 0.5019 0.7557 0.1092  0.0314  0.1443  264 GLU A C   
1948  O O   . GLU A 264 ? 0.9750 0.7443 1.0220 0.1217  0.0317  0.1452  264 GLU A O   
1949  C CB  . GLU A 264 ? 0.7801 0.6319 0.8690 0.1171  0.0486  0.1418  264 GLU A CB  
1950  C CG  . GLU A 264 ? 0.7815 0.6616 0.8825 0.1106  0.0607  0.1370  264 GLU A CG  
1951  C CD  . GLU A 264 ? 0.9962 0.9216 1.1413 0.1158  0.0593  0.1427  264 GLU A CD  
1952  O OE1 . GLU A 264 ? 1.1056 1.0507 1.2620 0.1107  0.0421  0.1508  264 GLU A OE1 
1953  O OE2 . GLU A 264 ? 1.1384 1.0809 1.3069 0.1248  0.0753  0.1389  264 GLU A OE2 
1954  N N   . VAL A 265 ? 0.7325 0.5312 0.7712 0.0954  0.0192  0.1511  265 VAL A N   
1955  C CA  . VAL A 265 ? 0.8145 0.6010 0.8502 0.0920  0.0062  0.1618  265 VAL A CA  
1956  C C   . VAL A 265 ? 0.8144 0.6366 0.8658 0.0890  -0.0017 0.1723  265 VAL A C   
1957  O O   . VAL A 265 ? 0.7960 0.6373 0.8443 0.0785  -0.0022 0.1696  265 VAL A O   
1958  C CB  . VAL A 265 ? 0.7906 0.5550 0.8032 0.0775  0.0006  0.1594  265 VAL A CB  
1959  C CG1 . VAL A 265 ? 0.5848 0.3459 0.5994 0.0710  -0.0104 0.1728  265 VAL A CG1 
1960  C CG2 . VAL A 265 ? 0.6336 0.3594 0.6261 0.0796  0.0050  0.1479  265 VAL A CG2 
1961  N N   . PRO A 266 ? 0.7512 0.5816 0.8176 0.0986  -0.0087 0.1841  266 PRO A N   
1962  C CA  . PRO A 266 ? 0.6351 0.4989 0.7109 0.0955  -0.0181 0.1932  266 PRO A CA  
1963  C C   . PRO A 266 ? 0.7781 0.6480 0.8367 0.0795  -0.0223 0.1944  266 PRO A C   
1964  O O   . PRO A 266 ? 0.9481 0.7968 0.9918 0.0722  -0.0232 0.1975  266 PRO A O   
1965  C CB  . PRO A 266 ? 0.5503 0.4077 0.6331 0.1069  -0.0272 0.2084  266 PRO A CB  
1966  C CG  . PRO A 266 ? 0.7410 0.5729 0.8314 0.1212  -0.0201 0.2043  266 PRO A CG  
1967  C CD  . PRO A 266 ? 0.7497 0.5569 0.8226 0.1134  -0.0095 0.1896  266 PRO A CD  
1968  N N   . THR A 267 ? 0.7369 0.6364 0.7997 0.0740  -0.0246 0.1914  267 THR A N   
1969  C CA  . THR A 267 ? 0.6365 0.5445 0.6842 0.0615  -0.0272 0.1906  267 THR A CA  
1970  C C   . THR A 267 ? 0.6426 0.5349 0.6775 0.0523  -0.0203 0.1815  267 THR A C   
1971  O O   . THR A 267 ? 0.8588 0.7594 0.8846 0.0442  -0.0212 0.1797  267 THR A O   
1972  C CB  . THR A 267 ? 0.7128 0.6198 0.7489 0.0599  -0.0347 0.2049  267 THR A CB  
1973  O OG1 . THR A 267 ? 0.7153 0.5958 0.7426 0.0559  -0.0317 0.2093  267 THR A OG1 
1974  C CG2 . THR A 267 ? 0.5843 0.4997 0.6289 0.0709  -0.0439 0.2173  267 THR A CG2 
1975  N N   . LEU A 268 ? 0.6888 0.5583 0.7213 0.0544  -0.0142 0.1756  268 LEU A N   
1976  C CA  . LEU A 268 ? 0.6923 0.5469 0.7109 0.0462  -0.0112 0.1682  268 LEU A CA  
1977  C C   . LEU A 268 ? 0.7647 0.6129 0.7795 0.0472  -0.0029 0.1569  268 LEU A C   
1978  O O   . LEU A 268 ? 0.8351 0.6835 0.8409 0.0405  -0.0015 0.1516  268 LEU A O   
1979  C CB  . LEU A 268 ? 0.6707 0.4987 0.6814 0.0439  -0.0143 0.1717  268 LEU A CB  
1980  C CG  . LEU A 268 ? 0.7246 0.5552 0.7372 0.0399  -0.0202 0.1849  268 LEU A CG  
1981  C CD1 . LEU A 268 ? 0.6246 0.4253 0.6337 0.0370  -0.0231 0.1883  268 LEU A CD1 
1982  C CD2 . LEU A 268 ? 0.5490 0.3983 0.5588 0.0309  -0.0209 0.1861  268 LEU A CD2 
1983  N N   . LEU A 269 ? 0.7639 0.6050 0.7844 0.0563  0.0038  0.1539  269 LEU A N   
1984  C CA  . LEU A 269 ? 0.6553 0.4907 0.6700 0.0574  0.0152  0.1443  269 LEU A CA  
1985  C C   . LEU A 269 ? 0.6773 0.5352 0.7161 0.0658  0.0224  0.1446  269 LEU A C   
1986  O O   . LEU A 269 ? 0.7945 0.6494 0.8446 0.0773  0.0237  0.1472  269 LEU A O   
1987  C CB  . LEU A 269 ? 0.5715 0.3722 0.5655 0.0606  0.0188  0.1383  269 LEU A CB  
1988  C CG  . LEU A 269 ? 0.7370 0.5265 0.7160 0.0624  0.0322  0.1289  269 LEU A CG  
1989  C CD1 . LEU A 269 ? 0.6574 0.4520 0.6249 0.0519  0.0324  0.1274  269 LEU A CD1 
1990  C CD2 . LEU A 269 ? 0.7240 0.4759 0.6766 0.0659  0.0333  0.1217  269 LEU A CD2 
1991  N N   . LEU A 270 ? 0.5863 0.4674 0.6360 0.0600  0.0264  0.1423  270 LEU A N   
1992  C CA  . LEU A 270 ? 0.6978 0.6076 0.7777 0.0656  0.0315  0.1431  270 LEU A CA  
1993  C C   . LEU A 270 ? 0.7773 0.6930 0.8617 0.0618  0.0476  0.1367  270 LEU A C   
1994  O O   . LEU A 270 ? 0.7672 0.6678 0.8298 0.0523  0.0518  0.1330  270 LEU A O   
1995  C CB  . LEU A 270 ? 0.6193 0.5585 0.7157 0.0600  0.0184  0.1479  270 LEU A CB  
1996  C CG  . LEU A 270 ? 0.5624 0.4976 0.6494 0.0611  0.0038  0.1559  270 LEU A CG  
1997  C CD1 . LEU A 270 ? 0.5520 0.5100 0.6418 0.0528  -0.0072 0.1572  270 LEU A CD1 
1998  C CD2 . LEU A 270 ? 0.6848 0.6196 0.7849 0.0753  -0.0001 0.1638  270 LEU A CD2 
1999  N N   . THR A 271 ? 0.6777 0.6169 0.7924 0.0695  0.0569  0.1367  271 THR A N   
2000  C CA  . THR A 271 ? 0.6547 0.6048 0.7796 0.0655  0.0755  0.1325  271 THR A CA  
2001  C C   . THR A 271 ? 0.7757 0.7696 0.9430 0.0597  0.0737  0.1348  271 THR A C   
2002  O O   . THR A 271 ? 0.8567 0.8776 1.0588 0.0708  0.0726  0.1378  271 THR A O   
2003  C CB  . THR A 271 ? 0.6712 0.6110 0.7968 0.0806  0.0941  0.1287  271 THR A CB  
2004  O OG1 . THR A 271 ? 0.8014 0.6978 0.8829 0.0822  0.0973  0.1238  271 THR A OG1 
2005  C CG2 . THR A 271 ? 0.7470 0.7085 0.8932 0.0784  0.1162  0.1264  271 THR A CG2 
2006  N N   . GLN A 272 ? 0.6725 0.6726 0.8381 0.0425  0.0721  0.1334  272 GLN A N   
2007  C CA  . GLN A 272 ? 0.6411 0.6800 0.8455 0.0326  0.0689  0.1340  272 GLN A CA  
2008  C C   . GLN A 272 ? 0.7858 0.8261 0.9953 0.0208  0.0898  0.1319  272 GLN A C   
2009  O O   . GLN A 272 ? 0.8048 0.8170 0.9825 0.0099  0.0936  0.1302  272 GLN A O   
2010  C CB  . GLN A 272 ? 0.4305 0.4706 0.6256 0.0208  0.0476  0.1334  272 GLN A CB  
2011  C CG  . GLN A 272 ? 0.6996 0.7721 0.9269 0.0060  0.0412  0.1313  272 GLN A CG  
2012  C CD  . GLN A 272 ? 0.7057 0.8216 0.9786 0.0132  0.0322  0.1348  272 GLN A CD  
2013  O OE1 . GLN A 272 ? 0.6007 0.7426 0.9104 0.0164  0.0456  0.1362  272 GLN A OE1 
2014  N NE2 . GLN A 272 ? 0.7167 0.8427 0.9884 0.0164  0.0094  0.1369  272 GLN A NE2 
2015  N N   . LYS A 273 ? 0.6669 0.7396 0.9167 0.0237  0.1042  0.1330  273 LYS A N   
2016  C CA  . LYS A 273 ? 0.5728 0.6492 0.8297 0.0120  0.1279  0.1329  273 LYS A CA  
2017  C C   . LYS A 273 ? 0.7412 0.8430 1.0277 -0.0100 0.1208  0.1334  273 LYS A C   
2018  O O   . LYS A 273 ? 0.9740 1.0635 1.2511 -0.0257 0.1349  0.1341  273 LYS A O   
2019  C CB  . LYS A 273 ? 0.7426 0.8432 1.0307 0.0253  0.1518  0.1338  273 LYS A CB  
2020  C CG  . LYS A 273 ? 0.6682 0.7375 0.9232 0.0458  0.1650  0.1309  273 LYS A CG  
2021  C CD  . LYS A 273 ? 1.3545 1.4487 1.6420 0.0611  0.1908  0.1300  273 LYS A CD  
2022  C CE  . LYS A 273 ? 1.1716 1.2296 1.4220 0.0816  0.2044  0.1244  273 LYS A CE  
2023  N NZ  . LYS A 273 ? 1.4904 1.5728 1.7731 0.0989  0.2317  0.1221  273 LYS A NZ  
2024  N N   . ASP A 274 ? 0.7273 0.8627 1.0481 -0.0118 0.0988  0.1331  274 ASP A N   
2025  C CA  . ASP A 274 ? 0.5184 0.6773 0.8675 -0.0339 0.0889  0.1314  274 ASP A CA  
2026  C C   . ASP A 274 ? 0.7416 0.8626 1.0480 -0.0475 0.0761  0.1271  274 ASP A C   
2027  O O   . ASP A 274 ? 0.7752 0.8882 1.0632 -0.0432 0.0543  0.1244  274 ASP A O   
2028  C CB  . ASP A 274 ? 0.5975 0.8032 0.9925 -0.0306 0.0663  0.1316  274 ASP A CB  
2029  C CG  . ASP A 274 ? 0.8546 1.0902 1.2860 -0.0545 0.0548  0.1285  274 ASP A CG  
2030  O OD1 . ASP A 274 ? 1.0935 1.3181 1.5244 -0.0739 0.0696  0.1274  274 ASP A OD1 
2031  O OD2 . ASP A 274 ? 0.8372 1.1058 1.2967 -0.0544 0.0303  0.1275  274 ASP A OD2 
2032  N N   . TYR A 275 ? 0.7453 0.8424 1.0356 -0.0632 0.0908  0.1272  275 TYR A N   
2033  C CA  . TYR A 275 ? 0.6584 0.7165 0.9097 -0.0743 0.0809  0.1233  275 TYR A CA  
2034  C C   . TYR A 275 ? 0.6727 0.7459 0.9398 -0.0872 0.0566  0.1164  275 TYR A C   
2035  O O   . TYR A 275 ? 0.8316 0.8786 1.0658 -0.0869 0.0421  0.1112  275 TYR A O   
2036  C CB  . TYR A 275 ? 0.6252 0.6557 0.8606 -0.0886 0.1015  0.1268  275 TYR A CB  
2037  C CG  . TYR A 275 ? 0.6227 0.6320 0.8305 -0.0759 0.1240  0.1327  275 TYR A CG  
2038  C CD1 . TYR A 275 ? 0.6750 0.6439 0.8326 -0.0643 0.1206  0.1326  275 TYR A CD1 
2039  C CD2 . TYR A 275 ? 0.7338 0.7649 0.9662 -0.0753 0.1487  0.1376  275 TYR A CD2 
2040  C CE1 . TYR A 275 ? 0.7768 0.7241 0.9049 -0.0536 0.1384  0.1364  275 TYR A CE1 
2041  C CE2 . TYR A 275 ? 0.5942 0.6026 0.7947 -0.0633 0.1697  0.1412  275 TYR A CE2 
2042  C CZ  . TYR A 275 ? 0.6940 0.6591 0.8405 -0.0529 0.1631  0.1402  275 TYR A CZ  
2043  O OH  . TYR A 275 ? 0.8072 0.7485 0.9189 -0.0420 0.1814  0.1423  275 TYR A OH  
2044  N N   . ASP A 276 ? 0.6018 0.7183 0.9193 -0.0978 0.0516  0.1156  276 ASP A N   
2045  C CA  . ASP A 276 ? 0.6550 0.7869 0.9866 -0.1111 0.0259  0.1075  276 ASP A CA  
2046  C C   . ASP A 276 ? 0.7545 0.8939 1.0713 -0.0948 0.0025  0.1052  276 ASP A C   
2047  O O   . ASP A 276 ? 0.8290 0.9758 1.1454 -0.1035 -0.0203 0.0976  276 ASP A O   
2048  C CB  . ASP A 276 ? 0.6403 0.8220 1.0346 -0.1267 0.0243  0.1080  276 ASP A CB  
2049  C CG  . ASP A 276 ? 1.0053 1.1804 1.4164 -0.1485 0.0461  0.1107  276 ASP A CG  
2050  O OD1 . ASP A 276 ? 1.0556 1.1875 1.4332 -0.1621 0.0474  0.1070  276 ASP A OD1 
2051  O OD2 . ASP A 276 ? 1.0076 1.2204 1.4658 -0.1514 0.0628  0.1172  276 ASP A OD2 
2052  N N   . LYS A 277 ? 0.7546 0.8894 1.0564 -0.0722 0.0080  0.1115  277 LYS A N   
2053  C CA  . LYS A 277 ? 0.7071 0.8454 0.9928 -0.0565 -0.0110 0.1125  277 LYS A CA  
2054  C C   . LYS A 277 ? 0.6691 0.7650 0.9038 -0.0449 -0.0065 0.1135  277 LYS A C   
2055  O O   . LYS A 277 ? 0.6751 0.7683 0.8907 -0.0350 -0.0206 0.1146  277 LYS A O   
2056  C CB  . LYS A 277 ? 0.6018 0.7758 0.9228 -0.0395 -0.0110 0.1206  277 LYS A CB  
2057  C CG  . LYS A 277 ? 0.5133 0.7353 0.8787 -0.0439 -0.0319 0.1204  277 LYS A CG  
2058  C CD  . LYS A 277 ? 0.7949 1.0437 1.1824 -0.0211 -0.0396 0.1297  277 LYS A CD  
2059  C CE  . LYS A 277 ? 0.9611 1.2131 1.3680 -0.0049 -0.0146 0.1359  277 LYS A CE  
2060  N NZ  . LYS A 277 ? 1.0178 1.3105 1.4821 -0.0120 -0.0014 0.1362  277 LYS A NZ  
2061  N N   . MET A 278 ? 0.6149 0.6794 0.8282 -0.0463 0.0125  0.1142  278 MET A N   
2062  C CA  . MET A 278 ? 0.7080 0.7356 0.8783 -0.0363 0.0157  0.1153  278 MET A CA  
2063  C C   . MET A 278 ? 0.7321 0.7437 0.8740 -0.0385 0.0000  0.1097  278 MET A C   
2064  O O   . MET A 278 ? 0.6813 0.6790 0.7992 -0.0270 -0.0030 0.1123  278 MET A O   
2065  C CB  . MET A 278 ? 0.5748 0.5723 0.7268 -0.0407 0.0351  0.1165  278 MET A CB  
2066  C CG  . MET A 278 ? 0.6018 0.5641 0.7134 -0.0310 0.0365  0.1177  278 MET A CG  
2067  S SD  . MET A 278 ? 0.6626 0.6268 0.7686 -0.0110 0.0360  0.1231  278 MET A SD  
2068  C CE  . MET A 278 ? 0.6516 0.5952 0.7451 -0.0074 0.0584  0.1257  278 MET A CE  
2069  N N   . VAL A 279 ? 0.7537 0.7663 0.8980 -0.0531 -0.0089 0.1015  279 VAL A N   
2070  C CA  . VAL A 279 ? 0.6258 0.6219 0.7407 -0.0537 -0.0215 0.0942  279 VAL A CA  
2071  C C   . VAL A 279 ? 0.6702 0.6886 0.7837 -0.0442 -0.0372 0.0963  279 VAL A C   
2072  O O   . VAL A 279 ? 0.7795 0.7852 0.8670 -0.0336 -0.0384 0.0989  279 VAL A O   
2073  C CB  . VAL A 279 ? 0.5066 0.4927 0.6211 -0.0716 -0.0273 0.0828  279 VAL A CB  
2074  C CG1 . VAL A 279 ? 0.5682 0.5391 0.6511 -0.0697 -0.0397 0.0732  279 VAL A CG1 
2075  C CG2 . VAL A 279 ? 0.8000 0.7561 0.9088 -0.0797 -0.0112 0.0834  279 VAL A CG2 
2076  N N   . LYS A 280 ? 0.6103 0.6627 0.7527 -0.0480 -0.0494 0.0966  280 LYS A N   
2077  C CA  . LYS A 280 ? 0.5393 0.6126 0.6789 -0.0387 -0.0665 0.1008  280 LYS A CA  
2078  C C   . LYS A 280 ? 0.6814 0.7508 0.8146 -0.0206 -0.0596 0.1132  280 LYS A C   
2079  O O   . LYS A 280 ? 0.7509 0.8180 0.8622 -0.0120 -0.0681 0.1178  280 LYS A O   
2080  C CB  . LYS A 280 ? 0.6173 0.7313 0.7967 -0.0439 -0.0809 0.1015  280 LYS A CB  
2081  C CG  . LYS A 280 ? 0.7777 0.8984 0.9616 -0.0634 -0.0954 0.0883  280 LYS A CG  
2082  C CD  . LYS A 280 ? 0.9622 1.1284 1.1946 -0.0699 -0.1101 0.0898  280 LYS A CD  
2083  C CE  . LYS A 280 ? 1.2028 1.3740 1.4495 -0.0940 -0.1203 0.0763  280 LYS A CE  
2084  N NZ  . LYS A 280 ? 0.6803 0.9013 0.9822 -0.1019 -0.1348 0.0783  280 LYS A NZ  
2085  N N   . THR A 281 ? 0.6621 0.7287 0.8123 -0.0155 -0.0435 0.1184  281 THR A N   
2086  C CA  . THR A 281 ? 0.5736 0.6313 0.7182 0.0004  -0.0362 0.1282  281 THR A CA  
2087  C C   . THR A 281 ? 0.6296 0.6558 0.7361 0.0034  -0.0326 0.1283  281 THR A C   
2088  O O   . THR A 281 ? 0.7317 0.7546 0.8254 0.0127  -0.0377 0.1356  281 THR A O   
2089  C CB  . THR A 281 ? 0.6469 0.7030 0.8114 0.0035  -0.0178 0.1300  281 THR A CB  
2090  O OG1 . THR A 281 ? 0.7022 0.7922 0.9080 -0.0004 -0.0185 0.1297  281 THR A OG1 
2091  C CG2 . THR A 281 ? 0.5519 0.5964 0.7110 0.0196  -0.0113 0.1376  281 THR A CG2 
2092  N N   . SER A 282 ? 0.6238 0.6275 0.7144 -0.0045 -0.0240 0.1214  282 SER A N   
2093  C CA  . SER A 282 ? 0.6497 0.6277 0.7107 -0.0012 -0.0207 0.1214  282 SER A CA  
2094  C C   . SER A 282 ? 0.7421 0.7233 0.7844 -0.0010 -0.0315 0.1195  282 SER A C   
2095  O O   . SER A 282 ? 0.8037 0.7776 0.8308 0.0060  -0.0310 0.1253  282 SER A O   
2096  C CB  . SER A 282 ? 0.5322 0.4872 0.5829 -0.0084 -0.0112 0.1151  282 SER A CB  
2097  O OG  . SER A 282 ? 0.6365 0.5856 0.6972 -0.0082 0.0008  0.1179  282 SER A OG  
2098  N N   . LEU A 283 ? 0.5624 0.5542 0.6047 -0.0092 -0.0410 0.1113  283 LEU A N   
2099  C CA  . LEU A 283 ? 0.5628 0.5560 0.5810 -0.0085 -0.0502 0.1080  283 LEU A CA  
2100  C C   . LEU A 283 ? 0.7154 0.7240 0.7312 0.0006  -0.0579 0.1201  283 LEU A C   
2101  O O   . LEU A 283 ? 0.7414 0.7440 0.7337 0.0054  -0.0574 0.1239  283 LEU A O   
2102  C CB  . LEU A 283 ? 0.5827 0.5827 0.5991 -0.0198 -0.0613 0.0953  283 LEU A CB  
2103  C CG  . LEU A 283 ? 0.7092 0.6900 0.7275 -0.0307 -0.0551 0.0835  283 LEU A CG  
2104  C CD1 . LEU A 283 ? 0.7231 0.7103 0.7416 -0.0437 -0.0687 0.0704  283 LEU A CD1 
2105  C CD2 . LEU A 283 ? 0.6877 0.6400 0.6814 -0.0260 -0.0446 0.0796  283 LEU A CD2 
2106  N N   . GLU A 284 ? 0.7291 0.7569 0.7703 0.0038  -0.0638 0.1273  284 GLU A N   
2107  C CA  . GLU A 284 ? 0.6718 0.7104 0.7116 0.0141  -0.0719 0.1408  284 GLU A CA  
2108  C C   . GLU A 284 ? 0.6376 0.6570 0.6702 0.0224  -0.0604 0.1507  284 GLU A C   
2109  O O   . GLU A 284 ? 0.5993 0.6141 0.6129 0.0270  -0.0626 0.1597  284 GLU A O   
2110  C CB  . GLU A 284 ? 0.5171 0.5808 0.5916 0.0180  -0.0804 0.1458  284 GLU A CB  
2111  C CG  . GLU A 284 ? 0.6139 0.6847 0.6889 0.0311  -0.0891 0.1616  284 GLU A CG  
2112  C CD  . GLU A 284 ? 0.7050 0.8025 0.8184 0.0383  -0.0977 0.1671  284 GLU A CD  
2113  O OE1 . GLU A 284 ? 0.7373 0.8579 0.8747 0.0302  -0.1042 0.1586  284 GLU A OE1 
2114  O OE2 . GLU A 284 ? 0.7488 0.8439 0.8706 0.0521  -0.0980 0.1800  284 GLU A OE2 
2115  N N   . ALA A 285 ? 0.6546 0.6619 0.7009 0.0231  -0.0482 0.1490  285 ALA A N   
2116  C CA  . ALA A 285 ? 0.6564 0.6436 0.6967 0.0291  -0.0392 0.1559  285 ALA A CA  
2117  C C   . ALA A 285 ? 0.6445 0.6183 0.6604 0.0268  -0.0361 0.1568  285 ALA A C   
2118  O O   . ALA A 285 ? 0.6593 0.6222 0.6703 0.0306  -0.0334 0.1659  285 ALA A O   
2119  C CB  . ALA A 285 ? 0.6437 0.6182 0.6946 0.0283  -0.0275 0.1505  285 ALA A CB  
2120  N N   . ARG A 286 ? 0.6395 0.6138 0.6422 0.0205  -0.0358 0.1472  286 ARG A N   
2121  C CA  . ARG A 286 ? 0.6661 0.6321 0.6497 0.0200  -0.0308 0.1471  286 ARG A CA  
2122  C C   . ARG A 286 ? 0.7632 0.7405 0.7264 0.0193  -0.0364 0.1464  286 ARG A C   
2123  O O   . ARG A 286 ? 0.9200 0.8934 0.8671 0.0186  -0.0306 0.1413  286 ARG A O   
2124  C CB  . ARG A 286 ? 0.6077 0.5600 0.5899 0.0165  -0.0234 0.1363  286 ARG A CB  
2125  C CG  . ARG A 286 ? 0.6843 0.6295 0.6561 0.0182  -0.0168 0.1366  286 ARG A CG  
2126  C CD  . ARG A 286 ? 0.7262 0.6708 0.7014 0.0208  -0.0146 0.1494  286 ARG A CD  
2127  N NE  . ARG A 286 ? 0.6876 0.6285 0.6626 0.0213  -0.0082 0.1494  286 ARG A NE  
2128  C CZ  . ARG A 286 ? 0.6181 0.5614 0.5972 0.0209  -0.0056 0.1598  286 ARG A CZ  
2129  N NH1 . ARG A 286 ? 0.7223 0.6663 0.7023 0.0203  -0.0084 0.1714  286 ARG A NH1 
2130  N NH2 . ARG A 286 ? 0.6554 0.6005 0.6405 0.0210  -0.0005 0.1592  286 ARG A NH2 
2131  N N   . ASN A 287 ? 0.7988 0.7904 0.7617 0.0208  -0.0477 0.1515  287 ASN A N   
2132  C CA  . ASN A 287 ? 0.8903 0.8917 0.8281 0.0204  -0.0556 0.1516  287 ASN A CA  
2133  C C   . ASN A 287 ? 0.7887 0.7868 0.7077 0.0150  -0.0544 0.1343  287 ASN A C   
2134  O O   . ASN A 287 ? 0.9784 0.9777 0.8685 0.0160  -0.0539 0.1329  287 ASN A O   
2135  C CB  . ASN A 287 ? 0.7571 0.7555 0.6770 0.0247  -0.0503 0.1666  287 ASN A CB  
2136  C CG  . ASN A 287 ? 1.2134 1.2225 1.1099 0.0271  -0.0615 0.1753  287 ASN A CG  
2137  O OD1 . ASN A 287 ? 1.4123 1.4308 1.3187 0.0303  -0.0754 0.1823  287 ASN A OD1 
2138  N ND2 . ASN A 287 ? 1.4251 1.4336 1.2892 0.0265  -0.0558 0.1755  287 ASN A ND2 
2139  N N   . ILE A 288 ? 0.7606 0.7524 0.6939 0.0095  -0.0532 0.1213  288 ILE A N   
2140  C CA  . ILE A 288 ? 0.8200 0.8027 0.7372 0.0043  -0.0527 0.1039  288 ILE A CA  
2141  C C   . ILE A 288 ? 0.9077 0.9027 0.8192 -0.0023 -0.0697 0.0962  288 ILE A C   
2142  O O   . ILE A 288 ? 1.0192 1.0244 0.9570 -0.0077 -0.0779 0.0959  288 ILE A O   
2143  C CB  . ILE A 288 ? 0.6645 0.6308 0.5986 0.0002  -0.0448 0.0952  288 ILE A CB  
2144  C CG1 . ILE A 288 ? 0.7334 0.6878 0.6708 0.0068  -0.0312 0.1017  288 ILE A CG1 
2145  C CG2 . ILE A 288 ? 0.7497 0.7026 0.6687 -0.0058 -0.0465 0.0769  288 ILE A CG2 
2146  C CD1 . ILE A 288 ? 0.5933 0.5342 0.5489 0.0046  -0.0259 0.1007  288 ILE A CD1 
2147  N N   . LYS A 289 ? 1.1357 1.1310 1.0134 -0.0021 -0.0752 0.0897  289 LYS A N   
2148  C CA  . LYS A 289 ? 1.3316 1.3377 1.1994 -0.0093 -0.0948 0.0809  289 LYS A CA  
2149  C C   . LYS A 289 ? 1.3623 1.3499 1.2142 -0.0172 -0.0948 0.0582  289 LYS A C   
2150  O O   . LYS A 289 ? 1.4560 1.4270 1.2789 -0.0123 -0.0833 0.0501  289 LYS A O   
2151  C CB  . LYS A 289 ? 1.3240 1.3409 1.1581 -0.0038 -0.1043 0.0894  289 LYS A CB  
2152  C CG  . LYS A 289 ? 1.3760 1.4029 1.2191 0.0056  -0.1012 0.1136  289 LYS A CG  
2153  C CD  . LYS A 289 ? 1.3707 1.4158 1.2522 0.0061  -0.1145 0.1242  289 LYS A CD  
2154  C CE  . LYS A 289 ? 1.4685 1.5125 1.3684 0.0153  -0.1051 0.1442  289 LYS A CE  
2155  N NZ  . LYS A 289 ? 1.2085 1.2552 1.1521 0.0149  -0.1010 0.1443  289 LYS A NZ  
2156  N N   . ILE A 290 ? 1.1903 1.1800 1.0634 -0.0295 -0.1062 0.0478  290 ILE A N   
2157  C CA  . ILE A 290 ? 1.4357 1.4028 1.2952 -0.0390 -0.1076 0.0259  290 ILE A CA  
2158  C C   . ILE A 290 ? 1.6469 1.6189 1.4754 -0.0454 -0.1281 0.0131  290 ILE A C   
2159  O O   . ILE A 290 ? 1.6415 1.6397 1.4798 -0.0488 -0.1469 0.0202  290 ILE A O   
2160  C CB  . ILE A 290 ? 1.3252 1.2878 1.2238 -0.0515 -0.1072 0.0222  290 ILE A CB  
2161  C CG1 . ILE A 290 ? 1.2036 1.1585 1.1250 -0.0443 -0.0875 0.0349  290 ILE A CG1 
2162  C CG2 . ILE A 290 ? 1.4955 1.4301 1.3800 -0.0633 -0.1104 -0.0002 290 ILE A CG2 
2163  C CD1 . ILE A 290 ? 0.9523 0.8808 0.8520 -0.0337 -0.0701 0.0321  290 ILE A CD1 
2164  N N   . LYS A 291 ? 1.7747 1.7208 1.5643 -0.0458 -0.1251 -0.0064 291 LYS A N   
2165  C CA  . LYS A 291 ? 1.9530 1.8972 1.7030 -0.0517 -0.1441 -0.0222 291 LYS A CA  
2166  C C   . LYS A 291 ? 1.9335 1.8852 1.7083 -0.0714 -0.1678 -0.0333 291 LYS A C   
2167  O O   . LYS A 291 ? 1.7573 1.7304 1.5246 -0.0773 -0.1919 -0.0336 291 LYS A O   
2168  C CB  . LYS A 291 ? 2.0838 1.9935 1.7871 -0.0465 -0.1319 -0.0432 291 LYS A CB  
2169  C CG  . LYS A 291 ? 1.9720 1.8757 1.6585 -0.0278 -0.1051 -0.0340 291 LYS A CG  
2170  C CD  . LYS A 291 ? 1.6655 1.5948 1.3363 -0.0177 -0.1033 -0.0129 291 LYS A CD  
2171  C CE  . LYS A 291 ? 1.8861 1.8171 1.5018 -0.0174 -0.1160 -0.0207 291 LYS A CE  
2172  N NZ  . LYS A 291 ? 1.8369 1.7401 1.4050 -0.0113 -0.1022 -0.0429 291 LYS A NZ  
2173  N N   . ILE A 292 ? 2.1125 2.0477 1.9183 -0.0820 -0.1613 -0.0408 292 ILE A N   
2174  C CA  . ILE A 292 ? 2.0767 2.0186 1.9133 -0.1035 -0.1802 -0.0503 292 ILE A CA  
2175  C C   . ILE A 292 ? 1.9831 1.9682 1.8713 -0.1055 -0.1875 -0.0294 292 ILE A C   
2176  O O   . ILE A 292 ? 2.0268 2.0190 1.9404 -0.0956 -0.1695 -0.0119 292 ILE A O   
2177  C CB  . ILE A 292 ? 2.0668 1.9735 1.9187 -0.1137 -0.1670 -0.0617 292 ILE A CB  
2178  C CG1 . ILE A 292 ? 1.9617 1.8222 1.7643 -0.1075 -0.1574 -0.0826 292 ILE A CG1 
2179  C CG2 . ILE A 292 ? 1.9751 1.8896 1.8637 -0.1390 -0.1845 -0.0698 292 ILE A CG2 
2180  C CD1 . ILE A 292 ? 1.6956 1.5427 1.4512 -0.1143 -0.1773 -0.1068 292 ILE A CD1 
2181  N N   . THR A 293 ? 1.6577 1.6717 1.5617 -0.1175 -0.2145 -0.0320 293 THR A N   
2182  C CA  . THR A 293 ? 1.6268 1.6850 1.5833 -0.1176 -0.2224 -0.0133 293 THR A CA  
2183  C C   . THR A 293 ? 1.5420 1.6153 1.5476 -0.1409 -0.2344 -0.0213 293 THR A C   
2184  O O   . THR A 293 ? 1.6018 1.6496 1.6193 -0.1526 -0.2205 -0.0296 293 THR A O   
2185  C CB  . THR A 293 ? 1.6577 1.7448 1.5964 -0.1077 -0.2444 -0.0039 293 THR A CB  
2186  O OG1 . THR A 293 ? 1.8022 1.8702 1.6904 -0.0894 -0.2311 0.0022  293 THR A OG1 
2187  C CG2 . THR A 293 ? 1.6180 1.7489 1.6100 -0.1016 -0.2504 0.0176  293 THR A CG2 
2188  N N   . PRO A 296 ? 1.5638 1.7124 1.7735 -0.2523 -0.2890 -0.0541 296 PRO A N   
2189  C CA  . PRO A 296 ? 1.6070 1.8042 1.8958 -0.2701 -0.2923 -0.0453 296 PRO A CA  
2190  C C   . PRO A 296 ? 1.7846 1.9996 2.0949 -0.3002 -0.3279 -0.0634 296 PRO A C   
2191  O O   . PRO A 296 ? 1.7862 2.0488 2.1667 -0.3169 -0.3352 -0.0573 296 PRO A O   
2192  C CB  . PRO A 296 ? 1.6241 1.8743 1.9405 -0.2463 -0.2954 -0.0242 296 PRO A CB  
2193  C CG  . PRO A 296 ? 1.6024 1.8442 1.8585 -0.2308 -0.3188 -0.0300 296 PRO A CG  
2194  C CD  . PRO A 296 ? 1.5637 1.7391 1.7500 -0.2303 -0.3061 -0.0461 296 PRO A CD  
2195  N N   . ILE A 297 ? 1.9948 2.1720 2.2453 -0.3067 -0.3490 -0.0861 297 ILE A N   
2196  C CA  . ILE A 297 ? 2.2650 2.4538 2.5255 -0.3359 -0.3882 -0.1069 297 ILE A CA  
2197  C C   . ILE A 297 ? 2.3957 2.5149 2.6097 -0.3551 -0.3864 -0.1332 297 ILE A C   
2198  O O   . ILE A 297 ? 2.4113 2.4807 2.5533 -0.3370 -0.3761 -0.1423 297 ILE A O   
2199  C CB  . ILE A 297 ? 2.3274 2.5443 2.5555 -0.3225 -0.4236 -0.1093 297 ILE A CB  
2200  C CG1 . ILE A 297 ? 2.4859 2.6906 2.6853 -0.3470 -0.4645 -0.1375 297 ILE A CG1 
2201  C CG2 . ILE A 297 ? 2.1270 2.3156 2.2857 -0.2882 -0.4069 -0.1019 297 ILE A CG2 
2202  C CD1 . ILE A 297 ? 2.4505 2.6807 2.6103 -0.3332 -0.5008 -0.1387 297 ILE A CD1 
2203  N N   . PRO A 298 ? 2.4034 2.5162 2.6566 -0.3906 -0.3951 -0.1455 298 PRO A N   
2204  C CA  . PRO A 298 ? 2.4968 2.5379 2.7090 -0.4092 -0.3923 -0.1700 298 PRO A CA  
2205  C C   . PRO A 298 ? 2.6198 2.6195 2.7482 -0.4022 -0.4152 -0.1967 298 PRO A C   
2206  O O   . PRO A 298 ? 2.8637 2.7974 2.9376 -0.3963 -0.3988 -0.2108 298 PRO A O   
2207  C CB  . PRO A 298 ? 2.1218 2.1817 2.3978 -0.4519 -0.4118 -0.1788 298 PRO A CB  
2208  C CG  . PRO A 298 ? 1.9870 2.1337 2.3262 -0.4535 -0.4356 -0.1645 298 PRO A CG  
2209  C CD  . PRO A 298 ? 2.0836 2.2585 2.4246 -0.4152 -0.4091 -0.1369 298 PRO A CD  
2210  N N   . VAL A 299 ? 2.4772 2.5155 2.5958 -0.4019 -0.4518 -0.2026 299 VAL A N   
2211  C CA  . VAL A 299 ? 2.3494 2.3481 2.3830 -0.3977 -0.4755 -0.2300 299 VAL A CA  
2212  C C   . VAL A 299 ? 2.4006 2.3788 2.3679 -0.3580 -0.4523 -0.2214 299 VAL A C   
2213  O O   . VAL A 299 ? 2.3057 2.3228 2.2990 -0.3354 -0.4351 -0.1931 299 VAL A O   
2214  C CB  . VAL A 299 ? 2.1799 2.2251 2.2212 -0.4124 -0.5254 -0.2392 299 VAL A CB  
2215  C CG1 . VAL A 299 ? 2.2866 2.4071 2.4286 -0.4293 -0.5381 -0.2195 299 VAL A CG1 
2216  C CG2 . VAL A 299 ? 2.2729 2.3316 2.2520 -0.3821 -0.5377 -0.2344 299 VAL A CG2 
2217  N N   . SER A 300 ? 2.2543 2.1735 2.1406 -0.3502 -0.4510 -0.2455 300 SER A N   
2218  C CA  . SER A 300 ? 2.1890 2.0884 2.0121 -0.3145 -0.4279 -0.2390 300 SER A CA  
2219  C C   . SER A 300 ? 2.1635 2.1139 1.9728 -0.2948 -0.4438 -0.2214 300 SER A C   
2220  O O   . SER A 300 ? 2.1238 2.1106 1.9432 -0.3080 -0.4817 -0.2251 300 SER A O   
2221  C CB  . SER A 300 ? 1.9741 1.8052 1.7144 -0.3118 -0.4269 -0.2713 300 SER A CB  
2222  O OG  . SER A 300 ? 2.0891 1.8978 1.7792 -0.2785 -0.3958 -0.2643 300 SER A OG  
2223  N N   . PHE A 301 ? 2.3045 2.2564 2.0912 -0.2635 -0.4154 -0.2014 301 PHE A N   
2224  C CA  . PHE A 301 ? 2.2577 2.2499 2.0275 -0.2419 -0.4243 -0.1810 301 PHE A CA  
2225  C C   . PHE A 301 ? 2.3548 2.3119 2.0508 -0.2145 -0.3988 -0.1813 301 PHE A C   
2226  O O   . PHE A 301 ? 2.3161 2.2567 2.0205 -0.1995 -0.3629 -0.1699 301 PHE A O   
2227  C CB  . PHE A 301 ? 2.0658 2.1090 1.9101 -0.2333 -0.4119 -0.1476 301 PHE A CB  
2228  C CG  . PHE A 301 ? 1.9450 2.0262 1.7792 -0.2096 -0.4178 -0.1230 301 PHE A CG  
2229  C CD1 . PHE A 301 ? 1.8980 1.9646 1.6993 -0.1829 -0.3881 -0.1075 301 PHE A CD1 
2230  C CD2 . PHE A 301 ? 1.9471 2.0794 1.8107 -0.2144 -0.4529 -0.1136 301 PHE A CD2 
2231  C CE1 . PHE A 301 ? 1.8441 1.9411 1.6364 -0.1626 -0.3930 -0.0836 301 PHE A CE1 
2232  C CE2 . PHE A 301 ? 1.9788 2.1417 1.8332 -0.1916 -0.4583 -0.0892 301 PHE A CE2 
2233  C CZ  . PHE A 301 ? 1.8775 2.0204 1.6951 -0.1664 -0.4277 -0.0742 301 PHE A CZ  
2234  N N   . ALA A 302 ? 2.2089 2.1552 1.8323 -0.2084 -0.4172 -0.1943 302 ALA A N   
2235  C CA  . ALA A 302 ? 1.9965 1.9124 1.5481 -0.1835 -0.3921 -0.1952 302 ALA A CA  
2236  C C   . ALA A 302 ? 2.1191 2.0400 1.5982 -0.1776 -0.4179 -0.2013 302 ALA A C   
2237  O O   . ALA A 302 ? 2.1821 2.1173 1.6571 -0.1955 -0.4576 -0.2135 302 ALA A O   
2238  C CB  . ALA A 302 ? 1.8011 1.6565 1.3203 -0.1848 -0.3692 -0.2222 302 ALA A CB  
2239  N N   . ALA A 303 ? 2.4158 2.3290 1.8425 -0.5618 -0.3496 0.3491  303 ALA A N   
2240  C CA  . ALA A 303 ? 2.4090 2.3163 1.8861 -0.5390 -0.3352 0.3243  303 ALA A CA  
2241  C C   . ALA A 303 ? 2.5004 2.4177 2.0627 -0.4903 -0.3366 0.3387  303 ALA A C   
2242  O O   . ALA A 303 ? 2.4402 2.3428 2.0412 -0.4671 -0.3189 0.3165  303 ALA A O   
2243  C CB  . ALA A 303 ? 2.2512 2.2045 1.7335 -0.5608 -0.3542 0.3197  303 ALA A CB  
2244  N N   . ALA A 304 ? 2.4274 2.3674 2.0166 -0.4750 -0.3570 0.3755  304 ALA A N   
2245  C CA  . ALA A 304 ? 2.3117 2.2552 1.9778 -0.4305 -0.3577 0.3895  304 ALA A CA  
2246  C C   . ALA A 304 ? 2.2864 2.1725 1.9577 -0.4113 -0.3244 0.3687  304 ALA A C   
2247  O O   . ALA A 304 ? 2.3106 2.1928 2.0435 -0.3774 -0.3165 0.3630  304 ALA A O   
2248  C CB  . ALA A 304 ? 2.1765 2.1477 1.8591 -0.4213 -0.3848 0.4350  304 ALA A CB  
2249  N N   . PHE A 305 ? 2.2904 2.1356 1.8976 -0.4335 -0.3046 0.3565  305 PHE A N   
2250  C CA  . PHE A 305 ? 2.2240 2.0216 1.8328 -0.4187 -0.2726 0.3365  305 PHE A CA  
2251  C C   . PHE A 305 ? 2.2688 2.0428 1.8667 -0.4182 -0.2461 0.2951  305 PHE A C   
2252  O O   . PHE A 305 ? 2.2563 1.9927 1.8351 -0.4149 -0.2179 0.2750  305 PHE A O   
2253  C CB  . PHE A 305 ? 2.2382 2.0072 1.7858 -0.4407 -0.2628 0.3461  305 PHE A CB  
2254  C CG  . PHE A 305 ? 2.2683 2.0580 1.8143 -0.4449 -0.2890 0.3899  305 PHE A CG  
2255  C CD1 . PHE A 305 ? 2.2292 2.0518 1.7346 -0.4722 -0.3156 0.4100  305 PHE A CD1 
2256  C CD2 . PHE A 305 ? 2.3420 2.1183 1.9266 -0.4216 -0.2875 0.4116  305 PHE A CD2 
2257  C CE1 . PHE A 305 ? 2.1054 1.9501 1.6094 -0.4731 -0.3411 0.4535  305 PHE A CE1 
2258  C CE2 . PHE A 305 ? 2.2730 2.0639 1.8550 -0.4230 -0.3111 0.4550  305 PHE A CE2 
2259  C CZ  . PHE A 305 ? 2.2172 2.0435 1.7589 -0.4472 -0.3383 0.4768  305 PHE A CZ  
2260  N N   . GLU A 306 ? 2.2464 2.0437 1.8574 -0.4208 -0.2546 0.2837  306 GLU A N   
2261  C CA  . GLU A 306 ? 2.2231 1.9966 1.8234 -0.4193 -0.2308 0.2481  306 GLU A CA  
2262  C C   . GLU A 306 ? 2.2006 1.9686 1.8646 -0.3798 -0.2161 0.2353  306 GLU A C   
2263  O O   . GLU A 306 ? 2.2763 2.0129 1.9290 -0.3713 -0.1891 0.2087  306 GLU A O   
2264  C CB  . GLU A 306 ? 2.1874 1.9881 1.7788 -0.4390 -0.2451 0.2427  306 GLU A CB  
2265  C CG  . GLU A 306 ? 2.2178 1.9832 1.7736 -0.4486 -0.2197 0.2082  306 GLU A CG  
2266  C CD  . GLU A 306 ? 2.1477 1.9376 1.6986 -0.4693 -0.2318 0.2023  306 GLU A CD  
2267  O OE1 . GLU A 306 ? 2.1528 1.9933 1.7209 -0.4818 -0.2618 0.2248  306 GLU A OE1 
2268  O OE2 . GLU A 306 ? 2.0693 1.8288 1.5995 -0.4729 -0.2107 0.1760  306 GLU A OE2 
2269  N N   . GLY A 307 ? 2.0109 1.8101 1.7402 -0.3554 -0.2336 0.2538  307 GLY A N   
2270  C CA  . GLY A 307 ? 1.8294 1.6272 1.6203 -0.3195 -0.2222 0.2420  307 GLY A CA  
2271  C C   . GLY A 307 ? 1.8291 1.5911 1.6158 -0.3086 -0.1974 0.2296  307 GLY A C   
2272  O O   . GLY A 307 ? 1.6474 1.3947 1.4426 -0.2942 -0.1759 0.2034  307 GLY A O   
2273  N N   . GLU A 308 ? 1.8246 1.5752 1.5965 -0.3167 -0.2004 0.2494  308 GLU A N   
2274  C CA  . GLU A 308 ? 1.7845 1.5048 1.5513 -0.3109 -0.1761 0.2390  308 GLU A CA  
2275  C C   . GLU A 308 ? 1.7385 1.4467 1.4690 -0.3312 -0.1813 0.2646  308 GLU A C   
2276  O O   . GLU A 308 ? 1.7823 1.5044 1.4812 -0.3515 -0.2019 0.2854  308 GLU A O   
2277  C CB  . GLU A 308 ? 1.8109 1.5356 1.6464 -0.2792 -0.1712 0.2333  308 GLU A CB  
2278  C CG  . GLU A 308 ? 1.7880 1.5008 1.6319 -0.2651 -0.1443 0.2002  308 GLU A CG  
2279  C CD  . GLU A 308 ? 1.7516 1.4781 1.6626 -0.2350 -0.1428 0.1890  308 GLU A CD  
2280  O OE1 . GLU A 308 ? 1.6447 1.3691 1.5917 -0.2260 -0.1467 0.2008  308 GLU A OE1 
2281  O OE2 . GLU A 308 ? 1.8214 1.5587 1.7461 -0.2216 -0.1370 0.1684  308 GLU A OE2 
2282  N N   . ASN A 313 ? 1.8721 1.4717 1.9028 -0.2540 -0.0932 0.2506  313 ASN A N   
2283  C CA  . ASN A 313 ? 2.1083 1.6987 2.0828 -0.2806 -0.0828 0.2624  313 ASN A CA  
2284  C C   . ASN A 313 ? 2.1283 1.7379 2.0861 -0.2860 -0.0595 0.2293  313 ASN A C   
2285  O O   . ASN A 313 ? 2.2721 1.9046 2.2424 -0.2699 -0.0587 0.2043  313 ASN A O   
2286  C CB  . ASN A 313 ? 2.3036 1.8963 2.2314 -0.2890 -0.1026 0.2893  313 ASN A CB  
2287  C CG  . ASN A 313 ? 2.4075 1.9827 2.3421 -0.2868 -0.1243 0.3296  313 ASN A CG  
2288  O OD1 . ASN A 313 ? 2.3309 1.8840 2.3038 -0.2781 -0.1234 0.3392  313 ASN A OD1 
2289  N ND2 . ASN A 313 ? 2.2051 1.7896 2.1016 -0.2946 -0.1443 0.3544  313 ASN A ND2 
2290  N N   . ASP A 314 ? 2.1739 1.7749 2.1032 -0.3077 -0.0397 0.2306  314 ASP A N   
2291  C CA  . ASP A 314 ? 2.2244 1.8451 2.1380 -0.3118 -0.0152 0.2017  314 ASP A CA  
2292  C C   . ASP A 314 ? 2.1801 1.7967 2.0249 -0.3291 -0.0105 0.2098  314 ASP A C   
2293  O O   . ASP A 314 ? 2.0467 1.6474 1.8572 -0.3411 -0.0269 0.2382  314 ASP A O   
2294  C CB  . ASP A 314 ? 2.2583 1.8789 2.1945 -0.3239 0.0069  0.1932  314 ASP A CB  
2295  C CG  . ASP A 314 ? 2.2035 1.8553 2.1414 -0.3215 0.0318  0.1605  314 ASP A CG  
2296  O OD1 . ASP A 314 ? 1.9759 1.6515 1.9336 -0.2992 0.0308  0.1363  314 ASP A OD1 
2297  O OD2 . ASP A 314 ? 2.0216 1.6757 1.9410 -0.3410 0.0528  0.1605  314 ASP A OD2 
2298  N N   . MET A 315 ? 2.2491 1.8810 2.0745 -0.3299 0.0125  0.1847  315 MET A N   
2299  C CA  . MET A 315 ? 2.1894 1.8142 1.9468 -0.3454 0.0211  0.1865  315 MET A CA  
2300  C C   . MET A 315 ? 2.1763 1.7993 1.9079 -0.3664 0.0474  0.1870  315 MET A C   
2301  O O   . MET A 315 ? 2.2556 1.8960 2.0250 -0.3619 0.0656  0.1705  315 MET A O   
2302  C CB  . MET A 315 ? 2.2446 1.8827 1.9917 -0.3283 0.0298  0.1577  315 MET A CB  
2303  C CG  . MET A 315 ? 2.1517 1.8156 1.9431 -0.3082 0.0489  0.1284  315 MET A CG  
2304  S SD  . MET A 315 ? 2.2401 1.9191 2.0585 -0.2762 0.0398  0.1060  315 MET A SD  
2305  C CE  . MET A 315 ? 2.0169 1.7294 1.8660 -0.2575 0.0682  0.0744  315 MET A CE  
2306  N N   . LEU A 316 ? 2.1985 1.8048 1.8677 -0.3897 0.0493  0.2047  316 LEU A N   
2307  C CA  . LEU A 316 ? 2.2257 1.8308 1.8625 -0.4115 0.0758  0.2059  316 LEU A CA  
2308  C C   . LEU A 316 ? 2.2716 1.8945 1.8931 -0.4021 0.1038  0.1722  316 LEU A C   
2309  O O   . LEU A 316 ? 2.2183 1.8604 1.8575 -0.4032 0.1295  0.1581  316 LEU A O   
2310  C CB  . LEU A 316 ? 2.1556 1.7379 1.7243 -0.4388 0.0674  0.2354  316 LEU A CB  
2311  C CG  . LEU A 316 ? 2.2947 1.8695 1.8304 -0.4668 0.0877  0.2510  316 LEU A CG  
2312  C CD1 . LEU A 316 ? 2.2825 1.8703 1.7839 -0.4725 0.1220  0.2246  316 LEU A CD1 
2313  C CD2 . LEU A 316 ? 2.3382 1.9121 1.9268 -0.4696 0.0917  0.2622  316 LEU A CD2 
2314  N N   . ALA A 317 ? 2.4148 2.0316 2.0046 -0.3925 0.0993  0.1597  317 ALA A N   
2315  C CA  . ALA A 317 ? 2.3813 2.0069 1.9523 -0.3798 0.1256  0.1293  317 ALA A CA  
2316  C C   . ALA A 317 ? 2.4227 2.0462 2.0033 -0.3558 0.1136  0.1135  317 ALA A C   
2317  O O   . ALA A 317 ? 2.3840 1.9906 1.9441 -0.3617 0.0896  0.1261  317 ALA A O   
2318  C CB  . ALA A 317 ? 2.3780 1.9846 1.8715 -0.4027 0.1423  0.1309  317 ALA A CB  
2319  N N   . GLU A 318 ? 2.3565 2.0001 1.9693 -0.3292 0.1300  0.0875  318 GLU A N   
2320  C CA  . GLU A 318 ? 2.2682 1.9068 1.8847 -0.3060 0.1223  0.0725  318 GLU A CA  
2321  C C   . GLU A 318 ? 2.2294 1.8592 1.8055 -0.2955 0.1519  0.0494  318 GLU A C   
2322  O O   . GLU A 318 ? 2.2118 1.8606 1.7942 -0.2909 0.1785  0.0384  318 GLU A O   
2323  C CB  . GLU A 318 ? 2.1715 1.8387 1.8600 -0.2791 0.1132  0.0633  318 GLU A CB  
2324  C CG  . GLU A 318 ? 2.1955 1.8625 1.8865 -0.2520 0.1153  0.0442  318 GLU A CG  
2325  C CD  . GLU A 318 ? 2.1876 1.8885 1.9458 -0.2247 0.1104  0.0325  318 GLU A CD  
2326  O OE1 . GLU A 318 ? 1.9971 1.7290 1.7925 -0.2202 0.1225  0.0254  318 GLU A OE1 
2327  O OE2 . GLU A 318 ? 2.2503 1.9491 2.0229 -0.2098 0.0947  0.0302  318 GLU A OE2 
2328  N N   . PHE A 319 ? 2.1888 1.7905 1.7253 -0.2924 0.1484  0.0425  319 PHE A N   
2329  C CA  . PHE A 319 ? 2.0430 1.6255 1.5350 -0.2816 0.1783  0.0204  319 PHE A CA  
2330  C C   . PHE A 319 ? 1.9841 1.5523 1.4797 -0.2575 0.1745  0.0073  319 PHE A C   
2331  O O   . PHE A 319 ? 1.9473 1.5014 1.4380 -0.2667 0.1489  0.0170  319 PHE A O   
2332  C CB  . PHE A 319 ? 2.2836 1.8289 1.6953 -0.3122 0.1859  0.0235  319 PHE A CB  
2333  C CG  . PHE A 319 ? 2.3797 1.9308 1.7737 -0.3434 0.1821  0.0434  319 PHE A CG  
2334  C CD1 . PHE A 319 ? 2.2555 1.8072 1.6556 -0.3641 0.1494  0.0698  319 PHE A CD1 
2335  C CD2 . PHE A 319 ? 2.4529 2.0086 1.8218 -0.3514 0.2120  0.0371  319 PHE A CD2 
2336  C CE1 . PHE A 319 ? 2.4325 1.9861 1.8123 -0.3917 0.1462  0.0912  319 PHE A CE1 
2337  C CE2 . PHE A 319 ? 2.4172 1.9764 1.7658 -0.3815 0.2095  0.0572  319 PHE A CE2 
2338  C CZ  . PHE A 319 ? 2.4524 2.0087 1.8053 -0.4015 0.1762  0.0851  319 PHE A CZ  
2339  N N   . GLY A 320 ? 2.0454 1.6189 1.5496 -0.2271 0.1995  -0.0126 320 GLY A N   
2340  C CA  . GLY A 320 ? 2.1581 1.7106 1.6566 -0.2040 0.2000  -0.0239 320 GLY A CA  
2341  C C   . GLY A 320 ? 2.0501 1.6401 1.6178 -0.1739 0.1878  -0.0254 320 GLY A C   
2342  O O   . GLY A 320 ? 2.0151 1.6488 1.6311 -0.1595 0.1947  -0.0285 320 GLY A O   
2343  N N   . GLY A 321 ? 2.4629 2.0386 2.0342 -0.1666 0.1711  -0.0241 321 GLY A N   
2344  C CA  . GLY A 321 ? 2.4088 2.0177 2.0393 -0.1384 0.1598  -0.0264 321 GLY A CA  
2345  C C   . GLY A 321 ? 2.3997 2.0353 2.0534 -0.1038 0.1844  -0.0410 321 GLY A C   
2346  O O   . GLY A 321 ? 2.4904 2.0997 2.1048 -0.0907 0.2101  -0.0515 321 GLY A O   
2347  N N   . ASN A 322 ? 2.1063 1.7950 1.8235 -0.0890 0.1772  -0.0421 322 ASN A N   
2348  C CA  . ASN A 322 ? 2.1170 1.8445 1.8634 -0.0565 0.1975  -0.0550 322 ASN A CA  
2349  C C   . ASN A 322 ? 2.0277 1.7950 1.7998 -0.0674 0.2080  -0.0565 322 ASN A C   
2350  O O   . ASN A 322 ? 2.0652 1.8859 1.8857 -0.0478 0.2136  -0.0646 322 ASN A O   
2351  C CB  . ASN A 322 ? 2.1026 1.8669 1.9012 -0.0306 0.1824  -0.0580 322 ASN A CB  
2352  C CG  . ASN A 322 ? 2.3255 2.1170 2.1377 0.0099  0.2015  -0.0693 322 ASN A CG  
2353  O OD1 . ASN A 322 ? 2.4455 2.2275 2.2303 0.0226  0.2282  -0.0755 322 ASN A OD1 
2354  N ND2 . ASN A 322 ? 2.2267 2.0539 2.0809 0.0323  0.1887  -0.0719 322 ASN A ND2 
2355  N N   . LYS A 323 ? 1.9172 1.6611 1.6558 -0.1001 0.2110  -0.0485 323 LYS A N   
2356  C CA  . LYS A 323 ? 1.8813 1.6578 1.6383 -0.1155 0.2225  -0.0479 323 LYS A CA  
2357  C C   . LYS A 323 ? 2.1458 1.9001 1.8489 -0.1221 0.2528  -0.0530 323 LYS A C   
2358  O O   . LYS A 323 ? 2.0328 1.8241 1.7532 -0.1111 0.2762  -0.0623 323 LYS A O   
2359  C CB  . LYS A 323 ? 1.8360 1.6081 1.6055 -0.1499 0.1989  -0.0308 323 LYS A CB  
2360  C CG  . LYS A 323 ? 1.8877 1.6995 1.6931 -0.1647 0.2065  -0.0294 323 LYS A CG  
2361  C CD  . LYS A 323 ? 1.7117 1.5142 1.5338 -0.1935 0.1822  -0.0110 323 LYS A CD  
2362  C CE  . LYS A 323 ? 1.5715 1.3984 1.4131 -0.2157 0.1935  -0.0068 323 LYS A CE  
2363  N NZ  . LYS A 323 ? 1.5571 1.3664 1.4114 -0.2419 0.1713  0.0134  323 LYS A NZ  
2364  N N   . THR A 324 ? 2.3099 2.0071 1.9491 -0.1396 0.2524  -0.0485 324 THR A N   
2365  C CA  . THR A 324 ? 2.2798 1.9493 1.8599 -0.1463 0.2828  -0.0562 324 THR A CA  
2366  C C   . THR A 324 ? 2.3132 1.9230 1.8345 -0.1396 0.2885  -0.0632 324 THR A C   
2367  O O   . THR A 324 ? 2.3521 1.9417 1.8745 -0.1412 0.2646  -0.0572 324 THR A O   
2368  C CB  . THR A 324 ? 2.3332 1.9939 1.8847 -0.1875 0.2805  -0.0435 324 THR A CB  
2369  O OG1 . THR A 324 ? 2.2629 1.8925 1.7950 -0.2129 0.2497  -0.0274 324 THR A OG1 
2370  C CG2 . THR A 324 ? 2.2257 1.9404 1.8323 -0.1945 0.2805  -0.0379 324 THR A CG2 
2371  N N   . LYS A 325 ? 2.3637 1.9458 1.8354 -0.1328 0.3212  -0.0765 325 LYS A N   
2372  C CA  . LYS A 325 ? 2.3486 1.8660 1.7594 -0.1266 0.3320  -0.0863 325 LYS A CA  
2373  C C   . LYS A 325 ? 2.4879 1.9565 1.8304 -0.1710 0.3246  -0.0814 325 LYS A C   
2374  O O   . LYS A 325 ? 2.5749 2.0254 1.8692 -0.1851 0.3492  -0.0891 325 LYS A O   
2375  C CB  . LYS A 325 ? 2.3061 1.8128 1.6961 -0.0937 0.3731  -0.1046 325 LYS A CB  
2376  C CG  . LYS A 325 ? 2.2173 1.7853 1.6748 -0.0500 0.3832  -0.1087 325 LYS A CG  
2377  C CD  . LYS A 325 ? 2.2228 1.7879 1.6618 -0.0176 0.4253  -0.1245 325 LYS A CD  
2378  C CE  . LYS A 325 ? 2.1772 1.7240 1.5656 -0.0437 0.4502  -0.1313 325 LYS A CE  
2379  N NZ  . LYS A 325 ? 2.3720 1.8744 1.7100 -0.0177 0.4908  -0.1491 325 LYS A NZ  
2380  N N   . ALA A 326 ? 2.6689 2.1211 2.0074 -0.1921 0.2922  -0.0693 326 ALA A N   
2381  C CA  . ALA A 326 ? 2.7650 2.1753 2.0376 -0.2347 0.2820  -0.0642 326 ALA A CA  
2382  C C   . ALA A 326 ? 2.7702 2.1232 1.9955 -0.2342 0.2848  -0.0753 326 ALA A C   
2383  O O   . ALA A 326 ? 2.6508 2.0024 1.9055 -0.2021 0.2866  -0.0803 326 ALA A O   
2384  C CB  . ALA A 326 ? 2.8241 2.2615 2.1250 -0.2616 0.2438  -0.0408 326 ALA A CB  
2385  N N   . TRP A 327 ? 2.8354 2.1432 1.9885 -0.2701 0.2855  -0.0789 327 TRP A N   
2386  C CA  . TRP A 327 ? 2.8248 2.0719 1.9260 -0.2755 0.2912  -0.0919 327 TRP A CA  
2387  C C   . TRP A 327 ? 2.8693 2.0870 1.9047 -0.3267 0.2763  -0.0894 327 TRP A C   
2388  O O   . TRP A 327 ? 2.9855 2.2164 1.9966 -0.3519 0.2763  -0.0838 327 TRP A O   
2389  C CB  . TRP A 327 ? 2.7795 1.9833 1.8455 -0.2469 0.3352  -0.1156 327 TRP A CB  
2390  C CG  . TRP A 327 ? 2.8943 2.0888 1.9146 -0.2593 0.3632  -0.1262 327 TRP A CG  
2391  C CD1 . TRP A 327 ? 2.9479 2.1899 2.0013 -0.2461 0.3763  -0.1232 327 TRP A CD1 
2392  C CD2 . TRP A 327 ? 3.0710 2.2075 2.0020 -0.2921 0.3810  -0.1418 327 TRP A CD2 
2393  N NE1 . TRP A 327 ? 3.0661 2.2840 2.0575 -0.2659 0.4027  -0.1353 327 TRP A NE1 
2394  C CE2 . TRP A 327 ? 3.0726 2.2250 1.9869 -0.2940 0.4060  -0.1475 327 TRP A CE2 
2395  C CE3 . TRP A 327 ? 3.1012 2.1748 1.9637 -0.3217 0.3794  -0.1529 327 TRP A CE3 
2396  C CZ2 . TRP A 327 ? 3.0901 2.1968 1.9202 -0.3228 0.4294  -0.1641 327 TRP A CZ2 
2397  C CZ3 . TRP A 327 ? 3.0795 2.1070 1.8586 -0.3518 0.4016  -0.1704 327 TRP A CZ3 
2398  C CH2 . TRP A 327 ? 3.0767 2.1201 1.8389 -0.3515 0.4264  -0.1761 327 TRP A CH2 
2399  N N   . GLU A 328 ? 2.5579 1.7401 1.5653 -0.3430 0.2638  -0.0927 328 GLU A N   
2400  C CA  . GLU A 328 ? 2.6187 1.7757 1.5600 -0.3943 0.2494  -0.0925 328 GLU A CA  
2401  C C   . GLU A 328 ? 2.7820 1.8640 1.6527 -0.4040 0.2737  -0.1176 328 GLU A C   
2402  O O   . GLU A 328 ? 2.8226 1.8806 1.7118 -0.3744 0.2850  -0.1251 328 GLU A O   
2403  C CB  . GLU A 328 ? 2.5885 1.7873 1.5675 -0.4153 0.2035  -0.0683 328 GLU A CB  
2404  C CG  . GLU A 328 ? 2.6835 1.8652 1.6722 -0.4140 0.1907  -0.0706 328 GLU A CG  
2405  C CD  . GLU A 328 ? 2.5493 1.7796 1.5785 -0.4334 0.1464  -0.0463 328 GLU A CD  
2406  O OE1 . GLU A 328 ? 2.4428 1.7181 1.4991 -0.4403 0.1268  -0.0266 328 GLU A OE1 
2407  O OE2 . GLU A 328 ? 2.4854 1.7080 1.5187 -0.4410 0.1328  -0.0466 328 GLU A OE2 
2408  N N   . LEU A 329 ? 2.8191 1.8641 1.6099 -0.4451 0.2814  -0.1297 329 LEU A N   
2409  C CA  . LEU A 329 ? 2.8096 1.7738 1.5246 -0.4576 0.3097  -0.1577 329 LEU A CA  
2410  C C   . LEU A 329 ? 2.8710 1.8130 1.5074 -0.5175 0.2989  -0.1648 329 LEU A C   
2411  O O   . LEU A 329 ? 3.0206 1.9839 1.6309 -0.5377 0.2983  -0.1611 329 LEU A O   
2412  C CB  . LEU A 329 ? 2.7917 1.7168 1.4829 -0.4234 0.3585  -0.1794 329 LEU A CB  
2413  C CG  . LEU A 329 ? 2.9559 1.7907 1.5556 -0.4396 0.3939  -0.2107 329 LEU A CG  
2414  C CD1 . LEU A 329 ? 2.9443 1.7299 1.5358 -0.4398 0.3914  -0.2169 329 LEU A CD1 
2415  C CD2 . LEU A 329 ? 3.2689 2.0725 1.8528 -0.3999 0.4427  -0.2299 329 LEU A CD2 
2416  N N   . VAL A 330 ? 2.8081 1.7109 1.4072 -0.5465 0.2907  -0.1744 330 VAL A N   
2417  C CA  . VAL A 330 ? 2.9396 1.8204 1.4596 -0.6062 0.2814  -0.1847 330 VAL A CA  
2418  C C   . VAL A 330 ? 3.1713 1.9561 1.6130 -0.6133 0.3229  -0.2207 330 VAL A C   
2419  O O   . VAL A 330 ? 3.2003 1.9454 1.6459 -0.6056 0.3284  -0.2282 330 VAL A O   
2420  C CB  . VAL A 330 ? 2.7424 1.6637 1.2834 -0.6412 0.2347  -0.1661 330 VAL A CB  
2421  C CG1 . VAL A 330 ? 3.0063 1.9056 1.4619 -0.7050 0.2258  -0.1796 330 VAL A CG1 
2422  C CG2 . VAL A 330 ? 2.6364 1.6468 1.2552 -0.6299 0.1960  -0.1302 330 VAL A CG2 
2423  N N   . MET A 331 ? 3.5610 2.3076 1.9304 -0.6292 0.3523  -0.2424 331 MET A N   
2424  C CA  . MET A 331 ? 3.7409 2.3878 2.0299 -0.6348 0.3969  -0.2797 331 MET A CA  
2425  C C   . MET A 331 ? 3.8759 2.4919 2.0693 -0.7023 0.3931  -0.2993 331 MET A C   
2426  O O   . MET A 331 ? 3.7923 2.4542 1.9670 -0.7285 0.3779  -0.2906 331 MET A O   
2427  C CB  . MET A 331 ? 3.7050 2.3237 1.9854 -0.5903 0.4440  -0.2949 331 MET A CB  
2428  C CG  . MET A 331 ? 3.9258 2.4381 2.1281 -0.5877 0.4933  -0.3323 331 MET A CG  
2429  S SD  . MET A 331 ? 3.6979 2.1879 1.9035 -0.5262 0.5489  -0.3472 331 MET A SD  
2430  C CE  . MET A 331 ? 3.5992 2.0895 1.8907 -0.4566 0.5546  -0.3323 331 MET A CE  
2431  N N   . CYS A 332 ? 3.9048 2.4455 2.0385 -0.7305 0.4067  -0.3245 332 CYS A N   
2432  C CA  . CYS A 332 ? 3.7782 2.2829 1.8134 -0.7986 0.4062  -0.3488 332 CYS A CA  
2433  C C   . CYS A 332 ? 3.8930 2.3048 1.8442 -0.7936 0.4632  -0.3882 332 CYS A C   
2434  O O   . CYS A 332 ? 3.9660 2.2960 1.9018 -0.7682 0.4987  -0.4083 332 CYS A O   
2435  C CB  . CYS A 332 ? 3.5878 2.0644 1.6036 -0.8394 0.3881  -0.3556 332 CYS A CB  
2436  S SG  . CYS A 332 ? 4.3399 2.7431 2.2241 -0.9190 0.4024  -0.3974 332 CYS A SG  
2437  N N   . ALA A 333 ? 3.6927 2.1159 1.5915 -0.8152 0.4726  -0.3980 333 ALA A N   
2438  C CA  . ALA A 333 ? 3.4366 1.7885 1.2783 -0.8030 0.5259  -0.4293 333 ALA A CA  
2439  C C   . ALA A 333 ? 3.4997 1.8720 1.2866 -0.8533 0.5204  -0.4361 333 ALA A C   
2440  O O   . ALA A 333 ? 3.7202 2.1648 1.5127 -0.8661 0.4955  -0.4173 333 ALA A O   
2441  C CB  . ALA A 333 ? 3.3293 1.6876 1.2050 -0.7388 0.5585  -0.4275 333 ALA A CB  
2442  N N   . ASP A 334 ? 3.6594 1.9694 1.3942 -0.8803 0.5435  -0.4608 334 ASP A N   
2443  C CA  . ASP A 334 ? 3.9540 2.2803 1.6321 -0.9318 0.5385  -0.4699 334 ASP A CA  
2444  C C   . ASP A 334 ? 4.0916 2.4226 1.7555 -0.9054 0.5713  -0.4781 334 ASP A C   
2445  O O   . ASP A 334 ? 4.0167 2.3830 1.6429 -0.9439 0.5602  -0.4782 334 ASP A O   
2446  C CB  . ASP A 334 ? 3.8895 2.1533 1.5169 -0.9751 0.5486  -0.4926 334 ASP A CB  
2447  C CG  . ASP A 334 ? 3.8131 1.9822 1.4123 -0.9440 0.6067  -0.5215 334 ASP A CG  
2448  O OD1 . ASP A 334 ? 3.8291 1.9532 1.4619 -0.8928 0.6302  -0.5220 334 ASP A OD1 
2449  O OD2 . ASP A 334 ? 3.9098 2.0520 1.4538 -0.9699 0.6277  -0.5424 334 ASP A OD2 
2450  N N   . GLN A 335 ? 4.3629 2.6649 2.0574 -0.8420 0.6098  -0.4837 335 GLN A N   
2451  C CA  . GLN A 335 ? 4.3337 2.6535 2.0227 -0.8157 0.6399  -0.4891 335 GLN A CA  
2452  C C   . GLN A 335 ? 4.3462 2.6897 2.0979 -0.7482 0.6579  -0.4768 335 GLN A C   
2453  O O   . GLN A 335 ? 4.3401 2.7038 2.1392 -0.7293 0.6360  -0.4588 335 GLN A O   
2454  C CB  . GLN A 335 ? 4.3827 2.6236 2.0194 -0.8179 0.6847  -0.5224 335 GLN A CB  
2455  C CG  . GLN A 335 ? 4.3557 2.5834 1.9261 -0.8878 0.6699  -0.5358 335 GLN A CG  
2456  C CD  . GLN A 335 ? 4.4932 2.6366 2.0118 -0.8877 0.7167  -0.5697 335 GLN A CD  
2457  O OE1 . GLN A 335 ? 4.5234 2.6041 2.0563 -0.8392 0.7552  -0.5817 335 GLN A OE1 
2458  N NE2 . GLN A 335 ? 4.7619 2.9041 2.2192 -0.9415 0.7135  -0.5843 335 GLN A NE2 
2459  N N   . GLY A 336 ? 4.0435 2.3887 1.7964 -0.7140 0.6962  -0.4865 336 GLY A N   
2460  C CA  . GLY A 336 ? 3.8826 2.2631 1.6983 -0.6515 0.7142  -0.4741 336 GLY A CA  
2461  C C   . GLY A 336 ? 3.8237 2.2942 1.6592 -0.6622 0.6918  -0.4492 336 GLY A C   
2462  O O   . GLY A 336 ? 3.6533 2.1591 1.5326 -0.6166 0.7140  -0.4421 336 GLY A O   
2463  N N   . GLU A 337 ? 4.0616 2.5704 1.8677 -0.7202 0.6495  -0.4345 337 GLU A N   
2464  C CA  . GLU A 337 ? 4.0770 2.6709 1.8994 -0.7343 0.6244  -0.4050 337 GLU A CA  
2465  C C   . GLU A 337 ? 4.1213 2.7419 1.8954 -0.8016 0.5833  -0.3946 337 GLU A C   
2466  O O   . GLU A 337 ? 4.1144 2.6927 1.8523 -0.8350 0.5718  -0.4097 337 GLU A O   
2467  C CB  . GLU A 337 ? 3.9604 2.6087 1.8715 -0.7026 0.5955  -0.3717 337 GLU A CB  
2468  C CG  . GLU A 337 ? 3.8336 2.5721 1.7999 -0.6965 0.5761  -0.3363 337 GLU A CG  
2469  C CD  . GLU A 337 ? 3.8168 2.6144 1.7939 -0.7400 0.5174  -0.3012 337 GLU A CD  
2470  O OE1 . GLU A 337 ? 3.5347 2.3377 1.5466 -0.7457 0.4807  -0.2879 337 GLU A OE1 
2471  O OE2 . GLU A 337 ? 3.7374 2.5760 1.6875 -0.7672 0.5094  -0.2862 337 GLU A OE2 
2472  N N   . VAL A 338 ? 4.3362 3.0264 2.1122 -0.8206 0.5620  -0.3678 338 VAL A N   
2473  C CA  . VAL A 338 ? 4.2803 3.0069 2.0164 -0.8814 0.5183  -0.3518 338 VAL A CA  
2474  C C   . VAL A 338 ? 4.2874 3.0327 2.0462 -0.9004 0.4693  -0.3312 338 VAL A C   
2475  O O   . VAL A 338 ? 4.3485 3.1452 2.1745 -0.8773 0.4448  -0.2982 338 VAL A O   
2476  C CB  . VAL A 338 ? 4.2209 3.0178 1.9596 -0.8917 0.5069  -0.3224 338 VAL A CB  
2477  C CG1 . VAL A 338 ? 4.1618 2.9828 1.8455 -0.9491 0.4782  -0.3161 338 VAL A CG1 
2478  C CG2 . VAL A 338 ? 4.1872 2.9805 1.9349 -0.8538 0.5575  -0.3351 338 VAL A CG2 
2479  N N   . GLU A 339 ? 3.8029 2.5160 1.5273 -0.9379 0.4535  -0.3470 339 GLU A N   
2480  C CA  . GLU A 339 ? 3.5587 2.2949 1.3045 -0.9605 0.4056  -0.3286 339 GLU A CA  
2481  C C   . GLU A 339 ? 3.3463 2.1578 1.0803 -1.0064 0.3553  -0.2964 339 GLU A C   
2482  O O   . GLU A 339 ? 3.4228 2.2315 1.1087 -1.0519 0.3454  -0.3076 339 GLU A O   
2483  C CB  . GLU A 339 ? 3.5054 2.1763 1.2238 -0.9812 0.4132  -0.3588 339 GLU A CB  
2484  C CG  . GLU A 339 ? 3.4135 2.0107 1.1515 -0.9329 0.4562  -0.3834 339 GLU A CG  
2485  C CD  . GLU A 339 ? 3.4754 2.0957 1.2775 -0.8825 0.4539  -0.3640 339 GLU A CD  
2486  O OE1 . GLU A 339 ? 3.5128 2.1682 1.3758 -0.8816 0.4142  -0.3401 339 GLU A OE1 
2487  O OE2 . GLU A 339 ? 3.6546 2.2776 1.4873 -0.8356 0.4860  -0.3639 339 GLU A OE2 
2488  N N   . ASP A 340 ? 3.2621 2.1385 1.0396 -0.9938 0.3255  -0.2563 340 ASP A N   
2489  C CA  . ASP A 340 ? 3.2537 2.2052 1.0272 -1.0309 0.2760  -0.2188 340 ASP A CA  
2490  C C   . ASP A 340 ? 3.2572 2.2770 1.1375 -0.9958 0.2400  -0.1705 340 ASP A C   
2491  O O   . ASP A 340 ? 3.3113 2.3199 1.2696 -0.9471 0.2517  -0.1706 340 ASP A O   
2492  C CB  . ASP A 340 ? 3.3923 2.3598 1.1257 -1.0454 0.2913  -0.2177 340 ASP A CB  
2493  C CG  . ASP A 340 ? 3.6148 2.5742 1.3666 -1.0023 0.3333  -0.2183 340 ASP A CG  
2494  O OD1 . ASP A 340 ? 3.5275 2.4411 1.3018 -0.9628 0.3689  -0.2405 340 ASP A OD1 
2495  O OD2 . ASP A 340 ? 3.6669 2.6681 1.4124 -1.0082 0.3303  -0.1957 340 ASP A OD2 
2496  N N   . HIS A 341 ? 3.5912 2.6789 1.4780 -1.0197 0.1955  -0.1307 341 HIS A N   
2497  C CA  . HIS A 341 ? 3.7566 2.9086 1.7475 -0.9862 0.1606  -0.0826 341 HIS A CA  
2498  C C   . HIS A 341 ? 3.7510 2.9080 1.7583 -0.9569 0.1910  -0.0733 341 HIS A C   
2499  O O   . HIS A 341 ? 3.6063 2.8095 1.6121 -0.9675 0.1720  -0.0384 341 HIS A O   
2500  C CB  . HIS A 341 ? 3.7238 2.9420 1.7098 -1.0214 0.1047  -0.0432 341 HIS A CB  
2501  C CG  . HIS A 341 ? 3.9492 3.2239 2.0412 -0.9895 0.0659  0.0004  341 HIS A CG  
2502  N ND1 . HIS A 341 ? 4.0304 3.3163 2.2024 -0.9408 0.0770  0.0194  341 HIS A ND1 
2503  C CD2 . HIS A 341 ? 3.9412 3.2649 2.0719 -0.9996 0.0173  0.0276  341 HIS A CD2 
2504  C CE1 . HIS A 341 ? 3.9189 3.2533 2.1719 -0.9226 0.0373  0.0554  341 HIS A CE1 
2505  N NE2 . HIS A 341 ? 3.9716 3.3306 2.2025 -0.9559 0.0010  0.0616  341 HIS A NE2 
2506  N N   . LYS A 342 ? 3.5428 2.6537 1.5648 -0.9208 0.2381  -0.1032 342 LYS A N   
2507  C CA  . LYS A 342 ? 3.2515 2.3698 1.2909 -0.8930 0.2715  -0.0984 342 LYS A CA  
2508  C C   . LYS A 342 ? 3.3476 2.5071 1.5051 -0.8486 0.2498  -0.0669 342 LYS A C   
2509  O O   . LYS A 342 ? 3.3045 2.4427 1.5138 -0.8160 0.2574  -0.0820 342 LYS A O   
2510  C CB  . LYS A 342 ? 3.1354 2.1916 1.1360 -0.8746 0.3311  -0.1447 342 LYS A CB  
2511  C CG  . LYS A 342 ? 3.2537 2.3222 1.2683 -0.8488 0.3686  -0.1431 342 LYS A CG  
2512  C CD  . LYS A 342 ? 3.3897 2.3996 1.3648 -0.8289 0.4280  -0.1891 342 LYS A CD  
2513  C CE  . LYS A 342 ? 3.4074 2.4388 1.4024 -0.8029 0.4656  -0.1872 342 LYS A CE  
2514  N NZ  . LYS A 342 ? 3.6673 2.6442 1.6261 -0.7798 0.5243  -0.2319 342 LYS A NZ  
2515  N N   . ILE A 343 ? 3.5530 2.7667 1.7477 -0.8496 0.2224  -0.0243 343 ILE A N   
2516  C CA  . ILE A 343 ? 3.4370 2.6866 1.7426 -0.8070 0.2071  0.0035  343 ILE A CA  
2517  C C   . ILE A 343 ? 3.6242 2.8719 1.9479 -0.7803 0.2496  -0.0038 343 ILE A C   
2518  O O   . ILE A 343 ? 3.8286 3.0943 2.1178 -0.7996 0.2555  0.0128  343 ILE A O   
2519  C CB  . ILE A 343 ? 3.4861 2.7895 1.8241 -0.8202 0.1570  0.0529  343 ILE A CB  
2520  C CG1 . ILE A 343 ? 3.3206 2.6337 1.6225 -0.8553 0.1168  0.0594  343 ILE A CG1 
2521  C CG2 . ILE A 343 ? 3.1992 2.5318 1.6482 -0.7776 0.1427  0.0764  343 ILE A CG2 
2522  C CD1 . ILE A 343 ? 3.5011 2.8418 1.7355 -0.8989 0.0928  0.0855  343 ILE A CD1 
2523  N N   . GLU A 344 ? 3.3261 2.5529 1.6961 -0.7395 0.2795  -0.0289 344 GLU A N   
2524  C CA  . GLU A 344 ? 3.3512 2.5799 1.7385 -0.7129 0.3236  -0.0405 344 GLU A CA  
2525  C C   . GLU A 344 ? 3.2115 2.4678 1.7072 -0.6654 0.3219  -0.0307 344 GLU A C   
2526  O O   . GLU A 344 ? 3.0895 2.3334 1.6262 -0.6424 0.3117  -0.0402 344 GLU A O   
2527  C CB  . GLU A 344 ? 3.1783 2.3532 1.5025 -0.7087 0.3715  -0.0865 344 GLU A CB  
2528  C CG  . GLU A 344 ? 3.1359 2.3167 1.4821 -0.6771 0.4189  -0.1010 344 GLU A CG  
2529  C CD  . GLU A 344 ? 3.1022 2.2290 1.3806 -0.6721 0.4691  -0.1455 344 GLU A CD  
2530  O OE1 . GLU A 344 ? 3.0904 2.1670 1.3344 -0.6748 0.4704  -0.1695 344 GLU A OE1 
2531  O OE2 . GLU A 344 ? 3.3216 2.4553 1.5816 -0.6657 0.5081  -0.1562 344 GLU A OE2 
2532  N N   . VAL A 345 ? 3.2263 2.5189 1.7640 -0.6538 0.3320  -0.0131 345 VAL A N   
2533  C CA  . VAL A 345 ? 3.0127 2.3360 1.6506 -0.6124 0.3327  -0.0056 345 VAL A CA  
2534  C C   . VAL A 345 ? 3.0708 2.3994 1.7141 -0.5907 0.3825  -0.0271 345 VAL A C   
2535  O O   . VAL A 345 ? 3.0992 2.4440 1.7146 -0.6097 0.3988  -0.0182 345 VAL A O   
2536  C CB  . VAL A 345 ? 2.7856 2.1519 1.4778 -0.6196 0.2973  0.0371  345 VAL A CB  
2537  C CG1 . VAL A 345 ? 2.8057 2.2039 1.5962 -0.5810 0.3026  0.0410  345 VAL A CG1 
2538  C CG2 . VAL A 345 ? 2.5813 1.9485 1.2750 -0.6361 0.2482  0.0594  345 VAL A CG2 
2539  N N   . ILE A 346 ? 3.0102 2.3275 1.6881 -0.5509 0.4072  -0.0540 346 ILE A N   
2540  C CA  . ILE A 346 ? 3.0134 2.3420 1.7023 -0.5255 0.4548  -0.0748 346 ILE A CA  
2541  C C   . ILE A 346 ? 2.8629 2.2374 1.6557 -0.4853 0.4537  -0.0680 346 ILE A C   
2542  O O   . ILE A 346 ? 2.7505 2.1170 1.5812 -0.4487 0.4592  -0.0842 346 ILE A O   
2543  C CB  . ILE A 346 ? 3.0292 2.3054 1.6606 -0.5112 0.4931  -0.1146 346 ILE A CB  
2544  C CG1 . ILE A 346 ? 3.1041 2.3312 1.6301 -0.5553 0.4902  -0.1241 346 ILE A CG1 
2545  C CG2 . ILE A 346 ? 3.0458 2.3387 1.6827 -0.4866 0.5444  -0.1343 346 ILE A CG2 
2546  C CD1 . ILE A 346 ? 3.0510 2.2131 1.5223 -0.5450 0.5166  -0.1616 346 ILE A CD1 
2547  N N   . GLY A 347 ? 3.0404 2.4617 1.8759 -0.4939 0.4469  -0.0441 347 GLY A N   
2548  C CA  . GLY A 347 ? 2.9233 2.3929 1.8551 -0.4627 0.4457  -0.0379 347 GLY A CA  
2549  C C   . GLY A 347 ? 2.9733 2.4798 1.9461 -0.4837 0.4214  -0.0041 347 GLY A C   
2550  O O   . GLY A 347 ? 3.0334 2.5269 1.9629 -0.5197 0.4002  0.0189  347 GLY A O   
2551  N N   . PRO A 348 ? 2.8766 2.4292 1.9328 -0.4623 0.4237  0.0002  348 PRO A N   
2552  C CA  . PRO A 348 ? 2.7479 2.3283 1.8428 -0.4834 0.4025  0.0317  348 PRO A CA  
2553  C C   . PRO A 348 ? 2.7549 2.3143 1.8510 -0.4980 0.3549  0.0581  348 PRO A C   
2554  O O   . PRO A 348 ? 2.7654 2.3186 1.8968 -0.4761 0.3329  0.0534  348 PRO A O   
2555  C CB  . PRO A 348 ? 2.5566 2.1854 1.7437 -0.4534 0.4107  0.0242  348 PRO A CB  
2556  C CG  . PRO A 348 ? 2.5255 2.1621 1.7123 -0.4207 0.4462  -0.0089 348 PRO A CG  
2557  C CD  . PRO A 348 ? 2.7578 2.3394 1.8751 -0.4191 0.4453  -0.0227 348 PRO A CD  
2558  N N   . ASP A 349 ? 2.9284 2.4788 1.9855 -0.5339 0.3395  0.0868  349 ASP A N   
2559  C CA  . ASP A 349 ? 2.8853 2.4203 1.9424 -0.5473 0.2944  0.1153  349 ASP A CA  
2560  C C   . ASP A 349 ? 2.8420 2.4000 1.9886 -0.5306 0.2710  0.1315  349 ASP A C   
2561  O O   . ASP A 349 ? 2.8879 2.4751 2.0897 -0.5173 0.2896  0.1241  349 ASP A O   
2562  C CB  . ASP A 349 ? 3.0014 2.5244 1.9919 -0.5880 0.2862  0.1442  349 ASP A CB  
2563  C CG  . ASP A 349 ? 3.1317 2.6274 2.0272 -0.6086 0.2991  0.1295  349 ASP A CG  
2564  O OD1 . ASP A 349 ? 3.1486 2.6260 2.0289 -0.5926 0.3073  0.0998  349 ASP A OD1 
2565  O OD2 . ASP A 349 ? 3.2554 2.7461 2.0895 -0.6418 0.3016  0.1478  349 ASP A OD2 
2566  N N   . ILE A 350 ? 2.6447 2.1915 1.8044 -0.5328 0.2311  0.1532  350 ILE A N   
2567  C CA  . ILE A 350 ? 2.4520 2.0159 1.6955 -0.5150 0.2091  0.1660  350 ILE A CA  
2568  C C   . ILE A 350 ? 2.5739 2.1479 1.8365 -0.5340 0.2123  0.1926  350 ILE A C   
2569  O O   . ILE A 350 ? 2.4151 2.0090 1.7480 -0.5201 0.2140  0.1908  350 ILE A O   
2570  C CB  . ILE A 350 ? 2.2994 1.8500 1.5523 -0.5100 0.1678  0.1808  350 ILE A CB  
2571  C CG1 . ILE A 350 ? 2.3057 1.8525 1.5693 -0.4840 0.1674  0.1513  350 ILE A CG1 
2572  C CG2 . ILE A 350 ? 2.3688 1.9291 1.6885 -0.5032 0.1433  0.2054  350 ILE A CG2 
2573  C CD1 . ILE A 350 ? 2.2973 1.8364 1.5730 -0.4795 0.1293  0.1635  350 ILE A CD1 
2574  N N   . ASP A 351 ? 2.7642 2.3246 1.9649 -0.5659 0.2141  0.2158  351 ASP A N   
2575  C CA  . ASP A 351 ? 2.6644 2.2280 1.8784 -0.5863 0.2169  0.2457  351 ASP A CA  
2576  C C   . ASP A 351 ? 2.6208 2.2134 1.8839 -0.5790 0.2512  0.2254  351 ASP A C   
2577  O O   . ASP A 351 ? 2.6493 2.2476 1.9569 -0.5861 0.2495  0.2431  351 ASP A O   
2578  C CB  . ASP A 351 ? 2.5418 2.0892 1.6726 -0.6217 0.2201  0.2705  351 ASP A CB  
2579  C CG  . ASP A 351 ? 2.5983 2.1256 1.7030 -0.6330 0.1789  0.3074  351 ASP A CG  
2580  O OD1 . ASP A 351 ? 2.5853 2.1102 1.7179 -0.6136 0.1504  0.3047  351 ASP A OD1 
2581  O OD2 . ASP A 351 ? 2.4071 1.9240 1.4638 -0.6607 0.1757  0.3397  351 ASP A OD2 
2582  N N   . THR A 352 ? 2.5782 2.1886 1.8344 -0.5650 0.2813  0.1900  352 THR A N   
2583  C CA  . THR A 352 ? 2.4704 2.1183 1.7731 -0.5568 0.3149  0.1694  352 THR A CA  
2584  C C   . THR A 352 ? 2.4775 2.1467 1.8713 -0.5351 0.3008  0.1648  352 THR A C   
2585  O O   . THR A 352 ? 2.5236 2.2217 1.9632 -0.5404 0.3179  0.1623  352 THR A O   
2586  C CB  . THR A 352 ? 2.2301 1.8920 1.5111 -0.5373 0.3461  0.1323  352 THR A CB  
2587  O OG1 . THR A 352 ? 2.3508 1.9865 1.5429 -0.5580 0.3568  0.1341  352 THR A OG1 
2588  C CG2 . THR A 352 ? 2.1440 1.8528 1.4674 -0.5296 0.3833  0.1123  352 THR A CG2 
2589  N N   . ILE A 353 ? 2.4729 2.1294 1.8914 -0.5127 0.2706  0.1624  353 ILE A N   
2590  C CA  . ILE A 353 ? 2.4300 2.1043 1.9295 -0.4911 0.2555  0.1561  353 ILE A CA  
2591  C C   . ILE A 353 ? 2.5553 2.2203 2.0860 -0.5112 0.2421  0.1850  353 ILE A C   
2592  O O   . ILE A 353 ? 2.4981 2.1299 1.9935 -0.5296 0.2226  0.2167  353 ILE A O   
2593  C CB  . ILE A 353 ? 2.3214 1.9810 1.8305 -0.4650 0.2267  0.1492  353 ILE A CB  
2594  C CG1 . ILE A 353 ? 2.3354 2.0064 1.8308 -0.4399 0.2451  0.1158  353 ILE A CG1 
2595  C CG2 . ILE A 353 ? 2.2707 1.9410 1.8557 -0.4481 0.2052  0.1502  353 ILE A CG2 
2596  C CD1 . ILE A 353 ? 2.4567 2.1010 1.9257 -0.4267 0.2232  0.1124  353 ILE A CD1 
2597  N N   . ASP A 354 ? 2.6325 2.3267 2.2286 -0.5077 0.2529  0.1740  354 ASP A N   
2598  C CA  . ASP A 354 ? 2.5143 2.1964 2.1451 -0.5267 0.2446  0.1966  354 ASP A CA  
2599  C C   . ASP A 354 ? 2.4195 2.1021 2.1177 -0.5046 0.2202  0.1899  354 ASP A C   
2600  O O   . ASP A 354 ? 2.4938 2.1469 2.2092 -0.5140 0.2022  0.2136  354 ASP A O   
2601  C CB  . ASP A 354 ? 2.4298 2.1437 2.0803 -0.5479 0.2783  0.1890  354 ASP A CB  
2602  C CG  . ASP A 354 ? 2.6538 2.3708 2.2397 -0.5700 0.3059  0.1942  354 ASP A CG  
2603  O OD1 . ASP A 354 ? 2.6750 2.3539 2.1992 -0.5877 0.2958  0.2223  354 ASP A OD1 
2604  O OD2 . ASP A 354 ? 2.6418 2.4024 2.2385 -0.5691 0.3378  0.1703  354 ASP A OD2 
2605  N N   . LYS A 355 ? 2.1978 1.9121 1.9318 -0.4744 0.2207  0.1582  355 LYS A N   
2606  C CA  . LYS A 355 ? 1.8866 1.6062 1.6815 -0.4521 0.1994  0.1479  355 LYS A CA  
2607  C C   . LYS A 355 ? 1.8757 1.6004 1.6651 -0.4198 0.1862  0.1309  355 LYS A C   
2608  O O   . LYS A 355 ? 2.0263 1.7648 1.7838 -0.4107 0.2024  0.1155  355 LYS A O   
2609  C CB  . LYS A 355 ? 1.8101 1.5745 1.6683 -0.4512 0.2166  0.1238  355 LYS A CB  
2610  C CG  . LYS A 355 ? 2.0099 1.7614 1.8908 -0.4823 0.2221  0.1400  355 LYS A CG  
2611  C CD  . LYS A 355 ? 2.1019 1.9041 2.0444 -0.4853 0.2397  0.1128  355 LYS A CD  
2612  C CE  . LYS A 355 ? 2.1873 1.9782 2.1423 -0.5234 0.2534  0.1269  355 LYS A CE  
2613  N NZ  . LYS A 355 ? 1.6608 1.5085 1.6746 -0.5308 0.2716  0.0983  355 LYS A NZ  
2614  N N   . ALA A 356 ? 1.9370 1.6489 1.7572 -0.4023 0.1586  0.1334  356 ALA A N   
2615  C CA  . ALA A 356 ? 2.1091 1.8232 1.9270 -0.3736 0.1440  0.1198  356 ALA A CA  
2616  C C   . ALA A 356 ? 1.9888 1.7385 1.8085 -0.3526 0.1655  0.0887  356 ALA A C   
2617  O O   . ALA A 356 ? 1.7334 1.4724 1.5058 -0.3461 0.1710  0.0842  356 ALA A O   
2618  C CB  . ALA A 356 ? 1.7777 1.4910 1.6497 -0.3563 0.1201  0.1180  356 ALA A CB  
2619  N N   . MET A 360 ? 2.3261 2.0102 1.8702 -0.2847 0.2645  0.0045  360 MET A N   
2620  C CA  . MET A 360 ? 2.4336 2.0866 1.9038 -0.2944 0.2900  -0.0040 360 MET A CA  
2621  C C   . MET A 360 ? 2.5127 2.1219 1.9416 -0.2831 0.2842  -0.0135 360 MET A C   
2622  O O   . MET A 360 ? 2.4961 2.0974 1.9460 -0.2792 0.2548  -0.0056 360 MET A O   
2623  C CB  . MET A 360 ? 2.4881 2.1211 1.9097 -0.3360 0.2849  0.0162  360 MET A CB  
2624  C CG  . MET A 360 ? 2.4810 2.1421 1.9473 -0.3537 0.2723  0.0369  360 MET A CG  
2625  S SD  . MET A 360 ? 2.9154 2.6138 2.3876 -0.3644 0.3108  0.0314  360 MET A SD  
2626  C CE  . MET A 360 ? 2.4773 2.1408 1.8558 -0.3745 0.3403  0.0190  360 MET A CE  
2627  N N   . PRO A 361 ? 3.2735 2.8527 2.6447 -0.2783 0.3123  -0.0308 361 PRO A N   
2628  C CA  . PRO A 361 ? 3.2858 2.8151 2.6103 -0.2737 0.3085  -0.0401 361 PRO A CA  
2629  C C   . PRO A 361 ? 3.3711 2.8632 2.6336 -0.3151 0.2892  -0.0265 361 PRO A C   
2630  O O   . PRO A 361 ? 3.3846 2.8885 2.6361 -0.3429 0.2838  -0.0105 361 PRO A O   
2631  C CB  . PRO A 361 ? 3.3081 2.8193 2.5946 -0.2539 0.3507  -0.0643 361 PRO A CB  
2632  C CG  . PRO A 361 ? 3.3265 2.8641 2.6043 -0.2708 0.3727  -0.0623 361 PRO A CG  
2633  C CD  . PRO A 361 ? 3.2952 2.8852 2.6431 -0.2769 0.3510  -0.0435 361 PRO A CD  
2634  N N   . LEU A 362 ? 2.9848 2.4352 2.2084 -0.3193 0.2790  -0.0321 362 LEU A N   
2635  C CA  . LEU A 362 ? 2.9735 2.3943 2.1367 -0.3603 0.2589  -0.0203 362 LEU A CA  
2636  C C   . LEU A 362 ? 2.9225 2.2884 2.0193 -0.3646 0.2720  -0.0409 362 LEU A C   
2637  O O   . LEU A 362 ? 2.8524 2.2025 1.9527 -0.3653 0.2503  -0.0391 362 LEU A O   
2638  C CB  . LEU A 362 ? 2.9476 2.3883 2.1539 -0.3687 0.2156  0.0038  362 LEU A CB  
2639  C CG  . LEU A 362 ? 2.8881 2.3225 2.0528 -0.4099 0.1897  0.0258  362 LEU A CG  
2640  C CD1 . LEU A 362 ? 2.9425 2.3934 2.0938 -0.4289 0.1993  0.0393  362 LEU A CD1 
2641  C CD2 . LEU A 362 ? 2.8019 2.2571 2.0147 -0.4108 0.1487  0.0483  362 LEU A CD2 
2642  N N   . GLY A 363 ? 2.8963 2.2329 1.9347 -0.3679 0.3079  -0.0605 363 GLY A N   
2643  C CA  . GLY A 363 ? 2.7038 1.9799 1.6778 -0.3707 0.3243  -0.0832 363 GLY A CA  
2644  C C   . GLY A 363 ? 2.5585 1.8069 1.4669 -0.4184 0.3024  -0.0771 363 GLY A C   
2645  O O   . GLY A 363 ? 2.5817 1.8467 1.4642 -0.4490 0.2946  -0.0635 363 GLY A O   
2646  N N   . MET A 364 ? 2.4698 1.6800 1.3516 -0.4260 0.2926  -0.0859 364 MET A N   
2647  C CA  . MET A 364 ? 2.4438 1.6366 1.2677 -0.4743 0.2674  -0.0796 364 MET A CA  
2648  C C   . MET A 364 ? 2.6188 1.7428 1.3671 -0.4878 0.2893  -0.1086 364 MET A C   
2649  O O   . MET A 364 ? 2.7047 1.8080 1.4641 -0.4819 0.2793  -0.1130 364 MET A O   
2650  C CB  . MET A 364 ? 2.3660 1.5932 1.2426 -0.4798 0.2219  -0.0553 364 MET A CB  
2651  C CG  . MET A 364 ? 2.3321 1.6194 1.2830 -0.4663 0.2006  -0.0276 364 MET A CG  
2652  S SD  . MET A 364 ? 2.2078 1.5339 1.2048 -0.4810 0.1465  0.0032  364 MET A SD  
2653  C CE  . MET A 364 ? 2.0887 1.4062 1.0022 -0.5372 0.1290  0.0130  364 MET A CE  
2654  N N   . LEU A 365 ? 2.5746 1.6627 1.2475 -0.5065 0.3193  -0.1280 365 LEU A N   
2655  C CA  . LEU A 365 ? 2.5919 1.6073 1.1852 -0.5236 0.3424  -0.1580 365 LEU A CA  
2656  C C   . LEU A 365 ? 2.7068 1.7133 1.2284 -0.5830 0.3206  -0.1564 365 LEU A C   
2657  O O   . LEU A 365 ? 2.8021 1.8234 1.2841 -0.6078 0.3234  -0.1525 365 LEU A O   
2658  C CB  . LEU A 365 ? 2.5158 1.4909 1.0687 -0.5021 0.3953  -0.1856 365 LEU A CB  
2659  C CG  . LEU A 365 ? 2.7099 1.6006 1.1693 -0.5211 0.4267  -0.2202 365 LEU A CG  
2660  C CD1 . LEU A 365 ? 2.8043 1.6492 1.2658 -0.5151 0.4208  -0.2287 365 LEU A CD1 
2661  C CD2 . LEU A 365 ? 2.9293 1.7874 1.3644 -0.4888 0.4803  -0.2449 365 LEU A CD2 
2662  N N   . ILE A 366 ? 2.8209 1.8065 1.3256 -0.6067 0.2987  -0.1591 366 ILE A N   
2663  C CA  . ILE A 366 ? 3.0958 2.0787 1.5352 -0.6648 0.2744  -0.1583 366 ILE A CA  
2664  C C   . ILE A 366 ? 3.1489 2.0500 1.4989 -0.6888 0.3048  -0.1965 366 ILE A C   
2665  O O   . ILE A 366 ? 3.1407 1.9944 1.4982 -0.6666 0.3232  -0.2132 366 ILE A O   
2666  C CB  . ILE A 366 ? 2.9643 1.9944 1.4553 -0.6778 0.2242  -0.1316 366 ILE A CB  
2667  C CG1 . ILE A 366 ? 2.6868 1.7924 1.2627 -0.6546 0.1957  -0.0942 366 ILE A CG1 
2668  C CG2 . ILE A 366 ? 3.0250 2.0565 1.4495 -0.7385 0.1980  -0.1320 366 ILE A CG2 
2669  C CD1 . ILE A 366 ? 2.5113 1.6355 1.1797 -0.6021 0.1963  -0.0860 366 ILE A CD1 
2670  N N   . LYS A 367 ? 3.1272 2.0116 1.3917 -0.7351 0.3094  -0.2092 367 LYS A N   
2671  C CA  . LYS A 367 ? 3.2663 2.0669 1.4360 -0.7632 0.3412  -0.2495 367 LYS A CA  
2672  C C   . LYS A 367 ? 3.4951 2.3028 1.6039 -0.8295 0.3087  -0.2504 367 LYS A C   
2673  O O   . LYS A 367 ? 3.4985 2.3567 1.5877 -0.8593 0.2849  -0.2324 367 LYS A O   
2674  C CB  . LYS A 367 ? 3.3866 2.1484 1.5001 -0.7533 0.3897  -0.2742 367 LYS A CB  
2675  C CG  . LYS A 367 ? 3.2846 2.0292 1.4493 -0.6881 0.4281  -0.2808 367 LYS A CG  
2676  C CD  . LYS A 367 ? 3.3087 1.9639 1.4034 -0.6773 0.4841  -0.3224 367 LYS A CD  
2677  C CE  . LYS A 367 ? 3.2157 1.8784 1.3216 -0.6368 0.5245  -0.3289 367 LYS A CE  
2678  N NZ  . LYS A 367 ? 3.1635 1.9067 1.2960 -0.6477 0.5032  -0.3016 367 LYS A NZ  
2679  N N   . VAL A 368 ? 3.5546 2.3158 1.6361 -0.8515 0.3075  -0.2692 368 VAL A N   
2680  C CA  . VAL A 368 ? 3.5233 2.2920 1.5437 -0.9191 0.2776  -0.2741 368 VAL A CA  
2681  C C   . VAL A 368 ? 3.4421 2.1146 1.3771 -0.9490 0.3104  -0.3187 368 VAL A C   
2682  O O   . VAL A 368 ? 3.6752 2.2984 1.6347 -0.9234 0.3279  -0.3295 368 VAL A O   
2683  C CB  . VAL A 368 ? 3.3972 2.2360 1.4879 -0.9279 0.2244  -0.2412 368 VAL A CB  
2684  C CG1 . VAL A 368 ? 3.4645 2.3923 1.6325 -0.9019 0.1924  -0.1979 368 VAL A CG1 
2685  C CG2 . VAL A 368 ? 3.2169 2.0246 1.3590 -0.8981 0.2314  -0.2458 368 VAL A CG2 
2686  N N   . SER A 369 ? 3.3943 2.0394 1.2305 -1.0019 0.3190  -0.3432 369 SER A N   
2687  C CA  . SER A 369 ? 3.3624 1.9282 1.1499 -1.0232 0.3510  -0.3770 369 SER A CA  
2688  C C   . SER A 369 ? 3.5415 2.1329 1.2966 -1.0901 0.3209  -0.3773 369 SER A C   
2689  O O   . SER A 369 ? 4.0406 2.5841 1.7431 -1.1170 0.3462  -0.4020 369 SER A O   
2690  C CB  . SER A 369 ? 3.6187 2.1342 1.3668 -1.0029 0.4009  -0.3999 369 SER A CB  
2691  O OG  . SER A 369 ? 3.4834 2.0362 1.1893 -1.0422 0.3903  -0.3982 369 SER A OG  
2692  N N   . GLY A 370 ? 3.4078 2.0759 1.1955 -1.1156 0.2682  -0.3501 370 GLY A N   
2693  C CA  . GLY A 370 ? 3.7800 2.4862 1.5461 -1.1771 0.2366  -0.3470 370 GLY A CA  
2694  C C   . GLY A 370 ? 3.8131 2.4595 1.5679 -1.1965 0.2532  -0.3690 370 GLY A C   
2695  O O   . GLY A 370 ? 3.5068 2.0950 1.2840 -1.1602 0.2781  -0.3786 370 GLY A O   
2696  N N   . THR A 371 ? 3.6737 2.3345 1.3930 -1.2538 0.2407  -0.3760 371 THR A N   
2697  C CA  . THR A 371 ? 3.7664 2.3732 1.4691 -1.2790 0.2572  -0.3959 371 THR A CA  
2698  C C   . THR A 371 ? 3.7621 2.3902 1.5255 -1.2669 0.2344  -0.3798 371 THR A C   
2699  O O   . THR A 371 ? 3.5798 2.2894 1.3960 -1.2593 0.1913  -0.3505 371 THR A O   
2700  C CB  . THR A 371 ? 3.6699 2.3073 1.3271 -1.3469 0.2413  -0.4026 371 THR A CB  
2701  O OG1 . THR A 371 ? 3.7485 2.3158 1.3763 -1.3697 0.2694  -0.4272 371 THR A OG1 
2702  C CG2 . THR A 371 ? 3.6096 2.3641 1.3061 -1.3796 0.1798  -0.3701 371 THR A CG2 
2703  N N   . ASN A 372 ? 3.9253 2.4788 1.6806 -1.2646 0.2643  -0.3982 372 ASN A N   
2704  C CA  . ASN A 372 ? 4.0193 2.5828 1.8273 -1.2551 0.2489  -0.3862 372 ASN A CA  
2705  C C   . ASN A 372 ? 4.0710 2.6414 1.9386 -1.1946 0.2443  -0.3704 372 ASN A C   
2706  O O   . ASN A 372 ? 4.0191 2.6505 1.9449 -1.1916 0.2077  -0.3482 372 ASN A O   
2707  C CB  . ASN A 372 ? 3.8723 2.5363 1.7062 -1.3053 0.1963  -0.3654 372 ASN A CB  
2708  C CG  . ASN A 372 ? 4.0748 2.7342 1.9336 -1.3221 0.1917  -0.3648 372 ASN A CG  
2709  O OD1 . ASN A 372 ? 4.3625 2.9322 2.1994 -1.3118 0.2319  -0.3846 372 ASN A OD1 
2710  N ND2 . ASN A 372 ? 4.1390 2.8976 2.0452 -1.3475 0.1430  -0.3404 372 ASN A ND2 
2711  N N   . MET A 373 ? 3.7966 2.3069 1.6518 -1.1460 0.2821  -0.3822 373 MET A N   
2712  C CA  . MET A 373 ? 3.5376 2.0518 1.4455 -1.0874 0.2818  -0.3698 373 MET A CA  
2713  C C   . MET A 373 ? 3.5437 1.9586 1.4513 -1.0414 0.3308  -0.3869 373 MET A C   
2714  O O   . MET A 373 ? 3.6643 2.0107 1.5317 -1.0206 0.3752  -0.4068 373 MET A O   
2715  C CB  . MET A 373 ? 3.5478 2.0944 1.4504 -1.0637 0.2810  -0.3631 373 MET A CB  
2716  C CG  . MET A 373 ? 3.3690 1.9718 1.3638 -1.0036 0.2653  -0.3311 373 MET A CG  
2717  S SD  . MET A 373 ? 3.3711 2.0914 1.4586 -1.0148 0.2002  -0.2878 373 MET A SD  
2718  C CE  . MET A 373 ? 3.0594 1.8540 1.2422 -0.9478 0.1873  -0.2492 373 MET A CE  
2719  N N   . GLN A 374 ? 3.6070 2.0164 1.5619 -1.0242 0.3226  -0.3774 374 GLN A N   
2720  C CA  . GLN A 374 ? 3.5414 1.8618 1.5012 -0.9784 0.3656  -0.3879 374 GLN A CA  
2721  C C   . GLN A 374 ? 3.5892 1.9117 1.5964 -0.9074 0.3782  -0.3781 374 GLN A C   
2722  O O   . GLN A 374 ? 3.6577 2.0794 1.7365 -0.8866 0.3441  -0.3469 374 GLN A O   
2723  C CB  . GLN A 374 ? 3.4202 1.7386 1.4124 -0.9914 0.3523  -0.3787 374 GLN A CB  
2724  C CG  . GLN A 374 ? 3.4460 1.7752 1.4033 -1.0579 0.3406  -0.3844 374 GLN A CG  
2725  C CD  . GLN A 374 ? 3.6587 1.9878 1.6479 -1.0689 0.3312  -0.3752 374 GLN A CD  
2726  O OE1 . GLN A 374 ? 3.8203 2.1576 1.8659 -1.0320 0.3238  -0.3605 374 GLN A OE1 
2727  N NE2 . GLN A 374 ? 3.4243 1.7462 1.3779 -1.1215 0.3319  -0.3840 374 GLN A NE2 
2728  N N   . LYS A 375 ? 3.4749 1.7083 1.4653 -0.8609 0.4264  -0.3937 375 LYS A N   
2729  C CA  . LYS A 375 ? 3.3582 1.6139 1.4159 -0.7831 0.4407  -0.3754 375 LYS A CA  
2730  C C   . LYS A 375 ? 3.4073 1.7237 1.5653 -0.7430 0.4147  -0.3413 375 LYS A C   
2731  O O   . LYS A 375 ? 3.3901 1.7525 1.6158 -0.6850 0.4144  -0.3215 375 LYS A O   
2732  C CB  . LYS A 375 ? 3.2602 1.4020 1.2746 -0.7422 0.4994  -0.3999 375 LYS A CB  
2733  C CG  . LYS A 375 ? 3.3921 1.4872 1.3387 -0.7552 0.5337  -0.4239 375 LYS A CG  
2734  C CD  . LYS A 375 ? 3.5139 1.5196 1.4465 -0.7044 0.5876  -0.4350 375 LYS A CD  
2735  C CE  . LYS A 375 ? 3.6996 1.6656 1.5756 -0.7136 0.6212  -0.4563 375 LYS A CE  
2736  N NZ  . LYS A 375 ? 3.6388 1.5189 1.5034 -0.6626 0.6726  -0.4654 375 LYS A NZ  
2737  N N   . ASP A 376 ? 3.5652 1.8845 1.7322 -0.7758 0.3933  -0.3356 376 ASP A N   
2738  C CA  . ASP A 376 ? 3.5323 1.9076 1.7888 -0.7431 0.3692  -0.3053 376 ASP A CA  
2739  C C   . ASP A 376 ? 3.4287 1.9179 1.7362 -0.7773 0.3131  -0.2809 376 ASP A C   
2740  O O   . ASP A 376 ? 3.3293 1.8735 1.7064 -0.7644 0.2871  -0.2573 376 ASP A O   
2741  C CB  . ASP A 376 ? 3.7792 2.0818 2.0184 -0.7492 0.3865  -0.3123 376 ASP A CB  
2742  C CG  . ASP A 376 ? 3.8199 2.0249 2.0359 -0.6959 0.4373  -0.3243 376 ASP A CG  
2743  O OD1 . ASP A 376 ? 3.6994 1.9129 1.9352 -0.6441 0.4545  -0.3217 376 ASP A OD1 
2744  O OD2 . ASP A 376 ? 3.9096 2.0308 2.0885 -0.7056 0.4603  -0.3351 376 ASP A OD2 
2745  N N   . PHE A 377 ? 3.2328 1.7534 1.5017 -0.8203 0.2967  -0.2871 377 PHE A N   
2746  C CA  . PHE A 377 ? 3.1806 1.8104 1.4946 -0.8505 0.2434  -0.2618 377 PHE A CA  
2747  C C   . PHE A 377 ? 3.2353 1.9391 1.6149 -0.8044 0.2286  -0.2362 377 PHE A C   
2748  O O   . PHE A 377 ? 3.1121 1.9087 1.5543 -0.8072 0.1862  -0.2076 377 PHE A O   
2749  C CB  . PHE A 377 ? 3.1282 1.7569 1.3639 -0.9220 0.2313  -0.2793 377 PHE A CB  
2750  C CG  . PHE A 377 ? 3.1557 1.7690 1.3550 -0.9841 0.2189  -0.2918 377 PHE A CG  
2751  C CD1 . PHE A 377 ? 3.1948 1.8073 1.4382 -0.9772 0.2139  -0.2828 377 PHE A CD1 
2752  C CD2 . PHE A 377 ? 3.2766 1.8793 1.3955 -1.0525 0.2122  -0.3132 377 PHE A CD2 
2753  C CE1 . PHE A 377 ? 3.1695 1.7715 1.3801 -1.0379 0.2033  -0.2945 377 PHE A CE1 
2754  C CE2 . PHE A 377 ? 3.3974 1.9971 1.4904 -1.1095 0.2010  -0.3226 377 PHE A CE2 
2755  C CZ  . PHE A 377 ? 3.4607 2.0587 1.5984 -1.1038 0.1965  -0.3142 377 PHE A CZ  
2756  N N   . GLU A 378 ? 3.5045 2.1683 1.8712 -0.7631 0.2635  -0.2462 378 GLU A N   
2757  C CA  . GLU A 378 ? 3.4742 2.2041 1.8968 -0.7236 0.2535  -0.2247 378 GLU A CA  
2758  C C   . GLU A 378 ? 3.4020 2.2046 1.9294 -0.6824 0.2262  -0.1931 378 GLU A C   
2759  O O   . GLU A 378 ? 3.3723 2.2553 1.9478 -0.6815 0.1935  -0.1686 378 GLU A O   
2760  C CB  . GLU A 378 ? 3.5091 2.1821 1.9058 -0.6824 0.3002  -0.2425 378 GLU A CB  
2761  C CG  . GLU A 378 ? 3.7460 2.3143 2.0427 -0.7075 0.3413  -0.2801 378 GLU A CG  
2762  C CD  . GLU A 378 ? 3.8426 2.3517 2.1195 -0.6591 0.3910  -0.2975 378 GLU A CD  
2763  O OE1 . GLU A 378 ? 3.6114 2.1295 1.9507 -0.6006 0.4014  -0.2852 378 GLU A OE1 
2764  O OE2 . GLU A 378 ? 4.0049 2.4623 2.2044 -0.6796 0.4192  -0.3237 378 GLU A OE2 
2765  N N   . PRO A 379 ? 2.8861 1.6632 1.4496 -0.6470 0.2391  -0.1920 379 PRO A N   
2766  C CA  . PRO A 379 ? 2.6403 1.4863 1.3006 -0.6065 0.2156  -0.1645 379 PRO A CA  
2767  C C   . PRO A 379 ? 2.6542 1.5877 1.3581 -0.6360 0.1661  -0.1402 379 PRO A C   
2768  O O   . PRO A 379 ? 2.5486 1.5496 1.3234 -0.6070 0.1452  -0.1172 379 PRO A O   
2769  C CB  . PRO A 379 ? 2.6098 1.4069 1.2742 -0.5921 0.2314  -0.1705 379 PRO A CB  
2770  C CG  . PRO A 379 ? 2.6186 1.3109 1.2012 -0.5929 0.2782  -0.2004 379 PRO A CG  
2771  C CD  . PRO A 379 ? 2.9382 1.6179 1.4500 -0.6434 0.2775  -0.2163 379 PRO A CD  
2772  N N   . VAL A 380 ? 2.7396 1.6706 1.4008 -0.6923 0.1494  -0.1461 380 VAL A N   
2773  C CA  . VAL A 380 ? 2.7560 1.7740 1.4583 -0.7209 0.1015  -0.1221 380 VAL A CA  
2774  C C   . VAL A 380 ? 2.6910 1.7618 1.4058 -0.7172 0.0842  -0.1058 380 VAL A C   
2775  O O   . VAL A 380 ? 2.5923 1.7425 1.3659 -0.7158 0.0468  -0.0781 380 VAL A O   
2776  C CB  . VAL A 380 ? 2.5676 1.5734 1.2116 -0.7867 0.0893  -0.1346 380 VAL A CB  
2777  C CG1 . VAL A 380 ? 2.4408 1.5418 1.1353 -0.8108 0.0405  -0.1084 380 VAL A CG1 
2778  C CG2 . VAL A 380 ? 2.4698 1.4002 1.0814 -0.7949 0.1167  -0.1562 380 VAL A CG2 
2779  N N   . LEU A 381 ? 2.7337 1.7597 1.3945 -0.7145 0.1125  -0.1219 381 LEU A N   
2780  C CA  . LEU A 381 ? 2.6494 1.7197 1.3144 -0.7133 0.1002  -0.1068 381 LEU A CA  
2781  C C   . LEU A 381 ? 2.5658 1.6700 1.3092 -0.6552 0.1029  -0.0890 381 LEU A C   
2782  O O   . LEU A 381 ? 2.4741 1.6455 1.2661 -0.6502 0.0732  -0.0619 381 LEU A O   
2783  C CB  . LEU A 381 ? 2.8834 1.8955 1.4568 -0.7371 0.1305  -0.1324 381 LEU A CB  
2784  C CG  . LEU A 381 ? 2.8871 1.8925 1.3840 -0.8035 0.1161  -0.1435 381 LEU A CG  
2785  C CD1 . LEU A 381 ? 2.5996 1.5390 1.0497 -0.8300 0.1332  -0.1708 381 LEU A CD1 
2786  C CD2 . LEU A 381 ? 2.9512 1.9325 1.3736 -0.8244 0.1340  -0.1572 381 LEU A CD2 
2787  N N   . GLU A 382 ? 2.5671 1.6268 1.3219 -0.6134 0.1369  -0.1031 382 GLU A N   
2788  C CA  . GLU A 382 ? 2.1930 1.2874 1.0226 -0.5592 0.1405  -0.0889 382 GLU A CA  
2789  C C   . GLU A 382 ? 2.3284 1.4949 1.2404 -0.5489 0.1013  -0.0611 382 GLU A C   
2790  O O   . GLU A 382 ? 2.3363 1.5509 1.3044 -0.5234 0.0901  -0.0429 382 GLU A O   
2791  C CB  . GLU A 382 ? 2.3298 1.3716 1.1629 -0.5171 0.1780  -0.1066 382 GLU A CB  
2792  C CG  . GLU A 382 ? 2.5719 1.5276 1.3170 -0.5332 0.2158  -0.1369 382 GLU A CG  
2793  C CD  . GLU A 382 ? 2.6674 1.5988 1.3825 -0.5141 0.2494  -0.1501 382 GLU A CD  
2794  O OE1 . GLU A 382 ? 2.4158 1.4013 1.1763 -0.4944 0.2412  -0.1347 382 GLU A OE1 
2795  O OE2 . GLU A 382 ? 3.0334 1.8908 1.6797 -0.5195 0.2851  -0.1763 382 GLU A OE2 
2796  N N   . ARG A 383 ? 2.4598 1.6332 1.3782 -0.5692 0.0826  -0.0586 383 ARG A N   
2797  C CA  . ARG A 383 ? 2.3989 1.6402 1.3984 -0.5554 0.0485  -0.0339 383 ARG A CA  
2798  C C   . ARG A 383 ? 2.4444 1.7471 1.4578 -0.5794 0.0127  -0.0100 383 ARG A C   
2799  O O   . ARG A 383 ? 2.2218 1.5758 1.3025 -0.5526 -0.0052 0.0117  383 ARG A O   
2800  C CB  . ARG A 383 ? 2.2286 1.4619 1.2294 -0.5718 0.0411  -0.0384 383 ARG A CB  
2801  C CG  . ARG A 383 ? 2.0003 1.3059 1.0793 -0.5625 0.0063  -0.0145 383 ARG A CG  
2802  C CD  . ARG A 383 ? 1.9982 1.3265 1.1505 -0.5078 0.0108  -0.0060 383 ARG A CD  
2803  N NE  . ARG A 383 ? 2.0485 1.4461 1.2747 -0.4979 -0.0215 0.0162  383 ARG A NE  
2804  C CZ  . ARG A 383 ? 2.0954 1.5322 1.3889 -0.4600 -0.0293 0.0295  383 ARG A CZ  
2805  N NH1 . ARG A 383 ? 1.9155 1.3346 1.2136 -0.4307 -0.0087 0.0237  383 ARG A NH1 
2806  N NH2 . ARG A 383 ? 2.1028 1.5974 1.4593 -0.4522 -0.0568 0.0475  383 ARG A NH2 
2807  N N   . ARG A 384 ? 2.6300 1.9261 1.5799 -0.6282 0.0030  -0.0137 384 ARG A N   
2808  C CA  . ARG A 384 ? 2.5354 1.8916 1.4941 -0.6515 -0.0327 0.0117  384 ARG A CA  
2809  C C   . ARG A 384 ? 2.4682 1.8405 1.4425 -0.6299 -0.0300 0.0261  384 ARG A C   
2810  O O   . ARG A 384 ? 2.5183 1.9459 1.5282 -0.6312 -0.0604 0.0544  384 ARG A O   
2811  C CB  . ARG A 384 ? 2.3502 1.6978 1.2310 -0.7102 -0.0428 0.0033  384 ARG A CB  
2812  C CG  . ARG A 384 ? 2.3845 1.7440 1.2639 -0.7406 -0.0595 -0.0012 384 ARG A CG  
2813  C CD  . ARG A 384 ? 2.3476 1.7877 1.3070 -0.7315 -0.0989 0.0285  384 ARG A CD  
2814  N NE  . ARG A 384 ? 2.2216 1.7239 1.1977 -0.7385 -0.1316 0.0584  384 ARG A NE  
2815  C CZ  . ARG A 384 ? 2.3263 1.8994 1.3754 -0.7221 -0.1647 0.0886  384 ARG A CZ  
2816  N NH1 . ARG A 384 ? 2.3062 1.9006 1.4192 -0.6989 -0.1697 0.0913  384 ARG A NH1 
2817  N NH2 . ARG A 384 ? 2.4410 2.0624 1.4981 -0.7275 -0.1921 0.1169  384 ARG A NH2 
2818  N N   . LEU A 385 ? 2.3533 1.6800 1.3056 -0.6082 0.0064  0.0085  385 LEU A N   
2819  C CA  . LEU A 385 ? 2.2688 1.6123 1.2380 -0.5891 0.0118  0.0211  385 LEU A CA  
2820  C C   . LEU A 385 ? 2.2503 1.6460 1.3125 -0.5536 -0.0089 0.0459  385 LEU A C   
2821  O O   . LEU A 385 ? 2.3288 1.7601 1.4132 -0.5533 -0.0261 0.0696  385 LEU A O   
2822  C CB  . LEU A 385 ? 2.1659 1.4592 1.1100 -0.5652 0.0560  -0.0031 385 LEU A CB  
2823  C CG  . LEU A 385 ? 2.1737 1.4042 1.0258 -0.5920 0.0857  -0.0320 385 LEU A CG  
2824  C CD1 . LEU A 385 ? 2.1476 1.3356 0.9931 -0.5569 0.1291  -0.0535 385 LEU A CD1 
2825  C CD2 . LEU A 385 ? 2.2844 1.5224 1.0752 -0.6330 0.0771  -0.0262 385 LEU A CD2 
2826  N N   . HIS A 386 ? 2.1495 1.5468 1.2632 -0.5245 -0.0063 0.0401  386 HIS A N   
2827  C CA  . HIS A 386 ? 2.2183 1.6613 1.4194 -0.4904 -0.0236 0.0586  386 HIS A CA  
2828  C C   . HIS A 386 ? 2.2556 1.7523 1.4854 -0.5070 -0.0640 0.0883  386 HIS A C   
2829  O O   . HIS A 386 ? 2.2842 1.8141 1.5655 -0.4879 -0.0773 0.1090  386 HIS A O   
2830  C CB  . HIS A 386 ? 2.2000 1.6349 1.4367 -0.4656 -0.0162 0.0460  386 HIS A CB  
2831  C CG  . HIS A 386 ? 2.1194 1.6058 1.4350 -0.4454 -0.0426 0.0643  386 HIS A CG  
2832  N ND1 . HIS A 386 ? 2.2425 1.7546 1.6216 -0.4098 -0.0431 0.0729  386 HIS A ND1 
2833  C CD2 . HIS A 386 ? 2.1052 1.6208 1.4437 -0.4567 -0.0669 0.0734  386 HIS A CD2 
2834  C CE1 . HIS A 386 ? 2.0603 1.6124 1.4964 -0.3997 -0.0669 0.0862  386 HIS A CE1 
2835  N NE2 . HIS A 386 ? 1.8300 1.3879 1.2457 -0.4260 -0.0817 0.0876  386 HIS A NE2 
2836  N N   . TYR A 387 ? 2.4292 1.9346 1.6257 -0.5426 -0.0829 0.0907  387 TYR A N   
2837  C CA  . TYR A 387 ? 2.4249 1.9866 1.6473 -0.5582 -0.1223 0.1199  387 TYR A CA  
2838  C C   . TYR A 387 ? 2.3680 1.9416 1.5586 -0.5763 -0.1330 0.1396  387 TYR A C   
2839  O O   . TYR A 387 ? 2.4259 2.0397 1.6627 -0.5636 -0.1560 0.1686  387 TYR A O   
2840  C CB  . TYR A 387 ? 2.3647 1.9383 1.5607 -0.5933 -0.1388 0.1150  387 TYR A CB  
2841  C CG  . TYR A 387 ? 2.2308 1.8007 1.4649 -0.5761 -0.1322 0.1017  387 TYR A CG  
2842  C CD1 . TYR A 387 ? 2.1715 1.6824 1.3702 -0.5734 -0.0991 0.0720  387 TYR A CD1 
2843  C CD2 . TYR A 387 ? 2.1961 1.8200 1.5009 -0.5606 -0.1574 0.1195  387 TYR A CD2 
2844  C CE1 . TYR A 387 ? 2.1614 1.6671 1.3920 -0.5574 -0.0923 0.0622  387 TYR A CE1 
2845  C CE2 . TYR A 387 ? 2.0582 1.6802 1.3961 -0.5455 -0.1501 0.1078  387 TYR A CE2 
2846  C CZ  . TYR A 387 ? 2.1695 1.7319 1.4691 -0.5445 -0.1178 0.0799  387 TYR A CZ  
2847  O OH  . TYR A 387 ? 2.2815 1.8395 1.6096 -0.5298 -0.1096 0.0703  387 TYR A OH  
2848  N N   . PHE A 388 ? 2.2659 1.8021 1.3770 -0.6047 -0.1148 0.1245  388 PHE A N   
2849  C CA  . PHE A 388 ? 2.2089 1.7548 1.2819 -0.6243 -0.1228 0.1429  388 PHE A CA  
2850  C C   . PHE A 388 ? 2.2493 1.7990 1.3663 -0.5910 -0.1135 0.1574  388 PHE A C   
2851  O O   . PHE A 388 ? 2.2771 1.8580 1.4094 -0.5930 -0.1350 0.1883  388 PHE A O   
2852  C CB  . PHE A 388 ? 2.3009 1.8000 1.2783 -0.6581 -0.0981 0.1183  388 PHE A CB  
2853  C CG  . PHE A 388 ? 2.4447 1.9231 1.3658 -0.6947 -0.0977 0.0953  388 PHE A CG  
2854  C CD1 . PHE A 388 ? 2.4648 1.9867 1.4016 -0.7159 -0.1320 0.1084  388 PHE A CD1 
2855  C CD2 . PHE A 388 ? 2.5419 1.9574 1.3935 -0.7090 -0.0619 0.0604  388 PHE A CD2 
2856  C CE1 . PHE A 388 ? 2.5833 2.0866 1.4678 -0.7540 -0.1308 0.0860  388 PHE A CE1 
2857  C CE2 . PHE A 388 ? 2.5563 1.9460 1.3530 -0.7456 -0.0598 0.0379  388 PHE A CE2 
2858  C CZ  . PHE A 388 ? 2.5480 1.9821 1.3608 -0.7700 -0.0946 0.0505  388 PHE A CZ  
2859  N N   . LEU A 389 ? 2.2855 1.8045 1.4228 -0.5611 -0.0816 0.1361  389 LEU A N   
2860  C CA  . LEU A 389 ? 2.3188 1.8424 1.4981 -0.5326 -0.0701 0.1457  389 LEU A CA  
2861  C C   . LEU A 389 ? 2.3283 1.8917 1.5940 -0.5046 -0.0944 0.1694  389 LEU A C   
2862  O O   . LEU A 389 ? 2.4651 2.0397 1.7611 -0.4919 -0.0960 0.1875  389 LEU A O   
2863  C CB  . LEU A 389 ? 2.2481 1.7354 1.4268 -0.5083 -0.0300 0.1155  389 LEU A CB  
2864  C CG  . LEU A 389 ? 2.1277 1.5692 1.2239 -0.5289 0.0010  0.0894  389 LEU A CG  
2865  C CD1 . LEU A 389 ? 2.1405 1.5521 1.2480 -0.4973 0.0381  0.0619  389 LEU A CD1 
2866  C CD2 . LEU A 389 ? 2.0005 1.4419 1.0494 -0.5521 0.0052  0.1012  389 LEU A CD2 
2867  N N   . ASN A 390 ? 2.2685 1.8514 1.5706 -0.4971 -0.1119 0.1688  390 ASN A N   
2868  C CA  . ASN A 390 ? 2.2211 1.8414 1.6054 -0.4691 -0.1336 0.1888  390 ASN A CA  
2869  C C   . ASN A 390 ? 2.3531 2.0085 1.7431 -0.4831 -0.1672 0.2255  390 ASN A C   
2870  O O   . ASN A 390 ? 2.3179 1.9901 1.7613 -0.4611 -0.1771 0.2466  390 ASN A O   
2871  C CB  . ASN A 390 ? 2.0616 1.6945 1.4821 -0.4566 -0.1401 0.1768  390 ASN A CB  
2872  C CG  . ASN A 390 ? 2.0977 1.7236 1.5726 -0.4180 -0.1214 0.1608  390 ASN A CG  
2873  O OD1 . ASN A 390 ? 2.1358 1.7836 1.6718 -0.3932 -0.1298 0.1736  390 ASN A OD1 
2874  N ND2 . ASN A 390 ? 2.1218 1.7163 1.5734 -0.4128 -0.0958 0.1328  390 ASN A ND2 
2875  N N   . TYR A 391 ? 2.4574 2.1228 1.7930 -0.5186 -0.1836 0.2328  391 TYR A N   
2876  C CA  . TYR A 391 ? 2.3670 2.0726 1.7065 -0.5314 -0.2184 0.2700  391 TYR A CA  
2877  C C   . TYR A 391 ? 2.4174 2.1137 1.7442 -0.5306 -0.2156 0.2930  391 TYR A C   
2878  O O   . TYR A 391 ? 2.3818 2.1076 1.7314 -0.5272 -0.2420 0.3287  391 TYR A O   
2879  C CB  . TYR A 391 ? 2.2324 1.9540 1.5089 -0.5740 -0.2360 0.2707  391 TYR A CB  
2880  C CG  . TYR A 391 ? 2.2883 2.0202 1.5706 -0.5830 -0.2402 0.2502  391 TYR A CG  
2881  C CD1 . TYR A 391 ? 2.3666 2.1161 1.7219 -0.5519 -0.2435 0.2472  391 TYR A CD1 
2882  C CD2 . TYR A 391 ? 2.2122 1.9351 1.4247 -0.6247 -0.2399 0.2331  391 TYR A CD2 
2883  C CE1 . TYR A 391 ? 2.3413 2.1001 1.7006 -0.5618 -0.2458 0.2297  391 TYR A CE1 
2884  C CE2 . TYR A 391 ? 2.1081 1.8373 1.3243 -0.6363 -0.2421 0.2144  391 TYR A CE2 
2885  C CZ  . TYR A 391 ? 2.2928 2.0406 1.5830 -0.6046 -0.2450 0.2138  391 TYR A CZ  
2886  O OH  . TYR A 391 ? 2.2563 2.0108 1.5498 -0.6174 -0.2461 0.1968  391 TYR A OH  
2887  N N   . ILE A 392 ? 2.5017 2.1580 1.7930 -0.5331 -0.1830 0.2743  392 ILE A N   
2888  C CA  . ILE A 392 ? 2.4800 2.1261 1.7576 -0.5348 -0.1762 0.2944  392 ILE A CA  
2889  C C   . ILE A 392 ? 2.5290 2.1854 1.8880 -0.4994 -0.1819 0.3127  392 ILE A C   
2890  O O   . ILE A 392 ? 2.4606 2.1101 1.8697 -0.4723 -0.1673 0.2920  392 ILE A O   
2891  C CB  . ILE A 392 ? 2.3863 1.9917 1.6134 -0.5435 -0.1366 0.2663  392 ILE A CB  
2892  C CG1 . ILE A 392 ? 2.3937 1.9843 1.5318 -0.5820 -0.1311 0.2503  392 ILE A CG1 
2893  C CG2 . ILE A 392 ? 2.5132 2.1104 1.7404 -0.5412 -0.1258 0.2857  392 ILE A CG2 
2894  C CD1 . ILE A 392 ? 2.2754 1.8235 1.3682 -0.5851 -0.0893 0.2140  392 ILE A CD1 
2895  N N   . GLU A 393 ? 2.5686 2.2405 1.9391 -0.4996 -0.2035 0.3517  393 GLU A N   
2896  C CA  . GLU A 393 ? 2.6276 2.3033 2.0708 -0.4684 -0.2095 0.3713  393 GLU A CA  
2897  C C   . GLU A 393 ? 2.7523 2.3973 2.2137 -0.4551 -0.1765 0.3541  393 GLU A C   
2898  O O   . GLU A 393 ? 2.7314 2.3574 2.1529 -0.4713 -0.1612 0.3610  393 GLU A O   
2899  C CB  . GLU A 393 ? 2.5971 2.2876 2.0362 -0.4738 -0.2365 0.4189  393 GLU A CB  
2900  C CG  . GLU A 393 ? 2.6127 2.3001 2.1233 -0.4421 -0.2426 0.4411  393 GLU A CG  
2901  C CD  . GLU A 393 ? 2.5128 2.2188 2.0284 -0.4403 -0.2742 0.4905  393 GLU A CD  
2902  O OE1 . GLU A 393 ? 2.2911 2.0024 1.7442 -0.4674 -0.2843 0.5127  393 GLU A OE1 
2903  O OE2 . GLU A 393 ? 2.5403 2.2557 2.1212 -0.4106 -0.2883 0.5074  393 GLU A OE2 
2904  N N   . GLY A 394 ? 2.9051 2.5496 2.4265 -0.4269 -0.1661 0.3322  394 GLY A N   
2905  C CA  . GLY A 394 ? 2.8238 2.4486 2.3720 -0.4127 -0.1370 0.3136  394 GLY A CA  
2906  C C   . GLY A 394 ? 2.8205 2.4326 2.3429 -0.4143 -0.1069 0.2744  394 GLY A C   
2907  O O   . GLY A 394 ? 2.9131 2.5145 2.4502 -0.4059 -0.0813 0.2589  394 GLY A O   
2908  N N   . VAL A 395 ? 2.3777 1.9909 1.8624 -0.4249 -0.1088 0.2580  395 VAL A N   
2909  C CA  . VAL A 395 ? 2.2484 1.8437 1.7061 -0.4235 -0.0795 0.2217  395 VAL A CA  
2910  C C   . VAL A 395 ? 2.3200 1.9236 1.8028 -0.4083 -0.0861 0.2035  395 VAL A C   
2911  O O   . VAL A 395 ? 2.2955 1.9153 1.7775 -0.4168 -0.1117 0.2159  395 VAL A O   
2912  C CB  . VAL A 395 ? 2.2285 1.8037 1.6004 -0.4554 -0.0666 0.2155  395 VAL A CB  
2913  C CG1 . VAL A 395 ? 2.1925 1.7447 1.5371 -0.4502 -0.0360 0.1779  395 VAL A CG1 
2914  C CG2 . VAL A 395 ? 2.2230 1.7908 1.5694 -0.4700 -0.0561 0.2324  395 VAL A CG2 
2915  N N   . MET A 396 ? 2.1663 1.7621 1.6723 -0.3858 -0.0631 0.1756  396 MET A N   
2916  C CA  . MET A 396 ? 2.1046 1.7052 1.6336 -0.3694 -0.0654 0.1580  396 MET A CA  
2917  C C   . MET A 396 ? 2.2154 1.7879 1.7039 -0.3673 -0.0350 0.1274  396 MET A C   
2918  O O   . MET A 396 ? 2.1018 1.6627 1.5806 -0.3612 -0.0096 0.1161  396 MET A O   
2919  C CB  . MET A 396 ? 2.2058 1.8275 1.8136 -0.3368 -0.0694 0.1568  396 MET A CB  
2920  C CG  . MET A 396 ? 2.3579 1.9911 1.9947 -0.3201 -0.0765 0.1447  396 MET A CG  
2921  S SD  . MET A 396 ? 2.3766 2.0381 2.1030 -0.2854 -0.0851 0.1456  396 MET A SD  
2922  C CE  . MET A 396 ? 1.6113 1.2645 1.3487 -0.2658 -0.0525 0.1198  396 MET A CE  
2923  N N   . HIS A 397 ? 2.2117 1.7729 1.6750 -0.3738 -0.0372 0.1156  397 HIS A N   
2924  C CA  . HIS A 397 ? 2.1390 1.6649 1.5588 -0.3710 -0.0072 0.0875  397 HIS A CA  
2925  C C   . HIS A 397 ? 2.1802 1.7065 1.6297 -0.3494 -0.0066 0.0741  397 HIS A C   
2926  O O   . HIS A 397 ? 2.2135 1.7522 1.6705 -0.3598 -0.0288 0.0821  397 HIS A O   
2927  C CB  . HIS A 397 ? 2.0368 1.5330 1.3751 -0.4075 -0.0036 0.0829  397 HIS A CB  
2928  C CG  . HIS A 397 ? 2.2122 1.6657 1.5062 -0.4048 0.0247  0.0547  397 HIS A CG  
2929  N ND1 . HIS A 397 ? 2.3828 1.8250 1.6802 -0.3999 0.0227  0.0442  397 HIS A ND1 
2930  C CD2 . HIS A 397 ? 2.2494 1.6667 1.4949 -0.4049 0.0573  0.0353  397 HIS A CD2 
2931  C CE1 . HIS A 397 ? 2.3177 1.7133 1.5683 -0.3970 0.0530  0.0204  397 HIS A CE1 
2932  N NE2 . HIS A 397 ? 2.4011 1.7814 1.6203 -0.3986 0.0745  0.0141  397 HIS A NE2 
2933  N N   . VAL A 398 ? 2.2927 1.8090 1.7582 -0.3204 0.0180  0.0555  398 VAL A N   
2934  C CA  . VAL A 398 ? 2.2961 1.8075 1.7796 -0.3005 0.0214  0.0431  398 VAL A CA  
2935  C C   . VAL A 398 ? 2.3456 1.8205 1.7951 -0.2844 0.0563  0.0205  398 VAL A C   
2936  O O   . VAL A 398 ? 2.4349 1.8962 1.8556 -0.2879 0.0755  0.0149  398 VAL A O   
2937  C CB  . VAL A 398 ? 2.0816 1.6333 1.6429 -0.2716 0.0077  0.0489  398 VAL A CB  
2938  C CG1 . VAL A 398 ? 1.9718 1.5543 1.5648 -0.2843 -0.0255 0.0698  398 VAL A CG1 
2939  C CG2 . VAL A 398 ? 2.2776 1.8482 1.8763 -0.2507 0.0188  0.0469  398 VAL A CG2 
2940  N N   . GLY A 399 ? 2.3786 1.8385 1.8311 -0.2662 0.0651  0.0091  399 GLY A N   
2941  C CA  . GLY A 399 ? 2.5327 1.9519 1.9483 -0.2486 0.0990  -0.0105 399 GLY A CA  
2942  C C   . GLY A 399 ? 2.5758 1.9405 1.9134 -0.2794 0.1099  -0.0195 399 GLY A C   
2943  O O   . GLY A 399 ? 2.6199 1.9866 1.9304 -0.3159 0.0927  -0.0107 399 GLY A O   
2944  N N   . GLN A 400 ? 2.5919 1.9076 1.8904 -0.2666 0.1379  -0.0365 400 GLN A N   
2945  C CA  . GLN A 400 ? 2.6005 1.8583 1.8222 -0.3008 0.1474  -0.0471 400 GLN A CA  
2946  C C   . GLN A 400 ? 2.6831 1.8951 1.8357 -0.3156 0.1748  -0.0622 400 GLN A C   
2947  O O   . GLN A 400 ? 2.8165 2.0239 1.9284 -0.3561 0.1635  -0.0597 400 GLN A O   
2948  C CB  . GLN A 400 ? 2.5913 1.8060 1.7956 -0.2885 0.1616  -0.0571 400 GLN A CB  
2949  C CG  . GLN A 400 ? 2.7050 1.9176 1.9393 -0.2373 0.1843  -0.0627 400 GLN A CG  
2950  C CD  . GLN A 400 ? 2.8876 2.0438 2.0896 -0.2258 0.2041  -0.0719 400 GLN A CD  
2951  O OE1 . GLN A 400 ? 2.9144 2.0789 2.1384 -0.2250 0.1902  -0.0648 400 GLN A OE1 
2952  N NE2 . GLN A 400 ? 2.8789 1.9750 2.0273 -0.2159 0.2386  -0.0875 400 GLN A NE2 
2953  N N   . ARG A 401 ? 2.3258 1.5056 1.4632 -0.2843 0.2097  -0.0773 401 ARG A N   
2954  C CA  . ARG A 401 ? 2.5094 1.6412 1.5776 -0.2969 0.2398  -0.0943 401 ARG A CA  
2955  C C   . ARG A 401 ? 2.5149 1.6714 1.6099 -0.2624 0.2618  -0.0974 401 ARG A C   
2956  O O   . ARG A 401 ? 2.6319 1.8151 1.7245 -0.2790 0.2582  -0.0926 401 ARG A O   
2957  C CB  . ARG A 401 ? 2.5814 1.6338 1.5885 -0.2931 0.2707  -0.1145 401 ARG A CB  
2958  C CG  . ARG A 401 ? 2.5534 1.5784 1.5455 -0.3147 0.2560  -0.1132 401 ARG A CG  
2959  C CD  . ARG A 401 ? 2.6606 1.6215 1.6278 -0.2856 0.2878  -0.1264 401 ARG A CD  
2960  N NE  . ARG A 401 ? 2.6078 1.5253 1.5389 -0.3169 0.2812  -0.1298 401 ARG A NE  
2961  C CZ  . ARG A 401 ? 2.5412 1.3874 1.4341 -0.3058 0.3076  -0.1412 401 ARG A CZ  
2962  N NH1 . ARG A 401 ? 2.4722 1.2911 1.3693 -0.2562 0.3387  -0.1464 401 ARG A NH1 
2963  N NH2 . ARG A 401 ? 2.4989 1.3022 1.3501 -0.3445 0.3030  -0.1465 401 ARG A NH2 
2964  N N   . ASN A 402 ? 2.1936 1.3430 1.3121 -0.2168 0.2840  -0.1043 402 ASN A N   
2965  C CA  . ASN A 402 ? 2.3329 1.5092 1.4760 -0.1831 0.3080  -0.1092 402 ASN A CA  
2966  C C   . ASN A 402 ? 2.5180 1.7730 1.7452 -0.1704 0.2796  -0.0916 402 ASN A C   
2967  O O   . ASN A 402 ? 2.6559 1.9525 1.9070 -0.1725 0.2797  -0.0874 402 ASN A O   
2968  C CB  . ASN A 402 ? 2.2835 1.4278 1.4207 -0.1367 0.3424  -0.1219 402 ASN A CB  
2969  C CG  . ASN A 402 ? 2.3871 1.5865 1.5771 -0.0966 0.3568  -0.1215 402 ASN A CG  
2970  O OD1 . ASN A 402 ? 2.3585 1.5877 1.5985 -0.0569 0.3563  -0.1170 402 ASN A OD1 
2971  N ND2 . ASN A 402 ? 2.4816 1.6986 1.6608 -0.1082 0.3693  -0.1259 402 ASN A ND2 
2972  N N   . LEU A 403 ? 2.4602 1.7328 1.7284 -0.1591 0.2578  -0.0824 403 LEU A N   
2973  C CA  . LEU A 403 ? 2.2133 1.5566 1.5607 -0.1466 0.2317  -0.0682 403 LEU A CA  
2974  C C   . LEU A 403 ? 2.2478 1.6119 1.6020 -0.1866 0.1987  -0.0533 403 LEU A C   
2975  O O   . LEU A 403 ? 2.2784 1.6476 1.6483 -0.1960 0.1744  -0.0447 403 LEU A O   
2976  C CB  . LEU A 403 ? 1.9918 1.3439 1.3755 -0.1173 0.2241  -0.0658 403 LEU A CB  
2977  C CG  . LEU A 403 ? 2.2459 1.5507 1.5977 -0.0863 0.2541  -0.0774 403 LEU A CG  
2978  C CD1 . LEU A 403 ? 2.0861 1.3925 1.4624 -0.0679 0.2424  -0.0715 403 LEU A CD1 
2979  C CD2 . LEU A 403 ? 2.1035 1.4317 1.4753 -0.0477 0.2803  -0.0848 403 LEU A CD2 
2980  N N   . THR A 404 ? 2.2896 1.6680 1.6341 -0.2077 0.1983  -0.0490 404 THR A N   
2981  C CA  . THR A 404 ? 2.4035 1.7979 1.7482 -0.2451 0.1669  -0.0317 404 THR A CA  
2982  C C   . THR A 404 ? 2.2418 1.6911 1.6463 -0.2400 0.1534  -0.0181 404 THR A C   
2983  O O   . THR A 404 ? 2.1776 1.6433 1.5964 -0.2232 0.1744  -0.0249 404 THR A O   
2984  C CB  . THR A 404 ? 2.6210 1.9733 1.8873 -0.2836 0.1736  -0.0356 404 THR A CB  
2985  O OG1 . THR A 404 ? 2.5478 1.8864 1.7844 -0.2768 0.2059  -0.0482 404 THR A OG1 
2986  C CG2 . THR A 404 ? 2.6872 1.9880 1.9023 -0.2963 0.1777  -0.0466 404 THR A CG2 
2987  N N   . TRP A 405 ? 2.2529 1.7289 1.6913 -0.2539 0.1208  0.0000  405 TRP A N   
2988  C CA  . TRP A 405 ? 2.2093 1.7304 1.7056 -0.2494 0.1078  0.0132  405 TRP A CA  
2989  C C   . TRP A 405 ? 2.1759 1.7018 1.6605 -0.2831 0.0828  0.0352  405 TRP A C   
2990  O O   . TRP A 405 ? 2.0526 1.5793 1.5397 -0.2945 0.0577  0.0459  405 TRP A O   
2991  C CB  . TRP A 405 ? 2.1948 1.7489 1.7601 -0.2212 0.0945  0.0134  405 TRP A CB  
2992  C CG  . TRP A 405 ? 2.1868 1.7814 1.8108 -0.2165 0.0837  0.0231  405 TRP A CG  
2993  C CD1 . TRP A 405 ? 2.1630 1.7696 1.7906 -0.2248 0.0943  0.0264  405 TRP A CD1 
2994  C CD2 . TRP A 405 ? 2.1353 1.7607 1.8214 -0.2039 0.0619  0.0298  405 TRP A CD2 
2995  N NE1 . TRP A 405 ? 2.0672 1.7067 1.7546 -0.2197 0.0804  0.0347  405 TRP A NE1 
2996  C CE2 . TRP A 405 ? 2.0973 1.7479 1.8210 -0.2060 0.0606  0.0360  405 TRP A CE2 
2997  C CE3 . TRP A 405 ? 2.0773 1.7105 1.7896 -0.1919 0.0449  0.0302  405 TRP A CE3 
2998  C CZ2 . TRP A 405 ? 2.1463 1.8250 1.9311 -0.1963 0.0433  0.0412  405 TRP A CZ2 
2999  C CZ3 . TRP A 405 ? 1.8731 1.5383 1.6465 -0.1808 0.0278  0.0354  405 TRP A CZ3 
3000  C CH2 . TRP A 405 ? 2.1353 1.8207 1.9436 -0.1828 0.0272  0.0401  405 TRP A CH2 
3001  N N   . VAL A 406 ? 2.1440 1.6752 1.6164 -0.2978 0.0898  0.0428  406 VAL A N   
3002  C CA  . VAL A 406 ? 2.1366 1.6728 1.5962 -0.3276 0.0672  0.0671  406 VAL A CA  
3003  C C   . VAL A 406 ? 2.2191 1.7836 1.7275 -0.3229 0.0645  0.0802  406 VAL A C   
3004  O O   . VAL A 406 ? 2.1607 1.7336 1.6797 -0.3122 0.0888  0.0690  406 VAL A O   
3005  C CB  . VAL A 406 ? 2.0397 1.5458 1.4185 -0.3593 0.0781  0.0665  406 VAL A CB  
3006  C CG1 . VAL A 406 ? 2.0514 1.5674 1.4163 -0.3885 0.0552  0.0947  406 VAL A CG1 
3007  C CG2 . VAL A 406 ? 2.1599 1.6338 1.4884 -0.3694 0.0791  0.0530  406 VAL A CG2 
3008  N N   . ARG A 407 ? 2.3276 1.9064 1.8649 -0.3315 0.0361  0.1042  407 ARG A N   
3009  C CA  . ARG A 407 ? 2.2302 1.8277 1.8110 -0.3302 0.0335  0.1185  407 ARG A CA  
3010  C C   . ARG A 407 ? 2.2854 1.8760 1.8391 -0.3583 0.0149  0.1490  407 ARG A C   
3011  O O   . ARG A 407 ? 2.3262 1.9216 1.8914 -0.3613 -0.0138 0.1671  407 ARG A O   
3012  C CB  . ARG A 407 ? 2.1286 1.7491 1.7835 -0.3051 0.0193  0.1177  407 ARG A CB  
3013  C CG  . ARG A 407 ? 2.0982 1.7332 1.7854 -0.2767 0.0384  0.0903  407 ARG A CG  
3014  C CD  . ARG A 407 ? 2.1806 1.8397 1.9372 -0.2550 0.0240  0.0888  407 ARG A CD  
3015  N NE  . ARG A 407 ? 2.3072 1.9901 2.1040 -0.2365 0.0422  0.0703  407 ARG A NE  
3016  C CZ  . ARG A 407 ? 2.1231 1.8300 1.9787 -0.2176 0.0347  0.0629  407 ARG A CZ  
3017  N NH1 . ARG A 407 ? 1.8151 1.5231 1.6986 -0.2130 0.0111  0.0728  407 ARG A NH1 
3018  N NH2 . ARG A 407 ? 2.1738 1.9069 2.0592 -0.2034 0.0523  0.0444  407 ARG A NH2 
3019  N N   . ILE A 408 ? 2.3275 1.9101 1.8470 -0.3771 0.0308  0.1555  408 ILE A N   
3020  C CA  . ILE A 408 ? 2.4834 2.0596 1.9735 -0.4039 0.0139  0.1880  408 ILE A CA  
3021  C C   . ILE A 408 ? 2.5005 2.0867 2.0483 -0.3970 0.0006  0.2101  408 ILE A C   
3022  O O   . ILE A 408 ? 2.5111 2.1061 2.1016 -0.3840 0.0178  0.1977  408 ILE A O   
3023  C CB  . ILE A 408 ? 2.3710 1.9340 1.7998 -0.4280 0.0379  0.1875  408 ILE A CB  
3024  C CG1 . ILE A 408 ? 2.5094 2.0807 1.9682 -0.4276 0.0564  0.1920  408 ILE A CG1 
3025  C CG2 . ILE A 408 ? 2.3105 1.8606 1.6948 -0.4263 0.0635  0.1561  408 ILE A CG2 
3026  C CD1 . ILE A 408 ? 2.4816 2.0447 1.9135 -0.4540 0.0483  0.2257  408 ILE A CD1 
3027  N N   . GLY A 409 ? 2.6876 2.2728 2.2367 -0.4052 -0.0285 0.2414  409 GLY A N   
3028  C CA  . GLY A 409 ? 2.6983 2.2850 2.3011 -0.3965 -0.0411 0.2638  409 GLY A CA  
3029  C C   . GLY A 409 ? 2.7798 2.3522 2.3631 -0.4168 -0.0336 0.2888  409 GLY A C   
3030  O O   . GLY A 409 ? 2.8424 2.4066 2.3611 -0.4414 -0.0282 0.2986  409 GLY A O   
3031  N N   . LYS A 410 ? 2.5466 2.1141 2.1813 -0.4084 -0.0323 0.2983  410 LYS A N   
3032  C CA  . LYS A 410 ? 2.3520 1.9015 1.9712 -0.4284 -0.0239 0.3238  410 LYS A CA  
3033  C C   . LYS A 410 ? 2.4347 1.9729 2.0123 -0.4430 -0.0492 0.3650  410 LYS A C   
3034  O O   . LYS A 410 ? 2.6128 2.1398 2.1377 -0.4680 -0.0413 0.3837  410 LYS A O   
3035  C CB  . LYS A 410 ? 2.2625 1.8040 1.9475 -0.4167 -0.0197 0.3255  410 LYS A CB  
3036  C CG  . LYS A 410 ? 2.1098 1.6692 1.8339 -0.4061 0.0056  0.2861  410 LYS A CG  
3037  C CD  . LYS A 410 ? 1.9982 1.5492 1.7821 -0.4009 0.0105  0.2861  410 LYS A CD  
3038  C CE  . LYS A 410 ? 1.9423 1.5176 1.7564 -0.3983 0.0376  0.2500  410 LYS A CE  
3039  N NZ  . LYS A 410 ? 1.9311 1.5017 1.8068 -0.3933 0.0402  0.2440  410 LYS A NZ  
3040  N N   . GLU A 411 ? 2.4527 1.9974 2.0558 -0.4267 -0.0793 0.3799  411 GLU A N   
3041  C CA  . GLU A 411 ? 2.4931 2.0356 2.0627 -0.4369 -0.1074 0.4218  411 GLU A CA  
3042  C C   . GLU A 411 ? 2.7359 2.2834 2.2237 -0.4658 -0.1031 0.4217  411 GLU A C   
3043  O O   . GLU A 411 ? 2.8153 2.3528 2.2575 -0.4865 -0.1082 0.4542  411 GLU A O   
3044  C CB  . GLU A 411 ? 2.5136 2.0752 2.1207 -0.4143 -0.1382 0.4288  411 GLU A CB  
3045  C CG  . GLU A 411 ? 2.5312 2.1140 2.1524 -0.4025 -0.1349 0.3897  411 GLU A CG  
3046  C CD  . GLU A 411 ? 2.5393 2.1221 2.2262 -0.3774 -0.1201 0.3600  411 GLU A CD  
3047  O OE1 . GLU A 411 ? 2.3774 1.9650 2.1198 -0.3545 -0.1356 0.3669  411 GLU A OE1 
3048  O OE2 . GLU A 411 ? 2.6378 2.2183 2.3200 -0.3803 -0.0928 0.3299  411 GLU A OE2 
3049  N N   . ALA A 412 ? 3.0397 2.5993 2.5076 -0.4669 -0.0929 0.3865  412 ALA A N   
3050  C CA  . ALA A 412 ? 3.0743 2.6341 2.4615 -0.4948 -0.0857 0.3803  412 ALA A CA  
3051  C C   . ALA A 412 ? 3.1195 2.6627 2.4670 -0.5160 -0.0575 0.3837  412 ALA A C   
3052  O O   . ALA A 412 ? 3.1474 2.6868 2.4293 -0.5426 -0.0618 0.4048  412 ALA A O   
3053  C CB  . ALA A 412 ? 3.1029 2.6690 2.4821 -0.4889 -0.0734 0.3388  412 ALA A CB  
3054  N N   . PHE A 413 ? 2.9818 2.5197 2.3678 -0.5057 -0.0298 0.3634  413 PHE A N   
3055  C CA  . PHE A 413 ? 2.8813 2.4081 2.2374 -0.5261 -0.0010 0.3671  413 PHE A CA  
3056  C C   . PHE A 413 ? 2.9874 2.4996 2.3309 -0.5404 -0.0171 0.4150  413 PHE A C   
3057  O O   . PHE A 413 ? 3.0466 2.5510 2.3283 -0.5676 -0.0070 0.4315  413 PHE A O   
3058  C CB  . PHE A 413 ? 2.7795 2.3108 2.1921 -0.5113 0.0268  0.3399  413 PHE A CB  
3059  C CG  . PHE A 413 ? 2.9322 2.4583 2.3244 -0.5321 0.0575  0.3426  413 PHE A CG  
3060  C CD1 . PHE A 413 ? 2.8505 2.3844 2.1982 -0.5439 0.0879  0.3176  413 PHE A CD1 
3061  C CD2 . PHE A 413 ? 3.0115 2.5236 2.4287 -0.5402 0.0578  0.3702  413 PHE A CD2 
3062  C CE1 . PHE A 413 ? 2.9368 2.4714 2.2678 -0.5635 0.1176  0.3200  413 PHE A CE1 
3063  C CE2 . PHE A 413 ? 2.9974 2.5065 2.3959 -0.5623 0.0874  0.3730  413 PHE A CE2 
3064  C CZ  . PHE A 413 ? 3.0279 2.5516 2.3844 -0.5741 0.1171  0.3479  413 PHE A CZ  
3065  N N   . GLU A 414 ? 2.9277 2.4349 2.3266 -0.5215 -0.0404 0.4371  414 GLU A N   
3066  C CA  . GLU A 414 ? 2.8494 2.3380 2.2389 -0.5301 -0.0577 0.4868  414 GLU A CA  
3067  C C   . GLU A 414 ? 2.8457 2.3450 2.1695 -0.5462 -0.0832 0.5132  414 GLU A C   
3068  O O   . GLU A 414 ? 2.7214 2.2082 2.0029 -0.5648 -0.0886 0.5518  414 GLU A O   
3069  C CB  . GLU A 414 ? 2.7667 2.2465 2.2305 -0.5018 -0.0769 0.5014  414 GLU A CB  
3070  C CG  . GLU A 414 ? 2.6162 2.0840 2.1412 -0.4909 -0.0527 0.4782  414 GLU A CG  
3071  C CD  . GLU A 414 ? 2.5375 1.9935 2.1344 -0.4630 -0.0692 0.4868  414 GLU A CD  
3072  O OE1 . GLU A 414 ? 2.6578 2.1205 2.2635 -0.4470 -0.0995 0.5072  414 GLU A OE1 
3073  O OE2 . GLU A 414 ? 2.4861 1.9281 2.1300 -0.4580 -0.0510 0.4721  414 GLU A OE2 
3074  N N   . LYS A 415 ? 2.9989 2.5212 2.3138 -0.5405 -0.0985 0.4935  415 LYS A N   
3075  C CA  . LYS A 415 ? 3.0135 2.5523 2.2640 -0.5597 -0.1234 0.5133  415 LYS A CA  
3076  C C   . LYS A 415 ? 2.9894 2.5234 2.1584 -0.5922 -0.0984 0.4978  415 LYS A C   
3077  O O   . LYS A 415 ? 2.8310 2.3756 1.9338 -0.6156 -0.1146 0.5151  415 LYS A O   
3078  C CB  . LYS A 415 ? 2.9283 2.4931 2.1967 -0.5468 -0.1456 0.4947  415 LYS A CB  
3079  C CG  . LYS A 415 ? 2.6840 2.2609 2.0276 -0.5152 -0.1728 0.5098  415 LYS A CG  
3080  C CD  . LYS A 415 ? 2.4971 2.0735 1.8480 -0.5105 -0.1999 0.5634  415 LYS A CD  
3081  C CE  . LYS A 415 ? 2.2063 1.7927 1.6350 -0.4756 -0.2227 0.5760  415 LYS A CE  
3082  N NZ  . LYS A 415 ? 2.3587 1.9460 1.7893 -0.4689 -0.2503 0.6308  415 LYS A NZ  
3083  N N   . GLY A 416 ? 2.9281 2.4500 2.1023 -0.5934 -0.0604 0.4657  416 GLY A N   
3084  C CA  . GLY A 416 ? 2.7792 2.2960 1.8793 -0.6213 -0.0317 0.4484  416 GLY A CA  
3085  C C   . GLY A 416 ? 3.0183 2.5434 2.0798 -0.6265 -0.0288 0.4121  416 GLY A C   
3086  O O   . GLY A 416 ? 2.9938 2.5133 1.9831 -0.6515 -0.0090 0.3988  416 GLY A O   
3087  N N   . PHE A 417 ? 3.0946 2.6301 2.2006 -0.6045 -0.0461 0.3960  417 PHE A N   
3088  C CA  . PHE A 417 ? 3.0610 2.5984 2.1333 -0.6092 -0.0415 0.3598  417 PHE A CA  
3089  C C   . PHE A 417 ? 3.0613 2.5828 2.1045 -0.6133 0.0028  0.3220  417 PHE A C   
3090  O O   . PHE A 417 ? 2.8981 2.4172 1.9848 -0.5981 0.0265  0.3143  417 PHE A O   
3091  C CB  . PHE A 417 ? 2.9095 2.4574 2.0474 -0.5803 -0.0571 0.3442  417 PHE A CB  
3092  C CG  . PHE A 417 ? 3.0195 2.5601 2.1362 -0.5789 -0.0414 0.3015  417 PHE A CG  
3093  C CD1 . PHE A 417 ? 3.0269 2.5713 2.0945 -0.5984 -0.0587 0.2965  417 PHE A CD1 
3094  C CD2 . PHE A 417 ? 2.9047 2.4345 2.0490 -0.5587 -0.0088 0.2671  417 PHE A CD2 
3095  C CE1 . PHE A 417 ? 2.8925 2.4220 1.9376 -0.5983 -0.0421 0.2576  417 PHE A CE1 
3096  C CE2 . PHE A 417 ? 2.7635 2.2809 1.8860 -0.5549 0.0069  0.2305  417 PHE A CE2 
3097  C CZ  . PHE A 417 ? 2.8161 2.3293 1.8879 -0.5752 -0.0088 0.2257  417 PHE A CZ  
3098  N N   . ARG A 418 ? 3.4855 2.9975 2.4588 -0.6329 0.0144  0.2982  418 ARG A N   
3099  C CA  . ARG A 418 ? 3.3987 2.8944 2.3466 -0.6316 0.0588  0.2600  418 ARG A CA  
3100  C C   . ARG A 418 ? 3.4429 2.9248 2.3741 -0.6243 0.0675  0.2211  418 ARG A C   
3101  O O   . ARG A 418 ? 3.5143 2.9977 2.4248 -0.6353 0.0401  0.2245  418 ARG A O   
3102  C CB  . ARG A 418 ? 3.3607 2.8478 2.2260 -0.6649 0.0778  0.2661  418 ARG A CB  
3103  C CG  . ARG A 418 ? 3.3820 2.8551 2.2199 -0.6630 0.1258  0.2288  418 ARG A CG  
3104  C CD  . ARG A 418 ? 3.2569 2.7405 2.1691 -0.6342 0.1500  0.2192  418 ARG A CD  
3105  N NE  . ARG A 418 ? 3.2864 2.7828 2.2287 -0.6401 0.1436  0.2543  418 ARG A NE  
3106  C CZ  . ARG A 418 ? 3.3998 2.8967 2.3051 -0.6616 0.1661  0.2656  418 ARG A CZ  
3107  N NH1 . ARG A 418 ? 3.3655 2.8526 2.1915 -0.6836 0.1899  0.2496  418 ARG A NH1 
3108  N NH2 . ARG A 418 ? 3.4182 2.9238 2.3646 -0.6623 0.1660  0.2922  418 ARG A NH2 
3109  N N   . LEU A 419 ? 2.9606 2.4302 1.9008 -0.6064 0.1047  0.1864  419 LEU A N   
3110  C CA  . LEU A 419 ? 3.0290 2.4763 1.9449 -0.5992 0.1182  0.1493  419 LEU A CA  
3111  C C   . LEU A 419 ? 3.0317 2.4595 1.8545 -0.6362 0.1136  0.1438  419 LEU A C   
3112  O O   . LEU A 419 ? 3.0961 2.5044 1.8967 -0.6378 0.1120  0.1210  419 LEU A O   
3113  C CB  . LEU A 419 ? 2.9421 2.3763 1.8524 -0.5828 0.1654  0.1169  419 LEU A CB  
3114  C CG  . LEU A 419 ? 2.8293 2.2766 1.8226 -0.5412 0.1769  0.1028  419 LEU A CG  
3115  C CD1 . LEU A 419 ? 2.7234 2.2017 1.7893 -0.5315 0.1564  0.1319  419 LEU A CD1 
3116  C CD2 . LEU A 419 ? 2.7737 2.2161 1.7587 -0.5260 0.2232  0.0746  419 LEU A CD2 
3117  N N   . LYS A 420 ? 2.8480 2.2806 1.6162 -0.6665 0.1123  0.1639  420 LYS A N   
3118  C CA  . LYS A 420 ? 2.9081 2.3265 1.5814 -0.7063 0.1063  0.1595  420 LYS A CA  
3119  C C   . LYS A 420 ? 3.1018 2.5334 1.7828 -0.7158 0.0624  0.1728  420 LYS A C   
3120  O O   . LYS A 420 ? 3.1258 2.5389 1.7502 -0.7373 0.0615  0.1505  420 LYS A O   
3121  C CB  . LYS A 420 ? 2.7859 2.2153 1.4075 -0.7355 0.1066  0.1867  420 LYS A CB  
3122  C CG  . LYS A 420 ? 2.6628 2.0816 1.2636 -0.7335 0.1526  0.1716  420 LYS A CG  
3123  C CD  . LYS A 420 ? 2.5337 1.9638 1.0819 -0.7643 0.1522  0.2014  420 LYS A CD  
3124  C CE  . LYS A 420 ? 2.6178 2.0415 1.1458 -0.7640 0.2001  0.1854  420 LYS A CE  
3125  N NZ  . LYS A 420 ? 2.6297 2.0642 1.1048 -0.7955 0.2000  0.2168  420 LYS A NZ  
3126  N N   . HIS A 421 ? 3.2360 2.6981 1.9859 -0.7002 0.0291  0.2063  421 HIS A N   
3127  C CA  . HIS A 421 ? 3.2485 2.7326 2.0119 -0.7079 -0.0141 0.2228  421 HIS A CA  
3128  C C   . HIS A 421 ? 3.1586 2.6281 1.9494 -0.6910 -0.0095 0.1903  421 HIS A C   
3129  O O   . HIS A 421 ? 3.2129 2.6940 1.9936 -0.7061 -0.0368 0.1917  421 HIS A O   
3130  C CB  . HIS A 421 ? 3.2210 2.7387 2.0523 -0.6915 -0.0468 0.2669  421 HIS A CB  
3131  C CG  . HIS A 421 ? 3.2195 2.7457 2.0178 -0.7095 -0.0505 0.3010  421 HIS A CG  
3132  N ND1 . HIS A 421 ? 3.0065 2.5439 1.8597 -0.6914 -0.0582 0.3345  421 HIS A ND1 
3133  C CD2 . HIS A 421 ? 3.0958 2.6180 1.8077 -0.7453 -0.0458 0.3064  421 HIS A CD2 
3134  C CE1 . HIS A 421 ? 2.8693 2.4081 1.6705 -0.7153 -0.0582 0.3614  421 HIS A CE1 
3135  N NE2 . HIS A 421 ? 2.8945 2.4268 1.6095 -0.7480 -0.0514 0.3451  421 HIS A NE2 
3136  N N   . PHE A 422 ? 2.9093 2.3567 1.7331 -0.6614 0.0240  0.1627  422 PHE A N   
3137  C CA  . PHE A 422 ? 2.8218 2.2513 1.6675 -0.6438 0.0309  0.1335  422 PHE A CA  
3138  C C   . PHE A 422 ? 2.7872 2.1833 1.5447 -0.6765 0.0428  0.1057  422 PHE A C   
3139  O O   . PHE A 422 ? 2.6656 2.0621 1.4140 -0.6903 0.0223  0.1008  422 PHE A O   
3140  C CB  . PHE A 422 ? 2.6248 2.0404 1.5202 -0.6041 0.0649  0.1116  422 PHE A CB  
3141  C CG  . PHE A 422 ? 2.4784 1.9232 1.4699 -0.5691 0.0517  0.1285  422 PHE A CG  
3142  C CD1 . PHE A 422 ? 2.3533 1.8216 1.3940 -0.5615 0.0166  0.1453  422 PHE A CD1 
3143  C CD2 . PHE A 422 ? 2.5372 1.9870 1.5702 -0.5439 0.0762  0.1243  422 PHE A CD2 
3144  C CE1 . PHE A 422 ? 2.3105 1.8020 1.4361 -0.5295 0.0068  0.1573  422 PHE A CE1 
3145  C CE2 . PHE A 422 ? 2.4444 1.9193 1.5625 -0.5145 0.0649  0.1361  422 PHE A CE2 
3146  C CZ  . PHE A 422 ? 2.3432 1.8362 1.5054 -0.5073 0.0307  0.1520  422 PHE A CZ  
3147  N N   . GLY A 423 ? 2.7881 2.1559 1.4807 -0.6903 0.0762  0.0872  423 GLY A N   
3148  C CA  . GLY A 423 ? 2.8352 2.1648 1.4373 -0.7229 0.0919  0.0577  423 GLY A CA  
3149  C C   . GLY A 423 ? 3.0102 2.3591 1.5625 -0.7671 0.0550  0.0733  423 GLY A C   
3150  O O   . GLY A 423 ? 3.0903 2.4146 1.5929 -0.7919 0.0548  0.0497  423 GLY A O   
3151  N N   . GLU A 424 ? 2.9789 2.3725 1.5440 -0.7778 0.0234  0.1138  424 GLU A N   
3152  C CA  . GLU A 424 ? 2.8901 2.3144 1.4136 -0.8173 -0.0161 0.1350  424 GLU A CA  
3153  C C   . GLU A 424 ? 2.8716 2.3213 1.4468 -0.8122 -0.0504 0.1417  424 GLU A C   
3154  O O   . GLU A 424 ? 2.9202 2.3719 1.4487 -0.8463 -0.0658 0.1308  424 GLU A O   
3155  C CB  . GLU A 424 ? 2.7980 2.2628 1.3270 -0.8233 -0.0396 0.1808  424 GLU A CB  
3156  C CG  . GLU A 424 ? 2.9513 2.3975 1.4144 -0.8396 -0.0100 0.1776  424 GLU A CG  
3157  C CD  . GLU A 424 ? 2.8802 2.3629 1.3320 -0.8535 -0.0349 0.2246  424 GLU A CD  
3158  O OE1 . GLU A 424 ? 2.9078 2.4261 1.4252 -0.8361 -0.0692 0.2622  424 GLU A OE1 
3159  O OE2 . GLU A 424 ? 2.7408 2.2147 1.1166 -0.8809 -0.0190 0.2245  424 GLU A OE2 
3160  N N   . VAL A 425 ? 2.9010 2.3714 1.5710 -0.7718 -0.0614 0.1585  425 VAL A N   
3161  C CA  . VAL A 425 ? 2.7605 2.2582 1.4873 -0.7625 -0.0914 0.1655  425 VAL A CA  
3162  C C   . VAL A 425 ? 2.7587 2.2172 1.4605 -0.7700 -0.0721 0.1240  425 VAL A C   
3163  O O   . VAL A 425 ? 2.7664 2.2422 1.4637 -0.7909 -0.0959 0.1226  425 VAL A O   
3164  C CB  . VAL A 425 ? 2.2598 1.7798 1.0907 -0.7147 -0.0994 0.1860  425 VAL A CB  
3165  C CG1 . VAL A 425 ? 2.1758 1.7073 1.0638 -0.6978 -0.1131 0.1777  425 VAL A CG1 
3166  C CG2 . VAL A 425 ? 2.2393 1.8031 1.1003 -0.7117 -0.1307 0.2329  425 VAL A CG2 
3167  N N   . ILE A 426 ? 2.7094 2.1159 1.3954 -0.7529 -0.0285 0.0914  426 ILE A N   
3168  C CA  . ILE A 426 ? 2.7624 2.1218 1.4235 -0.7554 -0.0056 0.0532  426 ILE A CA  
3169  C C   . ILE A 426 ? 2.9042 2.2426 1.4674 -0.8094 -0.0067 0.0347  426 ILE A C   
3170  O O   . ILE A 426 ? 2.8561 2.2015 1.4113 -0.8329 -0.0264 0.0291  426 ILE A O   
3171  C CB  . ILE A 426 ? 2.6348 1.9486 1.3103 -0.7172 0.0403  0.0276  426 ILE A CB  
3172  C CG1 . ILE A 426 ? 2.6061 1.9497 1.3825 -0.6679 0.0354  0.0460  426 ILE A CG1 
3173  C CG2 . ILE A 426 ? 2.8575 2.1135 1.4975 -0.7194 0.0671  -0.0108 426 ILE A CG2 
3174  C CD1 . ILE A 426 ? 2.6016 1.9724 1.4474 -0.6516 0.0077  0.0564  426 ILE A CD1 
3175  N N   . TYR A 427 ? 3.0280 2.3437 1.5178 -0.8308 0.0143  0.0248  427 TYR A N   
3176  C CA  . TYR A 427 ? 3.0565 2.3521 1.4468 -0.8855 0.0138  0.0049  427 TYR A CA  
3177  C C   . TYR A 427 ? 3.0869 2.4392 1.4724 -0.9227 -0.0363 0.0291  427 TYR A C   
3178  O O   . TYR A 427 ? 3.1753 2.5126 1.5114 -0.9608 -0.0413 0.0069  427 TYR A O   
3179  C CB  . TYR A 427 ? 3.2775 2.5593 1.5954 -0.9042 0.0348  0.0012  427 TYR A CB  
3180  C CG  . TYR A 427 ? 3.4956 2.7066 1.7637 -0.8953 0.0896  -0.0407 427 TYR A CG  
3181  C CD1 . TYR A 427 ? 3.2264 2.3779 1.4510 -0.9075 0.1127  -0.0808 427 TYR A CD1 
3182  C CD2 . TYR A 427 ? 3.6901 2.8934 1.9554 -0.8739 0.1195  -0.0396 427 TYR A CD2 
3183  C CE1 . TYR A 427 ? 3.1873 2.2710 1.3668 -0.8951 0.1646  -0.1183 427 TYR A CE1 
3184  C CE2 . TYR A 427 ? 3.6250 2.7682 1.8482 -0.8621 0.1710  -0.0773 427 TYR A CE2 
3185  C CZ  . TYR A 427 ? 3.3345 2.4166 1.5147 -0.8709 0.1937  -0.1165 427 TYR A CZ  
3186  O OH  . TYR A 427 ? 2.9710 1.9907 1.1099 -0.8554 0.2462  -0.1532 427 TYR A OH  
3187  N N   . ALA A 428 ? 2.8545 2.2700 1.2901 -0.9121 -0.0714 0.0733  428 ALA A N   
3188  C CA  . ALA A 428 ? 2.8119 2.2902 1.2437 -0.9445 -0.1205 0.1013  428 ALA A CA  
3189  C C   . ALA A 428 ? 2.9568 2.4539 1.4406 -0.9417 -0.1408 0.0971  428 ALA A C   
3190  O O   . ALA A 428 ? 2.9244 2.4466 1.3738 -0.9832 -0.1651 0.0936  428 ALA A O   
3191  C CB  . ALA A 428 ? 2.5982 2.1336 1.0790 -0.9251 -0.1503 0.1517  428 ALA A CB  
3192  N N   . LYS A 429 ? 2.9879 2.4761 1.5541 -0.8945 -0.1307 0.0972  429 LYS A N   
3193  C CA  . LYS A 429 ? 2.8021 2.3061 1.4209 -0.8881 -0.1457 0.0928  429 LYS A CA  
3194  C C   . LYS A 429 ? 2.8158 2.2576 1.3779 -0.9127 -0.1170 0.0473  429 LYS A C   
3195  O O   . LYS A 429 ? 2.9131 2.3702 1.4823 -0.9340 -0.1337 0.0408  429 LYS A O   
3196  C CB  . LYS A 429 ? 2.5321 2.0428 1.2502 -0.8304 -0.1411 0.1051  429 LYS A CB  
3197  C CG  . LYS A 429 ? 2.4380 2.0127 1.2255 -0.8063 -0.1751 0.1509  429 LYS A CG  
3198  C CD  . LYS A 429 ? 2.2579 1.8990 1.0883 -0.8168 -0.2189 0.1743  429 LYS A CD  
3199  C CE  . LYS A 429 ? 2.5649 2.2604 1.3631 -0.8483 -0.2553 0.2057  429 LYS A CE  
3200  N NZ  . LYS A 429 ? 2.5358 2.3059 1.4013 -0.8404 -0.2981 0.2383  429 LYS A NZ  
3201  N N   . MET A 430 ? 2.8172 2.1895 1.3247 -0.9094 -0.0733 0.0168  430 MET A N   
3202  C CA  . MET A 430 ? 2.7840 2.0849 1.2308 -0.9311 -0.0412 -0.0277 430 MET A CA  
3203  C C   . MET A 430 ? 2.8983 2.2071 1.2633 -0.9971 -0.0589 -0.0394 430 MET A C   
3204  O O   . MET A 430 ? 2.9673 2.2512 1.3115 -1.0231 -0.0564 -0.0627 430 MET A O   
3205  C CB  . MET A 430 ? 2.7292 1.9572 1.1319 -0.9121 0.0098  -0.0561 430 MET A CB  
3206  C CG  . MET A 430 ? 2.7735 1.9879 1.2516 -0.8496 0.0321  -0.0526 430 MET A CG  
3207  S SD  . MET A 430 ? 3.2724 2.4594 1.8024 -0.8248 0.0397  -0.0672 430 MET A SD  
3208  C CE  . MET A 430 ? 2.5262 1.6926 1.1196 -0.7553 0.0731  -0.0678 430 MET A CE  
3209  N N   . LEU A 431 ? 2.7593 2.1023 1.0787 -1.0245 -0.0762 -0.0234 431 LEU A N   
3210  C CA  . LEU A 431 ? 2.9135 2.2713 1.1516 -1.0892 -0.0952 -0.0339 431 LEU A CA  
3211  C C   . LEU A 431 ? 3.0988 2.5366 1.3838 -1.1091 -0.1458 -0.0081 431 LEU A C   
3212  O O   . LEU A 431 ? 3.2403 2.6831 1.4760 -1.1606 -0.1578 -0.0263 431 LEU A O   
3213  C CB  . LEU A 431 ? 3.0099 2.3884 1.1875 -1.1103 -0.1011 -0.0199 431 LEU A CB  
3214  C CG  . LEU A 431 ? 3.0650 2.3684 1.1684 -1.1100 -0.0512 -0.0521 431 LEU A CG  
3215  C CD1 . LEU A 431 ? 3.0851 2.4220 1.1546 -1.1174 -0.0597 -0.0268 431 LEU A CD1 
3216  C CD2 . LEU A 431 ? 3.2708 2.5109 1.2756 -1.1600 -0.0269 -0.1010 431 LEU A CD2 
3217  N N   . ASP A 432 ? 2.8758 2.3768 1.2553 -1.0691 -0.1746 0.0331  432 ASP A N   
3218  C CA  . ASP A 432 ? 2.8947 2.4780 1.3295 -1.0795 -0.2218 0.0610  432 ASP A CA  
3219  C C   . ASP A 432 ? 2.9332 2.4991 1.4032 -1.0794 -0.2150 0.0392  432 ASP A C   
3220  O O   . ASP A 432 ? 2.9213 2.5206 1.3735 -1.1234 -0.2374 0.0331  432 ASP A O   
3221  C CB  . ASP A 432 ? 2.6795 2.3250 1.2042 -1.0315 -0.2487 0.1099  432 ASP A CB  
3222  C CG  . ASP A 432 ? 2.5211 2.2536 1.1154 -1.0310 -0.2951 0.1414  432 ASP A CG  
3223  O OD1 . ASP A 432 ? 2.6596 2.4438 1.2177 -1.0776 -0.3261 0.1476  432 ASP A OD1 
3224  O OD2 . ASP A 432 ? 2.5550 2.3069 1.2402 -0.9839 -0.3003 0.1595  432 ASP A OD2 
3225  N N   . GLU A 433 ? 3.2297 2.7461 1.7480 -1.0320 -0.1842 0.0279  433 GLU A N   
3226  C CA  . GLU A 433 ? 3.2682 2.7643 1.8208 -1.0273 -0.1751 0.0098  433 GLU A CA  
3227  C C   . GLU A 433 ? 3.3010 2.7110 1.7692 -1.0638 -0.1387 -0.0378 433 GLU A C   
3228  O O   . GLU A 433 ? 3.2902 2.7038 1.7435 -1.1018 -0.1471 -0.0523 433 GLU A O   
3229  C CB  . GLU A 433 ? 3.2758 2.7561 1.9128 -0.9609 -0.1579 0.0183  433 GLU A CB  
3230  C CG  . GLU A 433 ? 3.0583 2.6173 1.7875 -0.9232 -0.1918 0.0620  433 GLU A CG  
3231  C CD  . GLU A 433 ? 3.2857 2.9273 2.0604 -0.9413 -0.2351 0.0846  433 GLU A CD  
3232  O OE1 . GLU A 433 ? 3.5939 3.2305 2.3694 -0.9622 -0.2335 0.0665  433 GLU A OE1 
3233  O OE2 . GLU A 433 ? 3.1906 2.9025 2.0016 -0.9335 -0.2698 0.1216  433 GLU A OE2 
3234  N N   . PHE A 434 ? 3.2069 2.5407 1.6182 -1.0544 -0.0983 -0.0619 434 PHE A N   
3235  C CA  . PHE A 434 ? 3.2378 2.4763 1.5702 -1.0811 -0.0572 -0.1087 434 PHE A CA  
3236  C C   . PHE A 434 ? 3.3177 2.5403 1.5440 -1.1425 -0.0565 -0.1297 434 PHE A C   
3237  O O   . PHE A 434 ? 3.3744 2.5085 1.5238 -1.1572 -0.0151 -0.1685 434 PHE A O   
3238  C CB  . PHE A 434 ? 3.1769 2.3407 1.5207 -1.0269 -0.0104 -0.1240 434 PHE A CB  
3239  C CG  . PHE A 434 ? 3.2943 2.4883 1.7433 -0.9691 -0.0173 -0.1001 434 PHE A CG  
3240  C CD1 . PHE A 434 ? 3.1920 2.4229 1.6942 -0.9734 -0.0405 -0.0901 434 PHE A CD1 
3241  C CD2 . PHE A 434 ? 3.2775 2.4691 1.7729 -0.9133 -0.0018 -0.0876 434 PHE A CD2 
3242  C CE1 . PHE A 434 ? 3.0386 2.2990 1.6345 -0.9219 -0.0469 -0.0694 434 PHE A CE1 
3243  C CE2 . PHE A 434 ? 3.1312 2.3526 1.7206 -0.8635 -0.0092 -0.0677 434 PHE A CE2 
3244  C CZ  . PHE A 434 ? 3.0616 2.3159 1.6996 -0.8673 -0.0314 -0.0590 434 PHE A CZ  
3245  N N   . GLY A 435 ? 3.1811 2.4868 1.4025 -1.1766 -0.1006 -0.1049 435 GLY A N   
3246  C CA  . GLY A 435 ? 3.1515 2.4559 1.2731 -1.2394 -0.1065 -0.1222 435 GLY A CA  
3247  C C   . GLY A 435 ? 3.3287 2.5719 1.3883 -1.2855 -0.0804 -0.1636 435 GLY A C   
3248  O O   . GLY A 435 ? 3.4170 2.6225 1.4124 -1.3095 -0.0554 -0.1839 435 GLY A O   
3249  N N   . SER A 436 ? 3.5067 2.7426 1.6006 -1.2917 -0.0819 -0.1719 436 SER A N   
3250  C CA  . SER A 436 ? 3.5527 2.7336 1.6081 -1.3273 -0.0535 -0.2035 436 SER A CA  
3251  C C   . SER A 436 ? 3.5489 2.6037 1.5580 -1.3050 0.0067  -0.2413 436 SER A C   
3252  O O   . SER A 436 ? 3.4987 2.4952 1.4553 -1.3343 0.0374  -0.2690 436 SER A O   
3253  C CB  . SER A 436 ? 3.5932 2.8135 1.7046 -1.3389 -0.0747 -0.1954 436 SER A CB  
3254  O OG  . SER A 436 ? 3.4516 2.6614 1.6215 -1.2938 -0.0767 -0.1872 436 SER A OG  
3255  N N   . VAL A 437 ? 3.3909 2.4047 1.4198 -1.2524 0.0241  -0.2419 437 VAL A N   
3256  C CA  . VAL A 437 ? 3.4093 2.3089 1.4027 -1.2228 0.0813  -0.2742 437 VAL A CA  
3257  C C   . VAL A 437 ? 3.3234 2.1918 1.2780 -1.1968 0.1072  -0.2811 437 VAL A C   
3258  O O   . VAL A 437 ? 3.2414 2.0201 1.1564 -1.1793 0.1569  -0.3094 437 VAL A O   
3259  C CB  . VAL A 437 ? 3.2770 2.1421 1.3274 -1.1783 0.0927  -0.2737 437 VAL A CB  
3260  C CG1 . VAL A 437 ? 3.1879 2.0664 1.2620 -1.2092 0.0777  -0.2740 437 VAL A CG1 
3261  C CG2 . VAL A 437 ? 3.1447 2.0874 1.2995 -1.1172 0.0695  -0.2305 437 VAL A CG2 
3262  N N   . VAL A 438 ? 3.3740 2.3181 1.3437 -1.1927 0.0746  -0.2528 438 VAL A N   
3263  C CA  . VAL A 438 ? 3.2330 2.1613 1.1759 -1.1666 0.0983  -0.2528 438 VAL A CA  
3264  C C   . VAL A 438 ? 3.3149 2.2500 1.1913 -1.2140 0.1003  -0.2627 438 VAL A C   
3265  O O   . VAL A 438 ? 3.2363 2.2511 1.1209 -1.2513 0.0570  -0.2403 438 VAL A O   
3266  C CB  . VAL A 438 ? 3.0202 2.0347 1.0518 -1.1219 0.0687  -0.2047 438 VAL A CB  
3267  C CG1 . VAL A 438 ? 3.0474 2.0662 1.0409 -1.1150 0.0818  -0.1999 438 VAL A CG1 
3268  C CG2 . VAL A 438 ? 2.9815 1.9915 1.1096 -1.0559 0.0791  -0.1905 438 VAL A CG2 
3269  N N   . THR A 444 ? 2.5373 1.6547 1.0230 -0.6449 0.2909  -0.1035 444 THR A N   
3270  C CA  . THR A 444 ? 2.5742 1.7076 1.0774 -0.6203 0.3233  -0.1046 444 THR A CA  
3271  C C   . THR A 444 ? 2.6922 1.8672 1.3011 -0.5743 0.3164  -0.0879 444 THR A C   
3272  O O   . THR A 444 ? 2.7065 1.8630 1.3516 -0.5406 0.3263  -0.1021 444 THR A O   
3273  C CB  . THR A 444 ? 2.6066 1.6842 1.0512 -0.6097 0.3763  -0.1439 444 THR A CB  
3274  O OG1 . THR A 444 ? 2.7061 1.7497 1.0497 -0.6574 0.3818  -0.1588 444 THR A OG1 
3275  C CG2 . THR A 444 ? 2.7613 1.8616 1.2339 -0.5793 0.4116  -0.1466 444 THR A CG2 
3276  N N   . ILE A 445 ? 2.7239 1.9511 1.3779 -0.5743 0.2998  -0.0585 445 ILE A N   
3277  C CA  . ILE A 445 ? 2.6048 1.8736 1.3588 -0.5345 0.2930  -0.0438 445 ILE A CA  
3278  C C   . ILE A 445 ? 2.5469 1.8233 1.3169 -0.5061 0.3364  -0.0595 445 ILE A C   
3279  O O   . ILE A 445 ? 2.6767 1.9463 1.3916 -0.5250 0.3613  -0.0663 445 ILE A O   
3280  C CB  . ILE A 445 ? 2.3631 1.6799 1.1616 -0.5479 0.2541  -0.0048 445 ILE A CB  
3281  C CG1 . ILE A 445 ? 2.2542 1.5697 1.0278 -0.5795 0.2124  0.0124  445 ILE A CG1 
3282  C CG2 . ILE A 445 ? 2.4544 1.8078 1.3524 -0.5099 0.2457  0.0062  445 ILE A CG2 
3283  C CD1 . ILE A 445 ? 2.6964 2.0146 1.3997 -0.6235 0.2026  0.0275  445 ILE A CD1 
3284  N N   . ILE A 446 ? 2.4360 1.7304 1.2789 -0.4627 0.3447  -0.0648 446 ILE A N   
3285  C CA  . ILE A 446 ? 2.4485 1.7619 1.3178 -0.4320 0.3846  -0.0788 446 ILE A CA  
3286  C C   . ILE A 446 ? 2.5923 1.9628 1.5596 -0.4056 0.3705  -0.0614 446 ILE A C   
3287  O O   . ILE A 446 ? 2.6404 2.0161 1.6598 -0.3759 0.3591  -0.0640 446 ILE A O   
3288  C CB  . ILE A 446 ? 2.5842 1.8553 1.4307 -0.4009 0.4205  -0.1116 446 ILE A CB  
3289  C CG1 . ILE A 446 ? 2.6965 1.9081 1.4407 -0.4289 0.4429  -0.1334 446 ILE A CG1 
3290  C CG2 . ILE A 446 ? 2.5979 1.9027 1.4934 -0.3602 0.4548  -0.1221 446 ILE A CG2 
3291  C CD1 . ILE A 446 ? 2.6721 1.8326 1.3742 -0.4463 0.4236  -0.1406 446 ILE A CD1 
3292  N N   . THR A 447 ? 2.8171 2.2272 1.8057 -0.4184 0.3711  -0.0444 447 THR A N   
3293  C CA  . THR A 447 ? 2.7870 2.2502 1.8674 -0.3960 0.3615  -0.0313 447 THR A CA  
3294  C C   . THR A 447 ? 2.8074 2.2993 1.9098 -0.3713 0.4035  -0.0491 447 THR A C   
3295  O O   . THR A 447 ? 2.5835 2.1252 1.7564 -0.3581 0.4018  -0.0410 447 THR A O   
3296  C CB  . THR A 447 ? 2.6472 2.1325 1.7467 -0.4254 0.3282  0.0022  447 THR A CB  
3297  O OG1 . THR A 447 ? 2.7281 2.2083 1.7684 -0.4589 0.3422  0.0099  447 THR A OG1 
3298  C CG2 . THR A 447 ? 2.7211 2.1882 1.8167 -0.4386 0.2857  0.0188  447 THR A CG2 
3299  N N   . ASP A 448 ? 3.0625 2.5245 2.1086 -0.3643 0.4397  -0.0737 448 ASP A N   
3300  C CA  . ASP A 448 ? 3.0325 2.5236 2.0985 -0.3362 0.4828  -0.0924 448 ASP A CA  
3301  C C   . ASP A 448 ? 3.0834 2.5704 2.1855 -0.2872 0.4935  -0.1111 448 ASP A C   
3302  O O   . ASP A 448 ? 3.1968 2.6282 2.2551 -0.2815 0.4929  -0.1231 448 ASP A O   
3303  C CB  . ASP A 448 ? 3.0335 2.4955 2.0171 -0.3545 0.5195  -0.1081 448 ASP A CB  
3304  C CG  . ASP A 448 ? 3.0201 2.5060 2.0168 -0.3215 0.5677  -0.1309 448 ASP A CG  
3305  O OD1 . ASP A 448 ? 2.9996 2.4853 2.0296 -0.2777 0.5797  -0.1462 448 ASP A OD1 
3306  O OD2 . ASP A 448 ? 3.0889 2.5946 2.0611 -0.3392 0.5936  -0.1322 448 ASP A OD2 
3307  N N   . PRO A 449 ? 2.8191 2.3630 1.9974 -0.2528 0.5033  -0.1135 449 PRO A N   
3308  C CA  . PRO A 449 ? 2.7627 2.3083 1.9781 -0.2042 0.5103  -0.1272 449 PRO A CA  
3309  C C   . PRO A 449 ? 2.8759 2.3687 2.0316 -0.1815 0.5475  -0.1520 449 PRO A C   
3310  O O   . PRO A 449 ? 2.8450 2.2943 1.9878 -0.1626 0.5412  -0.1585 449 PRO A O   
3311  C CB  . PRO A 449 ? 2.5046 2.1301 1.7992 -0.1785 0.5233  -0.1274 449 PRO A CB  
3312  C CG  . PRO A 449 ? 2.2818 1.9434 1.5985 -0.2184 0.5044  -0.1069 449 PRO A CG  
3313  C CD  . PRO A 449 ? 2.5520 2.1625 1.7836 -0.2606 0.5072  -0.1024 449 PRO A CD  
3314  N N   . GLY A 450 ? 2.9809 2.4756 2.1002 -0.1841 0.5865  -0.1654 450 GLY A N   
3315  C CA  . GLY A 450 ? 2.9552 2.3993 2.0220 -0.1575 0.6259  -0.1907 450 GLY A CA  
3316  C C   . GLY A 450 ? 3.0695 2.4250 2.0571 -0.1786 0.6171  -0.1982 450 GLY A C   
3317  O O   . GLY A 450 ? 3.1524 2.4605 2.1255 -0.1492 0.6267  -0.2110 450 GLY A O   
3318  N N   . LYS A 451 ? 3.0059 2.3387 1.9410 -0.2310 0.5982  -0.1893 451 LYS A N   
3319  C CA  . LYS A 451 ? 3.0675 2.3221 1.9241 -0.2574 0.5895  -0.1979 451 LYS A CA  
3320  C C   . LYS A 451 ? 3.1394 2.3789 2.0298 -0.2460 0.5546  -0.1883 451 LYS A C   
3321  O O   . LYS A 451 ? 3.2378 2.4148 2.0897 -0.2352 0.5634  -0.2034 451 LYS A O   
3322  C CB  . LYS A 451 ? 3.0275 2.2725 1.8223 -0.3149 0.5768  -0.1892 451 LYS A CB  
3323  C CG  . LYS A 451 ? 3.0863 2.3257 1.8247 -0.3257 0.6197  -0.2061 451 LYS A CG  
3324  C CD  . LYS A 451 ? 3.1159 2.3170 1.7637 -0.3818 0.6109  -0.2058 451 LYS A CD  
3325  C CE  . LYS A 451 ? 3.2320 2.3484 1.7958 -0.3887 0.6285  -0.2342 451 LYS A CE  
3326  N NZ  . LYS A 451 ? 3.0592 2.1463 1.5849 -0.3623 0.6857  -0.2658 451 LYS A NZ  
3327  N N   . ALA A 452 ? 3.0204 2.3133 1.9803 -0.2491 0.5166  -0.1639 452 ALA A N   
3328  C CA  . ALA A 452 ? 3.0025 2.2902 2.0036 -0.2315 0.4875  -0.1560 452 ALA A CA  
3329  C C   . ALA A 452 ? 3.0775 2.3423 2.0923 -0.1810 0.5119  -0.1723 452 ALA A C   
3330  O O   . ALA A 452 ? 2.9921 2.2074 1.9863 -0.1761 0.5033  -0.1764 452 ALA A O   
3331  C CB  . ALA A 452 ? 2.6435 1.9990 1.7278 -0.2309 0.4521  -0.1315 452 ALA A CB  
3332  N N   . GLU A 453 ? 3.1828 2.4855 2.2329 -0.1430 0.5429  -0.1805 453 GLU A N   
3333  C CA  . GLU A 453 ? 3.1314 2.4210 2.2019 -0.0879 0.5660  -0.1924 453 GLU A CA  
3334  C C   . GLU A 453 ? 3.3096 2.5055 2.2956 -0.0858 0.5951  -0.2138 453 GLU A C   
3335  O O   . GLU A 453 ? 3.3409 2.4873 2.3125 -0.0797 0.5833  -0.2140 453 GLU A O   
3336  C CB  . GLU A 453 ? 3.0094 2.3639 2.1304 -0.0500 0.5954  -0.1972 453 GLU A CB  
3337  C CG  . GLU A 453 ? 2.9465 2.3925 2.1561 -0.0478 0.5689  -0.1790 453 GLU A CG  
3338  C CD  . GLU A 453 ? 3.0389 2.5580 2.3002 -0.0164 0.5970  -0.1842 453 GLU A CD  
3339  O OE1 . GLU A 453 ? 3.0006 2.5023 2.2264 0.0011  0.6384  -0.2010 453 GLU A OE1 
3340  O OE2 . GLU A 453 ? 3.0841 2.6787 2.4212 -0.0102 0.5779  -0.1724 453 GLU A OE2 
3341  N N   . GLU A 454 ? 3.2329 2.4043 2.1644 -0.0915 0.6331  -0.2318 454 GLU A N   
3342  C CA  . GLU A 454 ? 3.2246 2.3010 2.0715 -0.0884 0.6667  -0.2563 454 GLU A CA  
3343  C C   . GLU A 454 ? 3.3399 2.3534 2.1365 -0.1301 0.6372  -0.2542 454 GLU A C   
3344  O O   . GLU A 454 ? 3.3839 2.3397 2.1645 -0.1106 0.6417  -0.2606 454 GLU A O   
3345  C CB  . GLU A 454 ? 3.1454 2.2080 1.9335 -0.1051 0.7046  -0.2750 454 GLU A CB  
3346  C CG  . GLU A 454 ? 3.2216 2.3434 2.0565 -0.0604 0.7400  -0.2802 454 GLU A CG  
3347  C CD  . GLU A 454 ? 3.5164 2.6325 2.2969 -0.0771 0.7788  -0.2982 454 GLU A CD  
3348  O OE1 . GLU A 454 ? 3.5419 2.6165 2.2497 -0.1291 0.7734  -0.3040 454 GLU A OE1 
3349  O OE2 . GLU A 454 ? 3.7136 2.8707 2.5246 -0.0383 0.8145  -0.3063 454 GLU A OE2 
3350  N N   . LEU A 455 ? 3.3380 2.3641 2.1110 -0.1848 0.6086  -0.2445 455 LEU A N   
3351  C CA  . LEU A 455 ? 3.3485 2.3219 2.0712 -0.2287 0.5802  -0.2431 455 LEU A CA  
3352  C C   . LEU A 455 ? 3.3864 2.3582 2.1566 -0.2095 0.5523  -0.2302 455 LEU A C   
3353  O O   . LEU A 455 ? 3.5664 2.4698 2.2884 -0.2232 0.5512  -0.2398 455 LEU A O   
3354  C CB  . LEU A 455 ? 3.3087 2.3222 2.0243 -0.2815 0.5462  -0.2256 455 LEU A CB  
3355  C CG  . LEU A 455 ? 3.0810 2.0521 1.7019 -0.3279 0.5614  -0.2414 455 LEU A CG  
3356  C CD1 . LEU A 455 ? 3.0532 2.0517 1.6620 -0.3817 0.5174  -0.2201 455 LEU A CD1 
3357  C CD2 . LEU A 455 ? 3.1447 2.0212 1.6870 -0.3328 0.5866  -0.2697 455 LEU A CD2 
3358  N N   . GLU A 456 ? 3.2516 2.2966 2.1109 -0.1833 0.5300  -0.2097 456 GLU A N   
3359  C CA  . GLU A 456 ? 3.1934 2.2435 2.1007 -0.1640 0.5034  -0.1970 456 GLU A CA  
3360  C C   . GLU A 456 ? 3.3008 2.2727 2.1674 -0.1368 0.5318  -0.2141 456 GLU A C   
3361  O O   . GLU A 456 ? 3.2837 2.2085 2.1233 -0.1559 0.5158  -0.2136 456 GLU A O   
3362  C CB  . GLU A 456 ? 2.9905 2.1210 1.9931 -0.1231 0.4933  -0.1819 456 GLU A CB  
3363  C CG  . GLU A 456 ? 2.7424 1.9069 1.8006 -0.1273 0.4499  -0.1618 456 GLU A CG  
3364  C CD  . GLU A 456 ? 2.7401 1.9936 1.8793 -0.1191 0.4293  -0.1452 456 GLU A CD  
3365  O OE1 . GLU A 456 ? 2.8467 2.1402 2.0134 -0.0949 0.4520  -0.1498 456 GLU A OE1 
3366  O OE2 . GLU A 456 ? 2.7069 1.9893 1.8816 -0.1379 0.3915  -0.1284 456 GLU A OE2 
3367  N N   . GLY A 457 ? 3.3439 2.3036 2.2073 -0.0932 0.5735  -0.2280 457 GLY A N   
3368  C CA  . GLY A 457 ? 3.2497 2.1309 2.0762 -0.0601 0.6041  -0.2423 457 GLY A CA  
3369  C C   . GLY A 457 ? 3.3550 2.1412 2.0833 -0.0796 0.6408  -0.2693 457 GLY A C   
3370  O O   . GLY A 457 ? 3.3943 2.1021 2.0852 -0.0590 0.6636  -0.2805 457 GLY A O   
3371  N N   . LYS A 458 ? 3.2616 2.0522 1.9472 -0.1182 0.6475  -0.2795 458 LYS A N   
3372  C CA  . LYS A 458 ? 3.1443 1.8460 1.7303 -0.1412 0.6838  -0.3086 458 LYS A CA  
3373  C C   . LYS A 458 ? 3.3906 2.0264 1.9187 -0.1908 0.6620  -0.3131 458 LYS A C   
3374  O O   . LYS A 458 ? 3.4038 1.9441 1.8618 -0.1929 0.6919  -0.3359 458 LYS A O   
3375  C CB  . LYS A 458 ? 3.2232 1.9553 1.7779 -0.1763 0.6909  -0.3158 458 LYS A CB  
3376  C CG  . LYS A 458 ? 3.4282 2.0764 1.8769 -0.2070 0.7258  -0.3471 458 LYS A CG  
3377  C CD  . LYS A 458 ? 3.4732 2.0562 1.8900 -0.1590 0.7825  -0.3723 458 LYS A CD  
3378  C CE  . LYS A 458 ? 3.4483 1.9536 1.7596 -0.1917 0.8191  -0.4056 458 LYS A CE  
3379  N NZ  . LYS A 458 ? 3.3829 1.8080 1.6579 -0.1442 0.8749  -0.4312 458 LYS A NZ  
3380  N N   . TYR A 459 ? 3.7932 2.4775 2.3495 -0.2295 0.6130  -0.2925 459 TYR A N   
3381  C CA  . TYR A 459 ? 3.8060 2.4383 2.3070 -0.2825 0.5907  -0.2969 459 TYR A CA  
3382  C C   . TYR A 459 ? 3.8324 2.4961 2.3932 -0.2809 0.5493  -0.2730 459 TYR A C   
3383  O O   . TYR A 459 ? 3.9667 2.5675 2.4963 -0.2904 0.5499  -0.2797 459 TYR A O   
3384  C CB  . TYR A 459 ? 3.8159 2.4708 2.2738 -0.3432 0.5710  -0.2975 459 TYR A CB  
3385  C CG  . TYR A 459 ? 3.9360 2.5535 2.3211 -0.3544 0.6114  -0.3235 459 TYR A CG  
3386  C CD1 . TYR A 459 ? 4.0141 2.5384 2.3330 -0.3403 0.6582  -0.3543 459 TYR A CD1 
3387  C CD2 . TYR A 459 ? 3.8292 2.5017 2.2098 -0.3785 0.6046  -0.3173 459 TYR A CD2 
3388  C CE1 . TYR A 459 ? 4.0937 2.5824 2.3443 -0.3494 0.6978  -0.3805 459 TYR A CE1 
3389  C CE2 . TYR A 459 ? 3.8765 2.5172 2.1885 -0.3895 0.6431  -0.3418 459 TYR A CE2 
3390  C CZ  . TYR A 459 ? 4.0712 2.6207 2.3183 -0.3746 0.6901  -0.3745 459 TYR A CZ  
3391  O OH  . TYR A 459 ? 4.0824 2.5992 2.2600 -0.3846 0.7305  -0.4009 459 TYR A OH  
3392  N N   . ALA A 460 ? 3.8185 2.5741 2.4605 -0.2711 0.5160  -0.2470 460 ALA A N   
3393  C CA  . ALA A 460 ? 3.7693 2.5593 2.4680 -0.2722 0.4756  -0.2250 460 ALA A CA  
3394  C C   . ALA A 460 ? 3.7824 2.5368 2.5026 -0.2240 0.4931  -0.2264 460 ALA A C   
3395  O O   . ALA A 460 ? 3.8831 2.5827 2.5722 -0.2405 0.4886  -0.2300 460 ALA A O   
3396  C CB  . ALA A 460 ? 3.6896 2.5779 2.4696 -0.2654 0.4431  -0.1999 460 ALA A CB  
3397  N N   . VAL A 461 ? 3.3424 2.1294 2.1137 -0.1678 0.5117  -0.2225 461 VAL A N   
3398  C CA  . VAL A 461 ? 3.2433 2.0042 2.0393 -0.1191 0.5242  -0.2190 461 VAL A CA  
3399  C C   . VAL A 461 ? 3.3771 2.0262 2.0913 -0.1305 0.5511  -0.2378 461 VAL A C   
3400  O O   . VAL A 461 ? 3.3253 1.9464 2.0427 -0.1315 0.5387  -0.2302 461 VAL A O   
3401  C CB  . VAL A 461 ? 2.9577 1.7557 1.8001 -0.0567 0.5507  -0.2180 461 VAL A CB  
3402  C CG1 . VAL A 461 ? 2.8901 1.6256 1.7178 -0.0079 0.5819  -0.2230 461 VAL A CG1 
3403  C CG2 . VAL A 461 ? 2.9404 1.8443 1.8772 -0.0383 0.5191  -0.1959 461 VAL A CG2 
3404  N N   . PRO A 462 ? 3.3701 1.9521 2.0098 -0.1410 0.5884  -0.2627 462 PRO A N   
3405  C CA  . PRO A 462 ? 3.1325 1.6012 1.6890 -0.1580 0.6147  -0.2832 462 PRO A CA  
3406  C C   . PRO A 462 ? 3.3702 1.8248 1.9058 -0.2160 0.5792  -0.2784 462 PRO A C   
3407  O O   . PRO A 462 ? 3.3501 1.7607 1.8819 -0.2101 0.5785  -0.2742 462 PRO A O   
3408  C CB  . PRO A 462 ? 3.0001 1.4258 1.4835 -0.1806 0.6469  -0.3103 462 PRO A CB  
3409  C CG  . PRO A 462 ? 3.1264 1.6302 1.6636 -0.1422 0.6563  -0.3039 462 PRO A CG  
3410  C CD  . PRO A 462 ? 3.3766 1.9852 2.0057 -0.1383 0.6092  -0.2737 462 PRO A CD  
3411  N N   . ARG A 463 ? 3.7986 2.2938 2.3221 -0.2698 0.5510  -0.2777 463 ARG A N   
3412  C CA  . ARG A 463 ? 3.7266 2.2200 2.2325 -0.3273 0.5151  -0.2725 463 ARG A CA  
3413  C C   . ARG A 463 ? 3.7025 2.2315 2.2771 -0.3058 0.4881  -0.2487 463 ARG A C   
3414  O O   . ARG A 463 ? 3.7580 2.2380 2.3050 -0.3293 0.4835  -0.2513 463 ARG A O   
3415  C CB  . ARG A 463 ? 3.6934 2.2580 2.2065 -0.3724 0.4807  -0.2640 463 ARG A CB  
3416  C CG  . ARG A 463 ? 3.7029 2.2266 2.1366 -0.4416 0.4721  -0.2799 463 ARG A CG  
3417  C CD  . ARG A 463 ? 3.7284 2.1464 2.0674 -0.4513 0.5194  -0.3145 463 ARG A CD  
3418  N NE  . ARG A 463 ? 3.8713 2.2299 2.1418 -0.5099 0.5132  -0.3302 463 ARG A NE  
3419  C CZ  . ARG A 463 ? 3.8930 2.2132 2.1657 -0.5151 0.5081  -0.3279 463 ARG A CZ  
3420  N NH1 . ARG A 463 ? 3.7657 2.0852 2.0943 -0.4605 0.5156  -0.3133 463 ARG A NH1 
3421  N NH2 . ARG A 463 ? 3.9262 2.2115 2.1443 -0.5763 0.4956  -0.3398 463 ARG A NH2 
3422  N N   . TYR A 464 ? 3.4376 2.0494 2.0970 -0.2651 0.4715  -0.2273 464 TYR A N   
3423  C CA  . TYR A 464 ? 3.2729 1.9241 1.9994 -0.2423 0.4464  -0.2054 464 TYR A CA  
3424  C C   . TYR A 464 ? 3.2536 1.8301 1.9594 -0.2069 0.4765  -0.2105 464 TYR A C   
3425  O O   . TYR A 464 ? 3.2425 1.7883 1.9381 -0.2248 0.4659  -0.2060 464 TYR A O   
3426  C CB  . TYR A 464 ? 3.1581 1.9002 1.9723 -0.1974 0.4332  -0.1870 464 TYR A CB  
3427  C CG  . TYR A 464 ? 3.0575 1.8757 1.9024 -0.2211 0.4071  -0.1784 464 TYR A CG  
3428  C CD1 . TYR A 464 ? 3.0478 1.8680 1.8578 -0.2790 0.3844  -0.1792 464 TYR A CD1 
3429  C CD2 . TYR A 464 ? 2.8385 1.7271 1.7467 -0.1859 0.4052  -0.1686 464 TYR A CD2 
3430  C CE1 . TYR A 464 ? 2.9464 1.8327 1.7820 -0.2990 0.3609  -0.1682 464 TYR A CE1 
3431  C CE2 . TYR A 464 ? 2.7500 1.7024 1.6845 -0.2083 0.3832  -0.1594 464 TYR A CE2 
3432  C CZ  . TYR A 464 ? 2.9530 1.9018 1.8503 -0.2635 0.3612  -0.1580 464 TYR A CZ  
3433  O OH  . TYR A 464 ? 3.0129 2.0213 1.9336 -0.2841 0.3397  -0.1458 464 TYR A OH  
3434  N N   . LYS A 465 ? 3.2446 1.7963 1.9471 -0.1561 0.5133  -0.2178 465 LYS A N   
3435  C CA  . LYS A 465 ? 3.2020 1.6864 1.8901 -0.1139 0.5422  -0.2181 465 LYS A CA  
3436  C C   . LYS A 465 ? 3.3671 1.7468 1.9754 -0.1539 0.5560  -0.2328 465 LYS A C   
3437  O O   . LYS A 465 ? 3.2886 1.6366 1.8994 -0.1481 0.5529  -0.2229 465 LYS A O   
3438  C CB  . LYS A 465 ? 3.1076 1.5693 1.7876 -0.0595 0.5848  -0.2281 465 LYS A CB  
3439  C CG  . LYS A 465 ? 3.3060 1.6946 1.9686 -0.0093 0.6177  -0.2265 465 LYS A CG  
3440  C CD  . LYS A 465 ? 3.2940 1.6491 1.9353 0.0387  0.6639  -0.2402 465 LYS A CD  
3441  C CE  . LYS A 465 ? 3.2617 1.5713 1.9089 0.1033  0.6912  -0.2300 465 LYS A CE  
3442  N NZ  . LYS A 465 ? 3.1485 1.4423 1.7884 0.1582  0.7343  -0.2401 465 LYS A NZ  
3443  N N   . GLU A 466 ? 3.5523 1.8771 2.0870 -0.1972 0.5719  -0.2571 466 GLU A N   
3444  C CA  . GLU A 466 ? 3.6155 1.8447 2.0715 -0.2457 0.5825  -0.2741 466 GLU A CA  
3445  C C   . GLU A 466 ? 3.5792 1.8501 2.0594 -0.2927 0.5383  -0.2596 466 GLU A C   
3446  O O   . GLU A 466 ? 3.5194 1.7276 1.9656 -0.3153 0.5425  -0.2623 466 GLU A O   
3447  C CB  . GLU A 466 ? 3.6507 1.8309 2.0273 -0.2889 0.6021  -0.3036 466 GLU A CB  
3448  C CG  . GLU A 466 ? 3.9596 2.0085 2.2404 -0.3151 0.6386  -0.3305 466 GLU A CG  
3449  C CD  . GLU A 466 ? 4.1649 2.1644 2.3670 -0.3466 0.6651  -0.3625 466 GLU A CD  
3450  O OE1 . GLU A 466 ? 3.9913 2.0646 2.2079 -0.3671 0.6449  -0.3619 466 GLU A OE1 
3451  O OE2 . GLU A 466 ? 4.2885 2.1855 2.4228 -0.3499 0.7041  -0.3834 466 GLU A OE2 
3452  N N   . ARG A 467 ? 3.4553 1.8316 1.9948 -0.3075 0.4969  -0.2436 467 ARG A N   
3453  C CA  . ARG A 467 ? 3.2528 1.6808 1.8249 -0.3463 0.4538  -0.2278 467 ARG A CA  
3454  C C   . ARG A 467 ? 3.2665 1.7068 1.8909 -0.3100 0.4470  -0.2076 467 ARG A C   
3455  O O   . ARG A 467 ? 3.3346 1.7356 1.9379 -0.3357 0.4435  -0.2067 467 ARG A O   
3456  C CB  . ARG A 467 ? 3.1523 1.6878 1.7793 -0.3605 0.4145  -0.2134 467 ARG A CB  
3457  C CG  . ARG A 467 ? 3.0417 1.6121 1.6614 -0.4241 0.3766  -0.2093 467 ARG A CG  
3458  C CD  . ARG A 467 ? 3.0219 1.6816 1.6798 -0.4357 0.3462  -0.1972 467 ARG A CD  
3459  N NE  . ARG A 467 ? 2.8631 1.4972 1.4641 -0.4518 0.3660  -0.2153 467 ARG A NE  
3460  C CZ  . ARG A 467 ? 2.8429 1.5341 1.4480 -0.4786 0.3430  -0.2090 467 ARG A CZ  
3461  N NH1 . ARG A 467 ? 2.7602 1.5344 1.4252 -0.4903 0.2998  -0.1846 467 ARG A NH1 
3462  N NH2 . ARG A 467 ? 2.9404 1.6043 1.4885 -0.4928 0.3645  -0.2263 467 ARG A NH2 
3463  N N   . ASP A 468 ? 3.2059 1.7035 1.8979 -0.2520 0.4451  -0.1916 468 ASP A N   
3464  C CA  . ASP A 468 ? 3.1542 1.6690 1.8961 -0.2136 0.4388  -0.1719 468 ASP A CA  
3465  C C   . ASP A 468 ? 3.3652 1.7698 2.0480 -0.1995 0.4766  -0.1799 468 ASP A C   
3466  O O   . ASP A 468 ? 3.2775 1.6704 1.9714 -0.1985 0.4697  -0.1672 468 ASP A O   
3467  C CB  . ASP A 468 ? 2.8793 1.4675 1.6943 -0.1525 0.4357  -0.1574 468 ASP A CB  
3468  C CG  . ASP A 468 ? 2.8175 1.5122 1.6967 -0.1655 0.3972  -0.1465 468 ASP A CG  
3469  O OD1 . ASP A 468 ? 2.7547 1.4798 1.6427 -0.2102 0.3656  -0.1409 468 ASP A OD1 
3470  O OD2 . ASP A 468 ? 3.0304 1.7766 1.9501 -0.1310 0.3999  -0.1436 468 ASP A OD2 
3471  N N   . ALA A 469 ? 3.4758 1.8009 2.0968 -0.1893 0.5166  -0.2002 469 ALA A N   
3472  C CA  . ALA A 469 ? 3.3660 1.5766 1.9289 -0.1688 0.5576  -0.2074 469 ALA A CA  
3473  C C   . ALA A 469 ? 3.3135 1.4696 1.8355 -0.2229 0.5499  -0.2096 469 ALA A C   
3474  O O   . ALA A 469 ? 3.5143 1.6119 2.0234 -0.2021 0.5668  -0.2005 469 ALA A O   
3475  C CB  . ALA A 469 ? 3.3769 1.5070 1.8711 -0.1636 0.5999  -0.2336 469 ALA A CB  
3476  N N   . ARG A 470 ? 3.3061 1.4863 1.8107 -0.2899 0.5241  -0.2194 470 ARG A N   
3477  C CA  . ARG A 470 ? 3.1914 1.3311 1.6597 -0.3487 0.5143  -0.2228 470 ARG A CA  
3478  C C   . ARG A 470 ? 3.5794 1.7499 2.1008 -0.3259 0.4991  -0.1965 470 ARG A C   
3479  O O   . ARG A 470 ? 3.6099 1.6936 2.0917 -0.3213 0.5249  -0.1962 470 ARG A O   
3480  C CB  . ARG A 470 ? 3.1249 1.3286 1.5952 -0.4150 0.4769  -0.2286 470 ARG A CB  
3481  C CG  . ARG A 470 ? 3.2366 1.4085 1.6454 -0.4461 0.4906  -0.2552 470 ARG A CG  
3482  C CD  . ARG A 470 ? 3.2231 1.2635 1.5320 -0.4777 0.5305  -0.2837 470 ARG A CD  
3483  N NE  . ARG A 470 ? 3.3885 1.3997 1.6349 -0.5096 0.5441  -0.3112 470 ARG A NE  
3484  C CZ  . ARG A 470 ? 3.8163 1.7115 1.9713 -0.5304 0.5846  -0.3415 470 ARG A CZ  
3485  N NH1 . ARG A 470 ? 3.8140 1.6353 1.9514 -0.5065 0.6154  -0.3370 470 ARG A NH1 
3486  N NH2 . ARG A 470 ? 3.7823 1.6779 1.8907 -0.5672 0.5883  -0.3615 470 ARG A NH2 
3487  N N   . LEU A 471 ? 3.7948 2.0808 2.3996 -0.3122 0.4604  -0.1755 471 LEU A N   
3488  C CA  . LEU A 471 ? 3.7948 2.1207 2.4529 -0.2926 0.4435  -0.1513 471 LEU A CA  
3489  C C   . LEU A 471 ? 3.7626 2.0855 2.4511 -0.2155 0.4635  -0.1371 471 LEU A C   
3490  O O   . LEU A 471 ? 3.7583 2.1267 2.4973 -0.1899 0.4489  -0.1158 471 LEU A O   
3491  C CB  . LEU A 471 ? 3.6198 2.0687 2.3523 -0.3106 0.3951  -0.1372 471 LEU A CB  
3492  C CG  . LEU A 471 ? 3.4473 1.9147 2.1593 -0.3841 0.3701  -0.1460 471 LEU A CG  
3493  C CD1 . LEU A 471 ? 3.2373 1.8272 2.0271 -0.3910 0.3244  -0.1302 471 LEU A CD1 
3494  C CD2 . LEU A 471 ? 3.5486 1.9589 2.2221 -0.4237 0.3769  -0.1476 471 LEU A CD2 
3495  N N   . GLU A 472 ? 3.7772 2.0522 2.4361 -0.1799 0.4957  -0.1485 472 GLU A N   
3496  C CA  . GLU A 472 ? 3.7386 2.0212 2.4302 -0.1032 0.5139  -0.1342 472 GLU A CA  
3497  C C   . GLU A 472 ? 3.7476 1.9643 2.4186 -0.0826 0.5318  -0.1198 472 GLU A C   
3498  O O   . GLU A 472 ? 3.7983 2.0661 2.5225 -0.0340 0.5233  -0.0976 472 GLU A O   
3499  C CB  . GLU A 472 ? 3.7283 1.9609 2.3835 -0.0718 0.5502  -0.1507 472 GLU A CB  
3500  C CG  . GLU A 472 ? 3.7599 2.0121 2.4529 0.0078  0.5674  -0.1359 472 GLU A CG  
3501  C CD  . GLU A 472 ? 3.9275 2.0850 2.5814 0.0441  0.6005  -0.1262 472 GLU A CD  
3502  O OE1 . GLU A 472 ? 4.0837 2.1282 2.6602 0.0143  0.6277  -0.1407 472 GLU A OE1 
3503  O OE2 . GLU A 472 ? 3.9359 2.1320 2.6351 0.1010  0.5990  -0.1040 472 GLU A OE2 
3504  N N   . SER A 473 ? 3.4999 1.6068 2.0944 -0.1197 0.5560  -0.1321 473 SER A N   
3505  C CA  . SER A 473 ? 3.5458 1.5755 2.1117 -0.1019 0.5778  -0.1176 473 SER A CA  
3506  C C   . SER A 473 ? 3.4740 1.4904 2.0218 -0.1683 0.5608  -0.1170 473 SER A C   
3507  O O   . SER A 473 ? 3.3293 1.3006 1.8639 -0.1601 0.5717  -0.1012 473 SER A O   
3508  C CB  . SER A 473 ? 3.5219 1.4199 2.0114 -0.0786 0.6288  -0.1300 473 SER A CB  
3509  O OG  . SER A 473 ? 3.4402 1.2693 1.8616 -0.1362 0.6428  -0.1606 473 SER A OG  
3510  N N   . LEU A 474 ? 3.4201 1.4774 1.9675 -0.2312 0.5352  -0.1324 474 LEU A N   
3511  C CA  . LEU A 474 ? 3.4866 1.5383 2.0174 -0.2990 0.5186  -0.1338 474 LEU A CA  
3512  C C   . LEU A 474 ? 3.4167 1.5529 2.0175 -0.2837 0.4901  -0.1062 474 LEU A C   
3513  O O   . LEU A 474 ? 3.2515 1.4827 1.9234 -0.2400 0.4684  -0.0922 474 LEU A O   
3514  C CB  . LEU A 474 ? 3.3416 1.4433 1.8702 -0.3609 0.4916  -0.1523 474 LEU A CB  
3515  C CG  . LEU A 474 ? 3.2892 1.3567 1.7730 -0.4403 0.4852  -0.1643 474 LEU A CG  
3516  C CD1 . LEU A 474 ? 2.9281 0.9909 1.3699 -0.4943 0.4793  -0.1910 474 LEU A CD1 
3517  C CD2 . LEU A 474 ? 3.0316 1.1982 1.5805 -0.4619 0.4458  -0.1445 474 LEU A CD2 
3518  N N   . VAL A 475 ? 3.6275 1.7308 2.2077 -0.3208 0.4910  -0.1001 475 VAL A N   
3519  C CA  . VAL A 475 ? 3.3560 1.5388 1.9990 -0.3109 0.4656  -0.0750 475 VAL A CA  
3520  C C   . VAL A 475 ? 3.4417 1.6557 2.0849 -0.3858 0.4421  -0.0800 475 VAL A C   
3521  O O   . VAL A 475 ? 3.6579 1.7947 2.2345 -0.4407 0.4578  -0.0991 475 VAL A O   
3522  C CB  . VAL A 475 ? 3.2881 1.4063 1.9133 -0.2659 0.4937  -0.0550 475 VAL A CB  
3523  C CG1 . VAL A 475 ? 3.0369 1.1808 1.6968 -0.1843 0.5011  -0.0417 475 VAL A CG1 
3524  C CG2 . VAL A 475 ? 3.6227 1.5931 2.1544 -0.2901 0.5362  -0.0663 475 VAL A CG2 
3525  N N   . ASP A 476 ? 3.2768 1.6013 1.9924 -0.3879 0.4066  -0.0644 476 ASP A N   
3526  C CA  . ASP A 476 ? 3.1994 1.5722 1.9275 -0.4547 0.3813  -0.0664 476 ASP A CA  
3527  C C   . ASP A 476 ? 3.4763 1.7635 2.1510 -0.4873 0.4066  -0.0641 476 ASP A C   
3528  O O   . ASP A 476 ? 3.4641 1.7757 2.1374 -0.5489 0.3923  -0.0679 476 ASP A O   
3529  C CB  . ASP A 476 ? 2.9249 1.4299 1.7444 -0.4398 0.3426  -0.0485 476 ASP A CB  
3530  C CG  . ASP A 476 ? 3.1050 1.6930 1.9798 -0.4073 0.3182  -0.0491 476 ASP A CG  
3531  O OD1 . ASP A 476 ? 3.4050 1.9514 2.2489 -0.3932 0.3320  -0.0620 476 ASP A OD1 
3532  O OD2 . ASP A 476 ? 2.8931 1.5848 1.8406 -0.3966 0.2870  -0.0369 476 ASP A OD2 
3533  N N   . GLU A 477 ? 3.6684 1.8610 2.3020 -0.4460 0.4432  -0.0569 477 GLU A N   
3534  C CA  . GLU A 477 ? 3.6389 1.7378 2.2175 -0.4715 0.4717  -0.0513 477 GLU A CA  
3535  C C   . GLU A 477 ? 3.5183 1.5436 2.0274 -0.5494 0.4837  -0.0771 477 GLU A C   
3536  O O   . GLU A 477 ? 3.6680 1.6294 2.1359 -0.5886 0.5017  -0.0751 477 GLU A O   
3537  C CB  . GLU A 477 ? 3.7565 1.7550 2.2949 -0.4099 0.5113  -0.0400 477 GLU A CB  
3538  C CG  . GLU A 477 ? 3.6851 1.7581 2.2884 -0.3315 0.4996  -0.0174 477 GLU A CG  
3539  C CD  . GLU A 477 ? 3.4094 1.6075 2.0908 -0.3323 0.4632  0.0001  477 GLU A CD  
3540  O OE1 . GLU A 477 ? 3.7380 1.9250 2.4121 -0.3554 0.4673  0.0131  477 GLU A OE1 
3541  O OE2 . GLU A 477 ? 3.0640 1.3681 1.8120 -0.3107 0.4323  0.0002  477 GLU A OE2 
3542  N N   . LYS A 478 ? 3.2868 1.3217 1.7809 -0.5759 0.4739  -0.1009 478 LYS A N   
3543  C CA  . LYS A 478 ? 3.3163 1.2848 1.7396 -0.6450 0.4871  -0.1284 478 LYS A CA  
3544  C C   . LYS A 478 ? 3.2735 1.3217 1.7127 -0.7063 0.4514  -0.1452 478 LYS A C   
3545  O O   . LYS A 478 ? 3.3975 1.4168 1.7848 -0.7467 0.4588  -0.1702 478 LYS A O   
3546  C CB  . LYS A 478 ? 3.4331 1.3048 1.7944 -0.6129 0.5245  -0.1450 478 LYS A CB  
3547  C CG  . LYS A 478 ? 3.6983 1.4824 2.0303 -0.5620 0.5631  -0.1309 478 LYS A CG  
3548  C CD  . LYS A 478 ? 3.8239 1.5192 2.0996 -0.5283 0.6003  -0.1461 478 LYS A CD  
3549  C CE  . LYS A 478 ? 3.9885 1.6007 2.2369 -0.4767 0.6374  -0.1294 478 LYS A CE  
3550  N NZ  . LYS A 478 ? 3.9794 1.5108 2.1773 -0.4421 0.6740  -0.1429 478 LYS A NZ  
3551  N N   . VAL A 479 ? 3.2011 1.3778 1.7209 -0.7032 0.4101  -0.1301 479 VAL A N   
3552  C CA  . VAL A 479 ? 3.1220 1.3871 1.6627 -0.7594 0.3728  -0.1415 479 VAL A CA  
3553  C C   . VAL A 479 ? 3.2723 1.5831 1.8280 -0.8211 0.3558  -0.1369 479 VAL A C   
3554  O O   . VAL A 479 ? 3.1844 1.5034 1.7679 -0.8032 0.3612  -0.1175 479 VAL A O   
3555  C CB  . VAL A 479 ? 2.9820 1.3681 1.6043 -0.7163 0.3367  -0.1285 479 VAL A CB  
3556  C CG1 . VAL A 479 ? 2.8637 1.2147 1.4635 -0.6779 0.3495  -0.1399 479 VAL A CG1 
3557  C CG2 . VAL A 479 ? 3.2050 1.6578 1.9025 -0.6613 0.3257  -0.1008 479 VAL A CG2 
3558  N N   . ASP A 480 ? 3.4342 1.7780 1.9723 -0.8909 0.3361  -0.1537 480 ASP A N   
3559  C CA  . ASP A 480 ? 3.3608 1.7755 1.9263 -0.9437 0.3158  -0.1483 480 ASP A CA  
3560  C C   . ASP A 480 ? 3.2413 1.7985 1.8823 -0.9608 0.2664  -0.1379 480 ASP A C   
3561  O O   . ASP A 480 ? 3.2692 1.8995 1.9471 -0.9988 0.2466  -0.1296 480 ASP A O   
3562  C CB  . ASP A 480 ? 3.5171 1.8965 2.0188 -0.9993 0.3279  -0.1717 480 ASP A CB  
3563  C CG  . ASP A 480 ? 3.6999 1.9606 2.1382 -0.9863 0.3736  -0.1785 480 ASP A CG  
3564  O OD1 . ASP A 480 ? 3.7249 1.9411 2.1746 -0.9375 0.3936  -0.1609 480 ASP A OD1 
3565  O OD2 . ASP A 480 ? 3.8611 2.0739 2.2375 -1.0247 0.3895  -0.2003 480 ASP A OD2 
3566  N N   . THR A 481 ? 3.2663 1.8731 1.9351 -0.9269 0.2464  -0.1371 481 THR A N   
3567  C CA  . THR A 481 ? 3.1432 1.8877 1.8853 -0.9315 0.1997  -0.1251 481 THR A CA  
3568  C C   . THR A 481 ? 2.9003 1.6851 1.6881 -0.8634 0.1879  -0.1143 481 THR A C   
3569  O O   . THR A 481 ? 2.9270 1.6399 1.6715 -0.8374 0.2094  -0.1258 481 THR A O   
3570  C CB  . THR A 481 ? 3.1805 1.9485 1.8856 -1.0057 0.1804  -0.1433 481 THR A CB  
3571  O OG1 . THR A 481 ? 3.1184 2.0135 1.8910 -1.0005 0.1361  -0.1294 481 THR A OG1 
3572  C CG2 . THR A 481 ? 3.1483 1.8121 1.7639 -1.0217 0.2054  -0.1703 481 THR A CG2 
3573  N N   . PHE A 482 ? 2.6120 1.5117 1.4876 -0.8356 0.1550  -0.0930 482 PHE A N   
3574  C CA  . PHE A 482 ? 2.5804 1.5294 1.5071 -0.7759 0.1404  -0.0818 482 PHE A CA  
3575  C C   . PHE A 482 ? 2.6505 1.6812 1.5986 -0.8022 0.1037  -0.0810 482 PHE A C   
3576  O O   . PHE A 482 ? 2.6828 1.7442 1.6158 -0.8623 0.0872  -0.0864 482 PHE A O   
3577  C CB  . PHE A 482 ? 2.5942 1.6094 1.6018 -0.7244 0.1307  -0.0594 482 PHE A CB  
3578  C CG  . PHE A 482 ? 2.5804 1.5229 1.5717 -0.6851 0.1647  -0.0560 482 PHE A CG  
3579  C CD1 . PHE A 482 ? 2.6254 1.4750 1.5676 -0.6511 0.1958  -0.0649 482 PHE A CD1 
3580  C CD2 . PHE A 482 ? 2.3784 1.3511 1.4061 -0.6784 0.1653  -0.0421 482 PHE A CD2 
3581  C CE1 . PHE A 482 ? 2.6768 1.4638 1.6053 -0.6115 0.2255  -0.0585 482 PHE A CE1 
3582  C CE2 . PHE A 482 ? 2.2776 1.1859 1.2884 -0.6407 0.1954  -0.0362 482 PHE A CE2 
3583  C CZ  . PHE A 482 ? 2.4253 1.2415 1.3869 -0.6067 0.2245  -0.0435 482 PHE A CZ  
3584  N N   . TYR A 483 ? 2.6404 1.7064 1.6215 -0.7592 0.0911  -0.0737 483 TYR A N   
3585  C CA  . TYR A 483 ? 2.6408 1.7804 1.6405 -0.7797 0.0571  -0.0694 483 TYR A CA  
3586  C C   . TYR A 483 ? 2.3646 1.6064 1.4574 -0.7365 0.0271  -0.0456 483 TYR A C   
3587  O O   . TYR A 483 ? 2.2773 1.5137 1.4036 -0.6795 0.0369  -0.0387 483 TYR A O   
3588  C CB  . TYR A 483 ? 2.5493 1.6299 1.4893 -0.7792 0.0707  -0.0848 483 TYR A CB  
3589  C CG  . TYR A 483 ? 2.6897 1.6606 1.5344 -0.8187 0.1040  -0.1110 483 TYR A CG  
3590  C CD1 . TYR A 483 ? 2.6826 1.6496 1.4848 -0.8891 0.0972  -0.1232 483 TYR A CD1 
3591  C CD2 . TYR A 483 ? 2.7631 1.6341 1.5608 -0.7856 0.1432  -0.1242 483 TYR A CD2 
3592  C CE1 . TYR A 483 ? 2.6936 1.5532 1.4054 -0.9279 0.1297  -0.1496 483 TYR A CE1 
3593  C CE2 . TYR A 483 ? 2.9250 1.6879 1.6338 -0.8195 0.1765  -0.1490 483 TYR A CE2 
3594  C CZ  . TYR A 483 ? 2.8867 1.6405 1.5510 -0.8918 0.1703  -0.1625 483 TYR A CZ  
3595  O OH  . TYR A 483 ? 2.9135 1.5542 1.4868 -0.9280 0.2049  -0.1893 483 TYR A OH  
3596  N N   . SER A 484 ? 2.2004 1.5356 1.3347 -0.7641 -0.0091 -0.0333 484 SER A N   
3597  C CA  . SER A 484 ? 2.2242 1.6569 1.4464 -0.7275 -0.0387 -0.0106 484 SER A CA  
3598  C C   . SER A 484 ? 2.2667 1.7402 1.4954 -0.7275 -0.0634 -0.0029 484 SER A C   
3599  O O   . SER A 484 ? 2.1228 1.6173 1.3205 -0.7759 -0.0806 -0.0053 484 SER A O   
3600  C CB  . SER A 484 ? 2.2081 1.7232 1.4802 -0.7525 -0.0616 0.0014  484 SER A CB  
3601  O OG  . SER A 484 ? 2.0078 1.5398 1.2420 -0.8175 -0.0756 -0.0051 484 SER A OG  
3602  N N   . CYS A 485 ? 2.1814 1.6694 1.4505 -0.6752 -0.0659 0.0070  485 CYS A N   
3603  C CA  . CYS A 485 ? 2.0462 1.5703 1.3240 -0.6711 -0.0875 0.0172  485 CYS A CA  
3604  C C   . CYS A 485 ? 2.1653 1.7851 1.5313 -0.6440 -0.1191 0.0420  485 CYS A C   
3605  O O   . CYS A 485 ? 2.1955 1.8346 1.6167 -0.6054 -0.1150 0.0477  485 CYS A O   
3606  C CB  . CYS A 485 ? 1.8272 1.2899 1.0772 -0.6372 -0.0643 0.0085  485 CYS A CB  
3607  S SG  . CYS A 485 ? 2.0828 1.5872 1.3462 -0.6283 -0.0876 0.0233  485 CYS A SG  
3608  N N   . ASN A 486 ? 2.2314 1.9095 1.6085 -0.6634 -0.1499 0.0567  486 ASN A N   
3609  C CA  . ASN A 486 ? 2.0352 1.8014 1.4929 -0.6381 -0.1804 0.0820  486 ASN A CA  
3610  C C   . ASN A 486 ? 2.0578 1.8384 1.5167 -0.6260 -0.1962 0.0961  486 ASN A C   
3611  O O   . ASN A 486 ? 2.0748 1.9269 1.5795 -0.6225 -0.2267 0.1190  486 ASN A O   
3612  C CB  . ASN A 486 ? 1.8773 1.7185 1.3593 -0.6745 -0.2072 0.0927  486 ASN A CB  
3613  C CG  . ASN A 486 ? 1.9161 1.7676 1.3422 -0.7300 -0.2237 0.0916  486 ASN A CG  
3614  O OD1 . ASN A 486 ? 2.1072 1.9044 1.4635 -0.7719 -0.2070 0.0704  486 ASN A OD1 
3615  N ND2 . ASN A 486 ? 1.8483 1.7679 1.3012 -0.7318 -0.2566 0.1144  486 ASN A ND2 
3616  N N   . LEU A 487 ? 2.1060 1.8192 1.5152 -0.6184 -0.1744 0.0836  487 LEU A N   
3617  C CA  . LEU A 487 ? 1.9354 1.6554 1.3394 -0.6090 -0.1851 0.0960  487 LEU A CA  
3618  C C   . LEU A 487 ? 1.8817 1.6341 1.3613 -0.5563 -0.1917 0.1127  487 LEU A C   
3619  O O   . LEU A 487 ? 1.7915 1.5843 1.2970 -0.5489 -0.2141 0.1341  487 LEU A O   
3620  C CB  . LEU A 487 ? 1.8594 1.4978 1.1881 -0.6165 -0.1555 0.0752  487 LEU A CB  
3621  C CG  . LEU A 487 ? 2.0575 1.6939 1.3408 -0.6381 -0.1651 0.0817  487 LEU A CG  
3622  C CD1 . LEU A 487 ? 2.0592 1.7495 1.3252 -0.6856 -0.1975 0.0941  487 LEU A CD1 
3623  C CD2 . LEU A 487 ? 2.0595 1.6121 1.2630 -0.6501 -0.1311 0.0556  487 LEU A CD2 
3624  N N   . CYS A 488 ? 1.9710 1.7086 1.4866 -0.5213 -0.1737 0.1038  488 CYS A N   
3625  C CA  . CYS A 488 ? 1.7893 1.5554 1.3761 -0.4725 -0.1781 0.1155  488 CYS A CA  
3626  C C   . CYS A 488 ? 1.7986 1.6424 1.4539 -0.4658 -0.2071 0.1360  488 CYS A C   
3627  O O   . CYS A 488 ? 1.7914 1.6610 1.5079 -0.4271 -0.2120 0.1456  488 CYS A O   
3628  C CB  . CYS A 488 ? 1.8870 1.6172 1.4874 -0.4390 -0.1505 0.0985  488 CYS A CB  
3629  S SG  . CYS A 488 ? 1.8148 1.4670 1.3599 -0.4263 -0.1173 0.0797  488 CYS A SG  
3630  N N   . GLN A 489 ? 1.8110 1.6918 1.4568 -0.5022 -0.2245 0.1416  489 GLN A N   
3631  C CA  . GLN A 489 ? 1.7494 1.7097 1.4621 -0.4953 -0.2507 0.1609  489 GLN A CA  
3632  C C   . GLN A 489 ? 1.6931 1.6983 1.4401 -0.4816 -0.2779 0.1883  489 GLN A C   
3633  O O   . GLN A 489 ? 1.7367 1.8074 1.5453 -0.4671 -0.2993 0.2069  489 GLN A O   
3634  C CB  . GLN A 489 ? 1.8648 1.8582 1.5579 -0.5413 -0.2619 0.1591  489 GLN A CB  
3635  C CG  . GLN A 489 ? 1.8535 1.9181 1.6165 -0.5301 -0.2749 0.1687  489 GLN A CG  
3636  C CD  . GLN A 489 ? 1.7713 1.8659 1.5137 -0.5782 -0.2815 0.1638  489 GLN A CD  
3637  O OE1 . GLN A 489 ? 2.0563 2.1038 1.7282 -0.6194 -0.2698 0.1474  489 GLN A OE1 
3638  N NE2 . GLN A 489 ? 1.5417 1.7162 1.3460 -0.5750 -0.2993 0.1770  489 GLN A NE2 
3639  N N   . SER A 490 ? 1.6657 1.6350 1.3727 -0.4850 -0.2758 0.1917  490 SER A N   
3640  C CA  . SER A 490 ? 1.6818 1.6828 1.4135 -0.4722 -0.2987 0.2192  490 SER A CA  
3641  C C   . SER A 490 ? 1.7427 1.7574 1.5492 -0.4211 -0.2975 0.2277  490 SER A C   
3642  O O   . SER A 490 ? 1.7109 1.7758 1.5675 -0.4048 -0.3207 0.2528  490 SER A O   
3643  C CB  . SER A 490 ? 1.6681 1.6194 1.3375 -0.4860 -0.2902 0.2177  490 SER A CB  
3644  O OG  . SER A 490 ? 1.5982 1.4821 1.2387 -0.4743 -0.2566 0.1921  490 SER A OG  
3645  N N   . PHE A 491 ? 1.6991 1.6697 1.5123 -0.3958 -0.2702 0.2064  491 PHE A N   
3646  C CA  . PHE A 491 ? 1.5756 1.5544 1.4543 -0.3504 -0.2659 0.2086  491 PHE A CA  
3647  C C   . PHE A 491 ? 1.6913 1.6947 1.6130 -0.3344 -0.2594 0.1966  491 PHE A C   
3648  O O   . PHE A 491 ? 1.7724 1.8159 1.7585 -0.3063 -0.2694 0.2067  491 PHE A O   
3649  C CB  . PHE A 491 ? 1.5965 1.5188 1.4584 -0.3316 -0.2422 0.1950  491 PHE A CB  
3650  C CG  . PHE A 491 ? 1.5175 1.3863 1.3244 -0.3431 -0.2144 0.1683  491 PHE A CG  
3651  C CD1 . PHE A 491 ? 1.5123 1.3470 1.2481 -0.3765 -0.2086 0.1635  491 PHE A CD1 
3652  C CD2 . PHE A 491 ? 1.4268 1.2776 1.2520 -0.3180 -0.1931 0.1486  491 PHE A CD2 
3653  C CE1 . PHE A 491 ? 1.5880 1.3689 1.2738 -0.3832 -0.1808 0.1393  491 PHE A CE1 
3654  C CE2 . PHE A 491 ? 1.6166 1.4171 1.3921 -0.3241 -0.1672 0.1270  491 PHE A CE2 
3655  C CZ  . PHE A 491 ? 1.6997 1.4637 1.4067 -0.3555 -0.1604 0.1224  491 PHE A CZ  
3656  N N   . ALA A 492 ? 1.6372 1.6146 1.5221 -0.3517 -0.2415 0.1756  492 ALA A N   
3657  C CA  . ALA A 492 ? 1.5627 1.5604 1.4799 -0.3407 -0.2334 0.1648  492 ALA A CA  
3658  C C   . ALA A 492 ? 1.7641 1.8079 1.6782 -0.3749 -0.2493 0.1719  492 ALA A C   
3659  O O   . ALA A 492 ? 1.8278 1.8435 1.6874 -0.4088 -0.2392 0.1594  492 ALA A O   
3660  C CB  . ALA A 492 ? 1.5361 1.4754 1.4138 -0.3382 -0.2030 0.1399  492 ALA A CB  
3661  N N   . PRO A 493 ? 1.9544 2.0687 1.9250 -0.3679 -0.2733 0.1914  493 PRO A N   
3662  C CA  . PRO A 493 ? 1.8543 2.0213 1.8233 -0.4035 -0.2897 0.1987  493 PRO A CA  
3663  C C   . PRO A 493 ? 1.8518 2.0165 1.8064 -0.4246 -0.2739 0.1809  493 PRO A C   
3664  O O   . PRO A 493 ? 1.7818 1.9771 1.7170 -0.4651 -0.2848 0.1836  493 PRO A O   
3665  C CB  . PRO A 493 ? 1.7228 1.9675 1.7677 -0.3790 -0.3144 0.2225  493 PRO A CB  
3666  C CG  . PRO A 493 ? 1.8063 2.0341 1.8972 -0.3294 -0.3026 0.2189  493 PRO A CG  
3667  C CD  . PRO A 493 ? 1.8409 1.9911 1.8836 -0.3253 -0.2831 0.2049  493 PRO A CD  
3668  N N   . ALA A 494 ? 1.7190 1.8502 1.6817 -0.3998 -0.2490 0.1639  494 ALA A N   
3669  C CA  . ALA A 494 ? 1.6386 1.7624 1.5847 -0.4187 -0.2321 0.1492  494 ALA A CA  
3670  C C   . ALA A 494 ? 1.6971 1.7329 1.5760 -0.4259 -0.2026 0.1283  494 ALA A C   
3671  O O   . ALA A 494 ? 1.6546 1.6710 1.5202 -0.4313 -0.1836 0.1164  494 ALA A O   
3672  C CB  . ALA A 494 ? 1.5210 1.6872 1.5327 -0.3849 -0.2273 0.1488  494 ALA A CB  
3673  N N   . HIS A 495 ? 1.7433 1.7262 1.5794 -0.4253 -0.1976 0.1248  495 HIS A N   
3674  C CA  . HIS A 495 ? 1.6851 1.5862 1.4597 -0.4277 -0.1688 0.1058  495 HIS A CA  
3675  C C   . HIS A 495 ? 1.8740 1.7384 1.5776 -0.4788 -0.1628 0.0970  495 HIS A C   
3676  O O   . HIS A 495 ? 1.9892 1.8618 1.6656 -0.5087 -0.1787 0.1030  495 HIS A O   
3677  C CB  . HIS A 495 ? 1.6271 1.4896 1.3889 -0.4033 -0.1629 0.1042  495 HIS A CB  
3678  C CG  . HIS A 495 ? 1.5510 1.3347 1.2538 -0.4014 -0.1330 0.0856  495 HIS A CG  
3679  N ND1 . HIS A 495 ? 1.6213 1.3803 1.3355 -0.3675 -0.1114 0.0752  495 HIS A ND1 
3680  C CD2 . HIS A 495 ? 1.8025 1.5300 1.4353 -0.4279 -0.1215 0.0764  495 HIS A CD2 
3681  C CE1 . HIS A 495 ? 1.7015 1.3916 1.3557 -0.3718 -0.0878 0.0618  495 HIS A CE1 
3682  N NE2 . HIS A 495 ? 1.7789 1.4456 1.3824 -0.4077 -0.0917 0.0609  495 HIS A NE2 
3683  N N   . VAL A 496 ? 2.0176 1.8386 1.6884 -0.4891 -0.1390 0.0827  496 VAL A N   
3684  C CA  . VAL A 496 ? 2.0693 1.8414 1.6678 -0.5378 -0.1273 0.0706  496 VAL A CA  
3685  C C   . VAL A 496 ? 2.0948 1.7771 1.6443 -0.5201 -0.0924 0.0539  496 VAL A C   
3686  O O   . VAL A 496 ? 2.2551 1.9207 1.8113 -0.5053 -0.0747 0.0495  496 VAL A O   
3687  C CB  . VAL A 496 ? 2.1765 1.9860 1.7839 -0.5733 -0.1319 0.0717  496 VAL A CB  
3688  C CG1 . VAL A 496 ? 2.0988 1.8698 1.6333 -0.6332 -0.1276 0.0604  496 VAL A CG1 
3689  C CG2 . VAL A 496 ? 2.0726 1.9859 1.7552 -0.5693 -0.1634 0.0907  496 VAL A CG2 
3690  N N   . CYS A 497 ? 1.8683 1.4954 1.3679 -0.5217 -0.0823 0.0457  497 CYS A N   
3691  C CA  . CYS A 497 ? 1.8561 1.4018 1.3144 -0.4971 -0.0486 0.0312  497 CYS A CA  
3692  C C   . CYS A 497 ? 2.0438 1.5173 1.4295 -0.5335 -0.0247 0.0162  497 CYS A C   
3693  O O   . CYS A 497 ? 2.0848 1.5246 1.4132 -0.5721 -0.0236 0.0073  497 CYS A O   
3694  C CB  . CYS A 497 ? 1.8877 1.4044 1.3250 -0.4801 -0.0439 0.0277  497 CYS A CB  
3695  S SG  . CYS A 497 ? 2.0484 1.4977 1.4684 -0.4307 -0.0084 0.0158  497 CYS A SG  
3696  N N   . ILE A 498 ? 2.2211 1.6693 1.6067 -0.5224 -0.0056 0.0134  498 ILE A N   
3697  C CA  . ILE A 498 ? 2.1561 1.5208 1.4683 -0.5534 0.0223  -0.0007 498 ILE A CA  
3698  C C   . ILE A 498 ? 2.1547 1.4356 1.4175 -0.5260 0.0511  -0.0125 498 ILE A C   
3699  O O   . ILE A 498 ? 2.0003 1.2953 1.2988 -0.4760 0.0529  -0.0077 498 ILE A O   
3700  C CB  . ILE A 498 ? 1.8774 1.2421 1.2048 -0.5502 0.0339  0.0033  498 ILE A CB  
3701  C CG1 . ILE A 498 ? 1.9022 1.3598 1.2862 -0.5733 0.0060  0.0152  498 ILE A CG1 
3702  C CG2 . ILE A 498 ? 1.8864 1.1561 1.1362 -0.5805 0.0649  -0.0099 498 ILE A CG2 
3703  C CD1 . ILE A 498 ? 1.9404 1.4207 1.3002 -0.6340 -0.0122 0.0121  498 ILE A CD1 
3704  N N   . VAL A 499 ? 2.1411 1.3398 1.3258 -0.5577 0.0734  -0.0283 499 VAL A N   
3705  C CA  . VAL A 499 ? 2.2518 1.3716 1.3885 -0.5308 0.1022  -0.0403 499 VAL A CA  
3706  C C   . VAL A 499 ? 2.3093 1.3292 1.3791 -0.5411 0.1384  -0.0523 499 VAL A C   
3707  O O   . VAL A 499 ? 2.2957 1.2883 1.3234 -0.5946 0.1405  -0.0604 499 VAL A O   
3708  C CB  . VAL A 499 ? 2.4022 1.5153 1.5034 -0.5559 0.0948  -0.0496 499 VAL A CB  
3709  C CG1 . VAL A 499 ? 2.3735 1.4142 1.4304 -0.5269 0.1249  -0.0622 499 VAL A CG1 
3710  C CG2 . VAL A 499 ? 2.2033 1.4123 1.3666 -0.5513 0.0580  -0.0347 499 VAL A CG2 
3711  N N   . THR A 500 ? 2.5883 1.5570 1.6494 -0.4919 0.1656  -0.0527 500 THR A N   
3712  C CA  . THR A 500 ? 2.6302 1.4971 1.6276 -0.4952 0.2022  -0.0609 500 THR A CA  
3713  C C   . THR A 500 ? 2.6282 1.4227 1.5857 -0.4564 0.2326  -0.0707 500 THR A C   
3714  O O   . THR A 500 ? 2.7237 1.5622 1.7220 -0.4149 0.2246  -0.0660 500 THR A O   
3715  C CB  . THR A 500 ? 2.4088 1.2875 1.4389 -0.4696 0.2073  -0.0459 500 THR A CB  
3716  O OG1 . THR A 500 ? 2.4783 1.3623 1.5371 -0.4042 0.2166  -0.0388 500 THR A OG1 
3717  C CG2 . THR A 500 ? 2.2395 1.2183 1.3360 -0.4861 0.1742  -0.0327 500 THR A CG2 
3718  N N   . PRO A 501 ? 2.5850 1.2709 1.4658 -0.4677 0.2680  -0.0844 501 PRO A N   
3719  C CA  . PRO A 501 ? 2.7515 1.3684 1.5958 -0.4264 0.2996  -0.0933 501 PRO A CA  
3720  C C   . PRO A 501 ? 2.4978 1.1535 1.3991 -0.3550 0.3012  -0.0769 501 PRO A C   
3721  O O   . PRO A 501 ? 2.4871 1.1176 1.3787 -0.3155 0.3195  -0.0817 501 PRO A O   
3722  C CB  . PRO A 501 ? 2.8099 1.3063 1.5749 -0.4442 0.3374  -0.1039 501 PRO A CB  
3723  C CG  . PRO A 501 ? 2.8168 1.3166 1.5582 -0.5182 0.3226  -0.1111 501 PRO A CG  
3724  C CD  . PRO A 501 ? 2.5893 1.2125 1.4141 -0.5218 0.2807  -0.0929 501 PRO A CD  
3725  N N   . GLU A 502 ? 2.5377 1.2565 1.4962 -0.3412 0.2825  -0.0591 502 GLU A N   
3726  C CA  . GLU A 502 ? 2.5449 1.3093 1.5590 -0.2764 0.2811  -0.0443 502 GLU A CA  
3727  C C   . GLU A 502 ? 2.4946 1.3753 1.5897 -0.2703 0.2428  -0.0357 502 GLU A C   
3728  O O   . GLU A 502 ? 2.1623 1.0825 1.2956 -0.2268 0.2394  -0.0330 502 GLU A O   
3729  C CB  . GLU A 502 ? 2.4441 1.1776 1.4529 -0.2563 0.2965  -0.0308 502 GLU A CB  
3730  C CG  . GLU A 502 ? 2.7174 1.3311 1.6506 -0.2457 0.3382  -0.0359 502 GLU A CG  
3731  C CD  . GLU A 502 ? 2.8643 1.4415 1.7876 -0.2235 0.3551  -0.0193 502 GLU A CD  
3732  O OE1 . GLU A 502 ? 2.8153 1.4167 1.7694 -0.1653 0.3590  -0.0055 502 GLU A OE1 
3733  O OE2 . GLU A 502 ? 2.8598 1.3860 1.7434 -0.2658 0.3643  -0.0197 502 GLU A OE2 
3734  N N   . ARG A 503 ? 2.6917 1.6269 1.8143 -0.3102 0.2158  -0.0314 503 ARG A N   
3735  C CA  . ARG A 503 ? 2.4120 1.4520 1.6098 -0.3035 0.1805  -0.0235 503 ARG A CA  
3736  C C   . ARG A 503 ? 2.4243 1.4769 1.6101 -0.3341 0.1668  -0.0326 503 ARG A C   
3737  O O   . ARG A 503 ? 2.5867 1.6222 1.7371 -0.3864 0.1611  -0.0387 503 ARG A O   
3738  C CB  . ARG A 503 ? 2.2869 1.3850 1.5251 -0.3256 0.1587  -0.0129 503 ARG A CB  
3739  C CG  . ARG A 503 ? 2.3670 1.5579 1.6652 -0.3395 0.1223  -0.0075 503 ARG A CG  
3740  C CD  . ARG A 503 ? 2.1689 1.4237 1.5169 -0.3471 0.1041  0.0037  503 ARG A CD  
3741  N NE  . ARG A 503 ? 2.2618 1.6071 1.6823 -0.3332 0.0741  0.0114  503 ARG A NE  
3742  C CZ  . ARG A 503 ? 2.3163 1.7104 1.7575 -0.3646 0.0482  0.0143  503 ARG A CZ  
3743  N NH1 . ARG A 503 ? 2.3326 1.7078 1.7343 -0.4155 0.0454  0.0106  503 ARG A NH1 
3744  N NH2 . ARG A 503 ? 2.1652 1.6264 1.6658 -0.3451 0.0252  0.0211  503 ARG A NH2 
3745  N N   . LEU A 504 ? 2.0577 1.1415 1.2707 -0.3054 0.1613  -0.0331 504 LEU A N   
3746  C CA  . LEU A 504 ? 2.1798 1.2662 1.3706 -0.3362 0.1519  -0.0410 504 LEU A CA  
3747  C C   . LEU A 504 ? 2.1463 1.3234 1.3970 -0.3503 0.1138  -0.0296 504 LEU A C   
3748  O O   . LEU A 504 ? 2.1164 1.3527 1.4302 -0.3261 0.0984  -0.0180 504 LEU A O   
3749  C CB  . LEU A 504 ? 2.1375 1.1989 1.3158 -0.3009 0.1716  -0.0484 504 LEU A CB  
3750  C CG  . LEU A 504 ? 2.4151 1.3784 1.5225 -0.2932 0.2107  -0.0618 504 LEU A CG  
3751  C CD1 . LEU A 504 ? 2.2659 1.2216 1.3834 -0.2396 0.2312  -0.0640 504 LEU A CD1 
3752  C CD2 . LEU A 504 ? 2.7048 1.6155 1.7431 -0.3433 0.2180  -0.0773 504 LEU A CD2 
3753  N N   . GLY A 505 ? 2.0716 1.2574 1.3008 -0.3873 0.1000  -0.0327 505 GLY A N   
3754  C CA  . GLY A 505 ? 2.0378 1.3067 1.3219 -0.3972 0.0643  -0.0192 505 GLY A CA  
3755  C C   . GLY A 505 ? 2.0471 1.3618 1.3930 -0.3493 0.0584  -0.0113 505 GLY A C   
3756  O O   . GLY A 505 ? 2.0547 1.3415 1.3853 -0.3249 0.0769  -0.0184 505 GLY A O   
3757  N N   . LEU A 506 ? 2.0172 1.4003 1.4307 -0.3368 0.0348  0.0018  506 LEU A N   
3758  C CA  . LEU A 506 ? 1.7457 1.1716 1.2192 -0.2933 0.0296  0.0073  506 LEU A CA  
3759  C C   . LEU A 506 ? 1.8301 1.2557 1.2979 -0.2884 0.0302  0.0059  506 LEU A C   
3760  O O   . LEU A 506 ? 1.9435 1.3828 1.4419 -0.2529 0.0369  0.0047  506 LEU A O   
3761  C CB  . LEU A 506 ? 1.7984 1.2982 1.3418 -0.2886 0.0013  0.0207  506 LEU A CB  
3762  C CG  . LEU A 506 ? 1.8772 1.3920 1.4330 -0.2988 -0.0030 0.0240  506 LEU A CG  
3763  C CD1 . LEU A 506 ? 1.8583 1.4470 1.4886 -0.2831 -0.0264 0.0351  506 LEU A CD1 
3764  C CD2 . LEU A 506 ? 1.9122 1.3822 1.4448 -0.2772 0.0239  0.0162  506 LEU A CD2 
3765  N N   . CYS A 507 ? 1.9748 1.3858 1.4015 -0.3249 0.0242  0.0056  507 CYS A N   
3766  C CA  . CYS A 507 ? 1.9852 1.3999 1.4084 -0.3199 0.0251  0.0061  507 CYS A CA  
3767  C C   . CYS A 507 ? 1.9190 1.2770 1.2997 -0.3003 0.0595  -0.0097 507 CYS A C   
3768  O O   . CYS A 507 ? 1.8935 1.2613 1.2853 -0.2833 0.0653  -0.0102 507 CYS A O   
3769  C CB  . CYS A 507 ? 2.2116 1.6307 1.6011 -0.3634 0.0085  0.0117  507 CYS A CB  
3770  S SG  . CYS A 507 ? 2.2116 1.5592 1.5076 -0.4065 0.0273  -0.0053 507 CYS A SG  
3771  N N   . GLY A 508 ? 1.9601 1.2623 1.2967 -0.3011 0.0822  -0.0211 508 GLY A N   
3772  C CA  . GLY A 508 ? 1.9260 1.1720 1.2238 -0.2767 0.1170  -0.0351 508 GLY A CA  
3773  C C   . GLY A 508 ? 2.0354 1.2218 1.2561 -0.3092 0.1340  -0.0483 508 GLY A C   
3774  O O   . GLY A 508 ? 2.1189 1.2469 1.2975 -0.2923 0.1663  -0.0618 508 GLY A O   
3775  N N   . ALA A 509 ? 1.8047 1.0058 1.0062 -0.3535 0.1132  -0.0447 509 ALA A N   
3776  C CA  . ALA A 509 ? 2.0204 1.1692 1.1448 -0.3887 0.1276  -0.0586 509 ALA A CA  
3777  C C   . ALA A 509 ? 2.3247 1.4248 1.3950 -0.4276 0.1323  -0.0684 509 ALA A C   
3778  O O   . ALA A 509 ? 2.3867 1.4106 1.3991 -0.4267 0.1648  -0.0860 509 ALA A O   
3779  C CB  . ALA A 509 ? 2.0139 1.2076 1.1431 -0.4151 0.1031  -0.0486 509 ALA A CB  
3780  N N   . VAL A 510 ? 2.3523 1.4950 1.4417 -0.4603 0.1019  -0.0575 510 VAL A N   
3781  C CA  . VAL A 510 ? 2.4063 1.5102 1.4448 -0.5057 0.1039  -0.0672 510 VAL A CA  
3782  C C   . VAL A 510 ? 2.3203 1.3657 1.3458 -0.4839 0.1321  -0.0756 510 VAL A C   
3783  O O   . VAL A 510 ? 2.2611 1.3417 1.3451 -0.4518 0.1252  -0.0632 510 VAL A O   
3784  C CB  . VAL A 510 ? 2.1398 1.3149 1.2167 -0.5373 0.0652  -0.0512 510 VAL A CB  
3785  C CG1 . VAL A 510 ? 2.1725 1.3147 1.2025 -0.5855 0.0674  -0.0615 510 VAL A CG1 
3786  C CG2 . VAL A 510 ? 2.3923 1.6230 1.4791 -0.5571 0.0368  -0.0395 510 VAL A CG2 
3787  N N   . SER A 511 ? 2.7410 1.6984 1.6901 -0.5010 0.1633  -0.0957 511 SER A N   
3788  C CA  . SER A 511 ? 2.6913 1.5816 1.6190 -0.4828 0.1924  -0.1023 511 SER A CA  
3789  C C   . SER A 511 ? 2.7898 1.6478 1.6742 -0.5382 0.1902  -0.1096 511 SER A C   
3790  O O   . SER A 511 ? 2.9122 1.7897 1.7712 -0.5890 0.1716  -0.1145 511 SER A O   
3791  C CB  . SER A 511 ? 2.7360 1.5442 1.6120 -0.4554 0.2331  -0.1186 511 SER A CB  
3792  O OG  . SER A 511 ? 3.0635 1.7933 1.8536 -0.5002 0.2529  -0.1403 511 SER A OG  
3793  N N   . TRP A 512 ? 2.6090 1.4226 1.4848 -0.5310 0.2077  -0.1095 512 TRP A N   
3794  C CA  . TRP A 512 ? 2.7691 1.5580 1.6084 -0.5881 0.2047  -0.1158 512 TRP A CA  
3795  C C   . TRP A 512 ? 2.8204 1.5504 1.5767 -0.6407 0.2159  -0.1393 512 TRP A C   
3796  O O   . TRP A 512 ? 2.8317 1.5713 1.5646 -0.6998 0.2012  -0.1447 512 TRP A O   
3797  C CB  . TRP A 512 ? 2.6728 1.3994 1.4978 -0.5732 0.2310  -0.1146 512 TRP A CB  
3798  C CG  . TRP A 512 ? 2.6368 1.3357 1.4247 -0.6332 0.2309  -0.1212 512 TRP A CG  
3799  C CD1 . TRP A 512 ? 2.6956 1.4647 1.5270 -0.6615 0.2035  -0.1087 512 TRP A CD1 
3800  C CD2 . TRP A 512 ? 2.7509 1.3433 1.4496 -0.6744 0.2613  -0.1435 512 TRP A CD2 
3801  N NE1 . TRP A 512 ? 2.8103 1.5293 1.5881 -0.7188 0.2138  -0.1208 512 TRP A NE1 
3802  C CE2 . TRP A 512 ? 2.9570 1.5642 1.6513 -0.7292 0.2492  -0.1428 512 TRP A CE2 
3803  C CE3 . TRP A 512 ? 2.7208 1.2067 1.3435 -0.6704 0.2988  -0.1648 512 TRP A CE3 
3804  C CZ2 . TRP A 512 ? 3.0526 1.5699 1.6677 -0.7831 0.2728  -0.1632 512 TRP A CZ2 
3805  C CZ3 . TRP A 512 ? 2.7443 1.1364 1.2870 -0.7211 0.3231  -0.1854 512 TRP A CZ3 
3806  C CH2 . TRP A 512 ? 2.8284 1.2357 1.3673 -0.7779 0.3098  -0.1848 512 TRP A CH2 
3807  N N   . LEU A 513 ? 2.6491 1.3242 1.3631 -0.6208 0.2411  -0.1535 513 LEU A N   
3808  C CA  . LEU A 513 ? 2.6415 1.2537 1.2695 -0.6698 0.2558  -0.1792 513 LEU A CA  
3809  C C   . LEU A 513 ? 2.7736 1.4572 1.4086 -0.6974 0.2249  -0.1773 513 LEU A C   
3810  O O   . LEU A 513 ? 2.9401 1.6097 1.5194 -0.7576 0.2184  -0.1924 513 LEU A O   
3811  C CB  . LEU A 513 ? 2.7257 1.2448 1.3028 -0.6331 0.3005  -0.1962 513 LEU A CB  
3812  C CG  . LEU A 513 ? 2.7063 1.1254 1.2470 -0.6148 0.3390  -0.2032 513 LEU A CG  
3813  C CD1 . LEU A 513 ? 2.7384 1.0817 1.2448 -0.5652 0.3807  -0.2150 513 LEU A CD1 
3814  C CD2 . LEU A 513 ? 2.7969 1.1462 1.2654 -0.6818 0.3492  -0.2225 513 LEU A CD2 
3815  N N   . ASP A 514 ? 2.7300 1.4855 1.4280 -0.6564 0.2071  -0.1595 514 ASP A N   
3816  C CA  . ASP A 514 ? 2.8791 1.7012 1.5856 -0.6785 0.1781  -0.1534 514 ASP A CA  
3817  C C   . ASP A 514 ? 2.8699 1.7657 1.6060 -0.7232 0.1376  -0.1399 514 ASP A C   
3818  O O   . ASP A 514 ? 2.8581 1.7837 1.5663 -0.7693 0.1167  -0.1424 514 ASP A O   
3819  C CB  . ASP A 514 ? 2.9229 1.8062 1.6986 -0.6236 0.1679  -0.1346 514 ASP A CB  
3820  C CG  . ASP A 514 ? 2.9488 1.7772 1.7164 -0.5701 0.2057  -0.1434 514 ASP A CG  
3821  O OD1 . ASP A 514 ? 2.9773 1.7142 1.6768 -0.5749 0.2420  -0.1653 514 ASP A OD1 
3822  O OD2 . ASP A 514 ? 2.7576 1.6352 1.5872 -0.5234 0.1996  -0.1286 514 ASP A OD2 
3823  N N   . ALA A 515 ? 2.6963 1.6247 1.4885 -0.7093 0.1267  -0.1254 515 ALA A N   
3824  C CA  . ALA A 515 ? 2.5496 1.5513 1.3764 -0.7474 0.0911  -0.1122 515 ALA A CA  
3825  C C   . ALA A 515 ? 2.6615 1.6188 1.4147 -0.8164 0.0964  -0.1325 515 ALA A C   
3826  O O   . ALA A 515 ? 2.6448 1.6656 1.4054 -0.8623 0.0647  -0.1266 515 ALA A O   
3827  C CB  . ALA A 515 ? 2.5188 1.5515 1.4128 -0.7153 0.0870  -0.0963 515 ALA A CB  
3828  N N   . LYS A 516 ? 2.9018 1.7503 1.5846 -0.8233 0.1369  -0.1564 516 LYS A N   
3829  C CA  . LYS A 516 ? 2.8907 1.6779 1.4937 -0.8891 0.1494  -0.1807 516 LYS A CA  
3830  C C   . LYS A 516 ? 2.8435 1.6352 1.3908 -0.9298 0.1399  -0.1949 516 LYS A C   
3831  O O   . LYS A 516 ? 2.8391 1.6571 1.3564 -0.9929 0.1201  -0.2024 516 LYS A O   
3832  C CB  . LYS A 516 ? 3.0063 1.6659 1.5498 -0.8745 0.1996  -0.2012 516 LYS A CB  
3833  C CG  . LYS A 516 ? 3.2283 1.7937 1.6700 -0.9361 0.2243  -0.2339 516 LYS A CG  
3834  C CD  . LYS A 516 ? 3.2143 1.6516 1.5913 -0.9052 0.2766  -0.2552 516 LYS A CD  
3835  C CE  . LYS A 516 ? 3.1516 1.5374 1.5530 -0.8532 0.3034  -0.2445 516 LYS A CE  
3836  N NZ  . LYS A 516 ? 3.1266 1.4893 1.5196 -0.8918 0.3052  -0.2441 516 LYS A NZ  
3837  N N   . ALA A 517 ? 2.6847 1.4552 1.2187 -0.8940 0.1541  -0.1984 517 ALA A N   
3838  C CA  . ALA A 517 ? 2.7105 1.4855 1.1915 -0.9261 0.1477  -0.2103 517 ALA A CA  
3839  C C   . ALA A 517 ? 2.8600 1.7557 1.3909 -0.9467 0.0962  -0.1856 517 ALA A C   
3840  O O   . ALA A 517 ? 2.9512 1.8659 1.4345 -0.9997 0.0799  -0.1941 517 ALA A O   
3841  C CB  . ALA A 517 ? 2.6807 1.4166 1.1499 -0.8762 0.1747  -0.2153 517 ALA A CB  
3842  N N   . THR A 518 ? 2.6385 1.6150 1.2637 -0.9047 0.0709  -0.1550 518 THR A N   
3843  C CA  . THR A 518 ? 2.5355 1.6256 1.2164 -0.9155 0.0231  -0.1280 518 THR A CA  
3844  C C   . THR A 518 ? 2.6574 1.7898 1.3264 -0.9792 -0.0029 -0.1294 518 THR A C   
3845  O O   . THR A 518 ? 2.6844 1.8872 1.3534 -1.0120 -0.0369 -0.1184 518 THR A O   
3846  C CB  . THR A 518 ? 2.3163 1.4701 1.0983 -0.8558 0.0077  -0.0990 518 THR A CB  
3847  O OG1 . THR A 518 ? 2.3887 1.5149 1.1803 -0.8035 0.0278  -0.0979 518 THR A OG1 
3848  C CG2 . THR A 518 ? 2.2491 1.5167 1.0940 -0.8636 -0.0404 -0.0697 518 THR A CG2 
3849  N N   . LEU A 519 ? 2.8242 1.9162 1.4831 -0.9972 0.0130  -0.1417 519 LEU A N   
3850  C CA  . LEU A 519 ? 2.8315 1.9613 1.4784 -1.0612 -0.0079 -0.1456 519 LEU A CA  
3851  C C   . LEU A 519 ? 2.9372 2.0168 1.4829 -1.1273 0.0005  -0.1751 519 LEU A C   
3852  O O   . LEU A 519 ? 2.9794 2.1216 1.5142 -1.1834 -0.0299 -0.1740 519 LEU A O   
3853  C CB  . LEU A 519 ? 2.7584 1.8504 1.4199 -1.0609 0.0117  -0.1508 519 LEU A CB  
3854  C CG  . LEU A 519 ? 3.0092 2.1376 1.6623 -1.1277 -0.0053 -0.1560 519 LEU A CG  
3855  C CD1 . LEU A 519 ? 2.7822 2.0495 1.5184 -1.1301 -0.0543 -0.1257 519 LEU A CD1 
3856  C CD2 . LEU A 519 ? 3.1043 2.1694 1.7540 -1.1278 0.0242  -0.1648 519 LEU A CD2 
3857  N N   . GLU A 520 ? 2.8542 1.8243 1.3264 -1.1204 0.0418  -0.2018 520 GLU A N   
3858  C CA  . GLU A 520 ? 2.8793 1.7909 1.2495 -1.1802 0.0551  -0.2338 520 GLU A CA  
3859  C C   . GLU A 520 ? 2.8811 1.8675 1.2440 -1.1963 0.0224  -0.2229 520 GLU A C   
3860  O O   . GLU A 520 ? 2.9074 1.9330 1.2353 -1.2493 0.0053  -0.2270 520 GLU A O   
3861  C CB  . GLU A 520 ? 2.9235 1.7031 1.2253 -1.1561 0.1096  -0.2622 520 GLU A CB  
3862  C CG  . GLU A 520 ? 3.1395 1.8383 1.4401 -1.1362 0.1465  -0.2705 520 GLU A CG  
3863  C CD  . GLU A 520 ? 3.3703 2.0629 1.6426 -1.1835 0.1536  -0.2790 520 GLU A CD  
3864  O OE1 . GLU A 520 ? 3.1906 1.8730 1.4022 -1.2247 0.1601  -0.2947 520 GLU A OE1 
3865  O OE2 . GLU A 520 ? 3.1877 1.8860 1.4978 -1.1807 0.1535  -0.2700 520 GLU A OE2 
3866  N N   . LEU A 521 ? 2.8537 1.8719 1.2620 -1.1388 0.0170  -0.2012 521 LEU A N   
3867  C CA  . LEU A 521 ? 2.8814 1.9671 1.2863 -1.1463 -0.0120 -0.1859 521 LEU A CA  
3868  C C   . LEU A 521 ? 2.9322 2.1444 1.4009 -1.1657 -0.0660 -0.1543 521 LEU A C   
3869  O O   . LEU A 521 ? 3.0260 2.2863 1.4574 -1.2173 -0.0929 -0.1543 521 LEU A O   
3870  C CB  . LEU A 521 ? 2.7905 1.8721 1.2332 -1.0773 -0.0001 -0.1702 521 LEU A CB  
3871  C CG  . LEU A 521 ? 2.8086 1.7789 1.1919 -1.0526 0.0516  -0.1984 521 LEU A CG  
3872  C CD1 . LEU A 521 ? 3.0278 2.0113 1.4645 -0.9838 0.0596  -0.1796 521 LEU A CD1 
3873  C CD2 . LEU A 521 ? 2.8538 1.7779 1.1334 -1.1037 0.0646  -0.2269 521 LEU A CD2 
3874  N N   . ASN A 522 ? 2.7223 1.9902 1.2862 -1.1234 -0.0815 -0.1274 522 ASN A N   
3875  C CA  . ASN A 522 ? 2.5692 1.9576 1.2041 -1.1318 -0.1299 -0.0956 522 ASN A CA  
3876  C C   . ASN A 522 ? 2.5981 2.0031 1.2668 -1.1507 -0.1327 -0.0983 522 ASN A C   
3877  O O   . ASN A 522 ? 2.6759 2.0929 1.4157 -1.1040 -0.1285 -0.0840 522 ASN A O   
3878  C CB  . ASN A 522 ? 2.4111 1.8570 1.1334 -1.0650 -0.1463 -0.0606 522 ASN A CB  
3879  C CG  . ASN A 522 ? 2.6453 2.0955 1.3442 -1.0506 -0.1510 -0.0509 522 ASN A CG  
3880  O OD1 . ASN A 522 ? 2.7836 2.2359 1.4147 -1.0959 -0.1596 -0.0594 522 ASN A OD1 
3881  N ND2 . ASN A 522 ? 2.3493 1.8020 1.1021 -0.9892 -0.1450 -0.0331 522 ASN A ND2 
3882  N N   . PRO A 523 ? 2.6837 2.0921 1.3026 -1.2205 -0.1394 -0.1169 523 PRO A N   
3883  C CA  . PRO A 523 ? 2.8391 2.2660 1.4909 -1.2419 -0.1409 -0.1190 523 PRO A CA  
3884  C C   . PRO A 523 ? 2.8711 2.4129 1.6330 -1.2088 -0.1760 -0.0820 523 PRO A C   
3885  O O   . PRO A 523 ? 2.9006 2.4442 1.7093 -1.1936 -0.1670 -0.0789 523 PRO A O   
3886  C CB  . PRO A 523 ? 3.0079 2.4514 1.6018 -1.3115 -0.1465 -0.1345 523 PRO A CB  
3887  C CG  . PRO A 523 ? 2.9444 2.3262 1.4539 -1.3237 -0.1281 -0.1530 523 PRO A CG  
3888  C CD  . PRO A 523 ? 2.7668 2.1636 1.2958 -1.2860 -0.1453 -0.1380 523 PRO A CD  
3889  N N   . THR A 524 ? 2.9360 2.5713 1.7379 -1.1960 -0.2146 -0.0533 524 THR A N   
3890  C CA  . THR A 524 ? 2.8395 2.5844 1.7458 -1.1608 -0.2484 -0.0171 524 THR A CA  
3891  C C   . THR A 524 ? 2.7412 2.4819 1.6992 -1.0854 -0.2449 0.0044  524 THR A C   
3892  O O   . THR A 524 ? 2.7720 2.5973 1.7900 -1.0595 -0.2775 0.0361  524 THR A O   
3893  C CB  . THR A 524 ? 2.8089 2.6698 1.7289 -1.2029 -0.2965 0.0023  524 THR A CB  
3894  O OG1 . THR A 524 ? 2.7153 2.6788 1.7386 -1.1676 -0.3256 0.0358  524 THR A OG1 
3895  C CG2 . THR A 524 ? 2.7759 2.6484 1.6514 -1.2094 -0.3136 0.0110  524 THR A CG2 
3896  N N   . GLY A 525 ? 2.6166 2.2591 1.5515 -1.0511 -0.2049 -0.0128 525 GLY A N   
3897  C CA  . GLY A 525 ? 2.3574 1.9867 1.3348 -0.9834 -0.1964 0.0022  525 GLY A CA  
3898  C C   . GLY A 525 ? 2.2146 1.8561 1.2716 -0.9324 -0.1887 0.0128  525 GLY A C   
3899  O O   . GLY A 525 ? 2.2627 1.9448 1.3558 -0.9467 -0.1975 0.0159  525 GLY A O   
3900  N N   . PRO A 526 ? 2.4382 2.0483 1.5242 -0.8735 -0.1720 0.0181  526 PRO A N   
3901  C CA  . PRO A 526 ? 2.4721 2.0956 1.6319 -0.8247 -0.1650 0.0271  526 PRO A CA  
3902  C C   . PRO A 526 ? 2.4404 1.9899 1.5723 -0.8278 -0.1299 0.0041  526 PRO A C   
3903  O O   . PRO A 526 ? 2.5117 2.0904 1.6899 -0.8209 -0.1319 0.0094  526 PRO A O   
3904  C CB  . PRO A 526 ? 2.3062 1.9177 1.4951 -0.7682 -0.1582 0.0373  526 PRO A CB  
3905  C CG  . PRO A 526 ? 2.3881 1.9367 1.4984 -0.7855 -0.1415 0.0217  526 PRO A CG  
3906  C CD  . PRO A 526 ? 2.4517 2.0173 1.5051 -0.8505 -0.1586 0.0156  526 PRO A CD  
3907  N N   . CYS A 527 ? 2.3905 1.8433 1.4460 -0.8373 -0.0967 -0.0205 527 CYS A N   
3908  C CA  . CYS A 527 ? 2.4001 1.7702 1.4208 -0.8382 -0.0604 -0.0413 527 CYS A CA  
3909  C C   . CYS A 527 ? 2.6409 2.0066 1.6219 -0.9027 -0.0628 -0.0542 527 CYS A C   
3910  O O   . CYS A 527 ? 2.6682 1.9992 1.5765 -0.9521 -0.0594 -0.0719 527 CYS A O   
3911  C CB  . CYS A 527 ? 2.1627 1.4321 1.1170 -0.8231 -0.0235 -0.0622 527 CYS A CB  
3912  S SG  . CYS A 527 ? 2.4033 1.6787 1.4042 -0.7499 -0.0175 -0.0492 527 CYS A SG  
3913  N N   . GLN A 528 ? 2.9294 2.3319 1.9573 -0.9044 -0.0681 -0.0462 528 GLN A N   
3914  C CA  . GLN A 528 ? 2.8072 2.2132 1.8065 -0.9664 -0.0700 -0.0571 528 GLN A CA  
3915  C C   . GLN A 528 ? 2.7676 2.0988 1.7503 -0.9606 -0.0345 -0.0690 528 GLN A C   
3916  O O   . GLN A 528 ? 2.7195 2.0354 1.7414 -0.9045 -0.0199 -0.0603 528 GLN A O   
3917  C CB  . GLN A 528 ? 2.8012 2.3335 1.8716 -0.9829 -0.1117 -0.0347 528 GLN A CB  
3918  C CG  . GLN A 528 ? 2.7946 2.3977 1.8703 -0.9970 -0.1476 -0.0219 528 GLN A CG  
3919  C CD  . GLN A 528 ? 3.0071 2.7374 2.1572 -1.0063 -0.1888 0.0030  528 GLN A CD  
3920  O OE1 . GLN A 528 ? 3.2059 2.9817 2.4224 -0.9843 -0.1920 0.0150  528 GLN A OE1 
3921  N NE2 . GLN A 528 ? 2.6710 2.4638 1.8113 -1.0376 -0.2211 0.0122  528 GLN A NE2 
3922  N N   . ALA A 529 ? 2.8536 2.1363 1.7753 -1.0200 -0.0201 -0.0888 529 ALA A N   
3923  C CA  . ALA A 529 ? 2.6303 1.8318 1.5254 -1.0216 0.0156  -0.0998 529 ALA A CA  
3924  C C   . ALA A 529 ? 2.5731 1.8432 1.5422 -1.0099 0.0054  -0.0810 529 ALA A C   
3925  O O   . ALA A 529 ? 2.5958 1.9714 1.6163 -1.0335 -0.0281 -0.0678 529 ALA A O   
3926  C CB  . ALA A 529 ? 2.4870 1.6161 1.2934 -1.0943 0.0335  -0.1271 529 ALA A CB  
3927  N N   . VAL A 530 ? 2.5734 1.7843 1.5467 -0.9720 0.0353  -0.0793 530 VAL A N   
3928  C CA  . VAL A 530 ? 2.5349 1.7946 1.5692 -0.9564 0.0335  -0.0633 530 VAL A CA  
3929  C C   . VAL A 530 ? 2.7691 1.9188 1.7437 -0.9707 0.0753  -0.0761 530 VAL A C   
3930  O O   . VAL A 530 ? 2.7945 1.8649 1.7478 -0.9231 0.1037  -0.0775 530 VAL A O   
3931  C CB  . VAL A 530 ? 2.3765 1.6815 1.4852 -0.8789 0.0263  -0.0433 530 VAL A CB  
3932  C CG1 . VAL A 530 ? 2.1442 1.4882 1.3071 -0.8609 0.0298  -0.0295 530 VAL A CG1 
3933  C CG2 . VAL A 530 ? 2.2436 1.6472 1.4087 -0.8639 -0.0125 -0.0297 530 VAL A CG2 
3934  N N   . PRO A 531 ? 2.9803 2.1192 1.9243 -1.0352 0.0812  -0.0853 531 PRO A N   
3935  C CA  . PRO A 531 ? 3.0430 2.0647 1.9243 -1.0482 0.1239  -0.0964 531 PRO A CA  
3936  C C   . PRO A 531 ? 3.0151 2.0299 1.9370 -0.9935 0.1407  -0.0780 531 PRO A C   
3937  O O   . PRO A 531 ? 2.9281 2.0429 1.9261 -0.9783 0.1194  -0.0596 531 PRO A O   
3938  C CB  . PRO A 531 ? 3.0544 2.0857 1.9043 -1.1341 0.1209  -0.1088 531 PRO A CB  
3939  C CG  . PRO A 531 ? 2.9030 2.0814 1.8247 -1.1536 0.0749  -0.0963 531 PRO A CG  
3940  C CD  . PRO A 531 ? 2.8908 2.1221 1.8544 -1.0996 0.0503  -0.0855 531 PRO A CD  
3941  N N   . LYS A 532 ? 2.9375 1.8344 1.8072 -0.9619 0.1795  -0.0829 532 LYS A N   
3942  C CA  . LYS A 532 ? 2.7551 1.6346 1.6521 -0.9078 0.1981  -0.0654 532 LYS A CA  
3943  C C   . LYS A 532 ? 2.7295 1.5923 1.6142 -0.9490 0.2142  -0.0613 532 LYS A C   
3944  O O   . LYS A 532 ? 2.6406 1.3873 1.4550 -0.9644 0.2508  -0.0692 532 LYS A O   
3945  C CB  . LYS A 532 ? 2.5594 1.3212 1.4034 -0.8578 0.2332  -0.0703 532 LYS A CB  
3946  C CG  . LYS A 532 ? 2.6774 1.4522 1.5671 -0.7823 0.2405  -0.0496 532 LYS A CG  
3947  C CD  . LYS A 532 ? 2.5854 1.2320 1.4131 -0.7488 0.2837  -0.0502 532 LYS A CD  
3948  C CE  . LYS A 532 ? 2.5712 1.1415 1.3488 -0.7282 0.2993  -0.0661 532 LYS A CE  
3949  N NZ  . LYS A 532 ? 2.6267 1.0932 1.3634 -0.6758 0.3376  -0.0612 532 LYS A NZ  
3950  N N   . GLU A 533 ? 2.8855 1.8632 1.8388 -0.9658 0.1882  -0.0484 533 GLU A N   
3951  C CA  . GLU A 533 ? 2.9913 1.9706 1.9420 -1.0070 0.2013  -0.0431 533 GLU A CA  
3952  C C   . GLU A 533 ? 3.0246 2.0961 2.0570 -0.9641 0.1903  -0.0197 533 GLU A C   
3953  O O   . GLU A 533 ? 2.8628 2.0230 1.9636 -0.9188 0.1631  -0.0099 533 GLU A O   
3954  C CB  . GLU A 533 ? 2.9174 1.9469 1.8605 -1.0928 0.1840  -0.0554 533 GLU A CB  
3955  C CG  . GLU A 533 ? 2.9590 1.8975 1.8145 -1.1424 0.1987  -0.0818 533 GLU A CG  
3956  C CD  . GLU A 533 ? 3.2357 2.2552 2.0965 -1.2056 0.1752  -0.0933 533 GLU A CD  
3957  O OE1 . GLU A 533 ? 3.0963 2.2407 2.0299 -1.2229 0.1446  -0.0802 533 GLU A OE1 
3958  O OE2 . GLU A 533 ? 3.4322 2.3925 2.2247 -1.2368 0.1880  -0.1152 533 GLU A OE2 
3959  N N   . GLY A 534 ? 3.0339 2.0802 2.0555 -0.9801 0.2130  -0.0114 534 GLY A N   
3960  C CA  . GLY A 534 ? 2.8819 2.0077 1.9716 -0.9448 0.2076  0.0092  534 GLY A CA  
3961  C C   . GLY A 534 ? 2.8610 1.9583 1.9635 -0.8621 0.2178  0.0212  534 GLY A C   
3962  O O   . GLY A 534 ? 2.8542 2.0409 2.0271 -0.8149 0.1938  0.0302  534 GLY A O   
3963  N N   . VAL A 535 ? 2.5802 1.5528 1.6143 -0.8440 0.2537  0.0216  535 VAL A N   
3964  C CA  . VAL A 535 ? 2.4894 1.4318 1.5302 -0.7660 0.2648  0.0334  535 VAL A CA  
3965  C C   . VAL A 535 ? 2.5058 1.5138 1.5980 -0.7375 0.2647  0.0535  535 VAL A C   
3966  O O   . VAL A 535 ? 2.5721 1.5554 1.6416 -0.7694 0.2844  0.0609  535 VAL A O   
3967  C CB  . VAL A 535 ? 2.5862 1.3774 1.5388 -0.7531 0.3044  0.0302  535 VAL A CB  
3968  C CG1 . VAL A 535 ? 2.4808 1.2529 1.4449 -0.6701 0.3123  0.0427  535 VAL A CG1 
3969  C CG2 . VAL A 535 ? 2.5279 1.2502 1.4233 -0.7893 0.3081  0.0071  535 VAL A CG2 
3970  N N   . VAL A 536 ? 2.3731 1.4637 1.5327 -0.6800 0.2435  0.0615  536 VAL A N   
3971  C CA  . VAL A 536 ? 2.2256 1.3838 1.4355 -0.6488 0.2422  0.0781  536 VAL A CA  
3972  C C   . VAL A 536 ? 2.3015 1.4133 1.4988 -0.5780 0.2579  0.0887  536 VAL A C   
3973  O O   . VAL A 536 ? 2.4710 1.5613 1.6543 -0.5624 0.2780  0.1035  536 VAL A O   
3974  C CB  . VAL A 536 ? 2.0337 1.3329 1.3351 -0.6424 0.2053  0.0780  536 VAL A CB  
3975  C CG1 . VAL A 536 ? 2.1371 1.5046 1.4883 -0.6093 0.2062  0.0925  536 VAL A CG1 
3976  C CG2 . VAL A 536 ? 2.1346 1.4866 1.4498 -0.7111 0.1887  0.0699  536 VAL A CG2 
3977  N N   . ASP A 537 ? 2.3635 1.4628 1.5650 -0.5362 0.2489  0.0820  537 ASP A N   
3978  C CA  . ASP A 537 ? 2.5092 1.5731 1.7022 -0.4687 0.2614  0.0910  537 ASP A CA  
3979  C C   . ASP A 537 ? 2.4569 1.4499 1.6118 -0.4494 0.2672  0.0799  537 ASP A C   
3980  O O   . ASP A 537 ? 2.4670 1.4948 1.6436 -0.4616 0.2458  0.0667  537 ASP A O   
3981  C CB  . ASP A 537 ? 2.3813 1.5550 1.6539 -0.4218 0.2372  0.0964  537 ASP A CB  
3982  C CG  . ASP A 537 ? 2.4273 1.5852 1.6958 -0.3612 0.2513  0.1101  537 ASP A CG  
3983  O OD1 . ASP A 537 ? 2.6080 1.6758 1.8223 -0.3363 0.2731  0.1135  537 ASP A OD1 
3984  O OD2 . ASP A 537 ? 2.3617 1.5991 1.6807 -0.3380 0.2407  0.1172  537 ASP A OD2 
3985  N N   . GLU A 538 ? 2.6222 1.5174 1.7204 -0.4180 0.2966  0.0865  538 GLU A N   
3986  C CA  . GLU A 538 ? 2.6804 1.5041 1.7401 -0.3954 0.3070  0.0764  538 GLU A CA  
3987  C C   . GLU A 538 ? 2.6893 1.5615 1.7931 -0.3271 0.2947  0.0799  538 GLU A C   
3988  O O   . GLU A 538 ? 2.8138 1.6746 1.9153 -0.3126 0.2900  0.0682  538 GLU A O   
3989  C CB  . GLU A 538 ? 2.7298 1.4182 1.7043 -0.3950 0.3474  0.0813  538 GLU A CB  
3990  C CG  . GLU A 538 ? 2.8876 1.5105 1.8079 -0.4674 0.3630  0.0733  538 GLU A CG  
3991  C CD  . GLU A 538 ? 3.0554 1.6315 1.9383 -0.5077 0.3629  0.0494  538 GLU A CD  
3992  O OE1 . GLU A 538 ? 3.0540 1.7121 1.9796 -0.5345 0.3322  0.0375  538 GLU A OE1 
3993  O OE2 . GLU A 538 ? 3.0187 1.4747 1.8276 -0.5121 0.3942  0.0429  538 GLU A OE2 
3994  N N   . ASN A 539 ? 2.7522 1.6794 1.8946 -0.2872 0.2903  0.0951  539 ASN A N   
3995  C CA  . ASN A 539 ? 2.7372 1.7164 1.9228 -0.2253 0.2781  0.0976  539 ASN A CA  
3996  C C   . ASN A 539 ? 2.5905 1.6737 1.8480 -0.2294 0.2429  0.0861  539 ASN A C   
3997  O O   . ASN A 539 ? 2.5574 1.6594 1.8359 -0.1989 0.2332  0.0788  539 ASN A O   
3998  C CB  . ASN A 539 ? 2.7971 1.8019 1.9960 -0.1852 0.2847  0.1164  539 ASN A CB  
3999  C CG  . ASN A 539 ? 2.9587 1.8604 2.0877 -0.1696 0.3194  0.1321  539 ASN A CG  
4000  O OD1 . ASN A 539 ? 2.8266 1.6351 1.9010 -0.1682 0.3401  0.1284  539 ASN A OD1 
4001  N ND2 . ASN A 539 ? 3.1222 2.0361 2.2494 -0.1565 0.3278  0.1506  539 ASN A ND2 
4002  N N   . LEU A 540 ? 2.5049 1.6556 1.8007 -0.2664 0.2250  0.0852  540 LEU A N   
4003  C CA  . LEU A 540 ? 2.3897 1.6370 1.7540 -0.2705 0.1922  0.0767  540 LEU A CA  
4004  C C   . LEU A 540 ? 2.3506 1.5876 1.7034 -0.3161 0.1806  0.0638  540 LEU A C   
4005  O O   . LEU A 540 ? 2.1624 1.4584 1.5599 -0.3116 0.1563  0.0572  540 LEU A O   
4006  C CB  . LEU A 540 ? 2.2608 1.5939 1.6776 -0.2826 0.1781  0.0828  540 LEU A CB  
4007  C CG  . LEU A 540 ? 2.2128 1.5657 1.6403 -0.2457 0.1885  0.0953  540 LEU A CG  
4008  C CD1 . LEU A 540 ? 2.2239 1.6640 1.7036 -0.2630 0.1751  0.0982  540 LEU A CD1 
4009  C CD2 . LEU A 540 ? 2.2759 1.6535 1.7298 -0.1861 0.1826  0.0945  540 LEU A CD2 
4010  N N   . GLY A 541 ? 2.4085 1.5712 1.7004 -0.3607 0.1980  0.0604  541 GLY A N   
4011  C CA  . GLY A 541 ? 2.1943 1.3444 1.4668 -0.4086 0.1883  0.0473  541 GLY A CA  
4012  C C   . GLY A 541 ? 2.1645 1.4008 1.4831 -0.4515 0.1623  0.0473  541 GLY A C   
4013  O O   . GLY A 541 ? 2.1610 1.4686 1.5287 -0.4492 0.1346  0.0442  541 GLY A O   
4014  N N   . ILE A 542 ? 2.0724 1.3046 1.3768 -0.4903 0.1717  0.0519  542 ILE A N   
4015  C CA  . ILE A 542 ? 2.1082 1.4279 1.4582 -0.5322 0.1488  0.0529  542 ILE A CA  
4016  C C   . ILE A 542 ? 2.0847 1.3591 1.3819 -0.6019 0.1584  0.0455  542 ILE A C   
4017  O O   . ILE A 542 ? 2.2974 1.5180 1.5545 -0.6226 0.1833  0.0495  542 ILE A O   
4018  C CB  . ILE A 542 ? 1.9962 1.3845 1.3973 -0.5131 0.1475  0.0657  542 ILE A CB  
4019  C CG1 . ILE A 542 ? 1.8984 1.3357 1.3521 -0.4471 0.1368  0.0700  542 ILE A CG1 
4020  C CG2 . ILE A 542 ? 1.9503 1.4328 1.4008 -0.5558 0.1258  0.0669  542 ILE A CG2 
4021  C CD1 . ILE A 542 ? 1.9588 1.4279 1.4371 -0.4184 0.1467  0.0813  542 ILE A CD1 
4022  N N   . TRP A 543 ? 2.1778 1.4739 1.4734 -0.6398 0.1387  0.0351  543 TRP A N   
4023  C CA  . TRP A 543 ? 2.3562 1.6203 1.6042 -0.7114 0.1436  0.0253  543 TRP A CA  
4024  C C   . TRP A 543 ? 2.4525 1.8361 1.7628 -0.7460 0.1102  0.0282  543 TRP A C   
4025  O O   . TRP A 543 ? 2.3617 1.8190 1.7244 -0.7239 0.0816  0.0308  543 TRP A O   
4026  C CB  . TRP A 543 ? 2.3638 1.5461 1.5464 -0.7294 0.1506  0.0088  543 TRP A CB  
4027  C CG  . TRP A 543 ? 2.3878 1.4447 1.5015 -0.7035 0.1876  0.0048  543 TRP A CG  
4028  C CD1 . TRP A 543 ? 2.4730 1.4254 1.5121 -0.7370 0.2201  -0.0015 543 TRP A CD1 
4029  C CD2 . TRP A 543 ? 2.3752 1.3990 1.4896 -0.6374 0.1964  0.0076  543 TRP A CD2 
4030  N NE1 . TRP A 543 ? 2.4773 1.3318 1.4707 -0.6920 0.2489  -0.0016 543 TRP A NE1 
4031  C CE2 . TRP A 543 ? 2.4973 1.3981 1.5373 -0.6306 0.2343  0.0040  543 TRP A CE2 
4032  C CE3 . TRP A 543 ? 2.3772 1.4636 1.5482 -0.5840 0.1766  0.0128  543 TRP A CE3 
4033  C CZ2 . TRP A 543 ? 2.4648 1.3118 1.4891 -0.5703 0.2515  0.0064  543 TRP A CZ2 
4034  C CZ3 . TRP A 543 ? 2.4038 1.4371 1.5581 -0.5287 0.1936  0.0135  543 TRP A CZ3 
4035  C CH2 . TRP A 543 ? 2.4109 1.3299 1.4944 -0.5209 0.2300  0.0109  543 TRP A CH2 
4036  N N   . GLU A 544 ? 2.5295 1.9340 1.8357 -0.7991 0.1144  0.0291  544 GLU A N   
4037  C CA  . GLU A 544 ? 2.4481 1.9729 1.8162 -0.8328 0.0843  0.0334  544 GLU A CA  
4038  C C   . GLU A 544 ? 2.5043 2.0669 1.8747 -0.8614 0.0552  0.0253  544 GLU A C   
4039  O O   . GLU A 544 ? 2.5752 2.2474 2.0147 -0.8552 0.0234  0.0336  544 GLU A O   
4040  C CB  . GLU A 544 ? 2.5955 2.1250 1.9476 -0.8924 0.0983  0.0334  544 GLU A CB  
4041  C CG  . GLU A 544 ? 2.7463 2.2630 2.1077 -0.8665 0.1229  0.0454  544 GLU A CG  
4042  C CD  . GLU A 544 ? 2.8993 2.4134 2.2405 -0.9267 0.1404  0.0463  544 GLU A CD  
4043  O OE1 . GLU A 544 ? 2.8433 2.3531 2.1547 -0.9937 0.1362  0.0350  544 GLU A OE1 
4044  O OE2 . GLU A 544 ? 2.8775 2.3953 2.2313 -0.9089 0.1587  0.0580  544 GLU A OE2 
4045  N N   . LYS A 545 ? 2.4655 1.9379 1.7601 -0.8908 0.0667  0.0100  545 LYS A N   
4046  C CA  . LYS A 545 ? 2.5227 2.0258 1.8101 -0.9195 0.0400  0.0018  545 LYS A CA  
4047  C C   . LYS A 545 ? 2.4703 1.9988 1.7945 -0.8582 0.0226  0.0083  545 LYS A C   
4048  O O   . LYS A 545 ? 2.3512 1.9675 1.7211 -0.8613 -0.0111 0.0146  545 LYS A O   
4049  C CB  . LYS A 545 ? 2.5414 1.9338 1.7318 -0.9675 0.0610  -0.0191 545 LYS A CB  
4050  C CG  . LYS A 545 ? 2.6578 2.0780 1.8289 -1.0073 0.0356  -0.0295 545 LYS A CG  
4051  C CD  . LYS A 545 ? 2.5351 2.0455 1.7283 -1.0735 0.0116  -0.0294 545 LYS A CD  
4052  C CE  . LYS A 545 ? 2.5816 2.1785 1.8012 -1.0867 -0.0283 -0.0265 545 LYS A CE  
4053  N NZ  . LYS A 545 ? 2.4598 2.1878 1.7432 -1.1209 -0.0591 -0.0150 545 LYS A NZ  
4054  N N   . VAL A 546 ? 2.3935 1.8498 1.6992 -0.8048 0.0447  0.0080  546 VAL A N   
4055  C CA  . VAL A 546 ? 2.1078 1.5801 1.4434 -0.7491 0.0318  0.0123  546 VAL A CA  
4056  C C   . VAL A 546 ? 2.1044 1.6965 1.5347 -0.7191 0.0023  0.0286  546 VAL A C   
4057  O O   . VAL A 546 ? 2.2813 1.9260 1.7457 -0.7049 -0.0236 0.0334  546 VAL A O   
4058  C CB  . VAL A 546 ? 1.9588 1.3436 1.2653 -0.6959 0.0617  0.0102  546 VAL A CB  
4059  C CG1 . VAL A 546 ? 1.8761 1.2953 1.2280 -0.6372 0.0474  0.0162  546 VAL A CG1 
4060  C CG2 . VAL A 546 ? 2.0205 1.2848 1.2342 -0.7195 0.0904  -0.0064 546 VAL A CG2 
4061  N N   . ASN A 547 ? 2.1614 1.7938 1.6319 -0.7091 0.0077  0.0373  547 ASN A N   
4062  C CA  . ASN A 547 ? 2.2441 1.9909 1.8050 -0.6816 -0.0183 0.0511  547 ASN A CA  
4063  C C   . ASN A 547 ? 2.2719 2.1034 1.8615 -0.7248 -0.0497 0.0551  547 ASN A C   
4064  O O   . ASN A 547 ? 2.2862 2.1889 1.9317 -0.6993 -0.0769 0.0646  547 ASN A O   
4065  C CB  . ASN A 547 ? 2.0860 1.8641 1.6803 -0.6709 -0.0052 0.0581  547 ASN A CB  
4066  C CG  . ASN A 547 ? 2.1025 1.8141 1.6776 -0.6230 0.0220  0.0578  547 ASN A CG  
4067  O OD1 . ASN A 547 ? 2.1098 1.7425 1.6396 -0.6023 0.0349  0.0514  547 ASN A OD1 
4068  N ND2 . ASN A 547 ? 2.1322 1.8794 1.7417 -0.6051 0.0309  0.0652  547 ASN A ND2 
4069  N N   . GLU A 548 ? 2.6327 2.4562 2.1846 -0.7880 -0.0459 0.0486  548 GLU A N   
4070  C CA  . GLU A 548 ? 2.6031 2.5170 2.1832 -0.8331 -0.0763 0.0530  548 GLU A CA  
4071  C C   . GLU A 548 ? 2.5993 2.5225 2.1696 -0.8336 -0.1012 0.0532  548 GLU A C   
4072  O O   . GLU A 548 ? 2.5687 2.5879 2.1988 -0.8251 -0.1329 0.0667  548 GLU A O   
4073  C CB  . GLU A 548 ? 2.7150 2.6052 2.2443 -0.9065 -0.0641 0.0423  548 GLU A CB  
4074  C CG  . GLU A 548 ? 2.8760 2.8580 2.4253 -0.9614 -0.0952 0.0446  548 GLU A CG  
4075  C CD  . GLU A 548 ? 2.9313 3.0519 2.5789 -0.9416 -0.1243 0.0636  548 GLU A CD  
4076  O OE1 . GLU A 548 ? 3.0486 3.2049 2.7408 -0.9236 -0.1132 0.0701  548 GLU A OE1 
4077  O OE2 . GLU A 548 ? 2.8019 2.9952 2.4810 -0.9432 -0.1576 0.0725  548 GLU A OE2 
4078  N N   . THR A 549 ? 2.2295 2.0542 1.7249 -0.8419 -0.0862 0.0393  549 THR A N   
4079  C CA  . THR A 549 ? 2.1902 2.0183 1.6684 -0.8449 -0.1069 0.0388  549 THR A CA  
4080  C C   . THR A 549 ? 1.9334 1.8053 1.4731 -0.7811 -0.1238 0.0537  549 THR A C   
4081  O O   . THR A 549 ? 1.7883 1.7127 1.3480 -0.7823 -0.1521 0.0631  549 THR A O   
4082  C CB  . THR A 549 ? 2.2314 1.9397 1.6156 -0.8631 -0.0817 0.0190  549 THR A CB  
4083  O OG1 . THR A 549 ? 2.3138 1.9423 1.6827 -0.8164 -0.0502 0.0149  549 THR A OG1 
4084  C CG2 . THR A 549 ? 2.2144 1.8829 1.5329 -0.9363 -0.0703 0.0025  549 THR A CG2 
4085  N N   . VAL A 550 ? 2.0083 1.8588 1.5764 -0.7268 -0.1067 0.0563  550 VAL A N   
4086  C CA  . VAL A 550 ? 1.9330 1.8209 1.5595 -0.6676 -0.1200 0.0680  550 VAL A CA  
4087  C C   . VAL A 550 ? 1.9323 1.9380 1.6418 -0.6615 -0.1500 0.0856  550 VAL A C   
4088  O O   . VAL A 550 ? 2.0147 2.0658 1.7637 -0.6367 -0.1730 0.0975  550 VAL A O   
4089  C CB  . VAL A 550 ? 1.6550 1.4935 1.2883 -0.6152 -0.0937 0.0643  550 VAL A CB  
4090  C CG1 . VAL A 550 ? 1.5232 1.4161 1.2284 -0.5590 -0.1084 0.0755  550 VAL A CG1 
4091  C CG2 . VAL A 550 ? 1.6174 1.3467 1.1767 -0.6100 -0.0674 0.0501  550 VAL A CG2 
4092  N N   . SER A 551 ? 1.9224 1.9770 1.6580 -0.6841 -0.1487 0.0878  551 SER A N   
4093  C CA  . SER A 551 ? 1.8223 1.9925 1.6384 -0.6785 -0.1744 0.1038  551 SER A CA  
4094  C C   . SER A 551 ? 1.8629 2.0956 1.6870 -0.7092 -0.2081 0.1143  551 SER A C   
4095  O O   . SER A 551 ? 1.8525 2.1677 1.7434 -0.6834 -0.2334 0.1314  551 SER A O   
4096  C CB  . SER A 551 ? 1.8160 2.0220 1.6479 -0.7059 -0.1631 0.1021  551 SER A CB  
4097  O OG  . SER A 551 ? 1.9990 2.1428 1.8139 -0.6820 -0.1312 0.0938  551 SER A OG  
4098  N N   . LYS A 552 ? 2.1010 2.2943 1.8559 -0.7637 -0.2082 0.1042  552 LYS A N   
4099  C CA  . LYS A 552 ? 2.0175 2.2696 1.7707 -0.7979 -0.2406 0.1134  552 LYS A CA  
4100  C C   . LYS A 552 ? 1.9756 2.2175 1.7310 -0.7628 -0.2563 0.1233  552 LYS A C   
4101  O O   . LYS A 552 ? 2.0632 2.3868 1.8661 -0.7539 -0.2877 0.1432  552 LYS A O   
4102  C CB  . LYS A 552 ? 2.1880 2.3918 1.8581 -0.8682 -0.2336 0.0959  552 LYS A CB  
4103  C CG  . LYS A 552 ? 2.2444 2.4836 1.9163 -0.9188 -0.2276 0.0897  552 LYS A CG  
4104  C CD  . LYS A 552 ? 2.3745 2.5647 1.9619 -0.9915 -0.2224 0.0709  552 LYS A CD  
4105  C CE  . LYS A 552 ? 2.5169 2.7251 2.0972 -1.0458 -0.2107 0.0618  552 LYS A CE  
4106  N NZ  . LYS A 552 ? 2.4121 2.5482 1.9000 -1.1157 -0.1983 0.0388  552 LYS A NZ  
4107  N N   . ILE A 553 ? 1.7050 1.8484 1.4094 -0.7429 -0.2343 0.1110  553 ILE A N   
4108  C CA  . ILE A 553 ? 1.7123 1.8395 1.4134 -0.7129 -0.2455 0.1191  553 ILE A CA  
4109  C C   . ILE A 553 ? 1.7124 1.8863 1.4945 -0.6503 -0.2548 0.1359  553 ILE A C   
4110  O O   . ILE A 553 ? 1.8348 2.0532 1.6475 -0.6337 -0.2796 0.1538  553 ILE A O   
4111  C CB  . ILE A 553 ? 1.6379 1.6495 1.2611 -0.7119 -0.2168 0.0994  553 ILE A CB  
4112  C CG1 . ILE A 553 ? 1.6935 1.6595 1.2332 -0.7773 -0.2099 0.0822  553 ILE A CG1 
4113  C CG2 . ILE A 553 ? 1.7337 1.7296 1.3581 -0.6776 -0.2249 0.1077  553 ILE A CG2 
4114  C CD1 . ILE A 553 ? 1.7461 1.5957 1.2126 -0.7816 -0.1716 0.0587  553 ILE A CD1 
4115  N N   . SER A 554 ? 1.6487 1.8125 1.4641 -0.6167 -0.2350 0.1305  554 SER A N   
4116  C CA  . SER A 554 ? 1.6682 1.8721 1.5578 -0.5591 -0.2410 0.1423  554 SER A CA  
4117  C C   . SER A 554 ? 1.7532 2.0671 1.7188 -0.5545 -0.2684 0.1621  554 SER A C   
4118  O O   . SER A 554 ? 1.7494 2.0989 1.7767 -0.5081 -0.2765 0.1735  554 SER A O   
4119  C CB  . SER A 554 ? 1.7022 1.8670 1.6010 -0.5276 -0.2120 0.1295  554 SER A CB  
4120  O OG  . SER A 554 ? 1.6716 1.8722 1.5872 -0.5474 -0.2050 0.1269  554 SER A OG  
4121  N N   . GLN A 555 ? 1.6608 2.0292 1.6231 -0.6020 -0.2817 0.1656  555 GLN A N   
4122  C CA  . GLN A 555 ? 1.5135 1.9946 1.5477 -0.6009 -0.3079 0.1849  555 GLN A CA  
4123  C C   . GLN A 555 ? 1.5948 2.1172 1.6940 -0.5684 -0.2955 0.1841  555 GLN A C   
4124  O O   . GLN A 555 ? 1.6434 2.2381 1.8160 -0.5331 -0.3110 0.2001  555 GLN A O   
4125  C CB  . GLN A 555 ? 1.6004 2.1247 1.6707 -0.5732 -0.3372 0.2082  555 GLN A CB  
4126  C CG  . GLN A 555 ? 1.6767 2.1765 1.6853 -0.6087 -0.3531 0.2121  555 GLN A CG  
4127  C CD  . GLN A 555 ? 1.8375 2.3901 1.8846 -0.5835 -0.3839 0.2398  555 GLN A CD  
4128  O OE1 . GLN A 555 ? 2.0345 2.6051 2.1414 -0.5306 -0.3865 0.2521  555 GLN A OE1 
4129  N NE2 . GLN A 555 ? 1.5820 2.1583 1.5934 -0.6209 -0.4075 0.2504  555 GLN A NE2 
4130  N N   . GLY A 556 ? 1.7140 2.1889 1.7840 -0.5803 -0.2666 0.1660  556 GLY A N   
4131  C CA  . GLY A 556 ? 1.6378 2.1465 1.7587 -0.5548 -0.2515 0.1633  556 GLY A CA  
4132  C C   . GLY A 556 ? 1.6588 2.1293 1.8033 -0.4948 -0.2358 0.1584  556 GLY A C   
4133  O O   . GLY A 556 ? 1.6987 2.1921 1.8801 -0.4722 -0.2213 0.1542  556 GLY A O   
4134  N N   . ALA A 557 ? 1.5361 1.9510 1.6592 -0.4701 -0.2381 0.1582  557 ALA A N   
4135  C CA  . ALA A 557 ? 1.5767 1.9564 1.7208 -0.4163 -0.2243 0.1521  557 ALA A CA  
4136  C C   . ALA A 557 ? 1.7330 2.0372 1.8293 -0.4150 -0.1923 0.1333  557 ALA A C   
4137  O O   . ALA A 557 ? 1.7259 2.0356 1.8520 -0.3822 -0.1777 0.1273  557 ALA A O   
4138  C CB  . ALA A 557 ? 1.6564 2.0023 1.7910 -0.3956 -0.2359 0.1580  557 ALA A CB  
4139  N N   . VAL A 558 ? 1.7249 1.9591 1.7461 -0.4496 -0.1809 0.1244  558 VAL A N   
4140  C CA  . VAL A 558 ? 1.8208 1.9775 1.7911 -0.4482 -0.1502 0.1092  558 VAL A CA  
4141  C C   . VAL A 558 ? 1.8150 1.9673 1.7500 -0.4981 -0.1393 0.1051  558 VAL A C   
4142  O O   . VAL A 558 ? 1.7377 1.8733 1.6288 -0.5435 -0.1457 0.1040  558 VAL A O   
4143  C CB  . VAL A 558 ? 1.6550 1.7246 1.5650 -0.4437 -0.1406 0.1009  558 VAL A CB  
4144  C CG1 . VAL A 558 ? 1.6352 1.6290 1.5002 -0.4317 -0.1089 0.0877  558 VAL A CG1 
4145  C CG2 . VAL A 558 ? 1.6383 1.7181 1.5831 -0.4032 -0.1540 0.1065  558 VAL A CG2 
4146  N N   . THR A 559 ? 1.7574 1.9246 1.7096 -0.4919 -0.1224 0.1025  559 THR A N   
4147  C CA  . THR A 559 ? 1.7043 1.8679 1.6260 -0.5398 -0.1095 0.0994  559 THR A CA  
4148  C C   . THR A 559 ? 1.8883 1.9565 1.7463 -0.5395 -0.0759 0.0887  559 THR A C   
4149  O O   . THR A 559 ? 1.9315 1.9379 1.7240 -0.5811 -0.0638 0.0821  559 THR A O   
4150  C CB  . THR A 559 ? 1.7197 1.9810 1.7093 -0.5397 -0.1160 0.1073  559 THR A CB  
4151  O OG1 . THR A 559 ? 1.9824 2.2532 2.0101 -0.4880 -0.1042 0.1060  559 THR A OG1 
4152  C CG2 . THR A 559 ? 1.4903 1.8466 1.5389 -0.5446 -0.1490 0.1200  559 THR A CG2 
4153  N N   . SER A 560 ? 1.8933 1.9486 1.7685 -0.4927 -0.0605 0.0871  560 SER A N   
4154  C CA  . SER A 560 ? 1.8507 1.8207 1.6693 -0.4851 -0.0296 0.0804  560 SER A CA  
4155  C C   . SER A 560 ? 1.8100 1.7119 1.5979 -0.4509 -0.0243 0.0746  560 SER A C   
4156  O O   . SER A 560 ? 1.7383 1.6723 1.5681 -0.4158 -0.0399 0.0758  560 SER A O   
4157  C CB  . SER A 560 ? 1.8007 1.8023 1.6531 -0.4556 -0.0159 0.0830  560 SER A CB  
4158  O OG  . SER A 560 ? 1.8203 1.7424 1.6153 -0.4512 0.0135  0.0802  560 SER A OG  
4159  N N   . VAL A 561 ? 1.9238 1.7313 1.6391 -0.4611 -0.0013 0.0683  561 VAL A N   
4160  C CA  . VAL A 561 ? 1.9652 1.7096 1.6502 -0.4292 0.0060  0.0624  561 VAL A CA  
4161  C C   . VAL A 561 ? 2.0483 1.6966 1.6652 -0.4245 0.0384  0.0582  561 VAL A C   
4162  O O   . VAL A 561 ? 1.9649 1.5748 1.5395 -0.4605 0.0546  0.0581  561 VAL A O   
4163  C CB  . VAL A 561 ? 1.9229 1.6576 1.5908 -0.4507 -0.0110 0.0591  561 VAL A CB  
4164  C CG1 . VAL A 561 ? 1.8906 1.5558 1.4837 -0.5013 0.0022  0.0519  561 VAL A CG1 
4165  C CG2 . VAL A 561 ? 2.0984 1.8066 1.7670 -0.4086 -0.0114 0.0556  561 VAL A CG2 
4166  N N   . THR A 562 ? 2.1238 1.7347 1.7316 -0.3792 0.0479  0.0554  562 THR A N   
4167  C CA  . THR A 562 ? 2.0668 1.5897 1.6156 -0.3621 0.0774  0.0534  562 THR A CA  
4168  C C   . THR A 562 ? 2.1795 1.6513 1.6971 -0.3490 0.0799  0.0456  562 THR A C   
4169  O O   . THR A 562 ? 2.2528 1.7668 1.8098 -0.3286 0.0614  0.0439  562 THR A O   
4170  C CB  . THR A 562 ? 2.0906 1.6327 1.6660 -0.3132 0.0864  0.0590  562 THR A CB  
4171  O OG1 . THR A 562 ? 2.1421 1.7405 1.7732 -0.2755 0.0677  0.0566  562 THR A OG1 
4172  C CG2 . THR A 562 ? 2.0806 1.6662 1.6786 -0.3260 0.0890  0.0666  562 THR A CG2 
4173  N N   . LEU A 563 ? 2.0795 1.4588 1.5260 -0.3607 0.1044  0.0406  563 LEU A N   
4174  C CA  . LEU A 563 ? 2.0208 1.3465 1.4317 -0.3501 0.1112  0.0318  563 LEU A CA  
4175  C C   . LEU A 563 ? 2.1164 1.4159 1.5262 -0.2922 0.1268  0.0330  563 LEU A C   
4176  O O   . LEU A 563 ? 2.1946 1.4939 1.6104 -0.2707 0.1228  0.0276  563 LEU A O   
4177  C CB  . LEU A 563 ? 1.9634 1.1991 1.2951 -0.3936 0.1315  0.0234  563 LEU A CB  
4178  C CG  . LEU A 563 ? 1.9117 1.1341 1.2170 -0.4286 0.1213  0.0122  563 LEU A CG  
4179  C CD1 . LEU A 563 ? 1.9876 1.3040 1.3468 -0.4554 0.0859  0.0161  563 LEU A CD1 
4180  C CD2 . LEU A 563 ? 2.0386 1.1722 1.2647 -0.4749 0.1435  0.0018  563 LEU A CD2 
4181  N N   . TYR A 564 ? 2.1300 1.4110 1.5322 -0.2676 0.1442  0.0410  564 TYR A N   
4182  C CA  . TYR A 564 ? 2.1084 1.3706 1.5092 -0.2119 0.1583  0.0440  564 TYR A CA  
4183  C C   . TYR A 564 ? 2.0672 1.4027 1.5252 -0.1775 0.1479  0.0522  564 TYR A C   
4184  O O   . TYR A 564 ? 2.1223 1.4370 1.5653 -0.1482 0.1645  0.0605  564 TYR A O   
4185  C CB  . TYR A 564 ? 2.1354 1.2967 1.4642 -0.2061 0.1924  0.0474  564 TYR A CB  
4186  C CG  . TYR A 564 ? 2.1690 1.2522 1.4341 -0.2543 0.2062  0.0388  564 TYR A CG  
4187  C CD1 . TYR A 564 ? 2.1038 1.1675 1.3517 -0.2681 0.2024  0.0258  564 TYR A CD1 
4188  C CD2 . TYR A 564 ? 2.3607 1.3882 1.5799 -0.2880 0.2242  0.0428  564 TYR A CD2 
4189  C CE1 . TYR A 564 ? 2.2136 1.2059 1.3995 -0.3145 0.2153  0.0152  564 TYR A CE1 
4190  C CE2 . TYR A 564 ? 2.3406 1.2943 1.4989 -0.3360 0.2376  0.0321  564 TYR A CE2 
4191  C CZ  . TYR A 564 ? 2.2958 1.2327 1.4371 -0.3490 0.2327  0.0175  564 TYR A CZ  
4192  O OH  . TYR A 564 ? 2.5719 1.4354 1.6491 -0.3981 0.2463  0.0045  564 TYR A OH  
4193  N N   . SER A 565 ? 2.0143 1.4341 1.5359 -0.1799 0.1210  0.0499  565 SER A N   
4194  C CA  . SER A 565 ? 1.9491 1.4401 1.5259 -0.1495 0.1108  0.0540  565 SER A CA  
4195  C C   . SER A 565 ? 1.8612 1.4257 1.5018 -0.1424 0.0839  0.0476  565 SER A C   
4196  O O   . SER A 565 ? 1.9311 1.5150 1.5849 -0.1748 0.0681  0.0457  565 SER A O   
4197  C CB  . SER A 565 ? 1.9830 1.4963 1.5653 -0.1729 0.1127  0.0615  565 SER A CB  
4198  O OG  . SER A 565 ? 1.7936 1.3853 1.4345 -0.1497 0.0999  0.0625  565 SER A OG  
4199  N N   . ILE A 566 ? 1.6987 1.3035 1.3776 -0.1008 0.0787  0.0449  566 ILE A N   
4200  C CA  . ILE A 566 ? 1.6243 1.2920 1.3627 -0.0916 0.0557  0.0384  566 ILE A CA  
4201  C C   . ILE A 566 ? 1.6398 1.3800 1.4342 -0.0859 0.0425  0.0387  566 ILE A C   
4202  O O   . ILE A 566 ? 1.6451 1.4342 1.4887 -0.0850 0.0234  0.0346  566 ILE A O   
4203  C CB  . ILE A 566 ? 1.3960 1.0626 1.1430 -0.0547 0.0575  0.0317  566 ILE A CB  
4204  C CG1 . ILE A 566 ? 1.4386 1.1308 1.2004 -0.0145 0.0645  0.0313  566 ILE A CG1 
4205  C CG2 . ILE A 566 ? 1.7580 1.3536 1.4493 -0.0585 0.0735  0.0310  566 ILE A CG2 
4206  C CD1 . ILE A 566 ? 1.5801 1.2933 1.3650 0.0193  0.0615  0.0231  566 ILE A CD1 
4207  N N   . LEU A 567 ? 1.4807 1.2266 1.2669 -0.0813 0.0538  0.0439  567 LEU A N   
4208  C CA  . LEU A 567 ? 1.4999 1.3148 1.3366 -0.0750 0.0444  0.0428  567 LEU A CA  
4209  C C   . LEU A 567 ? 1.5835 1.4157 1.4240 -0.1136 0.0417  0.0493  567 LEU A C   
4210  O O   . LEU A 567 ? 1.6523 1.5426 1.5434 -0.1217 0.0246  0.0474  567 LEU A O   
4211  C CB  . LEU A 567 ? 1.4095 1.2328 1.2401 -0.0422 0.0578  0.0436  567 LEU A CB  
4212  C CG  . LEU A 567 ? 1.3049 1.1329 1.1433 -0.0018 0.0577  0.0361  567 LEU A CG  
4213  C CD1 . LEU A 567 ? 1.4887 1.3123 1.3033 0.0261  0.0731  0.0412  567 LEU A CD1 
4214  C CD2 . LEU A 567 ? 1.2524 1.1448 1.1545 0.0122  0.0388  0.0235  567 LEU A CD2 
4215  N N   . GLN A 568 ? 1.6275 1.4107 1.4162 -0.1373 0.0590  0.0572  568 GLN A N   
4216  C CA  . GLN A 568 ? 1.6345 1.4356 1.4247 -0.1782 0.0579  0.0629  568 GLN A CA  
4217  C C   . GLN A 568 ? 1.6365 1.4286 1.4220 -0.2152 0.0442  0.0619  568 GLN A C   
4218  O O   . GLN A 568 ? 1.7258 1.4509 1.4598 -0.2286 0.0528  0.0610  568 GLN A O   
4219  C CB  . GLN A 568 ? 1.7567 1.5028 1.4893 -0.1938 0.0831  0.0715  568 GLN A CB  
4220  C CG  . GLN A 568 ? 1.7880 1.5496 1.5178 -0.2422 0.0841  0.0768  568 GLN A CG  
4221  C CD  . GLN A 568 ? 1.9162 1.6239 1.5911 -0.2571 0.1107  0.0860  568 GLN A CD  
4222  O OE1 . GLN A 568 ? 1.9608 1.6485 1.6175 -0.2249 0.1261  0.0911  568 GLN A OE1 
4223  N NE2 . GLN A 568 ? 1.7820 1.4651 1.4280 -0.3076 0.1168  0.0889  568 GLN A NE2 
4224  N N   . ASP A 569 ? 1.7727 1.6332 1.6108 -0.2305 0.0233  0.0624  569 ASP A N   
4225  C CA  . ASP A 569 ? 1.8290 1.6971 1.6693 -0.2657 0.0059  0.0637  569 ASP A CA  
4226  C C   . ASP A 569 ? 1.8192 1.6218 1.6147 -0.2675 0.0076  0.0595  569 ASP A C   
4227  O O   . ASP A 569 ? 1.9261 1.6733 1.6665 -0.3007 0.0172  0.0593  569 ASP A O   
4228  C CB  . ASP A 569 ? 1.8719 1.7414 1.6905 -0.3153 0.0102  0.0690  569 ASP A CB  
4229  C CG  . ASP A 569 ? 1.7462 1.6836 1.6081 -0.3173 0.0105  0.0734  569 ASP A CG  
4230  O OD1 . ASP A 569 ? 1.6307 1.6437 1.5577 -0.3026 -0.0078 0.0741  569 ASP A OD1 
4231  O OD2 . ASP A 569 ? 1.7225 1.6359 1.5525 -0.3336 0.0304  0.0766  569 ASP A OD2 
4232  N N   . PRO A 570 ? 1.6480 1.4531 1.4634 -0.2330 0.0010  0.0550  570 PRO A N   
4233  C CA  . PRO A 570 ? 1.7279 1.4730 1.5004 -0.2334 0.0056  0.0507  570 PRO A CA  
4234  C C   . PRO A 570 ? 1.8062 1.5511 1.5690 -0.2694 -0.0104 0.0522  570 PRO A C   
4235  O O   . PRO A 570 ? 1.5724 1.3744 1.3729 -0.2884 -0.0303 0.0579  570 PRO A O   
4236  C CB  . PRO A 570 ? 1.6548 1.4195 1.4627 -0.1885 0.0010  0.0458  570 PRO A CB  
4237  C CG  . PRO A 570 ? 1.5411 1.3827 1.4170 -0.1782 -0.0168 0.0476  570 PRO A CG  
4238  C CD  . PRO A 570 ? 1.6301 1.4904 1.5056 -0.1935 -0.0091 0.0520  570 PRO A CD  
4239  N N   . MET A 571 ? 1.8490 1.5313 1.5605 -0.2769 -0.0014 0.0472  571 MET A N   
4240  C CA  . MET A 571 ? 1.9122 1.5881 1.6048 -0.3104 -0.0150 0.0475  571 MET A CA  
4241  C C   . MET A 571 ? 1.8805 1.6046 1.6241 -0.2891 -0.0365 0.0509  571 MET A C   
4242  O O   . MET A 571 ? 1.8448 1.5659 1.6061 -0.2512 -0.0314 0.0471  571 MET A O   
4243  C CB  . MET A 571 ? 2.0390 1.6298 1.6592 -0.3206 0.0051  0.0391  571 MET A CB  
4244  C CG  . MET A 571 ? 2.2024 1.7381 1.7617 -0.3608 0.0218  0.0356  571 MET A CG  
4245  S SD  . MET A 571 ? 2.3129 1.8826 1.8659 -0.4249 0.0010  0.0384  571 MET A SD  
4246  C CE  . MET A 571 ? 2.2965 1.8939 1.8630 -0.4269 -0.0234 0.0400  571 MET A CE  
4247  N N   . THR A 572 ? 1.8001 1.5692 1.5673 -0.3134 -0.0604 0.0588  572 THR A N   
4248  C CA  . THR A 572 ? 1.6289 1.4401 1.4433 -0.2947 -0.0809 0.0649  572 THR A CA  
4249  C C   . THR A 572 ? 1.6361 1.4011 1.4183 -0.2862 -0.0748 0.0601  572 THR A C   
4250  O O   . THR A 572 ? 1.7706 1.4778 1.4910 -0.3064 -0.0606 0.0535  572 THR A O   
4251  C CB  . THR A 572 ? 1.4687 1.3360 1.3095 -0.3233 -0.1075 0.0776  572 THR A CB  
4252  O OG1 . THR A 572 ? 1.7392 1.5762 1.5226 -0.3692 -0.1071 0.0766  572 THR A OG1 
4253  C CG2 . THR A 572 ? 1.5987 1.5307 1.4927 -0.3203 -0.1160 0.0836  572 THR A CG2 
4254  N N   . SER A 573 ? 1.5596 1.3489 1.3835 -0.2569 -0.0838 0.0624  573 SER A N   
4255  C CA  . SER A 573 ? 1.6156 1.3707 1.4174 -0.2478 -0.0784 0.0587  573 SER A CA  
4256  C C   . SER A 573 ? 1.5416 1.3257 1.3619 -0.2610 -0.1019 0.0712  573 SER A C   
4257  O O   . SER A 573 ? 1.4371 1.2745 1.3057 -0.2603 -0.1221 0.0825  573 SER A O   
4258  C CB  . SER A 573 ? 1.6479 1.4033 1.4779 -0.2051 -0.0670 0.0506  573 SER A CB  
4259  O OG  . SER A 573 ? 1.5673 1.3005 1.3804 -0.1908 -0.0470 0.0422  573 SER A OG  
4260  N N   . CYS A 574 ? 1.6190 1.3685 1.4003 -0.2722 -0.0986 0.0704  574 CYS A N   
4261  C CA  . CYS A 574 ? 1.6147 1.3860 1.4039 -0.2867 -0.1197 0.0845  574 CYS A CA  
4262  C C   . CYS A 574 ? 1.6774 1.4526 1.4971 -0.2589 -0.1206 0.0870  574 CYS A C   
4263  O O   . CYS A 574 ? 1.6097 1.4255 1.4873 -0.2395 -0.1346 0.0955  574 CYS A O   
4264  C CB  . CYS A 574 ? 1.5803 1.3161 1.3014 -0.3262 -0.1180 0.0837  574 CYS A CB  
4265  S SG  . CYS A 574 ? 1.9996 1.6551 1.6495 -0.3264 -0.0827 0.0624  574 CYS A SG  
4266  N N   . GLY A 575 ? 1.6287 1.3620 1.4098 -0.2582 -0.1047 0.0791  575 GLY A N   
4267  C CA  . GLY A 575 ? 1.5344 1.2705 1.3408 -0.2368 -0.1033 0.0805  575 GLY A CA  
4268  C C   . GLY A 575 ? 1.6044 1.2964 1.3626 -0.2405 -0.0837 0.0715  575 GLY A C   
4269  O O   . GLY A 575 ? 1.5741 1.2682 1.3500 -0.2261 -0.0803 0.0719  575 GLY A O   
4270  N N   . CYS A 576 ? 1.5386 1.1896 1.2354 -0.2605 -0.0690 0.0624  576 CYS A N   
4271  C CA  . CYS A 576 ? 1.3657 0.9714 1.0110 -0.2643 -0.0470 0.0519  576 CYS A CA  
4272  C C   . CYS A 576 ? 1.4752 1.0502 1.1077 -0.2382 -0.0192 0.0346  576 CYS A C   
4273  O O   . CYS A 576 ? 1.6234 1.1579 1.2106 -0.2389 0.0025  0.0243  576 CYS A O   
4274  C CB  . CYS A 576 ? 1.7481 1.3243 1.3285 -0.3050 -0.0481 0.0525  576 CYS A CB  
4275  S SG  . CYS A 576 ? 1.6918 1.2549 1.2450 -0.3288 -0.0490 0.0475  576 CYS A SG  
4276  N N   . PHE A 577 ? 1.5515 1.1484 1.2246 -0.2138 -0.0200 0.0323  577 PHE A N   
4277  C CA  . PHE A 577 ? 1.4366 1.0098 1.1001 -0.1856 0.0043  0.0192  577 PHE A CA  
4278  C C   . PHE A 577 ? 1.5319 1.1080 1.2085 -0.1595 0.0179  0.0124  577 PHE A C   
4279  O O   . PHE A 577 ? 1.4634 1.0789 1.1887 -0.1496 0.0051  0.0169  577 PHE A O   
4280  C CB  . PHE A 577 ? 1.4560 1.0591 1.1611 -0.1664 -0.0018 0.0200  577 PHE A CB  
4281  C CG  . PHE A 577 ? 1.3934 1.0534 1.1626 -0.1611 -0.0262 0.0290  577 PHE A CG  
4282  C CD1 . PHE A 577 ? 1.4195 1.1092 1.2348 -0.1379 -0.0298 0.0275  577 PHE A CD1 
4283  C CD2 . PHE A 577 ? 1.4463 1.1304 1.2311 -0.1787 -0.0439 0.0382  577 PHE A CD2 
4284  C CE1 . PHE A 577 ? 1.5221 1.2564 1.3940 -0.1318 -0.0497 0.0343  577 PHE A CE1 
4285  C CE2 . PHE A 577 ? 1.3077 1.0422 1.1523 -0.1698 -0.0641 0.0462  577 PHE A CE2 
4286  C CZ  . PHE A 577 ? 1.4736 1.2296 1.3607 -0.1457 -0.0663 0.0439  577 PHE A CZ  
4287  N N   . GLU A 578 ? 1.6096 1.1458 1.2456 -0.1485 0.0438  0.0017  578 GLU A N   
4288  C CA  . GLU A 578 ? 1.6341 1.1813 1.2865 -0.1221 0.0579  -0.0052 578 GLU A CA  
4289  C C   . GLU A 578 ? 1.6608 1.2388 1.3567 -0.0844 0.0612  -0.0097 578 GLU A C   
4290  O O   . GLU A 578 ? 1.7742 1.3893 1.5114 -0.0659 0.0600  -0.0127 578 GLU A O   
4291  C CB  . GLU A 578 ? 1.6919 1.1883 1.2849 -0.1240 0.0849  -0.0144 578 GLU A CB  
4292  C CG  . GLU A 578 ? 1.7554 1.2642 1.3645 -0.0896 0.1045  -0.0228 578 GLU A CG  
4293  C CD  . GLU A 578 ? 2.0632 1.6117 1.7083 -0.0896 0.0985  -0.0214 578 GLU A CD  
4294  O OE1 . GLU A 578 ? 2.1857 1.7188 1.8029 -0.1148 0.0996  -0.0191 578 GLU A OE1 
4295  O OE2 . GLU A 578 ? 2.0556 1.6499 1.7545 -0.0660 0.0935  -0.0230 578 GLU A OE2 
4296  N N   . CYS A 579 ? 1.5828 1.1473 1.2685 -0.0757 0.0652  -0.0100 579 CYS A N   
4297  C CA  . CYS A 579 ? 1.4642 1.0593 1.1863 -0.0412 0.0673  -0.0130 579 CYS A CA  
4298  C C   . CYS A 579 ? 1.4698 1.0901 1.2199 -0.0467 0.0492  -0.0071 579 CYS A C   
4299  O O   . CYS A 579 ? 1.5102 1.1111 1.2379 -0.0741 0.0421  -0.0012 579 CYS A O   
4300  C CB  . CYS A 579 ? 1.4518 1.0090 1.1356 -0.0169 0.0933  -0.0178 579 CYS A CB  
4301  S SG  . CYS A 579 ? 1.8975 1.4266 1.5489 -0.0059 0.1186  -0.0259 579 CYS A SG  
4302  N N   . ILE A 580 ? 1.3135 0.9803 1.1126 -0.0217 0.0422  -0.0097 580 ILE A N   
4303  C CA  . ILE A 580 ? 1.2819 0.9774 1.1109 -0.0224 0.0277  -0.0060 580 ILE A CA  
4304  C C   . ILE A 580 ? 1.3060 1.0113 1.1383 0.0093  0.0390  -0.0099 580 ILE A C   
4305  O O   . ILE A 580 ? 1.2953 1.0109 1.1333 0.0358  0.0496  -0.0161 580 ILE A O   
4306  C CB  . ILE A 580 ? 1.1752 0.9202 1.0624 -0.0256 0.0061  -0.0055 580 ILE A CB  
4307  C CG1 . ILE A 580 ? 1.3728 1.1072 1.2532 -0.0574 -0.0069 0.0034  580 ILE A CG1 
4308  C CG2 . ILE A 580 ? 1.1730 0.9518 1.0940 -0.0191 -0.0050 -0.0045 580 ILE A CG2 
4309  C CD1 . ILE A 580 ? 1.2871 1.0560 1.2161 -0.0572 -0.0224 0.0048  580 ILE A CD1 
4310  N N   . THR A 581 ? 1.3187 1.0232 1.1464 0.0062  0.0370  -0.0052 581 THR A N   
4311  C CA  . THR A 581 ? 1.3633 1.0763 1.1898 0.0342  0.0469  -0.0059 581 THR A CA  
4312  C C   . THR A 581 ? 1.3627 1.1245 1.2326 0.0359  0.0318  -0.0061 581 THR A C   
4313  O O   . THR A 581 ? 1.3108 1.0695 1.1783 0.0132  0.0247  0.0000  581 THR A O   
4314  C CB  . THR A 581 ? 1.3356 0.9879 1.1017 0.0291  0.0659  0.0008  581 THR A CB  
4315  O OG1 . THR A 581 ? 1.4242 1.0351 1.1540 0.0382  0.0836  -0.0017 581 THR A OG1 
4316  C CG2 . THR A 581 ? 1.4472 1.1056 1.2089 0.0522  0.0741  0.0048  581 THR A CG2 
4317  N N   . GLY A 582 ? 1.5025 1.3110 1.4113 0.0621  0.0277  -0.0142 582 GLY A N   
4318  C CA  . GLY A 582 ? 1.4975 1.3542 1.4482 0.0675  0.0156  -0.0180 582 GLY A CA  
4319  C C   . GLY A 582 ? 1.4830 1.3572 1.4284 0.0942  0.0244  -0.0193 582 GLY A C   
4320  O O   . GLY A 582 ? 1.4582 1.3314 1.3902 0.1186  0.0347  -0.0213 582 GLY A O   
4321  N N   . ILE A 583 ? 1.3328 1.2273 1.2892 0.0908  0.0204  -0.0171 583 ILE A N   
4322  C CA  . ILE A 583 ? 1.3565 1.2695 1.3049 0.1141  0.0284  -0.0166 583 ILE A CA  
4323  C C   . ILE A 583 ? 1.2984 1.2679 1.2856 0.1398  0.0219  -0.0311 583 ILE A C   
4324  O O   . ILE A 583 ? 1.2801 1.2844 1.3119 0.1344  0.0088  -0.0428 583 ILE A O   
4325  C CB  . ILE A 583 ? 1.2277 1.1458 1.1736 0.0994  0.0281  -0.0097 583 ILE A CB  
4326  C CG1 . ILE A 583 ? 1.1682 1.0895 1.0885 0.1207  0.0409  -0.0039 583 ILE A CG1 
4327  C CG2 . ILE A 583 ? 1.2599 1.2293 1.2607 0.0923  0.0121  -0.0194 583 ILE A CG2 
4328  C CD1 . ILE A 583 ? 1.2109 1.1192 1.1112 0.1028  0.0473  0.0069  583 ILE A CD1 
4329  N N   . MET A 584 ? 1.2483 1.2259 1.2168 0.1676  0.0314  -0.0300 584 MET A N   
4330  C CA  . MET A 584 ? 1.0970 1.1318 1.0960 0.1915  0.0257  -0.0439 584 MET A CA  
4331  C C   . MET A 584 ? 1.2069 1.2600 1.1876 0.2097  0.0319  -0.0382 584 MET A C   
4332  O O   . MET A 584 ? 1.2966 1.3396 1.2450 0.2325  0.0425  -0.0282 584 MET A O   
4333  C CB  . MET A 584 ? 1.0727 1.1097 1.0672 0.2096  0.0303  -0.0466 584 MET A CB  
4334  C CG  . MET A 584 ? 1.1362 1.2381 1.1641 0.2301  0.0229  -0.0627 584 MET A CG  
4335  S SD  . MET A 584 ? 1.1364 1.2509 1.1694 0.2459  0.0268  -0.0673 584 MET A SD  
4336  C CE  . MET A 584 ? 1.2050 1.4041 1.2783 0.2633  0.0157  -0.0878 584 MET A CE  
4337  N N   . PRO A 585 ? 1.2772 1.3563 1.2763 0.2009  0.0265  -0.0427 585 PRO A N   
4338  C CA  . PRO A 585 ? 1.2485 1.3450 1.2267 0.2161  0.0337  -0.0362 585 PRO A CA  
4339  C C   . PRO A 585 ? 1.2907 1.4338 1.2706 0.2473  0.0328  -0.0431 585 PRO A C   
4340  O O   . PRO A 585 ? 1.3085 1.4481 1.2530 0.2654  0.0423  -0.0293 585 PRO A O   
4341  C CB  . PRO A 585 ? 1.1568 1.2817 1.1650 0.1996  0.0271  -0.0447 585 PRO A CB  
4342  C CG  . PRO A 585 ? 1.1542 1.2593 1.1867 0.1738  0.0190  -0.0473 585 PRO A CG  
4343  C CD  . PRO A 585 ? 1.2957 1.3898 1.3346 0.1783  0.0151  -0.0526 585 PRO A CD  
4344  N N   . GLU A 586 ? 1.3540 1.5413 1.3732 0.2526  0.0215  -0.0635 586 GLU A N   
4345  C CA  . GLU A 586 ? 1.3567 1.5973 1.3803 0.2792  0.0185  -0.0722 586 GLU A CA  
4346  C C   . GLU A 586 ? 1.4065 1.6286 1.3924 0.3044  0.0282  -0.0540 586 GLU A C   
4347  O O   . GLU A 586 ? 1.4672 1.7256 1.4397 0.3303  0.0291  -0.0503 586 GLU A O   
4348  C CB  . GLU A 586 ? 1.3100 1.5962 1.3822 0.2747  0.0055  -0.0987 586 GLU A CB  
4349  C CG  . GLU A 586 ? 1.3896 1.6507 1.4751 0.2645  0.0041  -0.1002 586 GLU A CG  
4350  C CD  . GLU A 586 ? 1.4269 1.6617 1.5389 0.2356  -0.0016 -0.1064 586 GLU A CD  
4351  O OE1 . GLU A 586 ? 1.2752 1.4777 1.3750 0.2220  0.0011  -0.0953 586 GLU A OE1 
4352  O OE2 . GLU A 586 ? 1.5882 1.8360 1.7331 0.2263  -0.0087 -0.1212 586 GLU A OE2 
4353  N N   . ALA A 587 ? 1.3752 1.5417 1.3432 0.2981  0.0361  -0.0424 587 ALA A N   
4354  C CA  . ALA A 587 ? 1.2572 1.3969 1.1889 0.3232  0.0484  -0.0249 587 ALA A CA  
4355  C C   . ALA A 587 ? 1.1595 1.2271 1.0380 0.3206  0.0650  -0.0007 587 ALA A C   
4356  O O   . ALA A 587 ? 1.2867 1.3112 1.1314 0.3363  0.0784  0.0141  587 ALA A O   
4357  C CB  . ALA A 587 ? 1.0578 1.1842 1.0035 0.3190  0.0488  -0.0310 587 ALA A CB  
4358  N N   . ASN A 588 ? 1.2338 1.2879 1.1051 0.3003  0.0654  0.0027  588 ASN A N   
4359  C CA  . ASN A 588 ? 1.3667 1.3547 1.1896 0.2904  0.0809  0.0236  588 ASN A CA  
4360  C C   . ASN A 588 ? 1.3779 1.2944 1.1743 0.2777  0.0916  0.0311  588 ASN A C   
4361  O O   . ASN A 588 ? 1.6241 1.4795 1.3708 0.2826  0.1090  0.0494  588 ASN A O   
4362  C CB  . ASN A 588 ? 1.5176 1.5030 1.3004 0.3211  0.0925  0.0429  588 ASN A CB  
4363  C CG  . ASN A 588 ? 1.4726 1.4006 1.2099 0.3070  0.1078  0.0626  588 ASN A CG  
4364  O OD1 . ASN A 588 ? 1.3544 1.2538 1.0933 0.2719  0.1084  0.0603  588 ASN A OD1 
4365  N ND2 . ASN A 588 ? 1.5800 1.4912 1.2752 0.3334  0.1207  0.0836  588 ASN A ND2 
4366  N N   . GLY A 589 ? 1.4290 1.3506 1.2559 0.2608  0.0823  0.0167  589 GLY A N   
4367  C CA  . GLY A 589 ? 1.4064 1.2657 1.2086 0.2473  0.0917  0.0210  589 GLY A CA  
4368  C C   . GLY A 589 ? 1.3460 1.2022 1.1754 0.2128  0.0803  0.0092  589 GLY A C   
4369  O O   . GLY A 589 ? 1.1344 1.0112 0.9885 0.1902  0.0689  0.0040  589 GLY A O   
4370  N N   . VAL A 590 ? 1.4403 1.2699 1.2631 0.2104  0.0844  0.0063  590 VAL A N   
4371  C CA  . VAL A 590 ? 1.3235 1.1484 1.1682 0.1787  0.0736  -0.0027 590 VAL A CA  
4372  C C   . VAL A 590 ? 1.2125 1.0489 1.0717 0.1896  0.0742  -0.0111 590 VAL A C   
4373  O O   . VAL A 590 ? 1.3986 1.2324 1.2409 0.2192  0.0865  -0.0076 590 VAL A O   
4374  C CB  . VAL A 590 ? 1.2549 1.0139 1.0596 0.1469  0.0810  0.0062  590 VAL A CB  
4375  C CG1 . VAL A 590 ? 1.5310 1.2875 1.3293 0.1293  0.0788  0.0131  590 VAL A CG1 
4376  C CG2 . VAL A 590 ? 1.3944 1.0877 1.1438 0.1569  0.1031  0.0147  590 VAL A CG2 
4377  N N   . VAL A 591 ? 1.2229 1.0728 1.1122 0.1675  0.0620  -0.0204 591 VAL A N   
4378  C CA  . VAL A 591 ? 1.4346 1.2971 1.3401 0.1717  0.0625  -0.0287 591 VAL A CA  
4379  C C   . VAL A 591 ? 1.3719 1.1836 1.2530 0.1423  0.0657  -0.0253 591 VAL A C   
4380  O O   . VAL A 591 ? 1.1962 0.9798 1.0628 0.1159  0.0610  -0.0195 591 VAL A O   
4381  C CB  . VAL A 591 ? 1.1380 1.0652 1.1018 0.1724  0.0460  -0.0435 591 VAL A CB  
4382  C CG1 . VAL A 591 ? 1.2069 1.1867 1.1914 0.1981  0.0421  -0.0491 591 VAL A CG1 
4383  C CG2 . VAL A 591 ? 1.1599 1.0890 1.1498 0.1419  0.0303  -0.0463 591 VAL A CG2 
4384  N N   . MET A 592 ? 1.2992 1.1029 1.1750 0.1459  0.0739  -0.0291 592 MET A N   
4385  C CA  . MET A 592 ? 1.2564 1.0143 1.1054 0.1183  0.0779  -0.0269 592 MET A CA  
4386  C C   . MET A 592 ? 1.3670 1.1533 1.2470 0.1117  0.0723  -0.0350 592 MET A C   
4387  O O   . MET A 592 ? 1.4575 1.2845 1.3637 0.1341  0.0751  -0.0424 592 MET A O   
4388  C CB  . MET A 592 ? 1.3726 1.0708 1.1643 0.1276  0.1017  -0.0215 592 MET A CB  
4389  C CG  . MET A 592 ? 1.3459 0.9846 1.0950 0.0929  0.1057  -0.0181 592 MET A CG  
4390  S SD  . MET A 592 ? 1.8652 1.4225 1.5412 0.1025  0.1362  -0.0138 592 MET A SD  
4391  C CE  . MET A 592 ? 1.4981 1.0435 1.1612 0.1129  0.1375  -0.0039 592 MET A CE  
4392  N N   . VAL A 593 ? 1.3126 1.0797 1.1889 0.0797  0.0642  -0.0328 593 VAL A N   
4393  C CA  . VAL A 593 ? 1.2843 1.0732 1.1871 0.0693  0.0594  -0.0382 593 VAL A CA  
4394  C C   . VAL A 593 ? 1.4169 1.1589 1.2808 0.0407  0.0638  -0.0324 593 VAL A C   
4395  O O   . VAL A 593 ? 1.5479 1.2588 1.3867 0.0187  0.0577  -0.0249 593 VAL A O   
4396  C CB  . VAL A 593 ? 1.2575 1.0904 1.2144 0.0606  0.0381  -0.0416 593 VAL A CB  
4397  C CG1 . VAL A 593 ? 1.4591 1.2767 1.4143 0.0377  0.0232  -0.0328 593 VAL A CG1 
4398  C CG2 . VAL A 593 ? 1.2937 1.1447 1.2764 0.0497  0.0350  -0.0461 593 VAL A CG2 
4399  N N   . ASN A 594 ? 1.4456 1.1866 1.3043 0.0398  0.0744  -0.0364 594 ASN A N   
4400  C CA  . ASN A 594 ? 1.3695 1.0690 1.1886 0.0125  0.0798  -0.0321 594 ASN A CA  
4401  C C   . ASN A 594 ? 1.3629 1.0856 1.2131 -0.0104 0.0635  -0.0289 594 ASN A C   
4402  O O   . ASN A 594 ? 1.4392 1.2062 1.3389 -0.0011 0.0552  -0.0334 594 ASN A O   
4403  C CB  . ASN A 594 ? 1.4228 1.0984 1.2066 0.0258  0.1062  -0.0377 594 ASN A CB  
4404  C CG  . ASN A 594 ? 1.5184 1.2415 1.3386 0.0524  0.1148  -0.0460 594 ASN A CG  
4405  O OD1 . ASN A 594 ? 1.6714 1.4460 1.5436 0.0583  0.1010  -0.0493 594 ASN A OD1 
4406  N ND2 . ASN A 594 ? 1.6297 1.3381 1.4238 0.0688  0.1388  -0.0505 594 ASN A ND2 
4407  N N   . ARG A 595 ? 1.4655 1.1573 1.2851 -0.0410 0.0590  -0.0208 595 ARG A N   
4408  C CA  . ARG A 595 ? 1.3266 1.0342 1.1698 -0.0628 0.0435  -0.0134 595 ARG A CA  
4409  C C   . ARG A 595 ? 1.3593 1.0917 1.2259 -0.0563 0.0531  -0.0196 595 ARG A C   
4410  O O   . ARG A 595 ? 1.2926 1.0473 1.1948 -0.0663 0.0406  -0.0155 595 ARG A O   
4411  C CB  . ARG A 595 ? 1.4507 1.1206 1.2472 -0.0959 0.0391  -0.0027 595 ARG A CB  
4412  C CG  . ARG A 595 ? 1.5229 1.2078 1.3435 -0.1180 0.0163  0.0113  595 ARG A CG  
4413  C CD  . ARG A 595 ? 1.6968 1.3515 1.4689 -0.1505 0.0130  0.0223  595 ARG A CD  
4414  N NE  . ARG A 595 ? 1.7056 1.3358 1.4402 -0.1660 0.0076  0.0255  595 ARG A NE  
4415  C CZ  . ARG A 595 ? 1.8040 1.3948 1.4834 -0.1715 0.0254  0.0169  595 ARG A CZ  
4416  N NH1 . ARG A 595 ? 1.7697 1.3411 1.4248 -0.1588 0.0509  0.0051  595 ARG A NH1 
4417  N NH2 . ARG A 595 ? 1.8971 1.4672 1.5455 -0.1901 0.0190  0.0196  595 ARG A NH2 
4418  N N   . GLU A 596 ? 1.4709 1.1999 1.3189 -0.0392 0.0762  -0.0292 596 GLU A N   
4419  C CA  . GLU A 596 ? 1.5347 1.2928 1.4046 -0.0335 0.0879  -0.0360 596 GLU A CA  
4420  C C   . GLU A 596 ? 1.4883 1.3014 1.4200 -0.0153 0.0801  -0.0443 596 GLU A C   
4421  O O   . GLU A 596 ? 1.3956 1.2368 1.3581 -0.0230 0.0799  -0.0473 596 GLU A O   
4422  C CB  . GLU A 596 ? 1.6656 1.4097 1.5011 -0.0156 0.1159  -0.0442 596 GLU A CB  
4423  C CG  . GLU A 596 ? 1.8329 1.5184 1.6020 -0.0329 0.1279  -0.0405 596 GLU A CG  
4424  C CD  . GLU A 596 ? 2.1017 1.7711 1.8379 -0.0150 0.1585  -0.0498 596 GLU A CD  
4425  O OE1 . GLU A 596 ? 1.9995 1.7029 1.7632 0.0176  0.1698  -0.0573 596 GLU A OE1 
4426  O OE2 . GLU A 596 ? 2.1646 1.7889 1.8470 -0.0330 0.1714  -0.0497 596 GLU A OE2 
4427  N N   . PHE A 597 ? 1.4940 1.3220 1.4413 0.0068  0.0745  -0.0486 597 PHE A N   
4428  C CA  . PHE A 597 ? 1.1890 1.0701 1.1899 0.0243  0.0670  -0.0588 597 PHE A CA  
4429  C C   . PHE A 597 ? 1.1372 1.0320 1.1773 0.0054  0.0469  -0.0568 597 PHE A C   
4430  O O   . PHE A 597 ? 1.3901 1.2626 1.4246 -0.0067 0.0325  -0.0473 597 PHE A O   
4431  C CB  . PHE A 597 ? 1.1725 1.0607 1.1718 0.0505  0.0657  -0.0615 597 PHE A CB  
4432  C CG  . PHE A 597 ? 1.2270 1.1732 1.2684 0.0754  0.0649  -0.0741 597 PHE A CG  
4433  C CD1 . PHE A 597 ? 1.1293 1.1065 1.1766 0.0942  0.0804  -0.0816 597 PHE A CD1 
4434  C CD2 . PHE A 597 ? 1.2999 1.2728 1.3737 0.0805  0.0489  -0.0789 597 PHE A CD2 
4435  C CE1 . PHE A 597 ? 1.1681 1.2056 1.2538 0.1157  0.0777  -0.0931 597 PHE A CE1 
4436  C CE2 . PHE A 597 ? 1.2063 1.2348 1.3150 0.1012  0.0475  -0.0919 597 PHE A CE2 
4437  C CZ  . PHE A 597 ? 1.2862 1.3483 1.4007 0.1181  0.0609  -0.0986 597 PHE A CZ  
4438  N N   . GLY A 598 ? 1.4177 1.3496 1.4979 0.0033  0.0468  -0.0659 598 GLY A N   
4439  C CA  . GLY A 598 ? 1.4209 1.3612 1.5391 -0.0133 0.0309  -0.0655 598 GLY A CA  
4440  C C   . GLY A 598 ? 1.3473 1.3328 1.5135 0.0005  0.0238  -0.0819 598 GLY A C   
4441  O O   . GLY A 598 ? 1.4520 1.4442 1.6520 -0.0123 0.0141  -0.0853 598 GLY A O   
4442  N N   . ALA A 599 ? 1.2225 1.2375 1.3901 0.0267  0.0289  -0.0920 599 ALA A N   
4443  C CA  . ALA A 599 ? 1.0272 1.0901 1.2354 0.0403  0.0221  -0.1089 599 ALA A CA  
4444  C C   . ALA A 599 ? 1.0643 1.1213 1.2691 0.0537  0.0114  -0.1072 599 ALA A C   
4445  O O   . ALA A 599 ? 1.1538 1.1736 1.3240 0.0540  0.0114  -0.0933 599 ALA A O   
4446  C CB  . ALA A 599 ? 1.1168 1.2268 1.3309 0.0612  0.0344  -0.1203 599 ALA A CB  
4447  N N   . THR A 600 ? 1.2195 1.3137 1.4590 0.0623  0.0029  -0.1223 600 THR A N   
4448  C CA  . THR A 600 ? 1.0051 1.0991 1.2432 0.0747  -0.0057 -0.1220 600 THR A CA  
4449  C C   . THR A 600 ? 1.0060 1.1066 1.2131 0.0998  0.0025  -0.1177 600 THR A C   
4450  O O   . THR A 600 ? 1.0822 1.1982 1.2779 0.1124  0.0140  -0.1188 600 THR A O   
4451  C CB  . THR A 600 ? 0.9717 1.1029 1.2526 0.0762  -0.0150 -0.1414 600 THR A CB  
4452  O OG1 . THR A 600 ? 1.2191 1.4009 1.5181 0.0852  -0.0101 -0.1585 600 THR A OG1 
4453  C CG2 . THR A 600 ? 1.0201 1.1305 1.3280 0.0535  -0.0228 -0.1427 600 THR A CG2 
4454  N N   . THR A 601 ? 1.0670 1.1550 1.2605 0.1075  -0.0022 -0.1116 601 THR A N   
4455  C CA  . THR A 601 ? 1.0823 1.1671 1.2426 0.1300  0.0060  -0.1046 601 THR A CA  
4456  C C   . THR A 601 ? 0.9918 1.1169 1.1697 0.1472  -0.0004 -0.1147 601 THR A C   
4457  O O   . THR A 601 ? 1.0476 1.1979 1.2617 0.1396  -0.0105 -0.1284 601 THR A O   
4458  C CB  . THR A 601 ? 1.0697 1.0979 1.1902 0.1189  0.0085  -0.0865 601 THR A CB  
4459  O OG1 . THR A 601 ? 1.0135 1.0376 1.1486 0.1076  -0.0040 -0.0846 601 THR A OG1 
4460  C CG2 . THR A 601 ? 1.1121 1.1027 1.2136 0.0988  0.0136  -0.0781 601 THR A CG2 
4461  N N   . PRO A 602 ? 0.9826 1.1129 1.1341 0.1705  0.0062  -0.1087 602 PRO A N   
4462  C CA  . PRO A 602 ? 0.9280 1.0992 1.0935 0.1857  0.0001  -0.1179 602 PRO A CA  
4463  C C   . PRO A 602 ? 0.9380 1.1013 1.1187 0.1715  -0.0098 -0.1203 602 PRO A C   
4464  O O   . PRO A 602 ? 1.1331 1.3355 1.3391 0.1768  -0.0164 -0.1352 602 PRO A O   
4465  C CB  . PRO A 602 ? 1.0116 1.1728 1.1362 0.2106  0.0108  -0.1037 602 PRO A CB  
4466  C CG  . PRO A 602 ? 1.1283 1.2610 1.2284 0.2146  0.0233  -0.0941 602 PRO A CG  
4467  C CD  . PRO A 602 ? 1.0560 1.1528 1.1619 0.1845  0.0206  -0.0931 602 PRO A CD  
4468  N N   . LEU A 603 ? 0.9928 1.1091 1.1592 0.1532  -0.0106 -0.1067 603 LEU A N   
4469  C CA  . LEU A 603 ? 0.8751 0.9873 1.0590 0.1409  -0.0198 -0.1069 603 LEU A CA  
4470  C C   . LEU A 603 ? 0.8654 0.9887 1.0933 0.1264  -0.0297 -0.1195 603 LEU A C   
4471  O O   . LEU A 603 ? 1.0924 1.2107 1.3388 0.1175  -0.0371 -0.1187 603 LEU A O   
4472  C CB  . LEU A 603 ? 0.9181 0.9826 1.0720 0.1254  -0.0183 -0.0871 603 LEU A CB  
4473  C CG  . LEU A 603 ? 0.9212 0.9616 1.0280 0.1350  -0.0067 -0.0737 603 LEU A CG  
4474  C CD1 . LEU A 603 ? 1.0408 1.0327 1.1184 0.1129  -0.0055 -0.0574 603 LEU A CD1 
4475  C CD2 . LEU A 603 ? 1.1637 1.2315 1.2709 0.1503  -0.0058 -0.0764 603 LEU A CD2 
4476  N N   . GLY A 604 ? 1.0038 1.1418 1.2484 0.1246  -0.0289 -0.1303 604 GLY A N   
4477  C CA  . GLY A 604 ? 0.9947 1.1370 1.2777 0.1099  -0.0359 -0.1420 604 GLY A CA  
4478  C C   . GLY A 604 ? 1.0197 1.1187 1.3011 0.0894  -0.0402 -0.1261 604 GLY A C   
4479  O O   . GLY A 604 ? 1.1298 1.2236 1.4415 0.0791  -0.0473 -0.1304 604 GLY A O   
4480  N N   . MET A 605 ? 1.0489 1.1153 1.2933 0.0835  -0.0356 -0.1075 605 MET A N   
4481  C CA  . MET A 605 ? 1.0265 1.0548 1.2631 0.0628  -0.0406 -0.0908 605 MET A CA  
4482  C C   . MET A 605 ? 1.1513 1.1555 1.3578 0.0537  -0.0321 -0.0822 605 MET A C   
4483  O O   . MET A 605 ? 1.0139 1.0192 1.1930 0.0654  -0.0210 -0.0827 605 MET A O   
4484  C CB  . MET A 605 ? 1.0513 1.0613 1.2680 0.0590  -0.0449 -0.0757 605 MET A CB  
4485  C CG  . MET A 605 ? 0.9562 0.9862 1.2053 0.0636  -0.0538 -0.0804 605 MET A CG  
4486  S SD  . MET A 605 ? 0.9788 0.9933 1.2067 0.0545  -0.0586 -0.0611 605 MET A SD  
4487  C CE  . MET A 605 ? 1.0788 1.1042 1.2762 0.0715  -0.0464 -0.0656 605 MET A CE  
4488  N N   . THR A 606 ? 1.1306 1.1119 1.3406 0.0339  -0.0363 -0.0733 606 THR A N   
4489  C CA  . THR A 606 ? 1.0720 1.0290 1.2513 0.0223  -0.0275 -0.0648 606 THR A CA  
4490  C C   . THR A 606 ? 1.1178 1.0380 1.2550 0.0108  -0.0286 -0.0467 606 THR A C   
4491  O O   . THR A 606 ? 1.1574 1.0752 1.2971 0.0092  -0.0380 -0.0403 606 THR A O   
4492  C CB  . THR A 606 ? 1.0856 1.0372 1.2863 0.0050  -0.0302 -0.0638 606 THR A CB  
4493  O OG1 . THR A 606 ? 1.4421 1.3784 1.6134 -0.0039 -0.0184 -0.0589 606 THR A OG1 
4494  C CG2 . THR A 606 ? 0.9763 0.9048 1.1861 -0.0110 -0.0443 -0.0482 606 THR A CG2 
4495  N N   . PHE A 607 ? 1.2667 1.1598 1.3649 0.0013  -0.0184 -0.0398 607 PHE A N   
4496  C CA  . PHE A 607 ? 1.2169 1.0729 1.2702 -0.0135 -0.0183 -0.0256 607 PHE A CA  
4497  C C   . PHE A 607 ? 1.1487 0.9970 1.2120 -0.0332 -0.0365 -0.0113 607 PHE A C   
4498  O O   . PHE A 607 ? 1.2438 1.0830 1.2910 -0.0393 -0.0424 -0.0035 607 PHE A O   
4499  C CB  . PHE A 607 ? 1.3322 1.1597 1.3441 -0.0236 -0.0041 -0.0226 607 PHE A CB  
4500  C CG  . PHE A 607 ? 1.2846 1.0715 1.2442 -0.0394 -0.0014 -0.0122 607 PHE A CG  
4501  C CD1 . PHE A 607 ? 1.2885 1.0569 1.2147 -0.0277 0.0116  -0.0158 607 PHE A CD1 
4502  C CD2 . PHE A 607 ? 1.3041 1.0713 1.2471 -0.0669 -0.0122 0.0014  607 PHE A CD2 
4503  C CE1 . PHE A 607 ? 1.3983 1.1253 1.2744 -0.0460 0.0152  -0.0085 607 PHE A CE1 
4504  C CE2 . PHE A 607 ? 1.2354 0.9686 1.1293 -0.0852 -0.0107 0.0087  607 PHE A CE2 
4505  C CZ  . PHE A 607 ? 1.3905 1.1020 1.2508 -0.0760 0.0038  0.0024  607 PHE A CZ  
4506  N N   . GLY A 608 ? 1.1611 1.0141 1.2511 -0.0426 -0.0448 -0.0070 608 GLY A N   
4507  C CA  . GLY A 608 ? 1.1652 1.0136 1.2688 -0.0572 -0.0626 0.0092  608 GLY A CA  
4508  C C   . GLY A 608 ? 1.2269 1.0989 1.3655 -0.0453 -0.0739 0.0075  608 GLY A C   
4509  O O   . GLY A 608 ? 1.2429 1.1142 1.3810 -0.0549 -0.0868 0.0218  608 GLY A O   
4510  N N   . GLU A 609 ? 1.2385 1.1360 1.4081 -0.0246 -0.0690 -0.0104 609 GLU A N   
4511  C CA  . GLU A 609 ? 0.9711 0.8936 1.1735 -0.0114 -0.0766 -0.0153 609 GLU A CA  
4512  C C   . GLU A 609 ? 0.9600 0.8828 1.1340 -0.0097 -0.0737 -0.0125 609 GLU A C   
4513  O O   . GLU A 609 ? 1.0665 1.0010 1.2534 -0.0113 -0.0831 -0.0056 609 GLU A O   
4514  C CB  . GLU A 609 ? 1.0336 0.9832 1.2715 0.0077  -0.0711 -0.0374 609 GLU A CB  
4515  C CG  . GLU A 609 ? 1.0488 0.9980 1.3240 0.0045  -0.0758 -0.0411 609 GLU A CG  
4516  C CD  . GLU A 609 ? 1.0835 1.0574 1.3891 0.0172  -0.0694 -0.0658 609 GLU A CD  
4517  O OE1 . GLU A 609 ? 1.1849 1.1779 1.4777 0.0276  -0.0600 -0.0789 609 GLU A OE1 
4518  O OE2 . GLU A 609 ? 0.9076 0.8815 1.2490 0.0166  -0.0736 -0.0720 609 GLU A OE2 
4519  N N   . LEU A 610 ? 0.9736 0.8824 1.1092 -0.0068 -0.0597 -0.0172 610 LEU A N   
4520  C CA  . LEU A 610 ? 0.9828 0.8810 1.0835 -0.0071 -0.0536 -0.0137 610 LEU A CA  
4521  C C   . LEU A 610 ? 1.1676 1.0436 1.2422 -0.0331 -0.0620 0.0035  610 LEU A C   
4522  O O   . LEU A 610 ? 1.2574 1.1399 1.3285 -0.0384 -0.0662 0.0087  610 LEU A O   
4523  C CB  . LEU A 610 ? 1.1664 1.0446 1.2287 0.0015  -0.0356 -0.0198 610 LEU A CB  
4524  C CG  . LEU A 610 ? 1.0255 0.9224 1.0892 0.0277  -0.0250 -0.0313 610 LEU A CG  
4525  C CD1 . LEU A 610 ? 0.9951 0.9177 1.0821 0.0340  -0.0324 -0.0325 610 LEU A CD1 
4526  C CD2 . LEU A 610 ? 0.9970 0.9215 1.0883 0.0447  -0.0211 -0.0455 610 LEU A CD2 
4527  N N   . ALA A 611 ? 1.2476 1.1015 1.3039 -0.0504 -0.0643 0.0118  611 ALA A N   
4528  C CA  . ALA A 611 ? 1.2011 1.0350 1.2261 -0.0779 -0.0727 0.0275  611 ALA A CA  
4529  C C   . ALA A 611 ? 1.2648 1.1270 1.3250 -0.0838 -0.0924 0.0391  611 ALA A C   
4530  O O   . ALA A 611 ? 1.3427 1.2045 1.3843 -0.1019 -0.0992 0.0486  611 ALA A O   
4531  C CB  . ALA A 611 ? 1.2768 1.0886 1.2813 -0.0930 -0.0725 0.0340  611 ALA A CB  
4532  N N   . SER A 612 ? 1.2063 1.0938 1.3181 -0.0688 -0.1007 0.0375  612 SER A N   
4533  C CA  . SER A 612 ? 1.2114 1.1278 1.3630 -0.0679 -0.1177 0.0480  612 SER A CA  
4534  C C   . SER A 612 ? 1.1650 1.1079 1.3310 -0.0580 -0.1156 0.0413  612 SER A C   
4535  O O   . SER A 612 ? 1.0994 1.0711 1.2971 -0.0572 -0.1278 0.0495  612 SER A O   
4536  C CB  . SER A 612 ? 1.0875 1.0148 1.2873 -0.0526 -0.1231 0.0460  612 SER A CB  
4537  O OG  . SER A 612 ? 1.2585 1.2021 1.4869 -0.0296 -0.1137 0.0255  612 SER A OG  
4538  N N   . MET A 613 ? 1.2312 1.1645 1.3719 -0.0505 -0.0998 0.0282  613 MET A N   
4539  C CA  . MET A 613 ? 1.1832 1.1392 1.3324 -0.0416 -0.0954 0.0223  613 MET A CA  
4540  C C   . MET A 613 ? 1.2641 1.1986 1.3638 -0.0628 -0.0896 0.0292  613 MET A C   
4541  O O   . MET A 613 ? 1.3884 1.3408 1.4917 -0.0633 -0.0876 0.0291  613 MET A O   
4542  C CB  . MET A 613 ? 1.1671 1.1326 1.3278 -0.0153 -0.0825 0.0037  613 MET A CB  
4543  C CG  . MET A 613 ? 1.1457 1.1254 1.3481 0.0004  -0.0861 -0.0063 613 MET A CG  
4544  S SD  . MET A 613 ? 1.1607 1.1837 1.4228 0.0171  -0.0940 -0.0131 613 MET A SD  
4545  C CE  . MET A 613 ? 1.2328 1.2750 1.4821 0.0325  -0.0802 -0.0270 613 MET A CE  
4546  N N   . THR A 614 ? 1.2493 1.1452 1.3032 -0.0809 -0.0856 0.0338  614 THR A N   
4547  C CA  . THR A 614 ? 1.3684 1.2341 1.3689 -0.1035 -0.0774 0.0376  614 THR A CA  
4548  C C   . THR A 614 ? 1.5212 1.3865 1.5065 -0.1369 -0.0922 0.0519  614 THR A C   
4549  O O   . THR A 614 ? 1.6261 1.4997 1.6005 -0.1553 -0.0944 0.0564  614 THR A O   
4550  C CB  . THR A 614 ? 1.3385 1.1579 1.2925 -0.0991 -0.0588 0.0297  614 THR A CB  
4551  O OG1 . THR A 614 ? 1.5800 1.3883 1.5308 -0.1060 -0.0640 0.0329  614 THR A OG1 
4552  C CG2 . THR A 614 ? 1.2696 1.0949 1.2357 -0.0664 -0.0450 0.0171  614 THR A CG2 
4553  N N   . GLY A 615 ? 1.4152 1.2741 1.3992 -0.1458 -0.1022 0.0593  615 GLY A N   
4554  C CA  . GLY A 615 ? 1.3666 1.2262 1.3298 -0.1785 -0.1173 0.0738  615 GLY A CA  
4555  C C   . GLY A 615 ? 1.2800 1.1917 1.2891 -0.1830 -0.1392 0.0876  615 GLY A C   
4556  O O   . GLY A 615 ? 1.2449 1.1890 1.2949 -0.1646 -0.1390 0.0838  615 GLY A O   
4557  N N   . GLY A 616 ? 1.2409 1.1628 1.2428 -0.2057 -0.1571 0.1037  616 GLY A N   
4558  C CA  . GLY A 616 ? 1.1912 1.1663 1.2348 -0.2107 -0.1799 0.1205  616 GLY A CA  
4559  C C   . GLY A 616 ? 1.3306 1.3294 1.3610 -0.2380 -0.1848 0.1235  616 GLY A C   
4560  O O   . GLY A 616 ? 1.5470 1.5992 1.6170 -0.2405 -0.2028 0.1368  616 GLY A O   
4561  N N   . GLY A 617 ? 1.4070 1.3668 1.3828 -0.2584 -0.1682 0.1115  617 GLY A N   
4562  C CA  . GLY A 617 ? 1.2790 1.2536 1.2359 -0.2894 -0.1696 0.1121  617 GLY A CA  
4563  C C   . GLY A 617 ? 1.3756 1.3916 1.3781 -0.2737 -0.1664 0.1094  617 GLY A C   
4564  O O   . GLY A 617 ? 1.3130 1.3720 1.3294 -0.2949 -0.1767 0.1166  617 GLY A O   
4565  N N   . VAL A 618 ? 1.4492 1.4574 1.4759 -0.2374 -0.1522 0.0986  618 VAL A N   
4566  C CA  . VAL A 618 ? 1.4141 1.4616 1.4828 -0.2199 -0.1473 0.0946  618 VAL A CA  
4567  C C   . VAL A 618 ? 1.4790 1.4868 1.5120 -0.2151 -0.1219 0.0803  618 VAL A C   
4568  O O   . VAL A 618 ? 1.5740 1.5302 1.5713 -0.2054 -0.1079 0.0716  618 VAL A O   
4569  C CB  . VAL A 618 ? 1.3672 1.4481 1.4997 -0.1802 -0.1537 0.0943  618 VAL A CB  
4570  C CG1 . VAL A 618 ? 1.3695 1.4980 1.5469 -0.1640 -0.1497 0.0902  618 VAL A CG1 
4571  C CG2 . VAL A 618 ? 1.3911 1.4991 1.5541 -0.1808 -0.1770 0.1110  618 VAL A CG2 
4572  N N   . GLN A 619 ? 1.2315 1.2652 1.2746 -0.2209 -0.1155 0.0791  619 GLN A N   
4573  C CA  . GLN A 619 ? 1.2847 1.2826 1.2942 -0.2153 -0.0914 0.0690  619 GLN A CA  
4574  C C   . GLN A 619 ? 1.4002 1.4059 1.4413 -0.1711 -0.0837 0.0596  619 GLN A C   
4575  O O   . GLN A 619 ? 1.2451 1.3013 1.3361 -0.1533 -0.0876 0.0585  619 GLN A O   
4576  C CB  . GLN A 619 ? 1.3290 1.3562 1.3416 -0.2369 -0.0869 0.0722  619 GLN A CB  
4577  C CG  . GLN A 619 ? 1.2703 1.2873 1.2453 -0.2860 -0.0920 0.0786  619 GLN A CG  
4578  C CD  . GLN A 619 ? 1.3331 1.3523 1.2902 -0.3095 -0.0776 0.0781  619 GLN A CD  
4579  O OE1 . GLN A 619 ? 1.3409 1.4237 1.3382 -0.3204 -0.0858 0.0839  619 GLN A OE1 
4580  N NE2 . GLN A 619 ? 1.5561 1.5055 1.4526 -0.3174 -0.0546 0.0719  619 GLN A NE2 
4581  N N   . THR A 620 ? 1.4619 1.4209 1.4746 -0.1542 -0.0728 0.0518  620 THR A N   
4582  C CA  . THR A 620 ? 1.3070 1.2773 1.3494 -0.1145 -0.0673 0.0415  620 THR A CA  
4583  C C   . THR A 620 ? 1.3431 1.2814 1.3488 -0.1009 -0.0451 0.0344  620 THR A C   
4584  O O   . THR A 620 ? 1.4075 1.2955 1.3697 -0.0991 -0.0340 0.0319  620 THR A O   
4585  C CB  . THR A 620 ? 1.2918 1.2475 1.3417 -0.1020 -0.0740 0.0388  620 THR A CB  
4586  O OG1 . THR A 620 ? 1.5362 1.4352 1.5293 -0.1122 -0.0624 0.0375  620 THR A OG1 
4587  C CG2 . THR A 620 ? 1.2392 1.2213 1.3207 -0.1140 -0.0955 0.0492  620 THR A CG2 
4588  N N   . PRO A 621 ? 1.3609 1.3268 1.3815 -0.0898 -0.0376 0.0321  621 PRO A N   
4589  C CA  . PRO A 621 ? 1.3259 1.2643 1.3121 -0.0732 -0.0174 0.0283  621 PRO A CA  
4590  C C   . PRO A 621 ? 1.3548 1.2905 1.3493 -0.0380 -0.0138 0.0179  621 PRO A C   
4591  O O   . PRO A 621 ? 1.3107 1.2856 1.3528 -0.0208 -0.0246 0.0101  621 PRO A O   
4592  C CB  . PRO A 621 ? 1.1244 1.1062 1.1341 -0.0708 -0.0138 0.0290  621 PRO A CB  
4593  C CG  . PRO A 621 ? 1.0633 1.0879 1.1107 -0.0932 -0.0298 0.0347  621 PRO A CG  
4594  C CD  . PRO A 621 ? 1.2463 1.2725 1.3159 -0.0914 -0.0467 0.0342  621 PRO A CD  
4595  N N   . GLY A 622 ? 1.2595 1.1493 1.2078 -0.0280 0.0020  0.0178  622 GLY A N   
4596  C CA  . GLY A 622 ? 1.3420 1.2326 1.2946 0.0045  0.0065  0.0090  622 GLY A CA  
4597  C C   . GLY A 622 ? 1.3385 1.2012 1.2808 0.0033  0.0041  0.0066  622 GLY A C   
4598  O O   . GLY A 622 ? 1.4546 1.2997 1.3791 0.0245  0.0142  0.0026  622 GLY A O   
4599  N N   . PHE A 623 ? 1.3541 1.2162 1.3078 -0.0206 -0.0091 0.0098  623 PHE A N   
4600  C CA  . PHE A 623 ? 1.5113 1.3488 1.4543 -0.0246 -0.0113 0.0084  623 PHE A CA  
4601  C C   . PHE A 623 ? 1.4968 1.2917 1.3972 -0.0587 -0.0107 0.0168  623 PHE A C   
4602  O O   . PHE A 623 ? 1.4913 1.2958 1.3934 -0.0837 -0.0188 0.0238  623 PHE A O   
4603  C CB  . PHE A 623 ? 1.3507 1.2277 1.3475 -0.0194 -0.0285 0.0040  623 PHE A CB  
4604  C CG  . PHE A 623 ? 1.2866 1.2036 1.3242 0.0104  -0.0291 -0.0080 623 PHE A CG  
4605  C CD1 . PHE A 623 ? 1.2830 1.2384 1.3509 0.0186  -0.0326 -0.0111 623 PHE A CD1 
4606  C CD2 . PHE A 623 ? 1.3094 1.2285 1.3554 0.0282  -0.0260 -0.0175 623 PHE A CD2 
4607  C CE1 . PHE A 623 ? 1.2898 1.2812 1.3914 0.0439  -0.0327 -0.0247 623 PHE A CE1 
4608  C CE2 . PHE A 623 ? 1.3818 1.3398 1.4635 0.0519  -0.0272 -0.0307 623 PHE A CE2 
4609  C CZ  . PHE A 623 ? 1.4712 1.4634 1.5789 0.0594  -0.0306 -0.0348 623 PHE A CZ  
4610  N N   . MET A 624 ? 1.5771 1.3281 1.4394 -0.0605 -0.0006 0.0151  624 MET A N   
4611  C CA  . MET A 624 ? 1.6073 1.3140 1.4229 -0.0937 0.0018  0.0200  624 MET A CA  
4612  C C   . MET A 624 ? 1.6218 1.3009 1.4168 -0.0936 0.0062  0.0163  624 MET A C   
4613  O O   . MET A 624 ? 1.5558 1.2376 1.3600 -0.0657 0.0147  0.0098  624 MET A O   
4614  C CB  . MET A 624 ? 1.6259 1.2830 1.3873 -0.1019 0.0215  0.0215  624 MET A CB  
4615  C CG  . MET A 624 ? 1.6530 1.2732 1.3847 -0.0716 0.0438  0.0168  624 MET A CG  
4616  S SD  . MET A 624 ? 1.7041 1.2391 1.3557 -0.0879 0.0699  0.0190  624 MET A SD  
4617  C CE  . MET A 624 ? 1.7212 1.2351 1.3591 -0.0393 0.0917  0.0167  624 MET A CE  
4618  N N   . GLY A 625 ? 1.7708 1.4265 1.5369 -0.1263 0.0010  0.0203  625 GLY A N   
4619  C CA  . GLY A 625 ? 1.6877 1.3151 1.4272 -0.1323 0.0062  0.0174  625 GLY A CA  
4620  C C   . GLY A 625 ? 1.7105 1.2716 1.3797 -0.1491 0.0266  0.0135  625 GLY A C   
4621  O O   . GLY A 625 ? 1.7146 1.2548 1.3546 -0.1761 0.0270  0.0160  625 GLY A O   
4622  N N   . HIS A 626 ? 1.6206 1.1478 1.2619 -0.1337 0.0451  0.0063  626 HIS A N   
4623  C CA  . HIS A 626 ? 1.7073 1.1644 1.2795 -0.1451 0.0687  0.0003  626 HIS A CA  
4624  C C   . HIS A 626 ? 1.9285 1.3626 1.4789 -0.1354 0.0830  -0.0069 626 HIS A C   
4625  O O   . HIS A 626 ? 1.8970 1.3707 1.4880 -0.1160 0.0767  -0.0071 626 HIS A O   
4626  C CB  . HIS A 626 ? 1.6318 1.0598 1.1866 -0.1207 0.0888  -0.0008 626 HIS A CB  
4627  C CG  . HIS A 626 ? 1.5301 0.9897 1.1224 -0.0743 0.0941  -0.0021 626 HIS A CG  
4628  N ND1 . HIS A 626 ? 1.5250 0.9570 1.0959 -0.0462 0.1160  -0.0076 626 HIS A ND1 
4629  C CD2 . HIS A 626 ? 1.5213 1.0406 1.1706 -0.0531 0.0799  0.0007  626 HIS A CD2 
4630  C CE1 . HIS A 626 ? 1.5993 1.0788 1.2153 -0.0103 0.1128  -0.0073 626 HIS A CE1 
4631  N NE2 . HIS A 626 ? 1.6574 1.1881 1.3195 -0.0141 0.0916  -0.0034 626 HIS A NE2 
4632  N N   . GLY A 627 ? 1.9117 1.2813 1.3976 -0.1502 0.1036  -0.0138 627 GLY A N   
4633  C CA  . GLY A 627 ? 1.9270 1.2703 1.3857 -0.1418 0.1213  -0.0220 627 GLY A CA  
4634  C C   . GLY A 627 ? 1.9689 1.3015 1.4310 -0.0954 0.1450  -0.0267 627 GLY A C   
4635  O O   . GLY A 627 ? 2.0002 1.3505 1.4884 -0.0685 0.1451  -0.0225 627 GLY A O   
4636  N N   . ARG A 628 ? 1.9679 1.2731 1.4018 -0.0853 0.1658  -0.0351 628 ARG A N   
4637  C CA  . ARG A 628 ? 1.8367 1.1395 1.2775 -0.0376 0.1886  -0.0386 628 ARG A CA  
4638  C C   . ARG A 628 ? 2.1219 1.3498 1.5056 -0.0266 0.2162  -0.0414 628 ARG A C   
4639  O O   . ARG A 628 ? 2.0516 1.2759 1.4402 0.0167  0.2343  -0.0406 628 ARG A O   
4640  C CB  . ARG A 628 ? 1.7334 1.0466 1.1745 -0.0292 0.2003  -0.0460 628 ARG A CB  
4641  C CG  . ARG A 628 ? 1.8112 1.1823 1.2953 -0.0490 0.1758  -0.0425 628 ARG A CG  
4642  C CD  . ARG A 628 ? 1.7648 1.2002 1.3100 -0.0159 0.1723  -0.0423 628 ARG A CD  
4643  N NE  . ARG A 628 ? 1.6249 1.0526 1.1569 0.0090  0.1990  -0.0505 628 ARG A NE  
4644  C CZ  . ARG A 628 ? 1.7550 1.2073 1.2985 0.0031  0.2023  -0.0543 628 ARG A CZ  
4645  N NH1 . ARG A 628 ? 1.8959 1.3760 1.4608 -0.0272 0.1804  -0.0491 628 ARG A NH1 
4646  N NH2 . ARG A 628 ? 1.8870 1.3363 1.4207 0.0283  0.2285  -0.0620 628 ARG A NH2 
4647  N N   . GLN A 629 ? 2.3637 1.5344 1.6948 -0.0646 0.2194  -0.0441 629 GLN A N   
4648  C CA  . GLN A 629 ? 2.3347 1.4209 1.6039 -0.0593 0.2485  -0.0479 629 GLN A CA  
4649  C C   . GLN A 629 ? 2.1793 1.2646 1.4594 -0.0517 0.2433  -0.0369 629 GLN A C   
4650  O O   . GLN A 629 ? 2.2112 1.2472 1.4630 -0.0229 0.2676  -0.0345 629 GLN A O   
4651  C CB  . GLN A 629 ? 2.3175 1.3422 1.5221 -0.1090 0.2552  -0.0587 629 GLN A CB  
4652  C CG  . GLN A 629 ? 2.3284 1.3737 1.5303 -0.1283 0.2496  -0.0665 629 GLN A CG  
4653  C CD  . GLN A 629 ? 2.4727 1.5768 1.7071 -0.1662 0.2137  -0.0598 629 GLN A CD  
4654  O OE1 . GLN A 629 ? 2.5684 1.7245 1.8530 -0.1651 0.1894  -0.0483 629 GLN A OE1 
4655  N NE2 . GLN A 629 ? 2.4180 1.5145 1.6228 -0.1989 0.2108  -0.0663 629 GLN A NE2 
4656  N N   . PHE A 630 ? 2.0791 1.2168 1.3982 -0.0748 0.2139  -0.0297 630 PHE A N   
4657  C CA  . PHE A 630 ? 2.1340 1.2752 1.4631 -0.0732 0.2086  -0.0196 630 PHE A CA  
4658  C C   . PHE A 630 ? 2.0555 1.2210 1.4147 -0.0186 0.2167  -0.0119 630 PHE A C   
4659  O O   . PHE A 630 ? 1.9325 1.0686 1.2738 -0.0073 0.2274  -0.0038 630 PHE A O   
4660  C CB  . PHE A 630 ? 2.0433 1.2502 1.4190 -0.1027 0.1752  -0.0140 630 PHE A CB  
4661  C CG  . PHE A 630 ? 1.9188 1.1241 1.2953 -0.1141 0.1711  -0.0056 630 PHE A CG  
4662  C CD1 . PHE A 630 ? 2.0136 1.1421 1.3308 -0.1248 0.1945  -0.0057 630 PHE A CD1 
4663  C CD2 . PHE A 630 ? 1.8278 1.1063 1.2632 -0.1144 0.1458  0.0019  630 PHE A CD2 
4664  C CE1 . PHE A 630 ? 2.0300 1.1576 1.3471 -0.1376 0.1923  0.0027  630 PHE A CE1 
4665  C CE2 . PHE A 630 ? 1.6937 0.9742 1.1300 -0.1253 0.1439  0.0093  630 PHE A CE2 
4666  C CZ  . PHE A 630 ? 1.9216 1.1282 1.2991 -0.1379 0.1669  0.0103  630 PHE A CZ  
4667  N N   . ILE A 631 ? 1.9902 1.2096 1.3926 0.0124  0.2115  -0.0137 631 ILE A N   
4668  C CA  . ILE A 631 ? 1.9164 1.1728 1.3522 0.0639  0.2158  -0.0069 631 ILE A CA  
4669  C C   . ILE A 631 ? 2.1127 1.2978 1.4971 0.0905  0.2459  -0.0013 631 ILE A C   
4670  O O   . ILE A 631 ? 2.0611 1.2539 1.4527 0.1098  0.2456  0.0100  631 ILE A O   
4671  C CB  . ILE A 631 ? 1.9899 1.2987 1.4646 0.0899  0.2137  -0.0130 631 ILE A CB  
4672  C CG1 . ILE A 631 ? 2.0338 1.3888 1.5427 0.0574  0.1898  -0.0187 631 ILE A CG1 
4673  C CG2 . ILE A 631 ? 2.0209 1.3893 1.5414 0.1353  0.2095  -0.0070 631 ILE A CG2 
4674  C CD1 . ILE A 631 ? 1.8920 1.2913 1.4336 0.0758  0.1903  -0.0251 631 ILE A CD1 
4675  N N   . ALA A 632 ? 2.2823 1.3986 1.6150 0.0921  0.2721  -0.0085 632 ALA A N   
4676  C CA  . ALA A 632 ? 2.2893 1.3314 1.5724 0.1226  0.3038  -0.0026 632 ALA A CA  
4677  C C   . ALA A 632 ? 2.2530 1.2214 1.4847 0.0931  0.3129  0.0025  632 ALA A C   
4678  O O   . ALA A 632 ? 2.2509 1.1671 1.4508 0.1203  0.3345  0.0129  632 ALA A O   
4679  C CB  . ALA A 632 ? 2.4281 1.4177 1.6722 0.1346  0.3312  -0.0137 632 ALA A CB  
4680  N N   . SER A 633 ? 2.2683 1.2334 1.4919 0.0377  0.2971  -0.0038 633 SER A N   
4681  C CA  . SER A 633 ? 2.2346 1.1370 1.4122 0.0012  0.3042  -0.0009 633 SER A CA  
4682  C C   . SER A 633 ? 2.2933 1.2073 1.4844 0.0228  0.3034  0.0166  633 SER A C   
4683  O O   . SER A 633 ? 2.2803 1.2776 1.5308 0.0436  0.2821  0.0242  633 SER A O   
4684  C CB  . SER A 633 ? 2.1755 1.1064 1.3628 -0.0581 0.2789  -0.0081 633 SER A CB  
4685  O OG  . SER A 633 ? 2.1328 1.0284 1.2918 -0.0953 0.2798  -0.0040 633 SER A OG  
4686  N N   . LYS A 634 ? 2.2790 1.1068 1.4121 0.0156  0.3278  0.0226  634 LYS A N   
4687  C CA  . LYS A 634 ? 2.2419 1.0708 1.3781 0.0326  0.3303  0.0410  634 LYS A CA  
4688  C C   . LYS A 634 ? 2.1770 1.0714 1.3523 -0.0060 0.3016  0.0435  634 LYS A C   
4689  O O   . LYS A 634 ? 2.2812 1.2261 1.4904 0.0146  0.2916  0.0566  634 LYS A O   
4690  C CB  . LYS A 634 ? 2.3966 1.1083 1.4560 0.0267  0.3648  0.0467  634 LYS A CB  
4691  C CG  . LYS A 634 ? 2.3241 0.9687 1.3461 0.0766  0.3967  0.0491  634 LYS A CG  
4692  C CD  . LYS A 634 ? 2.5916 1.1177 1.5397 0.0747  0.4312  0.0583  634 LYS A CD  
4693  C CE  . LYS A 634 ? 2.6714 1.1251 1.5809 0.1268  0.4651  0.0613  634 LYS A CE  
4694  N NZ  . LYS A 634 ? 2.7767 1.1044 1.6105 0.1243  0.5008  0.0705  634 LYS A NZ  
4695  N N   . LYS A 635 ? 2.1652 1.0615 1.3357 -0.0603 0.2887  0.0310  635 LYS A N   
4696  C CA  . LYS A 635 ? 2.2890 1.2480 1.4969 -0.0986 0.2623  0.0336  635 LYS A CA  
4697  C C   . LYS A 635 ? 2.1945 1.2618 1.4800 -0.0822 0.2310  0.0325  635 LYS A C   
4698  O O   . LYS A 635 ? 2.0950 1.2199 1.4170 -0.1132 0.2070  0.0320  635 LYS A O   
4699  C CB  . LYS A 635 ? 2.1626 1.0879 1.3365 -0.1624 0.2593  0.0219  635 LYS A CB  
4700  C CG  . LYS A 635 ? 2.3241 1.1348 1.4163 -0.1860 0.2915  0.0183  635 LYS A CG  
4701  C CD  . LYS A 635 ? 2.1144 0.9051 1.1894 -0.2160 0.2967  0.0281  635 LYS A CD  
4702  C CE  . LYS A 635 ? 2.2740 0.9777 1.2799 -0.2731 0.3143  0.0170  635 LYS A CE  
4703  N NZ  . LYS A 635 ? 2.8417 1.5644 1.8460 -0.3144 0.2977  -0.0010 635 LYS A NZ  
4704  N N   . PHE A 636 ? 2.1114 1.2041 1.4207 -0.0355 0.2323  0.0319  636 PHE A N   
4705  C CA  . PHE A 636 ? 1.8137 1.0046 1.1956 -0.0193 0.2048  0.0299  636 PHE A CA  
4706  C C   . PHE A 636 ? 1.9483 1.1958 1.3701 0.0045  0.1952  0.0408  636 PHE A C   
4707  O O   . PHE A 636 ? 2.0270 1.2715 1.4457 0.0484  0.2075  0.0484  636 PHE A O   
4708  C CB  . PHE A 636 ? 2.0380 1.2409 1.4327 0.0180  0.2099  0.0240  636 PHE A CB  
4709  C CG  . PHE A 636 ? 1.8961 1.1938 1.3625 0.0380  0.1854  0.0224  636 PHE A CG  
4710  C CD1 . PHE A 636 ? 1.7700 1.1145 1.2728 0.0104  0.1620  0.0152  636 PHE A CD1 
4711  C CD2 . PHE A 636 ? 2.0407 1.3802 1.5365 0.0829  0.1857  0.0283  636 PHE A CD2 
4712  C CE1 . PHE A 636 ? 1.6245 1.0484 1.1910 0.0272  0.1414  0.0129  636 PHE A CE1 
4713  C CE2 . PHE A 636 ? 1.8999 1.3238 1.4594 0.0971  0.1639  0.0240  636 PHE A CE2 
4714  C CZ  . PHE A 636 ? 1.7809 1.2433 1.3752 0.0690  0.1428  0.0158  636 PHE A CZ  
4715  N N   . MET A 637 ? 2.1034 1.4029 1.5607 -0.0228 0.1741  0.0416  637 MET A N   
4716  C CA  . MET A 637 ? 2.0707 1.4302 1.5680 -0.0024 0.1645  0.0495  637 MET A CA  
4717  C C   . MET A 637 ? 2.1691 1.4752 1.6206 0.0138  0.1885  0.0628  637 MET A C   
4718  O O   . MET A 637 ? 2.4377 1.7813 1.9095 0.0484  0.1878  0.0707  637 MET A O   
4719  C CB  . MET A 637 ? 1.9836 1.4106 1.5328 0.0389  0.1524  0.0455  637 MET A CB  
4720  C CG  . MET A 637 ? 1.8942 1.3834 1.4976 0.0242  0.1269  0.0350  637 MET A CG  
4721  S SD  . MET A 637 ? 1.8483 1.4267 1.5189 0.0641  0.1108  0.0301  637 MET A SD  
4722  C CE  . MET A 637 ? 1.8723 1.4441 1.5208 0.0963  0.1263  0.0423  637 MET A CE  
4723  N N   . LYS A 638 ? 1.9546 1.1736 1.3436 -0.0099 0.2097  0.0652  638 LYS A N   
4724  C CA  . LYS A 638 ? 2.0903 1.2442 1.4284 0.0051  0.2359  0.0799  638 LYS A CA  
4725  C C   . LYS A 638 ? 2.0925 1.2906 1.4520 -0.0023 0.2285  0.0906  638 LYS A C   
4726  O O   . LYS A 638 ? 1.9440 1.1339 1.2900 0.0308  0.2408  0.1051  638 LYS A O   
4727  C CB  . LYS A 638 ? 2.1139 1.1649 1.3822 -0.0299 0.2591  0.0777  638 LYS A CB  
4728  C CG  . LYS A 638 ? 2.3451 1.3141 1.5546 -0.0174 0.2891  0.0936  638 LYS A CG  
4729  C CD  . LYS A 638 ? 2.3303 1.1907 1.4686 -0.0541 0.3138  0.0881  638 LYS A CD  
4730  C CE  . LYS A 638 ? 2.5143 1.2837 1.5915 -0.0406 0.3460  0.1051  638 LYS A CE  
4731  N NZ  . LYS A 638 ? 2.8789 1.5363 1.8843 -0.0796 0.3716  0.0966  638 LYS A NZ  
4732  N N   . GLY A 639 ? 1.9464 1.1928 1.3386 -0.0426 0.2092  0.0843  639 GLY A N   
4733  C CA  . GLY A 639 ? 1.9268 1.2223 1.3435 -0.0518 0.2027  0.0926  639 GLY A CA  
4734  C C   . GLY A 639 ? 1.9337 1.3046 1.3984 -0.0066 0.1910  0.0951  639 GLY A C   
4735  O O   . GLY A 639 ? 1.8787 1.2835 1.3550 -0.0043 0.1909  0.1035  639 GLY A O   
4736  N N   . GLU A 640 ? 2.0274 1.4253 1.5182 0.0258  0.1820  0.0871  640 GLU A N   
4737  C CA  . GLU A 640 ? 1.8183 1.2920 1.3562 0.0664  0.1694  0.0860  640 GLU A CA  
4738  C C   . GLU A 640 ? 1.8552 1.3019 1.3666 0.1145  0.1845  0.0944  640 GLU A C   
4739  O O   . GLU A 640 ? 1.7876 1.2960 1.3330 0.1494  0.1750  0.0932  640 GLU A O   
4740  C CB  . GLU A 640 ? 1.8269 1.3669 1.4248 0.0637  0.1446  0.0694  640 GLU A CB  
4741  C CG  . GLU A 640 ? 1.7159 1.3024 1.3519 0.0276  0.1269  0.0637  640 GLU A CG  
4742  C CD  . GLU A 640 ? 1.9710 1.5255 1.5943 -0.0159 0.1227  0.0595  640 GLU A CD  
4743  O OE1 . GLU A 640 ? 2.2504 1.7397 1.8297 -0.0209 0.1354  0.0592  640 GLU A OE1 
4744  O OE2 . GLU A 640 ? 1.9341 1.5311 1.5910 -0.0440 0.1068  0.0563  640 GLU A OE2 
4745  N N   . GLY A 641 ? 1.8487 1.2079 1.3020 0.1164  0.2076  0.1020  641 GLY A N   
4746  C CA  . GLY A 641 ? 1.7325 1.0630 1.1595 0.1657  0.2239  0.1124  641 GLY A CA  
4747  C C   . GLY A 641 ? 2.0762 1.3593 1.4838 0.1729  0.2339  0.1043  641 GLY A C   
4748  O O   . GLY A 641 ? 2.0210 1.2799 1.4083 0.2159  0.2490  0.1127  641 GLY A O   
4749  N N   . GLY A 642 ? 2.0307 1.3045 1.4448 0.1338  0.2260  0.0892  642 GLY A N   
4750  C CA  . GLY A 642 ? 1.8908 1.1168 1.2817 0.1355  0.2371  0.0800  642 GLY A CA  
4751  C C   . GLY A 642 ? 1.9751 1.2716 1.4172 0.1651  0.2224  0.0703  642 GLY A C   
4752  O O   . GLY A 642 ? 2.0460 1.4252 1.5436 0.1670  0.1992  0.0660  642 GLY A O   
4753  N N   . LEU A 643 ? 2.1204 1.3843 1.5440 0.1869  0.2371  0.0664  643 LEU A N   
4754  C CA  . LEU A 643 ? 2.0154 1.3448 1.4862 0.2116  0.2255  0.0563  643 LEU A CA  
4755  C C   . LEU A 643 ? 2.0056 1.3998 1.5091 0.2591  0.2198  0.0648  643 LEU A C   
4756  O O   . LEU A 643 ? 2.0180 1.4849 1.5714 0.2738  0.2047  0.0553  643 LEU A O   
4757  C CB  . LEU A 643 ? 1.8847 1.1594 1.3226 0.2216  0.2465  0.0503  643 LEU A CB  
4758  C CG  . LEU A 643 ? 1.9479 1.1332 1.3226 0.2464  0.2790  0.0620  643 LEU A CG  
4759  C CD1 . LEU A 643 ? 2.1123 1.3307 1.5018 0.3078  0.2868  0.0732  643 LEU A CD1 
4760  C CD2 . LEU A 643 ? 2.2432 1.3504 1.5712 0.2288  0.3001  0.0510  643 LEU A CD2 
4761  N N   . GLY A 644 ? 2.0069 1.3764 1.4819 0.2801  0.2313  0.0821  644 GLY A N   
4762  C CA  . GLY A 644 ? 2.0020 1.4359 1.5033 0.3240  0.2246  0.0919  644 GLY A CA  
4763  C C   . GLY A 644 ? 1.7666 1.2989 1.3323 0.3143  0.1954  0.0794  644 GLY A C   
4764  O O   . GLY A 644 ? 1.6780 1.2790 1.2764 0.3484  0.1864  0.0794  644 GLY A O   
4765  N N   . ARG A 645 ? 1.7248 1.2645 1.3081 0.2696  0.1813  0.0688  645 ARG A N   
4766  C CA  . ARG A 645 ? 1.5590 1.1847 1.2028 0.2590  0.1551  0.0563  645 ARG A CA  
4767  C C   . ARG A 645 ? 1.5645 1.2352 1.2507 0.2618  0.1435  0.0400  645 ARG A C   
4768  O O   . ARG A 645 ? 1.5650 1.3058 1.3022 0.2582  0.1236  0.0284  645 ARG A O   
4769  C CB  . ARG A 645 ? 1.3950 1.0123 1.0434 0.2135  0.1455  0.0530  645 ARG A CB  
4770  C CG  . ARG A 645 ? 1.6629 1.2449 1.2747 0.2057  0.1563  0.0682  645 ARG A CG  
4771  C CD  . ARG A 645 ? 1.7432 1.3902 1.3816 0.2241  0.1467  0.0713  645 ARG A CD  
4772  N NE  . ARG A 645 ? 1.7203 1.3301 1.3170 0.2230  0.1612  0.0891  645 ARG A NE  
4773  C CZ  . ARG A 645 ? 1.6316 1.2864 1.2392 0.2328  0.1567  0.0945  645 ARG A CZ  
4774  N NH1 . ARG A 645 ? 1.6613 1.3991 1.3196 0.2460  0.1381  0.0816  645 ARG A NH1 
4775  N NH2 . ARG A 645 ? 1.7942 1.4090 1.3598 0.2279  0.1720  0.1121  645 ARG A NH2 
4776  N N   . ILE A 646 ? 1.7037 1.3334 1.3702 0.2624  0.1557  0.0373  646 ILE A N   
4777  C CA  . ILE A 646 ? 1.6141 1.2890 1.3226 0.2590  0.1445  0.0218  646 ILE A CA  
4778  C C   . ILE A 646 ? 1.5908 1.3396 1.3366 0.2977  0.1385  0.0188  646 ILE A C   
4779  O O   . ILE A 646 ? 1.6318 1.3707 1.3557 0.3347  0.1536  0.0288  646 ILE A O   
4780  C CB  . ILE A 646 ? 1.6243 1.2443 1.3035 0.2499  0.1598  0.0184  646 ILE A CB  
4781  C CG1 . ILE A 646 ? 1.4113 0.9651 1.0539 0.2067  0.1631  0.0192  646 ILE A CG1 
4782  C CG2 . ILE A 646 ? 1.6367 1.3077 1.3590 0.2488  0.1500  0.0045  646 ILE A CG2 
4783  C CD1 . ILE A 646 ? 1.7354 1.2109 1.3238 0.2039  0.1871  0.0199  646 ILE A CD1 
4784  N N   . VAL A 647 ? 1.4326 1.2518 1.2320 0.2891  0.1175  0.0053  647 VAL A N   
4785  C CA  . VAL A 647 ? 1.3924 1.2895 1.2291 0.3205  0.1093  -0.0005 647 VAL A CA  
4786  C C   . VAL A 647 ? 1.4113 1.3463 1.2853 0.3163  0.1041  -0.0155 647 VAL A C   
4787  O O   . VAL A 647 ? 1.3751 1.3432 1.2575 0.3466  0.1105  -0.0156 647 VAL A O   
4788  C CB  . VAL A 647 ? 1.3411 1.2906 1.2077 0.3145  0.0914  -0.0063 647 VAL A CB  
4789  C CG1 . VAL A 647 ? 1.4345 1.4677 1.3542 0.3234  0.0761  -0.0235 647 VAL A CG1 
4790  C CG2 . VAL A 647 ? 1.3463 1.2856 1.1808 0.3358  0.0985  0.0098  647 VAL A CG2 
4791  N N   . TRP A 648 ? 1.3828 1.3152 1.2788 0.2806  0.0932  -0.0264 648 TRP A N   
4792  C CA  . TRP A 648 ? 1.3055 1.2705 1.2356 0.2724  0.0888  -0.0396 648 TRP A CA  
4793  C C   . TRP A 648 ? 1.3991 1.3042 1.3037 0.2466  0.0976  -0.0376 648 TRP A C   
4794  O O   . TRP A 648 ? 1.2950 1.1488 1.1724 0.2228  0.0975  -0.0313 648 TRP A O   
4795  C CB  . TRP A 648 ? 1.3414 1.3610 1.3231 0.2541  0.0676  -0.0545 648 TRP A CB  
4796  C CG  . TRP A 648 ? 1.2599 1.3245 1.2812 0.2494  0.0630  -0.0687 648 TRP A CG  
4797  C CD1 . TRP A 648 ? 1.1525 1.2855 1.2064 0.2692  0.0594  -0.0791 648 TRP A CD1 
4798  C CD2 . TRP A 648 ? 1.3080 1.3558 1.3416 0.2198  0.0605  -0.0741 648 TRP A CD2 
4799  N NE1 . TRP A 648 ? 1.3081 1.4657 1.3941 0.2522  0.0564  -0.0915 648 TRP A NE1 
4800  C CE2 . TRP A 648 ? 1.3799 1.4839 1.4531 0.2225  0.0574  -0.0877 648 TRP A CE2 
4801  C CE3 . TRP A 648 ? 1.2543 1.2470 1.2681 0.1901  0.0602  -0.0680 648 TRP A CE3 
4802  C CZ2 . TRP A 648 ? 1.3509 1.4523 1.4426 0.1970  0.0559  -0.0940 648 TRP A CZ2 
4803  C CZ3 . TRP A 648 ? 1.3043 1.2969 1.3356 0.1670  0.0572  -0.0734 648 TRP A CZ3 
4804  C CH2 . TRP A 648 ? 1.2511 1.2950 1.3202 0.1706  0.0559  -0.0857 648 TRP A CH2 
4805  N N   . MET A 649 ? 1.4992 1.4145 1.4118 0.2504  0.1056  -0.0433 649 MET A N   
4806  C CA  . MET A 649 ? 1.3962 1.2594 1.2823 0.2273  0.1156  -0.0426 649 MET A CA  
4807  C C   . MET A 649 ? 1.4135 1.3162 1.3290 0.2282  0.1186  -0.0526 649 MET A C   
4808  O O   . MET A 649 ? 1.5388 1.4885 1.4733 0.2585  0.1244  -0.0557 649 MET A O   
4809  C CB  . MET A 649 ? 1.4659 1.2631 1.2938 0.2434  0.1391  -0.0318 649 MET A CB  
4810  C CG  . MET A 649 ? 1.5001 1.2342 1.2894 0.2173  0.1509  -0.0319 649 MET A CG  
4811  S SD  . MET A 649 ? 1.6990 1.3525 1.4193 0.2401  0.1820  -0.0226 649 MET A SD  
4812  C CE  . MET A 649 ? 1.5943 1.1894 1.2780 0.2111  0.1760  -0.0143 649 MET A CE  
4813  N N   . PRO A 650 ? 1.3674 1.2560 1.2872 0.1962  0.1154  -0.0569 650 PRO A N   
4814  C CA  . PRO A 650 ? 1.2588 1.1854 1.2051 0.1962  0.1208  -0.0657 650 PRO A CA  
4815  C C   . PRO A 650 ? 1.3947 1.3091 1.3142 0.2238  0.1461  -0.0637 650 PRO A C   
4816  O O   . PRO A 650 ? 1.6065 1.4578 1.4755 0.2291  0.1613  -0.0559 650 PRO A O   
4817  C CB  . PRO A 650 ? 1.3741 1.2709 1.3153 0.1557  0.1148  -0.0657 650 PRO A CB  
4818  C CG  . PRO A 650 ? 1.3074 1.1724 1.2373 0.1359  0.0998  -0.0591 650 PRO A CG  
4819  C CD  . PRO A 650 ? 1.4066 1.2483 1.3073 0.1588  0.1069  -0.0526 650 PRO A CD  
4820  N N   . LYS A 651 ? 1.3065 1.2808 1.2597 0.2412  0.1517  -0.0712 651 LYS A N   
4821  C CA  . LYS A 651 ? 1.4216 1.3941 1.3564 0.2717  0.1766  -0.0695 651 LYS A CA  
4822  C C   . LYS A 651 ? 1.7026 1.6027 1.5883 0.2526  0.1950  -0.0674 651 LYS A C   
4823  O O   . LYS A 651 ? 1.7223 1.5714 1.5632 0.2732  0.2157  -0.0617 651 LYS A O   
4824  C CB  . LYS A 651 ? 1.1878 1.2470 1.1740 0.2863  0.1774  -0.0791 651 LYS A CB  
4825  C CG  . LYS A 651 ? 1.3368 1.4088 1.3121 0.3266  0.2024  -0.0761 651 LYS A CG  
4826  C CD  . LYS A 651 ? 1.2884 1.4544 1.3181 0.3375  0.2026  -0.0860 651 LYS A CD  
4827  C CE  . LYS A 651 ? 1.3668 1.5456 1.3873 0.3750  0.2298  -0.0830 651 LYS A CE  
4828  N NZ  . LYS A 651 ? 1.3698 1.6397 1.4434 0.3758  0.2321  -0.0940 651 LYS A NZ  
4829  N N   . GLU A 652 ? 1.8970 1.7901 1.7885 0.2135  0.1881  -0.0720 652 GLU A N   
4830  C CA  . GLU A 652 ? 1.9484 1.7780 1.7919 0.1910  0.2035  -0.0709 652 GLU A CA  
4831  C C   . GLU A 652 ? 1.9759 1.7236 1.7588 0.1888  0.2114  -0.0637 652 GLU A C   
4832  O O   . GLU A 652 ? 2.0055 1.7036 1.7425 0.1966  0.2358  -0.0645 652 GLU A O   
4833  C CB  . GLU A 652 ? 2.0159 1.8475 1.8726 0.1465  0.1881  -0.0725 652 GLU A CB  
4834  C CG  . GLU A 652 ? 2.3172 2.2171 2.2256 0.1419  0.1854  -0.0801 652 GLU A CG  
4835  C CD  . GLU A 652 ? 2.5023 2.3959 2.4190 0.0992  0.1726  -0.0787 652 GLU A CD  
4836  O OE1 . GLU A 652 ? 2.3152 2.1777 2.2227 0.0770  0.1542  -0.0720 652 GLU A OE1 
4837  O OE2 . GLU A 652 ? 2.5044 2.4255 2.4370 0.0884  0.1816  -0.0832 652 GLU A OE2 
4838  N N   . LEU A 653 ? 1.7788 1.5120 1.5612 0.1769  0.1921  -0.0579 653 LEU A N   
4839  C CA  . LEU A 653 ? 1.6322 1.2921 1.3605 0.1701  0.1979  -0.0513 653 LEU A CA  
4840  C C   . LEU A 653 ? 1.6918 1.3343 1.3996 0.2130  0.2164  -0.0467 653 LEU A C   
4841  O O   . LEU A 653 ? 1.9039 1.4756 1.5563 0.2158  0.2363  -0.0441 653 LEU A O   
4842  C CB  . LEU A 653 ? 1.5896 1.2520 1.3318 0.1458  0.1717  -0.0462 653 LEU A CB  
4843  C CG  . LEU A 653 ? 1.6447 1.2367 1.3346 0.1261  0.1740  -0.0399 653 LEU A CG  
4844  C CD1 . LEU A 653 ? 1.8134 1.3583 1.4637 0.0890  0.1784  -0.0422 653 LEU A CD1 
4845  C CD2 . LEU A 653 ? 1.7111 1.3223 1.4252 0.1122  0.1498  -0.0346 653 LEU A CD2 
4846  N N   . LYS A 654 ? 1.6490 1.3548 1.3996 0.2451  0.2098  -0.0454 654 LYS A N   
4847  C CA  . LYS A 654 ? 1.7023 1.3985 1.4360 0.2905  0.2258  -0.0375 654 LYS A CA  
4848  C C   . LYS A 654 ? 1.8890 1.5492 1.5890 0.3127  0.2571  -0.0392 654 LYS A C   
4849  O O   . LYS A 654 ? 2.0277 1.6164 1.6757 0.3274  0.2771  -0.0326 654 LYS A O   
4850  C CB  . LYS A 654 ? 1.6534 1.4394 1.4438 0.3193  0.2121  -0.0378 654 LYS A CB  
4851  C CG  . LYS A 654 ? 1.6430 1.4300 1.4254 0.3507  0.2102  -0.0260 654 LYS A CG  
4852  C CD  . LYS A 654 ? 1.4569 1.3290 1.2833 0.3892  0.2068  -0.0263 654 LYS A CD  
4853  C CE  . LYS A 654 ? 1.5709 1.5244 1.4566 0.3708  0.1798  -0.0375 654 LYS A CE  
4854  N NZ  . LYS A 654 ? 1.5775 1.5953 1.4896 0.4018  0.1683  -0.0336 654 LYS A NZ  
4855  N N   . ASP A 655 ? 1.9349 1.6406 1.6627 0.3142  0.2628  -0.0482 655 ASP A N   
4856  C CA  . ASP A 655 ? 1.9984 1.6804 1.7004 0.3386  0.2942  -0.0512 655 ASP A CA  
4857  C C   . ASP A 655 ? 2.0093 1.5924 1.6431 0.3132  0.3128  -0.0542 655 ASP A C   
4858  O O   . ASP A 655 ? 2.1843 1.7125 1.7753 0.3396  0.3414  -0.0529 655 ASP A O   
4859  C CB  . ASP A 655 ? 2.0485 1.8047 1.7966 0.3379  0.2956  -0.0611 655 ASP A CB  
4860  C CG  . ASP A 655 ? 1.9789 1.8347 1.7907 0.3675  0.2827  -0.0603 655 ASP A CG  
4861  O OD1 . ASP A 655 ? 1.8704 1.7358 1.6831 0.4043  0.2819  -0.0507 655 ASP A OD1 
4862  O OD2 . ASP A 655 ? 1.8348 1.7589 1.6936 0.3525  0.2735  -0.0692 655 ASP A OD2 
4863  N N   . PHE A 656 ? 1.8432 1.4029 1.4653 0.2628  0.2973  -0.0581 656 PHE A N   
4864  C CA  . PHE A 656 ? 1.7849 1.2566 1.3412 0.2331  0.3120  -0.0623 656 PHE A CA  
4865  C C   . PHE A 656 ? 1.9334 1.3300 1.4406 0.2424  0.3214  -0.0551 656 PHE A C   
4866  O O   . PHE A 656 ? 2.0434 1.3729 1.4994 0.2582  0.3512  -0.0577 656 PHE A O   
4867  C CB  . PHE A 656 ? 1.8265 1.3001 1.3854 0.1785  0.2886  -0.0649 656 PHE A CB  
4868  C CG  . PHE A 656 ? 1.9341 1.3250 1.4253 0.1426  0.2992  -0.0693 656 PHE A CG  
4869  C CD1 . PHE A 656 ? 1.9807 1.3373 1.4330 0.1385  0.3251  -0.0794 656 PHE A CD1 
4870  C CD2 . PHE A 656 ? 2.0745 1.4261 1.5411 0.1113  0.2833  -0.0646 656 PHE A CD2 
4871  C CE1 . PHE A 656 ? 2.1960 1.4779 1.5826 0.1026  0.3343  -0.0856 656 PHE A CE1 
4872  C CE2 . PHE A 656 ? 2.0842 1.3656 1.4885 0.0747  0.2914  -0.0700 656 PHE A CE2 
4873  C CZ  . PHE A 656 ? 2.0234 1.2691 1.3865 0.0700  0.3166  -0.0810 656 PHE A CZ  
4874  N N   . VAL A 657 ? 1.9911 1.3980 1.5136 0.2337  0.2985  -0.0463 657 VAL A N   
4875  C CA  . VAL A 657 ? 2.0618 1.4012 1.5402 0.2406  0.3074  -0.0380 657 VAL A CA  
4876  C C   . VAL A 657 ? 1.9587 1.3314 1.4610 0.2947  0.3126  -0.0271 657 VAL A C   
4877  O O   . VAL A 657 ? 2.1248 1.5362 1.6568 0.2992  0.2921  -0.0187 657 VAL A O   
4878  C CB  . VAL A 657 ? 2.1578 1.4820 1.6305 0.1983  0.2832  -0.0338 657 VAL A CB  
4879  C CG1 . VAL A 657 ? 2.1041 1.3793 1.5368 0.1472  0.2826  -0.0424 657 VAL A CG1 
4880  C CG2 . VAL A 657 ? 1.9332 1.3442 1.4732 0.1936  0.2505  -0.0305 657 VAL A CG2 
4881  N N   . ALA A 658 ? 1.9775 1.3403 1.4683 0.3372  0.3397  -0.0269 658 ALA A N   
4882  C CA  . ALA A 658 ? 1.8595 1.2578 1.3720 0.3927  0.3450  -0.0142 658 ALA A CA  
4883  C C   . ALA A 658 ? 2.1839 1.4889 1.6343 0.4220  0.3757  -0.0045 658 ALA A C   
4884  O O   . ALA A 658 ? 2.2483 1.5403 1.6906 0.4412  0.3727  0.0106  658 ALA A O   
4885  C CB  . ALA A 658 ? 1.8934 1.3736 1.4546 0.4252  0.3492  -0.0189 658 ALA A CB  
4886  N N   . GLU A 659 ? 2.4147 1.6510 1.8187 0.4246  0.4066  -0.0132 659 GLU A N   
4887  C CA  . GLU A 659 ? 2.4148 1.5516 1.7560 0.4518  0.4393  -0.0057 659 GLU A CA  
4888  C C   . GLU A 659 ? 2.4760 1.5242 1.7628 0.4085  0.4376  -0.0045 659 GLU A C   
4889  O O   . GLU A 659 ? 2.5483 1.5284 1.7947 0.4288  0.4541  0.0083  659 GLU A O   
4890  C CB  . GLU A 659 ? 2.5353 1.6239 1.8424 0.4659  0.4747  -0.0186 659 GLU A CB  
4891  C CG  . GLU A 659 ? 2.4645 1.6305 1.8185 0.5201  0.4847  -0.0165 659 GLU A CG  
4892  C CD  . GLU A 659 ? 2.6950 1.8103 2.0136 0.5423  0.5245  -0.0278 659 GLU A CD  
4893  O OE1 . GLU A 659 ? 2.5526 1.5710 1.8077 0.5101  0.5438  -0.0407 659 GLU A OE1 
4894  O OE2 . GLU A 659 ? 2.9102 2.0855 2.2649 0.5918  0.5369  -0.0247 659 GLU A OE2 
4895  N N   . LYS A 660 ? 2.4827 1.5333 1.7689 0.3491  0.4178  -0.0164 660 LYS A N   
4896  C CA  . LYS A 660 ? 2.5572 1.5368 1.7976 0.3032  0.4134  -0.0163 660 LYS A CA  
4897  C C   . LYS A 660 ? 2.5950 1.6077 1.8614 0.3064  0.3908  0.0005  660 LYS A C   
4898  O O   . LYS A 660 ? 2.6410 1.5854 1.8643 0.2891  0.3972  0.0070  660 LYS A O   
4899  C CB  . LYS A 660 ? 2.6016 1.5859 1.8382 0.2418  0.3968  -0.0321 660 LYS A CB  
4900  C CG  . LYS A 660 ? 2.6116 1.5494 1.8083 0.2331  0.4222  -0.0494 660 LYS A CG  
4901  C CD  . LYS A 660 ? 2.4914 1.4263 1.6741 0.1707  0.4062  -0.0627 660 LYS A CD  
4902  C CE  . LYS A 660 ? 2.4758 1.3652 1.6145 0.1620  0.4327  -0.0803 660 LYS A CE  
4903  N NZ  . LYS A 660 ? 2.6011 1.4983 1.7281 0.1028  0.4147  -0.0911 660 LYS A NZ  
4904  N N   . LEU A 661 ? 2.6676 1.7834 2.0021 0.3269  0.3660  0.0067  661 LEU A N   
4905  C CA  . LEU A 661 ? 2.5894 1.7428 1.9492 0.3328  0.3457  0.0213  661 LEU A CA  
4906  C C   . LEU A 661 ? 2.6833 1.8216 2.0305 0.3905  0.3639  0.0395  661 LEU A C   
4907  O O   . LEU A 661 ? 2.8566 1.9643 2.1826 0.3925  0.3639  0.0538  661 LEU A O   
4908  C CB  . LEU A 661 ? 2.4481 1.7160 1.8831 0.3291  0.3121  0.0181  661 LEU A CB  
4909  C CG  . LEU A 661 ? 2.5410 1.8374 1.9992 0.2764  0.2890  0.0045  661 LEU A CG  
4910  C CD1 . LEU A 661 ? 2.3557 1.7535 1.8841 0.2769  0.2579  0.0040  661 LEU A CD1 
4911  C CD2 . LEU A 661 ? 2.6348 1.8683 2.0525 0.2285  0.2857  0.0042  661 LEU A CD2 
4912  N N   . ASN A 662 ? 2.3854 1.5480 1.7460 0.4382  0.3794  0.0404  662 ASN A N   
4913  C CA  . ASN A 662 ? 2.3471 1.5023 1.6986 0.4990  0.3962  0.0602  662 ASN A CA  
4914  C C   . ASN A 662 ? 2.5747 1.6037 1.8495 0.5048  0.4275  0.0706  662 ASN A C   
4915  O O   . ASN A 662 ? 2.5657 1.5766 1.8255 0.5414  0.4350  0.0923  662 ASN A O   
4916  C CB  . ASN A 662 ? 2.5287 1.7348 1.9097 0.5464  0.4087  0.0575  662 ASN A CB  
4917  C CG  . ASN A 662 ? 2.3830 1.7173 1.8408 0.5470  0.3794  0.0501  662 ASN A CG  
4918  O OD1 . ASN A 662 ? 2.3081 1.6978 1.7999 0.5225  0.3496  0.0498  662 ASN A OD1 
4919  N ND2 . ASN A 662 ? 2.4350 1.8192 1.9221 0.5741  0.3887  0.0429  662 ASN A ND2 
4920  N N   . LYS A 663 ? 2.8299 1.7703 2.0538 0.4678  0.4461  0.0555  663 LYS A N   
4921  C CA  . LYS A 663 ? 2.9788 1.7909 2.1259 0.4661  0.4775  0.0616  663 LYS A CA  
4922  C C   . LYS A 663 ? 2.9705 1.7500 2.0961 0.4210  0.4636  0.0681  663 LYS A C   
4923  O O   . LYS A 663 ? 3.1393 1.8603 2.2290 0.4388  0.4778  0.0869  663 LYS A O   
4924  C CB  . LYS A 663 ? 2.9920 1.7219 2.0895 0.4417  0.5040  0.0398  663 LYS A CB  
4925  C CG  . LYS A 663 ? 2.9944 1.7165 2.0892 0.4964  0.5333  0.0374  663 LYS A CG  
4926  C CD  . LYS A 663 ? 3.0979 1.7140 2.1269 0.4755  0.5673  0.0169  663 LYS A CD  
4927  C CE  . LYS A 663 ? 3.1150 1.7779 2.1651 0.4440  0.5594  -0.0076 663 LYS A CE  
4928  N NZ  . LYS A 663 ? 3.1579 1.8693 2.2320 0.3798  0.5223  -0.0159 663 LYS A NZ  
4929  N N   . THR A 664 ? 2.6052 1.4242 1.7538 0.3639  0.4363  0.0541  664 THR A N   
4930  C CA  . THR A 664 ? 2.6804 1.4808 1.8156 0.3194  0.4219  0.0593  664 THR A CA  
4931  C C   . THR A 664 ? 2.5856 1.4475 1.7560 0.3498  0.4057  0.0810  664 THR A C   
4932  O O   . THR A 664 ? 2.6743 1.4913 1.8143 0.3379  0.4101  0.0943  664 THR A O   
4933  C CB  . THR A 664 ? 2.5853 1.4194 1.7398 0.2566  0.3968  0.0407  664 THR A CB  
4934  O OG1 . THR A 664 ? 2.5507 1.4949 1.7756 0.2658  0.3701  0.0351  664 THR A OG1 
4935  C CG2 . THR A 664 ? 2.7613 1.5146 1.8619 0.2199  0.4160  0.0214  664 THR A CG2 
4936  N N   . ALA A 665 ? 2.5235 1.4879 1.7556 0.3870  0.3878  0.0841  665 ALA A N   
4937  C CA  . ALA A 665 ? 2.3128 1.3428 1.5778 0.4182  0.3722  0.1029  665 ALA A CA  
4938  C C   . ALA A 665 ? 2.3993 1.3662 1.6198 0.4671  0.3991  0.1273  665 ALA A C   
4939  O O   . ALA A 665 ? 2.5430 1.5122 1.7562 0.4740  0.3944  0.1458  665 ALA A O   
4940  C CB  . ALA A 665 ? 2.1469 1.2954 1.4828 0.4461  0.3502  0.0977  665 ALA A CB  
4941  N N   . LYS A 666 ? 2.4221 1.3322 1.6120 0.5025  0.4284  0.1282  666 LYS A N   
4942  C CA  . LYS A 666 ? 2.5062 1.3471 1.6509 0.5527  0.4568  0.1528  666 LYS A CA  
4943  C C   . LYS A 666 ? 2.5579 1.2790 1.6322 0.5184  0.4764  0.1602  666 LYS A C   
4944  O O   . LYS A 666 ? 2.6191 1.3003 1.6634 0.5453  0.4883  0.1858  666 LYS A O   
4945  C CB  . LYS A 666 ? 2.4811 1.2867 1.6107 0.5974  0.4856  0.1495  666 LYS A CB  
4946  C CG  . LYS A 666 ? 2.3892 1.1405 1.4834 0.6626  0.5131  0.1783  666 LYS A CG  
4947  C CD  . LYS A 666 ? 2.4633 1.1585 1.5331 0.7023  0.5476  0.1730  666 LYS A CD  
4948  C CE  . LYS A 666 ? 2.6733 1.2508 1.6767 0.7444  0.5853  0.1970  666 LYS A CE  
4949  N NZ  . LYS A 666 ? 2.7333 1.2562 1.7145 0.7865  0.6209  0.1908  666 LYS A NZ  
4950  N N   . GLU A 667 ? 2.6037 1.2717 1.6523 0.4582  0.4791  0.1381  667 GLU A N   
4951  C CA  . GLU A 667 ? 2.6445 1.2010 1.6265 0.4163  0.4972  0.1413  667 GLU A CA  
4952  C C   . GLU A 667 ? 2.6007 1.2012 1.6008 0.3937  0.4744  0.1556  667 GLU A C   
4953  O O   . GLU A 667 ? 2.6951 1.2125 1.6435 0.3678  0.4899  0.1653  667 GLU A O   
4954  C CB  . GLU A 667 ? 2.7520 1.2616 1.7093 0.3531  0.4998  0.1126  667 GLU A CB  
4955  C CG  . GLU A 667 ? 2.8549 1.3302 1.7965 0.3706  0.5210  0.0951  667 GLU A CG  
4956  C CD  . GLU A 667 ? 3.1834 1.6886 2.1405 0.3178  0.5052  0.0662  667 GLU A CD  
4957  O OE1 . GLU A 667 ? 3.2270 1.7486 2.1896 0.2603  0.4837  0.0591  667 GLU A OE1 
4958  O OE2 . GLU A 667 ? 3.2981 1.8128 2.2621 0.3352  0.5145  0.0522  667 GLU A OE2 
4959  N N   . LEU A 668 ? 2.5162 1.2409 1.5858 0.4009  0.4404  0.1555  668 LEU A N   
4960  C CA  . LEU A 668 ? 2.5398 1.3128 1.6295 0.3765  0.4185  0.1656  668 LEU A CA  
4961  C C   . LEU A 668 ? 2.5680 1.4111 1.6870 0.4328  0.4093  0.1887  668 LEU A C   
4962  O O   . LEU A 668 ? 2.5126 1.3086 1.5934 0.4494  0.4237  0.2133  668 LEU A O   
4963  C CB  . LEU A 668 ? 2.4058 1.2635 1.5505 0.3292  0.3853  0.1432  668 LEU A CB  
4964  C CG  . LEU A 668 ? 2.2465 1.0609 1.3740 0.2808  0.3887  0.1187  668 LEU A CG  
4965  C CD1 . LEU A 668 ? 2.0245 0.9334 1.2129 0.2450  0.3540  0.1011  668 LEU A CD1 
4966  C CD2 . LEU A 668 ? 2.4816 1.1885 1.5428 0.2355  0.4091  0.1190  668 LEU A CD2 
4967  N N   . TYR A 669 ? 2.6565 1.6077 1.8382 0.4608  0.3868  0.1821  669 TYR A N   
4968  C CA  . TYR A 669 ? 2.5449 1.5751 1.7565 0.5103  0.3744  0.2021  669 TYR A CA  
4969  C C   . TYR A 669 ? 2.5871 1.6074 1.7898 0.5761  0.3929  0.2157  669 TYR A C   
4970  O O   . TYR A 669 ? 2.6797 1.7726 1.9088 0.6229  0.3825  0.2321  669 TYR A O   
4971  C CB  . TYR A 669 ? 2.5234 1.6818 1.8093 0.4980  0.3379  0.1860  669 TYR A CB  
4972  C CG  . TYR A 669 ? 2.5203 1.6782 1.8207 0.4341  0.3244  0.1623  669 TYR A CG  
4973  C CD1 . TYR A 669 ? 2.4909 1.6279 1.7764 0.3912  0.3195  0.1647  669 TYR A CD1 
4974  C CD2 . TYR A 669 ? 2.5259 1.6971 1.8494 0.4169  0.3194  0.1395  669 TYR A CD2 
4975  C CE1 . TYR A 669 ? 2.2771 1.4155 1.5758 0.3342  0.3070  0.1451  669 TYR A CE1 
4976  C CE2 . TYR A 669 ? 2.5256 1.6943 1.8589 0.3597  0.3069  0.1208  669 TYR A CE2 
4977  C CZ  . TYR A 669 ? 2.3573 1.5100 1.6785 0.3197  0.3004  0.1240  669 TYR A CZ  
4978  O OH  . TYR A 669 ? 2.3568 1.5146 1.6909 0.2653  0.2865  0.1071  669 TYR A OH  
4979  N N   . ASN A 670 ? 2.9270 1.8599 2.0915 0.5804  0.4205  0.2093  670 ASN A N   
4980  C CA  . ASN A 670 ? 2.9631 1.8792 2.1174 0.6458  0.4426  0.2219  670 ASN A CA  
4981  C C   . ASN A 670 ? 2.9639 2.0057 2.1901 0.6734  0.4207  0.2104  670 ASN A C   
4982  O O   . ASN A 670 ? 3.1058 2.1580 2.3365 0.7294  0.4350  0.2197  670 ASN A O   
4983  C CB  . ASN A 670 ? 2.9060 1.7844 2.0235 0.6969  0.4586  0.2584  670 ASN A CB  
4984  C CG  . ASN A 670 ? 3.0825 1.8848 2.1619 0.7524  0.4938  0.2719  670 ASN A CG  
4985  O OD1 . ASN A 670 ? 3.1670 1.8807 2.2112 0.7359  0.5186  0.2562  670 ASN A OD1 
4986  N ND2 . ASN A 670 ? 2.9588 1.7963 2.0444 0.8193  0.4967  0.3006  670 ASN A ND2 
4987  N N   . ILE A 671 ? 2.6263 1.7590 1.9069 0.6357  0.3883  0.1911  671 ILE A N   
4988  C CA  . ILE A 671 ? 2.4608 1.7105 1.8101 0.6539  0.3677  0.1770  671 ILE A CA  
4989  C C   . ILE A 671 ? 2.2678 1.4826 1.6103 0.6634  0.3891  0.1628  671 ILE A C   
4990  O O   . ILE A 671 ? 2.2391 1.3789 1.5501 0.6203  0.4007  0.1467  671 ILE A O   
4991  C CB  . ILE A 671 ? 2.5278 1.8575 1.9285 0.6037  0.3338  0.1558  671 ILE A CB  
4992  C CG1 . ILE A 671 ? 2.0552 1.4322 1.4677 0.6002  0.3134  0.1683  671 ILE A CG1 
4993  C CG2 . ILE A 671 ? 2.4077 1.8372 1.8718 0.6123  0.3176  0.1375  671 ILE A CG2 
4994  C CD1 . ILE A 671 ? 2.3407 1.7737 1.7937 0.5480  0.2851  0.1481  671 ILE A CD1 
4995  N N   . ASP A 672 ? 2.2527 1.5241 1.6235 0.7173  0.3941  0.1682  672 ASP A N   
4996  C CA  . ASP A 672 ? 2.5816 1.8221 1.9456 0.7325  0.4184  0.1557  672 ASP A CA  
4997  C C   . ASP A 672 ? 2.4127 1.7553 1.8417 0.7126  0.3971  0.1311  672 ASP A C   
4998  O O   . ASP A 672 ? 2.3916 1.7087 1.8155 0.7035  0.4133  0.1142  672 ASP A O   
4999  C CB  . ASP A 672 ? 2.7885 2.0149 2.1377 0.8066  0.4435  0.1784  672 ASP A CB  
5000  C CG  . ASP A 672 ? 2.8330 1.9616 2.1192 0.8295  0.4633  0.2069  672 ASP A CG  
5001  O OD1 . ASP A 672 ? 2.7751 1.7842 2.0016 0.7968  0.4842  0.2026  672 ASP A OD1 
5002  O OD2 . ASP A 672 ? 2.9167 2.0897 2.2127 0.8781  0.4575  0.2333  672 ASP A OD2 
5003  N N   . ASN A 673 ? 2.1222 1.5732 1.6076 0.7048  0.3637  0.1286  673 ASN A N   
5004  C CA  . ASN A 673 ? 2.0087 1.5552 1.5565 0.6824  0.3431  0.1053  673 ASN A CA  
5005  C C   . ASN A 673 ? 1.9275 1.5152 1.5032 0.6305  0.3111  0.0937  673 ASN A C   
5006  O O   . ASN A 673 ? 1.9269 1.6198 1.5593 0.6333  0.2860  0.0878  673 ASN A O   
5007  C CB  . ASN A 673 ? 2.0574 1.7136 1.6579 0.7327  0.3365  0.1102  673 ASN A CB  
5008  C CG  . ASN A 673 ? 2.2755 1.9191 1.8726 0.7678  0.3644  0.1081  673 ASN A CG  
5009  O OD1 . ASN A 673 ? 2.1959 1.7676 1.7486 0.8081  0.3928  0.1248  673 ASN A OD1 
5010  N ND2 . ASN A 673 ? 2.2803 1.9915 1.9234 0.7532  0.3584  0.0877  673 ASN A ND2 
5011  N N   . PHE A 674 ? 1.9698 1.4787 1.5075 0.5848  0.3126  0.0899  674 PHE A N   
5012  C CA  . PHE A 674 ? 2.0310 1.5758 1.5948 0.5380  0.2841  0.0801  674 PHE A CA  
5013  C C   . PHE A 674 ? 2.0847 1.7140 1.7084 0.5184  0.2648  0.0588  674 PHE A C   
5014  O O   . PHE A 674 ? 2.1637 1.8779 1.8354 0.5151  0.2399  0.0540  674 PHE A O   
5015  C CB  . PHE A 674 ? 2.1060 1.5550 1.6206 0.4912  0.2907  0.0786  674 PHE A CB  
5016  C CG  . PHE A 674 ? 2.1040 1.5831 1.6389 0.4517  0.2648  0.0751  674 PHE A CG  
5017  C CD1 . PHE A 674 ? 1.9978 1.5238 1.5478 0.4696  0.2516  0.0874  674 PHE A CD1 
5018  C CD2 . PHE A 674 ? 2.0963 1.5577 1.6339 0.3979  0.2543  0.0601  674 PHE A CD2 
5019  C CE1 . PHE A 674 ? 2.0380 1.5922 1.6071 0.4348  0.2301  0.0828  674 PHE A CE1 
5020  C CE2 . PHE A 674 ? 1.7758 1.2674 1.3349 0.3653  0.2318  0.0575  674 PHE A CE2 
5021  C CZ  . PHE A 674 ? 1.9227 1.4600 1.4981 0.3841  0.2207  0.0679  674 PHE A CZ  
5022  N N   . ALA A 675 ? 2.0243 1.6295 1.6435 0.5053  0.2776  0.0457  675 ALA A N   
5023  C CA  . ALA A 675 ? 1.8124 1.4902 1.4841 0.4852  0.2626  0.0270  675 ALA A CA  
5024  C C   . ALA A 675 ? 1.8550 1.6466 1.5874 0.5140  0.2458  0.0257  675 ALA A C   
5025  O O   . ALA A 675 ? 1.7956 1.6525 1.5750 0.4877  0.2233  0.0118  675 ALA A O   
5026  C CB  . ALA A 675 ? 1.9801 1.6214 1.6342 0.4835  0.2854  0.0177  675 ALA A CB  
5027  N N   . ASP A 676 ? 2.1328 1.9479 1.8634 0.5676  0.2567  0.0402  676 ASP A N   
5028  C CA  . ASP A 676 ? 2.1239 2.0521 1.9091 0.5968  0.2405  0.0399  676 ASP A CA  
5029  C C   . ASP A 676 ? 2.0168 1.9909 1.8222 0.5833  0.2130  0.0407  676 ASP A C   
5030  O O   . ASP A 676 ? 1.9804 2.0495 1.8381 0.5804  0.1921  0.0295  676 ASP A O   
5031  C CB  . ASP A 676 ? 2.1368 2.0739 1.9093 0.6603  0.2593  0.0593  676 ASP A CB  
5032  C CG  . ASP A 676 ? 2.1382 2.1980 1.9648 0.6940  0.2427  0.0610  676 ASP A CG  
5033  O OD1 . ASP A 676 ? 2.2699 2.4104 2.1483 0.6667  0.2207  0.0422  676 ASP A OD1 
5034  O OD2 . ASP A 676 ? 1.9484 2.0233 1.7647 0.7473  0.2518  0.0815  676 ASP A OD2 
5035  N N   . MET A 677 ? 1.8326 1.7393 1.5959 0.5732  0.2144  0.0526  677 MET A N   
5036  C CA  . MET A 677 ? 1.6724 1.6146 1.4485 0.5604  0.1920  0.0539  677 MET A CA  
5037  C C   . MET A 677 ? 1.5785 1.5365 1.3844 0.5065  0.1719  0.0329  677 MET A C   
5038  O O   . MET A 677 ? 1.6146 1.6281 1.4492 0.4962  0.1509  0.0267  677 MET A O   
5039  C CB  . MET A 677 ? 1.6988 1.5606 1.4177 0.5667  0.2035  0.0748  677 MET A CB  
5040  C CG  . MET A 677 ? 1.7883 1.6138 1.4692 0.6195  0.2268  0.0985  677 MET A CG  
5041  S SD  . MET A 677 ? 1.8563 1.6437 1.4914 0.6396  0.2299  0.1265  677 MET A SD  
5042  C CE  . MET A 677 ? 1.7408 1.6617 1.4263 0.6714  0.2044  0.1284  677 MET A CE  
5043  N N   . ILE A 678 ? 1.6592 1.5685 1.4568 0.4745  0.1792  0.0227  678 ILE A N   
5044  C CA  . ILE A 678 ? 1.4679 1.3866 1.2921 0.4247  0.1608  0.0058  678 ILE A CA  
5045  C C   . ILE A 678 ? 1.5276 1.5387 1.4129 0.4217  0.1447  -0.0115 678 ILE A C   
5046  O O   . ILE A 678 ? 1.6270 1.6690 1.5264 0.4430  0.1542  -0.0140 678 ILE A O   
5047  C CB  . ILE A 678 ? 1.5882 1.4286 1.3813 0.3912  0.1725  0.0021  678 ILE A CB  
5048  C CG1 . ILE A 678 ? 1.4921 1.2498 1.2342 0.3738  0.1795  0.0133  678 ILE A CG1 
5049  C CG2 . ILE A 678 ? 1.6344 1.5058 1.4665 0.3514  0.1555  -0.0150 678 ILE A CG2 
5050  C CD1 . ILE A 678 ? 1.7416 1.4568 1.4402 0.4111  0.1987  0.0321  678 ILE A CD1 
5051  N N   . CYS A 679 ? 1.4611 1.5132 1.3809 0.3959  0.1226  -0.0234 679 CYS A N   
5052  C CA  . CYS A 679 ? 1.3936 1.5255 1.3696 0.3864  0.1076  -0.0419 679 CYS A CA  
5053  C C   . CYS A 679 ? 1.3703 1.4769 1.3567 0.3498  0.1085  -0.0526 679 CYS A C   
5054  O O   . CYS A 679 ? 1.4499 1.4853 1.4039 0.3271  0.1143  -0.0472 679 CYS A O   
5055  C CB  . CYS A 679 ? 1.4061 1.5867 1.4113 0.3757  0.0860  -0.0511 679 CYS A CB  
5056  S SG  . CYS A 679 ? 1.3325 1.6159 1.4040 0.3686  0.0686  -0.0754 679 CYS A SG  
5057  N N   . ASP A 680 ? 1.4713 1.6367 1.5011 0.3426  0.1030  -0.0672 680 ASP A N   
5058  C CA  . ASP A 680 ? 1.4495 1.5951 1.4896 0.3082  0.1040  -0.0757 680 ASP A CA  
5059  C C   . ASP A 680 ? 1.4778 1.6938 1.5742 0.2903  0.0888  -0.0941 680 ASP A C   
5060  O O   . ASP A 680 ? 1.5377 1.8214 1.6639 0.3066  0.0793  -0.1018 680 ASP A O   
5061  C CB  . ASP A 680 ? 1.4440 1.5619 1.4600 0.3202  0.1270  -0.0705 680 ASP A CB  
5062  C CG  . ASP A 680 ? 1.6083 1.7925 1.6467 0.3567  0.1358  -0.0722 680 ASP A CG  
5063  O OD1 . ASP A 680 ? 1.6043 1.8672 1.6861 0.3628  0.1214  -0.0817 680 ASP A OD1 
5064  O OD2 . ASP A 680 ? 1.7088 1.8678 1.7215 0.3791  0.1575  -0.0646 680 ASP A OD2 
5065  N N   . GLU A 681 ? 1.4025 1.6019 1.5117 0.2558  0.0866  -0.1010 681 GLU A N   
5066  C CA  . GLU A 681 ? 1.3197 1.5744 1.4793 0.2346  0.0745  -0.1182 681 GLU A CA  
5067  C C   . GLU A 681 ? 1.4710 1.8050 1.6626 0.2548  0.0791  -0.1276 681 GLU A C   
5068  O O   . GLU A 681 ? 1.3667 1.7609 1.6009 0.2442  0.0669  -0.1438 681 GLU A O   
5069  C CB  . GLU A 681 ? 1.2977 1.5138 1.4584 0.1971  0.0754  -0.1192 681 GLU A CB  
5070  C CG  . GLU A 681 ? 1.4295 1.6383 1.5787 0.1960  0.0942  -0.1165 681 GLU A CG  
5071  C CD  . GLU A 681 ? 1.3892 1.5250 1.4832 0.1996  0.1098  -0.1019 681 GLU A CD  
5072  O OE1 . GLU A 681 ? 1.4420 1.5435 1.5042 0.2169  0.1111  -0.0925 681 GLU A OE1 
5073  O OE2 . GLU A 681 ? 1.4016 1.5135 1.4819 0.1834  0.1219  -0.1005 681 GLU A OE2 
5074  N N   . THR A 682 ? 1.5258 1.8607 1.6974 0.2835  0.0972  -0.1182 682 THR A N   
5075  C CA  . THR A 682 ? 1.2773 1.6925 1.4796 0.3070  0.1028  -0.1245 682 THR A CA  
5076  C C   . THR A 682 ? 1.3459 1.8237 1.5652 0.3336  0.0894  -0.1270 682 THR A C   
5077  O O   . THR A 682 ? 1.4757 2.0367 1.7381 0.3329  0.0803  -0.1415 682 THR A O   
5078  C CB  . THR A 682 ? 1.2173 1.6096 1.3899 0.3358  0.1273  -0.1118 682 THR A CB  
5079  O OG1 . THR A 682 ? 1.4919 1.8340 1.6495 0.3074  0.1394  -0.1123 682 THR A OG1 
5080  C CG2 . THR A 682 ? 1.2226 1.7038 1.4276 0.3675  0.1337  -0.1153 682 THR A CG2 
5081  N N   . ILE A 683 ? 1.4152 1.8544 1.5992 0.3549  0.0883  -0.1131 683 ILE A N   
5082  C CA  . ILE A 683 ? 1.3185 1.8116 1.5106 0.3809  0.0761  -0.1124 683 ILE A CA  
5083  C C   . ILE A 683 ? 1.2570 1.7757 1.4774 0.3509  0.0546  -0.1304 683 ILE A C   
5084  O O   . ILE A 683 ? 1.1684 1.7681 1.4264 0.3510  0.0428  -0.1461 683 ILE A O   
5085  C CB  . ILE A 683 ? 1.2301 1.6668 1.3711 0.4118  0.0845  -0.0897 683 ILE A CB  
5086  C CG1 . ILE A 683 ? 1.2007 1.6176 1.3158 0.4479  0.1076  -0.0734 683 ILE A CG1 
5087  C CG2 . ILE A 683 ? 1.2090 1.6968 1.3547 0.4334  0.0701  -0.0881 683 ILE A CG2 
5088  C CD1 . ILE A 683 ? 1.3787 1.6975 1.4336 0.4606  0.1232  -0.0531 683 ILE A CD1 
5089  N N   . ALA A 684 ? 1.3237 1.7755 1.5267 0.3250  0.0502  -0.1292 684 ALA A N   
5090  C CA  . ALA A 684 ? 1.2994 1.7646 1.5271 0.2982  0.0326  -0.1456 684 ALA A CA  
5091  C C   . ALA A 684 ? 1.2444 1.6291 1.4489 0.2748  0.0316  -0.1384 684 ALA A C   
5092  O O   . ALA A 684 ? 1.3115 1.6359 1.4751 0.2834  0.0421  -0.1200 684 ALA A O   
5093  C CB  . ALA A 684 ? 1.2315 1.7498 1.4631 0.3197  0.0213  -0.1495 684 ALA A CB  
5094  N N   . THR A 685 ? 1.3835 1.7680 1.6142 0.2454  0.0193  -0.1530 685 THR A N   
5095  C CA  . THR A 685 ? 1.3935 1.7132 1.6096 0.2238  0.0160  -0.1463 685 THR A CA  
5096  C C   . THR A 685 ? 1.3698 1.7033 1.5935 0.2246  0.0041  -0.1537 685 THR A C   
5097  O O   . THR A 685 ? 1.3313 1.6209 1.5305 0.2232  0.0043  -0.1417 685 THR A O   
5098  C CB  . THR A 685 ? 1.4179 1.7167 1.6560 0.1904  0.0138  -0.1533 685 THR A CB  
5099  O OG1 . THR A 685 ? 1.7737 2.1255 2.0555 0.1787  0.0047  -0.1758 685 THR A OG1 
5100  C CG2 . THR A 685 ? 1.3842 1.6625 1.6085 0.1871  0.0274  -0.1446 685 THR A CG2 
5101  N N   . GLU A 686 ? 1.3019 1.6983 1.5588 0.2252  -0.0054 -0.1745 686 GLU A N   
5102  C CA  . GLU A 686 ? 1.2099 1.6261 1.4751 0.2261  -0.0154 -0.1856 686 GLU A CA  
5103  C C   . GLU A 686 ? 1.2904 1.6979 1.5180 0.2522  -0.0118 -0.1684 686 GLU A C   
5104  O O   . GLU A 686 ? 1.4528 1.8817 1.6618 0.2783  -0.0059 -0.1580 686 GLU A O   
5105  C CB  . GLU A 686 ? 1.1999 1.6915 1.5002 0.2252  -0.0239 -0.2119 686 GLU A CB  
5106  C CG  . GLU A 686 ? 1.2556 1.7770 1.5614 0.2287  -0.0328 -0.2266 686 GLU A CG  
5107  C CD  . GLU A 686 ? 1.4950 1.9754 1.8118 0.2077  -0.0365 -0.2340 686 GLU A CD  
5108  O OE1 . GLU A 686 ? 1.6259 2.0713 1.9609 0.1847  -0.0361 -0.2367 686 GLU A OE1 
5109  O OE2 . GLU A 686 ? 1.5209 2.0058 1.8282 0.2155  -0.0391 -0.2360 686 GLU A OE2 
5110  N N   . SER A 687 ? 1.3046 1.6810 1.5215 0.2455  -0.0143 -0.1644 687 SER A N   
5111  C CA  . SER A 687 ? 1.2053 1.5678 1.3853 0.2651  -0.0097 -0.1474 687 SER A CA  
5112  C C   . SER A 687 ? 1.2779 1.7009 1.4513 0.2934  -0.0114 -0.1499 687 SER A C   
5113  O O   . SER A 687 ? 1.3904 1.8020 1.5287 0.3178  -0.0030 -0.1294 687 SER A O   
5114  C CB  . SER A 687 ? 1.0653 1.4061 1.2472 0.2507  -0.0138 -0.1495 687 SER A CB  
5115  O OG  . SER A 687 ? 1.4765 1.8676 1.6881 0.2481  -0.0230 -0.1732 687 SER A OG  
5116  N N   . GLU A 688 ? 1.3243 1.8102 1.5289 0.2904  -0.0220 -0.1743 688 GLU A N   
5117  C CA  . GLU A 688 ? 1.1834 1.7360 1.3823 0.3155  -0.0263 -0.1778 688 GLU A CA  
5118  C C   . GLU A 688 ? 1.1549 1.7317 1.3461 0.3394  -0.0214 -0.1652 688 GLU A C   
5119  O O   . GLU A 688 ? 1.2220 1.8201 1.3867 0.3699  -0.0188 -0.1491 688 GLU A O   
5120  C CB  . GLU A 688 ? 1.2191 1.8358 1.4549 0.3020  -0.0386 -0.2108 688 GLU A CB  
5121  C CG  . GLU A 688 ? 1.4033 2.0206 1.6385 0.2937  -0.0426 -0.2232 688 GLU A CG  
5122  C CD  . GLU A 688 ? 1.3320 2.0267 1.5759 0.3003  -0.0520 -0.2458 688 GLU A CD  
5123  O OE1 . GLU A 688 ? 1.4150 2.1560 1.6905 0.2879  -0.0593 -0.2707 688 GLU A OE1 
5124  O OE2 . GLU A 688 ? 1.2419 1.9519 1.4593 0.3161  -0.0518 -0.2389 688 GLU A OE2 
5125  N N   . GLU A 689 ? 1.2533 1.8280 1.4674 0.3270  -0.0191 -0.1713 689 GLU A N   
5126  C CA  . GLU A 689 ? 1.3334 1.9339 1.5447 0.3497  -0.0125 -0.1604 689 GLU A CA  
5127  C C   . GLU A 689 ? 1.4082 1.9397 1.5755 0.3687  0.0033  -0.1303 689 GLU A C   
5128  O O   . GLU A 689 ? 1.5719 2.1211 1.7222 0.4014  0.0105  -0.1146 689 GLU A O   
5129  C CB  . GLU A 689 ? 1.5087 2.1276 1.7576 0.3276  -0.0129 -0.1768 689 GLU A CB  
5130  C CG  . GLU A 689 ? 1.4784 2.1733 1.7696 0.3114  -0.0264 -0.2071 689 GLU A CG  
5131  C CD  . GLU A 689 ? 1.6776 2.3940 2.0052 0.2886  -0.0251 -0.2223 689 GLU A CD  
5132  O OE1 . GLU A 689 ? 1.6605 2.3185 1.9836 0.2747  -0.0155 -0.2132 689 GLU A OE1 
5133  O OE2 . GLU A 689 ? 1.6330 2.4262 1.9923 0.2827  -0.0336 -0.2436 689 GLU A OE2 
5134  N N   . VAL A 690 ? 1.2346 1.6884 1.3832 0.3488  0.0090  -0.1224 690 VAL A N   
5135  C CA  . VAL A 690 ? 1.2618 1.6436 1.3658 0.3604  0.0247  -0.0970 690 VAL A CA  
5136  C C   . VAL A 690 ? 1.3603 1.7369 1.4270 0.3885  0.0285  -0.0786 690 VAL A C   
5137  O O   . VAL A 690 ? 1.4805 1.8332 1.5148 0.4164  0.0417  -0.0581 690 VAL A O   
5138  C CB  . VAL A 690 ? 1.2895 1.5971 1.3841 0.3275  0.0276  -0.0948 690 VAL A CB  
5139  C CG1 . VAL A 690 ? 1.3596 1.5921 1.4026 0.3358  0.0431  -0.0707 690 VAL A CG1 
5140  C CG2 . VAL A 690 ? 1.2790 1.5833 1.4009 0.3041  0.0272  -0.1064 690 VAL A CG2 
5141  N N   . VAL A 691 ? 1.3590 1.7563 1.4288 0.3823  0.0187  -0.0852 691 VAL A N   
5142  C CA  . VAL A 691 ? 1.1775 1.5712 1.2099 0.4070  0.0228  -0.0667 691 VAL A CA  
5143  C C   . VAL A 691 ? 1.4038 1.8602 1.4335 0.4458  0.0215  -0.0594 691 VAL A C   
5144  O O   . VAL A 691 ? 1.5370 1.9722 1.5270 0.4751  0.0313  -0.0346 691 VAL A O   
5145  C CB  . VAL A 691 ? 1.0967 1.5013 1.1312 0.3921  0.0144  -0.0752 691 VAL A CB  
5146  C CG1 . VAL A 691 ? 0.9875 1.3316 1.0237 0.3582  0.0164  -0.0778 691 VAL A CG1 
5147  C CG2 . VAL A 691 ? 1.1451 1.6328 1.2194 0.3876  -0.0017 -0.1026 691 VAL A CG2 
5148  N N   . LYS A 692 ? 1.5612 2.0944 1.6322 0.4460  0.0099  -0.0798 692 LYS A N   
5149  C CA  . LYS A 692 ? 1.5104 2.1160 1.5845 0.4819  0.0063  -0.0737 692 LYS A CA  
5150  C C   . LYS A 692 ? 1.5388 2.1104 1.5917 0.5107  0.0229  -0.0503 692 LYS A C   
5151  O O   . LYS A 692 ? 1.7003 2.2808 1.7252 0.5497  0.0286  -0.0273 692 LYS A O   
5152  C CB  . LYS A 692 ? 1.4621 2.1563 1.5881 0.4685  -0.0091 -0.1034 692 LYS A CB  
5153  C CG  . LYS A 692 ? 1.6248 2.4099 1.7590 0.5032  -0.0163 -0.0992 692 LYS A CG  
5154  C CD  . LYS A 692 ? 1.7627 2.6339 1.9495 0.4842  -0.0302 -0.1303 692 LYS A CD  
5155  C CE  . LYS A 692 ? 1.7170 2.6870 1.9149 0.5176  -0.0385 -0.1257 692 LYS A CE  
5156  N NZ  . LYS A 692 ? 1.5831 2.6395 1.8330 0.4945  -0.0516 -0.1575 692 LYS A NZ  
5157  N N   . PHE A 693 ? 1.3884 1.9193 1.4529 0.4926  0.0316  -0.0557 693 PHE A N   
5158  C CA  . PHE A 693 ? 1.3506 1.8434 1.3952 0.5166  0.0500  -0.0375 693 PHE A CA  
5159  C C   . PHE A 693 ? 1.5135 1.9207 1.4995 0.5352  0.0666  -0.0090 693 PHE A C   
5160  O O   . PHE A 693 ? 1.6596 2.0539 1.6203 0.5738  0.0803  0.0122  693 PHE A O   
5161  C CB  . PHE A 693 ? 1.3352 1.7922 1.3981 0.4852  0.0562  -0.0507 693 PHE A CB  
5162  C CG  . PHE A 693 ? 1.3811 1.7778 1.4155 0.5020  0.0785  -0.0342 693 PHE A CG  
5163  C CD1 . PHE A 693 ? 1.2824 1.7243 1.3310 0.5326  0.0865  -0.0305 693 PHE A CD1 
5164  C CD2 . PHE A 693 ? 1.4133 1.7106 1.4076 0.4858  0.0919  -0.0242 693 PHE A CD2 
5165  C CE1 . PHE A 693 ? 1.2875 1.6717 1.3090 0.5492  0.1095  -0.0174 693 PHE A CE1 
5166  C CE2 . PHE A 693 ? 1.4804 1.7191 1.4451 0.4995  0.1138  -0.0122 693 PHE A CE2 
5167  C CZ  . PHE A 693 ? 1.4434 1.7235 1.4211 0.5322  0.1234  -0.0090 693 PHE A CZ  
5168  N N   . LEU A 694 ? 1.4311 1.7800 1.3964 0.5075  0.0661  -0.0087 694 LEU A N   
5169  C CA  . LEU A 694 ? 1.4731 1.7381 1.3829 0.5160  0.0816  0.0158  694 LEU A CA  
5170  C C   . LEU A 694 ? 1.5644 1.8560 1.4481 0.5550  0.0821  0.0366  694 LEU A C   
5171  O O   . LEU A 694 ? 1.6322 1.8657 1.4703 0.5811  0.0998  0.0624  694 LEU A O   
5172  C CB  . LEU A 694 ? 1.5165 1.7361 1.4200 0.4747  0.0772  0.0085  694 LEU A CB  
5173  C CG  . LEU A 694 ? 1.4854 1.6214 1.3722 0.4438  0.0879  0.0085  694 LEU A CG  
5174  C CD1 . LEU A 694 ? 1.4765 1.6270 1.3968 0.4288  0.0857  -0.0084 694 LEU A CD1 
5175  C CD2 . LEU A 694 ? 1.2042 1.3158 1.0908 0.4080  0.0804  0.0027  694 LEU A CD2 
5176  N N   . GLU A 695 ? 1.5907 1.9664 1.5001 0.5581  0.0635  0.0256  695 GLU A N   
5177  C CA  . GLU A 695 ? 1.5709 1.9832 1.4563 0.5941  0.0611  0.0451  695 GLU A CA  
5178  C C   . GLU A 695 ? 1.6405 2.0904 1.5254 0.6417  0.0664  0.0614  695 GLU A C   
5179  O O   . GLU A 695 ? 1.6934 2.1223 1.5383 0.6794  0.0765  0.0909  695 GLU A O   
5180  C CB  . GLU A 695 ? 1.3290 1.8284 1.2438 0.5819  0.0390  0.0245  695 GLU A CB  
5181  C CG  . GLU A 695 ? 1.4926 1.9585 1.3992 0.5468  0.0363  0.0154  695 GLU A CG  
5182  C CD  . GLU A 695 ? 1.6719 2.2146 1.6160 0.5258  0.0166  -0.0143 695 GLU A CD  
5183  O OE1 . GLU A 695 ? 1.7655 2.3897 1.7434 0.5338  0.0034  -0.0307 695 GLU A OE1 
5184  O OE2 . GLU A 695 ? 1.3769 1.8989 1.3167 0.5006  0.0151  -0.0223 695 GLU A OE2 
5185  N N   . GLU A 696 ? 1.6092 2.1150 1.5388 0.6406  0.0603  0.0434  696 GLU A N   
5186  C CA  . GLU A 696 ? 1.7193 2.2735 1.6579 0.6851  0.0648  0.0563  696 GLU A CA  
5187  C C   . GLU A 696 ? 1.7919 2.2538 1.6876 0.7126  0.0918  0.0830  696 GLU A C   
5188  O O   . GLU A 696 ? 1.8973 2.3677 1.7710 0.7615  0.1001  0.1094  696 GLU A O   
5189  C CB  . GLU A 696 ? 1.7813 2.4057 1.7779 0.6693  0.0558  0.0290  696 GLU A CB  
5190  C CG  . GLU A 696 ? 1.9013 2.6262 1.9419 0.6475  0.0303  0.0016  696 GLU A CG  
5191  C CD  . GLU A 696 ? 2.0372 2.8105 2.1323 0.6172  0.0231  -0.0288 696 GLU A CD  
5192  O OE1 . GLU A 696 ? 1.9920 2.7262 2.0923 0.6142  0.0378  -0.0278 696 GLU A OE1 
5193  O OE2 . GLU A 696 ? 2.1139 2.9625 2.2446 0.5950  0.0038  -0.0542 696 GLU A OE2 
5194  N N   . LYS A 697 ? 1.7093 2.0826 1.5917 0.6818  0.1058  0.0763  697 LYS A N   
5195  C CA  . LYS A 697 ? 1.7893 2.0666 1.6282 0.7012  0.1332  0.0966  697 LYS A CA  
5196  C C   . LYS A 697 ? 1.9027 2.0972 1.6804 0.7123  0.1460  0.1235  697 LYS A C   
5197  O O   . LYS A 697 ? 2.0982 2.2461 1.8382 0.7529  0.1656  0.1495  697 LYS A O   
5198  C CB  . LYS A 697 ? 1.6596 1.8740 1.5024 0.6602  0.1425  0.0785  697 LYS A CB  
5199  C CG  . LYS A 697 ? 1.5737 1.8557 1.4706 0.6496  0.1355  0.0552  697 LYS A CG  
5200  C CD  . LYS A 697 ? 1.7375 2.0178 1.6319 0.6884  0.1556  0.0652  697 LYS A CD  
5201  C CE  . LYS A 697 ? 1.6210 1.9971 1.5750 0.6850  0.1460  0.0448  697 LYS A CE  
5202  N NZ  . LYS A 697 ? 1.5400 1.9223 1.4952 0.7246  0.1667  0.0543  697 LYS A NZ  
5203  N N   . GLY A 698 ? 1.6805 1.8519 1.4485 0.6749  0.1371  0.1168  698 GLY A N   
5204  C CA  . GLY A 698 ? 1.5864 1.6775 1.2967 0.6775  0.1503  0.1408  698 GLY A CA  
5205  C C   . GLY A 698 ? 1.5669 1.5499 1.2466 0.6396  0.1665  0.1375  698 GLY A C   
5206  O O   . GLY A 698 ? 1.5462 1.4404 1.1750 0.6560  0.1905  0.1585  698 GLY A O   
5207  N N   . HIS A 699 ? 1.8326 1.8221 1.5410 0.5908  0.1541  0.1123  699 HIS A N   
5208  C CA  . HIS A 699 ? 1.8223 1.7195 1.5053 0.5499  0.1659  0.1075  699 HIS A CA  
5209  C C   . HIS A 699 ? 1.8837 1.7174 1.5190 0.5386  0.1748  0.1253  699 HIS A C   
5210  O O   . HIS A 699 ? 1.9548 1.8351 1.5965 0.5410  0.1627  0.1292  699 HIS A O   
5211  C CB  . HIS A 699 ? 1.6635 1.5958 1.3931 0.5046  0.1474  0.0789  699 HIS A CB  
5212  C CG  . HIS A 699 ? 1.7069 1.5703 1.4249 0.4713  0.1571  0.0702  699 HIS A CG  
5213  N ND1 . HIS A 699 ? 1.7764 1.6528 1.5185 0.4682  0.1581  0.0563  699 HIS A ND1 
5214  C CD2 . HIS A 699 ? 1.7845 1.5706 1.4693 0.4377  0.1654  0.0729  699 HIS A CD2 
5215  C CE1 . HIS A 699 ? 1.8965 1.7035 1.6175 0.4348  0.1667  0.0515  699 HIS A CE1 
5216  N NE2 . HIS A 699 ? 1.9382 1.6909 1.6248 0.4155  0.1706  0.0610  699 HIS A NE2 
5217  N N   . PRO A 700 ? 1.7861 1.5159 1.3725 0.5237  0.1964  0.1353  700 PRO A N   
5218  C CA  . PRO A 700 ? 1.8364 1.5042 1.3779 0.5065  0.2061  0.1510  700 PRO A CA  
5219  C C   . PRO A 700 ? 1.6917 1.3980 1.2629 0.4624  0.1867  0.1351  700 PRO A C   
5220  O O   . PRO A 700 ? 1.7640 1.4699 1.3176 0.4580  0.1868  0.1466  700 PRO A O   
5221  C CB  . PRO A 700 ? 1.9325 1.4888 1.4269 0.4870  0.2301  0.1545  700 PRO A CB  
5222  C CG  . PRO A 700 ? 1.7879 1.3604 1.3141 0.4776  0.2257  0.1327  700 PRO A CG  
5223  C CD  . PRO A 700 ? 1.8069 1.4727 1.3764 0.5192  0.2135  0.1304  700 PRO A CD  
5224  N N   . ALA A 701 ? 1.7913 1.5290 1.4058 0.4323  0.1719  0.1103  701 ALA A N   
5225  C CA  . ALA A 701 ? 1.7721 1.5408 1.4151 0.3928  0.1553  0.0962  701 ALA A CA  
5226  C C   . ALA A 701 ? 1.6902 1.5326 1.3526 0.4074  0.1421  0.0974  701 ALA A C   
5227  O O   . ALA A 701 ? 1.6625 1.5086 1.3251 0.3829  0.1380  0.0965  701 ALA A O   
5228  C CB  . ALA A 701 ? 1.4913 1.2959 1.1835 0.3681  0.1394  0.0712  701 ALA A CB  
5229  N N   . LEU A 702 ? 1.6142 1.5182 1.2924 0.4464  0.1358  0.0991  702 LEU A N   
5230  C CA  . LEU A 702 ? 1.5539 1.5319 1.2471 0.4607  0.1229  0.0988  702 LEU A CA  
5231  C C   . LEU A 702 ? 1.6056 1.5445 1.2466 0.4719  0.1369  0.1258  702 LEU A C   
5232  O O   . LEU A 702 ? 1.5213 1.4959 1.1664 0.4619  0.1297  0.1241  702 LEU A O   
5233  C CB  . LEU A 702 ? 1.5216 1.5766 1.2405 0.4994  0.1128  0.0953  702 LEU A CB  
5234  C CG  . LEU A 702 ? 1.4372 1.5423 1.2097 0.4909  0.0993  0.0689  702 LEU A CG  
5235  C CD1 . LEU A 702 ? 1.3848 1.5776 1.1819 0.5267  0.0883  0.0660  702 LEU A CD1 
5236  C CD2 . LEU A 702 ? 1.2163 1.3484 1.0299 0.4491  0.0836  0.0424  702 LEU A CD2 
5237  N N   . LYS A 703 ? 1.7755 1.6393 1.3662 0.4926  0.1583  0.1505  703 LYS A N   
5238  C CA  . LYS A 703 ? 1.7523 1.5664 1.2876 0.5033  0.1747  0.1793  703 LYS A CA  
5239  C C   . LYS A 703 ? 1.7079 1.4354 1.2106 0.4600  0.1897  0.1832  703 LYS A C   
5240  O O   . LYS A 703 ? 1.7366 1.4112 1.1901 0.4620  0.2063  0.2070  703 LYS A O   
5241  C CB  . LYS A 703 ? 1.8488 1.6264 1.3449 0.5531  0.1913  0.2064  703 LYS A CB  
5242  C CG  . LYS A 703 ? 1.7865 1.6593 1.3116 0.5977  0.1760  0.2072  703 LYS A CG  
5243  C CD  . LYS A 703 ? 2.2527 2.0928 1.7393 0.6513  0.1926  0.2380  703 LYS A CD  
5244  C CE  . LYS A 703 ? 2.2287 2.1726 1.7414 0.6956  0.1758  0.2424  703 LYS A CE  
5245  N NZ  . LYS A 703 ? 2.1809 2.0971 1.6603 0.7522  0.1916  0.2742  703 LYS A NZ  
5246  N N   . MET A 704 ? 1.7238 1.4393 1.2531 0.4200  0.1835  0.1610  704 MET A N   
5247  C CA  . MET A 704 ? 1.6748 1.3207 1.1793 0.3751  0.1943  0.1618  704 MET A CA  
5248  C C   . MET A 704 ? 1.6759 1.3686 1.2009 0.3472  0.1835  0.1557  704 MET A C   
5249  O O   . MET A 704 ? 1.6398 1.4161 1.2012 0.3605  0.1670  0.1461  704 MET A O   
5250  C CB  . MET A 704 ? 1.5951 1.2193 1.1217 0.3449  0.1896  0.1411  704 MET A CB  
5251  C CG  . MET A 704 ? 1.7139 1.2483 1.1966 0.3508  0.2108  0.1494  704 MET A CG  
5252  S SD  . MET A 704 ? 1.7972 1.3234 1.3086 0.3198  0.2025  0.1239  704 MET A SD  
5253  C CE  . MET A 704 ? 1.8932 1.2919 1.3341 0.2971  0.2312  0.1340  704 MET A CE  
5254  N N   . ASP A 705 ? 1.7827 1.4241 1.2850 0.3076  0.1934  0.1598  705 ASP A N   
5255  C CA  . ASP A 705 ? 1.6930 1.3785 1.2159 0.2798  0.1857  0.1543  705 ASP A CA  
5256  C C   . ASP A 705 ? 1.6334 1.3883 1.2230 0.2610  0.1619  0.1253  705 ASP A C   
5257  O O   . ASP A 705 ? 1.6774 1.4215 1.2857 0.2554  0.1553  0.1127  705 ASP A O   
5258  C CB  . ASP A 705 ? 1.7244 1.3397 1.2095 0.2388  0.2024  0.1650  705 ASP A CB  
5259  C CG  . ASP A 705 ? 2.0732 1.6023 1.4882 0.2526  0.2289  0.1931  705 ASP A CG  
5260  O OD1 . ASP A 705 ? 2.0035 1.5412 1.3941 0.2676  0.2371  0.2117  705 ASP A OD1 
5261  O OD2 . ASP A 705 ? 2.2831 1.7336 1.6654 0.2487  0.2425  0.1968  705 ASP A OD2 
5262  N N   . PRO A 706 ? 1.5301 1.3535 1.1555 0.2511  0.1499  0.1144  706 PRO A N   
5263  C CA  . PRO A 706 ? 1.4532 1.3340 1.1408 0.2352  0.1291  0.0878  706 PRO A CA  
5264  C C   . PRO A 706 ? 1.5596 1.3992 1.2548 0.1972  0.1276  0.0818  706 PRO A C   
5265  O O   . PRO A 706 ? 1.5918 1.3950 1.2649 0.1672  0.1372  0.0909  706 PRO A O   
5266  C CB  . PRO A 706 ? 1.2972 1.2405 1.0092 0.2283  0.1237  0.0811  706 PRO A CB  
5267  C CG  . PRO A 706 ? 1.3463 1.2857 1.0148 0.2521  0.1368  0.1012  706 PRO A CG  
5268  C CD  . PRO A 706 ? 1.5262 1.3766 1.1366 0.2544  0.1560  0.1253  706 PRO A CD  
5269  N N   . ILE A 707 ? 1.4778 1.3244 1.2023 0.1972  0.1157  0.0672  707 ILE A N   
5270  C CA  . ILE A 707 ? 1.4228 1.2347 1.1535 0.1628  0.1122  0.0617  707 ILE A CA  
5271  C C   . ILE A 707 ? 1.3692 1.2098 1.1294 0.1283  0.1037  0.0559  707 ILE A C   
5272  O O   . ILE A 707 ? 1.4049 1.2049 1.1465 0.0952  0.1085  0.0617  707 ILE A O   
5273  C CB  . ILE A 707 ? 1.3985 1.2240 1.1596 0.1706  0.0999  0.0470  707 ILE A CB  
5274  C CG1 . ILE A 707 ? 1.3368 1.1165 1.0909 0.1361  0.0988  0.0451  707 ILE A CG1 
5275  C CG2 . ILE A 707 ? 1.2116 1.1165 1.0334 0.1789  0.0806  0.0280  707 ILE A CG2 
5276  C CD1 . ILE A 707 ? 1.3634 1.1287 1.1223 0.1439  0.0959  0.0375  707 ILE A CD1 
5277  N N   . MET A 708 ? 1.3130 1.2247 1.1186 0.1359  0.0917  0.0439  708 MET A N   
5278  C CA  . MET A 708 ? 1.2180 1.1651 1.0573 0.1092  0.0844  0.0381  708 MET A CA  
5279  C C   . MET A 708 ? 1.2205 1.1937 1.0490 0.1133  0.0944  0.0451  708 MET A C   
5280  O O   . MET A 708 ? 1.1910 1.2107 1.0335 0.1395  0.0919  0.0378  708 MET A O   
5281  C CB  . MET A 708 ? 1.2617 1.2672 1.1637 0.1139  0.0649  0.0174  708 MET A CB  
5282  C CG  . MET A 708 ? 1.1488 1.1393 1.0724 0.0899  0.0533  0.0132  708 MET A CG  
5283  S SD  . MET A 708 ? 1.0804 1.1353 1.0774 0.0931  0.0329  -0.0074 708 MET A SD  
5284  C CE  . MET A 708 ? 1.0911 1.1825 1.1118 0.0725  0.0331  -0.0049 708 MET A CE  
5285  N N   . GLU B 3   ? 1.0272 1.1703 1.4607 -0.0057 -0.0115 -0.0443 3   GLU B N   
5286  C CA  . GLU B 3   ? 1.0988 1.2212 1.4903 -0.0021 -0.0008 -0.0284 3   GLU B CA  
5287  C C   . GLU B 3   ? 1.1746 1.3012 1.5520 0.0124  -0.0004 -0.0240 3   GLU B C   
5288  O O   . GLU B 3   ? 1.2634 1.4116 1.6665 0.0134  0.0021  -0.0300 3   GLU B O   
5289  C CB  . GLU B 3   ? 1.1788 1.2996 1.5714 -0.0195 0.0215  -0.0194 3   GLU B CB  
5290  C CG  . GLU B 3   ? 1.3036 1.4004 1.6544 -0.0175 0.0300  -0.0040 3   GLU B CG  
5291  C CD  . GLU B 3   ? 1.3771 1.4686 1.7247 -0.0336 0.0497  0.0051  3   GLU B CD  
5292  O OE1 . GLU B 3   ? 1.3237 1.4281 1.7007 -0.0482 0.0583  -0.0001 3   GLU B OE1 
5293  O OE2 . GLU B 3   ? 1.3938 1.4677 1.7096 -0.0316 0.0566  0.0173  3   GLU B OE2 
5294  N N   . LYS B 4   ? 0.9935 1.0991 1.3310 0.0237  -0.0023 -0.0140 4   LYS B N   
5295  C CA  . LYS B 4   ? 0.8636 0.9697 1.1849 0.0371  -0.0013 -0.0088 4   LYS B CA  
5296  C C   . LYS B 4   ? 0.8144 0.9271 1.1359 0.0290  0.0194  0.0001  4   LYS B C   
5297  O O   . LYS B 4   ? 0.8646 0.9712 1.1815 0.0163  0.0322  0.0066  4   LYS B O   
5298  C CB  . LYS B 4   ? 0.8216 0.9025 1.1014 0.0503  -0.0084 -0.0011 4   LYS B CB  
5299  C CG  . LYS B 4   ? 1.1146 1.1939 1.3787 0.0665  -0.0129 0.0015  4   LYS B CG  
5300  C CD  . LYS B 4   ? 1.1054 1.1608 1.3330 0.0808  -0.0239 0.0052  4   LYS B CD  
5301  C CE  . LYS B 4   ? 1.0456 1.0819 1.2428 0.0788  -0.0124 0.0180  4   LYS B CE  
5302  N NZ  . LYS B 4   ? 0.9399 0.9567 1.1024 0.0942  -0.0178 0.0235  4   LYS B NZ  
5303  N N   . ALA B 5   ? 0.6324 0.7560 0.9576 0.0367  0.0222  0.0003  5   ALA B N   
5304  C CA  . ALA B 5   ? 0.5312 0.6605 0.8552 0.0304  0.0406  0.0077  5   ALA B CA  
5305  C C   . ALA B 5   ? 0.5896 0.6972 0.8768 0.0312  0.0483  0.0216  5   ALA B C   
5306  O O   . ALA B 5   ? 0.7140 0.8056 0.9761 0.0424  0.0394  0.0257  5   ALA B O   
5307  C CB  . ALA B 5   ? 0.5550 0.6978 0.8885 0.0405  0.0396  0.0043  5   ALA B CB  
5308  N N   . LYS B 6   ? 0.4915 0.5985 0.7752 0.0198  0.0646  0.0288  6   LYS B N   
5309  C CA  . LYS B 6   ? 0.4915 0.5785 0.7425 0.0201  0.0711  0.0415  6   LYS B CA  
5310  C C   . LYS B 6   ? 0.6235 0.7092 0.8598 0.0300  0.0744  0.0472  6   LYS B C   
5311  O O   . LYS B 6   ? 0.7172 0.7864 0.9270 0.0359  0.0739  0.0557  6   LYS B O   
5312  C CB  . LYS B 6   ? 0.6025 0.6869 0.8535 0.0045  0.0856  0.0468  6   LYS B CB  
5313  C CG  . LYS B 6   ? 0.7330 0.8143 0.9953 -0.0068 0.0840  0.0431  6   LYS B CG  
5314  C CD  . LYS B 6   ? 0.6166 0.6872 0.8685 -0.0202 0.0973  0.0513  6   LYS B CD  
5315  C CE  . LYS B 6   ? 0.7662 0.8268 1.0223 -0.0296 0.0941  0.0495  6   LYS B CE  
5316  N NZ  . LYS B 6   ? 1.2368 1.2887 1.4870 -0.0443 0.1084  0.0565  6   LYS B NZ  
5317  N N   . SER B 7   ? 0.6272 0.7296 0.8810 0.0318  0.0778  0.0423  7   SER B N   
5318  C CA  . SER B 7   ? 0.5352 0.6365 0.7772 0.0403  0.0813  0.0469  7   SER B CA  
5319  C C   . SER B 7   ? 0.5109 0.6307 0.7763 0.0458  0.0789  0.0378  7   SER B C   
5320  O O   . SER B 7   ? 0.5295 0.6656 0.8228 0.0408  0.0776  0.0282  7   SER B O   
5321  C CB  . SER B 7   ? 0.5754 0.6734 0.8070 0.0315  0.0966  0.0549  7   SER B CB  
5322  O OG  . SER B 7   ? 0.5964 0.6949 0.8202 0.0383  0.1005  0.0580  7   SER B OG  
5323  N N   . ILE B 8   ? 0.5994 0.7167 0.8548 0.0561  0.0785  0.0406  8   ILE B N   
5324  C CA  . ILE B 8   ? 0.4977 0.6305 0.7732 0.0629  0.0762  0.0326  8   ILE B CA  
5325  C C   . ILE B 8   ? 0.5276 0.6698 0.8099 0.0560  0.0918  0.0336  8   ILE B C   
5326  O O   . ILE B 8   ? 0.6430 0.8028 0.9496 0.0566  0.0939  0.0251  8   ILE B O   
5327  C CB  . ILE B 8   ? 0.4154 0.5380 0.6760 0.0795  0.0648  0.0341  8   ILE B CB  
5328  C CG1 . ILE B 8   ? 0.5970 0.7031 0.8295 0.0826  0.0719  0.0456  8   ILE B CG1 
5329  C CG2 . ILE B 8   ? 0.5054 0.6182 0.7579 0.0864  0.0495  0.0321  8   ILE B CG2 
5330  C CD1 . ILE B 8   ? 0.5987 0.6978 0.8214 0.0967  0.0658  0.0468  8   ILE B CD1 
5331  N N   . ASP B 9   ? 0.5075 0.6380 0.7685 0.0500  0.1022  0.0434  9   ASP B N   
5332  C CA  . ASP B 9   ? 0.5479 0.6835 0.8093 0.0437  0.1164  0.0450  9   ASP B CA  
5333  C C   . ASP B 9   ? 0.5881 0.7378 0.8695 0.0302  0.1272  0.0396  9   ASP B C   
5334  O O   . ASP B 9   ? 0.6185 0.7637 0.8979 0.0208  0.1290  0.0419  9   ASP B O   
5335  C CB  . ASP B 9   ? 0.5880 0.7057 0.8203 0.0416  0.1218  0.0565  9   ASP B CB  
5336  C CG  . ASP B 9   ? 0.7376 0.8572 0.9654 0.0358  0.1348  0.0587  9   ASP B CG  
5337  O OD1 . ASP B 9   ? 0.8924 1.0250 1.1355 0.0377  0.1391  0.0519  9   ASP B OD1 
5338  O OD2 . ASP B 9   ? 0.8696 0.9771 1.0781 0.0300  0.1402  0.0666  9   ASP B OD2 
5339  N N   . GLN B 10  ? 0.6419 0.8077 0.9422 0.0291  0.1353  0.0327  10  GLN B N   
5340  C CA  . GLN B 10  ? 0.5042 0.6842 0.8247 0.0162  0.1479  0.0271  10  GLN B CA  
5341  C C   . GLN B 10  ? 0.5881 0.7565 0.8878 0.0039  0.1617  0.0356  10  GLN B C   
5342  O O   . GLN B 10  ? 0.6902 0.8609 0.9973 -0.0082 0.1690  0.0350  10  GLN B O   
5343  C CB  . GLN B 10  ? 0.5574 0.7574 0.9028 0.0191  0.1540  0.0171  10  GLN B CB  
5344  C CG  . GLN B 10  ? 0.5682 0.7891 0.9475 0.0091  0.1620  0.0070  10  GLN B CG  
5345  C CD  . GLN B 10  ? 0.7925 1.0207 1.1930 0.0106  0.1481  0.0006  10  GLN B CD  
5346  O OE1 . GLN B 10  ? 0.6999 0.9245 1.0986 0.0234  0.1311  -0.0008 10  GLN B OE1 
5347  N NE2 . GLN B 10  ? 0.8874 1.1245 1.3075 -0.0025 0.1548  -0.0035 10  GLN B NE2 
5348  N N   . ALA B 11  ? 0.5968 0.7518 0.8705 0.0069  0.1648  0.0434  11  ALA B N   
5349  C CA  . ALA B 11  ? 0.5872 0.7291 0.8382 -0.0032 0.1758  0.0516  11  ALA B CA  
5350  C C   . ALA B 11  ? 0.5363 0.6642 0.7749 -0.0089 0.1711  0.0584  11  ALA B C   
5351  O O   . ALA B 11  ? 0.5587 0.6814 0.7919 -0.0207 0.1803  0.0615  11  ALA B O   
5352  C CB  . ALA B 11  ? 0.5041 0.6340 0.7311 0.0029  0.1760  0.0580  11  ALA B CB  
5353  N N   . THR B 12  ? 0.4854 0.6061 0.7190 -0.0001 0.1571  0.0606  12  THR B N   
5354  C CA  . THR B 12  ? 0.4608 0.5677 0.6830 -0.0033 0.1510  0.0661  12  THR B CA  
5355  C C   . THR B 12  ? 0.5684 0.6838 0.8117 -0.0128 0.1524  0.0600  12  THR B C   
5356  O O   . THR B 12  ? 0.6377 0.7427 0.8726 -0.0226 0.1565  0.0646  12  THR B O   
5357  C CB  . THR B 12  ? 0.5172 0.6167 0.7317 0.0095  0.1365  0.0678  12  THR B CB  
5358  O OG1 . THR B 12  ? 0.7267 0.8172 0.9220 0.0164  0.1370  0.0742  12  THR B OG1 
5359  C CG2 . THR B 12  ? 0.5595 0.6460 0.7646 0.0079  0.1293  0.0715  12  THR B CG2 
5360  N N   . LEU B 13  ? 0.5480 0.6819 0.8198 -0.0100 0.1487  0.0495  13  LEU B N   
5361  C CA  . LEU B 13  ? 0.4650 0.6097 0.7623 -0.0190 0.1493  0.0421  13  LEU B CA  
5362  C C   . LEU B 13  ? 0.5497 0.6989 0.8531 -0.0342 0.1675  0.0422  13  LEU B C   
5363  O O   . LEU B 13  ? 0.5730 0.7197 0.8834 -0.0456 0.1712  0.0420  13  LEU B O   
5364  C CB  . LEU B 13  ? 0.4177 0.5829 0.7461 -0.0112 0.1402  0.0298  13  LEU B CB  
5365  C CG  . LEU B 13  ? 0.4139 0.5730 0.7356 0.0038  0.1213  0.0289  13  LEU B CG  
5366  C CD1 . LEU B 13  ? 0.4776 0.6546 0.8234 0.0141  0.1135  0.0184  13  LEU B CD1 
5367  C CD2 . LEU B 13  ? 0.5884 0.7393 0.9102 0.0013  0.1108  0.0281  13  LEU B CD2 
5368  N N   . GLN B 14  ? 0.5099 0.6639 0.8089 -0.0346 0.1793  0.0428  14  GLN B N   
5369  C CA  . GLN B 14  ? 0.4846 0.6408 0.7849 -0.0483 0.1980  0.0433  14  GLN B CA  
5370  C C   . GLN B 14  ? 0.4683 0.6008 0.7388 -0.0574 0.2027  0.0548  14  GLN B C   
5371  O O   . GLN B 14  ? 0.5017 0.6320 0.7779 -0.0704 0.2116  0.0551  14  GLN B O   
5372  C CB  . GLN B 14  ? 0.4432 0.6056 0.7385 -0.0450 0.2084  0.0420  14  GLN B CB  
5373  C CG  . GLN B 14  ? 0.4756 0.6638 0.8055 -0.0403 0.2100  0.0292  14  GLN B CG  
5374  C CD  . GLN B 14  ? 0.6155 0.8081 0.9391 -0.0367 0.2203  0.0276  14  GLN B CD  
5375  O OE1 . GLN B 14  ? 0.6029 0.7817 0.8995 -0.0417 0.2308  0.0348  14  GLN B OE1 
5376  N NE2 . GLN B 14  ? 0.5514 0.7623 0.8993 -0.0272 0.2167  0.0178  14  GLN B NE2 
5377  N N   . LEU B 15  ? 0.5774 0.6921 0.8173 -0.0505 0.1967  0.0640  15  LEU B N   
5378  C CA  . LEU B 15  ? 0.5935 0.6850 0.8043 -0.0570 0.1992  0.0748  15  LEU B CA  
5379  C C   . LEU B 15  ? 0.6476 0.7298 0.8605 -0.0604 0.1905  0.0766  15  LEU B C   
5380  O O   . LEU B 15  ? 0.7740 0.8395 0.9708 -0.0696 0.1956  0.0834  15  LEU B O   
5381  C CB  . LEU B 15  ? 0.4656 0.5427 0.6474 -0.0480 0.1939  0.0829  15  LEU B CB  
5382  C CG  . LEU B 15  ? 0.4690 0.5480 0.6400 -0.0478 0.2042  0.0833  15  LEU B CG  
5383  C CD1 . LEU B 15  ? 0.4937 0.5656 0.6479 -0.0362 0.1955  0.0874  15  LEU B CD1 
5384  C CD2 . LEU B 15  ? 0.4907 0.5553 0.6403 -0.0595 0.2171  0.0895  15  LEU B CD2 
5385  N N   . LEU B 16  ? 0.6142 0.7054 0.8454 -0.0529 0.1773  0.0702  16  LEU B N   
5386  C CA  . LEU B 16  ? 0.4671 0.5496 0.7013 -0.0560 0.1687  0.0704  16  LEU B CA  
5387  C C   . LEU B 16  ? 0.6002 0.6884 0.8542 -0.0717 0.1792  0.0661  16  LEU B C   
5388  O O   . LEU B 16  ? 0.5867 0.6599 0.8332 -0.0797 0.1791  0.0703  16  LEU B O   
5389  C CB  . LEU B 16  ? 0.4554 0.5465 0.7043 -0.0442 0.1523  0.0633  16  LEU B CB  
5390  C CG  . LEU B 16  ? 0.4489 0.5266 0.6743 -0.0308 0.1406  0.0693  16  LEU B CG  
5391  C CD1 . LEU B 16  ? 0.6265 0.7146 0.8649 -0.0180 0.1272  0.0618  16  LEU B CD1 
5392  C CD2 . LEU B 16  ? 0.5636 0.6202 0.7703 -0.0332 0.1355  0.0760  16  LEU B CD2 
5393  N N   . ASP B 17  ? 0.5674 0.6767 0.8471 -0.0762 0.1893  0.0579  17  ASP B N   
5394  C CA  . ASP B 17  ? 0.5586 0.6752 0.8597 -0.0919 0.2021  0.0536  17  ASP B CA  
5395  C C   . ASP B 17  ? 0.5359 0.6325 0.8087 -0.1031 0.2173  0.0643  17  ASP B C   
5396  O O   . ASP B 17  ? 0.7371 0.8222 1.0088 -0.1152 0.2224  0.0673  17  ASP B O   
5397  C CB  . ASP B 17  ? 0.6963 0.8411 1.0311 -0.0930 0.2108  0.0422  17  ASP B CB  
5398  C CG  . ASP B 17  ? 0.7652 0.9304 1.1323 -0.0834 0.1955  0.0302  17  ASP B CG  
5399  O OD1 . ASP B 17  ? 0.8535 1.0197 1.2374 -0.0868 0.1863  0.0256  17  ASP B OD1 
5400  O OD2 . ASP B 17  ? 0.9028 1.0820 1.2779 -0.0722 0.1922  0.0252  17  ASP B OD2 
5401  N N   . LYS B 18  ? 0.6460 0.7363 0.8940 -0.0988 0.2237  0.0703  18  LYS B N   
5402  C CA  . LYS B 18  ? 0.6165 0.6856 0.8332 -0.1077 0.2365  0.0807  18  LYS B CA  
5403  C C   . LYS B 18  ? 0.6381 0.6810 0.8299 -0.1087 0.2276  0.0904  18  LYS B C   
5404  O O   . LYS B 18  ? 0.7057 0.7317 0.8837 -0.1205 0.2369  0.0967  18  LYS B O   
5405  C CB  . LYS B 18  ? 0.5298 0.5960 0.7233 -0.1003 0.2404  0.0846  18  LYS B CB  
5406  C CG  . LYS B 18  ? 0.5903 0.6330 0.7483 -0.1084 0.2521  0.0950  18  LYS B CG  
5407  C CD  . LYS B 18  ? 0.5679 0.6089 0.7049 -0.1019 0.2562  0.0970  18  LYS B CD  
5408  C CE  . LYS B 18  ? 0.6680 0.6887 0.7729 -0.1111 0.2705  0.1049  18  LYS B CE  
5409  N NZ  . LYS B 18  ? 0.6281 0.6200 0.7003 -0.1115 0.2626  0.1166  18  LYS B NZ  
5410  N N   . ALA B 19  ? 0.6401 0.6788 0.8260 -0.0962 0.2102  0.0917  19  ALA B N   
5411  C CA  . ALA B 19  ? 0.6440 0.6589 0.8081 -0.0953 0.2008  0.0998  19  ALA B CA  
5412  C C   . ALA B 19  ? 0.6414 0.6510 0.8193 -0.1071 0.2021  0.0979  19  ALA B C   
5413  O O   . ALA B 19  ? 0.7150 0.7014 0.8724 -0.1136 0.2038  0.1060  19  ALA B O   
5414  C CB  . ALA B 19  ? 0.5426 0.5584 0.7046 -0.0800 0.1833  0.0990  19  ALA B CB  
5415  N N   . LYS B 20  ? 0.6110 0.6417 0.8244 -0.1097 0.2009  0.0868  20  LYS B N   
5416  C CA  . LYS B 20  ? 0.6298 0.6588 0.8624 -0.1215 0.2018  0.0828  20  LYS B CA  
5417  C C   . LYS B 20  ? 0.5762 0.5975 0.8052 -0.1387 0.2219  0.0869  20  LYS B C   
5418  O O   . LYS B 20  ? 0.6735 0.6744 0.8920 -0.1484 0.2243  0.0926  20  LYS B O   
5419  C CB  . LYS B 20  ? 0.5379 0.5943 0.8118 -0.1195 0.1954  0.0686  20  LYS B CB  
5420  C CG  . LYS B 20  ? 0.5475 0.6030 0.8441 -0.1291 0.1911  0.0626  20  LYS B CG  
5421  C CD  . LYS B 20  ? 0.8628 0.9486 1.2047 -0.1314 0.1907  0.0479  20  LYS B CD  
5422  C CE  . LYS B 20  ? 0.7647 0.8526 1.1302 -0.1337 0.1769  0.0393  20  LYS B CE  
5423  N NZ  . LYS B 20  ? 0.8705 0.9880 1.2834 -0.1388 0.1784  0.0248  20  LYS B NZ  
5424  N N   . GLN B 21  ? 0.6228 0.6587 0.8585 -0.1421 0.2369  0.0845  21  GLN B N   
5425  C CA  . GLN B 21  ? 0.6866 0.7156 0.9170 -0.1581 0.2586  0.0883  21  GLN B CA  
5426  C C   . GLN B 21  ? 0.6445 0.6402 0.8290 -0.1605 0.2623  0.1029  21  GLN B C   
5427  O O   . GLN B 21  ? 0.7965 0.7744 0.9713 -0.1744 0.2735  0.1085  21  GLN B O   
5428  C CB  . GLN B 21  ? 0.7698 0.8206 1.0126 -0.1581 0.2727  0.0825  21  GLN B CB  
5429  C CG  . GLN B 21  ? 1.0625 1.1466 1.3547 -0.1588 0.2727  0.0675  21  GLN B CG  
5430  C CD  . GLN B 21  ? 1.3405 1.4468 1.6428 -0.1482 0.2745  0.0608  21  GLN B CD  
5431  O OE1 . GLN B 21  ? 1.3532 1.4521 1.6290 -0.1453 0.2830  0.0664  21  GLN B OE1 
5432  N NE2 . GLN B 21  ? 1.1591 1.2924 1.4999 -0.1418 0.2657  0.0481  21  GLN B NE2 
5433  N N   . ASP B 22  ? 0.7260 0.7126 0.8828 -0.1473 0.2526  0.1088  22  ASP B N   
5434  C CA  . ASP B 22  ? 0.7684 0.7240 0.8823 -0.1473 0.2528  0.1220  22  ASP B CA  
5435  C C   . ASP B 22  ? 0.7593 0.6928 0.8637 -0.1483 0.2412  0.1273  22  ASP B C   
5436  O O   . ASP B 22  ? 0.9259 0.8314 0.9981 -0.1513 0.2426  0.1380  22  ASP B O   
5437  C CB  . ASP B 22  ? 0.8050 0.7597 0.8973 -0.1321 0.2438  0.1252  22  ASP B CB  
5438  C CG  . ASP B 22  ? 0.8646 0.8328 0.9554 -0.1312 0.2558  0.1223  22  ASP B CG  
5439  O OD1 . ASP B 22  ? 0.8274 0.8049 0.9315 -0.1424 0.2728  0.1182  22  ASP B OD1 
5440  O OD2 . ASP B 22  ? 0.6988 0.6682 0.7760 -0.1194 0.2485  0.1236  22  ASP B OD2 
5441  N N   . GLY B 23  ? 0.7194 0.6646 0.8506 -0.1450 0.2292  0.1197  23  GLY B N   
5442  C CA  . GLY B 23  ? 0.6510 0.5770 0.7761 -0.1451 0.2175  0.1229  23  GLY B CA  
5443  C C   . GLY B 23  ? 0.7626 0.6740 0.8613 -0.1303 0.2025  0.1294  23  GLY B C   
5444  O O   . GLY B 23  ? 0.9133 0.7981 0.9882 -0.1314 0.1987  0.1378  23  GLY B O   
5445  N N   . VAL B 24  ? 0.7041 0.6325 0.8076 -0.1163 0.1940  0.1254  24  VAL B N   
5446  C CA  . VAL B 24  ? 0.7213 0.6390 0.8035 -0.1021 0.1809  0.1307  24  VAL B CA  
5447  C C   . VAL B 24  ? 0.8472 0.7771 0.9467 -0.0906 0.1660  0.1234  24  VAL B C   
5448  O O   . VAL B 24  ? 0.9131 0.8646 1.0399 -0.0903 0.1652  0.1137  24  VAL B O   
5449  C CB  . VAL B 24  ? 0.6290 0.5491 0.6933 -0.0954 0.1844  0.1350  24  VAL B CB  
5450  C CG1 . VAL B 24  ? 0.7244 0.6273 0.7647 -0.1056 0.1975  0.1430  24  VAL B CG1 
5451  C CG2 . VAL B 24  ? 0.6137 0.5618 0.7000 -0.0910 0.1873  0.1263  24  VAL B CG2 
5452  N N   . GLU B 25  ? 0.6678 0.5831 0.7509 -0.0807 0.1542  0.1278  25  GLU B N   
5453  C CA  . GLU B 25  ? 0.6066 0.5291 0.7002 -0.0692 0.1408  0.1219  25  GLU B CA  
5454  C C   . GLU B 25  ? 0.7229 0.6594 0.8159 -0.0562 0.1370  0.1207  25  GLU B C   
5455  O O   . GLU B 25  ? 0.8098 0.7422 0.8863 -0.0531 0.1404  0.1269  25  GLU B O   
5456  C CB  . GLU B 25  ? 0.7162 0.6158 0.7926 -0.0645 0.1311  0.1268  25  GLU B CB  
5457  C CG  . GLU B 25  ? 1.0802 0.9716 1.1672 -0.0709 0.1266  0.1223  25  GLU B CG  
5458  C CD  . GLU B 25  ? 1.3902 1.2618 1.4625 -0.0629 0.1153  0.1249  25  GLU B CD  
5459  O OE1 . GLU B 25  ? 1.3692 1.2284 1.4203 -0.0559 0.1135  0.1326  25  GLU B OE1 
5460  O OE2 . GLU B 25  ? 1.3621 1.2308 1.4448 -0.0635 0.1080  0.1185  25  GLU B OE2 
5461  N N   . THR B 26  ? 0.7647 0.7164 0.8749 -0.0484 0.1293  0.1126  26  THR B N   
5462  C CA  . THR B 26  ? 0.6160 0.5797 0.7264 -0.0358 0.1253  0.1111  26  THR B CA  
5463  C C   . THR B 26  ? 0.6361 0.5960 0.7450 -0.0241 0.1127  0.1084  26  THR B C   
5464  O O   . THR B 26  ? 0.7356 0.6876 0.8477 -0.0263 0.1068  0.1054  26  THR B O   
5465  C CB  . THR B 26  ? 0.5699 0.5568 0.7023 -0.0371 0.1301  0.1035  26  THR B CB  
5466  O OG1 . THR B 26  ? 0.7407 0.7372 0.8948 -0.0379 0.1238  0.0942  26  THR B OG1 
5467  C CG2 . THR B 26  ? 0.7940 0.7851 0.9286 -0.0490 0.1443  0.1050  26  THR B CG2 
5468  N N   . VAL B 27  ? 0.6425 0.6068 0.7455 -0.0120 0.1090  0.1094  27  VAL B N   
5469  C CA  . VAL B 27  ? 0.6062 0.5663 0.7048 -0.0001 0.0987  0.1073  27  VAL B CA  
5470  C C   . VAL B 27  ? 0.6807 0.6482 0.7957 0.0002  0.0913  0.0975  27  VAL B C   
5471  O O   . VAL B 27  ? 0.7727 0.7305 0.8823 0.0058  0.0826  0.0952  27  VAL B O   
5472  C CB  . VAL B 27  ? 0.4926 0.4583 0.5849 0.0113  0.0985  0.1096  27  VAL B CB  
5473  C CG1 . VAL B 27  ? 0.5296 0.5141 0.6373 0.0124  0.1007  0.1041  27  VAL B CG1 
5474  C CG2 . VAL B 27  ? 0.5585 0.5159 0.6410 0.0234  0.0904  0.1094  27  VAL B CG2 
5475  N N   . TRP B 28  ? 0.6314 0.6159 0.7671 -0.0057 0.0945  0.0912  28  TRP B N   
5476  C CA  . TRP B 28  ? 0.6180 0.6115 0.7730 -0.0058 0.0865  0.0809  28  TRP B CA  
5477  C C   . TRP B 28  ? 0.7005 0.6839 0.8602 -0.0158 0.0845  0.0787  28  TRP B C   
5478  O O   . TRP B 28  ? 0.7951 0.7763 0.9607 -0.0126 0.0738  0.0717  28  TRP B O   
5479  C CB  . TRP B 28  ? 0.6245 0.6400 0.8035 -0.0100 0.0914  0.0744  28  TRP B CB  
5480  C CG  . TRP B 28  ? 0.6024 0.6285 0.7808 0.0012  0.0901  0.0737  28  TRP B CG  
5481  C CD1 . TRP B 28  ? 0.4874 0.5198 0.6713 0.0125  0.0795  0.0673  28  TRP B CD1 
5482  C CD2 . TRP B 28  ? 0.6472 0.6775 0.8190 0.0021  0.0995  0.0792  28  TRP B CD2 
5483  N NE1 . TRP B 28  ? 0.7066 0.7462 0.8877 0.0202  0.0823  0.0692  28  TRP B NE1 
5484  C CE2 . TRP B 28  ? 0.6108 0.6497 0.7853 0.0138  0.0945  0.0761  28  TRP B CE2 
5485  C CE3 . TRP B 28  ? 0.6063 0.6320 0.7681 -0.0054 0.1109  0.0865  28  TRP B CE3 
5486  C CZ2 . TRP B 28  ? 0.5542 0.5981 0.7242 0.0174  0.1009  0.0796  28  TRP B CZ2 
5487  C CZ3 . TRP B 28  ? 0.4435 0.4748 0.6004 -0.0015 0.1166  0.0894  28  TRP B CZ3 
5488  C CH2 . TRP B 28  ? 0.5072 0.5477 0.6691 0.0095  0.1118  0.0858  28  TRP B CH2 
5489  N N   . ASP B 29  ? 0.7816 0.7574 0.9376 -0.0280 0.0946  0.0845  29  ASP B N   
5490  C CA  . ASP B 29  ? 0.7732 0.7368 0.9324 -0.0388 0.0942  0.0837  29  ASP B CA  
5491  C C   . ASP B 29  ? 0.6823 0.6249 0.8216 -0.0313 0.0848  0.0866  29  ASP B C   
5492  O O   . ASP B 29  ? 0.6545 0.5906 0.7999 -0.0327 0.0766  0.0807  29  ASP B O   
5493  C CB  . ASP B 29  ? 0.6115 0.5679 0.7654 -0.0524 0.1080  0.0911  29  ASP B CB  
5494  C CG  . ASP B 29  ? 0.8298 0.8055 1.0011 -0.0604 0.1197  0.0884  29  ASP B CG  
5495  O OD1 . ASP B 29  ? 0.8967 0.8929 1.0878 -0.0555 0.1165  0.0801  29  ASP B OD1 
5496  O OD2 . ASP B 29  ? 1.0028 0.9723 1.1669 -0.0709 0.1320  0.0946  29  ASP B OD2 
5497  N N   . ARG B 30  ? 0.6536 0.5863 0.7707 -0.0230 0.0858  0.0950  30  ARG B N   
5498  C CA  . ARG B 30  ? 0.6733 0.5870 0.7720 -0.0149 0.0783  0.0978  30  ARG B CA  
5499  C C   . ARG B 30  ? 0.7460 0.6626 0.8458 -0.0027 0.0669  0.0904  30  ARG B C   
5500  O O   . ARG B 30  ? 0.8730 0.7747 0.9637 0.0015  0.0594  0.0886  30  ARG B O   
5501  C CB  . ARG B 30  ? 0.6305 0.5354 0.7090 -0.0090 0.0825  0.1078  30  ARG B CB  
5502  C CG  . ARG B 30  ? 0.6509 0.5456 0.7216 -0.0199 0.0910  0.1157  30  ARG B CG  
5503  C CD  . ARG B 30  ? 0.7986 0.6827 0.8497 -0.0129 0.0919  0.1245  30  ARG B CD  
5504  N NE  . ARG B 30  ? 0.7432 0.6419 0.7949 -0.0057 0.0946  0.1255  30  ARG B NE  
5505  C CZ  . ARG B 30  ? 0.7880 0.6966 0.8422 -0.0108 0.1026  0.1278  30  ARG B CZ  
5506  N NH1 . ARG B 30  ? 0.8704 0.7761 0.9256 -0.0234 0.1098  0.1296  30  ARG B NH1 
5507  N NH2 . ARG B 30  ? 0.5910 0.5115 0.6460 -0.0036 0.1040  0.1282  30  ARG B NH2 
5508  N N   . LYS B 31  ? 0.7452 0.6791 0.8545 0.0035  0.0654  0.0859  31  LYS B N   
5509  C CA  . LYS B 31  ? 0.6719 0.6068 0.7795 0.0155  0.0543  0.0789  31  LYS B CA  
5510  C C   . LYS B 31  ? 0.7377 0.6720 0.8599 0.0100  0.0454  0.0690  31  LYS B C   
5511  O O   . LYS B 31  ? 0.8139 0.7368 0.9270 0.0173  0.0352  0.0646  31  LYS B O   
5512  C CB  . LYS B 31  ? 0.5663 0.5186 0.6810 0.0227  0.0545  0.0766  31  LYS B CB  
5513  C CG  . LYS B 31  ? 0.6683 0.6217 0.7819 0.0344  0.0421  0.0686  31  LYS B CG  
5514  C CD  . LYS B 31  ? 0.7881 0.7252 0.8758 0.0475  0.0385  0.0723  31  LYS B CD  
5515  C CE  . LYS B 31  ? 0.8084 0.7449 0.8898 0.0604  0.0276  0.0658  31  LYS B CE  
5516  N NZ  . LYS B 31  ? 0.8903 0.8211 0.9764 0.0597  0.0152  0.0559  31  LYS B NZ  
5517  N N   . ALA B 32  ? 0.6416 0.5882 0.7870 -0.0029 0.0495  0.0650  32  ALA B N   
5518  C CA  . ALA B 32  ? 0.5949 0.5431 0.7593 -0.0100 0.0417  0.0549  32  ALA B CA  
5519  C C   . ALA B 32  ? 0.7546 0.6803 0.9077 -0.0147 0.0391  0.0567  32  ALA B C   
5520  O O   . ALA B 32  ? 0.8852 0.8040 1.0411 -0.0125 0.0274  0.0485  32  ALA B O   
5521  C CB  . ALA B 32  ? 0.6110 0.5768 0.8034 -0.0243 0.0502  0.0516  32  ALA B CB  
5522  N N   . ASP B 33  ? 0.7734 0.6864 0.9126 -0.0204 0.0490  0.0672  33  ASP B N   
5523  C CA  . ASP B 33  ? 0.8381 0.7276 0.9649 -0.0245 0.0471  0.0701  33  ASP B CA  
5524  C C   . ASP B 33  ? 0.7582 0.6327 0.8654 -0.0102 0.0363  0.0683  33  ASP B C   
5525  O O   . ASP B 33  ? 0.9211 0.7782 1.0235 -0.0120 0.0301  0.0656  33  ASP B O   
5526  C CB  . ASP B 33  ? 0.8080 0.6864 0.9205 -0.0306 0.0589  0.0824  33  ASP B CB  
5527  C CG  . ASP B 33  ? 1.1521 1.0381 1.2792 -0.0468 0.0707  0.0847  33  ASP B CG  
5528  O OD1 . ASP B 33  ? 1.1759 1.0695 1.3256 -0.0569 0.0700  0.0768  33  ASP B OD1 
5529  O OD2 . ASP B 33  ? 1.0045 0.8884 1.1204 -0.0495 0.0809  0.0940  33  ASP B OD2 
5530  N N   . MET B 34  ? 0.7817 0.6618 0.8773 0.0039  0.0346  0.0698  34  MET B N   
5531  C CA  . MET B 34  ? 0.7840 0.6504 0.8597 0.0181  0.0264  0.0683  34  MET B CA  
5532  C C   . MET B 34  ? 0.8527 0.7187 0.9339 0.0228  0.0126  0.0558  34  MET B C   
5533  O O   . MET B 34  ? 0.9052 0.7570 0.9684 0.0340  0.0053  0.0532  34  MET B O   
5534  C CB  . MET B 34  ? 0.7072 0.5794 0.7692 0.0307  0.0308  0.0741  34  MET B CB  
5535  C CG  . MET B 34  ? 0.5779 0.4329 0.6167 0.0413  0.0311  0.0793  34  MET B CG  
5536  S SD  . MET B 34  ? 0.8361 0.6723 0.8673 0.0340  0.0358  0.0869  34  MET B SD  
5537  C CE  . MET B 34  ? 0.8620 0.7108 0.8994 0.0258  0.0480  0.0967  34  MET B CE  
5538  N N   . LYS B 35  ? 0.8863 0.7676 0.9922 0.0147  0.0088  0.0477  35  LYS B N   
5539  C CA  . LYS B 35  ? 0.7570 0.6398 0.8721 0.0180  -0.0059 0.0346  35  LYS B CA  
5540  C C   . LYS B 35  ? 0.8546 0.7316 0.9477 0.0366  -0.0150 0.0318  35  LYS B C   
5541  O O   . LYS B 35  ? 0.8774 0.7616 0.9614 0.0446  -0.0093 0.0378  35  LYS B O   
5542  C CB  . LYS B 35  ? 0.6814 0.5479 0.8007 0.0091  -0.0117 0.0295  35  LYS B CB  
5543  C CG  . LYS B 35  ? 0.8637 0.7305 0.9988 -0.0092 -0.0008 0.0344  35  LYS B CG  
5544  C CD  . LYS B 35  ? 0.7704 0.6583 0.9397 -0.0217 0.0000  0.0269  35  LYS B CD  
5545  C CE  . LYS B 35  ? 0.9466 0.8367 1.1279 -0.0389 0.0154  0.0343  35  LYS B CE  
5546  N NZ  . LYS B 35  ? 1.0818 0.9466 1.2510 -0.0467 0.0178  0.0393  35  LYS B NZ  
5547  N N   . VAL B 36  ? 0.9105 0.7734 0.9938 0.0433  -0.0285 0.0230  36  VAL B N   
5548  C CA  . VAL B 36  ? 0.8171 0.6717 0.8755 0.0611  -0.0360 0.0208  36  VAL B CA  
5549  C C   . VAL B 36  ? 0.8196 0.6583 0.8517 0.0681  -0.0266 0.0309  36  VAL B C   
5550  O O   . VAL B 36  ? 0.8989 0.7210 0.9233 0.0655  -0.0265 0.0315  36  VAL B O   
5551  C CB  . VAL B 36  ? 0.7149 0.5583 0.7689 0.0666  -0.0538 0.0075  36  VAL B CB  
5552  C CG1 . VAL B 36  ? 0.6769 0.5059 0.6976 0.0853  -0.0592 0.0068  36  VAL B CG1 
5553  C CG2 . VAL B 36  ? 0.8831 0.7450 0.9654 0.0617  -0.0646 -0.0034 36  VAL B CG2 
5554  N N   . GLN B 37  ? 0.8465 0.6924 0.8693 0.0752  -0.0176 0.0391  37  GLN B N   
5555  C CA  . GLN B 37  ? 0.9137 0.7480 0.9156 0.0817  -0.0075 0.0488  37  GLN B CA  
5556  C C   . GLN B 37  ? 0.9283 0.7429 0.9047 0.0950  -0.0147 0.0440  37  GLN B C   
5557  O O   . GLN B 37  ? 0.9467 0.7587 0.9188 0.1009  -0.0269 0.0345  37  GLN B O   
5558  C CB  . GLN B 37  ? 0.6805 0.5275 0.6804 0.0861  0.0027  0.0572  37  GLN B CB  
5559  C CG  . GLN B 37  ? 0.6697 0.5368 0.6937 0.0744  0.0084  0.0598  37  GLN B CG  
5560  C CD  . GLN B 37  ? 0.5879 0.4624 0.6089 0.0755  0.0211  0.0704  37  GLN B CD  
5561  O OE1 . GLN B 37  ? 0.7937 0.6667 0.8169 0.0686  0.0294  0.0774  37  GLN B OE1 
5562  N NE2 . GLN B 37  ? 0.7400 0.6214 0.7555 0.0845  0.0220  0.0714  37  GLN B NE2 
5563  N N   . CYS B 38  ? 0.8293 0.6305 0.7895 0.1000  -0.0075 0.0499  38  CYS B N   
5564  C CA  . CYS B 38  ? 0.9280 0.7090 0.8634 0.1125  -0.0131 0.0447  38  CYS B CA  
5565  C C   . CYS B 38  ? 0.8985 0.6793 0.8154 0.1263  -0.0153 0.0427  38  CYS B C   
5566  O O   . CYS B 38  ? 0.9671 0.7603 0.8861 0.1281  -0.0071 0.0497  38  CYS B O   
5567  C CB  . CYS B 38  ? 0.7557 0.5244 0.6787 0.1166  -0.0035 0.0515  38  CYS B CB  
5568  S SG  . CYS B 38  ? 1.0436 0.7868 0.9381 0.1306  -0.0104 0.0432  38  CYS B SG  
5569  N N   . GLY B 39  ? 0.9038 0.6690 0.8016 0.1359  -0.0260 0.0337  39  GLY B N   
5570  C CA  . GLY B 39  ? 0.9141 0.6748 0.7893 0.1499  -0.0291 0.0316  39  GLY B CA  
5571  C C   . GLY B 39  ? 0.9605 0.7067 0.8079 0.1623  -0.0181 0.0371  39  GLY B C   
5572  O O   . GLY B 39  ? 1.0975 0.8423 0.9275 0.1723  -0.0143 0.0400  39  GLY B O   
5573  N N   . PHE B 40  ? 0.8605 0.5954 0.7036 0.1620  -0.0127 0.0383  40  PHE B N   
5574  C CA  . PHE B 40  ? 0.8854 0.6090 0.7060 0.1736  -0.0001 0.0436  40  PHE B CA  
5575  C C   . PHE B 40  ? 1.0289 0.7686 0.8614 0.1706  0.0152  0.0555  40  PHE B C   
5576  O O   . PHE B 40  ? 1.1619 0.8992 0.9782 0.1801  0.0249  0.0602  40  PHE B O   
5577  C CB  . PHE B 40  ? 0.9985 0.7066 0.8139 0.1747  0.0008  0.0408  40  PHE B CB  
5578  C CG  . PHE B 40  ? 1.0310 0.7218 0.8339 0.1778  -0.0146 0.0283  40  PHE B CG  
5579  C CD1 . PHE B 40  ? 1.0638 0.7364 0.8348 0.1923  -0.0176 0.0221  40  PHE B CD1 
5580  C CD2 . PHE B 40  ? 1.0258 0.7177 0.8483 0.1660  -0.0259 0.0226  40  PHE B CD2 
5581  C CE1 . PHE B 40  ? 1.0445 0.7005 0.8032 0.1954  -0.0331 0.0097  40  PHE B CE1 
5582  C CE2 . PHE B 40  ? 0.9617 0.6378 0.7745 0.1684  -0.0409 0.0103  40  PHE B CE2 
5583  C CZ  . PHE B 40  ? 0.9386 0.5969 0.7195 0.1833  -0.0453 0.0036  40  PHE B CZ  
5584  N N   . GLY B 41  ? 0.9225 0.6769 0.7816 0.1576  0.0174  0.0602  41  GLY B N   
5585  C CA  . GLY B 41  ? 0.9177 0.6874 0.7893 0.1540  0.0301  0.0706  41  GLY B CA  
5586  C C   . GLY B 41  ? 0.8456 0.6271 0.7179 0.1555  0.0306  0.0726  41  GLY B C   
5587  O O   . GLY B 41  ? 0.9516 0.7386 0.8213 0.1592  0.0418  0.0799  41  GLY B O   
5588  N N   . SER B 42  ? 0.7974 0.5824 0.6742 0.1529  0.0179  0.0655  42  SER B N   
5589  C CA  . SER B 42  ? 0.6644 0.4598 0.5427 0.1550  0.0157  0.0660  42  SER B CA  
5590  C C   . SER B 42  ? 0.8584 0.6404 0.7070 0.1699  0.0178  0.0665  42  SER B C   
5591  O O   . SER B 42  ? 0.9248 0.7128 0.7707 0.1731  0.0249  0.0725  42  SER B O   
5592  C CB  . SER B 42  ? 0.8149 0.6163 0.7063 0.1498  0.0001  0.0566  42  SER B CB  
5593  O OG  . SER B 42  ? 1.0544 0.8685 0.9736 0.1351  0.0001  0.0568  42  SER B OG  
5594  N N   . ALA B 43  ? 0.9082 0.6708 0.7331 0.1790  0.0120  0.0600  43  ALA B N   
5595  C CA  . ALA B 43  ? 0.9977 0.7440 0.7894 0.1936  0.0149  0.0604  43  ALA B CA  
5596  C C   . ALA B 43  ? 0.8855 0.6261 0.6664 0.1985  0.0335  0.0688  43  ALA B C   
5597  O O   . ALA B 43  ? 1.0019 0.7311 0.7576 0.2092  0.0407  0.0716  43  ALA B O   
5598  C CB  . ALA B 43  ? 0.9647 0.6913 0.7333 0.2019  0.0011  0.0495  43  ALA B CB  
5599  N N   . GLY B 44  ? 0.9188 0.6669 0.7188 0.1908  0.0412  0.0726  44  GLY B N   
5600  C CA  . GLY B 44  ? 0.8540 0.6001 0.6506 0.1945  0.0580  0.0796  44  GLY B CA  
5601  C C   . GLY B 44  ? 0.9670 0.6934 0.7413 0.2042  0.0606  0.0751  44  GLY B C   
5602  O O   . GLY B 44  ? 1.1944 0.9164 0.9598 0.2107  0.0753  0.0797  44  GLY B O   
5603  N N   . VAL B 45  ? 0.8593 0.5738 0.6257 0.2052  0.0469  0.0655  45  VAL B N   
5604  C CA  . VAL B 45  ? 0.8993 0.5933 0.6428 0.2151  0.0483  0.0599  45  VAL B CA  
5605  C C   . VAL B 45  ? 1.0380 0.7310 0.7975 0.2097  0.0477  0.0580  45  VAL B C   
5606  O O   . VAL B 45  ? 1.0926 0.7681 0.8364 0.2159  0.0432  0.0504  45  VAL B O   
5607  C CB  . VAL B 45  ? 0.9296 0.6054 0.6453 0.2235  0.0338  0.0496  45  VAL B CB  
5608  C CG1 . VAL B 45  ? 1.1127 0.7815 0.8017 0.2337  0.0382  0.0523  45  VAL B CG1 
5609  C CG2 . VAL B 45  ? 1.0748 0.7576 0.8079 0.2140  0.0148  0.0427  45  VAL B CG2 
5610  N N   . CYS B 46  ? 0.8281 0.5378 0.6164 0.1989  0.0521  0.0647  46  CYS B N   
5611  C CA  . CYS B 46  ? 0.7754 0.4830 0.5778 0.1942  0.0517  0.0642  46  CYS B CA  
5612  C C   . CYS B 46  ? 0.9371 0.6513 0.7473 0.1972  0.0680  0.0721  46  CYS B C   
5613  O O   . CYS B 46  ? 1.0019 0.7320 0.8246 0.1934  0.0758  0.0798  46  CYS B O   
5614  C CB  . CYS B 46  ? 0.8677 0.5868 0.6955 0.1793  0.0426  0.0652  46  CYS B CB  
5615  S SG  . CYS B 46  ? 0.9052 0.6193 0.7486 0.1731  0.0422  0.0665  46  CYS B SG  
5616  N N   . CYS B 47  ? 0.8575 0.5603 0.6619 0.2043  0.0728  0.0696  47  CYS B N   
5617  C CA  . CYS B 47  ? 0.8384 0.5484 0.6532 0.2080  0.0878  0.0758  47  CYS B CA  
5618  C C   . CYS B 47  ? 1.0408 0.7505 0.8737 0.2041  0.0854  0.0764  47  CYS B C   
5619  O O   . CYS B 47  ? 1.0801 0.7743 0.9058 0.2062  0.0773  0.0698  47  CYS B O   
5620  C CB  . CYS B 47  ? 1.0031 0.7011 0.7950 0.2222  0.0995  0.0732  47  CYS B CB  
5621  S SG  . CYS B 47  ? 1.1237 0.8337 0.9316 0.2267  0.1199  0.0803  47  CYS B SG  
5622  N N   . ARG B 48  ? 0.9126 0.6381 0.7680 0.1990  0.0920  0.0842  48  ARG B N   
5623  C CA  . ARG B 48  ? 0.8837 0.6092 0.7561 0.1962  0.0897  0.0859  48  ARG B CA  
5624  C C   . ARG B 48  ? 0.8730 0.6099 0.7595 0.2014  0.1032  0.0910  48  ARG B C   
5625  O O   . ARG B 48  ? 0.8659 0.6133 0.7730 0.1958  0.1024  0.0963  48  ARG B O   
5626  C CB  . ARG B 48  ? 0.9625 0.6959 0.8508 0.1820  0.0802  0.0901  48  ARG B CB  
5627  C CG  . ARG B 48  ? 1.0253 0.7489 0.9053 0.1754  0.0671  0.0847  48  ARG B CG  
5628  C CD  . ARG B 48  ? 1.0696 0.7962 0.9652 0.1619  0.0591  0.0883  48  ARG B CD  
5629  N NE  . ARG B 48  ? 1.4353 1.1762 1.3383 0.1517  0.0571  0.0911  48  ARG B NE  
5630  C CZ  . ARG B 48  ? 1.3341 1.0924 1.2493 0.1473  0.0635  0.0983  48  ARG B CZ  
5631  N NH1 . ARG B 48  ? 1.2448 1.0096 1.1676 0.1517  0.0719  0.1035  48  ARG B NH1 
5632  N NH2 . ARG B 48  ? 1.0170 0.7869 0.9384 0.1386  0.0611  0.0997  48  ARG B NH2 
5633  N N   . ASN B 49  ? 0.8328 0.5671 0.7081 0.2123  0.1153  0.0889  49  ASN B N   
5634  C CA  . ASN B 49  ? 0.8625 0.6094 0.7540 0.2170  0.1298  0.0932  49  ASN B CA  
5635  C C   . ASN B 49  ? 0.8556 0.5950 0.7531 0.2258  0.1322  0.0889  49  ASN B C   
5636  O O   . ASN B 49  ? 0.8541 0.6043 0.7681 0.2305  0.1437  0.0909  49  ASN B O   
5637  C CB  . ASN B 49  ? 0.8061 0.5557 0.6852 0.2229  0.1443  0.0945  49  ASN B CB  
5638  C CG  . ASN B 49  ? 0.9630 0.7241 0.8437 0.2144  0.1437  0.1003  49  ASN B CG  
5639  O OD1 . ASN B 49  ? 1.0320 0.7935 0.9122 0.2060  0.1310  0.1006  49  ASN B OD1 
5640  N ND2 . ASN B 49  ? 1.0674 0.8373 0.9508 0.2165  0.1579  0.1048  49  ASN B ND2 
5641  N N   . CYS B 50  ? 0.7346 0.4565 0.6211 0.2277  0.1213  0.0828  50  CYS B N   
5642  C CA  . CYS B 50  ? 0.8929 0.6064 0.7861 0.2362  0.1219  0.0785  50  CYS B CA  
5643  C C   . CYS B 50  ? 0.8498 0.5455 0.7359 0.2328  0.1056  0.0742  50  CYS B C   
5644  O O   . CYS B 50  ? 0.8786 0.5677 0.7515 0.2258  0.0962  0.0729  50  CYS B O   
5645  C CB  . CYS B 50  ? 0.9578 0.6636 0.8371 0.2503  0.1355  0.0724  50  CYS B CB  
5646  S SG  . CYS B 50  ? 0.8641 0.5431 0.7057 0.2567  0.1290  0.0625  50  CYS B SG  
5647  N N   . SER B 51  ? 0.8085 0.4965 0.7041 0.2378  0.1022  0.0719  51  SER B N   
5648  C CA  . SER B 51  ? 0.8507 0.5202 0.7413 0.2337  0.0868  0.0689  51  SER B CA  
5649  C C   . SER B 51  ? 0.9369 0.5841 0.8027 0.2414  0.0837  0.0587  51  SER B C   
5650  O O   . SER B 51  ? 1.0838 0.7132 0.9447 0.2389  0.0715  0.0549  51  SER B O   
5651  C CB  . SER B 51  ? 0.7793 0.4473 0.6883 0.2362  0.0831  0.0710  51  SER B CB  
5652  O OG  . SER B 51  ? 1.2390 0.8929 1.1427 0.2499  0.0859  0.0631  51  SER B OG  
5653  N N   . MET B 52  ? 0.9397 0.5862 0.7897 0.2508  0.0947  0.0542  52  MET B N   
5654  C CA  . MET B 52  ? 0.9122 0.5362 0.7346 0.2580  0.0905  0.0439  52  MET B CA  
5655  C C   . MET B 52  ? 0.9954 0.6163 0.8075 0.2466  0.0780  0.0439  52  MET B C   
5656  O O   . MET B 52  ? 0.9826 0.5842 0.7784 0.2471  0.0671  0.0358  52  MET B O   
5657  C CB  . MET B 52  ? 0.9163 0.5390 0.7209 0.2709  0.1060  0.0398  52  MET B CB  
5658  C CG  . MET B 52  ? 1.1498 0.7754 0.9659 0.2828  0.1194  0.0382  52  MET B CG  
5659  S SD  . MET B 52  ? 0.9785 0.5886 0.7641 0.3000  0.1344  0.0285  52  MET B SD  
5660  C CE  . MET B 52  ? 0.9040 0.5287 0.6795 0.2970  0.1477  0.0355  52  MET B CE  
5661  N N   . GLY B 53  ? 1.0507 0.6907 0.8742 0.2365  0.0793  0.0520  53  GLY B N   
5662  C CA  . GLY B 53  ? 0.8443 0.4851 0.6627 0.2253  0.0681  0.0521  53  GLY B CA  
5663  C C   . GLY B 53  ? 0.9757 0.6145 0.8093 0.2125  0.0554  0.0546  53  GLY B C   
5664  O O   . GLY B 53  ? 1.1066 0.7384 0.9496 0.2137  0.0538  0.0554  53  GLY B O   
5665  N N   . PRO B 54  ? 1.0253 0.6692 0.8616 0.2002  0.0468  0.0558  54  PRO B N   
5666  C CA  . PRO B 54  ? 0.8665 0.5237 0.6978 0.1982  0.0494  0.0573  54  PRO B CA  
5667  C C   . PRO B 54  ? 1.0262 0.6697 0.8314 0.2071  0.0462  0.0478  54  PRO B C   
5668  O O   . PRO B 54  ? 1.0895 0.7139 0.8834 0.2104  0.0378  0.0394  54  PRO B O   
5669  C CB  . PRO B 54  ? 0.7703 0.4353 0.6151 0.1824  0.0396  0.0600  54  PRO B CB  
5670  C CG  . PRO B 54  ? 0.7704 0.4276 0.6280 0.1756  0.0346  0.0624  54  PRO B CG  
5671  C CD  . PRO B 54  ? 1.0824 0.7198 0.9280 0.1876  0.0346  0.0560  54  PRO B CD  
5672  N N   . CYS B 55  ? 0.9328 0.5847 0.7276 0.2111  0.0524  0.0493  55  CYS B N   
5673  C CA  . CYS B 55  ? 0.9484 0.5860 0.7147 0.2202  0.0483  0.0407  55  CYS B CA  
5674  C C   . CYS B 55  ? 0.9707 0.6185 0.7359 0.2141  0.0419  0.0416  55  CYS B C   
5675  O O   . CYS B 55  ? 1.0089 0.6760 0.7903 0.2077  0.0480  0.0504  55  CYS B O   
5676  C CB  . CYS B 55  ? 0.8523 0.4846 0.5995 0.2348  0.0635  0.0407  55  CYS B CB  
5677  S SG  . CYS B 55  ? 1.0344 0.6606 0.7893 0.2428  0.0742  0.0405  55  CYS B SG  
5678  N N   . ARG B 56  ? 0.8483 0.4833 0.5956 0.2166  0.0291  0.0324  56  ARG B N   
5679  C CA  . ARG B 56  ? 0.9221 0.5659 0.6685 0.2123  0.0208  0.0317  56  ARG B CA  
5680  C C   . ARG B 56  ? 1.0934 0.7192 0.8061 0.2246  0.0142  0.0227  56  ARG B C   
5681  O O   . ARG B 56  ? 1.1635 0.7732 0.8664 0.2260  0.0008  0.0121  56  ARG B O   
5682  C CB  . ARG B 56  ? 0.9319 0.5843 0.7026 0.1972  0.0072  0.0298  56  ARG B CB  
5683  C CG  . ARG B 56  ? 1.1054 0.7413 0.8765 0.1941  -0.0052 0.0205  56  ARG B CG  
5684  C CD  . ARG B 56  ? 1.0387 0.6859 0.8371 0.1776  -0.0149 0.0206  56  ARG B CD  
5685  N NE  . ARG B 56  ? 1.1255 0.7573 0.9287 0.1726  -0.0230 0.0147  56  ARG B NE  
5686  C CZ  . ARG B 56  ? 1.0264 0.6652 0.8537 0.1573  -0.0288 0.0157  56  ARG B CZ  
5687  N NH1 . ARG B 56  ? 1.1615 0.8218 1.0073 0.1479  -0.0266 0.0217  56  ARG B NH1 
5688  N NH2 . ARG B 56  ? 1.4007 1.0244 1.2331 0.1514  -0.0360 0.0110  56  ARG B NH2 
5689  N N   . VAL B 57  ? 0.9715 0.5986 0.6662 0.2330  0.0232  0.0268  57  VAL B N   
5690  C CA  . VAL B 57  ? 0.9778 0.5857 0.6352 0.2459  0.0177  0.0193  57  VAL B CA  
5691  C C   . VAL B 57  ? 1.1939 0.8080 0.8534 0.2415  0.0016  0.0160  57  VAL B C   
5692  O O   . VAL B 57  ? 1.1288 0.7636 0.8192 0.2289  -0.0013 0.0207  57  VAL B O   
5693  C CB  . VAL B 57  ? 1.1291 0.7319 0.7628 0.2577  0.0365  0.0257  57  VAL B CB  
5694  C CG1 . VAL B 57  ? 1.0075 0.6015 0.6362 0.2645  0.0510  0.0258  57  VAL B CG1 
5695  C CG2 . VAL B 57  ? 1.0223 0.6465 0.6739 0.2518  0.0475  0.0378  57  VAL B CG2 
5696  N N   . SER B 58  ? 1.0990 0.6956 0.7268 0.2521  -0.0088 0.0079  58  SER B N   
5697  C CA  . SER B 58  ? 1.1554 0.7571 0.7853 0.2495  -0.0266 0.0031  58  SER B CA  
5698  C C   . SER B 58  ? 1.2375 0.8473 0.8590 0.2536  -0.0185 0.0121  58  SER B C   
5699  O O   . SER B 58  ? 1.4392 1.0350 1.0294 0.2655  -0.0063 0.0159  58  SER B O   
5700  C CB  . SER B 58  ? 1.1741 0.7530 0.7751 0.2589  -0.0448 -0.0107 58  SER B CB  
5701  O OG  . SER B 58  ? 1.3339 0.9160 0.9303 0.2607  -0.0599 -0.0143 58  SER B OG  
5702  N N   . PRO B 59  ? 1.1460 0.7766 0.7938 0.2442  -0.0242 0.0156  59  PRO B N   
5703  C CA  . PRO B 59  ? 1.0902 0.7268 0.7298 0.2483  -0.0187 0.0233  59  PRO B CA  
5704  C C   . PRO B 59  ? 1.2159 0.8330 0.8197 0.2614  -0.0332 0.0157  59  PRO B C   
5705  O O   . PRO B 59  ? 1.4471 1.0589 1.0299 0.2694  -0.0269 0.0219  59  PRO B O   
5706  C CB  . PRO B 59  ? 1.1301 0.7935 0.8103 0.2342  -0.0243 0.0259  59  PRO B CB  
5707  C CG  . PRO B 59  ? 1.1748 0.8404 0.8747 0.2257  -0.0407 0.0152  59  PRO B CG  
5708  C CD  . PRO B 59  ? 1.1836 0.8321 0.8699 0.2291  -0.0353 0.0122  59  PRO B CD  
5709  N N   . VAL B 60  ? 1.2195 0.8253 0.8166 0.2634  -0.0526 0.0025  60  VAL B N   
5710  C CA  . VAL B 60  ? 1.2584 0.8443 0.8207 0.2763  -0.0693 -0.0062 60  VAL B CA  
5711  C C   . VAL B 60  ? 1.3287 0.8850 0.8450 0.2907  -0.0615 -0.0085 60  VAL B C   
5712  O O   . VAL B 60  ? 1.3627 0.9088 0.8766 0.2905  -0.0650 -0.0164 60  VAL B O   
5713  C CB  . VAL B 60  ? 1.1991 0.7880 0.7789 0.2711  -0.0953 -0.0206 60  VAL B CB  
5714  C CG1 . VAL B 60  ? 1.3322 0.8980 0.8737 0.2858  -0.1148 -0.0312 60  VAL B CG1 
5715  C CG2 . VAL B 60  ? 1.1474 0.7661 0.7732 0.2570  -0.1014 -0.0189 60  VAL B CG2 
5716  N N   . PRO B 61  ? 1.3575 0.8984 0.8365 0.3031  -0.0502 -0.0017 61  PRO B N   
5717  C CA  . PRO B 61  ? 1.2962 0.8084 0.7305 0.3167  -0.0408 -0.0041 61  PRO B CA  
5718  C C   . PRO B 61  ? 1.5655 1.0547 0.9728 0.3253  -0.0629 -0.0200 61  PRO B C   
5719  O O   . PRO B 61  ? 1.6589 1.1481 1.0672 0.3261  -0.0861 -0.0280 61  PRO B O   
5720  C CB  . PRO B 61  ? 1.2488 0.7489 0.6485 0.3274  -0.0278 0.0059  61  PRO B CB  
5721  C CG  . PRO B 61  ? 1.1912 0.7175 0.6250 0.3173  -0.0235 0.0161  61  PRO B CG  
5722  C CD  . PRO B 61  ? 1.3834 0.9306 0.8578 0.3054  -0.0443 0.0084  61  PRO B CD  
5723  N N   . GLY B 62  ? 1.6161 1.0858 1.0004 0.3321  -0.0558 -0.0250 62  GLY B N   
5724  C CA  . GLY B 62  ? 1.4238 0.8688 0.7792 0.3411  -0.0753 -0.0407 62  GLY B CA  
5725  C C   . GLY B 62  ? 1.5814 1.0336 0.9689 0.3306  -0.0875 -0.0509 62  GLY B C   
5726  O O   . GLY B 62  ? 1.8534 1.2851 1.2203 0.3370  -0.0891 -0.0600 62  GLY B O   
5727  N N   . LYS B 63  ? 1.9022 1.3821 1.3395 0.3145  -0.0956 -0.0497 63  LYS B N   
5728  C CA  . LYS B 63  ? 1.9617 1.4484 1.4316 0.3028  -0.1069 -0.0586 63  LYS B CA  
5729  C C   . LYS B 63  ? 1.8177 1.3229 1.3235 0.2904  -0.0879 -0.0487 63  LYS B C   
5730  O O   . LYS B 63  ? 1.8325 1.3522 1.3475 0.2881  -0.0690 -0.0352 63  LYS B O   
5731  C CB  . LYS B 63  ? 1.8880 1.3905 1.3883 0.2931  -0.1311 -0.0661 63  LYS B CB  
5732  C CG  . LYS B 63  ? 2.2099 1.6957 1.6783 0.3055  -0.1534 -0.0768 63  LYS B CG  
5733  C CD  . LYS B 63  ? 2.5069 1.9635 1.9446 0.3148  -0.1695 -0.0930 63  LYS B CD  
5734  C CE  . LYS B 63  ? 2.3271 1.7651 1.7291 0.3285  -0.1922 -0.1035 63  LYS B CE  
5735  N NZ  . LYS B 63  ? 1.9398 1.3476 1.3088 0.3384  -0.2074 -0.1195 63  LYS B NZ  
5736  N N   . GLY B 64  ? 1.5258 1.0289 1.0504 0.2829  -0.0937 -0.0558 64  GLY B N   
5737  C CA  . GLY B 64  ? 1.4956 1.0129 1.0527 0.2717  -0.0789 -0.0478 64  GLY B CA  
5738  C C   . GLY B 64  ? 1.4136 0.9215 0.9522 0.2806  -0.0562 -0.0410 64  GLY B C   
5739  O O   . GLY B 64  ? 1.4368 0.9231 0.9346 0.2958  -0.0516 -0.0445 64  GLY B O   
5740  N N   . VAL B 65  ? 1.2472 0.7712 0.8160 0.2714  -0.0415 -0.0314 65  VAL B N   
5741  C CA  . VAL B 65  ? 1.1506 0.6699 0.7100 0.2788  -0.0196 -0.0250 65  VAL B CA  
5742  C C   . VAL B 65  ? 1.2961 0.8215 0.8400 0.2857  -0.0028 -0.0146 65  VAL B C   
5743  O O   . VAL B 65  ? 1.3216 0.8669 0.8845 0.2780  -0.0017 -0.0063 65  VAL B O   
5744  C CB  . VAL B 65  ? 1.1681 0.7026 0.7652 0.2671  -0.0115 -0.0184 65  VAL B CB  
5745  C CG1 . VAL B 65  ? 1.2967 0.8282 0.8871 0.2755  0.0102  -0.0126 65  VAL B CG1 
5746  C CG2 . VAL B 65  ? 1.3206 0.8460 0.9310 0.2600  -0.0274 -0.0281 65  VAL B CG2 
5747  N N   . GLU B 66  ? 1.2030 0.7105 0.7126 0.3001  0.0109  -0.0150 66  GLU B N   
5748  C CA  . GLU B 66  ? 1.1398 0.6489 0.6306 0.3073  0.0283  -0.0055 66  GLU B CA  
5749  C C   . GLU B 66  ? 1.0929 0.6198 0.6070 0.3037  0.0523  0.0068  66  GLU B C   
5750  O O   . GLU B 66  ? 1.2409 0.7812 0.7610 0.3012  0.0624  0.0171  66  GLU B O   
5751  C CB  . GLU B 66  ? 1.2749 0.7539 0.7136 0.3249  0.0322  -0.0122 66  GLU B CB  
5752  C CG  . GLU B 66  ? 1.5682 1.0425 0.9786 0.3330  0.0458  -0.0037 66  GLU B CG  
5753  C CD  . GLU B 66  ? 1.7769 1.2199 1.1335 0.3504  0.0535  -0.0091 66  GLU B CD  
5754  O OE1 . GLU B 66  ? 1.6531 1.0808 0.9977 0.3568  0.0546  -0.0181 66  GLU B OE1 
5755  O OE2 . GLU B 66  ? 1.6535 1.0860 0.9786 0.3580  0.0589  -0.0042 66  GLU B OE2 
5756  N N   . ARG B 67  ? 1.0756 0.6019 0.6026 0.3041  0.0610  0.0054  67  ARG B N   
5757  C CA  . ARG B 67  ? 1.0299 0.5727 0.5798 0.3018  0.0827  0.0156  67  ARG B CA  
5758  C C   . ARG B 67  ? 1.1260 0.6827 0.7152 0.2916  0.0794  0.0164  67  ARG B C   
5759  O O   . ARG B 67  ? 1.0788 0.6270 0.6720 0.2884  0.0636  0.0081  67  ARG B O   
5760  C CB  . ARG B 67  ? 1.0624 0.5889 0.5845 0.3164  0.1023  0.0139  67  ARG B CB  
5761  C CG  . ARG B 67  ? 1.1020 0.6082 0.5771 0.3284  0.1062  0.0123  67  ARG B CG  
5762  C CD  . ARG B 67  ? 1.1435 0.6273 0.5853 0.3436  0.1215  0.0066  67  ARG B CD  
5763  N NE  . ARG B 67  ? 1.3892 0.8804 0.8316 0.3472  0.1492  0.0163  67  ARG B NE  
5764  C CZ  . ARG B 67  ? 1.4292 0.9115 0.8419 0.3533  0.1615  0.0221  67  ARG B CZ  
5765  N NH1 . ARG B 67  ? 1.2569 0.7217 0.6343 0.3577  0.1473  0.0192  67  ARG B NH1 
5766  N NH2 . ARG B 67  ? 1.3228 0.8129 0.7412 0.3550  0.1877  0.0307  67  ARG B NH2 
5767  N N   . GLY B 68  ? 1.0579 0.6345 0.6751 0.2865  0.0942  0.0263  68  GLY B N   
5768  C CA  . GLY B 68  ? 1.0660 0.6550 0.7184 0.2779  0.0924  0.0285  68  GLY B CA  
5769  C C   . GLY B 68  ? 1.1500 0.7257 0.7979 0.2872  0.0987  0.0222  68  GLY B C   
5770  O O   . GLY B 68  ? 0.9981 0.5553 0.6153 0.3001  0.1052  0.0158  68  GLY B O   
5771  N N   . ILE B 69  ? 1.1697 0.7539 0.8470 0.2818  0.0980  0.0241  69  ILE B N   
5772  C CA  . ILE B 69  ? 1.0139 0.5837 0.6871 0.2917  0.1025  0.0171  69  ILE B CA  
5773  C C   . ILE B 69  ? 1.0259 0.5989 0.6929 0.3031  0.1258  0.0195  69  ILE B C   
5774  O O   . ILE B 69  ? 1.1069 0.6618 0.7520 0.3159  0.1321  0.0113  69  ILE B O   
5775  C CB  . ILE B 69  ? 1.0119 0.5879 0.7167 0.2838  0.0948  0.0188  69  ILE B CB  
5776  C CG1 . ILE B 69  ? 0.9451 0.5128 0.6514 0.2733  0.0732  0.0146  69  ILE B CG1 
5777  C CG2 . ILE B 69  ? 1.0701 0.6352 0.7757 0.2949  0.1021  0.0131  69  ILE B CG2 
5778  C CD1 . ILE B 69  ? 0.9967 0.5646 0.7280 0.2660  0.0653  0.0159  69  ILE B CD1 
5779  N N   . CYS B 70  ? 1.0203 0.6148 0.7058 0.2987  0.1387  0.0300  70  CYS B N   
5780  C CA  . CYS B 70  ? 0.9585 0.5575 0.6405 0.3079  0.1622  0.0328  70  CYS B CA  
5781  C C   . CYS B 70  ? 1.0807 0.6639 0.7219 0.3169  0.1708  0.0306  70  CYS B C   
5782  O O   . CYS B 70  ? 1.1117 0.6928 0.7433 0.3261  0.1914  0.0312  70  CYS B O   
5783  C CB  . CYS B 70  ? 0.9220 0.5482 0.6378 0.2994  0.1722  0.0441  70  CYS B CB  
5784  S SG  . CYS B 70  ? 0.8974 0.5364 0.6146 0.2868  0.1648  0.0531  70  CYS B SG  
5785  N N   . GLY B 71  ? 1.1556 0.7279 0.7737 0.3143  0.1553  0.0282  71  GLY B N   
5786  C CA  . GLY B 71  ? 1.0875 0.6425 0.6637 0.3228  0.1598  0.0263  71  GLY B CA  
5787  C C   . GLY B 71  ? 1.0783 0.6452 0.6547 0.3163  0.1622  0.0362  71  GLY B C   
5788  O O   . GLY B 71  ? 1.2052 0.7584 0.7474 0.3235  0.1685  0.0369  71  GLY B O   
5789  N N   . ALA B 72  ? 1.1169 0.7077 0.7301 0.3030  0.1571  0.0439  72  ALA B N   
5790  C CA  . ALA B 72  ? 1.1209 0.7247 0.7390 0.2959  0.1588  0.0532  72  ALA B CA  
5791  C C   . ALA B 72  ? 1.1160 0.7093 0.7115 0.2947  0.1398  0.0498  72  ALA B C   
5792  O O   . ALA B 72  ? 1.0412 0.6346 0.6458 0.2887  0.1201  0.0442  72  ALA B O   
5793  C CB  . ALA B 72  ? 1.1314 0.7622 0.7943 0.2825  0.1571  0.0608  72  ALA B CB  
5794  N N   . THR B 73  ? 1.1504 0.7344 0.7171 0.3004  0.1456  0.0530  73  THR B N   
5795  C CA  . THR B 73  ? 1.0346 0.6086 0.5794 0.3007  0.1272  0.0497  73  THR B CA  
5796  C C   . THR B 73  ? 1.2233 0.8202 0.7995 0.2872  0.1173  0.0560  73  THR B C   
5797  O O   . THR B 73  ? 1.2157 0.8334 0.8233 0.2791  0.1279  0.0644  73  THR B O   
5798  C CB  . THR B 73  ? 1.1140 0.6667 0.6133 0.3129  0.1361  0.0509  73  THR B CB  
5799  O OG1 . THR B 73  ? 1.7873 1.3284 1.2645 0.3147  0.1147  0.0456  73  THR B OG1 
5800  C CG2 . THR B 73  ? 1.1271 0.6901 0.6316 0.3109  0.1559  0.0636  73  THR B CG2 
5801  N N   . ALA B 74  ? 1.1520 0.7455 0.7208 0.2849  0.0968  0.0514  74  ALA B N   
5802  C CA  . ALA B 74  ? 1.0075 0.6223 0.6056 0.2726  0.0871  0.0561  74  ALA B CA  
5803  C C   . ALA B 74  ? 1.0644 0.6924 0.6713 0.2699  0.1025  0.0681  74  ALA B C   
5804  O O   . ALA B 74  ? 1.0040 0.6543 0.6459 0.2588  0.1049  0.0741  74  ALA B O   
5805  C CB  . ALA B 74  ? 1.2383 0.8450 0.8218 0.2737  0.0649  0.0487  74  ALA B CB  
5806  N N   . ASP B 75  ? 1.1340 0.7469 0.7083 0.2799  0.1133  0.0716  75  ASP B N   
5807  C CA  . ASP B 75  ? 1.1021 0.7243 0.6821 0.2777  0.1285  0.0829  75  ASP B CA  
5808  C C   . ASP B 75  ? 1.0896 0.7298 0.7015 0.2713  0.1472  0.0897  75  ASP B C   
5809  O O   . ASP B 75  ? 1.0823 0.7399 0.7176 0.2635  0.1536  0.0979  75  ASP B O   
5810  C CB  . ASP B 75  ? 1.2704 0.8684 0.8054 0.2904  0.1389  0.0854  75  ASP B CB  
5811  C CG  . ASP B 75  ? 1.4120 0.9904 0.9128 0.2982  0.1192  0.0785  75  ASP B CG  
5812  O OD1 . ASP B 75  ? 1.2345 0.8206 0.7430 0.2941  0.1063  0.0802  75  ASP B OD1 
5813  O OD2 . ASP B 75  ? 1.4941 1.0495 0.9609 0.3089  0.1160  0.0708  75  ASP B OD2 
5814  N N   . VAL B 76  ? 1.1024 0.7385 0.7158 0.2751  0.1550  0.0857  76  VAL B N   
5815  C CA  . VAL B 76  ? 0.9820 0.6349 0.6268 0.2704  0.1710  0.0906  76  VAL B CA  
5816  C C   . VAL B 76  ? 1.0512 0.7262 0.7356 0.2573  0.1583  0.0912  76  VAL B C   
5817  O O   . VAL B 76  ? 1.0563 0.7504 0.7680 0.2491  0.1644  0.0987  76  VAL B O   
5818  C CB  . VAL B 76  ? 0.9569 0.5977 0.5908 0.2796  0.1817  0.0850  76  VAL B CB  
5819  C CG1 . VAL B 76  ? 0.9465 0.6067 0.6188 0.2745  0.1929  0.0879  76  VAL B CG1 
5820  C CG2 . VAL B 76  ? 1.1095 0.7301 0.7053 0.2916  0.1988  0.0862  76  VAL B CG2 
5821  N N   . ILE B 77  ? 0.9806 0.6517 0.6670 0.2552  0.1405  0.0834  77  ILE B N   
5822  C CA  . ILE B 77  ? 0.9637 0.6523 0.6839 0.2427  0.1285  0.0837  77  ILE B CA  
5823  C C   . ILE B 77  ? 1.0225 0.7277 0.7587 0.2334  0.1248  0.0903  77  ILE B C   
5824  O O   . ILE B 77  ? 1.0545 0.7783 0.8205 0.2244  0.1285  0.0960  77  ILE B O   
5825  C CB  . ILE B 77  ? 0.8524 0.5305 0.5666 0.2419  0.1092  0.0739  77  ILE B CB  
5826  C CG1 . ILE B 77  ? 0.9946 0.6579 0.6987 0.2501  0.1130  0.0675  77  ILE B CG1 
5827  C CG2 . ILE B 77  ? 0.8770 0.5718 0.6231 0.2280  0.0971  0.0750  77  ILE B CG2 
5828  C CD1 . ILE B 77  ? 0.8688 0.5128 0.5518 0.2543  0.0967  0.0564  77  ILE B CD1 
5829  N N   . VAL B 78  ? 0.9354 0.6329 0.6509 0.2364  0.1173  0.0891  78  VAL B N   
5830  C CA  . VAL B 78  ? 0.8893 0.6005 0.6173 0.2292  0.1131  0.0943  78  VAL B CA  
5831  C C   . VAL B 78  ? 1.0312 0.7533 0.7708 0.2273  0.1313  0.1043  78  VAL B C   
5832  O O   . VAL B 78  ? 1.0445 0.7857 0.8125 0.2174  0.1314  0.1091  78  VAL B O   
5833  C CB  . VAL B 78  ? 0.8871 0.5846 0.5869 0.2357  0.1018  0.0904  78  VAL B CB  
5834  C CG1 . VAL B 78  ? 0.8721 0.5822 0.5826 0.2305  0.1002  0.0963  78  VAL B CG1 
5835  C CG2 . VAL B 78  ? 0.9536 0.6447 0.6498 0.2350  0.0813  0.0799  78  VAL B CG2 
5836  N N   . SER B 79  ? 1.0202 0.7299 0.7380 0.2366  0.1472  0.1073  79  SER B N   
5837  C CA  . SER B 79  ? 0.9465 0.6649 0.6750 0.2349  0.1656  0.1164  79  SER B CA  
5838  C C   . SER B 79  ? 0.9102 0.6479 0.6753 0.2273  0.1732  0.1191  79  SER B C   
5839  O O   . SER B 79  ? 0.9260 0.6785 0.7124 0.2208  0.1807  0.1258  79  SER B O   
5840  C CB  . SER B 79  ? 0.9069 0.6063 0.6041 0.2461  0.1824  0.1183  79  SER B CB  
5841  O OG  . SER B 79  ? 1.0692 0.7635 0.7652 0.2514  0.1921  0.1147  79  SER B OG  
5842  N N   . ARG B 80  ? 0.9052 0.6419 0.6774 0.2285  0.1705  0.1138  80  ARG B N   
5843  C CA  . ARG B 80  ? 0.8706 0.6241 0.6763 0.2225  0.1755  0.1159  80  ARG B CA  
5844  C C   . ARG B 80  ? 0.8900 0.6596 0.7208 0.2105  0.1619  0.1174  80  ARG B C   
5845  O O   . ARG B 80  ? 0.8756 0.6619 0.7328 0.2036  0.1666  0.1224  80  ARG B O   
5846  C CB  . ARG B 80  ? 0.8360 0.5818 0.6407 0.2282  0.1753  0.1095  80  ARG B CB  
5847  C CG  . ARG B 80  ? 0.8869 0.6176 0.6685 0.2403  0.1912  0.1076  80  ARG B CG  
5848  C CD  . ARG B 80  ? 0.8628 0.5890 0.6494 0.2461  0.1940  0.1017  80  ARG B CD  
5849  N NE  . ARG B 80  ? 0.9426 0.6585 0.7210 0.2462  0.1757  0.0942  80  ARG B NE  
5850  C CZ  . ARG B 80  ? 0.7983 0.5045 0.5736 0.2525  0.1747  0.0875  80  ARG B CZ  
5851  N NH1 . ARG B 80  ? 1.0133 0.7199 0.7938 0.2599  0.1910  0.0870  80  ARG B NH1 
5852  N NH2 . ARG B 80  ? 1.1225 0.8184 0.8908 0.2514  0.1575  0.0808  80  ARG B NH2 
5853  N N   . ASN B 81  ? 0.8872 0.6518 0.7098 0.2079  0.1452  0.1126  81  ASN B N   
5854  C CA  . ASN B 81  ? 0.9503 0.7289 0.7945 0.1964  0.1332  0.1135  81  ASN B CA  
5855  C C   . ASN B 81  ? 0.9341 0.7249 0.7871 0.1912  0.1368  0.1198  81  ASN B C   
5856  O O   . ASN B 81  ? 0.9439 0.7505 0.8212 0.1820  0.1357  0.1234  81  ASN B O   
5857  C CB  . ASN B 81  ? 0.7537 0.5238 0.5870 0.1951  0.1161  0.1063  81  ASN B CB  
5858  C CG  . ASN B 81  ? 0.8818 0.6420 0.7134 0.1969  0.1101  0.1002  81  ASN B CG  
5859  O OD1 . ASN B 81  ? 0.7667 0.5293 0.6105 0.1973  0.1167  0.1017  81  ASN B OD1 
5860  N ND2 . ASN B 81  ? 0.7971 0.5455 0.6145 0.1982  0.0969  0.0927  81  ASN B ND2 
5861  N N   . PHE B 82  ? 0.8218 0.6039 0.6536 0.1974  0.1410  0.1211  82  PHE B N   
5862  C CA  . PHE B 82  ? 0.8314 0.6221 0.6689 0.1938  0.1447  0.1269  82  PHE B CA  
5863  C C   . PHE B 82  ? 0.8683 0.6702 0.7251 0.1908  0.1601  0.1337  82  PHE B C   
5864  O O   . PHE B 82  ? 0.9255 0.7421 0.8029 0.1828  0.1599  0.1375  82  PHE B O   
5865  C CB  . PHE B 82  ? 0.7084 0.4830 0.5150 0.2027  0.1459  0.1271  82  PHE B CB  
5866  C CG  . PHE B 82  ? 0.8494 0.6299 0.6595 0.2001  0.1499  0.1332  82  PHE B CG  
5867  C CD1 . PHE B 82  ? 0.7240 0.5117 0.5406 0.1954  0.1369  0.1318  82  PHE B CD1 
5868  C CD2 . PHE B 82  ? 0.8930 0.6715 0.7009 0.2024  0.1671  0.1401  82  PHE B CD2 
5869  C CE1 . PHE B 82  ? 0.7720 0.5640 0.5916 0.1937  0.1402  0.1370  82  PHE B CE1 
5870  C CE2 . PHE B 82  ? 0.8265 0.6085 0.6374 0.1998  0.1706  0.1457  82  PHE B CE2 
5871  C CZ  . PHE B 82  ? 0.8902 0.6787 0.7064 0.1959  0.1567  0.1441  82  PHE B CZ  
5872  N N   . ALA B 83  ? 0.8257 0.6210 0.6769 0.1974  0.1737  0.1344  83  ALA B N   
5873  C CA  . ALA B 83  ? 0.8083 0.6148 0.6803 0.1949  0.1887  0.1398  83  ALA B CA  
5874  C C   . ALA B 83  ? 0.8360 0.6604 0.7405 0.1861  0.1832  0.1399  83  ALA B C   
5875  O O   . ALA B 83  ? 0.9017 0.7396 0.8273 0.1802  0.1885  0.1444  83  ALA B O   
5876  C CB  . ALA B 83  ? 0.7274 0.5240 0.5891 0.2038  0.2039  0.1391  83  ALA B CB  
5877  N N   . ARG B 84  ? 0.7165 0.5395 0.6238 0.1853  0.1721  0.1350  84  ARG B N   
5878  C CA  . ARG B 84  ? 0.7995 0.6363 0.7336 0.1775  0.1661  0.1356  84  ARG B CA  
5879  C C   . ARG B 84  ? 0.7222 0.5705 0.6678 0.1675  0.1580  0.1384  84  ARG B C   
5880  O O   . ARG B 84  ? 0.6662 0.5275 0.6339 0.1611  0.1580  0.1411  84  ARG B O   
5881  C CB  . ARG B 84  ? 0.7701 0.5996 0.7019 0.1789  0.1560  0.1303  84  ARG B CB  
5882  C CG  . ARG B 84  ? 0.9340 0.7557 0.8623 0.1883  0.1649  0.1275  84  ARG B CG  
5883  C CD  . ARG B 84  ? 0.8189 0.6401 0.7591 0.1877  0.1572  0.1244  84  ARG B CD  
5884  N NE  . ARG B 84  ? 0.9318 0.7493 0.8748 0.1969  0.1674  0.1219  84  ARG B NE  
5885  C CZ  . ARG B 84  ? 0.9768 0.7893 0.9254 0.2002  0.1624  0.1181  84  ARG B CZ  
5886  N NH1 . ARG B 84  ? 0.9245 0.7338 0.8753 0.1944  0.1475  0.1169  84  ARG B NH1 
5887  N NH2 . ARG B 84  ? 0.8203 0.6307 0.7728 0.2093  0.1729  0.1154  84  ARG B NH2 
5888  N N   . MET B 85  ? 0.7229 0.5665 0.6537 0.1667  0.1511  0.1372  85  MET B N   
5889  C CA  . MET B 85  ? 0.6657 0.5203 0.6072 0.1581  0.1446  0.1390  85  MET B CA  
5890  C C   . MET B 85  ? 0.8192 0.6828 0.7718 0.1562  0.1553  0.1447  85  MET B C   
5891  O O   . MET B 85  ? 0.7801 0.6565 0.7513 0.1484  0.1533  0.1470  85  MET B O   
5892  C CB  . MET B 85  ? 0.6806 0.5283 0.6048 0.1594  0.1357  0.1358  85  MET B CB  
5893  C CG  . MET B 85  ? 0.8650 0.7047 0.7810 0.1598  0.1239  0.1295  85  MET B CG  
5894  S SD  . MET B 85  ? 0.9175 0.7560 0.8247 0.1581  0.1106  0.1248  85  MET B SD  
5895  C CE  . MET B 85  ? 0.9667 0.8219 0.9000 0.1443  0.1038  0.1252  85  MET B CE  
5896  N N   . VAL B 86  ? 0.7206 0.5762 0.6608 0.1633  0.1670  0.1470  86  VAL B N   
5897  C CA  . VAL B 86  ? 0.7200 0.5816 0.6699 0.1617  0.1786  0.1524  86  VAL B CA  
5898  C C   . VAL B 86  ? 0.8037 0.6781 0.7804 0.1578  0.1845  0.1539  86  VAL B C   
5899  O O   . VAL B 86  ? 0.8865 0.7727 0.8819 0.1511  0.1854  0.1566  86  VAL B O   
5900  C CB  . VAL B 86  ? 0.6671 0.5142 0.5949 0.1703  0.1910  0.1546  86  VAL B CB  
5901  C CG1 . VAL B 86  ? 0.6311 0.4835 0.5715 0.1681  0.2056  0.1604  86  VAL B CG1 
5902  C CG2 . VAL B 86  ? 0.8946 0.7292 0.7963 0.1745  0.1833  0.1534  86  VAL B CG2 
5903  N N   . ALA B 87  ? 0.6995 0.5712 0.6784 0.1623  0.1874  0.1514  87  ALA B N   
5904  C CA  . ALA B 87  ? 0.6175 0.5010 0.6226 0.1601  0.1914  0.1519  87  ALA B CA  
5905  C C   . ALA B 87  ? 0.7321 0.6271 0.7547 0.1514  0.1789  0.1517  87  ALA B C   
5906  O O   . ALA B 87  ? 0.8392 0.7464 0.8838 0.1469  0.1810  0.1537  87  ALA B O   
5907  C CB  . ALA B 87  ? 0.6942 0.5712 0.6963 0.1675  0.1938  0.1481  87  ALA B CB  
5908  N N   . ALA B 88  ? 0.6743 0.5648 0.6867 0.1489  0.1660  0.1493  88  ALA B N   
5909  C CA  . ALA B 88  ? 0.6664 0.5652 0.6911 0.1406  0.1550  0.1494  88  ALA B CA  
5910  C C   . ALA B 88  ? 0.6754 0.5831 0.7064 0.1338  0.1549  0.1522  88  ALA B C   
5911  O O   . ALA B 88  ? 0.6410 0.5588 0.6887 0.1280  0.1525  0.1536  88  ALA B O   
5912  C CB  . ALA B 88  ? 0.6647 0.5552 0.6763 0.1392  0.1434  0.1462  88  ALA B CB  
5913  N N   . GLY B 89  ? 0.7169 0.6200 0.7340 0.1354  0.1572  0.1526  89  GLY B N   
5914  C CA  . GLY B 89  ? 0.6393 0.5493 0.6612 0.1302  0.1574  0.1547  89  GLY B CA  
5915  C C   . GLY B 89  ? 0.6146 0.5324 0.6532 0.1288  0.1670  0.1580  89  GLY B C   
5916  O O   . GLY B 89  ? 0.7234 0.6506 0.7754 0.1223  0.1646  0.1591  89  GLY B O   
5917  N N   . THR B 90  ? 0.6570 0.5706 0.6954 0.1348  0.1782  0.1593  90  THR B N   
5918  C CA  . THR B 90  ? 0.7006 0.6215 0.7574 0.1335  0.1891  0.1619  90  THR B CA  
5919  C C   . THR B 90  ? 0.7753 0.7085 0.8564 0.1291  0.1841  0.1606  90  THR B C   
5920  O O   . THR B 90  ? 0.8679 0.8108 0.9674 0.1241  0.1856  0.1618  90  THR B O   
5921  C CB  . THR B 90  ? 0.7461 0.6591 0.7965 0.1410  0.2033  0.1630  90  THR B CB  
5922  O OG1 . THR B 90  ? 0.9030 0.8023 0.9276 0.1454  0.2071  0.1647  90  THR B OG1 
5923  C CG2 . THR B 90  ? 0.7314 0.6530 0.8048 0.1390  0.2157  0.1652  90  THR B CG2 
5924  N N   . ALA B 91  ? 0.7011 0.6327 0.7818 0.1314  0.1772  0.1580  91  ALA B N   
5925  C CA  . ALA B 91  ? 0.6708 0.6115 0.7715 0.1286  0.1705  0.1568  91  ALA B CA  
5926  C C   . ALA B 91  ? 0.7081 0.6549 0.8129 0.1203  0.1603  0.1573  91  ALA B C   
5927  O O   . ALA B 91  ? 0.7029 0.6591 0.8265 0.1168  0.1579  0.1573  91  ALA B O   
5928  C CB  . ALA B 91  ? 0.6670 0.6010 0.7614 0.1330  0.1641  0.1542  91  ALA B CB  
5929  N N   . ALA B 92  ? 0.6689 0.6105 0.7568 0.1174  0.1541  0.1572  92  ALA B N   
5930  C CA  . ALA B 92  ? 0.5715 0.5183 0.6615 0.1096  0.1459  0.1573  92  ALA B CA  
5931  C C   . ALA B 92  ? 0.6696 0.6246 0.7720 0.1060  0.1507  0.1586  92  ALA B C   
5932  O O   . ALA B 92  ? 0.7549 0.7169 0.8693 0.1011  0.1456  0.1583  92  ALA B O   
5933  C CB  . ALA B 92  ? 0.5594 0.5004 0.6317 0.1076  0.1410  0.1563  92  ALA B CB  
5934  N N   . HIS B 93  ? 0.6267 0.5793 0.7252 0.1085  0.1601  0.1601  93  HIS B N   
5935  C CA  . HIS B 93  ? 0.6213 0.5796 0.7313 0.1051  0.1654  0.1614  93  HIS B CA  
5936  C C   . HIS B 93  ? 0.7139 0.6798 0.8468 0.1051  0.1706  0.1615  93  HIS B C   
5937  O O   . HIS B 93  ? 0.7920 0.7654 0.9401 0.1001  0.1697  0.1611  93  HIS B O   
5938  C CB  . HIS B 93  ? 0.5181 0.4688 0.6152 0.1084  0.1740  0.1635  93  HIS B CB  
5939  C CG  . HIS B 93  ? 0.6395 0.5859 0.7200 0.1076  0.1676  0.1626  93  HIS B CG  
5940  N ND1 . HIS B 93  ? 0.8445 0.7806 0.9055 0.1134  0.1696  0.1630  93  HIS B ND1 
5941  C CD2 . HIS B 93  ? 0.7672 0.7189 0.8490 0.1020  0.1594  0.1608  93  HIS B CD2 
5942  C CE1 . HIS B 93  ? 0.8395 0.7761 0.8933 0.1112  0.1619  0.1611  93  HIS B CE1 
5943  N NE2 . HIS B 93  ? 0.9090 0.8552 0.9751 0.1041  0.1566  0.1598  93  HIS B NE2 
5944  N N   . SER B 94  ? 0.6890 0.6533 0.8257 0.1106  0.1759  0.1612  94  SER B N   
5945  C CA  . SER B 94  ? 0.7471 0.7202 0.9089 0.1113  0.1812  0.1604  94  SER B CA  
5946  C C   . SER B 94  ? 0.7058 0.6883 0.8844 0.1069  0.1689  0.1580  94  SER B C   
5947  O O   . SER B 94  ? 0.7208 0.7122 0.9199 0.1032  0.1698  0.1571  94  SER B O   
5948  C CB  . SER B 94  ? 0.6861 0.6555 0.8471 0.1189  0.1873  0.1595  94  SER B CB  
5949  O OG  . SER B 94  ? 0.7110 0.6908 0.8996 0.1199  0.1907  0.1576  94  SER B OG  
5950  N N   . ASP B 95  ? 0.6016 0.5806 0.7698 0.1072  0.1572  0.1569  95  ASP B N   
5951  C CA  . ASP B 95  ? 0.6951 0.6798 0.8744 0.1039  0.1447  0.1550  95  ASP B CA  
5952  C C   . ASP B 95  ? 0.7430 0.7310 0.9221 0.0966  0.1402  0.1550  95  ASP B C   
5953  O O   . ASP B 95  ? 0.8827 0.8773 1.0764 0.0938  0.1329  0.1531  95  ASP B O   
5954  C CB  . ASP B 95  ? 0.6054 0.5822 0.7701 0.1056  0.1343  0.1548  95  ASP B CB  
5955  C CG  . ASP B 95  ? 0.7178 0.6957 0.8953 0.1118  0.1320  0.1530  95  ASP B CG  
5956  O OD1 . ASP B 95  ? 0.7853 0.7719 0.9846 0.1145  0.1390  0.1516  95  ASP B OD1 
5957  O OD2 . ASP B 95  ? 0.9216 0.8916 1.0882 0.1137  0.1235  0.1529  95  ASP B OD2 
5958  N N   . HIS B 96  ? 0.6310 0.6145 0.7942 0.0943  0.1438  0.1565  96  HIS B N   
5959  C CA  . HIS B 96  ? 0.6747 0.6607 0.8363 0.0880  0.1402  0.1560  96  HIS B CA  
5960  C C   . HIS B 96  ? 0.6463 0.6398 0.8294 0.0862  0.1460  0.1552  96  HIS B C   
5961  O O   . HIS B 96  ? 0.7077 0.7070 0.9031 0.0825  0.1391  0.1529  96  HIS B O   
5962  C CB  . HIS B 96  ? 0.5757 0.5556 0.7176 0.0873  0.1431  0.1572  96  HIS B CB  
5963  C CG  . HIS B 96  ? 0.5356 0.5178 0.6761 0.0821  0.1417  0.1562  96  HIS B CG  
5964  N ND1 . HIS B 96  ? 0.7892 0.7760 0.9443 0.0799  0.1458  0.1557  96  HIS B ND1 
5965  C CD2 . HIS B 96  ? 0.6628 0.6430 0.7897 0.0789  0.1375  0.1553  96  HIS B CD2 
5966  C CE1 . HIS B 96  ? 0.4929 0.4796 0.6416 0.0760  0.1434  0.1544  96  HIS B CE1 
5967  N NE2 . HIS B 96  ? 1.0133 0.9968 1.1456 0.0754  0.1388  0.1540  96  HIS B NE2 
5968  N N   . GLY B 97  ? 0.6159 0.6080 0.8026 0.0888  0.1585  0.1571  97  GLY B N   
5969  C CA  . GLY B 97  ? 0.5782 0.5760 0.7857 0.0864  0.1662  0.1568  97  GLY B CA  
5970  C C   . GLY B 97  ? 0.6364 0.6444 0.8712 0.0863  0.1637  0.1540  97  GLY B C   
5971  O O   . GLY B 97  ? 0.6288 0.6438 0.8835 0.0820  0.1629  0.1518  97  GLY B O   
5972  N N   . ARG B 98  ? 0.5571 0.5659 0.7943 0.0915  0.1620  0.1534  98  ARG B N   
5973  C CA  . ARG B 98  ? 0.5199 0.5390 0.7844 0.0929  0.1585  0.1500  98  ARG B CA  
5974  C C   . ARG B 98  ? 0.6222 0.6460 0.8932 0.0889  0.1423  0.1467  98  ARG B C   
5975  O O   . ARG B 98  ? 0.5910 0.6245 0.8880 0.0871  0.1390  0.1431  98  ARG B O   
5976  C CB  . ARG B 98  ? 0.5278 0.5445 0.7885 0.1001  0.1577  0.1499  98  ARG B CB  
5977  C CG  . ARG B 98  ? 0.4082 0.4358 0.6986 0.1034  0.1546  0.1459  98  ARG B CG  
5978  C CD  . ARG B 98  ? 0.5973 0.6202 0.8793 0.1097  0.1455  0.1451  98  ARG B CD  
5979  N NE  . ARG B 98  ? 0.5588 0.5697 0.8144 0.1136  0.1520  0.1480  98  ARG B NE  
5980  C CZ  . ARG B 98  ? 0.5552 0.5644 0.8116 0.1189  0.1659  0.1485  98  ARG B CZ  
5981  N NH1 . ARG B 98  ? 0.6150 0.6345 0.8986 0.1205  0.1767  0.1467  98  ARG B NH1 
5982  N NH2 . ARG B 98  ? 0.6521 0.6490 0.8822 0.1225  0.1693  0.1505  98  ARG B NH2 
5983  N N   . SER B 99  ? 0.6833 0.6993 0.9300 0.0875  0.1323  0.1476  99  SER B N   
5984  C CA  . SER B 99  ? 0.6186 0.6357 0.8646 0.0840  0.1175  0.1450  99  SER B CA  
5985  C C   . SER B 99  ? 0.5722 0.5936 0.8274 0.0779  0.1183  0.1430  99  SER B C   
5986  O O   . SER B 99  ? 0.6133 0.6396 0.8811 0.0756  0.1080  0.1391  99  SER B O   
5987  C CB  . SER B 99  ? 0.5784 0.5849 0.7944 0.0830  0.1103  0.1471  99  SER B CB  
5988  O OG  . SER B 99  ? 0.9953 0.9999 1.2074 0.0819  0.0957  0.1453  99  SER B OG  
5989  N N   . ILE B 100 ? 0.6814 0.7000 0.9300 0.0758  0.1297  0.1452  100 ILE B N   
5990  C CA  . ILE B 100 ? 0.5205 0.5411 0.7765 0.0703  0.1316  0.1435  100 ILE B CA  
5991  C C   . ILE B 100 ? 0.6721 0.7023 0.9611 0.0692  0.1359  0.1409  100 ILE B C   
5992  O O   . ILE B 100 ? 0.7497 0.7849 1.0535 0.0650  0.1290  0.1366  100 ILE B O   
5993  C CB  . ILE B 100 ? 0.5540 0.5674 0.7942 0.0697  0.1428  0.1470  100 ILE B CB  
5994  C CG1 . ILE B 100 ? 0.5771 0.5826 0.7883 0.0713  0.1401  0.1492  100 ILE B CG1 
5995  C CG2 . ILE B 100 ? 0.7706 0.7843 1.0166 0.0643  0.1435  0.1449  100 ILE B CG2 
5996  C CD1 . ILE B 100 ? 0.7199 0.7241 0.9186 0.0685  0.1278  0.1470  100 ILE B CD1 
5997  N N   . ALA B 101 ? 0.5872 0.6201 0.8881 0.0728  0.1476  0.1429  101 ALA B N   
5998  C CA  . ALA B 101 ? 0.5730 0.6161 0.9081 0.0715  0.1541  0.1403  101 ALA B CA  
5999  C C   . ALA B 101 ? 0.6221 0.6758 0.9799 0.0717  0.1393  0.1344  101 ALA B C   
6000  O O   . ALA B 101 ? 0.6053 0.6677 0.9907 0.0677  0.1376  0.1300  101 ALA B O   
6001  C CB  . ALA B 101 ? 0.5041 0.5473 0.8444 0.0762  0.1697  0.1435  101 ALA B CB  
6002  N N   . LEU B 102 ? 0.6470 0.6987 0.9930 0.0764  0.1278  0.1340  102 LEU B N   
6003  C CA  . LEU B 102 ? 0.4767 0.5358 0.8403 0.0780  0.1117  0.1287  102 LEU B CA  
6004  C C   . LEU B 102 ? 0.6477 0.7053 1.0067 0.0727  0.0983  0.1251  102 LEU B C   
6005  O O   . LEU B 102 ? 0.7409 0.8068 1.1236 0.0718  0.0877  0.1193  102 LEU B O   
6006  C CB  . LEU B 102 ? 0.3983 0.4519 0.7457 0.0846  0.1026  0.1301  102 LEU B CB  
6007  C CG  . LEU B 102 ? 0.3991 0.4562 0.7579 0.0913  0.1123  0.1312  102 LEU B CG  
6008  C CD1 . LEU B 102 ? 0.4041 0.4503 0.7364 0.0967  0.1067  0.1342  102 LEU B CD1 
6009  C CD2 . LEU B 102 ? 0.3997 0.4715 0.7978 0.0941  0.1083  0.1253  102 LEU B CD2 
6010  N N   . SER B 103 ? 0.6241 0.6713 0.9536 0.0694  0.0985  0.1279  103 SER B N   
6011  C CA  . SER B 103 ? 0.6112 0.6555 0.9331 0.0646  0.0875  0.1243  103 SER B CA  
6012  C C   . SER B 103 ? 0.6227 0.6742 0.9711 0.0594  0.0925  0.1205  103 SER B C   
6013  O O   . SER B 103 ? 0.7096 0.7651 1.0714 0.0569  0.0805  0.1144  103 SER B O   
6014  C CB  . SER B 103 ? 0.5869 0.6197 0.8739 0.0626  0.0896  0.1279  103 SER B CB  
6015  O OG  . SER B 103 ? 0.6761 0.7014 0.9391 0.0658  0.0821  0.1304  103 SER B OG  
6016  N N   . LEU B 104 ? 0.6362 0.6882 0.9917 0.0579  0.1099  0.1239  104 LEU B N   
6017  C CA  . LEU B 104 ? 0.5491 0.6061 0.9298 0.0524  0.1173  0.1212  104 LEU B CA  
6018  C C   . LEU B 104 ? 0.6485 0.7195 1.0690 0.0520  0.1120  0.1152  104 LEU B C   
6019  O O   . LEU B 104 ? 0.6690 0.7450 1.1121 0.0466  0.1092  0.1099  104 LEU B O   
6020  C CB  . LEU B 104 ? 0.4706 0.5232 0.8488 0.0522  0.1379  0.1273  104 LEU B CB  
6021  C CG  . LEU B 104 ? 0.4630 0.5161 0.8614 0.0460  0.1484  0.1264  104 LEU B CG  
6022  C CD1 . LEU B 104 ? 0.5209 0.5661 0.9046 0.0416  0.1423  0.1244  104 LEU B CD1 
6023  C CD2 . LEU B 104 ? 0.5454 0.5927 0.9396 0.0473  0.1689  0.1333  104 LEU B CD2 
6024  N N   . TYR B 105 ? 0.6159 0.6933 1.0461 0.0578  0.1102  0.1153  105 TYR B N   
6025  C CA  . TYR B 105 ? 0.5078 0.6001 0.9775 0.0589  0.1044  0.1091  105 TYR B CA  
6026  C C   . TYR B 105 ? 0.6319 0.7263 1.1046 0.0594  0.0805  0.1021  105 TYR B C   
6027  O O   . TYR B 105 ? 0.6326 0.7397 1.1406 0.0592  0.0725  0.0951  105 TYR B O   
6028  C CB  . TYR B 105 ? 0.4663 0.5630 0.9417 0.0664  0.1101  0.1114  105 TYR B CB  
6029  C CG  . TYR B 105 ? 0.6160 0.7299 1.1362 0.0684  0.1074  0.1050  105 TYR B CG  
6030  C CD1 . TYR B 105 ? 0.6274 0.7522 1.1830 0.0640  0.1230  0.1032  105 TYR B CD1 
6031  C CD2 . TYR B 105 ? 0.5945 0.7134 1.1219 0.0749  0.0900  0.1008  105 TYR B CD2 
6032  C CE1 . TYR B 105 ? 0.6060 0.7486 1.2066 0.0656  0.1214  0.0965  105 TYR B CE1 
6033  C CE2 . TYR B 105 ? 0.5424 0.6784 1.1135 0.0776  0.0868  0.0940  105 TYR B CE2 
6034  C CZ  . TYR B 105 ? 0.5832 0.7322 1.1924 0.0727  0.1028  0.0915  105 TYR B CZ  
6035  O OH  . TYR B 105 ? 0.6678 0.8357 1.3243 0.0750  0.1008  0.0842  105 TYR B OH  
6036  N N   . HIS B 106 ? 0.5966 0.6785 1.0328 0.0601  0.0690  0.1036  106 HIS B N   
6037  C CA  . HIS B 106 ? 0.6955 0.7757 1.1273 0.0611  0.0465  0.0977  106 HIS B CA  
6038  C C   . HIS B 106 ? 0.6270 0.6993 1.0425 0.0551  0.0411  0.0950  106 HIS B C   
6039  O O   . HIS B 106 ? 0.7779 0.8415 1.1698 0.0562  0.0256  0.0930  106 HIS B O   
6040  C CB  . HIS B 106 ? 0.5690 0.6396 0.9705 0.0676  0.0365  0.1014  106 HIS B CB  
6041  C CG  . HIS B 106 ? 0.6228 0.6997 1.0388 0.0744  0.0403  0.1033  106 HIS B CG  
6042  N ND1 . HIS B 106 ? 0.8752 0.9431 1.2649 0.0784  0.0469  0.1102  106 HIS B ND1 
6043  C CD2 . HIS B 106 ? 0.8160 0.9075 1.2710 0.0777  0.0386  0.0985  106 HIS B CD2 
6044  C CE1 . HIS B 106 ? 1.0782 1.1542 1.4896 0.0845  0.0488  0.1094  106 HIS B CE1 
6045  N NE2 . HIS B 106 ? 0.9399 1.0308 1.3914 0.0844  0.0443  0.1025  106 HIS B NE2 
6046  N N   . THR B 107 ? 0.4199 0.7887 0.9033 0.1015  0.0520  0.1150  107 THR B N   
6047  C CA  . THR B 107 ? 0.4599 0.8402 0.9234 0.0795  0.0515  0.1039  107 THR B CA  
6048  C C   . THR B 107 ? 0.5342 0.9850 1.0218 0.0712  0.0381  0.0853  107 THR B C   
6049  O O   . THR B 107 ? 0.5765 1.0713 1.1075 0.0764  0.0352  0.0756  107 THR B O   
6050  C CB  . THR B 107 ? 0.4890 0.8249 0.9415 0.0618  0.0739  0.0889  107 THR B CB  
6051  O OG1 . THR B 107 ? 0.6544 0.9959 1.1339 0.0520  0.0898  0.0725  107 THR B OG1 
6052  C CG2 . THR B 107 ? 0.5292 0.8075 0.9553 0.0686  0.0796  0.1054  107 THR B CG2 
6053  N N   . SER B 108 ? 0.5532 1.0204 1.0141 0.0579  0.0303  0.0768  108 SER B N   
6054  C CA  . SER B 108 ? 0.4488 0.9840 0.9235 0.0458  0.0131  0.0547  108 SER B CA  
6055  C C   . SER B 108 ? 0.5080 1.0344 0.9498 0.0231  0.0196  0.0295  108 SER B C   
6056  O O   . SER B 108 ? 0.6498 1.1374 1.0562 0.0272  0.0297  0.0390  108 SER B O   
6057  C CB  . SER B 108 ? 0.3915 0.9733 0.8583 0.0674  -0.0184 0.0773  108 SER B CB  
6058  O OG  . SER B 108 ? 0.9975 1.5883 1.5024 0.0945  -0.0259 0.0939  108 SER B OG  
6059  N N   . LYS B 109 ? 0.5501 1.1140 1.0065 -0.0002 0.0144  -0.0047 109 LYS B N   
6060  C CA  . LYS B 109 ? 0.6175 1.1651 1.0413 -0.0203 0.0211  -0.0364 109 LYS B CA  
6061  C C   . LYS B 109 ? 0.8008 1.3707 1.1740 -0.0089 0.0088  -0.0265 109 LYS B C   
6062  O O   . LYS B 109 ? 0.7633 1.2999 1.1039 -0.0080 0.0251  -0.0350 109 LYS B O   
6063  C CB  . LYS B 109 ? 0.7104 1.2992 1.1579 -0.0521 0.0125  -0.0768 109 LYS B CB  
6064  C CG  . LYS B 109 ? 0.8704 1.4367 1.2797 -0.0734 0.0172  -0.1173 109 LYS B CG  
6065  C CD  . LYS B 109 ? 0.9876 1.5946 1.4195 -0.1124 0.0054  -0.1608 109 LYS B CD  
6066  C CE  . LYS B 109 ? 0.7985 1.5109 1.2405 -0.1118 -0.0326 -0.1619 109 LYS B CE  
6067  N NZ  . LYS B 109 ? 0.8975 1.6435 1.3211 -0.1469 -0.0487 -0.2130 109 LYS B NZ  
6068  N N   . ASP B 110 ? 0.9519 1.5799 1.3178 0.0014  -0.0193 -0.0072 110 ASP B N   
6069  C CA  . ASP B 110 ? 0.9333 1.5830 1.2400 0.0086  -0.0311 0.0094  110 ASP B CA  
6070  C C   . ASP B 110 ? 0.9224 1.5524 1.2185 0.0329  -0.0367 0.0630  110 ASP B C   
6071  O O   . ASP B 110 ? 1.0667 1.7249 1.3269 0.0432  -0.0608 0.0905  110 ASP B O   
6072  C CB  . ASP B 110 ? 1.0166 1.7401 1.3058 -0.0003 -0.0645 -0.0077 110 ASP B CB  
6073  C CG  . ASP B 110 ? 1.0015 1.7400 1.3019 -0.0309 -0.0613 -0.0652 110 ASP B CG  
6074  O OD1 . ASP B 110 ? 1.0825 1.7744 1.3604 -0.0421 -0.0344 -0.0927 110 ASP B OD1 
6075  O OD2 . ASP B 110 ? 0.8930 1.6899 1.2273 -0.0434 -0.0864 -0.0846 110 ASP B OD2 
6076  N N   . GLY B 111 ? 0.7255 1.3004 1.0463 0.0406  -0.0159 0.0774  111 GLY B N   
6077  C CA  . GLY B 111 ? 0.7170 1.2573 1.0295 0.0585  -0.0179 0.1219  111 GLY B CA  
6078  C C   . GLY B 111 ? 0.5915 1.0912 0.8788 0.0509  0.0065  0.1323  111 GLY B C   
6079  O O   . GLY B 111 ? 0.6844 1.1814 0.9720 0.0397  0.0259  0.1037  111 GLY B O   
6080  N N   . ASP B 112 ? 0.7161 1.1842 0.9842 0.0570  0.0049  0.1717  112 ASP B N   
6081  C CA  . ASP B 112 ? 0.4706 0.9126 0.7229 0.0444  0.0269  0.1822  112 ASP B CA  
6082  C C   . ASP B 112 ? 0.4706 0.8810 0.7631 0.0453  0.0441  0.1617  112 ASP B C   
6083  O O   . ASP B 112 ? 0.5519 0.9692 0.8458 0.0373  0.0615  0.1456  112 ASP B O   
6084  C CB  . ASP B 112 ? 0.5474 0.9517 0.7715 0.0441  0.0200  0.2292  112 ASP B CB  
6085  C CG  . ASP B 112 ? 0.6972 1.1234 0.8591 0.0324  0.0141  0.2562  112 ASP B CG  
6086  O OD1 . ASP B 112 ? 0.7064 1.1856 0.8452 0.0238  0.0181  0.2341  112 ASP B OD1 
6087  O OD2 . ASP B 112 ? 0.6342 1.0179 0.7635 0.0305  0.0063  0.2994  112 ASP B OD2 
6088  N N   . ILE B 113 ? 0.4756 0.8555 0.7991 0.0574  0.0390  0.1616  113 ILE B N   
6089  C CA  . ILE B 113 ? 0.4414 0.7861 0.7901 0.0581  0.0528  0.1462  113 ILE B CA  
6090  C C   . ILE B 113 ? 0.5461 0.9021 0.9154 0.0567  0.0568  0.1144  113 ILE B C   
6091  O O   . ILE B 113 ? 0.5091 0.8847 0.8963 0.0600  0.0480  0.1099  113 ILE B O   
6092  C CB  . ILE B 113 ? 0.4610 0.7593 0.8195 0.0679  0.0500  0.1644  113 ILE B CB  
6093  C CG1 . ILE B 113 ? 0.4243 0.6998 0.7579 0.0641  0.0439  0.1968  113 ILE B CG1 
6094  C CG2 . ILE B 113 ? 0.6332 0.8954 1.0026 0.0662  0.0627  0.1508  113 ILE B CG2 
6095  C CD1 . ILE B 113 ? 0.7971 1.0186 1.1337 0.0765  0.0380  0.2122  113 ILE B CD1 
6096  N N   . LYS B 114 ? 0.5034 0.8468 0.8724 0.0515  0.0696  0.0921  114 LYS B N   
6097  C CA  . LYS B 114 ? 0.5155 0.8517 0.8953 0.0442  0.0756  0.0626  114 LYS B CA  
6098  C C   . LYS B 114 ? 0.5629 0.8415 0.9460 0.0464  0.0878  0.0581  114 LYS B C   
6099  O O   . LYS B 114 ? 0.6744 0.9287 1.0530 0.0555  0.0886  0.0746  114 LYS B O   
6100  C CB  . LYS B 114 ? 0.5587 0.9206 0.9217 0.0381  0.0775  0.0363  114 LYS B CB  
6101  C CG  . LYS B 114 ? 0.6012 1.0206 0.9459 0.0337  0.0640  0.0406  114 LYS B CG  
6102  C CD  . LYS B 114 ? 0.6765 1.1209 0.9920 0.0305  0.0717  0.0184  114 LYS B CD  
6103  C CE  . LYS B 114 ? 0.8007 1.3004 1.0851 0.0219  0.0569  0.0162  114 LYS B CE  
6104  N NZ  . LYS B 114 ? 0.9683 1.4848 1.2302 0.0128  0.0631  -0.0288 114 LYS B NZ  
6105  N N   . VAL B 115 ? 0.5527 0.8066 0.9390 0.0352  0.0958  0.0366  115 VAL B N   
6106  C CA  . VAL B 115 ? 0.4946 0.6826 0.8704 0.0359  0.1065  0.0357  115 VAL B CA  
6107  C C   . VAL B 115 ? 0.6399 0.8018 1.0010 0.0454  0.1082  0.0172  115 VAL B C   
6108  O O   . VAL B 115 ? 0.8206 0.9650 1.1765 0.0337  0.1130  -0.0083 115 VAL B O   
6109  C CB  . VAL B 115 ? 0.4153 0.5832 0.7984 0.0131  0.1181  0.0260  115 VAL B CB  
6110  C CG1 . VAL B 115 ? 0.5665 0.6537 0.9225 0.0108  0.1300  0.0299  115 VAL B CG1 
6111  C CG2 . VAL B 115 ? 0.4393 0.6455 0.8465 0.0109  0.1188  0.0388  115 VAL B CG2 
6112  N N   . LYS B 116 ? 0.5232 0.6856 0.8815 0.0668  0.1040  0.0265  116 LYS B N   
6113  C CA  . LYS B 116 ? 0.5110 0.6604 0.8650 0.0855  0.1057  0.0066  116 LYS B CA  
6114  C C   . LYS B 116 ? 0.7005 0.7650 1.0367 0.0959  0.1070  0.0031  116 LYS B C   
6115  O O   . LYS B 116 ? 0.7492 0.7766 1.0756 0.1011  0.1116  -0.0222 116 LYS B O   
6116  C CB  . LYS B 116 ? 0.4562 0.6531 0.8246 0.1035  0.1014  0.0158  116 LYS B CB  
6117  C CG  . LYS B 116 ? 0.3987 0.6691 0.7714 0.0926  0.1045  0.0150  116 LYS B CG  
6118  C CD  . LYS B 116 ? 0.6041 0.9241 0.9931 0.1029  0.1068  0.0208  116 LYS B CD  
6119  C CE  . LYS B 116 ? 0.4538 0.8388 0.8350 0.0866  0.1136  0.0260  116 LYS B CE  
6120  N NZ  . LYS B 116 ? 0.7191 1.1516 1.1186 0.0838  0.1181  0.0405  116 LYS B NZ  
6121  N N   . ASP B 117 ? 0.6757 0.7015 0.9999 0.0989  0.1027  0.0282  117 ASP B N   
6122  C CA  . ASP B 117 ? 0.6582 0.5944 0.9513 0.1079  0.1021  0.0331  117 ASP B CA  
6123  C C   . ASP B 117 ? 0.6766 0.5699 0.9497 0.0735  0.1165  0.0388  117 ASP B C   
6124  O O   . ASP B 117 ? 0.7714 0.6671 1.0365 0.0629  0.1196  0.0590  117 ASP B O   
6125  C CB  . ASP B 117 ? 0.6499 0.5716 0.9322 0.1325  0.0863  0.0566  117 ASP B CB  
6126  C CG  . ASP B 117 ? 0.9226 0.7539 1.1686 0.1552  0.0779  0.0631  117 ASP B CG  
6127  O OD1 . ASP B 117 ? 0.9903 0.7439 1.2015 0.1364  0.0899  0.0642  117 ASP B OD1 
6128  O OD2 . ASP B 117 ? 0.8294 0.6675 1.0817 0.1910  0.0582  0.0681  117 ASP B OD2 
6129  N N   . GLU B 118 ? 0.7611 0.6190 1.0277 0.0533  0.1273  0.0174  118 GLU B N   
6130  C CA  . GLU B 118 ? 0.7407 0.5697 0.9970 0.0127  0.1446  0.0191  118 GLU B CA  
6131  C C   . GLU B 118 ? 0.9781 0.7080 1.1840 0.0102  0.1512  0.0429  118 GLU B C   
6132  O O   . GLU B 118 ? 1.0278 0.7529 1.2217 -0.0160 0.1666  0.0580  118 GLU B O   
6133  C CB  . GLU B 118 ? 0.8768 0.7002 1.1424 -0.0162 0.1527  -0.0143 118 GLU B CB  
6134  C CG  . GLU B 118 ? 0.9611 0.8834 1.2643 -0.0163 0.1440  -0.0368 118 GLU B CG  
6135  C CD  . GLU B 118 ? 1.0464 0.9866 1.3623 -0.0545 0.1488  -0.0703 118 GLU B CD  
6136  O OE1 . GLU B 118 ? 1.0961 0.9672 1.3959 -0.0867 0.1620  -0.0792 118 GLU B OE1 
6137  O OE2 . GLU B 118 ? 1.0313 1.0538 1.3693 -0.0554 0.1383  -0.0872 118 GLU B OE2 
6138  N N   . ASN B 119 ? 1.0888 0.7410 1.2624 0.0403  0.1395  0.0470  119 ASN B N   
6139  C CA  . ASN B 119 ? 0.9843 0.5301 1.0965 0.0431  0.1401  0.0754  119 ASN B CA  
6140  C C   . ASN B 119 ? 1.0374 0.6074 1.1316 0.0484  0.1359  0.1052  119 ASN B C   
6141  O O   . ASN B 119 ? 1.1517 0.6695 1.1993 0.0227  0.1516  0.1259  119 ASN B O   
6142  C CB  . ASN B 119 ? 1.1533 0.6257 1.2420 0.0906  0.1190  0.0758  119 ASN B CB  
6143  C CG  . ASN B 119 ? 1.3758 0.7692 1.4532 0.0835  0.1268  0.0497  119 ASN B CG  
6144  O OD1 . ASN B 119 ? 1.4322 0.7632 1.4840 0.0360  0.1477  0.0475  119 ASN B OD1 
6145  N ND2 . ASN B 119 ? 1.5532 0.9474 1.6503 0.1288  0.1118  0.0262  119 ASN B ND2 
6146  N N   . LYS B 120 ? 1.0081 0.6558 1.1351 0.0774  0.1170  0.1055  120 LYS B N   
6147  C CA  . LYS B 120 ? 0.8764 0.5448 0.9853 0.0814  0.1104  0.1272  120 LYS B CA  
6148  C C   . LYS B 120 ? 0.9158 0.6187 1.0314 0.0441  0.1361  0.1267  120 LYS B C   
6149  O O   . LYS B 120 ? 1.0849 0.7558 1.1558 0.0328  0.1456  0.1442  120 LYS B O   
6150  C CB  . LYS B 120 ? 0.8876 0.6338 1.0368 0.1108  0.0867  0.1234  120 LYS B CB  
6151  C CG  . LYS B 120 ? 0.8205 0.5750 0.9442 0.1146  0.0748  0.1419  120 LYS B CG  
6152  C CD  . LYS B 120 ? 0.7911 0.5652 0.9217 0.1502  0.0414  0.1467  120 LYS B CD  
6153  C CE  . LYS B 120 ? 0.8014 0.5756 0.8973 0.1483  0.0270  0.1614  120 LYS B CE  
6154  N NZ  . LYS B 120 ? 0.8512 0.6597 0.9628 0.1792  -0.0096 0.1631  120 LYS B NZ  
6155  N N   . LEU B 121 ? 0.8372 0.6080 1.0066 0.0272  0.1471  0.1057  121 LEU B N   
6156  C CA  . LEU B 121 ? 0.8064 0.6227 0.9953 -0.0006 0.1691  0.1021  121 LEU B CA  
6157  C C   . LEU B 121 ? 0.9653 0.7263 1.1188 -0.0368 0.1978  0.1072  121 LEU B C   
6158  O O   . LEU B 121 ? 0.9882 0.7631 1.1309 -0.0526 0.2183  0.1132  121 LEU B O   
6159  C CB  . LEU B 121 ? 0.6804 0.5798 0.9322 -0.0080 0.1688  0.0799  121 LEU B CB  
6160  C CG  . LEU B 121 ? 0.7068 0.6637 0.9928 -0.0325 0.1890  0.0716  121 LEU B CG  
6161  C CD1 . LEU B 121 ? 0.6762 0.6620 0.9649 -0.0162 0.1896  0.0820  121 LEU B CD1 
6162  C CD2 . LEU B 121 ? 0.5972 0.6266 0.9365 -0.0393 0.1818  0.0507  121 LEU B CD2 
6163  N N   . LYS B 122 ? 1.0237 0.7184 1.1563 -0.0516 0.2020  0.1037  122 LYS B N   
6164  C CA  . LYS B 122 ? 0.8801 0.5105 0.9738 -0.0950 0.2318  0.1110  122 LYS B CA  
6165  C C   . LYS B 122 ? 1.1068 0.6644 1.1216 -0.0899 0.2366  0.1439  122 LYS B C   
6166  O O   . LYS B 122 ? 1.2770 0.8309 1.2667 -0.1240 0.2681  0.1521  122 LYS B O   
6167  C CB  . LYS B 122 ? 0.9543 0.5074 1.0336 -0.1100 0.2311  0.1006  122 LYS B CB  
6168  C CG  . LYS B 122 ? 1.0296 0.6530 1.1763 -0.1192 0.2256  0.0633  122 LYS B CG  
6169  C CD  . LYS B 122 ? 0.9232 0.5695 1.0975 -0.1798 0.2528  0.0429  122 LYS B CD  
6170  C CE  . LYS B 122 ? 0.9914 0.6647 1.2048 -0.1911 0.2416  0.0051  122 LYS B CE  
6171  N NZ  . LYS B 122 ? 1.2657 0.8218 1.4328 -0.1785 0.2315  -0.0011 122 LYS B NZ  
6172  N N   . GLU B 123 ? 1.1504 0.6601 1.1269 -0.0470 0.2052  0.1613  123 GLU B N   
6173  C CA  . GLU B 123 ? 1.1363 0.5803 1.0305 -0.0378 0.2009  0.1931  123 GLU B CA  
6174  C C   . GLU B 123 ? 1.1059 0.6203 1.0054 -0.0388 0.2093  0.1915  123 GLU B C   
6175  O O   . GLU B 123 ? 1.2758 0.7537 1.1099 -0.0571 0.2288  0.2084  123 GLU B O   
6176  C CB  . GLU B 123 ? 1.0841 0.4802 0.9498 0.0137  0.1579  0.2081  123 GLU B CB  
6177  C CG  . GLU B 123 ? 1.3245 0.6074 1.1486 0.0211  0.1506  0.2196  123 GLU B CG  
6178  C CD  . GLU B 123 ? 1.8213 0.9837 1.5456 -0.0087 0.1698  0.2538  123 GLU B CD  
6179  O OE1 . GLU B 123 ? 1.6803 0.8473 1.3543 -0.0271 0.1842  0.2723  123 GLU B OE1 
6180  O OE2 . GLU B 123 ? 2.0017 1.0588 1.6921 -0.0149 0.1720  0.2616  123 GLU B OE2 
6181  N N   . VAL B 124 ? 1.0026 0.6103 0.9723 -0.0199 0.1963  0.1709  124 VAL B N   
6182  C CA  . VAL B 124 ? 0.8780 0.5423 0.8556 -0.0173 0.2028  0.1651  124 VAL B CA  
6183  C C   . VAL B 124 ? 1.0033 0.7009 0.9959 -0.0539 0.2468  0.1538  124 VAL B C   
6184  O O   . VAL B 124 ? 1.1258 0.8288 1.0855 -0.0598 0.2656  0.1546  124 VAL B O   
6185  C CB  . VAL B 124 ? 0.8329 0.5740 0.8785 0.0092  0.1781  0.1494  124 VAL B CB  
6186  C CG1 . VAL B 124 ? 0.8365 0.6279 0.8987 0.0087  0.1898  0.1386  124 VAL B CG1 
6187  C CG2 . VAL B 124 ? 0.8710 0.5946 0.9016 0.0417  0.1390  0.1593  124 VAL B CG2 
6188  N N   . ALA B 125 ? 0.9957 0.7209 1.0388 -0.0790 0.2638  0.1397  125 ALA B N   
6189  C CA  . ALA B 125 ? 0.9255 0.7012 0.9991 -0.1158 0.3049  0.1253  125 ALA B CA  
6190  C C   . ALA B 125 ? 0.9455 0.6554 0.9392 -0.1495 0.3399  0.1436  125 ALA B C   
6191  O O   . ALA B 125 ? 1.0392 0.7957 1.0395 -0.1690 0.3760  0.1340  125 ALA B O   
6192  C CB  . ALA B 125 ? 0.8133 0.6247 0.9494 -0.1414 0.3099  0.1068  125 ALA B CB  
6193  N N   . LYS B 126 ? 1.0375 0.6381 0.9520 -0.1543 0.3302  0.1707  126 LYS B N   
6194  C CA  . LYS B 126 ? 1.1633 0.6847 0.9824 -0.1876 0.3615  0.1962  126 LYS B CA  
6195  C C   . LYS B 126 ? 1.1764 0.7113 0.9436 -0.1700 0.3659  0.2014  126 LYS B C   
6196  O O   . LYS B 126 ? 1.5538 1.0974 1.2844 -0.2022 0.4100  0.2018  126 LYS B O   
6197  C CB  . LYS B 126 ? 1.3325 0.7208 1.0678 -0.1816 0.3383  0.2296  126 LYS B CB  
6198  C CG  . LYS B 126 ? 1.4404 0.7845 1.2042 -0.2057 0.3402  0.2238  126 LYS B CG  
6199  C CD  . LYS B 126 ? 1.7093 0.9134 1.3926 -0.1841 0.3109  0.2551  126 LYS B CD  
6200  C CE  . LYS B 126 ? 1.7795 0.9565 1.5118 -0.1779 0.2937  0.2361  126 LYS B CE  
6201  N NZ  . LYS B 126 ? 1.8157 0.8609 1.4776 -0.1470 0.2621  0.2616  126 LYS B NZ  
6202  N N   . SER B 127 ? 1.1279 0.6693 0.8932 -0.1221 0.3226  0.2016  127 SER B N   
6203  C CA  . SER B 127 ? 1.1459 0.6948 0.8599 -0.1054 0.3202  0.2010  127 SER B CA  
6204  C C   . SER B 127 ? 1.2214 0.8608 0.9890 -0.1145 0.3573  0.1692  127 SER B C   
6205  O O   . SER B 127 ? 1.2902 0.9245 0.9978 -0.1230 0.3835  0.1662  127 SER B O   
6206  C CB  . SER B 127 ? 1.2412 0.7946 0.9650 -0.0591 0.2655  0.2008  127 SER B CB  
6207  O OG  . SER B 127 ? 1.4402 0.9322 1.1435 -0.0419 0.2299  0.2232  127 SER B OG  
6208  N N   . PHE B 128 ? 1.1602 0.8823 1.0366 -0.1097 0.3590  0.1445  128 PHE B N   
6209  C CA  . PHE B 128 ? 1.1309 0.9434 1.0700 -0.1087 0.3895  0.1136  128 PHE B CA  
6210  C C   . PHE B 128 ? 1.1407 0.9996 1.1121 -0.1530 0.4424  0.1031  128 PHE B C   
6211  O O   . PHE B 128 ? 1.2369 1.1847 1.2734 -0.1498 0.4694  0.0749  128 PHE B O   
6212  C CB  . PHE B 128 ? 0.8376 0.7178 0.8737 -0.0753 0.3586  0.0953  128 PHE B CB  
6213  C CG  . PHE B 128 ? 0.8398 0.6970 0.8552 -0.0379 0.3196  0.0971  128 PHE B CG  
6214  C CD1 . PHE B 128 ? 0.8352 0.7051 0.8377 -0.0203 0.3280  0.0793  128 PHE B CD1 
6215  C CD2 . PHE B 128 ? 0.9384 0.7627 0.9489 -0.0224 0.2763  0.1130  128 PHE B CD2 
6216  C CE1 . PHE B 128 ? 0.9679 0.8121 0.9512 0.0057  0.2920  0.0787  128 PHE B CE1 
6217  C CE2 . PHE B 128 ? 0.9319 0.7453 0.9305 0.0039  0.2424  0.1129  128 PHE B CE2 
6218  C CZ  . PHE B 128 ? 0.9020 0.7223 0.8857 0.0145  0.2495  0.0964  128 PHE B CZ  
6219  N N   . ASN B 129 ? 1.1329 0.9321 1.0609 -0.1943 0.4573  0.1246  129 ASN B N   
6220  C CA  . ASN B 129 ? 1.2339 1.0712 1.1896 -0.2489 0.5086  0.1164  129 ASN B CA  
6221  C C   . ASN B 129 ? 1.1317 1.0809 1.2189 -0.2510 0.5063  0.0854  129 ASN B C   
6222  O O   . ASN B 129 ? 1.1892 1.2378 1.3420 -0.2691 0.5444  0.0599  129 ASN B O   
6223  C CB  . ASN B 129 ? 1.4734 1.3367 1.3854 -0.2704 0.5639  0.1090  129 ASN B CB  
6224  C CG  . ASN B 129 ? 1.6927 1.4393 1.4587 -0.2847 0.5705  0.1443  129 ASN B CG  
6225  O OD1 . ASN B 129 ? 1.6837 1.3386 1.3825 -0.2585 0.5255  0.1711  129 ASN B OD1 
6226  N ND2 . ASN B 129 ? 1.5747 1.3364 1.2969 -0.3159 0.6064  0.1418  129 ASN B ND2 
6227  N N   . VAL B 130 ? 0.9905 0.9286 1.1151 -0.2307 0.4606  0.0866  130 VAL B N   
6228  C CA  . VAL B 130 ? 0.8489 0.8820 1.0831 -0.2314 0.4480  0.0607  130 VAL B CA  
6229  C C   . VAL B 130 ? 1.0276 1.0075 1.2527 -0.2773 0.4482  0.0662  130 VAL B C   
6230  O O   . VAL B 130 ? 1.2272 1.0937 1.3777 -0.2742 0.4294  0.0904  130 VAL B O   
6231  C CB  . VAL B 130 ? 0.7538 0.8137 1.0272 -0.1739 0.3975  0.0558  130 VAL B CB  
6232  C CG1 . VAL B 130 ? 0.6855 0.8325 1.0537 -0.1754 0.3791  0.0339  130 VAL B CG1 
6233  C CG2 . VAL B 130 ? 0.7845 0.8805 1.0628 -0.1332 0.3987  0.0487  130 VAL B CG2 
6234  N N   . GLU B 131 ? 1.0564 1.1161 1.3571 -0.3198 0.4689  0.0419  131 GLU B N   
6235  C CA  . GLU B 131 ? 0.9488 0.9565 1.2391 -0.3665 0.4651  0.0404  131 GLU B CA  
6236  C C   . GLU B 131 ? 1.0885 1.0708 1.3986 -0.3414 0.4207  0.0338  131 GLU B C   
6237  O O   . GLU B 131 ? 0.9636 1.0259 1.3315 -0.2982 0.3902  0.0197  131 GLU B O   
6238  C CB  . GLU B 131 ? 1.0305 1.1450 1.3909 -0.4069 0.4784  0.0123  131 GLU B CB  
6239  C CG  . GLU B 131 ? 1.5864 1.6352 1.9184 -0.4660 0.4844  0.0124  131 GLU B CG  
6240  C CD  . GLU B 131 ? 1.7180 1.6111 1.9310 -0.4859 0.4986  0.0488  131 GLU B CD  
6241  O OE1 . GLU B 131 ? 1.5152 1.4025 1.6842 -0.5029 0.5289  0.0641  131 GLU B OE1 
6242  O OE2 . GLU B 131 ? 1.5808 1.3576 1.7429 -0.4804 0.4775  0.0621  131 GLU B OE2 
6243  N N   . THR B 132 ? 1.2142 1.0799 1.4673 -0.3626 0.4129  0.0443  132 THR B N   
6244  C CA  . THR B 132 ? 1.1289 0.9628 1.3885 -0.3349 0.3707  0.0340  132 THR B CA  
6245  C C   . THR B 132 ? 1.3140 1.0985 1.5760 -0.3899 0.3776  0.0147  132 THR B C   
6246  O O   . THR B 132 ? 1.6365 1.3321 1.8625 -0.3743 0.3537  0.0133  132 THR B O   
6247  C CB  . THR B 132 ? 1.1003 0.8216 1.2783 -0.2856 0.3459  0.0644  132 THR B CB  
6248  O OG1 . THR B 132 ? 1.3550 0.9615 1.4444 -0.3107 0.3704  0.0954  132 THR B OG1 
6249  C CG2 . THR B 132 ? 0.9616 0.7380 1.1497 -0.2288 0.3253  0.0733  132 THR B CG2 
6250  N N   . GLU B 133 ? 1.2342 1.0795 1.5405 -0.4526 0.4084  -0.0040 133 GLU B N   
6251  C CA  . GLU B 133 ? 1.2700 1.0703 1.5704 -0.5036 0.4066  -0.0241 133 GLU B CA  
6252  C C   . GLU B 133 ? 1.2065 1.1440 1.6057 -0.5243 0.3915  -0.0690 133 GLU B C   
6253  O O   . GLU B 133 ? 1.3089 1.3775 1.7720 -0.5316 0.3987  -0.0800 133 GLU B O   
6254  C CB  . GLU B 133 ? 1.6361 1.3883 1.8853 -0.5495 0.4358  -0.0051 133 GLU B CB  
6255  C CG  . GLU B 133 ? 1.9113 1.5653 2.1253 -0.5989 0.4351  -0.0138 133 GLU B CG  
6256  C CD  . GLU B 133 ? 2.0739 1.5585 2.2060 -0.5736 0.4152  0.0023  133 GLU B CD  
6257  O OE1 . GLU B 133 ? 2.1725 1.5840 2.2425 -0.5272 0.4101  0.0376  133 GLU B OE1 
6258  O OE2 . GLU B 133 ? 2.1455 1.5722 2.2760 -0.5962 0.4021  -0.0226 133 GLU B OE2 
6259  N N   . GLY B 134 ? 1.2257 1.1309 1.6330 -0.5300 0.3683  -0.0959 134 GLY B N   
6260  C CA  . GLY B 134 ? 1.1759 1.2019 1.6627 -0.5498 0.3461  -0.1405 134 GLY B CA  
6261  C C   . GLY B 134 ? 0.9190 1.1124 1.4895 -0.5106 0.3289  -0.1484 134 GLY B C   
6262  O O   . GLY B 134 ? 1.1933 1.5115 1.8291 -0.5265 0.3189  -0.1702 134 GLY B O   
6263  N N   . ARG B 135 ? 0.8391 1.0224 1.3872 -0.4416 0.3131  -0.1230 135 ARG B N   
6264  C CA  . ARG B 135 ? 0.7302 1.0486 1.3412 -0.3919 0.2912  -0.1231 135 ARG B CA  
6265  C C   . ARG B 135 ? 0.7100 1.0108 1.2935 -0.3315 0.2503  -0.1172 135 ARG B C   
6266  O O   . ARG B 135 ? 0.9134 1.0969 1.4269 -0.3130 0.2475  -0.1024 135 ARG B O   
6267  C CB  . ARG B 135 ? 0.7014 1.0300 1.3068 -0.3630 0.3150  -0.0932 135 ARG B CB  
6268  C CG  . ARG B 135 ? 0.8322 1.1399 1.4238 -0.4116 0.3605  -0.0860 135 ARG B CG  
6269  C CD  . ARG B 135 ? 0.7366 1.0728 1.3237 -0.3708 0.3768  -0.0642 135 ARG B CD  
6270  N NE  . ARG B 135 ? 0.7300 1.1728 1.3804 -0.3153 0.3519  -0.0709 135 ARG B NE  
6271  C CZ  . ARG B 135 ? 0.7157 1.1801 1.3654 -0.2740 0.3618  -0.0578 135 ARG B CZ  
6272  N NH1 . ARG B 135 ? 0.8131 1.2085 1.4012 -0.2840 0.3967  -0.0395 135 ARG B NH1 
6273  N NH2 . ARG B 135 ? 0.7916 1.3384 1.4940 -0.2221 0.3352  -0.0629 135 ARG B NH2 
6274  N N   . ASP B 136 ? 0.7607 1.1759 1.3969 -0.3013 0.2204  -0.1271 136 ASP B N   
6275  C CA  . ASP B 136 ? 0.5947 1.0048 1.2041 -0.2482 0.1858  -0.1178 136 ASP B CA  
6276  C C   . ASP B 136 ? 0.6295 0.9655 1.1897 -0.2025 0.1919  -0.0807 136 ASP B C   
6277  O O   . ASP B 136 ? 0.6829 1.0278 1.2525 -0.1930 0.2107  -0.0624 136 ASP B O   
6278  C CB  . ASP B 136 ? 0.5226 1.0665 1.1923 -0.2241 0.1547  -0.1257 136 ASP B CB  
6279  C CG  . ASP B 136 ? 0.7248 1.2694 1.3636 -0.1730 0.1228  -0.1096 136 ASP B CG  
6280  O OD1 . ASP B 136 ? 0.9149 1.4032 1.5052 -0.1733 0.1137  -0.1182 136 ASP B OD1 
6281  O OD2 . ASP B 136 ? 0.8618 1.4610 1.5237 -0.1333 0.1088  -0.0891 136 ASP B OD2 
6282  N N   . ILE B 137 ? 0.6119 0.9072 1.3532 -0.1259 0.1547  -0.0339 137 ILE B N   
6283  C CA  . ILE B 137 ? 0.5173 0.7679 1.2166 -0.1129 0.1573  -0.0230 137 ILE B CA  
6284  C C   . ILE B 137 ? 0.6007 0.8577 1.2652 -0.0930 0.1579  -0.0102 137 ILE B C   
6285  O O   . ILE B 137 ? 0.7540 0.9794 1.3892 -0.0807 0.1660  0.0055  137 ILE B O   
6286  C CB  . ILE B 137 ? 0.5042 0.7310 1.1943 -0.1180 0.1461  -0.0411 137 ILE B CB  
6287  C CG1 . ILE B 137 ? 0.8254 1.0001 1.4844 -0.1094 0.1514  -0.0301 137 ILE B CG1 
6288  C CG2 . ILE B 137 ? 0.6161 0.8675 1.2893 -0.1135 0.1329  -0.0547 137 ILE B CG2 
6289  C CD1 . ILE B 137 ? 0.8194 0.9645 1.4919 -0.1157 0.1630  -0.0165 137 ILE B CD1 
6290  N N   . TYR B 138 ? 0.5287 0.8255 1.1964 -0.0894 0.1489  -0.0163 138 TYR B N   
6291  C CA  . TYR B 138 ? 0.5598 0.8611 1.1963 -0.0703 0.1475  -0.0039 138 TYR B CA  
6292  C C   . TYR B 138 ? 0.6093 0.9209 1.2529 -0.0601 0.1599  0.0133  138 TYR B C   
6293  O O   . TYR B 138 ? 0.7597 1.0583 1.3742 -0.0424 0.1629  0.0266  138 TYR B O   
6294  C CB  . TYR B 138 ? 0.4861 0.8229 1.1200 -0.0697 0.1320  -0.0150 138 TYR B CB  
6295  C CG  . TYR B 138 ? 0.4758 0.8006 1.0950 -0.0780 0.1214  -0.0311 138 TYR B CG  
6296  C CD1 . TYR B 138 ? 0.4190 0.7147 0.9960 -0.0687 0.1186  -0.0263 138 TYR B CD1 
6297  C CD2 . TYR B 138 ? 0.5431 0.8837 1.1918 -0.0958 0.1154  -0.0522 138 TYR B CD2 
6298  C CE1 . TYR B 138 ? 0.5173 0.8045 1.0819 -0.0771 0.1102  -0.0424 138 TYR B CE1 
6299  C CE2 . TYR B 138 ? 0.5643 0.8961 1.2014 -0.1030 0.1064  -0.0694 138 TYR B CE2 
6300  C CZ  . TYR B 138 ? 0.4306 0.7368 1.0254 -0.0937 0.1042  -0.0644 138 TYR B CZ  
6301  O OH  . TYR B 138 ? 0.6290 0.9313 1.2136 -0.1015 0.0959  -0.0828 138 TYR B OH  
6302  N N   . ASP B 139 ? 0.5710 0.9058 1.2536 -0.0716 0.1677  0.0122  139 ASP B N   
6303  C CA  . ASP B 139 ? 0.5892 0.9374 1.2814 -0.0639 0.1813  0.0269  139 ASP B CA  
6304  C C   . ASP B 139 ? 0.6101 0.9132 1.2795 -0.0597 0.1953  0.0420  139 ASP B C   
6305  O O   . ASP B 139 ? 0.6512 0.9515 1.3044 -0.0444 0.2043  0.0558  139 ASP B O   
6306  C CB  . ASP B 139 ? 0.4825 0.8688 1.2236 -0.0806 0.1865  0.0206  139 ASP B CB  
6307  C CG  . ASP B 139 ? 0.8166 1.2545 1.5825 -0.0827 0.1736  0.0064  139 ASP B CG  
6308  O OD1 . ASP B 139 ? 0.7805 1.2289 1.5244 -0.0674 0.1624  0.0064  139 ASP B OD1 
6309  O OD2 . ASP B 139 ? 0.9112 1.3787 1.7182 -0.1001 0.1743  -0.0043 139 ASP B OD2 
6310  N N   . ILE B 140 ? 0.6610 0.9291 1.3286 -0.0722 0.1961  0.0387  140 ILE B N   
6311  C CA  . ILE B 140 ? 0.5984 0.8219 1.2424 -0.0686 0.2072  0.0527  140 ILE B CA  
6312  C C   . ILE B 140 ? 0.5533 0.7511 1.1520 -0.0491 0.2031  0.0576  140 ILE B C   
6313  O O   . ILE B 140 ? 0.7233 0.9046 1.2997 -0.0363 0.2133  0.0720  140 ILE B O   
6314  C CB  . ILE B 140 ? 0.4415 0.6328 1.0949 -0.0854 0.2053  0.0464  140 ILE B CB  
6315  C CG1 . ILE B 140 ? 0.6327 0.8438 1.3315 -0.1066 0.2102  0.0429  140 ILE B CG1 
6316  C CG2 . ILE B 140 ? 0.4561 0.5994 1.0788 -0.0788 0.2140  0.0613  140 ILE B CG2 
6317  C CD1 . ILE B 140 ? 0.8276 1.0174 1.5449 -0.1238 0.2014  0.0284  140 ILE B CD1 
6318  N N   . ALA B 141 ? 0.4961 0.6917 1.0813 -0.0478 0.1885  0.0449  141 ALA B N   
6319  C CA  . ALA B 141 ? 0.5733 0.7450 1.1164 -0.0322 0.1836  0.0481  141 ALA B CA  
6320  C C   . ALA B 141 ? 0.6364 0.8193 1.1634 -0.0132 0.1877  0.0607  141 ALA B C   
6321  O O   . ALA B 141 ? 0.6379 0.7923 1.1336 0.0003  0.1927  0.0705  141 ALA B O   
6322  C CB  . ALA B 141 ? 0.4396 0.6196 0.9764 -0.0368 0.1675  0.0319  141 ALA B CB  
6323  N N   . HIS B 142 ? 0.5128 0.7376 1.0625 -0.0114 0.1850  0.0594  142 HIS B N   
6324  C CA  . HIS B 142 ? 0.5710 0.8088 1.1095 0.0081  0.1869  0.0695  142 HIS B CA  
6325  C C   . HIS B 142 ? 0.6040 0.8352 1.1436 0.0154  0.2043  0.0823  142 HIS B C   
6326  O O   . HIS B 142 ? 0.6288 0.8476 1.1441 0.0337  0.2079  0.0911  142 HIS B O   
6327  C CB  . HIS B 142 ? 0.6185 0.9052 1.1837 0.0085  0.1780  0.0635  142 HIS B CB  
6328  C CG  . HIS B 142 ? 0.6526 0.9492 1.2132 0.0020  0.1606  0.0516  142 HIS B CG  
6329  N ND1 . HIS B 142 ? 0.5894 0.9301 1.1808 -0.0067 0.1518  0.0411  142 HIS B ND1 
6330  C CD2 . HIS B 142 ? 0.5932 0.8636 1.1219 0.0022  0.1513  0.0483  142 HIS B CD2 
6331  C CE1 . HIS B 142 ? 0.6350 0.9751 1.2109 -0.0112 0.1375  0.0322  142 HIS B CE1 
6332  N NE2 . HIS B 142 ? 0.5453 0.8441 1.0836 -0.0066 0.1371  0.0363  142 HIS B NE2 
6333  N N   . ASP B 143 ? 0.6644 0.9033 1.2315 0.0004  0.2154  0.0834  143 ASP B N   
6334  C CA  . ASP B 143 ? 0.6050 0.8401 1.1728 0.0040  0.2333  0.0961  143 ASP B CA  
6335  C C   . ASP B 143 ? 0.5993 0.7851 1.1290 0.0106  0.2384  0.1044  143 ASP B C   
6336  O O   . ASP B 143 ? 0.6663 0.8446 1.1775 0.0248  0.2483  0.1143  143 ASP B O   
6337  C CB  . ASP B 143 ? 0.6084 0.8609 1.2136 -0.0175 0.2431  0.0961  143 ASP B CB  
6338  C CG  . ASP B 143 ? 0.7315 1.0386 1.3771 -0.0227 0.2429  0.0897  143 ASP B CG  
6339  O OD1 . ASP B 143 ? 0.6549 0.9877 1.3001 -0.0083 0.2337  0.0852  143 ASP B OD1 
6340  O OD2 . ASP B 143 ? 0.7290 1.0528 1.4069 -0.0413 0.2515  0.0894  143 ASP B OD2 
6341  N N   . VAL B 144 ? 0.6544 0.8089 1.1729 0.0010  0.2311  0.0988  144 VAL B N   
6342  C CA  . VAL B 144 ? 0.5479 0.6568 1.0312 0.0071  0.2337  0.1045  144 VAL B CA  
6343  C C   . VAL B 144 ? 0.6316 0.7288 1.0804 0.0274  0.2284  0.1056  144 VAL B C   
6344  O O   . VAL B 144 ? 0.7047 0.7780 1.1267 0.0394  0.2359  0.1141  144 VAL B O   
6345  C CB  . VAL B 144 ? 0.5397 0.6222 1.0229 -0.0069 0.2248  0.0949  144 VAL B CB  
6346  C CG1 . VAL B 144 ? 0.6045 0.6428 1.0499 0.0018  0.2246  0.0983  144 VAL B CG1 
6347  C CG2 . VAL B 144 ? 0.5857 0.6712 1.1011 -0.0264 0.2304  0.0957  144 VAL B CG2 
6348  N N   . ALA B 145 ? 0.5719 0.6857 1.0209 0.0308  0.2150  0.0971  145 ALA B N   
6349  C CA  . ALA B 145 ? 0.5890 0.6908 1.0066 0.0483  0.2084  0.0988  145 ALA B CA  
6350  C C   . ALA B 145 ? 0.7166 0.8300 1.1315 0.0663  0.2177  0.1086  145 ALA B C   
6351  O O   . ALA B 145 ? 0.6633 0.7521 1.0485 0.0812  0.2201  0.1136  145 ALA B O   
6352  C CB  . ALA B 145 ? 0.5377 0.6593 0.9592 0.0462  0.1925  0.0899  145 ALA B CB  
6353  N N   . LYS B 146 ? 0.5783 0.7310 1.0258 0.0649  0.2229  0.1097  146 LYS B N   
6354  C CA  . LYS B 146 ? 0.5477 0.7183 0.9979 0.0820  0.2320  0.1163  146 LYS B CA  
6355  C C   . LYS B 146 ? 0.7182 0.8676 1.1531 0.0855  0.2486  0.1251  146 LYS B C   
6356  O O   . LYS B 146 ? 0.6649 0.8057 1.0797 0.1040  0.2529  0.1290  146 LYS B O   
6357  C CB  . LYS B 146 ? 0.6182 0.8394 1.1104 0.0769  0.2350  0.1137  146 LYS B CB  
6358  C CG  . LYS B 146 ? 0.7145 0.9630 1.2177 0.0836  0.2188  0.1071  146 LYS B CG  
6359  C CD  . LYS B 146 ? 0.8178 1.1203 1.3639 0.0808  0.2215  0.1033  146 LYS B CD  
6360  C CE  . LYS B 146 ? 0.9871 1.3123 1.5635 0.0581  0.2159  0.0945  146 LYS B CE  
6361  N NZ  . LYS B 146 ? 0.7961 1.1662 1.3975 0.0623  0.2036  0.0871  146 LYS B NZ  
6362  N N   . GLU B 147 ? 0.7181 0.8586 1.1619 0.0680  0.2571  0.1280  147 GLU B N   
6363  C CA  . GLU B 147 ? 0.6566 0.7767 1.0840 0.0694  0.2723  0.1379  147 GLU B CA  
6364  C C   . GLU B 147 ? 0.6343 0.7101 1.0200 0.0802  0.2682  0.1388  147 GLU B C   
6365  O O   . GLU B 147 ? 0.6889 0.7523 1.0535 0.0917  0.2783  0.1454  147 GLU B O   
6366  C CB  . GLU B 147 ? 0.6575 0.7744 1.1035 0.0470  0.2801  0.1423  147 GLU B CB  
6367  C CG  . GLU B 147 ? 0.6341 0.7947 1.1195 0.0357  0.2896  0.1440  147 GLU B CG  
6368  C CD  . GLU B 147 ? 0.9953 1.1826 1.4816 0.0489  0.3043  0.1502  147 GLU B CD  
6369  O OE1 . GLU B 147 ? 1.0916 1.2657 1.5622 0.0486  0.3184  0.1608  147 GLU B OE1 
6370  O OE2 . GLU B 147 ? 0.9883 1.2107 1.4906 0.0601  0.3010  0.1441  147 GLU B OE2 
6371  N N   . GLY B 148 ? 0.6051 0.6603 0.9796 0.0761  0.2538  0.1311  148 GLY B N   
6372  C CA  . GLY B 148 ? 0.6275 0.6437 0.9647 0.0848  0.2487  0.1298  148 GLY B CA  
6373  C C   . GLY B 148 ? 0.7738 0.7893 1.0913 0.1057  0.2464  0.1301  148 GLY B C   
6374  O O   . GLY B 148 ? 0.8672 0.8582 1.1565 0.1177  0.2509  0.1330  148 GLY B O   
6375  N N   . LEU B 149 ? 0.6275 0.6697 0.9605 0.1108  0.2386  0.1269  149 LEU B N   
6376  C CA  . LEU B 149 ? 0.6204 0.6612 0.9378 0.1314  0.2343  0.1273  149 LEU B CA  
6377  C C   . LEU B 149 ? 0.6667 0.7167 0.9836 0.1465  0.2489  0.1326  149 LEU B C   
6378  O O   . LEU B 149 ? 0.6896 0.7237 0.9843 0.1644  0.2480  0.1325  149 LEU B O   
6379  C CB  . LEU B 149 ? 0.6337 0.7032 0.9702 0.1337  0.2220  0.1239  149 LEU B CB  
6380  C CG  . LEU B 149 ? 0.5708 0.6301 0.8983 0.1239  0.2055  0.1184  149 LEU B CG  
6381  C CD1 . LEU B 149 ? 0.6385 0.7335 0.9898 0.1232  0.1946  0.1159  149 LEU B CD1 
6382  C CD2 . LEU B 149 ? 0.5164 0.5393 0.8061 0.1343  0.1979  0.1189  149 LEU B CD2 
6383  N N   . SER B 150 ? 0.6358 0.7117 0.9770 0.1384  0.2622  0.1364  150 SER B N   
6384  C CA  . SER B 150 ? 0.5570 0.6473 0.8984 0.1507  0.2780  0.1407  150 SER B CA  
6385  C C   . SER B 150 ? 0.7218 0.7748 1.0264 0.1585  0.2838  0.1436  150 SER B C   
6386  O O   . SER B 150 ? 0.7904 0.8447 1.0825 0.1772  0.2892  0.1427  150 SER B O   
6387  C CB  . SER B 150 ? 0.5320 0.6533 0.9027 0.1357  0.2919  0.1454  150 SER B CB  
6388  O OG  . SER B 150 ? 1.1098 1.2059 1.4682 0.1210  0.2994  0.1521  150 SER B OG  
6389  N N   . ASN B 151 ? 0.7515 0.7739 1.0404 0.1455  0.2818  0.1455  151 ASN B N   
6390  C CA  . ASN B 151 ? 0.6768 0.6651 0.9314 0.1519  0.2865  0.1478  151 ASN B CA  
6391  C C   . ASN B 151 ? 0.6823 0.6487 0.9099 0.1706  0.2781  0.1416  151 ASN B C   
6392  O O   . ASN B 151 ? 0.7616 0.7056 0.9621 0.1798  0.2830  0.1419  151 ASN B O   
6393  C CB  . ASN B 151 ? 0.6256 0.5855 0.8710 0.1356  0.2821  0.1488  151 ASN B CB  
6394  C CG  . ASN B 151 ? 0.7876 0.7542 1.0473 0.1199  0.2932  0.1577  151 ASN B CG  
6395  O OD1 . ASN B 151 ? 0.7436 0.7384 1.0197 0.1189  0.3063  0.1643  151 ASN B OD1 
6396  N ND2 . ASN B 151 ? 0.9222 0.8629 1.1763 0.1070  0.2879  0.1580  151 ASN B ND2 
6397  N N   . TYR B 152 ? 0.6419 0.6139 0.8761 0.1760  0.2651  0.1364  152 TYR B N   
6398  C CA  . TYR B 152 ? 0.6543 0.6028 0.8636 0.1922  0.2562  0.1318  152 TYR B CA  
6399  C C   . TYR B 152 ? 0.6784 0.6426 0.8909 0.2139  0.2612  0.1305  152 TYR B C   
6400  O O   . TYR B 152 ? 0.8635 0.8039 1.0519 0.2288  0.2589  0.1269  152 TYR B O   
6401  C CB  . TYR B 152 ? 0.5409 0.4836 0.7512 0.1872  0.2386  0.1283  152 TYR B CB  
6402  C CG  . TYR B 152 ? 0.5890 0.5094 0.7876 0.1697  0.2318  0.1256  152 TYR B CG  
6403  C CD1 . TYR B 152 ? 0.5941 0.4787 0.7610 0.1717  0.2273  0.1219  152 TYR B CD1 
6404  C CD2 . TYR B 152 ? 0.6440 0.5804 0.8647 0.1510  0.2304  0.1251  152 TYR B CD2 
6405  C CE1 . TYR B 152 ? 0.6573 0.5250 0.8152 0.1562  0.2214  0.1174  152 TYR B CE1 
6406  C CE2 . TYR B 152 ? 0.6685 0.5864 0.8806 0.1361  0.2240  0.1203  152 TYR B CE2 
6407  C CZ  . TYR B 152 ? 0.7014 0.5860 0.8823 0.1391  0.2196  0.1162  152 TYR B CZ  
6408  O OH  . TYR B 152 ? 0.8375 0.7072 1.0116 0.1251  0.2132  0.1093  152 TYR B OH  
6409  N N   . GLY B 153 ? 0.5771 0.5815 0.8202 0.2159  0.2674  0.1318  153 GLY B N   
6410  C CA  . GLY B 153 ? 0.6079 0.6317 0.8579 0.2379  0.2713  0.1281  153 GLY B CA  
6411  C C   . GLY B 153 ? 0.7550 0.8243 1.0335 0.2390  0.2867  0.1290  153 GLY B C   
6412  O O   . GLY B 153 ? 0.8662 0.9623 1.1619 0.2555  0.2858  0.1239  153 GLY B O   
6413  N N   . LYS B 154 ? 0.6668 0.7453 0.9506 0.2217  0.3002  0.1353  154 LYS B N   
6414  C CA  . LYS B 154 ? 0.5753 0.6989 0.8847 0.2204  0.3172  0.1369  154 LYS B CA  
6415  C C   . LYS B 154 ? 0.7931 0.9196 1.0855 0.2384  0.3299  0.1338  154 LYS B C   
6416  O O   . LYS B 154 ? 0.7047 0.7987 0.9653 0.2385  0.3334  0.1363  154 LYS B O   
6417  C CB  . LYS B 154 ? 0.6047 0.7367 0.9266 0.1943  0.3270  0.1461  154 LYS B CB  
6418  C CG  . LYS B 154 ? 0.8481 0.9407 1.1399 0.1836  0.3307  0.1532  154 LYS B CG  
6419  C CD  . LYS B 154 ? 0.7045 0.8053 1.0126 0.1586  0.3388  0.1627  154 LYS B CD  
6420  C CE  . LYS B 154 ? 0.8649 1.0157 1.2059 0.1525  0.3531  0.1651  154 LYS B CE  
6421  N NZ  . LYS B 154 ? 1.1063 1.2609 1.4628 0.1262  0.3606  0.1752  154 LYS B NZ  
6422  N N   . GLN B 155 ? 0.7815 0.9476 1.0952 0.2535  0.3359  0.1270  155 GLN B N   
6423  C CA  . GLN B 155 ? 0.7778 0.9537 1.0791 0.2720  0.3481  0.1209  155 GLN B CA  
6424  C C   . GLN B 155 ? 0.8141 1.0264 1.1250 0.2600  0.3705  0.1263  155 GLN B C   
6425  O O   . GLN B 155 ? 0.7744 0.9849 1.0620 0.2654  0.3786  0.1235  155 GLN B O   
6426  C CB  . GLN B 155 ? 0.6732 0.8685 0.9880 0.2949  0.3370  0.1071  155 GLN B CB  
6427  C CG  . GLN B 155 ? 0.7067 0.8649 1.0106 0.3069  0.3148  0.1038  155 GLN B CG  
6428  C CD  . GLN B 155 ? 0.7504 0.8562 1.0116 0.3097  0.3088  0.1030  155 GLN B CD  
6429  O OE1 . GLN B 155 ? 0.6631 0.7644 0.9037 0.3162  0.3144  0.0968  155 GLN B OE1 
6430  N NE2 . GLN B 155 ? 0.6487 0.7164 0.8962 0.3040  0.2969  0.1082  155 GLN B NE2 
6431  N N   . LEU B 156 ? 0.8451 1.0879 1.1861 0.2400  0.3763  0.1329  156 LEU B N   
6432  C CA  . LEU B 156 ? 0.7782 1.0558 1.1303 0.2242  0.3976  0.1401  156 LEU B CA  
6433  C C   . LEU B 156 ? 0.7717 1.0306 1.1242 0.1948  0.3990  0.1547  156 LEU B C   
6434  O O   . LEU B 156 ? 0.8396 1.0826 1.2028 0.1858  0.3841  0.1552  156 LEU B O   
6435  C CB  . LEU B 156 ? 0.6250 0.9610 1.0154 0.2247  0.4005  0.1310  156 LEU B CB  
6436  C CG  . LEU B 156 ? 0.6353 0.9910 1.0276 0.2516  0.3931  0.1129  156 LEU B CG  
6437  C CD1 . LEU B 156 ? 0.6310 1.0422 1.0662 0.2527  0.3921  0.1031  156 LEU B CD1 
6438  C CD2 . LEU B 156 ? 0.7770 1.1374 1.1435 0.2583  0.4045  0.1079  156 LEU B CD2 
6439  N N   . GLY B 157 ? 0.6565 0.9173 0.9971 0.1801  0.4158  0.1662  157 GLY B N   
6440  C CA  . GLY B 157 ? 0.7573 0.9968 1.0972 0.1527  0.4169  0.1808  157 GLY B CA  
6441  C C   . GLY B 157 ? 0.8278 1.0097 1.1284 0.1526  0.4083  0.1866  157 GLY B C   
6442  O O   . GLY B 157 ? 1.0125 1.1721 1.2867 0.1728  0.4019  0.1791  157 GLY B O   
6443  N N   . GLU B 158 ? 0.8352 0.9924 1.1327 0.1302  0.4075  0.1990  158 GLU B N   
6444  C CA  . GLU B 158 ? 0.9248 1.0292 1.1875 0.1298  0.3985  0.2038  158 GLU B CA  
6445  C C   . GLU B 158 ? 0.9028 0.9783 1.1723 0.1246  0.3784  0.1981  158 GLU B C   
6446  O O   . GLU B 158 ? 1.0040 1.0968 1.3058 0.1123  0.3735  0.1960  158 GLU B O   
6447  C CB  . GLU B 158 ? 1.1318 1.2225 1.3815 0.1107  0.4097  0.2216  158 GLU B CB  
6448  C CG  . GLU B 158 ? 1.2701 1.3763 1.4966 0.1174  0.4279  0.2284  158 GLU B CG  
6449  C CD  . GLU B 158 ? 1.5884 1.6662 1.7876 0.1036  0.4339  0.2467  158 GLU B CD  
6450  O OE1 . GLU B 158 ? 1.4543 1.4900 1.6449 0.0954  0.4207  0.2512  158 GLU B OE1 
6451  O OE2 . GLU B 158 ? 1.9554 2.0541 2.1416 0.1013  0.4516  0.2563  158 GLU B OE2 
6452  N N   . VAL B 159 ? 0.8799 0.9137 1.1190 0.1334  0.3669  0.1946  159 VAL B N   
6453  C CA  . VAL B 159 ? 0.7400 0.7466 0.9814 0.1286  0.3483  0.1880  159 VAL B CA  
6454  C C   . VAL B 159 ? 0.7763 0.7623 1.0231 0.1065  0.3461  0.1969  159 VAL B C   
6455  O O   . VAL B 159 ? 1.0001 0.9798 1.2369 0.0983  0.3570  0.2096  159 VAL B O   
6456  C CB  . VAL B 159 ? 0.7814 0.7538 0.9895 0.1455  0.3372  0.1794  159 VAL B CB  
6457  C CG1 . VAL B 159 ? 0.8591 0.8476 1.0676 0.1661  0.3348  0.1690  159 VAL B CG1 
6458  C CG2 . VAL B 159 ? 0.7365 0.6837 0.9097 0.1498  0.3441  0.1858  159 VAL B CG2 
6459  N N   . THR B 160 ? 0.7717 0.7472 1.0341 0.0970  0.3316  0.1900  160 THR B N   
6460  C CA  . THR B 160 ? 0.6096 0.5643 0.8808 0.0773  0.3268  0.1951  160 THR B CA  
6461  C C   . THR B 160 ? 0.7016 0.6126 0.9442 0.0816  0.3146  0.1909  160 THR B C   
6462  O O   . THR B 160 ? 0.9295 0.8316 1.1654 0.0895  0.3021  0.1783  160 THR B O   
6463  C CB  . THR B 160 ? 0.7099 0.6840 1.0183 0.0640  0.3182  0.1873  160 THR B CB  
6464  O OG1 . THR B 160 ? 0.8210 0.8376 1.1579 0.0587  0.3301  0.1912  160 THR B OG1 
6465  C CG2 . THR B 160 ? 0.6509 0.6014 0.9704 0.0450  0.3105  0.1884  160 THR B CG2 
6466  N N   . LEU B 161 ? 0.7507 0.6357 0.9770 0.0756  0.3180  0.2015  161 LEU B N   
6467  C CA  . LEU B 161 ? 0.6561 0.5006 0.8568 0.0799  0.3058  0.1967  161 LEU B CA  
6468  C C   . LEU B 161 ? 0.6804 0.5058 0.8989 0.0620  0.2969  0.1978  161 LEU B C   
6469  O O   . LEU B 161 ? 0.8406 0.6765 1.0814 0.0467  0.3042  0.2086  161 LEU B O   
6470  C CB  . LEU B 161 ? 0.6431 0.4709 0.8081 0.0905  0.3141  0.2067  161 LEU B CB  
6471  C CG  . LEU B 161 ? 0.6419 0.4851 0.7876 0.1098  0.3217  0.2028  161 LEU B CG  
6472  C CD1 . LEU B 161 ? 0.8610 0.6873 0.9704 0.1195  0.3286  0.2108  161 LEU B CD1 
6473  C CD2 . LEU B 161 ? 0.7787 0.6165 0.9199 0.1211  0.3089  0.1855  161 LEU B CD2 
6474  N N   . PRO B 162 ? 0.6925 0.4913 0.9037 0.0631  0.2813  0.1860  162 PRO B N   
6475  C CA  . PRO B 162 ? 0.7197 0.5002 0.9499 0.0482  0.2710  0.1833  162 PRO B CA  
6476  C C   . PRO B 162 ? 0.7392 0.4946 0.9612 0.0412  0.2755  0.2006  162 PRO B C   
6477  O O   . PRO B 162 ? 0.9142 0.6583 1.1061 0.0511  0.2824  0.2113  162 PRO B O   
6478  C CB  . PRO B 162 ? 0.7781 0.5373 0.9940 0.0557  0.2550  0.1658  162 PRO B CB  
6479  C CG  . PRO B 162 ? 0.7607 0.5153 0.9412 0.0742  0.2591  0.1658  162 PRO B CG  
6480  C CD  . PRO B 162 ? 0.7344 0.5208 0.9204 0.0783  0.2727  0.1730  162 PRO B CD  
6481  N N   . PRO B 163 ? 0.8054 0.5510 1.0535 0.0239  0.2709  0.2037  163 PRO B N   
6482  C CA  . PRO B 163 ? 0.8789 0.5974 1.1205 0.0155  0.2740  0.2225  163 PRO B CA  
6483  C C   . PRO B 163 ? 0.9047 0.5838 1.1143 0.0272  0.2637  0.2228  163 PRO B C   
6484  O O   . PRO B 163 ? 0.9078 0.5695 1.0957 0.0280  0.2700  0.2416  163 PRO B O   
6485  C CB  . PRO B 163 ? 0.6985 0.4114 0.9784 -0.0039 0.2659  0.2185  163 PRO B CB  
6486  C CG  . PRO B 163 ? 0.8842 0.6359 1.1929 -0.0078 0.2659  0.2029  163 PRO B CG  
6487  C CD  . PRO B 163 ? 0.7065 0.4666 0.9918 0.0113  0.2622  0.1894  163 PRO B CD  
6488  N N   . SER B 164 ? 0.8621 0.5301 1.0692 0.0354  0.2483  0.2021  164 SER B N   
6489  C CA  . SER B 164 ? 0.7389 0.3732 0.9192 0.0462  0.2358  0.1987  164 SER B CA  
6490  C C   . SER B 164 ? 0.8159 0.4476 0.9570 0.0596  0.2459  0.2124  164 SER B C   
6491  O O   . SER B 164 ? 1.0397 0.6499 1.1565 0.0649  0.2366  0.2157  164 SER B O   
6492  C CB  . SER B 164 ? 0.6810 0.3130 0.8653 0.0524  0.2203  0.1727  164 SER B CB  
6493  O OG  . SER B 164 ? 0.9330 0.5841 1.1024 0.0638  0.2253  0.1639  164 SER B OG  
6494  N N   . LEU B 165 ? 0.8608 0.5191 0.9954 0.0650  0.2613  0.2166  165 LEU B N   
6495  C CA  . LEU B 165 ? 0.7768 0.4350 0.8750 0.0789  0.2712  0.2265  165 LEU B CA  
6496  C C   . LEU B 165 ? 0.8462 0.4949 0.9310 0.0726  0.2819  0.2525  165 LEU B C   
6497  O O   . LEU B 165 ? 0.9594 0.6296 1.0606 0.0604  0.2954  0.2653  165 LEU B O   
6498  C CB  . LEU B 165 ? 0.7068 0.4007 0.8064 0.0858  0.2826  0.2207  165 LEU B CB  
6499  C CG  . LEU B 165 ? 0.7908 0.4913 0.8564 0.1013  0.2937  0.2265  165 LEU B CG  
6500  C CD1 . LEU B 165 ? 0.8473 0.5232 0.8819 0.1166  0.2830  0.2158  165 LEU B CD1 
6501  C CD2 . LEU B 165 ? 0.8354 0.5698 0.9090 0.1077  0.3031  0.2194  165 LEU B CD2 
6502  N N   . PRO B 166 ? 0.8515 0.4768 0.9066 0.0791  0.2727  0.2567  166 PRO B N   
6503  C CA  . PRO B 166 ? 0.9678 0.5884 1.0080 0.0712  0.2794  0.2798  166 PRO B CA  
6504  C C   . PRO B 166 ? 1.0273 0.6764 1.0564 0.0716  0.3034  0.2956  166 PRO B C   
6505  O O   . PRO B 166 ? 0.8954 0.5597 0.9107 0.0862  0.3137  0.2898  166 PRO B O   
6506  C CB  . PRO B 166 ? 1.0020 0.5957 1.0077 0.0835  0.2656  0.2788  166 PRO B CB  
6507  C CG  . PRO B 166 ? 0.9907 0.5718 1.0058 0.0903  0.2466  0.2543  166 PRO B CG  
6508  C CD  . PRO B 166 ? 0.9745 0.5787 1.0092 0.0925  0.2548  0.2405  166 PRO B CD  
6509  N N   . GLU B 167 ? 1.0620 0.7188 1.0963 0.0552  0.3117  0.3147  167 GLU B N   
6510  C CA  . GLU B 167 ? 1.0394 0.7291 1.0643 0.0532  0.3341  0.3285  167 GLU B CA  
6511  C C   . GLU B 167 ? 0.9619 0.6484 0.9418 0.0694  0.3386  0.3341  167 GLU B C   
6512  O O   . GLU B 167 ? 1.1068 0.8236 1.0751 0.0763  0.3565  0.3365  167 GLU B O   
6513  C CB  . GLU B 167 ? 1.1871 0.8846 1.2260 0.0295  0.3397  0.3468  167 GLU B CB  
6514  C CG  . GLU B 167 ? 1.2279 0.9434 1.3129 0.0130  0.3425  0.3417  167 GLU B CG  
6515  C CD  . GLU B 167 ? 1.3542 1.1151 1.4576 0.0165  0.3610  0.3353  167 GLU B CD  
6516  O OE1 . GLU B 167 ? 1.5209 1.3058 1.6024 0.0266  0.3758  0.3393  167 GLU B OE1 
6517  O OE2 . GLU B 167 ? 1.2619 1.0360 1.4025 0.0095  0.3600  0.3250  167 GLU B OE2 
6518  N N   . LYS B 168 ? 0.9245 0.5768 0.8798 0.0760  0.3220  0.3346  168 LYS B N   
6519  C CA  . LYS B 168 ? 0.9454 0.5932 0.8575 0.0918  0.3243  0.3388  168 LYS B CA  
6520  C C   . LYS B 168 ? 0.9301 0.5892 0.8326 0.1128  0.3301  0.3209  168 LYS B C   
6521  O O   . LYS B 168 ? 1.1242 0.8030 1.0021 0.1239  0.3444  0.3234  168 LYS B O   
6522  C CB  . LYS B 168 ? 0.9688 0.5775 0.8617 0.0951  0.3024  0.3403  168 LYS B CB  
6523  C CG  . LYS B 168 ? 1.0080 0.6004 0.9054 0.0751  0.2955  0.3600  168 LYS B CG  
6524  C CD  . LYS B 168 ? 1.0346 0.5886 0.9124 0.0802  0.2728  0.3620  168 LYS B CD  
6525  C CE  . LYS B 168 ? 1.0875 0.6262 0.9529 0.0637  0.2696  0.3876  168 LYS B CE  
6526  N NZ  . LYS B 168 ? 1.4164 0.9136 1.2791 0.0640  0.2433  0.3877  168 LYS B NZ  
6527  N N   . ARG B 169 ? 0.9917 0.6398 0.9145 0.1173  0.3187  0.3021  169 ARG B N   
6528  C CA  . ARG B 169 ? 0.9065 0.5659 0.8248 0.1342  0.3179  0.2799  169 ARG B CA  
6529  C C   . ARG B 169 ? 0.9457 0.6467 0.8784 0.1344  0.3349  0.2766  169 ARG B C   
6530  O O   . ARG B 169 ? 1.0389 0.7559 0.9541 0.1498  0.3408  0.2665  169 ARG B O   
6531  C CB  . ARG B 169 ? 0.9442 0.5872 0.8854 0.1337  0.2997  0.2600  169 ARG B CB  
6532  C CG  . ARG B 169 ? 0.8309 0.4815 0.7671 0.1487  0.2944  0.2355  169 ARG B CG  
6533  C CD  . ARG B 169 ? 0.9242 0.5690 0.8218 0.1668  0.2944  0.2301  169 ARG B CD  
6534  N NE  . ARG B 169 ? 0.9499 0.5663 0.8228 0.1697  0.2856  0.2390  169 ARG B NE  
6535  C CZ  . ARG B 169 ? 0.9995 0.6071 0.8391 0.1849  0.2817  0.2331  169 ARG B CZ  
6536  N NH1 . ARG B 169 ? 0.9622 0.5853 0.7896 0.1979  0.2864  0.2176  169 ARG B NH1 
6537  N NH2 . ARG B 169 ? 0.9434 0.5256 0.7619 0.1877  0.2723  0.2422  169 ARG B NH2 
6538  N N   . LYS B 170 ? 1.0325 0.7515 0.9981 0.1179  0.3422  0.2841  170 LYS B N   
6539  C CA  . LYS B 170 ? 0.9397 0.7009 0.9230 0.1181  0.3574  0.2804  170 LYS B CA  
6540  C C   . LYS B 170 ? 0.9636 0.7483 0.9216 0.1237  0.3759  0.2916  170 LYS B C   
6541  O O   . LYS B 170 ? 0.9609 0.7717 0.9143 0.1378  0.3835  0.2795  170 LYS B O   
6542  C CB  . LYS B 170 ? 0.8039 0.5807 0.8279 0.0977  0.3613  0.2869  170 LYS B CB  
6543  C CG  . LYS B 170 ? 0.8765 0.6389 0.9282 0.0931  0.3443  0.2721  170 LYS B CG  
6544  C CD  . LYS B 170 ? 0.8044 0.5962 0.8979 0.0794  0.3492  0.2698  170 LYS B CD  
6545  C CE  . LYS B 170 ? 0.8899 0.6682 1.0069 0.0570  0.3463  0.2821  170 LYS B CE  
6546  N NZ  . LYS B 170 ? 1.0550 0.8686 1.2109 0.0424  0.3552  0.2825  170 LYS B NZ  
6547  N N   . GLU B 171 ? 0.9691 0.7443 0.9100 0.1128  0.3824  0.3145  171 GLU B N   
6548  C CA  . GLU B 171 ? 0.9562 0.7554 0.8701 0.1159  0.4004  0.3268  171 GLU B CA  
6549  C C   . GLU B 171 ? 0.9099 0.7025 0.7857 0.1387  0.3971  0.3154  171 GLU B C   
6550  O O   . GLU B 171 ? 0.9935 0.8168 0.8541 0.1481  0.4115  0.3127  171 GLU B O   
6551  C CB  . GLU B 171 ? 0.9958 0.7847 0.8998 0.0972  0.3976  0.3480  171 GLU B CB  
6552  C CG  . GLU B 171 ? 1.2055 1.0289 1.1336 0.0764  0.4109  0.3587  171 GLU B CG  
6553  C CD  . GLU B 171 ? 1.4326 1.3053 1.3544 0.0831  0.4303  0.3542  171 GLU B CD  
6554  O OE1 . GLU B 171 ? 1.5644 1.4449 1.4526 0.0861  0.4358  0.3618  171 GLU B OE1 
6555  O OE2 . GLU B 171 ? 1.4407 1.3456 1.3918 0.0859  0.4389  0.3418  171 GLU B OE2 
6556  N N   . LEU B 172 ? 0.9424 0.6975 0.8042 0.1475  0.3783  0.3070  172 LEU B N   
6557  C CA  . LEU B 172 ? 0.9075 0.6553 0.7353 0.1684  0.3735  0.2940  172 LEU B CA  
6558  C C   . LEU B 172 ? 0.9878 0.7595 0.8267 0.1830  0.3764  0.2698  172 LEU B C   
6559  O O   . LEU B 172 ? 1.0861 0.8751 0.9028 0.1977  0.3845  0.2621  172 LEU B O   
6560  C CB  . LEU B 172 ? 0.9048 0.6097 0.7222 0.1729  0.3516  0.2879  172 LEU B CB  
6561  C CG  . LEU B 172 ? 0.9038 0.5983 0.6903 0.1936  0.3433  0.2708  172 LEU B CG  
6562  C CD1 . LEU B 172 ? 1.1768 0.8875 0.9259 0.2026  0.3558  0.2793  172 LEU B CD1 
6563  C CD2 . LEU B 172 ? 1.1463 0.8016 0.9245 0.1953  0.3226  0.2678  172 LEU B CD2 
6564  N N   . TRP B 173 ? 0.9200 0.6928 0.7933 0.1790  0.3695  0.2580  173 TRP B N   
6565  C CA  . TRP B 173 ? 0.8892 0.6813 0.7746 0.1920  0.3705  0.2371  173 TRP B CA  
6566  C C   . TRP B 173 ? 0.9783 0.8134 0.8696 0.1945  0.3903  0.2400  173 TRP B C   
6567  O O   . TRP B 173 ? 1.0786 0.9293 0.9593 0.2115  0.3949  0.2258  173 TRP B O   
6568  C CB  . TRP B 173 ? 0.8251 0.6133 0.7463 0.1847  0.3600  0.2277  173 TRP B CB  
6569  C CG  . TRP B 173 ? 0.7687 0.5213 0.6883 0.1837  0.3405  0.2189  173 TRP B CG  
6570  C CD1 . TRP B 173 ? 0.8295 0.5552 0.7206 0.1930  0.3302  0.2126  173 TRP B CD1 
6571  C CD2 . TRP B 173 ? 0.7983 0.5426 0.7475 0.1729  0.3291  0.2131  173 TRP B CD2 
6572  N NE1 . TRP B 173 ? 0.8410 0.5427 0.7430 0.1882  0.3135  0.2032  173 TRP B NE1 
6573  C CE2 . TRP B 173 ? 0.9047 0.6174 0.8418 0.1758  0.3126  0.2033  173 TRP B CE2 
6574  C CE3 . TRP B 173 ? 0.8670 0.6299 0.8523 0.1609  0.3310  0.2143  173 TRP B CE3 
6575  C CZ2 . TRP B 173 ? 0.9875 0.6879 0.9469 0.1667  0.2990  0.1946  173 TRP B CZ2 
6576  C CZ3 . TRP B 173 ? 0.7050 0.4545 0.7113 0.1522  0.3169  0.2060  173 TRP B CZ3 
6577  C CH2 . TRP B 173 ? 0.8082 0.5273 0.8015 0.1550  0.3014  0.1962  173 TRP B CH2 
6578  N N   . ARG B 174 ? 0.8939 0.7489 0.8032 0.1774  0.4020  0.2574  174 ARG B N   
6579  C CA  . ARG B 174 ? 0.8443 0.7452 0.7620 0.1774  0.4221  0.2603  174 ARG B CA  
6580  C C   . ARG B 174 ? 0.8732 0.7862 0.7529 0.1898  0.4331  0.2614  174 ARG B C   
6581  O O   . ARG B 174 ? 0.8724 0.8158 0.7516 0.2044  0.4423  0.2475  174 ARG B O   
6582  C CB  . ARG B 174 ? 0.8567 0.7733 0.7962 0.1533  0.4327  0.2811  174 ARG B CB  
6583  C CG  . ARG B 174 ? 0.9449 0.8678 0.9287 0.1420  0.4270  0.2766  174 ARG B CG  
6584  C CD  . ARG B 174 ? 1.0318 0.9811 1.0393 0.1193  0.4413  0.2942  174 ARG B CD  
6585  N NE  . ARG B 174 ? 1.0530 0.9722 1.0755 0.0990  0.4314  0.3068  174 ARG B NE  
6586  C CZ  . ARG B 174 ? 1.2786 1.1979 1.3382 0.0894  0.4229  0.3003  174 ARG B CZ  
6587  N NH1 . ARG B 174 ? 0.9215 0.8690 1.0064 0.0982  0.4224  0.2828  174 ARG B NH1 
6588  N NH2 . ARG B 174 ? 1.2856 1.1765 1.3572 0.0714  0.4139  0.3108  174 ARG B NH2 
6589  N N   . LYS B 175 ? 1.0226 0.9116 0.8706 0.1849  0.4310  0.2770  175 LYS B N   
6590  C CA  . LYS B 175 ? 0.9357 0.8354 0.7457 0.1947  0.4375  0.2780  175 LYS B CA  
6591  C C   . LYS B 175 ? 0.9203 0.8155 0.7124 0.2200  0.4327  0.2540  175 LYS B C   
6592  O O   . LYS B 175 ? 1.0720 0.9932 0.8489 0.2305  0.4377  0.2435  175 LYS B O   
6593  C CB  . LYS B 175 ? 1.1788 1.0470 0.9597 0.1851  0.4300  0.2985  175 LYS B CB  
6594  C CG  . LYS B 175 ? 1.3490 1.2366 1.0958 0.1869  0.4364  0.3047  175 LYS B CG  
6595  C CD  . LYS B 175 ? 1.5509 1.4010 1.2602 0.1896  0.4240  0.3157  175 LYS B CD  
6596  C CE  . LYS B 175 ? 1.5431 1.4136 1.2163 0.1918  0.4297  0.3215  175 LYS B CE  
6597  N NZ  . LYS B 175 ? 1.7383 1.6385 1.4004 0.2121  0.4361  0.2975  175 LYS B NZ  
6598  N N   . LEU B 176 ? 0.9875 0.8503 0.7867 0.2262  0.4143  0.2403  176 LEU B N   
6599  C CA  . LEU B 176 ? 1.0357 0.8893 0.8210 0.2471  0.4059  0.2161  176 LEU B CA  
6600  C C   . LEU B 176 ? 0.9939 0.8720 0.8048 0.2582  0.4097  0.1967  176 LEU B C   
6601  O O   . LEU B 176 ? 0.9478 0.8263 0.7476 0.2755  0.4056  0.1769  176 LEU B O   
6602  C CB  . LEU B 176 ? 0.8673 0.6770 0.6502 0.2465  0.3845  0.2102  176 LEU B CB  
6603  C CG  . LEU B 176 ? 0.8611 0.6539 0.6245 0.2646  0.3738  0.1877  176 LEU B CG  
6604  C CD1 . LEU B 176 ? 0.9888 0.7836 0.7120 0.2750  0.3780  0.1886  176 LEU B CD1 
6605  C CD2 . LEU B 176 ? 1.0179 0.7739 0.7862 0.2606  0.3542  0.1816  176 LEU B CD2 
6606  N N   . GLY B 177 ? 0.9493 0.8464 0.7955 0.2475  0.4146  0.2018  177 GLY B N   
6607  C CA  . GLY B 177 ? 0.8707 0.7913 0.7442 0.2574  0.4168  0.1857  177 GLY B CA  
6608  C C   . GLY B 177 ? 0.8429 0.7360 0.7331 0.2599  0.3986  0.1733  177 GLY B C   
6609  O O   . GLY B 177 ? 0.9739 0.8749 0.8770 0.2720  0.3937  0.1567  177 GLY B O   
6610  N N   . VAL B 178 ? 0.9529 0.8133 0.8433 0.2472  0.3856  0.1806  178 VAL B N   
6611  C CA  . VAL B 178 ? 0.8386 0.6742 0.7429 0.2470  0.3684  0.1694  178 VAL B CA  
6612  C C   . VAL B 178 ? 0.8113 0.6482 0.7480 0.2286  0.3642  0.1788  178 VAL B C   
6613  O O   . VAL B 178 ? 0.8396 0.6538 0.7845 0.2242  0.3495  0.1726  178 VAL B O   
6614  C CB  . VAL B 178 ? 0.7606 0.5578 0.6383 0.2508  0.3541  0.1622  178 VAL B CB  
6615  C CG1 . VAL B 178 ? 0.9348 0.7315 0.7824 0.2693  0.3572  0.1499  178 VAL B CG1 
6616  C CG2 . VAL B 178 ? 0.8034 0.5818 0.6715 0.2370  0.3505  0.1778  178 VAL B CG2 
6617  N N   . TYR B 179 ? 0.8396 0.7049 0.7948 0.2176  0.3771  0.1923  179 TYR B N   
6618  C CA  . TYR B 179 ? 0.7311 0.6010 0.7204 0.2000  0.3734  0.1993  179 TYR B CA  
6619  C C   . TYR B 179 ? 0.8162 0.6933 0.8289 0.2068  0.3645  0.1843  179 TYR B C   
6620  O O   . TYR B 179 ? 0.9325 0.8272 0.9447 0.2229  0.3688  0.1737  179 TYR B O   
6621  C CB  . TYR B 179 ? 0.8583 0.7610 0.8645 0.1867  0.3901  0.2150  179 TYR B CB  
6622  C CG  . TYR B 179 ? 0.7851 0.6835 0.8187 0.1647  0.3861  0.2259  179 TYR B CG  
6623  C CD1 . TYR B 179 ? 0.9881 0.8570 1.0109 0.1513  0.3811  0.2391  179 TYR B CD1 
6624  C CD2 . TYR B 179 ? 0.7449 0.6682 0.8159 0.1581  0.3862  0.2220  179 TYR B CD2 
6625  C CE1 . TYR B 179 ? 1.0938 0.9569 1.1433 0.1314  0.3767  0.2474  179 TYR B CE1 
6626  C CE2 . TYR B 179 ? 0.7100 0.6306 0.8075 0.1377  0.3823  0.2300  179 TYR B CE2 
6627  C CZ  . TYR B 179 ? 0.9085 0.7980 0.9955 0.1241  0.3776  0.2423  179 TYR B CZ  
6628  O OH  . TYR B 179 ? 1.0497 0.9349 1.1644 0.1041  0.3731  0.2487  179 TYR B OH  
6629  N N   . PRO B 180 ? 0.8569 0.7211 0.8896 0.1955  0.3518  0.1828  180 PRO B N   
6630  C CA  . PRO B 180 ? 0.7913 0.6592 0.8416 0.2016  0.3416  0.1698  180 PRO B CA  
6631  C C   . PRO B 180 ? 0.8251 0.7320 0.9071 0.2026  0.3484  0.1693  180 PRO B C   
6632  O O   . PRO B 180 ? 0.9030 0.8325 1.0051 0.1893  0.3576  0.1798  180 PRO B O   
6633  C CB  . PRO B 180 ? 0.6851 0.5311 0.7461 0.1862  0.3274  0.1698  180 PRO B CB  
6634  C CG  . PRO B 180 ? 0.8011 0.6477 0.8687 0.1694  0.3339  0.1850  180 PRO B CG  
6635  C CD  . PRO B 180 ? 0.9411 0.7864 0.9800 0.1770  0.3458  0.1927  180 PRO B CD  
6636  N N   . ARG B 181 ? 0.7772 0.6907 0.8634 0.2182  0.3432  0.1572  181 ARG B N   
6637  C CA  . ARG B 181 ? 0.6414 0.5913 0.7587 0.2220  0.3464  0.1546  181 ARG B CA  
6638  C C   . ARG B 181 ? 0.6691 0.6083 0.8022 0.2170  0.3292  0.1495  181 ARG B C   
6639  O O   . ARG B 181 ? 0.7043 0.6157 0.8285 0.2058  0.3195  0.1505  181 ARG B O   
6640  C CB  . ARG B 181 ? 0.6535 0.6190 0.7641 0.2452  0.3522  0.1445  181 ARG B CB  
6641  C CG  . ARG B 181 ? 0.7516 0.7337 0.8467 0.2495  0.3701  0.1484  181 ARG B CG  
6642  C CD  . ARG B 181 ? 0.6883 0.6864 0.7766 0.2702  0.3715  0.1348  181 ARG B CD  
6643  N NE  . ARG B 181 ? 0.8406 0.8019 0.8990 0.2803  0.3559  0.1234  181 ARG B NE  
6644  C CZ  . ARG B 181 ? 0.9386 0.9032 0.9854 0.2943  0.3495  0.1092  181 ARG B CZ  
6645  N NH1 . ARG B 181 ? 0.9285 0.9320 0.9909 0.3022  0.3573  0.1032  181 ARG B NH1 
6646  N NH2 . ARG B 181 ? 0.9189 0.8497 0.9402 0.2992  0.3349  0.0996  181 ARG B NH2 
6647  N N   . ALA B 182 ? 0.6446 0.6061 0.8003 0.2250  0.3247  0.1438  182 ALA B N   
6648  C CA  . ALA B 182 ? 0.6891 0.6414 0.8565 0.2198  0.3079  0.1402  182 ALA B CA  
6649  C C   . ALA B 182 ? 0.7773 0.6883 0.9154 0.2257  0.2948  0.1335  182 ALA B C   
6650  O O   . ALA B 182 ? 0.7723 0.6677 0.8868 0.2402  0.2974  0.1286  182 ALA B O   
6651  C CB  . ALA B 182 ? 0.7549 0.7381 0.9486 0.2302  0.3047  0.1358  182 ALA B CB  
6652  N N   . VAL B 183 ? 0.6944 0.6561 0.8402 0.1284  0.2648  0.1596  183 VAL B N   
6653  C CA  . VAL B 183 ? 0.7161 0.6655 0.8494 0.1311  0.2519  0.1555  183 VAL B CA  
6654  C C   . VAL B 183 ? 0.7397 0.6895 0.8704 0.1404  0.2478  0.1525  183 VAL B C   
6655  O O   . VAL B 183 ? 0.7424 0.6763 0.8532 0.1480  0.2461  0.1501  183 VAL B O   
6656  C CB  . VAL B 183 ? 0.6300 0.5848 0.7746 0.1215  0.2415  0.1536  183 VAL B CB  
6657  C CG1 . VAL B 183 ? 0.6331 0.5744 0.7632 0.1239  0.2300  0.1495  183 VAL B CG1 
6658  C CG2 . VAL B 183 ? 0.6747 0.6286 0.8231 0.1123  0.2457  0.1559  183 VAL B CG2 
6659  N N   . ASP B 184 ? 0.7026 0.6697 0.8530 0.1398  0.2456  0.1524  184 ASP B N   
6660  C CA  . ASP B 184 ? 0.7112 0.6770 0.8597 0.1487  0.2411  0.1500  184 ASP B CA  
6661  C C   . ASP B 184 ? 0.7368 0.6964 0.8738 0.1596  0.2505  0.1500  184 ASP B C   
6662  O O   . ASP B 184 ? 0.7876 0.7352 0.9122 0.1678  0.2467  0.1467  184 ASP B O   
6663  C CB  . ASP B 184 ? 0.7112 0.6973 0.8826 0.1471  0.2374  0.1508  184 ASP B CB  
6664  C CG  . ASP B 184 ? 0.8420 0.8377 1.0262 0.1358  0.2304  0.1510  184 ASP B CG  
6665  O OD1 . ASP B 184 ? 0.7159 0.6992 0.8894 0.1310  0.2241  0.1494  184 ASP B OD1 
6666  O OD2 . ASP B 184 ? 0.9913 1.0079 1.1964 0.1323  0.2311  0.1523  184 ASP B OD2 
6667  N N   . ARG B 185 ? 0.6805 0.6478 0.8215 0.1593  0.2628  0.1533  185 ARG B N   
6668  C CA  . ARG B 185 ? 0.7885 0.7521 0.9189 0.1699  0.2734  0.1535  185 ARG B CA  
6669  C C   . ARG B 185 ? 0.7367 0.6757 0.8378 0.1758  0.2714  0.1507  185 ARG B C   
6670  O O   . ARG B 185 ? 0.8298 0.7611 0.9192 0.1865  0.2728  0.1475  185 ARG B O   
6671  C CB  . ARG B 185 ? 0.6466 0.6225 0.7861 0.1663  0.2876  0.1582  185 ARG B CB  
6672  C CG  . ARG B 185 ? 0.6821 0.6576 0.8127 0.1768  0.3002  0.1588  185 ARG B CG  
6673  C CD  . ARG B 185 ? 0.7639 0.7187 0.8666 0.1800  0.3059  0.1599  185 ARG B CD  
6674  N NE  . ARG B 185 ? 0.8697 0.8238 0.9617 0.1908  0.3179  0.1600  185 ARG B NE  
6675  C CZ  . ARG B 185 ? 0.7282 0.6824 0.8173 0.2022  0.3169  0.1557  185 ARG B CZ  
6676  N NH1 . ARG B 185 ? 0.8124 0.7623 0.9038 0.2044  0.3039  0.1511  185 ARG B NH1 
6677  N NH2 . ARG B 185 ? 0.8993 0.8569 0.9826 0.2111  0.3292  0.1560  185 ARG B NH2 
6678  N N   . GLU B 186 ? 0.7286 0.6564 0.8185 0.1697  0.2680  0.1513  186 GLU B N   
6679  C CA  . GLU B 186 ? 0.8174 0.7234 0.8793 0.1755  0.2654  0.1483  186 GLU B CA  
6680  C C   . GLU B 186 ? 0.7867 0.6833 0.8423 0.1789  0.2527  0.1419  186 GLU B C   
6681  O O   . GLU B 186 ? 0.7726 0.6550 0.8084 0.1875  0.2519  0.1376  186 GLU B O   
6682  C CB  . GLU B 186 ? 0.7744 0.6721 0.8277 0.1685  0.2642  0.1508  186 GLU B CB  
6683  C CG  . GLU B 186 ? 0.8536 0.7543 0.9069 0.1662  0.2780  0.1573  186 GLU B CG  
6684  C CD  . GLU B 186 ? 1.0400 0.9267 1.0674 0.1757  0.2866  0.1585  186 GLU B CD  
6685  O OE1 . GLU B 186 ? 0.9575 0.8322 0.9665 0.1844  0.2808  0.1532  186 GLU B OE1 
6686  O OE2 . GLU B 186 ? 1.0551 0.9427 1.0805 0.1742  0.2992  0.1645  186 GLU B OE2 
6687  N N   . ILE B 187 ? 0.7204 0.6242 0.7916 0.1721  0.2434  0.1412  187 ILE B N   
6688  C CA  . ILE B 187 ? 0.6925 0.5872 0.7591 0.1739  0.2323  0.1358  187 ILE B CA  
6689  C C   . ILE B 187 ? 0.7732 0.6653 0.8369 0.1847  0.2358  0.1334  187 ILE B C   
6690  O O   . ILE B 187 ? 0.8769 0.7535 0.9249 0.1904  0.2314  0.1279  187 ILE B O   
6691  C CB  . ILE B 187 ? 0.5855 0.4905 0.6706 0.1651  0.2236  0.1367  187 ILE B CB  
6692  C CG1 . ILE B 187 ? 0.6164 0.5233 0.7036 0.1552  0.2202  0.1381  187 ILE B CG1 
6693  C CG2 . ILE B 187 ? 0.5212 0.4161 0.6016 0.1669  0.2137  0.1320  187 ILE B CG2 
6694  C CD1 . ILE B 187 ? 0.6815 0.6018 0.7877 0.1465  0.2142  0.1395  187 ILE B CD1 
6695  N N   . ALA B 188 ? 0.6922 0.5996 0.7712 0.1875  0.2440  0.1371  188 ALA B N   
6696  C CA  . ALA B 188 ? 0.7305 0.6372 0.8084 0.1987  0.2484  0.1351  188 ALA B CA  
6697  C C   . ALA B 188 ? 0.7687 0.6616 0.8236 0.2077  0.2552  0.1320  188 ALA B C   
6698  O O   . ALA B 188 ? 0.7963 0.6770 0.8395 0.2166  0.2535  0.1267  188 ALA B O   
6699  C CB  . ALA B 188 ? 0.5863 0.5155 0.6863 0.1998  0.2565  0.1397  188 ALA B CB  
6700  N N   . ALA B 189 ? 0.7027 0.5963 0.7498 0.2055  0.2629  0.1351  189 ALA B N   
6701  C CA  . ALA B 189 ? 0.6685 0.5494 0.6917 0.2141  0.2698  0.1330  189 ALA B CA  
6702  C C   . ALA B 189 ? 0.7943 0.6544 0.7953 0.2172  0.2595  0.1257  189 ALA B C   
6703  O O   . ALA B 189 ? 0.9179 0.7667 0.9014 0.2272  0.2616  0.1205  189 ALA B O   
6704  C CB  . ALA B 189 ? 0.6770 0.5608 0.6954 0.2097  0.2789  0.1389  189 ALA B CB  
6705  N N   . VAL B 190 ? 0.7527 0.6083 0.7546 0.2086  0.2485  0.1245  190 VAL B N   
6706  C CA  . VAL B 190 ? 0.6238 0.4623 0.6075 0.2102  0.2382  0.1170  190 VAL B CA  
6707  C C   . VAL B 190 ? 0.8030 0.6354 0.7898 0.2140  0.2321  0.1111  190 VAL B C   
6708  O O   . VAL B 190 ? 0.9912 0.8093 0.9606 0.2214  0.2300  0.1039  190 VAL B O   
6709  C CB  . VAL B 190 ? 0.8104 0.6480 0.7961 0.2001  0.2285  0.1173  190 VAL B CB  
6710  C CG1 . VAL B 190 ? 0.7234 0.5465 0.6943 0.2012  0.2171  0.1085  190 VAL B CG1 
6711  C CG2 . VAL B 190 ? 0.8640 0.7034 0.8431 0.1977  0.2343  0.1228  190 VAL B CG2 
6712  N N   . MET B 191 ? 0.7506 0.5929 0.7586 0.2092  0.2294  0.1140  191 MET B N   
6713  C CA  . MET B 191 ? 0.7758 0.6108 0.7871 0.2128  0.2241  0.1097  191 MET B CA  
6714  C C   . MET B 191 ? 0.7907 0.6207 0.7944 0.2257  0.2319  0.1069  191 MET B C   
6715  O O   . MET B 191 ? 0.8450 0.6606 0.8408 0.2310  0.2277  0.1005  191 MET B O   
6716  C CB  . MET B 191 ? 0.6375 0.4854 0.6723 0.2066  0.2208  0.1149  191 MET B CB  
6717  C CG  . MET B 191 ? 0.8405 0.6907 0.8817 0.1944  0.2115  0.1160  191 MET B CG  
6718  S SD  . MET B 191 ? 0.7657 0.5962 0.7907 0.1908  0.2001  0.1075  191 MET B SD  
6719  C CE  . MET B 191 ? 0.8341 0.6519 0.8597 0.1964  0.1971  0.1037  191 MET B CE  
6720  N N   . HIS B 192 ? 0.7721 0.6136 0.7779 0.2306  0.2438  0.1113  192 HIS B N   
6721  C CA  . HIS B 192 ? 0.8482 0.6874 0.8471 0.2435  0.2526  0.1087  192 HIS B CA  
6722  C C   . HIS B 192 ? 0.8344 0.6559 0.8054 0.2506  0.2532  0.1014  192 HIS B C   
6723  O O   . HIS B 192 ? 0.8815 0.6890 0.8418 0.2586  0.2509  0.0940  192 HIS B O   
6724  C CB  . HIS B 192 ? 0.8543 0.7140 0.8662 0.2454  0.2658  0.1159  192 HIS B CB  
6725  C CG  . HIS B 192 ? 0.7718 0.6312 0.7752 0.2587  0.2768  0.1135  192 HIS B CG  
6726  N ND1 . HIS B 192 ? 0.8251 0.6959 0.8271 0.2610  0.2902  0.1179  192 HIS B ND1 
6727  C CD2 . HIS B 192 ? 0.9237 0.7732 0.9192 0.2682  0.2752  0.1070  192 HIS B CD2 
6728  C CE1 . HIS B 192 ? 0.9535 0.8226 0.9465 0.2703  0.2947  0.1139  192 HIS B CE1 
6729  N NE2 . HIS B 192 ? 0.9083 0.7645 0.8970 0.2753  0.2858  0.1069  192 HIS B NE2 
6730  N N   . SER B 193 ? 0.9418 0.7628 0.8999 0.2480  0.2560  0.1033  193 SER B N   
6731  C CA  . SER B 193 ? 0.8782 0.6839 0.8082 0.2553  0.2563  0.0967  193 SER B CA  
6732  C C   . SER B 193 ? 0.8902 0.6783 0.8083 0.2543  0.2427  0.0869  193 SER B C   
6733  O O   . SER B 193 ? 0.9639 0.7384 0.8604 0.2625  0.2418  0.0787  193 SER B O   
6734  C CB  . SER B 193 ? 0.8416 0.6501 0.7608 0.2523  0.2610  0.1021  193 SER B CB  
6735  O OG  . SER B 193 ? 0.8763 0.6998 0.8052 0.2533  0.2750  0.1104  193 SER B OG  
6736  N N   . THR B 194 ? 0.8103 0.5991 0.7426 0.2440  0.2323  0.0871  194 THR B N   
6737  C CA  . THR B 194 ? 0.8611 0.6348 0.7854 0.2413  0.2198  0.0778  194 THR B CA  
6738  C C   . THR B 194 ? 0.9424 0.7057 0.8698 0.2467  0.2183  0.0722  194 THR B C   
6739  O O   . THR B 194 ? 0.9344 0.6821 0.8522 0.2464  0.2100  0.0629  194 THR B O   
6740  C CB  . THR B 194 ? 0.8435 0.6223 0.7810 0.2281  0.2102  0.0805  194 THR B CB  
6741  O OG1 . THR B 194 ? 0.8985 0.6907 0.8597 0.2229  0.2127  0.0886  194 THR B OG1 
6742  C CG2 . THR B 194 ? 0.8445 0.6274 0.7736 0.2240  0.2089  0.0828  194 THR B CG2 
6743  N N   . HIS B 195 ? 0.8512 0.6227 0.7921 0.2518  0.2263  0.0774  195 HIS B N   
6744  C CA  . HIS B 195 ? 0.8942 0.6554 0.8379 0.2586  0.2257  0.0731  195 HIS B CA  
6745  C C   . HIS B 195 ? 0.8886 0.6331 0.8090 0.2699  0.2278  0.0627  195 HIS B C   
6746  O O   . HIS B 195 ? 1.0695 0.8163 0.9745 0.2753  0.2338  0.0616  195 HIS B O   
6747  C CB  . HIS B 195 ? 0.8646 0.6415 0.8272 0.2634  0.2344  0.0812  195 HIS B CB  
6748  C CG  . HIS B 195 ? 0.9227 0.6908 0.8874 0.2714  0.2341  0.0774  195 HIS B CG  
6749  N ND1 . HIS B 195 ? 1.0325 0.7819 0.9956 0.2692  0.2250  0.0721  195 HIS B ND1 
6750  C CD2 . HIS B 195 ? 1.0103 0.7874 0.9789 0.2793  0.2408  0.0784  195 HIS B CD2 
6751  C CE1 . HIS B 195 ? 1.0729 0.8189 1.0374 0.2764  0.2262  0.0700  195 HIS B CE1 
6752  N NE2 . HIS B 195 ? 0.8027 0.5659 0.7712 0.2829  0.2353  0.0736  195 HIS B NE2 
6753  N N   . ILE B 196 ? 0.8953 0.6228 0.8131 0.2737  0.2232  0.0553  196 ILE B N   
6754  C CA  . ILE B 196 ? 0.8163 0.5254 0.7115 0.2841  0.2238  0.0433  196 ILE B CA  
6755  C C   . ILE B 196 ? 1.0021 0.7209 0.8894 0.2951  0.2353  0.0447  196 ILE B C   
6756  O O   . ILE B 196 ? 1.1325 0.8680 1.0362 0.2958  0.2416  0.0529  196 ILE B O   
6757  C CB  . ILE B 196 ? 0.9539 0.6431 0.8507 0.2858  0.2180  0.0362  196 ILE B CB  
6758  C CG1 . ILE B 196 ? 0.9498 0.6171 0.8232 0.2914  0.2139  0.0214  196 ILE B CG1 
6759  C CG2 . ILE B 196 ? 1.1074 0.8050 1.0169 0.2907  0.2227  0.0410  196 ILE B CG2 
6760  C CD1 . ILE B 196 ? 0.9762 0.6413 0.8378 0.3034  0.2202  0.0160  196 ILE B CD1 
6761  N N   . GLY B 197 ? 1.0158 0.7262 0.8790 0.3023  0.2373  0.0368  197 GLY B N   
6762  C CA  . GLY B 197 ? 0.8767 0.5950 0.7292 0.3119  0.2477  0.0371  197 GLY B CA  
6763  C C   . GLY B 197 ? 0.9599 0.6989 0.8171 0.3105  0.2580  0.0485  197 GLY B C   
6764  O O   . GLY B 197 ? 0.9593 0.7095 0.8161 0.3166  0.2680  0.0517  197 GLY B O   
6765  N N   . CYS B 198 ? 0.9876 0.7316 0.8495 0.3026  0.2561  0.0546  198 CYS B N   
6766  C CA  . CYS B 198 ? 0.8934 0.6549 0.7597 0.3005  0.2663  0.0655  198 CYS B CA  
6767  C C   . CYS B 198 ? 1.0387 0.7944 0.8806 0.3010  0.2658  0.0641  198 CYS B C   
6768  O O   . CYS B 198 ? 0.9648 0.7112 0.7826 0.3116  0.2695  0.0575  198 CYS B O   
6769  C CB  . CYS B 198 ? 0.8083 0.5847 0.7023 0.2890  0.2646  0.0755  198 CYS B CB  
6770  S SG  . CYS B 198 ? 1.2566 1.0464 1.1785 0.2887  0.2666  0.0798  198 CYS B SG  
6771  N N   . ASN B 199 ? 0.9478 0.7089 0.7947 0.2901  0.2606  0.0701  199 ASN B N   
6772  C CA  . ASN B 199 ? 0.9014 0.6577 0.7259 0.2905  0.2591  0.0698  199 ASN B CA  
6773  C C   . ASN B 199 ? 1.0149 0.7544 0.8206 0.2924  0.2458  0.0570  199 ASN B C   
6774  O O   . ASN B 199 ? 1.1050 0.8396 0.9218 0.2852  0.2343  0.0518  199 ASN B O   
6775  C CB  . ASN B 199 ? 0.9051 0.6715 0.7423 0.2787  0.2573  0.0796  199 ASN B CB  
6776  C CG  . ASN B 199 ? 1.0833 0.8452 0.8979 0.2801  0.2573  0.0815  199 ASN B CG  
6777  O OD1 . ASN B 199 ? 1.0292 0.7959 0.8361 0.2835  0.2695  0.0895  199 ASN B OD1 
6778  N ND2 . ASN B 199 ? 1.0085 0.7612 0.8122 0.2776  0.2437  0.0744  199 ASN B ND2 
6779  N N   . ALA B 200 ? 1.0328 0.7639 0.8096 0.3019  0.2475  0.0516  200 ALA B N   
6780  C CA  . ALA B 200 ? 0.9593 0.6760 0.7161 0.3046  0.2349  0.0383  200 ALA B CA  
6781  C C   . ALA B 200 ? 1.1302 0.8453 0.8609 0.3092  0.2348  0.0395  200 ALA B C   
6782  O O   . ALA B 200 ? 1.0844 0.7898 0.7885 0.3193  0.2331  0.0303  200 ALA B O   
6783  C CB  . ALA B 200 ? 1.1551 0.8601 0.9002 0.3153  0.2364  0.0267  200 ALA B CB  
6784  N N   . ASP B 201 ? 1.0630 0.7873 0.8011 0.3020  0.2364  0.0508  201 ASP B N   
6785  C CA  . ASP B 201 ? 1.0377 0.7603 0.7532 0.3056  0.2363  0.0544  201 ASP B CA  
6786  C C   . ASP B 201 ? 1.0525 0.7806 0.7830 0.2936  0.2273  0.0596  201 ASP B C   
6787  O O   . ASP B 201 ? 1.0385 0.7766 0.7925 0.2849  0.2324  0.0696  201 ASP B O   
6788  C CB  . ASP B 201 ? 0.9494 0.6766 0.6556 0.3119  0.2543  0.0661  201 ASP B CB  
6789  C CG  . ASP B 201 ? 1.1863 0.9085 0.8640 0.3180  0.2558  0.0703  201 ASP B CG  
6790  O OD1 . ASP B 201 ? 1.2251 0.9428 0.8941 0.3162  0.2424  0.0659  201 ASP B OD1 
6791  O OD2 . ASP B 201 ? 1.2403 0.9631 0.9040 0.3250  0.2707  0.0781  201 ASP B OD2 
6792  N N   . ALA B 202 ? 1.0641 0.7870 0.7819 0.2935  0.2136  0.0520  202 ALA B N   
6793  C CA  . ALA B 202 ? 0.9211 0.6497 0.6525 0.2832  0.2043  0.0555  202 ALA B CA  
6794  C C   . ALA B 202 ? 1.0382 0.7722 0.7708 0.2812  0.2137  0.0704  202 ALA B C   
6795  O O   . ALA B 202 ? 1.0552 0.7974 0.8117 0.2705  0.2137  0.0773  202 ALA B O   
6796  C CB  . ALA B 202 ? 1.0163 0.7397 0.7308 0.2859  0.1890  0.0444  202 ALA B CB  
6797  N N   . GLU B 203 ? 1.0843 0.8131 0.7911 0.2912  0.2222  0.0754  203 GLU B N   
6798  C CA  . GLU B 203 ? 1.0354 0.7665 0.7413 0.2892  0.2320  0.0898  203 GLU B CA  
6799  C C   . GLU B 203 ? 1.0402 0.7812 0.7732 0.2807  0.2446  0.0999  203 GLU B C   
6800  O O   . GLU B 203 ? 0.8925 0.6386 0.6405 0.2720  0.2462  0.1087  203 GLU B O   
6801  C CB  . GLU B 203 ? 1.1055 0.8278 0.7774 0.3022  0.2412  0.0939  203 GLU B CB  
6802  C CG  . GLU B 203 ? 1.2680 0.9818 0.9120 0.3106  0.2287  0.0870  203 GLU B CG  
6803  C CD  . GLU B 203 ? 1.3864 1.0915 0.9974 0.3221  0.2376  0.0950  203 GLU B CD  
6804  O OE1 . GLU B 203 ? 1.4656 1.1710 1.0790 0.3201  0.2529  0.1089  203 GLU B OE1 
6805  O OE2 . GLU B 203 ? 1.4889 1.1869 1.0713 0.3330  0.2293  0.0875  203 GLU B OE2 
6806  N N   . ALA B 204 ? 1.0983 0.8427 0.8377 0.2836  0.2532  0.0982  204 ALA B N   
6807  C CA  . ALA B 204 ? 0.7678 0.5239 0.5334 0.2767  0.2649  0.1069  204 ALA B CA  
6808  C C   . ALA B 204 ? 0.9606 0.7251 0.7570 0.2644  0.2555  0.1056  204 ALA B C   
6809  O O   . ALA B 204 ? 1.1137 0.8877 0.9306 0.2553  0.2603  0.1144  204 ALA B O   
6810  C CB  . ALA B 204 ? 1.0422 0.8002 0.8056 0.2848  0.2756  0.1043  204 ALA B CB  
6811  N N   . MET B 205 ? 0.8828 0.6436 0.6824 0.2636  0.2425  0.0946  205 MET B N   
6812  C CA  . MET B 205 ? 0.8742 0.6421 0.7011 0.2523  0.2336  0.0934  205 MET B CA  
6813  C C   . MET B 205 ? 0.9166 0.6881 0.7510 0.2431  0.2271  0.0981  205 MET B C   
6814  O O   . MET B 205 ? 0.8583 0.6398 0.7168 0.2333  0.2278  0.1038  205 MET B O   
6815  C CB  . MET B 205 ? 0.9329 0.6935 0.7582 0.2532  0.2213  0.0805  205 MET B CB  
6816  C CG  . MET B 205 ? 0.8114 0.5783 0.6641 0.2428  0.2148  0.0799  205 MET B CG  
6817  S SD  . MET B 205 ? 1.0192 0.7923 0.8905 0.2447  0.2249  0.0830  205 MET B SD  
6818  C CE  . MET B 205 ? 0.7466 0.5371 0.6434 0.2345  0.2313  0.0962  205 MET B CE  
6819  N N   . ILE B 206 ? 0.9887 0.7524 0.8023 0.2470  0.2205  0.0955  206 ILE B N   
6820  C CA  . ILE B 206 ? 0.8523 0.6183 0.6708 0.2402  0.2140  0.0993  206 ILE B CA  
6821  C C   . ILE B 206 ? 0.9380 0.7082 0.7628 0.2367  0.2267  0.1125  206 ILE B C   
6822  O O   . ILE B 206 ? 0.9581 0.7342 0.7998 0.2274  0.2241  0.1169  206 ILE B O   
6823  C CB  . ILE B 206 ? 0.7321 0.4893 0.5260 0.2469  0.2035  0.0929  206 ILE B CB  
6824  C CG1 . ILE B 206 ? 0.8478 0.6018 0.6375 0.2489  0.1909  0.0785  206 ILE B CG1 
6825  C CG2 . ILE B 206 ? 0.7779 0.5380 0.5779 0.2408  0.1968  0.0965  206 ILE B CG2 
6826  C CD1 . ILE B 206 ? 0.8602 0.6212 0.6753 0.2373  0.1801  0.0729  206 ILE B CD1 
6827  N N   . LYS B 207 ? 0.8900 0.6575 0.7025 0.2435  0.2408  0.1185  207 LYS B N   
6828  C CA  . LYS B 207 ? 0.8775 0.6490 0.6973 0.2391  0.2541  0.1309  207 LYS B CA  
6829  C C   . LYS B 207 ? 0.9378 0.7241 0.7906 0.2289  0.2583  0.1339  207 LYS B C   
6830  O O   . LYS B 207 ? 1.0740 0.8663 0.9424 0.2201  0.2623  0.1413  207 LYS B O   
6831  C CB  . LYS B 207 ? 0.7727 0.5385 0.5710 0.2488  0.2691  0.1363  207 LYS B CB  
6832  C CG  . LYS B 207 ? 0.9768 0.7281 0.7415 0.2582  0.2677  0.1376  207 LYS B CG  
6833  C CD  . LYS B 207 ? 0.8842 0.6302 0.6353 0.2609  0.2846  0.1501  207 LYS B CD  
6834  C CE  . LYS B 207 ? 1.1017 0.8431 0.8291 0.2729  0.2957  0.1500  207 LYS B CE  
6835  N NZ  . LYS B 207 ? 1.2018 0.9297 0.8940 0.2856  0.2879  0.1445  207 LYS B NZ  
6836  N N   . MET B 208 ? 0.7092 0.5009 0.5723 0.2305  0.2571  0.1280  208 MET B N   
6837  C CA  . MET B 208 ? 0.7947 0.6009 0.6879 0.2225  0.2598  0.1304  208 MET B CA  
6838  C C   . MET B 208 ? 0.8756 0.6867 0.7872 0.2116  0.2480  0.1293  208 MET B C   
6839  O O   . MET B 208 ? 0.9642 0.7870 0.8981 0.2028  0.2512  0.1347  208 MET B O   
6840  C CB  . MET B 208 ? 0.8050 0.6130 0.7024 0.2281  0.2592  0.1237  208 MET B CB  
6841  C CG  . MET B 208 ? 0.9349 0.7465 0.8281 0.2359  0.2740  0.1267  208 MET B CG  
6842  S SD  . MET B 208 ? 0.7320 0.5465 0.6350 0.2420  0.2726  0.1191  208 MET B SD  
6843  C CE  . MET B 208 ? 1.1378 0.9360 1.0063 0.2566  0.2741  0.1112  208 MET B CE  
6844  N N   . SER B 209 ? 0.8240 0.6276 0.7270 0.2120  0.2345  0.1216  209 SER B N   
6845  C CA  . SER B 209 ? 0.8391 0.6477 0.7582 0.2022  0.2234  0.1200  209 SER B CA  
6846  C C   . SER B 209 ? 0.8642 0.6740 0.7852 0.1966  0.2254  0.1270  209 SER B C   
6847  O O   . SER B 209 ? 0.7981 0.6167 0.7392 0.1870  0.2224  0.1292  209 SER B O   
6848  C CB  . SER B 209 ? 0.7816 0.5823 0.6900 0.2042  0.2097  0.1099  209 SER B CB  
6849  O OG  . SER B 209 ? 0.9197 0.7112 0.8053 0.2099  0.2067  0.1086  209 SER B OG  
6850  N N   . MET B 210 ? 0.8248 0.6248 0.7241 0.2030  0.2306  0.1305  210 MET B N   
6851  C CA  . MET B 210 ? 0.8247 0.6223 0.7233 0.1986  0.2331  0.1376  210 MET B CA  
6852  C C   . MET B 210 ? 0.8464 0.6540 0.7655 0.1907  0.2449  0.1460  210 MET B C   
6853  O O   . MET B 210 ? 0.7610 0.5728 0.6944 0.1818  0.2430  0.1491  210 MET B O   
6854  C CB  . MET B 210 ? 0.9388 0.7222 0.8076 0.2084  0.2374  0.1407  210 MET B CB  
6855  C CG  . MET B 210 ? 0.8592 0.6343 0.7076 0.2164  0.2247  0.1318  210 MET B CG  
6856  S SD  . MET B 210 ? 0.9147 0.6743 0.7247 0.2312  0.2307  0.1342  210 MET B SD  
6857  C CE  . MET B 210 ? 0.8970 0.6505 0.7048 0.2278  0.2420  0.1481  210 MET B CE  
6858  N N   . ARG B 211 ? 0.8129 0.6250 0.7340 0.1938  0.2564  0.1488  211 ARG B N   
6859  C CA  . ARG B 211 ? 0.8150 0.6393 0.7573 0.1864  0.2678  0.1557  211 ARG B CA  
6860  C C   . ARG B 211 ? 0.8865 0.7255 0.8575 0.1768  0.2603  0.1530  211 ARG B C   
6861  O O   . ARG B 211 ? 0.9341 0.7818 0.9234 0.1674  0.2634  0.1574  211 ARG B O   
6862  C CB  . ARG B 211 ? 0.7725 0.6009 0.7120 0.1932  0.2802  0.1573  211 ARG B CB  
6863  C CG  . ARG B 211 ? 0.7082 0.5498 0.6673 0.1866  0.2940  0.1647  211 ARG B CG  
6864  C CD  . ARG B 211 ? 0.9127 0.7606 0.8702 0.1944  0.3052  0.1648  211 ARG B CD  
6865  N NE  . ARG B 211 ? 1.0379 0.8937 1.0035 0.1906  0.3219  0.1731  211 ARG B NE  
6866  C CZ  . ARG B 211 ? 1.0696 0.9315 1.0330 0.1968  0.3350  0.1749  211 ARG B CZ  
6867  N NH1 . ARG B 211 ? 1.1760 1.0361 1.1287 0.2080  0.3330  0.1687  211 ARG B NH1 
6868  N NH2 . ARG B 211 ? 0.9907 0.8607 0.9632 0.1918  0.3506  0.1825  211 ARG B NH2 
6869  N N   . CYS B 212 ? 0.8007 0.6418 0.7749 0.1792  0.2505  0.1457  212 CYS B N   
6870  C CA  . CYS B 212 ? 0.7865 0.6400 0.7846 0.1713  0.2431  0.1434  212 CYS B CA  
6871  C C   . CYS B 212 ? 0.8497 0.7025 0.8529 0.1632  0.2340  0.1429  212 CYS B C   
6872  O O   . CYS B 212 ? 0.8375 0.7017 0.8610 0.1542  0.2338  0.1453  212 CYS B O   
6873  C CB  . CYS B 212 ? 0.6723 0.5242 0.6688 0.1764  0.2355  0.1363  212 CYS B CB  
6874  S SG  . CYS B 212 ? 0.8536 0.7175 0.8750 0.1678  0.2253  0.1338  212 CYS B SG  
6875  N N   . SER B 213 ? 0.9058 0.7463 0.8906 0.1667  0.2264  0.1393  213 SER B N   
6876  C CA  . SER B 213 ? 0.7699 0.6095 0.7579 0.1605  0.2177  0.1381  213 SER B CA  
6877  C C   . SER B 213 ? 0.7163 0.5576 0.7117 0.1542  0.2248  0.1451  213 SER B C   
6878  O O   . SER B 213 ? 0.7616 0.6087 0.7705 0.1463  0.2195  0.1446  213 SER B O   
6879  C CB  . SER B 213 ? 0.7542 0.5809 0.7196 0.1674  0.2099  0.1333  213 SER B CB  
6880  O OG  . SER B 213 ? 0.8006 0.6162 0.7469 0.1733  0.2170  0.1383  213 SER B OG  
6881  N N   . LEU B 214 ? 0.7460 0.5821 0.7327 0.1574  0.2372  0.1514  214 LEU B N   
6882  C CA  . LEU B 214 ? 0.7472 0.5830 0.7410 0.1505  0.2452  0.1582  214 LEU B CA  
6883  C C   . LEU B 214 ? 0.6996 0.5530 0.7225 0.1399  0.2471  0.1591  214 LEU B C   
6884  O O   . LEU B 214 ? 0.7831 0.6382 0.8166 0.1317  0.2477  0.1613  214 LEU B O   
6885  C CB  . LEU B 214 ? 0.6698 0.4964 0.6485 0.1555  0.2595  0.1654  214 LEU B CB  
6886  C CG  . LEU B 214 ? 0.7453 0.5530 0.6929 0.1658  0.2585  0.1662  214 LEU B CG  
6887  C CD1 . LEU B 214 ? 0.8419 0.6418 0.7751 0.1704  0.2740  0.1740  214 LEU B CD1 
6888  C CD2 . LEU B 214 ? 0.7513 0.5492 0.6929 0.1638  0.2511  0.1664  214 LEU B CD2 
6889  N N   . THR B 215 ? 0.6664 0.5327 0.7020 0.1405  0.2475  0.1570  215 THR B N   
6890  C CA  . THR B 215 ? 0.6718 0.5566 0.7348 0.1317  0.2480  0.1574  215 THR B CA  
6891  C C   . THR B 215 ? 0.7017 0.5913 0.7750 0.1254  0.2350  0.1528  215 THR B C   
6892  O O   . THR B 215 ? 0.7378 0.6423 0.8324 0.1178  0.2337  0.1526  215 THR B O   
6893  C CB  . THR B 215 ? 0.7889 0.6857 0.8616 0.1357  0.2508  0.1563  215 THR B CB  
6894  O OG1 . THR B 215 ? 0.7398 0.6331 0.8061 0.1410  0.2405  0.1507  215 THR B OG1 
6895  C CG2 . THR B 215 ? 0.9005 0.7949 0.9643 0.1424  0.2641  0.1602  215 THR B CG2 
6896  N N   . ASP B 216 ? 0.8164 0.6950 0.8751 0.1287  0.2255  0.1487  216 ASP B N   
6897  C CA  . ASP B 216 ? 0.7078 0.5909 0.7747 0.1232  0.2139  0.1442  216 ASP B CA  
6898  C C   . ASP B 216 ? 0.7925 0.6702 0.8585 0.1181  0.2131  0.1454  216 ASP B C   
6899  O O   . ASP B 216 ? 0.7285 0.6160 0.8111 0.1097  0.2106  0.1448  216 ASP B O   
6900  C CB  . ASP B 216 ? 0.6959 0.5716 0.7492 0.1292  0.2042  0.1384  216 ASP B CB  
6901  C CG  . ASP B 216 ? 0.7784 0.6590 0.8393 0.1237  0.1928  0.1336  216 ASP B CG  
6902  O OD1 . ASP B 216 ? 0.9713 0.8623 1.0486 0.1157  0.1918  0.1345  216 ASP B OD1 
6903  O OD2 . ASP B 216 ? 0.8593 0.7342 0.9102 0.1272  0.1849  0.1285  216 ASP B OD2 
6904  N N   . GLY B 217 ? 0.8614 0.7234 0.9077 0.1236  0.2151  0.1471  217 GLY B N   
6905  C CA  . GLY B 217 ? 0.7037 0.5574 0.7463 0.1206  0.2143  0.1484  217 GLY B CA  
6906  C C   . GLY B 217 ? 0.6400 0.4946 0.6934 0.1133  0.2245  0.1539  217 GLY B C   
6907  O O   . GLY B 217 ? 0.7031 0.5620 0.7693 0.1054  0.2217  0.1526  217 GLY B O   
6908  N N   . TRP B 218 ? 0.7536 0.6039 0.8016 0.1156  0.2366  0.1598  218 TRP B N   
6909  C CA  . TRP B 218 ? 0.7806 0.6301 0.8382 0.1078  0.2477  0.1654  218 TRP B CA  
6910  C C   . TRP B 218 ? 0.8124 0.6832 0.8976 0.0986  0.2507  0.1645  218 TRP B C   
6911  O O   . TRP B 218 ? 0.8116 0.6848 0.9085 0.0906  0.2595  0.1680  218 TRP B O   
6912  C CB  . TRP B 218 ? 0.5366 0.3702 0.5746 0.1137  0.2599  0.1726  218 TRP B CB  
6913  C CG  . TRP B 218 ? 0.7493 0.5619 0.7613 0.1219  0.2562  0.1738  218 TRP B CG  
6914  C CD1 . TRP B 218 ? 0.5628 0.3668 0.5523 0.1337  0.2514  0.1721  218 TRP B CD1 
6915  C CD2 . TRP B 218 ? 0.8098 0.6074 0.8155 0.1196  0.2565  0.1765  218 TRP B CD2 
6916  N NE1 . TRP B 218 ? 0.7049 0.4911 0.6747 0.1392  0.2483  0.1737  218 TRP B NE1 
6917  C CE2 . TRP B 218 ? 0.8187 0.5999 0.7976 0.1312  0.2515  0.1767  218 TRP B CE2 
6918  C CE3 . TRP B 218 ? 0.7236 0.5197 0.7435 0.1091  0.2603  0.1782  218 TRP B CE3 
6919  C CZ2 . TRP B 218 ? 0.7812 0.5445 0.7470 0.1335  0.2502  0.1793  218 TRP B CZ2 
6920  C CZ3 . TRP B 218 ? 0.9508 0.7276 0.9576 0.1108  0.2594  0.1805  218 TRP B CZ3 
6921  C CH2 . TRP B 218 ? 0.9559 0.7164 0.9358 0.1233  0.2545  0.1814  218 TRP B CH2 
6922  N N   . MET B 219 ? 0.7565 0.6419 0.8516 0.0998  0.2433  0.1600  219 MET B N   
6923  C CA  . MET B 219 ? 0.6340 0.5411 0.7545 0.0930  0.2453  0.1592  219 MET B CA  
6924  C C   . MET B 219 ? 0.6337 0.5541 0.7679 0.0892  0.2329  0.1535  219 MET B C   
6925  O O   . MET B 219 ? 0.8636 0.7891 1.0097 0.0808  0.2297  0.1516  219 MET B O   
6926  C CB  . MET B 219 ? 0.7920 0.7043 0.9100 0.1005  0.2513  0.1610  219 MET B CB  
6927  C CG  . MET B 219 ? 0.8215 0.7291 0.9350 0.1013  0.2664  0.1671  219 MET B CG  
6928  S SD  . MET B 219 ? 0.9072 0.8186 1.0133 0.1123  0.2737  0.1685  219 MET B SD  
6929  C CE  . MET B 219 ? 0.7750 0.7142 0.9136 0.1052  0.2803  0.1691  219 MET B CE  
6930  N N   . GLY B 220 ? 0.5263 0.4512 0.6581 0.0951  0.2266  0.1509  220 GLY B N   
6931  C CA  . GLY B 220 ? 0.7503 0.6878 0.8946 0.0916  0.2160  0.1466  220 GLY B CA  
6932  C C   . GLY B 220 ? 0.6973 0.6295 0.8385 0.0874  0.2075  0.1430  220 GLY B C   
6933  O O   . GLY B 220 ? 0.7331 0.6771 0.8896 0.0797  0.2037  0.1409  220 GLY B O   
6934  N N   . SER B 221 ? 0.5340 0.4500 0.6561 0.0926  0.2045  0.1419  221 SER B N   
6935  C CA  . SER B 221 ? 0.6330 0.5443 0.7516 0.0899  0.1964  0.1381  221 SER B CA  
6936  C C   . SER B 221 ? 0.6566 0.5651 0.7810 0.0833  0.2010  0.1396  221 SER B C   
6937  O O   . SER B 221 ? 0.8456 0.7593 0.9784 0.0774  0.1952  0.1359  221 SER B O   
6938  C CB  . SER B 221 ? 0.7517 0.6481 0.8495 0.0978  0.1922  0.1363  221 SER B CB  
6939  O OG  . SER B 221 ? 0.8532 0.7525 0.9477 0.1021  0.1866  0.1335  221 SER B OG  
6940  N N   . PHE B 222 ? 0.5810 0.4809 0.7006 0.0840  0.2116  0.1448  222 PHE B N   
6941  C CA  . PHE B 222 ? 0.6292 0.5233 0.7534 0.0773  0.2172  0.1466  222 PHE B CA  
6942  C C   . PHE B 222 ? 0.7016 0.6147 0.8507 0.0670  0.2179  0.1448  222 PHE B C   
6943  O O   . PHE B 222 ? 0.7997 0.7141 0.9570 0.0600  0.2149  0.1416  222 PHE B O   
6944  C CB  . PHE B 222 ? 0.5424 0.4229 0.6555 0.0802  0.2299  0.1535  222 PHE B CB  
6945  C CG  . PHE B 222 ? 0.6616 0.5233 0.7648 0.0787  0.2340  0.1562  222 PHE B CG  
6946  C CD1 . PHE B 222 ? 0.6908 0.5540 0.8088 0.0682  0.2388  0.1564  222 PHE B CD1 
6947  C CD2 . PHE B 222 ? 0.7698 0.6118 0.8487 0.0881  0.2332  0.1584  222 PHE B CD2 
6948  C CE1 . PHE B 222 ? 0.7120 0.5552 0.8201 0.0670  0.2431  0.1592  222 PHE B CE1 
6949  C CE2 . PHE B 222 ? 0.7695 0.5925 0.8379 0.0878  0.2371  0.1616  222 PHE B CE2 
6950  C CZ  . PHE B 222 ? 0.7601 0.5826 0.8430 0.0772  0.2423  0.1622  222 PHE B CZ  
6951  N N   . MET B 223 ? 0.7024 0.6309 0.8634 0.0667  0.2212  0.1460  223 MET B N   
6952  C CA  . MET B 223 ? 0.6604 0.6095 0.8455 0.0579  0.2210  0.1439  223 MET B CA  
6953  C C   . MET B 223 ? 0.6745 0.6340 0.8665 0.0553  0.2088  0.1381  223 MET B C   
6954  O O   . MET B 223 ? 0.6552 0.6238 0.8610 0.0470  0.2065  0.1347  223 MET B O   
6955  C CB  . MET B 223 ? 0.6729 0.6374 0.8686 0.0603  0.2262  0.1463  223 MET B CB  
6956  C CG  . MET B 223 ? 0.8225 0.7828 1.0179 0.0600  0.2399  0.1516  223 MET B CG  
6957  S SD  . MET B 223 ? 0.9136 0.8977 1.1279 0.0612  0.2460  0.1531  223 MET B SD  
6958  C CE  . MET B 223 ? 0.9300 0.9045 1.1241 0.0753  0.2446  0.1548  223 MET B CE  
6959  N N   . GLY B 224 ? 0.6378 0.5956 0.8197 0.0621  0.2013  0.1368  224 GLY B N   
6960  C CA  . GLY B 224 ? 0.5724 0.5392 0.7587 0.0602  0.1905  0.1321  224 GLY B CA  
6961  C C   . GLY B 224 ? 0.6414 0.6023 0.8261 0.0554  0.1864  0.1281  224 GLY B C   
6962  O O   . GLY B 224 ? 0.6823 0.6554 0.8788 0.0492  0.1812  0.1241  224 GLY B O   
6963  N N   . THR B 225 ? 0.5870 0.5290 0.7566 0.0587  0.1888  0.1291  225 THR B N   
6964  C CA  . THR B 225 ? 0.6321 0.5661 0.7988 0.0557  0.1855  0.1255  225 THR B CA  
6965  C C   . THR B 225 ? 0.6532 0.5903 0.8338 0.0464  0.1907  0.1249  225 THR B C   
6966  O O   . THR B 225 ? 0.6963 0.6415 0.8865 0.0404  0.1855  0.1196  225 THR B O   
6967  C CB  . THR B 225 ? 0.4906 0.4033 0.6368 0.0632  0.1870  0.1274  225 THR B CB  
6968  O OG1 . THR B 225 ? 0.5925 0.5047 0.7281 0.0704  0.1803  0.1259  225 THR B OG1 
6969  C CG2 . THR B 225 ? 0.6508 0.5527 0.7934 0.0612  0.1850  0.1244  225 THR B CG2 
6970  N N   . GLU B 226 ? 0.5302 0.4617 0.7124 0.0448  0.2012  0.1298  226 GLU B N   
6971  C CA  . GLU B 226 ? 0.6244 0.5580 0.8207 0.0350  0.2075  0.1293  226 GLU B CA  
6972  C C   . GLU B 226 ? 0.6275 0.5853 0.8459 0.0269  0.2031  0.1243  226 GLU B C   
6973  O O   . GLU B 226 ? 0.6516 0.6115 0.8793 0.0191  0.2012  0.1194  226 GLU B O   
6974  C CB  . GLU B 226 ? 0.7796 0.7077 0.9759 0.0346  0.2204  0.1361  226 GLU B CB  
6975  C CG  . GLU B 226 ? 0.9310 0.8327 1.1078 0.0388  0.2275  0.1412  226 GLU B CG  
6976  C CD  . GLU B 226 ? 1.2133 1.1105 1.3917 0.0365  0.2416  0.1480  226 GLU B CD  
6977  O OE1 . GLU B 226 ? 0.8536 0.7687 1.0453 0.0348  0.2454  0.1490  226 GLU B OE1 
6978  O OE2 . GLU B 226 ? 1.4767 1.3522 1.6427 0.0367  0.2491  0.1525  226 GLU B OE2 
6979  N N   . PHE B 227 ? 0.6040 0.5795 0.8303 0.0293  0.2012  0.1253  227 PHE B N   
6980  C CA  . PHE B 227 ? 0.5540 0.5536 0.8000 0.0233  0.1963  0.1211  227 PHE B CA  
6981  C C   . PHE B 227 ? 0.6603 0.6651 0.9047 0.0228  0.1849  0.1152  227 PHE B C   
6982  O O   . PHE B 227 ? 0.7228 0.7427 0.9812 0.0160  0.1807  0.1101  227 PHE B O   
6983  C CB  . PHE B 227 ? 0.5433 0.5589 0.7965 0.0277  0.1975  0.1244  227 PHE B CB  
6984  C CG  . PHE B 227 ? 0.5409 0.5570 0.7994 0.0277  0.2092  0.1294  227 PHE B CG  
6985  C CD1 . PHE B 227 ? 0.5616 0.5671 0.8220 0.0213  0.2186  0.1308  227 PHE B CD1 
6986  C CD2 . PHE B 227 ? 0.6777 0.7039 0.9388 0.0342  0.2115  0.1329  227 PHE B CD2 
6987  C CE1 . PHE B 227 ? 0.6409 0.6476 0.9061 0.0209  0.2304  0.1357  227 PHE B CE1 
6988  C CE2 . PHE B 227 ? 0.5995 0.6274 0.8656 0.0345  0.2229  0.1372  227 PHE B CE2 
6989  C CZ  . PHE B 227 ? 0.6481 0.6669 0.9164 0.0276  0.2325  0.1387  227 PHE B CZ  
6990  N N   . SER B 228 ? 0.5347 0.5281 0.7625 0.0298  0.1800  0.1155  228 SER B N   
6991  C CA  . SER B 228 ? 0.4761 0.4746 0.7020 0.0293  0.1702  0.1102  228 SER B CA  
6992  C C   . SER B 228 ? 0.5780 0.5699 0.8057 0.0232  0.1696  0.1048  228 SER B C   
6993  O O   . SER B 228 ? 0.6076 0.6118 0.8439 0.0182  0.1638  0.0990  228 SER B O   
6994  C CB  . SER B 228 ? 0.4825 0.4707 0.6916 0.0374  0.1661  0.1114  228 SER B CB  
6995  O OG  . SER B 228 ? 0.6972 0.6914 0.9052 0.0425  0.1659  0.1154  228 SER B OG  
6996  N N   . ASP B 229 ? 0.5384 0.5101 0.7573 0.0240  0.1756  0.1066  229 ASP B N   
6997  C CA  . ASP B 229 ? 0.5694 0.5311 0.7890 0.0189  0.1758  0.1018  229 ASP B CA  
6998  C C   . ASP B 229 ? 0.5871 0.5610 0.8260 0.0081  0.1782  0.0980  229 ASP B C   
6999  O O   . ASP B 229 ? 0.7123 0.6861 0.9559 0.0027  0.1749  0.0913  229 ASP B O   
7000  C CB  . ASP B 229 ? 0.6119 0.5478 0.8175 0.0226  0.1831  0.1062  229 ASP B CB  
7001  C CG  . ASP B 229 ? 0.6801 0.6031 0.8662 0.0332  0.1794  0.1079  229 ASP B CG  
7002  O OD1 . ASP B 229 ? 0.7389 0.6723 0.9232 0.0366  0.1713  0.1050  229 ASP B OD1 
7003  O OD2 . ASP B 229 ? 0.7160 0.6187 0.8886 0.0380  0.1846  0.1122  229 ASP B OD2 
7004  N N   . ILE B 230 ? 0.5887 0.5739 0.8393 0.0051  0.1838  0.1016  230 ILE B N   
7005  C CA  . ILE B 230 ? 0.5538 0.5535 0.8249 -0.0055 0.1859  0.0975  230 ILE B CA  
7006  C C   . ILE B 230 ? 0.5818 0.6045 0.8633 -0.0082 0.1756  0.0906  230 ILE B C   
7007  O O   . ILE B 230 ? 0.6031 0.6310 0.8940 -0.0159 0.1727  0.0831  230 ILE B O   
7008  C CB  . ILE B 230 ? 0.5306 0.5387 0.8122 -0.0071 0.1948  0.1032  230 ILE B CB  
7009  C CG1 . ILE B 230 ? 0.6823 0.6666 0.9546 -0.0071 0.2066  0.1093  230 ILE B CG1 
7010  C CG2 . ILE B 230 ? 0.4630 0.4941 0.7689 -0.0174 0.1945  0.0978  230 ILE B CG2 
7011  C CD1 . ILE B 230 ? 0.6462 0.6349 0.9229 -0.0058 0.2167  0.1164  230 ILE B CD1 
7012  N N   . MET B 231 ? 0.5301 0.5658 0.8091 -0.0016 0.1702  0.0931  231 MET B N   
7013  C CA  . MET B 231 ? 0.5975 0.6551 0.8844 -0.0028 0.1608  0.0883  231 MET B CA  
7014  C C   . MET B 231 ? 0.5781 0.6318 0.8547 -0.0013 0.1529  0.0831  231 MET B C   
7015  O O   . MET B 231 ? 0.6322 0.6998 0.9162 -0.0059 0.1468  0.0763  231 MET B O   
7016  C CB  . MET B 231 ? 0.3936 0.4643 0.6806 0.0041  0.1587  0.0938  231 MET B CB  
7017  C CG  . MET B 231 ? 0.5551 0.6328 0.8530 0.0039  0.1662  0.0985  231 MET B CG  
7018  S SD  . MET B 231 ? 0.6871 0.7798 0.9855 0.0131  0.1631  0.1043  231 MET B SD  
7019  C CE  . MET B 231 ? 0.5981 0.6662 0.8743 0.0223  0.1664  0.1105  231 MET B CE  
7020  N N   . PHE B 232 ? 0.4794 0.5162 0.7392 0.0054  0.1529  0.0859  232 PHE B N   
7021  C CA  . PHE B 232 ? 0.5929 0.6278 0.8434 0.0076  0.1459  0.0812  232 PHE B CA  
7022  C C   . PHE B 232 ? 0.6196 0.6362 0.8633 0.0065  0.1473  0.0767  232 PHE B C   
7023  O O   . PHE B 232 ? 0.6307 0.6476 0.8687 0.0079  0.1417  0.0715  232 PHE B O   
7024  C CB  . PHE B 232 ? 0.5412 0.5735 0.7793 0.0159  0.1433  0.0861  232 PHE B CB  
7025  C CG  . PHE B 232 ? 0.4993 0.5444 0.7420 0.0185  0.1432  0.0917  232 PHE B CG  
7026  C CD1 . PHE B 232 ? 0.4416 0.5075 0.6956 0.0154  0.1389  0.0900  232 PHE B CD1 
7027  C CD2 . PHE B 232 ? 0.5649 0.6007 0.8001 0.0248  0.1472  0.0983  232 PHE B CD2 
7028  C CE1 . PHE B 232 ? 0.4957 0.5724 0.7536 0.0190  0.1388  0.0953  232 PHE B CE1 
7029  C CE2 . PHE B 232 ? 0.5635 0.6096 0.8027 0.0279  0.1472  0.1031  232 PHE B CE2 
7030  C CZ  . PHE B 232 ? 0.5657 0.6319 0.8164 0.0253  0.1431  0.1018  232 PHE B CZ  
7031  N N   . GLY B 233 ? 0.5871 0.5880 0.8312 0.0043  0.1549  0.0789  233 GLY B N   
7032  C CA  . GLY B 233 ? 0.4716 0.4520 0.7084 0.0040  0.1571  0.0757  233 GLY B CA  
7033  C C   . GLY B 233 ? 0.6378 0.5970 0.8577 0.0126  0.1607  0.0818  233 GLY B C   
7034  O O   . GLY B 233 ? 0.5890 0.5509 0.8004 0.0197  0.1580  0.0854  233 GLY B O   
7035  N N   . THR B 234 ? 0.6103 0.5476 0.8245 0.0122  0.1668  0.0830  234 THR B N   
7036  C CA  . THR B 234 ? 0.5702 0.4866 0.7667 0.0214  0.1700  0.0888  234 THR B CA  
7037  C C   . THR B 234 ? 0.6270 0.5382 0.8129 0.0281  0.1626  0.0837  234 THR B C   
7038  O O   . THR B 234 ? 0.6870 0.5961 0.8763 0.0248  0.1600  0.0767  234 THR B O   
7039  C CB  . THR B 234 ? 0.6534 0.5474 0.8466 0.0189  0.1795  0.0926  234 THR B CB  
7040  O OG1 . THR B 234 ? 0.7904 0.6926 0.9970 0.0109  0.1866  0.0959  234 THR B OG1 
7041  C CG2 . THR B 234 ? 0.6735 0.5462 0.8469 0.0292  0.1831  0.0998  234 THR B CG2 
7042  N N   . PRO B 235 ? 0.5891 0.4988 0.7628 0.0374  0.1591  0.0862  235 PRO B N   
7043  C CA  . PRO B 235 ? 0.5411 0.4487 0.7068 0.0434  0.1522  0.0807  235 PRO B CA  
7044  C C   . PRO B 235 ? 0.6628 0.5481 0.8198 0.0471  0.1541  0.0789  235 PRO B C   
7045  O O   . PRO B 235 ? 0.7815 0.6474 0.9311 0.0488  0.1611  0.0848  235 PRO B O   
7046  C CB  . PRO B 235 ? 0.5341 0.4428 0.6889 0.0522  0.1494  0.0845  235 PRO B CB  
7047  C CG  . PRO B 235 ? 0.5987 0.5144 0.7575 0.0498  0.1532  0.0906  235 PRO B CG  
7048  C CD  . PRO B 235 ? 0.6237 0.5345 0.7908 0.0427  0.1609  0.0932  235 PRO B CD  
7049  N N   . HIS B 236 ? 0.7446 0.6325 0.9015 0.0488  0.1483  0.0710  236 HIS B N   
7050  C CA  . HIS B 236 ? 0.6886 0.5563 0.8369 0.0540  0.1485  0.0680  236 HIS B CA  
7051  C C   . HIS B 236 ? 0.6947 0.5701 0.8370 0.0628  0.1405  0.0627  236 HIS B C   
7052  O O   . HIS B 236 ? 0.6885 0.5854 0.8365 0.0613  0.1356  0.0602  236 HIS B O   
7053  C CB  . HIS B 236 ? 0.6776 0.5411 0.8356 0.0455  0.1504  0.0617  236 HIS B CB  
7054  C CG  . HIS B 236 ? 0.7677 0.6531 0.9367 0.0405  0.1440  0.0523  236 HIS B CG  
7055  N ND1 . HIS B 236 ? 1.0230 0.9300 1.2049 0.0318  0.1430  0.0517  236 HIS B ND1 
7056  C CD2 . HIS B 236 ? 0.8508 0.7394 1.0188 0.0437  0.1385  0.0435  236 HIS B CD2 
7057  C CE1 . HIS B 236 ? 0.8772 0.7992 1.0642 0.0299  0.1370  0.0430  236 HIS B CE1 
7058  N NE2 . HIS B 236 ? 0.9033 0.8153 1.0826 0.0366  0.1344  0.0376  236 HIS B NE2 
7059  N N   . SER B 237 ? 0.6124 0.4710 0.7435 0.0720  0.1393  0.0610  237 SER B N   
7060  C CA  . SER B 237 ? 0.6302 0.4974 0.7566 0.0810  0.1318  0.0555  237 SER B CA  
7061  C C   . SER B 237 ? 0.6265 0.5172 0.7649 0.0755  0.1267  0.0468  237 SER B C   
7062  O O   . SER B 237 ? 0.6340 0.5248 0.7797 0.0692  0.1276  0.0413  237 SER B O   
7063  C CB  . SER B 237 ? 0.5512 0.3971 0.6661 0.0913  0.1314  0.0538  237 SER B CB  
7064  O OG  . SER B 237 ? 1.0015 0.8358 1.1206 0.0868  0.1340  0.0491  237 SER B OG  
7065  N N   . ILE B 238 ? 0.5983 0.5088 0.7386 0.0772  0.1218  0.0456  238 ILE B N   
7066  C CA  . ILE B 238 ? 0.5510 0.4846 0.7010 0.0720  0.1177  0.0388  238 ILE B CA  
7067  C C   . ILE B 238 ? 0.5835 0.5309 0.7313 0.0786  0.1123  0.0355  238 ILE B C   
7068  O O   . ILE B 238 ? 0.6714 0.6153 0.8124 0.0847  0.1112  0.0396  238 ILE B O   
7069  C CB  . ILE B 238 ? 0.4820 0.4296 0.6411 0.0619  0.1194  0.0426  238 ILE B CB  
7070  C CG1 . ILE B 238 ? 0.5392 0.5091 0.7070 0.0562  0.1157  0.0360  238 ILE B CG1 
7071  C CG2 . ILE B 238 ? 0.5785 0.5295 0.7342 0.0637  0.1197  0.0501  238 ILE B CG2 
7072  C CD1 . ILE B 238 ? 0.5043 0.4845 0.6813 0.0464  0.1173  0.0375  238 ILE B CD1 
7073  N N   . ASP B 239 ? 0.5127 0.4769 0.6666 0.0769  0.1089  0.0276  239 ASP B N   
7074  C CA  . ASP B 239 ? 0.5882 0.5684 0.7424 0.0816  0.1044  0.0236  239 ASP B CA  
7075  C C   . ASP B 239 ? 0.5646 0.5649 0.7251 0.0741  0.1037  0.0260  239 ASP B C   
7076  O O   . ASP B 239 ? 0.6772 0.6838 0.8431 0.0658  0.1055  0.0275  239 ASP B O   
7077  C CB  . ASP B 239 ? 0.6768 0.6641 0.8337 0.0847  0.1020  0.0135  239 ASP B CB  
7078  C CG  . ASP B 239 ? 0.7761 0.7436 0.9258 0.0944  0.1018  0.0104  239 ASP B CG  
7079  O OD1 . ASP B 239 ? 0.6889 0.6489 0.8315 0.1038  0.0999  0.0128  239 ASP B OD1 
7080  O OD2 . ASP B 239 ? 0.8530 0.8124 1.0038 0.0931  0.1031  0.0054  239 ASP B OD2 
7081  N N   . THR B 240 ? 0.4869 0.4974 0.6468 0.0773  0.1010  0.0261  240 THR B N   
7082  C CA  . THR B 240 ? 0.4846 0.5122 0.6494 0.0707  0.1006  0.0286  240 THR B CA  
7083  C C   . THR B 240 ? 0.4440 0.4843 0.6098 0.0748  0.0971  0.0244  240 THR B C   
7084  O O   . THR B 240 ? 0.5728 0.6090 0.7355 0.0833  0.0946  0.0199  240 THR B O   
7085  C CB  . THR B 240 ? 0.5924 0.6117 0.7549 0.0675  0.1030  0.0378  240 THR B CB  
7086  O OG1 . THR B 240 ? 0.6350 0.6684 0.8027 0.0599  0.1035  0.0406  240 THR B OG1 
7087  C CG2 . THR B 240 ? 0.6287 0.6397 0.7844 0.0741  0.1017  0.0406  240 THR B CG2 
7088  N N   . GLU B 241 ? 0.4312 0.4867 0.6016 0.0688  0.0969  0.0258  241 GLU B N   
7089  C CA  . GLU B 241 ? 0.4539 0.5229 0.6272 0.0704  0.0943  0.0220  241 GLU B CA  
7090  C C   . GLU B 241 ? 0.4934 0.5604 0.6656 0.0667  0.0946  0.0284  241 GLU B C   
7091  O O   . GLU B 241 ? 0.6245 0.6875 0.7962 0.0609  0.0973  0.0348  241 GLU B O   
7092  C CB  . GLU B 241 ? 0.3970 0.4871 0.5775 0.0655  0.0947  0.0167  241 GLU B CB  
7093  C CG  . GLU B 241 ? 0.5486 0.6444 0.7307 0.0721  0.0931  0.0076  241 GLU B CG  
7094  C CD  . GLU B 241 ? 0.7239 0.8391 0.9117 0.0676  0.0946  0.0022  241 GLU B CD  
7095  O OE1 . GLU B 241 ? 0.6621 0.7831 0.8508 0.0592  0.0972  0.0062  241 GLU B OE1 
7096  O OE2 . GLU B 241 ? 0.9276 1.0524 1.1184 0.0731  0.0932  -0.0061 241 GLU B OE2 
7097  N N   . ALA B 242 ? 0.4147 0.4842 0.5864 0.0706  0.0916  0.0261  242 ALA B N   
7098  C CA  . ALA B 242 ? 0.3952 0.4613 0.5652 0.0678  0.0915  0.0307  242 ALA B CA  
7099  C C   . ALA B 242 ? 0.4190 0.5020 0.5961 0.0637  0.0897  0.0265  242 ALA B C   
7100  O O   . ALA B 242 ? 0.4456 0.5431 0.6285 0.0653  0.0880  0.0193  242 ALA B O   
7101  C CB  . ALA B 242 ? 0.4273 0.4768 0.5883 0.0763  0.0895  0.0323  242 ALA B CB  
7102  N N   . ASN B 243 ? 0.4245 0.5054 0.6016 0.0582  0.0906  0.0308  243 ASN B N   
7103  C CA  . ASN B 243 ? 0.4946 0.5882 0.6782 0.0525  0.0897  0.0278  243 ASN B CA  
7104  C C   . ASN B 243 ? 0.5497 0.6556 0.7396 0.0425  0.0939  0.0300  243 ASN B C   
7105  O O   . ASN B 243 ? 0.6172 0.7269 0.8073 0.0413  0.0962  0.0310  243 ASN B O   
7106  C CB  . ASN B 243 ? 0.4605 0.5663 0.6489 0.0579  0.0851  0.0183  243 ASN B CB  
7107  C CG  . ASN B 243 ? 0.5688 0.6790 0.7605 0.0553  0.0823  0.0152  243 ASN B CG  
7108  O OD1 . ASN B 243 ? 0.4239 0.5282 0.6149 0.0484  0.0844  0.0199  243 ASN B OD1 
7109  N ND2 . ASN B 243 ? 0.6448 0.7655 0.8404 0.0613  0.0772  0.0068  243 ASN B ND2 
7110  N N   . LEU B 244 ? 0.5502 0.6613 0.7442 0.0352  0.0949  0.0306  244 LEU B N   
7111  C CA  . LEU B 244 ? 0.4527 0.5726 0.6506 0.0254  0.0995  0.0344  244 LEU B CA  
7112  C C   . LEU B 244 ? 0.4369 0.5757 0.6406 0.0232  0.1014  0.0300  244 LEU B C   
7113  O O   . LEU B 244 ? 0.5014 0.6461 0.7056 0.0162  0.1057  0.0343  244 LEU B O   
7114  C CB  . LEU B 244 ? 0.4402 0.5611 0.6419 0.0180  0.1002  0.0348  244 LEU B CB  
7115  C CG  . LEU B 244 ? 0.4777 0.5789 0.6726 0.0190  0.0994  0.0400  244 LEU B CG  
7116  C CD1 . LEU B 244 ? 0.3580 0.4601 0.5574 0.0131  0.0988  0.0371  244 LEU B CD1 
7117  C CD2 . LEU B 244 ? 0.4684 0.5589 0.6575 0.0163  0.1034  0.0501  244 LEU B CD2 
7118  N N   . GLY B 245 ? 0.4794 0.6268 0.6864 0.0299  0.0985  0.0218  245 GLY B N   
7119  C CA  . GLY B 245 ? 0.3938 0.5590 0.6059 0.0292  0.1004  0.0167  245 GLY B CA  
7120  C C   . GLY B 245 ? 0.3838 0.5448 0.5901 0.0298  0.1026  0.0203  245 GLY B C   
7121  O O   . GLY B 245 ? 0.3331 0.5079 0.5418 0.0280  0.1050  0.0172  245 GLY B O   
7122  N N   . VAL B 246 ? 0.4875 0.6301 0.6865 0.0323  0.1018  0.0263  246 VAL B N   
7123  C CA  . VAL B 246 ? 0.5217 0.6598 0.7162 0.0324  0.1032  0.0295  246 VAL B CA  
7124  C C   . VAL B 246 ? 0.5052 0.6505 0.6987 0.0241  0.1071  0.0354  246 VAL B C   
7125  O O   . VAL B 246 ? 0.5127 0.6612 0.7039 0.0236  0.1080  0.0357  246 VAL B O   
7126  C CB  . VAL B 246 ? 0.3834 0.5014 0.5720 0.0366  0.1019  0.0344  246 VAL B CB  
7127  C CG1 . VAL B 246 ? 0.5146 0.6240 0.7016 0.0456  0.0985  0.0294  246 VAL B CG1 
7128  C CG2 . VAL B 246 ? 0.4901 0.5981 0.6760 0.0330  0.1029  0.0425  246 VAL B CG2 
7129  N N   . LEU B 247 ? 0.4057 0.5526 0.6004 0.0179  0.1092  0.0400  247 LEU B N   
7130  C CA  . LEU B 247 ? 0.4605 0.6124 0.6527 0.0107  0.1131  0.0467  247 LEU B CA  
7131  C C   . LEU B 247 ? 0.5546 0.7261 0.7495 0.0080  0.1158  0.0418  247 LEU B C   
7132  O O   . LEU B 247 ? 0.5691 0.7519 0.7705 0.0085  0.1158  0.0345  247 LEU B O   
7133  C CB  . LEU B 247 ? 0.3282 0.4751 0.5210 0.0047  0.1152  0.0524  247 LEU B CB  
7134  C CG  . LEU B 247 ? 0.2935 0.4212 0.4829 0.0072  0.1132  0.0574  247 LEU B CG  
7135  C CD1 . LEU B 247 ? 0.3929 0.5165 0.5845 0.0020  0.1145  0.0591  247 LEU B CD1 
7136  C CD2 . LEU B 247 ? 0.4247 0.5434 0.6077 0.0076  0.1141  0.0659  247 LEU B CD2 
7137  N N   . GLU B 248 ? 0.3840 0.5607 0.5738 0.0057  0.1179  0.0452  248 GLU B N   
7138  C CA  . GLU B 248 ? 0.4374 0.6327 0.6278 0.0035  0.1209  0.0406  248 GLU B CA  
7139  C C   . GLU B 248 ? 0.4526 0.6549 0.6396 -0.0046 0.1264  0.0481  248 GLU B C   
7140  O O   . GLU B 248 ? 0.5087 0.7025 0.6887 -0.0066 0.1270  0.0571  248 GLU B O   
7141  C CB  . GLU B 248 ? 0.4206 0.6178 0.6066 0.0078  0.1189  0.0372  248 GLU B CB  
7142  C CG  . GLU B 248 ? 0.4652 0.6583 0.6547 0.0154  0.1150  0.0282  248 GLU B CG  
7143  C CD  . GLU B 248 ? 0.9819 1.1667 1.1674 0.0189  0.1122  0.0272  248 GLU B CD  
7144  O OE1 . GLU B 248 ? 0.9613 1.1482 1.1417 0.0158  0.1128  0.0319  248 GLU B OE1 
7145  O OE2 . GLU B 248 ? 1.1864 1.3626 1.3738 0.0248  0.1093  0.0218  248 GLU B OE2 
7146  N N   . LYS B 249 ? 0.4768 0.6944 0.6687 -0.0091 0.1307  0.0445  249 LYS B N   
7147  C CA  . LYS B 249 ? 0.4316 0.6551 0.6200 -0.0176 0.1371  0.0519  249 LYS B CA  
7148  C C   . LYS B 249 ? 0.5417 0.7707 0.7193 -0.0182 0.1395  0.0568  249 LYS B C   
7149  O O   . LYS B 249 ? 0.5679 0.7929 0.7383 -0.0234 0.1433  0.0669  249 LYS B O   
7150  C CB  . LYS B 249 ? 0.4103 0.6519 0.6077 -0.0226 0.1419  0.0459  249 LYS B CB  
7151  C CG  . LYS B 249 ? 0.4066 0.6554 0.6001 -0.0321 0.1501  0.0535  249 LYS B CG  
7152  C CD  . LYS B 249 ? 0.6190 0.8734 0.8233 -0.0403 0.1544  0.0522  249 LYS B CD  
7153  C CE  . LYS B 249 ? 0.4877 0.7581 0.6914 -0.0490 0.1638  0.0549  249 LYS B CE  
7154  N NZ  . LYS B 249 ? 0.7503 1.0256 0.9659 -0.0586 0.1684  0.0538  249 LYS B NZ  
7155  N N   . ASN B 250 ? 0.5227 0.7605 0.6982 -0.0128 0.1372  0.0497  250 ASN B N   
7156  C CA  . ASN B 250 ? 0.5004 0.7450 0.6649 -0.0129 0.1386  0.0530  250 ASN B CA  
7157  C C   . ASN B 250 ? 0.4996 0.7326 0.6583 -0.0080 0.1328  0.0556  250 ASN B C   
7158  O O   . ASN B 250 ? 0.5030 0.7431 0.6539 -0.0065 0.1320  0.0551  250 ASN B O   
7159  C CB  . ASN B 250 ? 0.4675 0.7316 0.6323 -0.0111 0.1408  0.0431  250 ASN B CB  
7160  C CG  . ASN B 250 ? 0.6134 0.8919 0.7851 -0.0162 0.1474  0.0404  250 ASN B CG  
7161  O OD1 . ASN B 250 ? 0.6693 0.9464 0.8407 -0.0235 0.1525  0.0487  250 ASN B OD1 
7162  N ND2 . ASN B 250 ? 0.7670 1.0599 0.9458 -0.0124 0.1475  0.0287  250 ASN B ND2 
7163  N N   . SER B 251 ? 0.5342 0.7506 0.6967 -0.0058 0.1288  0.0581  251 SER B N   
7164  C CA  . SER B 251 ? 0.5443 0.7509 0.7034 -0.0019 0.1238  0.0607  251 SER B CA  
7165  C C   . SER B 251 ? 0.5885 0.7806 0.7451 -0.0034 0.1237  0.0720  251 SER B C   
7166  O O   . SER B 251 ? 0.6248 0.8114 0.7832 -0.0072 0.1269  0.0765  251 SER B O   
7167  C CB  . SER B 251 ? 0.4713 0.6707 0.6372 0.0035  0.1193  0.0524  251 SER B CB  
7168  O OG  . SER B 251 ? 0.7179 0.9285 0.8869 0.0058  0.1194  0.0415  251 SER B OG  
7169  N N   . VAL B 252 ? 0.5262 0.7125 0.6791 -0.0005 0.1201  0.0761  252 VAL B N   
7170  C CA  . VAL B 252 ? 0.4579 0.6306 0.6086 -0.0005 0.1198  0.0864  252 VAL B CA  
7171  C C   . VAL B 252 ? 0.4718 0.6312 0.6303 0.0022  0.1176  0.0836  252 VAL B C   
7172  O O   . VAL B 252 ? 0.5729 0.7305 0.7350 0.0059  0.1142  0.0783  252 VAL B O   
7173  C CB  . VAL B 252 ? 0.3533 0.5275 0.4982 0.0023  0.1166  0.0915  252 VAL B CB  
7174  C CG1 . VAL B 252 ? 0.4726 0.6325 0.6162 0.0038  0.1161  0.1015  252 VAL B CG1 
7175  C CG2 . VAL B 252 ? 0.4929 0.6807 0.6279 0.0006  0.1185  0.0941  252 VAL B CG2 
7176  N N   . ASN B 253 ? 0.4199 0.5699 0.5805 0.0000  0.1198  0.0868  253 ASN B N   
7177  C CA  . ASN B 253 ? 0.4049 0.5423 0.5711 0.0030  0.1178  0.0843  253 ASN B CA  
7178  C C   . ASN B 253 ? 0.5886 0.7119 0.7525 0.0054  0.1167  0.0923  253 ASN B C   
7179  O O   . ASN B 253 ? 0.6946 0.8108 0.8550 0.0032  0.1189  0.0999  253 ASN B O   
7180  C CB  . ASN B 253 ? 0.4978 0.6334 0.6678 -0.0002 0.1199  0.0818  253 ASN B CB  
7181  C CG  . ASN B 253 ? 0.4682 0.6181 0.6428 -0.0010 0.1205  0.0724  253 ASN B CG  
7182  O OD1 . ASN B 253 ? 0.5790 0.7311 0.7566 0.0037  0.1176  0.0649  253 ASN B OD1 
7183  N ND2 . ASN B 253 ? 0.4136 0.5733 0.5889 -0.0068 0.1246  0.0726  253 ASN B ND2 
7184  N N   . VAL B 254 ? 0.5134 0.6326 0.6796 0.0099  0.1138  0.0905  254 VAL B N   
7185  C CA  . VAL B 254 ? 0.4661 0.5739 0.6317 0.0130  0.1130  0.0972  254 VAL B CA  
7186  C C   . VAL B 254 ? 0.4982 0.5943 0.6676 0.0162  0.1124  0.0936  254 VAL B C   
7187  O O   . VAL B 254 ? 0.6005 0.6976 0.7730 0.0186  0.1108  0.0876  254 VAL B O   
7188  C CB  . VAL B 254 ? 0.4343 0.5487 0.6000 0.0152  0.1106  0.0986  254 VAL B CB  
7189  C CG1 . VAL B 254 ? 0.4225 0.5273 0.5887 0.0187  0.1102  0.1056  254 VAL B CG1 
7190  C CG2 . VAL B 254 ? 0.3377 0.4654 0.4979 0.0128  0.1107  0.1009  254 VAL B CG2 
7191  N N   . VAL B 255 ? 0.5107 0.5950 0.6788 0.0163  0.1137  0.0970  255 VAL B N   
7192  C CA  . VAL B 255 ? 0.4574 0.5302 0.6269 0.0199  0.1130  0.0940  255 VAL B CA  
7193  C C   . VAL B 255 ? 0.5638 0.6258 0.7324 0.0241  0.1133  0.0996  255 VAL B C   
7194  O O   . VAL B 255 ? 0.5450 0.6019 0.7110 0.0239  0.1145  0.1065  255 VAL B O   
7195  C CB  . VAL B 255 ? 0.4001 0.4678 0.5691 0.0175  0.1138  0.0922  255 VAL B CB  
7196  C CG1 . VAL B 255 ? 0.5289 0.5858 0.6979 0.0222  0.1124  0.0883  255 VAL B CG1 
7197  C CG2 . VAL B 255 ? 0.3155 0.3966 0.4871 0.0130  0.1141  0.0867  255 VAL B CG2 
7198  N N   . LEU B 256 ? 0.5800 0.6382 0.7508 0.0280  0.1128  0.0968  256 LEU B N   
7199  C CA  . LEU B 256 ? 0.4554 0.5050 0.6265 0.0320  0.1139  0.1013  256 LEU B CA  
7200  C C   . LEU B 256 ? 0.4791 0.5148 0.6469 0.0354  0.1147  0.1002  256 LEU B C   
7201  O O   . LEU B 256 ? 0.5041 0.5371 0.6714 0.0372  0.1140  0.0949  256 LEU B O   
7202  C CB  . LEU B 256 ? 0.2922 0.3463 0.4678 0.0331  0.1136  0.0988  256 LEU B CB  
7203  C CG  . LEU B 256 ? 0.4140 0.4827 0.5929 0.0301  0.1120  0.0983  256 LEU B CG  
7204  C CD1 . LEU B 256 ? 0.3642 0.4362 0.5482 0.0301  0.1115  0.0934  256 LEU B CD1 
7205  C CD2 . LEU B 256 ? 0.5442 0.6166 0.7232 0.0307  0.1119  0.1057  256 LEU B CD2 
7206  N N   . HIS B 257 ? 0.4953 0.5219 0.6602 0.0370  0.1160  0.1051  257 HIS B N   
7207  C CA  . HIS B 257 ? 0.4814 0.4947 0.6420 0.0405  0.1166  0.1038  257 HIS B CA  
7208  C C   . HIS B 257 ? 0.5501 0.5563 0.7103 0.0454  0.1191  0.1089  257 HIS B C   
7209  O O   . HIS B 257 ? 0.5818 0.5939 0.7455 0.0454  0.1198  0.1135  257 HIS B O   
7210  C CB  . HIS B 257 ? 0.6362 0.6457 0.7941 0.0371  0.1160  0.1032  257 HIS B CB  
7211  C CG  . HIS B 257 ? 0.5964 0.5925 0.7495 0.0402  0.1159  0.1010  257 HIS B CG  
7212  N ND1 . HIS B 257 ? 0.5783 0.5691 0.7284 0.0453  0.1153  0.0971  257 HIS B ND1 
7213  C CD2 . HIS B 257 ? 0.4971 0.4841 0.6471 0.0387  0.1161  0.1018  257 HIS B CD2 
7214  C CE1 . HIS B 257 ? 0.5993 0.5792 0.7444 0.0472  0.1148  0.0953  257 HIS B CE1 
7215  N NE2 . HIS B 257 ? 0.6384 0.6155 0.7839 0.0430  0.1153  0.0976  257 HIS B NE2 
7216  N N   . GLY B 258 ? 0.5106 0.5056 0.6665 0.0501  0.1204  0.1076  258 GLY B N   
7217  C CA  . GLY B 258 ? 0.6428 0.6315 0.7984 0.0551  0.1236  0.1118  258 GLY B CA  
7218  C C   . GLY B 258 ? 0.6061 0.5911 0.7607 0.0587  0.1260  0.1102  258 GLY B C   
7219  O O   . GLY B 258 ? 0.6971 0.6782 0.8475 0.0595  0.1247  0.1055  258 GLY B O   
7220  N N   . HIS B 259 ? 0.6112 0.5971 0.7695 0.0612  0.1296  0.1141  259 HIS B N   
7221  C CA  . HIS B 259 ? 0.5587 0.5393 0.7155 0.0643  0.1333  0.1136  259 HIS B CA  
7222  C C   . HIS B 259 ? 0.7655 0.7561 0.9325 0.0621  0.1360  0.1158  259 HIS B C   
7223  O O   . HIS B 259 ? 0.8242 0.8137 0.9924 0.0610  0.1380  0.1140  259 HIS B O   
7224  C CB  . HIS B 259 ? 0.4317 0.3995 0.5805 0.0707  0.1367  0.1154  259 HIS B CB  
7225  C CG  . HIS B 259 ? 0.5540 0.5115 0.6923 0.0731  0.1341  0.1111  259 HIS B CG  
7226  N ND1 . HIS B 259 ? 0.6935 0.6499 0.8295 0.0712  0.1300  0.1088  259 HIS B ND1 
7227  C CD2 . HIS B 259 ? 0.6695 0.6178 0.7988 0.0772  0.1349  0.1087  259 HIS B CD2 
7228  C CE1 . HIS B 259 ? 1.0472 0.9955 1.1746 0.0738  0.1279  0.1041  259 HIS B CE1 
7229  N NE2 . HIS B 259 ? 0.8191 0.7624 0.9416 0.0781  0.1306  0.1041  259 HIS B NE2 
7230  N N   . GLU B 260 ? 0.7506 0.7503 0.9246 0.0615  0.1359  0.1195  260 GLU B N   
7231  C CA  . GLU B 260 ? 0.6590 0.6709 0.8445 0.0593  0.1378  0.1209  260 GLU B CA  
7232  C C   . GLU B 260 ? 0.6630 0.6833 0.8531 0.0532  0.1348  0.1164  260 GLU B C   
7233  O O   . GLU B 260 ? 0.9570 0.9806 1.1444 0.0508  0.1303  0.1141  260 GLU B O   
7234  C CB  . GLU B 260 ? 0.7351 0.7569 0.9266 0.0607  0.1365  0.1252  260 GLU B CB  
7235  C CG  . GLU B 260 ? 0.9725 0.9844 1.1580 0.0671  0.1384  0.1290  260 GLU B CG  
7236  C CD  . GLU B 260 ? 0.8879 0.9002 1.0780 0.0720  0.1440  0.1319  260 GLU B CD  
7237  O OE1 . GLU B 260 ? 1.0273 1.0317 1.2141 0.0733  0.1486  0.1307  260 GLU B OE1 
7238  O OE2 . GLU B 260 ? 0.7542 0.7749 0.9507 0.0750  0.1440  0.1355  260 GLU B OE2 
7239  N N   . PRO B 261 ? 0.6610 0.6847 0.8580 0.0505  0.1376  0.1147  261 PRO B N   
7240  C CA  . PRO B 261 ? 0.5841 0.6135 0.7849 0.0450  0.1350  0.1095  261 PRO B CA  
7241  C C   . PRO B 261 ? 0.5908 0.6383 0.8028 0.0405  0.1320  0.1083  261 PRO B C   
7242  O O   . PRO B 261 ? 0.7111 0.7646 0.9240 0.0367  0.1283  0.1036  261 PRO B O   
7243  C CB  . PRO B 261 ? 0.6002 0.6206 0.8020 0.0446  0.1405  0.1088  261 PRO B CB  
7244  C CG  . PRO B 261 ? 0.6791 0.7010 0.8859 0.0470  0.1458  0.1138  261 PRO B CG  
7245  C CD  . PRO B 261 ? 0.9287 0.9499 1.1301 0.0522  0.1439  0.1174  261 PRO B CD  
7246  N N   . LEU B 262 ? 0.6355 0.6922 0.8558 0.0417  0.1334  0.1120  262 LEU B N   
7247  C CA  . LEU B 262 ? 0.4911 0.5667 0.7225 0.0380  0.1299  0.1104  262 LEU B CA  
7248  C C   . LEU B 262 ? 0.5822 0.6659 0.8092 0.0377  0.1236  0.1101  262 LEU B C   
7249  O O   . LEU B 262 ? 0.6530 0.7478 0.8837 0.0333  0.1198  0.1055  262 LEU B O   
7250  C CB  . LEU B 262 ? 0.4864 0.5719 0.7279 0.0406  0.1323  0.1145  262 LEU B CB  
7251  C CG  . LEU B 262 ? 0.5002 0.6076 0.7540 0.0377  0.1278  0.1125  262 LEU B CG  
7252  C CD1 . LEU B 262 ? 0.3222 0.4360 0.5861 0.0302  0.1285  0.1058  262 LEU B CD1 
7253  C CD2 . LEU B 262 ? 0.7033 0.8212 0.9657 0.0426  0.1292  0.1172  262 LEU B CD2 
7254  N N   . LEU B 263 ? 0.5474 0.6252 0.7659 0.0421  0.1227  0.1149  263 LEU B N   
7255  C CA  . LEU B 263 ? 0.4084 0.4922 0.6215 0.0414  0.1179  0.1157  263 LEU B CA  
7256  C C   . LEU B 263 ? 0.4800 0.5626 0.6886 0.0370  0.1160  0.1096  263 LEU B C   
7257  O O   . LEU B 263 ? 0.6286 0.7233 0.8383 0.0339  0.1123  0.1069  263 LEU B O   
7258  C CB  . LEU B 263 ? 0.4521 0.5255 0.6565 0.0460  0.1185  0.1216  263 LEU B CB  
7259  C CG  . LEU B 263 ? 0.4336 0.5087 0.6302 0.0445  0.1152  0.1230  263 LEU B CG  
7260  C CD1 . LEU B 263 ? 0.3427 0.4328 0.5419 0.0452  0.1115  0.1263  263 LEU B CD1 
7261  C CD2 . LEU B 263 ? 0.5688 0.6291 0.7570 0.0474  0.1169  0.1273  263 LEU B CD2 
7262  N N   . SER B 264 ? 0.4824 0.5512 0.6855 0.0374  0.1184  0.1074  264 SER B N   
7263  C CA  . SER B 264 ? 0.5140 0.5818 0.7133 0.0344  0.1167  0.1012  264 SER B CA  
7264  C C   . SER B 264 ? 0.4929 0.5698 0.6994 0.0303  0.1154  0.0953  264 SER B C   
7265  O O   . SER B 264 ? 0.5919 0.6773 0.7973 0.0276  0.1122  0.0909  264 SER B O   
7266  C CB  . SER B 264 ? 0.3996 0.4519 0.5929 0.0368  0.1191  0.0997  264 SER B CB  
7267  O OG  . SER B 264 ? 0.8028 0.8479 0.9993 0.0379  0.1228  0.0996  264 SER B OG  
7268  N N   . GLU B 265 ? 0.4405 0.5155 0.6541 0.0297  0.1183  0.0950  265 GLU B N   
7269  C CA  . GLU B 265 ? 0.4666 0.5483 0.6879 0.0249  0.1176  0.0888  265 GLU B CA  
7270  C C   . GLU B 265 ? 0.5048 0.6056 0.7308 0.0223  0.1126  0.0870  265 GLU B C   
7271  O O   . GLU B 265 ? 0.6120 0.7192 0.8395 0.0186  0.1098  0.0801  265 GLU B O   
7272  C CB  . GLU B 265 ? 0.5627 0.6408 0.7925 0.0239  0.1223  0.0900  265 GLU B CB  
7273  C CG  . GLU B 265 ? 0.6487 0.7267 0.8853 0.0183  0.1232  0.0831  265 GLU B CG  
7274  C CD  . GLU B 265 ? 0.7087 0.7681 0.9383 0.0190  0.1262  0.0804  265 GLU B CD  
7275  O OE1 . GLU B 265 ? 0.6553 0.7020 0.8755 0.0242  0.1283  0.0843  265 GLU B OE1 
7276  O OE2 . GLU B 265 ? 0.7595 0.8170 0.9929 0.0147  0.1263  0.0741  265 GLU B OE2 
7277  N N   . MET B 266 ? 0.3866 0.4955 0.6135 0.0250  0.1112  0.0931  266 MET B N   
7278  C CA  . MET B 266 ? 0.3908 0.5184 0.6208 0.0238  0.1060  0.0923  266 MET B CA  
7279  C C   . MET B 266 ? 0.5997 0.7301 0.8192 0.0238  0.1029  0.0918  266 MET B C   
7280  O O   . MET B 266 ? 0.5715 0.7155 0.7915 0.0214  0.0988  0.0874  266 MET B O   
7281  C CB  . MET B 266 ? 0.4213 0.5561 0.6552 0.0281  0.1056  0.0996  266 MET B CB  
7282  C CG  . MET B 266 ? 0.4248 0.5630 0.6716 0.0275  0.1085  0.0993  266 MET B CG  
7283  S SD  . MET B 266 ? 0.5345 0.6890 0.7946 0.0202  0.1055  0.0897  266 MET B SD  
7284  C CE  . MET B 266 ? 0.5401 0.6764 0.8026 0.0158  0.1123  0.0855  266 MET B CE  
7285  N N   . VAL B 267 ? 0.4889 0.6075 0.6994 0.0261  0.1049  0.0957  267 VAL B N   
7286  C CA  . VAL B 267 ? 0.4055 0.5272 0.6072 0.0252  0.1030  0.0951  267 VAL B CA  
7287  C C   . VAL B 267 ? 0.4790 0.6033 0.6808 0.0217  0.1021  0.0857  267 VAL B C   
7288  O O   . VAL B 267 ? 0.5375 0.6719 0.7351 0.0200  0.0996  0.0828  267 VAL B O   
7289  C CB  . VAL B 267 ? 0.3993 0.5085 0.5932 0.0274  0.1056  0.1004  267 VAL B CB  
7290  C CG1 . VAL B 267 ? 0.4303 0.5445 0.6166 0.0252  0.1045  0.0996  267 VAL B CG1 
7291  C CG2 . VAL B 267 ? 0.3978 0.5031 0.5910 0.0314  0.1065  0.1091  267 VAL B CG2 
7292  N N   . VAL B 268 ? 0.4420 0.5568 0.6479 0.0210  0.1042  0.0810  268 VAL B N   
7293  C CA  . VAL B 268 ? 0.4114 0.5264 0.6175 0.0186  0.1034  0.0720  268 VAL B CA  
7294  C C   . VAL B 268 ? 0.4856 0.6154 0.6971 0.0151  0.0999  0.0665  268 VAL B C   
7295  O O   . VAL B 268 ? 0.5576 0.6955 0.7657 0.0136  0.0974  0.0605  268 VAL B O   
7296  C CB  . VAL B 268 ? 0.4261 0.5253 0.6345 0.0193  0.1068  0.0695  268 VAL B CB  
7297  C CG1 . VAL B 268 ? 0.4553 0.5538 0.6653 0.0170  0.1059  0.0600  268 VAL B CG1 
7298  C CG2 . VAL B 268 ? 0.4053 0.4916 0.6067 0.0232  0.1090  0.0728  268 VAL B CG2 
7299  N N   . GLU B 269 ? 0.4779 0.6125 0.6982 0.0139  0.0995  0.0680  269 GLU B N   
7300  C CA  . GLU B 269 ? 0.4988 0.6489 0.7257 0.0103  0.0955  0.0620  269 GLU B CA  
7301  C C   . GLU B 269 ? 0.5509 0.7171 0.7716 0.0117  0.0909  0.0640  269 GLU B C   
7302  O O   . GLU B 269 ? 0.5864 0.7648 0.8068 0.0093  0.0870  0.0568  269 GLU B O   
7303  C CB  . GLU B 269 ? 0.3712 0.5249 0.6104 0.0089  0.0963  0.0637  269 GLU B CB  
7304  C CG  . GLU B 269 ? 0.5063 0.6664 0.7558 0.0030  0.0947  0.0541  269 GLU B CG  
7305  C CD  . GLU B 269 ? 0.8902 1.0605 1.1538 0.0006  0.0946  0.0550  269 GLU B CD  
7306  O OE1 . GLU B 269 ? 0.9086 1.0697 1.1768 0.0018  0.0998  0.0607  269 GLU B OE1 
7307  O OE2 . GLU B 269 ? 1.0781 1.2665 1.3484 -0.0022 0.0893  0.0495  269 GLU B OE2 
7308  N N   . ALA B 270 ? 0.4960 0.6613 0.7110 0.0156  0.0916  0.0736  270 ALA B N   
7309  C CA  . ALA B 270 ? 0.4614 0.6388 0.6683 0.0175  0.0882  0.0776  270 ALA B CA  
7310  C C   . ALA B 270 ? 0.5120 0.6908 0.7093 0.0161  0.0882  0.0733  270 ALA B C   
7311  O O   . ALA B 270 ? 0.6402 0.8328 0.8322 0.0158  0.0848  0.0713  270 ALA B O   
7312  C CB  . ALA B 270 ? 0.4134 0.5841 0.6155 0.0219  0.0902  0.0890  270 ALA B CB  
7313  N N   . ALA B 271 ? 0.4478 0.6137 0.6428 0.0156  0.0920  0.0715  271 ALA B N   
7314  C CA  . ALA B 271 ? 0.5037 0.6723 0.6914 0.0145  0.0926  0.0668  271 ALA B CA  
7315  C C   . ALA B 271 ? 0.6597 0.8387 0.8486 0.0122  0.0895  0.0558  271 ALA B C   
7316  O O   . ALA B 271 ? 0.7125 0.8980 0.8945 0.0118  0.0896  0.0517  271 ALA B O   
7317  C CB  . ALA B 271 ? 0.4291 0.5831 0.6162 0.0152  0.0964  0.0659  271 ALA B CB  
7318  N N   . SER B 272 ? 0.4504 0.6313 0.6481 0.0104  0.0873  0.0506  272 SER B N   
7319  C CA  . SER B 272 ? 0.4722 0.6620 0.6718 0.0077  0.0840  0.0391  272 SER B CA  
7320  C C   . SER B 272 ? 0.5771 0.7860 0.7758 0.0072  0.0785  0.0382  272 SER B C   
7321  O O   . SER B 272 ? 0.5880 0.8064 0.7869 0.0050  0.0750  0.0282  272 SER B O   
7322  C CB  . SER B 272 ? 0.4453 0.6246 0.6553 0.0050  0.0850  0.0327  272 SER B CB  
7323  O OG  . SER B 272 ? 0.7760 0.9381 0.9845 0.0066  0.0894  0.0328  272 SER B OG  
7324  N N   . ASP B 273 ? 0.6603 0.8749 0.8574 0.0097  0.0774  0.0483  273 ASP B N   
7325  C CA  . ASP B 273 ? 0.4458 0.6789 0.6410 0.0108  0.0715  0.0485  273 ASP B CA  
7326  C C   . ASP B 273 ? 0.5615 0.8052 0.7435 0.0114  0.0699  0.0451  273 ASP B C   
7327  O O   . ASP B 273 ? 0.6737 0.9131 0.8455 0.0132  0.0735  0.0516  273 ASP B O   
7328  C CB  . ASP B 273 ? 0.4670 0.7011 0.6606 0.0152  0.0714  0.0614  273 ASP B CB  
7329  C CG  . ASP B 273 ? 0.6478 0.9012 0.8383 0.0180  0.0649  0.0630  273 ASP B CG  
7330  O OD1 . ASP B 273 ? 0.7596 1.0263 0.9567 0.0156  0.0597  0.0535  273 ASP B OD1 
7331  O OD2 . ASP B 273 ? 0.8755 1.1302 1.0566 0.0227  0.0648  0.0736  273 ASP B OD2 
7332  N N   . PRO B 274 ? 0.5756 0.8330 0.7574 0.0096  0.0649  0.0344  274 PRO B N   
7333  C CA  . PRO B 274 ? 0.5826 0.8505 0.7503 0.0107  0.0639  0.0308  274 PRO B CA  
7334  C C   . PRO B 274 ? 0.4978 0.7711 0.6519 0.0148  0.0648  0.0431  274 PRO B C   
7335  O O   . PRO B 274 ? 0.6430 0.9163 0.7859 0.0152  0.0684  0.0443  274 PRO B O   
7336  C CB  . PRO B 274 ? 0.7050 0.9892 0.8754 0.0091  0.0567  0.0193  274 PRO B CB  
7337  C CG  . PRO B 274 ? 0.5471 0.8245 0.7344 0.0050  0.0560  0.0131  274 PRO B CG  
7338  C CD  . PRO B 274 ? 0.5438 0.8081 0.7380 0.0062  0.0602  0.0247  274 PRO B CD  
7339  N N   . GLU B 275 ? 0.4931 0.7705 0.6481 0.0179  0.0618  0.0523  275 GLU B N   
7340  C CA  . GLU B 275 ? 0.5571 0.8369 0.6984 0.0224  0.0627  0.0650  275 GLU B CA  
7341  C C   . GLU B 275 ? 0.6072 0.8700 0.7444 0.0218  0.0706  0.0737  275 GLU B C   
7342  O O   . GLU B 275 ? 0.7027 0.9665 0.8263 0.0226  0.0738  0.0794  275 GLU B O   
7343  C CB  . GLU B 275 ? 0.6518 0.9367 0.7969 0.0269  0.0581  0.0731  275 GLU B CB  
7344  C CG  . GLU B 275 ? 0.8611 1.1675 1.0059 0.0289  0.0493  0.0668  275 GLU B CG  
7345  C CD  . GLU B 275 ? 1.3188 1.6332 1.4651 0.0352  0.0443  0.0758  275 GLU B CD  
7346  O OE1 . GLU B 275 ? 1.4213 1.7252 1.5609 0.0395  0.0477  0.0893  275 GLU B OE1 
7347  O OE2 . GLU B 275 ? 1.4423 1.7736 1.5967 0.0359  0.0367  0.0688  275 GLU B OE2 
7348  N N   . LEU B 276 ? 0.5152 0.7628 0.6638 0.0202  0.0739  0.0746  276 LEU B N   
7349  C CA  . LEU B 276 ? 0.5157 0.7476 0.6618 0.0195  0.0807  0.0814  276 LEU B CA  
7350  C C   . LEU B 276 ? 0.5586 0.7892 0.7019 0.0162  0.0845  0.0737  276 LEU B C   
7351  O O   . LEU B 276 ? 0.6421 0.8671 0.7792 0.0153  0.0895  0.0789  276 LEU B O   
7352  C CB  . LEU B 276 ? 0.4515 0.6684 0.6092 0.0197  0.0826  0.0843  276 LEU B CB  
7353  C CG  . LEU B 276 ? 0.4998 0.7160 0.6601 0.0238  0.0804  0.0935  276 LEU B CG  
7354  C CD1 . LEU B 276 ? 0.5650 0.7665 0.7359 0.0240  0.0832  0.0953  276 LEU B CD1 
7355  C CD2 . LEU B 276 ? 0.5281 0.7422 0.6755 0.0271  0.0819  0.1057  276 LEU B CD2 
7356  N N   . VAL B 277 ? 0.5342 0.7704 0.6826 0.0144  0.0822  0.0611  277 VAL B N   
7357  C CA  . VAL B 277 ? 0.4823 0.7186 0.6282 0.0125  0.0854  0.0528  277 VAL B CA  
7358  C C   . VAL B 277 ? 0.5817 0.8312 0.7136 0.0130  0.0866  0.0546  277 VAL B C   
7359  O O   . VAL B 277 ? 0.6163 0.8644 0.7436 0.0118  0.0918  0.0554  277 VAL B O   
7360  C CB  . VAL B 277 ? 0.4480 0.6860 0.6015 0.0112  0.0823  0.0388  277 VAL B CB  
7361  C CG1 . VAL B 277 ? 0.4276 0.6695 0.5765 0.0108  0.0848  0.0294  277 VAL B CG1 
7362  C CG2 . VAL B 277 ? 0.5299 0.7525 0.6961 0.0104  0.0831  0.0377  277 VAL B CG2 
7363  N N   . GLU B 278 ? 0.4708 0.7335 0.5955 0.0148  0.0818  0.0554  278 GLU B N   
7364  C CA  . GLU B 278 ? 0.4158 0.6911 0.5248 0.0159  0.0829  0.0580  278 GLU B CA  
7365  C C   . GLU B 278 ? 0.5437 0.8124 0.6444 0.0164  0.0879  0.0730  278 GLU B C   
7366  O O   . GLU B 278 ? 0.6226 0.8955 0.7128 0.0152  0.0930  0.0756  278 GLU B O   
7367  C CB  . GLU B 278 ? 0.4666 0.7576 0.5695 0.0186  0.0755  0.0552  278 GLU B CB  
7368  C CG  . GLU B 278 ? 0.6569 0.9572 0.7640 0.0173  0.0711  0.0388  278 GLU B CG  
7369  C CD  . GLU B 278 ? 0.8599 1.1642 0.9605 0.0162  0.0754  0.0303  278 GLU B CD  
7370  O OE1 . GLU B 278 ? 0.7869 1.1025 0.8723 0.0177  0.0772  0.0328  278 GLU B OE1 
7371  O OE2 . GLU B 278 ? 0.8542 1.1504 0.9647 0.0142  0.0774  0.0213  278 GLU B OE2 
7372  N N   . LEU B 279 ? 0.5492 0.8073 0.6545 0.0179  0.0870  0.0827  279 LEU B N   
7373  C CA  . LEU B 279 ? 0.5601 0.8090 0.6575 0.0184  0.0919  0.0969  279 LEU B CA  
7374  C C   . LEU B 279 ? 0.5866 0.8263 0.6860 0.0139  0.0995  0.0968  279 LEU B C   
7375  O O   . LEU B 279 ? 0.7237 0.9625 0.8133 0.0121  0.1049  0.1045  279 LEU B O   
7376  C CB  . LEU B 279 ? 0.4869 0.7247 0.5905 0.0214  0.0896  0.1056  279 LEU B CB  
7377  C CG  . LEU B 279 ? 0.3764 0.6024 0.4711 0.0226  0.0940  0.1204  279 LEU B CG  
7378  C CD1 . LEU B 279 ? 0.3949 0.6302 0.4726 0.0260  0.0929  0.1283  279 LEU B CD1 
7379  C CD2 . LEU B 279 ? 0.5616 0.7750 0.6647 0.0257  0.0924  0.1266  279 LEU B CD2 
7380  N N   . ALA B 280 ? 0.5499 0.7836 0.6621 0.0120  0.0999  0.0880  280 ALA B N   
7381  C CA  . ALA B 280 ? 0.4594 0.6868 0.5751 0.0084  0.1059  0.0862  280 ALA B CA  
7382  C C   . ALA B 280 ? 0.5438 0.7851 0.6515 0.0064  0.1097  0.0814  280 ALA B C   
7383  O O   . ALA B 280 ? 0.5637 0.8036 0.6700 0.0030  0.1159  0.0842  280 ALA B O   
7384  C CB  . ALA B 280 ? 0.4670 0.6872 0.5961 0.0084  0.1045  0.0768  280 ALA B CB  
7385  N N   . LYS B 281 ? 0.4585 0.7136 0.5609 0.0083  0.1061  0.0740  281 LYS B N   
7386  C CA  . LYS B 281 ? 0.5658 0.8353 0.6593 0.0072  0.1097  0.0690  281 LYS B CA  
7387  C C   . LYS B 281 ? 0.6240 0.8980 0.7016 0.0068  0.1134  0.0813  281 LYS B C   
7388  O O   . LYS B 281 ? 0.7000 0.9796 0.7715 0.0039  0.1204  0.0829  281 LYS B O   
7389  C CB  . LYS B 281 ? 0.5182 0.8000 0.6103 0.0097  0.1043  0.0563  281 LYS B CB  
7390  C CG  . LYS B 281 ? 0.4323 0.7072 0.5389 0.0102  0.1006  0.0449  281 LYS B CG  
7391  C CD  . LYS B 281 ? 0.5841 0.8700 0.6893 0.0114  0.0985  0.0301  281 LYS B CD  
7392  C CE  . LYS B 281 ? 0.4698 0.7494 0.5859 0.0122  0.0928  0.0199  281 LYS B CE  
7393  N NZ  . LYS B 281 ? 0.5335 0.8256 0.6443 0.0133  0.0873  0.0100  281 LYS B NZ  
7394  N N   . SER B 282 ? 0.5689 0.8407 0.6401 0.0100  0.1090  0.0902  282 SER B N   
7395  C CA  . SER B 282 ? 0.6032 0.8767 0.6576 0.0109  0.1120  0.1032  282 SER B CA  
7396  C C   . SER B 282 ? 0.7204 0.9817 0.7741 0.0062  0.1206  0.1135  282 SER B C   
7397  O O   . SER B 282 ? 0.8139 1.0790 0.8546 0.0041  0.1269  0.1207  282 SER B O   
7398  C CB  . SER B 282 ? 0.5004 0.7706 0.5512 0.0162  0.1051  0.1112  282 SER B CB  
7399  O OG  . SER B 282 ? 0.9065 1.1904 0.9576 0.0200  0.0969  0.1017  282 SER B OG  
7400  N N   . VAL B 283 ? 0.5574 0.8039 0.6248 0.0042  0.1212  0.1141  283 VAL B N   
7401  C CA  . VAL B 283 ? 0.5331 0.7675 0.6017 -0.0010 0.1288  0.1224  283 VAL B CA  
7402  C C   . VAL B 283 ? 0.6787 0.9207 0.7531 -0.0067 0.1354  0.1143  283 VAL B C   
7403  O O   . VAL B 283 ? 0.7273 0.9627 0.8031 -0.0122 0.1423  0.1198  283 VAL B O   
7404  C CB  . VAL B 283 ? 0.5649 0.7804 0.6439 -0.0005 0.1268  0.1267  283 VAL B CB  
7405  C CG1 . VAL B 283 ? 0.5009 0.7109 0.5747 0.0057  0.1210  0.1348  283 VAL B CG1 
7406  C CG2 . VAL B 283 ? 0.5511 0.7648 0.6464 -0.0006 0.1238  0.1148  283 VAL B CG2 
7407  N N   . GLY B 284 ? 0.5204 0.7765 0.5984 -0.0052 0.1332  0.1012  284 GLY B N   
7408  C CA  . GLY B 284 ? 0.4855 0.7515 0.5692 -0.0089 0.1387  0.0923  284 GLY B CA  
7409  C C   . GLY B 284 ? 0.4751 0.7346 0.5759 -0.0094 0.1372  0.0837  284 GLY B C   
7410  O O   . GLY B 284 ? 0.5911 0.8524 0.6986 -0.0137 0.1428  0.0818  284 GLY B O   
7411  N N   . ALA B 285 ? 0.5022 0.7549 0.6102 -0.0051 0.1300  0.0782  285 ALA B N   
7412  C CA  . ALA B 285 ? 0.5159 0.7609 0.6382 -0.0046 0.1283  0.0707  285 ALA B CA  
7413  C C   . ALA B 285 ? 0.5607 0.8127 0.6879 -0.0006 0.1242  0.0568  285 ALA B C   
7414  O O   . ALA B 285 ? 0.6706 0.9303 0.7913 0.0019  0.1209  0.0531  285 ALA B O   
7415  C CB  . ALA B 285 ? 0.5231 0.7504 0.6502 -0.0032 0.1246  0.0771  285 ALA B CB  
7416  N N   . ASP B 286 ? 0.5738 0.8222 0.7118 0.0005  0.1241  0.0489  286 ASP B N   
7417  C CA  . ASP B 286 ? 0.6122 0.8632 0.7551 0.0048  0.1205  0.0360  286 ASP B CA  
7418  C C   . ASP B 286 ? 0.5362 0.7760 0.6811 0.0075  0.1142  0.0355  286 ASP B C   
7419  O O   . ASP B 286 ? 0.5468 0.7897 0.6916 0.0101  0.1108  0.0264  286 ASP B O   
7420  C CB  . ASP B 286 ? 0.5136 0.7613 0.6671 0.0063  0.1217  0.0295  286 ASP B CB  
7421  C CG  . ASP B 286 ? 0.8266 1.0893 0.9817 0.0042  0.1275  0.0260  286 ASP B CG  
7422  O OD1 . ASP B 286 ? 0.9400 1.2173 1.0873 0.0029  0.1308  0.0250  286 ASP B OD1 
7423  O OD2 . ASP B 286 ? 0.9141 1.1751 1.0780 0.0042  0.1289  0.0239  286 ASP B OD2 
7424  N N   . GLY B 287 ? 0.4562 0.6829 0.6032 0.0067  0.1130  0.0446  287 GLY B N   
7425  C CA  . GLY B 287 ? 0.5232 0.7398 0.6735 0.0086  0.1081  0.0456  287 GLY B CA  
7426  C C   . GLY B 287 ? 0.5186 0.7205 0.6724 0.0082  0.1085  0.0551  287 GLY B C   
7427  O O   . GLY B 287 ? 0.5739 0.7739 0.7254 0.0059  0.1121  0.0623  287 GLY B O   
7428  N N   . ILE B 288 ? 0.4729 0.6642 0.6322 0.0102  0.1052  0.0550  288 ILE B N   
7429  C CA  . ILE B 288 ? 0.4258 0.6029 0.5880 0.0106  0.1057  0.0632  288 ILE B CA  
7430  C C   . ILE B 288 ? 0.4198 0.5854 0.5886 0.0125  0.1062  0.0585  288 ILE B C   
7431  O O   . ILE B 288 ? 0.5645 0.7253 0.7376 0.0146  0.1041  0.0524  288 ILE B O   
7432  C CB  . ILE B 288 ? 0.3397 0.5138 0.5032 0.0119  0.1024  0.0679  288 ILE B CB  
7433  C CG1 . ILE B 288 ? 0.3458 0.5330 0.5018 0.0113  0.1008  0.0718  288 ILE B CG1 
7434  C CG2 . ILE B 288 ? 0.3400 0.5003 0.5057 0.0130  0.1036  0.0766  288 ILE B CG2 
7435  C CD1 . ILE B 288 ? 0.4868 0.6773 0.6458 0.0129  0.0963  0.0721  288 ILE B CD1 
7436  N N   . ASN B 289 ? 0.5120 0.6732 0.6814 0.0117  0.1089  0.0611  289 ASN B N   
7437  C CA  . ASN B 289 ? 0.4401 0.5913 0.6144 0.0143  0.1088  0.0570  289 ASN B CA  
7438  C C   . ASN B 289 ? 0.4295 0.5655 0.6048 0.0157  0.1085  0.0640  289 ASN B C   
7439  O O   . ASN B 289 ? 0.5844 0.7165 0.7579 0.0139  0.1101  0.0708  289 ASN B O   
7440  C CB  . ASN B 289 ? 0.4854 0.6423 0.6608 0.0127  0.1112  0.0547  289 ASN B CB  
7441  C CG  . ASN B 289 ? 0.4911 0.6407 0.6712 0.0166  0.1101  0.0490  289 ASN B CG  
7442  O OD1 . ASN B 289 ? 0.4691 0.6148 0.6507 0.0209  0.1080  0.0428  289 ASN B OD1 
7443  N ND2 . ASN B 289 ? 0.5644 0.7115 0.7463 0.0153  0.1112  0.0508  289 ASN B ND2 
7444  N N   . LEU B 290 ? 0.5323 0.6596 0.7103 0.0187  0.1068  0.0620  290 LEU B N   
7445  C CA  . LEU B 290 ? 0.4392 0.5525 0.6181 0.0206  0.1070  0.0682  290 LEU B CA  
7446  C C   . LEU B 290 ? 0.5484 0.6506 0.7278 0.0238  0.1074  0.0659  290 LEU B C   
7447  O O   . LEU B 290 ? 0.7535 0.8540 0.9341 0.0265  0.1065  0.0589  290 LEU B O   
7448  C CB  . LEU B 290 ? 0.5224 0.6330 0.7045 0.0216  0.1058  0.0671  290 LEU B CB  
7449  C CG  . LEU B 290 ? 0.5989 0.7173 0.7812 0.0197  0.1047  0.0721  290 LEU B CG  
7450  C CD1 . LEU B 290 ? 0.4737 0.5883 0.6617 0.0204  0.1040  0.0714  290 LEU B CD1 
7451  C CD2 . LEU B 290 ? 0.6044 0.7197 0.7835 0.0198  0.1060  0.0815  290 LEU B CD2 
7452  N N   . CYS B 291 ? 0.4735 0.5678 0.6513 0.0239  0.1085  0.0713  291 CYS B N   
7453  C CA  . CYS B 291 ? 0.4083 0.4922 0.5855 0.0275  0.1082  0.0691  291 CYS B CA  
7454  C C   . CYS B 291 ? 0.4647 0.5351 0.6400 0.0297  0.1091  0.0754  291 CYS B C   
7455  O O   . CYS B 291 ? 0.4403 0.5106 0.6153 0.0281  0.1101  0.0818  291 CYS B O   
7456  C CB  . CYS B 291 ? 0.3453 0.4346 0.5228 0.0254  0.1082  0.0668  291 CYS B CB  
7457  S SG  . CYS B 291 ? 0.6735 0.7821 0.8537 0.0220  0.1085  0.0604  291 CYS B SG  
7458  N N   . GLY B 292 ? 0.4012 0.4605 0.5745 0.0342  0.1088  0.0736  292 GLY B N   
7459  C CA  . GLY B 292 ? 0.2927 0.3388 0.4632 0.0371  0.1102  0.0789  292 GLY B CA  
7460  C C   . GLY B 292 ? 0.4706 0.5088 0.6372 0.0398  0.1093  0.0774  292 GLY B C   
7461  O O   . GLY B 292 ? 0.5715 0.6143 0.7385 0.0403  0.1071  0.0715  292 GLY B O   
7462  N N   . MET B 293 ? 0.4452 0.4725 0.6083 0.0418  0.1106  0.0821  293 MET B N   
7463  C CA  . MET B 293 ? 0.4666 0.4854 0.6251 0.0446  0.1095  0.0803  293 MET B CA  
7464  C C   . MET B 293 ? 0.6271 0.6321 0.7803 0.0499  0.1115  0.0841  293 MET B C   
7465  O O   . MET B 293 ? 0.7769 0.7801 0.9315 0.0497  0.1143  0.0896  293 MET B O   
7466  C CB  . MET B 293 ? 0.4246 0.4453 0.5841 0.0396  0.1094  0.0819  293 MET B CB  
7467  C CG  . MET B 293 ? 0.5075 0.5418 0.6717 0.0342  0.1081  0.0776  293 MET B CG  
7468  S SD  . MET B 293 ? 0.5333 0.5670 0.6983 0.0287  0.1079  0.0765  293 MET B SD  
7469  C CE  . MET B 293 ? 0.7319 0.7576 0.8945 0.0260  0.1113  0.0864  293 MET B CE  
7470  N N   . CYS B 294 ? 0.5114 0.5077 0.6583 0.0550  0.1101  0.0810  294 CYS B N   
7471  C CA  . CYS B 294 ? 0.6151 0.5977 0.7550 0.0607  0.1126  0.0844  294 CYS B CA  
7472  C C   . CYS B 294 ? 0.6160 0.5960 0.7566 0.0627  0.1162  0.0878  294 CYS B C   
7473  O O   . CYS B 294 ? 0.5876 0.5742 0.7325 0.0607  0.1155  0.0855  294 CYS B O   
7474  C CB  . CYS B 294 ? 0.7092 0.6868 0.8483 0.0595  0.1145  0.0888  294 CYS B CB  
7475  S SG  . CYS B 294 ? 0.6376 0.6100 0.7721 0.0592  0.1111  0.0841  294 CYS B SG  
7476  N N   . CYS B 295 ? 0.6366 0.6074 0.7736 0.0660  0.1202  0.0925  295 CYS B N   
7477  C CA  . CYS B 295 ? 0.5818 0.5495 0.7201 0.0673  0.1245  0.0956  295 CYS B CA  
7478  C C   . CYS B 295 ? 0.5108 0.4907 0.6599 0.0612  0.1248  0.0964  295 CYS B C   
7479  O O   . CYS B 295 ? 0.7074 0.6880 0.8588 0.0603  0.1255  0.0945  295 CYS B O   
7480  C CB  . CYS B 295 ? 0.6059 0.5648 0.7403 0.0711  0.1295  0.1008  295 CYS B CB  
7481  S SG  . CYS B 295 ? 1.0559 0.9987 1.1750 0.0797  0.1305  0.0998  295 CYS B SG  
7482  N N   . THR B 296 ? 0.5207 0.5090 0.6756 0.0575  0.1243  0.0990  296 THR B N   
7483  C CA  . THR B 296 ? 0.5466 0.5472 0.7106 0.0525  0.1241  0.0996  296 THR B CA  
7484  C C   . THR B 296 ? 0.4796 0.4866 0.6453 0.0498  0.1211  0.0937  296 THR B C   
7485  O O   . THR B 296 ? 0.6086 0.6201 0.7795 0.0475  0.1217  0.0922  296 THR B O   
7486  C CB  . THR B 296 ? 0.5906 0.5996 0.7585 0.0498  0.1230  0.1032  296 THR B CB  
7487  O OG1 . THR B 296 ? 0.5851 0.6056 0.7611 0.0466  0.1231  0.1043  296 THR B OG1 
7488  C CG2 . THR B 296 ? 0.5549 0.5685 0.7210 0.0469  0.1195  0.1009  296 THR B CG2 
7489  N N   . GLY B 297 ? 0.5763 0.5839 0.7383 0.0501  0.1179  0.0898  297 GLY B N   
7490  C CA  . GLY B 297 ? 0.4822 0.4967 0.6458 0.0486  0.1152  0.0837  297 GLY B CA  
7491  C C   . GLY B 297 ? 0.5303 0.5362 0.6910 0.0525  0.1160  0.0808  297 GLY B C   
7492  O O   . GLY B 297 ? 0.6532 0.6636 0.8168 0.0512  0.1150  0.0765  297 GLY B O   
7493  N N   . ASN B 298 ? 0.5079 0.5002 0.6618 0.0577  0.1182  0.0833  298 ASN B N   
7494  C CA  . ASN B 298 ? 0.4649 0.4458 0.6138 0.0622  0.1198  0.0822  298 ASN B CA  
7495  C C   . ASN B 298 ? 0.6148 0.5947 0.7695 0.0586  0.1239  0.0844  298 ASN B C   
7496  O O   . ASN B 298 ? 0.5976 0.5741 0.7530 0.0585  0.1242  0.0813  298 ASN B O   
7497  C CB  . ASN B 298 ? 0.5175 0.4843 0.6560 0.0688  0.1216  0.0852  298 ASN B CB  
7498  C CG  . ASN B 298 ? 0.5732 0.5382 0.7044 0.0739  0.1169  0.0808  298 ASN B CG  
7499  O OD1 . ASN B 298 ? 0.6642 0.6323 0.7953 0.0757  0.1135  0.0756  298 ASN B OD1 
7500  N ND2 . ASN B 298 ? 0.6570 0.6176 0.7823 0.0767  0.1165  0.0823  298 ASN B ND2 
7501  N N   . GLU B 299 ? 0.5415 0.5248 0.7013 0.0557  0.1270  0.0894  299 GLU B N   
7502  C CA  . GLU B 299 ? 0.5954 0.5803 0.7629 0.0517  0.1308  0.0911  299 GLU B CA  
7503  C C   . GLU B 299 ? 0.6416 0.6380 0.8170 0.0462  0.1279  0.0860  299 GLU B C   
7504  O O   . GLU B 299 ? 0.7418 0.7352 0.9212 0.0436  0.1300  0.0840  299 GLU B O   
7505  C CB  . GLU B 299 ? 0.4635 0.4540 0.6364 0.0502  0.1336  0.0967  299 GLU B CB  
7506  C CG  . GLU B 299 ? 0.7578 0.7369 0.9231 0.0557  0.1374  0.1016  299 GLU B CG  
7507  C CD  . GLU B 299 ? 0.9668 0.9363 1.1315 0.0568  0.1444  0.1049  299 GLU B CD  
7508  O OE1 . GLU B 299 ? 0.8593 0.8215 1.0228 0.0559  0.1461  0.1030  299 GLU B OE1 
7509  O OE2 . GLU B 299 ? 0.9604 0.9289 1.1256 0.0588  0.1486  0.1096  299 GLU B OE2 
7510  N N   . VAL B 300 ? 0.5256 0.5345 0.7029 0.0442  0.1234  0.0836  300 VAL B N   
7511  C CA  . VAL B 300 ? 0.4959 0.5170 0.6793 0.0395  0.1206  0.0784  300 VAL B CA  
7512  C C   . VAL B 300 ? 0.6716 0.6883 0.8512 0.0416  0.1187  0.0717  300 VAL B C   
7513  O O   . VAL B 300 ? 0.5892 0.6096 0.7730 0.0387  0.1179  0.0667  300 VAL B O   
7514  C CB  . VAL B 300 ? 0.3985 0.4345 0.5840 0.0368  0.1174  0.0792  300 VAL B CB  
7515  C CG1 . VAL B 300 ? 0.6133 0.6626 0.8045 0.0321  0.1150  0.0745  300 VAL B CG1 
7516  C CG2 . VAL B 300 ? 0.5982 0.6363 0.7857 0.0368  0.1189  0.0863  300 VAL B CG2 
7517  N N   . SER B 301 ? 0.6521 0.6618 0.8242 0.0469  0.1175  0.0711  301 SER B N   
7518  C CA  . SER B 301 ? 0.4873 0.4933 0.6557 0.0507  0.1153  0.0648  301 SER B CA  
7519  C C   . SER B 301 ? 0.6444 0.6336 0.8096 0.0535  0.1185  0.0648  301 SER B C   
7520  O O   . SER B 301 ? 0.5818 0.5679 0.7467 0.0548  0.1174  0.0592  301 SER B O   
7521  C CB  . SER B 301 ? 0.3655 0.3706 0.5278 0.0558  0.1127  0.0640  301 SER B CB  
7522  O OG  . SER B 301 ? 0.6952 0.7022 0.8560 0.0595  0.1097  0.0571  301 SER B OG  
7523  N N   . MET B 302 ? 0.6311 0.6090 0.7936 0.0544  0.1229  0.0711  302 MET B N   
7524  C CA  . MET B 302 ? 0.5035 0.4640 0.6622 0.0564  0.1273  0.0725  302 MET B CA  
7525  C C   . MET B 302 ? 0.5988 0.5617 0.7668 0.0494  0.1293  0.0697  302 MET B C   
7526  O O   . MET B 302 ? 0.6756 0.6262 0.8416 0.0502  0.1309  0.0670  302 MET B O   
7527  C CB  . MET B 302 ? 0.5839 0.5344 0.7383 0.0582  0.1325  0.0804  302 MET B CB  
7528  C CG  . MET B 302 ? 0.5844 0.5270 0.7269 0.0663  0.1313  0.0827  302 MET B CG  
7529  S SD  . MET B 302 ? 0.5877 0.5093 0.7159 0.0757  0.1319  0.0823  302 MET B SD  
7530  C CE  . MET B 302 ? 0.6511 0.5562 0.7768 0.0740  0.1415  0.0900  302 MET B CE  
7531  N N   . ARG B 303 ? 0.5176 0.4957 0.6957 0.0426  0.1289  0.0703  303 ARG B N   
7532  C CA  . ARG B 303 ? 0.5433 0.5265 0.7315 0.0353  0.1301  0.0668  303 ARG B CA  
7533  C C   . ARG B 303 ? 0.6495 0.6467 0.8420 0.0322  0.1248  0.0589  303 ARG B C   
7534  O O   . ARG B 303 ? 0.8929 0.8897 1.0910 0.0277  0.1251  0.0535  303 ARG B O   
7535  C CB  . ARG B 303 ? 0.4580 0.4510 0.6552 0.0303  0.1326  0.0718  303 ARG B CB  
7536  C CG  . ARG B 303 ? 0.6029 0.5838 0.7963 0.0332  0.1387  0.0794  303 ARG B CG  
7537  C CD  . ARG B 303 ? 0.4737 0.4649 0.6779 0.0284  0.1418  0.0834  303 ARG B CD  
7538  N NE  . ARG B 303 ? 0.5604 0.5394 0.7612 0.0309  0.1490  0.0901  303 ARG B NE  
7539  C CZ  . ARG B 303 ? 0.5996 0.5746 0.7923 0.0371  0.1501  0.0955  303 ARG B CZ  
7540  N NH1 . ARG B 303 ? 0.6663 0.6476 0.8543 0.0407  0.1446  0.0950  303 ARG B NH1 
7541  N NH2 . ARG B 303 ? 0.4813 0.4454 0.6703 0.0394  0.1572  0.1011  303 ARG B NH2 
7542  N N   . HIS B 304 ? 0.4933 0.5029 0.6835 0.0342  0.1205  0.0578  304 HIS B N   
7543  C CA  . HIS B 304 ? 0.4975 0.5216 0.6908 0.0314  0.1162  0.0507  304 HIS B CA  
7544  C C   . HIS B 304 ? 0.5571 0.5838 0.7444 0.0364  0.1131  0.0464  304 HIS B C   
7545  O O   . HIS B 304 ? 0.5219 0.5623 0.7110 0.0345  0.1101  0.0410  304 HIS B O   
7546  C CB  . HIS B 304 ? 0.5427 0.5851 0.7415 0.0269  0.1143  0.0534  304 HIS B CB  
7547  C CG  . HIS B 304 ? 0.5560 0.5993 0.7623 0.0229  0.1169  0.0575  304 HIS B CG  
7548  N ND1 . HIS B 304 ? 0.7121 0.7563 0.9261 0.0176  0.1176  0.0528  304 HIS B ND1 
7549  C CD2 . HIS B 304 ? 0.5724 0.6158 0.7802 0.0235  0.1192  0.0653  304 HIS B CD2 
7550  C CE1 . HIS B 304 ? 0.8522 0.8989 1.0731 0.0149  0.1202  0.0578  304 HIS B CE1 
7551  N NE2 . HIS B 304 ? 0.6043 0.6505 0.8213 0.0189  0.1214  0.0655  304 HIS B NE2 
7552  N N   . GLY B 305 ? 0.5582 0.5733 0.7385 0.0428  0.1137  0.0484  305 GLY B N   
7553  C CA  . GLY B 305 ? 0.5350 0.5539 0.7110 0.0479  0.1105  0.0439  305 GLY B CA  
7554  C C   . GLY B 305 ? 0.5403 0.5771 0.7181 0.0456  0.1082  0.0442  305 GLY B C   
7555  O O   . GLY B 305 ? 0.4722 0.5174 0.6493 0.0477  0.1058  0.0389  305 GLY B O   
7556  N N   . ILE B 306 ? 0.5185 0.5610 0.6986 0.0413  0.1091  0.0505  306 ILE B N   
7557  C CA  . ILE B 306 ? 0.4889 0.5457 0.6697 0.0387  0.1076  0.0522  306 ILE B CA  
7558  C C   . ILE B 306 ? 0.3789 0.4337 0.5557 0.0429  0.1065  0.0519  306 ILE B C   
7559  O O   . ILE B 306 ? 0.4483 0.4911 0.6213 0.0466  0.1073  0.0554  306 ILE B O   
7560  C CB  . ILE B 306 ? 0.4623 0.5220 0.6453 0.0349  0.1089  0.0599  306 ILE B CB  
7561  C CG1 . ILE B 306 ? 0.2939 0.3614 0.4823 0.0304  0.1087  0.0588  306 ILE B CG1 
7562  C CG2 . ILE B 306 ? 0.4698 0.5384 0.6513 0.0332  0.1082  0.0634  306 ILE B CG2 
7563  C CD1 . ILE B 306 ? 0.5685 0.6505 0.7581 0.0276  0.1064  0.0528  306 ILE B CD1 
7564  N N   . LYS B 307 ? 0.4008 0.4682 0.5787 0.0422  0.1048  0.0473  307 LYS B N   
7565  C CA  . LYS B 307 ? 0.4853 0.5544 0.6618 0.0452  0.1034  0.0454  307 LYS B CA  
7566  C C   . LYS B 307 ? 0.5754 0.6382 0.7496 0.0447  0.1040  0.0520  307 LYS B C   
7567  O O   . LYS B 307 ? 0.5285 0.5924 0.7034 0.0403  0.1056  0.0580  307 LYS B O   
7568  C CB  . LYS B 307 ? 0.4530 0.5405 0.6331 0.0420  0.1027  0.0406  307 LYS B CB  
7569  C CG  . LYS B 307 ? 0.4606 0.5543 0.6422 0.0442  0.1019  0.0325  307 LYS B CG  
7570  C CD  . LYS B 307 ? 0.5782 0.6900 0.7631 0.0429  0.1016  0.0268  307 LYS B CD  
7571  C CE  . LYS B 307 ? 0.6360 0.7614 0.8219 0.0355  0.1037  0.0297  307 LYS B CE  
7572  N NZ  . LYS B 307 ? 1.0437 1.1870 1.2322 0.0346  0.1045  0.0229  307 LYS B NZ  
7573  N N   . ILE B 308 ? 0.5141 0.5698 0.6850 0.0498  0.1024  0.0505  308 ILE B N   
7574  C CA  . ILE B 308 ? 0.3049 0.3533 0.4727 0.0501  0.1025  0.0550  308 ILE B CA  
7575  C C   . ILE B 308 ? 0.4724 0.5320 0.6434 0.0469  0.1009  0.0522  308 ILE B C   
7576  O O   . ILE B 308 ? 0.4910 0.5562 0.6633 0.0502  0.0982  0.0458  308 ILE B O   
7577  C CB  . ILE B 308 ? 0.4240 0.4574 0.5849 0.0581  0.1016  0.0549  308 ILE B CB  
7578  C CG1 . ILE B 308 ? 0.5333 0.5543 0.6914 0.0597  0.1047  0.0590  308 ILE B CG1 
7579  C CG2 . ILE B 308 ? 0.4574 0.4846 0.6143 0.0591  0.1010  0.0575  308 ILE B CG2 
7580  C CD1 . ILE B 308 ? 0.5009 0.5064 0.6509 0.0679  0.1046  0.0588  308 ILE B CD1 
7581  N N   . ALA B 309 ? 0.5884 0.6510 0.7609 0.0407  0.1027  0.0571  309 ALA B N   
7582  C CA  . ALA B 309 ? 0.5028 0.5746 0.6788 0.0360  0.1023  0.0551  309 ALA B CA  
7583  C C   . ALA B 309 ? 0.4899 0.5548 0.6638 0.0389  0.0998  0.0527  309 ALA B C   
7584  O O   . ALA B 309 ? 0.5368 0.6115 0.7152 0.0374  0.0979  0.0469  309 ALA B O   
7585  C CB  . ALA B 309 ? 0.4673 0.5409 0.6438 0.0289  0.1054  0.0619  309 ALA B CB  
7586  N N   . GLY B 310 ? 0.4634 0.5128 0.6309 0.0430  0.1000  0.0567  310 GLY B N   
7587  C CA  . GLY B 310 ? 0.5153 0.5576 0.6792 0.0464  0.0973  0.0540  310 GLY B CA  
7588  C C   . GLY B 310 ? 0.5046 0.5297 0.6604 0.0506  0.0985  0.0592  310 GLY B C   
7589  O O   . GLY B 310 ? 0.5143 0.5333 0.6683 0.0508  0.1018  0.0654  310 GLY B O   
7590  N N   . ASN B 311 ? 0.4345 0.4531 0.5856 0.0541  0.0958  0.0561  311 ASN B N   
7591  C CA  . ASN B 311 ? 0.5008 0.5032 0.6429 0.0591  0.0970  0.0600  311 ASN B CA  
7592  C C   . ASN B 311 ? 0.5694 0.5665 0.7112 0.0545  0.0978  0.0617  311 ASN B C   
7593  O O   . ASN B 311 ? 0.5485 0.5535 0.6973 0.0468  0.0980  0.0608  311 ASN B O   
7594  C CB  . ASN B 311 ? 0.5040 0.5002 0.6377 0.0684  0.0935  0.0557  311 ASN B CB  
7595  C CG  . ASN B 311 ? 0.6181 0.6233 0.7541 0.0690  0.0876  0.0469  311 ASN B CG  
7596  O OD1 . ASN B 311 ? 0.7207 0.7374 0.8657 0.0615  0.0866  0.0435  311 ASN B OD1 
7597  N ND2 . ASN B 311 ? 0.5268 0.5276 0.6547 0.0781  0.0837  0.0430  311 ASN B ND2 
7598  N N   . PHE B 312 ? 0.5972 0.5799 0.7306 0.0592  0.0990  0.0643  312 PHE B N   
7599  C CA  . PHE B 312 ? 0.5699 0.5441 0.7015 0.0564  0.1001  0.0659  312 PHE B CA  
7600  C C   . PHE B 312 ? 0.5588 0.5391 0.6967 0.0485  0.0978  0.0610  312 PHE B C   
7601  O O   . PHE B 312 ? 0.6454 0.6266 0.7881 0.0416  0.1007  0.0652  312 PHE B O   
7602  C CB  . PHE B 312 ? 0.6198 0.5797 0.7401 0.0643  0.0998  0.0652  312 PHE B CB  
7603  C CG  . PHE B 312 ? 0.6068 0.5557 0.7244 0.0624  0.1015  0.0669  312 PHE B CG  
7604  C CD1 . PHE B 312 ? 0.7052 0.6498 0.8249 0.0604  0.1063  0.0747  312 PHE B CD1 
7605  C CD2 . PHE B 312 ? 0.6141 0.5572 0.7272 0.0631  0.0979  0.0601  312 PHE B CD2 
7606  C CE1 . PHE B 312 ? 0.5655 0.4986 0.6823 0.0597  0.1079  0.0762  312 PHE B CE1 
7607  C CE2 . PHE B 312 ? 0.5919 0.5230 0.7022 0.0615  0.0996  0.0611  312 PHE B CE2 
7608  C CZ  . PHE B 312 ? 0.6485 0.5740 0.7604 0.0601  0.1048  0.0694  312 PHE B CZ  
7609  N N   . MET B 313 ? 0.5965 0.5809 0.7345 0.0494  0.0928  0.0522  313 MET B N   
7610  C CA  . MET B 313 ? 0.4706 0.4608 0.6160 0.0407  0.0910  0.0470  313 MET B CA  
7611  C C   . MET B 313 ? 0.5351 0.5426 0.6920 0.0326  0.0920  0.0461  313 MET B C   
7612  O O   . MET B 313 ? 0.6081 0.6212 0.7722 0.0242  0.0917  0.0424  313 MET B O   
7613  C CB  . MET B 313 ? 0.5569 0.5475 0.6998 0.0437  0.0849  0.0370  313 MET B CB  
7614  C CG  . MET B 313 ? 0.4623 0.4349 0.5937 0.0491  0.0847  0.0372  313 MET B CG  
7615  S SD  . MET B 313 ? 0.5952 0.5663 0.7254 0.0479  0.0781  0.0251  313 MET B SD  
7616  C CE  . MET B 313 ? 0.8536 0.8435 0.9874 0.0526  0.0709  0.0160  313 MET B CE  
7617  N N   . GLN B 314 ? 0.5597 0.5751 0.7186 0.0344  0.0937  0.0495  314 GLN B N   
7618  C CA  . GLN B 314 ? 0.4535 0.4853 0.6220 0.0274  0.0951  0.0488  314 GLN B CA  
7619  C C   . GLN B 314 ? 0.5945 0.6238 0.7637 0.0214  0.1006  0.0579  314 GLN B C   
7620  O O   . GLN B 314 ? 0.5837 0.6248 0.7595 0.0142  0.1027  0.0582  314 GLN B O   
7621  C CB  . GLN B 314 ? 0.4946 0.5367 0.6642 0.0331  0.0935  0.0462  314 GLN B CB  
7622  C CG  . GLN B 314 ? 0.4943 0.5451 0.6659 0.0381  0.0878  0.0366  314 GLN B CG  
7623  C CD  . GLN B 314 ? 0.6405 0.7019 0.8146 0.0425  0.0870  0.0343  314 GLN B CD  
7624  O OE1 . GLN B 314 ? 0.5839 0.6375 0.7521 0.0481  0.0884  0.0385  314 GLN B OE1 
7625  N NE2 . GLN B 314 ? 0.6846 0.7641 0.8680 0.0400  0.0851  0.0272  314 GLN B NE2 
7626  N N   . GLN B 315 ? 0.5889 0.6038 0.7512 0.0248  0.1030  0.0653  315 GLN B N   
7627  C CA  . GLN B 315 ? 0.4691 0.4816 0.6312 0.0212  0.1073  0.0742  315 GLN B CA  
7628  C C   . GLN B 315 ? 0.6090 0.6234 0.7749 0.0115  0.1099  0.0762  315 GLN B C   
7629  O O   . GLN B 315 ? 0.7498 0.7714 0.9175 0.0075  0.1128  0.0813  315 GLN B O   
7630  C CB  . GLN B 315 ? 0.4172 0.4139 0.5722 0.0269  0.1091  0.0807  315 GLN B CB  
7631  C CG  . GLN B 315 ? 0.5723 0.5538 0.7227 0.0276  0.1087  0.0797  315 GLN B CG  
7632  C CD  . GLN B 315 ? 0.5564 0.5247 0.7002 0.0347  0.1108  0.0854  315 GLN B CD  
7633  O OE1 . GLN B 315 ? 0.6500 0.6113 0.7925 0.0339  0.1137  0.0922  315 GLN B OE1 
7634  N NE2 . GLN B 315 ? 0.5514 0.5162 0.6904 0.0423  0.1096  0.0830  315 GLN B NE2 
7635  N N   . GLU B 316 ? 0.5893 0.5969 0.7559 0.0077  0.1091  0.0724  316 GLU B N   
7636  C CA  . GLU B 316 ? 0.5319 0.5394 0.7022 -0.0025 0.1124  0.0744  316 GLU B CA  
7637  C C   . GLU B 316 ? 0.6081 0.6357 0.7872 -0.0090 0.1129  0.0699  316 GLU B C   
7638  O O   . GLU B 316 ? 0.6678 0.7003 0.8489 -0.0162 0.1173  0.0748  316 GLU B O   
7639  C CB  . GLU B 316 ? 0.5202 0.5155 0.6903 -0.0058 0.1112  0.0698  316 GLU B CB  
7640  C CG  . GLU B 316 ? 0.6194 0.5932 0.7806 -0.0005 0.1120  0.0748  316 GLU B CG  
7641  C CD  . GLU B 316 ? 0.7083 0.6709 0.8682 -0.0013 0.1093  0.0672  316 GLU B CD  
7642  O OE1 . GLU B 316 ? 0.6563 0.6246 0.8164 0.0032  0.1044  0.0587  316 GLU B OE1 
7643  O OE2 . GLU B 316 ? 0.5878 0.5355 0.7458 -0.0062 0.1118  0.0696  316 GLU B OE2 
7644  N N   . LEU B 317 ? 0.5503 0.5900 0.7341 -0.0059 0.1086  0.0606  317 LEU B N   
7645  C CA  . LEU B 317 ? 0.4550 0.5157 0.6481 -0.0108 0.1088  0.0549  317 LEU B CA  
7646  C C   . LEU B 317 ? 0.5187 0.5900 0.7114 -0.0097 0.1115  0.0595  317 LEU B C   
7647  O O   . LEU B 317 ? 0.6068 0.6941 0.8059 -0.0156 0.1139  0.0575  317 LEU B O   
7648  C CB  . LEU B 317 ? 0.4422 0.5125 0.6399 -0.0057 0.1028  0.0439  317 LEU B CB  
7649  C CG  . LEU B 317 ? 0.3731 0.4354 0.5714 -0.0070 0.0993  0.0376  317 LEU B CG  
7650  C CD1 . LEU B 317 ? 0.5060 0.5751 0.7048 0.0016  0.0924  0.0283  317 LEU B CD1 
7651  C CD2 . LEU B 317 ? 0.5043 0.5737 0.7126 -0.0196 0.1018  0.0343  317 LEU B CD2 
7652  N N   . ALA B 318 ? 0.5042 0.5675 0.6896 -0.0026 0.1113  0.0653  318 ALA B N   
7653  C CA  . ALA B 318 ? 0.4522 0.5249 0.6368 -0.0019 0.1133  0.0690  318 ALA B CA  
7654  C C   . ALA B 318 ? 0.4799 0.5531 0.6632 -0.0098 0.1185  0.0768  318 ALA B C   
7655  O O   . ALA B 318 ? 0.5917 0.6792 0.7773 -0.0135 0.1209  0.0769  318 ALA B O   
7656  C CB  . ALA B 318 ? 0.4729 0.5361 0.6511 0.0062  0.1120  0.0733  318 ALA B CB  
7657  N N   . VAL B 319 ? 0.4427 0.4998 0.6216 -0.0120 0.1203  0.0833  319 VAL B N   
7658  C CA  . VAL B 319 ? 0.5006 0.5547 0.6764 -0.0188 0.1254  0.0918  319 VAL B CA  
7659  C C   . VAL B 319 ? 0.5511 0.6159 0.7339 -0.0290 0.1287  0.0879  319 VAL B C   
7660  O O   . VAL B 319 ? 0.5790 0.6525 0.7611 -0.0343 0.1332  0.0923  319 VAL B O   
7661  C CB  . VAL B 319 ? 0.5231 0.5552 0.6924 -0.0177 0.1265  0.0991  319 VAL B CB  
7662  C CG1 . VAL B 319 ? 0.4892 0.5157 0.6542 -0.0245 0.1319  0.1084  319 VAL B CG1 
7663  C CG2 . VAL B 319 ? 0.4577 0.4821 0.6214 -0.0078 0.1241  0.1031  319 VAL B CG2 
7664  N N   . VAL B 320 ? 0.4682 0.5336 0.6581 -0.0315 0.1264  0.0792  320 VAL B N   
7665  C CA  . VAL B 320 ? 0.5334 0.6106 0.7327 -0.0418 0.1292  0.0738  320 VAL B CA  
7666  C C   . VAL B 320 ? 0.5473 0.6489 0.7526 -0.0436 0.1310  0.0700  320 VAL B C   
7667  O O   . VAL B 320 ? 0.5346 0.6467 0.7460 -0.0532 0.1359  0.0692  320 VAL B O   
7668  C CB  . VAL B 320 ? 0.4758 0.5518 0.6823 -0.0426 0.1247  0.0634  320 VAL B CB  
7669  C CG1 . VAL B 320 ? 0.4215 0.5145 0.6407 -0.0533 0.1271  0.0562  320 VAL B CG1 
7670  C CG2 . VAL B 320 ? 0.4810 0.5329 0.6815 -0.0428 0.1241  0.0667  320 VAL B CG2 
7671  N N   . THR B 321 ? 0.5126 0.6226 0.7161 -0.0347 0.1276  0.0676  321 THR B N   
7672  C CA  . THR B 321 ? 0.4682 0.6003 0.6764 -0.0355 0.1294  0.0635  321 THR B CA  
7673  C C   . THR B 321 ? 0.4856 0.6211 0.6891 -0.0425 0.1365  0.0723  321 THR B C   
7674  O O   . THR B 321 ? 0.6367 0.7901 0.8452 -0.0477 0.1405  0.0695  321 THR B O   
7675  C CB  . THR B 321 ? 0.4472 0.5834 0.6521 -0.0250 0.1252  0.0609  321 THR B CB  
7676  O OG1 . THR B 321 ? 0.5213 0.6441 0.7161 -0.0212 0.1254  0.0700  321 THR B OG1 
7677  C CG2 . THR B 321 ? 0.4141 0.5486 0.6223 -0.0171 0.1187  0.0524  321 THR B CG2 
7678  N N   . GLY B 322 ? 0.5684 0.6869 0.7616 -0.0418 0.1380  0.0830  322 GLY B N   
7679  C CA  . GLY B 322 ? 0.4949 0.6133 0.6805 -0.0465 0.1440  0.0930  322 GLY B CA  
7680  C C   . GLY B 322 ? 0.5712 0.6998 0.7509 -0.0404 0.1429  0.0945  322 GLY B C   
7681  O O   . GLY B 322 ? 0.6805 0.8133 0.8531 -0.0432 0.1474  0.1016  322 GLY B O   
7682  N N   . ALA B 323 ? 0.4750 0.6072 0.6568 -0.0319 0.1370  0.0879  323 ALA B N   
7683  C CA  . ALA B 323 ? 0.4705 0.6120 0.6480 -0.0262 0.1354  0.0872  323 ALA B CA  
7684  C C   . ALA B 323 ? 0.5027 0.6315 0.6741 -0.0188 0.1312  0.0919  323 ALA B C   
7685  O O   . ALA B 323 ? 0.5496 0.6854 0.7179 -0.0146 0.1294  0.0911  323 ALA B O   
7686  C CB  . ALA B 323 ? 0.3487 0.5052 0.5340 -0.0228 0.1327  0.0754  323 ALA B CB  
7687  N N   . VAL B 324 ? 0.4968 0.6077 0.6666 -0.0173 0.1299  0.0963  324 VAL B N   
7688  C CA  . VAL B 324 ? 0.4576 0.5581 0.6229 -0.0103 0.1266  0.1006  324 VAL B CA  
7689  C C   . VAL B 324 ? 0.5476 0.6450 0.7045 -0.0113 0.1290  0.1113  324 VAL B C   
7690  O O   . VAL B 324 ? 0.6036 0.6898 0.7569 -0.0148 0.1320  0.1182  324 VAL B O   
7691  C CB  . VAL B 324 ? 0.4108 0.4944 0.5774 -0.0069 0.1243  0.1003  324 VAL B CB  
7692  C CG1 . VAL B 324 ? 0.4176 0.4914 0.5800 -0.0003 0.1223  0.1059  324 VAL B CG1 
7693  C CG2 . VAL B 324 ? 0.3253 0.4125 0.4984 -0.0044 0.1212  0.0900  324 VAL B CG2 
7694  N N   . ASP B 325 ? 0.4051 0.5123 0.5584 -0.0082 0.1276  0.1124  325 ASP B N   
7695  C CA  . ASP B 325 ? 0.3498 0.4561 0.4942 -0.0077 0.1289  0.1224  325 ASP B CA  
7696  C C   . ASP B 325 ? 0.4907 0.5827 0.6327 -0.0019 0.1264  0.1288  325 ASP B C   
7697  O O   . ASP B 325 ? 0.4853 0.5686 0.6204 -0.0016 0.1282  0.1385  325 ASP B O   
7698  C CB  . ASP B 325 ? 0.4241 0.5473 0.5654 -0.0060 0.1274  0.1200  325 ASP B CB  
7699  C CG  . ASP B 325 ? 0.6360 0.7742 0.7789 -0.0110 0.1305  0.1137  325 ASP B CG  
7700  O OD1 . ASP B 325 ? 0.5564 0.6941 0.6976 -0.0173 0.1357  0.1170  325 ASP B OD1 
7701  O OD2 . ASP B 325 ? 0.7120 0.8622 0.8583 -0.0088 0.1280  0.1051  325 ASP B OD2 
7702  N N   . GLY B 326 ? 0.4986 0.5883 0.6463 0.0031  0.1227  0.1238  326 GLY B N   
7703  C CA  . GLY B 326 ? 0.3885 0.4669 0.5357 0.0089  0.1207  0.1287  326 GLY B CA  
7704  C C   . GLY B 326 ? 0.5520 0.6222 0.7053 0.0118  0.1192  0.1227  326 GLY B C   
7705  O O   . GLY B 326 ? 0.5396 0.6169 0.6978 0.0124  0.1175  0.1148  326 GLY B O   
7706  N N   . LEU B 327 ? 0.4695 0.5239 0.6216 0.0139  0.1201  0.1266  327 LEU B N   
7707  C CA  . LEU B 327 ? 0.5221 0.5673 0.6777 0.0174  0.1190  0.1219  327 LEU B CA  
7708  C C   . LEU B 327 ? 0.5230 0.5619 0.6782 0.0240  0.1183  0.1272  327 LEU B C   
7709  O O   . LEU B 327 ? 0.6087 0.6360 0.7600 0.0260  0.1196  0.1336  327 LEU B O   
7710  C CB  . LEU B 327 ? 0.4790 0.5119 0.6336 0.0142  0.1206  0.1206  327 LEU B CB  
7711  C CG  . LEU B 327 ? 0.4384 0.4603 0.5943 0.0182  0.1194  0.1158  327 LEU B CG  
7712  C CD1 . LEU B 327 ? 0.5039 0.5343 0.6640 0.0200  0.1172  0.1076  327 LEU B CD1 
7713  C CD2 . LEU B 327 ? 0.4206 0.4322 0.5755 0.0142  0.1204  0.1138  327 LEU B CD2 
7714  N N   . ILE B 328 ? 0.4392 0.4860 0.5987 0.0272  0.1165  0.1244  328 ILE B N   
7715  C CA  . ILE B 328 ? 0.4374 0.4819 0.5988 0.0330  0.1161  0.1285  328 ILE B CA  
7716  C C   . ILE B 328 ? 0.5416 0.5744 0.7044 0.0367  0.1172  0.1259  328 ILE B C   
7717  O O   . ILE B 328 ? 0.6629 0.6963 0.8278 0.0361  0.1169  0.1194  328 ILE B O   
7718  C CB  . ILE B 328 ? 0.3879 0.4480 0.5543 0.0335  0.1138  0.1266  328 ILE B CB  
7719  C CG1 . ILE B 328 ? 0.4008 0.4735 0.5639 0.0301  0.1124  0.1281  328 ILE B CG1 
7720  C CG2 . ILE B 328 ? 0.4956 0.5560 0.6657 0.0391  0.1135  0.1309  328 ILE B CG2 
7721  C CD1 . ILE B 328 ? 0.4080 0.4961 0.5754 0.0288  0.1099  0.1226  328 ILE B CD1 
7722  N N   . VAL B 329 ? 0.5675 0.5892 0.7282 0.0413  0.1187  0.1309  329 VAL B N   
7723  C CA  . VAL B 329 ? 0.5994 0.6095 0.7598 0.0455  0.1203  0.1288  329 VAL B CA  
7724  C C   . VAL B 329 ? 0.6159 0.6259 0.7795 0.0518  0.1216  0.1330  329 VAL B C   
7725  O O   . VAL B 329 ? 0.5379 0.5545 0.7032 0.0536  0.1208  0.1383  329 VAL B O   
7726  C CB  . VAL B 329 ? 0.4992 0.4938 0.6534 0.0449  0.1213  0.1287  329 VAL B CB  
7727  C CG1 . VAL B 329 ? 0.4747 0.4723 0.6279 0.0380  0.1202  0.1242  329 VAL B CG1 
7728  C CG2 . VAL B 329 ? 0.4019 0.3878 0.5525 0.0475  0.1225  0.1362  329 VAL B CG2 
7729  N N   . ASP B 330 ? 0.5208 0.5234 0.6846 0.0556  0.1237  0.1306  330 ASP B N   
7730  C CA  . ASP B 330 ? 0.5851 0.5878 0.7527 0.0618  0.1262  0.1340  330 ASP B CA  
7731  C C   . ASP B 330 ? 0.7045 0.6907 0.8659 0.0669  0.1290  0.1339  330 ASP B C   
7732  O O   . ASP B 330 ? 0.6463 0.6237 0.8037 0.0696  0.1293  0.1376  330 ASP B O   
7733  C CB  . ASP B 330 ? 0.4787 0.4917 0.6538 0.0610  0.1272  0.1311  330 ASP B CB  
7734  C CG  . ASP B 330 ? 0.7114 0.7202 0.8839 0.0584  0.1275  0.1250  330 ASP B CG  
7735  O OD1 . ASP B 330 ? 0.8217 0.8180 0.9867 0.0599  0.1280  0.1230  330 ASP B OD1 
7736  O OD2 . ASP B 330 ? 0.7869 0.8046 0.9645 0.0552  0.1269  0.1220  330 ASP B OD2 
7737  N N   . VAL B 331 ? 0.5979 0.5790 0.7576 0.0686  0.1312  0.1300  331 VAL B N   
7738  C CA  . VAL B 331 ? 0.5145 0.4807 0.6671 0.0743  0.1339  0.1294  331 VAL B CA  
7739  C C   . VAL B 331 ? 0.6944 0.6522 0.8398 0.0733  0.1332  0.1233  331 VAL B C   
7740  O O   . VAL B 331 ? 0.7421 0.7060 0.8891 0.0694  0.1314  0.1199  331 VAL B O   
7741  C CB  . VAL B 331 ? 0.4416 0.4097 0.5981 0.0804  0.1386  0.1321  331 VAL B CB  
7742  C CG1 . VAL B 331 ? 0.5804 0.5571 0.7441 0.0831  0.1387  0.1378  331 VAL B CG1 
7743  C CG2 . VAL B 331 ? 0.6007 0.5764 0.7619 0.0785  0.1406  0.1300  331 VAL B CG2 
7744  N N   . GLN B 332 ? 0.7275 0.6713 0.8646 0.0777  0.1343  0.1216  332 GLN B N   
7745  C CA  . GLN B 332 ? 0.6238 0.5597 0.7527 0.0787  0.1333  0.1156  332 GLN B CA  
7746  C C   . GLN B 332 ? 0.6005 0.5376 0.7281 0.0729  0.1283  0.1104  332 GLN B C   
7747  O O   . GLN B 332 ? 0.5223 0.4707 0.6557 0.0680  0.1264  0.1098  332 GLN B O   
7748  C CB  . GLN B 332 ? 0.6431 0.5826 0.7724 0.0810  0.1361  0.1155  332 GLN B CB  
7749  C CG  . GLN B 332 ? 0.4467 0.3792 0.5718 0.0883  0.1417  0.1179  332 GLN B CG  
7750  C CD  . GLN B 332 ? 0.7800 0.7193 0.9102 0.0886  0.1462  0.1203  332 GLN B CD  
7751  O OE1 . GLN B 332 ? 0.9158 0.8536 1.0424 0.0879  0.1463  0.1181  332 GLN B OE1 
7752  N NE2 . GLN B 332 ? 0.5896 0.5363 0.7284 0.0897  0.1500  0.1249  332 GLN B NE2 
7753  N N   . CYS B 333 ? 0.6634 0.5901 0.7843 0.0734  0.1263  0.1062  333 CYS B N   
7754  C CA  . CYS B 333 ? 0.5924 0.5215 0.7130 0.0680  0.1217  0.0999  333 CYS B CA  
7755  C C   . CYS B 333 ? 0.6557 0.5945 0.7841 0.0600  0.1202  0.1016  333 CYS B C   
7756  O O   . CYS B 333 ? 0.6094 0.5577 0.7410 0.0557  0.1174  0.0975  333 CYS B O   
7757  C CB  . CYS B 333 ? 0.4683 0.4018 0.5866 0.0702  0.1201  0.0956  333 CYS B CB  
7758  S SG  . CYS B 333 ? 0.7045 0.6280 0.8135 0.0799  0.1243  0.0972  333 CYS B SG  
7759  N N   . ILE B 334 ? 0.6289 0.5653 0.7593 0.0586  0.1220  0.1075  334 ILE B N   
7760  C CA  . ILE B 334 ? 0.5240 0.4677 0.6594 0.0511  0.1211  0.1098  334 ILE B CA  
7761  C C   . ILE B 334 ? 0.5989 0.5301 0.7309 0.0478  0.1209  0.1087  334 ILE B C   
7762  O O   . ILE B 334 ? 0.7336 0.6552 0.8634 0.0499  0.1231  0.1144  334 ILE B O   
7763  C CB  . ILE B 334 ? 0.5352 0.4860 0.6747 0.0520  0.1230  0.1177  334 ILE B CB  
7764  C CG1 . ILE B 334 ? 0.5061 0.4688 0.6500 0.0541  0.1232  0.1175  334 ILE B CG1 
7765  C CG2 . ILE B 334 ? 0.5949 0.5515 0.7366 0.0451  0.1224  0.1208  334 ILE B CG2 
7766  C CD1 . ILE B 334 ? 0.4548 0.4200 0.6016 0.0591  0.1256  0.1237  334 ILE B CD1 
7767  N N   . MET B 335 ? 0.5344 0.4653 0.6662 0.0432  0.1183  0.1013  335 MET B N   
7768  C CA  . MET B 335 ? 0.5307 0.4487 0.6599 0.0394  0.1181  0.0989  335 MET B CA  
7769  C C   . MET B 335 ? 0.6473 0.5587 0.7768 0.0360  0.1211  0.1070  335 MET B C   
7770  O O   . MET B 335 ? 0.5867 0.5088 0.7204 0.0310  0.1219  0.1111  335 MET B O   
7771  C CB  . MET B 335 ? 0.4093 0.3347 0.5426 0.0317  0.1150  0.0907  335 MET B CB  
7772  C CG  . MET B 335 ? 0.4352 0.3632 0.5661 0.0361  0.1112  0.0820  335 MET B CG  
7773  S SD  . MET B 335 ? 0.5895 0.5279 0.7269 0.0277  0.1069  0.0716  335 MET B SD  
7774  C CE  . MET B 335 ? 0.6517 0.6004 0.7872 0.0353  0.1027  0.0655  335 MET B CE  
7775  N N   . PRO B 336 ? 0.6228 0.5163 0.7470 0.0394  0.1230  0.1096  336 PRO B N   
7776  C CA  . PRO B 336 ? 0.5580 0.4435 0.6811 0.0370  0.1258  0.1181  336 PRO B CA  
7777  C C   . PRO B 336 ? 0.7510 0.6376 0.8771 0.0255  0.1263  0.1175  336 PRO B C   
7778  O O   . PRO B 336 ? 0.8198 0.7049 0.9453 0.0224  0.1288  0.1256  336 PRO B O   
7779  C CB  . PRO B 336 ? 0.5646 0.4285 0.6810 0.0429  0.1273  0.1185  336 PRO B CB  
7780  C CG  . PRO B 336 ? 0.6277 0.4916 0.7414 0.0502  0.1259  0.1122  336 PRO B CG  
7781  C CD  . PRO B 336 ? 0.5435 0.4223 0.6611 0.0459  0.1227  0.1050  336 PRO B CD  
7782  N N   . ALA B 337 ? 0.6288 0.5187 0.7581 0.0192  0.1240  0.1079  337 ALA B N   
7783  C CA  . ALA B 337 ? 0.6153 0.5088 0.7494 0.0074  0.1249  0.1060  337 ALA B CA  
7784  C C   . ALA B 337 ? 0.6163 0.5267 0.7544 0.0032  0.1266  0.1119  337 ALA B C   
7785  O O   . ALA B 337 ? 0.7666 0.6771 0.9065 -0.0058 0.1295  0.1147  337 ALA B O   
7786  C CB  . ALA B 337 ? 0.6771 0.5783 0.8161 0.0032  0.1211  0.0938  337 ALA B CB  
7787  N N   . LEU B 338 ? 0.5278 0.4523 0.6669 0.0093  0.1252  0.1136  338 LEU B N   
7788  C CA  . LEU B 338 ? 0.5584 0.4997 0.7005 0.0063  0.1263  0.1180  338 LEU B CA  
7789  C C   . LEU B 338 ? 0.6850 0.6195 0.8226 0.0045  0.1300  0.1290  338 LEU B C   
7790  O O   . LEU B 338 ? 0.6799 0.6252 0.8188 -0.0016 0.1319  0.1319  338 LEU B O   
7791  C CB  . LEU B 338 ? 0.5419 0.4958 0.6852 0.0139  0.1241  0.1179  338 LEU B CB  
7792  C CG  . LEU B 338 ? 0.4873 0.4507 0.6344 0.0157  0.1207  0.1082  338 LEU B CG  
7793  C CD1 . LEU B 338 ? 0.4737 0.4410 0.6200 0.0242  0.1196  0.1093  338 LEU B CD1 
7794  C CD2 . LEU B 338 ? 0.4479 0.4285 0.6011 0.0089  0.1200  0.1034  338 LEU B CD2 
7795  N N   . ALA B 339 ? 0.6882 0.6048 0.8196 0.0103  0.1312  0.1351  339 ALA B N   
7796  C CA  . ALA B 339 ? 0.6476 0.5560 0.7732 0.0102  0.1344  0.1463  339 ALA B CA  
7797  C C   . ALA B 339 ? 0.7133 0.6134 0.8380 -0.0011 0.1382  0.1477  339 ALA B C   
7798  O O   . ALA B 339 ? 0.8826 0.7883 1.0049 -0.0053 0.1410  0.1548  339 ALA B O   
7799  C CB  . ALA B 339 ? 0.6017 0.4921 0.7215 0.0197  0.1347  0.1515  339 ALA B CB  
7800  N N   . LYS B 340 ? 0.6843 0.5719 0.8109 -0.0063 0.1385  0.1406  340 LYS B N   
7801  C CA  . LYS B 340 ? 0.5775 0.4570 0.7051 -0.0185 0.1425  0.1407  340 LYS B CA  
7802  C C   . LYS B 340 ? 0.6101 0.5125 0.7460 -0.0279 0.1429  0.1354  340 LYS B C   
7803  O O   . LYS B 340 ? 0.7149 0.6199 0.8505 -0.0364 0.1476  0.1406  340 LYS B O   
7804  C CB  . LYS B 340 ? 0.8413 0.7023 0.9699 -0.0214 0.1418  0.1328  340 LYS B CB  
7805  C CG  . LYS B 340 ? 0.8816 0.7339 1.0132 -0.0356 0.1461  0.1314  340 LYS B CG  
7806  C CD  . LYS B 340 ? 0.8339 0.6609 0.9636 -0.0377 0.1461  0.1261  340 LYS B CD  
7807  C CE  . LYS B 340 ? 1.0743 0.9086 1.2140 -0.0469 0.1434  0.1117  340 LYS B CE  
7808  N NZ  . LYS B 340 ? 1.3212 1.1304 1.4596 -0.0528 0.1447  0.1072  340 LYS B NZ  
7809  N N   . LEU B 341 ? 0.6626 0.5816 0.8056 -0.0259 0.1384  0.1252  341 LEU B N   
7810  C CA  . LEU B 341 ? 0.6309 0.5726 0.7825 -0.0329 0.1382  0.1189  341 LEU B CA  
7811  C C   . LEU B 341 ? 0.6288 0.5849 0.7782 -0.0334 0.1409  0.1266  341 LEU B C   
7812  O O   . LEU B 341 ? 0.7115 0.6789 0.8650 -0.0425 0.1444  0.1261  341 LEU B O   
7813  C CB  . LEU B 341 ? 0.5416 0.4962 0.6984 -0.0270 0.1322  0.1082  341 LEU B CB  
7814  C CG  . LEU B 341 ? 0.4107 0.3892 0.5769 -0.0320 0.1310  0.1002  341 LEU B CG  
7815  C CD1 . LEU B 341 ? 0.5479 0.5279 0.7221 -0.0426 0.1318  0.0924  341 LEU B CD1 
7816  C CD2 . LEU B 341 ? 0.5279 0.5163 0.6959 -0.0232 0.1253  0.0929  341 LEU B CD2 
7817  N N   . SER B 342 ? 0.5819 0.5384 0.7252 -0.0238 0.1394  0.1332  342 SER B N   
7818  C CA  . SER B 342 ? 0.5671 0.5377 0.7074 -0.0232 0.1409  0.1399  342 SER B CA  
7819  C C   . SER B 342 ? 0.6546 0.6173 0.7882 -0.0297 0.1469  0.1501  342 SER B C   
7820  O O   . SER B 342 ? 0.7189 0.6952 0.8501 -0.0320 0.1492  0.1542  342 SER B O   
7821  C CB  . SER B 342 ? 0.6026 0.5743 0.7386 -0.0118 0.1376  0.1443  342 SER B CB  
7822  O OG  . SER B 342 ? 0.7187 0.6985 0.8603 -0.0065 0.1331  0.1357  342 SER B OG  
7823  N N   . LYS B 343 ? 0.6940 0.6337 0.8235 -0.0324 0.1498  0.1544  343 LYS B N   
7824  C CA  . LYS B 343 ? 0.5875 0.5158 0.7095 -0.0387 0.1562  0.1650  343 LYS B CA  
7825  C C   . LYS B 343 ? 0.6233 0.5629 0.7516 -0.0524 0.1612  0.1612  343 LYS B C   
7826  O O   . LYS B 343 ? 0.8158 0.7544 0.9379 -0.0580 0.1672  0.1700  343 LYS B O   
7827  C CB  . LYS B 343 ? 0.6397 0.5380 0.7559 -0.0378 0.1580  0.1697  343 LYS B CB  
7828  C CG  . LYS B 343 ? 0.7412 0.6295 0.8510 -0.0237 0.1540  0.1743  343 LYS B CG  
7829  C CD  . LYS B 343 ? 1.0587 0.9166 1.1611 -0.0215 0.1563  0.1802  343 LYS B CD  
7830  C CE  . LYS B 343 ? 1.0927 0.9436 1.1888 -0.0066 0.1530  0.1862  343 LYS B CE  
7831  N NZ  . LYS B 343 ? 1.2808 1.1332 1.3671 -0.0016 0.1544  0.1995  343 LYS B NZ  
7832  N N   . SER B 344 ? 0.5671 0.5184 0.7077 -0.0574 0.1590  0.1483  344 SER B N   
7833  C CA  . SER B 344 ? 0.6792 0.6449 0.8285 -0.0701 0.1633  0.1430  344 SER B CA  
7834  C C   . SER B 344 ? 0.6562 0.6498 0.8081 -0.0691 0.1632  0.1411  344 SER B C   
7835  O O   . SER B 344 ? 0.6899 0.6987 0.8489 -0.0787 0.1675  0.1373  344 SER B O   
7836  C CB  . SER B 344 ? 0.5338 0.5020 0.6957 -0.0748 0.1600  0.1293  344 SER B CB  
7837  O OG  . SER B 344 ? 0.7754 0.7190 0.9343 -0.0728 0.1582  0.1287  344 SER B OG  
7838  N N   . TYR B 345 ? 0.5666 0.5676 0.7136 -0.0579 0.1585  0.1428  345 TYR B N   
7839  C CA  . TYR B 345 ? 0.6188 0.6444 0.7673 -0.0558 0.1577  0.1402  345 TYR B CA  
7840  C C   . TYR B 345 ? 0.6727 0.6974 0.8090 -0.0481 0.1573  0.1506  345 TYR B C   
7841  O O   . TYR B 345 ? 0.6931 0.6990 0.8210 -0.0434 0.1571  0.1594  345 TYR B O   
7842  C CB  . TYR B 345 ? 0.5086 0.5466 0.6661 -0.0498 0.1507  0.1280  345 TYR B CB  
7843  C CG  . TYR B 345 ? 0.5541 0.5949 0.7233 -0.0559 0.1499  0.1171  345 TYR B CG  
7844  C CD1 . TYR B 345 ? 0.4679 0.5288 0.6466 -0.0634 0.1523  0.1099  345 TYR B CD1 
7845  C CD2 . TYR B 345 ? 0.4997 0.5240 0.6704 -0.0539 0.1465  0.1135  345 TYR B CD2 
7846  C CE1 . TYR B 345 ? 0.4649 0.5305 0.6554 -0.0687 0.1508  0.0992  345 TYR B CE1 
7847  C CE2 . TYR B 345 ? 0.6203 0.6481 0.8014 -0.0594 0.1449  0.1028  345 TYR B CE2 
7848  C CZ  . TYR B 345 ? 0.6524 0.7014 0.8438 -0.0668 0.1467  0.0956  345 TYR B CZ  
7849  O OH  . TYR B 345 ? 0.5867 0.6415 0.7895 -0.0717 0.1444  0.0844  345 TYR B OH  
7850  N N   . HIS B 346 ? 0.6180 0.6634 0.7533 -0.0462 0.1568  0.1493  346 HIS B N   
7851  C CA  . HIS B 346 ? 0.6201 0.6675 0.7443 -0.0388 0.1555  0.1579  346 HIS B CA  
7852  C C   . HIS B 346 ? 0.5504 0.5958 0.6756 -0.0277 0.1480  0.1555  346 HIS B C   
7853  O O   . HIS B 346 ? 0.5941 0.6362 0.7110 -0.0208 0.1461  0.1632  346 HIS B O   
7854  C CB  . HIS B 346 ? 0.5526 0.6228 0.6748 -0.0407 0.1575  0.1562  346 HIS B CB  
7855  C CG  . HIS B 346 ? 0.4794 0.5676 0.6097 -0.0361 0.1520  0.1447  346 HIS B CG  
7856  N ND1 . HIS B 346 ? 0.6015 0.6959 0.7442 -0.0387 0.1506  0.1332  346 HIS B ND1 
7857  C CD2 . HIS B 346 ? 0.6036 0.7034 0.7309 -0.0290 0.1477  0.1431  346 HIS B CD2 
7858  C CE1 . HIS B 346 ? 0.6290 0.7370 0.7750 -0.0328 0.1458  0.1258  346 HIS B CE1 
7859  N NE2 . HIS B 346 ? 0.5962 0.7077 0.7336 -0.0275 0.1441  0.1310  346 HIS B NE2 
7860  N N   . THR B 347 ? 0.6410 0.6890 0.7762 -0.0259 0.1439  0.1450  347 THR B N   
7861  C CA  . THR B 347 ? 0.5648 0.6114 0.7023 -0.0165 0.1379  0.1418  347 THR B CA  
7862  C C   . THR B 347 ? 0.5804 0.6119 0.7108 -0.0094 0.1366  0.1510  347 THR B C   
7863  O O   . THR B 347 ? 0.7623 0.7759 0.8886 -0.0108 0.1392  0.1571  347 THR B O   
7864  C CB  . THR B 347 ? 0.4419 0.4841 0.5881 -0.0165 0.1354  0.1321  347 THR B CB  
7865  O OG1 . THR B 347 ? 0.6778 0.7358 0.8314 -0.0217 0.1360  0.1231  347 THR B OG1 
7866  C CG2 . THR B 347 ? 0.5314 0.5717 0.6795 -0.0074 0.1304  0.1291  347 THR B CG2 
7867  N N   . LYS B 348 ? 0.5904 0.6295 0.7203 -0.0017 0.1325  0.1515  348 LYS B N   
7868  C CA  . LYS B 348 ? 0.6905 0.7193 0.8156 0.0061  0.1306  0.1593  348 LYS B CA  
7869  C C   . LYS B 348 ? 0.6493 0.6725 0.7812 0.0116  0.1275  0.1536  348 LYS B C   
7870  O O   . LYS B 348 ? 0.6586 0.6935 0.7960 0.0145  0.1244  0.1476  348 LYS B O   
7871  C CB  . LYS B 348 ? 0.3880 0.4307 0.5088 0.0109  0.1281  0.1635  348 LYS B CB  
7872  C CG  . LYS B 348 ? 0.6300 0.6680 0.7390 0.0111  0.1306  0.1752  348 LYS B CG  
7873  C CD  . LYS B 348 ? 0.8643 0.9185 0.9688 0.0164  0.1270  0.1780  348 LYS B CD  
7874  C CE  . LYS B 348 ? 0.7529 0.8025 0.8437 0.0180  0.1290  0.1902  348 LYS B CE  
7875  N NZ  . LYS B 348 ? 1.0220 1.0862 1.1086 0.0257  0.1237  0.1929  348 LYS B NZ  
7876  N N   . PHE B 349 ? 0.6950 0.6995 0.8260 0.0129  0.1287  0.1554  349 PHE B N   
7877  C CA  . PHE B 349 ? 0.5852 0.5829 0.7207 0.0185  0.1266  0.1507  349 PHE B CA  
7878  C C   . PHE B 349 ? 0.5960 0.5931 0.7301 0.0275  0.1248  0.1567  349 PHE B C   
7879  O O   . PHE B 349 ? 0.6054 0.5901 0.7338 0.0310  0.1261  0.1646  349 PHE B O   
7880  C CB  . PHE B 349 ? 0.4997 0.4782 0.6340 0.0164  0.1286  0.1493  349 PHE B CB  
7881  C CG  . PHE B 349 ? 0.4582 0.4290 0.5953 0.0221  0.1268  0.1440  349 PHE B CG  
7882  C CD1 . PHE B 349 ? 0.5753 0.5565 0.7178 0.0232  0.1245  0.1359  349 PHE B CD1 
7883  C CD2 . PHE B 349 ? 0.4845 0.4366 0.6177 0.0266  0.1279  0.1470  349 PHE B CD2 
7884  C CE1 . PHE B 349 ? 0.4909 0.4644 0.6342 0.0287  0.1235  0.1318  349 PHE B CE1 
7885  C CE2 . PHE B 349 ? 0.4723 0.4179 0.6068 0.0322  0.1268  0.1421  349 PHE B CE2 
7886  C CZ  . PHE B 349 ? 0.5844 0.5408 0.7236 0.0331  0.1248  0.1348  349 PHE B CZ  
7887  N N   . ILE B 350 ? 0.5237 0.5346 0.6634 0.0311  0.1220  0.1529  350 ILE B N   
7888  C CA  . ILE B 350 ? 0.6266 0.6414 0.7676 0.0390  0.1201  0.1574  350 ILE B CA  
7889  C C   . ILE B 350 ? 0.5617 0.5708 0.7079 0.0445  0.1200  0.1539  350 ILE B C   
7890  O O   . ILE B 350 ? 0.6193 0.6331 0.7705 0.0429  0.1195  0.1466  350 ILE B O   
7891  C CB  . ILE B 350 ? 0.5242 0.5600 0.6682 0.0386  0.1171  0.1560  350 ILE B CB  
7892  C CG1 . ILE B 350 ? 0.3633 0.4052 0.4999 0.0342  0.1176  0.1603  350 ILE B CG1 
7893  C CG2 . ILE B 350 ? 0.5504 0.5932 0.6982 0.0463  0.1146  0.1592  350 ILE B CG2 
7894  C CD1 . ILE B 350 ? 0.5353 0.5971 0.6742 0.0311  0.1154  0.1549  350 ILE B CD1 
7895  N N   . THR B 351 ? 0.5794 0.5785 0.7239 0.0515  0.1207  0.1596  351 THR B N   
7896  C CA  . THR B 351 ? 0.5389 0.5331 0.6877 0.0577  0.1215  0.1573  351 THR B CA  
7897  C C   . THR B 351 ? 0.6104 0.6202 0.7657 0.0630  0.1195  0.1598  351 THR B C   
7898  O O   . THR B 351 ? 0.6665 0.6816 0.8195 0.0657  0.1178  0.1662  351 THR B O   
7899  C CB  . THR B 351 ? 0.6009 0.5745 0.7441 0.0622  0.1239  0.1609  351 THR B CB  
7900  O OG1 . THR B 351 ? 0.6156 0.5836 0.7529 0.0646  0.1238  0.1695  351 THR B OG1 
7901  C CG2 . THR B 351 ? 0.4845 0.4440 0.6239 0.0570  0.1254  0.1555  351 THR B CG2 
7902  N N   . THR B 352 ? 0.5905 0.6107 0.8234 0.0810  0.1360  0.0936  352 THR B N   
7903  C CA  . THR B 352 ? 0.4498 0.5173 0.7288 0.0866  0.1371  0.0915  352 THR B CA  
7904  C C   . THR B 352 ? 0.4725 0.5545 0.7775 0.0980  0.1593  0.0837  352 THR B C   
7905  O O   . THR B 352 ? 0.6226 0.7494 0.9744 0.1035  0.1600  0.0821  352 THR B O   
7906  C CB  . THR B 352 ? 0.4511 0.5432 0.7373 0.0668  0.1333  0.0904  352 THR B CB  
7907  O OG1 . THR B 352 ? 0.6206 0.7005 0.8918 0.0556  0.1506  0.0842  352 THR B OG1 
7908  C CG2 . THR B 352 ? 0.4395 0.5212 0.7013 0.0565  0.1158  0.0969  352 THR B CG2 
7909  N N   . SER B 353 ? 0.5623 0.6085 0.8380 0.1008  0.1777  0.0784  353 SER B N   
7910  C CA  . SER B 353 ? 0.5768 0.6345 0.8720 0.1114  0.2041  0.0704  353 SER B CA  
7911  C C   . SER B 353 ? 0.4992 0.5353 0.7917 0.1387  0.2122  0.0679  353 SER B C   
7912  O O   . SER B 353 ? 0.6512 0.6342 0.8972 0.1426  0.2075  0.0687  353 SER B O   
7913  C CB  . SER B 353 ? 0.6746 0.7038 0.9332 0.0966  0.2232  0.0649  353 SER B CB  
7914  O OG  . SER B 353 ? 0.4758 0.5181 0.7517 0.1037  0.2528  0.0576  353 SER B OG  
7915  N N   . PRO B 354 ? 0.4430 0.5182 0.7847 0.1581  0.2256  0.0640  354 PRO B N   
7916  C CA  . PRO B 354 ? 0.5792 0.6300 0.9159 0.1884  0.2363  0.0601  354 PRO B CA  
7917  C C   . PRO B 354 ? 0.6941 0.6950 0.9818 0.1890  0.2642  0.0511  354 PRO B C   
7918  O O   . PRO B 354 ? 0.7395 0.6995 1.0017 0.2115  0.2722  0.0468  354 PRO B O   
7919  C CB  . PRO B 354 ? 0.6675 0.7851 1.0789 0.2073  0.2446  0.0576  354 PRO B CB  
7920  C CG  . PRO B 354 ? 0.4401 0.6070 0.8852 0.1817  0.2528  0.0562  354 PRO B CG  
7921  C CD  . PRO B 354 ? 0.4800 0.6233 0.8854 0.1533  0.2325  0.0622  354 PRO B CD  
7922  N N   . LYS B 355 ? 0.6074 0.6051 0.8755 0.1648  0.2775  0.0483  355 LYS B N   
7923  C CA  . LYS B 355 ? 0.6804 0.6253 0.8922 0.1622  0.3009  0.0406  355 LYS B CA  
7924  C C   . LYS B 355 ? 0.7514 0.6291 0.8966 0.1543  0.2802  0.0428  355 LYS B C   
7925  O O   . LYS B 355 ? 0.7114 0.5327 0.8030 0.1591  0.2924  0.0359  355 LYS B O   
7926  C CB  . LYS B 355 ? 0.6061 0.5635 0.8121 0.1375  0.3171  0.0389  355 LYS B CB  
7927  C CG  . LYS B 355 ? 0.7624 0.7873 1.0338 0.1353  0.3373  0.0375  355 LYS B CG  
7928  C CD  . LYS B 355 ? 0.7275 0.7518 0.9816 0.1069  0.3490  0.0378  355 LYS B CD  
7929  C CE  . LYS B 355 ? 0.9220 1.0048 1.2268 0.0937  0.3526  0.0364  355 LYS B CE  
7930  N NZ  . LYS B 355 ? 1.1840 1.2554 1.4630 0.0646  0.3573  0.0376  355 LYS B NZ  
7931  N N   . ALA B 356 ? 0.6721 0.5561 0.8197 0.1403  0.2496  0.0519  356 ALA B N   
7932  C CA  . ALA B 356 ? 0.6631 0.4949 0.7589 0.1287  0.2292  0.0551  356 ALA B CA  
7933  C C   . ALA B 356 ? 0.7978 0.6316 0.9047 0.1316  0.2030  0.0645  356 ALA B C   
7934  O O   . ALA B 356 ? 0.6291 0.4862 0.7480 0.1150  0.1848  0.0722  356 ALA B O   
7935  C CB  . ALA B 356 ? 0.6045 0.4361 0.6812 0.1022  0.2219  0.0567  356 ALA B CB  
7936  N N   . HIS B 357 ? 0.7108 0.5151 0.8085 0.1536  0.2022  0.0641  357 HIS B N   
7937  C CA  . HIS B 357 ? 0.5942 0.3863 0.6906 0.1572  0.1785  0.0740  357 HIS B CA  
7938  C C   . HIS B 357 ? 0.6729 0.4041 0.7123 0.1396  0.1661  0.0756  357 HIS B C   
7939  O O   . HIS B 357 ? 0.8718 0.5564 0.8705 0.1407  0.1765  0.0669  357 HIS B O   
7940  C CB  . HIS B 357 ? 0.7269 0.5060 0.8337 0.1907  0.1823  0.0728  357 HIS B CB  
7941  C CG  . HIS B 357 ? 0.7329 0.5779 0.9049 0.2092  0.1856  0.0739  357 HIS B CG  
7942  N ND1 . HIS B 357 ? 0.5818 0.4558 0.7817 0.2115  0.1622  0.0847  357 HIS B ND1 
7943  C CD2 . HIS B 357 ? 0.7188 0.6047 0.9320 0.2248  0.2090  0.0655  357 HIS B CD2 
7944  C CE1 . HIS B 357 ? 0.5837 0.5163 0.8423 0.2282  0.1684  0.0821  357 HIS B CE1 
7945  N NE2 . HIS B 357 ? 0.7176 0.6627 0.9903 0.2359  0.1975  0.0707  357 HIS B NE2 
7946  N N   . ILE B 358 ? 0.8328 0.5637 0.8678 0.1222  0.1446  0.0862  358 ILE B N   
7947  C CA  . ILE B 358 ? 0.7205 0.4009 0.7097 0.1018  0.1318  0.0885  358 ILE B CA  
7948  C C   . ILE B 358 ? 0.7021 0.3586 0.6821 0.1039  0.1159  0.0996  358 ILE B C   
7949  O O   . ILE B 358 ? 0.7805 0.4736 0.7876 0.1015  0.1068  0.1094  358 ILE B O   
7950  C CB  . ILE B 358 ? 0.6152 0.3207 0.6075 0.0731  0.1240  0.0906  358 ILE B CB  
7951  C CG1 . ILE B 358 ? 0.5890 0.3050 0.5790 0.0715  0.1386  0.0803  358 ILE B CG1 
7952  C CG2 . ILE B 358 ? 0.6975 0.3614 0.6543 0.0508  0.1080  0.0945  358 ILE B CG2 
7953  C CD1 . ILE B 358 ? 0.5769 0.3325 0.5845 0.0527  0.1331  0.0825  358 ILE B CD1 
7954  N N   . THR B 359 ? 0.8227 0.4123 0.7590 0.1086  0.1126  0.0982  359 THR B N   
7955  C CA  . THR B 359 ? 0.7638 0.3169 0.6813 0.1102  0.0981  0.1095  359 THR B CA  
7956  C C   . THR B 359 ? 0.8870 0.4545 0.8053 0.0782  0.0834  0.1217  359 THR B C   
7957  O O   . THR B 359 ? 0.9544 0.5290 0.8677 0.0524  0.0814  0.1192  359 THR B O   
7958  C CB  . THR B 359 ? 0.8438 0.3129 0.7061 0.1164  0.0974  0.1041  359 THR B CB  
7959  O OG1 . THR B 359 ? 0.9473 0.4064 0.8103 0.1494  0.1152  0.0917  359 THR B OG1 
7960  C CG2 . THR B 359 ? 0.8941 0.3142 0.7295 0.1180  0.0826  0.1164  359 THR B CG2 
7961  N N   . ASP B 360 ? 0.8070 0.3796 0.7314 0.0812  0.0737  0.1350  360 ASP B N   
7962  C CA  . ASP B 360 ? 0.9018 0.4870 0.8249 0.0534  0.0636  0.1481  360 ASP B CA  
7963  C C   . ASP B 360 ? 0.8343 0.4919 0.7978 0.0418  0.0668  0.1481  360 ASP B C   
7964  O O   . ASP B 360 ? 0.9491 0.6216 0.9132 0.0157  0.0633  0.1544  360 ASP B O   
7965  C CB  . ASP B 360 ? 0.9765 0.5146 0.8632 0.0228  0.0576  0.1501  360 ASP B CB  
7966  C CG  . ASP B 360 ? 1.1172 0.5760 0.9560 0.0258  0.0501  0.1559  360 ASP B CG  
7967  O OD1 . ASP B 360 ? 1.2082 0.6454 1.0404 0.0564  0.0495  0.1580  360 ASP B OD1 
7968  O OD2 . ASP B 360 ? 1.4474 0.8649 1.2560 -0.0024 0.0436  0.1583  360 ASP B OD2 
7969  N N   . SER B 361 ? 0.6531 0.3552 0.6508 0.0612  0.0739  0.1411  361 SER B N   
7970  C CA  . SER B 361 ? 0.7095 0.4732 0.7412 0.0523  0.0765  0.1401  361 SER B CA  
7971  C C   . SER B 361 ? 0.6415 0.4384 0.6993 0.0714  0.0724  0.1441  361 SER B C   
7972  O O   . SER B 361 ? 0.9501 0.7355 1.0129 0.0961  0.0720  0.1425  361 SER B O   
7973  C CB  . SER B 361 ? 0.6142 0.3982 0.6599 0.0522  0.0879  0.1269  361 SER B CB  
7974  O OG  . SER B 361 ? 0.6974 0.4861 0.7576 0.0769  0.0978  0.1190  361 SER B OG  
7975  N N   . ILE B 362 ? 0.6351 0.4720 0.7090 0.0613  0.0683  0.1487  362 ILE B N   
7976  C CA  . ILE B 362 ? 0.6063 0.4731 0.7018 0.0770  0.0603  0.1520  362 ILE B CA  
7977  C C   . ILE B 362 ? 0.6657 0.5685 0.7993 0.0917  0.0687  0.1401  362 ILE B C   
7978  O O   . ILE B 362 ? 0.6436 0.5687 0.7892 0.0802  0.0788  0.1321  362 ILE B O   
7979  C CB  . ILE B 362 ? 0.5258 0.4208 0.6217 0.0615  0.0549  0.1581  362 ILE B CB  
7980  C CG1 . ILE B 362 ? 0.5113 0.3718 0.5693 0.0467  0.0500  0.1715  362 ILE B CG1 
7981  C CG2 . ILE B 362 ? 0.4779 0.4047 0.5959 0.0763  0.0442  0.1587  362 ILE B CG2 
7982  C CD1 . ILE B 362 ? 0.8862 0.7446 0.9348 0.0206  0.0591  0.1714  362 ILE B CD1 
7983  N N   . TYR B 363 ? 0.6553 0.5635 0.8085 0.1169  0.0653  0.1391  363 TYR B N   
7984  C CA  . TYR B 363 ? 0.5563 0.5035 0.7513 0.1292  0.0765  0.1281  363 TYR B CA  
7985  C C   . TYR B 363 ? 0.5361 0.5352 0.7701 0.1337  0.0654  0.1289  363 TYR B C   
7986  O O   . TYR B 363 ? 0.6746 0.6776 0.9187 0.1518  0.0497  0.1348  363 TYR B O   
7987  C CB  . TYR B 363 ? 0.6242 0.5496 0.8234 0.1556  0.0847  0.1234  363 TYR B CB  
7988  C CG  . TYR B 363 ? 0.5162 0.4840 0.7601 0.1666  0.1019  0.1120  363 TYR B CG  
7989  C CD1 . TYR B 363 ? 0.5942 0.5609 0.8325 0.1544  0.1228  0.1024  363 TYR B CD1 
7990  C CD2 . TYR B 363 ? 0.5303 0.5404 0.8222 0.1882  0.0969  0.1112  363 TYR B CD2 
7991  C CE1 . TYR B 363 ? 0.6147 0.6181 0.8904 0.1615  0.1420  0.0930  363 TYR B CE1 
7992  C CE2 . TYR B 363 ? 0.5069 0.5616 0.8453 0.1952  0.1153  0.1011  363 TYR B CE2 
7993  C CZ  . TYR B 363 ? 0.4639 0.5135 0.7922 0.1809  0.1398  0.0923  363 TYR B CZ  
7994  O OH  . TYR B 363 ? 0.6097 0.7003 0.9800 0.1852  0.1617  0.0833  363 TYR B OH  
7995  N N   . MET B 364 ? 0.5215 0.5571 0.7752 0.1176  0.0717  0.1227  364 MET B N   
7996  C CA  . MET B 364 ? 0.5233 0.6068 0.8128 0.1168  0.0611  0.1215  364 MET B CA  
7997  C C   . MET B 364 ? 0.4700 0.5887 0.7995 0.1164  0.0789  0.1104  364 MET B C   
7998  O O   . MET B 364 ? 0.4084 0.5306 0.7318 0.0981  0.0911  0.1050  364 MET B O   
7999  C CB  . MET B 364 ? 0.3803 0.4678 0.6494 0.0949  0.0534  0.1241  364 MET B CB  
8000  C CG  . MET B 364 ? 0.3844 0.4383 0.6123 0.0923  0.0410  0.1354  364 MET B CG  
8001  S SD  . MET B 364 ? 0.5944 0.6582 0.8011 0.0720  0.0335  0.1378  364 MET B SD  
8002  C CE  . MET B 364 ? 0.5962 0.6899 0.8249 0.0825  0.0094  0.1390  364 MET B CE  
8003  N N   . GLU B 365 ? 0.4532 0.5967 0.8230 0.1371  0.0818  0.1072  365 GLU B N   
8004  C CA  . GLU B 365 ? 0.4358 0.6148 0.8461 0.1360  0.1032  0.0972  365 GLU B CA  
8005  C C   . GLU B 365 ? 0.4422 0.6610 0.8766 0.1137  0.0997  0.0939  365 GLU B C   
8006  O O   . GLU B 365 ? 0.4813 0.7224 0.9290 0.1109  0.0763  0.0977  365 GLU B O   
8007  C CB  . GLU B 365 ? 0.3683 0.5767 0.8267 0.1642  0.1060  0.0948  365 GLU B CB  
8008  C CG  . GLU B 365 ? 0.4413 0.6798 0.9367 0.1649  0.1364  0.0845  365 GLU B CG  
8009  C CD  . GLU B 365 ? 0.7743 1.0278 1.3057 0.1977  0.1478  0.0809  365 GLU B CD  
8010  O OE1 . GLU B 365 ? 0.9087 1.1159 1.4054 0.2119  0.1646  0.0782  365 GLU B OE1 
8011  O OE2 . GLU B 365 ? 0.7876 1.0990 1.3825 0.2100  0.1393  0.0802  365 GLU B OE2 
8012  N N   . PHE B 366 ? 0.3089 0.5299 0.7420 0.0971  0.1217  0.0870  366 PHE B N   
8013  C CA  . PHE B 366 ? 0.2887 0.5382 0.7388 0.0745  0.1201  0.0835  366 PHE B CA  
8014  C C   . PHE B 366 ? 0.3362 0.6419 0.8516 0.0774  0.1261  0.0786  366 PHE B C   
8015  O O   . PHE B 366 ? 0.4974 0.8125 1.0308 0.0782  0.1535  0.0731  366 PHE B O   
8016  C CB  . PHE B 366 ? 0.3869 0.6080 0.8022 0.0557  0.1396  0.0794  366 PHE B CB  
8017  C CG  . PHE B 366 ? 0.2844 0.5254 0.7112 0.0324  0.1400  0.0755  366 PHE B CG  
8018  C CD1 . PHE B 366 ? 0.4895 0.7386 0.9125 0.0222  0.1168  0.0773  366 PHE B CD1 
8019  C CD2 . PHE B 366 ? 0.3062 0.5511 0.7407 0.0199  0.1643  0.0701  366 PHE B CD2 
8020  C CE1 . PHE B 366 ? 0.5075 0.7670 0.9354 0.0004  0.1163  0.0729  366 PHE B CE1 
8021  C CE2 . PHE B 366 ? 0.5165 0.7721 0.9565 -0.0034 0.1642  0.0671  366 PHE B CE2 
8022  C CZ  . PHE B 366 ? 0.3906 0.6525 0.8275 -0.0128 0.1394  0.0681  366 PHE B CZ  
8023  N N   . ASP B 367 ? 0.4027 0.7466 0.9538 0.0789  0.1007  0.0807  367 ASP B N   
8024  C CA  . ASP B 367 ? 0.2881 0.6949 0.9113 0.0805  0.1017  0.0763  367 ASP B CA  
8025  C C   . ASP B 367 ? 0.3424 0.7689 0.9820 0.0509  0.1193  0.0699  367 ASP B C   
8026  O O   . ASP B 367 ? 0.5286 0.9513 1.1530 0.0284  0.1042  0.0694  367 ASP B O   
8027  C CB  . ASP B 367 ? 0.3266 0.7645 0.9769 0.0865  0.0637  0.0803  367 ASP B CB  
8028  C CG  . ASP B 367 ? 0.4365 0.9470 1.1692 0.0873  0.0587  0.0760  367 ASP B CG  
8029  O OD1 . ASP B 367 ? 0.6248 1.1514 1.3763 0.0918  0.0843  0.0675  367 ASP B OD1 
8030  O OD2 . ASP B 367 ? 0.5837 1.1222 1.3375 0.0801  0.0266  0.0770  367 ASP B OD2 
8031  N N   . GLU B 368 ? 0.4614 0.8986 1.1148 0.0495  0.1481  0.0627  368 GLU B N   
8032  C CA  . GLU B 368 ? 0.2869 0.7279 0.9356 0.0190  0.1653  0.0563  368 GLU B CA  
8033  C C   . GLU B 368 ? 0.4701 0.9691 1.1733 0.0034  0.1490  0.0524  368 GLU B C   
8034  O O   . GLU B 368 ? 0.4886 0.9913 1.1898 -0.0252 0.1587  0.0485  368 GLU B O   
8035  C CB  . GLU B 368 ? 0.3302 0.7544 0.9611 0.0222  0.2001  0.0510  368 GLU B CB  
8036  C CG  . GLU B 368 ? 1.0924 1.5445 1.7574 0.0502  0.2075  0.0476  368 GLU B CG  
8037  C CD  . GLU B 368 ? 1.1200 1.5366 1.7608 0.0809  0.2056  0.0518  368 GLU B CD  
8038  O OE1 . GLU B 368 ? 1.1828 1.5528 1.7791 0.0854  0.2282  0.0508  368 GLU B OE1 
8039  O OE2 . GLU B 368 ? 0.9246 1.3570 1.5883 0.0999  0.1804  0.0564  368 GLU B OE2 
8040  N N   . GLU B 369 ? 0.5601 1.0998 1.3074 0.0210  0.1236  0.0537  369 GLU B N   
8041  C CA  . GLU B 369 ? 0.7208 1.3178 1.5214 0.0070  0.1023  0.0499  369 GLU B CA  
8042  C C   . GLU B 369 ? 0.6221 1.2110 1.4130 -0.0124 0.0709  0.0538  369 GLU B C   
8043  O O   . GLU B 369 ? 0.7618 1.3747 1.5730 -0.0404 0.0617  0.0493  369 GLU B O   
8044  C CB  . GLU B 369 ? 0.7879 1.4305 1.6371 0.0368  0.0852  0.0493  369 GLU B CB  
8045  C CG  . GLU B 369 ? 0.9263 1.5901 1.7971 0.0533  0.1156  0.0431  369 GLU B CG  
8046  C CD  . GLU B 369 ? 1.1393 1.8491 2.0593 0.0853  0.0987  0.0416  369 GLU B CD  
8047  O OE1 . GLU B 369 ? 1.1447 1.8465 2.0620 0.1045  0.0660  0.0479  369 GLU B OE1 
8048  O OE2 . GLU B 369 ? 1.1593 1.9124 2.1188 0.0921  0.1179  0.0347  369 GLU B OE2 
8049  N N   . ASN B 370 ? 0.2901 0.8442 1.0486 0.0014  0.0545  0.0626  370 ASN B N   
8050  C CA  . ASN B 370 ? 0.4438 0.9698 1.1591 -0.0140 0.0247  0.0639  370 ASN B CA  
8051  C C   . ASN B 370 ? 0.3617 0.8189 0.9985 -0.0155 0.0411  0.0659  370 ASN B C   
8052  O O   . ASN B 370 ? 0.4476 0.8701 1.0413 0.0018  0.0304  0.0717  370 ASN B O   
8053  C CB  . ASN B 370 ? 0.4009 0.9344 1.1169 0.0069  -0.0142 0.0694  370 ASN B CB  
8054  C CG  . ASN B 370 ? 0.5360 1.1408 1.3339 0.0136  -0.0347 0.0680  370 ASN B CG  
8055  O OD1 . ASN B 370 ? 0.7245 1.3720 1.5690 -0.0060 -0.0255 0.0601  370 ASN B OD1 
8056  N ND2 . ASN B 370 ? 0.8064 1.4184 1.6106 0.0412  -0.0634 0.0742  370 ASN B ND2 
8057  N N   . PRO B 371 ? 0.2659 0.7024 0.8841 -0.0356 0.0677  0.0619  371 PRO B N   
8058  C CA  . PRO B 371 ? 0.3698 0.7457 0.9196 -0.0340 0.0817  0.0638  371 PRO B CA  
8059  C C   . PRO B 371 ? 0.4536 0.7902 0.9468 -0.0386 0.0605  0.0651  371 PRO B C   
8060  O O   . PRO B 371 ? 0.4572 0.7599 0.9093 -0.0245 0.0610  0.0698  371 PRO B O   
8061  C CB  . PRO B 371 ? 0.3937 0.7594 0.9401 -0.0545 0.1115  0.0594  371 PRO B CB  
8062  C CG  . PRO B 371 ? 0.2715 0.6943 0.8877 -0.0636 0.1207  0.0561  371 PRO B CG  
8063  C CD  . PRO B 371 ? 0.3327 0.7984 0.9902 -0.0604 0.0868  0.0562  371 PRO B CD  
8064  N N   . LEU B 372 ? 0.4803 0.8195 0.9699 -0.0588 0.0434  0.0606  372 LEU B N   
8065  C CA  . LEU B 372 ? 0.4822 0.7819 0.9148 -0.0613 0.0269  0.0605  372 LEU B CA  
8066  C C   . LEU B 372 ? 0.5056 0.8055 0.9262 -0.0417 0.0040  0.0668  372 LEU B C   
8067  O O   . LEU B 372 ? 0.5857 0.8495 0.9571 -0.0335 0.0042  0.0704  372 LEU B O   
8068  C CB  . LEU B 372 ? 0.3813 0.6774 0.8071 -0.0868 0.0128  0.0530  372 LEU B CB  
8069  C CG  . LEU B 372 ? 0.3371 0.5854 0.6977 -0.0900 0.0018  0.0503  372 LEU B CG  
8070  C CD1 . LEU B 372 ? 0.3517 0.5589 0.6682 -0.0811 0.0241  0.0522  372 LEU B CD1 
8071  C CD2 . LEU B 372 ? 0.3658 0.6034 0.7179 -0.1164 -0.0085 0.0414  372 LEU B CD2 
8072  N N   . ASP B 373 ? 0.3484 0.6886 0.8136 -0.0338 -0.0154 0.0687  373 ASP B N   
8073  C CA  . ASP B 373 ? 0.3418 0.6761 0.7902 -0.0142 -0.0388 0.0762  373 ASP B CA  
8074  C C   . ASP B 373 ? 0.4444 0.7560 0.8742 0.0070  -0.0221 0.0840  373 ASP B C   
8075  O O   . ASP B 373 ? 0.5787 0.8584 0.9633 0.0162  -0.0303 0.0905  373 ASP B O   
8076  C CB  . ASP B 373 ? 0.4442 0.8279 0.9489 -0.0069 -0.0645 0.0770  373 ASP B CB  
8077  C CG  . ASP B 373 ? 0.8499 1.2535 1.3678 -0.0286 -0.0911 0.0701  373 ASP B CG  
8078  O OD1 . ASP B 373 ? 0.7492 1.1182 1.2201 -0.0473 -0.0916 0.0649  373 ASP B OD1 
8079  O OD2 . ASP B 373 ? 0.7921 1.2451 1.3675 -0.0263 -0.1125 0.0694  373 ASP B OD2 
8080  N N   . SER B 374 ? 0.4361 0.7611 0.8974 0.0131  0.0024  0.0830  374 SER B N   
8081  C CA  . SER B 374 ? 0.4016 0.7012 0.8443 0.0311  0.0185  0.0887  374 SER B CA  
8082  C C   . SER B 374 ? 0.5090 0.7623 0.8935 0.0233  0.0298  0.0899  374 SER B C   
8083  O O   . SER B 374 ? 0.5591 0.7845 0.9102 0.0335  0.0266  0.0970  374 SER B O   
8084  C CB  . SER B 374 ? 0.3009 0.6198 0.7824 0.0361  0.0446  0.0848  374 SER B CB  
8085  O OG  . SER B 374 ? 0.4810 0.7750 0.9465 0.0558  0.0559  0.0894  374 SER B OG  
8086  N N   . ALA B 375 ? 0.5284 0.7736 0.9019 0.0052  0.0425  0.0833  375 ALA B N   
8087  C CA  . ALA B 375 ? 0.4998 0.7072 0.8252 -0.0002 0.0518  0.0836  375 ALA B CA  
8088  C C   . ALA B 375 ? 0.4680 0.6590 0.7571 0.0004  0.0344  0.0871  375 ALA B C   
8089  O O   . ALA B 375 ? 0.4528 0.6190 0.7092 0.0046  0.0400  0.0915  375 ALA B O   
8090  C CB  . ALA B 375 ? 0.3629 0.5631 0.6829 -0.0174 0.0644  0.0760  375 ALA B CB  
8091  N N   . LYS B 376 ? 0.3956 0.6003 0.6893 -0.0046 0.0137  0.0851  376 LYS B N   
8092  C CA  . LYS B 376 ? 0.4672 0.6521 0.7190 -0.0037 -0.0020 0.0880  376 LYS B CA  
8093  C C   . LYS B 376 ? 0.5953 0.7695 0.8328 0.0122  -0.0076 0.0992  376 LYS B C   
8094  O O   . LYS B 376 ? 0.5706 0.7189 0.7663 0.0133  -0.0049 0.1040  376 LYS B O   
8095  C CB  . LYS B 376 ? 0.3455 0.5443 0.6028 -0.0122 -0.0269 0.0832  376 LYS B CB  
8096  C CG  . LYS B 376 ? 0.3599 0.5514 0.6083 -0.0311 -0.0242 0.0723  376 LYS B CG  
8097  C CD  . LYS B 376 ? 0.5999 0.7885 0.8306 -0.0407 -0.0516 0.0672  376 LYS B CD  
8098  C CE  . LYS B 376 ? 0.6446 0.8689 0.9245 -0.0547 -0.0674 0.0614  376 LYS B CE  
8099  N NZ  . LYS B 376 ? 0.7873 0.9934 1.0457 -0.0766 -0.0744 0.0504  376 LYS B NZ  
8100  N N   . LYS B 377 ? 0.4851 0.6782 0.7573 0.0247  -0.0138 0.1035  377 LYS B N   
8101  C CA  . LYS B 377 ? 0.4258 0.6026 0.6830 0.0409  -0.0206 0.1147  377 LYS B CA  
8102  C C   . LYS B 377 ? 0.4348 0.5846 0.6709 0.0427  0.0010  0.1190  377 LYS B C   
8103  O O   . LYS B 377 ? 0.5686 0.6917 0.7716 0.0474  -0.0018 0.1284  377 LYS B O   
8104  C CB  . LYS B 377 ? 0.3825 0.5859 0.6852 0.0572  -0.0321 0.1167  377 LYS B CB  
8105  C CG  . LYS B 377 ? 0.5667 0.7987 0.8914 0.0572  -0.0610 0.1147  377 LYS B CG  
8106  C CD  . LYS B 377 ? 0.7577 1.0139 1.1237 0.0795  -0.0768 0.1193  377 LYS B CD  
8107  C CE  . LYS B 377 ? 0.8782 1.1799 1.2894 0.0779  -0.1039 0.1146  377 LYS B CE  
8108  N NZ  . LYS B 377 ? 0.7313 1.0841 1.2182 0.0865  -0.0951 0.1093  377 LYS B NZ  
8109  N N   . ILE B 378 ? 0.5233 0.6774 0.7761 0.0375  0.0213  0.1126  378 ILE B N   
8110  C CA  . ILE B 378 ? 0.5159 0.6449 0.7494 0.0375  0.0383  0.1155  378 ILE B CA  
8111  C C   . ILE B 378 ? 0.5620 0.6756 0.7607 0.0261  0.0428  0.1160  378 ILE B C   
8112  O O   . ILE B 378 ? 0.6921 0.7855 0.8653 0.0260  0.0452  0.1236  378 ILE B O   
8113  C CB  . ILE B 378 ? 0.3122 0.4464 0.5680 0.0364  0.0567  0.1084  378 ILE B CB  
8114  C CG1 . ILE B 378 ? 0.3770 0.5253 0.6665 0.0513  0.0573  0.1083  378 ILE B CG1 
8115  C CG2 . ILE B 378 ? 0.3510 0.4572 0.5812 0.0328  0.0698  0.1102  378 ILE B CG2 
8116  C CD1 . ILE B 378 ? 0.5620 0.7237 0.8774 0.0493  0.0756  0.1001  378 ILE B CD1 
8117  N N   . LEU B 379 ? 0.5360 0.6587 0.7342 0.0165  0.0446  0.1078  379 LEU B N   
8118  C CA  . LEU B 379 ? 0.4687 0.5795 0.6372 0.0094  0.0503  0.1063  379 LEU B CA  
8119  C C   . LEU B 379 ? 0.5799 0.6795 0.7169 0.0109  0.0419  0.1137  379 LEU B C   
8120  O O   . LEU B 379 ? 0.6101 0.6991 0.7248 0.0080  0.0519  0.1169  379 LEU B O   
8121  C CB  . LEU B 379 ? 0.4748 0.5914 0.6448 0.0014  0.0505  0.0958  379 LEU B CB  
8122  C CG  . LEU B 379 ? 0.3890 0.4925 0.5292 -0.0021 0.0568  0.0918  379 LEU B CG  
8123  C CD1 . LEU B 379 ? 0.4648 0.5621 0.6024 -0.0004 0.0715  0.0938  379 LEU B CD1 
8124  C CD2 . LEU B 379 ? 0.3439 0.4448 0.4831 -0.0092 0.0557  0.0812  379 LEU B CD2 
8125  N N   . LYS B 380 ? 0.5421 0.6444 0.6769 0.0154  0.0238  0.1169  380 LYS B N   
8126  C CA  . LYS B 380 ? 0.5246 0.6091 0.6202 0.0169  0.0149  0.1250  380 LYS B CA  
8127  C C   . LYS B 380 ? 0.4943 0.5601 0.5740 0.0188  0.0243  0.1368  380 LYS B C   
8128  O O   . LYS B 380 ? 0.6112 0.6619 0.6567 0.0139  0.0318  0.1421  380 LYS B O   
8129  C CB  . LYS B 380 ? 0.4114 0.5002 0.5088 0.0235  -0.0108 0.1275  380 LYS B CB  
8130  C CG  . LYS B 380 ? 0.4775 0.5402 0.5249 0.0257  -0.0220 0.1370  380 LYS B CG  
8131  C CD  . LYS B 380 ? 0.6937 0.7605 0.7387 0.0312  -0.0525 0.1371  380 LYS B CD  
8132  C CE  . LYS B 380 ? 0.7845 0.8178 0.7707 0.0341  -0.0654 0.1476  380 LYS B CE  
8133  N NZ  . LYS B 380 ? 0.9576 0.9903 0.9247 0.0329  -0.0930 0.1423  380 LYS B NZ  
8134  N N   . GLU B 381 ? 0.5186 0.5835 0.6214 0.0249  0.0255  0.1403  381 GLU B N   
8135  C CA  . GLU B 381 ? 0.6833 0.7244 0.7693 0.0243  0.0326  0.1510  381 GLU B CA  
8136  C C   . GLU B 381 ? 0.6717 0.7125 0.7523 0.0122  0.0519  0.1497  381 GLU B C   
8137  O O   . GLU B 381 ? 0.7609 0.7852 0.8178 0.0050  0.0587  0.1589  381 GLU B O   
8138  C CB  . GLU B 381 ? 0.5744 0.6100 0.6838 0.0350  0.0300  0.1526  381 GLU B CB  
8139  C CG  . GLU B 381 ? 0.7348 0.7680 0.8481 0.0506  0.0096  0.1575  381 GLU B CG  
8140  C CD  . GLU B 381 ? 0.9753 0.9804 1.0443 0.0515  -0.0025 0.1703  381 GLU B CD  
8141  O OE1 . GLU B 381 ? 1.0674 1.0399 1.1090 0.0481  0.0038  0.1806  381 GLU B OE1 
8142  O OE2 . GLU B 381 ? 0.8601 0.8720 0.9177 0.0537  -0.0184 0.1702  381 GLU B OE2 
8143  N N   . ALA B 382 ? 0.5285 0.5876 0.6314 0.0093  0.0603  0.1387  382 ALA B N   
8144  C CA  . ALA B 382 ? 0.5734 0.6370 0.6768 0.0007  0.0751  0.1364  382 ALA B CA  
8145  C C   . ALA B 382 ? 0.5073 0.5749 0.5876 -0.0037 0.0812  0.1371  382 ALA B C   
8146  O O   . ALA B 382 ? 0.6236 0.6922 0.6974 -0.0110 0.0929  0.1418  382 ALA B O   
8147  C CB  . ALA B 382 ? 0.5225 0.5987 0.6487 0.0014  0.0794  0.1251  382 ALA B CB  
8148  N N   . ILE B 383 ? 0.5352 0.6051 0.6028 0.0002  0.0738  0.1320  383 ILE B N   
8149  C CA  . ILE B 383 ? 0.5277 0.5954 0.5653 -0.0016 0.0803  0.1308  383 ILE B CA  
8150  C C   . ILE B 383 ? 0.5601 0.6111 0.5661 -0.0056 0.0835  0.1441  383 ILE B C   
8151  O O   . ILE B 383 ? 0.6170 0.6703 0.6083 -0.0111 0.1004  0.1469  383 ILE B O   
8152  C CB  . ILE B 383 ? 0.4689 0.5340 0.4928 0.0021  0.0674  0.1219  383 ILE B CB  
8153  C CG1 . ILE B 383 ? 0.4896 0.5659 0.5367 0.0025  0.0692  0.1089  383 ILE B CG1 
8154  C CG2 . ILE B 383 ? 0.4830 0.5351 0.4622 0.0017  0.0727  0.1219  383 ILE B CG2 
8155  C CD1 . ILE B 383 ? 0.5618 0.6374 0.6104 0.0019  0.0525  0.1011  383 ILE B CD1 
8156  N N   . LEU B 384 ? 0.5827 0.6165 0.5778 -0.0024 0.0680  0.1526  384 LEU B N   
8157  C CA  . LEU B 384 ? 0.6100 0.6185 0.5669 -0.0063 0.0691  0.1669  384 LEU B CA  
8158  C C   . LEU B 384 ? 0.6426 0.6483 0.6061 -0.0175 0.0862  0.1754  384 LEU B C   
8159  O O   . LEU B 384 ? 0.7161 0.7077 0.6486 -0.0266 0.0978  0.1855  384 LEU B O   
8160  C CB  . LEU B 384 ? 0.5553 0.5433 0.5013 0.0029  0.0455  0.1743  384 LEU B CB  
8161  C CG  . LEU B 384 ? 0.5270 0.5191 0.4662 0.0116  0.0239  0.1675  384 LEU B CG  
8162  C CD1 . LEU B 384 ? 0.7359 0.7215 0.6871 0.0239  -0.0007 0.1728  384 LEU B CD1 
8163  C CD2 . LEU B 384 ? 0.5750 0.5477 0.4594 0.0083  0.0239  0.1697  384 LEU B CD2 
8164  N N   . ASN B 385 ? 0.6015 0.6193 0.6029 -0.0186 0.0880  0.1713  385 ASN B N   
8165  C CA  . ASN B 385 ? 0.4854 0.5002 0.4950 -0.0316 0.1002  0.1781  385 ASN B CA  
8166  C C   . ASN B 385 ? 0.5855 0.6248 0.6009 -0.0420 0.1205  0.1762  385 ASN B C   
8167  O O   . ASN B 385 ? 0.7835 0.8230 0.8027 -0.0566 0.1314  0.1840  385 ASN B O   
8168  C CB  . ASN B 385 ? 0.4501 0.4685 0.4930 -0.0296 0.0953  0.1724  385 ASN B CB  
8169  C CG  . ASN B 385 ? 0.6054 0.6054 0.6471 -0.0429 0.0994  0.1811  385 ASN B CG  
8170  O OD1 . ASN B 385 ? 0.7811 0.7492 0.7954 -0.0471 0.0961  0.1932  385 ASN B OD1 
8171  N ND2 . ASN B 385 ? 0.7059 0.7217 0.7739 -0.0506 0.1046  0.1754  385 ASN B ND2 
8172  N N   . PHE B 386 ? 0.5788 0.6386 0.5961 -0.0347 0.1259  0.1658  386 PHE B N   
8173  C CA  . PHE B 386 ? 0.5795 0.6652 0.6046 -0.0396 0.1466  0.1629  386 PHE B CA  
8174  C C   . PHE B 386 ? 0.6007 0.6772 0.5963 -0.0524 0.1628  0.1760  386 PHE B C   
8175  O O   . PHE B 386 ? 0.6449 0.7452 0.6589 -0.0633 0.1816  0.1786  386 PHE B O   
8176  C CB  . PHE B 386 ? 0.5595 0.6549 0.5762 -0.0267 0.1485  0.1501  386 PHE B CB  
8177  C CG  . PHE B 386 ? 0.5205 0.6428 0.5457 -0.0257 0.1707  0.1451  386 PHE B CG  
8178  C CD1 . PHE B 386 ? 0.5969 0.7480 0.6636 -0.0221 0.1744  0.1372  386 PHE B CD1 
8179  C CD2 . PHE B 386 ? 0.4825 0.6002 0.4724 -0.0258 0.1874  0.1476  386 PHE B CD2 
8180  C CE1 . PHE B 386 ? 0.4671 0.6469 0.5470 -0.0171 0.1937  0.1320  386 PHE B CE1 
8181  C CE2 . PHE B 386 ? 0.4828 0.6285 0.4839 -0.0216 0.2106  0.1417  386 PHE B CE2 
8182  C CZ  . PHE B 386 ? 0.4425 0.6214 0.4919 -0.0163 0.2132  0.1339  386 PHE B CZ  
8183  N N   . LYS B 387 ? 0.5699 0.6118 0.5200 -0.0514 0.1550  0.1847  387 LYS B N   
8184  C CA  . LYS B 387 ? 0.6349 0.6560 0.5437 -0.0640 0.1695  0.1991  387 LYS B CA  
8185  C C   . LYS B 387 ? 0.6674 0.6838 0.5901 -0.0837 0.1771  0.2116  387 LYS B C   
8186  O O   . LYS B 387 ? 0.9314 0.9433 0.8335 -0.0998 0.1974  0.2227  387 LYS B O   
8187  C CB  . LYS B 387 ? 0.6219 0.5994 0.4769 -0.0569 0.1517  0.2066  387 LYS B CB  
8188  C CG  . LYS B 387 ? 0.6587 0.6357 0.4908 -0.0421 0.1434  0.1952  387 LYS B CG  
8189  C CD  . LYS B 387 ? 0.8170 0.7505 0.5883 -0.0377 0.1265  0.2043  387 LYS B CD  
8190  C CE  . LYS B 387 ? 1.0501 0.9637 0.7615 -0.0438 0.1467  0.2101  387 LYS B CE  
8191  N NZ  . LYS B 387 ? 1.3154 1.2141 0.9861 -0.0317 0.1335  0.2002  387 LYS B NZ  
8192  N N   . ASN B 388 ? 0.6147 0.6293 0.5689 -0.0840 0.1620  0.2098  388 ASN B N   
8193  C CA  . ASN B 388 ? 0.7205 0.7241 0.6850 -0.1036 0.1653  0.2200  388 ASN B CA  
8194  C C   . ASN B 388 ? 0.6309 0.6785 0.6478 -0.1147 0.1759  0.2131  388 ASN B C   
8195  O O   . ASN B 388 ? 0.6647 0.7045 0.6966 -0.1308 0.1727  0.2181  388 ASN B O   
8196  C CB  . ASN B 388 ? 0.7224 0.6897 0.6823 -0.0966 0.1422  0.2219  388 ASN B CB  
8197  C CG  . ASN B 388 ? 0.7532 0.6808 0.6687 -0.0829 0.1274  0.2288  388 ASN B CG  
8198  O OD1 . ASN B 388 ? 0.8031 0.7045 0.6736 -0.0897 0.1336  0.2413  388 ASN B OD1 
8199  N ND2 . ASN B 388 ? 0.9164 0.8393 0.8435 -0.0632 0.1072  0.2211  388 ASN B ND2 
8200  N N   . ARG B 389 ? 0.7188 0.8097 0.7617 -0.1059 0.1866  0.2017  389 ARG B N   
8201  C CA  . ARG B 389 ? 0.5500 0.6852 0.6447 -0.1133 0.1936  0.1953  389 ARG B CA  
8202  C C   . ARG B 389 ? 0.5738 0.7266 0.6740 -0.1355 0.2129  0.1997  389 ARG B C   
8203  O O   . ARG B 389 ? 0.7912 0.9344 0.8571 -0.1395 0.2291  0.2048  389 ARG B O   
8204  C CB  . ARG B 389 ? 0.4332 0.6035 0.5509 -0.0928 0.1961  0.1798  389 ARG B CB  
8205  C CG  . ARG B 389 ? 0.7296 0.9353 0.8995 -0.0933 0.1905  0.1715  389 ARG B CG  
8206  C CD  . ARG B 389 ? 0.5559 0.7911 0.7448 -0.0722 0.1933  0.1576  389 ARG B CD  
8207  N NE  . ARG B 389 ? 0.4837 0.6963 0.6622 -0.0552 0.1746  0.1479  389 ARG B NE  
8208  C CZ  . ARG B 389 ? 0.6352 0.8596 0.8209 -0.0368 0.1735  0.1358  389 ARG B CZ  
8209  N NH1 . ARG B 389 ? 0.6121 0.8702 0.8155 -0.0290 0.1889  0.1309  389 ARG B NH1 
8210  N NH2 . ARG B 389 ? 0.5462 0.7477 0.7210 -0.0259 0.1581  0.1285  389 ARG B NH2 
8211  N N   . ASP B 390 ? 0.5753 0.7505 0.7149 -0.1506 0.2094  0.1954  390 ASP B N   
8212  C CA  . ASP B 390 ? 0.6999 0.8972 0.8541 -0.1735 0.2259  0.1952  390 ASP B CA  
8213  C C   . ASP B 390 ? 0.8054 1.0637 1.0138 -0.1635 0.2305  0.1809  390 ASP B C   
8214  O O   . ASP B 390 ? 0.9018 1.1824 1.1520 -0.1683 0.2172  0.1762  390 ASP B O   
8215  C CB  . ASP B 390 ? 0.7611 0.9338 0.9194 -0.1993 0.2157  0.2019  390 ASP B CB  
8216  C CG  . ASP B 390 ? 0.8906 1.0818 1.0651 -0.2264 0.2341  0.2026  390 ASP B CG  
8217  O OD1 . ASP B 390 ? 1.0728 1.3122 1.2737 -0.2243 0.2528  0.1946  390 ASP B OD1 
8218  O OD2 . ASP B 390 ? 1.1447 1.3004 1.3067 -0.2489 0.2311  0.2108  390 ASP B OD2 
8219  N N   . GLN B 391 ? 0.7205 1.0024 0.9251 -0.1476 0.2477  0.1743  391 GLN B N   
8220  C CA  . GLN B 391 ? 0.5745 0.9099 0.8264 -0.1321 0.2522  0.1606  391 GLN B CA  
8221  C C   . GLN B 391 ? 0.6730 1.0539 0.9781 -0.1503 0.2563  0.1565  391 GLN B C   
8222  O O   . GLN B 391 ? 0.7176 1.1420 1.0697 -0.1369 0.2512  0.1463  391 GLN B O   
8223  C CB  . GLN B 391 ? 0.7001 1.0456 0.9306 -0.1134 0.2734  0.1544  391 GLN B CB  
8224  C CG  . GLN B 391 ? 0.6076 0.9150 0.7933 -0.0926 0.2668  0.1558  391 GLN B CG  
8225  C CD  . GLN B 391 ? 0.5930 0.9073 0.8017 -0.0705 0.2489  0.1475  391 GLN B CD  
8226  O OE1 . GLN B 391 ? 0.7113 1.0481 0.9630 -0.0718 0.2353  0.1436  391 GLN B OE1 
8227  N NE2 . GLN B 391 ? 0.6998 0.9922 0.8769 -0.0509 0.2484  0.1449  391 GLN B NE2 
8228  N N   . SER B 392 ? 0.8009 1.1706 1.0995 -0.1804 0.2647  0.1645  392 SER B N   
8229  C CA  . SER B 392 ? 0.8589 1.2719 1.2110 -0.2011 0.2690  0.1608  392 SER B CA  
8230  C C   . SER B 392 ? 0.8028 1.2201 1.1900 -0.2066 0.2392  0.1602  392 SER B C   
8231  O O   . SER B 392 ? 0.9217 1.3884 1.3655 -0.2119 0.2346  0.1534  392 SER B O   
8232  C CB  . SER B 392 ? 0.8373 1.2294 1.1683 -0.2336 0.2891  0.1698  392 SER B CB  
8233  O OG  . SER B 392 ? 0.9853 1.3231 1.2894 -0.2518 0.2729  0.1811  392 SER B OG  
8234  N N   . LYS B 393 ? 0.7083 1.0747 1.0620 -0.2053 0.2187  0.1673  393 LYS B N   
8235  C CA  . LYS B 393 ? 0.7164 1.0783 1.0931 -0.2114 0.1906  0.1673  393 LYS B CA  
8236  C C   . LYS B 393 ? 0.6692 1.0405 1.0579 -0.1820 0.1731  0.1609  393 LYS B C   
8237  O O   . LYS B 393 ? 0.6522 1.0106 1.0497 -0.1848 0.1497  0.1619  393 LYS B O   
8238  C CB  . LYS B 393 ? 0.8340 1.1309 1.1677 -0.2315 0.1803  0.1786  393 LYS B CB  
8239  C CG  . LYS B 393 ? 1.3170 1.5985 1.6433 -0.2640 0.1931  0.1854  393 LYS B CG  
8240  C CD  . LYS B 393 ? 1.5898 1.7979 1.8676 -0.2781 0.1812  0.1963  393 LYS B CD  
8241  C CE  . LYS B 393 ? 1.1486 1.3341 1.4179 -0.3087 0.1939  0.2044  393 LYS B CE  
8242  N NZ  . LYS B 393 ? 1.3402 1.4486 1.5587 -0.3172 0.1810  0.2148  393 LYS B NZ  
8243  N N   . VAL B 394 ? 0.6337 1.0237 1.0205 -0.1552 0.1850  0.1542  394 VAL B N   
8244  C CA  . VAL B 394 ? 0.4363 0.8302 0.8311 -0.1278 0.1714  0.1482  394 VAL B CA  
8245  C C   . VAL B 394 ? 0.4790 0.9272 0.9310 -0.1199 0.1624  0.1398  394 VAL B C   
8246  O O   . VAL B 394 ? 0.4760 0.9680 0.9593 -0.1230 0.1761  0.1346  394 VAL B O   
8247  C CB  . VAL B 394 ? 0.3689 0.7514 0.7319 -0.1025 0.1860  0.1443  394 VAL B CB  
8248  C CG1 . VAL B 394 ? 0.3088 0.6964 0.6824 -0.0754 0.1743  0.1370  394 VAL B CG1 
8249  C CG2 . VAL B 394 ? 0.6923 1.0221 1.0009 -0.1078 0.1893  0.1533  394 VAL B CG2 
8250  N N   . MET B 395 ? 0.3847 0.8302 0.8505 -0.1085 0.1396  0.1385  395 MET B N   
8251  C CA  . MET B 395 ? 0.3380 0.8304 0.8554 -0.0974 0.1248  0.1317  395 MET B CA  
8252  C C   . MET B 395 ? 0.2809 0.7429 0.7781 -0.0732 0.1042  0.1251  395 MET B C   
8253  O O   . MET B 395 ? 0.3913 0.8141 0.8666 -0.0815 0.0815  0.1246  395 MET B O   
8254  C CB  . MET B 395 ? 0.3024 0.8144 0.8549 -0.1258 0.1067  0.1345  395 MET B CB  
8255  C CG  . MET B 395 ? 0.3764 0.9474 0.9885 -0.1161 0.0923  0.1266  395 MET B CG  
8256  S SD  . MET B 395 ? 0.5595 1.1152 1.1742 -0.0955 0.0539  0.1227  395 MET B SD  
8257  C CE  . MET B 395 ? 0.6659 1.2309 1.3101 -0.1309 0.0219  0.1261  395 MET B CE  
8258  N N   . ILE B 396 ? 0.3483 0.8174 0.8413 -0.0432 0.1120  0.1173  396 ILE B N   
8259  C CA  . ILE B 396 ? 0.2612 0.6925 0.7249 -0.0201 0.0935  0.1087  396 ILE B CA  
8260  C C   . ILE B 396 ? 0.2614 0.7328 0.7686 -0.0021 0.0773  0.1024  396 ILE B C   
8261  O O   . ILE B 396 ? 0.3029 0.8176 0.8411 0.0158  0.0922  0.0989  396 ILE B O   
8262  C CB  . ILE B 396 ? 0.2605 0.6625 0.6831 0.0003  0.1099  0.1040  396 ILE B CB  
8263  C CG1 . ILE B 396 ? 0.3642 0.7290 0.7460 -0.0154 0.1220  0.1105  396 ILE B CG1 
8264  C CG2 . ILE B 396 ? 0.3779 0.7411 0.7720 0.0210  0.0923  0.0959  396 ILE B CG2 
8265  C CD1 . ILE B 396 ? 0.2687 0.6209 0.6203 -0.0013 0.1414  0.1075  396 ILE B CD1 
8266  N N   . PRO B 397 ? 0.2803 0.7369 0.7885 -0.0040 0.0467  0.1005  397 PRO B N   
8267  C CA  . PRO B 397 ? 0.2733 0.7670 0.8216 0.0160  0.0274  0.0950  397 PRO B CA  
8268  C C   . PRO B 397 ? 0.2763 0.7640 0.8116 0.0523  0.0361  0.0874  397 PRO B C   
8269  O O   . PRO B 397 ? 0.4551 0.8859 0.9346 0.0611  0.0398  0.0847  397 PRO B O   
8270  C CB  . PRO B 397 ? 0.2887 0.7393 0.8101 0.0099  -0.0069 0.0940  397 PRO B CB  
8271  C CG  . PRO B 397 ? 0.2900 0.7053 0.7822 -0.0207 -0.0042 0.0998  397 PRO B CG  
8272  C CD  . PRO B 397 ? 0.4036 0.8065 0.8729 -0.0220 0.0278  0.1027  397 PRO B CD  
8273  N N   . GLU B 398 ? 0.2784 0.8240 0.8654 0.0730  0.0401  0.0836  398 GLU B N   
8274  C CA  . GLU B 398 ? 0.2896 0.8266 0.8633 0.1099  0.0484  0.0754  398 GLU B CA  
8275  C C   . GLU B 398 ? 0.4178 0.9164 0.9682 0.1300  0.0150  0.0712  398 GLU B C   
8276  O O   . GLU B 398 ? 0.5919 1.1216 1.1768 0.1565  0.0012  0.0669  398 GLU B O   
8277  C CB  . GLU B 398 ? 0.3373 0.9521 0.9773 0.1268  0.0666  0.0726  398 GLU B CB  
8278  C CG  . GLU B 398 ? 0.5252 1.1295 1.1449 0.1615  0.0884  0.0640  398 GLU B CG  
8279  C CD  . GLU B 398 ? 1.0405 1.6942 1.6954 0.1677  0.1116  0.0530  398 GLU B CD  
8280  O OE1 . GLU B 398 ? 0.9956 1.7026 1.7023 0.1483  0.1096  0.0527  398 GLU B OE1 
8281  O OE2 . GLU B 398 ? 1.4560 2.0923 2.0850 0.1910  0.1322  0.0441  398 GLU B OE2 
8282  N N   . LEU B 399 ? 0.4497 0.8799 0.9406 0.1181  0.0023  0.0729  399 LEU B N   
8283  C CA  . LEU B 399 ? 0.3418 0.7248 0.7981 0.1322  -0.0275 0.0705  399 LEU B CA  
8284  C C   . LEU B 399 ? 0.5064 0.8099 0.8875 0.1292  -0.0224 0.0698  399 LEU B C   
8285  O O   . LEU B 399 ? 0.4343 0.7077 0.7877 0.1045  -0.0218 0.0737  399 LEU B O   
8286  C CB  . LEU B 399 ? 0.3475 0.7396 0.8210 0.1122  -0.0574 0.0746  399 LEU B CB  
8287  C CG  . LEU B 399 ? 0.3439 0.8165 0.8972 0.1133  -0.0713 0.0752  399 LEU B CG  
8288  C CD1 . LEU B 399 ? 0.3420 0.8262 0.9121 0.0783  -0.0889 0.0803  399 LEU B CD1 
8289  C CD2 . LEU B 399 ? 0.3725 0.8524 0.9394 0.1466  -0.1000 0.0709  399 LEU B CD2 
8290  N N   . LYS B 400 ? 0.5296 0.7992 0.8788 0.1547  -0.0188 0.0645  400 LYS B N   
8291  C CA  . LYS B 400 ? 0.3880 0.5850 0.6699 0.1526  -0.0138 0.0634  400 LYS B CA  
8292  C C   . LYS B 400 ? 0.4317 0.5862 0.6818 0.1785  -0.0344 0.0604  400 LYS B C   
8293  O O   . LYS B 400 ? 0.5823 0.7681 0.8656 0.2024  -0.0488 0.0582  400 LYS B O   
8294  C CB  . LYS B 400 ? 0.3765 0.5678 0.6442 0.1530  0.0155  0.0601  400 LYS B CB  
8295  C CG  . LYS B 400 ? 0.5750 0.7924 0.8632 0.1819  0.0260  0.0535  400 LYS B CG  
8296  C CD  . LYS B 400 ? 0.3957 0.5830 0.6478 0.1849  0.0488  0.0484  400 LYS B CD  
8297  C CE  . LYS B 400 ? 0.6364 0.8524 0.9018 0.1640  0.0713  0.0511  400 LYS B CE  
8298  N NZ  . LYS B 400 ? 1.1022 1.2925 1.3335 0.1701  0.0903  0.0449  400 LYS B NZ  
8299  N N   . CYS B 401 ? 0.6049 0.6556 0.7028 0.0218  0.2629  0.1053  401 CYS B N   
8300  C CA  . CYS B 401 ? 0.5638 0.6331 0.6930 0.0279  0.2506  0.0953  401 CYS B CA  
8301  C C   . CYS B 401 ? 0.6630 0.7214 0.7626 0.0352  0.2340  0.0911  401 CYS B C   
8302  O O   . CYS B 401 ? 0.5688 0.6129 0.6388 0.0350  0.2211  0.0969  401 CYS B O   
8303  C CB  . CYS B 401 ? 0.4934 0.5791 0.6623 0.0251  0.2352  0.0971  401 CYS B CB  
8304  S SG  . CYS B 401 ? 0.6330 0.7414 0.8462 0.0319  0.2240  0.0864  401 CYS B SG  
8305  N N   . LYS B 402 ? 0.5742 0.6392 0.6845 0.0417  0.2334  0.0807  402 LYS B N   
8306  C CA  . LYS B 402 ? 0.4567 0.5111 0.5432 0.0472  0.2173  0.0759  402 LYS B CA  
8307  C C   . LYS B 402 ? 0.5963 0.6597 0.7034 0.0476  0.1947  0.0781  402 LYS B C   
8308  O O   . LYS B 402 ? 0.6744 0.7537 0.8179 0.0470  0.1920  0.0783  402 LYS B O   
8309  C CB  . LYS B 402 ? 0.4297 0.4844 0.5196 0.0539  0.2251  0.0640  402 LYS B CB  
8310  C CG  . LYS B 402 ? 0.6723 0.7126 0.7309 0.0551  0.2477  0.0604  402 LYS B CG  
8311  C CD  . LYS B 402 ? 0.7658 0.7967 0.8109 0.0629  0.2493  0.0477  402 LYS B CD  
8312  C CE  . LYS B 402 ? 0.8748 0.8933 0.8944 0.0654  0.2762  0.0423  402 LYS B CE  
8313  N NZ  . LYS B 402 ? 1.1945 1.2029 1.2029 0.0739  0.2779  0.0283  402 LYS B NZ  
8314  N N   . ALA B 403 ? 0.5570 0.6098 0.6411 0.0488  0.1785  0.0794  403 ALA B N   
8315  C CA  . ALA B 403 ? 0.4053 0.4651 0.5063 0.0491  0.1602  0.0818  403 ALA B CA  
8316  C C   . ALA B 403 ? 0.5404 0.5912 0.6244 0.0515  0.1463  0.0783  403 ALA B C   
8317  O O   . ALA B 403 ? 0.6239 0.6610 0.6770 0.0518  0.1458  0.0765  403 ALA B O   
8318  C CB  . ALA B 403 ? 0.4125 0.4726 0.5132 0.0451  0.1552  0.0917  403 ALA B CB  
8319  N N   . ILE B 404 ? 0.5043 0.5616 0.6081 0.0527  0.1348  0.0773  404 ILE B N   
8320  C CA  . ILE B 404 ? 0.5717 0.6227 0.6678 0.0533  0.1217  0.0745  404 ILE B CA  
8321  C C   . ILE B 404 ? 0.4802 0.5365 0.5852 0.0513  0.1106  0.0822  404 ILE B C   
8322  O O   . ILE B 404 ? 0.5403 0.6047 0.6640 0.0513  0.1110  0.0862  404 ILE B O   
8323  C CB  . ILE B 404 ? 0.6017 0.6526 0.7128 0.0564  0.1203  0.0670  404 ILE B CB  
8324  C CG1 . ILE B 404 ? 0.6102 0.6582 0.7188 0.0602  0.1340  0.0588  404 ILE B CG1 
8325  C CG2 . ILE B 404 ? 0.5946 0.6367 0.6973 0.0550  0.1078  0.0637  404 ILE B CG2 
8326  C CD1 . ILE B 404 ? 0.8386 0.8840 0.9614 0.0649  0.1328  0.0509  404 ILE B CD1 
8327  N N   . LEU B 405 ? 0.5330 0.5843 0.6251 0.0500  0.1004  0.0835  405 LEU B N   
8328  C CA  . LEU B 405 ? 0.5781 0.6352 0.6806 0.0490  0.0914  0.0902  405 LEU B CA  
8329  C C   . LEU B 405 ? 0.5355 0.5905 0.6375 0.0476  0.0791  0.0873  405 LEU B C   
8330  O O   . LEU B 405 ? 0.5909 0.6390 0.6862 0.0471  0.0770  0.0797  405 LEU B O   
8331  C CB  . LEU B 405 ? 0.4851 0.5414 0.5777 0.0490  0.0926  0.0977  405 LEU B CB  
8332  C CG  . LEU B 405 ? 0.5921 0.6376 0.6571 0.0494  0.0886  0.0986  405 LEU B CG  
8333  C CD1 . LEU B 405 ? 0.6200 0.6637 0.6799 0.0502  0.0869  0.1075  405 LEU B CD1 
8334  C CD2 . LEU B 405 ? 0.5608 0.5962 0.6041 0.0494  0.0997  0.0942  405 LEU B CD2 
8335  N N   . GLY B 406 ? 0.5317 0.5928 0.6434 0.0471  0.0713  0.0926  406 GLY B N   
8336  C CA  . GLY B 406 ? 0.5354 0.5981 0.6547 0.0449  0.0594  0.0900  406 GLY B CA  
8337  C C   . GLY B 406 ? 0.4879 0.5561 0.6315 0.0423  0.0604  0.0900  406 GLY B C   
8338  O O   . GLY B 406 ? 0.5909 0.6592 0.7442 0.0387  0.0528  0.0862  406 GLY B O   
8339  N N   . TYR B 407 ? 0.4723 0.5434 0.6248 0.0438  0.0692  0.0943  407 TYR B N   
8340  C CA  . TYR B 407 ? 0.2701 0.3421 0.4393 0.0421  0.0716  0.0958  407 TYR B CA  
8341  C C   . TYR B 407 ? 0.3889 0.4694 0.5739 0.0410  0.0707  0.1017  407 TYR B C   
8342  O O   . TYR B 407 ? 0.4478 0.5299 0.6357 0.0435  0.0770  0.1071  407 TYR B O   
8343  C CB  . TYR B 407 ? 0.3632 0.4314 0.5312 0.0451  0.0793  0.0972  407 TYR B CB  
8344  C CG  . TYR B 407 ? 0.5091 0.5706 0.6699 0.0465  0.0812  0.0904  407 TYR B CG  
8345  C CD1 . TYR B 407 ? 0.5618 0.6152 0.7260 0.0451  0.0794  0.0854  407 TYR B CD1 
8346  C CD2 . TYR B 407 ? 0.5989 0.6614 0.7507 0.0490  0.0860  0.0886  407 TYR B CD2 
8347  C CE1 . TYR B 407 ? 0.5574 0.6039 0.7157 0.0477  0.0819  0.0782  407 TYR B CE1 
8348  C CE2 . TYR B 407 ? 0.6149 0.6726 0.7627 0.0511  0.0902  0.0817  407 TYR B CE2 
8349  C CZ  . TYR B 407 ? 0.5758 0.6254 0.7264 0.0512  0.0879  0.0761  407 TYR B CZ  
8350  O OH  . TYR B 407 ? 0.7084 0.7522 0.8556 0.0546  0.0926  0.0684  407 TYR B OH  
8351  N N   . SER B 408 ? 0.4499 0.5355 0.6460 0.0376  0.0628  0.0998  408 SER B N   
8352  C CA  . SER B 408 ? 0.4804 0.5768 0.6985 0.0365  0.0632  0.1046  408 SER B CA  
8353  C C   . SER B 408 ? 0.5166 0.6094 0.7478 0.0323  0.0711  0.1062  408 SER B C   
8354  O O   . SER B 408 ? 0.5046 0.5863 0.7276 0.0307  0.0723  0.1030  408 SER B O   
8355  C CB  . SER B 408 ? 0.5066 0.6112 0.7372 0.0339  0.0500  0.1012  408 SER B CB  
8356  O OG  . SER B 408 ? 0.4480 0.5457 0.6768 0.0286  0.0424  0.0936  408 SER B OG  
8357  N N   . VAL B 409 ? 0.5797 0.6804 0.8309 0.0309  0.0773  0.1114  409 VAL B N   
8358  C CA  . VAL B 409 ? 0.4967 0.5906 0.7567 0.0265  0.0869  0.1145  409 VAL B CA  
8359  C C   . VAL B 409 ? 0.5807 0.6705 0.8516 0.0185  0.0800  0.1088  409 VAL B C   
8360  O O   . VAL B 409 ? 0.6481 0.7234 0.9126 0.0160  0.0841  0.1087  409 VAL B O   
8361  C CB  . VAL B 409 ? 0.4985 0.6012 0.7776 0.0262  0.0981  0.1211  409 VAL B CB  
8362  C CG1 . VAL B 409 ? 0.4317 0.5236 0.7158 0.0208  0.1100  0.1255  409 VAL B CG1 
8363  C CG2 . VAL B 409 ? 0.5510 0.6534 0.8151 0.0346  0.1044  0.1253  409 VAL B CG2 
8364  N N   . GLU B 410 ? 0.5580 0.6583 0.8433 0.0151  0.0676  0.1034  410 GLU B N   
8365  C CA  . GLU B 410 ? 0.4473 0.5427 0.7423 0.0072  0.0580  0.0961  410 GLU B CA  
8366  C C   . GLU B 410 ? 0.5463 0.6234 0.8136 0.0092  0.0550  0.0899  410 GLU B C   
8367  O O   . GLU B 410 ? 0.6574 0.7217 0.9272 0.0040  0.0552  0.0865  410 GLU B O   
8368  C CB  . GLU B 410 ? 0.3350 0.4435 0.6437 0.0055  0.0411  0.0904  410 GLU B CB  
8369  C CG  . GLU B 410 ? 0.5993 0.7286 0.9462 0.0027  0.0419  0.0945  410 GLU B CG  
8370  C CD  . GLU B 410 ? 0.6647 0.8063 1.0124 0.0114  0.0478  0.1013  410 GLU B CD  
8371  O OE1 . GLU B 410 ? 0.6341 0.7677 0.9513 0.0192  0.0502  0.1031  410 GLU B OE1 
8372  O OE2 . GLU B 410 ? 0.7005 0.8599 1.0819 0.0104  0.0505  0.1044  410 GLU B OE2 
8373  N N   . GLU B 411 ? 0.5124 0.5877 0.7549 0.0167  0.0534  0.0884  411 GLU B N   
8374  C CA  . GLU B 411 ? 0.4942 0.5547 0.7131 0.0197  0.0530  0.0821  411 GLU B CA  
8375  C C   . GLU B 411 ? 0.5218 0.5722 0.7363 0.0224  0.0639  0.0860  411 GLU B C   
8376  O O   . GLU B 411 ? 0.6089 0.6453 0.8166 0.0224  0.0637  0.0807  411 GLU B O   
8377  C CB  . GLU B 411 ? 0.4613 0.5236 0.6579 0.0261  0.0507  0.0804  411 GLU B CB  
8378  C CG  . GLU B 411 ? 0.5848 0.6338 0.7595 0.0294  0.0526  0.0731  411 GLU B CG  
8379  C CD  . GLU B 411 ? 0.7542 0.7904 0.9234 0.0257  0.0445  0.0626  411 GLU B CD  
8380  O OE1 . GLU B 411 ? 0.8283 0.8656 1.0145 0.0188  0.0362  0.0608  411 GLU B OE1 
8381  O OE2 . GLU B 411 ? 0.8061 0.8309 0.9553 0.0295  0.0470  0.0556  411 GLU B OE2 
8382  N N   . ILE B 412 ? 0.5173 0.5724 0.7341 0.0255  0.0725  0.0947  412 ILE B N   
8383  C CA  . ILE B 412 ? 0.4860 0.5295 0.6960 0.0289  0.0803  0.0990  412 ILE B CA  
8384  C C   . ILE B 412 ? 0.6041 0.6352 0.8241 0.0228  0.0822  0.0998  412 ILE B C   
8385  O O   . ILE B 412 ? 0.5997 0.6153 0.8120 0.0246  0.0821  0.0975  412 ILE B O   
8386  C CB  . ILE B 412 ? 0.4106 0.4591 0.6180 0.0329  0.0876  0.1075  412 ILE B CB  
8387  C CG1 . ILE B 412 ? 0.4245 0.4801 0.6203 0.0388  0.0859  0.1063  412 ILE B CG1 
8388  C CG2 . ILE B 412 ? 0.3776 0.4108 0.5771 0.0354  0.0938  0.1129  412 ILE B CG2 
8389  C CD1 . ILE B 412 ? 0.6110 0.6733 0.8063 0.0415  0.0901  0.1124  412 ILE B CD1 
8390  N N   . ILE B 413 ? 0.4874 0.5253 0.7269 0.0154  0.0837  0.1028  413 ILE B N   
8391  C CA  . ILE B 413 ? 0.4619 0.4881 0.7146 0.0072  0.0867  0.1043  413 ILE B CA  
8392  C C   . ILE B 413 ? 0.5912 0.6059 0.8422 0.0040  0.0767  0.0938  413 ILE B C   
8393  O O   . ILE B 413 ? 0.7727 0.7676 1.0186 0.0032  0.0789  0.0938  413 ILE B O   
8394  C CB  . ILE B 413 ? 0.4954 0.5358 0.7764 -0.0010 0.0909  0.1085  413 ILE B CB  
8395  C CG1 . ILE B 413 ? 0.5178 0.5598 0.7969 0.0021  0.1061  0.1197  413 ILE B CG1 
8396  C CG2 . ILE B 413 ? 0.5028 0.5338 0.8035 -0.0123 0.0903  0.1067  413 ILE B CG2 
8397  C CD1 . ILE B 413 ? 0.4548 0.5169 0.7617 -0.0020 0.1119  0.1231  413 ILE B CD1 
8398  N N   . ASN B 414 ? 0.5461 0.5699 0.7978 0.0030  0.0654  0.0849  414 ASN B N   
8399  C CA  . ASN B 414 ? 0.6224 0.6329 0.8675 0.0007  0.0557  0.0734  414 ASN B CA  
8400  C C   . ASN B 414 ? 0.5660 0.5595 0.7894 0.0089  0.0593  0.0703  414 ASN B C   
8401  O O   . ASN B 414 ? 0.6576 0.6326 0.8785 0.0071  0.0568  0.0640  414 ASN B O   
8402  C CB  . ASN B 414 ? 0.5946 0.6149 0.8331 0.0013  0.0432  0.0649  414 ASN B CB  
8403  C CG  . ASN B 414 ? 0.7683 0.8021 1.0321 -0.0074 0.0335  0.0640  414 ASN B CG  
8404  O OD1 . ASN B 414 ? 0.8391 0.8798 1.1303 -0.0143 0.0390  0.0705  414 ASN B OD1 
8405  N ND2 . ASN B 414 ? 0.8732 0.9109 1.1290 -0.0070 0.0189  0.0558  414 ASN B ND2 
8406  N N   . LYS B 415 ? 0.5312 0.5312 0.7416 0.0180  0.0649  0.0741  415 LYS B N   
8407  C CA  . LYS B 415 ? 0.5939 0.5827 0.7902 0.0267  0.0683  0.0713  415 LYS B CA  
8408  C C   . LYS B 415 ? 0.6861 0.6594 0.8852 0.0282  0.0735  0.0782  415 LYS B C   
8409  O O   . LYS B 415 ? 0.7233 0.6806 0.9166 0.0331  0.0730  0.0739  415 LYS B O   
8410  C CB  . LYS B 415 ? 0.3336 0.3359 0.5202 0.0345  0.0718  0.0732  415 LYS B CB  
8411  C CG  . LYS B 415 ? 0.5444 0.5527 0.7191 0.0358  0.0683  0.0648  415 LYS B CG  
8412  C CD  . LYS B 415 ? 0.8744 0.8825 1.0386 0.0444  0.0743  0.0611  415 LYS B CD  
8413  C CE  . LYS B 415 ? 1.0416 1.0486 1.1889 0.0458  0.0740  0.0520  415 LYS B CE  
8414  N NZ  . LYS B 415 ? 1.0283 1.0403 1.1704 0.0531  0.0835  0.0507  415 LYS B NZ  
8415  N N   . LEU B 416 ? 0.6407 0.6166 0.8466 0.0247  0.0788  0.0891  416 LEU B N   
8416  C CA  . LEU B 416 ? 0.6269 0.5842 0.8293 0.0260  0.0841  0.0974  416 LEU B CA  
8417  C C   . LEU B 416 ? 0.6501 0.5872 0.8599 0.0185  0.0831  0.0954  416 LEU B C   
8418  O O   . LEU B 416 ? 0.7645 0.6794 0.9668 0.0215  0.0852  0.0998  416 LEU B O   
8419  C CB  . LEU B 416 ? 0.6513 0.6142 0.8546 0.0241  0.0923  0.1093  416 LEU B CB  
8420  C CG  . LEU B 416 ? 0.6107 0.5871 0.8041 0.0319  0.0936  0.1126  416 LEU B CG  
8421  C CD1 . LEU B 416 ? 0.5115 0.4925 0.7062 0.0290  0.1026  0.1222  416 LEU B CD1 
8422  C CD2 . LEU B 416 ? 0.3431 0.3077 0.5213 0.0422  0.0909  0.1135  416 LEU B CD2 
8423  N N   . ASP B 417 ? 0.5571 0.4999 0.7813 0.0086  0.0786  0.0890  417 ASP B N   
8424  C CA  . ASP B 417 ? 0.6485 0.5715 0.8824 -0.0003 0.0765  0.0859  417 ASP B CA  
8425  C C   . ASP B 417 ? 0.7172 0.6174 0.9380 0.0063  0.0716  0.0772  417 ASP B C   
8426  O O   . ASP B 417 ? 0.8649 0.7419 1.0897 0.0008  0.0710  0.0762  417 ASP B O   
8427  C CB  . ASP B 417 ? 0.7324 0.6679 0.9855 -0.0116 0.0685  0.0780  417 ASP B CB  
8428  C CG  . ASP B 417 ? 0.9159 0.8677 1.1936 -0.0215 0.0742  0.0865  417 ASP B CG  
8429  O OD1 . ASP B 417 ? 0.8940 0.8472 1.1697 -0.0193 0.0866  0.0988  417 ASP B OD1 
8430  O OD2 . ASP B 417 ? 0.8631 0.8259 1.1623 -0.0311 0.0661  0.0804  417 ASP B OD2 
8431  N N   . LYS B 418 ? 0.6623 0.5683 0.8693 0.0178  0.0693  0.0709  418 LYS B N   
8432  C CA  . LYS B 418 ? 0.6179 0.5046 0.8152 0.0259  0.0664  0.0617  418 LYS B CA  
8433  C C   . LYS B 418 ? 0.7445 0.6123 0.9364 0.0342  0.0701  0.0700  418 LYS B C   
8434  O O   . LYS B 418 ? 0.8933 0.7411 1.0808 0.0409  0.0677  0.0636  418 LYS B O   
8435  C CB  . LYS B 418 ? 0.7779 0.6786 0.9651 0.0349  0.0651  0.0516  418 LYS B CB  
8436  C CG  . LYS B 418 ? 1.0156 0.9332 1.2016 0.0284  0.0604  0.0451  418 LYS B CG  
8437  C CD  . LYS B 418 ? 0.8693 0.7726 1.0568 0.0192  0.0517  0.0345  418 LYS B CD  
8438  C CE  . LYS B 418 ? 1.0740 0.9945 1.2649 0.0112  0.0440  0.0318  418 LYS B CE  
8439  N NZ  . LYS B 418 ? 1.5305 1.4396 1.7068 0.0099  0.0340  0.0161  418 LYS B NZ  
8440  N N   . VAL B 419 ? 0.6242 0.4960 0.8145 0.0346  0.0751  0.0837  419 VAL B N   
8441  C CA  . VAL B 419 ? 0.5980 0.4493 0.7785 0.0428  0.0764  0.0930  419 VAL B CA  
8442  C C   . VAL B 419 ? 0.7659 0.5955 0.9457 0.0330  0.0821  0.1047  419 VAL B C   
8443  O O   . VAL B 419 ? 0.9396 0.7525 1.1060 0.0383  0.0847  0.1161  419 VAL B O   
8444  C CB  . VAL B 419 ? 0.5161 0.3823 0.6888 0.0529  0.0766  0.0990  419 VAL B CB  
8445  C CG1 . VAL B 419 ? 0.6304 0.5171 0.8072 0.0611  0.0732  0.0879  419 VAL B CG1 
8446  C CG2 . VAL B 419 ? 0.4547 0.3360 0.6263 0.0461  0.0826  0.1084  419 VAL B CG2 
8447  N N   . VAL B 420 ? 0.7052 0.5329 0.8989 0.0193  0.0834  0.1012  420 VAL B N   
8448  C CA  . VAL B 420 ? 0.7699 0.5798 0.9687 0.0074  0.0918  0.1127  420 VAL B CA  
8449  C C   . VAL B 420 ? 0.7194 0.5012 0.9247 0.0005  0.0882  0.1069  420 VAL B C   
8450  O O   . VAL B 420 ? 0.7455 0.5346 0.9624 -0.0043 0.0806  0.0929  420 VAL B O   
8451  C CB  . VAL B 420 ? 0.6104 0.4472 0.8277 -0.0047 0.0976  0.1152  420 VAL B CB  
8452  C CG1 . VAL B 420 ? 0.5061 0.3301 0.7407 -0.0206 0.1058  0.1217  420 VAL B CG1 
8453  C CG2 . VAL B 420 ? 0.7257 0.5803 0.9332 0.0016  0.1042  0.1243  420 VAL B CG2 
8454  N N   . ASN B 421 ? 0.6763 0.4239 0.8714 0.0004  0.0929  0.1172  421 ASN B N   
8455  C CA  . ASN B 421 ? 0.6773 0.3926 0.8770 -0.0056 0.0894  0.1119  421 ASN B CA  
8456  C C   . ASN B 421 ? 0.7048 0.4261 0.9309 -0.0262 0.0925  0.1095  421 ASN B C   
8457  O O   . ASN B 421 ? 0.8553 0.5910 1.0922 -0.0357 0.1031  0.1202  421 ASN B O   
8458  C CB  . ASN B 421 ? 0.6722 0.3467 0.8527 -0.0004 0.0936  0.1252  421 ASN B CB  
8459  C CG  . ASN B 421 ? 0.8536 0.4928 1.0339 0.0002  0.0869  0.1174  421 ASN B CG  
8460  O OD1 . ASN B 421 ? 1.0744 0.7038 1.2717 -0.0150 0.0871  0.1120  421 ASN B OD1 
8461  N ND2 . ASN B 421 ? 0.8729 0.4929 1.0362 0.0178  0.0801  0.1162  421 ASN B ND2 
8462  N N   . THR B 422 ? 0.8148 0.5249 1.0519 -0.0325 0.0832  0.0953  422 THR B N   
8463  C CA  . THR B 422 ? 0.7507 0.4672 1.0172 -0.0528 0.0820  0.0905  422 THR B CA  
8464  C C   . THR B 422 ? 0.7461 0.4376 1.0227 -0.0667 0.0951  0.1057  422 THR B C   
8465  O O   . THR B 422 ? 1.0152 0.7186 1.3225 -0.0848 0.0986  0.1062  422 THR B O   
8466  C CB  . THR B 422 ? 0.6393 0.3436 0.9097 -0.0554 0.0670  0.0706  422 THR B CB  
8467  O OG1 . THR B 422 ? 0.7552 0.4747 1.0076 -0.0394 0.0590  0.0589  422 THR B OG1 
8468  C CG2 . THR B 422 ? 1.2253 0.9444 1.5267 -0.0744 0.0601  0.0622  422 THR B CG2 
8469  N N   . GLN B 423 ? 0.7313 0.3912 0.9834 -0.0583 0.1029  0.1189  423 GLN B N   
8470  C CA  . GLN B 423 ? 0.8159 0.4444 1.0714 -0.0713 0.1172  0.1348  423 GLN B CA  
8471  C C   . GLN B 423 ? 0.9211 0.5517 1.1587 -0.0671 0.1340  0.1550  423 GLN B C   
8472  O O   . GLN B 423 ? 1.0977 0.6969 1.3284 -0.0750 0.1481  0.1704  423 GLN B O   
8473  C CB  . GLN B 423 ? 0.7581 0.3368 0.9952 -0.0662 0.1127  0.1351  423 GLN B CB  
8474  C CG  . GLN B 423 ? 0.7819 0.3571 1.0152 -0.0555 0.0947  0.1145  423 GLN B CG  
8475  C CD  . GLN B 423 ? 0.9333 0.4969 1.1909 -0.0722 0.0871  0.1005  423 GLN B CD  
8476  O OE1 . GLN B 423 ? 0.9738 0.5018 1.2379 -0.0844 0.0917  0.1061  423 GLN B OE1 
8477  N NE2 . GLN B 423 ? 1.0367 0.6284 1.3065 -0.0731 0.0747  0.0820  423 GLN B NE2 
8478  N N   . ILE B 424 ? 0.7292 0.3923 0.9577 -0.0558 0.1334  0.1551  424 ILE B N   
8479  C CA  . ILE B 424 ? 0.8426 0.5055 1.0517 -0.0524 0.1496  0.1732  424 ILE B CA  
8480  C C   . ILE B 424 ? 0.9376 0.6428 1.1585 -0.0536 0.1569  0.1744  424 ILE B C   
8481  O O   . ILE B 424 ? 1.2789 0.9895 1.5155 -0.0666 0.1743  0.1841  424 ILE B O   
8482  C CB  . ILE B 424 ? 0.7173 0.3596 0.8847 -0.0314 0.1439  0.1795  424 ILE B CB  
8483  C CG1 . ILE B 424 ? 0.9231 0.5228 1.0758 -0.0252 0.1349  0.1785  424 ILE B CG1 
8484  C CG2 . ILE B 424 ? 1.0948 0.7264 1.2356 -0.0290 0.1599  0.1983  424 ILE B CG2 
8485  C CD1 . ILE B 424 ? 1.0296 0.6069 1.1445 -0.0046 0.1283  0.1863  424 ILE B CD1 
8486  N N   . GLY B 425 ? 1.0835 0.8166 1.2983 -0.0406 0.1453  0.1650  425 GLY B N   
8487  C CA  . GLY B 425 ? 0.8703 0.6396 1.0913 -0.0392 0.1513  0.1665  425 GLY B CA  
8488  C C   . GLY B 425 ? 1.0090 0.8097 1.2716 -0.0528 0.1483  0.1561  425 GLY B C   
8489  O O   . GLY B 425 ? 1.0771 0.8745 1.3550 -0.0581 0.1357  0.1439  425 GLY B O   
8490  N N   . PRO B 426 ? 0.8388 0.6688 1.1200 -0.0577 0.1585  0.1598  426 PRO B N   
8491  C CA  . PRO B 426 ? 0.6864 0.5490 1.0093 -0.0689 0.1530  0.1499  426 PRO B CA  
8492  C C   . PRO B 426 ? 0.7815 0.6693 1.1016 -0.0589 0.1342  0.1358  426 PRO B C   
8493  O O   . PRO B 426 ? 0.8131 0.6981 1.1032 -0.0444 0.1303  0.1358  426 PRO B O   
8494  C CB  . PRO B 426 ? 0.6608 0.5433 0.9990 -0.0731 0.1722  0.1606  426 PRO B CB  
8495  C CG  . PRO B 426 ? 0.8132 0.6847 1.1084 -0.0576 0.1797  0.1699  426 PRO B CG  
8496  C CD  . PRO B 426 ? 0.7846 0.6164 1.0465 -0.0516 0.1747  0.1730  426 PRO B CD  
8497  N N   . MET B 427 ? 0.6715 0.5820 1.0225 -0.0672 0.1227  0.1244  427 MET B N   
8498  C CA  . MET B 427 ? 0.5920 0.5226 0.9368 -0.0585 0.1057  0.1118  427 MET B CA  
8499  C C   . MET B 427 ? 0.7257 0.6913 1.0870 -0.0569 0.1080  0.1137  427 MET B C   
8500  O O   . MET B 427 ? 0.7422 0.7207 1.1317 -0.0656 0.1196  0.1208  427 MET B O   
8501  C CB  . MET B 427 ? 0.6731 0.6010 1.0333 -0.0667 0.0879  0.0967  427 MET B CB  
8502  C CG  . MET B 427 ? 0.8302 0.7218 1.1771 -0.0687 0.0853  0.0933  427 MET B CG  
8503  S SD  . MET B 427 ? 0.6172 0.4880 0.9187 -0.0490 0.0832  0.0918  427 MET B SD  
8504  C CE  . MET B 427 ? 0.9776 0.8626 1.2720 -0.0434 0.0642  0.0726  427 MET B CE  
8505  N N   . GLN B 428 ? 0.7227 0.7028 1.0674 -0.0456 0.0978  0.1075  428 GLN B N   
8506  C CA  . GLN B 428 ? 0.5970 0.6070 0.9522 -0.0416 0.0975  0.1085  428 GLN B CA  
8507  C C   . GLN B 428 ? 0.6444 0.6586 0.9958 -0.0376 0.1167  0.1218  428 GLN B C   
8508  O O   . GLN B 428 ? 0.7372 0.7744 1.1117 -0.0394 0.1219  0.1246  428 GLN B O   
8509  C CB  . GLN B 428 ? 0.4246 0.4569 0.8192 -0.0520 0.0871  0.1017  428 GLN B CB  
8510  C CG  . GLN B 428 ? 0.5101 0.5391 0.9002 -0.0533 0.0650  0.0868  428 GLN B CG  
8511  C CD  . GLN B 428 ? 0.7731 0.8075 1.1324 -0.0400 0.0557  0.0817  428 GLN B CD  
8512  O OE1 . GLN B 428 ? 0.8178 0.8740 1.1821 -0.0353 0.0524  0.0828  428 GLN B OE1 
8513  N NE2 . GLN B 428 ? 0.8894 0.9035 1.2172 -0.0336 0.0523  0.0761  428 GLN B NE2 
8514  N N   . THR B 429 ? 0.6630 0.6542 0.9838 -0.0311 0.1261  0.1294  429 THR B N   
8515  C CA  . THR B 429 ? 0.6705 0.6597 0.9780 -0.0259 0.1431  0.1412  429 THR B CA  
8516  C C   . THR B 429 ? 0.6750 0.6543 0.9442 -0.0116 0.1389  0.1418  429 THR B C   
8517  O O   . THR B 429 ? 0.7738 0.7441 1.0292 -0.0069 0.1267  0.1349  429 THR B O   
8518  C CB  . THR B 429 ? 0.6381 0.6046 0.9462 -0.0339 0.1611  0.1525  429 THR B CB  
8519  O OG1 . THR B 429 ? 0.8234 0.7573 1.0983 -0.0287 0.1593  0.1558  429 THR B OG1 
8520  C CG2 . THR B 429 ? 0.7238 0.6959 1.0729 -0.0503 0.1632  0.1507  429 THR B CG2 
8521  N N   . VAL B 430 ? 0.7336 0.7142 0.9870 -0.0047 0.1493  0.1492  430 VAL B N   
8522  C CA  . VAL B 430 ? 0.6193 0.5912 0.8396 0.0079  0.1444  0.1496  430 VAL B CA  
8523  C C   . VAL B 430 ? 0.7531 0.6925 0.9445 0.0117  0.1487  0.1574  430 VAL B C   
8524  O O   . VAL B 430 ? 0.6984 0.6289 0.8630 0.0221  0.1446  0.1589  430 VAL B O   
8525  C CB  . VAL B 430 ? 0.5957 0.5822 0.8096 0.0145  0.1500  0.1521  430 VAL B CB  
8526  C CG1 . VAL B 430 ? 0.7168 0.7331 0.9577 0.0124  0.1440  0.1452  430 VAL B CG1 
8527  C CG2 . VAL B 430 ? 0.5977 0.5738 0.8041 0.0133  0.1696  0.1628  430 VAL B CG2 
8528  N N   . LYS B 431 ? 0.6622 0.5822 0.8585 0.0035  0.1554  0.1624  431 LYS B N   
8529  C CA  . LYS B 431 ? 0.6975 0.5823 0.8633 0.0076  0.1590  0.1712  431 LYS B CA  
8530  C C   . LYS B 431 ? 0.7353 0.6095 0.8798 0.0199  0.1423  0.1661  431 LYS B C   
8531  O O   . LYS B 431 ? 0.7471 0.6032 0.8613 0.0292  0.1417  0.1724  431 LYS B O   
8532  C CB  . LYS B 431 ? 0.6247 0.4884 0.8014 -0.0039 0.1668  0.1763  431 LYS B CB  
8533  C CG  . LYS B 431 ? 0.7986 0.6245 0.9420 -0.0018 0.1788  0.1907  431 LYS B CG  
8534  C CD  . LYS B 431 ? 0.9017 0.7007 1.0520 -0.0121 0.1838  0.1956  431 LYS B CD  
8535  C CE  . LYS B 431 ? 1.1088 0.8808 1.2396 -0.0038 0.1683  0.1932  431 LYS B CE  
8536  N NZ  . LYS B 431 ? 1.1281 0.8617 1.2148 0.0057  0.1716  0.2063  431 LYS B NZ  
8537  N N   . PRO B 432 ? 0.6342 0.5190 0.7931 0.0209  0.1287  0.1545  432 PRO B N   
8538  C CA  . PRO B 432 ? 0.5986 0.4754 0.7418 0.0331  0.1156  0.1499  432 PRO B CA  
8539  C C   . PRO B 432 ? 0.6256 0.5127 0.7532 0.0433  0.1118  0.1505  432 PRO B C   
8540  O O   . PRO B 432 ? 0.6107 0.4825 0.7193 0.0533  0.1043  0.1525  432 PRO B O   
8541  C CB  . PRO B 432 ? 0.5676 0.4597 0.7313 0.0311  0.1063  0.1364  432 PRO B CB  
8542  C CG  . PRO B 432 ? 0.5850 0.4788 0.7694 0.0176  0.1116  0.1355  432 PRO B CG  
8543  C CD  . PRO B 432 ? 0.6496 0.5525 0.8382 0.0118  0.1243  0.1447  432 PRO B CD  
8544  N N   . LEU B 433 ? 0.7003 0.6119 0.8368 0.0409  0.1156  0.1485  433 LEU B N   
8545  C CA  . LEU B 433 ? 0.6291 0.5492 0.7519 0.0492  0.1121  0.1485  433 LEU B CA  
8546  C C   . LEU B 433 ? 0.7805 0.6780 0.8747 0.0528  0.1193  0.1594  433 LEU B C   
8547  O O   . LEU B 433 ? 0.8203 0.7071 0.8930 0.0623  0.1110  0.1604  433 LEU B O   
8548  C CB  . LEU B 433 ? 0.4784 0.4269 0.6174 0.0457  0.1147  0.1440  433 LEU B CB  
8549  C CG  . LEU B 433 ? 0.4592 0.4151 0.5854 0.0526  0.1127  0.1441  433 LEU B CG  
8550  C CD1 . LEU B 433 ? 0.3514 0.3083 0.4728 0.0604  0.0996  0.1383  433 LEU B CD1 
8551  C CD2 . LEU B 433 ? 0.5416 0.5218 0.6841 0.0490  0.1162  0.1409  433 LEU B CD2 
8552  N N   . ALA B 434 ? 0.7027 0.5921 0.7959 0.0455  0.1347  0.1673  434 ALA B N   
8553  C CA  . ALA B 434 ? 0.6805 0.5436 0.7396 0.0496  0.1438  0.1781  434 ALA B CA  
8554  C C   . ALA B 434 ? 0.7947 0.6248 0.8282 0.0559  0.1355  0.1833  434 ALA B C   
8555  O O   . ALA B 434 ? 0.8371 0.6467 0.8362 0.0650  0.1313  0.1882  434 ALA B O   
8556  C CB  . ALA B 434 ? 0.5766 0.4379 0.6429 0.0400  0.1650  0.1857  434 ALA B CB  
8557  N N   . ASP B 435 ? 0.7486 0.5719 0.7972 0.0519  0.1317  0.1817  435 ASP B N   
8558  C CA  . ASP B 435 ? 0.6780 0.4690 0.7055 0.0589  0.1228  0.1864  435 ASP B CA  
8559  C C   . ASP B 435 ? 0.7333 0.5248 0.7477 0.0730  0.1036  0.1814  435 ASP B C   
8560  O O   . ASP B 435 ? 0.8036 0.5677 0.7845 0.0818  0.0980  0.1888  435 ASP B O   
8561  C CB  . ASP B 435 ? 0.8510 0.6391 0.9024 0.0534  0.1195  0.1816  435 ASP B CB  
8562  C CG  . ASP B 435 ? 1.0466 0.8209 1.1065 0.0398  0.1355  0.1888  435 ASP B CG  
8563  O OD1 . ASP B 435 ? 1.0260 0.7958 1.0763 0.0340  0.1522  0.1980  435 ASP B OD1 
8564  O OD2 . ASP B 435 ? 0.9342 0.7017 1.0113 0.0348  0.1321  0.1846  435 ASP B OD2 
8565  N N   . VAL B 436 ? 0.7199 0.5413 0.7602 0.0752  0.0935  0.1692  436 VAL B N   
8566  C CA  . VAL B 436 ? 0.6814 0.5077 0.7180 0.0872  0.0761  0.1636  436 VAL B CA  
8567  C C   . VAL B 436 ? 0.7181 0.5418 0.7299 0.0919  0.0742  0.1671  436 VAL B C   
8568  O O   . VAL B 436 ? 0.8417 0.6537 0.8375 0.1024  0.0591  0.1671  436 VAL B O   
8569  C CB  . VAL B 436 ? 0.5847 0.4433 0.6545 0.0875  0.0693  0.1503  436 VAL B CB  
8570  C CG1 . VAL B 436 ? 0.5356 0.3902 0.6233 0.0870  0.0673  0.1451  436 VAL B CG1 
8571  C CG2 . VAL B 436 ? 0.5289 0.4158 0.6145 0.0787  0.0787  0.1460  436 VAL B CG2 
8572  N N   . LEU B 437 ? 0.6575 0.4914 0.6670 0.0849  0.0881  0.1692  437 LEU B N   
8573  C CA  . LEU B 437 ? 0.7060 0.5348 0.6896 0.0895  0.0876  0.1714  437 LEU B CA  
8574  C C   . LEU B 437 ? 0.9168 0.7055 0.8558 0.0949  0.0893  0.1827  437 LEU B C   
8575  O O   . LEU B 437 ? 0.9691 0.7435 0.8802 0.1040  0.0770  0.1830  437 LEU B O   
8576  C CB  . LEU B 437 ? 0.6110 0.4595 0.6047 0.0818  0.1037  0.1706  437 LEU B CB  
8577  C CG  . LEU B 437 ? 0.7190 0.6035 0.7476 0.0782  0.1003  0.1602  437 LEU B CG  
8578  C CD1 . LEU B 437 ? 0.5146 0.4156 0.5563 0.0706  0.1161  0.1609  437 LEU B CD1 
8579  C CD2 . LEU B 437 ? 0.6477 0.5406 0.6730 0.0852  0.0857  0.1536  437 LEU B CD2 
8580  N N   . VAL B 438 ? 0.8261 0.5951 0.7574 0.0891  0.1038  0.1920  438 VAL B N   
8581  C CA  . VAL B 438 ? 0.7800 0.5053 0.6634 0.0936  0.1085  0.2049  438 VAL B CA  
8582  C C   . VAL B 438 ? 0.8018 0.5038 0.6704 0.1047  0.0865  0.2061  438 VAL B C   
8583  O O   . VAL B 438 ? 1.0141 0.6852 0.8391 0.1144  0.0772  0.2122  438 VAL B O   
8584  C CB  . VAL B 438 ? 0.6946 0.4058 0.5779 0.0825  0.1328  0.2152  438 VAL B CB  
8585  C CG1 . VAL B 438 ? 0.7181 0.3797 0.5510 0.0870  0.1377  0.2297  438 VAL B CG1 
8586  C CG2 . VAL B 438 ? 0.7864 0.5191 0.6834 0.0736  0.1545  0.2148  438 VAL B CG2 
8587  N N   . SER B 439 ? 0.8587 0.5742 0.7617 0.1041  0.0777  0.1999  439 SER B N   
8588  C CA  . SER B 439 ? 0.9775 0.6725 0.8730 0.1158  0.0571  0.2004  439 SER B CA  
8589  C C   . SER B 439 ? 0.7935 0.4956 0.6822 0.1280  0.0343  0.1938  439 SER B C   
8590  O O   . SER B 439 ? 0.9178 0.5912 0.7797 0.1400  0.0170  0.1986  439 SER B O   
8591  C CB  . SER B 439 ? 0.8072 0.5180 0.7431 0.1132  0.0543  0.1929  439 SER B CB  
8592  O OG  . SER B 439 ? 0.8824 0.6353 0.8562 0.1111  0.0506  0.1792  439 SER B OG  
8593  N N   . GLY B 440 ? 0.8144 0.5524 0.7274 0.1250  0.0334  0.1835  440 GLY B N   
8594  C CA  . GLY B 440 ? 0.9799 0.7273 0.8923 0.1344  0.0122  0.1762  440 GLY B CA  
8595  C C   . GLY B 440 ? 0.9135 0.6957 0.8748 0.1362  0.0012  0.1637  440 GLY B C   
8596  O O   . GLY B 440 ? 0.9856 0.7820 0.9567 0.1418  -0.0149 0.1565  440 GLY B O   
8597  N N   . VAL B 441 ? 0.8628 0.6569 0.8532 0.1313  0.0099  0.1609  441 VAL B N   
8598  C CA  . VAL B 441 ? 0.7461 0.5732 0.7815 0.1326  0.0039  0.1484  441 VAL B CA  
8599  C C   . VAL B 441 ? 0.7757 0.6345 0.8270 0.1259  0.0087  0.1414  441 VAL B C   
8600  O O   . VAL B 441 ? 0.8918 0.7704 0.9650 0.1304  -0.0032 0.1333  441 VAL B O   
8601  C CB  . VAL B 441 ? 0.7586 0.5899 0.8157 0.1273  0.0151  0.1459  441 VAL B CB  
8602  C CG1 . VAL B 441 ? 0.7016 0.5658 0.7993 0.1278  0.0135  0.1330  441 VAL B CG1 
8603  C CG2 . VAL B 441 ? 0.5975 0.3948 0.6399 0.1342  0.0097  0.1527  441 VAL B CG2 
8604  N N   . LEU B 442 ? 0.6869 0.5498 0.7297 0.1157  0.0256  0.1446  442 LEU B N   
8605  C CA  . LEU B 442 ? 0.6936 0.5818 0.7470 0.1102  0.0301  0.1392  442 LEU B CA  
8606  C C   . LEU B 442 ? 0.8595 0.7297 0.8776 0.1124  0.0282  0.1447  442 LEU B C   
8607  O O   . LEU B 442 ? 0.8511 0.7034 0.8445 0.1088  0.0416  0.1529  442 LEU B O   
8608  C CB  . LEU B 442 ? 0.5693 0.4739 0.6376 0.0992  0.0479  0.1384  442 LEU B CB  
8609  C CG  . LEU B 442 ? 0.4903 0.4187 0.5923 0.0965  0.0490  0.1295  442 LEU B CG  
8610  C CD1 . LEU B 442 ? 0.5198 0.4651 0.6325 0.0863  0.0625  0.1280  442 LEU B CD1 
8611  C CD2 . LEU B 442 ? 0.6706 0.6178 0.7916 0.1013  0.0383  0.1215  442 LEU B CD2 
8612  N N   . ARG B 443 ? 0.7238 0.5975 0.7397 0.1178  0.0130  0.1399  443 ARG B N   
8613  C CA  . ARG B 443 ? 0.6749 0.5257 0.6509 0.1215  0.0084  0.1438  443 ARG B CA  
8614  C C   . ARG B 443 ? 0.8025 0.6587 0.7692 0.1139  0.0271  0.1452  443 ARG B C   
8615  O O   . ARG B 443 ? 0.8988 0.7316 0.8274 0.1166  0.0298  0.1497  443 ARG B O   
8616  C CB  . ARG B 443 ? 0.5039 0.3600 0.4857 0.1278  -0.0143 0.1361  443 ARG B CB  
8617  C CG  . ARG B 443 ? 0.6744 0.5395 0.6851 0.1345  -0.0317 0.1316  443 ARG B CG  
8618  C CD  . ARG B 443 ? 0.7141 0.5458 0.6960 0.1446  -0.0436 0.1390  443 ARG B CD  
8619  N NE  . ARG B 443 ? 0.7720 0.5690 0.7002 0.1485  -0.0473 0.1458  443 ARG B NE  
8620  C CZ  . ARG B 443 ? 1.0186 0.7798 0.9055 0.1519  -0.0418 0.1570  443 ARG B CZ  
8621  N NH1 . ARG B 443 ? 1.0010 0.7544 0.8961 0.1535  -0.0382 0.1623  443 ARG B NH1 
8622  N NH2 . ARG B 443 ? 1.0640 0.7950 0.8998 0.1537  -0.0388 0.1630  443 ARG B NH2 
8623  N N   . GLY B 444 ? 0.6646 0.5489 0.6632 0.1057  0.0393  0.1415  444 GLY B N   
8624  C CA  . GLY B 444 ? 0.6378 0.5300 0.6337 0.0996  0.0554  0.1424  444 GLY B CA  
8625  C C   . GLY B 444 ? 0.5035 0.4274 0.5365 0.0925  0.0619  0.1370  444 GLY B C   
8626  O O   . GLY B 444 ? 0.5604 0.4982 0.6184 0.0915  0.0571  0.1330  444 GLY B O   
8627  N N   . ALA B 445 ? 0.4702 0.4041 0.5053 0.0883  0.0728  0.1367  445 ALA B N   
8628  C CA  . ALA B 445 ? 0.5482 0.5088 0.6133 0.0824  0.0776  0.1323  445 ALA B CA  
8629  C C   . ALA B 445 ? 0.6455 0.6125 0.7084 0.0821  0.0792  0.1296  445 ALA B C   
8630  O O   . ALA B 445 ? 0.7112 0.6689 0.7576 0.0832  0.0884  0.1329  445 ALA B O   
8631  C CB  . ALA B 445 ? 0.3974 0.3644 0.4739 0.0766  0.0908  0.1360  445 ALA B CB  
8632  N N   . ALA B 446 ? 0.5973 0.5786 0.6768 0.0809  0.0713  0.1237  446 ALA B N   
8633  C CA  . ALA B 446 ? 0.5073 0.4924 0.5858 0.0802  0.0716  0.1210  446 ALA B CA  
8634  C C   . ALA B 446 ? 0.5822 0.5871 0.6823 0.0751  0.0783  0.1202  446 ALA B C   
8635  O O   . ALA B 446 ? 0.6237 0.6415 0.7413 0.0720  0.0783  0.1188  446 ALA B O   
8636  C CB  . ALA B 446 ? 0.5363 0.5195 0.6167 0.0817  0.0571  0.1155  446 ALA B CB  
8637  N N   . ALA B 447 ? 0.5324 0.5375 0.6286 0.0751  0.0836  0.1206  447 ALA B N   
8638  C CA  . ALA B 447 ? 0.4594 0.4796 0.5716 0.0717  0.0881  0.1207  447 ALA B CA  
8639  C C   . ALA B 447 ? 0.5679 0.5872 0.6807 0.0709  0.0832  0.1176  447 ALA B C   
8640  O O   . ALA B 447 ? 0.6802 0.6874 0.7793 0.0740  0.0832  0.1170  447 ALA B O   
8641  C CB  . ALA B 447 ? 0.4177 0.4384 0.5282 0.0732  0.0983  0.1244  447 ALA B CB  
8642  N N   . VAL B 448 ? 0.4807 0.5106 0.6084 0.0667  0.0802  0.1154  448 VAL B N   
8643  C CA  . VAL B 448 ? 0.4158 0.4444 0.5469 0.0642  0.0771  0.1133  448 VAL B CA  
8644  C C   . VAL B 448 ? 0.5873 0.6217 0.7222 0.0623  0.0834  0.1164  448 VAL B C   
8645  O O   . VAL B 448 ? 0.6030 0.6478 0.7460 0.0597  0.0863  0.1174  448 VAL B O   
8646  C CB  . VAL B 448 ? 0.4417 0.4770 0.5880 0.0604  0.0711  0.1092  448 VAL B CB  
8647  C CG1 . VAL B 448 ? 0.4037 0.4366 0.5560 0.0561  0.0691  0.1074  448 VAL B CG1 
8648  C CG2 . VAL B 448 ? 0.5751 0.6042 0.7180 0.0640  0.0617  0.1063  448 VAL B CG2 
8649  N N   . VAL B 449 ? 0.6551 0.6805 0.7815 0.0648  0.0849  0.1178  449 VAL B N   
8650  C CA  . VAL B 449 ? 0.5593 0.5866 0.6871 0.0652  0.0889  0.1214  449 VAL B CA  
8651  C C   . VAL B 449 ? 0.6125 0.6278 0.7362 0.0639  0.0869  0.1208  449 VAL B C   
8652  O O   . VAL B 449 ? 0.8574 0.8638 0.9777 0.0629  0.0822  0.1167  449 VAL B O   
8653  C CB  . VAL B 449 ? 0.5655 0.5931 0.6905 0.0713  0.0935  0.1239  449 VAL B CB  
8654  C CG1 . VAL B 449 ? 0.5700 0.6065 0.6999 0.0711  0.0957  0.1243  449 VAL B CG1 
8655  C CG2 . VAL B 449 ? 0.3424 0.3551 0.4547 0.0767  0.0952  0.1222  449 VAL B CG2 
8656  N N   . GLY B 450 ? 0.4618 0.4749 0.5850 0.0641  0.0891  0.1248  450 GLY B N   
8657  C CA  . GLY B 450 ? 0.5748 0.5730 0.6933 0.0627  0.0878  0.1249  450 GLY B CA  
8658  C C   . GLY B 450 ? 0.4832 0.4792 0.6035 0.0573  0.0899  0.1293  450 GLY B C   
8659  O O   . GLY B 450 ? 0.6144 0.6207 0.7388 0.0534  0.0925  0.1312  450 GLY B O   
8660  N N   . CYS B 451 ? 0.4908 0.4698 0.6053 0.0573  0.0894  0.1308  451 CYS B N   
8661  C CA  . CYS B 451 ? 0.7077 0.6779 0.8197 0.0519  0.0924  0.1366  451 CYS B CA  
8662  C C   . CYS B 451 ? 0.6499 0.6165 0.7719 0.0414  0.0931  0.1334  451 CYS B C   
8663  O O   . CYS B 451 ? 0.6892 0.6667 0.8223 0.0388  0.0903  0.1274  451 CYS B O   
8664  C CB  . CYS B 451 ? 0.6754 0.6267 0.7769 0.0582  0.0911  0.1401  451 CYS B CB  
8665  S SG  . CYS B 451 ? 0.6030 0.5538 0.7020 0.0702  0.0886  0.1351  451 CYS B SG  
8666  N N   . ASN B 452 ? 0.5408 0.4928 0.6612 0.0351  0.0966  0.1377  452 ASN B N   
8667  C CA  . ASN B 452 ? 0.5420 0.4914 0.6779 0.0237  0.0977  0.1346  452 ASN B CA  
8668  C C   . ASN B 452 ? 0.6644 0.5887 0.7957 0.0215  0.0944  0.1344  452 ASN B C   
8669  O O   . ASN B 452 ? 0.8949 0.8023 1.0107 0.0257  0.0967  0.1411  452 ASN B O   
8670  C CB  . ASN B 452 ? 0.6697 0.6220 0.8106 0.0145  0.1090  0.1408  452 ASN B CB  
8671  C CG  . ASN B 452 ? 0.7644 0.7401 0.9176 0.0121  0.1142  0.1386  452 ASN B CG  
8672  O OD1 . ASN B 452 ? 0.8228 0.8014 0.9661 0.0120  0.1229  0.1441  452 ASN B OD1 
8673  N ND2 . ASN B 452 ? 0.9162 0.9069 1.0896 0.0106  0.1087  0.1302  452 ASN B ND2 
8674  N N   . ASN B 453 ? 0.6626 0.5829 0.8067 0.0156  0.0876  0.1264  453 ASN B N   
8675  C CA  . ASN B 453 ? 0.6227 0.5165 0.7621 0.0128  0.0833  0.1246  453 ASN B CA  
8676  C C   . ASN B 453 ? 0.6198 0.5094 0.7819 -0.0027 0.0834  0.1223  453 ASN B C   
8677  O O   . ASN B 453 ? 0.7518 0.6589 0.9358 -0.0085 0.0786  0.1154  453 ASN B O   
8678  C CB  . ASN B 453 ? 0.6003 0.4879 0.7295 0.0218  0.0721  0.1150  453 ASN B CB  
8679  C CG  . ASN B 453 ? 0.7123 0.5695 0.8258 0.0257  0.0681  0.1126  453 ASN B CG  
8680  O OD1 . ASN B 453 ? 0.8946 0.7334 1.0120 0.0176  0.0693  0.1149  453 ASN B OD1 
8681  N ND2 . ASN B 453 ? 0.6092 0.4588 0.7044 0.0384  0.0647  0.1080  453 ASN B ND2 
8682  N N   . PRO B 454 ? 0.5989 0.4658 0.7590 -0.0100 0.0885  0.1278  454 PRO B N   
8683  C CA  . PRO B 454 ? 0.6896 0.5540 0.8768 -0.0267 0.0897  0.1255  454 PRO B CA  
8684  C C   . PRO B 454 ? 0.7772 0.6424 0.9815 -0.0305 0.0733  0.1116  454 PRO B C   
8685  O O   . PRO B 454 ? 0.9792 0.8530 1.2152 -0.0443 0.0721  0.1077  454 PRO B O   
8686  C CB  . PRO B 454 ? 0.5062 0.3382 0.6807 -0.0312 0.0957  0.1336  454 PRO B CB  
8687  C CG  . PRO B 454 ? 0.6406 0.4657 0.7853 -0.0181 0.1013  0.1433  454 PRO B CG  
8688  C CD  . PRO B 454 ? 0.6606 0.5028 0.7962 -0.0036 0.0931  0.1369  454 PRO B CD  
8689  N N   . LYS B 455 ? 0.6130 0.4696 0.7969 -0.0185 0.0608  0.1039  455 LYS B N   
8690  C CA  . LYS B 455 ? 0.6902 0.5435 0.8822 -0.0205 0.0427  0.0900  455 LYS B CA  
8691  C C   . LYS B 455 ? 0.6638 0.5491 0.8810 -0.0232 0.0380  0.0857  455 LYS B C   
8692  O O   . LYS B 455 ? 0.7606 0.6474 0.9960 -0.0291 0.0226  0.0753  455 LYS B O   
8693  C CB  . LYS B 455 ? 0.5395 0.3739 0.6967 -0.0053 0.0341  0.0840  455 LYS B CB  
8694  C CG  . LYS B 455 ? 0.8880 0.6965 1.0199 0.0025  0.0418  0.0899  455 LYS B CG  
8695  C CD  . LYS B 455 ? 0.7681 0.5583 0.8690 0.0175  0.0360  0.0829  455 LYS B CD  
8696  C CE  . LYS B 455 ? 0.8540 0.6112 0.9380 0.0219  0.0389  0.0844  455 LYS B CE  
8697  N NZ  . LYS B 455 ? 0.7320 0.4773 0.7873 0.0399  0.0407  0.0813  455 LYS B NZ  
8698  N N   . VAL B 456 ? 0.6675 0.5759 0.8856 -0.0184 0.0492  0.0927  456 VAL B N   
8699  C CA  . VAL B 456 ? 0.5283 0.4663 0.7690 -0.0190 0.0468  0.0896  456 VAL B CA  
8700  C C   . VAL B 456 ? 0.6965 0.6530 0.9624 -0.0286 0.0642  0.0973  456 VAL B C   
8701  O O   . VAL B 456 ? 0.7540 0.7019 1.0053 -0.0291 0.0789  0.1073  456 VAL B O   
8702  C CB  . VAL B 456 ? 0.4901 0.4364 0.7067 -0.0042 0.0462  0.0906  456 VAL B CB  
8703  C CG1 . VAL B 456 ? 0.6582 0.6300 0.8957 -0.0034 0.0406  0.0863  456 VAL B CG1 
8704  C CG2 . VAL B 456 ? 0.5980 0.5218 0.7823 0.0064  0.0358  0.0856  456 VAL B CG2 
8705  N N   . VAL B 457 ? 0.7562 0.7373 1.0588 -0.0352 0.0627  0.0927  457 VAL B N   
8706  C CA  . VAL B 457 ? 0.4954 0.4954 0.8235 -0.0439 0.0817  0.0988  457 VAL B CA  
8707  C C   . VAL B 457 ? 0.6615 0.6696 0.9652 -0.0336 0.0937  0.1059  457 VAL B C   
8708  O O   . VAL B 457 ? 0.7303 0.7495 1.0274 -0.0234 0.0856  0.1019  457 VAL B O   
8709  C CB  . VAL B 457 ? 0.3727 0.3997 0.7489 -0.0505 0.0761  0.0906  457 VAL B CB  
8710  C CG1 . VAL B 457 ? 0.5305 0.5783 0.9316 -0.0573 0.0991  0.0964  457 VAL B CG1 
8711  C CG2 . VAL B 457 ? 0.3908 0.4102 0.7948 -0.0620 0.0618  0.0828  457 VAL B CG2 
8712  N N   . GLN B 458 ? 0.6255 0.6252 0.9132 -0.0360 0.1116  0.1163  458 GLN B N   
8713  C CA  . GLN B 458 ? 0.5199 0.5240 0.7817 -0.0267 0.1209  0.1225  458 GLN B CA  
8714  C C   . GLN B 458 ? 0.6237 0.6540 0.8995 -0.0214 0.1208  0.1174  458 GLN B C   
8715  O O   . GLN B 458 ? 0.5721 0.6205 0.8800 -0.0280 0.1278  0.1143  458 GLN B O   
8716  C CB  . GLN B 458 ? 0.6208 0.6149 0.8702 -0.0326 0.1409  0.1335  458 GLN B CB  
8717  C CG  . GLN B 458 ? 0.5528 0.5339 0.7614 -0.0225 0.1435  0.1414  458 GLN B CG  
8718  C CD  . GLN B 458 ? 0.7357 0.7301 0.9353 -0.0189 0.1547  0.1439  458 GLN B CD  
8719  O OE1 . GLN B 458 ? 0.7716 0.7817 0.9922 -0.0248 0.1664  0.1418  458 GLN B OE1 
8720  N NE2 . GLN B 458 ? 0.9000 0.8877 1.0688 -0.0087 0.1512  0.1478  458 GLN B NE2 
8721  N N   . ASP B 459 ? 0.6399 0.6713 0.8936 -0.0093 0.1129  0.1163  459 ASP B N   
8722  C CA  . ASP B 459 ? 0.5549 0.6055 0.8153 -0.0026 0.1111  0.1121  459 ASP B CA  
8723  C C   . ASP B 459 ? 0.6050 0.6689 0.8934 -0.0021 0.0972  0.1027  459 ASP B C   
8724  O O   . ASP B 459 ? 0.6776 0.7521 0.9666 0.0054  0.0922  0.0994  459 ASP B O   
8725  C CB  . ASP B 459 ? 0.6704 0.7328 0.9362 -0.0052 0.1291  0.1153  459 ASP B CB  
8726  C CG  . ASP B 459 ? 0.7684 0.8204 0.9990 -0.0001 0.1369  0.1225  459 ASP B CG  
8727  O OD1 . ASP B 459 ? 0.5792 0.6149 0.7858 0.0038  0.1308  0.1268  459 ASP B OD1 
8728  O OD2 . ASP B 459 ? 0.7225 0.7825 0.9500 0.0008  0.1483  0.1232  459 ASP B OD2 
8729  N N   . SER B 460 ? 0.5859 0.6474 0.8965 -0.0099 0.0893  0.0983  460 SER B N   
8730  C CA  . SER B 460 ? 0.5343 0.6074 0.8719 -0.0091 0.0727  0.0891  460 SER B CA  
8731  C C   . SER B 460 ? 0.6141 0.6798 0.9272 0.0030  0.0561  0.0856  460 SER B C   
8732  O O   . SER B 460 ? 0.6097 0.6886 0.9331 0.0091  0.0501  0.0821  460 SER B O   
8733  C CB  . SER B 460 ? 0.3838 0.4507 0.7443 -0.0196 0.0637  0.0844  460 SER B CB  
8734  O OG  . SER B 460 ? 0.8839 0.9659 1.2779 -0.0200 0.0473  0.0752  460 SER B OG  
8735  N N   . ALA B 461 ? 0.5665 0.6099 0.8472 0.0069  0.0499  0.0869  461 ALA B N   
8736  C CA  . ALA B 461 ? 0.5810 0.6146 0.8355 0.0178  0.0375  0.0844  461 ALA B CA  
8737  C C   . ALA B 461 ? 0.5989 0.6406 0.8396 0.0258  0.0460  0.0890  461 ALA B C   
8738  O O   . ALA B 461 ? 0.6852 0.7283 0.9203 0.0330  0.0372  0.0865  461 ALA B O   
8739  C CB  . ALA B 461 ? 0.7011 0.7093 0.9245 0.0206  0.0335  0.0847  461 ALA B CB  
8740  N N   . HIS B 462 ? 0.6185 0.6632 0.8522 0.0246  0.0619  0.0958  462 HIS B N   
8741  C CA  . HIS B 462 ? 0.4833 0.5349 0.7052 0.0309  0.0689  0.0993  462 HIS B CA  
8742  C C   . HIS B 462 ? 0.6066 0.6754 0.8500 0.0323  0.0677  0.0955  462 HIS B C   
8743  O O   . HIS B 462 ? 0.5302 0.5991 0.7651 0.0394  0.0622  0.0946  462 HIS B O   
8744  C CB  . HIS B 462 ? 0.5013 0.5533 0.7147 0.0283  0.0837  0.1060  462 HIS B CB  
8745  C CG  . HIS B 462 ? 0.5013 0.5371 0.6914 0.0306  0.0848  0.1108  462 HIS B CG  
8746  N ND1 . HIS B 462 ? 0.7313 0.7589 0.9030 0.0384  0.0794  0.1108  462 HIS B ND1 
8747  C CD2 . HIS B 462 ? 0.6449 0.6711 0.8284 0.0266  0.0915  0.1159  462 HIS B CD2 
8748  C CE1 . HIS B 462 ? 0.8213 0.8370 0.9794 0.0397  0.0825  0.1150  462 HIS B CE1 
8749  N NE2 . HIS B 462 ? 0.6078 0.6210 0.7711 0.0330  0.0887  0.1185  462 HIS B NE2 
8750  N N   . ILE B 463 ? 0.5911 0.6737 0.8635 0.0256  0.0737  0.0935  463 ILE B N   
8751  C CA  . ILE B 463 ? 0.4554 0.5558 0.7529 0.0278  0.0744  0.0893  463 ILE B CA  
8752  C C   . ILE B 463 ? 0.5513 0.6531 0.8614 0.0326  0.0550  0.0831  463 ILE B C   
8753  O O   . ILE B 463 ? 0.5790 0.6850 0.8896 0.0402  0.0504  0.0815  463 ILE B O   
8754  C CB  . ILE B 463 ? 0.3101 0.4252 0.6373 0.0193  0.0890  0.0887  463 ILE B CB  
8755  C CG1 . ILE B 463 ? 0.4049 0.5136 0.7108 0.0159  0.1076  0.0957  463 ILE B CG1 
8756  C CG2 . ILE B 463 ? 0.4958 0.6306 0.8536 0.0227  0.0909  0.0833  463 ILE B CG2 
8757  C CD1 . ILE B 463 ? 0.4466 0.5519 0.7255 0.0232  0.1122  0.0983  463 ILE B CD1 
8758  N N   . GLU B 464 ? 0.4673 0.5630 0.7854 0.0287  0.0422  0.0796  464 GLU B N   
8759  C CA  . GLU B 464 ? 0.4841 0.5783 0.8105 0.0338  0.0205  0.0733  464 GLU B CA  
8760  C C   . GLU B 464 ? 0.5206 0.5966 0.8082 0.0441  0.0116  0.0754  464 GLU B C   
8761  O O   . GLU B 464 ? 0.6042 0.6801 0.8940 0.0514  -0.0017 0.0726  464 GLU B O   
8762  C CB  . GLU B 464 ? 0.4461 0.5345 0.7860 0.0268  0.0069  0.0680  464 GLU B CB  
8763  C CG  . GLU B 464 ? 0.6356 0.7453 1.0253 0.0164  0.0120  0.0645  464 GLU B CG  
8764  C CD  . GLU B 464 ? 0.8483 0.9827 1.2769 0.0203  0.0098  0.0602  464 GLU B CD  
8765  O OE1 . GLU B 464 ? 0.9288 1.0622 1.3604 0.0284  -0.0113 0.0553  464 GLU B OE1 
8766  O OE2 . GLU B 464 ? 0.9510 1.1040 1.4053 0.0160  0.0295  0.0618  464 GLU B OE2 
8767  N N   . THR B 465 ? 0.4693 0.5294 0.7226 0.0451  0.0193  0.0806  465 THR B N   
8768  C CA  . THR B 465 ? 0.4577 0.5009 0.6756 0.0539  0.0151  0.0833  465 THR B CA  
8769  C C   . THR B 465 ? 0.5896 0.6410 0.8072 0.0587  0.0230  0.0867  465 THR B C   
8770  O O   . THR B 465 ? 0.6325 0.6767 0.8399 0.0658  0.0139  0.0866  465 THR B O   
8771  C CB  . THR B 465 ? 0.5153 0.5426 0.7039 0.0535  0.0233  0.0873  465 THR B CB  
8772  O OG1 . THR B 465 ? 0.6019 0.6183 0.7895 0.0494  0.0153  0.0832  465 THR B OG1 
8773  C CG2 . THR B 465 ? 0.4717 0.4829 0.6263 0.0618  0.0234  0.0906  465 THR B CG2 
8774  N N   . ILE B 466 ? 0.6039 0.6673 0.8299 0.0550  0.0391  0.0898  466 ILE B N   
8775  C CA  . ILE B 466 ? 0.4963 0.5654 0.7209 0.0588  0.0466  0.0919  466 ILE B CA  
8776  C C   . ILE B 466 ? 0.5186 0.5976 0.7665 0.0628  0.0390  0.0874  466 ILE B C   
8777  O O   . ILE B 466 ? 0.5359 0.6083 0.7741 0.0695  0.0345  0.0883  466 ILE B O   
8778  C CB  . ILE B 466 ? 0.3819 0.4602 0.6095 0.0540  0.0630  0.0945  466 ILE B CB  
8779  C CG1 . ILE B 466 ? 0.4561 0.5242 0.6608 0.0521  0.0686  0.0996  466 ILE B CG1 
8780  C CG2 . ILE B 466 ? 0.3425 0.4254 0.5699 0.0577  0.0685  0.0945  466 ILE B CG2 
8781  C CD1 . ILE B 466 ? 0.3016 0.3751 0.5073 0.0469  0.0812  0.1025  466 ILE B CD1 
8782  N N   . LYS B 467 ? 0.4851 0.5795 0.7657 0.0589  0.0381  0.0826  467 LYS B N   
8783  C CA  . LYS B 467 ? 0.4674 0.5745 0.7777 0.0636  0.0310  0.0774  467 LYS B CA  
8784  C C   . LYS B 467 ? 0.5135 0.6079 0.8143 0.0717  0.0096  0.0761  467 LYS B C   
8785  O O   . LYS B 467 ? 0.6141 0.7082 0.9191 0.0796  0.0041  0.0753  467 LYS B O   
8786  C CB  . LYS B 467 ? 0.3396 0.4667 0.6915 0.0569  0.0336  0.0724  467 LYS B CB  
8787  C CG  . LYS B 467 ? 0.3530 0.4942 0.7187 0.0517  0.0564  0.0730  467 LYS B CG  
8788  C CD  . LYS B 467 ? 0.4049 0.5629 0.8085 0.0429  0.0628  0.0698  467 LYS B CD  
8789  C CE  . LYS B 467 ? 0.4378 0.6176 0.8884 0.0463  0.0595  0.0627  467 LYS B CE  
8790  N NZ  . LYS B 467 ? 0.3584 0.5551 0.8508 0.0362  0.0638  0.0595  467 LYS B NZ  
8791  N N   . GLY B 468 ? 0.4617 0.5425 0.7462 0.0703  -0.0024 0.0758  468 GLY B N   
8792  C CA  . GLY B 468 ? 0.5222 0.5858 0.7894 0.0782  -0.0237 0.0746  468 GLY B CA  
8793  C C   . GLY B 468 ? 0.4512 0.4940 0.6791 0.0855  -0.0219 0.0810  468 GLY B C   
8794  O O   . GLY B 468 ? 0.5211 0.5527 0.7401 0.0940  -0.0358 0.0813  468 GLY B O   
8795  N N   . LEU B 469 ? 0.4809 0.5177 0.6860 0.0822  -0.0051 0.0865  469 LEU B N   
8796  C CA  . LEU B 469 ? 0.5167 0.5354 0.6890 0.0873  -0.0005 0.0929  469 LEU B CA  
8797  C C   . LEU B 469 ? 0.5949 0.6199 0.7795 0.0909  0.0039  0.0941  469 LEU B C   
8798  O O   . LEU B 469 ? 0.5568 0.5651 0.7229 0.0976  -0.0021 0.0975  469 LEU B O   
8799  C CB  . LEU B 469 ? 0.4552 0.4699 0.6083 0.0825  0.0159  0.0975  469 LEU B CB  
8800  C CG  . LEU B 469 ? 0.5502 0.5523 0.6834 0.0810  0.0133  0.0969  469 LEU B CG  
8801  C CD1 . LEU B 469 ? 0.6295 0.6369 0.7605 0.0757  0.0294  0.0998  469 LEU B CD1 
8802  C CD2 . LEU B 469 ? 0.5808 0.5559 0.6757 0.0878  0.0067  0.0997  469 LEU B CD2 
8803  N N   . ILE B 470 ? 0.5256 0.5716 0.7383 0.0868  0.0148  0.0913  470 ILE B N   
8804  C CA  . ILE B 470 ? 0.4554 0.5056 0.6791 0.0907  0.0196  0.0908  470 ILE B CA  
8805  C C   . ILE B 470 ? 0.5353 0.5863 0.7773 0.0992  0.0037  0.0870  470 ILE B C   
8806  O O   . ILE B 470 ? 0.6728 0.7137 0.9093 0.1059  0.0012  0.0887  470 ILE B O   
8807  C CB  . ILE B 470 ? 0.3524 0.4211 0.5949 0.0850  0.0362  0.0881  470 ILE B CB  
8808  C CG1 . ILE B 470 ? 0.4620 0.5505 0.7349 0.0806  0.0383  0.0829  470 ILE B CG1 
8809  C CG2 . ILE B 470 ? 0.4520 0.5158 0.6726 0.0791  0.0485  0.0928  470 ILE B CG2 
8810  C CD1 . ILE B 470 ? 0.4559 0.5594 0.7454 0.0772  0.0549  0.0799  470 ILE B CD1 
8811  N N   . LYS B 471 ? 0.4655 0.5275 0.7307 0.0992  -0.0081 0.0818  471 LYS B N   
8812  C CA  . LYS B 471 ? 0.4732 0.5369 0.7594 0.1086  -0.0268 0.0778  471 LYS B CA  
8813  C C   . LYS B 471 ? 0.5537 0.5875 0.8021 0.1170  -0.0423 0.0833  471 LYS B C   
8814  O O   . LYS B 471 ? 0.7403 0.7675 0.9938 0.1267  -0.0523 0.0835  471 LYS B O   
8815  C CB  . LYS B 471 ? 0.3862 0.4669 0.7057 0.1058  -0.0392 0.0710  471 LYS B CB  
8816  C CG  . LYS B 471 ? 0.5982 0.6932 0.9585 0.1144  -0.0542 0.0648  471 LYS B CG  
8817  C CD  . LYS B 471 ? 1.1071 1.2260 1.5058 0.1149  -0.0372 0.0608  471 LYS B CD  
8818  C CE  . LYS B 471 ? 0.6971 0.8336 1.1434 0.1239  -0.0518 0.0537  471 LYS B CE  
8819  N NZ  . LYS B 471 ? 0.6036 0.7524 1.0737 0.1298  -0.0364 0.0507  471 LYS B NZ  
8820  N N   . ASN B 472 ? 0.5424 0.5569 0.7530 0.1141  -0.0433 0.0878  472 ASN B N   
8821  C CA  . ASN B 472 ? 0.5652 0.5479 0.7338 0.1218  -0.0554 0.0936  472 ASN B CA  
8822  C C   . ASN B 472 ? 0.5931 0.5597 0.7347 0.1219  -0.0393 0.1019  472 ASN B C   
8823  O O   . ASN B 472 ? 0.8251 0.7656 0.9256 0.1234  -0.0382 0.1087  472 ASN B O   
8824  C CB  . ASN B 472 ? 0.5428 0.5098 0.6811 0.1193  -0.0623 0.0937  472 ASN B CB  
8825  C CG  . ASN B 472 ? 0.4892 0.4621 0.6465 0.1212  -0.0856 0.0858  472 ASN B CG  
8826  O OD1 . ASN B 472 ? 0.7465 0.6986 0.8827 0.1296  -0.1077 0.0856  472 ASN B OD1 
8827  N ND2 . ASN B 472 ? 0.5628 0.5628 0.7599 0.1132  -0.0822 0.0791  472 ASN B ND2 
8828  N N   . ASP B 473 ? 0.5226 0.5035 0.6872 0.1202  -0.0265 0.1011  473 ASP B N   
8829  C CA  . ASP B 473 ? 0.5762 0.5439 0.7225 0.1190  -0.0125 0.1075  473 ASP B CA  
8830  C C   . ASP B 473 ? 0.6068 0.5657 0.7253 0.1114  0.0025  0.1134  473 ASP B C   
8831  O O   . ASP B 473 ? 0.7048 0.6437 0.7989 0.1117  0.0092  0.1206  473 ASP B O   
8832  C CB  . ASP B 473 ? 0.6616 0.6026 0.7885 0.1290  -0.0243 0.1127  473 ASP B CB  
8833  C CG  . ASP B 473 ? 0.7895 0.7396 0.9481 0.1369  -0.0329 0.1077  473 ASP B CG  
8834  O OD1 . ASP B 473 ? 0.6900 0.6648 0.8818 0.1333  -0.0228 0.1011  473 ASP B OD1 
8835  O OD2 . ASP B 473 ? 0.8530 0.7834 1.0013 0.1475  -0.0492 0.1105  473 ASP B OD2 
8836  N N   . VAL B 474 ? 0.5176 0.4913 0.6423 0.1046  0.0087  0.1105  474 VAL B N   
8837  C CA  . VAL B 474 ? 0.4496 0.4186 0.5544 0.0986  0.0229  0.1151  474 VAL B CA  
8838  C C   . VAL B 474 ? 0.5230 0.5142 0.6508 0.0912  0.0367  0.1126  474 VAL B C   
8839  O O   . VAL B 474 ? 0.6770 0.6860 0.8247 0.0880  0.0366  0.1075  474 VAL B O   
8840  C CB  . VAL B 474 ? 0.5439 0.5078 0.6335 0.0981  0.0180  0.1138  474 VAL B CB  
8841  C CG1 . VAL B 474 ? 0.5208 0.4809 0.5933 0.0935  0.0337  0.1180  474 VAL B CG1 
8842  C CG2 . VAL B 474 ? 0.7113 0.6507 0.7741 0.1061  0.0013  0.1150  474 VAL B CG2 
8843  N N   . ILE B 475 ? 0.4716 0.4604 0.5963 0.0880  0.0480  0.1162  475 ILE B N   
8844  C CA  . ILE B 475 ? 0.4383 0.4452 0.5806 0.0816  0.0583  0.1134  475 ILE B CA  
8845  C C   . ILE B 475 ? 0.5668 0.5826 0.7070 0.0772  0.0634  0.1136  475 ILE B C   
8846  O O   . ILE B 475 ? 0.5407 0.5460 0.6629 0.0777  0.0655  0.1178  475 ILE B O   
8847  C CB  . ILE B 475 ? 0.5133 0.5149 0.6539 0.0785  0.0665  0.1162  475 ILE B CB  
8848  C CG1 . ILE B 475 ? 0.4577 0.4766 0.6147 0.0731  0.0729  0.1113  475 ILE B CG1 
8849  C CG2 . ILE B 475 ? 0.3245 0.3139 0.4468 0.0761  0.0739  0.1235  475 ILE B CG2 
8850  C CD1 . ILE B 475 ? 0.3459 0.3606 0.5068 0.0706  0.0765  0.1103  475 ILE B CD1 
8851  N N   . VAL B 476 ? 0.5168 0.5496 0.6737 0.0736  0.0661  0.1093  476 VAL B N   
8852  C CA  . VAL B 476 ? 0.4999 0.5387 0.6549 0.0701  0.0700  0.1099  476 VAL B CA  
8853  C C   . VAL B 476 ? 0.5270 0.5747 0.6858 0.0656  0.0786  0.1107  476 VAL B C   
8854  O O   . VAL B 476 ? 0.4949 0.5500 0.6632 0.0639  0.0808  0.1076  476 VAL B O   
8855  C CB  . VAL B 476 ? 0.3981 0.4454 0.5661 0.0691  0.0652  0.1056  476 VAL B CB  
8856  C CG1 . VAL B 476 ? 0.2878 0.3379 0.4526 0.0651  0.0697  0.1069  476 VAL B CG1 
8857  C CG2 . VAL B 476 ? 0.4601 0.4985 0.6253 0.0736  0.0529  0.1040  476 VAL B CG2 
8858  N N   . VAL B 477 ? 0.4230 0.4692 0.5738 0.0644  0.0827  0.1143  477 VAL B N   
8859  C CA  . VAL B 477 ? 0.3563 0.4108 0.5112 0.0611  0.0877  0.1153  477 VAL B CA  
8860  C C   . VAL B 477 ? 0.4361 0.4933 0.5895 0.0605  0.0881  0.1158  477 VAL B C   
8861  O O   . VAL B 477 ? 0.4889 0.5389 0.6354 0.0626  0.0864  0.1166  477 VAL B O   
8862  C CB  . VAL B 477 ? 0.3954 0.4475 0.5486 0.0607  0.0921  0.1192  477 VAL B CB  
8863  C CG1 . VAL B 477 ? 0.3475 0.3938 0.5022 0.0600  0.0923  0.1192  477 VAL B CG1 
8864  C CG2 . VAL B 477 ? 0.5092 0.5534 0.6522 0.0638  0.0954  0.1229  477 VAL B CG2 
8865  N N   . VAL B 478 ? 0.4971 0.5614 0.6538 0.0579  0.0898  0.1152  478 VAL B N   
8866  C CA  . VAL B 478 ? 0.3943 0.4581 0.5482 0.0570  0.0905  0.1168  478 VAL B CA  
8867  C C   . VAL B 478 ? 0.5317 0.5980 0.6825 0.0568  0.0915  0.1197  478 VAL B C   
8868  O O   . VAL B 478 ? 0.6003 0.6711 0.7526 0.0560  0.0906  0.1188  478 VAL B O   
8869  C CB  . VAL B 478 ? 0.3462 0.4128 0.5055 0.0539  0.0917  0.1140  478 VAL B CB  
8870  C CG1 . VAL B 478 ? 0.3921 0.4573 0.5588 0.0547  0.0876  0.1109  478 VAL B CG1 
8871  C CG2 . VAL B 478 ? 0.4498 0.5222 0.6112 0.0522  0.0951  0.1113  478 VAL B CG2 
8872  N N   . THR B 479 ? 0.4072 0.4690 0.5534 0.0580  0.0916  0.1227  479 THR B N   
8873  C CA  . THR B 479 ? 0.5836 0.6458 0.7263 0.0596  0.0903  0.1261  479 THR B CA  
8874  C C   . THR B 479 ? 0.6237 0.6769 0.7589 0.0593  0.0911  0.1291  479 THR B C   
8875  O O   . THR B 479 ? 0.7786 0.8260 0.9141 0.0581  0.0924  0.1280  479 THR B O   
8876  C CB  . THR B 479 ? 0.5351 0.6000 0.6840 0.0641  0.0897  0.1280  479 THR B CB  
8877  O OG1 . THR B 479 ? 0.6034 0.6604 0.7492 0.0673  0.0924  0.1286  479 THR B OG1 
8878  C CG2 . THR B 479 ? 0.5671 0.6390 0.7250 0.0630  0.0904  0.1262  479 THR B CG2 
8879  N N   . GLY B 480 ? 0.5270 0.5772 0.6548 0.0605  0.0890  0.1328  480 GLY B N   
8880  C CA  . GLY B 480 ? 0.6781 0.7161 0.7965 0.0604  0.0900  0.1371  480 GLY B CA  
8881  C C   . GLY B 480 ? 0.6100 0.6432 0.7254 0.0537  0.0959  0.1366  480 GLY B C   
8882  O O   . GLY B 480 ? 0.7572 0.7968 0.8739 0.0500  0.0993  0.1338  480 GLY B O   
8883  N N   . CYS B 481 ? 0.5524 0.5741 0.6660 0.0519  0.0977  0.1389  481 CYS B N   
8884  C CA  . CYS B 481 ? 0.5974 0.6154 0.7138 0.0441  0.1042  0.1387  481 CYS B CA  
8885  C C   . CYS B 481 ? 0.5668 0.5965 0.7003 0.0407  0.1050  0.1319  481 CYS B C   
8886  O O   . CYS B 481 ? 0.6637 0.6973 0.8051 0.0346  0.1115  0.1307  481 CYS B O   
8887  C CB  . CYS B 481 ? 0.4947 0.4964 0.6081 0.0421  0.1046  0.1421  481 CYS B CB  
8888  S SG  . CYS B 481 ? 0.6481 0.6319 0.7399 0.0462  0.1039  0.1516  481 CYS B SG  
8889  N N   . ALA B 482 ? 0.5313 0.5658 0.6704 0.0449  0.0990  0.1279  482 ALA B N   
8890  C CA  . ALA B 482 ? 0.4798 0.5230 0.6325 0.0434  0.0971  0.1220  482 ALA B CA  
8891  C C   . ALA B 482 ? 0.6122 0.6667 0.7685 0.0429  0.1010  0.1203  482 ALA B C   
8892  O O   . ALA B 482 ? 0.5271 0.5890 0.6969 0.0397  0.1038  0.1166  482 ALA B O   
8893  C CB  . ALA B 482 ? 0.4974 0.5382 0.6476 0.0489  0.0906  0.1196  482 ALA B CB  
8894  N N   . ALA B 483 ? 0.6261 0.6819 0.7723 0.0462  0.1007  0.1222  483 ALA B N   
8895  C CA  . ALA B 483 ? 0.4778 0.5406 0.6237 0.0459  0.1034  0.1196  483 ALA B CA  
8896  C C   . ALA B 483 ? 0.5201 0.5814 0.6614 0.0416  0.1122  0.1203  483 ALA B C   
8897  O O   . ALA B 483 ? 0.6146 0.6822 0.7630 0.0403  0.1176  0.1160  483 ALA B O   
8898  C CB  . ALA B 483 ? 0.4516 0.5143 0.5881 0.0494  0.0992  0.1211  483 ALA B CB  
8899  N N   . GLN B 484 ? 0.5910 0.6423 0.7198 0.0398  0.1148  0.1260  484 GLN B N   
8900  C CA  . GLN B 484 ? 0.5324 0.5783 0.6523 0.0352  0.1257  0.1284  484 GLN B CA  
8901  C C   . GLN B 484 ? 0.5722 0.6248 0.7143 0.0294  0.1337  0.1255  484 GLN B C   
8902  O O   . GLN B 484 ? 0.5862 0.6430 0.7319 0.0263  0.1450  0.1235  484 GLN B O   
8903  C CB  . GLN B 484 ? 0.4422 0.4720 0.5411 0.0353  0.1254  0.1365  484 GLN B CB  
8904  C CG  . GLN B 484 ? 0.4740 0.4997 0.5540 0.0413  0.1166  0.1384  484 GLN B CG  
8905  C CD  . GLN B 484 ? 0.5978 0.6065 0.6564 0.0432  0.1142  0.1468  484 GLN B CD  
8906  O OE1 . GLN B 484 ? 0.8105 0.8095 0.8701 0.0409  0.1171  0.1515  484 GLN B OE1 
8907  N NE2 . GLN B 484 ? 0.6620 0.6650 0.7005 0.0477  0.1071  0.1486  484 GLN B NE2 
8908  N N   . ALA B 485 ? 0.5358 0.5898 0.6941 0.0281  0.1275  0.1244  485 ALA B N   
8909  C CA  . ALA B 485 ? 0.5198 0.5820 0.7045 0.0226  0.1310  0.1206  485 ALA B CA  
8910  C C   . ALA B 485 ? 0.5375 0.6155 0.7398 0.0247  0.1326  0.1136  485 ALA B C   
8911  O O   . ALA B 485 ? 0.5232 0.6102 0.7447 0.0205  0.1424  0.1110  485 ALA B O   
8912  C CB  . ALA B 485 ? 0.6082 0.6670 0.8025 0.0227  0.1193  0.1188  485 ALA B CB  
8913  N N   . ALA B 486 ? 0.6275 0.7080 0.8246 0.0315  0.1238  0.1108  486 ALA B N   
8914  C CA  . ALA B 486 ? 0.4743 0.5658 0.6852 0.0351  0.1235  0.1046  486 ALA B CA  
8915  C C   . ALA B 486 ? 0.5557 0.6485 0.7580 0.0351  0.1360  0.1033  486 ALA B C   
8916  O O   . ALA B 486 ? 0.6923 0.7950 0.9122 0.0361  0.1422  0.0978  486 ALA B O   
8917  C CB  . ALA B 486 ? 0.3434 0.4322 0.5463 0.0413  0.1121  0.1037  486 ALA B CB  
8918  N N   . ALA B 487 ? 0.5885 0.6704 0.7632 0.0348  0.1390  0.1077  487 ALA B N   
8919  C CA  . ALA B 487 ? 0.5264 0.6045 0.6843 0.0352  0.1497  0.1062  487 ALA B CA  
8920  C C   . ALA B 487 ? 0.5271 0.6082 0.6945 0.0300  0.1670  0.1063  487 ALA B C   
8921  O O   . ALA B 487 ? 0.5605 0.6462 0.7317 0.0315  0.1782  0.1009  487 ALA B O   
8922  C CB  . ALA B 487 ? 0.3346 0.3984 0.4599 0.0361  0.1460  0.1117  487 ALA B CB  
8923  N N   . LYS B 488 ? 0.4603 0.5381 0.6334 0.0239  0.1704  0.1120  488 LYS B N   
8924  C CA  . LYS B 488 ? 0.4755 0.5554 0.6608 0.0167  0.1884  0.1137  488 LYS B CA  
8925  C C   . LYS B 488 ? 0.4797 0.5804 0.7080 0.0158  0.1925  0.1062  488 LYS B C   
8926  O O   . LYS B 488 ? 0.4995 0.6068 0.7394 0.0132  0.2109  0.1039  488 LYS B O   
8927  C CB  . LYS B 488 ? 0.4835 0.5534 0.6678 0.0097  0.1881  0.1215  488 LYS B CB  
8928  C CG  . LYS B 488 ? 0.4640 0.5124 0.6089 0.0114  0.1835  0.1299  488 LYS B CG  
8929  C CD  . LYS B 488 ? 0.5189 0.5537 0.6618 0.0043  0.1868  0.1380  488 LYS B CD  
8930  C CE  . LYS B 488 ? 0.6334 0.6710 0.7966 0.0038  0.1718  0.1364  488 LYS B CE  
8931  N NZ  . LYS B 488 ? 0.5830 0.6069 0.7493 -0.0044 0.1762  0.1427  488 LYS B NZ  
8932  N N   . TYR B 489 ? 0.4654 0.5758 0.7170 0.0183  0.1758  0.1024  489 TYR B N   
8933  C CA  . TYR B 489 ? 0.4225 0.5524 0.7166 0.0188  0.1745  0.0951  489 TYR B CA  
8934  C C   . TYR B 489 ? 0.4062 0.5447 0.7062 0.0265  0.1794  0.0881  489 TYR B C   
8935  O O   . TYR B 489 ? 0.4026 0.5571 0.7359 0.0265  0.1888  0.0826  489 TYR B O   
8936  C CB  . TYR B 489 ? 0.4694 0.6015 0.7772 0.0209  0.1526  0.0934  489 TYR B CB  
8937  C CG  . TYR B 489 ? 0.4105 0.5613 0.7630 0.0212  0.1470  0.0864  489 TYR B CG  
8938  C CD1 . TYR B 489 ? 0.4027 0.5623 0.7870 0.0123  0.1499  0.0858  489 TYR B CD1 
8939  C CD2 . TYR B 489 ? 0.5195 0.6783 0.8840 0.0303  0.1371  0.0804  489 TYR B CD2 
8940  C CE1 . TYR B 489 ? 0.5023 0.6811 0.9322 0.0128  0.1420  0.0786  489 TYR B CE1 
8941  C CE2 . TYR B 489 ? 0.6133 0.7891 1.0199 0.0321  0.1291  0.0740  489 TYR B CE2 
8942  C CZ  . TYR B 489 ? 0.5431 0.7303 0.9839 0.0234  0.1308  0.0727  489 TYR B CZ  
8943  O OH  . TYR B 489 ? 0.5292 0.7350 1.0159 0.0256  0.1201  0.0657  489 TYR B OH  
8944  N N   . GLY B 490 ? 0.4361 0.5642 0.7067 0.0328  0.1728  0.0878  490 GLY B N   
8945  C CA  . GLY B 490 ? 0.4119 0.5431 0.6828 0.0403  0.1760  0.0809  490 GLY B CA  
8946  C C   . GLY B 490 ? 0.4910 0.6226 0.7668 0.0475  0.1576  0.0778  490 GLY B C   
8947  O O   . GLY B 490 ? 0.6116 0.7474 0.8983 0.0541  0.1584  0.0713  490 GLY B O   
8948  N N   . LEU B 491 ? 0.3839 0.5088 0.6501 0.0468  0.1423  0.0825  491 LEU B N   
8949  C CA  . LEU B 491 ? 0.3650 0.4867 0.6313 0.0530  0.1266  0.0811  491 LEU B CA  
8950  C C   . LEU B 491 ? 0.4824 0.5920 0.7207 0.0557  0.1248  0.0818  491 LEU B C   
8951  O O   . LEU B 491 ? 0.6765 0.7822 0.9153 0.0608  0.1162  0.0800  491 LEU B O   
8952  C CB  . LEU B 491 ? 0.5060 0.6241 0.7722 0.0516  0.1127  0.0853  491 LEU B CB  
8953  C CG  . LEU B 491 ? 0.4175 0.5442 0.7085 0.0471  0.1107  0.0846  491 LEU B CG  
8954  C CD1 . LEU B 491 ? 0.4348 0.5519 0.7152 0.0462  0.0971  0.0881  491 LEU B CD1 
8955  C CD2 . LEU B 491 ? 0.3968 0.5378 0.7229 0.0511  0.1069  0.0780  491 LEU B CD2 
8956  N N   . LEU B 492 ? 0.5562 0.6586 0.7706 0.0522  0.1318  0.0845  492 LEU B N   
8957  C CA  . LEU B 492 ? 0.4634 0.5555 0.6545 0.0538  0.1280  0.0842  492 LEU B CA  
8958  C C   . LEU B 492 ? 0.5062 0.5961 0.6937 0.0571  0.1362  0.0766  492 LEU B C   
8959  O O   . LEU B 492 ? 0.6040 0.6847 0.7677 0.0562  0.1392  0.0753  492 LEU B O   
8960  C CB  . LEU B 492 ? 0.5283 0.6128 0.6954 0.0498  0.1287  0.0900  492 LEU B CB  
8961  C CG  . LEU B 492 ? 0.5220 0.6035 0.6840 0.0490  0.1180  0.0962  492 LEU B CG  
8962  C CD1 . LEU B 492 ? 0.5161 0.6022 0.6953 0.0490  0.1135  0.0982  492 LEU B CD1 
8963  C CD2 . LEU B 492 ? 0.3822 0.4570 0.5248 0.0464  0.1194  0.1017  492 LEU B CD2 
8964  N N   . GLN B 493 ? 0.4454 0.5425 0.6560 0.0616  0.1386  0.0710  493 GLN B N   
8965  C CA  . GLN B 493 ? 0.5140 0.6085 0.7239 0.0663  0.1474  0.0626  493 GLN B CA  
8966  C C   . GLN B 493 ? 0.4856 0.5783 0.7101 0.0728  0.1379  0.0586  493 GLN B C   
8967  O O   . GLN B 493 ? 0.4990 0.5965 0.7402 0.0744  0.1276  0.0620  493 GLN B O   
8968  C CB  . GLN B 493 ? 0.5116 0.6178 0.7409 0.0668  0.1639  0.0589  493 GLN B CB  
8969  C CG  . GLN B 493 ? 0.5372 0.6408 0.7482 0.0604  0.1777  0.0628  493 GLN B CG  
8970  C CD  . GLN B 493 ? 0.4391 0.5559 0.6749 0.0593  0.1962  0.0603  493 GLN B CD  
8971  O OE1 . GLN B 493 ? 0.5998 0.7316 0.8727 0.0633  0.1967  0.0556  493 GLN B OE1 
8972  N NE2 . GLN B 493 ? 0.6952 0.8063 0.9119 0.0539  0.2119  0.0638  493 GLN B NE2 
8973  N N   . LYS B 494 ? 0.5473 0.6306 0.7635 0.0772  0.1410  0.0513  494 LYS B N   
8974  C CA  . LYS B 494 ? 0.5329 0.6109 0.7619 0.0841  0.1327  0.0477  494 LYS B CA  
8975  C C   . LYS B 494 ? 0.5240 0.6164 0.7879 0.0908  0.1353  0.0447  494 LYS B C   
8976  O O   . LYS B 494 ? 0.5665 0.6585 0.8458 0.0958  0.1232  0.0463  494 LYS B O   
8977  C CB  . LYS B 494 ? 0.4340 0.4963 0.6459 0.0870  0.1360  0.0394  494 LYS B CB  
8978  C CG  . LYS B 494 ? 0.4341 0.4836 0.6171 0.0802  0.1294  0.0418  494 LYS B CG  
8979  C CD  . LYS B 494 ? 0.5342 0.5657 0.7068 0.0822  0.1243  0.0349  494 LYS B CD  
8980  C CE  . LYS B 494 ? 0.5659 0.5877 0.7181 0.0745  0.1149  0.0373  494 LYS B CE  
8981  N NZ  . LYS B 494 ? 0.8086 0.8145 0.9383 0.0743  0.1161  0.0270  494 LYS B NZ  
8982  N N   . GLU B 495 ? 0.4911 0.5961 0.7677 0.0906  0.1508  0.0408  495 GLU B N   
8983  C CA  . GLU B 495 ? 0.4962 0.6195 0.8128 0.0960  0.1552  0.0371  495 GLU B CA  
8984  C C   . GLU B 495 ? 0.5057 0.6406 0.8440 0.0935  0.1414  0.0435  495 GLU B C   
8985  O O   . GLU B 495 ? 0.5246 0.6729 0.8985 0.0993  0.1370  0.0404  495 GLU B O   
8986  C CB  . GLU B 495 ? 0.4185 0.5528 0.7421 0.0934  0.1782  0.0332  495 GLU B CB  
8987  C CG  . GLU B 495 ? 0.6812 0.8034 0.9843 0.0979  0.1938  0.0246  495 GLU B CG  
8988  C CD  . GLU B 495 ? 0.8881 0.9897 1.1423 0.0922  0.1944  0.0265  495 GLU B CD  
8989  O OE1 . GLU B 495 ? 0.8902 0.9908 1.1281 0.0836  0.1900  0.0351  495 GLU B OE1 
8990  O OE2 . GLU B 495 ? 0.8751 0.9607 1.1078 0.0967  0.1979  0.0187  495 GLU B OE2 
8991  N N   . ALA B 496 ? 0.4165 0.5458 0.7343 0.0857  0.1340  0.0517  496 ALA B N   
8992  C CA  . ALA B 496 ? 0.5016 0.6380 0.8340 0.0832  0.1211  0.0568  496 ALA B CA  
8993  C C   . ALA B 496 ? 0.5178 0.6461 0.8532 0.0904  0.1017  0.0582  496 ALA B C   
8994  O O   . ALA B 496 ? 0.6177 0.7520 0.9696 0.0912  0.0894  0.0598  496 ALA B O   
8995  C CB  . ALA B 496 ? 0.5171 0.6474 0.8247 0.0741  0.1204  0.0644  496 ALA B CB  
8996  N N   . ALA B 497 ? 0.5845 0.6972 0.9025 0.0952  0.0984  0.0576  497 ALA B N   
8997  C CA  . ALA B 497 ? 0.4616 0.5618 0.7771 0.1019  0.0817  0.0604  497 ALA B CA  
8998  C C   . ALA B 497 ? 0.4302 0.5399 0.7798 0.1119  0.0737  0.0555  497 ALA B C   
8999  O O   . ALA B 497 ? 0.5134 0.6205 0.8681 0.1154  0.0571  0.0588  497 ALA B O   
9000  C CB  . ALA B 497 ? 0.6180 0.6985 0.9103 0.1036  0.0823  0.0607  497 ALA B CB  
9001  N N   . GLU B 498 ? 0.3683 0.4882 0.7409 0.1172  0.0848  0.0473  498 GLU B N   
9002  C CA  . GLU B 498 ? 0.4832 0.6152 0.8948 0.1279  0.0774  0.0419  498 GLU B CA  
9003  C C   . GLU B 498 ? 0.4252 0.5808 0.8698 0.1241  0.0747  0.0411  498 GLU B C   
9004  O O   . GLU B 498 ? 0.7024 0.8652 1.1744 0.1313  0.0581  0.0397  498 GLU B O   
9005  C CB  . GLU B 498 ? 0.4397 0.5767 0.8691 0.1356  0.0926  0.0323  498 GLU B CB  
9006  C CG  . GLU B 498 ? 0.8993 1.0113 1.3061 0.1427  0.0894  0.0312  498 GLU B CG  
9007  C CD  . GLU B 498 ? 1.2122 1.3092 1.6202 0.1522  0.0672  0.0354  498 GLU B CD  
9008  O OE1 . GLU B 498 ? 1.2946 1.4030 1.7382 0.1630  0.0582  0.0316  498 GLU B OE1 
9009  O OE2 . GLU B 498 ? 1.1107 1.1841 1.4846 0.1491  0.0590  0.0427  498 GLU B OE2 
9010  N N   . LYS B 499 ? 0.3675 0.5337 0.8097 0.1129  0.0893  0.0422  499 LYS B N   
9011  C CA  . LYS B 499 ? 0.4112 0.5987 0.8864 0.1072  0.0886  0.0414  499 LYS B CA  
9012  C C   . LYS B 499 ? 0.5464 0.7277 1.0118 0.1029  0.0681  0.0472  499 LYS B C   
9013  O O   . LYS B 499 ? 0.5093 0.7052 1.0089 0.1034  0.0563  0.0445  499 LYS B O   
9014  C CB  . LYS B 499 ? 0.5548 0.7510 1.0267 0.0961  0.1124  0.0417  499 LYS B CB  
9015  C CG  . LYS B 499 ? 0.5438 0.7434 1.0178 0.0993  0.1359  0.0356  499 LYS B CG  
9016  C CD  . LYS B 499 ? 0.8916 1.1043 1.3757 0.0894  0.1587  0.0346  499 LYS B CD  
9017  C CE  . LYS B 499 ? 0.7074 0.9131 1.1654 0.0773  0.1622  0.0433  499 LYS B CE  
9018  N NZ  . LYS B 499 ? 0.7920 1.0011 1.2456 0.0686  0.1869  0.0433  499 LYS B NZ  
9019  N N   . TYR B 500 ? 0.4248 0.5850 0.8455 0.0986  0.0640  0.0543  500 TYR B N   
9020  C CA  . TYR B 500 ? 0.4520 0.6036 0.8582 0.0947  0.0478  0.0593  500 TYR B CA  
9021  C C   . TYR B 500 ? 0.5600 0.6867 0.9305 0.1000  0.0320  0.0649  500 TYR B C   
9022  O O   . TYR B 500 ? 0.5996 0.7179 0.9581 0.0986  0.0179  0.0678  500 TYR B O   
9023  C CB  . TYR B 500 ? 0.4100 0.5606 0.7973 0.0827  0.0600  0.0635  500 TYR B CB  
9024  C CG  . TYR B 500 ? 0.4799 0.6495 0.8934 0.0754  0.0783  0.0604  500 TYR B CG  
9025  C CD1 . TYR B 500 ? 0.5022 0.6882 0.9516 0.0705  0.0746  0.0575  500 TYR B CD1 
9026  C CD2 . TYR B 500 ? 0.4519 0.6209 0.8515 0.0724  0.0992  0.0608  500 TYR B CD2 
9027  C CE1 . TYR B 500 ? 0.4861 0.6880 0.9592 0.0624  0.0942  0.0560  500 TYR B CE1 
9028  C CE2 . TYR B 500 ? 0.5874 0.7698 1.0045 0.0655  0.1182  0.0592  500 TYR B CE2 
9029  C CZ  . TYR B 500 ? 0.5701 0.7692 1.0250 0.0602  0.1170  0.0573  500 TYR B CZ  
9030  O OH  . TYR B 500 ? 0.5370 0.7482 1.0099 0.0521  0.1384  0.0569  500 TYR B OH  
9031  N N   . ALA B 501 ? 0.4629 0.5755 0.8141 0.1054  0.0353  0.0666  501 ALA B N   
9032  C CA  . ALA B 501 ? 0.4753 0.5626 0.7917 0.1090  0.0239  0.0732  501 ALA B CA  
9033  C C   . ALA B 501 ? 0.6025 0.6797 0.9253 0.1209  0.0049  0.0729  501 ALA B C   
9034  O O   . ALA B 501 ? 0.5471 0.6360 0.9018 0.1284  0.0025  0.0669  501 ALA B O   
9035  C CB  . ALA B 501 ? 0.5450 0.6197 0.8365 0.1067  0.0366  0.0762  501 ALA B CB  
9036  N N   . GLY B 502 ? 0.5443 0.5983 0.8350 0.1233  -0.0080 0.0795  502 GLY B N   
9037  C CA  . GLY B 502 ? 0.5575 0.5947 0.8431 0.1349  -0.0282 0.0813  502 GLY B CA  
9038  C C   . GLY B 502 ? 0.6171 0.6403 0.8984 0.1426  -0.0255 0.0828  502 GLY B C   
9039  O O   . GLY B 502 ? 0.6943 0.7221 0.9785 0.1385  -0.0081 0.0810  502 GLY B O   
9040  N N   . PRO B 503 ? 0.6247 0.6268 0.8959 0.1541  -0.0433 0.0862  503 PRO B N   
9041  C CA  . PRO B 503 ? 0.5920 0.5785 0.8614 0.1620  -0.0413 0.0874  503 PRO B CA  
9042  C C   . PRO B 503 ? 0.6936 0.6594 0.9281 0.1542  -0.0255 0.0943  503 PRO B C   
9043  O O   . PRO B 503 ? 0.7281 0.6964 0.9719 0.1527  -0.0126 0.0908  503 PRO B O   
9044  C CB  . PRO B 503 ? 0.5671 0.5301 0.8239 0.1754  -0.0661 0.0920  503 PRO B CB  
9045  C CG  . PRO B 503 ? 0.9167 0.8717 1.1466 0.1714  -0.0771 0.0964  503 PRO B CG  
9046  C CD  . PRO B 503 ? 0.6957 0.6841 0.9528 0.1606  -0.0670 0.0892  503 PRO B CD  
9047  N N   . GLY B 504 ? 0.5666 0.5127 0.7631 0.1493  -0.0265 0.1033  504 GLY B N   
9048  C CA  . GLY B 504 ? 0.7369 0.6650 0.9050 0.1414  -0.0117 0.1103  504 GLY B CA  
9049  C C   . GLY B 504 ? 0.6863 0.6356 0.8658 0.1295  0.0071  0.1060  504 GLY B C   
9050  O O   . GLY B 504 ? 0.6980 0.6421 0.8771 0.1257  0.0179  0.1055  504 GLY B O   
9051  N N   . LEU B 505 ? 0.6213 0.5922 0.8099 0.1238  0.0100  0.1027  505 LEU B N   
9052  C CA  . LEU B 505 ? 0.6418 0.6307 0.8379 0.1135  0.0260  0.0994  505 LEU B CA  
9053  C C   . LEU B 505 ? 0.5956 0.5992 0.8180 0.1147  0.0333  0.0906  505 LEU B C   
9054  O O   . LEU B 505 ? 0.6508 0.6549 0.8691 0.1086  0.0449  0.0891  505 LEU B O   
9055  C CB  . LEU B 505 ? 0.5460 0.5512 0.7451 0.1082  0.0264  0.0984  505 LEU B CB  
9056  C CG  . LEU B 505 ? 0.4429 0.4655 0.6481 0.0986  0.0410  0.0958  505 LEU B CG  
9057  C CD1 . LEU B 505 ? 0.4626 0.4749 0.6476 0.0922  0.0506  0.1010  505 LEU B CD1 
9058  C CD2 . LEU B 505 ? 0.5138 0.5477 0.7214 0.0947  0.0395  0.0955  505 LEU B CD2 
9059  N N   . ALA B 506 ? 0.4489 0.4636 0.6979 0.1231  0.0265  0.0843  506 ALA B N   
9060  C CA  . ALA B 506 ? 0.4417 0.4688 0.7145 0.1256  0.0358  0.0753  506 ALA B CA  
9061  C C   . ALA B 506 ? 0.5377 0.5434 0.7989 0.1288  0.0384  0.0753  506 ALA B C   
9062  O O   . ALA B 506 ? 0.6469 0.6560 0.9124 0.1266  0.0500  0.0688  506 ALA B O   
9063  C CB  . ALA B 506 ? 0.4817 0.5247 0.7896 0.1352  0.0280  0.0689  506 ALA B CB  
9064  N N   . THR B 507 ? 0.5346 0.5156 0.7788 0.1339  0.0275  0.0825  507 THR B N   
9065  C CA  . THR B 507 ? 0.5722 0.5283 0.8042 0.1360  0.0290  0.0840  507 THR B CA  
9066  C C   . THR B 507 ? 0.6660 0.6163 0.8789 0.1230  0.0410  0.0867  507 THR B C   
9067  O O   . THR B 507 ? 0.6738 0.6183 0.8882 0.1206  0.0481  0.0812  507 THR B O   
9068  C CB  . THR B 507 ? 0.5609 0.4890 0.7749 0.1439  0.0147  0.0933  507 THR B CB  
9069  O OG1 . THR B 507 ? 0.5870 0.5205 0.8227 0.1575  0.0007  0.0896  507 THR B OG1 
9070  C CG2 . THR B 507 ? 0.4395 0.3373 0.6365 0.1434  0.0177  0.0974  507 THR B CG2 
9071  N N   . VAL B 508 ? 0.5796 0.5315 0.7759 0.1149  0.0425  0.0942  508 VAL B N   
9072  C CA  . VAL B 508 ? 0.4331 0.3830 0.6166 0.1029  0.0526  0.0971  508 VAL B CA  
9073  C C   . VAL B 508 ? 0.5237 0.4940 0.7196 0.0976  0.0614  0.0879  508 VAL B C   
9074  O O   . VAL B 508 ? 0.5767 0.5418 0.7689 0.0912  0.0669  0.0853  508 VAL B O   
9075  C CB  . VAL B 508 ? 0.4335 0.3830 0.6000 0.0975  0.0533  0.1062  508 VAL B CB  
9076  C CG1 . VAL B 508 ? 0.3942 0.3497 0.5568 0.0859  0.0639  0.1075  508 VAL B CG1 
9077  C CG2 . VAL B 508 ? 0.5499 0.4721 0.6950 0.1019  0.0474  0.1162  508 VAL B CG2 
9078  N N   . CYS B 509 ? 0.5147 0.5064 0.7246 0.0999  0.0622  0.0829  509 CYS B N   
9079  C CA  . CYS B 509 ? 0.4493 0.4573 0.6660 0.0956  0.0717  0.0752  509 CYS B CA  
9080  C C   . CYS B 509 ? 0.4990 0.4993 0.7203 0.0993  0.0757  0.0662  509 CYS B C   
9081  O O   . CYS B 509 ? 0.6029 0.6033 0.8166 0.0937  0.0822  0.0612  509 CYS B O   
9082  C CB  . CYS B 509 ? 0.5290 0.5585 0.7614 0.0977  0.0732  0.0725  509 CYS B CB  
9083  S SG  . CYS B 509 ? 0.6090 0.6470 0.8332 0.0914  0.0703  0.0807  509 CYS B SG  
9084  N N   . LYS B 510 ? 0.5458 0.5379 0.7787 0.1097  0.0709  0.0634  510 LYS B N   
9085  C CA  . LYS B 510 ? 0.4983 0.4805 0.7362 0.1152  0.0749  0.0539  510 LYS B CA  
9086  C C   . LYS B 510 ? 0.5730 0.5314 0.7932 0.1093  0.0740  0.0548  510 LYS B C   
9087  O O   . LYS B 510 ? 0.7459 0.6982 0.9620 0.1078  0.0795  0.0457  510 LYS B O   
9088  C CB  . LYS B 510 ? 0.4125 0.3908 0.6694 0.1292  0.0680  0.0517  510 LYS B CB  
9089  C CG  . LYS B 510 ? 0.3897 0.3634 0.6580 0.1376  0.0747  0.0396  510 LYS B CG  
9090  C CD  . LYS B 510 ? 0.7248 0.6984 1.0181 0.1530  0.0671  0.0375  510 LYS B CD  
9091  C CE  . LYS B 510 ? 0.9086 0.8928 1.2243 0.1624  0.0783  0.0239  510 LYS B CE  
9092  N NZ  . LYS B 510 ? 0.8353 0.8260 1.1833 0.1780  0.0701  0.0218  510 LYS B NZ  
9093  N N   . LEU B 511 ? 0.5679 0.5119 0.7772 0.1054  0.0678  0.0655  511 LEU B N   
9094  C CA  . LEU B 511 ? 0.5508 0.4725 0.7480 0.0980  0.0677  0.0677  511 LEU B CA  
9095  C C   . LEU B 511 ? 0.5920 0.5229 0.7825 0.0850  0.0725  0.0667  511 LEU B C   
9096  O O   . LEU B 511 ? 0.7727 0.6938 0.9600 0.0799  0.0736  0.0598  511 LEU B O   
9097  C CB  . LEU B 511 ? 0.5553 0.4577 0.7424 0.0979  0.0622  0.0807  511 LEU B CB  
9098  C CG  . LEU B 511 ? 0.4314 0.3182 0.6207 0.1114  0.0538  0.0833  511 LEU B CG  
9099  C CD1 . LEU B 511 ? 0.4857 0.3575 0.6582 0.1115  0.0485  0.0975  511 LEU B CD1 
9100  C CD2 . LEU B 511 ? 0.5830 0.4449 0.7737 0.1159  0.0527  0.0780  511 LEU B CD2 
9101  N N   . VAL B 512 ? 0.5182 0.4666 0.7067 0.0801  0.0739  0.0731  512 VAL B N   
9102  C CA  . VAL B 512 ? 0.5577 0.5162 0.7423 0.0693  0.0767  0.0731  512 VAL B CA  
9103  C C   . VAL B 512 ? 0.6057 0.5784 0.7895 0.0694  0.0800  0.0630  512 VAL B C   
9104  O O   . VAL B 512 ? 0.6878 0.6639 0.8662 0.0617  0.0797  0.0604  512 VAL B O   
9105  C CB  . VAL B 512 ? 0.4565 0.4254 0.6385 0.0652  0.0775  0.0837  512 VAL B CB  
9106  C CG1 . VAL B 512 ? 0.5857 0.5634 0.7679 0.0548  0.0793  0.0844  512 VAL B CG1 
9107  C CG2 . VAL B 512 ? 0.4525 0.4043 0.6289 0.0666  0.0761  0.0939  512 VAL B CG2 
9108  N N   . ASP B 513 ? 0.4731 0.4533 0.6624 0.0781  0.0833  0.0576  513 ASP B N   
9109  C CA  . ASP B 513 ? 0.4552 0.4464 0.6410 0.0789  0.0899  0.0489  513 ASP B CA  
9110  C C   . ASP B 513 ? 0.5906 0.5987 0.7714 0.0730  0.0917  0.0542  513 ASP B C   
9111  O O   . ASP B 513 ? 0.7089 0.7181 0.8774 0.0675  0.0923  0.0514  513 ASP B O   
9112  C CB  . ASP B 513 ? 0.4875 0.4643 0.6613 0.0763  0.0901  0.0388  513 ASP B CB  
9113  C CG  . ASP B 513 ? 0.6497 0.6311 0.8140 0.0795  0.0987  0.0289  513 ASP B CG  
9114  O OD1 . ASP B 513 ? 0.7753 0.7651 0.9501 0.0876  0.1066  0.0261  513 ASP B OD1 
9115  O OD2 . ASP B 513 ? 0.8578 0.8338 1.0040 0.0742  0.0975  0.0237  513 ASP B OD2 
9116  N N   . ILE B 514 ? 0.4892 0.5086 0.6786 0.0747  0.0912  0.0616  514 ILE B N   
9117  C CA  . ILE B 514 ? 0.4894 0.5223 0.6751 0.0700  0.0926  0.0671  514 ILE B CA  
9118  C C   . ILE B 514 ? 0.5192 0.5654 0.7167 0.0741  0.0956  0.0683  514 ILE B C   
9119  O O   . ILE B 514 ? 0.6640 0.7098 0.8750 0.0806  0.0933  0.0672  514 ILE B O   
9120  C CB  . ILE B 514 ? 0.5126 0.5426 0.6956 0.0653  0.0871  0.0764  514 ILE B CB  
9121  C CG1 . ILE B 514 ? 0.6014 0.6231 0.7897 0.0702  0.0829  0.0816  514 ILE B CG1 
9122  C CG2 . ILE B 514 ? 0.5425 0.5643 0.7197 0.0589  0.0847  0.0755  514 ILE B CG2 
9123  C CD1 . ILE B 514 ? 0.4329 0.4479 0.6146 0.0665  0.0808  0.0912  514 ILE B CD1 
9124  N N   . PRO B 515 ? 0.4967 0.5541 0.6912 0.0703  0.0995  0.0710  515 PRO B N   
9125  C CA  . PRO B 515 ? 0.4009 0.4703 0.6102 0.0725  0.1014  0.0724  515 PRO B CA  
9126  C C   . PRO B 515 ? 0.5305 0.5978 0.7436 0.0737  0.0917  0.0790  515 PRO B C   
9127  O O   . PRO B 515 ? 0.5988 0.6564 0.8003 0.0718  0.0872  0.0839  515 PRO B O   
9128  C CB  . PRO B 515 ? 0.4169 0.4934 0.6173 0.0669  0.1079  0.0746  515 PRO B CB  
9129  C CG  . PRO B 515 ? 0.5592 0.6276 0.7393 0.0633  0.1080  0.0738  515 PRO B CG  
9130  C CD  . PRO B 515 ? 0.4791 0.5375 0.6581 0.0641  0.1006  0.0734  515 PRO B CD  
9131  N N   . PRO B 516 ? 0.5482 0.6233 0.7766 0.0766  0.0884  0.0793  516 PRO B N   
9132  C CA  . PRO B 516 ? 0.3128 0.3816 0.5378 0.0783  0.0778  0.0849  516 PRO B CA  
9133  C C   . PRO B 516 ? 0.4702 0.5382 0.6809 0.0727  0.0782  0.0908  516 PRO B C   
9134  O O   . PRO B 516 ? 0.5043 0.5632 0.7048 0.0739  0.0717  0.0956  516 PRO B O   
9135  C CB  . PRO B 516 ? 0.4742 0.5528 0.7221 0.0828  0.0724  0.0815  516 PRO B CB  
9136  C CG  . PRO B 516 ? 0.5532 0.6475 0.8163 0.0795  0.0842  0.0767  516 PRO B CG  
9137  C CD  . PRO B 516 ? 0.4873 0.5768 0.7371 0.0781  0.0942  0.0741  516 PRO B CD  
9138  N N   . VAL B 517 ? 0.4991 0.5747 0.7070 0.0674  0.0861  0.0906  517 VAL B N   
9139  C CA  . VAL B 517 ? 0.4204 0.4954 0.6167 0.0630  0.0870  0.0956  517 VAL B CA  
9140  C C   . VAL B 517 ? 0.4577 0.5313 0.6423 0.0597  0.0917  0.0964  517 VAL B C   
9141  O O   . VAL B 517 ? 0.5472 0.6242 0.7311 0.0584  0.0973  0.0927  517 VAL B O   
9142  C CB  . VAL B 517 ? 0.3576 0.4411 0.5626 0.0601  0.0901  0.0950  517 VAL B CB  
9143  C CG1 . VAL B 517 ? 0.5306 0.6104 0.7232 0.0568  0.0902  0.1002  517 VAL B CG1 
9144  C CG2 . VAL B 517 ? 0.3582 0.4456 0.5808 0.0627  0.0833  0.0924  517 VAL B CG2 
9145  N N   . LEU B 518 ? 0.4518 0.5201 0.6275 0.0587  0.0894  0.1009  518 LEU B N   
9146  C CA  . LEU B 518 ? 0.4887 0.5573 0.6582 0.0556  0.0905  0.1012  518 LEU B CA  
9147  C C   . LEU B 518 ? 0.5455 0.6175 0.7092 0.0538  0.0911  0.1052  518 LEU B C   
9148  O O   . LEU B 518 ? 0.6730 0.7437 0.8361 0.0548  0.0903  0.1095  518 LEU B O   
9149  C CB  . LEU B 518 ? 0.3091 0.3717 0.4792 0.0549  0.0884  0.1032  518 LEU B CB  
9150  C CG  . LEU B 518 ? 0.3234 0.3774 0.4965 0.0573  0.0870  0.1013  518 LEU B CG  
9151  C CD1 . LEU B 518 ? 0.3363 0.3825 0.5090 0.0550  0.0871  0.1051  518 LEU B CD1 
9152  C CD2 . LEU B 518 ? 0.5168 0.5706 0.6926 0.0579  0.0877  0.0939  518 LEU B CD2 
9153  N N   . HIS B 519 ? 0.5821 0.6559 0.7390 0.0521  0.0924  0.1037  519 HIS B N   
9154  C CA  . HIS B 519 ? 0.5458 0.6201 0.6952 0.0514  0.0916  0.1079  519 HIS B CA  
9155  C C   . HIS B 519 ? 0.5286 0.6046 0.6799 0.0512  0.0860  0.1096  519 HIS B C   
9156  O O   . HIS B 519 ? 0.5487 0.6241 0.6973 0.0497  0.0822  0.1060  519 HIS B O   
9157  C CB  . HIS B 519 ? 0.4235 0.4954 0.5606 0.0501  0.0952  0.1064  519 HIS B CB  
9158  C CG  . HIS B 519 ? 0.5027 0.5713 0.6290 0.0500  0.0946  0.1118  519 HIS B CG  
9159  N ND1 . HIS B 519 ? 0.5976 0.6669 0.7258 0.0519  0.0884  0.1161  519 HIS B ND1 
9160  C CD2 . HIS B 519 ? 0.4673 0.5304 0.5811 0.0486  0.1002  0.1138  519 HIS B CD2 
9161  C CE1 . HIS B 519 ? 0.5527 0.6160 0.6690 0.0524  0.0886  0.1205  519 HIS B CE1 
9162  N NE2 . HIS B 519 ? 0.4389 0.4971 0.5447 0.0499  0.0958  0.1198  519 HIS B NE2 
9163  N N   . MET B 520 ? 0.4860 0.5638 0.6427 0.0528  0.0854  0.1143  520 MET B N   
9164  C CA  . MET B 520 ? 0.4658 0.5487 0.6323 0.0526  0.0815  0.1156  520 MET B CA  
9165  C C   . MET B 520 ? 0.5507 0.6364 0.7155 0.0549  0.0767  0.1187  520 MET B C   
9166  O O   . MET B 520 ? 0.4860 0.5789 0.6647 0.0557  0.0734  0.1201  520 MET B O   
9167  C CB  . MET B 520 ? 0.3883 0.4715 0.5643 0.0536  0.0863  0.1185  520 MET B CB  
9168  C CG  . MET B 520 ? 0.4646 0.5420 0.6402 0.0522  0.0890  0.1166  520 MET B CG  
9169  S SD  . MET B 520 ? 0.5538 0.6264 0.7338 0.0531  0.0958  0.1212  520 MET B SD  
9170  C CE  . MET B 520 ? 0.5749 0.6568 0.7749 0.0484  0.0955  0.1215  520 MET B CE  
9171  N N   . GLY B 521 ? 0.5396 0.6197 0.6896 0.0559  0.0765  0.1200  521 GLY B N   
9172  C CA  . GLY B 521 ? 0.5180 0.5967 0.6622 0.0590  0.0705  0.1236  521 GLY B CA  
9173  C C   . GLY B 521 ? 0.6101 0.6827 0.7494 0.0623  0.0736  0.1288  521 GLY B C   
9174  O O   . GLY B 521 ? 0.6022 0.6693 0.7365 0.0608  0.0802  0.1290  521 GLY B O   
9175  N N   . SER B 522 ? 0.5633 0.6370 0.7064 0.0671  0.0675  0.1324  522 SER B N   
9176  C CA  . SER B 522 ? 0.6135 0.6788 0.7521 0.0715  0.0697  0.1371  522 SER B CA  
9177  C C   . SER B 522 ? 0.6053 0.6747 0.7588 0.0743  0.0757  0.1366  522 SER B C   
9178  O O   . SER B 522 ? 0.7708 0.8473 0.9338 0.0718  0.0796  0.1335  522 SER B O   
9179  C CB  . SER B 522 ? 0.7825 0.8449 0.9176 0.0771  0.0600  0.1413  522 SER B CB  
9180  O OG  . SER B 522 ? 0.5796 0.6555 0.7321 0.0789  0.0513  0.1391  522 SER B OG  
9181  N N   . CYS B 523 ? 0.5061 0.5683 0.6586 0.0798  0.0769  0.1396  523 CYS B N   
9182  C CA  . CYS B 523 ? 0.7378 0.8002 0.8992 0.0838  0.0841  0.1385  523 CYS B CA  
9183  C C   . CYS B 523 ? 0.7135 0.7904 0.8971 0.0884  0.0838  0.1386  523 CYS B C   
9184  O O   . CYS B 523 ? 0.7558 0.8369 0.9482 0.0887  0.0923  0.1369  523 CYS B O   
9185  C CB  . CYS B 523 ? 0.5609 0.6077 0.7119 0.0880  0.0859  0.1403  523 CYS B CB  
9186  S SG  . CYS B 523 ? 1.3523 1.3853 1.4862 0.0803  0.0881  0.1388  523 CYS B SG  
9187  N N   . VAL B 524 ? 0.7026 0.7861 0.8953 0.0918  0.0744  0.1406  524 VAL B N   
9188  C CA  . VAL B 524 ? 0.5327 0.6345 0.7546 0.0947  0.0727  0.1398  524 VAL B CA  
9189  C C   . VAL B 524 ? 0.6839 0.7945 0.9127 0.0862  0.0757  0.1366  524 VAL B C   
9190  O O   . VAL B 524 ? 0.8062 0.9301 1.0596 0.0859  0.0805  0.1357  524 VAL B O   
9191  C CB  . VAL B 524 ? 0.4906 0.5984 0.7212 0.0992  0.0573  0.1417  524 VAL B CB  
9192  C CG1 . VAL B 524 ? 0.8202 0.9117 1.0332 0.1063  0.0526  0.1462  524 VAL B CG1 
9193  C CG2 . VAL B 524 ? 0.8623 0.9720 1.0844 0.0922  0.0464  0.1396  524 VAL B CG2 
9194  N N   . ASP B 525 ? 0.6454 0.7478 0.8543 0.0798  0.0742  0.1349  525 ASP B N   
9195  C CA  . ASP B 525 ? 0.4736 0.5806 0.6868 0.0726  0.0767  0.1317  525 ASP B CA  
9196  C C   . ASP B 525 ? 0.4715 0.5721 0.6793 0.0714  0.0889  0.1315  525 ASP B C   
9197  O O   . ASP B 525 ? 0.5494 0.6504 0.7585 0.0663  0.0915  0.1297  525 ASP B O   
9198  C CB  . ASP B 525 ? 0.6382 0.7402 0.8352 0.0675  0.0694  0.1290  525 ASP B CB  
9199  C CG  . ASP B 525 ? 0.8452 0.9519 1.0450 0.0679  0.0557  0.1279  525 ASP B CG  
9200  O OD1 . ASP B 525 ? 0.8400 0.9575 1.0608 0.0716  0.0500  0.1291  525 ASP B OD1 
9201  O OD2 . ASP B 525 ? 0.8279 0.9272 1.0087 0.0649  0.0504  0.1255  525 ASP B OD2 
9202  N N   . ILE B 526 ? 0.5096 0.6019 0.7095 0.0765  0.0955  0.1332  526 ILE B N   
9203  C CA  . ILE B 526 ? 0.4900 0.5735 0.6809 0.0765  0.1054  0.1328  526 ILE B CA  
9204  C C   . ILE B 526 ? 0.5450 0.6372 0.7543 0.0763  0.1142  0.1340  526 ILE B C   
9205  O O   . ILE B 526 ? 0.6261 0.7111 0.8277 0.0744  0.1220  0.1345  526 ILE B O   
9206  C CB  . ILE B 526 ? 0.4964 0.5664 0.6724 0.0822  0.1090  0.1330  526 ILE B CB  
9207  C CG1 . ILE B 526 ? 0.5145 0.5750 0.6747 0.0794  0.1022  0.1318  526 ILE B CG1 
9208  C CG2 . ILE B 526 ? 0.2837 0.3433 0.4490 0.0844  0.1192  0.1326  526 ILE B CG2 
9209  C CD1 . ILE B 526 ? 0.5437 0.5902 0.6916 0.0833  0.1028  0.1315  526 ILE B CD1 
9210  N N   . SER B 527 ? 0.4286 0.5362 0.6632 0.0780  0.1125  0.1348  527 SER B N   
9211  C CA  . SER B 527 ? 0.5518 0.6715 0.8119 0.0763  0.1213  0.1359  527 SER B CA  
9212  C C   . SER B 527 ? 0.5806 0.7000 0.8420 0.0670  0.1207  0.1350  527 SER B C   
9213  O O   . SER B 527 ? 0.6330 0.7534 0.9046 0.0639  0.1322  0.1370  527 SER B O   
9214  C CB  . SER B 527 ? 0.4946 0.6335 0.7866 0.0788  0.1142  0.1357  527 SER B CB  
9215  O OG  . SER B 527 ? 0.4910 0.6336 0.7820 0.0754  0.0969  0.1336  527 SER B OG  
9216  N N   . ARG B 528 ? 0.5067 0.6228 0.7567 0.0630  0.1086  0.1323  528 ARG B N   
9217  C CA  . ARG B 528 ? 0.5951 0.7078 0.8437 0.0555  0.1070  0.1304  528 ARG B CA  
9218  C C   . ARG B 528 ? 0.6703 0.7669 0.8989 0.0557  0.1169  0.1326  528 ARG B C   
9219  O O   . ARG B 528 ? 0.6795 0.7718 0.9119 0.0511  0.1225  0.1339  528 ARG B O   
9220  C CB  . ARG B 528 ? 0.5257 0.6356 0.7617 0.0534  0.0941  0.1263  528 ARG B CB  
9221  C CG  . ARG B 528 ? 0.4696 0.5903 0.7172 0.0534  0.0815  0.1240  528 ARG B CG  
9222  C CD  . ARG B 528 ? 0.4466 0.5618 0.6801 0.0496  0.0716  0.1191  528 ARG B CD  
9223  N NE  . ARG B 528 ? 0.5482 0.6642 0.7730 0.0526  0.0601  0.1182  528 ARG B NE  
9224  C CZ  . ARG B 528 ? 0.6466 0.7697 0.8822 0.0515  0.0472  0.1156  528 ARG B CZ  
9225  N NH1 . ARG B 528 ? 0.5262 0.6589 0.7874 0.0464  0.0443  0.1129  528 ARG B NH1 
9226  N NH2 . ARG B 528 ? 0.6538 0.7729 0.8740 0.0554  0.0363  0.1158  528 ARG B NH2 
9227  N N   . ILE B 529 ? 0.5369 0.6227 0.7437 0.0611  0.1180  0.1330  529 ILE B N   
9228  C CA  . ILE B 529 ? 0.4672 0.5360 0.6522 0.0626  0.1236  0.1344  529 ILE B CA  
9229  C C   . ILE B 529 ? 0.5818 0.6464 0.7689 0.0638  0.1382  0.1387  529 ILE B C   
9230  O O   . ILE B 529 ? 0.5825 0.6356 0.7604 0.0614  0.1441  0.1413  529 ILE B O   
9231  C CB  . ILE B 529 ? 0.5113 0.5706 0.6763 0.0675  0.1195  0.1328  529 ILE B CB  
9232  C CG1 . ILE B 529 ? 0.3968 0.4603 0.5615 0.0652  0.1085  0.1293  529 ILE B CG1 
9233  C CG2 . ILE B 529 ? 0.4038 0.4446 0.5456 0.0699  0.1222  0.1336  529 ILE B CG2 
9234  C CD1 . ILE B 529 ? 0.6693 0.7274 0.8231 0.0680  0.1048  0.1280  529 ILE B CD1 
9235  N N   . LEU B 530 ? 0.5974 0.6705 0.7969 0.0678  0.1453  0.1397  530 LEU B N   
9236  C CA  . LEU B 530 ? 0.5884 0.6590 0.7925 0.0693  0.1629  0.1435  530 LEU B CA  
9237  C C   . LEU B 530 ? 0.5229 0.6016 0.7500 0.0610  0.1685  0.1461  530 LEU B C   
9238  O O   . LEU B 530 ? 0.5886 0.6554 0.8071 0.0590  0.1823  0.1505  530 LEU B O   
9239  C CB  . LEU B 530 ? 0.5031 0.5860 0.7253 0.0757  0.1689  0.1431  530 LEU B CB  
9240  C CG  . LEU B 530 ? 0.5033 0.5755 0.7043 0.0843  0.1662  0.1407  530 LEU B CG  
9241  C CD1 . LEU B 530 ? 0.5760 0.6617 0.8005 0.0912  0.1706  0.1402  530 LEU B CD1 
9242  C CD2 . LEU B 530 ? 0.4802 0.5274 0.6456 0.0883  0.1760  0.1414  530 LEU B CD2 
9243  N N   . ASP B 531 ? 0.5817 0.6781 0.8357 0.0557  0.1573  0.1433  531 ASP B N   
9244  C CA  . ASP B 531 ? 0.5350 0.6395 0.8145 0.0465  0.1593  0.1441  531 ASP B CA  
9245  C C   . ASP B 531 ? 0.6187 0.7028 0.8752 0.0421  0.1600  0.1459  531 ASP B C   
9246  O O   . ASP B 531 ? 0.7568 0.8321 1.0147 0.0378  0.1734  0.1508  531 ASP B O   
9247  C CB  . ASP B 531 ? 0.6027 0.7260 0.9079 0.0429  0.1422  0.1389  531 ASP B CB  
9248  C CG  . ASP B 531 ? 0.6211 0.7530 0.9555 0.0324  0.1407  0.1379  531 ASP B CG  
9249  O OD1 . ASP B 531 ? 0.6594 0.7911 1.0088 0.0278  0.1565  0.1423  531 ASP B OD1 
9250  O OD2 . ASP B 531 ? 0.6210 0.7583 0.9622 0.0286  0.1241  0.1325  531 ASP B OD2 
9251  N N   . LEU B 532 ? 0.6591 0.7348 0.8950 0.0436  0.1464  0.1423  532 LEU B N   
9252  C CA  . LEU B 532 ? 0.5472 0.6042 0.7635 0.0414  0.1445  0.1431  532 LEU B CA  
9253  C C   . LEU B 532 ? 0.5772 0.6127 0.7677 0.0448  0.1571  0.1495  532 LEU B C   
9254  O O   . LEU B 532 ? 0.6612 0.6834 0.8483 0.0404  0.1642  0.1540  532 LEU B O   
9255  C CB  . LEU B 532 ? 0.4831 0.5373 0.6838 0.0448  0.1300  0.1378  532 LEU B CB  
9256  C CG  . LEU B 532 ? 0.4934 0.5321 0.6807 0.0437  0.1250  0.1369  532 LEU B CG  
9257  C CD1 . LEU B 532 ? 0.6901 0.7332 0.8954 0.0365  0.1200  0.1332  532 LEU B CD1 
9258  C CD2 . LEU B 532 ? 0.2832 0.3191 0.4551 0.0492  0.1153  0.1328  532 LEU B CD2 
9259  N N   . VAL B 533 ? 0.5713 0.6005 0.7412 0.0526  0.1597  0.1500  533 VAL B N   
9260  C CA  . VAL B 533 ? 0.5378 0.5429 0.6761 0.0570  0.1701  0.1553  533 VAL B CA  
9261  C C   . VAL B 533 ? 0.6780 0.6812 0.8259 0.0533  0.1910  0.1618  533 VAL B C   
9262  O O   . VAL B 533 ? 0.7127 0.6942 0.8408 0.0517  0.2003  0.1681  533 VAL B O   
9263  C CB  . VAL B 533 ? 0.5403 0.5390 0.6559 0.0657  0.1678  0.1528  533 VAL B CB  
9264  C CG1 . VAL B 533 ? 0.6316 0.6031 0.7107 0.0708  0.1790  0.1576  533 VAL B CG1 
9265  C CG2 . VAL B 533 ? 0.4654 0.4642 0.5731 0.0679  0.1489  0.1472  533 VAL B CG2 
9266  N N   . GLY B 534 ? 0.6440 0.6695 0.8235 0.0518  0.1984  0.1607  534 GLY B N   
9267  C CA  . GLY B 534 ? 0.5812 0.6110 0.7801 0.0476  0.2198  0.1661  534 GLY B CA  
9268  C C   . GLY B 534 ? 0.6613 0.6882 0.8761 0.0366  0.2232  0.1700  534 GLY B C   
9269  O O   . GLY B 534 ? 0.6470 0.6607 0.8573 0.0329  0.2428  0.1774  534 GLY B O   
9270  N N   . ARG B 535 ? 0.6058 0.6424 0.8375 0.0312  0.2050  0.1650  535 ARG B N   
9271  C CA  . ARG B 535 ? 0.5552 0.5873 0.8025 0.0205  0.2052  0.1669  535 ARG B CA  
9272  C C   . ARG B 535 ? 0.6171 0.6156 0.8261 0.0213  0.2091  0.1732  535 ARG B C   
9273  O O   . ARG B 535 ? 0.6325 0.6180 0.8458 0.0136  0.2213  0.1797  535 ARG B O   
9274  C CB  . ARG B 535 ? 0.5146 0.5606 0.7807 0.0167  0.1835  0.1584  535 ARG B CB  
9275  C CG  . ARG B 535 ? 0.4919 0.5686 0.7985 0.0139  0.1775  0.1530  535 ARG B CG  
9276  C CD  . ARG B 535 ? 0.6103 0.6948 0.9239 0.0116  0.1555  0.1444  535 ARG B CD  
9277  N NE  . ARG B 535 ? 0.6390 0.7229 0.9756 0.0001  0.1522  0.1424  535 ARG B NE  
9278  C CZ  . ARG B 535 ? 0.8431 0.9470 1.2170 -0.0069 0.1434  0.1371  535 ARG B CZ  
9279  N NH1 . ARG B 535 ? 0.6507 0.7776 1.0434 -0.0026 0.1366  0.1340  535 ARG B NH1 
9280  N NH2 . ARG B 535 ? 0.7262 0.8256 1.1185 -0.0181 0.1398  0.1347  535 ARG B NH2 
9281  N N   . VAL B 536 ? 0.6030 0.5866 0.7760 0.0306  0.1981  0.1715  536 VAL B N   
9282  C CA  . VAL B 536 ? 0.6230 0.5740 0.7578 0.0339  0.1978  0.1772  536 VAL B CA  
9283  C C   . VAL B 536 ? 0.7100 0.6404 0.8200 0.0356  0.2200  0.1868  536 VAL B C   
9284  O O   . VAL B 536 ? 0.6941 0.5996 0.7879 0.0320  0.2298  0.1952  536 VAL B O   
9285  C CB  . VAL B 536 ? 0.5711 0.5153 0.6793 0.0438  0.1792  0.1720  536 VAL B CB  
9286  C CG1 . VAL B 536 ? 0.6002 0.5100 0.6681 0.0492  0.1771  0.1781  536 VAL B CG1 
9287  C CG2 . VAL B 536 ? 0.4523 0.4138 0.5823 0.0420  0.1611  0.1632  536 VAL B CG2 
9288  N N   . ALA B 537 ? 0.6964 0.6350 0.8020 0.0414  0.2291  0.1858  537 ALA B N   
9289  C CA  . ALA B 537 ? 0.6897 0.6083 0.7690 0.0442  0.2526  0.1938  537 ALA B CA  
9290  C C   . ALA B 537 ? 0.6919 0.6131 0.7947 0.0341  0.2674  0.1953  537 ALA B C   
9291  O O   . ALA B 537 ? 0.8794 0.7728 0.9522 0.0335  0.2777  0.2008  537 ALA B O   
9292  C CB  . ALA B 537 ? 0.6875 0.6195 0.7674 0.0519  0.2587  0.1891  537 ALA B CB  
9293  N N   . ASN B 538 ? 0.7187 0.6720 0.8743 0.0261  0.2671  0.1906  538 ASN B N   
9294  C CA  . ASN B 538 ? 0.7929 0.7517 0.9777 0.0153  0.2795  0.1915  538 ASN B CA  
9295  C C   . ASN B 538 ? 0.6627 0.6002 0.8399 0.0069  0.2769  0.1968  538 ASN B C   
9296  O O   . ASN B 538 ? 0.7208 0.6422 0.8916 0.0011  0.2911  0.2013  538 ASN B O   
9297  C CB  . ASN B 538 ? 0.6668 0.6643 0.9103 0.0091  0.2741  0.1846  538 ASN B CB  
9298  C CG  . ASN B 538 ? 0.5750 0.5915 0.8317 0.0163  0.2809  0.1802  538 ASN B CG  
9299  O OD1 . ASN B 538 ? 0.7521 0.7540 0.9839 0.0222  0.2973  0.1824  538 ASN B OD1 
9300  N ND2 . ASN B 538 ? 0.8638 0.9112 1.1583 0.0165  0.2683  0.1739  538 ASN B ND2 
9301  N N   . LEU B 539 ? 0.6885 0.6239 0.8653 0.0064  0.2594  0.1964  539 LEU B N   
9302  C CA  . LEU B 539 ? 0.7465 0.6587 0.9162 -0.0006 0.2551  0.2010  539 LEU B CA  
9303  C C   . LEU B 539 ? 0.8000 0.6718 0.9140 0.0059  0.2613  0.2088  539 LEU B C   
9304  O O   . LEU B 539 ? 0.9189 0.7690 1.0255 -0.0009 0.2672  0.2139  539 LEU B O   
9305  C CB  . LEU B 539 ? 0.7502 0.6679 0.9282 0.0004  0.2335  0.1967  539 LEU B CB  
9306  C CG  . LEU B 539 ? 0.5476 0.4400 0.7173 -0.0042 0.2255  0.1988  539 LEU B CG  
9307  C CD1 . LEU B 539 ? 0.8118 0.7200 1.0282 -0.0183 0.2230  0.1938  539 LEU B CD1 
9308  C CD2 . LEU B 539 ? 0.7993 0.6839 0.9449 0.0066  0.2023  0.1922  539 LEU B CD2 
9309  N N   . LEU B 540 ? 0.8663 0.7272 0.9417 0.0184  0.2588  0.2096  540 LEU B N   
9310  C CA  . LEU B 540 ? 0.8094 0.6308 0.8282 0.0257  0.2615  0.2163  540 LEU B CA  
9311  C C   . LEU B 540 ? 0.9547 0.7669 0.9547 0.0263  0.2835  0.2184  540 LEU B C   
9312  O O   . LEU B 540 ? 1.0927 0.8711 1.0424 0.0324  0.2870  0.2237  540 LEU B O   
9313  C CB  . LEU B 540 ? 0.6845 0.4945 0.6682 0.0391  0.2448  0.2156  540 LEU B CB  
9314  C CG  . LEU B 540 ? 0.7343 0.5457 0.7269 0.0415  0.2222  0.2137  540 LEU B CG  
9315  C CD1 . LEU B 540 ? 0.5661 0.3804 0.5373 0.0538  0.2023  0.2061  540 LEU B CD1 
9316  C CD2 . LEU B 540 ? 0.9456 0.7238 0.9170 0.0409  0.2170  0.2206  540 LEU B CD2 
9317  N N   . GLY B 541 ? 0.9556 0.7966 0.9956 0.0207  0.2971  0.2142  541 GLY B N   
9318  C CA  . GLY B 541 ? 1.0167 0.8521 1.0466 0.0214  0.3196  0.2155  541 GLY B CA  
9319  C C   . GLY B 541 ? 0.9422 0.7602 0.9246 0.0349  0.3229  0.2149  541 GLY B C   
9320  O O   . GLY B 541 ? 1.1237 0.9172 1.0715 0.0377  0.3393  0.2187  541 GLY B O   
9321  N N   . VAL B 542 ? 0.8272 0.6565 0.8069 0.0431  0.3078  0.2099  542 VAL B N   
9322  C CA  . VAL B 542 ? 0.8566 0.6691 0.7919 0.0559  0.3080  0.2081  542 VAL B CA  
9323  C C   . VAL B 542 ? 0.9663 0.8113 0.9336 0.0598  0.3071  0.2004  542 VAL B C   
9324  O O   . VAL B 542 ? 0.9448 0.8241 0.9660 0.0529  0.3045  0.1969  542 VAL B O   
9325  C CB  . VAL B 542 ? 0.6820 0.4664 0.5710 0.0635  0.2868  0.2108  542 VAL B CB  
9326  C CG1 . VAL B 542 ? 0.9075 0.6569 0.7618 0.0614  0.2866  0.2185  542 VAL B CG1 
9327  C CG2 . VAL B 542 ? 0.7129 0.5200 0.6332 0.0621  0.2659  0.2083  542 VAL B CG2 
9328  N N   . ASP B 543 ? 0.8967 0.7292 0.8296 0.0710  0.3083  0.1975  543 ASP B N   
9329  C CA  . ASP B 543 ? 0.8086 0.6672 0.7664 0.0760  0.3070  0.1906  543 ASP B CA  
9330  C C   . ASP B 543 ? 0.9115 0.7766 0.8680 0.0789  0.2837  0.1894  543 ASP B C   
9331  O O   . ASP B 543 ? 0.9128 0.7583 0.8440 0.0789  0.2699  0.1937  543 ASP B O   
9332  C CB  . ASP B 543 ? 1.0034 0.8416 0.9225 0.0868  0.3208  0.1877  543 ASP B CB  
9333  C CG  . ASP B 543 ? 1.0481 0.9135 1.0017 0.0908  0.3283  0.1808  543 ASP B CG  
9334  O OD1 . ASP B 543 ? 1.0896 0.9896 1.0929 0.0866  0.3184  0.1780  543 ASP B OD1 
9335  O OD2 . ASP B 543 ? 1.0768 0.9273 1.0061 0.0987  0.3434  0.1781  543 ASP B OD2 
9336  N N   . MET B 544 ? 0.9474 0.8383 0.9307 0.0820  0.2788  0.1838  544 MET B N   
9337  C CA  . MET B 544 ? 0.7654 0.6665 0.7539 0.0835  0.2486  0.1759  544 MET B CA  
9338  C C   . MET B 544 ? 0.8526 0.7229 0.7878 0.0927  0.2360  0.1729  544 MET B C   
9339  O O   . MET B 544 ? 0.8204 0.6893 0.7509 0.0928  0.2121  0.1694  544 MET B O   
9340  C CB  . MET B 544 ? 0.7281 0.6621 0.7569 0.0843  0.2435  0.1684  544 MET B CB  
9341  C CG  . MET B 544 ? 0.7160 0.6819 0.7973 0.0750  0.2391  0.1682  544 MET B CG  
9342  S SD  . MET B 544 ? 0.9318 0.9331 1.0619 0.0766  0.2442  0.1635  544 MET B SD  
9343  C CE  . MET B 544 ? 0.8106 0.8268 0.9511 0.0767  0.2144  0.1560  544 MET B CE  
9344  N N   . SER B 545 ? 0.8191 0.6656 0.7165 0.1003  0.2512  0.1737  545 SER B N   
9345  C CA  . SER B 545 ? 0.8742 0.6879 0.7174 0.1091  0.2383  0.1701  545 SER B CA  
9346  C C   . SER B 545 ? 1.0559 0.8387 0.8602 0.1093  0.2289  0.1767  545 SER B C   
9347  O O   . SER B 545 ? 1.3379 1.0965 1.1028 0.1160  0.2104  0.1730  545 SER B O   
9348  C CB  . SER B 545 ? 0.9897 0.7822 0.7982 0.1175  0.2591  0.1689  545 SER B CB  
9349  O OG  . SER B 545 ? 1.0547 0.8457 0.8683 0.1149  0.2909  0.1773  545 SER B OG  
9350  N N   . ASP B 546 ? 0.9334 0.7156 0.7489 0.1022  0.2400  0.1861  546 ASP B N   
9351  C CA  . ASP B 546 ? 0.9232 0.6731 0.7013 0.1032  0.2316  0.1936  546 ASP B CA  
9352  C C   . ASP B 546 ? 0.9982 0.7611 0.7995 0.1005  0.2033  0.1904  546 ASP B C   
9353  O O   . ASP B 546 ? 1.1202 0.8565 0.8904 0.1042  0.1896  0.1944  546 ASP B O   
9354  C CB  . ASP B 546 ? 0.8881 0.6296 0.6683 0.0961  0.2553  0.2025  546 ASP B CB  
9355  C CG  . ASP B 546 ? 1.0822 0.8132 0.8437 0.0983  0.2802  0.2007  546 ASP B CG  
9356  O OD1 . ASP B 546 ? 1.1772 0.8796 0.8875 0.1083  0.2793  0.1982  546 ASP B OD1 
9357  O OD2 . ASP B 546 ? 1.1156 0.8661 0.9142 0.0905  0.2997  0.2013  546 ASP B OD2 
9358  N N   . LEU B 547 ? 0.9311 0.7328 0.7850 0.0951  0.1953  0.1836  547 LEU B N   
9359  C CA  . LEU B 547 ? 0.8373 0.6527 0.7160 0.0923  0.1725  0.1802  547 LEU B CA  
9360  C C   . LEU B 547 ? 0.8367 0.6521 0.7054 0.0990  0.1472  0.1713  547 LEU B C   
9361  O O   . LEU B 547 ? 0.8197 0.6354 0.6777 0.1030  0.1475  0.1658  547 LEU B O   
9362  C CB  . LEU B 547 ? 0.6644 0.5183 0.5994 0.0833  0.1764  0.1770  547 LEU B CB  
9363  C CG  . LEU B 547 ? 0.8966 0.7565 0.8518 0.0753  0.2004  0.1840  547 LEU B CG  
9364  C CD1 . LEU B 547 ? 0.7103 0.6090 0.7187 0.0683  0.2008  0.1785  547 LEU B CD1 
9365  C CD2 . LEU B 547 ? 0.8415 0.6811 0.7879 0.0709  0.2025  0.1923  547 LEU B CD2 
9366  N N   . PRO B 548 ? 0.8342 0.6494 0.7086 0.1003  0.1259  0.1692  548 PRO B N   
9367  C CA  . PRO B 548 ? 0.7631 0.5830 0.6379 0.1053  0.1020  0.1603  548 PRO B CA  
9368  C C   . PRO B 548 ? 0.7722 0.6299 0.6942 0.0997  0.0982  0.1523  548 PRO B C   
9369  O O   . PRO B 548 ? 0.8635 0.7368 0.8118 0.0979  0.0859  0.1489  548 PRO B O   
9370  C CB  . PRO B 548 ? 0.8018 0.6069 0.6681 0.1092  0.0843  0.1625  548 PRO B CB  
9371  C CG  . PRO B 548 ? 0.7549 0.5652 0.6411 0.1030  0.0967  0.1690  548 PRO B CG  
9372  C CD  . PRO B 548 ? 0.7283 0.5386 0.6121 0.0974  0.1234  0.1748  548 PRO B CD  
9373  N N   . VAL B 549 ? 0.7241 0.5948 0.6552 0.0977  0.1099  0.1499  549 VAL B N   
9374  C CA  . VAL B 549 ? 0.7002 0.6022 0.6697 0.0930  0.1076  0.1437  549 VAL B CA  
9375  C C   . VAL B 549 ? 0.6964 0.5964 0.6561 0.0965  0.1022  0.1374  549 VAL B C   
9376  O O   . VAL B 549 ? 0.8695 0.7456 0.7941 0.1021  0.1046  0.1376  549 VAL B O   
9377  C CB  . VAL B 549 ? 0.7100 0.6317 0.7070 0.0870  0.1251  0.1468  549 VAL B CB  
9378  C CG1 . VAL B 549 ? 0.6328 0.5575 0.6444 0.0819  0.1278  0.1513  549 VAL B CG1 
9379  C CG2 . VAL B 549 ? 0.8079 0.7198 0.7890 0.0893  0.1443  0.1505  549 VAL B CG2 
9380  N N   . ALA B 550 ? 0.6517 0.5741 0.6399 0.0932  0.0954  0.1317  550 ALA B N   
9381  C CA  . ALA B 550 ? 0.5532 0.4736 0.5363 0.0951  0.0901  0.1257  550 ALA B CA  
9382  C C   . ALA B 550 ? 0.6861 0.6325 0.7036 0.0899  0.0905  0.1231  550 ALA B C   
9383  O O   . ALA B 550 ? 0.7347 0.6991 0.7769 0.0853  0.0892  0.1239  550 ALA B O   
9384  C CB  . ALA B 550 ? 0.5416 0.4485 0.5101 0.0978  0.0700  0.1205  550 ALA B CB  
9385  N N   . GLY B 551 ? 0.6618 0.6066 0.6770 0.0912  0.0921  0.1198  551 GLY B N   
9386  C CA  . GLY B 551 ? 0.4455 0.4087 0.4864 0.0873  0.0920  0.1182  551 GLY B CA  
9387  C C   . GLY B 551 ? 0.6262 0.5828 0.6646 0.0864  0.0797  0.1122  551 GLY B C   
9388  O O   . GLY B 551 ? 0.6913 0.6271 0.7051 0.0903  0.0741  0.1085  551 GLY B O   
9389  N N   . VAL B 552 ? 0.5580 0.5302 0.6203 0.0807  0.0754  0.1109  552 VAL B N   
9390  C CA  . VAL B 552 ? 0.5161 0.4837 0.5822 0.0776  0.0651  0.1057  552 VAL B CA  
9391  C C   . VAL B 552 ? 0.6037 0.5810 0.6863 0.0735  0.0699  0.1072  552 VAL B C   
9392  O O   . VAL B 552 ? 0.6944 0.6879 0.7925 0.0709  0.0756  0.1110  552 VAL B O   
9393  C CB  . VAL B 552 ? 0.5598 0.5340 0.6394 0.0738  0.0524  0.1023  552 VAL B CB  
9394  C CG1 . VAL B 552 ? 0.7515 0.7160 0.8318 0.0711  0.0398  0.0958  552 VAL B CG1 
9395  C CG2 . VAL B 552 ? 0.5555 0.5235 0.6225 0.0783  0.0480  0.1033  552 VAL B CG2 
9396  N N   . ALA B 553 ? 0.5983 0.5627 0.6749 0.0732  0.0669  0.1040  553 ALA B N   
9397  C CA  . ALA B 553 ? 0.5854 0.5523 0.6730 0.0698  0.0704  0.1060  553 ALA B CA  
9398  C C   . ALA B 553 ? 0.6619 0.6226 0.7573 0.0628  0.0606  0.1011  553 ALA B C   
9399  O O   . ALA B 553 ? 0.7896 0.7317 0.8739 0.0636  0.0564  0.0971  553 ALA B O   
9400  C CB  . ALA B 553 ? 0.5102 0.4637 0.5836 0.0768  0.0769  0.1068  553 ALA B CB  
9401  N N   . PRO B 554 ? 0.5950 0.5707 0.7111 0.0560  0.0569  0.1005  554 PRO B N   
9402  C CA  . PRO B 554 ? 0.4642 0.4372 0.5947 0.0485  0.0475  0.0953  554 PRO B CA  
9403  C C   . PRO B 554 ? 0.5831 0.5466 0.7188 0.0423  0.0501  0.0960  554 PRO B C   
9404  O O   . PRO B 554 ? 0.6504 0.6026 0.7901 0.0378  0.0404  0.0900  554 PRO B O   
9405  C CB  . PRO B 554 ? 0.5007 0.4959 0.6568 0.0436  0.0480  0.0957  554 PRO B CB  
9406  C CG  . PRO B 554 ? 0.5810 0.5841 0.7288 0.0501  0.0524  0.0988  554 PRO B CG  
9407  C CD  . PRO B 554 ? 0.6252 0.6204 0.7540 0.0552  0.0610  0.1035  554 PRO B CD  
9408  N N   . GLU B 555 ? 0.6386 0.6048 0.7744 0.0418  0.0615  0.1032  555 GLU B N   
9409  C CA  . GLU B 555 ? 0.4722 0.4261 0.6106 0.0361  0.0646  0.1056  555 GLU B CA  
9410  C C   . GLU B 555 ? 0.5763 0.5211 0.6982 0.0433  0.0721  0.1120  555 GLU B C   
9411  O O   . GLU B 555 ? 0.9264 0.8736 1.0512 0.0406  0.0792  0.1190  555 GLU B O   
9412  C CB  . GLU B 555 ? 0.6602 0.6275 0.8215 0.0254  0.0709  0.1091  555 GLU B CB  
9413  C CG  . GLU B 555 ? 0.5951 0.5814 0.7793 0.0209  0.0667  0.1042  555 GLU B CG  
9414  C CD  . GLU B 555 ? 0.6876 0.6885 0.8949 0.0116  0.0770  0.1075  555 GLU B CD  
9415  O OE1 . GLU B 555 ? 0.8385 0.8309 1.0426 0.0064  0.0868  0.1138  555 GLU B OE1 
9416  O OE2 . GLU B 555 ? 0.6213 0.6409 0.8489 0.0101  0.0761  0.1039  555 GLU B OE2 
9417  N N   . TRP B 556 ? 0.6000 0.5333 0.7044 0.0530  0.0705  0.1095  556 TRP B N   
9418  C CA  . TRP B 556 ? 0.6042 0.5326 0.6986 0.0617  0.0772  0.1150  556 TRP B CA  
9419  C C   . TRP B 556 ? 0.6388 0.5442 0.7271 0.0615  0.0769  0.1160  556 TRP B C   
9420  O O   . TRP B 556 ? 0.5774 0.4687 0.6669 0.0547  0.0712  0.1109  556 TRP B O   
9421  C CB  . TRP B 556 ? 0.6198 0.5476 0.7018 0.0724  0.0791  0.1121  556 TRP B CB  
9422  C CG  . TRP B 556 ? 0.5949 0.5006 0.6600 0.0761  0.0745  0.1042  556 TRP B CG  
9423  C CD1 . TRP B 556 ? 0.6072 0.5075 0.6643 0.0742  0.0666  0.0972  556 TRP B CD1 
9424  C CD2 . TRP B 556 ? 0.6409 0.5239 0.6922 0.0833  0.0764  0.1018  556 TRP B CD2 
9425  N NE1 . TRP B 556 ? 0.7823 0.6570 0.8183 0.0793  0.0632  0.0902  556 TRP B NE1 
9426  C CE2 . TRP B 556 ? 0.6754 0.5390 0.7080 0.0849  0.0701  0.0925  556 TRP B CE2 
9427  C CE3 . TRP B 556 ? 0.6222 0.4979 0.6741 0.0895  0.0819  0.1062  556 TRP B CE3 
9428  C CZ2 . TRP B 556 ? 0.7649 0.6015 0.7783 0.0922  0.0708  0.0868  556 TRP B CZ2 
9429  C CZ3 . TRP B 556 ? 0.6513 0.5018 0.6879 0.0972  0.0827  0.1011  556 TRP B CZ3 
9430  C CH2 . TRP B 556 ? 0.7344 0.5653 0.7514 0.0984  0.0780  0.0911  556 TRP B CH2 
9431  N N   . MET B 557 ? 0.6155 0.5165 0.6988 0.0690  0.0816  0.1220  557 MET B N   
9432  C CA  . MET B 557 ? 0.5760 0.4518 0.6518 0.0709  0.0812  0.1238  557 MET B CA  
9433  C C   . MET B 557 ? 0.6036 0.4776 0.6746 0.0846  0.0847  0.1281  557 MET B C   
9434  O O   . MET B 557 ? 0.7595 0.6120 0.8217 0.0921  0.0846  0.1256  557 MET B O   
9435  C CB  . MET B 557 ? 0.6435 0.5144 0.7251 0.0601  0.0825  0.1307  557 MET B CB  
9436  C CG  . MET B 557 ? 0.8620 0.7527 0.9483 0.0584  0.0870  0.1387  557 MET B CG  
9437  S SD  . MET B 557 ? 0.6220 0.5032 0.6973 0.0693  0.0878  0.1487  557 MET B SD  
9438  C CE  . MET B 557 ? 0.7261 0.5713 0.7925 0.0656  0.0874  0.1515  557 MET B CE  
9439  N N   . SER B 558 ? 0.6098 0.5056 0.6881 0.0881  0.0871  0.1335  558 SER B N   
9440  C CA  . SER B 558 ? 0.6444 0.5423 0.7249 0.1010  0.0884  0.1376  558 SER B CA  
9441  C C   . SER B 558 ? 0.6452 0.5431 0.7256 0.1122  0.0929  0.1313  558 SER B C   
9442  O O   . SER B 558 ? 0.6952 0.5990 0.7726 0.1098  0.0952  0.1252  558 SER B O   
9443  C CB  . SER B 558 ? 0.6311 0.5521 0.7207 0.1006  0.0876  0.1435  558 SER B CB  
9444  O OG  . SER B 558 ? 0.7553 0.6974 0.8533 0.1006  0.0904  0.1393  558 SER B OG  
9445  N N   . GLU B 559 ? 0.7752 0.6660 0.8583 0.1247  0.0946  0.1329  559 GLU B N   
9446  C CA  . GLU B 559 ? 0.6433 0.5365 0.7289 0.1363  0.1024  0.1271  559 GLU B CA  
9447  C C   . GLU B 559 ? 0.6720 0.5956 0.7730 0.1360  0.1067  0.1283  559 GLU B C   
9448  O O   . GLU B 559 ? 0.8357 0.7632 0.9356 0.1402  0.1155  0.1234  559 GLU B O   
9449  C CB  . GLU B 559 ? 0.5960 0.4791 0.6879 0.1509  0.1040  0.1287  559 GLU B CB  
9450  C CG  . GLU B 559 ? 0.7708 0.6190 0.8454 0.1535  0.1023  0.1252  559 GLU B CG  
9451  C CD  . GLU B 559 ? 0.8307 0.6660 0.9113 0.1659  0.0996  0.1299  559 GLU B CD  
9452  O OE1 . GLU B 559 ? 0.8348 0.6769 0.9230 0.1648  0.0922  0.1394  559 GLU B OE1 
9453  O OE2 . GLU B 559 ? 0.9571 0.7729 1.0326 0.1775  0.1046  0.1240  559 GLU B OE2 
9454  N N   . LYS B 560 ? 0.6628 0.6050 0.7756 0.1304  0.1010  0.1347  560 LYS B N   
9455  C CA  . LYS B 560 ? 0.6400 0.6091 0.7679 0.1281  0.1032  0.1355  560 LYS B CA  
9456  C C   . LYS B 560 ? 0.6506 0.6207 0.7684 0.1204  0.1074  0.1307  560 LYS B C   
9457  O O   . LYS B 560 ? 0.7502 0.7320 0.8743 0.1224  0.1146  0.1289  560 LYS B O   
9458  C CB  . LYS B 560 ? 0.4841 0.4657 0.6181 0.1220  0.0943  0.1416  560 LYS B CB  
9459  C CG  . LYS B 560 ? 0.6258 0.6094 0.7703 0.1309  0.0875  0.1471  560 LYS B CG  
9460  C CD  . LYS B 560 ? 0.7136 0.7060 0.8573 0.1254  0.0777  0.1526  560 LYS B CD  
9461  C CE  . LYS B 560 ? 0.6638 0.6386 0.7850 0.1161  0.0755  0.1559  560 LYS B CE  
9462  N NZ  . LYS B 560 ? 0.7288 0.7074 0.8434 0.1129  0.0674  0.1614  560 LYS B NZ  
9463  N N   . ALA B 561 ? 0.5228 0.4798 0.6260 0.1118  0.1026  0.1288  561 ALA B N   
9464  C CA  . ALA B 561 ? 0.5279 0.4840 0.6217 0.1054  0.1031  0.1240  561 ALA B CA  
9465  C C   . ALA B 561 ? 0.6431 0.5865 0.7233 0.1128  0.1102  0.1182  561 ALA B C   
9466  O O   . ALA B 561 ? 0.6916 0.6394 0.7662 0.1116  0.1137  0.1163  561 ALA B O   
9467  C CB  . ALA B 561 ? 0.5098 0.4542 0.5960 0.0960  0.0958  0.1222  561 ALA B CB  
9468  N N   . VAL B 562 ? 0.6583 0.5835 0.7306 0.1212  0.1130  0.1156  562 VAL B N   
9469  C CA  . VAL B 562 ? 0.6118 0.5213 0.6666 0.1296  0.1217  0.1093  562 VAL B CA  
9470  C C   . VAL B 562 ? 0.6702 0.5980 0.7383 0.1363  0.1348  0.1118  562 VAL B C   
9471  O O   . VAL B 562 ? 0.6771 0.6012 0.7315 0.1378  0.1432  0.1092  562 VAL B O   
9472  C CB  . VAL B 562 ? 0.5983 0.4819 0.6414 0.1379  0.1225  0.1048  562 VAL B CB  
9473  C CG1 . VAL B 562 ? 0.5585 0.4235 0.5785 0.1472  0.1331  0.0973  562 VAL B CG1 
9474  C CG2 . VAL B 562 ? 0.5831 0.4480 0.6167 0.1293  0.1099  0.1026  562 VAL B CG2 
9475  N N   . ALA B 563 ? 0.6454 0.5924 0.7404 0.1401  0.1361  0.1172  563 ALA B N   
9476  C CA  . ALA B 563 ? 0.6003 0.5684 0.7166 0.1451  0.1477  0.1195  563 ALA B CA  
9477  C C   . ALA B 563 ? 0.6427 0.6259 0.7615 0.1354  0.1480  0.1217  563 ALA B C   
9478  O O   . ALA B 563 ? 0.6823 0.6700 0.8018 0.1372  0.1608  0.1216  563 ALA B O   
9479  C CB  . ALA B 563 ? 0.5247 0.5111 0.6717 0.1500  0.1434  0.1243  563 ALA B CB  
9480  N N   . ILE B 564 ? 0.6736 0.6624 0.7926 0.1253  0.1354  0.1239  564 ILE B N   
9481  C CA  . ILE B 564 ? 0.6032 0.6039 0.7244 0.1166  0.1341  0.1255  564 ILE B CA  
9482  C C   . ILE B 564 ? 0.7159 0.6992 0.8106 0.1164  0.1396  0.1219  564 ILE B C   
9483  O O   . ILE B 564 ? 0.7630 0.7500 0.8573 0.1173  0.1502  0.1231  564 ILE B O   
9484  C CB  . ILE B 564 ? 0.5306 0.5376 0.6550 0.1074  0.1208  0.1274  564 ILE B CB  
9485  C CG1 . ILE B 564 ? 0.5613 0.5865 0.7086 0.1076  0.1162  0.1317  564 ILE B CG1 
9486  C CG2 . ILE B 564 ? 0.5931 0.6038 0.7120 0.0995  0.1188  0.1268  564 ILE B CG2 
9487  C CD1 . ILE B 564 ? 0.6376 0.6607 0.7811 0.1021  0.1053  0.1338  564 ILE B CD1 
9488  N N   . GLY B 565 ? 0.6174 0.5804 0.6896 0.1152  0.1320  0.1176  565 GLY B N   
9489  C CA  . GLY B 565 ? 0.5033 0.4463 0.5463 0.1159  0.1329  0.1134  565 GLY B CA  
9490  C C   . GLY B 565 ? 0.6816 0.6147 0.7107 0.1247  0.1495  0.1125  565 GLY B C   
9491  O O   . GLY B 565 ? 0.7638 0.6912 0.7773 0.1241  0.1554  0.1136  565 GLY B O   
9492  N N   . THR B 566 ? 0.6283 0.5593 0.6641 0.1333  0.1585  0.1112  566 THR B N   
9493  C CA  . THR B 566 ? 0.6525 0.5750 0.6779 0.1427  0.1779  0.1100  566 THR B CA  
9494  C C   . THR B 566 ? 0.7866 0.7310 0.8332 0.1404  0.1913  0.1163  566 THR B C   
9495  O O   . THR B 566 ? 0.7741 0.7068 0.7999 0.1422  0.2048  0.1168  566 THR B O   
9496  C CB  . THR B 566 ? 0.6159 0.5341 0.6503 0.1534  0.1844  0.1069  566 THR B CB  
9497  O OG1 . THR B 566 ? 0.7312 0.6248 0.7431 0.1540  0.1719  0.1009  566 THR B OG1 
9498  C CG2 . THR B 566 ? 0.5710 0.4807 0.5962 0.1643  0.2074  0.1047  566 THR B CG2 
9499  N N   . TYR B 567 ? 0.7406 0.7141 0.8264 0.1362  0.1875  0.1210  567 TYR B N   
9500  C CA  . TYR B 567 ? 0.6684 0.6621 0.7775 0.1326  0.1989  0.1261  567 TYR B CA  
9501  C C   . TYR B 567 ? 0.6859 0.6751 0.7792 0.1232  0.1944  0.1287  567 TYR B C   
9502  O O   . TYR B 567 ? 0.6705 0.6627 0.7666 0.1211  0.2080  0.1325  567 TYR B O   
9503  C CB  . TYR B 567 ? 0.5910 0.6157 0.7465 0.1314  0.1950  0.1292  567 TYR B CB  
9504  C CG  . TYR B 567 ? 0.7045 0.7420 0.8724 0.1231  0.1750  0.1309  567 TYR B CG  
9505  C CD1 . TYR B 567 ? 0.5876 0.6299 0.7536 0.1131  0.1697  0.1329  567 TYR B CD1 
9506  C CD2 . TYR B 567 ? 0.7847 0.8308 0.9692 0.1259  0.1633  0.1310  567 TYR B CD2 
9507  C CE1 . TYR B 567 ? 0.4916 0.5452 0.6684 0.1063  0.1539  0.1338  567 TYR B CE1 
9508  C CE2 . TYR B 567 ? 0.7602 0.8165 0.9529 0.1188  0.1474  0.1329  567 TYR B CE2 
9509  C CZ  . TYR B 567 ? 0.6965 0.7569 0.8852 0.1090  0.1434  0.1338  567 TYR B CZ  
9510  O OH  . TYR B 567 ? 0.7120 0.7805 0.9060 0.1028  0.1295  0.1347  567 TYR B OH  
9511  N N   . VAL B 568 ? 0.7075 0.6885 0.7852 0.1180  0.1766  0.1268  568 VAL B N   
9512  C CA  . VAL B 568 ? 0.6664 0.6422 0.7303 0.1109  0.1708  0.1288  568 VAL B CA  
9513  C C   . VAL B 568 ? 0.7832 0.7313 0.8076 0.1154  0.1802  0.1281  568 VAL B C   
9514  O O   . VAL B 568 ? 0.8488 0.7930 0.8653 0.1126  0.1876  0.1326  568 VAL B O   
9515  C CB  . VAL B 568 ? 0.5940 0.5704 0.6562 0.1052  0.1504  0.1263  568 VAL B CB  
9516  C CG1 . VAL B 568 ? 0.5962 0.5637 0.6420 0.1006  0.1438  0.1271  568 VAL B CG1 
9517  C CG2 . VAL B 568 ? 0.4531 0.4540 0.5482 0.1004  0.1435  0.1281  568 VAL B CG2 
9518  N N   . VAL B 569 ? 0.7770 0.7031 0.7741 0.1227  0.1804  0.1226  569 VAL B N   
9519  C CA  . VAL B 569 ? 0.7322 0.6272 0.6845 0.1283  0.1885  0.1210  569 VAL B CA  
9520  C C   . VAL B 569 ? 0.7549 0.6507 0.7089 0.1329  0.2156  0.1253  569 VAL B C   
9521  O O   . VAL B 569 ? 0.7959 0.6773 0.7262 0.1322  0.2258  0.1297  569 VAL B O   
9522  C CB  . VAL B 569 ? 0.6731 0.5422 0.5946 0.1348  0.1805  0.1124  569 VAL B CB  
9523  C CG1 . VAL B 569 ? 0.7851 0.6187 0.6545 0.1414  0.1884  0.1102  569 VAL B CG1 
9524  C CG2 . VAL B 569 ? 0.7377 0.6070 0.6619 0.1286  0.1551  0.1085  569 VAL B CG2 
9525  N N   . THR B 570 ? 0.7083 0.6211 0.6921 0.1376  0.2276  0.1245  570 THR B N   
9526  C CA  . THR B 570 ? 0.6850 0.6037 0.6804 0.1418  0.2551  0.1281  570 THR B CA  
9527  C C   . THR B 570 ? 0.8504 0.7871 0.8693 0.1324  0.2623  0.1364  570 THR B C   
9528  O O   . THR B 570 ? 0.9178 0.8478 0.9293 0.1332  0.2854  0.1409  570 THR B O   
9529  C CB  . THR B 570 ? 0.6933 0.6318 0.7256 0.1489  0.2622  0.1254  570 THR B CB  
9530  O OG1 . THR B 570 ? 0.7990 0.7164 0.8065 0.1569  0.2540  0.1176  570 THR B OG1 
9531  C CG2 . THR B 570 ? 0.5789 0.5242 0.6265 0.1548  0.2924  0.1277  570 THR B CG2 
9532  N N   . SER B 571 ? 0.7936 0.7507 0.8392 0.1233  0.2438  0.1383  571 SER B N   
9533  C CA  . SER B 571 ? 0.6950 0.6669 0.7627 0.1136  0.2474  0.1450  571 SER B CA  
9534  C C   . SER B 571 ? 0.7485 0.6933 0.7751 0.1104  0.2472  0.1489  571 SER B C   
9535  O O   . SER B 571 ? 0.8565 0.8064 0.8948 0.1029  0.2529  0.1550  571 SER B O   
9536  C CB  . SER B 571 ? 0.6910 0.6892 0.7948 0.1063  0.2273  0.1444  571 SER B CB  
9537  O OG  . SER B 571 ? 0.6426 0.6657 0.7857 0.1090  0.2275  0.1425  571 SER B OG  
9538  N N   . GLY B 572 ? 0.8570 0.7721 0.8366 0.1161  0.2396  0.1453  572 GLY B N   
9539  C CA  . GLY B 572 ? 0.8667 0.7526 0.8029 0.1153  0.2364  0.1488  572 GLY B CA  
9540  C C   . GLY B 572 ? 0.7817 0.6633 0.7086 0.1122  0.2085  0.1461  572 GLY B C   
9541  O O   . GLY B 572 ? 0.9609 0.8195 0.8553 0.1123  0.2026  0.1491  572 GLY B O   
9542  N N   . ILE B 573 ? 0.7481 0.6505 0.7031 0.1099  0.1916  0.1407  573 ILE B N   
9543  C CA  . ILE B 573 ? 0.7438 0.6465 0.6975 0.1064  0.1674  0.1377  573 ILE B CA  
9544  C C   . ILE B 573 ? 0.8418 0.7294 0.7735 0.1112  0.1531  0.1298  573 ILE B C   
9545  O O   . ILE B 573 ? 0.9025 0.7968 0.8453 0.1136  0.1550  0.1256  573 ILE B O   
9546  C CB  . ILE B 573 ? 0.5828 0.5178 0.5821 0.0992  0.1597  0.1376  573 ILE B CB  
9547  C CG1 . ILE B 573 ? 0.4799 0.4280 0.5013 0.0933  0.1704  0.1441  573 ILE B CG1 
9548  C CG2 . ILE B 573 ? 0.6331 0.5701 0.6341 0.0962  0.1379  0.1337  573 ILE B CG2 
9549  C CD1 . ILE B 573 ? 0.4994 0.4778 0.5641 0.0881  0.1692  0.1436  573 ILE B CD1 
9550  N N   . ASP B 574 ? 0.7359 0.6025 0.6382 0.1126  0.1374  0.1277  574 ASP B N   
9551  C CA  . ASP B 574 ? 0.6520 0.5034 0.5353 0.1158  0.1211  0.1193  574 ASP B CA  
9552  C C   . ASP B 574 ? 0.7532 0.6290 0.6740 0.1101  0.1087  0.1151  574 ASP B C   
9553  O O   . ASP B 574 ? 0.7407 0.6371 0.6894 0.1041  0.1029  0.1176  574 ASP B O   
9554  C CB  . ASP B 574 ? 0.8226 0.6506 0.6739 0.1179  0.1034  0.1179  574 ASP B CB  
9555  C CG  . ASP B 574 ? 1.0630 0.8591 0.8665 0.1245  0.1143  0.1223  574 ASP B CG  
9556  O OD1 . ASP B 574 ? 1.0743 0.8496 0.8473 0.1307  0.1252  0.1193  574 ASP B OD1 
9557  O OD2 . ASP B 574 ? 0.9986 0.7880 0.7929 0.1238  0.1129  0.1290  574 ASP B OD2 
9558  N N   . THR B 575 ? 0.7263 0.5973 0.6458 0.1119  0.1057  0.1090  575 THR B N   
9559  C CA  . THR B 575 ? 0.5854 0.4755 0.5370 0.1061  0.0961  0.1062  575 THR B CA  
9560  C C   . THR B 575 ? 0.7083 0.5836 0.6491 0.1049  0.0776  0.0981  575 THR B C   
9561  O O   . THR B 575 ? 0.7553 0.6046 0.6647 0.1104  0.0755  0.0926  575 THR B O   
9562  C CB  . THR B 575 ? 0.6672 0.5678 0.6359 0.1081  0.1093  0.1073  575 THR B CB  
9563  O OG1 . THR B 575 ? 0.7748 0.6927 0.7604 0.1080  0.1240  0.1141  575 THR B OG1 
9564  C CG2 . THR B 575 ? 0.6582 0.5738 0.6543 0.1025  0.1007  0.1059  575 THR B CG2 
9565  N N   . TRP B 576 ? 0.7367 0.6284 0.7045 0.0975  0.0647  0.0968  576 TRP B N   
9566  C CA  . TRP B 576 ? 0.6989 0.5826 0.6683 0.0938  0.0468  0.0893  576 TRP B CA  
9567  C C   . TRP B 576 ? 0.7528 0.6481 0.7480 0.0883  0.0495  0.0888  576 TRP B C   
9568  O O   . TRP B 576 ? 0.7694 0.6864 0.7891 0.0850  0.0583  0.0945  576 TRP B O   
9569  C CB  . TRP B 576 ? 0.7042 0.5996 0.6905 0.0893  0.0319  0.0885  576 TRP B CB  
9570  C CG  . TRP B 576 ? 0.6579 0.5321 0.6147 0.0946  0.0181  0.0854  576 TRP B CG  
9571  C CD1 . TRP B 576 ? 0.6858 0.5457 0.6342 0.0942  -0.0030 0.0773  576 TRP B CD1 
9572  C CD2 . TRP B 576 ? 0.7576 0.6206 0.6883 0.1009  0.0234  0.0908  576 TRP B CD2 
9573  N NE1 . TRP B 576 ? 0.6878 0.5271 0.6032 0.1012  -0.0129 0.0773  576 TRP B NE1 
9574  C CE2 . TRP B 576 ? 0.7715 0.6113 0.6743 0.1053  0.0042  0.0861  576 TRP B CE2 
9575  C CE3 . TRP B 576 ? 0.8466 0.7159 0.7756 0.1028  0.0419  0.0992  576 TRP B CE3 
9576  C CZ2 . TRP B 576 ? 0.8411 0.6612 0.7096 0.1123  0.0042  0.0908  576 TRP B CZ2 
9577  C CZ3 . TRP B 576 ? 0.7960 0.6472 0.6949 0.1083  0.0434  0.1037  576 TRP B CZ3 
9578  C CH2 . TRP B 576 ? 0.8598 0.6854 0.7266 0.1133  0.0252  0.1000  576 TRP B CH2 
9579  N N   . LEU B 577 ? 0.6962 0.5743 0.6833 0.0873  0.0414  0.0820  577 LEU B N   
9580  C CA  . LEU B 577 ? 0.5680 0.4511 0.5756 0.0819  0.0435  0.0821  577 LEU B CA  
9581  C C   . LEU B 577 ? 0.6469 0.5303 0.6719 0.0725  0.0274  0.0764  577 LEU B C   
9582  O O   . LEU B 577 ? 0.7520 0.6176 0.7618 0.0730  0.0127  0.0684  577 LEU B O   
9583  C CB  . LEU B 577 ? 0.6309 0.4914 0.6167 0.0889  0.0506  0.0792  577 LEU B CB  
9584  C CG  . LEU B 577 ? 0.6411 0.5023 0.6148 0.0987  0.0684  0.0840  577 LEU B CG  
9585  C CD1 . LEU B 577 ? 0.6000 0.4394 0.5568 0.1063  0.0752  0.0800  577 LEU B CD1 
9586  C CD2 . LEU B 577 ? 0.4427 0.3326 0.4454 0.0964  0.0785  0.0931  577 LEU B CD2 
9587  N N   . GLY B 578 ? 0.6223 0.5254 0.6791 0.0640  0.0303  0.0803  578 GLY B N   
9588  C CA  . GLY B 578 ? 0.6612 0.5690 0.7429 0.0534  0.0191  0.0761  578 GLY B CA  
9589  C C   . GLY B 578 ? 0.6580 0.5477 0.7396 0.0487  0.0174  0.0728  578 GLY B C   
9590  O O   . GLY B 578 ? 0.8121 0.6999 0.9120 0.0393  0.0067  0.0676  578 GLY B O   
9591  N N   . VAL B 579 ? 0.5443 0.4208 0.6083 0.0550  0.0282  0.0760  579 VAL B N   
9592  C CA  . VAL B 579 ? 0.6505 0.5051 0.7098 0.0528  0.0279  0.0735  579 VAL B CA  
9593  C C   . VAL B 579 ? 0.7952 0.6239 0.8186 0.0647  0.0278  0.0677  579 VAL B C   
9594  O O   . VAL B 579 ? 0.7250 0.5583 0.7344 0.0747  0.0386  0.0716  579 VAL B O   
9595  C CB  . VAL B 579 ? 0.6191 0.4809 0.6901 0.0515  0.0418  0.0835  579 VAL B CB  
9596  C CG1 . VAL B 579 ? 0.7355 0.5698 0.7967 0.0521  0.0422  0.0818  579 VAL B CG1 
9597  C CG2 . VAL B 579 ? 0.6957 0.5795 0.7968 0.0398  0.0441  0.0889  579 VAL B CG2 
9598  N N   . ALA B 580 ? 0.7642 0.5653 0.7729 0.0635  0.0164  0.0579  580 ALA B N   
9599  C CA  . ALA B 580 ? 0.6738 0.4464 0.6438 0.0755  0.0173  0.0510  580 ALA B CA  
9600  C C   . ALA B 580 ? 0.7765 0.5397 0.7402 0.0838  0.0332  0.0552  580 ALA B C   
9601  O O   . ALA B 580 ? 0.9115 0.6679 0.8893 0.0785  0.0335  0.0571  580 ALA B O   
9602  C CB  . ALA B 580 ? 0.8977 0.6409 0.8525 0.0716  -0.0013 0.0379  580 ALA B CB  
9603  N N   . PRO B 581 ? 0.7926 0.5549 0.7373 0.0970  0.0468  0.0573  581 PRO B N   
9604  C CA  . PRO B 581 ? 0.6978 0.4524 0.6412 0.1064  0.0606  0.0605  581 PRO B CA  
9605  C C   . PRO B 581 ? 0.8833 0.5988 0.8010 0.1118  0.0568  0.0497  581 PRO B C   
9606  O O   . PRO B 581 ? 0.9730 0.6672 0.8684 0.1095  0.0441  0.0392  581 PRO B O   
9607  C CB  . PRO B 581 ? 0.7095 0.4779 0.6454 0.1176  0.0761  0.0648  581 PRO B CB  
9608  C CG  . PRO B 581 ? 0.7684 0.5320 0.6817 0.1173  0.0702  0.0600  581 PRO B CG  
9609  C CD  . PRO B 581 ? 0.8670 0.6333 0.7912 0.1041  0.0507  0.0569  581 PRO B CD  
9610  N N   . PRO B 582 ? 0.9206 0.6237 0.8395 0.1197  0.0660  0.0512  582 PRO B N   
9611  C CA  . PRO B 582 ? 1.0085 0.6712 0.9015 0.1255  0.0626  0.0398  582 PRO B CA  
9612  C C   . PRO B 582 ? 0.9948 0.6382 0.8504 0.1404  0.0718  0.0311  582 PRO B C   
9613  O O   . PRO B 582 ? 0.9452 0.5794 0.7940 0.1544  0.0868  0.0307  582 PRO B O   
9614  C CB  . PRO B 582 ? 0.8404 0.4987 0.7505 0.1298  0.0699  0.0462  582 PRO B CB  
9615  C CG  . PRO B 582 ? 0.7849 0.4786 0.7176 0.1346  0.0823  0.0586  582 PRO B CG  
9616  C CD  . PRO B 582 ? 0.7680 0.4910 0.7109 0.1245  0.0781  0.0626  582 PRO B CD  
9617  N N   . VAL B 583 ? 0.8829 0.5193 0.7136 0.1379  0.0631  0.0245  583 VAL B N   
9618  C CA  . VAL B 583 ? 0.8505 0.4651 0.6384 0.1512  0.0723  0.0168  583 VAL B CA  
9619  C C   . VAL B 583 ? 1.0577 0.6337 0.8041 0.1496  0.0541  0.0019  583 VAL B C   
9620  O O   . VAL B 583 ? 1.1682 0.7173 0.8708 0.1615  0.0617  -0.0060 583 VAL B O   
9621  C CB  . VAL B 583 ? 0.8341 0.4761 0.6228 0.1542  0.0846  0.0255  583 VAL B CB  
9622  C CG1 . VAL B 583 ? 0.8441 0.5200 0.6699 0.1579  0.1028  0.0379  583 VAL B CG1 
9623  C CG2 . VAL B 583 ? 0.7918 0.4504 0.5886 0.1414  0.0672  0.0281  583 VAL B CG2 
9624  N N   . THR B 584 ? 1.0061 0.5788 0.7657 0.1352  0.0307  -0.0024 584 THR B N   
9625  C CA  . THR B 584 ? 0.8609 0.3987 0.5864 0.1320  0.0083  -0.0174 584 THR B CA  
9626  C C   . THR B 584 ? 1.1209 0.6105 0.7986 0.1448  0.0121  -0.0315 584 THR B C   
9627  O O   . THR B 584 ? 1.3144 0.7745 0.9441 0.1505  0.0038  -0.0422 584 THR B O   
9628  C CB  . THR B 584 ? 1.0255 0.5676 0.7852 0.1140  -0.0143 -0.0200 584 THR B CB  
9629  O OG1 . THR B 584 ? 1.1658 0.7521 0.9702 0.1035  -0.0139 -0.0070 584 THR B OG1 
9630  C CG2 . THR B 584 ? 1.3733 0.8873 1.1076 0.1084  -0.0422 -0.0351 584 THR B CG2 
9631  N N   . GLY B 585 ? 1.2061 0.6852 0.8944 0.1499  0.0239  -0.0316 585 GLY B N   
9632  C CA  . GLY B 585 ? 1.0925 0.5249 0.7393 0.1626  0.0285  -0.0456 585 GLY B CA  
9633  C C   . GLY B 585 ? 1.1431 0.5611 0.7474 0.1820  0.0516  -0.0485 585 GLY B C   
9634  O O   . GLY B 585 ? 1.2996 0.6746 0.8616 0.1934  0.0553  -0.0622 585 GLY B O   
9635  N N   . GLY B 586 ? 1.2151 0.6670 0.8301 0.1856  0.0684  -0.0361 586 GLY B N   
9636  C CA  . GLY B 586 ? 1.1895 0.6326 0.7699 0.2024  0.0941  -0.0366 586 GLY B CA  
9637  C C   . GLY B 586 ? 1.1494 0.5889 0.6935 0.2013  0.0892  -0.0364 586 GLY B C   
9638  O O   . GLY B 586 ? 1.1262 0.6014 0.6925 0.1977  0.0970  -0.0233 586 GLY B O   
9639  N N   . PRO B 587 ? 1.1183 0.5126 0.6039 0.2046  0.0751  -0.0509 587 PRO B N   
9640  C CA  . PRO B 587 ? 1.1487 0.5349 0.5940 0.2045  0.0679  -0.0501 587 PRO B CA  
9641  C C   . PRO B 587 ? 1.2114 0.6150 0.6479 0.2136  0.0985  -0.0380 587 PRO B C   
9642  O O   . PRO B 587 ? 1.2683 0.6898 0.7059 0.2079  0.0932  -0.0289 587 PRO B O   
9643  C CB  . PRO B 587 ? 1.2029 0.5294 0.5782 0.2120  0.0546  -0.0691 587 PRO B CB  
9644  C CG  . PRO B 587 ? 1.3435 0.6545 0.7377 0.2073  0.0402  -0.0800 587 PRO B CG  
9645  C CD  . PRO B 587 ? 1.1868 0.5324 0.6380 0.2086  0.0628  -0.0690 587 PRO B CD  
9646  N N   . GLU B 588 ? 1.2421 0.6402 0.6720 0.2276  0.1307  -0.0381 588 GLU B N   
9647  C CA  . GLU B 588 ? 1.2170 0.6325 0.6445 0.2358  0.1633  -0.0270 588 GLU B CA  
9648  C C   . GLU B 588 ? 1.2386 0.7127 0.7367 0.2255  0.1672  -0.0099 588 GLU B C   
9649  O O   . GLU B 588 ? 1.2223 0.7152 0.7221 0.2226  0.1754  0.0010  588 GLU B O   
9650  C CB  . GLU B 588 ? 1.2949 0.6944 0.7096 0.2532  0.1966  -0.0323 588 GLU B CB  
9651  C CG  . GLU B 588 ? 1.5042 0.9081 0.9002 0.2631  0.2326  -0.0245 588 GLU B CG  
9652  C CD  . GLU B 588 ? 1.6243 1.0225 1.0233 0.2801  0.2683  -0.0286 588 GLU B CD  
9653  O OE1 . GLU B 588 ? 1.4500 0.8249 0.8438 0.2875  0.2643  -0.0411 588 GLU B OE1 
9654  O OE2 . GLU B 588 ? 1.3303 0.7474 0.7391 0.2859  0.3008  -0.0195 588 GLU B OE2 
9655  N N   . VAL B 589 ? 1.2112 0.7108 0.7640 0.2199  0.1603  -0.0075 589 VAL B N   
9656  C CA  . VAL B 589 ? 1.0191 0.5707 0.6350 0.2105  0.1621  0.0074  589 VAL B CA  
9657  C C   . VAL B 589 ? 1.1057 0.6728 0.7280 0.1961  0.1391  0.0131  589 VAL B C   
9658  O O   . VAL B 589 ? 1.1689 0.7681 0.8158 0.1916  0.1469  0.0251  589 VAL B O   
9659  C CB  . VAL B 589 ? 0.9516 0.5202 0.6162 0.2078  0.1568  0.0086  589 VAL B CB  
9660  C CG1 . VAL B 589 ? 0.9849 0.6038 0.7077 0.1986  0.1576  0.0236  589 VAL B CG1 
9661  C CG2 . VAL B 589 ? 1.0610 0.6146 0.7224 0.2240  0.1790  0.0032  589 VAL B CG2 
9662  N N   . VAL B 590 ? 1.0986 0.6425 0.7001 0.1890  0.1106  0.0038  590 VAL B N   
9663  C CA  . VAL B 590 ? 1.0194 0.5769 0.6288 0.1766  0.0871  0.0075  590 VAL B CA  
9664  C C   . VAL B 590 ? 1.0933 0.6434 0.6653 0.1817  0.0960  0.0125  590 VAL B C   
9665  O O   . VAL B 590 ? 1.0406 0.6202 0.6372 0.1753  0.0958  0.0236  590 VAL B O   
9666  C CB  . VAL B 590 ? 0.9885 0.5190 0.5811 0.1696  0.0547  -0.0054 590 VAL B CB  
9667  C CG1 . VAL B 590 ? 0.9577 0.4996 0.5546 0.1597  0.0306  -0.0028 590 VAL B CG1 
9668  C CG2 . VAL B 590 ? 0.8923 0.4314 0.5263 0.1619  0.0465  -0.0081 590 VAL B CG2 
9669  N N   . ASP B 591 ? 1.0303 0.5386 0.5409 0.1937  0.1055  0.0045  591 ASP B N   
9670  C CA  . ASP B 591 ? 1.0718 0.5649 0.5373 0.1995  0.1165  0.0096  591 ASP B CA  
9671  C C   . ASP B 591 ? 1.1859 0.7153 0.6860 0.2002  0.1466  0.0248  591 ASP B C   
9672  O O   . ASP B 591 ? 1.2057 0.7474 0.7060 0.1959  0.1467  0.0348  591 ASP B O   
9673  C CB  . ASP B 591 ? 1.0894 0.5285 0.4808 0.2134  0.1259  -0.0021 591 ASP B CB  
9674  C CG  . ASP B 591 ? 1.6076 1.0233 0.9426 0.2198  0.1378  0.0035  591 ASP B CG  
9675  O OD1 . ASP B 591 ? 1.5497 0.9651 0.8743 0.2135  0.1155  0.0078  591 ASP B OD1 
9676  O OD2 . ASP B 591 ? 1.6549 1.0517 0.9564 0.2316  0.1702  0.0039  591 ASP B OD2 
9677  N N   . ILE B 592 ? 1.2045 0.7504 0.7353 0.2057  0.1710  0.0262  592 ILE B N   
9678  C CA  . ILE B 592 ? 1.1307 0.7127 0.6998 0.2060  0.1983  0.0394  592 ILE B CA  
9679  C C   . ILE B 592 ? 1.0680 0.6932 0.6901 0.1923  0.1852  0.0506  592 ILE B C   
9680  O O   . ILE B 592 ? 1.0700 0.7073 0.6933 0.1891  0.1931  0.0604  592 ILE B O   
9681  C CB  . ILE B 592 ? 0.9487 0.5426 0.5477 0.2151  0.2225  0.0376  592 ILE B CB  
9682  C CG1 . ILE B 592 ? 1.0184 0.5695 0.5621 0.2307  0.2435  0.0274  592 ILE B CG1 
9683  C CG2 . ILE B 592 ? 0.9562 0.5942 0.6074 0.2132  0.2450  0.0509  592 ILE B CG2 
9684  C CD1 . ILE B 592 ? 1.2220 0.7711 0.7859 0.2410  0.2550  0.0195  592 ILE B CD1 
9685  N N   . LEU B 593 ? 1.0144 0.6598 0.6776 0.1844  0.1657  0.0490  593 LEU B N   
9686  C CA  . LEU B 593 ? 1.0725 0.7573 0.7848 0.1722  0.1544  0.0584  593 LEU B CA  
9687  C C   . LEU B 593 ? 1.0528 0.7333 0.7481 0.1649  0.1346  0.0605  593 LEU B C   
9688  O O   . LEU B 593 ? 1.0534 0.7582 0.7704 0.1595  0.1380  0.0704  593 LEU B O   
9689  C CB  . LEU B 593 ? 0.8757 0.5764 0.6277 0.1657  0.1390  0.0559  593 LEU B CB  
9690  C CG  . LEU B 593 ? 0.8729 0.5798 0.6479 0.1730  0.1542  0.0549  593 LEU B CG  
9691  C CD1 . LEU B 593 ? 0.8716 0.5773 0.6667 0.1674  0.1360  0.0505  593 LEU B CD1 
9692  C CD2 . LEU B 593 ? 0.9505 0.6958 0.7694 0.1731  0.1717  0.0661  593 LEU B CD2 
9693  N N   . THR B 594 ? 1.0473 0.6964 0.7053 0.1650  0.1125  0.0508  594 THR B N   
9694  C CA  . THR B 594 ? 1.0666 0.7113 0.7114 0.1593  0.0898  0.0518  594 THR B CA  
9695  C C   . THR B 594 ? 1.0806 0.6905 0.6637 0.1673  0.0932  0.0522  594 THR B C   
9696  O O   . THR B 594 ? 1.2315 0.8303 0.7966 0.1647  0.0698  0.0511  594 THR B O   
9697  C CB  . THR B 594 ? 1.1015 0.7378 0.7517 0.1528  0.0584  0.0413  594 THR B CB  
9698  O OG1 . THR B 594 ? 0.9496 0.5410 0.5459 0.1603  0.0509  0.0289  594 THR B OG1 
9699  C CG2 . THR B 594 ? 0.8212 0.4846 0.5251 0.1449  0.0564  0.0410  594 THR B CG2 
9700  N N   . ASN B 595 ? 1.1374 0.7294 0.6882 0.1771  0.1219  0.0543  595 ASN B N   
9701  C CA  . ASN B 595 ? 1.0318 0.5863 0.5177 0.1848  0.1277  0.0559  595 ASN B CA  
9702  C C   . ASN B 595 ? 1.0646 0.6176 0.5379 0.1916  0.1677  0.0647  595 ASN B C   
9703  O O   . ASN B 595 ? 1.1605 0.7249 0.6395 0.1884  0.1776  0.0767  595 ASN B O   
9704  C CB  . ASN B 595 ? 1.1436 0.6492 0.5680 0.1920  0.1103  0.0414  595 ASN B CB  
9705  C CG  . ASN B 595 ? 1.4513 0.9115 0.7990 0.2010  0.1140  0.0424  595 ASN B CG  
9706  O OD1 . ASN B 595 ? 1.4473 0.9067 0.7837 0.1986  0.1054  0.0514  595 ASN B OD1 
9707  N ND2 . ASN B 595 ? 1.6128 1.0313 0.9031 0.2122  0.1271  0.0333  595 ASN B ND2 
9708  N N   . LYS B 596 ? 1.0739 0.6129 0.5325 0.2010  0.1913  0.0587  596 LYS B N   
9709  C CA  . LYS B 596 ? 1.1506 0.6892 0.6008 0.2076  0.2314  0.0664  596 LYS B CA  
9710  C C   . LYS B 596 ? 1.0916 0.6799 0.6087 0.1996  0.2474  0.0795  596 LYS B C   
9711  O O   . LYS B 596 ? 1.1843 0.7734 0.6953 0.2010  0.2751  0.0889  596 LYS B O   
9712  C CB  . LYS B 596 ? 1.1317 0.6551 0.5698 0.2194  0.2547  0.0570  596 LYS B CB  
9713  C CG  . LYS B 596 ? 1.3247 0.7900 0.6823 0.2306  0.2516  0.0444  596 LYS B CG  
9714  C CD  . LYS B 596 ? 1.4195 0.8735 0.7715 0.2433  0.2806  0.0359  596 LYS B CD  
9715  C CE  . LYS B 596 ? 1.8322 1.2318 1.1163 0.2536  0.2701  0.0189  596 LYS B CE  
9716  N NZ  . LYS B 596 ? 1.7823 1.1863 1.0951 0.2592  0.2722  0.0076  596 LYS B NZ  
9717  N N   . MET B 597 ? 0.9135 0.5408 0.4921 0.1909  0.2306  0.0802  597 MET B N   
9718  C CA  . MET B 597 ? 0.9479 0.6219 0.5903 0.1835  0.2435  0.0912  597 MET B CA  
9719  C C   . MET B 597 ? 1.0282 0.7027 0.6608 0.1775  0.2475  0.1027  597 MET B C   
9720  O O   . MET B 597 ? 0.9970 0.6931 0.6586 0.1751  0.2717  0.1118  597 MET B O   
9721  C CB  . MET B 597 ? 0.9149 0.6227 0.6115 0.1746  0.2194  0.0900  597 MET B CB  
9722  C CG  . MET B 597 ? 0.8981 0.6511 0.6581 0.1687  0.2309  0.0986  597 MET B CG  
9723  S SD  . MET B 597 ? 1.3587 1.1297 1.1566 0.1767  0.2481  0.0946  597 MET B SD  
9724  C CE  . MET B 597 ? 0.8509 0.6266 0.6669 0.1723  0.2168  0.0875  597 MET B CE  
9725  N N   . GLU B 598 ? 1.1488 0.8001 0.7443 0.1754  0.2237  0.1021  598 GLU B N   
9726  C CA  . GLU B 598 ? 1.0507 0.6972 0.6325 0.1708  0.2235  0.1130  598 GLU B CA  
9727  C C   . GLU B 598 ? 1.0601 0.6860 0.6087 0.1761  0.2590  0.1208  598 GLU B C   
9728  O O   . GLU B 598 ? 1.2060 0.8438 0.7706 0.1703  0.2728  0.1324  598 GLU B O   
9729  C CB  . GLU B 598 ? 1.1754 0.7900 0.7103 0.1721  0.1921  0.1090  598 GLU B CB  
9730  C CG  . GLU B 598 ? 1.3674 0.9783 0.8935 0.1677  0.1849  0.1198  598 GLU B CG  
9731  C CD  . GLU B 598 ? 1.4787 1.0609 0.9643 0.1702  0.1508  0.1156  598 GLU B CD  
9732  O OE1 . GLU B 598 ? 1.2596 0.8243 0.7232 0.1743  0.1314  0.1035  598 GLU B OE1 
9733  O OE2 . GLU B 598 ? 1.6398 1.2163 1.1169 0.1681  0.1423  0.1243  598 GLU B OE2 
9734  N N   . ASP B 599 ? 1.1513 0.7453 0.6539 0.1869  0.2751  0.1141  599 ASP B N   
9735  C CA  . ASP B 599 ? 1.2819 0.8534 0.7492 0.1929  0.3127  0.1205  599 ASP B CA  
9736  C C   . ASP B 599 ? 1.0778 0.6879 0.6056 0.1915  0.3459  0.1244  599 ASP B C   
9737  O O   . ASP B 599 ? 1.2819 0.8891 0.8129 0.1904  0.3686  0.1282  599 ASP B O   
9738  C CB  . ASP B 599 ? 1.2883 0.8079 0.6789 0.2061  0.3175  0.1105  599 ASP B CB  
9739  C CG  . ASP B 599 ? 1.4888 0.9719 0.8245 0.2080  0.2794  0.1038  599 ASP B CG  
9740  O OD1 . ASP B 599 ? 1.6001 1.0727 0.9164 0.2037  0.2652  0.1124  599 ASP B OD1 
9741  O OD2 . ASP B 599 ? 1.4870 0.9519 0.8010 0.2139  0.2626  0.0897  599 ASP B OD2 
9742  N N   . TRP B 600 ? 0.9986 0.6503 0.5920 0.1880  0.3358  0.1199  600 TRP B N   
9743  C CA  . TRP B 600 ? 1.0539 0.7437 0.7084 0.1875  0.3621  0.1229  600 TRP B CA  
9744  C C   . TRP B 600 ? 1.1236 0.8563 0.8408 0.1742  0.3571  0.1327  600 TRP B C   
9745  O O   . TRP B 600 ? 1.1589 0.9136 0.9168 0.1683  0.3731  0.1374  600 TRP B O   
9746  C CB  . TRP B 600 ? 1.0639 0.7697 0.7494 0.1938  0.3549  0.1119  600 TRP B CB  
9747  C CG  . TRP B 600 ? 0.9020 0.5681 0.5341 0.2072  0.3595  0.1000  600 TRP B CG  
9748  C CD1 . TRP B 600 ? 1.0540 0.6726 0.6127 0.2153  0.3731  0.0978  600 TRP B CD1 
9749  C CD2 . TRP B 600 ? 1.0074 0.6753 0.6534 0.2144  0.3502  0.0885  600 TRP B CD2 
9750  N NE1 . TRP B 600 ? 1.0341 0.6248 0.5599 0.2270  0.3720  0.0842  600 TRP B NE1 
9751  C CE2 . TRP B 600 ? 1.0833 0.7036 0.6632 0.2265  0.3581  0.0785  600 TRP B CE2 
9752  C CE3 . TRP B 600 ? 0.9901 0.6919 0.6947 0.2119  0.3354  0.0859  600 TRP B CE3 
9753  C CZ2 . TRP B 600 ? 1.2514 0.8579 0.8255 0.2357  0.3515  0.0654  600 TRP B CZ2 
9754  C CZ3 . TRP B 600 ? 0.9926 0.6802 0.6907 0.2210  0.3293  0.0744  600 TRP B CZ3 
9755  C CH2 . TRP B 600 ? 1.0708 0.7117 0.7060 0.2326  0.3374  0.0640  600 TRP B CH2 
9756  N N   . VAL B 601 ? 0.9277 0.6745 0.6632 0.1664  0.3236  0.1319  601 VAL B N   
9757  C CA  . VAL B 601 ? 0.8957 0.6812 0.6882 0.1545  0.3165  0.1393  601 VAL B CA  
9758  C C   . VAL B 601 ? 0.9892 0.7653 0.7645 0.1465  0.2957  0.1449  601 VAL B C   
9759  O O   . VAL B 601 ? 0.8369 0.6417 0.6556 0.1369  0.2878  0.1497  601 VAL B O   
9760  C CB  . VAL B 601 ? 0.9369 0.7579 0.7836 0.1528  0.2998  0.1335  601 VAL B CB  
9761  C CG1 . VAL B 601 ? 0.8494 0.6824 0.7203 0.1615  0.3208  0.1293  601 VAL B CG1 
9762  C CG2 . VAL B 601 ? 0.9129 0.7207 0.7387 0.1535  0.2683  0.1254  601 VAL B CG2 
9763  N N   . GLY B 602 ? 1.0078 0.7435 0.7209 0.1510  0.2860  0.1437  602 GLY B N   
9764  C CA  . GLY B 602 ? 1.0895 0.8137 0.7849 0.1457  0.2652  0.1488  602 GLY B CA  
9765  C C   . GLY B 602 ? 1.0849 0.8263 0.8043 0.1415  0.2304  0.1426  602 GLY B C   
9766  O O   . GLY B 602 ? 1.0743 0.8174 0.7973 0.1363  0.2135  0.1466  602 GLY B O   
9767  N N   . ALA B 603 ? 1.0324 0.7854 0.7689 0.1440  0.2207  0.1329  603 ALA B N   
9768  C CA  . ALA B 603 ? 0.9630 0.7325 0.7242 0.1395  0.1910  0.1268  603 ALA B CA  
9769  C C   . ALA B 603 ? 0.9745 0.7340 0.7249 0.1452  0.1831  0.1157  603 ALA B C   
9770  O O   . ALA B 603 ? 0.9848 0.7352 0.7240 0.1522  0.2025  0.1131  603 ALA B O   
9771  C CB  . ALA B 603 ? 0.8200 0.6324 0.6438 0.1309  0.1909  0.1303  603 ALA B CB  
9772  N N   . LYS B 604 ? 0.9495 0.7101 0.7050 0.1422  0.1556  0.1090  604 LYS B N   
9773  C CA  . LYS B 604 ? 0.8555 0.6040 0.6016 0.1460  0.1462  0.0983  604 LYS B CA  
9774  C C   . LYS B 604 ? 0.8923 0.6642 0.6785 0.1381  0.1241  0.0944  604 LYS B C   
9775  O O   . LYS B 604 ? 0.9652 0.7610 0.7820 0.1306  0.1157  0.0993  604 LYS B O   
9776  C CB  . LYS B 604 ? 0.8855 0.5897 0.5693 0.1529  0.1352  0.0915  604 LYS B CB  
9777  C CG  . LYS B 604 ? 0.9153 0.6123 0.5884 0.1489  0.1069  0.0910  604 LYS B CG  
9778  C CD  . LYS B 604 ? 0.9577 0.6174 0.5839 0.1539  0.0848  0.0799  604 LYS B CD  
9779  C CE  . LYS B 604 ? 1.1252 0.7447 0.6869 0.1617  0.0849  0.0822  604 LYS B CE  
9780  N NZ  . LYS B 604 ? 1.2208 0.8451 0.7856 0.1586  0.0699  0.0899  604 LYS B NZ  
9781  N N   . PHE B 605 ? 0.8869 0.6499 0.6716 0.1397  0.1162  0.0856  605 PHE B N   
9782  C CA  . PHE B 605 ? 0.8530 0.6333 0.6720 0.1318  0.0976  0.0820  605 PHE B CA  
9783  C C   . PHE B 605 ? 0.9429 0.7055 0.7428 0.1288  0.0710  0.0750  605 PHE B C   
9784  O O   . PHE B 605 ? 0.9693 0.6986 0.7230 0.1351  0.0653  0.0693  605 PHE B O   
9785  C CB  . PHE B 605 ? 0.7772 0.5541 0.6052 0.1345  0.1024  0.0766  605 PHE B CB  
9786  C CG  . PHE B 605 ? 0.7058 0.5105 0.5720 0.1347  0.1192  0.0832  605 PHE B CG  
9787  C CD1 . PHE B 605 ? 0.6398 0.4735 0.5475 0.1262  0.1123  0.0877  605 PHE B CD1 
9788  C CD2 . PHE B 605 ? 0.7950 0.5961 0.6554 0.1439  0.1414  0.0844  605 PHE B CD2 
9789  C CE1 . PHE B 605 ? 0.6752 0.5319 0.6147 0.1271  0.1243  0.0933  605 PHE B CE1 
9790  C CE2 . PHE B 605 ? 0.6953 0.5232 0.5945 0.1447  0.1535  0.0899  605 PHE B CE2 
9791  C CZ  . PHE B 605 ? 0.6403 0.4948 0.5771 0.1364  0.1434  0.0943  605 PHE B CZ  
9792  N N   . PHE B 606 ? 0.8229 0.6074 0.6586 0.1196  0.0548  0.0749  606 PHE B N   
9793  C CA  . PHE B 606 ? 0.8144 0.5894 0.6454 0.1157  0.0283  0.0680  606 PHE B CA  
9794  C C   . PHE B 606 ? 0.8730 0.6648 0.7434 0.1066  0.0195  0.0642  606 PHE B C   
9795  O O   . PHE B 606 ? 0.8686 0.6905 0.7780 0.1005  0.0258  0.0705  606 PHE B O   
9796  C CB  . PHE B 606 ? 0.8598 0.6491 0.7022 0.1132  0.0192  0.0734  606 PHE B CB  
9797  C CG  . PHE B 606 ? 0.9241 0.6940 0.7270 0.1209  0.0248  0.0784  606 PHE B CG  
9798  C CD1 . PHE B 606 ? 1.0527 0.8318 0.8570 0.1230  0.0487  0.0880  606 PHE B CD1 
9799  C CD2 . PHE B 606 ? 0.7572 0.5002 0.5239 0.1254  0.0050  0.0742  606 PHE B CD2 
9800  C CE1 . PHE B 606 ? 0.9748 0.7345 0.7433 0.1288  0.0557  0.0939  606 PHE B CE1 
9801  C CE2 . PHE B 606 ? 0.8825 0.6041 0.6089 0.1326  0.0107  0.0805  606 PHE B CE2 
9802  C CZ  . PHE B 606 ? 0.9587 0.6883 0.6861 0.1337  0.0373  0.0907  606 PHE B CZ  
9803  N N   . ILE B 607 ? 0.8921 0.6632 0.7516 0.1053  0.0058  0.0542  607 ILE B N   
9804  C CA  . ILE B 607 ? 0.7188 0.5033 0.6160 0.0953  -0.0012 0.0514  607 ILE B CA  
9805  C C   . ILE B 607 ? 0.8062 0.5979 0.7234 0.0872  -0.0254 0.0463  607 ILE B C   
9806  O O   . ILE B 607 ? 0.9736 0.7413 0.8658 0.0892  -0.0446 0.0372  607 ILE B O   
9807  C CB  . ILE B 607 ? 0.7702 0.5289 0.6510 0.0972  0.0000  0.0439  607 ILE B CB  
9808  C CG1 . ILE B 607 ? 0.7103 0.4652 0.5777 0.1066  0.0249  0.0489  607 ILE B CG1 
9809  C CG2 . ILE B 607 ? 0.6116 0.3815 0.5310 0.0853  -0.0073 0.0422  607 ILE B CG2 
9810  C CD1 . ILE B 607 ? 0.7781 0.4985 0.6131 0.1141  0.0275  0.0400  607 ILE B CD1 
9811  N N   . GLU B 608 ? 0.7981 0.6223 0.7601 0.0787  -0.0248 0.0516  608 GLU B N   
9812  C CA  . GLU B 608 ? 0.8312 0.6674 0.8213 0.0711  -0.0456 0.0468  608 GLU B CA  
9813  C C   . GLU B 608 ? 0.7765 0.6408 0.8166 0.0594  -0.0398 0.0500  608 GLU B C   
9814  O O   . GLU B 608 ? 0.7015 0.5896 0.7611 0.0583  -0.0247 0.0586  608 GLU B O   
9815  C CB  . GLU B 608 ? 0.7195 0.5647 0.7061 0.0762  -0.0524 0.0501  608 GLU B CB  
9816  C CG  . GLU B 608 ? 0.8050 0.6605 0.8196 0.0712  -0.0768 0.0438  608 GLU B CG  
9817  C CD  . GLU B 608 ? 1.0155 0.8469 1.0176 0.0693  -0.1010 0.0315  608 GLU B CD  
9818  O OE1 . GLU B 608 ? 1.0018 0.8041 0.9587 0.0783  -0.1144 0.0270  608 GLU B OE1 
9819  O OE2 . GLU B 608 ? 1.1496 0.9891 1.1852 0.0585  -0.1064 0.0263  608 GLU B OE2 
9820  N N   . THR B 609 ? 0.8528 0.7122 0.9120 0.0502  -0.0517 0.0427  609 THR B N   
9821  C CA  . THR B 609 ? 0.7895 0.6711 0.8940 0.0378  -0.0449 0.0458  609 THR B CA  
9822  C C   . THR B 609 ? 0.8273 0.7384 0.9725 0.0323  -0.0522 0.0459  609 THR B C   
9823  O O   . THR B 609 ? 1.0435 0.9785 1.2210 0.0255  -0.0384 0.0521  609 THR B O   
9824  C CB  . THR B 609 ? 0.7060 0.5691 0.8166 0.0292  -0.0532 0.0385  609 THR B CB  
9825  O OG1 . THR B 609 ? 1.0017 0.8571 1.1181 0.0261  -0.0792 0.0272  609 THR B OG1 
9826  C CG2 . THR B 609 ? 0.6887 0.5210 0.7596 0.0362  -0.0457 0.0375  609 THR B CG2 
9827  N N   . ASP B 610 ? 0.7066 0.6152 0.8497 0.0359  -0.0736 0.0391  610 ASP B N   
9828  C CA  . ASP B 610 ? 0.7892 0.7262 0.9735 0.0328  -0.0816 0.0385  610 ASP B CA  
9829  C C   . ASP B 610 ? 0.8406 0.7915 1.0166 0.0414  -0.0683 0.0474  610 ASP B C   
9830  O O   . ASP B 610 ? 0.8288 0.7626 0.9661 0.0521  -0.0724 0.0485  610 ASP B O   
9831  C CB  . ASP B 610 ? 0.7020 0.6294 0.8862 0.0351  -0.1125 0.0279  610 ASP B CB  
9832  C CG  . ASP B 610 ? 0.7902 0.7471 1.0208 0.0336  -0.1237 0.0262  610 ASP B CG  
9833  O OD1 . ASP B 610 ? 0.7155 0.6990 0.9731 0.0323  -0.1054 0.0335  610 ASP B OD1 
9834  O OD2 . ASP B 610 ? 0.9428 0.8955 1.1827 0.0346  -0.1515 0.0171  610 ASP B OD2 
9835  N N   . PRO B 611 ? 0.7130 0.6919 0.9219 0.0371  -0.0518 0.0536  611 PRO B N   
9836  C CA  . PRO B 611 ? 0.6274 0.6162 0.8270 0.0449  -0.0405 0.0608  611 PRO B CA  
9837  C C   . PRO B 611 ? 0.7224 0.7138 0.9235 0.0527  -0.0575 0.0580  611 PRO B C   
9838  O O   . PRO B 611 ? 0.7030 0.6885 0.8793 0.0613  -0.0528 0.0632  611 PRO B O   
9839  C CB  . PRO B 611 ? 0.4868 0.5018 0.7211 0.0376  -0.0216 0.0657  611 PRO B CB  
9840  C CG  . PRO B 611 ? 0.6459 0.6711 0.9185 0.0266  -0.0273 0.0602  611 PRO B CG  
9841  C CD  . PRO B 611 ? 0.7439 0.7437 0.9965 0.0247  -0.0414 0.0544  611 PRO B CD  
9842  N N   . HIS B 612 ? 0.6628 0.6623 0.8942 0.0498  -0.0777 0.0502  612 HIS B N   
9843  C CA  . HIS B 612 ? 0.6575 0.6588 0.8926 0.0585  -0.0971 0.0475  612 HIS B CA  
9844  C C   . HIS B 612 ? 0.6609 0.6276 0.8406 0.0686  -0.1121 0.0466  612 HIS B C   
9845  O O   . HIS B 612 ? 0.7951 0.7545 0.9542 0.0785  -0.1161 0.0506  612 HIS B O   
9846  C CB  . HIS B 612 ? 0.7165 0.7371 1.0031 0.0529  -0.1162 0.0387  612 HIS B CB  
9847  C CG  . HIS B 612 ? 0.7650 0.8189 1.1050 0.0433  -0.0976 0.0401  612 HIS B CG  
9848  N ND1 . HIS B 612 ? 0.9165 0.9757 1.2759 0.0303  -0.0858 0.0394  612 HIS B ND1 
9849  C CD2 . HIS B 612 ? 0.5982 0.6777 0.9702 0.0457  -0.0872 0.0426  612 HIS B CD2 
9850  C CE1 . HIS B 612 ? 0.9036 0.9913 1.3048 0.0249  -0.0681 0.0419  612 HIS B CE1 
9851  N NE2 . HIS B 612 ? 0.7453 0.8464 1.1557 0.0341  -0.0682 0.0432  612 HIS B NE2 
9852  N N   . LYS B 613 ? 0.7168 0.6596 0.8692 0.0663  -0.1189 0.0418  613 LYS B N   
9853  C CA  . LYS B 613 ? 0.6984 0.6046 0.7918 0.0762  -0.1301 0.0406  613 LYS B CA  
9854  C C   . LYS B 613 ? 0.7006 0.5973 0.7574 0.0823  -0.1050 0.0509  613 LYS B C   
9855  O O   . LYS B 613 ? 0.9073 0.7853 0.9268 0.0920  -0.1080 0.0548  613 LYS B O   
9856  C CB  . LYS B 613 ? 0.7614 0.6430 0.8340 0.0724  -0.1409 0.0318  613 LYS B CB  
9857  C CG  . LYS B 613 ? 0.9728 0.8581 1.0766 0.0668  -0.1711 0.0201  613 LYS B CG  
9858  C CD  . LYS B 613 ? 0.9136 0.7750 1.0021 0.0606  -0.1803 0.0105  613 LYS B CD  
9859  C CE  . LYS B 613 ? 1.1487 0.9668 1.1730 0.0710  -0.1994 0.0042  613 LYS B CE  
9860  N NZ  . LYS B 613 ? 1.2792 1.0698 1.2813 0.0662  -0.2034 -0.0050 613 LYS B NZ  
9861  N N   . ALA B 614 ? 0.6343 0.5440 0.7033 0.0763  -0.0806 0.0558  614 ALA B N   
9862  C CA  . ALA B 614 ? 0.6715 0.5768 0.7150 0.0808  -0.0572 0.0649  614 ALA B CA  
9863  C C   . ALA B 614 ? 0.7116 0.6267 0.7576 0.0861  -0.0531 0.0718  614 ALA B C   
9864  O O   . ALA B 614 ? 0.8267 0.7251 0.8374 0.0929  -0.0447 0.0775  614 ALA B O   
9865  C CB  . ALA B 614 ? 0.5242 0.4468 0.5903 0.0733  -0.0365 0.0685  614 ALA B CB  
9866  N N   . VAL B 615 ? 0.7144 0.6550 0.8022 0.0830  -0.0580 0.0711  615 VAL B N   
9867  C CA  . VAL B 615 ? 0.6970 0.6455 0.7894 0.0883  -0.0549 0.0766  615 VAL B CA  
9868  C C   . VAL B 615 ? 0.7791 0.7015 0.8365 0.0985  -0.0731 0.0767  615 VAL B C   
9869  O O   . VAL B 615 ? 0.8079 0.7182 0.8396 0.1044  -0.0650 0.0841  615 VAL B O   
9870  C CB  . VAL B 615 ? 0.4269 0.4071 0.5719 0.0840  -0.0557 0.0744  615 VAL B CB  
9871  C CG1 . VAL B 615 ? 0.5197 0.5033 0.6673 0.0912  -0.0559 0.0786  615 VAL B CG1 
9872  C CG2 . VAL B 615 ? 0.6120 0.6128 0.7812 0.0749  -0.0345 0.0764  615 VAL B CG2 
9873  N N   . GLU B 616 ? 0.7354 0.6465 0.7892 0.1003  -0.0981 0.0689  616 GLU B N   
9874  C CA  . GLU B 616 ? 0.8316 0.7133 0.8460 0.1109  -0.1186 0.0689  616 GLU B CA  
9875  C C   . GLU B 616 ? 0.7783 0.6263 0.7313 0.1160  -0.1059 0.0743  616 GLU B C   
9876  O O   . GLU B 616 ? 0.9051 0.7331 0.8241 0.1239  -0.1044 0.0814  616 GLU B O   
9877  C CB  . GLU B 616 ? 0.6820 0.5566 0.7028 0.1111  -0.1497 0.0579  616 GLU B CB  
9878  C CG  . GLU B 616 ? 0.9978 0.9025 1.0777 0.1094  -0.1667 0.0528  616 GLU B CG  
9879  C CD  . GLU B 616 ? 1.5124 1.4094 1.5999 0.1107  -0.2017 0.0418  616 GLU B CD  
9880  O OE1 . GLU B 616 ? 1.4182 1.2964 1.4828 0.1068  -0.2088 0.0355  616 GLU B OE1 
9881  O OE2 . GLU B 616 ? 1.5404 1.4496 1.6580 0.1159  -0.2229 0.0390  616 GLU B OE2 
9882  N N   . GLN B 617 ? 0.5843 0.4257 0.5245 0.1115  -0.0949 0.0715  617 GLN B N   
9883  C CA  . GLN B 617 ? 0.7208 0.5325 0.6073 0.1164  -0.0798 0.0755  617 GLN B CA  
9884  C C   . GLN B 617 ? 0.8434 0.6620 0.7268 0.1172  -0.0530 0.0868  617 GLN B C   
9885  O O   . GLN B 617 ? 0.9045 0.6969 0.7432 0.1236  -0.0437 0.0927  617 GLN B O   
9886  C CB  . GLN B 617 ? 0.6802 0.4886 0.5641 0.1115  -0.0718 0.0696  617 GLN B CB  
9887  C CG  . GLN B 617 ? 0.6230 0.4170 0.5020 0.1104  -0.0980 0.0576  617 GLN B CG  
9888  C CD  . GLN B 617 ? 0.8575 0.6561 0.7515 0.1029  -0.0902 0.0519  617 GLN B CD  
9889  O OE1 . GLN B 617 ? 0.8519 0.6504 0.7376 0.1027  -0.0661 0.0563  617 GLN B OE1 
9890  N NE2 . GLN B 617 ? 1.0689 0.8713 0.9874 0.0965  -0.1111 0.0420  617 GLN B NE2 
9891  N N   . ILE B 618 ? 0.6865 0.5389 0.6162 0.1103  -0.0402 0.0897  618 ILE B N   
9892  C CA  . ILE B 618 ? 0.7468 0.6078 0.6791 0.1096  -0.0171 0.0990  618 ILE B CA  
9893  C C   . ILE B 618 ? 0.7911 0.6409 0.7097 0.1155  -0.0227 0.1051  618 ILE B C   
9894  O O   . ILE B 618 ? 0.7624 0.5943 0.6505 0.1189  -0.0088 0.1129  618 ILE B O   
9895  C CB  . ILE B 618 ? 0.6719 0.5686 0.6531 0.1012  -0.0054 0.0994  618 ILE B CB  
9896  C CG1 . ILE B 618 ? 0.6604 0.5627 0.6479 0.0963  0.0040  0.0962  618 ILE B CG1 
9897  C CG2 . ILE B 618 ? 0.5930 0.4988 0.5802 0.1005  0.0126  0.1077  618 ILE B CG2 
9898  C CD1 . ILE B 618 ? 0.7027 0.6348 0.7347 0.0880  0.0077  0.0944  618 ILE B CD1 
9899  N N   . VAL B 619 ? 0.8048 0.6644 0.7473 0.1170  -0.0424 0.1018  619 VAL B N   
9900  C CA  . VAL B 619 ? 0.7989 0.6468 0.7311 0.1239  -0.0506 0.1073  619 VAL B CA  
9901  C C   . VAL B 619 ? 0.7907 0.5963 0.6622 0.1327  -0.0580 0.1112  619 VAL B C   
9902  O O   . VAL B 619 ? 0.8530 0.6403 0.6984 0.1365  -0.0484 0.1205  619 VAL B O   
9903  C CB  . VAL B 619 ? 0.6562 0.5228 0.6282 0.1256  -0.0728 0.1013  619 VAL B CB  
9904  C CG1 . VAL B 619 ? 0.6673 0.5160 0.6241 0.1352  -0.0855 0.1065  619 VAL B CG1 
9905  C CG2 . VAL B 619 ? 0.5663 0.4715 0.5931 0.1175  -0.0607 0.0988  619 VAL B CG2 
9906  N N   . ASN B 620 ? 0.8016 0.5893 0.6482 0.1356  -0.0743 0.1042  620 ASN B N   
9907  C CA  . ASN B 620 ? 0.9182 0.6614 0.6998 0.1446  -0.0821 0.1069  620 ASN B CA  
9908  C C   . ASN B 620 ? 0.9213 0.6466 0.6654 0.1443  -0.0515 0.1149  620 ASN B C   
9909  O O   . ASN B 620 ? 1.0097 0.7048 0.7101 0.1503  -0.0453 0.1239  620 ASN B O   
9910  C CB  . ASN B 620 ? 0.8085 0.5363 0.5719 0.1469  -0.1059 0.0957  620 ASN B CB  
9911  C CG  . ASN B 620 ? 1.0237 0.7635 0.8190 0.1488  -0.1396 0.0880  620 ASN B CG  
9912  O OD1 . ASN B 620 ? 1.1532 0.8944 0.9582 0.1544  -0.1519 0.0922  620 ASN B OD1 
9913  N ND2 . ASN B 620 ? 1.3602 1.1092 1.1755 0.1441  -0.1555 0.0763  620 ASN B ND2 
9914  N N   . ARG B 621 ? 0.8714 0.6147 0.6336 0.1375  -0.0320 0.1122  621 ARG B N   
9915  C CA  . ARG B 621 ? 0.9296 0.6615 0.6661 0.1372  -0.0021 0.1187  621 ARG B CA  
9916  C C   . ARG B 621 ? 0.9683 0.7086 0.7170 0.1347  0.0168  0.1302  621 ARG B C   
9917  O O   . ARG B 621 ? 1.1070 0.8243 0.8201 0.1373  0.0358  0.1384  621 ARG B O   
9918  C CB  . ARG B 621 ? 0.9510 0.7051 0.7145 0.1311  0.0117  0.1130  621 ARG B CB  
9919  C CG  . ARG B 621 ? 1.0105 0.7619 0.7620 0.1307  0.0433  0.1191  621 ARG B CG  
9920  C CD  . ARG B 621 ? 0.9965 0.7065 0.6853 0.1389  0.0512  0.1198  621 ARG B CD  
9921  N NE  . ARG B 621 ? 1.0970 0.8102 0.7845 0.1385  0.0816  0.1225  621 ARG B NE  
9922  C CZ  . ARG B 621 ? 1.2892 0.9713 0.9287 0.1455  0.0958  0.1218  621 ARG B CZ  
9923  N NH1 . ARG B 621 ? 1.2388 0.8809 0.8211 0.1532  0.0811  0.1184  621 ARG B NH1 
9924  N NH2 . ARG B 621 ? 1.2135 0.9038 0.8614 0.1455  0.1244  0.1239  621 ARG B NH2 
9925  N N   . MET B 622 ? 0.8767 0.6480 0.6749 0.1295  0.0128  0.1305  622 MET B N   
9926  C CA  . MET B 622 ? 0.7540 0.5322 0.5658 0.1266  0.0281  0.1398  622 MET B CA  
9927  C C   . MET B 622 ? 0.9583 0.7020 0.7300 0.1340  0.0200  0.1476  622 MET B C   
9928  O O   . MET B 622 ? 1.0368 0.7639 0.7874 0.1334  0.0392  0.1575  622 MET B O   
9929  C CB  . MET B 622 ? 0.6385 0.4532 0.5069 0.1207  0.0234  0.1367  622 MET B CB  
9930  C CG  . MET B 622 ? 0.7045 0.5498 0.6083 0.1123  0.0404  0.1345  622 MET B CG  
9931  S SD  . MET B 622 ? 0.7783 0.6620 0.7396 0.1065  0.0319  0.1281  622 MET B SD  
9932  C CE  . MET B 622 ? 0.7068 0.6142 0.6907 0.0989  0.0510  0.1271  622 MET B CE  
9933  N N   . ASN B 623 ? 0.9198 0.6510 0.6807 0.1411  -0.0084 0.1434  623 ASN B N   
9934  C CA  . ASN B 623 ? 0.8708 0.5651 0.5892 0.1500  -0.0200 0.1511  623 ASN B CA  
9935  C C   . ASN B 623 ? 1.0438 0.6958 0.6951 0.1545  -0.0066 0.1577  623 ASN B C   
9936  O O   . ASN B 623 ? 1.1356 0.7577 0.7513 0.1579  0.0023  0.1692  623 ASN B O   
9937  C CB  . ASN B 623 ? 1.0452 0.7353 0.7659 0.1577  -0.0559 0.1438  623 ASN B CB  
9938  C CG  . ASN B 623 ? 1.0320 0.7571 0.8134 0.1556  -0.0674 0.1397  623 ASN B CG  
9939  O OD1 . ASN B 623 ? 0.9991 0.7317 0.7994 0.1537  -0.0561 0.1461  623 ASN B OD1 
9940  N ND2 . ASN B 623 ? 1.0879 0.8343 0.9020 0.1557  -0.0891 0.1285  623 ASN B ND2 
9941  N N   . GLU B 624 ? 1.1094 0.7571 0.7426 0.1546  -0.0033 0.1506  624 GLU B N   
9942  C CA  . GLU B 624 ? 1.1478 0.7564 0.7174 0.1593  0.0127  0.1549  624 GLU B CA  
9943  C C   . GLU B 624 ? 1.1403 0.7513 0.7124 0.1535  0.0501  0.1662  624 GLU B C   
9944  O O   . GLU B 624 ? 1.1272 0.7021 0.6510 0.1573  0.0632  0.1770  624 GLU B O   
9945  C CB  . GLU B 624 ? 1.1445 0.7554 0.7071 0.1594  0.0113  0.1430  624 GLU B CB  
9946  C CG  . GLU B 624 ? 1.5552 1.1293 1.0564 0.1644  0.0325  0.1453  624 GLU B CG  
9947  C CD  . GLU B 624 ? 1.6846 1.2678 1.1913 0.1631  0.0398  0.1342  624 GLU B CD  
9948  O OE1 . GLU B 624 ? 1.6439 1.2427 1.1758 0.1616  0.0160  0.1226  624 GLU B OE1 
9949  O OE2 . GLU B 624 ? 1.5099 1.0842 0.9974 0.1637  0.0700  0.1372  624 GLU B OE2 
9950  N N   . LYS B 625 ? 0.9772 0.6300 0.6065 0.1439  0.0664  0.1642  625 LYS B N   
9951  C CA  . LYS B 625 ? 0.9990 0.6600 0.6416 0.1372  0.0994  0.1734  625 LYS B CA  
9952  C C   . LYS B 625 ? 1.1025 0.7558 0.7496 0.1348  0.1015  0.1843  625 LYS B C   
9953  O O   . LYS B 625 ? 1.0401 0.6805 0.6745 0.1313  0.1271  0.1947  625 LYS B O   
9954  C CB  . LYS B 625 ? 0.8885 0.5956 0.5914 0.1285  0.1108  0.1675  625 LYS B CB  
9955  C CG  . LYS B 625 ? 0.9600 0.6702 0.6558 0.1305  0.1185  0.1596  625 LYS B CG  
9956  C CD  . LYS B 625 ? 1.0700 0.8187 0.8174 0.1230  0.1364  0.1577  625 LYS B CD  
9957  C CE  . LYS B 625 ? 0.9444 0.6907 0.6806 0.1266  0.1481  0.1516  625 LYS B CE  
9958  N NZ  . LYS B 625 ? 1.1654 0.9468 0.9504 0.1209  0.1659  0.1512  625 LYS B NZ  
9959  N N   . ARG B 626 ? 1.0151 0.6762 0.6823 0.1367  0.0755  0.1818  626 ARG B N   
9960  C CA  . ARG B 626 ? 0.8875 0.5385 0.5587 0.1360  0.0743  0.1911  626 ARG B CA  
9961  C C   . ARG B 626 ? 1.0899 0.6878 0.6930 0.1444  0.0735  0.2019  626 ARG B C   
9962  O O   . ARG B 626 ? 1.1985 0.7803 0.7924 0.1408  0.0884  0.2124  626 ARG B O   
9963  C CB  . ARG B 626 ? 1.0177 0.6880 0.7250 0.1387  0.0457  0.1844  626 ARG B CB  
9964  C CG  . ARG B 626 ? 1.0024 0.7218 0.7748 0.1304  0.0470  0.1753  626 ARG B CG  
9965  C CD  . ARG B 626 ? 0.9727 0.7077 0.7781 0.1337  0.0228  0.1697  626 ARG B CD  
9966  N NE  . ARG B 626 ? 0.9513 0.6715 0.7563 0.1351  0.0237  0.1779  626 ARG B NE  
9967  C CZ  . ARG B 626 ? 0.9279 0.6648 0.7656 0.1270  0.0386  0.1799  626 ARG B CZ  
9968  N NH1 . ARG B 626 ? 0.9700 0.7400 0.8430 0.1175  0.0530  0.1747  626 ARG B NH1 
9969  N NH2 . ARG B 626 ? 1.0020 0.7203 0.8358 0.1288  0.0378  0.1870  626 ARG B NH2 
9970  N N   . LYS B 627 ? 1.1132 0.6844 0.6701 0.1545  0.0543  0.1977  627 LYS B N   
9971  C CA  . LYS B 627 ? 1.2565 0.7821 0.7502 0.1608  0.0497  0.2030  627 LYS B CA  
9972  C C   . LYS B 627 ? 1.1783 0.6901 0.6449 0.1546  0.0853  0.2078  627 LYS B C   
9973  O O   . LYS B 627 ? 1.3041 0.7940 0.7479 0.1524  0.0951  0.2151  627 LYS B O   
9974  C CB  . LYS B 627 ? 1.3420 0.8456 0.7955 0.1719  0.0196  0.1943  627 LYS B CB  
9975  C CG  . LYS B 627 ? 1.4175 0.9227 0.8858 0.1794  -0.0196 0.1906  627 LYS B CG  
9976  C CD  . LYS B 627 ? 1.9142 1.4200 1.3774 0.1872  -0.0508 0.1786  627 LYS B CD  
9977  C CE  . LYS B 627 ? 2.0566 1.5736 1.5504 0.1936  -0.0882 0.1737  627 LYS B CE  
9978  N NZ  . LYS B 627 ? 2.1849 1.7072 1.6817 0.1981  -0.1199 0.1594  627 LYS B NZ  
9979  N N   . LYS B 628 ? 1.2377 0.7629 0.7099 0.1522  0.1053  0.2038  628 LYS B N   
9980  C CA  . LYS B 628 ? 1.1801 0.6973 0.6351 0.1472  0.1406  0.2066  628 LYS B CA  
9981  C C   . LYS B 628 ? 1.1605 0.6951 0.6542 0.1354  0.1642  0.2149  628 LYS B C   
9982  O O   . LYS B 628 ? 1.3646 0.8824 0.8379 0.1318  0.1871  0.2198  628 LYS B O   
9983  C CB  . LYS B 628 ? 1.2543 0.7898 0.7215 0.1472  0.1565  0.1999  628 LYS B CB  
9984  C CG  . LYS B 628 ? 1.3901 0.8992 0.8071 0.1582  0.1401  0.1913  628 LYS B CG  
9985  C CD  . LYS B 628 ? 1.4243 0.9501 0.8543 0.1585  0.1569  0.1850  628 LYS B CD  
9986  C CE  . LYS B 628 ? 1.8268 1.3359 1.2243 0.1674  0.1319  0.1728  628 LYS B CE  
9987  N NZ  . LYS B 628 ? 1.8397 1.3823 1.2785 0.1642  0.1380  0.1610  628 LYS B NZ  
9988  N N   . LEU B 629 ? 1.1250 0.6917 0.6743 0.1295  0.1582  0.2159  629 LEU B N   
9989  C CA  . LEU B 629 ? 1.0149 0.5992 0.6051 0.1178  0.1763  0.2221  629 LEU B CA  
9990  C C   . LEU B 629 ? 1.0583 0.6208 0.6372 0.1176  0.1628  0.2290  629 LEU B C   
9991  O O   . LEU B 629 ? 1.1952 0.7612 0.7951 0.1081  0.1784  0.2349  629 LEU B O   
9992  C CB  . LEU B 629 ? 1.0127 0.6407 0.6661 0.1122  0.1756  0.2186  629 LEU B CB  
9993  C CG  . LEU B 629 ? 0.9264 0.5816 0.6301 0.0989  0.1978  0.2214  629 LEU B CG  
9994  C CD1 . LEU B 629 ? 1.0958 0.7584 0.8021 0.0941  0.2272  0.2204  629 LEU B CD1 
9995  C CD2 . LEU B 629 ? 0.8091 0.5022 0.5686 0.0953  0.1897  0.2176  629 LEU B CD2 
9996  N N   . GLY B 630 ? 1.1380 0.6787 0.6863 0.1283  0.1330  0.2278  630 GLY B N   
9997  C CA  . GLY B 630 ? 1.0843 0.6030 0.6207 0.1307  0.1168  0.2337  630 GLY B CA  
9998  C C   . GLY B 630 ? 1.2006 0.7434 0.7895 0.1280  0.1050  0.2335  630 GLY B C   
9999  O O   . GLY B 630 ? 1.2415 0.7735 0.8366 0.1241  0.1062  0.2398  630 GLY B O   
10000 N N   . ILE B 631 ? 1.1369 0.7107 0.7630 0.1304  0.0940  0.2260  631 ILE B N   
10001 C CA  . ILE B 631 ? 1.1552 0.7537 0.8327 0.1292  0.0840  0.2242  631 ILE B CA  
10002 C C   . ILE B 631 ? 1.1541 0.7652 0.8455 0.1401  0.0517  0.2146  631 ILE B C   
10003 O O   . ILE B 631 ? 1.1738 0.7592 0.8280 0.1514  0.0297  0.2147  631 ILE B O   
10004 C CB  . ILE B 631 ? 0.9349 0.5722 0.6637 0.1172  0.1062  0.2213  631 ILE B CB  
10005 C CG1 . ILE B 631 ? 0.9189 0.5871 0.6636 0.1169  0.1045  0.2096  631 ILE B CG1 
10006 C CG2 . ILE B 631 ? 0.8920 0.5229 0.6177 0.1053  0.1365  0.2285  631 ILE B CG2 
10007 C CD1 . ILE B 631 ? 0.9707 0.6863 0.7759 0.1069  0.1120  0.2011  631 ILE B CD1 
10008 N N   . GLU C 2   ? 2.1915 1.3817 1.7694 0.0729  0.0725  -0.2781 2   GLU C N   
10009 C CA  . GLU C 2   ? 2.3620 1.5826 1.9609 0.0496  0.0654  -0.2784 2   GLU C CA  
10010 C C   . GLU C 2   ? 2.3086 1.5710 1.9201 0.0609  0.0572  -0.2495 2   GLU C C   
10011 O O   . GLU C 2   ? 2.3043 1.5549 1.9275 0.0562  0.0615  -0.2310 2   GLU C O   
10012 C CB  . GLU C 2   ? 2.3789 1.6368 1.9802 0.0325  0.0552  -0.3078 2   GLU C CB  
10013 C CG  . GLU C 2   ? 2.4243 1.6429 2.0138 0.0193  0.0634  -0.3398 2   GLU C CG  
10014 C CD  . GLU C 2   ? 2.4918 1.7516 2.0786 0.0084  0.0524  -0.3701 2   GLU C CD  
10015 O OE1 . GLU C 2   ? 2.4418 1.7624 2.0392 0.0068  0.0380  -0.3664 2   GLU C OE1 
10016 O OE2 . GLU C 2   ? 2.4748 1.7064 2.0486 0.0019  0.0584  -0.3977 2   GLU C OE2 
10017 N N   . GLU C 3   ? 2.1976 1.5074 1.8063 0.0760  0.0465  -0.2455 3   GLU C N   
10018 C CA  . GLU C 3   ? 2.1994 1.5478 1.8198 0.0874  0.0398  -0.2192 3   GLU C CA  
10019 C C   . GLU C 3   ? 2.0989 1.4223 1.7105 0.1109  0.0475  -0.1973 3   GLU C C   
10020 O O   . GLU C 3   ? 2.1087 1.4079 1.7029 0.1251  0.0530  -0.2040 3   GLU C O   
10021 C CB  . GLU C 3   ? 2.1815 1.5871 1.8010 0.0947  0.0271  -0.2235 3   GLU C CB  
10022 C CG  . GLU C 3   ? 2.3675 1.8143 2.0005 0.1038  0.0205  -0.1984 3   GLU C CG  
10023 C CD  . GLU C 3   ? 2.3819 1.8813 2.0120 0.1136  0.0098  -0.1999 3   GLU C CD  
10024 O OE1 . GLU C 3   ? 2.4127 1.9262 2.0337 0.1080  0.0046  -0.2227 3   GLU C OE1 
10025 O OE2 . GLU C 3   ? 2.1226 1.6492 1.7593 0.1268  0.0072  -0.1782 3   GLU C OE2 
10026 N N   . LYS C 4   ? 1.8521 1.1822 1.4759 0.1152  0.0483  -0.1724 4   LYS C N   
10027 C CA  . LYS C 4   ? 1.6784 0.9903 1.2957 0.1369  0.0548  -0.1519 4   LYS C CA  
10028 C C   . LYS C 4   ? 1.7033 1.0420 1.3108 0.1588  0.0507  -0.1492 4   LYS C C   
10029 O O   . LYS C 4   ? 2.0448 1.4274 1.6567 0.1584  0.0415  -0.1517 4   LYS C O   
10030 C CB  . LYS C 4   ? 1.6921 1.0152 1.3256 0.1359  0.0548  -0.1276 4   LYS C CB  
10031 C CG  . LYS C 4   ? 1.9482 1.2309 1.5857 0.1226  0.0637  -0.1236 4   LYS C CG  
10032 C CD  . LYS C 4   ? 1.8973 1.2029 1.5552 0.1070  0.0602  -0.1132 4   LYS C CD  
10033 C CE  . LYS C 4   ? 1.9489 1.2154 1.6099 0.0905  0.0694  -0.1127 4   LYS C CE  
10034 N NZ  . LYS C 4   ? 1.6752 0.9226 1.3346 0.0699  0.0715  -0.1375 4   LYS C NZ  
10035 N N   . ALA C 5   ? 1.5146 0.8277 1.1086 0.1783  0.0581  -0.1441 5   ALA C N   
10036 C CA  . ALA C 5   ? 1.3812 0.7179 0.9657 0.1993  0.0559  -0.1417 5   ALA C CA  
10037 C C   . ALA C 5   ? 1.4070 0.7887 1.0049 0.2063  0.0498  -0.1215 5   ALA C C   
10038 O O   . ALA C 5   ? 1.4718 0.8554 1.0833 0.2026  0.0505  -0.1047 5   ALA C O   
10039 C CB  . ALA C 5   ? 1.6296 0.9309 1.2004 0.2192  0.0657  -0.1372 5   ALA C CB  
10040 N N   . LYS C 6   ? 1.3073 0.7248 0.9010 0.2162  0.0447  -0.1233 6   LYS C N   
10041 C CA  . LYS C 6   ? 1.3209 0.7797 0.9268 0.2229  0.0404  -0.1048 6   LYS C CA  
10042 C C   . LYS C 6   ? 1.2840 0.7386 0.8894 0.2420  0.0467  -0.0877 6   LYS C C   
10043 O O   . LYS C 6   ? 1.4176 0.8893 1.0374 0.2434  0.0465  -0.0697 6   LYS C O   
10044 C CB  . LYS C 6   ? 1.4007 0.8987 1.0010 0.2269  0.0338  -0.1119 6   LYS C CB  
10045 C CG  . LYS C 6   ? 1.5268 1.0345 1.1249 0.2102  0.0267  -0.1321 6   LYS C CG  
10046 C CD  . LYS C 6   ? 1.3855 0.9254 1.0018 0.1971  0.0192  -0.1245 6   LYS C CD  
10047 C CE  . LYS C 6   ? 1.2683 0.8340 0.8813 0.1863  0.0104  -0.1429 6   LYS C CE  
10048 N NZ  . LYS C 6   ? 1.3245 0.9295 0.9287 0.2002  0.0058  -0.1407 6   LYS C NZ  
10049 N N   . SER C 7   ? 1.3202 0.7537 0.9099 0.2569  0.0525  -0.0941 7   SER C N   
10050 C CA  . SER C 7   ? 1.3079 0.7404 0.8970 0.2764  0.0583  -0.0797 7   SER C CA  
10051 C C   . SER C 7   ? 1.3856 0.7785 0.9581 0.2888  0.0661  -0.0885 7   SER C C   
10052 O O   . SER C 7   ? 1.4024 0.7711 0.9627 0.2829  0.0672  -0.1075 7   SER C O   
10053 C CB  . SER C 7   ? 1.3173 0.7906 0.9067 0.2886  0.0564  -0.0741 7   SER C CB  
10054 O OG  . SER C 7   ? 1.3879 0.8658 0.9794 0.3062  0.0620  -0.0608 7   SER C OG  
10055 N N   . ILE C 8   ? 1.3695 0.7564 0.9421 0.3063  0.0718  -0.0753 8   ILE C N   
10056 C CA  . ILE C 8   ? 1.3036 0.6550 0.8611 0.3222  0.0800  -0.0809 8   ILE C CA  
10057 C C   . ILE C 8   ? 1.2202 0.5915 0.7684 0.3420  0.0821  -0.0847 8   ILE C C   
10058 O O   . ILE C 8   ? 1.4660 0.8110 1.0001 0.3563  0.0888  -0.0926 8   ILE C O   
10059 C CB  . ILE C 8   ? 1.1604 0.4903 0.7224 0.3306  0.0853  -0.0643 8   ILE C CB  
10060 C CG1 . ILE C 8   ? 1.3116 0.6799 0.8869 0.3420  0.0839  -0.0452 8   ILE C CG1 
10061 C CG2 . ILE C 8   ? 1.2357 0.5423 0.8043 0.3111  0.0847  -0.0617 8   ILE C CG2 
10062 C CD1 . ILE C 8   ? 1.3088 0.6771 0.8903 0.3521  0.0880  -0.0310 8   ILE C CD1 
10063 N N   . ASP C 9   ? 1.2235 0.6401 0.7793 0.3433  0.0776  -0.0787 9   ASP C N   
10064 C CA  . ASP C 9   ? 1.4370 0.8770 0.9853 0.3607  0.0802  -0.0808 9   ASP C CA  
10065 C C   . ASP C 9   ? 1.5230 0.9659 1.0561 0.3565  0.0778  -0.1013 9   ASP C C   
10066 O O   . ASP C 9   ? 1.4680 0.9289 1.0047 0.3409  0.0708  -0.1054 9   ASP C O   
10067 C CB  . ASP C 9   ? 1.3644 0.8499 0.9284 0.3627  0.0779  -0.0639 9   ASP C CB  
10068 C CG  . ASP C 9   ? 1.5391 1.0514 1.0977 0.3802  0.0820  -0.0635 9   ASP C CG  
10069 O OD1 . ASP C 9   ? 1.7882 1.2837 1.3345 0.3962  0.0879  -0.0706 9   ASP C OD1 
10070 O OD2 . ASP C 9   ? 1.6476 1.1972 1.2145 0.3782  0.0801  -0.0555 9   ASP C OD2 
10071 N N   . GLN C 10  ? 1.4865 0.9135 1.0026 0.3710  0.0836  -0.1144 10  GLN C N   
10072 C CA  . GLN C 10  ? 1.4207 0.8503 0.9204 0.3679  0.0818  -0.1361 10  GLN C CA  
10073 C C   . GLN C 10  ? 1.4875 0.9666 0.9879 0.3690  0.0770  -0.1329 10  GLN C C   
10074 O O   . GLN C 10  ? 1.5564 1.0473 1.0486 0.3589  0.0715  -0.1469 10  GLN C O   
10075 C CB  . GLN C 10  ? 1.6872 1.0878 1.1684 0.3847  0.0903  -0.1509 10  GLN C CB  
10076 C CG  . GLN C 10  ? 1.7432 1.1234 1.2073 0.3752  0.0896  -0.1785 10  GLN C CG  
10077 C CD  . GLN C 10  ? 1.7803 1.1275 1.2487 0.3535  0.0872  -0.1862 10  GLN C CD  
10078 O OE1 . GLN C 10  ? 1.6246 0.9426 1.1014 0.3518  0.0908  -0.1749 10  GLN C OE1 
10079 N NE2 . GLN C 10  ? 1.7822 1.1352 1.2450 0.3362  0.0812  -0.2057 10  GLN C NE2 
10080 N N   . ALA C 11  ? 1.4487 0.9575 0.9589 0.3807  0.0794  -0.1145 11  ALA C N   
10081 C CA  . ALA C 11  ? 1.4540 1.0080 0.9654 0.3821  0.0768  -0.1086 11  ALA C CA  
10082 C C   . ALA C 11  ? 1.4332 1.0044 0.9560 0.3628  0.0681  -0.1031 11  ALA C C   
10083 O O   . ALA C 11  ? 1.4222 1.0193 0.9384 0.3588  0.0634  -0.1083 11  ALA C O   
10084 C CB  . ALA C 11  ? 1.5303 1.1086 1.0531 0.3960  0.0826  -0.0896 11  ALA C CB  
10085 N N   . THR C 12  ? 1.3959 0.9537 0.9352 0.3520  0.0661  -0.0925 12  THR C N   
10086 C CA  . THR C 12  ? 1.4637 1.0353 1.0160 0.3341  0.0585  -0.0868 12  THR C CA  
10087 C C   . THR C 12  ? 1.4532 1.0139 0.9950 0.3202  0.0522  -0.1073 12  THR C C   
10088 O O   . THR C 12  ? 1.4648 1.0529 1.0075 0.3120  0.0454  -0.1091 12  THR C O   
10089 C CB  . THR C 12  ? 1.4002 0.9559 0.9706 0.3268  0.0592  -0.0729 12  THR C CB  
10090 O OG1 . THR C 12  ? 1.4362 1.0098 1.0179 0.3379  0.0641  -0.0551 12  THR C OG1 
10091 C CG2 . THR C 12  ? 1.4355 1.0000 1.0192 0.3077  0.0521  -0.0692 12  THR C CG2 
10092 N N   . LEU C 13  ? 1.4121 0.9333 0.9442 0.3178  0.0548  -0.1229 13  LEU C N   
10093 C CA  . LEU C 13  ? 1.2809 0.7887 0.8041 0.3029  0.0500  -0.1450 13  LEU C CA  
10094 C C   . LEU C 13  ? 1.3591 0.8930 0.8656 0.3070  0.0466  -0.1605 13  LEU C C   
10095 O O   . LEU C 13  ? 1.3490 0.8961 0.8533 0.2931  0.0389  -0.1735 13  LEU C O   
10096 C CB  . LEU C 13  ? 1.2154 0.6714 0.7304 0.3016  0.0564  -0.1582 13  LEU C CB  
10097 C CG  . LEU C 13  ? 1.2832 0.7099 0.8124 0.2936  0.0591  -0.1460 13  LEU C CG  
10098 C CD1 . LEU C 13  ? 1.4436 0.8213 0.9628 0.3023  0.0687  -0.1518 13  LEU C CD1 
10099 C CD2 . LEU C 13  ? 1.3397 0.7641 0.8785 0.2693  0.0528  -0.1524 13  LEU C CD2 
10100 N N   . GLN C 14  ? 1.3441 0.8879 0.8388 0.3262  0.0521  -0.1595 14  GLN C N   
10101 C CA  . GLN C 14  ? 1.4216 0.9914 0.8982 0.3324  0.0500  -0.1734 14  GLN C CA  
10102 C C   . GLN C 14  ? 1.5192 1.1370 1.0017 0.3293  0.0428  -0.1613 14  GLN C C   
10103 O O   . GLN C 14  ? 1.4655 1.1040 0.9383 0.3225  0.0357  -0.1749 14  GLN C O   
10104 C CB  . GLN C 14  ? 1.4195 0.9888 0.8833 0.3546  0.0591  -0.1731 14  GLN C CB  
10105 C CG  . GLN C 14  ? 1.7466 1.2720 1.1966 0.3600  0.0659  -0.1927 14  GLN C CG  
10106 C CD  . GLN C 14  ? 1.7524 1.2760 1.1943 0.3834  0.0757  -0.1887 14  GLN C CD  
10107 O OE1 . GLN C 14  ? 1.6567 1.2164 1.0977 0.3951  0.0773  -0.1777 14  GLN C OE1 
10108 N NE2 . GLN C 14  ? 1.5471 1.0286 0.9832 0.3910  0.0833  -0.1974 14  GLN C NE2 
10109 N N   . LEU C 15  ? 1.4227 1.0585 0.9210 0.3344  0.0449  -0.1360 15  LEU C N   
10110 C CA  . LEU C 15  ? 1.3629 1.0405 0.8675 0.3326  0.0399  -0.1223 15  LEU C CA  
10111 C C   . LEU C 15  ? 1.3950 1.0781 0.9111 0.3138  0.0304  -0.1239 15  LEU C C   
10112 O O   . LEU C 15  ? 1.4539 1.1714 0.9693 0.3118  0.0243  -0.1204 15  LEU C O   
10113 C CB  . LEU C 15  ? 1.1435 0.8363 0.6630 0.3420  0.0463  -0.0962 15  LEU C CB  
10114 C CG  . LEU C 15  ? 1.3266 1.0334 0.8351 0.3611  0.0549  -0.0920 15  LEU C CG  
10115 C CD1 . LEU C 15  ? 1.2503 0.9596 0.7762 0.3677  0.0626  -0.0710 15  LEU C CD1 
10116 C CD2 . LEU C 15  ? 1.1961 0.9417 0.6925 0.3667  0.0531  -0.0900 15  LEU C CD2 
10117 N N   . LEU C 16  ? 1.3286 0.9791 0.8548 0.3007  0.0295  -0.1290 16  LEU C N   
10118 C CA  . LEU C 16  ? 1.4083 1.0642 0.9464 0.2818  0.0211  -0.1321 16  LEU C CA  
10119 C C   . LEU C 16  ? 1.4817 1.1504 1.0049 0.2743  0.0135  -0.1564 16  LEU C C   
10120 O O   . LEU C 16  ? 1.3617 1.0591 0.8910 0.2650  0.0049  -0.1566 16  LEU C O   
10121 C CB  . LEU C 16  ? 1.3539 0.9705 0.9046 0.2694  0.0233  -0.1327 16  LEU C CB  
10122 C CG  . LEU C 16  ? 1.2463 0.8623 0.8180 0.2689  0.0262  -0.1084 16  LEU C CG  
10123 C CD1 . LEU C 16  ? 1.3048 0.8783 0.8821 0.2634  0.0312  -0.1087 16  LEU C CD1 
10124 C CD2 . LEU C 16  ? 1.2816 0.9252 0.8693 0.2569  0.0189  -0.0997 16  LEU C CD2 
10125 N N   . ASP C 17  ? 1.4558 1.1054 0.9597 0.2789  0.0166  -0.1772 17  ASP C N   
10126 C CA  . ASP C 17  ? 1.4672 1.1300 0.9555 0.2719  0.0099  -0.2031 17  ASP C CA  
10127 C C   . ASP C 17  ? 1.4727 1.1859 0.9510 0.2831  0.0051  -0.1970 17  ASP C C   
10128 O O   . ASP C 17  ? 1.5039 1.2472 0.9792 0.2748  -0.0046 -0.2072 17  ASP C O   
10129 C CB  . ASP C 17  ? 1.4367 1.0651 0.9063 0.2761  0.0164  -0.2264 17  ASP C CB  
10130 C CG  . ASP C 17  ? 1.7019 1.2778 1.1788 0.2652  0.0219  -0.2338 17  ASP C CG  
10131 O OD1 . ASP C 17  ? 1.6785 1.2481 1.1729 0.2489  0.0184  -0.2286 17  ASP C OD1 
10132 O OD2 . ASP C 17  ? 1.8181 1.3590 1.2830 0.2736  0.0306  -0.2442 17  ASP C OD2 
10133 N N   . LYS C 18  ? 1.3841 1.1081 0.8576 0.3020  0.0121  -0.1798 18  LYS C N   
10134 C CA  . LYS C 18  ? 1.4128 1.1823 0.8762 0.3142  0.0099  -0.1703 18  LYS C CA  
10135 C C   . LYS C 18  ? 1.4561 1.2562 0.9358 0.3075  0.0027  -0.1528 18  LYS C C   
10136 O O   . LYS C 18  ? 1.4684 1.3059 0.9394 0.3087  -0.0047 -0.1556 18  LYS C O   
10137 C CB  . LYS C 18  ? 1.3570 1.1290 0.8166 0.3337  0.0208  -0.1526 18  LYS C CB  
10138 C CG  . LYS C 18  ? 1.2509 1.0683 0.7005 0.3463  0.0204  -0.1398 18  LYS C CG  
10139 C CD  . LYS C 18  ? 1.3268 1.1473 0.7685 0.3650  0.0321  -0.1285 18  LYS C CD  
10140 C CE  . LYS C 18  ? 1.3524 1.2150 0.7772 0.3777  0.0327  -0.1217 18  LYS C CE  
10141 N NZ  . LYS C 18  ? 1.2708 1.1621 0.7085 0.3773  0.0307  -0.0967 18  LYS C NZ  
10142 N N   . ALA C 19  ? 1.3937 1.1789 0.8965 0.3012  0.0050  -0.1351 19  ALA C N   
10143 C CA  . ALA C 19  ? 1.2710 1.0814 0.7913 0.2950  -0.0005 -0.1181 19  ALA C CA  
10144 C C   . ALA C 19  ? 1.3054 1.1321 0.8261 0.2801  -0.0126 -0.1354 19  ALA C C   
10145 O O   . ALA C 19  ? 1.4225 1.2865 0.9465 0.2811  -0.0191 -0.1266 19  ALA C O   
10146 C CB  . ALA C 19  ? 1.0840 0.8700 0.6279 0.2888  0.0043  -0.1015 19  ALA C CB  
10147 N N   . LYS C 20  ? 1.2009 1.0007 0.7186 0.2664  -0.0150 -0.1599 20  LYS C N   
10148 C CA  . LYS C 20  ? 1.1789 0.9947 0.6981 0.2501  -0.0260 -0.1795 20  LYS C CA  
10149 C C   . LYS C 20  ? 1.2930 1.1480 0.7905 0.2576  -0.0328 -0.1932 20  LYS C C   
10150 O O   . LYS C 20  ? 1.3732 1.2675 0.8734 0.2534  -0.0429 -0.1945 20  LYS C O   
10151 C CB  . LYS C 20  ? 1.2471 1.0206 0.7676 0.2332  -0.0245 -0.2032 20  LYS C CB  
10152 C CG  . LYS C 20  ? 1.1788 0.9650 0.7092 0.2120  -0.0344 -0.2205 20  LYS C CG  
10153 C CD  . LYS C 20  ? 1.5501 1.2963 1.0760 0.1961  -0.0317 -0.2485 20  LYS C CD  
10154 C CE  . LYS C 20  ? 1.5688 1.3208 1.1105 0.1722  -0.0390 -0.2626 20  LYS C CE  
10155 N NZ  . LYS C 20  ? 1.7389 1.4487 1.2762 0.1556  -0.0345 -0.2904 20  LYS C NZ  
10156 N N   . GLN C 21  ? 1.3047 1.1511 0.7802 0.2697  -0.0272 -0.2032 21  GLN C N   
10157 C CA  . GLN C 21  ? 1.3405 1.2232 0.7922 0.2784  -0.0325 -0.2170 21  GLN C CA  
10158 C C   . GLN C 21  ? 1.4347 1.3634 0.8842 0.2940  -0.0344 -0.1915 21  GLN C C   
10159 O O   . GLN C 21  ? 1.5611 1.5318 0.9970 0.2976  -0.0429 -0.1989 21  GLN C O   
10160 C CB  . GLN C 21  ? 1.5540 1.4142 0.9838 0.2895  -0.0239 -0.2308 21  GLN C CB  
10161 C CG  . GLN C 21  ? 1.7912 1.6068 1.2184 0.2757  -0.0214 -0.2592 21  GLN C CG  
10162 C CD  . GLN C 21  ? 1.8604 1.6923 1.2815 0.2590  -0.0321 -0.2897 21  GLN C CD  
10163 O OE1 . GLN C 21  ? 1.8109 1.6865 1.2164 0.2637  -0.0398 -0.2990 21  GLN C OE1 
10164 N NE2 . GLN C 21  ? 1.8861 1.6843 1.3191 0.2388  -0.0323 -0.3064 21  GLN C NE2 
10165 N N   . ASP C 22  ? 1.3809 1.3021 0.8434 0.3034  -0.0261 -0.1619 22  ASP C N   
10166 C CA  . ASP C 22  ? 1.3544 1.3124 0.8171 0.3178  -0.0252 -0.1352 22  ASP C CA  
10167 C C   . ASP C 22  ? 1.3034 1.2861 0.7847 0.3095  -0.0340 -0.1241 22  ASP C C   
10168 O O   . ASP C 22  ? 1.3655 1.3856 0.8437 0.3207  -0.0362 -0.1070 22  ASP C O   
10169 C CB  . ASP C 22  ? 1.1810 1.1202 0.6519 0.3294  -0.0116 -0.1097 22  ASP C CB  
10170 C CG  . ASP C 22  ? 1.4243 1.3507 0.8765 0.3423  -0.0022 -0.1155 22  ASP C CG  
10171 O OD1 . ASP C 22  ? 1.3858 1.3195 0.8158 0.3444  -0.0056 -0.1384 22  ASP C OD1 
10172 O OD2 . ASP C 22  ? 1.4258 1.3362 0.8858 0.3503  0.0089  -0.0982 22  ASP C OD2 
10173 N N   . GLY C 23  ? 1.2174 1.1792 0.7177 0.2911  -0.0382 -0.1332 23  GLY C N   
10174 C CA  . GLY C 23  ? 1.3603 1.3438 0.8801 0.2819  -0.0463 -0.1251 23  GLY C CA  
10175 C C   . GLY C 23  ? 1.2573 1.2305 0.7998 0.2844  -0.0393 -0.0959 23  GLY C C   
10176 O O   . GLY C 23  ? 1.3310 1.3269 0.8887 0.2817  -0.0444 -0.0842 23  GLY C O   
10177 N N   . VAL C 24  ? 1.1960 1.1361 0.7418 0.2894  -0.0275 -0.0847 24  VAL C N   
10178 C CA  . VAL C 24  ? 1.0736 1.0032 0.6410 0.2909  -0.0201 -0.0589 24  VAL C CA  
10179 C C   . VAL C 24  ? 1.2012 1.0971 0.7884 0.2735  -0.0200 -0.0645 24  VAL C C   
10180 O O   . VAL C 24  ? 1.2236 1.0941 0.8057 0.2634  -0.0215 -0.0855 24  VAL C O   
10181 C CB  . VAL C 24  ? 1.0361 0.9558 0.5986 0.3062  -0.0072 -0.0414 24  VAL C CB  
10182 C CG1 . VAL C 24  ? 0.9978 0.9501 0.5390 0.3232  -0.0061 -0.0359 24  VAL C CG1 
10183 C CG2 . VAL C 24  ? 1.2554 1.1366 0.8133 0.3043  -0.0007 -0.0531 24  VAL C CG2 
10184 N N   . GLU C 25  ? 1.2030 1.0983 0.8124 0.2703  -0.0173 -0.0454 25  GLU C N   
10185 C CA  . GLU C 25  ? 1.1714 1.0377 0.8001 0.2547  -0.0165 -0.0476 25  GLU C CA  
10186 C C   . GLU C 25  ? 1.2102 1.0473 0.8464 0.2592  -0.0050 -0.0336 25  GLU C C   
10187 O O   . GLU C 25  ? 1.1222 0.9690 0.7588 0.2720  0.0022  -0.0156 25  GLU C O   
10188 C CB  . GLU C 25  ? 1.2368 1.1232 0.8860 0.2463  -0.0220 -0.0392 25  GLU C CB  
10189 C CG  . GLU C 25  ? 1.5556 1.4575 1.2174 0.2569  -0.0161 -0.0122 25  GLU C CG  
10190 C CD  . GLU C 25  ? 1.5245 1.4358 1.2098 0.2477  -0.0190 -0.0038 25  GLU C CD  
10191 O OE1 . GLU C 25  ? 1.3859 1.3043 1.0763 0.2347  -0.0280 -0.0189 25  GLU C OE1 
10192 O OE2 . GLU C 25  ? 1.5268 1.4387 1.2260 0.2533  -0.0118 0.0170  25  GLU C OE2 
10193 N N   . THR C 26  ? 1.2358 1.0380 0.8778 0.2486  -0.0028 -0.0420 26  THR C N   
10194 C CA  . THR C 26  ? 1.0700 0.8452 0.7189 0.2521  0.0069  -0.0311 26  THR C CA  
10195 C C   . THR C 26  ? 1.1011 0.8597 0.7710 0.2384  0.0073  -0.0260 26  THR C C   
10196 O O   . THR C 26  ? 1.1715 0.9364 0.8493 0.2258  0.0005  -0.0329 26  THR C O   
10197 C CB  . THR C 26  ? 1.2297 0.9769 0.8618 0.2560  0.0104  -0.0456 26  THR C CB  
10198 O OG1 . THR C 26  ? 1.3609 1.0854 0.9912 0.2417  0.0058  -0.0646 26  THR C OG1 
10199 C CG2 . THR C 26  ? 1.3392 1.1030 0.9498 0.2695  0.0105  -0.0522 26  THR C CG2 
10200 N N   . VAL C 27  ? 1.0980 0.8378 0.7768 0.2409  0.0153  -0.0144 27  VAL C N   
10201 C CA  . VAL C 27  ? 1.1869 0.9101 0.8837 0.2295  0.0169  -0.0087 27  VAL C CA  
10202 C C   . VAL C 27  ? 1.1298 0.8294 0.8244 0.2150  0.0126  -0.0257 27  VAL C C   
10203 O O   . VAL C 27  ? 1.0898 0.7878 0.7988 0.2019  0.0104  -0.0247 27  VAL C O   
10204 C CB  . VAL C 27  ? 1.0989 0.8064 0.8009 0.2364  0.0260  0.0030  27  VAL C CB  
10205 C CG1 . VAL C 27  ? 1.0965 0.7792 0.7822 0.2432  0.0290  -0.0070 27  VAL C CG1 
10206 C CG2 . VAL C 27  ? 1.0589 0.7548 0.7794 0.2258  0.0279  0.0105  27  VAL C CG2 
10207 N N   . TRP C 28  ? 1.0901 0.7707 0.7669 0.2169  0.0125  -0.0413 28  TRP C N   
10208 C CA  . TRP C 28  ? 1.1398 0.7944 0.8132 0.2029  0.0101  -0.0585 28  TRP C CA  
10209 C C   . TRP C 28  ? 1.2390 0.9158 0.9170 0.1897  0.0012  -0.0698 28  TRP C C   
10210 O O   . TRP C 28  ? 1.2106 0.8740 0.8970 0.1736  -0.0004 -0.0778 28  TRP C O   
10211 C CB  . TRP C 28  ? 1.2031 0.8344 0.8555 0.2093  0.0126  -0.0739 28  TRP C CB  
10212 C CG  . TRP C 28  ? 1.1704 0.7731 0.8186 0.2198  0.0212  -0.0666 28  TRP C CG  
10213 C CD1 . TRP C 28  ? 1.1606 0.7267 0.8101 0.2146  0.0260  -0.0676 28  TRP C CD1 
10214 C CD2 . TRP C 28  ? 1.1932 0.8028 0.8339 0.2383  0.0263  -0.0579 28  TRP C CD2 
10215 N NE1 . TRP C 28  ? 1.1609 0.7126 0.8044 0.2298  0.0329  -0.0596 28  TRP C NE1 
10216 C CE2 . TRP C 28  ? 1.2253 0.8040 0.8643 0.2438  0.0332  -0.0543 28  TRP C CE2 
10217 C CE3 . TRP C 28  ? 1.2736 0.9138 0.9094 0.2508  0.0262  -0.0520 28  TRP C CE3 
10218 C CZ2 . TRP C 28  ? 1.3471 0.9271 0.9810 0.2611  0.0392  -0.0464 28  TRP C CZ2 
10219 C CZ3 . TRP C 28  ? 1.2293 0.8685 0.8599 0.2667  0.0332  -0.0441 28  TRP C CZ3 
10220 C CH2 . TRP C 28  ? 1.1593 0.7700 0.7898 0.2716  0.0393  -0.0420 28  TRP C CH2 
10221 N N   . ASP C 29  ? 1.3240 1.0362 0.9964 0.1970  -0.0043 -0.0705 29  ASP C N   
10222 C CA  . ASP C 29  ? 1.2432 0.9843 0.9193 0.1872  -0.0139 -0.0809 29  ASP C CA  
10223 C C   . ASP C 29  ? 1.1581 0.9161 0.8574 0.1800  -0.0155 -0.0669 29  ASP C C   
10224 O O   . ASP C 29  ? 1.1131 0.8765 0.8226 0.1645  -0.0207 -0.0766 29  ASP C O   
10225 C CB  . ASP C 29  ? 1.0275 0.8039 0.6893 0.2002  -0.0188 -0.0828 29  ASP C CB  
10226 C CG  . ASP C 29  ? 1.3735 1.1363 1.0118 0.2085  -0.0168 -0.0970 29  ASP C CG  
10227 O OD1 . ASP C 29  ? 1.4846 1.2121 1.1172 0.2009  -0.0137 -0.1115 29  ASP C OD1 
10228 O OD2 . ASP C 29  ? 1.3335 1.1203 0.9588 0.2231  -0.0174 -0.0932 29  ASP C OD2 
10229 N N   . ARG C 30  ? 1.0517 0.8175 0.7599 0.1906  -0.0104 -0.0451 30  ARG C N   
10230 C CA  . ARG C 30  ? 0.9709 0.7507 0.7012 0.1853  -0.0103 -0.0312 30  ARG C CA  
10231 C C   . ARG C 30  ? 1.1707 0.9220 0.9136 0.1699  -0.0072 -0.0336 30  ARG C C   
10232 O O   . ARG C 30  ? 1.1598 0.9226 0.9200 0.1601  -0.0093 -0.0302 30  ARG C O   
10233 C CB  . ARG C 30  ? 0.8294 0.6192 0.5655 0.1996  -0.0036 -0.0090 30  ARG C CB  
10234 C CG  . ARG C 30  ? 1.0051 0.8276 0.7319 0.2138  -0.0062 -0.0033 30  ARG C CG  
10235 C CD  . ARG C 30  ? 1.0244 0.8566 0.7607 0.2253  0.0017  0.0194  30  ARG C CD  
10236 N NE  . ARG C 30  ? 1.0522 0.8621 0.7841 0.2319  0.0109  0.0253  30  ARG C NE  
10237 C CZ  . ARG C 30  ? 1.1832 0.9939 0.8981 0.2441  0.0140  0.0248  30  ARG C CZ  
10238 N NH1 . ARG C 30  ? 1.1220 0.9540 0.8210 0.2513  0.0087  0.0186  30  ARG C NH1 
10239 N NH2 . ARG C 30  ? 1.2339 1.0267 0.9478 0.2495  0.0224  0.0301  30  ARG C NH2 
10240 N N   . LYS C 31  ? 1.1746 0.8895 0.9083 0.1686  -0.0018 -0.0388 31  LYS C N   
10241 C CA  . LYS C 31  ? 0.9659 0.6515 0.7082 0.1553  0.0020  -0.0404 31  LYS C CA  
10242 C C   . LYS C 31  ? 1.0584 0.7436 0.8033 0.1375  -0.0036 -0.0584 31  LYS C C   
10243 O O   . LYS C 31  ? 1.2009 0.8843 0.9613 0.1240  -0.0033 -0.0568 31  LYS C O   
10244 C CB  . LYS C 31  ? 1.0003 0.6483 0.7296 0.1610  0.0091  -0.0413 31  LYS C CB  
10245 C CG  . LYS C 31  ? 0.9959 0.6110 0.7306 0.1489  0.0139  -0.0420 31  LYS C CG  
10246 C CD  . LYS C 31  ? 1.0531 0.6726 0.8051 0.1477  0.0178  -0.0244 31  LYS C CD  
10247 C CE  . LYS C 31  ? 1.1683 0.7540 0.9212 0.1398  0.0237  -0.0228 31  LYS C CE  
10248 N NZ  . LYS C 31  ? 1.3073 0.8820 1.0642 0.1209  0.0221  -0.0353 31  LYS C NZ  
10249 N N   . ALA C 32  ? 1.0356 0.7244 0.7661 0.1366  -0.0085 -0.0763 32  ALA C N   
10250 C CA  . ALA C 32  ? 1.1017 0.7934 0.8351 0.1184  -0.0140 -0.0962 32  ALA C CA  
10251 C C   . ALA C 32  ? 1.1909 0.9253 0.9423 0.1126  -0.0214 -0.0928 32  ALA C C   
10252 O O   . ALA C 32  ? 1.1896 0.9256 0.9544 0.0951  -0.0232 -0.1006 32  ALA C O   
10253 C CB  . ALA C 32  ? 1.0678 0.7604 0.7817 0.1203  -0.0180 -0.1165 32  ALA C CB  
10254 N N   . ASP C 33  ? 1.1905 0.9591 0.9422 0.1278  -0.0250 -0.0803 33  ASP C N   
10255 C CA  . ASP C 33  ? 1.1843 0.9947 0.9520 0.1266  -0.0315 -0.0744 33  ASP C CA  
10256 C C   . ASP C 33  ? 1.1533 0.9586 0.9434 0.1186  -0.0270 -0.0614 33  ASP C C   
10257 O O   . ASP C 33  ? 1.2917 1.1230 1.0979 0.1098  -0.0320 -0.0634 33  ASP C O   
10258 C CB  . ASP C 33  ? 1.2590 1.1000 1.0209 0.1473  -0.0333 -0.0598 33  ASP C CB  
10259 C CG  . ASP C 33  ? 1.4696 1.3263 1.2099 0.1559  -0.0390 -0.0722 33  ASP C CG  
10260 O OD1 . ASP C 33  ? 1.4149 1.2616 1.1457 0.1448  -0.0427 -0.0946 33  ASP C OD1 
10261 O OD2 . ASP C 33  ? 1.3785 1.2568 1.1112 0.1734  -0.0391 -0.0597 33  ASP C OD2 
10262 N N   . MET C 34  ? 1.1100 0.8844 0.9011 0.1220  -0.0178 -0.0488 34  MET C N   
10263 C CA  . MET C 34  ? 1.0061 0.7749 0.8168 0.1145  -0.0129 -0.0373 34  MET C CA  
10264 C C   . MET C 34  ? 1.1258 0.8778 0.9441 0.0933  -0.0126 -0.0504 34  MET C C   
10265 O O   . MET C 34  ? 1.1890 0.9479 1.0256 0.0845  -0.0109 -0.0446 34  MET C O   
10266 C CB  . MET C 34  ? 0.9756 0.7184 0.7842 0.1236  -0.0035 -0.0219 34  MET C CB  
10267 C CG  . MET C 34  ? 1.0535 0.8174 0.8708 0.1377  -0.0008 -0.0029 34  MET C CG  
10268 S SD  . MET C 34  ? 1.1059 0.9030 0.9482 0.1330  -0.0031 0.0054  34  MET C SD  
10269 C CE  . MET C 34  ? 1.4644 1.2364 1.3193 0.1140  0.0016  0.0021  34  MET C CE  
10270 N N   . LYS C 35  ? 1.2188 0.9491 1.0234 0.0853  -0.0133 -0.0681 35  LYS C N   
10271 C CA  . LYS C 35  ? 1.1832 0.8947 0.9941 0.0636  -0.0116 -0.0821 35  LYS C CA  
10272 C C   . LYS C 35  ? 1.1121 0.7963 0.9320 0.0584  -0.0024 -0.0691 35  LYS C C   
10273 O O   . LYS C 35  ? 1.1607 0.8274 0.9739 0.0714  0.0033  -0.0551 35  LYS C O   
10274 C CB  . LYS C 35  ? 1.1636 0.9141 0.9905 0.0511  -0.0198 -0.0924 35  LYS C CB  
10275 C CG  . LYS C 35  ? 1.2422 1.0335 1.0633 0.0608  -0.0302 -0.0991 35  LYS C CG  
10276 C CD  . LYS C 35  ? 1.3339 1.1172 1.1379 0.0550  -0.0341 -0.1223 35  LYS C CD  
10277 C CE  . LYS C 35  ? 1.5938 1.4131 1.3858 0.0697  -0.0430 -0.1259 35  LYS C CE  
10278 N NZ  . LYS C 35  ? 1.7107 1.5723 1.5150 0.0822  -0.0476 -0.1083 35  LYS C NZ  
10279 N N   . VAL C 36  ? 1.2830 0.9660 1.1175 0.0397  -0.0008 -0.0743 36  VAL C N   
10280 C CA  . VAL C 36  ? 1.0931 0.7529 0.9360 0.0339  0.0082  -0.0621 36  VAL C CA  
10281 C C   . VAL C 36  ? 1.1318 0.8117 0.9843 0.0479  0.0090  -0.0422 36  VAL C C   
10282 O O   . VAL C 36  ? 1.3954 1.1134 1.2589 0.0526  0.0029  -0.0397 36  VAL C O   
10283 C CB  . VAL C 36  ? 1.2017 0.8645 1.0608 0.0114  0.0096  -0.0707 36  VAL C CB  
10284 C CG1 . VAL C 36  ? 1.1415 0.7905 1.0108 0.0072  0.0182  -0.0561 36  VAL C CG1 
10285 C CG2 . VAL C 36  ? 1.2991 0.9341 1.1488 -0.0044 0.0118  -0.0902 36  VAL C CG2 
10286 N N   . GLN C 37  ? 0.8985 0.5539 0.7461 0.0553  0.0166  -0.0289 37  GLN C N   
10287 C CA  . GLN C 37  ? 0.9422 0.6143 0.7989 0.0677  0.0186  -0.0116 37  GLN C CA  
10288 C C   . GLN C 37  ? 0.9864 0.6614 0.8608 0.0565  0.0233  -0.0051 37  GLN C C   
10289 O O   . GLN C 37  ? 1.2410 0.8909 1.1135 0.0439  0.0282  -0.0090 37  GLN C O   
10290 C CB  . GLN C 37  ? 1.0142 0.6647 0.8565 0.0826  0.0234  -0.0024 37  GLN C CB  
10291 C CG  . GLN C 37  ? 0.9321 0.5873 0.7594 0.0961  0.0191  -0.0066 37  GLN C CG  
10292 C CD  . GLN C 37  ? 1.1656 0.8115 0.9848 0.1121  0.0239  0.0051  37  GLN C CD  
10293 O OE1 . GLN C 37  ? 1.5115 1.1329 1.3265 0.1125  0.0298  0.0101  37  GLN C OE1 
10294 N NE2 . GLN C 37  ? 0.9809 0.6474 0.7980 0.1255  0.0218  0.0099  37  GLN C NE2 
10295 N N   . CYS C 38  ? 0.8529 0.5560 0.7433 0.0614  0.0229  0.0045  38  CYS C N   
10296 C CA  . CYS C 38  ? 0.8138 0.5234 0.7222 0.0508  0.0274  0.0094  38  CYS C CA  
10297 C C   . CYS C 38  ? 0.8773 0.5543 0.7790 0.0468  0.0359  0.0149  38  CYS C C   
10298 O O   . CYS C 38  ? 1.0518 0.7173 0.9447 0.0590  0.0392  0.0238  38  CYS C O   
10299 C CB  . CYS C 38  ? 0.7455 0.4830 0.6694 0.0604  0.0280  0.0208  38  CYS C CB  
10300 S SG  . CYS C 38  ? 1.0231 0.7738 0.9703 0.0472  0.0328  0.0238  38  CYS C SG  
10301 N N   . GLY C 39  ? 0.8110 0.4758 0.7170 0.0305  0.0395  0.0101  39  GLY C N   
10302 C CA  . GLY C 39  ? 1.0700 0.7049 0.9688 0.0268  0.0481  0.0167  39  GLY C CA  
10303 C C   . GLY C 39  ? 0.9919 0.6387 0.9010 0.0322  0.0528  0.0293  39  GLY C C   
10304 O O   . GLY C 39  ? 1.1772 0.8060 1.0760 0.0394  0.0576  0.0374  39  GLY C O   
10305 N N   . PHE C 40  ? 0.8838 0.5610 0.8129 0.0292  0.0515  0.0304  40  PHE C N   
10306 C CA  . PHE C 40  ? 0.8219 0.5115 0.7624 0.0341  0.0566  0.0408  40  PHE C CA  
10307 C C   . PHE C 40  ? 0.8681 0.5543 0.7996 0.0508  0.0568  0.0482  40  PHE C C   
10308 O O   . PHE C 40  ? 1.0235 0.6995 0.9513 0.0540  0.0625  0.0550  40  PHE C O   
10309 C CB  . PHE C 40  ? 0.8839 0.6075 0.8467 0.0320  0.0546  0.0403  40  PHE C CB  
10310 C CG  . PHE C 40  ? 0.8394 0.5707 0.8153 0.0152  0.0565  0.0348  40  PHE C CG  
10311 C CD1 . PHE C 40  ? 0.9180 0.6416 0.8985 0.0072  0.0648  0.0391  40  PHE C CD1 
10312 C CD2 . PHE C 40  ? 0.7276 0.4765 0.7116 0.0071  0.0503  0.0247  40  PHE C CD2 
10313 C CE1 . PHE C 40  ? 0.9447 0.6763 0.9378 -0.0087 0.0676  0.0342  40  PHE C CE1 
10314 C CE2 . PHE C 40  ? 0.7549 0.5133 0.7528 -0.0093 0.0527  0.0189  40  PHE C CE2 
10315 C CZ  . PHE C 40  ? 1.0062 0.7553 1.0088 -0.0173 0.0617  0.0240  40  PHE C CZ  
10316 N N   . GLY C 41  ? 0.8446 0.5412 0.7728 0.0609  0.0510  0.0465  41  GLY C N   
10317 C CA  . GLY C 41  ? 0.8616 0.5565 0.7823 0.0760  0.0520  0.0531  41  GLY C CA  
10318 C C   . GLY C 41  ? 0.8793 0.5464 0.7802 0.0802  0.0536  0.0532  41  GLY C C   
10319 O O   . GLY C 41  ? 0.9856 0.6493 0.8827 0.0892  0.0571  0.0598  41  GLY C O   
10320 N N   . SER C 42  ? 0.8684 0.5158 0.7571 0.0737  0.0513  0.0454  42  SER C N   
10321 C CA  . SER C 42  ? 0.7527 0.3705 0.6217 0.0785  0.0533  0.0453  42  SER C CA  
10322 C C   . SER C 42  ? 0.8482 0.4503 0.7146 0.0754  0.0602  0.0524  42  SER C C   
10323 O O   . SER C 42  ? 1.0403 0.6272 0.8936 0.0849  0.0626  0.0572  42  SER C O   
10324 C CB  . SER C 42  ? 0.7827 0.3819 0.6409 0.0709  0.0506  0.0342  42  SER C CB  
10325 O OG  . SER C 42  ? 0.8869 0.5034 0.7461 0.0738  0.0436  0.0265  42  SER C OG  
10326 N N   . ALA C 43  ? 0.9425 0.5502 0.8209 0.0627  0.0635  0.0532  43  ALA C N   
10327 C CA  . ALA C 43  ? 0.9806 0.5769 0.8567 0.0592  0.0703  0.0604  43  ALA C CA  
10328 C C   . ALA C 43  ? 0.9238 0.5414 0.8106 0.0654  0.0729  0.0676  43  ALA C C   
10329 O O   . ALA C 43  ? 0.9841 0.5964 0.8674 0.0653  0.0780  0.0734  43  ALA C O   
10330 C CB  . ALA C 43  ? 0.8286 0.4206 0.7119 0.0420  0.0738  0.0574  43  ALA C CB  
10331 N N   . GLY C 44  ? 0.9930 0.6341 0.8923 0.0707  0.0699  0.0669  44  GLY C N   
10332 C CA  . GLY C 44  ? 0.9000 0.5603 0.8113 0.0756  0.0733  0.0720  44  GLY C CA  
10333 C C   . GLY C 44  ? 0.8821 0.5577 0.8113 0.0657  0.0771  0.0723  44  GLY C C   
10334 O O   . GLY C 44  ? 1.0426 0.7311 0.9815 0.0680  0.0815  0.0756  44  GLY C O   
10335 N N   . VAL C 45  ? 0.9476 0.6233 0.8823 0.0540  0.0761  0.0680  45  VAL C N   
10336 C CA  . VAL C 45  ? 0.8312 0.5228 0.7836 0.0444  0.0802  0.0679  45  VAL C CA  
10337 C C   . VAL C 45  ? 0.9292 0.6469 0.9009 0.0460  0.0777  0.0661  45  VAL C C   
10338 O O   . VAL C 45  ? 0.9299 0.6616 0.9168 0.0377  0.0800  0.0646  45  VAL C O   
10339 C CB  . VAL C 45  ? 0.6627 0.3417 0.6122 0.0298  0.0829  0.0653  45  VAL C CB  
10340 C CG1 . VAL C 45  ? 0.9040 0.5619 0.8376 0.0299  0.0883  0.0707  45  VAL C CG1 
10341 C CG2 . VAL C 45  ? 0.9044 0.5731 0.8478 0.0242  0.0775  0.0582  45  VAL C CG2 
10342 N N   . CYS C 46  ? 0.8027 0.5269 0.7731 0.0574  0.0736  0.0672  46  CYS C N   
10343 C CA  . CYS C 46  ? 0.7311 0.4802 0.7188 0.0616  0.0721  0.0680  46  CYS C CA  
10344 C C   . CYS C 46  ? 0.8250 0.5812 0.8202 0.0716  0.0778  0.0743  46  CYS C C   
10345 O O   . CYS C 46  ? 1.0685 0.8151 1.0526 0.0797  0.0781  0.0767  46  CYS C O   
10346 C CB  . CYS C 46  ? 0.6233 0.3784 0.6056 0.0674  0.0640  0.0650  46  CYS C CB  
10347 S SG  . CYS C 46  ? 0.6868 0.4721 0.6876 0.0774  0.0633  0.0698  46  CYS C SG  
10348 N N   . CYS C 47  ? 0.6797 0.4521 0.6937 0.0707  0.0828  0.0762  47  CYS C N   
10349 C CA  . CYS C 47  ? 0.7877 0.5648 0.8107 0.0786  0.0903  0.0811  47  CYS C CA  
10350 C C   . CYS C 47  ? 0.7938 0.5884 0.8308 0.0877  0.0905  0.0854  47  CYS C C   
10351 O O   . CYS C 47  ? 0.7767 0.5860 0.8242 0.0850  0.0877  0.0841  47  CYS C O   
10352 C CB  . CYS C 47  ? 0.6066 0.3847 0.6391 0.0713  0.0986  0.0800  47  CYS C CB  
10353 S SG  . CYS C 47  ? 0.9416 0.7158 0.9758 0.0759  0.1076  0.0814  47  CYS C SG  
10354 N N   . ARG C 48  ? 0.7678 0.5615 0.8048 0.0985  0.0940  0.0906  48  ARG C N   
10355 C CA  . ARG C 48  ? 0.6579 0.4654 0.7070 0.1094  0.0966  0.0973  48  ARG C CA  
10356 C C   . ARG C 48  ? 0.8195 0.6221 0.8774 0.1141  0.1080  0.1014  48  ARG C C   
10357 O O   . ARG C 48  ? 0.7707 0.5765 0.8320 0.1250  0.1114  0.1085  48  ARG C O   
10358 C CB  . ARG C 48  ? 0.6379 0.4486 0.6748 0.1186  0.0887  0.1001  48  ARG C CB  
10359 C CG  . ARG C 48  ? 0.8591 0.6743 0.8872 0.1128  0.0777  0.0937  48  ARG C CG  
10360 C CD  . ARG C 48  ? 0.8754 0.6994 0.8937 0.1229  0.0702  0.0957  48  ARG C CD  
10361 N NE  . ARG C 48  ? 1.1668 0.9765 1.1647 0.1210  0.0641  0.0902  48  ARG C NE  
10362 C CZ  . ARG C 48  ? 1.0978 0.8974 1.0833 0.1292  0.0655  0.0933  48  ARG C CZ  
10363 N NH1 . ARG C 48  ? 0.7843 0.5834 0.7762 0.1369  0.0741  0.1013  48  ARG C NH1 
10364 N NH2 . ARG C 48  ? 1.2865 1.0764 1.2538 0.1294  0.0592  0.0878  48  ARG C NH2 
10365 N N   . ASN C 49  ? 0.9045 0.7002 0.9657 0.1059  0.1143  0.0968  49  ASN C N   
10366 C CA  . ASN C 49  ? 0.6097 0.4014 0.6800 0.1075  0.1256  0.0975  49  ASN C CA  
10367 C C   . ASN C 49  ? 0.6365 0.4359 0.7279 0.1107  0.1351  0.1005  49  ASN C C   
10368 O O   . ASN C 49  ? 0.7825 0.5771 0.8834 0.1109  0.1461  0.0998  49  ASN C O   
10369 C CB  . ASN C 49  ? 0.5378 0.3226 0.6029 0.0978  0.1280  0.0903  49  ASN C CB  
10370 C CG  . ASN C 49  ? 0.8057 0.5815 0.8511 0.0983  0.1214  0.0891  49  ASN C CG  
10371 O OD1 . ASN C 49  ? 0.8776 0.6507 0.9110 0.1019  0.1128  0.0911  49  ASN C OD1 
10372 N ND2 . ASN C 49  ? 0.8716 0.6440 0.9134 0.0952  0.1253  0.0852  49  ASN C ND2 
10373 N N   . CYS C 50  ? 0.6672 0.4785 0.7655 0.1145  0.1311  0.1040  50  CYS C N   
10374 C CA  . CYS C 50  ? 0.7725 0.5916 0.8909 0.1210  0.1403  0.1086  50  CYS C CA  
10375 C C   . CYS C 50  ? 0.6841 0.5210 0.8070 0.1266  0.1324  0.1126  50  CYS C C   
10376 O O   . CYS C 50  ? 0.7598 0.6015 0.8705 0.1229  0.1206  0.1098  50  CYS C O   
10377 C CB  . CYS C 50  ? 0.8042 0.6217 0.9353 0.1123  0.1498  0.1018  50  CYS C CB  
10378 S SG  . CYS C 50  ? 0.7234 0.5534 0.8574 0.1011  0.1436  0.0951  50  CYS C SG  
10379 N N   . SER C 51  ? 0.5489 0.3958 0.6889 0.1353  0.1390  0.1185  51  SER C N   
10380 C CA  . SER C 51  ? 0.6595 0.5286 0.8051 0.1433  0.1313  0.1232  51  SER C CA  
10381 C C   . SER C 51  ? 0.6729 0.5571 0.8316 0.1347  0.1300  0.1166  51  SER C C   
10382 O O   . SER C 51  ? 0.8364 0.7422 1.0067 0.1425  0.1273  0.1206  51  SER C O   
10383 C CB  . SER C 51  ? 0.5565 0.4302 0.7124 0.1609  0.1387  0.1356  51  SER C CB  
10384 O OG  . SER C 51  ? 0.8062 0.6827 0.9825 0.1631  0.1499  0.1363  51  SER C OG  
10385 N N   . MET C 52  ? 0.5481 0.4234 0.7051 0.1199  0.1322  0.1073  52  MET C N   
10386 C CA  . MET C 52  ? 0.6010 0.4918 0.7693 0.1107  0.1310  0.1010  52  MET C CA  
10387 C C   . MET C 52  ? 0.7229 0.6220 0.8795 0.1028  0.1172  0.0966  52  MET C C   
10388 O O   . MET C 52  ? 0.6766 0.5961 0.8438 0.0986  0.1132  0.0935  52  MET C O   
10389 C CB  . MET C 52  ? 0.6269 0.5065 0.7971 0.0982  0.1394  0.0933  52  MET C CB  
10390 C CG  . MET C 52  ? 0.5820 0.4607 0.7699 0.1037  0.1536  0.0943  52  MET C CG  
10391 S SD  . MET C 52  ? 0.5502 0.4302 0.7462 0.0894  0.1621  0.0838  52  MET C SD  
10392 C CE  . MET C 52  ? 0.5455 0.4055 0.7178 0.0770  0.1588  0.0780  52  MET C CE  
10393 N N   . GLY C 53  ? 0.6961 0.5804 0.8327 0.1011  0.1107  0.0960  53  GLY C N   
10394 C CA  . GLY C 53  ? 0.7612 0.6496 0.8855 0.0938  0.0985  0.0909  53  GLY C CA  
10395 C C   . GLY C 53  ? 0.6240 0.5258 0.7441 0.1058  0.0899  0.0955  53  GLY C C   
10396 O O   . GLY C 53  ? 0.9854 0.9025 1.1181 0.1189  0.0929  0.1031  53  GLY C O   
10397 N N   . PRO C 54  ? 0.7052 0.6019 0.8076 0.1028  0.0801  0.0916  54  PRO C N   
10398 C CA  . PRO C 54  ? 0.7660 0.6369 0.8502 0.0935  0.0794  0.0866  54  PRO C CA  
10399 C C   . PRO C 54  ? 0.8005 0.6668 0.8846 0.0761  0.0786  0.0779  54  PRO C C   
10400 O O   . PRO C 54  ? 0.7539 0.6377 0.8461 0.0698  0.0736  0.0730  54  PRO C O   
10401 C CB  . PRO C 54  ? 0.7563 0.6263 0.8235 0.0986  0.0695  0.0856  54  PRO C CB  
10402 C CG  . PRO C 54  ? 0.8622 0.7619 0.9393 0.1019  0.0620  0.0844  54  PRO C CG  
10403 C CD  . PRO C 54  ? 0.8392 0.7551 0.9375 0.1100  0.0696  0.0919  54  PRO C CD  
10404 N N   . CYS C 55  ? 0.7352 0.5795 0.8103 0.0691  0.0839  0.0766  55  CYS C N   
10405 C CA  . CYS C 55  ? 0.6516 0.4886 0.7254 0.0534  0.0857  0.0706  55  CYS C CA  
10406 C C   . CYS C 55  ? 0.7820 0.5982 0.8344 0.0471  0.0799  0.0664  55  CYS C C   
10407 O O   . CYS C 55  ? 0.7200 0.5224 0.7579 0.0552  0.0779  0.0689  55  CYS C O   
10408 C CB  . CYS C 55  ? 0.5638 0.3916 0.6405 0.0507  0.0958  0.0723  55  CYS C CB  
10409 S SG  . CYS C 55  ? 0.6301 0.4787 0.7328 0.0557  0.1050  0.0750  55  CYS C SG  
10410 N N   . ARG C 56  ? 0.6219 0.4356 0.6732 0.0331  0.0783  0.0602  56  ARG C N   
10411 C CA  . ARG C 56  ? 0.7350 0.5253 0.7667 0.0262  0.0748  0.0561  56  ARG C CA  
10412 C C   . ARG C 56  ? 0.8012 0.5815 0.8328 0.0105  0.0802  0.0533  56  ARG C C   
10413 O O   . ARG C 56  ? 0.8575 0.6512 0.9008 -0.0006 0.0796  0.0478  56  ARG C O   
10414 C CB  . ARG C 56  ? 0.6231 0.4197 0.6504 0.0264  0.0651  0.0497  56  ARG C CB  
10415 C CG  . ARG C 56  ? 0.8661 0.6941 0.9124 0.0223  0.0609  0.0450  56  ARG C CG  
10416 C CD  . ARG C 56  ? 0.7230 0.5550 0.7621 0.0186  0.0515  0.0358  56  ARG C CD  
10417 N NE  . ARG C 56  ? 0.9384 0.8073 0.9950 0.0201  0.0455  0.0323  56  ARG C NE  
10418 C CZ  . ARG C 56  ? 0.9763 0.8617 1.0294 0.0259  0.0360  0.0275  56  ARG C CZ  
10419 N NH1 . ARG C 56  ? 1.1008 0.9672 1.1332 0.0303  0.0318  0.0251  56  ARG C NH1 
10420 N NH2 . ARG C 56  ? 1.1034 1.0262 1.1733 0.0282  0.0306  0.0252  56  ARG C NH2 
10421 N N   . VAL C 57  ? 0.7230 0.4815 0.7416 0.0099  0.0860  0.0574  57  VAL C N   
10422 C CA  . VAL C 57  ? 0.6384 0.3848 0.6534 -0.0034 0.0926  0.0571  57  VAL C CA  
10423 C C   . VAL C 57  ? 0.7850 0.5045 0.7814 -0.0103 0.0904  0.0542  57  VAL C C   
10424 O O   . VAL C 57  ? 0.9530 0.6629 0.9383 -0.0032 0.0841  0.0523  57  VAL C O   
10425 C CB  . VAL C 57  ? 0.7730 0.5138 0.7840 0.0000  0.1004  0.0633  57  VAL C CB  
10426 C CG1 . VAL C 57  ? 0.6548 0.4192 0.6843 0.0070  0.1033  0.0646  57  VAL C CG1 
10427 C CG2 . VAL C 57  ? 0.8182 0.5372 0.8080 0.0094  0.0992  0.0674  57  VAL C CG2 
10428 N N   . SER C 58  ? 0.6800 0.3862 0.6728 -0.0239 0.0965  0.0537  58  SER C N   
10429 C CA  . SER C 58  ? 0.8431 0.5202 0.8191 -0.0315 0.0967  0.0511  58  SER C CA  
10430 C C   . SER C 58  ? 1.0245 0.6716 0.9761 -0.0216 0.0985  0.0582  58  SER C C   
10431 O O   . SER C 58  ? 1.0436 0.6883 0.9902 -0.0174 0.1040  0.0659  58  SER C O   
10432 C CB  . SER C 58  ? 0.8550 0.5269 0.8360 -0.0497 0.1046  0.0496  58  SER C CB  
10433 O OG  . SER C 58  ? 0.8886 0.5290 0.8539 -0.0581 0.1066  0.0471  58  SER C OG  
10434 N N   . PRO C 59  ? 1.0742 0.6991 1.0101 -0.0177 0.0943  0.0554  59  PRO C N   
10435 C CA  . PRO C 59  ? 0.9670 0.5643 0.8801 -0.0072 0.0965  0.0628  59  PRO C CA  
10436 C C   . PRO C 59  ? 1.0325 0.6017 0.9326 -0.0161 0.1056  0.0679  59  PRO C C   
10437 O O   . PRO C 59  ? 1.2285 0.7793 1.1110 -0.0067 0.1089  0.0766  59  PRO C O   
10438 C CB  . PRO C 59  ? 0.9496 0.5341 0.8521 -0.0002 0.0896  0.0570  59  PRO C CB  
10439 C CG  . PRO C 59  ? 0.9754 0.5765 0.8924 -0.0102 0.0844  0.0458  59  PRO C CG  
10440 C CD  . PRO C 59  ? 0.9688 0.5937 0.9065 -0.0224 0.0876  0.0448  59  PRO C CD  
10441 N N   . VAL C 60  ? 1.0305 0.5974 0.9392 -0.0338 0.1100  0.0629  60  VAL C N   
10442 C CA  . VAL C 60  ? 1.0083 0.5481 0.9061 -0.0443 0.1204  0.0682  60  VAL C CA  
10443 C C   . VAL C 60  ? 1.0994 0.6595 1.0088 -0.0509 0.1270  0.0736  60  VAL C C   
10444 O O   . VAL C 60  ? 1.0411 0.6252 0.9715 -0.0627 0.1271  0.0669  60  VAL C O   
10445 C CB  . VAL C 60  ? 0.8779 0.4014 0.7786 -0.0616 0.1224  0.0582  60  VAL C CB  
10446 C CG1 . VAL C 60  ? 1.0741 0.5679 0.9646 -0.0738 0.1354  0.0647  60  VAL C CG1 
10447 C CG2 . VAL C 60  ? 1.0372 0.5413 0.9260 -0.0549 0.1160  0.0512  60  VAL C CG2 
10448 N N   . PRO C 61  ? 1.1867 0.7406 1.0833 -0.0429 0.1326  0.0850  61  PRO C N   
10449 C CA  . PRO C 61  ? 1.0099 0.5847 0.9168 -0.0490 0.1392  0.0888  61  PRO C CA  
10450 C C   . PRO C 61  ? 1.0947 0.6637 1.0081 -0.0687 0.1486  0.0878  61  PRO C C   
10451 O O   . PRO C 61  ? 1.0524 0.5915 0.9552 -0.0770 0.1532  0.0881  61  PRO C O   
10452 C CB  . PRO C 61  ? 0.9497 0.5146 0.8365 -0.0365 0.1431  0.1007  61  PRO C CB  
10453 C CG  . PRO C 61  ? 1.2215 0.7695 1.0925 -0.0213 0.1366  0.1024  61  PRO C CG  
10454 C CD  . PRO C 61  ? 1.1657 0.6969 1.0383 -0.0273 0.1328  0.0942  61  PRO C CD  
10455 N N   . GLY C 62  ? 1.0525 0.6496 0.9836 -0.0760 0.1524  0.0865  62  GLY C N   
10456 C CA  . GLY C 62  ? 1.1360 0.7336 1.0762 -0.0951 0.1621  0.0853  62  GLY C CA  
10457 C C   . GLY C 62  ? 0.9995 0.6144 0.9631 -0.1090 0.1584  0.0723  62  GLY C C   
10458 O O   . GLY C 62  ? 1.2943 0.9174 1.2705 -0.1257 0.1660  0.0696  62  GLY C O   
10459 N N   . LYS C 63  ? 0.9670 0.5902 0.9368 -0.1022 0.1468  0.0641  63  LYS C N   
10460 C CA  . LYS C 63  ? 0.9978 0.6421 0.9892 -0.1137 0.1416  0.0512  63  LYS C CA  
10461 C C   . LYS C 63  ? 1.0332 0.7066 1.0371 -0.1000 0.1295  0.0462  63  LYS C C   
10462 O O   . LYS C 63  ? 1.1700 0.8379 1.1624 -0.0831 0.1247  0.0513  63  LYS C O   
10463 C CB  . LYS C 63  ? 1.0107 0.6265 0.9934 -0.1249 0.1417  0.0442  63  LYS C CB  
10464 C CG  . LYS C 63  ? 1.0060 0.5884 0.9638 -0.1113 0.1376  0.0477  63  LYS C CG  
10465 C CD  . LYS C 63  ? 1.1523 0.7045 1.1020 -0.1235 0.1392  0.0393  63  LYS C CD  
10466 C CE  . LYS C 63  ? 1.2816 0.7946 1.2156 -0.1338 0.1535  0.0472  63  LYS C CE  
10467 N NZ  . LYS C 63  ? 1.3638 0.8423 1.2888 -0.1443 0.1562  0.0387  63  LYS C NZ  
10468 N N   . GLY C 64  ? 0.9952 0.7005 1.0229 -0.1072 0.1252  0.0367  64  GLY C N   
10469 C CA  . GLY C 64  ? 0.9572 0.6914 0.9974 -0.0942 0.1146  0.0331  64  GLY C CA  
10470 C C   . GLY C 64  ? 0.7949 0.5488 0.8433 -0.0815 0.1164  0.0402  64  GLY C C   
10471 O O   . GLY C 64  ? 0.9371 0.6907 0.9864 -0.0856 0.1257  0.0454  64  GLY C O   
10472 N N   . VAL C 65  ? 0.7201 0.4908 0.7741 -0.0662 0.1084  0.0401  65  VAL C N   
10473 C CA  . VAL C 65  ? 0.6893 0.4770 0.7522 -0.0537 0.1106  0.0458  65  VAL C CA  
10474 C C   . VAL C 65  ? 0.7921 0.5554 0.8345 -0.0450 0.1145  0.0538  65  VAL C C   
10475 O O   . VAL C 65  ? 0.9044 0.6493 0.9303 -0.0363 0.1095  0.0556  65  VAL C O   
10476 C CB  . VAL C 65  ? 0.6345 0.4468 0.7104 -0.0401 0.1023  0.0442  65  VAL C CB  
10477 C CG1 . VAL C 65  ? 0.9019 0.7250 0.9853 -0.0274 0.1066  0.0502  65  VAL C CG1 
10478 C CG2 . VAL C 65  ? 0.6805 0.5237 0.7781 -0.0473 0.0982  0.0367  65  VAL C CG2 
10479 N N   . GLU C 66  ? 0.7465 0.5131 0.7909 -0.0464 0.1232  0.0579  66  GLU C N   
10480 C CA  . GLU C 66  ? 0.7529 0.4994 0.7771 -0.0393 0.1267  0.0647  66  GLU C CA  
10481 C C   . GLU C 66  ? 0.7445 0.5016 0.7725 -0.0240 0.1247  0.0662  66  GLU C C   
10482 O O   . GLU C 66  ? 0.9573 0.6988 0.9687 -0.0149 0.1220  0.0697  66  GLU C O   
10483 C CB  . GLU C 66  ? 1.0433 0.7873 1.0644 -0.0489 0.1373  0.0680  66  GLU C CB  
10484 C CG  . GLU C 66  ? 1.4188 1.1550 1.4247 -0.0404 0.1412  0.0739  66  GLU C CG  
10485 C CD  . GLU C 66  ? 1.3763 1.1250 1.3875 -0.0473 0.1514  0.0749  66  GLU C CD  
10486 O OE1 . GLU C 66  ? 1.4128 1.1804 1.4437 -0.0558 0.1549  0.0706  66  GLU C OE1 
10487 O OE2 . GLU C 66  ? 1.3340 1.0757 1.3296 -0.0436 0.1557  0.0797  66  GLU C OE2 
10488 N N   . ARG C 67  ? 0.7159 0.4981 0.7652 -0.0213 0.1266  0.0638  67  ARG C N   
10489 C CA  . ARG C 67  ? 0.7476 0.5369 0.8011 -0.0083 0.1270  0.0651  67  ARG C CA  
10490 C C   . ARG C 67  ? 0.7720 0.5777 0.8417 0.0005  0.1218  0.0637  67  ARG C C   
10491 O O   . ARG C 67  ? 0.6419 0.4617 0.7242 -0.0036 0.1187  0.0609  67  ARG C O   
10492 C CB  . ARG C 67  ? 0.7361 0.5374 0.7987 -0.0105 0.1369  0.0643  67  ARG C CB  
10493 C CG  . ARG C 67  ? 0.8586 0.6489 0.9062 -0.0195 0.1430  0.0664  67  ARG C CG  
10494 C CD  . ARG C 67  ? 0.7858 0.5920 0.8439 -0.0237 0.1530  0.0641  67  ARG C CD  
10495 N NE  . ARG C 67  ? 0.9310 0.7367 0.9817 -0.0167 0.1564  0.0637  67  ARG C NE  
10496 C CZ  . ARG C 67  ? 0.9985 0.7957 1.0303 -0.0184 0.1597  0.0662  67  ARG C CZ  
10497 N NH1 . ARG C 67  ? 0.8560 0.6407 0.8730 -0.0263 0.1611  0.0711  67  ARG C NH1 
10498 N NH2 . ARG C 67  ? 1.0369 0.8388 1.0645 -0.0121 0.1621  0.0638  67  ARG C NH2 
10499 N N   . GLY C 68  ? 0.7455 0.5502 0.8144 0.0127  0.1215  0.0658  68  GLY C N   
10500 C CA  . GLY C 68  ? 0.5910 0.4089 0.6732 0.0235  0.1184  0.0669  68  GLY C CA  
10501 C C   . GLY C 68  ? 0.6530 0.4914 0.7581 0.0246  0.1255  0.0659  68  GLY C C   
10502 O O   . GLY C 68  ? 0.7018 0.5436 0.8114 0.0170  0.1330  0.0635  68  GLY C O   
10503 N N   . ILE C 69  ? 0.6520 0.5041 0.7713 0.0350  0.1242  0.0681  69  ILE C N   
10504 C CA  . ILE C 69  ? 0.5532 0.4245 0.6953 0.0383  0.1315  0.0678  69  ILE C CA  
10505 C C   . ILE C 69  ? 0.6424 0.5079 0.7879 0.0386  0.1429  0.0661  69  ILE C C   
10506 O O   . ILE C 69  ? 0.5344 0.4114 0.6936 0.0346  0.1505  0.0630  69  ILE C O   
10507 C CB  . ILE C 69  ? 0.6478 0.5333 0.8023 0.0521  0.1282  0.0725  69  ILE C CB  
10508 C CG1 . ILE C 69  ? 0.6100 0.5076 0.7627 0.0496  0.1167  0.0716  69  ILE C CG1 
10509 C CG2 . ILE C 69  ? 0.5317 0.4346 0.7097 0.0578  0.1371  0.0732  69  ILE C CG2 
10510 C CD1 . ILE C 69  ? 0.5411 0.4536 0.7007 0.0634  0.1114  0.0765  69  ILE C CD1 
10511 N N   . CYS C 70  ? 0.7090 0.5581 0.8415 0.0423  0.1437  0.0670  70  CYS C N   
10512 C CA  . CYS C 70  ? 0.5443 0.3885 0.6788 0.0421  0.1539  0.0635  70  CYS C CA  
10513 C C   . CYS C 70  ? 0.6887 0.5295 0.8121 0.0301  0.1564  0.0591  70  CYS C C   
10514 O O   . CYS C 70  ? 0.7412 0.5859 0.8703 0.0274  0.1657  0.0541  70  CYS C O   
10515 C CB  . CYS C 70  ? 0.5308 0.3619 0.6557 0.0493  0.1533  0.0653  70  CYS C CB  
10516 S SG  . CYS C 70  ? 0.6868 0.5024 0.7849 0.0438  0.1472  0.0643  70  CYS C SG  
10517 N N   . GLY C 71  ? 0.6842 0.5174 0.7917 0.0236  0.1491  0.0608  71  GLY C N   
10518 C CA  . GLY C 71  ? 0.6150 0.4419 0.7081 0.0137  0.1512  0.0592  71  GLY C CA  
10519 C C   . GLY C 71  ? 0.7177 0.5267 0.7872 0.0151  0.1454  0.0621  71  GLY C C   
10520 O O   . GLY C 71  ? 0.9434 0.7452 0.9979 0.0089  0.1467  0.0627  71  GLY C O   
10521 N N   . ALA C 72  ? 0.5808 0.3828 0.6462 0.0241  0.1395  0.0644  72  ALA C N   
10522 C CA  . ALA C 72  ? 0.5816 0.3680 0.6258 0.0272  0.1340  0.0670  72  ALA C CA  
10523 C C   . ALA C 72  ? 0.7145 0.4881 0.7437 0.0207  0.1290  0.0696  72  ALA C C   
10524 O O   . ALA C 72  ? 0.7367 0.5118 0.7717 0.0176  0.1250  0.0695  72  ALA C O   
10525 C CB  . ALA C 72  ? 0.6571 0.4404 0.7017 0.0378  0.1291  0.0690  72  ALA C CB  
10526 N N   . THR C 73  ? 0.7489 0.5104 0.7591 0.0189  0.1295  0.0718  73  THR C N   
10527 C CA  . THR C 73  ? 0.6600 0.4043 0.6542 0.0132  0.1266  0.0752  73  THR C CA  
10528 C C   . THR C 73  ? 0.7546 0.4836 0.7361 0.0210  0.1185  0.0771  73  THR C C   
10529 O O   . THR C 73  ? 0.8056 0.5388 0.7894 0.0306  0.1158  0.0766  73  THR C O   
10530 C CB  . THR C 73  ? 0.7935 0.5311 0.7715 0.0102  0.1316  0.0784  73  THR C CB  
10531 O OG1 . THR C 73  ? 0.8175 0.5539 0.7845 0.0201  0.1300  0.0795  73  THR C OG1 
10532 C CG2 . THR C 73  ? 0.8805 0.6341 0.8693 0.0024  0.1402  0.0758  73  THR C CG2 
10533 N N   . ALA C 74  ? 0.8173 0.5276 0.7854 0.0166  0.1156  0.0790  74  ALA C N   
10534 C CA  . ALA C 74  ? 0.6915 0.3857 0.6464 0.0240  0.1086  0.0799  74  ALA C CA  
10535 C C   . ALA C 74  ? 0.8236 0.5127 0.7648 0.0357  0.1078  0.0832  74  ALA C C   
10536 O O   . ALA C 74  ? 0.8936 0.5822 0.8329 0.0451  0.1030  0.0826  74  ALA C O   
10537 C CB  . ALA C 74  ? 0.8286 0.5003 0.7703 0.0164  0.1081  0.0807  74  ALA C CB  
10538 N N   . ASP C 75  ? 0.8113 0.4993 0.7433 0.0354  0.1126  0.0867  75  ASP C N   
10539 C CA  . ASP C 75  ? 0.8611 0.5492 0.7809 0.0463  0.1117  0.0893  75  ASP C CA  
10540 C C   . ASP C 75  ? 0.8718 0.5802 0.8063 0.0520  0.1115  0.0849  75  ASP C C   
10541 O O   . ASP C 75  ? 0.8885 0.5969 0.8175 0.0618  0.1082  0.0852  75  ASP C O   
10542 C CB  . ASP C 75  ? 0.9751 0.6635 0.8833 0.0443  0.1170  0.0934  75  ASP C CB  
10543 C CG  . ASP C 75  ? 0.9892 0.6528 0.8793 0.0409  0.1185  0.1000  75  ASP C CG  
10544 O OD1 . ASP C 75  ? 0.9614 0.6051 0.8379 0.0476  0.1144  0.1029  75  ASP C OD1 
10545 O OD2 . ASP C 75  ? 1.0527 0.7158 0.9422 0.0315  0.1245  0.1023  75  ASP C OD2 
10546 N N   . VAL C 76  ? 0.8015 0.5265 0.7553 0.0460  0.1159  0.0807  76  VAL C N   
10547 C CA  . VAL C 76  ? 0.7329 0.4741 0.7021 0.0505  0.1178  0.0766  76  VAL C CA  
10548 C C   . VAL C 76  ? 0.8145 0.5520 0.7880 0.0570  0.1126  0.0772  76  VAL C C   
10549 O O   . VAL C 76  ? 0.8769 0.6166 0.8491 0.0651  0.1113  0.0771  76  VAL C O   
10550 C CB  . VAL C 76  ? 0.5959 0.3526 0.5849 0.0433  0.1249  0.0723  76  VAL C CB  
10551 C CG1 . VAL C 76  ? 0.5686 0.3370 0.5746 0.0481  0.1281  0.0686  76  VAL C CG1 
10552 C CG2 . VAL C 76  ? 0.8267 0.5898 0.8104 0.0377  0.1306  0.0707  76  VAL C CG2 
10553 N N   . ILE C 77  ? 0.8080 0.5415 0.7861 0.0531  0.1096  0.0775  77  ILE C N   
10554 C CA  . ILE C 77  ? 0.9179 0.6507 0.8990 0.0592  0.1042  0.0779  77  ILE C CA  
10555 C C   . ILE C 77  ? 0.9056 0.6252 0.8688 0.0679  0.0990  0.0798  77  ILE C C   
10556 O O   . ILE C 77  ? 0.9256 0.6498 0.8911 0.0764  0.0979  0.0803  77  ILE C O   
10557 C CB  . ILE C 77  ? 0.7311 0.4640 0.7177 0.0524  0.1009  0.0766  77  ILE C CB  
10558 C CG1 . ILE C 77  ? 0.6387 0.3898 0.6470 0.0472  0.1060  0.0750  77  ILE C CG1 
10559 C CG2 . ILE C 77  ? 0.6961 0.4277 0.6802 0.0593  0.0938  0.0765  77  ILE C CG2 
10560 C CD1 . ILE C 77  ? 0.6050 0.3604 0.6201 0.0379  0.1042  0.0728  77  ILE C CD1 
10561 N N   . VAL C 78  ? 0.8811 0.5838 0.8267 0.0660  0.0969  0.0813  78  VAL C N   
10562 C CA  . VAL C 78  ? 0.7670 0.4550 0.6944 0.0748  0.0926  0.0831  78  VAL C CA  
10563 C C   . VAL C 78  ? 0.7995 0.4961 0.7246 0.0839  0.0943  0.0842  78  VAL C C   
10564 O O   . VAL C 78  ? 0.8875 0.5831 0.8080 0.0931  0.0913  0.0845  78  VAL C O   
10565 C CB  . VAL C 78  ? 0.7089 0.3751 0.6186 0.0709  0.0923  0.0854  78  VAL C CB  
10566 C CG1 . VAL C 78  ? 0.7585 0.4095 0.6491 0.0820  0.0894  0.0881  78  VAL C CG1 
10567 C CG2 . VAL C 78  ? 0.7772 0.4338 0.6889 0.0615  0.0902  0.0825  78  VAL C CG2 
10568 N N   . SER C 79  ? 0.7635 0.4700 0.6916 0.0810  0.0991  0.0841  79  SER C N   
10569 C CA  . SER C 79  ? 0.7416 0.4601 0.6689 0.0879  0.1007  0.0833  79  SER C CA  
10570 C C   . SER C 79  ? 0.7843 0.5169 0.7280 0.0909  0.1028  0.0802  79  SER C C   
10571 O O   . SER C 79  ? 0.8369 0.5747 0.7781 0.0986  0.1021  0.0798  79  SER C O   
10572 C CB  . SER C 79  ? 0.7471 0.4764 0.6747 0.0829  0.1055  0.0822  79  SER C CB  
10573 O OG  . SER C 79  ? 0.8688 0.6122 0.8156 0.0749  0.1112  0.0776  79  SER C OG  
10574 N N   . ARG C 80  ? 0.8026 0.5415 0.7634 0.0852  0.1060  0.0785  80  ARG C N   
10575 C CA  . ARG C 80  ? 0.6275 0.3768 0.6039 0.0885  0.1097  0.0772  80  ARG C CA  
10576 C C   . ARG C 80  ? 0.7079 0.4503 0.6779 0.0969  0.1045  0.0803  80  ARG C C   
10577 O O   . ARG C 80  ? 0.7617 0.5094 0.7342 0.1033  0.1062  0.0806  80  ARG C O   
10578 C CB  . ARG C 80  ? 0.7168 0.4730 0.7118 0.0824  0.1147  0.0760  80  ARG C CB  
10579 C CG  . ARG C 80  ? 0.8213 0.5862 0.8241 0.0743  0.1212  0.0715  80  ARG C CG  
10580 C CD  . ARG C 80  ? 0.7640 0.5366 0.7873 0.0704  0.1278  0.0699  80  ARG C CD  
10581 N NE  . ARG C 80  ? 0.6885 0.4579 0.7141 0.0688  0.1239  0.0731  80  ARG C NE  
10582 C CZ  . ARG C 80  ? 0.7175 0.4947 0.7599 0.0661  0.1282  0.0727  80  ARG C CZ  
10583 N NH1 . ARG C 80  ? 0.8327 0.6178 0.8905 0.0650  0.1375  0.0692  80  ARG C NH1 
10584 N NH2 . ARG C 80  ? 0.8530 0.6309 0.8975 0.0647  0.1236  0.0749  80  ARG C NH2 
10585 N N   . ASN C 81  ? 0.8072 0.5386 0.7689 0.0963  0.0985  0.0820  81  ASN C N   
10586 C CA  . ASN C 81  ? 0.7678 0.4930 0.7213 0.1039  0.0930  0.0837  81  ASN C CA  
10587 C C   . ASN C 81  ? 0.8522 0.5721 0.7913 0.1124  0.0912  0.0842  81  ASN C C   
10588 O O   . ASN C 81  ? 0.9240 0.6470 0.8622 0.1204  0.0906  0.0852  81  ASN C O   
10589 C CB  . ASN C 81  ? 0.7287 0.4425 0.6741 0.0995  0.0870  0.0827  81  ASN C CB  
10590 C CG  . ASN C 81  ? 0.8051 0.5284 0.7652 0.0937  0.0872  0.0821  81  ASN C CG  
10591 O OD1 . ASN C 81  ? 0.8566 0.5934 0.8322 0.0957  0.0914  0.0837  81  ASN C OD1 
10592 N ND2 . ASN C 81  ? 0.7806 0.4975 0.7369 0.0866  0.0831  0.0796  81  ASN C ND2 
10593 N N   . PHE C 82  ? 0.7134 0.4267 0.6414 0.1115  0.0907  0.0840  82  PHE C N   
10594 C CA  . PHE C 82  ? 0.7286 0.4391 0.6433 0.1208  0.0889  0.0849  82  PHE C CA  
10595 C C   . PHE C 82  ? 0.7852 0.5145 0.7112 0.1244  0.0936  0.0834  82  PHE C C   
10596 O O   . PHE C 82  ? 0.9232 0.6554 0.8461 0.1329  0.0928  0.0838  82  PHE C O   
10597 C CB  . PHE C 82  ? 0.6654 0.3669 0.5665 0.1198  0.0883  0.0865  82  PHE C CB  
10598 C CG  . PHE C 82  ? 0.7732 0.4728 0.6600 0.1313  0.0862  0.0882  82  PHE C CG  
10599 C CD1 . PHE C 82  ? 0.7004 0.3808 0.5707 0.1390  0.0821  0.0901  82  PHE C CD1 
10600 C CD2 . PHE C 82  ? 0.8578 0.5763 0.7484 0.1347  0.0887  0.0872  82  PHE C CD2 
10601 C CE1 . PHE C 82  ? 0.6577 0.3371 0.5153 0.1513  0.0806  0.0921  82  PHE C CE1 
10602 C CE2 . PHE C 82  ? 0.8628 0.5834 0.7414 0.1464  0.0864  0.0889  82  PHE C CE2 
10603 C CZ  . PHE C 82  ? 0.7446 0.4454 0.6068 0.1554  0.0825  0.0920  82  PHE C CZ  
10604 N N   . ALA C 83  ? 0.7840 0.5261 0.7236 0.1170  0.0991  0.0808  83  ALA C N   
10605 C CA  . ALA C 83  ? 0.7623 0.5224 0.7152 0.1174  0.1051  0.0774  83  ALA C CA  
10606 C C   . ALA C 83  ? 0.7181 0.4801 0.6794 0.1219  0.1075  0.0790  83  ALA C C   
10607 O O   . ALA C 83  ? 0.8600 0.6304 0.8218 0.1276  0.1093  0.0781  83  ALA C O   
10608 C CB  . ALA C 83  ? 0.6445 0.4138 0.6125 0.1072  0.1114  0.0734  83  ALA C CB  
10609 N N   . ARG C 84  ? 0.6928 0.4492 0.6606 0.1199  0.1079  0.0816  84  ARG C N   
10610 C CA  . ARG C 84  ? 0.7251 0.4842 0.7008 0.1248  0.1112  0.0848  84  ARG C CA  
10611 C C   . ARG C 84  ? 0.7244 0.4797 0.6859 0.1350  0.1064  0.0871  84  ARG C C   
10612 O O   . ARG C 84  ? 0.7243 0.4858 0.6910 0.1399  0.1109  0.0891  84  ARG C O   
10613 C CB  . ARG C 84  ? 0.6712 0.4272 0.6544 0.1227  0.1109  0.0881  84  ARG C CB  
10614 C CG  . ARG C 84  ? 0.7566 0.5187 0.7581 0.1148  0.1185  0.0863  84  ARG C CG  
10615 C CD  . ARG C 84  ? 0.6813 0.4455 0.6955 0.1175  0.1226  0.0913  84  ARG C CD  
10616 N NE  . ARG C 84  ? 0.8067 0.5757 0.8394 0.1114  0.1318  0.0891  84  ARG C NE  
10617 C CZ  . ARG C 84  ? 0.8774 0.6483 0.9234 0.1133  0.1366  0.0934  84  ARG C CZ  
10618 N NH1 . ARG C 84  ? 0.8681 0.6392 0.9105 0.1213  0.1322  0.1004  84  ARG C NH1 
10619 N NH2 . ARG C 84  ? 0.6743 0.4478 0.7367 0.1081  0.1458  0.0904  84  ARG C NH2 
10620 N N   . MET C 85  ? 0.7300 0.4742 0.6737 0.1381  0.0985  0.0868  85  MET C N   
10621 C CA  . MET C 85  ? 0.7594 0.4987 0.6887 0.1483  0.0944  0.0878  85  MET C CA  
10622 C C   . MET C 85  ? 0.7850 0.5356 0.7151 0.1532  0.0978  0.0863  85  MET C C   
10623 O O   . MET C 85  ? 0.8749 0.6304 0.8033 0.1607  0.0992  0.0875  85  MET C O   
10624 C CB  . MET C 85  ? 0.6970 0.4191 0.6078 0.1499  0.0867  0.0869  85  MET C CB  
10625 C CG  . MET C 85  ? 0.7824 0.4953 0.6921 0.1445  0.0828  0.0866  85  MET C CG  
10626 S SD  . MET C 85  ? 1.0172 0.7069 0.9051 0.1458  0.0756  0.0841  85  MET C SD  
10627 C CE  . MET C 85  ? 1.1001 0.7886 0.9773 0.1573  0.0723  0.0830  85  MET C CE  
10628 N N   . VAL C 86  ? 0.7733 0.5305 0.7061 0.1489  0.0991  0.0834  86  VAL C N   
10629 C CA  . VAL C 86  ? 0.7215 0.4945 0.6565 0.1527  0.1018  0.0806  86  VAL C CA  
10630 C C   . VAL C 86  ? 0.8080 0.5958 0.7621 0.1493  0.1106  0.0790  86  VAL C C   
10631 O O   . VAL C 86  ? 0.8934 0.6909 0.8488 0.1552  0.1132  0.0787  86  VAL C O   
10632 C CB  . VAL C 86  ? 0.5777 0.3575 0.5115 0.1482  0.1011  0.0776  86  VAL C CB  
10633 C CG1 . VAL C 86  ? 0.6620 0.4654 0.6031 0.1500  0.1044  0.0728  86  VAL C CG1 
10634 C CG2 . VAL C 86  ? 0.7683 0.5317 0.6815 0.1535  0.0939  0.0808  86  VAL C CG2 
10635 N N   . ALA C 87  ? 0.7798 0.5683 0.7490 0.1400  0.1163  0.0783  87  ALA C N   
10636 C CA  . ALA C 87  ? 0.6101 0.4079 0.5981 0.1361  0.1267  0.0773  87  ALA C CA  
10637 C C   . ALA C 87  ? 0.7749 0.5686 0.7610 0.1439  0.1286  0.0836  87  ALA C C   
10638 O O   . ALA C 87  ? 0.8522 0.6551 0.8484 0.1443  0.1368  0.0833  87  ALA C O   
10639 C CB  . ALA C 87  ? 0.7649 0.5595 0.7669 0.1269  0.1321  0.0766  87  ALA C CB  
10640 N N   . ALA C 88  ? 0.8763 0.6572 0.8495 0.1496  0.1216  0.0888  88  ALA C N   
10641 C CA  . ALA C 88  ? 0.7406 0.5192 0.7091 0.1580  0.1225  0.0946  88  ALA C CA  
10642 C C   . ALA C 88  ? 0.7441 0.5278 0.7014 0.1666  0.1203  0.0934  88  ALA C C   
10643 O O   . ALA C 88  ? 0.8205 0.6111 0.7815 0.1710  0.1265  0.0962  88  ALA C O   
10644 C CB  . ALA C 88  ? 0.6879 0.4549 0.6456 0.1608  0.1147  0.0982  88  ALA C CB  
10645 N N   . GLY C 89  ? 0.7365 0.5167 0.6805 0.1694  0.1125  0.0898  89  GLY C N   
10646 C CA  . GLY C 89  ? 0.7354 0.5207 0.6686 0.1790  0.1102  0.0884  89  GLY C CA  
10647 C C   . GLY C 89  ? 0.8336 0.6394 0.7809 0.1772  0.1181  0.0852  89  GLY C C   
10648 O O   . GLY C 89  ? 0.9301 0.7449 0.8771 0.1839  0.1215  0.0860  89  GLY C O   
10649 N N   . THR C 90  ? 0.7939 0.6087 0.7544 0.1675  0.1215  0.0807  90  THR C N   
10650 C CA  . THR C 90  ? 0.7081 0.5448 0.6847 0.1627  0.1294  0.0751  90  THR C CA  
10651 C C   . THR C 90  ? 0.7876 0.6277 0.7783 0.1603  0.1406  0.0778  90  THR C C   
10652 O O   . THR C 90  ? 0.8508 0.7069 0.8491 0.1613  0.1466  0.0752  90  THR C O   
10653 C CB  . THR C 90  ? 0.7899 0.6336 0.7774 0.1514  0.1310  0.0688  90  THR C CB  
10654 O OG1 . THR C 90  ? 0.8186 0.6600 0.7912 0.1551  0.1215  0.0678  90  THR C OG1 
10655 C CG2 . THR C 90  ? 0.6425 0.5101 0.6489 0.1438  0.1399  0.0604  90  THR C CG2 
10656 N N   . ALA C 91  ? 0.7684 0.5941 0.7627 0.1576  0.1439  0.0836  91  ALA C N   
10657 C CA  . ALA C 91  ? 0.7380 0.5632 0.7440 0.1566  0.1554  0.0888  91  ALA C CA  
10658 C C   . ALA C 91  ? 0.9145 0.7415 0.9098 0.1677  0.1555  0.0943  91  ALA C C   
10659 O O   . ALA C 91  ? 0.9441 0.7795 0.9498 0.1669  0.1664  0.0959  91  ALA C O   
10660 C CB  . ALA C 91  ? 0.6873 0.4973 0.6962 0.1546  0.1569  0.0953  91  ALA C CB  
10661 N N   . ALA C 92  ? 0.8574 0.6764 0.8322 0.1776  0.1444  0.0966  92  ALA C N   
10662 C CA  . ALA C 92  ? 0.7212 0.5420 0.6839 0.1888  0.1441  0.1006  92  ALA C CA  
10663 C C   . ALA C 92  ? 0.8890 0.7285 0.8564 0.1909  0.1481  0.0956  92  ALA C C   
10664 O O   . ALA C 92  ? 1.0046 0.8524 0.9761 0.1939  0.1566  0.0988  92  ALA C O   
10665 C CB  . ALA C 92  ? 0.7358 0.5439 0.6761 0.1975  0.1314  0.1011  92  ALA C CB  
10666 N N   . HIS C 93  ? 0.8387 0.6865 0.8058 0.1895  0.1424  0.0881  93  HIS C N   
10667 C CA  . HIS C 93  ? 0.7672 0.6373 0.7399 0.1921  0.1453  0.0826  93  HIS C CA  
10668 C C   . HIS C 93  ? 0.8022 0.6894 0.7997 0.1798  0.1581  0.0784  93  HIS C C   
10669 O O   . HIS C 93  ? 0.9521 0.8587 0.9580 0.1808  0.1647  0.0756  93  HIS C O   
10670 C CB  . HIS C 93  ? 0.7321 0.6076 0.6963 0.1959  0.1353  0.0770  93  HIS C CB  
10671 C CG  . HIS C 93  ? 0.8917 0.7520 0.8322 0.2092  0.1251  0.0799  93  HIS C CG  
10672 N ND1 . HIS C 93  ? 0.9695 0.8149 0.8975 0.2103  0.1158  0.0795  93  HIS C ND1 
10673 C CD2 . HIS C 93  ? 0.9497 0.8068 0.8775 0.2212  0.1241  0.0825  93  HIS C CD2 
10674 C CE1 . HIS C 93  ? 0.9482 0.7801 0.8570 0.2224  0.1097  0.0816  93  HIS C CE1 
10675 N NE2 . HIS C 93  ? 1.0431 0.8820 0.9508 0.2295  0.1141  0.0829  93  HIS C NE2 
10676 N N   . SER C 94  ? 0.8858 0.7661 0.8958 0.1679  0.1625  0.0772  94  SER C N   
10677 C CA  . SER C 94  ? 0.9574 0.8500 0.9915 0.1548  0.1758  0.0719  94  SER C CA  
10678 C C   . SER C 94  ? 0.8385 0.7297 0.8802 0.1554  0.1889  0.0786  94  SER C C   
10679 O O   . SER C 94  ? 0.8853 0.7953 0.9401 0.1514  0.1980  0.0738  94  SER C O   
10680 C CB  . SER C 94  ? 1.0208 0.9012 1.0644 0.1439  0.1783  0.0703  94  SER C CB  
10681 O OG  . SER C 94  ? 0.8581 0.7455 0.9251 0.1310  0.1930  0.0650  94  SER C OG  
10682 N N   . ASP C 95  ? 0.9049 0.7759 0.9378 0.1610  0.1899  0.0898  95  ASP C N   
10683 C CA  . ASP C 95  ? 1.0835 0.9518 1.1213 0.1631  0.2032  0.0986  95  ASP C CA  
10684 C C   . ASP C 95  ? 1.0297 0.9137 1.0596 0.1721  0.2028  0.0985  95  ASP C C   
10685 O O   . ASP C 95  ? 1.0837 0.9768 1.1255 0.1690  0.2166  0.1003  95  ASP C O   
10686 C CB  . ASP C 95  ? 1.0571 0.9041 1.0840 0.1699  0.2022  0.1113  95  ASP C CB  
10687 C CG  . ASP C 95  ? 1.0847 0.9194 1.1281 0.1611  0.2139  0.1153  95  ASP C CG  
10688 O OD1 . ASP C 95  ? 1.0458 0.8865 1.1093 0.1485  0.2237  0.1074  95  ASP C OD1 
10689 O OD2 . ASP C 95  ? 1.1440 0.9640 1.1802 0.1673  0.2132  0.1259  95  ASP C OD2 
10690 N N   . HIS C 96  ? 0.8213 0.7077 0.8326 0.1827  0.1886  0.0962  96  HIS C N   
10691 C CA  . HIS C 96  ? 0.7663 0.6669 0.7688 0.1931  0.1875  0.0956  96  HIS C CA  
10692 C C   . HIS C 96  ? 0.7882 0.7159 0.8111 0.1852  0.1963  0.0867  96  HIS C C   
10693 O O   . HIS C 96  ? 0.8574 0.7960 0.8889 0.1845  0.2084  0.0890  96  HIS C O   
10694 C CB  . HIS C 96  ? 0.7364 0.6322 0.7169 0.2050  0.1712  0.0931  96  HIS C CB  
10695 C CG  . HIS C 96  ? 0.7460 0.6549 0.7162 0.2176  0.1695  0.0919  96  HIS C CG  
10696 N ND1 . HIS C 96  ? 1.0097 0.9454 0.9924 0.2167  0.1739  0.0850  96  HIS C ND1 
10697 C CD2 . HIS C 96  ? 0.9702 0.8700 0.9192 0.2312  0.1638  0.0958  96  HIS C CD2 
10698 C CE1 . HIS C 96  ? 0.9882 0.9298 0.9574 0.2307  0.1713  0.0858  96  HIS C CE1 
10699 N NE2 . HIS C 96  ? 1.1961 1.1155 1.1443 0.2397  0.1654  0.0919  96  HIS C NE2 
10700 N N   . GLY C 97  ? 0.7312 0.6712 0.7619 0.1789  0.1907  0.0764  97  GLY C N   
10701 C CA  . GLY C 97  ? 0.7254 0.6956 0.7761 0.1707  0.1974  0.0658  97  GLY C CA  
10702 C C   . GLY C 97  ? 0.8118 0.7857 0.8871 0.1548  0.2152  0.0639  97  GLY C C   
10703 O O   . GLY C 97  ? 0.7873 0.7852 0.8786 0.1492  0.2250  0.0578  97  GLY C O   
10704 N N   . ARG C 98  ? 0.8261 0.7764 0.9055 0.1472  0.2203  0.0686  98  ARG C N   
10705 C CA  . ARG C 98  ? 0.8407 0.7874 0.9428 0.1325  0.2388  0.0680  98  ARG C CA  
10706 C C   . ARG C 98  ? 0.9020 0.8490 1.0062 0.1360  0.2523  0.0771  98  ARG C C   
10707 O O   . ARG C 98  ? 0.8615 0.8201 0.9867 0.1243  0.2683  0.0725  98  ARG C O   
10708 C CB  . ARG C 98  ? 0.7791 0.6967 0.8804 0.1289  0.2404  0.0746  98  ARG C CB  
10709 C CG  . ARG C 98  ? 0.6735 0.5838 0.7989 0.1133  0.2594  0.0723  98  ARG C CG  
10710 C CD  . ARG C 98  ? 0.7825 0.6616 0.9039 0.1161  0.2641  0.0854  98  ARG C CD  
10711 N NE  . ARG C 98  ? 0.8238 0.6915 0.9292 0.1229  0.2477  0.0873  98  ARG C NE  
10712 C CZ  . ARG C 98  ? 0.8222 0.6893 0.9336 0.1147  0.2427  0.0779  98  ARG C CZ  
10713 N NH1 . ARG C 98  ? 0.6632 0.5414 0.7958 0.0995  0.2521  0.0646  98  ARG C NH1 
10714 N NH2 . ARG C 98  ? 0.8693 0.7258 0.9657 0.1212  0.2286  0.0809  98  ARG C NH2 
10715 N N   . SER C 99  ? 0.9869 0.9212 1.0690 0.1516  0.2465  0.0896  99  SER C N   
10716 C CA  . SER C 99  ? 0.8251 0.7594 0.9042 0.1577  0.2580  0.0999  99  SER C CA  
10717 C C   . SER C 99  ? 0.9118 0.8770 0.9977 0.1583  0.2608  0.0919  99  SER C C   
10718 O O   . SER C 99  ? 1.0167 0.9906 1.1160 0.1527  0.2774  0.0941  99  SER C O   
10719 C CB  . SER C 99  ? 0.6161 0.5336 0.6676 0.1749  0.2480  0.1124  99  SER C CB  
10720 O OG  . SER C 99  ? 1.0264 0.9391 1.0740 0.1802  0.2607  0.1250  99  SER C OG  
10721 N N   . ILE C 100 ? 0.8797 0.8619 0.9571 0.1654  0.2454  0.0830  100 ILE C N   
10722 C CA  . ILE C 100 ? 0.7957 0.8106 0.8791 0.1685  0.2460  0.0749  100 ILE C CA  
10723 C C   . ILE C 100 ? 0.8764 0.9147 0.9906 0.1497  0.2592  0.0631  100 ILE C C   
10724 O O   . ILE C 100 ? 0.8848 0.9441 1.0123 0.1461  0.2715  0.0609  100 ILE C O   
10725 C CB  . ILE C 100 ? 0.8177 0.8444 0.8864 0.1807  0.2267  0.0681  100 ILE C CB  
10726 C CG1 . ILE C 100 ? 0.8428 0.8430 0.8818 0.1967  0.2129  0.0771  100 ILE C CG1 
10727 C CG2 . ILE C 100 ? 0.7203 0.7822 0.7947 0.1868  0.2276  0.0612  100 ILE C CG2 
10728 C CD1 . ILE C 100 ? 0.8446 0.8337 0.8686 0.2076  0.2170  0.0878  100 ILE C CD1 
10729 N N   . ALA C 101 ? 0.7228 0.7585 0.8487 0.1370  0.2572  0.0545  101 ALA C N   
10730 C CA  . ALA C 101 ? 0.7430 0.8005 0.8983 0.1174  0.2692  0.0405  101 ALA C CA  
10731 C C   . ALA C 101 ? 0.8124 0.8585 0.9849 0.1053  0.2922  0.0459  101 ALA C C   
10732 O O   . ALA C 101 ? 0.8002 0.8707 0.9955 0.0926  0.3054  0.0364  101 ALA C O   
10733 C CB  . ALA C 101 ? 0.7352 0.7870 0.8961 0.1073  0.2628  0.0314  101 ALA C CB  
10734 N N   . LEU C 102 ? 0.8565 0.8666 1.0186 0.1091  0.2977  0.0612  102 LEU C N   
10735 C CA  . LEU C 102 ? 0.8448 0.8399 1.0206 0.1000  0.3205  0.0694  102 LEU C CA  
10736 C C   . LEU C 102 ? 0.8844 0.8960 1.0592 0.1060  0.3296  0.0751  102 LEU C C   
10737 O O   . LEU C 102 ? 0.8853 0.9023 1.0805 0.0931  0.3500  0.0740  102 LEU C O   
10738 C CB  . LEU C 102 ? 0.8107 0.7660 0.9725 0.1068  0.3227  0.0866  102 LEU C CB  
10739 C CG  . LEU C 102 ? 0.6347 0.5707 0.8035 0.0979  0.3207  0.0821  102 LEU C CG  
10740 C CD1 . LEU C 102 ? 0.7584 0.6624 0.9078 0.1103  0.3157  0.0989  102 LEU C CD1 
10741 C CD2 . LEU C 102 ? 0.6375 0.5692 0.8355 0.0772  0.3425  0.0747  102 LEU C CD2 
10742 N N   . SER C 103 ? 0.9560 0.9755 1.1076 0.1248  0.3154  0.0804  103 SER C N   
10743 C CA  . SER C 103 ? 0.8670 0.9044 1.0155 0.1325  0.3226  0.0850  103 SER C CA  
10744 C C   . SER C 103 ? 0.8581 0.9363 1.0312 0.1209  0.3279  0.0680  103 SER C C   
10745 O O   . SER C 103 ? 0.9680 1.0596 1.1560 0.1137  0.3456  0.0687  103 SER C O   
10746 C CB  . SER C 103 ? 0.7586 0.7953 0.8769 0.1551  0.3049  0.0914  103 SER C CB  
10747 O OG  . SER C 103 ? 0.7809 0.7852 0.8773 0.1656  0.3025  0.1073  103 SER C OG  
10748 N N   . LEU C 104 ? 0.8471 0.9464 1.0250 0.1188  0.3131  0.0528  104 LEU C N   
10749 C CA  . LEU C 104 ? 0.9118 1.0549 1.1134 0.1084  0.3158  0.0352  104 LEU C CA  
10750 C C   . LEU C 104 ? 0.9986 1.1459 1.2322 0.0831  0.3379  0.0269  104 LEU C C   
10751 O O   . LEU C 104 ? 0.9218 1.1026 1.1772 0.0730  0.3488  0.0167  104 LEU C O   
10752 C CB  . LEU C 104 ? 0.8156 0.9763 1.0140 0.1113  0.2956  0.0223  104 LEU C CB  
10753 C CG  . LEU C 104 ? 0.5877 0.7994 0.8074 0.1041  0.2940  0.0037  104 LEU C CG  
10754 C CD1 . LEU C 104 ? 0.5896 0.8296 0.8032 0.1199  0.2910  0.0056  104 LEU C CD1 
10755 C CD2 . LEU C 104 ? 0.5751 0.7988 0.7909 0.1057  0.2758  -0.0070 104 LEU C CD2 
10756 N N   . TYR C 105 ? 0.9272 1.0407 1.1645 0.0728  0.3451  0.0307  105 TYR C N   
10757 C CA  . TYR C 105 ? 0.8714 0.9804 1.1378 0.0489  0.3675  0.0235  105 TYR C CA  
10758 C C   . TYR C 105 ? 0.8737 0.9728 1.1466 0.0459  0.3908  0.0361  105 TYR C C   
10759 O O   . TYR C 105 ? 0.9446 1.0495 1.2449 0.0254  0.4118  0.0281  105 TYR C O   
10760 C CB  . TYR C 105 ? 0.8397 0.9110 1.1044 0.0427  0.3683  0.0263  105 TYR C CB  
10761 C CG  . TYR C 105 ? 0.9024 0.9648 1.1968 0.0179  0.3909  0.0170  105 TYR C CG  
10762 C CD1 . TYR C 105 ? 0.9774 1.0725 1.2982 -0.0017 0.3939  -0.0071 105 TYR C CD1 
10763 C CD2 . TYR C 105 ? 0.8048 0.8256 1.1003 0.0146  0.4090  0.0317  105 TYR C CD2 
10764 C CE1 . TYR C 105 ? 1.0136 1.0989 1.3619 -0.0257 0.4153  -0.0178 105 TYR C CE1 
10765 C CE2 . TYR C 105 ? 0.9231 0.9314 1.2457 -0.0078 0.4310  0.0230  105 TYR C CE2 
10766 C CZ  . TYR C 105 ? 0.9811 1.0209 1.3304 -0.0288 0.4344  -0.0027 105 TYR C CZ  
10767 O OH  . TYR C 105 ? 0.9775 1.0042 1.3543 -0.0524 0.4571  -0.0135 105 TYR C OH  
10768 N N   . HIS C 106 ? 0.8495 0.9340 1.0973 0.0657  0.3879  0.0553  106 HIS C N   
10769 C CA  . HIS C 106 ? 0.9394 1.0145 1.1886 0.0659  0.4091  0.0698  106 HIS C CA  
10770 C C   . HIS C 106 ? 0.9243 1.0333 1.1677 0.0772  0.4065  0.0698  106 HIS C C   
10771 O O   . HIS C 106 ? 1.0527 1.1504 1.2790 0.0902  0.4125  0.0866  106 HIS C O   
10772 C CB  . HIS C 106 ? 0.9858 1.0169 1.2101 0.0800  0.4103  0.0932  106 HIS C CB  
10773 C CG  . HIS C 106 ? 1.1526 1.1503 1.3815 0.0717  0.4130  0.0948  106 HIS C CG  
10774 N ND1 . HIS C 106 ? 1.2719 1.2439 1.4769 0.0863  0.3969  0.1049  106 HIS C ND1 
10775 C CD2 . HIS C 106 ? 1.1213 1.1084 1.3766 0.0505  0.4305  0.0868  106 HIS C CD2 
10776 C CE1 . HIS C 106 ? 1.2554 1.2033 1.4729 0.0746  0.4048  0.1035  106 HIS C CE1 
10777 N NE2 . HIS C 106 ? 1.0930 1.0475 1.3402 0.0532  0.4251  0.0926  106 HIS C NE2 
10778 N N   . THR C 107 ? 1.0518 0.9018 1.1004 0.2165  0.4490  0.3494  107 THR C N   
10779 C CA  . THR C 107 ? 1.0633 0.9641 1.1193 0.2104  0.4807  0.3573  107 THR C CA  
10780 C C   . THR C 107 ? 1.1750 1.0800 1.2456 0.1695  0.5080  0.3703  107 THR C C   
10781 O O   . THR C 107 ? 1.2002 1.0982 1.3044 0.1464  0.5001  0.3650  107 THR C O   
10782 C CB  . THR C 107 ? 1.0966 1.0760 1.2073 0.2237  0.4766  0.3374  107 THR C CB  
10783 O OG1 . THR C 107 ? 1.0877 1.0948 1.2506 0.2077  0.4629  0.3229  107 THR C OG1 
10784 C CG2 . THR C 107 ? 0.9804 0.9571 1.0703 0.2589  0.4565  0.3292  107 THR C CG2 
10785 N N   . SER C 108 ? 1.1804 1.1001 1.2268 0.1580  0.5411  0.3847  108 SER C N   
10786 C CA  . SER C 108 ? 1.1818 1.1132 1.2395 0.1130  0.5730  0.3974  108 SER C CA  
10787 C C   . SER C 108 ? 1.3297 1.3394 1.4036 0.1095  0.6103  0.3917  108 SER C C   
10788 O O   . SER C 108 ? 1.4361 1.4604 1.4853 0.1414  0.6118  0.3864  108 SER C O   
10789 C CB  . SER C 108 ? 1.2811 1.1171 1.2647 0.0907  0.5755  0.4291  108 SER C CB  
10790 O OG  . SER C 108 ? 1.5732 1.3752 1.4838 0.1149  0.5768  0.4426  108 SER C OG  
10791 N N   . LYS C 109 ? 1.2011 1.2648 1.3206 0.0707  0.6401  0.3886  109 LYS C N   
10792 C CA  . LYS C 109 ? 1.1868 1.3387 1.3340 0.0660  0.6774  0.3755  109 LYS C CA  
10793 C C   . LYS C 109 ? 1.4414 1.5727 1.5127 0.0576  0.6967  0.3860  109 LYS C C   
10794 O O   . LYS C 109 ? 1.6556 1.8521 1.7388 0.0722  0.7067  0.3618  109 LYS C O   
10795 C CB  . LYS C 109 ? 1.2943 1.5056 1.5012 0.0168  0.7029  0.3668  109 LYS C CB  
10796 C CG  . LYS C 109 ? 1.5575 1.8739 1.8077 0.0149  0.7218  0.3340  109 LYS C CG  
10797 C CD  . LYS C 109 ? 1.3670 1.7510 1.6797 -0.0352 0.7454  0.3206  109 LYS C CD  
10798 C CE  . LYS C 109 ? 1.2346 1.7301 1.5934 -0.0337 0.7638  0.2828  109 LYS C CE  
10799 N NZ  . LYS C 109 ? 1.3284 1.9062 1.7630 -0.0774 0.7825  0.2626  109 LYS C NZ  
10800 N N   . ASP C 110 ? 1.7009 1.7396 1.6932 0.0353  0.6971  0.4201  110 ASP C N   
10801 C CA  . ASP C 110 ? 1.7497 1.7611 1.6583 0.0233  0.7100  0.4335  110 ASP C CA  
10802 C C   . ASP C 110 ? 1.6670 1.5734 1.4994 0.0536  0.6794  0.4583  110 ASP C C   
10803 O O   . ASP C 110 ? 1.8491 1.6734 1.6058 0.0307  0.6740  0.4887  110 ASP C O   
10804 C CB  . ASP C 110 ? 1.7652 1.7675 1.6428 -0.0415 0.7368  0.4526  110 ASP C CB  
10805 C CG  . ASP C 110 ? 2.2323 2.2506 2.0399 -0.0574 0.7576  0.4553  110 ASP C CG  
10806 O OD1 . ASP C 110 ? 2.2472 2.3329 2.0695 -0.0257 0.7646  0.4257  110 ASP C OD1 
10807 O OD2 . ASP C 110 ? 2.4220 2.3848 2.1594 -0.1031 0.7654  0.4869  110 ASP C OD2 
10808 N N   . GLY C 111 ? 1.4430 1.3541 1.2970 0.1040  0.6566  0.4438  111 GLY C N   
10809 C CA  . GLY C 111 ? 1.5381 1.3657 1.3326 0.1379  0.6242  0.4578  111 GLY C CA  
10810 C C   . GLY C 111 ? 1.4741 1.3304 1.2556 0.1838  0.6171  0.4387  111 GLY C C   
10811 O O   . GLY C 111 ? 1.4764 1.4146 1.3065 0.1941  0.6307  0.4115  111 GLY C O   
10812 N N   . ASP C 112 ? 1.4801 1.2681 1.2014 0.2118  0.5873  0.4466  112 ASP C N   
10813 C CA  . ASP C 112 ? 1.3313 1.1361 1.0354 0.2540  0.5769  0.4283  112 ASP C CA  
10814 C C   . ASP C 112 ? 1.2291 1.0870 1.0115 0.2809  0.5583  0.3977  112 ASP C C   
10815 O O   . ASP C 112 ? 1.3452 1.2516 1.1452 0.3043  0.5646  0.3775  112 ASP C O   
10816 C CB  . ASP C 112 ? 1.4259 1.1454 1.0551 0.2759  0.5439  0.4416  112 ASP C CB  
10817 C CG  . ASP C 112 ? 1.5919 1.2673 1.1301 0.2608  0.5543  0.4644  112 ASP C CG  
10818 O OD1 . ASP C 112 ? 1.7169 1.4397 1.2514 0.2332  0.5861  0.4616  112 ASP C OD1 
10819 O OD2 . ASP C 112 ? 1.7350 1.3346 1.2113 0.2747  0.5231  0.4782  112 ASP C OD2 
10820 N N   . ILE C 113 ? 1.2341 1.0807 1.0606 0.2766  0.5342  0.3941  113 ILE C N   
10821 C CA  . ILE C 113 ? 1.1108 1.0028 1.0028 0.2952  0.5149  0.3701  113 ILE C CA  
10822 C C   . ILE C 113 ? 1.2343 1.1833 1.1952 0.2692  0.5304  0.3646  113 ILE C C   
10823 O O   . ILE C 113 ? 1.3850 1.3134 1.3513 0.2388  0.5356  0.3764  113 ILE C O   
10824 C CB  . ILE C 113 ? 1.1350 0.9824 1.0240 0.3093  0.4761  0.3648  113 ILE C CB  
10825 C CG1 . ILE C 113 ? 1.2437 1.0308 1.0634 0.3320  0.4596  0.3705  113 ILE C CG1 
10826 C CG2 . ILE C 113 ? 1.0008 0.8948 0.9435 0.3252  0.4578  0.3429  113 ILE C CG2 
10827 C CD1 . ILE C 113 ? 1.3857 1.1294 1.2022 0.3445  0.4226  0.3622  113 ILE C CD1 
10828 N N   . LYS C 114 ? 1.0789 1.0969 1.0931 0.2820  0.5346  0.3456  114 LYS C N   
10829 C CA  . LYS C 114 ? 1.1042 1.1869 1.1897 0.2608  0.5468  0.3364  114 LYS C CA  
10830 C C   . LYS C 114 ? 1.0173 1.1464 1.1582 0.2837  0.5227  0.3170  114 LYS C C   
10831 O O   . LYS C 114 ? 1.0806 1.1955 1.2027 0.3138  0.5045  0.3113  114 LYS C O   
10832 C CB  . LYS C 114 ? 1.1174 1.2523 1.2136 0.2458  0.5874  0.3336  114 LYS C CB  
10833 C CG  . LYS C 114 ? 1.4186 1.5113 1.4472 0.2203  0.6156  0.3561  114 LYS C CG  
10834 C CD  . LYS C 114 ? 1.1436 1.2762 1.1543 0.2208  0.6369  0.3417  114 LYS C CD  
10835 C CE  . LYS C 114 ? 1.3427 1.5143 1.3637 0.1734  0.6700  0.3421  114 LYS C CE  
10836 N NZ  . LYS C 114 ? 1.7631 1.8750 1.6959 0.1459  0.6856  0.3690  114 LYS C NZ  
10837 N N   . VAL C 115 ? 0.9149 1.0948 1.1191 0.2682  0.5207  0.3081  115 VAL C N   
10838 C CA  . VAL C 115 ? 0.8781 1.1020 1.1325 0.2874  0.4946  0.2930  115 VAL C CA  
10839 C C   . VAL C 115 ? 0.8702 1.1520 1.1602 0.3073  0.5068  0.2776  115 VAL C C   
10840 O O   . VAL C 115 ? 0.8591 1.1950 1.1889 0.2902  0.5332  0.2691  115 VAL C O   
10841 C CB  . VAL C 115 ? 0.8246 1.0800 1.1295 0.2639  0.4832  0.2881  115 VAL C CB  
10842 C CG1 . VAL C 115 ? 0.9302 1.2345 1.2831 0.2816  0.4563  0.2756  115 VAL C CG1 
10843 C CG2 . VAL C 115 ? 1.0716 1.2743 1.3478 0.2492  0.4671  0.2953  115 VAL C CG2 
10844 N N   . LYS C 116 ? 0.9408 1.2131 1.2204 0.3413  0.4879  0.2711  116 LYS C N   
10845 C CA  . LYS C 116 ? 0.8996 1.2156 1.2116 0.3636  0.4862  0.2493  116 LYS C CA  
10846 C C   . LYS C 116 ? 0.8562 1.2186 1.2348 0.3777  0.4584  0.2384  116 LYS C C   
10847 O O   . LYS C 116 ? 1.0152 1.4386 1.4478 0.3819  0.4625  0.2165  116 LYS C O   
10848 C CB  . LYS C 116 ? 0.8569 1.1291 1.1215 0.3914  0.4736  0.2454  116 LYS C CB  
10849 C CG  . LYS C 116 ? 0.8982 1.1389 1.1013 0.3836  0.5008  0.2507  116 LYS C CG  
10850 C CD  . LYS C 116 ? 0.9504 1.1628 1.1184 0.4123  0.4877  0.2391  116 LYS C CD  
10851 C CE  . LYS C 116 ? 0.9608 1.1451 1.0640 0.4074  0.5126  0.2443  116 LYS C CE  
10852 N NZ  . LYS C 116 ? 1.0131 1.1556 1.0742 0.4342  0.4936  0.2375  116 LYS C NZ  
10853 N N   . ASP C 117 ? 0.7860 1.1197 1.1572 0.3823  0.4255  0.2509  117 ASP C N   
10854 C CA  . ASP C 117 ? 0.7974 1.1646 1.2180 0.3927  0.3916  0.2453  117 ASP C CA  
10855 C C   . ASP C 117 ? 0.8065 1.2000 1.2522 0.3615  0.3873  0.2494  117 ASP C C   
10856 O O   . ASP C 117 ? 0.9272 1.2877 1.3426 0.3469  0.3698  0.2621  117 ASP C O   
10857 C CB  . ASP C 117 ? 0.7690 1.0865 1.1578 0.4118  0.3526  0.2559  117 ASP C CB  
10858 C CG  . ASP C 117 ? 0.8982 1.2408 1.3315 0.4335  0.3149  0.2505  117 ASP C CG  
10859 O OD1 . ASP C 117 ? 0.8967 1.2859 1.3738 0.4226  0.3045  0.2471  117 ASP C OD1 
10860 O OD2 . ASP C 117 ? 1.0831 1.3957 1.5074 0.4619  0.2929  0.2491  117 ASP C OD2 
10861 N N   . GLU C 118 ? 0.8513 1.3103 1.3560 0.3506  0.4040  0.2346  118 GLU C N   
10862 C CA  . GLU C 118 ? 0.7951 1.2853 1.3312 0.3201  0.4005  0.2336  118 GLU C CA  
10863 C C   . GLU C 118 ? 0.7913 1.2966 1.3482 0.3298  0.3546  0.2343  118 GLU C C   
10864 O O   . GLU C 118 ? 0.7617 1.2612 1.3092 0.3070  0.3412  0.2401  118 GLU C O   
10865 C CB  . GLU C 118 ? 0.8310 1.3937 1.4300 0.3042  0.4307  0.2147  118 GLU C CB  
10866 C CG  . GLU C 118 ? 1.0260 1.5735 1.5970 0.2811  0.4784  0.2191  118 GLU C CG  
10867 C CD  . GLU C 118 ? 0.9742 1.5987 1.6058 0.2592  0.5127  0.2001  118 GLU C CD  
10868 O OE1 . GLU C 118 ? 1.0190 1.7050 1.7170 0.2505  0.5001  0.1843  118 GLU C OE1 
10869 O OE2 . GLU C 118 ? 1.1744 1.7944 1.7789 0.2455  0.5461  0.1974  118 GLU C OE2 
10870 N N   . ASN C 119 ? 0.8133 1.3358 1.3961 0.3637  0.3284  0.2276  119 ASN C N   
10871 C CA  . ASN C 119 ? 0.7801 1.3099 1.3753 0.3738  0.2796  0.2329  119 ASN C CA  
10872 C C   . ASN C 119 ? 0.8434 1.3091 1.3686 0.3626  0.2581  0.2566  119 ASN C C   
10873 O O   . ASN C 119 ? 0.9004 1.3756 1.4205 0.3451  0.2337  0.2629  119 ASN C O   
10874 C CB  . ASN C 119 ? 0.7510 1.2938 1.3803 0.4162  0.2521  0.2231  119 ASN C CB  
10875 C CG  . ASN C 119 ? 0.9572 1.5807 1.6678 0.4289  0.2693  0.1920  119 ASN C CG  
10876 O OD1 . ASN C 119 ? 0.9034 1.5826 1.6535 0.4022  0.2923  0.1798  119 ASN C OD1 
10877 N ND2 . ASN C 119 ? 1.2756 1.9099 2.0167 0.4690  0.2588  0.1749  119 ASN C ND2 
10878 N N   . LYS C 120 ? 0.8624 1.2689 1.3343 0.3706  0.2680  0.2669  120 LYS C N   
10879 C CA  . LYS C 120 ? 0.7633 1.1164 1.1727 0.3578  0.2519  0.2850  120 LYS C CA  
10880 C C   . LYS C 120 ? 0.8157 1.1733 1.2100 0.3231  0.2679  0.2838  120 LYS C C   
10881 O O   . LYS C 120 ? 0.9145 1.2669 1.2840 0.3055  0.2473  0.2904  120 LYS C O   
10882 C CB  . LYS C 120 ? 0.7490 1.0453 1.1128 0.3731  0.2619  0.2906  120 LYS C CB  
10883 C CG  . LYS C 120 ? 0.7545 1.0031 1.0606 0.3603  0.2428  0.3062  120 LYS C CG  
10884 C CD  . LYS C 120 ? 0.7833 0.9827 1.0604 0.3826  0.2290  0.3130  120 LYS C CD  
10885 C CE  . LYS C 120 ? 0.9917 1.1533 1.2167 0.3631  0.2099  0.3279  120 LYS C CE  
10886 N NZ  . LYS C 120 ? 1.0628 1.1736 1.2621 0.3807  0.1926  0.3354  120 LYS C NZ  
10887 N N   . LEU C 121 ? 0.8133 1.1803 1.2215 0.3119  0.3036  0.2744  121 LEU C N   
10888 C CA  . LEU C 121 ? 0.7327 1.0967 1.1320 0.2815  0.3163  0.2705  121 LEU C CA  
10889 C C   . LEU C 121 ? 0.8312 1.2456 1.2681 0.2629  0.2981  0.2619  121 LEU C C   
10890 O O   . LEU C 121 ? 0.9714 1.3815 1.3906 0.2418  0.2901  0.2584  121 LEU C O   
10891 C CB  . LEU C 121 ? 0.7114 1.0688 1.1181 0.2717  0.3549  0.2661  121 LEU C CB  
10892 C CG  . LEU C 121 ? 0.7128 1.0643 1.1219 0.2404  0.3662  0.2603  121 LEU C CG  
10893 C CD1 . LEU C 121 ? 0.7872 1.0886 1.1465 0.2364  0.3567  0.2625  121 LEU C CD1 
10894 C CD2 . LEU C 121 ? 0.7444 1.0890 1.1622 0.2274  0.4014  0.2610  121 LEU C CD2 
10895 N N   . LYS C 122 ? 0.6970 1.1637 1.1880 0.2718  0.2903  0.2545  122 LYS C N   
10896 C CA  . LYS C 122 ? 0.6930 1.2127 1.2226 0.2559  0.2698  0.2443  122 LYS C CA  
10897 C C   . LYS C 122 ? 0.8140 1.3237 1.3065 0.2554  0.2296  0.2556  122 LYS C C   
10898 O O   . LYS C 122 ? 0.8015 1.3350 1.2935 0.2323  0.2168  0.2484  122 LYS C O   
10899 C CB  . LYS C 122 ? 0.7923 1.3748 1.3923 0.2703  0.2662  0.2310  122 LYS C CB  
10900 C CG  . LYS C 122 ? 0.7443 1.3491 1.3822 0.2638  0.3101  0.2183  122 LYS C CG  
10901 C CD  . LYS C 122 ? 0.6902 1.3439 1.3775 0.2302  0.3255  0.2012  122 LYS C CD  
10902 C CE  . LYS C 122 ? 0.6982 1.3903 1.4321 0.2221  0.3656  0.1883  122 LYS C CE  
10903 N NZ  . LYS C 122 ? 0.6982 1.4545 1.4913 0.2515  0.3565  0.1719  122 LYS C NZ  
10904 N N   . GLU C 123 ? 0.8972 1.3705 1.3556 0.2782  0.2101  0.2727  123 GLU C N   
10905 C CA  . GLU C 123 ? 0.9514 1.4068 1.3644 0.2735  0.1728  0.2893  123 GLU C CA  
10906 C C   . GLU C 123 ? 0.9054 1.3315 1.2632 0.2478  0.1837  0.2909  123 GLU C C   
10907 O O   . GLU C 123 ? 0.9484 1.3906 1.2817 0.2254  0.1649  0.2916  123 GLU C O   
10908 C CB  . GLU C 123 ? 0.8888 1.3040 1.2825 0.3030  0.1500  0.3075  123 GLU C CB  
10909 C CG  . GLU C 123 ? 1.0639 1.5096 1.5082 0.3307  0.1204  0.3054  123 GLU C CG  
10910 C CD  . GLU C 123 ? 1.3808 1.8524 1.8223 0.3212  0.0759  0.3142  123 GLU C CD  
10911 O OE1 . GLU C 123 ? 1.5330 1.9721 1.9115 0.3026  0.0540  0.3353  123 GLU C OE1 
10912 O OE2 . GLU C 123 ? 1.4771 2.0050 1.9783 0.3305  0.0630  0.2992  123 GLU C OE2 
10913 N N   . VAL C 124 ? 0.7174 1.1050 1.0558 0.2514  0.2129  0.2887  124 VAL C N   
10914 C CA  . VAL C 124 ? 0.7108 1.0744 1.0058 0.2321  0.2226  0.2841  124 VAL C CA  
10915 C C   . VAL C 124 ? 0.8313 1.2292 1.1470 0.2069  0.2314  0.2627  124 VAL C C   
10916 O O   . VAL C 124 ? 0.8993 1.3071 1.1889 0.1863  0.2231  0.2540  124 VAL C O   
10917 C CB  . VAL C 124 ? 0.7739 1.0895 1.0487 0.2462  0.2478  0.2847  124 VAL C CB  
10918 C CG1 . VAL C 124 ? 0.6999 0.9994 0.9454 0.2293  0.2581  0.2718  124 VAL C CG1 
10919 C CG2 . VAL C 124 ? 0.8593 1.1392 1.1077 0.2676  0.2352  0.3018  124 VAL C CG2 
10920 N N   . ALA C 125 ? 0.8127 1.2316 1.1767 0.2064  0.2482  0.2518  125 ALA C N   
10921 C CA  . ALA C 125 ? 0.7099 1.1561 1.0994 0.1819  0.2549  0.2299  125 ALA C CA  
10922 C C   . ALA C 125 ? 0.7542 1.2489 1.1465 0.1650  0.2264  0.2222  125 ALA C C   
10923 O O   . ALA C 125 ? 0.9576 1.4699 1.3512 0.1432  0.2266  0.2008  125 ALA C O   
10924 C CB  . ALA C 125 ? 0.6932 1.1563 1.1361 0.1804  0.2758  0.2231  125 ALA C CB  
10925 N N   . LYS C 126 ? 0.7501 1.2647 1.1414 0.1758  0.1995  0.2381  126 LYS C N   
10926 C CA  . LYS C 126 ? 0.8042 1.3622 1.1884 0.1598  0.1680  0.2352  126 LYS C CA  
10927 C C   . LYS C 126 ? 0.8302 1.3766 1.1513 0.1401  0.1604  0.2360  126 LYS C C   
10928 O O   . LYS C 126 ? 0.7649 1.3489 1.0792 0.1158  0.1524  0.2172  126 LYS C O   
10929 C CB  . LYS C 126 ? 0.7430 1.3137 1.1358 0.1798  0.1348  0.2559  126 LYS C CB  
10930 C CG  . LYS C 126 ? 1.0236 1.6374 1.4045 0.1646  0.0963  0.2567  126 LYS C CG  
10931 C CD  . LYS C 126 ? 1.3379 1.9567 1.7304 0.1897  0.0570  0.2776  126 LYS C CD  
10932 C CE  . LYS C 126 ? 1.3864 2.0425 1.7580 0.1751  0.0137  0.2824  126 LYS C CE  
10933 N NZ  . LYS C 126 ? 1.2028 1.8559 1.5869 0.2042  -0.0313 0.3032  126 LYS C NZ  
10934 N N   . SER C 127 ? 0.9025 1.4023 1.1795 0.1487  0.1642  0.2539  127 SER C N   
10935 C CA  . SER C 127 ? 0.9226 1.4181 1.1427 0.1268  0.1607  0.2525  127 SER C CA  
10936 C C   . SER C 127 ? 0.8430 1.3513 1.0710 0.1113  0.1842  0.2173  127 SER C C   
10937 O O   . SER C 127 ? 0.9985 1.5394 1.2003 0.0861  0.1788  0.2001  127 SER C O   
10938 C CB  . SER C 127 ? 0.9361 1.3795 1.1155 0.1384  0.1611  0.2763  127 SER C CB  
10939 O OG  . SER C 127 ? 1.1484 1.5576 1.3374 0.1528  0.1897  0.2660  127 SER C OG  
10940 N N   . PHE C 128 ? 0.7852 1.2680 1.0477 0.1256  0.2085  0.2054  128 PHE C N   
10941 C CA  . PHE C 128 ? 0.8485 1.3318 1.1221 0.1157  0.2251  0.1720  128 PHE C CA  
10942 C C   . PHE C 128 ? 0.8253 1.3486 1.1412 0.0999  0.2227  0.1453  128 PHE C C   
10943 O O   . PHE C 128 ? 0.9793 1.4977 1.3119 0.0934  0.2332  0.1153  128 PHE C O   
10944 C CB  . PHE C 128 ? 0.7457 1.1733 1.0283 0.1363  0.2474  0.1743  128 PHE C CB  
10945 C CG  . PHE C 128 ? 0.7479 1.1397 0.9891 0.1483  0.2508  0.1860  128 PHE C CG  
10946 C CD1 . PHE C 128 ? 0.8368 1.2331 1.0558 0.1392  0.2521  0.1630  128 PHE C CD1 
10947 C CD2 . PHE C 128 ? 0.7891 1.1476 1.0185 0.1687  0.2522  0.2151  128 PHE C CD2 
10948 C CE1 . PHE C 128 ? 0.8330 1.2019 1.0192 0.1482  0.2549  0.1707  128 PHE C CE1 
10949 C CE2 . PHE C 128 ? 0.8699 1.1956 1.0634 0.1782  0.2540  0.2231  128 PHE C CE2 
10950 C CZ  . PHE C 128 ? 0.8233 1.1547 0.9957 0.1669  0.2554  0.2018  128 PHE C CZ  
10951 N N   . ASN C 129 ? 0.7027 1.2642 1.0379 0.0948  0.2059  0.1536  129 ASN C N   
10952 C CA  . ASN C 129 ? 0.7404 1.3456 1.1188 0.0784  0.2009  0.1273  129 ASN C CA  
10953 C C   . ASN C 129 ? 0.7597 1.3385 1.1883 0.0820  0.2235  0.1159  129 ASN C C   
10954 O O   . ASN C 129 ? 0.9006 1.4891 1.3558 0.0662  0.2271  0.0847  129 ASN C O   
10955 C CB  . ASN C 129 ? 0.9023 1.5456 1.2612 0.0544  0.1927  0.0935  129 ASN C CB  
10956 C CG  . ASN C 129 ? 0.9253 1.6269 1.3154 0.0355  0.1769  0.0695  129 ASN C CG  
10957 O OD1 . ASN C 129 ? 0.8983 1.6250 1.3098 0.0384  0.1614  0.0847  129 ASN C OD1 
10958 N ND2 . ASN C 129 ? 0.9385 1.6660 1.3352 0.0175  0.1782  0.0272  129 ASN C ND2 
10959 N N   . VAL C 130 ? 0.7341 1.2782 1.1732 0.1007  0.2382  0.1409  130 VAL C N   
10960 C CA  . VAL C 130 ? 0.7352 1.2515 1.2122 0.1000  0.2619  0.1381  130 VAL C CA  
10961 C C   . VAL C 130 ? 0.8831 1.4414 1.4088 0.0996  0.2608  0.1452  130 VAL C C   
10962 O O   . VAL C 130 ? 0.8713 1.4433 1.3923 0.1178  0.2514  0.1654  130 VAL C O   
10963 C CB  . VAL C 130 ? 0.7080 1.1598 1.1561 0.1193  0.2821  0.1579  130 VAL C CB  
10964 C CG1 . VAL C 130 ? 0.7065 1.1294 1.1843 0.1146  0.3071  0.1621  130 VAL C CG1 
10965 C CG2 . VAL C 130 ? 0.8078 1.2251 1.2170 0.1213  0.2805  0.1450  130 VAL C CG2 
10966 N N   . GLU C 131 ? 0.8432 1.4234 1.4193 0.0789  0.2684  0.1257  131 GLU C N   
10967 C CA  . GLU C 131 ? 0.8638 1.4958 1.4965 0.0752  0.2684  0.1252  131 GLU C CA  
10968 C C   . GLU C 131 ? 0.8100 1.4234 1.4549 0.0896  0.2943  0.1461  131 GLU C C   
10969 O O   . GLU C 131 ? 0.8398 1.3952 1.4597 0.0904  0.3185  0.1566  131 GLU C O   
10970 C CB  . GLU C 131 ? 0.9616 1.6205 1.6468 0.0441  0.2722  0.0962  131 GLU C CB  
10971 C CG  . GLU C 131 ? 0.9606 1.6657 1.6487 0.0304  0.2427  0.0694  131 GLU C CG  
10972 C CD  . GLU C 131 ? 1.1912 1.9646 1.8928 0.0391  0.2127  0.0720  131 GLU C CD  
10973 O OE1 . GLU C 131 ? 0.8800 1.6801 1.6186 0.0514  0.2152  0.0837  131 GLU C OE1 
10974 O OE2 . GLU C 131 ? 1.3250 2.1268 1.9993 0.0340  0.1853  0.0610  131 GLU C OE2 
10975 N N   . THR C 132 ? 0.7458 1.4111 1.4288 0.1022  0.2873  0.1497  132 THR C N   
10976 C CA  . THR C 132 ? 0.8032 1.4677 1.5048 0.1167  0.3121  0.1621  132 THR C CA  
10977 C C   . THR C 132 ? 0.8597 1.5910 1.6393 0.1005  0.3252  0.1444  132 THR C C   
10978 O O   . THR C 132 ? 0.7791 1.5098 1.5773 0.0961  0.3586  0.1480  132 THR C O   
10979 C CB  . THR C 132 ? 0.6829 1.3489 1.3631 0.1537  0.2924  0.1787  132 THR C CB  
10980 O OG1 . THR C 132 ? 0.8461 1.5684 1.5539 0.1610  0.2548  0.1709  132 THR C OG1 
10981 C CG2 . THR C 132 ? 0.7649 1.3654 1.3704 0.1668  0.2854  0.1970  132 THR C CG2 
10982 N N   . GLU C 133 ? 0.8521 1.6457 1.6763 0.0901  0.2994  0.1239  133 GLU C N   
10983 C CA  . GLU C 133 ? 0.8828 1.7522 1.7896 0.0741  0.3071  0.1016  133 GLU C CA  
10984 C C   . GLU C 133 ? 0.8839 1.7389 1.8157 0.0371  0.3509  0.0960  133 GLU C C   
10985 O O   . GLU C 133 ? 0.9473 1.7601 1.8618 0.0091  0.3564  0.0917  133 GLU C O   
10986 C CB  . GLU C 133 ? 0.8316 1.7586 1.7719 0.0626  0.2705  0.0783  133 GLU C CB  
10987 C CG  . GLU C 133 ? 1.0640 2.0851 2.0942 0.0585  0.2649  0.0536  133 GLU C CG  
10988 C CD  . GLU C 133 ? 1.2125 2.2767 2.2627 0.1011  0.2373  0.0578  133 GLU C CD  
10989 O OE1 . GLU C 133 ? 1.2402 2.2889 2.2868 0.1232  0.2582  0.0701  133 GLU C OE1 
10990 O OE2 . GLU C 133 ? 1.3868 2.4985 2.4554 0.1134  0.1923  0.0477  133 GLU C OE2 
10991 N N   . GLY C 134 ? 0.7533 1.6442 1.7256 0.0362  0.3803  0.0948  134 GLY C N   
10992 C CA  . GLY C 134 ? 0.7486 1.6316 1.7424 -0.0038 0.4249  0.0933  134 GLY C CA  
10993 C C   . GLY C 134 ? 0.9661 1.7453 1.8899 -0.0215 0.4447  0.1159  134 GLY C C   
10994 O O   . GLY C 134 ? 1.0744 1.8275 2.0082 -0.0615 0.4564  0.1103  134 GLY C O   
10995 N N   . ARG C 135 ? 0.9944 1.7114 1.8489 0.0086  0.4455  0.1402  135 ARG C N   
10996 C CA  . ARG C 135 ? 0.8541 1.4715 1.6401 -0.0007 0.4587  0.1612  135 ARG C CA  
10997 C C   . ARG C 135 ? 0.8897 1.4708 1.6280 0.0183  0.4843  0.1854  135 ARG C C   
10998 O O   . ARG C 135 ? 0.9026 1.5238 1.6484 0.0501  0.4813  0.1851  135 ARG C O   
10999 C CB  . ARG C 135 ? 0.7826 1.3553 1.5237 0.0180  0.4237  0.1605  135 ARG C CB  
11000 C CG  . ARG C 135 ? 0.8911 1.4637 1.6558 -0.0093 0.4060  0.1377  135 ARG C CG  
11001 C CD  . ARG C 135 ? 0.7915 1.3671 1.5305 0.0110  0.3689  0.1268  135 ARG C CD  
11002 N NE  . ARG C 135 ? 0.8286 1.3366 1.4982 0.0350  0.3656  0.1436  135 ARG C NE  
11003 C CZ  . ARG C 135 ? 0.8260 1.2638 1.4617 0.0286  0.3673  0.1424  135 ARG C CZ  
11004 N NH1 . ARG C 135 ? 0.8269 1.2426 1.4883 -0.0017 0.3713  0.1271  135 ARG C NH1 
11005 N NH2 . ARG C 135 ? 0.8775 1.2659 1.4568 0.0530  0.3624  0.1544  135 ARG C NH2 
11006 N N   . ASP C 136 ? 0.8759 1.3781 1.5636 0.0000  0.5065  0.2054  136 ASP C N   
11007 C CA  . ASP C 136 ? 0.8798 1.3429 1.5130 0.0154  0.5302  0.2286  136 ASP C CA  
11008 C C   . ASP C 136 ? 0.9201 1.3567 1.5081 0.0621  0.5047  0.2349  136 ASP C C   
11009 O O   . ASP C 136 ? 0.9034 1.3035 1.4691 0.0710  0.4764  0.2324  136 ASP C O   
11010 C CB  . ASP C 136 ? 0.9440 1.3135 1.5205 -0.0117 0.5479  0.2517  136 ASP C CB  
11011 C CG  . ASP C 136 ? 1.2812 1.6616 1.8744 -0.0590 0.5877  0.2594  136 ASP C CG  
11012 O OD1 . ASP C 136 ? 1.5837 2.0521 2.2284 -0.0662 0.6103  0.2462  136 ASP C OD1 
11013 O OD2 . ASP C 136 ? 1.6550 1.9558 2.2099 -0.0896 0.5954  0.2780  136 ASP C OD2 
11014 N N   . ILE C 137 ? 0.7497 1.3722 1.5715 0.0144  0.4305  0.1208  137 ILE C N   
11015 C CA  . ILE C 137 ? 0.7397 1.3441 1.5195 0.0373  0.4178  0.1251  137 ILE C CA  
11016 C C   . ILE C 137 ? 0.8446 1.4006 1.5758 0.0353  0.4229  0.1469  137 ILE C C   
11017 O O   . ILE C 137 ? 0.8075 1.3427 1.5136 0.0490  0.4086  0.1493  137 ILE C O   
11018 C CB  . ILE C 137 ? 0.7673 1.3923 1.5301 0.0547  0.4205  0.1187  137 ILE C CB  
11019 C CG1 . ILE C 137 ? 1.0743 1.7052 1.8272 0.0432  0.4455  0.1263  137 ILE C CG1 
11020 C CG2 . ILE C 137 ? 0.8693 1.5365 1.6744 0.0653  0.4052  0.0954  137 ILE C CG2 
11021 C CD1 . ILE C 137 ? 1.2761 1.9128 1.9950 0.0594  0.4501  0.1255  137 ILE C CD1 
11022 N N   . TYR C 138 ? 0.8105 1.3480 1.5288 0.0188  0.4424  0.1621  138 TYR C N   
11023 C CA  . TYR C 138 ? 0.6729 1.1644 1.3459 0.0173  0.4463  0.1825  138 TYR C CA  
11024 C C   . TYR C 138 ? 0.7567 1.2267 1.4466 0.0055  0.4365  0.1846  138 TYR C C   
11025 O O   . TYR C 138 ? 0.8387 1.2742 1.4951 0.0108  0.4303  0.1952  138 TYR C O   
11026 C CB  . TYR C 138 ? 0.6628 1.1408 1.3110 0.0071  0.4693  0.1987  138 TYR C CB  
11027 C CG  . TYR C 138 ? 0.6722 1.1657 1.2931 0.0219  0.4764  0.1971  138 TYR C CG  
11028 C CD1 . TYR C 138 ? 0.7126 1.1836 1.2816 0.0398  0.4720  0.2046  138 TYR C CD1 
11029 C CD2 . TYR C 138 ? 0.6788 1.2123 1.3292 0.0191  0.4850  0.1843  138 TYR C CD2 
11030 C CE1 . TYR C 138 ? 0.8188 1.3053 1.3649 0.0535  0.4765  0.2001  138 TYR C CE1 
11031 C CE2 . TYR C 138 ? 0.8107 1.3603 1.4387 0.0326  0.4901  0.1803  138 TYR C CE2 
11032 C CZ  . TYR C 138 ? 0.8336 1.3594 1.4094 0.0497  0.4856  0.1881  138 TYR C CZ  
11033 O OH  . TYR C 138 ? 0.9464 1.4883 1.5014 0.0626  0.4896  0.1821  138 TYR C OH  
11034 N N   . ASP C 139 ? 0.6457 1.1369 1.3882 -0.0100 0.4339  0.1725  139 ASP C N   
11035 C CA  . ASP C 139 ? 0.6916 1.1664 1.4549 -0.0214 0.4223  0.1706  139 ASP C CA  
11036 C C   . ASP C 139 ? 0.7433 1.2129 1.4893 -0.0037 0.3906  0.1564  139 ASP C C   
11037 O O   . ASP C 139 ? 0.7809 1.2166 1.5035 -0.0045 0.3751  0.1586  139 ASP C O   
11038 C CB  . ASP C 139 ? 0.6027 1.1026 1.4241 -0.0415 0.4238  0.1566  139 ASP C CB  
11039 C CG  . ASP C 139 ? 0.9288 1.4134 1.7522 -0.0625 0.4453  0.1688  139 ASP C CG  
11040 O OD1 . ASP C 139 ? 1.1273 1.5772 1.9057 -0.0622 0.4572  0.1899  139 ASP C OD1 
11041 O OD2 . ASP C 139 ? 0.9708 1.4778 1.8403 -0.0783 0.4495  0.1568  139 ASP C OD2 
11042 N N   . ILE C 140 ? 0.7550 1.2560 1.5100 0.0125  0.3809  0.1418  140 ILE C N   
11043 C CA  . ILE C 140 ? 0.5370 1.0320 1.2720 0.0307  0.3520  0.1295  140 ILE C CA  
11044 C C   . ILE C 140 ? 0.6243 1.0802 1.2973 0.0446  0.3495  0.1425  140 ILE C C   
11045 O O   . ILE C 140 ? 0.8122 1.2384 1.4589 0.0490  0.3307  0.1409  140 ILE C O   
11046 C CB  . ILE C 140 ? 0.5263 1.0639 1.2861 0.0458  0.3447  0.1126  140 ILE C CB  
11047 C CG1 . ILE C 140 ? 0.5230 1.0997 1.3461 0.0336  0.3415  0.0953  140 ILE C CG1 
11048 C CG2 . ILE C 140 ? 0.5114 1.0365 1.2396 0.0679  0.3183  0.1045  140 ILE C CG2 
11049 C CD1 . ILE C 140 ? 0.5188 1.1433 1.3758 0.0441  0.3435  0.0807  140 ILE C CD1 
11050 N N   . ALA C 141 ? 0.5608 1.0178 1.2112 0.0514  0.3689  0.1540  141 ALA C N   
11051 C CA  . ALA C 141 ? 0.6314 1.0554 1.2255 0.0653  0.3682  0.1646  141 ALA C CA  
11052 C C   . ALA C 141 ? 0.7906 1.1700 1.3567 0.0562  0.3648  0.1762  141 ALA C C   
11053 O O   . ALA C 141 ? 0.8175 1.1675 1.3441 0.0678  0.3514  0.1765  141 ALA C O   
11054 C CB  . ALA C 141 ? 0.6715 1.1074 1.2517 0.0703  0.3928  0.1754  141 ALA C CB  
11055 N N   . HIS C 142 ? 0.6170 0.9908 1.2045 0.0355  0.3771  0.1851  142 HIS C N   
11056 C CA  . HIS C 142 ? 0.6918 1.0235 1.2564 0.0264  0.3741  0.1959  142 HIS C CA  
11057 C C   . HIS C 142 ? 0.7583 1.0770 1.3305 0.0238  0.3482  0.1825  142 HIS C C   
11058 O O   . HIS C 142 ? 0.7778 1.0610 1.3159 0.0277  0.3366  0.1852  142 HIS C O   
11059 C CB  . HIS C 142 ? 0.6836 1.0123 1.2699 0.0055  0.3968  0.2105  142 HIS C CB  
11060 C CG  . HIS C 142 ? 0.7780 1.1152 1.3500 0.0079  0.4237  0.2260  142 HIS C CG  
11061 N ND1 . HIS C 142 ? 0.9158 1.2601 1.5108 -0.0098 0.4451  0.2353  142 HIS C ND1 
11062 C CD2 . HIS C 142 ? 0.7091 1.0466 1.2425 0.0260  0.4292  0.2310  142 HIS C CD2 
11063 C CE1 . HIS C 142 ? 0.8074 1.1521 1.3694 -0.0018 0.4583  0.2442  142 HIS C CE1 
11064 N NE2 . HIS C 142 ? 0.7575 1.1006 1.2847 0.0197  0.4505  0.2421  142 HIS C NE2 
11065 N N   . ASP C 143 ? 0.6976 1.0459 1.3137 0.0180  0.3387  0.1668  143 ASP C N   
11066 C CA  . ASP C 143 ? 0.5835 0.9237 1.2070 0.0165  0.3137  0.1526  143 ASP C CA  
11067 C C   . ASP C 143 ? 0.7344 1.0621 1.3192 0.0379  0.2946  0.1456  143 ASP C C   
11068 O O   . ASP C 143 ? 0.8034 1.1044 1.3686 0.0387  0.2777  0.1414  143 ASP C O   
11069 C CB  . ASP C 143 ? 0.6638 1.0437 1.3431 0.0083  0.3076  0.1358  143 ASP C CB  
11070 C CG  . ASP C 143 ? 0.8804 1.2674 1.6034 -0.0159 0.3215  0.1382  143 ASP C CG  
11071 O OD1 . ASP C 143 ? 0.9244 1.2853 1.6339 -0.0264 0.3384  0.1556  143 ASP C OD1 
11072 O OD2 . ASP C 143 ? 0.6404 1.0589 1.4117 -0.0238 0.3154  0.1223  143 ASP C OD2 
11073 N N   . VAL C 144 ? 0.7045 1.0509 1.2794 0.0548  0.2982  0.1441  144 VAL C N   
11074 C CA  . VAL C 144 ? 0.7017 1.0360 1.2416 0.0755  0.2828  0.1381  144 VAL C CA  
11075 C C   . VAL C 144 ? 0.6963 0.9887 1.1881 0.0795  0.2851  0.1490  144 VAL C C   
11076 O O   . VAL C 144 ? 0.7044 0.9711 1.1703 0.0860  0.2690  0.1439  144 VAL C O   
11077 C CB  . VAL C 144 ? 0.6363 1.0010 1.1805 0.0921  0.2883  0.1340  144 VAL C CB  
11078 C CG1 . VAL C 144 ? 0.5797 0.9254 1.0834 0.1132  0.2771  0.1310  144 VAL C CG1 
11079 C CG2 . VAL C 144 ? 0.6567 1.0624 1.2477 0.0913  0.2808  0.1197  144 VAL C CG2 
11080 N N   . ALA C 145 ? 0.6586 0.9441 1.1382 0.0757  0.3053  0.1636  145 ALA C N   
11081 C CA  . ALA C 145 ? 0.7122 0.9603 1.1475 0.0803  0.3079  0.1736  145 ALA C CA  
11082 C C   . ALA C 145 ? 0.7849 1.0002 1.2138 0.0688  0.2958  0.1733  145 ALA C C   
11083 O O   . ALA C 145 ? 0.6704 0.8553 1.0646 0.0766  0.2862  0.1718  145 ALA C O   
11084 C CB  . ALA C 145 ? 0.6953 0.9444 1.1229 0.0764  0.3318  0.1901  145 ALA C CB  
11085 N N   . LYS C 146 ? 0.7911 1.0133 1.2554 0.0501  0.2964  0.1730  146 LYS C N   
11086 C CA  . LYS C 146 ? 0.6778 0.8716 1.1412 0.0381  0.2849  0.1711  146 LYS C CA  
11087 C C   . LYS C 146 ? 0.7289 0.9167 1.1841 0.0456  0.2613  0.1549  146 LYS C C   
11088 O O   . LYS C 146 ? 0.8326 0.9884 1.2635 0.0453  0.2508  0.1528  146 LYS C O   
11089 C CB  . LYS C 146 ? 0.6630 0.8696 1.1721 0.0163  0.2912  0.1721  146 LYS C CB  
11090 C CG  . LYS C 146 ? 0.6656 0.8575 1.1738 0.0047  0.3124  0.1909  146 LYS C CG  
11091 C CD  . LYS C 146 ? 0.9657 1.1699 1.5232 -0.0176 0.3202  0.1912  146 LYS C CD  
11092 C CE  . LYS C 146 ? 0.9941 1.2392 1.5895 -0.0224 0.3370  0.1912  146 LYS C CE  
11093 N NZ  . LYS C 146 ? 1.0477 1.2889 1.6638 -0.0400 0.3610  0.2069  146 LYS C NZ  
11094 N N   . GLU C 147 ? 0.6894 0.9075 1.1641 0.0527  0.2531  0.1434  147 GLU C N   
11095 C CA  . GLU C 147 ? 0.7036 0.9169 1.1684 0.0614  0.2314  0.1293  147 GLU C CA  
11096 C C   . GLU C 147 ? 0.7129 0.9027 1.1320 0.0797  0.2276  0.1299  147 GLU C C   
11097 O O   . GLU C 147 ? 0.7047 0.8708 1.1019 0.0830  0.2133  0.1229  147 GLU C O   
11098 C CB  . GLU C 147 ? 0.7272 0.9797 1.2246 0.0661  0.2237  0.1178  147 GLU C CB  
11099 C CG  . GLU C 147 ? 0.8431 1.1174 1.3873 0.0483  0.2210  0.1108  147 GLU C CG  
11100 C CD  . GLU C 147 ? 1.1603 1.4130 1.7021 0.0383  0.2053  0.1032  147 GLU C CD  
11101 O OE1 . GLU C 147 ? 1.0327 1.2785 1.5563 0.0483  0.1870  0.0932  147 GLU C OE1 
11102 O OE2 . GLU C 147 ? 1.1836 1.4255 1.7411 0.0206  0.2119  0.1074  147 GLU C OE2 
11103 N N   . GLY C 148 ? 0.6427 0.8399 1.0489 0.0908  0.2410  0.1371  148 GLY C N   
11104 C CA  . GLY C 148 ? 0.7469 0.9244 1.1137 0.1082  0.2397  0.1366  148 GLY C CA  
11105 C C   . GLY C 148 ? 0.7568 0.8957 1.0923 0.1049  0.2406  0.1417  148 GLY C C   
11106 O O   . GLY C 148 ? 0.8039 0.9182 1.1111 0.1136  0.2312  0.1352  148 GLY C O   
11107 N N   . LEU C 149 ? 0.7037 0.8362 1.0446 0.0924  0.2522  0.1529  149 LEU C N   
11108 C CA  . LEU C 149 ? 0.6402 0.7366 0.9532 0.0898  0.2526  0.1579  149 LEU C CA  
11109 C C   . LEU C 149 ? 0.7600 0.8328 1.0707 0.0819  0.2355  0.1481  149 LEU C C   
11110 O O   . LEU C 149 ? 0.7506 0.7930 1.0324 0.0860  0.2305  0.1454  149 LEU C O   
11111 C CB  . LEU C 149 ? 0.6205 0.7141 0.9416 0.0777  0.2681  0.1733  149 LEU C CB  
11112 C CG  . LEU C 149 ? 0.6701 0.7748 0.9780 0.0867  0.2868  0.1855  149 LEU C CG  
11113 C CD1 . LEU C 149 ? 0.6088 0.7151 0.9319 0.0721  0.3031  0.2016  149 LEU C CD1 
11114 C CD2 . LEU C 149 ? 0.6562 0.7364 0.9208 0.1020  0.2862  0.1857  149 LEU C CD2 
11115 N N   . SER C 150 ? 0.6770 0.7648 1.0185 0.0708  0.2266  0.1412  150 SER C N   
11116 C CA  . SER C 150 ? 0.7301 0.7988 1.0709 0.0628  0.2105  0.1307  150 SER C CA  
11117 C C   . SER C 150 ? 0.7028 0.7546 1.0122 0.0768  0.1988  0.1203  150 SER C C   
11118 O O   . SER C 150 ? 0.8110 0.8349 1.1032 0.0734  0.1903  0.1141  150 SER C O   
11119 C CB  . SER C 150 ? 0.6542 0.7478 1.0344 0.0509  0.2027  0.1233  150 SER C CB  
11120 O OG  . SER C 150 ? 0.7865 0.9028 1.1713 0.0621  0.1939  0.1144  150 SER C OG  
11121 N N   . ASN C 151 ? 0.7334 0.8008 1.0355 0.0924  0.2001  0.1186  151 ASN C N   
11122 C CA  . ASN C 151 ? 0.7178 0.7684 0.9909 0.1064  0.1910  0.1096  151 ASN C CA  
11123 C C   . ASN C 151 ? 0.6669 0.6841 0.9068 0.1110  0.1949  0.1099  151 ASN C C   
11124 O O   . ASN C 151 ? 0.7973 0.7938 1.0140 0.1184  0.1877  0.1010  151 ASN C O   
11125 C CB  . ASN C 151 ? 0.6319 0.7050 0.9059 0.1228  0.1929  0.1087  151 ASN C CB  
11126 C CG  . ASN C 151 ? 0.7440 0.8455 1.0456 0.1216  0.1834  0.1036  151 ASN C CG  
11127 O OD1 . ASN C 151 ? 0.8593 0.9689 1.1840 0.1074  0.1773  0.1012  151 ASN C OD1 
11128 N ND2 . ASN C 151 ? 0.7251 0.8425 1.0258 0.1371  0.1814  0.1009  151 ASN C ND2 
11129 N N   . TYR C 152 ? 0.6891 0.7012 0.9266 0.1073  0.2062  0.1195  152 TYR C N   
11130 C CA  . TYR C 152 ? 0.7562 0.7392 0.9635 0.1130  0.2090  0.1188  152 TYR C CA  
11131 C C   . TYR C 152 ? 0.8109 0.7652 1.0131 0.1009  0.2006  0.1140  152 TYR C C   
11132 O O   . TYR C 152 ? 0.8616 0.7901 1.0390 0.1067  0.1971  0.1060  152 TYR C O   
11133 C CB  . TYR C 152 ? 0.5145 0.5040 0.7168 0.1172  0.2241  0.1314  152 TYR C CB  
11134 C CG  . TYR C 152 ? 0.6200 0.6313 0.8176 0.1331  0.2327  0.1326  152 TYR C CG  
11135 C CD1 . TYR C 152 ? 0.7499 0.7949 0.9729 0.1324  0.2385  0.1376  152 TYR C CD1 
11136 C CD2 . TYR C 152 ? 0.6945 0.6937 0.8648 0.1489  0.2346  0.1265  152 TYR C CD2 
11137 C CE1 . TYR C 152 ? 0.7627 0.8286 0.9833 0.1472  0.2461  0.1373  152 TYR C CE1 
11138 C CE2 . TYR C 152 ? 0.7539 0.7737 0.9220 0.1637  0.2423  0.1260  152 TYR C CE2 
11139 C CZ  . TYR C 152 ? 0.7644 0.8175 0.9573 0.1629  0.2479  0.1317  152 TYR C CZ  
11140 O OH  . TYR C 152 ? 0.7902 0.8644 0.9828 0.1777  0.2552  0.1300  152 TYR C OH  
11141 N N   . GLY C 153 ? 0.7192 0.6780 0.9463 0.0844  0.1979  0.1174  153 GLY C N   
11142 C CA  . GLY C 153 ? 0.6930 0.6256 0.9184 0.0725  0.1901  0.1121  153 GLY C CA  
11143 C C   . GLY C 153 ? 0.7643 0.7034 1.0176 0.0561  0.1805  0.1067  153 GLY C C   
11144 O O   . GLY C 153 ? 0.8551 0.7774 1.1157 0.0438  0.1775  0.1059  153 GLY C O   
11145 N N   . LYS C 154 ? 0.6605 0.6237 0.9300 0.0564  0.1747  0.1015  154 LYS C N   
11146 C CA  . LYS C 154 ? 0.6025 0.5746 0.8992 0.0417  0.1644  0.0939  154 LYS C CA  
11147 C C   . LYS C 154 ? 0.7357 0.6833 1.0143 0.0396  0.1513  0.0796  154 LYS C C   
11148 O O   . LYS C 154 ? 0.8025 0.7391 1.0536 0.0517  0.1481  0.0737  154 LYS C O   
11149 C CB  . LYS C 154 ? 0.5537 0.5618 0.8749 0.0436  0.1615  0.0919  154 LYS C CB  
11150 C CG  . LYS C 154 ? 0.5920 0.6048 0.8936 0.0590  0.1536  0.0846  154 LYS C CG  
11151 C CD  . LYS C 154 ? 0.7006 0.7491 1.0211 0.0673  0.1563  0.0877  154 LYS C CD  
11152 C CE  . LYS C 154 ? 0.7562 0.8349 1.1179 0.0555  0.1510  0.0836  154 LYS C CE  
11153 N NZ  . LYS C 154 ? 1.0166 1.0998 1.3786 0.0563  0.1333  0.0701  154 LYS C NZ  
11154 N N   . GLN C 155 ? 0.6702 0.6080 0.9645 0.0240  0.1449  0.0738  155 GLN C N   
11155 C CA  . GLN C 155 ? 0.7229 0.6380 1.0021 0.0201  0.1333  0.0591  155 GLN C CA  
11156 C C   . GLN C 155 ? 0.7432 0.6753 1.0377 0.0140  0.1203  0.0470  155 GLN C C   
11157 O O   . GLN C 155 ? 0.7807 0.6979 1.0577 0.0138  0.1111  0.0346  155 GLN C O   
11158 C CB  . GLN C 155 ? 0.6503 0.5412 0.9343 0.0080  0.1334  0.0581  155 GLN C CB  
11159 C CG  . GLN C 155 ? 0.7177 0.5908 0.9846 0.0150  0.1445  0.0697  155 GLN C CG  
11160 C CD  . GLN C 155 ? 0.6607 0.5176 0.8907 0.0309  0.1457  0.0652  155 GLN C CD  
11161 O OE1 . GLN C 155 ? 0.6880 0.5291 0.9019 0.0317  0.1378  0.0512  155 GLN C OE1 
11162 N NE2 . GLN C 155 ? 0.7578 0.6187 0.9744 0.0436  0.1564  0.0761  155 GLN C NE2 
11163 N N   . LEU C 156 ? 0.7290 0.6928 1.0561 0.0092  0.1198  0.0496  156 LEU C N   
11164 C CA  . LEU C 156 ? 0.6805 0.6655 1.0247 0.0049  0.1066  0.0374  156 LEU C CA  
11165 C C   . LEU C 156 ? 0.7325 0.7500 1.0869 0.0158  0.1074  0.0417  156 LEU C C   
11166 O O   . LEU C 156 ? 0.8997 0.9274 1.2602 0.0210  0.1195  0.0540  156 LEU C O   
11167 C CB  . LEU C 156 ? 0.4686 0.4632 0.8525 -0.0144 0.1032  0.0318  156 LEU C CB  
11168 C CG  . LEU C 156 ? 0.6053 0.5703 0.9849 -0.0261 0.1003  0.0251  156 LEU C CG  
11169 C CD1 . LEU C 156 ? 0.5691 0.5425 0.9918 -0.0443 0.1017  0.0243  156 LEU C CD1 
11170 C CD2 . LEU C 156 ? 0.7140 0.6692 1.0744 -0.0259 0.0863  0.0082  156 LEU C CD2 
11171 N N   . GLY C 157 ? 0.7172 0.7511 1.0729 0.0199  0.0942  0.0312  157 GLY C N   
11172 C CA  . GLY C 157 ? 0.7430 0.8082 1.1089 0.0317  0.0922  0.0332  157 GLY C CA  
11173 C C   . GLY C 157 ? 0.9375 0.9914 1.2659 0.0514  0.0941  0.0384  157 GLY C C   
11174 O O   . GLY C 157 ? 0.8557 0.8774 1.1505 0.0554  0.0975  0.0396  157 GLY C O   
11175 N N   . GLU C 158 ? 0.9755 1.0559 1.3115 0.0641  0.0919  0.0404  158 GLU C N   
11176 C CA  . GLU C 158 ? 0.8453 0.9170 1.1498 0.0838  0.0934  0.0451  158 GLU C CA  
11177 C C   . GLU C 158 ? 0.6994 0.7814 1.0105 0.0914  0.1084  0.0567  158 GLU C C   
11178 O O   . GLU C 158 ? 0.7661 0.8748 1.1113 0.0850  0.1145  0.0602  158 GLU C O   
11179 C CB  . GLU C 158 ? 1.0748 1.1665 1.3788 0.0955  0.0785  0.0383  158 GLU C CB  
11180 C CG  . GLU C 158 ? 1.1699 1.2522 1.4623 0.0901  0.0634  0.0265  158 GLU C CG  
11181 C CD  . GLU C 158 ? 1.6635 1.7782 1.9734 0.0953  0.0471  0.0177  158 GLU C CD  
11182 O OE1 . GLU C 158 ? 1.6800 1.8269 2.0325 0.0861  0.0449  0.0129  158 GLU C OE1 
11183 O OE2 . GLU C 158 ? 1.7839 1.8917 2.0653 0.1091  0.0366  0.0152  158 GLU C OE2 
11184 N N   . VAL C 159 ? 0.7696 0.8310 1.0487 0.1051  0.1150  0.0617  159 VAL C N   
11185 C CA  . VAL C 159 ? 0.5993 0.6693 0.8809 0.1139  0.1297  0.0716  159 VAL C CA  
11186 C C   . VAL C 159 ? 0.6626 0.7639 0.9587 0.1277  0.1266  0.0720  159 VAL C C   
11187 O O   . VAL C 159 ? 0.8717 0.9742 1.1580 0.1369  0.1137  0.0662  159 VAL C O   
11188 C CB  . VAL C 159 ? 0.5557 0.5932 0.8009 0.1231  0.1380  0.0745  159 VAL C CB  
11189 C CG1 . VAL C 159 ? 0.9327 0.9774 1.1806 0.1287  0.1539  0.0837  159 VAL C CG1 
11190 C CG2 . VAL C 159 ? 0.8180 0.8224 1.0451 0.1120  0.1363  0.0699  159 VAL C CG2 
11191 N N   . THR C 160 ? 0.6869 0.8123 1.0047 0.1294  0.1382  0.0785  160 THR C N   
11192 C CA  . THR C 160 ? 0.6028 0.7607 0.9390 0.1422  0.1369  0.0780  160 THR C CA  
11193 C C   . THR C 160 ? 0.5668 0.7122 0.8757 0.1614  0.1419  0.0813  160 THR C C   
11194 O O   . THR C 160 ? 0.7271 0.8591 1.0227 0.1626  0.1555  0.0871  160 THR C O   
11195 C CB  . THR C 160 ? 0.5444 0.7344 0.9183 0.1335  0.1491  0.0825  160 THR C CB  
11196 O OG1 . THR C 160 ? 0.7483 0.9527 1.1528 0.1164  0.1436  0.0776  160 THR C OG1 
11197 C CG2 . THR C 160 ? 0.6922 0.9159 1.0852 0.1474  0.1507  0.0815  160 THR C CG2 
11198 N N   . LEU C 161 ? 0.5956 0.7446 0.8964 0.1766  0.1306  0.0770  161 LEU C N   
11199 C CA  . LEU C 161 ? 0.5871 0.7228 0.8639 0.1958  0.1349  0.0793  161 LEU C CA  
11200 C C   . LEU C 161 ? 0.6843 0.8557 0.9859 0.2091  0.1345  0.0789  161 LEU C C   
11201 O O   . LEU C 161 ? 0.6828 0.8859 1.0157 0.2047  0.1269  0.0750  161 LEU C O   
11202 C CB  . LEU C 161 ? 0.5513 0.6562 0.7950 0.2036  0.1236  0.0759  161 LEU C CB  
11203 C CG  . LEU C 161 ? 0.6047 0.6692 0.8178 0.1956  0.1285  0.0755  161 LEU C CG  
11204 C CD1 . LEU C 161 ? 0.5767 0.6119 0.7576 0.2037  0.1194  0.0722  161 LEU C CD1 
11205 C CD2 . LEU C 161 ? 0.5495 0.6025 0.7529 0.1995  0.1449  0.0792  161 LEU C CD2 
11206 N N   . PRO C 162 ? 0.6476 0.8163 0.9389 0.2253  0.1421  0.0811  162 PRO C N   
11207 C CA  . PRO C 162 ? 0.4986 0.7017 0.8149 0.2384  0.1428  0.0798  162 PRO C CA  
11208 C C   . PRO C 162 ? 0.6597 0.8729 0.9802 0.2511  0.1242  0.0748  162 PRO C C   
11209 O O   . PRO C 162 ? 0.8650 1.0503 1.1577 0.2551  0.1138  0.0743  162 PRO C O   
11210 C CB  . PRO C 162 ? 0.5691 0.7576 0.8663 0.2529  0.1543  0.0820  162 PRO C CB  
11211 C CG  . PRO C 162 ? 0.6471 0.8007 0.9165 0.2434  0.1632  0.0848  162 PRO C CG  
11212 C CD  . PRO C 162 ? 0.7969 0.9310 1.0549 0.2316  0.1509  0.0832  162 PRO C CD  
11213 N N   . PRO C 163 ? 0.6421 0.8950 0.9964 0.2582  0.1200  0.0708  163 PRO C N   
11214 C CA  . PRO C 163 ? 0.7119 0.9769 1.0710 0.2728  0.1009  0.0655  163 PRO C CA  
11215 C C   . PRO C 163 ? 0.6909 0.9320 1.0215 0.2951  0.0979  0.0683  163 PRO C C   
11216 O O   . PRO C 163 ? 0.6886 0.9225 1.0066 0.3070  0.0816  0.0668  163 PRO C O   
11217 C CB  . PRO C 163 ? 0.5192 0.8342 0.9253 0.2747  0.1013  0.0595  163 PRO C CB  
11218 C CG  . PRO C 163 ? 0.5723 0.8999 0.9984 0.2549  0.1199  0.0622  163 PRO C CG  
11219 C CD  . PRO C 163 ? 0.6909 0.9795 1.0804 0.2526  0.1333  0.0705  163 PRO C CD  
11220 N N   . SER C 164 ? 0.6009 0.8300 0.9218 0.3007  0.1136  0.0719  164 SER C N   
11221 C CA  . SER C 164 ? 0.6402 0.8482 0.9396 0.3222  0.1123  0.0735  164 SER C CA  
11222 C C   . SER C 164 ? 0.6974 0.8573 0.9536 0.3229  0.1080  0.0772  164 SER C C   
11223 O O   . SER C 164 ? 0.7137 0.8517 0.9498 0.3403  0.1052  0.0792  164 SER C O   
11224 C CB  . SER C 164 ? 0.6666 0.8773 0.9703 0.3275  0.1302  0.0740  164 SER C CB  
11225 O OG  . SER C 164 ? 0.7971 0.9881 1.0855 0.3126  0.1443  0.0767  164 SER C OG  
11226 N N   . LEU C 165 ? 0.7133 0.8569 0.9567 0.3045  0.1084  0.0778  165 LEU C N   
11227 C CA  . LEU C 165 ? 0.6940 0.7926 0.8976 0.3031  0.1065  0.0800  165 LEU C CA  
11228 C C   . LEU C 165 ? 0.7337 0.8281 0.9249 0.3109  0.0870  0.0798  165 LEU C C   
11229 O O   . LEU C 165 ? 0.8272 0.9409 1.0320 0.3007  0.0759  0.0763  165 LEU C O   
11230 C CB  . LEU C 165 ? 0.7298 0.8154 0.9272 0.2807  0.1132  0.0792  165 LEU C CB  
11231 C CG  . LEU C 165 ? 0.7180 0.7598 0.8780 0.2753  0.1125  0.0793  165 LEU C CG  
11232 C CD1 . LEU C 165 ? 0.7379 0.7467 0.8722 0.2875  0.1230  0.0807  165 LEU C CD1 
11233 C CD2 . LEU C 165 ? 0.5763 0.6110 0.7372 0.2540  0.1185  0.0773  165 LEU C CD2 
11234 N N   . PRO C 166 ? 0.7304 0.8004 0.8962 0.3293  0.0823  0.0834  166 PRO C N   
11235 C CA  . PRO C 166 ? 0.7217 0.7876 0.8720 0.3383  0.0632  0.0843  166 PRO C CA  
11236 C C   . PRO C 166 ? 0.7533 0.8039 0.8846 0.3222  0.0565  0.0823  166 PRO C C   
11237 O O   . PRO C 166 ? 0.6954 0.7177 0.8080 0.3088  0.0674  0.0825  166 PRO C O   
11238 C CB  . PRO C 166 ? 0.7668 0.7969 0.8857 0.3580  0.0652  0.0908  166 PRO C CB  
11239 C CG  . PRO C 166 ? 0.8346 0.8672 0.9677 0.3639  0.0811  0.0907  166 PRO C CG  
11240 C CD  . PRO C 166 ? 0.7095 0.7546 0.8598 0.3435  0.0941  0.0866  166 PRO C CD  
11241 N N   . GLU C 167 ? 0.8799 0.9506 1.0169 0.3241  0.0377  0.0790  167 GLU C N   
11242 C CA  . GLU C 167 ? 0.6994 0.7600 0.8205 0.3099  0.0294  0.0753  167 GLU C CA  
11243 C C   . GLU C 167 ? 0.8127 0.8231 0.8837 0.3134  0.0324  0.0807  167 GLU C C   
11244 O O   . GLU C 167 ? 0.9187 0.9108 0.9732 0.2975  0.0339  0.0776  167 GLU C O   
11245 C CB  . GLU C 167 ? 0.7323 0.8266 0.8692 0.3154  0.0073  0.0692  167 GLU C CB  
11246 C CG  . GLU C 167 ? 1.0188 1.1136 1.1504 0.2984  -0.0017 0.0621  167 GLU C CG  
11247 C CD  . GLU C 167 ? 1.2189 1.3275 1.3799 0.2734  0.0084  0.0562  167 GLU C CD  
11248 O OE1 . GLU C 167 ? 1.0359 1.1753 1.2357 0.2699  0.0146  0.0546  167 GLU C OE1 
11249 O OE2 . GLU C 167 ? 1.1031 1.1914 1.2482 0.2575  0.0103  0.0534  167 GLU C OE2 
11250 N N   . LYS C 168 ? 0.9016 0.8892 0.9497 0.3336  0.0342  0.0884  168 LYS C N   
11251 C CA  . LYS C 168 ? 0.7230 0.6611 0.7244 0.3373  0.0397  0.0942  168 LYS C CA  
11252 C C   . LYS C 168 ? 0.8130 0.7230 0.8066 0.3216  0.0604  0.0924  168 LYS C C   
11253 O O   . LYS C 168 ? 0.9469 0.8245 0.9109 0.3121  0.0648  0.0916  168 LYS C O   
11254 C CB  . LYS C 168 ? 0.7808 0.7012 0.7649 0.3627  0.0390  0.1033  168 LYS C CB  
11255 C CG  . LYS C 168 ? 0.8484 0.7908 0.8331 0.3813  0.0168  0.1055  168 LYS C CG  
11256 C CD  . LYS C 168 ? 0.8083 0.7301 0.7757 0.4072  0.0163  0.1154  168 LYS C CD  
11257 C CE  . LYS C 168 ? 0.8484 0.7685 0.7912 0.4254  -0.0048 0.1206  168 LYS C CE  
11258 N NZ  . LYS C 168 ? 1.2642 1.1695 1.1969 0.4523  -0.0070 0.1304  168 LYS C NZ  
11259 N N   . ARG C 169 ? 0.7789 0.7029 0.7994 0.3193  0.0728  0.0908  169 ARG C N   
11260 C CA  . ARG C 169 ? 0.6758 0.5782 0.6924 0.3063  0.0911  0.0878  169 ARG C CA  
11261 C C   . ARG C 169 ? 0.7760 0.6844 0.7994 0.2831  0.0902  0.0813  169 ARG C C   
11262 O O   . ARG C 169 ? 0.9546 0.8332 0.9590 0.2718  0.0996  0.0781  169 ARG C O   
11263 C CB  . ARG C 169 ? 0.7956 0.7176 0.8402 0.3114  0.1025  0.0874  169 ARG C CB  
11264 C CG  . ARG C 169 ? 0.6902 0.5930 0.7317 0.3017  0.1210  0.0834  169 ARG C CG  
11265 C CD  . ARG C 169 ? 0.7758 0.6306 0.7827 0.3022  0.1307  0.0824  169 ARG C CD  
11266 N NE  . ARG C 169 ? 0.7631 0.5958 0.7490 0.3206  0.1287  0.0885  169 ARG C NE  
11267 C CZ  . ARG C 169 ? 0.7869 0.5831 0.7465 0.3173  0.1371  0.0869  169 ARG C CZ  
11268 N NH1 . ARG C 169 ? 0.7559 0.5355 0.7084 0.2983  0.1475  0.0782  169 ARG C NH1 
11269 N NH2 . ARG C 169 ? 0.9203 0.7002 0.8622 0.3290  0.1334  0.0927  169 ARG C NH2 
11270 N N   . LYS C 170 ? 0.8191 0.7657 0.8713 0.2760  0.0791  0.0784  170 LYS C N   
11271 C CA  . LYS C 170 ? 0.7281 0.6822 0.7912 0.2540  0.0775  0.0722  170 LYS C CA  
11272 C C   . LYS C 170 ? 0.8419 0.7709 0.8744 0.2477  0.0697  0.0691  170 LYS C C   
11273 O O   . LYS C 170 ? 0.7539 0.6634 0.7772 0.2318  0.0760  0.0643  170 LYS C O   
11274 C CB  . LYS C 170 ? 0.6558 0.6567 0.7592 0.2485  0.0676  0.0691  170 LYS C CB  
11275 C CG  . LYS C 170 ? 0.8337 0.8625 0.9688 0.2535  0.0764  0.0717  170 LYS C CG  
11276 C CD  . LYS C 170 ? 0.7247 0.7892 0.8992 0.2379  0.0762  0.0680  170 LYS C CD  
11277 C CE  . LYS C 170 ? 0.8366 0.9335 1.0329 0.2379  0.0586  0.0625  170 LYS C CE  
11278 N NZ  . LYS C 170 ? 0.9093 1.0496 1.1512 0.2342  0.0608  0.0605  170 LYS C NZ  
11279 N N   . GLU C 171 ? 0.8209 0.7505 0.8367 0.2607  0.0557  0.0714  171 GLU C N   
11280 C CA  . GLU C 171 ? 0.8528 0.7596 0.8360 0.2564  0.0481  0.0689  171 GLU C CA  
11281 C C   . GLU C 171 ? 0.8793 0.7374 0.8252 0.2556  0.0630  0.0711  171 GLU C C   
11282 O O   . GLU C 171 ? 0.9162 0.7535 0.8422 0.2428  0.0640  0.0658  171 GLU C O   
11283 C CB  . GLU C 171 ? 0.8473 0.7649 0.8172 0.2739  0.0299  0.0722  171 GLU C CB  
11284 C CG  . GLU C 171 ? 1.1601 1.1133 1.1498 0.2668  0.0114  0.0636  171 GLU C CG  
11285 C CD  . GLU C 171 ? 1.2169 1.1575 1.1927 0.2480  0.0094  0.0551  171 GLU C CD  
11286 O OE1 . GLU C 171 ? 1.1763 1.0803 1.1104 0.2493  0.0129  0.0573  171 GLU C OE1 
11287 O OE2 . GLU C 171 ? 1.2520 1.2190 1.2597 0.2317  0.0051  0.0458  171 GLU C OE2 
11288 N N   . LEU C 172 ? 0.8741 0.7146 0.8129 0.2687  0.0750  0.0775  172 LEU C N   
11289 C CA  . LEU C 172 ? 0.8079 0.6030 0.7159 0.2680  0.0907  0.0781  172 LEU C CA  
11290 C C   . LEU C 172 ? 0.7756 0.5626 0.6928 0.2478  0.1023  0.0690  172 LEU C C   
11291 O O   . LEU C 172 ? 0.8799 0.6361 0.7732 0.2381  0.1087  0.0640  172 LEU C O   
11292 C CB  . LEU C 172 ? 0.7138 0.4970 0.6203 0.2861  0.1011  0.0850  172 LEU C CB  
11293 C CG  . LEU C 172 ? 0.7859 0.5232 0.6664 0.2865  0.1196  0.0843  172 LEU C CG  
11294 C CD1 . LEU C 172 ? 1.0574 0.7593 0.8968 0.2849  0.1189  0.0862  172 LEU C CD1 
11295 C CD2 . LEU C 172 ? 0.8117 0.5414 0.6950 0.3057  0.1277  0.0905  172 LEU C CD2 
11296 N N   . TRP C 173 ? 0.7606 0.5752 0.7121 0.2418  0.1049  0.0667  173 TRP C N   
11297 C CA  . TRP C 173 ? 0.8090 0.6179 0.7705 0.2243  0.1143  0.0589  173 TRP C CA  
11298 C C   . TRP C 173 ? 0.7731 0.5824 0.7319 0.2068  0.1055  0.0519  173 TRP C C   
11299 O O   . TRP C 173 ? 0.7903 0.5744 0.7358 0.1949  0.1125  0.0446  173 TRP C O   
11300 C CB  . TRP C 173 ? 0.6312 0.4726 0.6286 0.2223  0.1173  0.0600  173 TRP C CB  
11301 C CG  . TRP C 173 ? 0.7599 0.6037 0.7637 0.2373  0.1276  0.0643  173 TRP C CG  
11302 C CD1 . TRP C 173 ? 0.7617 0.5773 0.7449 0.2498  0.1373  0.0653  173 TRP C CD1 
11303 C CD2 . TRP C 173 ? 0.8697 0.7459 0.9040 0.2405  0.1307  0.0670  173 TRP C CD2 
11304 N NE1 . TRP C 173 ? 0.7154 0.5456 0.7157 0.2611  0.1449  0.0676  173 TRP C NE1 
11305 C CE2 . TRP C 173 ? 0.7843 0.6520 0.8148 0.2557  0.1412  0.0687  173 TRP C CE2 
11306 C CE3 . TRP C 173 ? 0.6804 0.5923 0.7458 0.2316  0.1264  0.0677  173 TRP C CE3 
11307 C CZ2 . TRP C 173 ? 0.8042 0.6993 0.8595 0.2626  0.1469  0.0707  173 TRP C CZ2 
11308 C CZ3 . TRP C 173 ? 0.6546 0.5918 0.7432 0.2379  0.1333  0.0708  173 TRP C CZ3 
11309 C CH2 . TRP C 173 ? 0.7440 0.6736 0.8269 0.2535  0.1431  0.0721  173 TRP C CH2 
11310 N N   . ARG C 174 ? 0.7819 0.6208 0.7550 0.2056  0.0898  0.0525  174 ARG C N   
11311 C CA  . ARG C 174 ? 0.7757 0.6196 0.7503 0.1896  0.0799  0.0445  174 ARG C CA  
11312 C C   . ARG C 174 ? 0.8172 0.6254 0.7527 0.1871  0.0812  0.0405  174 ARG C C   
11313 O O   . ARG C 174 ? 0.8838 0.6783 0.8155 0.1710  0.0840  0.0314  174 ARG C O   
11314 C CB  . ARG C 174 ? 0.6285 0.5099 0.6223 0.1929  0.0620  0.0446  174 ARG C CB  
11315 C CG  . ARG C 174 ? 0.6597 0.5792 0.6984 0.1854  0.0600  0.0437  174 ARG C CG  
11316 C CD  . ARG C 174 ? 0.9488 0.9043 1.0087 0.1849  0.0421  0.0393  174 ARG C CD  
11317 N NE  . ARG C 174 ? 1.0511 1.0373 1.1323 0.2000  0.0372  0.0447  174 ARG C NE  
11318 C CZ  . ARG C 174 ? 1.2794 1.2954 1.3992 0.1963  0.0413  0.0456  174 ARG C CZ  
11319 N NH1 . ARG C 174 ? 0.9553 0.9732 1.0954 0.1783  0.0504  0.0433  174 ARG C NH1 
11320 N NH2 . ARG C 174 ? 1.1218 1.1656 1.2601 0.2107  0.0367  0.0490  174 ARG C NH2 
11321 N N   . LYS C 175 ? 0.8413 0.6336 0.7476 0.2032  0.0796  0.0474  175 LYS C N   
11322 C CA  . LYS C 175 ? 0.8956 0.6528 0.7618 0.2018  0.0824  0.0452  175 LYS C CA  
11323 C C   . LYS C 175 ? 0.8927 0.6128 0.7452 0.1948  0.1020  0.0407  175 LYS C C   
11324 O O   . LYS C 175 ? 1.0986 0.7952 0.9312 0.1830  0.1061  0.0326  175 LYS C O   
11325 C CB  . LYS C 175 ? 0.7991 0.5475 0.6367 0.2223  0.0765  0.0559  175 LYS C CB  
11326 C CG  . LYS C 175 ? 0.9570 0.7407 0.8035 0.2288  0.0547  0.0569  175 LYS C CG  
11327 C CD  . LYS C 175 ? 1.4683 1.2443 1.2864 0.2520  0.0469  0.0684  175 LYS C CD  
11328 C CE  . LYS C 175 ? 1.6526 1.3931 1.4213 0.2534  0.0482  0.0702  175 LYS C CE  
11329 N NZ  . LYS C 175 ? 1.4423 1.1965 1.1915 0.2689  0.0286  0.0752  175 LYS C NZ  
11330 N N   . LEU C 176 ? 0.8562 0.5727 0.7210 0.2017  0.1138  0.0441  176 LEU C N   
11331 C CA  . LEU C 176 ? 0.7337 0.4186 0.5899 0.1963  0.1318  0.0376  176 LEU C CA  
11332 C C   . LEU C 176 ? 0.8701 0.5609 0.7469 0.1773  0.1341  0.0258  176 LEU C C   
11333 O O   . LEU C 176 ? 0.9062 0.5707 0.7743 0.1698  0.1462  0.0167  176 LEU C O   
11334 C CB  . LEU C 176 ? 0.7625 0.4453 0.6268 0.2115  0.1424  0.0437  176 LEU C CB  
11335 C CG  . LEU C 176 ? 0.8314 0.4814 0.6867 0.2103  0.1614  0.0365  176 LEU C CG  
11336 C CD1 . LEU C 176 ? 0.8372 0.4492 0.6570 0.2110  0.1691  0.0361  176 LEU C CD1 
11337 C CD2 . LEU C 176 ? 0.8104 0.4763 0.6831 0.2190  0.1659  0.0404  176 LEU C CD2 
11338 N N   . GLY C 177 ? 0.8916 0.6161 0.7962 0.1700  0.1226  0.0257  177 GLY C N   
11339 C CA  . GLY C 177 ? 0.6968 0.4284 0.6226 0.1531  0.1231  0.0168  177 GLY C CA  
11340 C C   . GLY C 177 ? 0.7195 0.4585 0.6662 0.1553  0.1324  0.0182  177 GLY C C   
11341 O O   . GLY C 177 ? 0.8949 0.6266 0.8498 0.1441  0.1372  0.0102  177 GLY C O   
11342 N N   . VAL C 178 ? 0.7948 0.5489 0.7498 0.1703  0.1346  0.0278  178 VAL C N   
11343 C CA  . VAL C 178 ? 0.6948 0.4585 0.6678 0.1744  0.1438  0.0295  178 VAL C CA  
11344 C C   . VAL C 178 ? 0.7890 0.5923 0.7911 0.1777  0.1375  0.0382  178 VAL C C   
11345 O O   . VAL C 178 ? 0.6848 0.4996 0.6993 0.1852  0.1451  0.0420  178 VAL C O   
11346 C CB  . VAL C 178 ? 0.7868 0.5299 0.7450 0.1892  0.1567  0.0299  178 VAL C CB  
11347 C CG1 . VAL C 178 ? 0.8556 0.5618 0.7888 0.1828  0.1641  0.0197  178 VAL C CG1 
11348 C CG2 . VAL C 178 ? 0.6893 0.4406 0.6427 0.2062  0.1531  0.0400  178 VAL C CG2 
11349 N N   . TYR C 179 ? 0.8076 0.6325 0.8216 0.1716  0.1243  0.0400  179 TYR C N   
11350 C CA  . TYR C 179 ? 0.5897 0.4537 0.6359 0.1723  0.1194  0.0464  179 TYR C CA  
11351 C C   . TYR C 179 ? 0.6655 0.5356 0.7307 0.1615  0.1271  0.0457  179 TYR C C   
11352 O O   . TYR C 179 ? 0.7715 0.6262 0.8336 0.1476  0.1272  0.0390  179 TYR C O   
11353 C CB  . TYR C 179 ? 0.7701 0.6560 0.8281 0.1663  0.1038  0.0452  179 TYR C CB  
11354 C CG  . TYR C 179 ? 0.5767 0.5021 0.6641 0.1728  0.0979  0.0510  179 TYR C CG  
11355 C CD1 . TYR C 179 ? 0.6178 0.5696 0.7387 0.1619  0.0992  0.0518  179 TYR C CD1 
11356 C CD2 . TYR C 179 ? 0.8248 0.7607 0.9073 0.1899  0.0916  0.0554  179 TYR C CD2 
11357 C CE1 . TYR C 179 ? 0.5510 0.5400 0.7014 0.1667  0.0954  0.0557  179 TYR C CE1 
11358 C CE2 . TYR C 179 ? 1.0029 0.9768 1.1149 0.1961  0.0860  0.0586  179 TYR C CE2 
11359 C CZ  . TYR C 179 ? 0.7313 0.7325 0.8782 0.1838  0.0884  0.0581  179 TYR C CZ  
11360 O OH  . TYR C 179 ? 0.9094 0.9492 1.0880 0.1888  0.0844  0.0598  179 TYR C OH  
11361 N N   . PRO C 180 ? 0.6378 0.5297 0.7219 0.1677  0.1338  0.0523  180 PRO C N   
11362 C CA  . PRO C 180 ? 0.6349 0.5298 0.7317 0.1596  0.1425  0.0534  180 PRO C CA  
11363 C C   . PRO C 180 ? 0.7123 0.6232 0.8331 0.1425  0.1371  0.0541  180 PRO C C   
11364 O O   . PRO C 180 ? 0.7696 0.7017 0.9068 0.1390  0.1276  0.0548  180 PRO C O   
11365 C CB  . PRO C 180 ? 0.5995 0.5172 0.7089 0.1725  0.1504  0.0609  180 PRO C CB  
11366 C CG  . PRO C 180 ? 0.5676 0.5070 0.6861 0.1814  0.1415  0.0641  180 PRO C CG  
11367 C CD  . PRO C 180 ? 0.5199 0.4344 0.6132 0.1832  0.1333  0.0589  180 PRO C CD  
11368 N N   . ARG C 181 ? 0.7285 0.6283 0.8514 0.1328  0.1431  0.0532  181 ARG C N   
11369 C CA  . ARG C 181 ? 0.6394 0.5516 0.7868 0.1164  0.1400  0.0550  181 ARG C CA  
11370 C C   . ARG C 181 ? 0.6806 0.6059 0.8410 0.1179  0.1515  0.0646  181 ARG C C   
11371 O O   . ARG C 181 ? 0.7838 0.7193 0.9404 0.1317  0.1586  0.0693  181 ARG C O   
11372 C CB  . ARG C 181 ? 0.7081 0.5934 0.8459 0.1035  0.1359  0.0458  181 ARG C CB  
11373 C CG  . ARG C 181 ? 0.8343 0.7060 0.9561 0.1018  0.1261  0.0359  181 ARG C CG  
11374 C CD  . ARG C 181 ? 0.7098 0.5518 0.8178 0.0914  0.1246  0.0248  181 ARG C CD  
11375 N NE  . ARG C 181 ? 0.8652 0.6798 0.9455 0.1005  0.1323  0.0196  181 ARG C NE  
11376 C CZ  . ARG C 181 ? 0.7975 0.5858 0.8662 0.0944  0.1348  0.0095  181 ARG C CZ  
11377 N NH1 . ARG C 181 ? 0.6926 0.4767 0.7730 0.0794  0.1290  0.0036  181 ARG C NH1 
11378 N NH2 . ARG C 181 ? 0.8449 0.6117 0.8928 0.1036  0.1431  0.0041  181 ARG C NH2 
11379 N N   . ALA C 182 ? 0.6845 0.6090 0.8589 0.1048  0.1537  0.0677  182 ALA C N   
11380 C CA  . ALA C 182 ? 0.6336 0.5672 0.8143 0.1075  0.1658  0.0780  182 ALA C CA  
11381 C C   . ALA C 182 ? 0.6690 0.5856 0.8233 0.1213  0.1742  0.0768  182 ALA C C   
11382 O O   . ALA C 182 ? 0.6699 0.5600 0.8029 0.1236  0.1713  0.0669  182 ALA C O   
11383 C CB  . ALA C 182 ? 0.7783 0.7077 0.9742 0.0919  0.1672  0.0824  182 ALA C CB  
11384 N N   . VAL C 183 ? 0.6733 0.6317 0.8432 0.1547  0.1191  0.0974  183 VAL C N   
11385 C CA  . VAL C 183 ? 0.6797 0.6289 0.8230 0.1552  0.1275  0.0937  183 VAL C CA  
11386 C C   . VAL C 183 ? 0.7202 0.6669 0.8454 0.1479  0.1269  0.0918  183 VAL C C   
11387 O O   . VAL C 183 ? 0.7504 0.6849 0.8529 0.1450  0.1238  0.0864  183 VAL C O   
11388 C CB  . VAL C 183 ? 0.7157 0.6709 0.8628 0.1619  0.1406  0.0971  183 VAL C CB  
11389 C CG1 . VAL C 183 ? 0.6455 0.5878 0.7630 0.1636  0.1470  0.0919  183 VAL C CG1 
11390 C CG2 . VAL C 183 ? 0.6697 0.6295 0.8372 0.1694  0.1417  0.0999  183 VAL C CG2 
11391 N N   . ASP C 184 ? 0.7299 0.6881 0.8654 0.1448  0.1297  0.0965  184 ASP C N   
11392 C CA  . ASP C 184 ? 0.6907 0.6475 0.8103 0.1381  0.1293  0.0951  184 ASP C CA  
11393 C C   . ASP C 184 ? 0.7385 0.6897 0.8516 0.1327  0.1173  0.0914  184 ASP C C   
11394 O O   . ASP C 184 ? 0.7301 0.6750 0.8229 0.1279  0.1162  0.0880  184 ASP C O   
11395 C CB  . ASP C 184 ? 0.7572 0.7283 0.8924 0.1361  0.1336  0.1015  184 ASP C CB  
11396 C CG  . ASP C 184 ? 0.8294 0.8083 0.9721 0.1418  0.1462  0.1065  184 ASP C CG  
11397 O OD1 . ASP C 184 ? 0.8255 0.7965 0.9517 0.1466  0.1534  0.1035  184 ASP C OD1 
11398 O OD2 . ASP C 184 ? 0.7722 0.7651 0.9370 0.1419  0.1487  0.1137  184 ASP C OD2 
11399 N N   . ARG C 185 ? 0.7159 0.6695 0.8460 0.1340  0.1083  0.0921  185 ARG C N   
11400 C CA  . ARG C 185 ? 0.7071 0.6560 0.8312 0.1303  0.0965  0.0889  185 ARG C CA  
11401 C C   . ARG C 185 ? 0.6945 0.6294 0.7934 0.1298  0.0956  0.0834  185 ARG C C   
11402 O O   . ARG C 185 ? 0.7867 0.7178 0.8699 0.1249  0.0917  0.0810  185 ARG C O   
11403 C CB  . ARG C 185 ? 0.5934 0.5455 0.7392 0.1334  0.0868  0.0903  185 ARG C CB  
11404 C CG  . ARG C 185 ? 0.5787 0.5293 0.7225 0.1304  0.0745  0.0883  185 ARG C CG  
11405 C CD  . ARG C 185 ? 0.6438 0.5830 0.7731 0.1322  0.0681  0.0835  185 ARG C CD  
11406 N NE  . ARG C 185 ? 0.5816 0.5185 0.7005 0.1293  0.0590  0.0812  185 ARG C NE  
11407 C CZ  . ARG C 185 ? 0.6773 0.6131 0.7781 0.1243  0.0610  0.0799  185 ARG C CZ  
11408 N NH1 . ARG C 185 ? 0.7965 0.7304 0.8844 0.1217  0.0711  0.0797  185 ARG C NH1 
11409 N NH2 . ARG C 185 ? 0.7583 0.6948 0.8537 0.1224  0.0526  0.0787  185 ARG C NH2 
11410 N N   . GLU C 186 ? 0.7061 0.6340 0.8019 0.1346  0.0989  0.0818  186 GLU C N   
11411 C CA  . GLU C 186 ? 0.7921 0.7063 0.8658 0.1341  0.0970  0.0771  186 GLU C CA  
11412 C C   . GLU C 186 ? 0.7579 0.6663 0.8091 0.1300  0.1030  0.0752  186 GLU C C   
11413 O O   . GLU C 186 ? 0.8794 0.7789 0.9127 0.1265  0.0992  0.0724  186 GLU C O   
11414 C CB  . GLU C 186 ? 0.5771 0.4843 0.6525 0.1404  0.0987  0.0756  186 GLU C CB  
11415 C CG  . GLU C 186 ? 0.6426 0.5523 0.7369 0.1443  0.0910  0.0765  186 GLU C CG  
11416 C CD  . GLU C 186 ? 0.8318 0.7362 0.9201 0.1422  0.0799  0.0743  186 GLU C CD  
11417 O OE1 . GLU C 186 ? 0.8458 0.7454 0.9155 0.1373  0.0782  0.0726  186 GLU C OE1 
11418 O OE2 . GLU C 186 ? 0.9539 0.8590 1.0562 0.1460  0.0729  0.0746  186 GLU C OE2 
11419 N N   . ILE C 187 ? 0.7178 0.6313 0.7701 0.1307  0.1120  0.0771  187 ILE C N   
11420 C CA  . ILE C 187 ? 0.7619 0.6696 0.7929 0.1273  0.1173  0.0751  187 ILE C CA  
11421 C C   . ILE C 187 ? 0.7076 0.6181 0.7323 0.1199  0.1120  0.0751  187 ILE C C   
11422 O O   . ILE C 187 ? 0.8103 0.7124 0.8156 0.1157  0.1103  0.0724  187 ILE C O   
11423 C CB  . ILE C 187 ? 0.6255 0.5390 0.6595 0.1305  0.1282  0.0775  187 ILE C CB  
11424 C CG1 . ILE C 187 ? 0.5400 0.4511 0.5795 0.1389  0.1339  0.0776  187 ILE C CG1 
11425 C CG2 . ILE C 187 ? 0.6051 0.5118 0.6164 0.1270  0.1325  0.0751  187 ILE C CG2 
11426 C CD1 . ILE C 187 ? 0.7192 0.6394 0.7671 0.1436  0.1442  0.0815  187 ILE C CD1 
11427 N N   . ALA C 188 ? 0.6760 0.5982 0.7177 0.1184  0.1087  0.0783  188 ALA C N   
11428 C CA  . ALA C 188 ? 0.5839 0.5097 0.6212 0.1123  0.1032  0.0782  188 ALA C CA  
11429 C C   . ALA C 188 ? 0.6530 0.5719 0.6808 0.1108  0.0942  0.0756  188 ALA C C   
11430 O O   . ALA C 188 ? 0.8229 0.7387 0.8352 0.1060  0.0921  0.0742  188 ALA C O   
11431 C CB  . ALA C 188 ? 0.5954 0.5340 0.6546 0.1122  0.1000  0.0821  188 ALA C CB  
11432 N N   . ALA C 189 ? 0.6399 0.5564 0.6767 0.1151  0.0892  0.0752  189 ALA C N   
11433 C CA  . ALA C 189 ? 0.5843 0.4946 0.6127 0.1148  0.0809  0.0732  189 ALA C CA  
11434 C C   . ALA C 189 ? 0.6427 0.5420 0.6481 0.1118  0.0830  0.0710  189 ALA C C   
11435 O O   . ALA C 189 ? 0.7681 0.6653 0.7622 0.1084  0.0779  0.0706  189 ALA C O   
11436 C CB  . ALA C 189 ? 0.6836 0.5918 0.7247 0.1207  0.0766  0.0731  189 ALA C CB  
11437 N N   . VAL C 190 ? 0.7531 0.6452 0.7517 0.1134  0.0899  0.0698  190 VAL C N   
11438 C CA  . VAL C 190 ? 0.6582 0.5385 0.6359 0.1106  0.0910  0.0678  190 VAL C CA  
11439 C C   . VAL C 190 ? 0.6666 0.5484 0.6319 0.1043  0.0931  0.0679  190 VAL C C   
11440 O O   . VAL C 190 ? 0.7416 0.6184 0.6930 0.0998  0.0896  0.0676  190 VAL C O   
11441 C CB  . VAL C 190 ? 0.5647 0.4360 0.5382 0.1150  0.0969  0.0660  190 VAL C CB  
11442 C CG1 . VAL C 190 ? 0.6235 0.4818 0.5753 0.1116  0.0974  0.0639  190 VAL C CG1 
11443 C CG2 . VAL C 190 ? 0.5757 0.4443 0.5598 0.1210  0.0940  0.0657  190 VAL C CG2 
11444 N N   . MET C 191 ? 0.6719 0.5609 0.6426 0.1040  0.0988  0.0688  191 MET C N   
11445 C CA  . MET C 191 ? 0.7508 0.6416 0.7106 0.0983  0.1010  0.0688  191 MET C CA  
11446 C C   . MET C 191 ? 0.7578 0.6545 0.7168 0.0937  0.0940  0.0699  191 MET C C   
11447 O O   . MET C 191 ? 0.8660 0.7603 0.8110 0.0884  0.0931  0.0695  191 MET C O   
11448 C CB  . MET C 191 ? 0.6922 0.5912 0.6607 0.0997  0.1080  0.0703  191 MET C CB  
11449 C CG  . MET C 191 ? 0.6675 0.5605 0.6319 0.1043  0.1162  0.0693  191 MET C CG  
11450 S SD  . MET C 191 ? 0.7358 0.6145 0.6733 0.1009  0.1182  0.0658  191 MET C SD  
11451 C CE  . MET C 191 ? 0.9669 0.8323 0.8990 0.1061  0.1173  0.0633  191 MET C CE  
11452 N N   . HIS C 192 ? 0.7136 0.6179 0.6873 0.0960  0.0886  0.0712  192 HIS C N   
11453 C CA  . HIS C 192 ? 0.7742 0.6841 0.7472 0.0934  0.0815  0.0719  192 HIS C CA  
11454 C C   . HIS C 192 ? 0.7174 0.6203 0.6768 0.0920  0.0767  0.0715  192 HIS C C   
11455 O O   . HIS C 192 ? 0.7866 0.6905 0.7348 0.0875  0.0748  0.0720  192 HIS C O   
11456 C CB  . HIS C 192 ? 0.6946 0.6128 0.6870 0.0974  0.0759  0.0731  192 HIS C CB  
11457 C CG  . HIS C 192 ? 0.5966 0.5186 0.5875 0.0970  0.0670  0.0732  192 HIS C CG  
11458 N ND1 . HIS C 192 ? 0.5766 0.5003 0.5787 0.1019  0.0595  0.0732  192 HIS C ND1 
11459 C CD2 . HIS C 192 ? 0.7017 0.6260 0.6807 0.0929  0.0647  0.0732  192 HIS C CD2 
11460 C CE1 . HIS C 192 ? 0.6963 0.6230 0.6922 0.1013  0.0528  0.0731  192 HIS C CE1 
11461 N NE2 . HIS C 192 ? 0.7476 0.6753 0.7299 0.0959  0.0560  0.0733  192 HIS C NE2 
11462 N N   . SER C 193 ? 0.6877 0.5838 0.6483 0.0959  0.0749  0.0710  193 SER C N   
11463 C CA  . SER C 193 ? 0.5147 0.4042 0.4637 0.0950  0.0705  0.0714  193 SER C CA  
11464 C C   . SER C 193 ? 0.6042 0.4853 0.5361 0.0898  0.0737  0.0714  193 SER C C   
11465 O O   . SER C 193 ? 0.8456 0.7243 0.7674 0.0870  0.0700  0.0731  193 SER C O   
11466 C CB  . SER C 193 ? 0.6458 0.5300 0.6014 0.1007  0.0677  0.0709  193 SER C CB  
11467 O OG  . SER C 193 ? 0.7442 0.6360 0.7153 0.1052  0.0629  0.0711  193 SER C OG  
11468 N N   . THR C 194 ? 0.6174 0.4941 0.5461 0.0888  0.0802  0.0698  194 THR C N   
11469 C CA  . THR C 194 ? 0.6413 0.5088 0.5536 0.0840  0.0821  0.0695  194 THR C CA  
11470 C C   . THR C 194 ? 0.7206 0.5942 0.6261 0.0779  0.0822  0.0706  194 THR C C   
11471 O O   . THR C 194 ? 0.8046 0.6721 0.6971 0.0730  0.0818  0.0711  194 THR C O   
11472 C CB  . THR C 194 ? 0.7280 0.5865 0.6369 0.0864  0.0882  0.0669  194 THR C CB  
11473 O OG1 . THR C 194 ? 0.8411 0.7074 0.7594 0.0888  0.0936  0.0663  194 THR C OG1 
11474 C CG2 . THR C 194 ? 0.6934 0.5432 0.6048 0.0917  0.0873  0.0658  194 THR C CG2 
11475 N N   . HIS C 195 ? 0.6532 0.5385 0.5679 0.0782  0.0820  0.0711  195 HIS C N   
11476 C CA  . HIS C 195 ? 0.7051 0.5971 0.6145 0.0729  0.0817  0.0719  195 HIS C CA  
11477 C C   . HIS C 195 ? 0.6669 0.5591 0.5670 0.0694  0.0765  0.0743  195 HIS C C   
11478 O O   . HIS C 195 ? 0.7402 0.6314 0.6421 0.0722  0.0722  0.0756  195 HIS C O   
11479 C CB  . HIS C 195 ? 0.6478 0.5520 0.5704 0.0749  0.0805  0.0723  195 HIS C CB  
11480 C CG  . HIS C 195 ? 0.6821 0.5935 0.6001 0.0701  0.0800  0.0729  195 HIS C CG  
11481 N ND1 . HIS C 195 ? 0.7086 0.6250 0.6220 0.0683  0.0744  0.0745  195 HIS C ND1 
11482 C CD2 . HIS C 195 ? 0.8027 0.7173 0.7204 0.0676  0.0843  0.0723  195 HIS C CD2 
11483 C CE1 . HIS C 195 ? 0.6207 0.5429 0.5311 0.0645  0.0754  0.0745  195 HIS C CE1 
11484 N NE2 . HIS C 195 ? 0.7974 0.7184 0.7101 0.0637  0.0812  0.0732  195 HIS C NE2 
11485 N N   . ILE C 196 ? 0.6106 0.5050 0.5016 0.0637  0.0767  0.0752  196 ILE C N   
11486 C CA  . ILE C 196 ? 0.6325 0.5285 0.5150 0.0600  0.0724  0.0785  196 ILE C CA  
11487 C C   . ILE C 196 ? 0.6409 0.5462 0.5299 0.0642  0.0672  0.0802  196 ILE C C   
11488 O O   . ILE C 196 ? 0.8893 0.8021 0.7877 0.0674  0.0664  0.0788  196 ILE C O   
11489 C CB  . ILE C 196 ? 0.5567 0.4560 0.4308 0.0537  0.0735  0.0793  196 ILE C CB  
11490 C CG1 . ILE C 196 ? 0.6434 0.5436 0.5090 0.0495  0.0698  0.0836  196 ILE C CG1 
11491 C CG2 . ILE C 196 ? 0.7626 0.6733 0.6432 0.0544  0.0736  0.0783  196 ILE C CG2 
11492 C CD1 . ILE C 196 ? 0.4951 0.4082 0.3627 0.0507  0.0662  0.0861  196 ILE C CD1 
11493 N N   . GLY C 197 ? 0.5624 0.4665 0.4464 0.0644  0.0636  0.0835  197 GLY C N   
11494 C CA  . GLY C 197 ? 0.7282 0.6402 0.6154 0.0691  0.0584  0.0853  197 GLY C CA  
11495 C C   . GLY C 197 ? 0.7421 0.6539 0.6405 0.0764  0.0560  0.0830  197 GLY C C   
11496 O O   . GLY C 197 ? 0.8190 0.7383 0.7220 0.0809  0.0514  0.0830  197 GLY C O   
11497 N N   . CYS C 198 ? 0.7817 0.6846 0.6843 0.0781  0.0584  0.0812  198 CYS C N   
11498 C CA  . CYS C 198 ? 0.7512 0.6536 0.6654 0.0850  0.0558  0.0794  198 CYS C CA  
11499 C C   . CYS C 198 ? 0.8841 0.7780 0.7946 0.0874  0.0539  0.0808  198 CYS C C   
11500 O O   . CYS C 198 ? 0.8042 0.6997 0.7079 0.0878  0.0502  0.0840  198 CYS C O   
11501 C CB  . CYS C 198 ? 0.6707 0.5720 0.5957 0.0861  0.0601  0.0763  198 CYS C CB  
11502 S SG  . CYS C 198 ? 1.0926 1.0054 1.0266 0.0853  0.0605  0.0752  198 CYS C SG  
11503 N N   . ASN C 199 ? 0.7838 0.6690 0.6984 0.0891  0.0565  0.0788  199 ASN C N   
11504 C CA  . ASN C 199 ? 0.6723 0.5486 0.5836 0.0915  0.0544  0.0800  199 ASN C CA  
11505 C C   . ASN C 199 ? 0.8605 0.7300 0.7583 0.0856  0.0554  0.0830  199 ASN C C   
11506 O O   . ASN C 199 ? 0.9226 0.7887 0.8150 0.0804  0.0593  0.0822  199 ASN C O   
11507 C CB  . ASN C 199 ? 0.7479 0.6170 0.6675 0.0953  0.0569  0.0768  199 ASN C CB  
11508 C CG  . ASN C 199 ? 0.8595 0.7210 0.7793 0.0996  0.0534  0.0774  199 ASN C CG  
11509 O OD1 . ASN C 199 ? 0.9356 0.7875 0.8464 0.0973  0.0539  0.0786  199 ASN C OD1 
11510 N ND2 . ASN C 199 ? 0.8415 0.7065 0.7716 0.1059  0.0492  0.0765  199 ASN C ND2 
11511 N N   . ALA C 200 ? 0.9233 0.7908 0.8158 0.0865  0.0514  0.0867  200 ALA C N   
11512 C CA  . ALA C 200 ? 0.7073 0.5685 0.5888 0.0810  0.0512  0.0909  200 ALA C CA  
11513 C C   . ALA C 200 ? 0.7962 0.6496 0.6767 0.0846  0.0479  0.0929  200 ALA C C   
11514 O O   . ALA C 200 ? 0.7903 0.6448 0.6647 0.0834  0.0451  0.0984  200 ALA C O   
11515 C CB  . ALA C 200 ? 0.8599 0.7308 0.7351 0.0773  0.0499  0.0957  200 ALA C CB  
11516 N N   . ASP C 201 ? 0.8009 0.6471 0.6879 0.0892  0.0483  0.0889  201 ASP C N   
11517 C CA  . ASP C 201 ? 0.7484 0.5862 0.6354 0.0931  0.0452  0.0899  201 ASP C CA  
11518 C C   . ASP C 201 ? 0.8745 0.7006 0.7637 0.0941  0.0479  0.0855  201 ASP C C   
11519 O O   . ASP C 201 ? 0.8857 0.7141 0.7839 0.0976  0.0506  0.0810  201 ASP C O   
11520 C CB  . ASP C 201 ? 0.6967 0.5406 0.5916 0.1010  0.0413  0.0892  201 ASP C CB  
11521 C CG  . ASP C 201 ? 0.8947 0.7304 0.7894 0.1057  0.0376  0.0903  201 ASP C CG  
11522 O OD1 . ASP C 201 ? 0.9352 0.7594 0.8287 0.1048  0.0388  0.0889  201 ASP C OD1 
11523 O OD2 . ASP C 201 ? 1.0500 0.8903 0.9450 0.1106  0.0333  0.0924  201 ASP C OD2 
11524 N N   . ALA C 202 ? 0.8429 0.6567 0.7242 0.0911  0.0471  0.0870  202 ALA C N   
11525 C CA  . ALA C 202 ? 0.8189 0.6204 0.7002 0.0926  0.0492  0.0827  202 ALA C CA  
11526 C C   . ALA C 202 ? 0.8437 0.6436 0.7352 0.1008  0.0489  0.0790  202 ALA C C   
11527 O O   . ALA C 202 ? 0.9172 0.7161 0.8144 0.1038  0.0529  0.0746  202 ALA C O   
11528 C CB  . ALA C 202 ? 0.7992 0.5870 0.6702 0.0884  0.0464  0.0855  202 ALA C CB  
11529 N N   . GLU C 203 ? 0.7462 0.5465 0.6404 0.1047  0.0444  0.0812  203 GLU C N   
11530 C CA  . GLU C 203 ? 0.6987 0.4972 0.6032 0.1125  0.0432  0.0779  203 GLU C CA  
11531 C C   . GLU C 203 ? 0.8054 0.6150 0.7230 0.1162  0.0456  0.0748  203 GLU C C   
11532 O O   . GLU C 203 ? 0.8834 0.6912 0.8098 0.1204  0.0482  0.0711  203 GLU C O   
11533 C CB  . GLU C 203 ? 0.7537 0.5514 0.6578 0.1161  0.0373  0.0811  203 GLU C CB  
11534 C CG  . GLU C 203 ? 0.8548 0.6400 0.7489 0.1138  0.0346  0.0843  203 GLU C CG  
11535 C CD  . GLU C 203 ? 1.0010 0.7834 0.8958 0.1190  0.0293  0.0865  203 GLU C CD  
11536 O OE1 . GLU C 203 ? 0.9437 0.7314 0.8479 0.1257  0.0275  0.0841  203 GLU C OE1 
11537 O OE2 . GLU C 203 ? 1.0204 0.7949 0.9067 0.1165  0.0266  0.0910  203 GLU C OE2 
11538 N N   . ALA C 204 ? 0.7231 0.5445 0.6425 0.1150  0.0444  0.0765  204 ALA C N   
11539 C CA  . ALA C 204 ? 0.7255 0.5575 0.6579 0.1180  0.0454  0.0741  204 ALA C CA  
11540 C C   . ALA C 204 ? 0.7286 0.5613 0.6635 0.1155  0.0522  0.0716  204 ALA C C   
11541 O O   . ALA C 204 ? 0.6895 0.5259 0.6373 0.1195  0.0545  0.0692  204 ALA C O   
11542 C CB  . ALA C 204 ? 0.9644 0.8072 0.8956 0.1169  0.0421  0.0765  204 ALA C CB  
11543 N N   . MET C 205 ? 0.6657 0.4951 0.5889 0.1092  0.0554  0.0724  205 MET C N   
11544 C CA  . MET C 205 ? 0.5757 0.4052 0.4990 0.1073  0.0619  0.0700  205 MET C CA  
11545 C C   . MET C 205 ? 0.7340 0.5546 0.6604 0.1120  0.0652  0.0668  205 MET C C   
11546 O O   . MET C 205 ? 0.8584 0.6839 0.7943 0.1150  0.0699  0.0649  205 MET C O   
11547 C CB  . MET C 205 ? 0.7148 0.5402 0.6234 0.0999  0.0634  0.0713  205 MET C CB  
11548 C CG  . MET C 205 ? 0.7074 0.5345 0.6150 0.0980  0.0696  0.0690  205 MET C CG  
11549 S SD  . MET C 205 ? 0.8623 0.7059 0.7770 0.0957  0.0708  0.0700  205 MET C SD  
11550 C CE  . MET C 205 ? 0.6235 0.4737 0.5565 0.1026  0.0745  0.0677  205 MET C CE  
11551 N N   . ILE C 206 ? 0.8143 0.6226 0.7333 0.1128  0.0626  0.0668  206 ILE C N   
11552 C CA  . ILE C 206 ? 0.7178 0.5166 0.6382 0.1179  0.0652  0.0636  206 ILE C CA  
11553 C C   . ILE C 206 ? 0.7916 0.5968 0.7293 0.1252  0.0653  0.0623  206 ILE C C   
11554 O O   . ILE C 206 ? 0.8783 0.6828 0.8224 0.1299  0.0701  0.0599  206 ILE C O   
11555 C CB  . ILE C 206 ? 0.6002 0.3837 0.5087 0.1169  0.0611  0.0640  206 ILE C CB  
11556 C CG1 . ILE C 206 ? 0.6847 0.4613 0.5775 0.1092  0.0606  0.0656  206 ILE C CG1 
11557 C CG2 . ILE C 206 ? 0.6261 0.3995 0.5360 0.1232  0.0630  0.0603  206 ILE C CG2 
11558 C CD1 . ILE C 206 ? 0.7592 0.5306 0.6450 0.1084  0.0659  0.0622  206 ILE C CD1 
11559 N N   . LYS C 207 ? 0.7193 0.5314 0.6650 0.1267  0.0600  0.0642  207 LYS C N   
11560 C CA  . LYS C 207 ? 0.7095 0.5277 0.6727 0.1333  0.0587  0.0632  207 LYS C CA  
11561 C C   . LYS C 207 ? 0.7087 0.5391 0.6846 0.1336  0.0635  0.0630  207 LYS C C   
11562 O O   . LYS C 207 ? 0.8641 0.6983 0.8547 0.1388  0.0658  0.0622  207 LYS C O   
11563 C CB  . LYS C 207 ? 0.6242 0.4459 0.5909 0.1348  0.0509  0.0651  207 LYS C CB  
11564 C CG  . LYS C 207 ? 0.6774 0.4878 0.6357 0.1365  0.0460  0.0657  207 LYS C CG  
11565 C CD  . LYS C 207 ? 0.6463 0.4601 0.6113 0.1410  0.0387  0.0667  207 LYS C CD  
11566 C CE  . LYS C 207 ? 0.8936 0.6969 0.8498 0.1427  0.0339  0.0680  207 LYS C CE  
11567 N NZ  . LYS C 207 ? 1.1930 0.9976 1.1370 0.1393  0.0302  0.0720  207 LYS C NZ  
11568 N N   . MET C 208 ? 0.6667 0.5035 0.6376 0.1281  0.0652  0.0642  208 MET C N   
11569 C CA  . MET C 208 ? 0.7088 0.5570 0.6908 0.1278  0.0696  0.0646  208 MET C CA  
11570 C C   . MET C 208 ? 0.7431 0.5888 0.7252 0.1297  0.0780  0.0631  208 MET C C   
11571 O O   . MET C 208 ? 0.8702 0.7246 0.8671 0.1328  0.0820  0.0637  208 MET C O   
11572 C CB  . MET C 208 ? 0.7146 0.5690 0.6890 0.1214  0.0691  0.0660  208 MET C CB  
11573 C CG  . MET C 208 ? 0.7095 0.5693 0.6859 0.1210  0.0614  0.0676  208 MET C CG  
11574 S SD  . MET C 208 ? 0.8393 0.7088 0.8103 0.1149  0.0609  0.0692  208 MET C SD  
11575 C CE  . MET C 208 ? 0.6314 0.5128 0.6234 0.1174  0.0627  0.0691  208 MET C CE  
11576 N N   . SER C 209 ? 0.6077 0.4415 0.5734 0.1282  0.0802  0.0615  209 SER C N   
11577 C CA  . SER C 209 ? 0.6691 0.4982 0.6316 0.1313  0.0877  0.0595  209 SER C CA  
11578 C C   . SER C 209 ? 0.7484 0.5762 0.7231 0.1394  0.0888  0.0585  209 SER C C   
11579 O O   . SER C 209 ? 0.8309 0.6635 0.8136 0.1439  0.0956  0.0584  209 SER C O   
11580 C CB  . SER C 209 ? 0.6728 0.4878 0.6144 0.1282  0.0879  0.0576  209 SER C CB  
11581 O OG  . SER C 209 ? 0.9193 0.7343 0.8503 0.1204  0.0843  0.0592  209 SER C OG  
11582 N N   . MET C 210 ? 0.6352 0.4572 0.6112 0.1413  0.0824  0.0582  210 MET C N   
11583 C CA  . MET C 210 ? 0.6290 0.4489 0.6162 0.1489  0.0825  0.0571  210 MET C CA  
11584 C C   . MET C 210 ? 0.7075 0.5422 0.7177 0.1525  0.0844  0.0592  210 MET C C   
11585 O O   . MET C 210 ? 0.7383 0.5764 0.7587 0.1582  0.0901  0.0592  210 MET C O   
11586 C CB  . MET C 210 ? 0.7810 0.5928 0.7658 0.1498  0.0743  0.0568  210 MET C CB  
11587 C CG  . MET C 210 ? 0.6383 0.4348 0.6031 0.1470  0.0721  0.0555  210 MET C CG  
11588 S SD  . MET C 210 ? 0.8840 0.6718 0.8479 0.1491  0.0631  0.0559  210 MET C SD  
11589 C CE  . MET C 210 ? 0.9635 0.7417 0.9065 0.1412  0.0597  0.0575  210 MET C CE  
11590 N N   . ARG C 211 ? 0.6841 0.5279 0.7026 0.1492  0.0794  0.0613  211 ARG C N   
11591 C CA  . ARG C 211 ? 0.7104 0.5679 0.7516 0.1516  0.0792  0.0638  211 ARG C CA  
11592 C C   . ARG C 211 ? 0.7252 0.5914 0.7724 0.1518  0.0886  0.0654  211 ARG C C   
11593 O O   . ARG C 211 ? 0.7142 0.5889 0.7800 0.1564  0.0920  0.0675  211 ARG C O   
11594 C CB  . ARG C 211 ? 0.6810 0.5448 0.7250 0.1474  0.0717  0.0652  211 ARG C CB  
11595 C CG  . ARG C 211 ? 0.6658 0.5413 0.7336 0.1501  0.0682  0.0674  211 ARG C CG  
11596 C CD  . ARG C 211 ? 0.7796 0.6587 0.8471 0.1471  0.0594  0.0679  211 ARG C CD  
11597 N NE  . ARG C 211 ? 0.8391 0.7255 0.9287 0.1509  0.0527  0.0693  211 ARG C NE  
11598 C CZ  . ARG C 211 ? 0.7825 0.6716 0.8750 0.1505  0.0434  0.0694  211 ARG C CZ  
11599 N NH1 . ARG C 211 ? 0.8361 0.7226 0.9109 0.1468  0.0405  0.0685  211 ARG C NH1 
11600 N NH2 . ARG C 211 ? 0.9444 0.8389 1.0577 0.1543  0.0365  0.0705  211 ARG C NH2 
11601 N N   . CYS C 212 ? 0.7731 0.6374 0.8045 0.1468  0.0927  0.0649  212 CYS C N   
11602 C CA  . CYS C 212 ? 0.6353 0.5067 0.6685 0.1467  0.1016  0.0663  212 CYS C CA  
11603 C C   . CYS C 212 ? 0.6546 0.5218 0.6869 0.1537  0.1094  0.0653  212 CYS C C   
11604 O O   . CYS C 212 ? 0.7130 0.5903 0.7599 0.1579  0.1159  0.0681  212 CYS C O   
11605 C CB  . CYS C 212 ? 0.6483 0.5164 0.6626 0.1399  0.1029  0.0654  212 CYS C CB  
11606 S SG  . CYS C 212 ? 0.7594 0.6331 0.7705 0.1402  0.1140  0.0665  212 CYS C SG  
11607 N N   . SER C 213 ? 0.8019 0.6543 0.8171 0.1553  0.1086  0.0616  213 SER C N   
11608 C CA  . SER C 213 ? 0.7189 0.5651 0.7300 0.1627  0.1151  0.0598  213 SER C CA  
11609 C C   . SER C 213 ? 0.6485 0.5025 0.6817 0.1703  0.1166  0.0618  213 SER C C   
11610 O O   . SER C 213 ? 0.7788 0.6360 0.8161 0.1770  0.1247  0.0625  213 SER C O   
11611 C CB  . SER C 213 ? 0.7179 0.5457 0.7084 0.1626  0.1111  0.0555  213 SER C CB  
11612 O OG  . SER C 213 ? 0.7039 0.5272 0.7001 0.1639  0.1037  0.0549  213 SER C OG  
11613 N N   . LEU C 214 ? 0.6706 0.5282 0.7183 0.1697  0.1090  0.0630  214 LEU C N   
11614 C CA  . LEU C 214 ? 0.6663 0.5314 0.7365 0.1765  0.1094  0.0651  214 LEU C CA  
11615 C C   . LEU C 214 ? 0.6483 0.5302 0.7378 0.1783  0.1167  0.0702  214 LEU C C   
11616 O O   . LEU C 214 ? 0.7965 0.6840 0.8988 0.1856  0.1225  0.0722  214 LEU C O   
11617 C CB  . LEU C 214 ? 0.5614 0.4266 0.6428 0.1753  0.0986  0.0653  214 LEU C CB  
11618 C CG  . LEU C 214 ? 0.6483 0.4978 0.7135 0.1749  0.0916  0.0613  214 LEU C CG  
11619 C CD1 . LEU C 214 ? 0.6891 0.5401 0.7655 0.1744  0.0814  0.0620  214 LEU C CD1 
11620 C CD2 . LEU C 214 ? 0.6693 0.5091 0.7293 0.1820  0.0951  0.0587  214 LEU C CD2 
11621 N N   . THR C 215 ? 0.6540 0.5443 0.7458 0.1721  0.1166  0.0727  215 THR C N   
11622 C CA  . THR C 215 ? 0.6899 0.5964 0.8001 0.1731  0.1234  0.0782  215 THR C CA  
11623 C C   . THR C 215 ? 0.7602 0.6675 0.8624 0.1783  0.1357  0.0789  215 THR C C   
11624 O O   . THR C 215 ? 0.8349 0.7560 0.9525 0.1805  0.1428  0.0842  215 THR C O   
11625 C CB  . THR C 215 ? 0.7111 0.6246 0.8222 0.1652  0.1207  0.0803  215 THR C CB  
11626 O OG1 . THR C 215 ? 0.6944 0.6000 0.7806 0.1610  0.1239  0.0772  215 THR C OG1 
11627 C CG2 . THR C 215 ? 0.6434 0.5569 0.7618 0.1611  0.1086  0.0798  215 THR C CG2 
11628 N N   . ASP C 216 ? 0.8167 0.7094 0.8949 0.1804  0.1378  0.0737  216 ASP C N   
11629 C CA  . ASP C 216 ? 0.6613 0.5522 0.7285 0.1865  0.1484  0.0732  216 ASP C CA  
11630 C C   . ASP C 216 ? 0.7794 0.6699 0.8557 0.1966  0.1517  0.0733  216 ASP C C   
11631 O O   . ASP C 216 ? 0.8308 0.7349 0.9250 0.2025  0.1592  0.0784  216 ASP C O   
11632 C CB  . ASP C 216 ? 0.6574 0.5314 0.6936 0.1836  0.1476  0.0674  216 ASP C CB  
11633 C CG  . ASP C 216 ? 0.8400 0.7092 0.8610 0.1907  0.1572  0.0657  216 ASP C CG  
11634 O OD1 . ASP C 216 ? 0.8102 0.6893 0.8439 0.1990  0.1655  0.0692  216 ASP C OD1 
11635 O OD2 . ASP C 216 ? 0.8505 0.7062 0.8470 0.1883  0.1562  0.0613  216 ASP C OD2 
11636 N N   . GLY C 217 ? 0.7102 0.5862 0.7756 0.1985  0.1459  0.0682  217 GLY C N   
11637 C CA  . GLY C 217 ? 0.7118 0.5853 0.7833 0.2081  0.1481  0.0673  217 GLY C CA  
11638 C C   . GLY C 217 ? 0.7642 0.6533 0.8669 0.2121  0.1486  0.0729  217 GLY C C   
11639 O O   . GLY C 217 ? 0.8184 0.7155 0.9316 0.2209  0.1570  0.0759  217 GLY C O   
11640 N N   . TRP C 218 ? 0.6892 0.5826 0.8070 0.2063  0.1394  0.0745  218 TRP C N   
11641 C CA  . TRP C 218 ? 0.6867 0.5934 0.8351 0.2095  0.1377  0.0796  218 TRP C CA  
11642 C C   . TRP C 218 ? 0.6975 0.6236 0.8687 0.2072  0.1417  0.0872  218 TRP C C   
11643 O O   . TRP C 218 ? 0.7312 0.6694 0.9300 0.2100  0.1406  0.0924  218 TRP C O   
11644 C CB  . TRP C 218 ? 0.6749 0.5750 0.8284 0.2060  0.1246  0.0771  218 TRP C CB  
11645 C CG  . TRP C 218 ? 0.5840 0.4665 0.7196 0.2091  0.1205  0.0709  218 TRP C CG  
11646 C CD1 . TRP C 218 ? 0.6553 0.5219 0.7656 0.2043  0.1154  0.0657  218 TRP C CD1 
11647 C CD2 . TRP C 218 ? 0.7234 0.6026 0.8655 0.2178  0.1214  0.0698  218 TRP C CD2 
11648 N NE1 . TRP C 218 ? 0.6765 0.5296 0.7772 0.2093  0.1127  0.0614  218 TRP C NE1 
11649 C CE2 . TRP C 218 ? 0.8247 0.6849 0.9440 0.2178  0.1163  0.0635  218 TRP C CE2 
11650 C CE3 . TRP C 218 ? 0.7601 0.6509 0.9257 0.2257  0.1260  0.0739  218 TRP C CE3 
11651 C CZ2 . TRP C 218 ? 0.8154 0.6672 0.9339 0.2254  0.1154  0.0606  218 TRP C CZ2 
11652 C CZ3 . TRP C 218 ? 0.7634 0.6464 0.9283 0.2336  0.1254  0.0710  218 TRP C CZ3 
11653 C CH2 . TRP C 218 ? 0.7504 0.6138 0.8916 0.2334  0.1200  0.0642  218 TRP C CH2 
11654 N N   . MET C 219 ? 0.6601 0.5892 0.8211 0.2020  0.1459  0.0883  219 MET C N   
11655 C CA  . MET C 219 ? 0.6497 0.5967 0.8318 0.1993  0.1495  0.0959  219 MET C CA  
11656 C C   . MET C 219 ? 0.7720 0.7251 0.9454 0.2019  0.1624  0.0987  219 MET C C   
11657 O O   . MET C 219 ? 0.8540 0.8202 1.0441 0.2085  0.1713  0.1049  219 MET C O   
11658 C CB  . MET C 219 ? 0.8081 0.7557 0.9916 0.1893  0.1397  0.0957  219 MET C CB  
11659 C CG  . MET C 219 ? 0.8007 0.7446 0.9950 0.1875  0.1270  0.0939  219 MET C CG  
11660 S SD  . MET C 219 ? 0.7547 0.7020 0.9535 0.1777  0.1163  0.0948  219 MET C SD  
11661 C CE  . MET C 219 ? 0.9148 0.8515 1.1143 0.1781  0.1025  0.0902  219 MET C CE  
11662 N N   . GLY C 220 ? 0.9089 0.8528 1.0568 0.1972  0.1635  0.0945  220 GLY C N   
11663 C CA  . GLY C 220 ? 0.8154 0.7633 0.9522 0.1996  0.1748  0.0965  220 GLY C CA  
11664 C C   . GLY C 220 ? 0.7752 0.7211 0.9049 0.2110  0.1850  0.0960  220 GLY C C   
11665 O O   . GLY C 220 ? 0.8299 0.7894 0.9709 0.2169  0.1954  0.1024  220 GLY C O   
11666 N N   . SER C 221 ? 0.7385 0.6679 0.8502 0.2148  0.1818  0.0889  221 SER C N   
11667 C CA  . SER C 221 ? 0.6819 0.6070 0.7835 0.2267  0.1906  0.0873  221 SER C CA  
11668 C C   . SER C 221 ? 0.7694 0.7084 0.8990 0.2346  0.1943  0.0931  221 SER C C   
11669 O O   . SER C 221 ? 0.9241 0.8738 1.0596 0.2435  0.2058  0.0980  221 SER C O   
11670 C CB  . SER C 221 ? 0.7801 0.6829 0.8552 0.2278  0.1849  0.0781  221 SER C CB  
11671 O OG  . SER C 221 ? 0.8227 0.7137 0.8741 0.2200  0.1812  0.0736  221 SER C OG  
11672 N N   . PHE C 222 ? 0.7134 0.6521 0.8593 0.2319  0.1848  0.0929  222 PHE C N   
11673 C CA  . PHE C 222 ? 0.8068 0.7584 0.9812 0.2390  0.1869  0.0984  222 PHE C CA  
11674 C C   . PHE C 222 ? 0.9030 0.8773 1.1017 0.2409  0.1964  0.1089  222 PHE C C   
11675 O O   . PHE C 222 ? 0.9291 0.9122 1.1334 0.2513  0.2075  0.1130  222 PHE C O   
11676 C CB  . PHE C 222 ? 0.6990 0.6491 0.8901 0.2332  0.1738  0.0977  222 PHE C CB  
11677 C CG  . PHE C 222 ? 0.7168 0.6625 0.9157 0.2407  0.1709  0.0957  222 PHE C CG  
11678 C CD1 . PHE C 222 ? 0.7595 0.7213 0.9884 0.2471  0.1747  0.1028  222 PHE C CD1 
11679 C CD2 . PHE C 222 ? 0.7618 0.6875 0.9388 0.2412  0.1643  0.0871  222 PHE C CD2 
11680 C CE1 . PHE C 222 ? 0.7687 0.7263 1.0048 0.2541  0.1719  0.1008  222 PHE C CE1 
11681 C CE2 . PHE C 222 ? 0.6526 0.5738 0.8365 0.2482  0.1614  0.0852  222 PHE C CE2 
11682 C CZ  . PHE C 222 ? 0.7060 0.6431 0.9191 0.2547  0.1652  0.0917  222 PHE C CZ  
11683 N N   . MET C 223 ? 0.7456 0.7293 0.9583 0.2315  0.1922  0.1134  223 MET C N   
11684 C CA  . MET C 223 ? 0.8121 0.8178 1.0505 0.2320  0.2000  0.1245  223 MET C CA  
11685 C C   . MET C 223 ? 0.8230 0.8322 1.0455 0.2389  0.2145  0.1264  223 MET C C   
11686 O O   . MET C 223 ? 0.8355 0.8622 1.0772 0.2455  0.2247  0.1355  223 MET C O   
11687 C CB  . MET C 223 ? 0.7638 0.7745 1.0115 0.2202  0.1923  0.1271  223 MET C CB  
11688 C CG  . MET C 223 ? 0.7832 0.7954 1.0535 0.2149  0.1788  0.1277  223 MET C CG  
11689 S SD  . MET C 223 ? 1.0159 1.0376 1.3022 0.2032  0.1710  0.1327  223 MET C SD  
11690 C CE  . MET C 223 ? 0.8412 0.8421 1.0915 0.1952  0.1626  0.1215  223 MET C CE  
11691 N N   . GLY C 224 ? 0.7500 0.7431 0.9388 0.2375  0.2150  0.1185  224 GLY C N   
11692 C CA  . GLY C 224 ? 0.7069 0.7007 0.8774 0.2450  0.2278  0.1192  224 GLY C CA  
11693 C C   . GLY C 224 ? 0.8028 0.7984 0.9732 0.2593  0.2368  0.1200  224 GLY C C   
11694 O O   . GLY C 224 ? 0.9218 0.9312 1.0984 0.2677  0.2495  0.1270  224 GLY C O   
11695 N N   . THR C 225 ? 0.7618 0.7442 0.9259 0.2626  0.2304  0.1132  225 THR C N   
11696 C CA  . THR C 225 ? 0.7220 0.7045 0.8853 0.2766  0.2375  0.1129  225 THR C CA  
11697 C C   . THR C 225 ? 0.7671 0.7724 0.9687 0.2811  0.2421  0.1236  225 THR C C   
11698 O O   . THR C 225 ? 0.9881 1.0063 1.1964 0.2921  0.2547  0.1299  225 THR C O   
11699 C CB  . THR C 225 ? 0.6518 0.6124 0.7973 0.2777  0.2279  0.1024  225 THR C CB  
11700 O OG1 . THR C 225 ? 0.7925 0.7328 0.9022 0.2759  0.2257  0.0934  225 THR C OG1 
11701 C CG2 . THR C 225 ? 0.7691 0.7307 0.9189 0.2914  0.2331  0.1023  225 THR C CG2 
11702 N N   . GLU C 226 ? 0.6792 0.6896 0.9059 0.2732  0.2318  0.1261  226 GLU C N   
11703 C CA  . GLU C 226 ? 0.7744 0.8055 1.0395 0.2765  0.2341  0.1363  226 GLU C CA  
11704 C C   . GLU C 226 ? 0.7881 0.8426 1.0734 0.2780  0.2457  0.1488  226 GLU C C   
11705 O O   . GLU C 226 ? 0.8383 0.9093 1.1435 0.2876  0.2554  0.1572  226 GLU C O   
11706 C CB  . GLU C 226 ? 0.8281 0.8588 1.1147 0.2664  0.2193  0.1362  226 GLU C CB  
11707 C CG  . GLU C 226 ? 0.9897 1.0031 1.2669 0.2681  0.2096  0.1272  226 GLU C CG  
11708 C CD  . GLU C 226 ? 1.1083 1.1215 1.4066 0.2600  0.1951  0.1273  226 GLU C CD  
11709 O OE1 . GLU C 226 ? 1.1944 1.2095 1.4979 0.2495  0.1882  0.1286  226 GLU C OE1 
11710 O OE2 . GLU C 226 ? 1.0191 1.0296 1.3281 0.2646  0.1903  0.1257  226 GLU C OE2 
11711 N N   . PHE C 227 ? 0.7825 0.8391 1.0633 0.2688  0.2450  0.1506  227 PHE C N   
11712 C CA  . PHE C 227 ? 0.7574 0.8355 1.0567 0.2694  0.2555  0.1628  227 PHE C CA  
11713 C C   . PHE C 227 ? 0.7993 0.8802 1.0790 0.2818  0.2717  0.1643  227 PHE C C   
11714 O O   . PHE C 227 ? 0.7179 0.8197 1.0174 0.2880  0.2834  0.1760  227 PHE C O   
11715 C CB  . PHE C 227 ? 0.6948 0.7732 0.9940 0.2560  0.2492  0.1638  227 PHE C CB  
11716 C CG  . PHE C 227 ? 0.6210 0.7006 0.9435 0.2446  0.2341  0.1646  227 PHE C CG  
11717 C CD1 . PHE C 227 ? 0.7116 0.7943 1.0579 0.2463  0.2270  0.1660  227 PHE C CD1 
11718 C CD2 . PHE C 227 ? 0.7346 0.8114 1.0537 0.2329  0.2265  0.1635  227 PHE C CD2 
11719 C CE1 . PHE C 227 ? 0.6193 0.7019 0.9853 0.2368  0.2124  0.1663  227 PHE C CE1 
11720 C CE2 . PHE C 227 ? 0.7822 0.8592 1.1209 0.2237  0.2122  0.1638  227 PHE C CE2 
11721 C CZ  . PHE C 227 ? 0.7452 0.8249 1.1069 0.2258  0.2051  0.1652  227 PHE C CZ  
11722 N N   . SER C 228 ? 0.7982 0.8584 1.0397 0.2858  0.2722  0.1529  228 SER C N   
11723 C CA  . SER C 228 ? 0.7298 0.7898 0.9494 0.2988  0.2863  0.1530  228 SER C CA  
11724 C C   . SER C 228 ? 0.8511 0.9217 1.0850 0.3134  0.2948  0.1577  228 SER C C   
11725 O O   . SER C 228 ? 0.8597 0.9448 1.0965 0.3244  0.3091  0.1655  228 SER C O   
11726 C CB  . SER C 228 ? 0.6899 0.7231 0.8666 0.2997  0.2823  0.1391  228 SER C CB  
11727 O OG  . SER C 228 ? 0.8612 0.8864 1.0244 0.2874  0.2762  0.1356  228 SER C OG  
11728 N N   . ASP C 229 ? 0.7874 0.8515 1.0304 0.3139  0.2862  0.1534  229 ASP C N   
11729 C CA  . ASP C 229 ? 0.7285 0.8025 0.9866 0.3272  0.2931  0.1576  229 ASP C CA  
11730 C C   . ASP C 229 ? 0.8178 0.9215 1.1195 0.3275  0.2994  0.1736  229 ASP C C   
11731 O O   . ASP C 229 ? 0.8159 0.9345 1.1289 0.3398  0.3108  0.1810  229 ASP C O   
11732 C CB  . ASP C 229 ? 0.8139 0.8726 1.0713 0.3264  0.2808  0.1488  229 ASP C CB  
11733 C CG  . ASP C 229 ? 0.9146 0.9448 1.1309 0.3286  0.2755  0.1341  229 ASP C CG  
11734 O OD1 . ASP C 229 ? 0.9406 0.9618 1.1279 0.3308  0.2806  0.1300  229 ASP C OD1 
11735 O OD2 . ASP C 229 ? 0.7965 0.8131 1.0100 0.3281  0.2657  0.1268  229 ASP C OD2 
11736 N N   . ILE C 230 ? 0.8626 0.9747 1.1884 0.3137  0.2913  0.1791  230 ILE C N   
11737 C CA  . ILE C 230 ? 0.6886 0.8281 1.0575 0.3127  0.2957  0.1948  230 ILE C CA  
11738 C C   . ILE C 230 ? 0.7846 0.9409 1.1522 0.3185  0.3117  0.2049  230 ILE C C   
11739 O O   . ILE C 230 ? 0.7668 0.9398 1.1492 0.3232  0.3188  0.2145  230 ILE C O   
11740 C CB  . ILE C 230 ? 0.5931 0.7349 0.9858 0.2963  0.2812  0.1972  230 ILE C CB  
11741 C CG1 . ILE C 230 ? 0.6572 0.7880 1.0596 0.2927  0.2663  0.1905  230 ILE C CG1 
11742 C CG2 . ILE C 230 ? 0.6717 0.8413 1.1052 0.2939  0.2864  0.2143  230 ILE C CG2 
11743 C CD1 . ILE C 230 ? 0.6711 0.7955 1.0835 0.2774  0.2497  0.1878  230 ILE C CD1 
11744 N N   . MET C 231 ? 0.8339 0.9824 1.1776 0.3140  0.3137  0.2015  231 MET C N   
11745 C CA  . MET C 231 ? 0.7494 0.9115 1.0886 0.3177  0.3272  0.2105  231 MET C CA  
11746 C C   . MET C 231 ? 0.8032 0.9594 1.1100 0.3312  0.3382  0.2067  231 MET C C   
11747 O O   . MET C 231 ? 0.9436 1.1150 1.2535 0.3351  0.3482  0.2166  231 MET C O   
11748 C CB  . MET C 231 ? 0.6224 0.7774 0.9471 0.3072  0.3240  0.2077  231 MET C CB  
11749 C CG  . MET C 231 ? 0.7518 0.9117 1.1039 0.2911  0.3108  0.2114  231 MET C CG  
11750 S SD  . MET C 231 ? 0.8122 0.9646 1.1461 0.2780  0.3066  0.2087  231 MET C SD  
11751 C CE  . MET C 231 ? 0.7314 0.8510 1.0185 0.2765  0.2980  0.1890  231 MET C CE  
11752 N N   . PHE C 232 ? 0.8459 0.9796 1.1210 0.3384  0.3359  0.1928  232 PHE C N   
11753 C CA  . PHE C 232 ? 0.8059 0.9313 1.0476 0.3516  0.3447  0.1879  232 PHE C CA  
11754 C C   . PHE C 232 ? 0.8563 0.9775 1.0954 0.3622  0.3442  0.1838  232 PHE C C   
11755 O O   . PHE C 232 ? 0.8608 0.9766 1.0744 0.3740  0.3511  0.1805  232 PHE C O   
11756 C CB  . PHE C 232 ? 0.8216 0.9224 1.0224 0.3528  0.3432  0.1749  232 PHE C CB  
11757 C CG  . PHE C 232 ? 0.6915 0.7925 0.8920 0.3410  0.3411  0.1764  232 PHE C CG  
11758 C CD1 . PHE C 232 ? 0.7185 0.8399 0.9349 0.3376  0.3488  0.1890  232 PHE C CD1 
11759 C CD2 . PHE C 232 ? 0.8855 0.9640 1.0657 0.3286  0.3270  0.1644  232 PHE C CD2 
11760 C CE1 . PHE C 232 ? 0.9403 1.0615 1.1560 0.3263  0.3461  0.1900  232 PHE C CE1 
11761 C CE2 . PHE C 232 ? 0.8463 0.9241 1.0241 0.3155  0.3227  0.1651  232 PHE C CE2 
11762 C CZ  . PHE C 232 ? 0.8304 0.9291 1.0257 0.3145  0.3320  0.1776  232 PHE C CZ  
11763 N N   . GLY C 233 ? 0.8537 0.9768 1.1181 0.3583  0.3356  0.1837  233 GLY C N   
11764 C CA  . GLY C 233 ? 0.7114 0.8308 0.9759 0.3673  0.3341  0.1799  233 GLY C CA  
11765 C C   . GLY C 233 ? 0.8844 0.9771 1.1277 0.3687  0.3240  0.1647  233 GLY C C   
11766 O O   . GLY C 233 ? 0.8633 0.9359 1.0745 0.3692  0.3225  0.1548  233 GLY C O   
11767 N N   . THR C 234 ? 0.9207 1.0125 1.1815 0.3690  0.3165  0.1630  234 THR C N   
11768 C CA  . THR C 234 ? 0.7134 0.7799 0.9557 0.3702  0.3063  0.1495  234 THR C CA  
11769 C C   . THR C 234 ? 0.8428 0.8933 1.0486 0.3836  0.3106  0.1403  234 THR C C   
11770 O O   . THR C 234 ? 0.9221 0.9840 1.1317 0.3929  0.3175  0.1445  234 THR C O   
11771 C CB  . THR C 234 ? 0.8441 0.9152 1.1156 0.3674  0.2974  0.1510  234 THR C CB  
11772 O OG1 . THR C 234 ? 1.0255 1.1128 1.3322 0.3556  0.2930  0.1604  234 THR C OG1 
11773 C CG2 . THR C 234 ? 0.8007 0.8452 1.0539 0.3662  0.2849  0.1376  234 THR C CG2 
11774 N N   . PRO C 235 ? 0.8274 0.8515 0.9976 0.3850  0.3062  0.1279  235 PRO C N   
11775 C CA  . PRO C 235 ? 0.8823 0.8904 1.0176 0.3980  0.3090  0.1190  235 PRO C CA  
11776 C C   . PRO C 235 ? 0.9400 0.9430 1.0775 0.4060  0.3049  0.1147  235 PRO C C   
11777 O O   . PRO C 235 ? 0.9305 0.9323 1.0880 0.4007  0.2963  0.1140  235 PRO C O   
11778 C CB  . PRO C 235 ? 0.7858 0.7653 0.8865 0.3937  0.3012  0.1067  235 PRO C CB  
11779 C CG  . PRO C 235 ? 0.9491 0.9332 1.0617 0.3757  0.2952  0.1101  235 PRO C CG  
11780 C CD  . PRO C 235 ? 0.8985 0.9051 1.0544 0.3697  0.2943  0.1205  235 PRO C CD  
11781 N N   A HIS C 236 ? 0.9419 0.9415 1.0579 0.4191  0.3107  0.1116  236 HIS C N   
11782 N N   B HIS C 236 ? 0.9595 0.9590 1.0756 0.4191  0.3107  0.1116  236 HIS C N   
11783 C CA  A HIS C 236 ? 0.9820 0.9762 1.0960 0.4285  0.3078  0.1069  236 HIS C CA  
11784 C CA  B HIS C 236 ? 0.9563 0.9505 1.0707 0.4284  0.3077  0.1069  236 HIS C CA  
11785 C C   A HIS C 236 ? 0.9663 0.9385 1.0376 0.4405  0.3082  0.0960  236 HIS C C   
11786 C C   B HIS C 236 ? 0.9775 0.9504 1.0495 0.4406  0.3084  0.0962  236 HIS C C   
11787 O O   A HIS C 236 ? 0.9617 0.9301 1.0106 0.4429  0.3135  0.0951  236 HIS C O   
11788 O O   B HIS C 236 ? 0.9739 0.9436 1.0238 0.4432  0.3140  0.0957  236 HIS C O   
11789 C CB  A HIS C 236 ? 0.9826 1.0055 1.1266 0.4334  0.3164  0.1190  236 HIS C CB  
11790 C CB  B HIS C 236 ? 0.9761 0.9992 1.1223 0.4326  0.3157  0.1191  236 HIS C CB  
11791 C CG  A HIS C 236 ? 0.8455 0.8831 0.9812 0.4412  0.3296  0.1264  236 HIS C CG  
11792 C CG  B HIS C 236 ? 0.9596 1.0015 1.1481 0.4208  0.3126  0.1289  236 HIS C CG  
11793 N ND1 A HIS C 236 ? 0.8745 0.9053 0.9833 0.4557  0.3345  0.1217  236 HIS C ND1 
11794 N ND1 B HIS C 236 ? 0.8954 0.9264 1.0954 0.4127  0.3002  0.1239  236 HIS C ND1 
11795 C CD2 A HIS C 236 ? 0.9061 0.9640 1.0569 0.4362  0.3381  0.1381  236 HIS C CD2 
11796 C CD2 B HIS C 236 ? 0.9422 1.0116 1.1625 0.4162  0.3195  0.1431  236 HIS C CD2 
11797 C CE1 A HIS C 236 ? 0.8813 0.9284 0.9891 0.4595  0.3460  0.1308  236 HIS C CE1 
11798 C CE1 B HIS C 236 ? 0.8109 0.8627 1.0488 0.4036  0.2995  0.1347  236 HIS C CE1 
11799 N NE2 A HIS C 236 ? 0.8840 0.9478 1.0167 0.4478  0.3486  0.1410  236 HIS C NE2 
11800 N NE2 B HIS C 236 ? 0.9040 0.9792 1.1558 0.4050  0.3107  0.1465  236 HIS C NE2 
11801 N N   . SER C 237 ? 0.9253 0.8826 0.9854 0.4480  0.3018  0.0874  237 SER C N   
11802 C CA  . SER C 237 ? 1.0024 0.9370 1.0223 0.4596  0.3001  0.0763  237 SER C CA  
11803 C C   . SER C 237 ? 1.0355 0.9799 1.0393 0.4697  0.3119  0.0805  237 SER C C   
11804 O O   . SER C 237 ? 1.1150 1.0827 1.1364 0.4761  0.3215  0.0900  237 SER C O   
11805 C CB  . SER C 237 ? 0.9219 0.8470 0.9396 0.4676  0.2939  0.0699  237 SER C CB  
11806 O OG  . SER C 237 ? 1.3652 1.3159 1.4161 0.4702  0.2995  0.0796  237 SER C OG  
11807 N N   . ILE C 238 ? 1.0046 0.9316 0.9763 0.4703  0.3110  0.0741  238 ILE C N   
11808 C CA  . ILE C 238 ? 1.0215 0.9554 0.9751 0.4790  0.3211  0.0775  238 ILE C CA  
11809 C C   . ILE C 238 ? 1.0233 0.9268 0.9316 0.4860  0.3149  0.0643  238 ILE C C   
11810 O O   . ILE C 238 ? 1.0974 0.9764 0.9905 0.4797  0.3037  0.0544  238 ILE C O   
11811 C CB  . ILE C 238 ? 0.9363 0.8890 0.9073 0.4687  0.3285  0.0882  238 ILE C CB  
11812 C CG1 . ILE C 238 ? 0.9961 0.9615 0.9549 0.4774  0.3404  0.0949  238 ILE C CG1 
11813 C CG2 . ILE C 238 ? 0.9421 0.8758 0.9007 0.4570  0.3203  0.0814  238 ILE C CG2 
11814 C CD1 . ILE C 238 ? 0.9319 0.9267 0.9213 0.4695  0.3504  0.1103  238 ILE C CD1 
11815 N N   . ASP C 239 ? 1.0502 0.9554 0.9377 0.4990  0.3217  0.0646  239 ASP C N   
11816 C CA  . ASP C 239 ? 1.1346 1.0103 0.9782 0.5070  0.3149  0.0519  239 ASP C CA  
11817 C C   . ASP C 239 ? 1.1144 0.9878 0.9402 0.5042  0.3187  0.0532  239 ASP C C   
11818 O O   . ASP C 239 ? 1.2343 1.1326 1.0791 0.5015  0.3298  0.0652  239 ASP C O   
11819 C CB  . ASP C 239 ? 1.0726 0.9461 0.8986 0.5244  0.3174  0.0492  239 ASP C CB  
11820 C CG  . ASP C 239 ? 1.2903 1.1664 1.1330 0.5281  0.3139  0.0479  239 ASP C CG  
11821 O OD1 . ASP C 239 ? 1.5231 1.4262 1.3999 0.5264  0.3219  0.0590  239 ASP C OD1 
11822 O OD2 . ASP C 239 ? 1.3682 1.2191 1.1901 0.5321  0.3027  0.0360  239 ASP C OD2 
11823 N N   . THR C 240 ? 1.0668 0.9105 0.8570 0.5055  0.3092  0.0411  240 THR C N   
11824 C CA  . THR C 240 ? 1.1149 0.9526 0.8846 0.5031  0.3112  0.0406  240 THR C CA  
11825 C C   . THR C 240 ? 1.2210 1.0235 0.9487 0.5081  0.2991  0.0260  240 THR C C   
11826 O O   . THR C 240 ? 1.4023 1.1857 1.1203 0.5114  0.2888  0.0170  240 THR C O   
11827 C CB  . THR C 240 ? 1.2224 1.0671 1.0121 0.4862  0.3112  0.0451  240 THR C CB  
11828 O OG1 . THR C 240 ? 1.2242 1.0762 1.0040 0.4861  0.3185  0.0499  240 THR C OG1 
11829 C CG2 . THR C 240 ? 1.3036 1.1204 1.0803 0.4767  0.2971  0.0340  240 THR C CG2 
11830 N N   . GLU C 241 ? 1.1319 0.9258 0.8362 0.5085  0.2996  0.0241  241 GLU C N   
11831 C CA  . GLU C 241 ? 1.1932 0.9537 0.8580 0.5125  0.2875  0.0109  241 GLU C CA  
11832 C C   . GLU C 241 ? 1.2122 0.9601 0.8731 0.4978  0.2812  0.0077  241 GLU C C   
11833 O O   . GLU C 241 ? 1.1792 0.9463 0.8594 0.4888  0.2894  0.0165  241 GLU C O   
11834 C CB  . GLU C 241 ? 1.2502 1.0091 0.8877 0.5273  0.2922  0.0106  241 GLU C CB  
11835 C CG  . GLU C 241 ? 1.4670 1.2214 1.0925 0.5435  0.2910  0.0070  241 GLU C CG  
11836 C CD  . GLU C 241 ? 1.6076 1.3724 1.2180 0.5594  0.3005  0.0117  241 GLU C CD  
11837 O OE1 . GLU C 241 ? 1.5923 1.3695 1.2022 0.5581  0.3089  0.0187  241 GLU C OE1 
11838 O OE2 . GLU C 241 ? 1.5695 1.3299 1.1682 0.5734  0.2994  0.0084  241 GLU C OE2 
11839 N N   . ALA C 242 ? 1.1892 0.9050 0.8260 0.4950  0.2663  -0.0046 242 ALA C N   
11840 C CA  . ALA C 242 ? 1.1628 0.8632 0.7938 0.4812  0.2587  -0.0087 242 ALA C CA  
11841 C C   . ALA C 242 ? 1.2508 0.9218 0.8423 0.4849  0.2485  -0.0190 242 ALA C C   
11842 O O   . ALA C 242 ? 1.3293 0.9878 0.8974 0.4980  0.2445  -0.0248 242 ALA C O   
11843 C CB  . ALA C 242 ? 1.1534 0.8419 0.7972 0.4714  0.2486  -0.0127 242 ALA C CB  
11844 N N   . ASN C 243 ? 1.2336 0.8945 0.8184 0.4736  0.2442  -0.0211 243 ASN C N   
11845 C CA  . ASN C 243 ? 1.2561 0.8876 0.8046 0.4751  0.2328  -0.0310 243 ASN C CA  
11846 C C   . ASN C 243 ? 1.2446 0.8866 0.7807 0.4811  0.2418  -0.0269 243 ASN C C   
11847 O O   . ASN C 243 ? 1.2414 0.9104 0.7920 0.4882  0.2558  -0.0174 243 ASN C O   
11848 C CB  . ASN C 243 ? 1.3963 0.9995 0.9193 0.4844  0.2189  -0.0421 243 ASN C CB  
11849 C CG  . ASN C 243 ? 1.4168 0.9853 0.9147 0.4772  0.2016  -0.0527 243 ASN C CG  
11850 O OD1 . ASN C 243 ? 1.1934 0.7580 0.6865 0.4683  0.2008  -0.0526 243 ASN C OD1 
11851 N ND2 . ASN C 243 ? 1.6313 1.1744 1.1140 0.4807  0.1872  -0.0618 243 ASN C ND2 
11852 N N   . LEU C 244 ? 1.2935 0.9144 0.8039 0.4781  0.2335  -0.0334 244 LEU C N   
11853 C CA  . LEU C 244 ? 1.3193 0.9466 0.8153 0.4830  0.2401  -0.0304 244 LEU C CA  
11854 C C   . LEU C 244 ? 1.2383 0.8693 0.7178 0.5014  0.2447  -0.0298 244 LEU C C   
11855 O O   . LEU C 244 ? 1.3025 0.9458 0.7762 0.5064  0.2534  -0.0242 244 LEU C O   
11856 C CB  . LEU C 244 ? 1.2003 0.8006 0.6711 0.4758  0.2277  -0.0389 244 LEU C CB  
11857 C CG  . LEU C 244 ? 1.3525 0.9533 0.8394 0.4575  0.2259  -0.0375 244 LEU C CG  
11858 C CD1 . LEU C 244 ? 1.4283 0.9962 0.8895 0.4507  0.2098  -0.0478 244 LEU C CD1 
11859 C CD2 . LEU C 244 ? 1.2714 0.9014 0.7782 0.4516  0.2409  -0.0264 244 LEU C CD2 
11860 N N   . GLY C 245 ? 1.2403 0.8617 0.7129 0.5115  0.2393  -0.0347 245 GLY C N   
11861 C CA  . GLY C 245 ? 1.4150 1.0407 0.8727 0.5297  0.2440  -0.0338 245 GLY C CA  
11862 C C   . GLY C 245 ? 1.4032 1.0661 0.8870 0.5345  0.2629  -0.0199 245 GLY C C   
11863 O O   . GLY C 245 ? 1.5052 1.1762 0.9792 0.5496  0.2695  -0.0167 245 GLY C O   
11864 N N   . VAL C 246 ? 1.2946 0.9799 0.8116 0.5216  0.2715  -0.0111 246 VAL C N   
11865 C CA  . VAL C 246 ? 1.3608 1.0827 0.9075 0.5242  0.2888  0.0033  246 VAL C CA  
11866 C C   . VAL C 246 ? 1.3758 1.1116 0.9170 0.5268  0.2988  0.0110  246 VAL C C   
11867 O O   . VAL C 246 ? 1.4560 1.2172 1.0109 0.5346  0.3119  0.0220  246 VAL C O   
11868 C CB  . VAL C 246 ? 1.1628 0.9035 0.7481 0.5096  0.2932  0.0102  246 VAL C CB  
11869 C CG1 . VAL C 246 ? 1.2615 0.9908 0.8542 0.5082  0.2845  0.0038  246 VAL C CG1 
11870 C CG2 . VAL C 246 ? 1.2702 1.0080 0.8603 0.4935  0.2909  0.0104  246 VAL C CG2 
11871 N N   . LEU C 247 ? 1.3803 1.1003 0.9028 0.5204  0.2925  0.0060  247 LEU C N   
11872 C CA  . LEU C 247 ? 1.3519 1.0831 0.8673 0.5230  0.3009  0.0128  247 LEU C CA  
11873 C C   . LEU C 247 ? 1.4690 1.1979 0.9604 0.5427  0.3038  0.0128  247 LEU C C   
11874 O O   . LEU C 247 ? 1.5465 1.2520 1.0127 0.5527  0.2934  0.0025  247 LEU C O   
11875 C CB  . LEU C 247 ? 1.3106 1.0208 0.8063 0.5136  0.2915  0.0055  247 LEU C CB  
11876 C CG  . LEU C 247 ? 1.2898 1.0006 0.8053 0.4943  0.2883  0.0053  247 LEU C CG  
11877 C CD1 . LEU C 247 ? 1.3118 0.9926 0.8010 0.4874  0.2745  -0.0058 247 LEU C CD1 
11878 C CD2 . LEU C 247 ? 1.2326 0.9746 0.7777 0.4852  0.3020  0.0189  247 LEU C CD2 
11879 N N   . GLU C 248 ? 1.4107 1.1637 0.9104 0.5480  0.3174  0.0248  248 GLU C N   
11880 C CA  . GLU C 248 ? 1.3871 1.1409 0.8652 0.5675  0.3219  0.0266  248 GLU C CA  
11881 C C   . GLU C 248 ? 1.4143 1.1610 0.8693 0.5699  0.3218  0.0266  248 GLU C C   
11882 O O   . GLU C 248 ? 1.5277 1.2917 1.0000 0.5597  0.3295  0.0354  248 GLU C O   
11883 C CB  . GLU C 248 ? 1.3909 1.1788 0.8969 0.5734  0.3382  0.0415  248 GLU C CB  
11884 C CG  . GLU C 248 ? 1.5266 1.3283 1.0656 0.5659  0.3404  0.0446  248 GLU C CG  
11885 C CD  . GLU C 248 ? 1.7689 1.5577 1.2973 0.5772  0.3340  0.0367  248 GLU C CD  
11886 O OE1 . GLU C 248 ? 1.7832 1.5483 1.2767 0.5895  0.3257  0.0270  248 GLU C OE1 
11887 O OE2 . GLU C 248 ? 1.8866 1.6886 1.4418 0.5737  0.3370  0.0402  248 GLU C OE2 
11888 N N   . LYS C 249 ? 1.5219 1.2442 0.9398 0.5832  0.3129  0.0173  249 LYS C N   
11889 C CA  . LYS C 249 ? 1.4996 1.2124 0.8929 0.5869  0.3112  0.0163  249 LYS C CA  
11890 C C   . LYS C 249 ? 1.4892 1.2295 0.8916 0.5941  0.3273  0.0309  249 LYS C C   
11891 O O   . LYS C 249 ? 1.4824 1.2271 0.8848 0.5874  0.3301  0.0349  249 LYS C O   
11892 C CB  . LYS C 249 ? 1.5628 1.2431 0.9146 0.6012  0.2973  0.0033  249 LYS C CB  
11893 C CG  . LYS C 249 ? 1.4305 1.0988 0.7541 0.6072  0.2944  0.0015  249 LYS C CG  
11894 C CD  . LYS C 249 ? 1.6209 1.2502 0.9081 0.6109  0.2747  -0.0145 249 LYS C CD  
11895 C CE  . LYS C 249 ? 1.7592 1.3760 1.0125 0.6276  0.2720  -0.0165 249 LYS C CE  
11896 N NZ  . LYS C 249 ? 1.7100 1.2893 0.9309 0.6277  0.2520  -0.0313 249 LYS C NZ  
11897 N N   . ASN C 250 ? 1.5089 1.2673 0.9192 0.6075  0.3376  0.0390  250 ASN C N   
11898 C CA  . ASN C 250 ? 1.4909 1.2752 0.9096 0.6154  0.3528  0.0535  250 ASN C CA  
11899 C C   . ASN C 250 ? 1.6200 1.4389 1.0823 0.6031  0.3667  0.0689  250 ASN C C   
11900 O O   . ASN C 250 ? 1.4831 1.3245 0.9552 0.6087  0.3793  0.0820  250 ASN C O   
11901 C CB  . ASN C 250 ? 1.5663 1.3520 0.9685 0.6376  0.3569  0.0552  250 ASN C CB  
11902 C CG  . ASN C 250 ? 1.7605 1.5133 1.1183 0.6512  0.3437  0.0417  250 ASN C CG  
11903 O OD1 . ASN C 250 ? 1.8806 1.6192 1.2168 0.6510  0.3384  0.0379  250 ASN C OD1 
11904 N ND2 . ASN C 250 ? 1.6907 1.4301 1.0338 0.6632  0.3373  0.0340  250 ASN C ND2 
11905 N N   . SER C 251 ? 1.5522 1.3736 1.0390 0.5867  0.3634  0.0669  251 SER C N   
11906 C CA  . SER C 251 ? 1.4543 1.3069 0.9835 0.5735  0.3746  0.0808  251 SER C CA  
11907 C C   . SER C 251 ? 1.3717 1.2212 0.9095 0.5547  0.3705  0.0793  251 SER C C   
11908 O O   . SER C 251 ? 1.4742 1.2964 0.9886 0.5503  0.3578  0.0662  251 SER C O   
11909 C CB  . SER C 251 ? 1.2728 1.1346 0.8278 0.5695  0.3752  0.0815  251 SER C CB  
11910 O OG  . SER C 251 ? 1.4911 1.3583 1.0411 0.5865  0.3799  0.0839  251 SER C OG  
11911 N N   . VAL C 252 ? 1.2146 1.0911 0.7850 0.5439  0.3805  0.0926  252 VAL C N   
11912 C CA  . VAL C 252 ? 1.2719 1.1471 0.8538 0.5248  0.3766  0.0916  252 VAL C CA  
11913 C C   . VAL C 252 ? 1.3189 1.1877 0.9169 0.5128  0.3692  0.0849  252 VAL C C   
11914 O O   . VAL C 252 ? 1.3722 1.2593 0.9986 0.5115  0.3748  0.0918  252 VAL C O   
11915 C CB  . VAL C 252 ? 1.1577 1.0632 0.7701 0.5167  0.3886  0.1080  252 VAL C CB  
11916 C CG1 . VAL C 252 ? 1.2050 1.1092 0.8285 0.4977  0.3843  0.1068  252 VAL C CG1 
11917 C CG2 . VAL C 252 ? 1.3627 1.2758 0.9607 0.5295  0.3966  0.1158  252 VAL C CG2 
11918 N N   . ASN C 253 ? 1.2758 1.1196 0.8566 0.5044  0.3570  0.0724  253 ASN C N   
11919 C CA  . ASN C 253 ? 1.1893 1.0259 0.7841 0.4929  0.3497  0.0661  253 ASN C CA  
11920 C C   . ASN C 253 ? 1.3135 1.1620 0.9332 0.4742  0.3511  0.0713  253 ASN C C   
11921 O O   . ASN C 253 ? 1.3893 1.2284 0.9959 0.4674  0.3475  0.0682  253 ASN C O   
11922 C CB  . ASN C 253 ? 1.2481 1.0492 0.8101 0.4953  0.3346  0.0493  253 ASN C CB  
11923 C CG  . ASN C 253 ? 1.3553 1.1430 0.8924 0.5136  0.3316  0.0434  253 ASN C CG  
11924 O OD1 . ASN C 253 ? 1.3171 1.1133 0.8666 0.5202  0.3347  0.0456  253 ASN C OD1 
11925 N ND2 . ASN C 253 ? 1.3006 1.0671 0.8024 0.5225  0.3251  0.0359  253 ASN C ND2 
11926 N N   . VAL C 254 ? 1.3450 1.2142 1.0009 0.4662  0.3562  0.0792  254 VAL C N   
11927 C CA  . VAL C 254 ? 1.1330 1.0153 0.8161 0.4487  0.3574  0.0848  254 VAL C CA  
11928 C C   . VAL C 254 ? 1.1762 1.0477 0.8688 0.4407  0.3490  0.0771  254 VAL C C   
11929 O O   . VAL C 254 ? 1.3233 1.2057 1.0369 0.4429  0.3514  0.0806  254 VAL C O   
11930 C CB  . VAL C 254 ? 1.0505 0.9675 0.7702 0.4462  0.3700  0.1019  254 VAL C CB  
11931 C CG1 . VAL C 254 ? 1.0864 1.0167 0.8351 0.4282  0.3703  0.1077  254 VAL C CG1 
11932 C CG2 . VAL C 254 ? 1.0591 0.9861 0.7684 0.4556  0.3784  0.1099  254 VAL C CG2 
11933 N N   . VAL C 255 ? 1.1707 1.0202 0.8473 0.4319  0.3389  0.0668  255 VAL C N   
11934 C CA  . VAL C 255 ? 1.1704 1.0067 0.8532 0.4242  0.3300  0.0591  255 VAL C CA  
11935 C C   . VAL C 255 ? 1.2138 1.0668 0.9285 0.4080  0.3323  0.0660  255 VAL C C   
11936 O O   . VAL C 255 ? 1.2201 1.0746 0.9331 0.3988  0.3326  0.0676  255 VAL C O   
11937 C CB  . VAL C 255 ? 1.0835 0.8845 0.7302 0.4242  0.3167  0.0438  255 VAL C CB  
11938 C CG1 . VAL C 255 ? 1.0304 0.8170 0.6834 0.4160  0.3072  0.0365  255 VAL C CG1 
11939 C CG2 . VAL C 255 ? 1.0538 0.8374 0.6689 0.4405  0.3130  0.0368  255 VAL C CG2 
11940 N N   . LEU C 256 ? 1.0504 0.9154 0.7940 0.4045  0.3334  0.0699  256 LEU C N   
11941 C CA  . LEU C 256 ? 0.9741 0.8547 0.7496 0.3900  0.3346  0.0764  256 LEU C CA  
11942 C C   . LEU C 256 ? 0.9290 0.7887 0.7003 0.3760  0.3175  0.0664  256 LEU C C   
11943 O O   . LEU C 256 ? 1.1373 0.9846 0.9044 0.3804  0.3112  0.0601  256 LEU C O   
11944 C CB  . LEU C 256 ? 0.9866 0.8946 0.8002 0.3908  0.3419  0.0881  256 LEU C CB  
11945 C CG  . LEU C 256 ? 1.0846 1.0152 0.9075 0.3990  0.3531  0.0998  256 LEU C CG  
11946 C CD1 . LEU C 256 ? 0.9558 0.9097 0.8149 0.4001  0.3583  0.1098  256 LEU C CD1 
11947 C CD2 . LEU C 256 ? 1.2127 1.1568 1.0409 0.3917  0.3586  0.1080  256 LEU C CD2 
11948 N N   . HIS C 257 ? 1.0422 0.8979 0.8143 0.3588  0.3092  0.0651  257 HIS C N   
11949 C CA  . HIS C 257 ? 1.0018 0.8391 0.7705 0.3438  0.2926  0.0568  257 HIS C CA  
11950 C C   . HIS C 257 ? 1.0740 0.9296 0.8749 0.3257  0.2901  0.0644  257 HIS C C   
11951 O O   . HIS C 257 ? 1.0346 0.9115 0.8525 0.3242  0.2996  0.0741  257 HIS C O   
11952 C CB  . HIS C 257 ? 1.0229 0.8330 0.7550 0.3430  0.2837  0.0462  257 HIS C CB  
11953 C CG  . HIS C 257 ? 1.0484 0.8383 0.7742 0.3290  0.2667  0.0378  257 HIS C CG  
11954 N ND1 . HIS C 257 ? 1.0074 0.7810 0.7140 0.3194  0.2575  0.0321  257 HIS C ND1 
11955 C CD2 . HIS C 257 ? 1.1041 0.8880 0.8405 0.3239  0.2579  0.0350  257 HIS C CD2 
11956 C CE1 . HIS C 257 ? 0.9382 0.6976 0.6451 0.3085  0.2438  0.0266  257 HIS C CE1 
11957 N NE2 . HIS C 257 ? 1.2046 0.9692 0.9286 0.3109  0.2435  0.0280  257 HIS C NE2 
11958 N N   . GLY C 258 ? 0.9392 0.7869 0.7488 0.3130  0.2775  0.0604  258 GLY C N   
11959 C CA  . GLY C 258 ? 0.9939 0.8567 0.8324 0.2967  0.2735  0.0665  258 GLY C CA  
11960 C C   . GLY C 258 ? 0.9830 0.8527 0.8467 0.2938  0.2695  0.0686  258 GLY C C   
11961 O O   . GLY C 258 ? 1.0300 0.8856 0.8843 0.2997  0.2646  0.0622  258 GLY C O   
11962 N N   . HIS C 259 ? 1.0333 0.9241 0.9291 0.2848  0.2708  0.0773  259 HIS C N   
11963 C CA  . HIS C 259 ? 0.9741 0.8722 0.8958 0.2813  0.2662  0.0797  259 HIS C CA  
11964 C C   . HIS C 259 ? 1.0135 0.9396 0.9708 0.2828  0.2750  0.0919  259 HIS C C   
11965 O O   . HIS C 259 ? 0.9003 0.8331 0.8767 0.2864  0.2749  0.0943  259 HIS C O   
11966 C CB  . HIS C 259 ? 0.8992 0.7889 0.8243 0.2645  0.2519  0.0757  259 HIS C CB  
11967 C CG  . HIS C 259 ? 0.9828 0.8465 0.8824 0.2631  0.2412  0.0648  259 HIS C CG  
11968 N ND1 . HIS C 259 ? 0.8575 0.7032 0.7262 0.2639  0.2389  0.0581  259 HIS C ND1 
11969 C CD2 . HIS C 259 ? 1.2061 1.0593 1.1079 0.2608  0.2319  0.0603  259 HIS C CD2 
11970 C CE1 . HIS C 259 ? 1.2548 1.0800 1.1088 0.2619  0.2282  0.0500  259 HIS C CE1 
11971 N NE2 . HIS C 259 ? 1.2813 1.1103 1.1541 0.2600  0.2240  0.0512  259 HIS C NE2 
11972 N N   . GLU C 260 ? 1.1284 1.0701 1.0952 0.2794  0.2818  0.0996  260 GLU C N   
11973 C CA  . GLU C 260 ? 1.1039 1.0726 1.1073 0.2790  0.2889  0.1123  260 GLU C CA  
11974 C C   . GLU C 260 ? 1.0169 0.9968 1.0266 0.2961  0.3019  0.1178  260 GLU C C   
11975 O O   . GLU C 260 ? 1.1724 1.1492 1.1605 0.3076  0.3114  0.1171  260 GLU C O   
11976 C CB  . GLU C 260 ? 1.2079 1.1893 1.2179 0.2719  0.2931  0.1193  260 GLU C CB  
11977 C CG  . GLU C 260 ? 1.0451 1.0217 1.0588 0.2546  0.2807  0.1164  260 GLU C CG  
11978 C CD  . GLU C 260 ? 1.3485 1.3425 1.3795 0.2469  0.2839  0.1255  260 GLU C CD  
11979 O OE1 . GLU C 260 ? 1.8329 1.8469 1.8840 0.2530  0.2946  0.1363  260 GLU C OE1 
11980 O OE2 . GLU C 260 ? 1.1973 1.1850 1.2220 0.2349  0.2756  0.1222  260 GLU C OE2 
11981 N N   . PRO C 261 ? 0.8083 0.8009 0.8461 0.2988  0.3026  0.1232  261 PRO C N   
11982 C CA  . PRO C 261 ? 0.9291 0.9336 0.9746 0.3153  0.3149  0.1290  261 PRO C CA  
11983 C C   . PRO C 261 ? 0.9490 0.9805 1.0169 0.3206  0.3292  0.1435  261 PRO C C   
11984 O O   . PRO C 261 ? 1.1608 1.2006 1.2266 0.3363  0.3415  0.1478  261 PRO C O   
11985 C CB  . PRO C 261 ? 0.8798 0.8864 0.9480 0.3139  0.3079  0.1288  261 PRO C CB  
11986 C CG  . PRO C 261 ? 0.7709 0.7809 0.8591 0.2965  0.2967  0.1304  261 PRO C CG  
11987 C CD  . PRO C 261 ? 0.8678 0.8638 0.9312 0.2869  0.2913  0.1240  261 PRO C CD  
11988 N N   . LEU C 262 ? 0.8976 0.9435 0.9874 0.3084  0.3279  0.1516  262 LEU C N   
11989 C CA  . LEU C 262 ? 0.8149 0.8871 0.9281 0.3127  0.3410  0.1665  262 LEU C CA  
11990 C C   . LEU C 262 ? 1.0225 1.0940 1.1093 0.3240  0.3538  0.1675  262 LEU C C   
11991 O O   . LEU C 262 ? 1.0822 1.1696 1.1769 0.3349  0.3656  0.1768  262 LEU C O   
11992 C CB  . LEU C 262 ? 0.8798 0.9650 1.0201 0.2967  0.3352  0.1741  262 LEU C CB  
11993 C CG  . LEU C 262 ? 0.7392 0.8518 0.9060 0.2992  0.3476  0.1906  262 LEU C CG  
11994 C CD1 . LEU C 262 ? 0.7864 0.9195 0.9861 0.3074  0.3544  0.2015  262 LEU C CD1 
11995 C CD2 . LEU C 262 ? 0.9122 1.0327 1.0989 0.2829  0.3400  0.1959  262 LEU C CD2 
11996 N N   . LEU C 263 ? 0.9731 1.0254 1.0276 0.3196  0.3491  0.1580  263 LEU C N   
11997 C CA  . LEU C 263 ? 0.8411 0.8904 0.8679 0.3305  0.3600  0.1579  263 LEU C CA  
11998 C C   . LEU C 263 ? 1.0262 1.0678 1.0327 0.3476  0.3654  0.1537  263 LEU C C   
11999 O O   . LEU C 263 ? 1.1065 1.1572 1.1076 0.3556  0.3731  0.1603  263 LEU C O   
12000 C CB  . LEU C 263 ? 0.9650 0.9915 0.9596 0.3219  0.3509  0.1466  263 LEU C CB  
12001 C CG  . LEU C 263 ? 0.8463 0.8623 0.8046 0.3341  0.3592  0.1426  263 LEU C CG  
12002 C CD1 . LEU C 263 ? 0.8062 0.8383 0.7713 0.3310  0.3668  0.1531  263 LEU C CD1 
12003 C CD2 . LEU C 263 ? 0.9670 0.9529 0.8899 0.3293  0.3470  0.1273  263 LEU C CD2 
12004 N N   . SER C 264 ? 1.0258 1.0496 1.0209 0.3514  0.3586  0.1429  264 SER C N   
12005 C CA  . SER C 264 ? 0.9680 0.9814 0.9407 0.3668  0.3610  0.1374  264 SER C CA  
12006 C C   . SER C 264 ? 0.9342 0.9703 0.9343 0.3730  0.3677  0.1489  264 SER C C   
12007 O O   . SER C 264 ? 1.0431 1.0804 1.0281 0.3853  0.3739  0.1504  264 SER C O   
12008 C CB  . SER C 264 ? 0.9717 0.9593 0.9250 0.3687  0.3511  0.1231  264 SER C CB  
12009 O OG  . SER C 264 ? 1.1229 1.1129 1.1020 0.3550  0.3401  0.1232  264 SER C OG  
12010 N N   . GLU C 265 ? 0.8710 0.9245 0.9099 0.3651  0.3663  0.1570  265 GLU C N   
12011 C CA  . GLU C 265 ? 1.0294 1.1055 1.0966 0.3700  0.3724  0.1688  265 GLU C CA  
12012 C C   . GLU C 265 ? 0.9851 1.0801 1.0574 0.3722  0.3825  0.1817  265 GLU C C   
12013 O O   . GLU C 265 ? 1.0851 1.1926 1.1638 0.3816  0.3895  0.1890  265 GLU C O   
12014 C CB  . GLU C 265 ? 0.9904 1.0810 1.0995 0.3597  0.3675  0.1754  265 GLU C CB  
12015 C CG  . GLU C 265 ? 0.9219 0.9984 1.0319 0.3608  0.3588  0.1656  265 GLU C CG  
12016 C CD  . GLU C 265 ? 1.1145 1.1940 1.2276 0.3724  0.3612  0.1661  265 GLU C CD  
12017 O OE1 . GLU C 265 ? 0.9878 1.0883 1.1191 0.3765  0.3691  0.1779  265 GLU C OE1 
12018 O OE2 . GLU C 265 ? 1.0607 1.1213 1.1580 0.3772  0.3549  0.1547  265 GLU C OE2 
12019 N N   . MET C 266 ? 1.0030 1.1001 1.0726 0.3637  0.3832  0.1845  266 MET C N   
12020 C CA  . MET C 266 ? 1.0160 1.1295 1.0897 0.3651  0.3919  0.1967  266 MET C CA  
12021 C C   . MET C 266 ? 1.0393 1.1396 1.0728 0.3776  0.3967  0.1911  266 MET C C   
12022 O O   . MET C 266 ? 1.2143 1.3280 1.2493 0.3852  0.4052  0.2009  266 MET C O   
12023 C CB  . MET C 266 ? 0.9097 1.0310 0.9978 0.3508  0.3900  0.2025  266 MET C CB  
12024 C CG  . MET C 266 ? 0.9407 1.0783 1.0721 0.3386  0.3854  0.2105  266 MET C CG  
12025 S SD  . MET C 266 ? 0.9906 1.1501 1.1599 0.3432  0.3886  0.2226  266 MET C SD  
12026 C CE  . MET C 266 ? 1.0089 1.1949 1.2163 0.3328  0.3913  0.2411  266 MET C CE  
12027 N N   . VAL C 267 ? 0.9552 1.0292 0.9531 0.3803  0.3909  0.1758  267 VAL C N   
12028 C CA  . VAL C 267 ? 0.8913 0.9508 0.8501 0.3929  0.3939  0.1696  267 VAL C CA  
12029 C C   . VAL C 267 ? 1.1324 1.1932 1.0863 0.4081  0.3978  0.1697  267 VAL C C   
12030 O O   . VAL C 267 ? 1.1745 1.2347 1.1081 0.4201  0.4037  0.1713  267 VAL C O   
12031 C CB  . VAL C 267 ? 0.8625 0.8926 0.7848 0.3914  0.3856  0.1536  267 VAL C CB  
12032 C CG1 . VAL C 267 ? 0.8964 0.9110 0.7790 0.4053  0.3875  0.1473  267 VAL C CG1 
12033 C CG2 . VAL C 267 ? 0.9527 0.9833 0.8797 0.3769  0.3826  0.1545  267 VAL C CG2 
12034 N N   . VAL C 268 ? 1.1178 1.1811 1.0908 0.4077  0.3945  0.1683  268 VAL C N   
12035 C CA  . VAL C 268 ? 1.0432 1.1090 1.0147 0.4212  0.3979  0.1687  268 VAL C CA  
12036 C C   . VAL C 268 ? 0.9500 1.0440 0.9460 0.4251  0.4088  0.1859  268 VAL C C   
12037 O O   . VAL C 268 ? 1.0598 1.1558 1.0405 0.4390  0.4153  0.1882  268 VAL C O   
12038 C CB  . VAL C 268 ? 0.8740 0.9360 0.8626 0.4184  0.3909  0.1634  268 VAL C CB  
12039 C CG1 . VAL C 268 ? 0.8866 0.9597 0.8859 0.4300  0.3957  0.1682  268 VAL C CG1 
12040 C CG2 . VAL C 268 ? 1.0449 1.0762 1.0030 0.4186  0.3806  0.1460  268 VAL C CG2 
12041 N N   . GLU C 269 ? 1.0249 1.1402 1.0588 0.4131  0.4102  0.1981  269 GLU C N   
12042 C CA  . GLU C 269 ? 1.0774 1.2197 1.1379 0.4151  0.4197  0.2156  269 GLU C CA  
12043 C C   . GLU C 269 ? 1.1469 1.2912 1.1871 0.4205  0.4269  0.2207  269 GLU C C   
12044 O O   . GLU C 269 ? 1.1406 1.2986 1.1828 0.4309  0.4359  0.2306  269 GLU C O   
12045 C CB  . GLU C 269 ? 1.0246 1.1863 1.1294 0.3997  0.4174  0.2267  269 GLU C CB  
12046 C CG  . GLU C 269 ? 1.2080 1.3942 1.3490 0.4018  0.4226  0.2411  269 GLU C CG  
12047 C CD  . GLU C 269 ? 1.4427 1.6479 1.6274 0.3868  0.4197  0.2530  269 GLU C CD  
12048 O OE1 . GLU C 269 ? 1.2385 1.4362 1.4330 0.3755  0.4104  0.2465  269 GLU C OE1 
12049 O OE2 . GLU C 269 ? 1.4079 1.6351 1.6171 0.3866  0.4263  0.2690  269 GLU C OE2 
12050 N N   . ALA C 270 ? 1.0988 1.2294 1.1189 0.4140  0.4230  0.2139  270 ALA C N   
12051 C CA  . ALA C 270 ? 1.1342 1.2643 1.1330 0.4187  0.4285  0.2174  270 ALA C CA  
12052 C C   . ALA C 270 ? 1.1148 1.2325 1.0780 0.4371  0.4322  0.2111  270 ALA C C   
12053 O O   . ALA C 270 ? 1.2497 1.3766 1.2058 0.4460  0.4403  0.2197  270 ALA C O   
12054 C CB  . ALA C 270 ? 1.1387 1.2529 1.1202 0.4084  0.4219  0.2087  270 ALA C CB  
12055 N N   . ALA C 271 ? 1.0875 1.1851 1.0298 0.4433  0.4261  0.1971  271 ALA C N   
12056 C CA  . ALA C 271 ? 1.1073 1.1906 1.0138 0.4611  0.4279  0.1898  271 ALA C CA  
12057 C C   . ALA C 271 ? 1.2404 1.3439 1.1611 0.4734  0.4378  0.2018  271 ALA C C   
12058 O O   . ALA C 271 ? 1.1802 1.2760 1.0731 0.4893  0.4411  0.1987  271 ALA C O   
12059 C CB  . ALA C 271 ? 0.9809 1.0386 0.8658 0.4636  0.4181  0.1727  271 ALA C CB  
12060 N N   . SER C 272 ? 1.3054 1.4334 1.2675 0.4664  0.4418  0.2149  272 SER C N   
12061 C CA  . SER C 272 ? 1.1872 1.3362 1.1669 0.4767  0.4511  0.2276  272 SER C CA  
12062 C C   . SER C 272 ? 1.2206 1.3935 1.2193 0.4754  0.4608  0.2458  272 SER C C   
12063 O O   . SER C 272 ? 1.2695 1.4627 1.2878 0.4822  0.4689  0.2587  272 SER C O   
12064 C CB  . SER C 272 ? 1.1259 1.2858 1.1398 0.4709  0.4485  0.2303  272 SER C CB  
12065 O OG  . SER C 272 ? 1.3491 1.4873 1.3461 0.4729  0.4397  0.2141  272 SER C OG  
12066 N N   . ASP C 273 ? 1.2666 1.4373 1.2602 0.4667  0.4598  0.2473  273 ASP C N   
12067 C CA  . ASP C 273 ? 1.2788 1.4707 1.2896 0.4652  0.4682  0.2643  273 ASP C CA  
12068 C C   . ASP C 273 ? 1.3440 1.5338 1.3249 0.4835  0.4763  0.2664  273 ASP C C   
12069 O O   . ASP C 273 ? 1.3087 1.4769 1.2513 0.4898  0.4730  0.2542  273 ASP C O   
12070 C CB  . ASP C 273 ? 1.2521 1.4410 1.2658 0.4504  0.4638  0.2642  273 ASP C CB  
12071 C CG  . ASP C 273 ? 1.4266 1.6371 1.4606 0.4471  0.4712  0.2819  273 ASP C CG  
12072 O OD1 . ASP C 273 ? 1.5269 1.7591 1.5858 0.4517  0.4788  0.2967  273 ASP C OD1 
12073 O OD2 . ASP C 273 ? 1.4768 1.6824 1.5022 0.4400  0.4693  0.2812  273 ASP C OD2 
12074 N N   . PRO C 274 ? 1.3369 1.5486 1.3342 0.4926  0.4865  0.2818  274 PRO C N   
12075 C CA  . PRO C 274 ? 1.2562 1.4663 1.2246 0.5112  0.4945  0.2844  274 PRO C CA  
12076 C C   . PRO C 274 ? 1.2538 1.4512 1.1922 0.5127  0.4941  0.2805  274 PRO C C   
12077 O O   . PRO C 274 ? 1.4291 1.6106 1.3300 0.5273  0.4946  0.2721  274 PRO C O   
12078 C CB  . PRO C 274 ? 1.3288 1.5690 1.3293 0.5149  0.5056  0.3055  274 PRO C CB  
12079 C CG  . PRO C 274 ? 1.1734 1.4264 1.2131 0.5037  0.5025  0.3098  274 PRO C CG  
12080 C CD  . PRO C 274 ? 1.2726 1.5108 1.3151 0.4869  0.4910  0.2979  274 PRO C CD  
12081 N N   . GLU C 275 ? 1.1734 1.3773 1.1279 0.4983  0.4926  0.2863  275 GLU C N   
12082 C CA  . GLU C 275 ? 1.2287 1.4210 1.1564 0.4989  0.4918  0.2828  275 GLU C CA  
12083 C C   . GLU C 275 ? 1.3220 1.4829 1.2111 0.4999  0.4818  0.2617  275 GLU C C   
12084 O O   . GLU C 275 ? 1.2883 1.4343 1.1420 0.5106  0.4819  0.2553  275 GLU C O   
12085 C CB  . GLU C 275 ? 1.3386 1.5425 1.2927 0.4812  0.4904  0.2915  275 GLU C CB  
12086 C CG  . GLU C 275 ? 1.3114 1.5444 1.2991 0.4807  0.4998  0.3132  275 GLU C CG  
12087 C CD  . GLU C 275 ? 1.6490 1.8932 1.6676 0.4617  0.4965  0.3213  275 GLU C CD  
12088 O OE1 . GLU C 275 ? 1.6309 1.8609 1.6346 0.4530  0.4900  0.3123  275 GLU C OE1 
12089 O OE2 . GLU C 275 ? 1.7341 2.0011 1.7919 0.4555  0.4999  0.3366  275 GLU C OE2 
12090 N N   . LEU C 276 ? 1.3076 1.4584 1.2040 0.4896  0.4731  0.2511  276 LEU C N   
12091 C CA  . LEU C 276 ? 1.1202 1.2407 0.9818 0.4890  0.4627  0.2314  276 LEU C CA  
12092 C C   . LEU C 276 ? 1.2073 1.3121 1.0376 0.5071  0.4622  0.2216  276 LEU C C   
12093 O O   . LEU C 276 ? 1.2937 1.3744 1.0862 0.5133  0.4565  0.2086  276 LEU C O   
12094 C CB  . LEU C 276 ? 1.1008 1.2164 0.9814 0.4725  0.4538  0.2243  276 LEU C CB  
12095 C CG  . LEU C 276 ? 0.9886 1.1090 0.8862 0.4546  0.4505  0.2277  276 LEU C CG  
12096 C CD1 . LEU C 276 ? 1.1260 1.2423 1.0427 0.4401  0.4420  0.2211  276 LEU C CD1 
12097 C CD2 . LEU C 276 ? 1.0233 1.1246 0.8868 0.4549  0.4467  0.2189  276 LEU C CD2 
12098 N N   . VAL C 277 ? 1.1883 1.3062 1.0339 0.5154  0.4675  0.2278  277 VAL C N   
12099 C CA  . VAL C 277 ? 1.2923 1.3955 1.1077 0.5333  0.4669  0.2186  277 VAL C CA  
12100 C C   . VAL C 277 ? 1.3455 1.4457 1.1313 0.5492  0.4729  0.2217  277 VAL C C   
12101 O O   . VAL C 277 ? 1.3796 1.4572 1.1276 0.5613  0.4681  0.2092  277 VAL C O   
12102 C CB  . VAL C 277 ? 1.1196 1.2367 0.9560 0.5398  0.4711  0.2238  277 VAL C CB  
12103 C CG1 . VAL C 277 ? 1.2193 1.3417 1.0885 0.5236  0.4655  0.2226  277 VAL C CG1 
12104 C CG2 . VAL C 277 ? 1.3477 1.4927 1.2038 0.5483  0.4842  0.2429  277 VAL C CG2 
12105 N N   . GLU C 278 ? 1.3997 1.5219 1.2024 0.5491  0.4825  0.2382  278 GLU C N   
12106 C CA  . GLU C 278 ? 1.4277 1.5491 1.2048 0.5641  0.4888  0.2427  278 GLU C CA  
12107 C C   . GLU C 278 ? 1.3830 1.4831 1.1312 0.5600  0.4817  0.2324  278 GLU C C   
12108 O O   . GLU C 278 ? 1.4400 1.5258 1.1529 0.5745  0.4816  0.2270  278 GLU C O   
12109 C CB  . GLU C 278 ? 1.4504 1.6025 1.2567 0.5649  0.5013  0.2643  278 GLU C CB  
12110 C CG  . GLU C 278 ? 1.6498 1.8225 1.4785 0.5736  0.5096  0.2756  278 GLU C CG  
12111 C CD  . GLU C 278 ? 1.8398 2.0015 1.6373 0.5950  0.5113  0.2689  278 GLU C CD  
12112 O OE1 . GLU C 278 ? 1.8968 2.0588 1.6718 0.6105  0.5176  0.2735  278 GLU C OE1 
12113 O OE2 . GLU C 278 ? 1.5200 1.6722 1.3151 0.5965  0.5060  0.2589  278 GLU C OE2 
12114 N N   . LEU C 279 ? 1.3504 1.4481 1.1130 0.5409  0.4755  0.2295  279 LEU C N   
12115 C CA  . LEU C 279 ? 1.4011 1.4786 1.1379 0.5357  0.4682  0.2193  279 LEU C CA  
12116 C C   . LEU C 279 ? 1.4293 1.4749 1.1271 0.5432  0.4577  0.1996  279 LEU C C   
12117 O O   . LEU C 279 ? 1.3458 1.3729 1.0102 0.5499  0.4537  0.1918  279 LEU C O   
12118 C CB  . LEU C 279 ? 1.3145 1.3962 1.0765 0.5134  0.4632  0.2198  279 LEU C CB  
12119 C CG  . LEU C 279 ? 1.1532 1.2158 0.8923 0.5058  0.4555  0.2100  279 LEU C CG  
12120 C CD1 . LEU C 279 ? 1.3290 1.3996 1.0607 0.5111  0.4621  0.2195  279 LEU C CD1 
12121 C CD2 . LEU C 279 ? 1.1603 1.2246 0.9230 0.4844  0.4493  0.2081  279 LEU C CD2 
12122 N N   . ALA C 280 ? 1.3462 1.3852 1.0487 0.5424  0.4528  0.1918  280 ALA C N   
12123 C CA  . ALA C 280 ? 1.2931 1.3022 0.9611 0.5494  0.4422  0.1736  280 ALA C CA  
12124 C C   . ALA C 280 ? 1.4619 1.4618 1.0963 0.5716  0.4449  0.1717  280 ALA C C   
12125 O O   . ALA C 280 ? 1.4763 1.4498 1.0741 0.5781  0.4365  0.1587  280 ALA C O   
12126 C CB  . ALA C 280 ? 1.1752 1.1830 0.8585 0.5457  0.4382  0.1684  280 ALA C CB  
12127 N N   . LYS C 281 ? 1.3536 1.3751 1.0004 0.5834  0.4564  0.1851  281 LYS C N   
12128 C CA  . LYS C 281 ? 1.2856 1.3013 0.9024 0.6057  0.4603  0.1851  281 LYS C CA  
12129 C C   . LYS C 281 ? 1.5264 1.5376 1.1222 0.6100  0.4620  0.1876  281 LYS C C   
12130 O O   . LYS C 281 ? 1.6206 1.6116 1.1786 0.6245  0.4578  0.1790  281 LYS C O   
12131 C CB  . LYS C 281 ? 1.3944 1.4371 1.0332 0.6162  0.4730  0.2005  281 LYS C CB  
12132 C CG  . LYS C 281 ? 1.2740 1.3266 0.9415 0.6098  0.4727  0.2011  281 LYS C CG  
12133 C CD  . LYS C 281 ? 1.3004 1.3471 0.9519 0.6276  0.4731  0.1964  281 LYS C CD  
12134 C CE  . LYS C 281 ? 1.4048 1.4659 1.0893 0.6213  0.4746  0.1998  281 LYS C CE  
12135 N NZ  . LYS C 281 ? 1.6377 1.7328 1.3579 0.6219  0.4881  0.2202  281 LYS C NZ  
12136 N N   . SER C 282 ? 1.5360 1.5652 1.1562 0.5975  0.4675  0.1992  282 SER C N   
12137 C CA  . SER C 282 ? 1.4652 1.4919 1.0694 0.5998  0.4693  0.2025  282 SER C CA  
12138 C C   . SER C 282 ? 1.3764 1.3704 0.9443 0.5983  0.4562  0.1845  282 SER C C   
12139 O O   . SER C 282 ? 1.5241 1.5066 1.0626 0.6095  0.4556  0.1822  282 SER C O   
12140 C CB  . SER C 282 ? 1.3743 1.4225 1.0131 0.5824  0.4744  0.2151  282 SER C CB  
12141 O OG  . SER C 282 ? 1.8520 1.9309 1.5259 0.5829  0.4860  0.2330  282 SER C OG  
12142 N N   . VAL C 283 ? 1.4432 1.4223 1.0136 0.5846  0.4455  0.1722  283 VAL C N   
12143 C CA  . VAL C 283 ? 1.4531 1.4008 0.9917 0.5814  0.4321  0.1551  283 VAL C CA  
12144 C C   . VAL C 283 ? 1.5474 1.4692 1.0484 0.5985  0.4242  0.1416  283 VAL C C   
12145 O O   . VAL C 283 ? 1.5143 1.4092 0.9839 0.6001  0.4133  0.1285  283 VAL C O   
12146 C CB  . VAL C 283 ? 1.4558 1.3983 1.0125 0.5598  0.4239  0.1482  283 VAL C CB  
12147 C CG1 . VAL C 283 ? 1.6300 1.5401 1.1543 0.5563  0.4098  0.1311  283 VAL C CG1 
12148 C CG2 . VAL C 283 ? 1.4291 1.3953 1.0205 0.5434  0.4303  0.1609  283 VAL C CG2 
12149 N N   . GLY C 284 ? 1.4794 1.4092 0.9841 0.6108  0.4292  0.1449  284 GLY C N   
12150 C CA  . GLY C 284 ? 1.3699 1.2770 0.8409 0.6278  0.4221  0.1331  284 GLY C CA  
12151 C C   . GLY C 284 ? 1.5112 1.4057 0.9862 0.6219  0.4130  0.1218  284 GLY C C   
12152 O O   . GLY C 284 ? 1.5756 1.4418 1.0200 0.6283  0.4011  0.1069  284 GLY C O   
12153 N N   . ALA C 285 ? 1.4932 1.4083 1.0061 0.6098  0.4182  0.1290  285 ALA C N   
12154 C CA  . ALA C 285 ? 1.4213 1.3272 0.9424 0.6033  0.4106  0.1198  285 ALA C CA  
12155 C C   . ALA C 285 ? 1.5137 1.4384 1.0538 0.6123  0.4189  0.1277  285 ALA C C   
12156 O O   . ALA C 285 ? 1.4992 1.4508 1.0593 0.6166  0.4319  0.1433  285 ALA C O   
12157 C CB  . ALA C 285 ? 1.5133 1.4252 1.0629 0.5804  0.4079  0.1202  285 ALA C CB  
12158 N N   . ASP C 286 ? 1.4316 1.3424 0.9663 0.6147  0.4112  0.1172  286 ASP C N   
12159 C CA  . ASP C 286 ? 1.4330 1.3597 0.9851 0.6228  0.4178  0.1231  286 ASP C CA  
12160 C C   . ASP C 286 ? 1.3892 1.3446 0.9886 0.6074  0.4258  0.1357  286 ASP C C   
12161 O O   . ASP C 286 ? 1.3468 1.3281 0.9689 0.6128  0.4374  0.1496  286 ASP C O   
12162 C CB  . ASP C 286 ? 1.4786 1.3814 1.0140 0.6270  0.4059  0.1077  286 ASP C CB  
12163 C CG  . ASP C 286 ? 1.7111 1.5844 1.2004 0.6428  0.3964  0.0948  286 ASP C CG  
12164 O OD1 . ASP C 286 ? 1.8401 1.7154 1.3104 0.6559  0.4017  0.0997  286 ASP C OD1 
12165 O OD2 . ASP C 286 ? 1.8353 1.6831 1.3076 0.6424  0.3833  0.0801  286 ASP C OD2 
12166 N N   . GLY C 287 ? 1.3637 1.3139 0.9775 0.5886  0.4190  0.1309  287 GLY C N   
12167 C CA  . GLY C 287 ? 1.3085 1.2827 0.9661 0.5727  0.4243  0.1413  287 GLY C CA  
12168 C C   . GLY C 287 ? 1.4065 1.3693 1.0704 0.5535  0.4151  0.1338  287 GLY C C   
12169 O O   . GLY C 287 ? 1.5384 1.4793 1.1749 0.5517  0.4073  0.1239  287 GLY C O   
12170 N N   . ILE C 288 ? 1.2837 1.2609 0.9835 0.5394  0.4158  0.1385  288 ILE C N   
12171 C CA  . ILE C 288 ? 1.1755 1.1436 0.8839 0.5212  0.4075  0.1322  288 ILE C CA  
12172 C C   . ILE C 288 ? 1.1817 1.1339 0.8898 0.5184  0.3978  0.1203  288 ILE C C   
12173 O O   . ILE C 288 ? 1.3495 1.3162 1.0849 0.5168  0.4006  0.1253  288 ILE C O   
12174 C CB  . ILE C 288 ? 1.0960 1.0912 0.8449 0.5060  0.4143  0.1464  288 ILE C CB  
12175 C CG1 . ILE C 288 ? 1.2193 1.2295 0.9679 0.5089  0.4235  0.1584  288 ILE C CG1 
12176 C CG2 . ILE C 288 ? 1.1309 1.1157 0.8866 0.4881  0.4054  0.1393  288 ILE C CG2 
12177 C CD1 . ILE C 288 ? 1.0927 1.1340 0.8836 0.4986  0.4322  0.1757  288 ILE C CD1 
12178 N N   . ASN C 289 ? 1.1957 1.1175 0.8731 0.5178  0.3858  0.1047  289 ASN C N   
12179 C CA  . ASN C 289 ? 1.1491 1.0521 0.8227 0.5151  0.3751  0.0925  289 ASN C CA  
12180 C C   . ASN C 289 ? 1.3041 1.2049 0.9958 0.4959  0.3694  0.0901  289 ASN C C   
12181 O O   . ASN C 289 ? 1.3634 1.2463 1.0366 0.4891  0.3622  0.0825  289 ASN C O   
12182 C CB  . ASN C 289 ? 1.2312 1.1014 0.8614 0.5257  0.3644  0.0772  289 ASN C CB  
12183 C CG  . ASN C 289 ? 1.3425 1.1922 0.9666 0.5252  0.3530  0.0650  289 ASN C CG  
12184 O OD1 . ASN C 289 ? 1.4366 1.2606 1.0420 0.5190  0.3410  0.0530  289 ASN C OD1 
12185 N ND2 . ASN C 289 ? 1.3092 1.1693 0.9488 0.5317  0.3562  0.0678  289 ASN C ND2 
12186 N N   . LEU C 290 ? 1.3302 1.2495 1.0581 0.4878  0.3725  0.0971  290 LEU C N   
12187 C CA  . LEU C 290 ? 1.2272 1.1466 0.9755 0.4700  0.3674  0.0959  290 LEU C CA  
12188 C C   . LEU C 290 ? 1.3434 1.2370 1.0790 0.4682  0.3549  0.0817  290 LEU C C   
12189 O O   . LEU C 290 ? 1.4219 1.3125 1.1573 0.4771  0.3533  0.0787  290 LEU C O   
12190 C CB  . LEU C 290 ? 1.1299 1.0802 0.9233 0.4626  0.3754  0.1100  290 LEU C CB  
12191 C CG  . LEU C 290 ? 1.2431 1.2180 1.0561 0.4569  0.3851  0.1245  290 LEU C CG  
12192 C CD1 . LEU C 290 ? 1.1349 1.1339 0.9927 0.4444  0.3882  0.1355  290 LEU C CD1 
12193 C CD2 . LEU C 290 ? 1.4530 1.4152 1.2453 0.4501  0.3817  0.1200  290 LEU C CD2 
12194 N N   . CYS C 291 ? 1.1957 1.0716 0.9213 0.4571  0.3462  0.0736  291 CYS C N   
12195 C CA  . CYS C 291 ? 1.0211 0.8716 0.7350 0.4540  0.3336  0.0607  291 CYS C CA  
12196 C C   . CYS C 291 ? 1.3020 1.1545 1.0362 0.4370  0.3300  0.0613  291 CYS C C   
12197 O O   . CYS C 291 ? 1.2737 1.1401 1.0201 0.4280  0.3350  0.0685  291 CYS C O   
12198 C CB  . CYS C 291 ? 1.0507 0.8695 0.7216 0.4605  0.3239  0.0474  291 CYS C CB  
12199 S SG  . CYS C 291 ? 1.3991 1.2136 1.0427 0.4817  0.3271  0.0461  291 CYS C SG  
12200 N N   . GLY C 292 ? 1.1366 0.9748 0.8738 0.4329  0.3209  0.0538  292 GLY C N   
12201 C CA  . GLY C 292 ? 0.9531 0.7911 0.7086 0.4177  0.3165  0.0538  292 GLY C CA  
12202 C C   . GLY C 292 ? 1.0555 0.8618 0.7871 0.4103  0.3006  0.0406  292 GLY C C   
12203 O O   . GLY C 292 ? 1.1472 0.9299 0.8501 0.4213  0.2948  0.0306  292 GLY C O   
12204 N N   . MET C 293 ? 0.9352 0.7420 0.6796 0.3896  0.2916  0.0413  293 MET C N   
12205 C CA  . MET C 293 ? 0.9383 0.7176 0.6644 0.3780  0.2743  0.0306  293 MET C CA  
12206 C C   . MET C 293 ? 0.9983 0.7864 0.7527 0.3579  0.2664  0.0342  293 MET C C   
12207 O O   . MET C 293 ? 1.1068 0.9184 0.8866 0.3501  0.2732  0.0438  293 MET C O   
12208 C CB  . MET C 293 ? 1.0452 0.8098 0.7441 0.3750  0.2707  0.0258  293 MET C CB  
12209 C CG  . MET C 293 ? 1.2073 0.9571 0.8728 0.3949  0.2751  0.0199  293 MET C CG  
12210 S SD  . MET C 293 ? 1.2290 0.9507 0.8581 0.3897  0.2638  0.0101  293 MET C SD  
12211 C CE  . MET C 293 ? 1.2943 0.9810 0.8973 0.3957  0.2477  -0.0035 293 MET C CE  
12212 N N   . CYS C 294 ? 0.9589 0.7288 0.7091 0.3505  0.2526  0.0271  294 CYS C N   
12213 C CA  . CYS C 294 ? 1.0787 0.8547 0.8527 0.3319  0.2441  0.0298  294 CYS C CA  
12214 C C   . CYS C 294 ? 1.0304 0.8334 0.8403 0.3322  0.2524  0.0397  294 CYS C C   
12215 O O   . CYS C 294 ? 1.0897 0.9015 0.9041 0.3474  0.2620  0.0424  294 CYS C O   
12216 C CB  . CYS C 294 ? 1.0529 0.8305 0.8260 0.3166  0.2404  0.0313  294 CYS C CB  
12217 S SG  . CYS C 294 ? 1.0142 0.7595 0.7489 0.3130  0.2278  0.0200  294 CYS C SG  
12218 N N   . CYS C 295 ? 1.0578 0.8735 0.8924 0.3166  0.2485  0.0448  295 CYS C N   
12219 C CA  . CYS C 295 ? 0.9013 0.7410 0.7716 0.3157  0.2539  0.0539  295 CYS C CA  
12220 C C   . CYS C 295 ? 0.9826 0.8446 0.8646 0.3278  0.2702  0.0629  295 CYS C C   
12221 O O   . CYS C 295 ? 1.1353 1.0065 1.0297 0.3392  0.2766  0.0661  295 CYS C O   
12222 C CB  . CYS C 295 ? 1.1545 1.0041 1.0464 0.2975  0.2474  0.0581  295 CYS C CB  
12223 S SG  . CYS C 295 ? 1.3385 1.1693 1.2281 0.2851  0.2299  0.0507  295 CYS C SG  
12224 N N   . THR C 296 ? 0.9996 0.8707 0.8790 0.3255  0.2769  0.0674  296 THR C N   
12225 C CA  . THR C 296 ? 0.9435 0.8386 0.8377 0.3362  0.2929  0.0779  296 THR C CA  
12226 C C   . THR C 296 ? 0.9072 0.7985 0.7879 0.3567  0.3010  0.0759  296 THR C C   
12227 O O   . THR C 296 ? 1.0365 0.9495 0.9379 0.3662  0.3129  0.0852  296 THR C O   
12228 C CB  . THR C 296 ? 0.9767 0.8778 0.8625 0.3331  0.2989  0.0817  296 THR C CB  
12229 O OG1 . THR C 296 ? 1.0755 1.0041 0.9856 0.3390  0.3129  0.0944  296 THR C OG1 
12230 C CG2 . THR C 296 ? 1.1081 0.9893 0.9549 0.3433  0.3001  0.0736  296 THR C CG2 
12231 N N   . GLY C 297 ? 0.8583 0.7232 0.7065 0.3633  0.2943  0.0643  297 GLY C N   
12232 C CA  . GLY C 297 ? 0.9782 0.8379 0.8118 0.3835  0.3009  0.0615  297 GLY C CA  
12233 C C   . GLY C 297 ? 1.0627 0.9264 0.9158 0.3866  0.2986  0.0621  297 GLY C C   
12234 O O   . GLY C 297 ? 1.1785 1.0550 1.0401 0.4017  0.3091  0.0668  297 GLY C O   
12235 N N   . ASN C 298 ? 0.9370 0.7907 0.7981 0.3724  0.2848  0.0577  298 ASN C N   
12236 C CA  . ASN C 298 ? 0.8888 0.7450 0.7690 0.3735  0.2809  0.0579  298 ASN C CA  
12237 C C   . ASN C 298 ? 1.0579 0.9452 0.9769 0.3736  0.2907  0.0707  298 ASN C C   
12238 O O   . ASN C 298 ? 1.0621 0.9584 0.9940 0.3849  0.2962  0.0737  298 ASN C O   
12239 C CB  . ASN C 298 ? 0.8458 0.6874 0.7282 0.3567  0.2647  0.0521  298 ASN C CB  
12240 C CG  . ASN C 298 ? 1.0245 0.8349 0.8742 0.3581  0.2532  0.0398  298 ASN C CG  
12241 O OD1 . ASN C 298 ? 1.1414 0.9398 0.9735 0.3731  0.2546  0.0344  298 ASN C OD1 
12242 N ND2 . ASN C 298 ? 1.0900 0.8864 0.9311 0.3428  0.2413  0.0353  298 ASN C ND2 
12243 N N   . GLU C 299 ? 0.9686 0.8723 0.9068 0.3612  0.2926  0.0785  299 GLU C N   
12244 C CA  . GLU C 299 ? 1.0036 0.9366 0.9806 0.3595  0.3005  0.0914  299 GLU C CA  
12245 C C   . GLU C 299 ? 1.0220 0.9736 1.0047 0.3774  0.3175  0.0997  299 GLU C C   
12246 O O   . GLU C 299 ? 1.0402 1.0139 1.0547 0.3805  0.3238  0.1095  299 GLU C O   
12247 C CB  . GLU C 299 ? 0.9536 0.8983 0.9461 0.3433  0.2986  0.0975  299 GLU C CB  
12248 C CG  . GLU C 299 ? 0.9701 0.9009 0.9616 0.3257  0.2828  0.0912  299 GLU C CG  
12249 C CD  . GLU C 299 ? 1.1902 1.1357 1.2173 0.3142  0.2770  0.0975  299 GLU C CD  
12250 O OE1 . GLU C 299 ? 1.0940 1.0516 1.1441 0.3205  0.2800  0.1024  299 GLU C OE1 
12251 O OE2 . GLU C 299 ? 1.2146 1.1592 1.2462 0.2994  0.2691  0.0973  299 GLU C OE2 
12252 N N   . VAL C 300 ? 0.9334 0.8755 0.8852 0.3897  0.3244  0.0958  300 VAL C N   
12253 C CA  . VAL C 300 ? 1.0483 1.0082 1.0024 0.4038  0.3381  0.1041  300 VAL C CA  
12254 C C   . VAL C 300 ? 1.1569 1.1058 1.0952 0.4174  0.3363  0.0976  300 VAL C C   
12255 O O   . VAL C 300 ? 1.1579 1.1254 1.1108 0.4250  0.3438  0.1056  300 VAL C O   
12256 C CB  . VAL C 300 ? 0.9790 0.9392 0.9115 0.4056  0.3443  0.1057  300 VAL C CB  
12257 C CG1 . VAL C 300 ? 0.9771 0.9477 0.9250 0.3919  0.3454  0.1118  300 VAL C CG1 
12258 C CG2 . VAL C 300 ? 1.0883 1.0188 0.9762 0.4126  0.3388  0.0922  300 VAL C CG2 
12259 N N   . SER C 301 ? 1.0531 0.9729 0.9630 0.4201  0.3266  0.0839  301 SER C N   
12260 C CA  . SER C 301 ? 1.0559 0.9634 0.9510 0.4323  0.3232  0.0770  301 SER C CA  
12261 C C   . SER C 301 ? 0.9938 0.9113 0.9192 0.4306  0.3206  0.0801  301 SER C C   
12262 O O   . SER C 301 ? 1.0537 0.9736 0.9791 0.4410  0.3221  0.0797  301 SER C O   
12263 C CB  . SER C 301 ? 1.2599 1.1324 1.1182 0.4340  0.3117  0.0618  301 SER C CB  
12264 O OG  . SER C 301 ? 1.4781 1.3399 1.3072 0.4361  0.3130  0.0582  301 SER C OG  
12265 N N   . MET C 302 ? 0.9847 0.9072 0.9352 0.4180  0.3162  0.0830  302 MET C N   
12266 C CA  . MET C 302 ? 0.8688 0.8003 0.8494 0.4153  0.3125  0.0861  302 MET C CA  
12267 C C   . MET C 302 ? 0.9419 0.9057 0.9559 0.4175  0.3226  0.1000  302 MET C C   
12268 O O   . MET C 302 ? 0.9769 0.9475 1.0052 0.4230  0.3223  0.1017  302 MET C O   
12269 C CB  . MET C 302 ? 0.8593 0.7882 0.8562 0.3953  0.3009  0.0857  302 MET C CB  
12270 C CG  . MET C 302 ? 0.8342 0.7328 0.8042 0.3869  0.2855  0.0727  302 MET C CG  
12271 S SD  . MET C 302 ? 1.1431 1.0265 1.1143 0.3903  0.2748  0.0652  302 MET C SD  
12272 C CE  . MET C 302 ? 1.0207 0.9239 1.0359 0.3753  0.2697  0.0738  302 MET C CE  
12273 N N   . ARG C 303 ? 1.0061 0.9896 1.0329 0.4128  0.3310  0.1103  303 ARG C N   
12274 C CA  . ARG C 303 ? 0.9541 0.9685 1.0142 0.4133  0.3400  0.1250  303 ARG C CA  
12275 C C   . ARG C 303 ? 0.9588 0.9837 1.0070 0.4258  0.3510  0.1301  303 ARG C C   
12276 O O   . ARG C 303 ? 1.1599 1.2054 1.2314 0.4302  0.3569  0.1397  303 ARG C O   
12277 C CB  . ARG C 303 ? 0.8013 0.8328 0.8869 0.4001  0.3421  0.1349  303 ARG C CB  
12278 C CG  . ARG C 303 ? 0.8087 0.8335 0.9111 0.3879  0.3315  0.1317  303 ARG C CG  
12279 C CD  . ARG C 303 ? 0.7507 0.7959 0.8849 0.3755  0.3328  0.1429  303 ARG C CD  
12280 N NE  . ARG C 303 ? 0.8377 0.8749 0.9849 0.3599  0.3179  0.1389  303 ARG C NE  
12281 C CZ  . ARG C 303 ? 1.0533 1.0702 1.1791 0.3478  0.3065  0.1293  303 ARG C CZ  
12282 N NH1 . ARG C 303 ? 1.1460 1.1481 1.2375 0.3500  0.3086  0.1228  303 ARG C NH1 
12283 N NH2 . ARG C 303 ? 0.9600 0.9714 1.0985 0.3339  0.2929  0.1265  303 ARG C NH2 
12284 N N   . HIS C 304 ? 0.9427 0.9540 0.9556 0.4316  0.3536  0.1246  304 HIS C N   
12285 C CA  . HIS C 304 ? 1.0065 1.0272 1.0063 0.4440  0.3638  0.1297  304 HIS C CA  
12286 C C   . HIS C 304 ? 0.9543 0.9509 0.9119 0.4576  0.3612  0.1174  304 HIS C C   
12287 O O   . HIS C 304 ? 0.9491 0.9503 0.8908 0.4684  0.3689  0.1205  304 HIS C O   
12288 C CB  . HIS C 304 ? 0.9236 0.9572 0.9252 0.4389  0.3712  0.1387  304 HIS C CB  
12289 C CG  . HIS C 304 ? 0.8575 0.9134 0.8997 0.4253  0.3726  0.1506  304 HIS C CG  
12290 N ND1 . HIS C 304 ? 1.0729 1.1525 1.1514 0.4249  0.3765  0.1623  304 HIS C ND1 
12291 C CD2 . HIS C 304 ? 0.9738 1.0305 1.0249 0.4119  0.3695  0.1521  304 HIS C CD2 
12292 C CE1 . HIS C 304 ? 1.2682 1.3619 1.3767 0.4113  0.3752  0.1705  304 HIS C CE1 
12293 N NE2 . HIS C 304 ? 0.9428 1.0236 1.0361 0.4033  0.3712  0.1647  304 HIS C NE2 
12294 N N   . GLY C 305 ? 1.0927 1.0637 1.0327 0.4572  0.3501  0.1040  305 GLY C N   
12295 C CA  . GLY C 305 ? 1.1546 1.1004 1.0552 0.4693  0.3455  0.0916  305 GLY C CA  
12296 C C   . GLY C 305 ? 1.0366 0.9691 0.9031 0.4727  0.3466  0.0872  305 GLY C C   
12297 O O   . GLY C 305 ? 1.1523 1.0698 0.9879 0.4853  0.3453  0.0800  305 GLY C O   
12298 N N   . ILE C 306 ? 1.1513 1.0881 1.0220 0.4618  0.3482  0.0909  306 ILE C N   
12299 C CA  . ILE C 306 ? 1.1266 1.0504 0.9653 0.4641  0.3486  0.0867  306 ILE C CA  
12300 C C   . ILE C 306 ? 1.1099 0.9985 0.9133 0.4664  0.3359  0.0703  306 ILE C C   
12301 O O   . ILE C 306 ? 1.2524 1.1281 1.0609 0.4590  0.3267  0.0638  306 ILE C O   
12302 C CB  . ILE C 306 ? 0.9948 0.9304 0.8475 0.4507  0.3520  0.0939  306 ILE C CB  
12303 C CG1 . ILE C 306 ? 0.9462 0.9150 0.8281 0.4506  0.3647  0.1107  306 ILE C CG1 
12304 C CG2 . ILE C 306 ? 1.0656 0.9811 0.8834 0.4505  0.3486  0.0862  306 ILE C CG2 
12305 C CD1 . ILE C 306 ? 1.3576 1.3341 1.2231 0.4648  0.3740  0.1159  306 ILE C CD1 
12306 N N   . LYS C 307 ? 1.0557 0.9284 0.8237 0.4770  0.3348  0.0639  307 LYS C N   
12307 C CA  . LYS C 307 ? 1.0955 0.9338 0.8289 0.4800  0.3219  0.0485  307 LYS C CA  
12308 C C   . LYS C 307 ? 1.1793 1.0011 0.9052 0.4662  0.3137  0.0426  307 LYS C C   
12309 O O   . LYS C 307 ? 1.2652 1.0991 0.9996 0.4581  0.3193  0.0491  307 LYS C O   
12310 C CB  . LYS C 307 ? 1.2547 1.0815 0.9533 0.4952  0.3226  0.0441  307 LYS C CB  
12311 C CG  . LYS C 307 ? 1.3176 1.1601 1.0218 0.5101  0.3308  0.0500  307 LYS C CG  
12312 C CD  . LYS C 307 ? 1.4340 1.2849 1.1212 0.5218  0.3398  0.0554  307 LYS C CD  
12313 C CE  . LYS C 307 ? 1.5340 1.4144 1.2463 0.5156  0.3526  0.0704  307 LYS C CE  
12314 N NZ  . LYS C 307 ? 1.5965 1.5069 1.3453 0.5166  0.3627  0.0833  307 LYS C NZ  
12315 N N   . ILE C 308 ? 1.2551 1.0496 0.9660 0.4632  0.3004  0.0307  308 ILE C N   
12316 C CA  . ILE C 308 ? 1.0400 0.8163 0.7427 0.4504  0.2915  0.0245  308 ILE C CA  
12317 C C   . ILE C 308 ? 1.0682 0.8161 0.7303 0.4549  0.2831  0.0138  308 ILE C C   
12318 O O   . ILE C 308 ? 1.1943 0.9209 0.8335 0.4639  0.2746  0.0047  308 ILE C O   
12319 C CB  . ILE C 308 ? 1.1606 0.9240 0.8740 0.4432  0.2814  0.0191  308 ILE C CB  
12320 C CG1 . ILE C 308 ? 1.2665 1.0577 1.0220 0.4374  0.2884  0.0298  308 ILE C CG1 
12321 C CG2 . ILE C 308 ? 1.1238 0.8671 0.8264 0.4266  0.2682  0.0127  308 ILE C CG2 
12322 C CD1 . ILE C 308 ? 1.0525 0.8354 0.8194 0.4352  0.2795  0.0259  308 ILE C CD1 
12323 N N   . ALA C 309 ? 1.1530 0.8997 0.8063 0.4483  0.2845  0.0146  309 ALA C N   
12324 C CA  . ALA C 309 ? 1.1707 0.8906 0.7864 0.4515  0.2758  0.0048  309 ALA C CA  
12325 C C   . ALA C 309 ? 1.1345 0.8232 0.7353 0.4440  0.2600  -0.0067 309 ALA C C   
12326 O O   . ALA C 309 ? 1.2230 0.8847 0.7938 0.4504  0.2491  -0.0168 309 ALA C O   
12327 C CB  . ALA C 309 ? 1.3016 1.0310 0.9143 0.4463  0.2822  0.0099  309 ALA C CB  
12328 N N   . GLY C 310 ? 1.1232 0.8177 0.7475 0.4260  0.2554  -0.0037 310 GLY C N   
12329 C CA  . GLY C 310 ? 1.1080 0.7784 0.7244 0.4116  0.2370  -0.0116 310 GLY C CA  
12330 C C   . GLY C 310 ? 1.1757 0.8588 0.8201 0.3886  0.2323  -0.0059 310 GLY C C   
12331 O O   . GLY C 310 ? 1.1784 0.8884 0.8483 0.3831  0.2427  0.0040  310 GLY C O   
12332 N N   . ASN C 311 ? 1.1425 0.8060 0.7819 0.3753  0.2162  -0.0118 311 ASN C N   
12333 C CA  . ASN C 311 ? 1.1395 0.8120 0.8024 0.3540  0.2101  -0.0074 311 ASN C CA  
12334 C C   . ASN C 311 ? 1.1327 0.7991 0.7862 0.3401  0.2042  -0.0082 311 ASN C C   
12335 O O   . ASN C 311 ? 1.1816 0.8370 0.8108 0.3470  0.2051  -0.0121 311 ASN C O   
12336 C CB  . ASN C 311 ? 1.1070 0.7658 0.7748 0.3478  0.1974  -0.0115 311 ASN C CB  
12337 C CG  . ASN C 311 ? 1.2547 0.8804 0.8924 0.3511  0.1835  -0.0220 311 ASN C CG  
12338 O OD1 . ASN C 311 ? 1.4438 1.0543 1.0562 0.3547  0.1806  -0.0270 311 ASN C OD1 
12339 N ND2 . ASN C 311 ? 1.2315 0.8450 0.8716 0.3499  0.1741  -0.0256 311 ASN C ND2 
12340 N N   . PHE C 312 ? 1.1816 0.8557 0.8544 0.3213  0.1985  -0.0043 312 PHE C N   
12341 C CA  . PHE C 312 ? 1.1903 0.8622 0.8594 0.3064  0.1931  -0.0038 312 PHE C CA  
12342 C C   . PHE C 312 ? 1.1804 0.8280 0.8164 0.3094  0.1860  -0.0116 312 PHE C C   
12343 O O   . PHE C 312 ? 1.3021 0.9555 0.9300 0.3119  0.1929  -0.0100 312 PHE C O   
12344 C CB  . PHE C 312 ? 1.2410 0.9123 0.9261 0.2881  0.1820  -0.0026 312 PHE C CB  
12345 C CG  . PHE C 312 ? 1.0667 0.7404 0.7524 0.2726  0.1778  -0.0006 312 PHE C CG  
12346 C CD1 . PHE C 312 ? 1.1692 0.8648 0.8683 0.2692  0.1878  0.0062  312 PHE C CD1 
12347 C CD2 . PHE C 312 ? 1.0578 0.7121 0.7311 0.2617  0.1638  -0.0052 312 PHE C CD2 
12348 C CE1 . PHE C 312 ? 1.1350 0.8324 0.8338 0.2556  0.1838  0.0076  312 PHE C CE1 
12349 C CE2 . PHE C 312 ? 1.0538 0.7110 0.7278 0.2480  0.1602  -0.0032 312 PHE C CE2 
12350 C CZ  . PHE C 312 ? 1.1535 0.8320 0.8398 0.2452  0.1702  0.0029  312 PHE C CZ  
12351 N N   . MET C 313 ? 1.2107 0.8311 0.8278 0.3087  0.1719  -0.0196 313 MET C N   
12352 C CA  . MET C 313 ? 1.0662 0.6625 0.6531 0.3104  0.1635  -0.0269 313 MET C CA  
12353 C C   . MET C 313 ? 1.1519 0.7395 0.7139 0.3311  0.1701  -0.0316 313 MET C C   
12354 O O   . MET C 313 ? 1.2462 0.8141 0.7823 0.3338  0.1635  -0.0377 313 MET C O   
12355 C CB  . MET C 313 ? 1.0725 0.6417 0.6475 0.3038  0.1456  -0.0336 313 MET C CB  
12356 C CG  . MET C 313 ? 1.0534 0.6259 0.6437 0.2824  0.1369  -0.0299 313 MET C CG  
12357 S SD  . MET C 313 ? 1.3197 0.8626 0.8991 0.2739  0.1164  -0.0357 313 MET C SD  
12358 C CE  . MET C 313 ? 1.3059 0.8269 0.8580 0.2715  0.1069  -0.0413 313 MET C CE  
12359 N N   . GLN C 314 ? 1.1500 0.7525 0.7195 0.3458  0.1832  -0.0285 314 GLN C N   
12360 C CA  . GLN C 314 ? 1.0754 0.6720 0.6216 0.3670  0.1911  -0.0321 314 GLN C CA  
12361 C C   . GLN C 314 ? 1.2030 0.8212 0.7535 0.3698  0.2059  -0.0252 314 GLN C C   
12362 O O   . GLN C 314 ? 1.2352 0.8488 0.7642 0.3864  0.2127  -0.0276 314 GLN C O   
12363 C CB  . GLN C 314 ? 1.1017 0.7034 0.6528 0.3833  0.1981  -0.0320 314 GLN C CB  
12364 C CG  . GLN C 314 ? 1.1852 0.7616 0.7250 0.3854  0.1838  -0.0402 314 GLN C CG  
12365 C CD  . GLN C 314 ? 1.3190 0.8955 0.8529 0.4066  0.1911  -0.0422 314 GLN C CD  
12366 O OE1 . GLN C 314 ? 1.2640 0.8645 0.8220 0.4102  0.2027  -0.0351 314 GLN C OE1 
12367 N NE2 . GLN C 314 ? 1.4532 1.0033 0.9552 0.4216  0.1841  -0.0519 314 GLN C NE2 
12368 N N   . GLN C 315 ? 1.1318 0.7732 0.7092 0.3544  0.2108  -0.0165 315 GLN C N   
12369 C CA  . GLN C 315 ? 1.0127 0.6757 0.5969 0.3557  0.2245  -0.0090 315 GLN C CA  
12370 C C   . GLN C 315 ? 1.2718 0.9201 0.8266 0.3601  0.2228  -0.0138 315 GLN C C   
12371 O O   . GLN C 315 ? 1.3868 1.0473 0.9367 0.3710  0.2357  -0.0098 315 GLN C O   
12372 C CB  . GLN C 315 ? 1.0479 0.7337 0.6640 0.3367  0.2264  -0.0003 315 GLN C CB  
12373 C CG  . GLN C 315 ? 1.0549 0.7290 0.6682 0.3178  0.2127  -0.0034 315 GLN C CG  
12374 C CD  . GLN C 315 ? 1.0139 0.7110 0.6589 0.3013  0.2148  0.0051  315 GLN C CD  
12375 O OE1 . GLN C 315 ? 1.1788 0.8902 0.8308 0.2956  0.2208  0.0104  315 GLN C OE1 
12376 N NE2 . GLN C 315 ? 1.1709 0.8718 0.8354 0.2938  0.2097  0.0065  315 GLN C NE2 
12377 N N   . GLU C 316 ? 1.3208 0.9441 0.8572 0.3514  0.2072  -0.0217 316 GLU C N   
12378 C CA  . GLU C 316 ? 1.2728 0.8796 0.7797 0.3559  0.2041  -0.0271 316 GLU C CA  
12379 C C   . GLU C 316 ? 1.3787 0.9671 0.8551 0.3791  0.2053  -0.0345 316 GLU C C   
12380 O O   . GLU C 316 ? 1.2727 0.8627 0.7321 0.3913  0.2139  -0.0343 316 GLU C O   
12381 C CB  . GLU C 316 ? 1.1550 0.7407 0.6523 0.3397  0.1865  -0.0327 316 GLU C CB  
12382 C CG  . GLU C 316 ? 1.3737 0.9769 0.8968 0.3181  0.1855  -0.0258 316 GLU C CG  
12383 C CD  . GLU C 316 ? 1.3588 0.9428 0.8756 0.3020  0.1682  -0.0304 316 GLU C CD  
12384 O OE1 . GLU C 316 ? 1.2985 0.8701 0.8182 0.2970  0.1574  -0.0334 316 GLU C OE1 
12385 O OE2 . GLU C 316 ? 1.3798 0.9617 0.8891 0.2946  0.1656  -0.0305 316 GLU C OE2 
12386 N N   . LEU C 317 ? 1.3058 0.8772 0.7752 0.3854  0.1969  -0.0407 317 LEU C N   
12387 C CA  . LEU C 317 ? 1.2593 0.8106 0.6981 0.4078  0.1961  -0.0488 317 LEU C CA  
12388 C C   . LEU C 317 ? 1.2684 0.8409 0.7099 0.4273  0.2157  -0.0430 317 LEU C C   
12389 O O   . LEU C 317 ? 1.3672 0.9329 0.7878 0.4405  0.2143  -0.0458 317 LEU C O   
12390 C CB  . LEU C 317 ? 1.2279 0.7574 0.6611 0.4095  0.1826  -0.0561 317 LEU C CB  
12391 C CG  . LEU C 317 ? 1.2193 0.7256 0.6480 0.3918  0.1624  -0.0617 317 LEU C CG  
12392 C CD1 . LEU C 317 ? 1.3128 0.8057 0.7459 0.3907  0.1518  -0.0656 317 LEU C CD1 
12393 C CD2 . LEU C 317 ? 1.3556 0.8332 0.7499 0.3968  0.1511  -0.0707 317 LEU C CD2 
12394 N N   . ALA C 318 ? 1.2169 0.8217 0.6916 0.4218  0.2292  -0.0319 318 ALA C N   
12395 C CA  . ALA C 318 ? 1.2156 0.8470 0.7013 0.4338  0.2450  -0.0229 318 ALA C CA  
12396 C C   . ALA C 318 ? 1.2666 0.9041 0.7386 0.4370  0.2503  -0.0196 318 ALA C C   
12397 O O   . ALA C 318 ? 1.3244 0.9673 0.7858 0.4507  0.2552  -0.0174 318 ALA C O   
12398 C CB  . ALA C 318 ? 1.1903 0.8524 0.7146 0.4264  0.2574  -0.0118 318 ALA C CB  
12399 N N   . VAL C 319 ? 1.3243 0.9598 0.7956 0.4247  0.2488  -0.0195 319 VAL C N   
12400 C CA  . VAL C 319 ? 1.5048 1.1447 0.9634 0.4259  0.2527  -0.0167 319 VAL C CA  
12401 C C   . VAL C 319 ? 1.5214 1.1316 0.9419 0.4362  0.2402  -0.0273 319 VAL C C   
12402 O O   . VAL C 319 ? 1.3604 0.9750 0.7676 0.4463  0.2446  -0.0248 319 VAL C O   
12403 C CB  . VAL C 319 ? 1.2512 0.8955 0.7191 0.4092  0.2531  -0.0145 319 VAL C CB  
12404 C CG1 . VAL C 319 ? 1.1550 0.8007 0.6078 0.4101  0.2551  -0.0127 319 VAL C CG1 
12405 C CG2 . VAL C 319 ? 1.2495 0.9246 0.7561 0.3993  0.2647  -0.0033 319 VAL C CG2 
12406 N N   . VAL C 320 ? 1.4269 1.0068 0.8308 0.4338  0.2242  -0.0386 320 VAL C N   
12407 C CA  . VAL C 320 ? 1.3643 0.9132 0.7332 0.4423  0.2097  -0.0493 320 VAL C CA  
12408 C C   . VAL C 320 ? 1.4503 1.0017 0.8073 0.4615  0.2130  -0.0488 320 VAL C C   
12409 O O   . VAL C 320 ? 1.4251 0.9601 0.7545 0.4711  0.2061  -0.0540 320 VAL C O   
12410 C CB  . VAL C 320 ? 1.3792 0.8967 0.7377 0.4351  0.1916  -0.0602 320 VAL C CB  
12411 C CG1 . VAL C 320 ? 1.5393 1.0249 0.8635 0.4447  0.1753  -0.0708 320 VAL C CG1 
12412 C CG2 . VAL C 320 ? 1.2317 0.7443 0.5973 0.4170  0.1874  -0.0609 320 VAL C CG2 
12413 N N   . THR C 321 ? 1.2929 0.9911 0.8287 0.4682  0.1148  -0.0292 321 THR C N   
12414 C CA  . THR C 321 ? 1.3155 0.9882 0.8120 0.4883  0.1386  -0.0377 321 THR C CA  
12415 C C   . THR C 321 ? 1.4212 1.0725 0.8468 0.5035  0.1479  -0.0386 321 THR C C   
12416 O O   . THR C 321 ? 1.5581 1.1790 0.9334 0.5212  0.1598  -0.0521 321 THR C O   
12417 C CB  . THR C 321 ? 1.2424 0.9415 0.7786 0.4914  0.1729  -0.0224 321 THR C CB  
12418 O OG1 . THR C 321 ? 1.3227 1.0520 0.8743 0.4855  0.1881  -0.0011 321 THR C OG1 
12419 C CG2 . THR C 321 ? 1.3797 1.0965 0.9788 0.4799  0.1670  -0.0207 321 THR C CG2 
12420 N N   . GLY C 322 ? 1.2674 0.9342 0.6893 0.4971  0.1434  -0.0239 322 GLY C N   
12421 C CA  . GLY C 322 ? 1.3410 0.9903 0.6988 0.5098  0.1511  -0.0198 322 GLY C CA  
12422 C C   . GLY C 322 ? 1.4615 1.1181 0.8071 0.5223  0.1932  -0.0056 322 GLY C C   
12423 O O   . GLY C 322 ? 1.6501 1.2895 0.9368 0.5353  0.2053  -0.0017 322 GLY C O   
12424 N N   . ALA C 323 ? 1.4053 1.0889 0.8073 0.5181  0.2155  0.0038  323 ALA C N   
12425 C CA  . ALA C 323 ? 1.3658 1.0622 0.7695 0.5283  0.2559  0.0184  323 ALA C CA  
12426 C C   . ALA C 323 ? 1.3770 1.1118 0.8313 0.5146  0.2689  0.0439  323 ALA C C   
12427 O O   . ALA C 323 ? 1.3798 1.1276 0.8383 0.5208  0.3014  0.0589  323 ALA C O   
12428 C CB  . ALA C 323 ? 1.2722 0.9695 0.7015 0.5362  0.2726  0.0096  323 ALA C CB  
12429 N N   . VAL C 324 ? 1.3385 1.0916 0.8319 0.4962  0.2448  0.0483  324 VAL C N   
12430 C CA  . VAL C 324 ? 1.2195 1.0056 0.7591 0.4828  0.2552  0.0693  324 VAL C CA  
12431 C C   . VAL C 324 ? 1.2887 1.0644 0.7887 0.4869  0.2595  0.0819  324 VAL C C   
12432 O O   . VAL C 324 ? 1.3790 1.1411 0.8559 0.4845  0.2337  0.0775  324 VAL C O   
12433 C CB  . VAL C 324 ? 1.1656 0.9753 0.7608 0.4627  0.2306  0.0682  324 VAL C CB  
12434 C CG1 . VAL C 324 ? 1.0468 0.8869 0.6842 0.4496  0.2413  0.0871  324 VAL C CG1 
12435 C CG2 . VAL C 324 ? 1.0677 0.8876 0.7014 0.4583  0.2265  0.0590  324 VAL C CG2 
12436 N N   . ASP C 325 ? 1.3591 1.1416 0.8532 0.4930  0.2916  0.0989  325 ASP C N   
12437 C CA  . ASP C 325 ? 1.2752 1.0474 0.7329 0.4968  0.2989  0.1149  325 ASP C CA  
12438 C C   . ASP C 325 ? 1.3164 1.1110 0.8224 0.4792  0.2908  0.1295  325 ASP C C   
12439 O O   . ASP C 325 ? 1.3419 1.1249 0.8277 0.4777  0.2743  0.1346  325 ASP C O   
12440 C CB  . ASP C 325 ? 1.2645 1.0358 0.6991 0.5096  0.3385  0.1287  325 ASP C CB  
12441 C CG  . ASP C 325 ? 1.4385 1.1861 0.8230 0.5290  0.3485  0.1120  325 ASP C CG  
12442 O OD1 . ASP C 325 ? 1.5494 1.2649 0.8676 0.5397  0.3341  0.1010  325 ASP C OD1 
12443 O OD2 . ASP C 325 ? 1.4620 1.2228 0.8757 0.5318  0.3680  0.1093  325 ASP C OD2 
12444 N N   . GLY C 326 ? 1.2598 1.0856 0.8291 0.4664  0.3011  0.1351  326 GLY C N   
12445 C CA  . GLY C 326 ? 1.1050 0.9527 0.7235 0.4490  0.2945  0.1455  326 GLY C CA  
12446 C C   . GLY C 326 ? 1.1621 1.0360 0.8377 0.4344  0.2812  0.1357  326 GLY C C   
12447 O O   . GLY C 326 ? 1.1231 1.0120 0.8234 0.4342  0.2933  0.1334  326 GLY C O   
12448 N N   . LEU C 327 ? 1.2599 1.1399 0.9565 0.4227  0.2567  0.1305  327 LEU C N   
12449 C CA  . LEU C 327 ? 1.0713 0.9771 0.8190 0.4077  0.2434  0.1224  327 LEU C CA  
12450 C C   . LEU C 327 ? 1.0912 1.0168 0.8784 0.3931  0.2451  0.1318  327 LEU C C   
12451 O O   . LEU C 327 ? 1.1263 1.0474 0.9141 0.3891  0.2284  0.1294  327 LEU C O   
12452 C CB  . LEU C 327 ? 0.9473 0.8434 0.6851 0.4071  0.2133  0.1059  327 LEU C CB  
12453 C CG  . LEU C 327 ? 0.8373 0.7591 0.6236 0.3915  0.1984  0.0984  327 LEU C CG  
12454 C CD1 . LEU C 327 ? 0.8696 0.8098 0.6847 0.3879  0.2111  0.0991  327 LEU C CD1 
12455 C CD2 . LEU C 327 ? 0.8618 0.7723 0.6364 0.3918  0.1706  0.0840  327 LEU C CD2 
12456 N N   . ILE C 328 ? 0.9591 0.9059 0.7802 0.3856  0.2652  0.1421  328 ILE C N   
12457 C CA  . ILE C 328 ? 0.9763 0.9400 0.8349 0.3710  0.2681  0.1497  328 ILE C CA  
12458 C C   . ILE C 328 ? 1.0170 1.0074 0.9187 0.3554  0.2537  0.1396  328 ILE C C   
12459 O O   . ILE C 328 ? 1.1967 1.2066 1.1213 0.3509  0.2575  0.1381  328 ILE C O   
12460 C CB  . ILE C 328 ? 0.9820 0.9557 0.8570 0.3690  0.2957  0.1664  328 ILE C CB  
12461 C CG1 . ILE C 328 ? 0.9350 0.8834 0.7630 0.3856  0.3135  0.1779  328 ILE C CG1 
12462 C CG2 . ILE C 328 ? 1.0666 1.0525 0.9783 0.3532  0.2969  0.1731  328 ILE C CG2 
12463 C CD1 . ILE C 328 ? 0.9823 0.9431 0.8232 0.3880  0.3433  0.1922  328 ILE C CD1 
12464 N N   . VAL C 329 ? 0.9380 0.9299 0.8514 0.3474  0.2385  0.1340  329 VAL C N   
12465 C CA  . VAL C 329 ? 1.0021 1.0194 0.9518 0.3329  0.2251  0.1235  329 VAL C CA  
12466 C C   . VAL C 329 ? 1.0140 1.0442 0.9951 0.3194  0.2290  0.1257  329 VAL C C   
12467 O O   . VAL C 329 ? 1.0508 1.0640 1.0230 0.3228  0.2351  0.1331  329 VAL C O   
12468 C CB  . VAL C 329 ? 0.8765 0.8866 0.8141 0.3358  0.2024  0.1112  329 VAL C CB  
12469 C CG1 . VAL C 329 ? 0.9358 0.9326 0.8458 0.3466  0.1961  0.1064  329 VAL C CG1 
12470 C CG2 . VAL C 329 ? 0.8339 0.8241 0.7548 0.3418  0.1949  0.1121  329 VAL C CG2 
12471 N N   . ASP C 330 ? 0.9549 1.0129 0.9701 0.3048  0.2253  0.1196  330 ASP C N   
12472 C CA  . ASP C 330 ? 0.8103 0.8808 0.8553 0.2906  0.2277  0.1180  330 ASP C CA  
12473 C C   . ASP C 330 ? 0.9796 1.0629 1.0365 0.2833  0.2112  0.1030  330 ASP C C   
12474 O O   . ASP C 330 ? 0.9630 1.0317 1.0114 0.2887  0.2033  0.0979  330 ASP C O   
12475 C CB  . ASP C 330 ? 0.8355 0.9280 0.9083 0.2792  0.2399  0.1251  330 ASP C CB  
12476 C CG  . ASP C 330 ? 0.9762 1.0943 1.0626 0.2741  0.2356  0.1230  330 ASP C CG  
12477 O OD1 . ASP C 330 ? 1.2130 1.3478 1.3110 0.2649  0.2228  0.1127  330 ASP C OD1 
12478 O OD2 . ASP C 330 ? 1.1186 1.2404 1.2055 0.2795  0.2460  0.1327  330 ASP C OD2 
12479 N N   . VAL C 331 ? 0.9697 1.0803 1.0459 0.2723  0.2064  0.0974  331 VAL C N   
12480 C CA  . VAL C 331 ? 0.7769 0.9024 0.8646 0.2646  0.1937  0.0840  331 VAL C CA  
12481 C C   . VAL C 331 ? 0.8297 0.9763 0.9224 0.2599  0.1852  0.0814  331 VAL C C   
12482 O O   . VAL C 331 ? 0.8531 1.0077 0.9484 0.2591  0.1896  0.0896  331 VAL C O   
12483 C CB  . VAL C 331 ? 0.6711 0.8103 0.7824 0.2505  0.1975  0.0776  331 VAL C CB  
12484 C CG1 . VAL C 331 ? 0.8247 0.9410 0.9359 0.2537  0.2046  0.0796  331 VAL C CG1 
12485 C CG2 . VAL C 331 ? 0.7998 0.9632 0.9292 0.2376  0.2023  0.0819  331 VAL C CG2 
12486 N N   . GLN C 332 ? 0.8516 1.0073 0.9482 0.2570  0.1742  0.0718  332 GLN C N   
12487 C CA  . GLN C 332 ? 0.7338 0.9106 0.8378 0.2505  0.1658  0.0703  332 GLN C CA  
12488 C C   . GLN C 332 ? 0.7369 0.9021 0.8271 0.2594  0.1605  0.0765  332 GLN C C   
12489 O O   . GLN C 332 ? 0.8683 1.0202 0.9480 0.2670  0.1676  0.0843  332 GLN C O   
12490 C CB  . GLN C 332 ? 0.6883 0.8935 0.8103 0.2356  0.1695  0.0723  332 GLN C CB  
12491 C CG  . GLN C 332 ? 0.6470 0.8652 0.7814 0.2246  0.1724  0.0624  332 GLN C CG  
12492 C CD  . GLN C 332 ? 0.8136 1.0545 0.9615 0.2110  0.1758  0.0656  332 GLN C CD  
12493 O OE1 . GLN C 332 ? 0.6748 0.9321 0.8271 0.2068  0.1727  0.0742  332 GLN C OE1 
12494 N NE2 . GLN C 332 ? 0.7939 1.0355 0.9502 0.2035  0.1809  0.0591  332 GLN C NE2 
12495 N N   . CYS C 333 ? 0.6675 0.8385 0.7600 0.2580  0.1485  0.0725  333 CYS C N   
12496 C CA  . CYS C 333 ? 0.6290 0.7886 0.7118 0.2642  0.1401  0.0757  333 CYS C CA  
12497 C C   . CYS C 333 ? 0.7755 0.9010 0.8304 0.2805  0.1384  0.0753  333 CYS C C   
12498 O O   . CYS C 333 ? 0.7153 0.8269 0.7585 0.2869  0.1346  0.0772  333 CYS C O   
12499 C CB  . CYS C 333 ? 0.7221 0.8947 0.8147 0.2591  0.1439  0.0846  333 CYS C CB  
12500 S SG  . CYS C 333 ? 0.6007 0.8139 0.7197 0.2396  0.1439  0.0867  333 CYS C SG  
12501 N N   . ILE C 334 ? 0.7875 0.8982 0.8303 0.2873  0.1405  0.0727  334 ILE C N   
12502 C CA  . ILE C 334 ? 0.6729 0.7517 0.6844 0.3026  0.1378  0.0731  334 ILE C CA  
12503 C C   . ILE C 334 ? 0.7571 0.8307 0.7668 0.3049  0.1191  0.0653  334 ILE C C   
12504 O O   . ILE C 334 ? 0.8005 0.8803 0.8215 0.3033  0.1161  0.0619  334 ILE C O   
12505 C CB  . ILE C 334 ? 0.6975 0.7636 0.6983 0.3082  0.1505  0.0782  334 ILE C CB  
12506 C CG1 . ILE C 334 ? 0.8438 0.9193 0.8538 0.3039  0.1689  0.0867  334 ILE C CG1 
12507 C CG2 . ILE C 334 ? 0.6592 0.6929 0.6229 0.3241  0.1473  0.0801  334 ILE C CG2 
12508 C CD1 . ILE C 334 ? 0.7296 0.8081 0.7510 0.2991  0.1799  0.0902  334 ILE C CD1 
12509 N N   . MET C 335 ? 0.7102 0.7730 0.7093 0.3084  0.1062  0.0622  335 MET C N   
12510 C CA  . MET C 335 ? 0.6312 0.6910 0.6326 0.3092  0.0863  0.0554  335 MET C CA  
12511 C C   . MET C 335 ? 0.7709 0.8103 0.7509 0.3209  0.0805  0.0545  335 MET C C   
12512 O O   . MET C 335 ? 0.8708 0.8832 0.8154 0.3327  0.0832  0.0572  335 MET C O   
12513 C CB  . MET C 335 ? 0.7740 0.8187 0.7632 0.3115  0.0732  0.0519  335 MET C CB  
12514 C CG  . MET C 335 ? 0.7568 0.8207 0.7710 0.2997  0.0748  0.0543  335 MET C CG  
12515 S SD  . MET C 335 ? 0.8601 0.9016 0.8641 0.3020  0.0572  0.0492  335 MET C SD  
12516 C CE  . MET C 335 ? 0.8288 0.8894 0.8585 0.2913  0.0667  0.0575  335 MET C CE  
12517 N N   . PRO C 336 ? 0.6932 0.7444 0.6928 0.3191  0.0730  0.0517  336 PRO C N   
12518 C CA  . PRO C 336 ? 0.7226 0.7534 0.7030 0.3314  0.0658  0.0532  336 PRO C CA  
12519 C C   . PRO C 336 ? 0.8753 0.8793 0.8215 0.3419  0.0473  0.0512  336 PRO C C   
12520 O O   . PRO C 336 ? 0.9196 0.9026 0.8395 0.3534  0.0423  0.0549  336 PRO C O   
12521 C CB  . PRO C 336 ? 0.7193 0.7719 0.7354 0.3271  0.0587  0.0491  336 PRO C CB  
12522 C CG  . PRO C 336 ? 0.7509 0.8345 0.7995 0.3127  0.0695  0.0461  336 PRO C CG  
12523 C CD  . PRO C 336 ? 0.7413 0.8250 0.7812 0.3070  0.0716  0.0476  336 PRO C CD  
12524 N N   . ALA C 337 ? 0.7951 0.7984 0.7405 0.3377  0.0363  0.0454  337 ALA C N   
12525 C CA  . ALA C 337 ? 0.8475 0.8235 0.7590 0.3465  0.0171  0.0405  337 ALA C CA  
12526 C C   . ALA C 337 ? 0.9512 0.8957 0.8118 0.3600  0.0279  0.0439  337 ALA C C   
12527 O O   . ALA C 337 ? 0.9616 0.8803 0.7843 0.3704  0.0133  0.0409  337 ALA C O   
12528 C CB  . ALA C 337 ? 0.8068 0.7859 0.7301 0.3381  0.0062  0.0334  337 ALA C CB  
12529 N N   . LEU C 338 ? 0.8717 0.8195 0.7309 0.3596  0.0532  0.0505  338 LEU C N   
12530 C CA  . LEU C 338 ? 1.0386 0.9610 0.8543 0.3719  0.0683  0.0554  338 LEU C CA  
12531 C C   . LEU C 338 ? 1.0967 0.9994 0.8798 0.3836  0.0656  0.0621  338 LEU C C   
12532 O O   . LEU C 338 ? 1.1533 1.0298 0.8893 0.3958  0.0710  0.0643  338 LEU C O   
12533 C CB  . LEU C 338 ? 0.9055 0.8420 0.7373 0.3676  0.0958  0.0635  338 LEU C CB  
12534 C CG  . LEU C 338 ? 0.8351 0.7877 0.6921 0.3588  0.1009  0.0603  338 LEU C CG  
12535 C CD1 . LEU C 338 ? 0.8069 0.7800 0.6881 0.3523  0.1239  0.0694  338 LEU C CD1 
12536 C CD2 . LEU C 338 ? 0.9657 0.8937 0.7910 0.3684  0.0995  0.0542  338 LEU C CD2 
12537 N N   . ALA C 339 ? 0.9207 0.8352 0.7274 0.3807  0.0582  0.0657  339 ALA C N   
12538 C CA  . ALA C 339 ? 0.9932 0.8887 0.7725 0.3920  0.0537  0.0744  339 ALA C CA  
12539 C C   . ALA C 339 ? 1.1216 0.9960 0.8652 0.4009  0.0263  0.0682  339 ALA C C   
12540 O O   . ALA C 339 ? 1.2432 1.0908 0.9368 0.4134  0.0255  0.0739  339 ALA C O   
12541 C CB  . ALA C 339 ? 0.9902 0.9036 0.8097 0.3872  0.0520  0.0786  339 ALA C CB  
12542 N N   . LYS C 340 ? 1.0565 0.9435 0.8250 0.3938  0.0038  0.0569  340 LYS C N   
12543 C CA  . LYS C 340 ? 1.0969 0.9670 0.8391 0.3993  -0.0263 0.0491  340 LYS C CA  
12544 C C   . LYS C 340 ? 1.2157 1.0595 0.9111 0.4045  -0.0259 0.0401  340 LYS C C   
12545 O O   . LYS C 340 ? 1.2984 1.1150 0.9442 0.4150  -0.0415 0.0366  340 LYS C O   
12546 C CB  . LYS C 340 ? 1.0070 0.9026 0.7996 0.3876  -0.0478 0.0406  340 LYS C CB  
12547 C CG  . LYS C 340 ? 0.9983 0.8811 0.7747 0.3900  -0.0823 0.0317  340 LYS C CG  
12548 C CD  . LYS C 340 ? 1.0198 0.9327 0.8548 0.3765  -0.1000 0.0257  340 LYS C CD  
12549 C CE  . LYS C 340 ? 1.0591 0.9608 0.8845 0.3754  -0.1348 0.0155  340 LYS C CE  
12550 N NZ  . LYS C 340 ? 1.2594 1.1560 1.0739 0.3848  -0.1592 0.0201  340 LYS C NZ  
12551 N N   . LEU C 341 ? 1.1320 0.9836 0.8428 0.3979  -0.0085 0.0359  341 LEU C N   
12552 C CA  . LEU C 341 ? 1.1736 1.0008 0.8468 0.4036  -0.0050 0.0264  341 LEU C CA  
12553 C C   . LEU C 341 ? 1.1859 0.9873 0.8018 0.4191  0.0138  0.0329  341 LEU C C   
12554 O O   . LEU C 341 ? 1.2981 1.0697 0.8613 0.4297  0.0044  0.0245  341 LEU C O   
12555 C CB  . LEU C 341 ? 0.9409 0.7859 0.6511 0.3935  0.0116  0.0243  341 LEU C CB  
12556 C CG  . LEU C 341 ? 0.9697 0.7916 0.6525 0.3992  0.0165  0.0140  341 LEU C CG  
12557 C CD1 . LEU C 341 ? 0.9926 0.7998 0.6715 0.3956  -0.0137 -0.0017 341 LEU C CD1 
12558 C CD2 . LEU C 341 ? 1.0539 0.8956 0.7735 0.3918  0.0381  0.0182  341 LEU C CD2 
12559 N N   . SER C 342 ? 1.1273 0.9396 0.7526 0.4201  0.0403  0.0478  342 SER C N   
12560 C CA  . SER C 342 ? 1.0508 0.8422 0.6268 0.4336  0.0617  0.0573  342 SER C CA  
12561 C C   . SER C 342 ? 1.3138 1.0789 0.8353 0.4458  0.0449  0.0602  342 SER C C   
12562 O O   . SER C 342 ? 1.5256 1.2687 0.9945 0.4584  0.0600  0.0660  342 SER C O   
12563 C CB  . SER C 342 ? 1.1513 0.9612 0.7558 0.4295  0.0888  0.0743  342 SER C CB  
12564 O OG  . SER C 342 ? 1.4053 1.2375 1.0510 0.4199  0.1061  0.0728  342 SER C OG  
12565 N N   . LYS C 343 ? 1.2245 0.9931 0.7580 0.4426  0.0143  0.0573  343 LYS C N   
12566 C CA  . LYS C 343 ? 1.3103 1.0556 0.7938 0.4539  -0.0059 0.0612  343 LYS C CA  
12567 C C   . LYS C 343 ? 1.4007 1.1165 0.8261 0.4621  -0.0215 0.0446  343 LYS C C   
12568 O O   . LYS C 343 ? 1.4842 1.1736 0.8457 0.4753  -0.0242 0.0485  343 LYS C O   
12569 C CB  . LYS C 343 ? 1.4386 1.1996 0.9592 0.4485  -0.0347 0.0635  343 LYS C CB  
12570 C CG  . LYS C 343 ? 1.3787 1.1612 0.9451 0.4442  -0.0192 0.0797  343 LYS C CG  
12571 C CD  . LYS C 343 ? 1.4206 1.2110 1.0098 0.4452  -0.0455 0.0853  343 LYS C CD  
12572 C CE  . LYS C 343 ? 1.5788 1.3824 1.2043 0.4440  -0.0284 0.1010  343 LYS C CE  
12573 N NZ  . LYS C 343 ? 1.5259 1.3051 1.1058 0.4556  -0.0139 0.1198  343 LYS C NZ  
12574 N N   . SER C 344 ? 1.3949 1.1132 0.8399 0.4545  -0.0312 0.0262  344 SER C N   
12575 C CA  . SER C 344 ? 1.4418 1.1293 0.8353 0.4613  -0.0466 0.0071  344 SER C CA  
12576 C C   . SER C 344 ? 1.5087 1.1744 0.8540 0.4736  -0.0154 0.0043  344 SER C C   
12577 O O   . SER C 344 ? 1.5771 1.2131 0.8715 0.4819  -0.0240 -0.0127 344 SER C O   
12578 C CB  . SER C 344 ? 1.2384 0.9345 0.6745 0.4481  -0.0668 -0.0103 344 SER C CB  
12579 O OG  . SER C 344 ? 1.4879 1.2093 0.9752 0.4365  -0.0912 -0.0065 344 SER C OG  
12580 N N   . TYR C 345 ? 1.4557 1.1364 0.8185 0.4747  0.0205  0.0200  345 TYR C N   
12581 C CA  . TYR C 345 ? 1.3810 1.0476 0.7082 0.4863  0.0538  0.0203  345 TYR C CA  
12582 C C   . TYR C 345 ? 1.4304 1.1006 0.7395 0.4933  0.0806  0.0441  345 TYR C C   
12583 O O   . TYR C 345 ? 1.4048 1.0885 0.7364 0.4879  0.0734  0.0593  345 TYR C O   
12584 C CB  . TYR C 345 ? 1.3574 1.0437 0.7383 0.4782  0.0728  0.0160  345 TYR C CB  
12585 C CG  . TYR C 345 ? 1.2798 0.9628 0.6842 0.4699  0.0480  -0.0042 345 TYR C CG  
12586 C CD1 . TYR C 345 ? 1.3941 1.0479 0.7616 0.4788  0.0458  -0.0238 345 TYR C CD1 
12587 C CD2 . TYR C 345 ? 1.3338 1.0423 0.7981 0.4531  0.0276  -0.0037 345 TYR C CD2 
12588 C CE1 . TYR C 345 ? 1.2771 0.9252 0.6686 0.4702  0.0224  -0.0415 345 TYR C CE1 
12589 C CE2 . TYR C 345 ? 1.4576 1.1637 0.9458 0.4442  0.0054  -0.0198 345 TYR C CE2 
12590 C CZ  . TYR C 345 ? 1.3858 1.0607 0.8386 0.4522  0.0021  -0.0382 345 TYR C CZ  
12591 O OH  . TYR C 345 ? 1.4336 1.1035 0.9126 0.4424  -0.0203 -0.0533 345 TYR C OH  
12592 N N   . HIS C 346 ? 1.4989 1.1578 0.7728 0.5050  0.1129  0.0477  346 HIS C N   
12593 C CA  . HIS C 346 ? 1.6037 1.2662 0.8623 0.5108  0.1418  0.0724  346 HIS C CA  
12594 C C   . HIS C 346 ? 1.5938 1.2905 0.9249 0.4982  0.1646  0.0864  346 HIS C C   
12595 O O   . HIS C 346 ? 1.6246 1.3282 0.9581 0.4990  0.1876  0.1079  346 HIS C O   
12596 C CB  . HIS C 346 ? 1.6249 1.2647 0.8186 0.5282  0.1696  0.0716  346 HIS C CB  
12597 C CG  . HIS C 346 ? 1.5485 1.2035 0.7740 0.5290  0.2043  0.0715  346 HIS C CG  
12598 N ND1 . HIS C 346 ? 1.3829 1.0441 0.6434 0.5247  0.1999  0.0529  346 HIS C ND1 
12599 C CD2 . HIS C 346 ? 1.6279 1.2945 0.8591 0.5333  0.2429  0.0892  346 HIS C CD2 
12600 C CE1 . HIS C 346 ? 1.4072 1.0835 0.6932 0.5274  0.2341  0.0592  346 HIS C CE1 
12601 N NE2 . HIS C 346 ? 1.5937 1.2746 0.8636 0.5324  0.2607  0.0807  346 HIS C NE2 
12602 N N   . THR C 347 ? 1.5731 1.2902 0.9612 0.4861  0.1575  0.0753  347 THR C N   
12603 C CA  . THR C 347 ? 1.2767 1.0269 0.7314 0.4737  0.1778  0.0865  347 THR C CA  
12604 C C   . THR C 347 ? 1.3990 1.1627 0.8793 0.4656  0.1763  0.1046  347 THR C C   
12605 O O   . THR C 347 ? 1.4318 1.1888 0.9053 0.4643  0.1494  0.1029  347 THR C O   
12606 C CB  . THR C 347 ? 1.2855 1.0547 0.7929 0.4612  0.1643  0.0725  347 THR C CB  
12607 O OG1 . THR C 347 ? 1.3027 1.0545 0.7854 0.4699  0.1653  0.0562  347 THR C OG1 
12608 C CG2 . THR C 347 ? 1.3883 1.1912 0.9586 0.4486  0.1830  0.0828  347 THR C CG2 
12609 N N   . LYS C 348 ? 1.3903 1.1717 0.9012 0.4606  0.2036  0.1209  348 LYS C N   
12610 C CA  . LYS C 348 ? 1.3140 1.1061 0.8540 0.4521  0.2039  0.1371  348 LYS C CA  
12611 C C   . LYS C 348 ? 1.4041 1.2283 1.0150 0.4346  0.2025  0.1336  348 LYS C C   
12612 O O   . LYS C 348 ? 1.3547 1.1968 0.9944 0.4293  0.2242  0.1370  348 LYS C O   
12613 C CB  . LYS C 348 ? 1.1191 0.9061 0.6425 0.4572  0.2346  0.1590  348 LYS C CB  
12614 C CG  . LYS C 348 ? 1.5192 1.2795 0.9888 0.4684  0.2303  0.1728  348 LYS C CG  
12615 C CD  . LYS C 348 ? 1.6356 1.3903 1.0850 0.4739  0.2639  0.1956  348 LYS C CD  
12616 C CE  . LYS C 348 ? 1.5031 1.2535 0.9641 0.4695  0.2648  0.2179  348 LYS C CE  
12617 N NZ  . LYS C 348 ? 1.5371 1.2905 1.0012 0.4689  0.3006  0.2410  348 LYS C NZ  
12618 N N   . PHE C 349 ? 1.3258 1.1582 0.9634 0.4265  0.1779  0.1271  349 PHE C N   
12619 C CA  . PHE C 349 ? 1.1489 1.0119 0.8492 0.4101  0.1759  0.1224  349 PHE C CA  
12620 C C   . PHE C 349 ? 1.0696 0.9410 0.7977 0.4031  0.1895  0.1369  349 PHE C C   
12621 O O   . PHE C 349 ? 1.0947 0.9576 0.8221 0.4046  0.1772  0.1413  349 PHE C O   
12622 C CB  . PHE C 349 ? 1.0269 0.8962 0.7440 0.4051  0.1461  0.1086  349 PHE C CB  
12623 C CG  . PHE C 349 ? 0.8957 0.7961 0.6685 0.3894  0.1438  0.1011  349 PHE C CG  
12624 C CD1 . PHE C 349 ? 1.1010 1.0181 0.8950 0.3827  0.1593  0.1000  349 PHE C CD1 
12625 C CD2 . PHE C 349 ? 0.9220 0.8360 0.7257 0.3820  0.1264  0.0957  349 PHE C CD2 
12626 C CE1 . PHE C 349 ? 1.0226 0.9685 0.8631 0.3681  0.1563  0.0945  349 PHE C CE1 
12627 C CE2 . PHE C 349 ? 0.8338 0.7769 0.6838 0.3678  0.1259  0.0890  349 PHE C CE2 
12628 C CZ  . PHE C 349 ? 0.8634 0.8218 0.7295 0.3605  0.1403  0.0887  349 PHE C CZ  
12629 N N   . ILE C 350 ? 0.9960 0.8831 0.7503 0.3958  0.2128  0.1441  350 ILE C N   
12630 C CA  . ILE C 350 ? 1.0116 0.9035 0.7921 0.3882  0.2265  0.1581  350 ILE C CA  
12631 C C   . ILE C 350 ? 0.9659 0.8864 0.8029 0.3710  0.2234  0.1500  350 ILE C C   
12632 O O   . ILE C 350 ? 1.1497 1.0909 1.0090 0.3636  0.2322  0.1463  350 ILE C O   
12633 C CB  . ILE C 350 ? 1.0228 0.9108 0.7913 0.3918  0.2556  0.1746  350 ILE C CB  
12634 C CG1 . ILE C 350 ? 1.0853 0.9448 0.7914 0.4096  0.2604  0.1822  350 ILE C CG1 
12635 C CG2 . ILE C 350 ? 1.0221 0.9146 0.8225 0.3816  0.2686  0.1889  350 ILE C CG2 
12636 C CD1 . ILE C 350 ? 1.0587 0.9190 0.7496 0.4157  0.2900  0.1928  350 ILE C CD1 
12637 N N   . THR C 351 ? 0.9149 0.8362 0.7731 0.3657  0.2115  0.1473  351 THR C N   
12638 C CA  . THR C 351 ? 0.8535 0.8004 0.7612 0.3496  0.2099  0.1383  351 THR C CA  
12639 C C   . THR C 351 ? 0.9826 0.9301 0.9125 0.3414  0.2283  0.1500  351 THR C C   
12640 O O   . THR C 351 ? 1.0550 0.9796 0.9676 0.3483  0.2344  0.1639  351 THR C O   
12641 C CB  . THR C 351 ? 0.7680 0.7167 0.6896 0.3489  0.1892  0.1271  351 THR C CB  
12642 O OG1 . THR C 351 ? 1.0284 0.9517 0.9317 0.3591  0.1853  0.1370  351 THR C OG1 
12643 C CG2 . THR C 351 ? 0.7593 0.7144 0.6713 0.3524  0.1707  0.1147  351 THR C CG2 
12644 N N   . THR C 352 ? 0.9801 0.9520 0.9471 0.3264  0.2356  0.1455  352 THR C N   
12645 C CA  . THR C 352 ? 0.9376 0.9101 0.9276 0.3169  0.2527  0.1570  352 THR C CA  
12646 C C   . THR C 352 ? 0.8826 0.8691 0.9135 0.3011  0.2477  0.1459  352 THR C C   
12647 O O   . THR C 352 ? 0.9568 0.9346 1.0053 0.2943  0.2570  0.1536  352 THR C O   
12648 C CB  . THR C 352 ? 0.8801 0.8681 0.8761 0.3136  0.2702  0.1657  352 THR C CB  
12649 O OG1 . THR C 352 ? 1.0196 1.0354 1.0360 0.3051  0.2628  0.1529  352 THR C OG1 
12650 C CG2 . THR C 352 ? 1.0508 1.0229 1.0053 0.3300  0.2799  0.1764  352 THR C CG2 
12651 N N   . SER C 353 ? 0.8060 0.8127 0.8510 0.2951  0.2344  0.1285  353 SER C N   
12652 C CA  . SER C 353 ? 0.8179 0.8394 0.8972 0.2801  0.2312  0.1160  353 SER C CA  
12653 C C   . SER C 353 ? 0.9025 0.9108 0.9853 0.2846  0.2200  0.1059  353 SER C C   
12654 O O   . SER C 353 ? 0.9234 0.9308 0.9920 0.2941  0.2077  0.1001  353 SER C O   
12655 C CB  . SER C 353 ? 0.9097 0.9634 1.0028 0.2701  0.2252  0.1040  353 SER C CB  
12656 O OG  . SER C 353 ? 0.8499 0.9194 0.9718 0.2544  0.2238  0.0920  353 SER C OG  
12657 N N   . PRO C 354 ? 0.8675 0.8660 0.9724 0.2778  0.2235  0.1029  354 PRO C N   
12658 C CA  . PRO C 354 ? 0.8527 0.8397 0.9652 0.2837  0.2136  0.0922  354 PRO C CA  
12659 C C   . PRO C 354 ? 0.9840 0.9973 1.1094 0.2788  0.2036  0.0712  354 PRO C C   
12660 O O   . PRO C 354 ? 0.9706 0.9797 1.1038 0.2853  0.1956  0.0613  354 PRO C O   
12661 C CB  . PRO C 354 ? 0.7765 0.7461 0.9120 0.2760  0.2215  0.0932  354 PRO C CB  
12662 C CG  . PRO C 354 ? 0.7089 0.6936 0.8578 0.2600  0.2319  0.0963  354 PRO C CG  
12663 C CD  . PRO C 354 ? 0.8602 0.8579 0.9877 0.2641  0.2357  0.1081  354 PRO C CD  
12664 N N   . LYS C 355 ? 0.8671 0.9086 0.9959 0.2679  0.2045  0.0659  355 LYS C N   
12665 C CA  . LYS C 355 ? 0.7817 0.8507 0.9198 0.2620  0.1967  0.0493  355 LYS C CA  
12666 C C   . LYS C 355 ? 0.7489 0.8214 0.8699 0.2734  0.1862  0.0513  355 LYS C C   
12667 O O   . LYS C 355 ? 0.8481 0.9345 0.9777 0.2741  0.1783  0.0396  355 LYS C O   
12668 C CB  . LYS C 355 ? 0.6161 0.7128 0.7621 0.2464  0.2003  0.0471  355 LYS C CB  
12669 C CG  . LYS C 355 ? 0.7120 0.8088 0.8762 0.2324  0.2083  0.0451  355 LYS C CG  
12670 C CD  . LYS C 355 ? 0.7422 0.8687 0.9135 0.2183  0.2088  0.0454  355 LYS C CD  
12671 C CE  . LYS C 355 ? 0.8699 0.9980 1.0604 0.2036  0.2150  0.0463  355 LYS C CE  
12672 N NZ  . LYS C 355 ? 1.1114 1.2680 1.3091 0.1925  0.2145  0.0524  355 LYS C NZ  
12673 N N   . ALA C 356 ? 0.6797 0.7401 0.7771 0.2819  0.1864  0.0656  356 ALA C N   
12674 C CA  . ALA C 356 ? 0.8564 0.9162 0.9356 0.2920  0.1749  0.0668  356 ALA C CA  
12675 C C   . ALA C 356 ? 0.8909 0.9199 0.9439 0.3079  0.1714  0.0782  356 ALA C C   
12676 O O   . ALA C 356 ? 0.9362 0.9524 0.9652 0.3133  0.1772  0.0899  356 ALA C O   
12677 C CB  . ALA C 356 ? 0.9519 1.0262 1.0225 0.2876  0.1763  0.0705  356 ALA C CB  
12678 N N   . HIS C 357 ? 0.8245 0.8425 0.8820 0.3162  0.1621  0.0750  357 HIS C N   
12679 C CA  . HIS C 357 ? 0.7758 0.7655 0.8079 0.3316  0.1552  0.0864  357 HIS C CA  
12680 C C   . HIS C 357 ? 0.8367 0.8310 0.8558 0.3389  0.1372  0.0821  357 HIS C C   
12681 O O   . HIS C 357 ? 0.9739 0.9878 1.0167 0.3357  0.1279  0.0704  357 HIS C O   
12682 C CB  . HIS C 357 ? 0.8677 0.8430 0.9166 0.3372  0.1528  0.0865  357 HIS C CB  
12683 C CG  . HIS C 357 ? 0.9061 0.8626 0.9587 0.3343  0.1677  0.0965  357 HIS C CG  
12684 N ND1 . HIS C 357 ? 0.9282 0.8548 0.9695 0.3456  0.1665  0.1106  357 HIS C ND1 
12685 C CD2 . HIS C 357 ? 1.1331 1.0971 1.2014 0.3206  0.1826  0.0951  357 HIS C CD2 
12686 C CE1 . HIS C 357 ? 0.8912 0.8073 0.9430 0.3380  0.1819  0.1177  357 HIS C CE1 
12687 N NE2 . HIS C 357 ? 1.0706 1.0090 1.1396 0.3226  0.1914  0.1080  357 HIS C NE2 
12688 N N   . ILE C 358 ? 0.9165 0.8934 0.8990 0.3484  0.1324  0.0908  358 ILE C N   
12689 C CA  . ILE C 358 ? 0.8619 0.8399 0.8310 0.3545  0.1127  0.0857  358 ILE C CA  
12690 C C   . ILE C 358 ? 0.8699 0.8212 0.8121 0.3697  0.0999  0.0948  358 ILE C C   
12691 O O   . ILE C 358 ? 0.9321 0.8597 0.8429 0.3769  0.1084  0.1077  358 ILE C O   
12692 C CB  . ILE C 358 ? 0.8115 0.7921 0.7597 0.3521  0.1145  0.0844  358 ILE C CB  
12693 C CG1 . ILE C 358 ? 0.7702 0.7793 0.7479 0.3369  0.1251  0.0776  358 ILE C CG1 
12694 C CG2 . ILE C 358 ? 0.7891 0.7661 0.7227 0.3578  0.0923  0.0784  358 ILE C CG2 
12695 C CD1 . ILE C 358 ? 0.7091 0.7186 0.6715 0.3349  0.1343  0.0806  358 ILE C CD1 
12696 N N   . THR C 359 ? 0.9238 0.8804 0.8797 0.3745  0.0796  0.0893  359 THR C N   
12697 C CA  . THR C 359 ? 0.9492 0.8832 0.8827 0.3891  0.0631  0.0983  359 THR C CA  
12698 C C   . THR C 359 ? 0.9695 0.8819 0.8497 0.3969  0.0558  0.1037  359 THR C C   
12699 O O   . THR C 359 ? 1.1139 1.0337 0.9850 0.3918  0.0544  0.0953  359 THR C O   
12700 C CB  . THR C 359 ? 0.8955 0.8459 0.8611 0.3914  0.0415  0.0902  359 THR C CB  
12701 O OG1 . THR C 359 ? 0.7938 0.7638 0.8062 0.3850  0.0519  0.0833  359 THR C OG1 
12702 C CG2 . THR C 359 ? 0.8434 0.7734 0.7912 0.4066  0.0214  0.1005  359 THR C CG2 
12703 N N   . ASP C 360 ? 1.0804 0.9651 0.9244 0.4097  0.0516  0.1178  360 ASP C N   
12704 C CA  . ASP C 360 ? 1.1312 0.9919 0.9166 0.4192  0.0454  0.1231  360 ASP C CA  
12705 C C   . ASP C 360 ? 1.0561 0.9137 0.8191 0.4151  0.0688  0.1231  360 ASP C C   
12706 O O   . ASP C 360 ? 1.3060 1.1582 1.0401 0.4170  0.0637  0.1154  360 ASP C O   
12707 C CB  . ASP C 360 ? 1.0614 0.9245 0.8367 0.4220  0.0158  0.1118  360 ASP C CB  
12708 C CG  . ASP C 360 ? 1.3464 1.2091 1.1352 0.4297  -0.0102 0.1153  360 ASP C CG  
12709 O OD1 . ASP C 360 ? 1.4018 1.2626 1.2113 0.4334  -0.0047 0.1259  360 ASP C OD1 
12710 O OD2 . ASP C 360 ? 1.6225 1.4867 1.4037 0.4319  -0.0368 0.1077  360 ASP C OD2 
12711 N N   . SER C 361 ? 1.0163 0.8768 0.7950 0.4096  0.0941  0.1314  361 SER C N   
12712 C CA  . SER C 361 ? 0.9902 0.8513 0.7555 0.4059  0.1181  0.1339  361 SER C CA  
12713 C C   . SER C 361 ? 1.0202 0.8671 0.7768 0.4082  0.1397  0.1528  361 SER C C   
12714 O O   . SER C 361 ? 1.0771 0.9214 0.8572 0.4069  0.1391  0.1600  361 SER C O   
12715 C CB  . SER C 361 ? 0.9086 0.7995 0.7187 0.3909  0.1265  0.1220  361 SER C CB  
12716 O OG  . SER C 361 ? 0.9223 0.8261 0.7736 0.3816  0.1370  0.1244  361 SER C OG  
12717 N N   . ILE C 362 ? 1.0275 0.8649 0.7530 0.4118  0.1596  0.1612  362 ILE C N   
12718 C CA  . ILE C 362 ? 0.9861 0.8114 0.7044 0.4129  0.1824  0.1815  362 ILE C CA  
12719 C C   . ILE C 362 ? 0.9981 0.8459 0.7730 0.3969  0.1966  0.1795  362 ILE C C   
12720 O O   . ILE C 362 ? 1.0857 0.9553 0.8820 0.3882  0.2021  0.1683  362 ILE C O   
12721 C CB  . ILE C 362 ? 1.0774 0.8897 0.7474 0.4219  0.2014  0.1903  362 ILE C CB  
12722 C CG1 . ILE C 362 ? 1.0797 0.8664 0.6866 0.4381  0.1846  0.1906  362 ILE C CG1 
12723 C CG2 . ILE C 362 ? 1.0433 0.8493 0.7155 0.4201  0.2290  0.2126  362 ILE C CG2 
12724 C CD1 . ILE C 362 ? 1.2015 0.9905 0.7886 0.4415  0.1697  0.1696  362 ILE C CD1 
12725 N N   . TYR C 363 ? 0.9414 0.7833 0.7408 0.3928  0.2007  0.1895  363 TYR C N   
12726 C CA  . TYR C 363 ? 0.9305 0.7914 0.7817 0.3768  0.2121  0.1853  363 TYR C CA  
12727 C C   . TYR C 363 ? 1.0300 0.8828 0.8844 0.3725  0.2371  0.2046  363 TYR C C   
12728 O O   . TYR C 363 ? 1.1965 1.0269 1.0432 0.3769  0.2404  0.2212  363 TYR C O   
12729 C CB  . TYR C 363 ? 0.9710 0.8338 0.8583 0.3728  0.1980  0.1771  363 TYR C CB  
12730 C CG  . TYR C 363 ? 0.9758 0.8558 0.9116 0.3561  0.2089  0.1700  363 TYR C CG  
12731 C CD1 . TYR C 363 ? 1.0256 0.9352 0.9860 0.3445  0.2082  0.1529  363 TYR C CD1 
12732 C CD2 . TYR C 363 ? 1.0128 0.8785 0.9688 0.3514  0.2190  0.1809  363 TYR C CD2 
12733 C CE1 . TYR C 363 ? 1.0486 0.9740 1.0489 0.3288  0.2163  0.1455  363 TYR C CE1 
12734 C CE2 . TYR C 363 ? 0.8861 0.7658 0.8848 0.3352  0.2272  0.1722  363 TYR C CE2 
12735 C CZ  . TYR C 363 ? 0.9324 0.8426 0.9514 0.3240  0.2254  0.1540  363 TYR C CZ  
12736 O OH  . TYR C 363 ? 0.9291 0.8533 0.9860 0.3076  0.2316  0.1445  363 TYR C OH  
12737 N N   . MET C 364 ? 0.9475 0.8195 0.8171 0.3633  0.2543  0.2038  364 MET C N   
12738 C CA  . MET C 364 ? 1.0178 0.8883 0.8995 0.3568  0.2788  0.2217  364 MET C CA  
12739 C C   . MET C 364 ? 1.0157 0.9123 0.9515 0.3379  0.2826  0.2113  364 MET C C   
12740 O O   . MET C 364 ? 1.0134 0.9340 0.9610 0.3322  0.2876  0.2039  364 MET C O   
12741 C CB  . MET C 364 ? 1.0183 0.8900 0.8677 0.3648  0.2973  0.2318  364 MET C CB  
12742 C CG  . MET C 364 ? 1.0880 0.9317 0.8781 0.3829  0.2971  0.2442  364 MET C CG  
12743 S SD  . MET C 364 ? 1.2953 1.1404 1.0476 0.3930  0.3243  0.2549  364 MET C SD  
12744 C CE  . MET C 364 ? 1.4726 1.3013 1.1646 0.4109  0.3036  0.2401  364 MET C CE  
12745 N N   . GLU C 365 ? 1.0664 0.9575 1.0344 0.3284  0.2789  0.2100  365 GLU C N   
12746 C CA  . GLU C 365 ? 1.0860 0.9994 1.1023 0.3097  0.2801  0.1979  365 GLU C CA  
12747 C C   . GLU C 365 ? 0.9611 0.8912 0.9958 0.2992  0.3004  0.2088  365 GLU C C   
12748 O O   . GLU C 365 ? 1.0630 0.9798 1.0875 0.3023  0.3175  0.2302  365 GLU C O   
12749 C CB  . GLU C 365 ? 1.2546 1.1515 1.2980 0.3031  0.2756  0.1965  365 GLU C CB  
12750 C CG  . GLU C 365 ? 1.0871 1.0044 1.1746 0.2848  0.2722  0.1780  365 GLU C CG  
12751 C CD  . GLU C 365 ? 1.2239 1.1217 1.3350 0.2810  0.2658  0.1716  365 GLU C CD  
12752 O OE1 . GLU C 365 ? 1.3384 1.2294 1.4438 0.2903  0.2512  0.1598  365 GLU C OE1 
12753 O OE2 . GLU C 365 ? 1.5130 1.4018 1.6508 0.2688  0.2754  0.1783  365 GLU C OE2 
12754 N N   . PHE C 366 ? 0.8517 0.8123 0.9143 0.2868  0.2985  0.1957  366 PHE C N   
12755 C CA  . PHE C 366 ? 0.8868 0.8683 0.9737 0.2764  0.3152  0.2054  366 PHE C CA  
12756 C C   . PHE C 366 ? 0.9291 0.9106 1.0581 0.2581  0.3193  0.2079  366 PHE C C   
12757 O O   . PHE C 366 ? 1.0375 1.0314 1.1931 0.2451  0.3069  0.1900  366 PHE C O   
12758 C CB  . PHE C 366 ? 0.8249 0.8391 0.9234 0.2716  0.3087  0.1916  366 PHE C CB  
12759 C CG  . PHE C 366 ? 0.7319 0.7723 0.8602 0.2616  0.3230  0.2009  366 PHE C CG  
12760 C CD1 . PHE C 366 ? 0.8870 0.9245 1.0073 0.2690  0.3446  0.2213  366 PHE C CD1 
12761 C CD2 . PHE C 366 ? 0.6996 0.7697 0.8634 0.2454  0.3148  0.1896  366 PHE C CD2 
12762 C CE1 . PHE C 366 ? 1.0022 1.0672 1.1556 0.2605  0.3580  0.2305  366 PHE C CE1 
12763 C CE2 . PHE C 366 ? 0.6901 0.7869 0.8847 0.2365  0.3257  0.1992  366 PHE C CE2 
12764 C CZ  . PHE C 366 ? 0.8705 0.9653 1.0625 0.2443  0.3474  0.2196  366 PHE C CZ  
12765 N N   . ASP C 367 ? 0.9471 0.9134 1.0812 0.2566  0.3365  0.2298  367 ASP C N   
12766 C CA  . ASP C 367 ? 0.9541 0.9167 1.1304 0.2381  0.3403  0.2336  367 ASP C CA  
12767 C C   . ASP C 367 ? 0.9808 0.9792 1.1978 0.2201  0.3431  0.2288  367 ASP C C   
12768 O O   . ASP C 367 ? 1.0633 1.0790 1.2878 0.2201  0.3593  0.2445  367 ASP C O   
12769 C CB  . ASP C 367 ? 0.9920 0.9297 1.1642 0.2408  0.3592  0.2619  367 ASP C CB  
12770 C CG  . ASP C 367 ? 1.1708 1.0976 1.3871 0.2216  0.3618  0.2667  367 ASP C CG  
12771 O OD1 . ASP C 367 ? 1.1231 1.0535 1.3661 0.2090  0.3463  0.2448  367 ASP C OD1 
12772 O OD2 . ASP C 367 ? 1.0384 0.9524 1.2622 0.2190  0.3800  0.2924  367 ASP C OD2 
12773 N N   . GLU C 368 ? 1.0876 1.0977 1.3317 0.2050  0.3275  0.2075  368 GLU C N   
12774 C CA  . GLU C 368 ? 0.8758 0.9218 1.1578 0.1867  0.3256  0.2017  368 GLU C CA  
12775 C C   . GLU C 368 ? 1.0377 1.0829 1.3604 0.1697  0.3378  0.2174  368 GLU C C   
12776 O O   . GLU C 368 ? 1.0535 1.1301 1.4097 0.1560  0.3398  0.2199  368 GLU C O   
12777 C CB  . GLU C 368 ? 1.1252 1.1829 1.4167 0.1761  0.3046  0.1734  368 GLU C CB  
12778 C CG  . GLU C 368 ? 1.4146 1.4442 1.7148 0.1696  0.2968  0.1608  368 GLU C CG  
12779 C CD  . GLU C 368 ? 1.3761 1.3766 1.6425 0.1883  0.2919  0.1563  368 GLU C CD  
12780 O OE1 . GLU C 368 ? 1.3537 1.3625 1.5905 0.2025  0.2869  0.1522  368 GLU C OE1 
12781 O OE2 . GLU C 368 ? 1.3000 1.2694 1.5721 0.1885  0.2921  0.1573  368 GLU C OE2 
12782 N N   . GLU C 369 ? 1.0554 1.0665 1.3780 0.1702  0.3447  0.2286  369 GLU C N   
12783 C CA  . GLU C 369 ? 1.1996 1.2069 1.5627 0.1534  0.3572  0.2461  369 GLU C CA  
12784 C C   . GLU C 369 ? 1.1476 1.1701 1.5110 0.1597  0.3813  0.2749  369 GLU C C   
12785 O O   . GLU C 369 ? 1.2501 1.2975 1.6558 0.1441  0.3897  0.2849  369 GLU C O   
12786 C CB  . GLU C 369 ? 1.4466 1.4097 1.8080 0.1537  0.3583  0.2526  369 GLU C CB  
12787 C CG  . GLU C 369 ? 1.4231 1.3702 1.7948 0.1454  0.3377  0.2244  369 GLU C CG  
12788 C CD  . GLU C 369 ? 1.4618 1.3632 1.8348 0.1478  0.3384  0.2309  369 GLU C CD  
12789 O OE1 . GLU C 369 ? 1.4536 1.3332 1.8040 0.1616  0.3517  0.2566  369 GLU C OE1 
12790 O OE2 . GLU C 369 ? 1.6295 1.5160 2.0249 0.1363  0.3257  0.2104  369 GLU C OE2 
12791 N N   . ASN C 370 ? 1.1114 1.1198 1.4278 0.1827  0.3923  0.2874  370 ASN C N   
12792 C CA  . ASN C 370 ? 1.0815 1.1016 1.3875 0.1931  0.4173  0.3124  370 ASN C CA  
12793 C C   . ASN C 370 ? 1.0570 1.0921 1.3253 0.2116  0.4127  0.3006  370 ASN C C   
12794 O O   . ASN C 370 ? 1.0676 1.0812 1.2853 0.2318  0.4148  0.3032  370 ASN C O   
12795 C CB  . ASN C 370 ? 1.1939 1.1786 1.4698 0.2048  0.4341  0.3372  370 ASN C CB  
12796 C CG  . ASN C 370 ? 1.4747 1.4377 1.7857 0.1877  0.4377  0.3502  370 ASN C CG  
12797 O OD1 . ASN C 370 ? 1.5773 1.5575 1.9425 0.1653  0.4367  0.3489  370 ASN C OD1 
12798 N ND2 . ASN C 370 ? 1.6230 1.5469 1.9049 0.1975  0.4407  0.3638  370 ASN C ND2 
12799 N N   . PRO C 371 ? 1.0126 1.0828 1.3043 0.2047  0.4037  0.2866  371 PRO C N   
12800 C CA  . PRO C 371 ? 0.9302 1.0114 1.1888 0.2213  0.3973  0.2747  371 PRO C CA  
12801 C C   . PRO C 371 ? 1.0192 1.1028 1.2498 0.2409  0.4196  0.2911  371 PRO C C   
12802 O O   . PRO C 371 ? 0.9591 1.0262 1.1408 0.2598  0.4161  0.2848  371 PRO C O   
12803 C CB  . PRO C 371 ? 0.8985 1.0169 1.1955 0.2065  0.3831  0.2600  371 PRO C CB  
12804 C CG  . PRO C 371 ? 0.9454 1.0682 1.2882 0.1823  0.3771  0.2585  371 PRO C CG  
12805 C CD  . PRO C 371 ? 0.8701 0.9704 1.2186 0.1810  0.3965  0.2808  371 PRO C CD  
12806 N N   . LEU C 372 ? 1.0840 1.1884 1.3457 0.2367  0.4422  0.3108  372 LEU C N   
12807 C CA  . LEU C 372 ? 0.9943 1.1025 1.2305 0.2563  0.4666  0.3253  372 LEU C CA  
12808 C C   . LEU C 372 ? 1.0551 1.1253 1.2363 0.2724  0.4791  0.3377  372 LEU C C   
12809 O O   . LEU C 372 ? 1.1005 1.1596 1.2324 0.2935  0.4846  0.3353  372 LEU C O   
12810 C CB  . LEU C 372 ? 1.0535 1.1949 1.3412 0.2477  0.4900  0.3453  372 LEU C CB  
12811 C CG  . LEU C 372 ? 0.9286 1.0812 1.1991 0.2680  0.5182  0.3588  372 LEU C CG  
12812 C CD1 . LEU C 372 ? 0.8342 0.9887 1.0724 0.2849  0.5053  0.3387  372 LEU C CD1 
12813 C CD2 . LEU C 372 ? 0.9647 1.1514 1.2944 0.2551  0.5303  0.3732  372 LEU C CD2 
12814 N N   . ASP C 373 ? 1.0394 1.0879 1.2274 0.2627  0.4819  0.3506  373 ASP C N   
12815 C CA  . ASP C 373 ? 1.0521 1.0636 1.1878 0.2773  0.4919  0.3653  373 ASP C CA  
12816 C C   . ASP C 373 ? 1.0613 1.0477 1.1449 0.2917  0.4678  0.3453  373 ASP C C   
12817 O O   . ASP C 373 ? 1.1073 1.0733 1.1343 0.3114  0.4739  0.3504  373 ASP C O   
12818 C CB  . ASP C 373 ? 1.2079 1.1997 1.3678 0.2623  0.4959  0.3828  373 ASP C CB  
12819 C CG  . ASP C 373 ? 1.4132 1.4270 1.6259 0.2468  0.5205  0.4063  373 ASP C CG  
12820 O OD1 . ASP C 373 ? 1.2382 1.2724 1.4480 0.2560  0.5460  0.4205  373 ASP C OD1 
12821 O OD2 . ASP C 373 ? 1.5078 1.5182 1.7664 0.2256  0.5148  0.4102  373 ASP C OD2 
12822 N N   . SER C 374 ? 1.0101 0.9989 1.1124 0.2816  0.4405  0.3224  374 SER C N   
12823 C CA  . SER C 374 ? 0.9563 0.9260 1.0188 0.2931  0.4167  0.3031  374 SER C CA  
12824 C C   . SER C 374 ? 1.0683 1.0481 1.0975 0.3093  0.4154  0.2920  374 SER C C   
12825 O O   . SER C 374 ? 1.1520 1.1097 1.1306 0.3257  0.4072  0.2871  374 SER C O   
12826 C CB  . SER C 374 ? 0.8635 0.8408 0.9595 0.2778  0.3920  0.2809  374 SER C CB  
12827 O OG  . SER C 374 ? 0.9751 0.9307 1.0394 0.2875  0.3711  0.2667  374 SER C OG  
12828 N N   . ALA C 375 ? 1.0578 1.0702 1.1169 0.3047  0.4223  0.2882  375 ALA C N   
12829 C CA  . ALA C 375 ? 1.1262 1.1477 1.1604 0.3195  0.4221  0.2780  375 ALA C CA  
12830 C C   . ALA C 375 ? 1.1642 1.1687 1.1502 0.3398  0.4447  0.2921  375 ALA C C   
12831 O O   . ALA C 375 ? 1.2383 1.2292 1.1787 0.3565  0.4384  0.2811  375 ALA C O   
12832 C CB  . ALA C 375 ? 1.0665 1.1265 1.1493 0.3100  0.4264  0.2753  375 ALA C CB  
12833 N N   . LYS C 376 ? 1.0078 1.0130 1.0032 0.3381  0.4713  0.3160  376 LYS C N   
12834 C CA  . LYS C 376 ? 1.1274 1.1176 1.0747 0.3571  0.4965  0.3313  376 LYS C CA  
12835 C C   . LYS C 376 ? 1.2573 1.2077 1.1400 0.3700  0.4848  0.3309  376 LYS C C   
12836 O O   . LYS C 376 ? 1.2438 1.1783 1.0698 0.3895  0.4914  0.3292  376 LYS C O   
12837 C CB  . LYS C 376 ? 1.0376 1.0392 1.0140 0.3499  0.5283  0.3598  376 LYS C CB  
12838 C CG  . LYS C 376 ? 1.0579 1.0996 1.0933 0.3407  0.5411  0.3623  376 LYS C CG  
12839 C CD  . LYS C 376 ? 1.2329 1.2801 1.2856 0.3363  0.5656  0.3864  376 LYS C CD  
12840 C CE  . LYS C 376 ? 1.1097 1.1945 1.2400 0.3160  0.5689  0.3923  376 LYS C CE  
12841 N NZ  . LYS C 376 ? 1.2392 1.3278 1.4145 0.2950  0.5718  0.4067  376 LYS C NZ  
12842 N N   . LYS C 377 ? 1.1610 1.0948 1.0519 0.3597  0.4667  0.3318  377 LYS C N   
12843 C CA  . LYS C 377 ? 1.1899 1.0879 1.0258 0.3715  0.4528  0.3332  377 LYS C CA  
12844 C C   . LYS C 377 ? 1.1734 1.0638 0.9731 0.3835  0.4277  0.3079  377 LYS C C   
12845 O O   . LYS C 377 ? 1.3011 1.1663 1.0408 0.3999  0.4230  0.3085  377 LYS C O   
12846 C CB  . LYS C 377 ? 1.0542 0.9380 0.9165 0.3581  0.4378  0.3380  377 LYS C CB  
12847 C CG  . LYS C 377 ? 1.2969 1.1770 1.1846 0.3478  0.4610  0.3665  377 LYS C CG  
12848 C CD  . LYS C 377 ? 1.4312 1.2843 1.3266 0.3412  0.4464  0.3738  377 LYS C CD  
12849 C CE  . LYS C 377 ? 1.4285 1.2883 1.3858 0.3195  0.4562  0.3865  377 LYS C CE  
12850 N NZ  . LYS C 377 ? 1.3801 1.2372 1.3366 0.3184  0.4883  0.4195  377 LYS C NZ  
12851 N N   . ILE C 378 ? 1.2050 1.1170 1.0404 0.3746  0.4110  0.2864  378 ILE C N   
12852 C CA  . ILE C 378 ? 1.2400 1.1474 1.0499 0.3831  0.3868  0.2631  378 ILE C CA  
12853 C C   . ILE C 378 ? 1.1653 1.0736 0.9409 0.3989  0.3997  0.2586  378 ILE C C   
12854 O O   . ILE C 378 ? 1.2657 1.1528 0.9895 0.4135  0.3882  0.2489  378 ILE C O   
12855 C CB  . ILE C 378 ? 1.0165 0.9475 0.8765 0.3675  0.3666  0.2441  378 ILE C CB  
12856 C CG1 . ILE C 378 ? 0.9790 0.9041 0.8666 0.3543  0.3531  0.2448  378 ILE C CG1 
12857 C CG2 . ILE C 378 ? 0.9364 0.8650 0.7739 0.3754  0.3441  0.2222  378 ILE C CG2 
12858 C CD1 . ILE C 378 ? 0.9921 0.9442 0.9359 0.3354  0.3441  0.2325  378 ILE C CD1 
12859 N N   . LEU C 379 ? 1.1205 1.0529 0.9259 0.3965  0.4231  0.2651  379 LEU C N   
12860 C CA  . LEU C 379 ? 1.1440 1.0779 0.9224 0.4127  0.4385  0.2605  379 LEU C CA  
12861 C C   . LEU C 379 ? 1.3202 1.2260 1.0317 0.4313  0.4557  0.2719  379 LEU C C   
12862 O O   . LEU C 379 ? 1.3655 1.2571 1.0304 0.4482  0.4557  0.2597  379 LEU C O   
12863 C CB  . LEU C 379 ? 1.0513 1.0196 0.8829 0.4063  0.4617  0.2686  379 LEU C CB  
12864 C CG  . LEU C 379 ? 1.2030 1.1723 1.0196 0.4171  0.4705  0.2627  379 LEU C CG  
12865 C CD1 . LEU C 379 ? 1.0414 1.0021 0.8373 0.4253  0.4484  0.2380  379 LEU C CD1 
12866 C CD2 . LEU C 379 ? 1.0432 1.0449 0.9214 0.4035  0.4809  0.2707  379 LEU C CD2 
12867 N N   . LYS C 380 ? 1.3038 1.2000 1.0083 0.4283  0.4697  0.2949  380 LYS C N   
12868 C CA  . LYS C 380 ? 1.3010 1.1707 0.9387 0.4451  0.4863  0.3090  380 LYS C CA  
12869 C C   . LYS C 380 ? 1.4123 1.2503 0.9877 0.4570  0.4578  0.2940  380 LYS C C   
12870 O O   . LYS C 380 ? 1.4811 1.2994 0.9926 0.4751  0.4650  0.2914  380 LYS C O   
12871 C CB  . LYS C 380 ? 1.2607 1.1250 0.9086 0.4366  0.5022  0.3387  380 LYS C CB  
12872 C CG  . LYS C 380 ? 1.2838 1.1207 0.8597 0.4532  0.5197  0.3570  380 LYS C CG  
12873 C CD  . LYS C 380 ? 1.3987 1.2352 0.9950 0.4433  0.5409  0.3892  380 LYS C CD  
12874 C CE  . LYS C 380 ? 1.6203 1.4292 1.1514 0.4559  0.5473  0.4037  380 LYS C CE  
12875 N NZ  . LYS C 380 ? 1.6960 1.5154 1.2544 0.4477  0.5745  0.4282  380 LYS C NZ  
12876 N N   . GLU C 381 ? 1.4694 1.3032 1.0638 0.4469  0.4254  0.2838  381 GLU C N   
12877 C CA  . GLU C 381 ? 1.5366 1.3444 1.0823 0.4562  0.3950  0.2702  381 GLU C CA  
12878 C C   . GLU C 381 ? 1.3839 1.1899 0.9051 0.4663  0.3836  0.2445  381 GLU C C   
12879 O O   . GLU C 381 ? 1.4059 1.1864 0.8665 0.4799  0.3697  0.2360  381 GLU C O   
12880 C CB  . GLU C 381 ? 1.3251 1.1350 0.9088 0.4426  0.3658  0.2647  381 GLU C CB  
12881 C CG  . GLU C 381 ? 1.5266 1.3276 1.1242 0.4355  0.3715  0.2885  381 GLU C CG  
12882 C CD  . GLU C 381 ? 1.7236 1.4927 1.2564 0.4497  0.3710  0.3054  381 GLU C CD  
12883 O OE1 . GLU C 381 ? 1.7091 1.4718 1.2104 0.4572  0.3994  0.3246  381 GLU C OE1 
12884 O OE2 . GLU C 381 ? 1.8179 1.5698 1.3316 0.4535  0.3423  0.3005  381 GLU C OE2 
12885 N N   . ALA C 382 ? 1.1986 1.0301 0.7666 0.4594  0.3878  0.2324  382 ALA C N   
12886 C CA  . ALA C 382 ? 1.3233 1.1525 0.8754 0.4681  0.3781  0.2091  382 ALA C CA  
12887 C C   . ALA C 382 ? 1.4579 1.2729 0.9572 0.4876  0.4040  0.2104  382 ALA C C   
12888 O O   . ALA C 382 ? 1.4442 1.2375 0.8947 0.5008  0.3922  0.1925  382 ALA C O   
12889 C CB  . ALA C 382 ? 1.1406 1.0016 0.7590 0.4557  0.3780  0.2007  382 ALA C CB  
12890 N N   . ILE C 383 ? 1.4510 1.2783 0.9608 0.4893  0.4396  0.2311  383 ILE C N   
12891 C CA  . ILE C 383 ? 1.4086 1.2256 0.8818 0.5017  0.4609  0.2337  383 ILE C CA  
12892 C C   . ILE C 383 ? 1.4669 1.2480 0.8551 0.5172  0.4565  0.2354  383 ILE C C   
12893 O O   . ILE C 383 ? 1.5581 1.3185 0.8965 0.5303  0.4516  0.2187  383 ILE C O   
12894 C CB  . ILE C 383 ? 1.3516 1.1919 0.8714 0.4912  0.4892  0.2570  383 ILE C CB  
12895 C CG1 . ILE C 383 ? 1.3465 1.2212 0.9431 0.4774  0.4908  0.2522  383 ILE C CG1 
12896 C CG2 . ILE C 383 ? 1.3838 1.2104 0.8606 0.5034  0.5096  0.2624  383 ILE C CG2 
12897 C CD1 . ILE C 383 ? 1.2820 1.1843 0.9382 0.4621  0.5099  0.2745  383 ILE C CD1 
12898 N N   . LEU C 384 ? 1.5817 1.3539 0.9529 0.5149  0.4563  0.2557  384 LEU C N   
12899 C CA  . LEU C 384 ? 1.4887 1.2276 0.7810 0.5275  0.4481  0.2612  384 LEU C CA  
12900 C C   . LEU C 384 ? 1.5782 1.2945 0.8280 0.5347  0.4109  0.2347  384 LEU C C   
12901 O O   . LEU C 384 ? 1.7128 1.4009 0.8860 0.5499  0.4062  0.2306  384 LEU C O   
12902 C CB  . LEU C 384 ? 1.5209 1.2550 0.8196 0.5187  0.4460  0.2888  384 LEU C CB  
12903 C CG  . LEU C 384 ? 1.4399 1.1920 0.7798 0.5092  0.4793  0.3169  384 LEU C CG  
12904 C CD1 . LEU C 384 ? 1.4255 1.1745 0.7908 0.4969  0.4724  0.3401  384 LEU C CD1 
12905 C CD2 . LEU C 384 ? 1.5097 1.2513 0.8088 0.5180  0.4989  0.3258  384 LEU C CD2 
12906 N N   . ASN C 385 ? 1.4680 1.1969 0.7684 0.5227  0.3831  0.2164  385 ASN C N   
12907 C CA  . ASN C 385 ? 1.3934 1.1041 0.6654 0.5262  0.3456  0.1914  385 ASN C CA  
12908 C C   . ASN C 385 ? 1.5128 1.2092 0.7429 0.5411  0.3505  0.1684  385 ASN C C   
12909 O O   . ASN C 385 ? 1.6761 1.3491 0.8629 0.5474  0.3222  0.1491  385 ASN C O   
12910 C CB  . ASN C 385 ? 1.5031 1.2337 0.8430 0.5089  0.3183  0.1801  385 ASN C CB  
12911 C CG  . ASN C 385 ? 1.6009 1.3146 0.9183 0.5093  0.2769  0.1622  385 ASN C CG  
12912 O OD1 . ASN C 385 ? 1.8049 1.5196 1.1329 0.5078  0.2594  0.1395  385 ASN C OD1 
12913 N ND2 . ASN C 385 ? 1.5423 1.2406 0.8308 0.5112  0.2597  0.1733  385 ASN C ND2 
12914 N N   . PHE C 386 ? 1.5047 1.2138 0.7479 0.5473  0.3853  0.1696  386 PHE C N   
12915 C CA  . PHE C 386 ? 1.6124 1.3061 0.8223 0.5605  0.3893  0.1470  386 PHE C CA  
12916 C C   . PHE C 386 ? 1.6601 1.3176 0.7801 0.5751  0.3827  0.1419  386 PHE C C   
12917 O O   . PHE C 386 ? 1.7695 1.4049 0.8509 0.5846  0.3707  0.1170  386 PHE C O   
12918 C CB  . PHE C 386 ? 1.5918 1.3090 0.8523 0.5554  0.4183  0.1540  386 PHE C CB  
12919 C CG  . PHE C 386 ? 1.7148 1.4184 0.9548 0.5653  0.4217  0.1325  386 PHE C CG  
12920 C CD1 . PHE C 386 ? 1.8390 1.5300 1.0760 0.5686  0.3989  0.1053  386 PHE C CD1 
12921 C CD2 . PHE C 386 ? 1.8193 1.5238 1.0484 0.5710  0.4490  0.1397  386 PHE C CD2 
12922 C CE1 . PHE C 386 ? 1.8415 1.5178 1.0615 0.5777  0.4027  0.0854  386 PHE C CE1 
12923 C CE2 . PHE C 386 ? 1.6989 1.3907 0.9102 0.5810  0.4537  0.1192  386 PHE C CE2 
12924 C CZ  . PHE C 386 ? 1.7228 1.3998 0.9301 0.5841  0.4305  0.0922  386 PHE C CZ  
12925 N N   . LYS C 387 ? 1.7360 1.3865 0.8238 0.5758  0.3882  0.1655  387 LYS C N   
12926 C CA  . LYS C 387 ? 1.8446 1.4636 0.8492 0.5875  0.3798  0.1646  387 LYS C CA  
12927 C C   . LYS C 387 ? 1.9294 1.5210 0.8814 0.5941  0.3392  0.1416  387 LYS C C   
12928 O O   . LYS C 387 ? 1.9795 1.5434 0.8640 0.6043  0.3274  0.1283  387 LYS C O   
12929 C CB  . LYS C 387 ? 1.7014 1.3209 0.6936 0.5841  0.3884  0.1974  387 LYS C CB  
12930 C CG  . LYS C 387 ? 1.7058 1.3448 0.7306 0.5796  0.4276  0.2204  387 LYS C CG  
12931 C CD  . LYS C 387 ? 1.9742 1.6133 0.9950 0.5743  0.4346  0.2536  387 LYS C CD  
12932 C CE  . LYS C 387 ? 1.8717 1.5093 0.8675 0.5782  0.4636  0.2702  387 LYS C CE  
12933 N NZ  . LYS C 387 ? 1.7759 1.4265 0.8056 0.5676  0.4808  0.3050  387 LYS C NZ  
12934 N N   . ASN C 388 ? 1.8062 1.4096 0.8072 0.5817  0.3109  0.1359  388 ASN C N   
12935 C CA  . ASN C 388 ? 1.7593 1.3450 0.7412 0.5791  0.2639  0.1151  388 ASN C CA  
12936 C C   . ASN C 388 ? 1.6214 1.2054 0.6268 0.5772  0.2491  0.0833  388 ASN C C   
12937 O O   . ASN C 388 ? 1.6145 1.1907 0.6248 0.5707  0.2098  0.0667  388 ASN C O   
12938 C CB  . ASN C 388 ? 1.6856 1.2869 0.7180 0.5632  0.2371  0.1291  388 ASN C CB  
12939 C CG  . ASN C 388 ? 1.6705 1.2748 0.6950 0.5632  0.2540  0.1624  388 ASN C CG  
12940 O OD1 . ASN C 388 ? 1.7190 1.3476 0.8029 0.5530  0.2751  0.1807  388 ASN C OD1 
12941 N ND2 . ASN C 388 ? 1.7510 1.3296 0.7012 0.5744  0.2444  0.1716  388 ASN C ND2 
12942 N N   . ARG C 389 ? 1.6144 1.2055 0.6359 0.5831  0.2798  0.0758  389 ARG C N   
12943 C CA  . ARG C 389 ? 1.6286 1.2159 0.6737 0.5824  0.2683  0.0478  389 ARG C CA  
12944 C C   . ARG C 389 ? 1.7614 1.3079 0.7269 0.5964  0.2492  0.0207  389 ARG C C   
12945 O O   . ARG C 389 ? 1.9533 1.4782 0.8456 0.6134  0.2686  0.0210  389 ARG C O   
12946 C CB  . ARG C 389 ? 1.6267 1.2323 0.7098 0.5874  0.3086  0.0498  389 ARG C CB  
12947 C CG  . ARG C 389 ? 1.6660 1.2662 0.7754 0.5887  0.3007  0.0232  389 ARG C CG  
12948 C CD  . ARG C 389 ? 1.5283 1.1619 0.7298 0.5695  0.2910  0.0279  389 ARG C CD  
12949 N NE  . ARG C 389 ? 1.5507 1.2184 0.8056 0.5664  0.3263  0.0494  389 ARG C NE  
12950 C CZ  . ARG C 389 ? 1.6444 1.3263 0.9402 0.5645  0.3444  0.0486  389 ARG C CZ  
12951 N NH1 . ARG C 389 ? 1.6959 1.3569 0.9778 0.5719  0.3376  0.0255  389 ARG C NH1 
12952 N NH2 . ARG C 389 ? 1.5654 1.2819 0.9181 0.5538  0.3673  0.0709  389 ARG C NH2 
12953 N N   . ASP C 390 ? 1.6631 1.1990 0.6424 0.5888  0.2113  -0.0028 390 ASP C N   
12954 C CA  . ASP C 390 ? 1.8941 1.3900 0.8044 0.5995  0.1885  -0.0320 390 ASP C CA  
12955 C C   . ASP C 390 ? 1.9938 1.4817 0.9240 0.6054  0.2023  -0.0550 390 ASP C C   
12956 O O   . ASP C 390 ? 2.0421 1.5297 1.0154 0.5946  0.1766  -0.0713 390 ASP C O   
12957 C CB  . ASP C 390 ? 1.9790 1.4680 0.8958 0.5862  0.1361  -0.0424 390 ASP C CB  
12958 C CG  . ASP C 390 ? 2.1290 1.5757 0.9659 0.5960  0.1077  -0.0696 390 ASP C CG  
12959 O OD1 . ASP C 390 ? 1.9812 1.4028 0.7867 0.6076  0.1185  -0.0939 390 ASP C OD1 
12960 O OD2 . ASP C 390 ? 2.1096 1.5478 0.9161 0.5922  0.0737  -0.0672 390 ASP C OD2 
12961 N N   . GLN C 391 ? 1.9774 1.4614 0.8846 0.6205  0.2424  -0.0536 391 GLN C N   
12962 C CA  . GLN C 391 ? 1.9515 1.4342 0.8934 0.6221  0.2565  -0.0692 391 GLN C CA  
12963 C C   . GLN C 391 ? 2.0189 1.4640 0.9342 0.6262  0.2262  -0.1059 391 GLN C C   
12964 O O   . GLN C 391 ? 2.0980 1.5449 1.0614 0.6241  0.2291  -0.1180 391 GLN C O   
12965 C CB  . GLN C 391 ? 2.0149 1.5017 0.9421 0.6292  0.2936  -0.0594 391 GLN C CB  
12966 C CG  . GLN C 391 ? 1.9459 1.4733 0.9221 0.6227  0.3271  -0.0244 391 GLN C CG  
12967 C CD  . GLN C 391 ? 2.0367 1.5975 1.1032 0.6126  0.3396  -0.0171 391 GLN C CD  
12968 O OE1 . GLN C 391 ? 2.0281 1.5881 1.1292 0.6076  0.3190  -0.0314 391 GLN C OE1 
12969 N NE2 . GLN C 391 ? 2.0797 1.6712 1.1880 0.6087  0.3723  0.0061  391 GLN C NE2 
12970 N N   . SER C 392 ? 2.0768 1.4880 0.9190 0.6308  0.1957  -0.1229 392 SER C N   
12971 C CA  . SER C 392 ? 2.0387 1.4117 0.8549 0.6328  0.1632  -0.1591 392 SER C CA  
12972 C C   . SER C 392 ? 2.0381 1.4247 0.9294 0.6129  0.1302  -0.1628 392 SER C C   
12973 O O   . SER C 392 ? 2.1118 1.4784 1.0211 0.6114  0.1163  -0.1868 392 SER C O   
12974 C CB  . SER C 392 ? 2.2917 1.6311 1.0194 0.6372  0.1334  -0.1727 392 SER C CB  
12975 O OG  . SER C 392 ? 2.4287 1.7814 1.1626 0.6246  0.1011  -0.1585 392 SER C OG  
12976 N N   . LYS C 393 ? 1.9679 1.3903 0.9092 0.5952  0.1175  -0.1374 393 LYS C N   
12977 C CA  . LYS C 393 ? 2.0138 1.4565 1.0323 0.5731  0.0872  -0.1365 393 LYS C CA  
12978 C C   . LYS C 393 ? 1.9096 1.3912 1.0156 0.5642  0.1120  -0.1186 393 LYS C C   
12979 O O   . LYS C 393 ? 1.8751 1.3795 1.0469 0.5453  0.0916  -0.1131 393 LYS C O   
12980 C CB  . LYS C 393 ? 2.0527 1.5097 1.0741 0.5595  0.0546  -0.1232 393 LYS C CB  
12981 C CG  . LYS C 393 ? 2.1308 1.5514 1.0674 0.5674  0.0258  -0.1395 393 LYS C CG  
12982 C CD  . LYS C 393 ? 2.3623 1.7952 1.3157 0.5520  -0.0169 -0.1321 393 LYS C CD  
12983 C CE  . LYS C 393 ? 2.2254 1.6777 1.1640 0.5540  -0.0088 -0.1032 393 LYS C CE  
12984 N NZ  . LYS C 393 ? 2.2710 1.7261 1.2082 0.5444  -0.0531 -0.1003 393 LYS C NZ  
12985 N N   . VAL C 394 ? 1.6772 1.1673 0.7843 0.5775  0.1552  -0.1096 394 VAL C N   
12986 C CA  . VAL C 394 ? 1.5483 1.0755 0.7352 0.5699  0.1779  -0.0925 394 VAL C CA  
12987 C C   . VAL C 394 ? 1.6003 1.1140 0.8211 0.5696  0.1711  -0.1118 394 VAL C C   
12988 O O   . VAL C 394 ? 1.8327 1.3081 1.0073 0.5849  0.1724  -0.1362 394 VAL C O   
12989 C CB  . VAL C 394 ? 1.6606 1.2043 0.8410 0.5837  0.2256  -0.0744 394 VAL C CB  
12990 C CG1 . VAL C 394 ? 1.6828 1.2609 0.9435 0.5779  0.2473  -0.0611 394 VAL C CG1 
12991 C CG2 . VAL C 394 ? 1.7646 1.3252 0.9255 0.5804  0.2321  -0.0503 394 VAL C CG2 
12992 N N   . MET C 395 ? 1.4659 1.0094 0.7655 0.5525  0.1637  -0.1011 395 MET C N   
12993 C CA  . MET C 395 ? 1.4978 1.0305 0.8362 0.5507  0.1566  -0.1149 395 MET C CA  
12994 C C   . MET C 395 ? 1.3665 0.9422 0.7870 0.5389  0.1703  -0.0928 395 MET C C   
12995 O O   . MET C 395 ? 1.3388 0.9383 0.8076 0.5184  0.1489  -0.0832 395 MET C O   
12996 C CB  . MET C 395 ? 1.5553 1.0664 0.8939 0.5369  0.1119  -0.1327 395 MET C CB  
12997 C CG  . MET C 395 ? 1.4771 0.9612 0.8360 0.5387  0.1026  -0.1524 395 MET C CG  
12998 S SD  . MET C 395 ? 1.4757 0.9982 0.9356 0.5209  0.1040  -0.1327 395 MET C SD  
12999 C CE  . MET C 395 ? 1.6823 1.1931 1.1651 0.4981  0.0549  -0.1440 395 MET C CE  
13000 N N   . ILE C 396 ? 1.3846 0.9715 0.8208 0.5520  0.2058  -0.0847 396 ILE C N   
13001 C CA  . ILE C 396 ? 1.2935 0.9213 0.8052 0.5424  0.2191  -0.0638 396 ILE C CA  
13002 C C   . ILE C 396 ? 1.3144 0.9256 0.8575 0.5466  0.2150  -0.0760 396 ILE C C   
13003 O O   . ILE C 396 ? 1.4987 1.0900 1.0229 0.5638  0.2348  -0.0866 396 ILE C O   
13004 C CB  . ILE C 396 ? 1.2845 0.9397 0.8031 0.5508  0.2585  -0.0445 396 ILE C CB  
13005 C CG1 . ILE C 396 ? 1.2838 0.9501 0.7692 0.5494  0.2647  -0.0317 396 ILE C CG1 
13006 C CG2 . ILE C 396 ? 1.2815 0.9804 0.8804 0.5370  0.2675  -0.0236 396 ILE C CG2 
13007 C CD1 . ILE C 396 ? 1.3001 0.9833 0.7768 0.5521  0.2976  -0.0153 396 ILE C CD1 
13008 N N   . PRO C 397 ? 1.3188 0.9394 0.9122 0.5282  0.1892  -0.0733 397 PRO C N   
13009 C CA  . PRO C 397 ? 1.2702 0.8722 0.8943 0.5327  0.1856  -0.0827 397 PRO C CA  
13010 C C   . PRO C 397 ? 1.3385 0.9573 0.9941 0.5479  0.2201  -0.0712 397 PRO C C   
13011 O O   . PRO C 397 ? 1.4022 1.0664 1.0961 0.5384  0.2345  -0.0469 397 PRO C O   
13012 C CB  . PRO C 397 ? 1.2817 0.9061 0.9626 0.5072  0.1579  -0.0712 397 PRO C CB  
13013 C CG  . PRO C 397 ? 1.2364 0.8736 0.8992 0.4920  0.1393  -0.0679 397 PRO C CG  
13014 C CD  . PRO C 397 ? 1.2684 0.9164 0.8937 0.5032  0.1639  -0.0610 397 PRO C CD  
13015 N N   . GLU C 398 ? 1.3237 0.9143 0.9700 0.5601  0.2283  -0.0869 398 GLU C N   
13016 C CA  . GLU C 398 ? 1.4149 1.0305 1.1011 0.5629  0.2549  -0.0744 398 GLU C CA  
13017 C C   . GLU C 398 ? 1.4272 1.0628 1.1865 0.5535  0.2452  -0.0596 398 GLU C C   
13018 O O   . GLU C 398 ? 1.5341 1.1473 1.3145 0.5601  0.2413  -0.0688 398 GLU C O   
13019 C CB  . GLU C 398 ? 1.5711 1.1499 1.2233 0.5801  0.2671  -0.0974 398 GLU C CB  
13020 C CG  . GLU C 398 ? 1.8006 1.3658 1.3816 0.5899  0.2820  -0.1077 398 GLU C CG  
13021 C CD  . GLU C 398 ? 1.9399 1.4994 1.5092 0.6043  0.3101  -0.1149 398 GLU C CD  
13022 O OE1 . GLU C 398 ? 2.0428 1.6060 1.6600 0.6083  0.3174  -0.1148 398 GLU C OE1 
13023 O OE2 . GLU C 398 ? 2.1814 1.7331 1.6939 0.6122  0.3250  -0.1199 398 GLU C OE2 
13024 N N   . LEU C 399 ? 1.4231 1.1002 1.2203 0.5381  0.2407  -0.0361 399 LEU C N   
13025 C CA  . LEU C 399 ? 1.2722 0.9734 1.1355 0.5275  0.2307  -0.0182 399 LEU C CA  
13026 C C   . LEU C 399 ? 1.1975 0.9557 1.0993 0.5130  0.2416  0.0094  399 LEU C C   
13027 O O   . LEU C 399 ? 1.0960 0.8719 0.9917 0.5024  0.2337  0.0168  399 LEU C O   
13028 C CB  . LEU C 399 ? 1.1241 0.8086 0.9914 0.5137  0.1971  -0.0234 399 LEU C CB  
13029 C CG  . LEU C 399 ? 1.1822 0.8119 1.0297 0.5213  0.1796  -0.0483 399 LEU C CG  
13030 C CD1 . LEU C 399 ? 1.4038 1.0192 1.2353 0.5012  0.1453  -0.0579 399 LEU C CD1 
13031 C CD2 . LEU C 399 ? 1.2181 0.8433 1.1193 0.5243  0.1782  -0.0404 399 LEU C CD2 
13032 N N   . LYS C 400 ? 1.2045 0.9904 1.1465 0.5129  0.2587  0.0234  400 LYS C N   
13033 C CA  . LYS C 400 ? 1.0035 0.8421 0.9854 0.4990  0.2681  0.0485  400 LYS C CA  
13034 C C   . LYS C 400 ? 1.1595 1.0198 1.2035 0.4958  0.2657  0.0641  400 LYS C C   
13035 O O   . LYS C 400 ? 1.2461 1.0799 1.2993 0.5069  0.2627  0.0551  400 LYS C O   
13036 C CB  . LYS C 400 ? 1.0879 0.9412 1.0500 0.5024  0.2940  0.0518  400 LYS C CB  
13037 C CG  . LYS C 400 ? 1.3426 1.1769 1.2942 0.5196  0.3130  0.0411  400 LYS C CG  
13038 C CD  . LYS C 400 ? 1.1296 0.9929 1.0869 0.5198  0.3397  0.0539  400 LYS C CD  
13039 C CE  . LYS C 400 ? 1.2388 1.1012 1.1489 0.5169  0.3479  0.0542  400 LYS C CE  
13040 N NZ  . LYS C 400 ? 1.3847 1.2600 1.2883 0.5228  0.3761  0.0616  400 LYS C NZ  
13041 N N   . CYS C 401 ? 1.4011 1.0492 0.9591 0.4556  0.1642  -0.1261 401 CYS C N   
13042 C CA  . CYS C 401 ? 1.2869 0.9271 0.8740 0.4462  0.1644  -0.1253 401 CYS C CA  
13043 C C   . CYS C 401 ? 1.3307 0.9955 0.9433 0.4423  0.1843  -0.1024 401 CYS C C   
13044 O O   . CYS C 401 ? 1.3270 1.0079 0.9458 0.4371  0.1940  -0.0869 401 CYS C O   
13045 C CB  . CYS C 401 ? 1.1459 0.7640 0.7503 0.4280  0.1490  -0.1330 401 CYS C CB  
13046 S SG  . CYS C 401 ? 1.4897 1.0911 1.1235 0.4188  0.1439  -0.1366 401 CYS C SG  
13047 N N   . LYS C 402 ? 1.3454 1.0126 0.9739 0.4447  0.1899  -0.1002 402 LYS C N   
13048 C CA  . LYS C 402 ? 1.2693 0.9602 0.9240 0.4412  0.2075  -0.0794 402 LYS C CA  
13049 C C   . LYS C 402 ? 1.2160 0.9036 0.9031 0.4206  0.2047  -0.0720 402 LYS C C   
13050 O O   . LYS C 402 ? 1.3423 1.0080 1.0342 0.4110  0.1897  -0.0835 402 LYS C O   
13051 C CB  . LYS C 402 ? 1.2020 0.8991 0.8604 0.4535  0.2146  -0.0799 402 LYS C CB  
13052 C CG  . LYS C 402 ? 1.3792 1.0815 1.0042 0.4752  0.2186  -0.0860 402 LYS C CG  
13053 C CD  . LYS C 402 ? 1.4252 1.1421 1.0546 0.4894  0.2311  -0.0807 402 LYS C CD  
13054 C CE  . LYS C 402 ? 1.6600 1.4037 1.2755 0.5043  0.2489  -0.0658 402 LYS C CE  
13055 N NZ  . LYS C 402 ? 1.4942 1.2346 1.0722 0.5155  0.2444  -0.0731 402 LYS C NZ  
13056 N N   . ALA C 403 ? 1.1472 0.8561 0.8568 0.4140  0.2190  -0.0527 403 ALA C N   
13057 C CA  . ALA C 403 ? 1.2319 0.9396 0.9714 0.3955  0.2169  -0.0451 403 ALA C CA  
13058 C C   . ALA C 403 ? 1.2669 0.9988 1.0338 0.3921  0.2329  -0.0259 403 ALA C C   
13059 O O   . ALA C 403 ? 1.3501 1.1013 1.1128 0.4020  0.2474  -0.0152 403 ALA C O   
13060 C CB  . ALA C 403 ? 1.1391 0.8408 0.8734 0.3852  0.2112  -0.0446 403 ALA C CB  
13061 N N   . ILE C 404 ? 1.1099 0.8403 0.9048 0.3791  0.2298  -0.0222 404 ILE C N   
13062 C CA  . ILE C 404 ? 1.1084 0.8610 0.9329 0.3746  0.2431  -0.0052 404 ILE C CA  
13063 C C   . ILE C 404 ? 1.0690 0.8209 0.9118 0.3572  0.2408  0.0017  404 ILE C C   
13064 O O   . ILE C 404 ? 1.0904 0.8247 0.9347 0.3475  0.2272  -0.0068 404 ILE C O   
13065 C CB  . ILE C 404 ? 1.0012 0.7558 0.8436 0.3772  0.2421  -0.0067 404 ILE C CB  
13066 C CG1 . ILE C 404 ? 1.1281 0.8855 0.9536 0.3958  0.2463  -0.0125 404 ILE C CG1 
13067 C CG2 . ILE C 404 ? 0.9971 0.7727 0.8733 0.3699  0.2523  0.0092  404 ILE C CG2 
13068 C CD1 . ILE C 404 ? 1.3873 1.1416 1.2265 0.3998  0.2424  -0.0170 404 ILE C CD1 
13069 N N   . LEU C 405 ? 0.9493 0.7192 0.8053 0.3539  0.2538  0.0169  405 LEU C N   
13070 C CA  . LEU C 405 ? 1.0435 0.8130 0.9170 0.3382  0.2525  0.0236  405 LEU C CA  
13071 C C   . LEU C 405 ? 1.0297 0.8209 0.9330 0.3349  0.2669  0.0401  405 LEU C C   
13072 O O   . LEU C 405 ? 1.1242 0.9300 1.0360 0.3438  0.2760  0.0455  405 LEU C O   
13073 C CB  . LEU C 405 ? 0.9670 0.7297 0.8193 0.3376  0.2511  0.0225  405 LEU C CB  
13074 C CG  . LEU C 405 ? 0.9634 0.7408 0.8050 0.3477  0.2659  0.0337  405 LEU C CG  
13075 C CD1 . LEU C 405 ? 1.2003 0.9722 1.0296 0.3436  0.2645  0.0358  405 LEU C CD1 
13076 C CD2 . LEU C 405 ? 1.0064 0.7844 0.8215 0.3652  0.2674  0.0270  405 LEU C CD2 
13077 N N   . GLY C 406 ? 0.9683 0.7615 0.8879 0.3228  0.2687  0.0477  406 GLY C N   
13078 C CA  . GLY C 406 ? 1.0294 0.8415 0.9818 0.3183  0.2812  0.0625  406 GLY C CA  
13079 C C   . GLY C 406 ? 1.0027 0.8145 0.9811 0.3085  0.2736  0.0602  406 GLY C C   
13080 O O   . GLY C 406 ? 1.1262 0.9549 1.1349 0.3063  0.2821  0.0703  406 GLY C O   
13081 N N   . TYR C 407 ? 0.9564 0.7505 0.9243 0.3032  0.2581  0.0481  407 TYR C N   
13082 C CA  . TYR C 407 ? 0.8752 0.6680 0.8639 0.2954  0.2499  0.0460  407 TYR C CA  
13083 C C   . TYR C 407 ? 0.9580 0.7508 0.9645 0.2822  0.2482  0.0502  407 TYR C C   
13084 O O   . TYR C 407 ? 1.0856 0.8642 1.0849 0.2742  0.2368  0.0437  407 TYR C O   
13085 C CB  . TYR C 407 ? 0.9483 0.7225 0.9202 0.2962  0.2352  0.0333  407 TYR C CB  
13086 C CG  . TYR C 407 ? 1.0285 0.8032 0.9900 0.3096  0.2364  0.0286  407 TYR C CG  
13087 C CD1 . TYR C 407 ? 0.8403 0.6305 0.8217 0.3154  0.2422  0.0340  407 TYR C CD1 
13088 C CD2 . TYR C 407 ? 1.0616 0.8225 0.9940 0.3175  0.2320  0.0187  407 TYR C CD2 
13089 C CE1 . TYR C 407 ? 1.0957 0.8868 1.0673 0.3288  0.2438  0.0297  407 TYR C CE1 
13090 C CE2 . TYR C 407 ? 1.1576 0.9178 1.0796 0.3307  0.2327  0.0132  407 TYR C CE2 
13091 C CZ  . TYR C 407 ? 1.1911 0.9664 1.1324 0.3365  0.2390  0.0189  407 TYR C CZ  
13092 O OH  . TYR C 407 ? 1.0208 0.7959 0.9520 0.3505  0.2402  0.0134  407 TYR C OH  
13093 N N   . SER C 408 ? 0.7501 0.5589 0.7814 0.2802  0.2598  0.0614  408 SER C N   
13094 C CA  . SER C 408 ? 0.8571 0.6689 0.9077 0.2642  0.2552  0.0647  408 SER C CA  
13095 C C   . SER C 408 ? 0.9512 0.7700 1.0240 0.2571  0.2457  0.0627  408 SER C C   
13096 O O   . SER C 408 ? 0.9130 0.7357 0.9884 0.2661  0.2458  0.0612  408 SER C O   
13097 C CB  . SER C 408 ? 0.9362 0.7630 1.0060 0.2617  0.2684  0.0774  408 SER C CB  
13098 O OG  . SER C 408 ? 0.8084 0.6546 0.8981 0.2695  0.2793  0.0856  408 SER C OG  
13099 N N   . VAL C 409 ? 0.8893 0.7098 0.9772 0.2424  0.2374  0.0624  409 VAL C N   
13100 C CA  . VAL C 409 ? 0.8094 0.6379 0.9166 0.2365  0.2275  0.0603  409 VAL C CA  
13101 C C   . VAL C 409 ? 0.9518 0.8025 1.0875 0.2407  0.2354  0.0681  409 VAL C C   
13102 O O   . VAL C 409 ? 0.9438 0.8013 1.0877 0.2454  0.2310  0.0667  409 VAL C O   
13103 C CB  . VAL C 409 ? 0.7829 0.6099 0.8988 0.2213  0.2173  0.0575  409 VAL C CB  
13104 C CG1 . VAL C 409 ? 0.7652 0.6039 0.9016 0.2163  0.2073  0.0558  409 VAL C CG1 
13105 C CG2 . VAL C 409 ? 0.9508 0.7587 1.0397 0.2185  0.2094  0.0503  409 VAL C CG2 
13106 N N   . GLU C 410 ? 0.8530 0.7157 1.0045 0.2396  0.2476  0.0774  410 GLU C N   
13107 C CA  . GLU C 410 ? 0.7607 0.6474 0.9427 0.2430  0.2567  0.0868  410 GLU C CA  
13108 C C   . GLU C 410 ? 0.8814 0.7718 1.0524 0.2612  0.2644  0.0874  410 GLU C C   
13109 O O   . GLU C 410 ? 0.9891 0.8955 1.1797 0.2657  0.2642  0.0897  410 GLU C O   
13110 C CB  . GLU C 410 ? 0.7723 0.6690 0.9710 0.2391  0.2701  0.0986  410 GLU C CB  
13111 C CG  . GLU C 410 ? 0.8923 0.7858 1.1075 0.2215  0.2630  0.0985  410 GLU C CG  
13112 C CD  . GLU C 410 ? 1.1435 1.0144 1.3318 0.2173  0.2594  0.0932  410 GLU C CD  
13113 O OE1 . GLU C 410 ? 0.9690 0.8259 1.1245 0.2267  0.2601  0.0884  410 GLU C OE1 
13114 O OE2 . GLU C 410 ? 1.0003 0.8676 1.2015 0.2047  0.2553  0.0935  410 GLU C OE2 
13115 N N   . GLU C 411 ? 0.8561 0.7317 0.9952 0.2724  0.2703  0.0844  411 GLU C N   
13116 C CA  . GLU C 411 ? 0.8400 0.7156 0.9641 0.2913  0.2772  0.0827  411 GLU C CA  
13117 C C   . GLU C 411 ? 0.8892 0.7536 1.0052 0.2947  0.2642  0.0727  411 GLU C C   
13118 O O   . GLU C 411 ? 0.9748 0.8489 1.0970 0.3047  0.2661  0.0735  411 GLU C O   
13119 C CB  . GLU C 411 ? 1.0442 0.9058 1.1326 0.2993  0.2822  0.0797  411 GLU C CB  
13120 C CG  . GLU C 411 ? 1.1054 0.9657 1.1709 0.3129  0.2823  0.0744  411 GLU C CG  
13121 C CD  . GLU C 411 ? 1.1363 1.0215 1.2203 0.3232  0.2952  0.0842  411 GLU C CD  
13122 O OE1 . GLU C 411 ? 1.0806 0.9863 1.1931 0.3204  0.3077  0.0978  411 GLU C OE1 
13123 O OE2 . GLU C 411 ? 1.2662 1.1506 1.3374 0.3342  0.2928  0.0785  411 GLU C OE2 
13124 N N   . ILE C 412 ? 0.9326 0.7778 1.0343 0.2848  0.2499  0.0642  412 ILE C N   
13125 C CA  . ILE C 412 ? 0.8651 0.6984 0.9595 0.2872  0.2376  0.0566  412 ILE C CA  
13126 C C   . ILE C 412 ? 0.8746 0.7280 1.0000 0.2846  0.2339  0.0614  412 ILE C C   
13127 O O   . ILE C 412 ? 0.8688 0.7234 0.9960 0.2955  0.2326  0.0603  412 ILE C O   
13128 C CB  . ILE C 412 ? 0.8013 0.6136 0.8776 0.2759  0.2241  0.0490  412 ILE C CB  
13129 C CG1 . ILE C 412 ? 0.7706 0.5634 0.8148 0.2805  0.2249  0.0426  412 ILE C CG1 
13130 C CG2 . ILE C 412 ? 0.6668 0.4717 0.7440 0.2750  0.2113  0.0450  412 ILE C CG2 
13131 C CD1 . ILE C 412 ? 0.9064 0.6839 0.9373 0.2696  0.2163  0.0382  412 ILE C CD1 
13132 N N   . ILE C 413 ? 0.8547 0.7239 1.0048 0.2710  0.2321  0.0665  413 ILE C N   
13133 C CA  . ILE C 413 ? 0.9030 0.7937 1.0843 0.2676  0.2272  0.0705  413 ILE C CA  
13134 C C   . ILE C 413 ? 0.8594 0.7709 1.0586 0.2815  0.2396  0.0780  413 ILE C C   
13135 O O   . ILE C 413 ? 0.8897 0.8109 1.1009 0.2884  0.2355  0.0785  413 ILE C O   
13136 C CB  . ILE C 413 ? 0.7814 0.6839 0.9858 0.2502  0.2226  0.0730  413 ILE C CB  
13137 C CG1 . ILE C 413 ? 0.8374 0.7228 1.0258 0.2389  0.2081  0.0648  413 ILE C CG1 
13138 C CG2 . ILE C 413 ? 0.8667 0.7964 1.1078 0.2476  0.2197  0.0781  413 ILE C CG2 
13139 C CD1 . ILE C 413 ? 0.8574 0.7461 1.0584 0.2234  0.2047  0.0647  413 ILE C CD1 
13140 N N   . ASN C 414 ? 0.8538 0.7728 1.0543 0.2869  0.2553  0.0845  414 ASN C N   
13141 C CA  . ASN C 414 ? 0.8867 0.8274 1.1030 0.3016  0.2695  0.0929  414 ASN C CA  
13142 C C   . ASN C 414 ? 0.8108 0.7402 1.0057 0.3202  0.2691  0.0866  414 ASN C C   
13143 O O   . ASN C 414 ? 0.8831 0.8306 1.0952 0.3286  0.2709  0.0903  414 ASN C O   
13144 C CB  . ASN C 414 ? 0.8711 0.8181 1.0844 0.3058  0.2871  0.1011  414 ASN C CB  
13145 C CG  . ASN C 414 ? 0.8883 0.8540 1.1340 0.2904  0.2915  0.1117  414 ASN C CG  
13146 O OD1 . ASN C 414 ? 0.8875 0.8624 1.1594 0.2759  0.2805  0.1116  414 ASN C OD1 
13147 N ND2 . ASN C 414 ? 0.8899 0.8612 1.1342 0.2936  0.3073  0.1211  414 ASN C ND2 
13148 N N   . LYS C 415 ? 0.8667 0.7677 1.0226 0.3208  0.2620  0.0759  415 LYS C N   
13149 C CA  . LYS C 415 ? 1.0146 0.9017 1.1463 0.3313  0.2555  0.0674  415 LYS C CA  
13150 C C   . LYS C 415 ? 0.9207 0.8031 1.0620 0.3311  0.2427  0.0643  415 LYS C C   
13151 O O   . LYS C 415 ? 0.9643 0.8485 1.1045 0.3417  0.2408  0.0626  415 LYS C O   
13152 C CB  . LYS C 415 ? 0.8201 0.6789 0.9124 0.3306  0.2503  0.0568  415 LYS C CB  
13153 C CG  . LYS C 415 ? 0.9522 0.8155 1.0283 0.3369  0.2625  0.0588  415 LYS C CG  
13154 C CD  . LYS C 415 ? 1.1985 1.0407 1.2385 0.3457  0.2572  0.0469  415 LYS C CD  
13155 C CE  . LYS C 415 ? 1.3914 1.2425 1.4161 0.3564  0.2699  0.0496  415 LYS C CE  
13156 N NZ  . LYS C 415 ? 1.5026 1.3318 1.4917 0.3652  0.2631  0.0361  415 LYS C NZ  
13157 N N   . LEU C 416 ? 0.8129 0.6895 0.9630 0.3199  0.2343  0.0642  416 LEU C N   
13158 C CA  . LEU C 416 ? 0.8875 0.7609 1.0463 0.3201  0.2224  0.0632  416 LEU C CA  
13159 C C   . LEU C 416 ? 0.9571 0.8617 1.1506 0.3242  0.2242  0.0714  416 LEU C C   
13160 O O   . LEU C 416 ? 1.0018 0.9069 1.2006 0.3300  0.2161  0.0714  416 LEU C O   
13161 C CB  . LEU C 416 ? 0.8241 0.6899 0.9806 0.3012  0.2092  0.0607  416 LEU C CB  
13162 C CG  . LEU C 416 ? 0.8618 0.6983 0.9872 0.2956  0.2041  0.0532  416 LEU C CG  
13163 C CD1 . LEU C 416 ? 0.8350 0.6711 0.9627 0.2779  0.1936  0.0525  416 LEU C CD1 
13164 C CD2 . LEU C 416 ? 0.7081 0.5204 0.8134 0.3053  0.1979  0.0477  416 LEU C CD2 
13165 N N   . ASP C 417 ? 0.8582 0.7894 1.0767 0.3211  0.2345  0.0792  417 ASP C N   
13166 C CA  . ASP C 417 ? 0.8384 0.8027 1.0938 0.3240  0.2364  0.0876  417 ASP C CA  
13167 C C   . ASP C 417 ? 0.9145 0.8836 1.1690 0.3458  0.2430  0.0890  417 ASP C C   
13168 O O   . ASP C 417 ? 0.9942 0.9855 1.2752 0.3512  0.2403  0.0943  417 ASP C O   
13169 C CB  . ASP C 417 ? 0.7145 0.7051 0.9974 0.3167  0.2481  0.0968  417 ASP C CB  
13170 C CG  . ASP C 417 ? 0.9148 0.9139 1.2178 0.2948  0.2382  0.0974  417 ASP C CG  
13171 O OD1 . ASP C 417 ? 1.0872 1.0676 1.3741 0.2850  0.2241  0.0895  417 ASP C OD1 
13172 O OD2 . ASP C 417 ? 0.9275 0.9519 1.2628 0.2878  0.2446  0.1059  417 ASP C OD2 
13173 N N   . LYS C 418 ? 0.9081 0.8576 1.1283 0.3525  0.2464  0.0824  418 LYS C N   
13174 C CA  . LYS C 418 ? 0.9497 0.9002 1.1604 0.3676  0.2481  0.0801  418 LYS C CA  
13175 C C   . LYS C 418 ? 0.9744 0.9132 1.1832 0.3722  0.2342  0.0761  418 LYS C C   
13176 O O   . LYS C 418 ? 1.0107 0.9610 1.2284 0.3843  0.2349  0.0780  418 LYS C O   
13177 C CB  . LYS C 418 ? 0.9380 0.8658 1.1103 0.3730  0.2519  0.0714  418 LYS C CB  
13178 C CG  . LYS C 418 ? 1.2091 1.1510 1.3815 0.3722  0.2671  0.0773  418 LYS C CG  
13179 C CD  . LYS C 418 ? 1.4152 1.3318 1.5471 0.3750  0.2678  0.0678  418 LYS C CD  
13180 C CE  . LYS C 418 ? 1.6555 1.5891 1.7847 0.3811  0.2842  0.0748  418 LYS C CE  
13181 N NZ  . LYS C 418 ? 1.3902 1.3011 1.4791 0.3861  0.2839  0.0650  418 LYS C NZ  
13182 N N   . VAL C 419 ? 0.9060 0.8225 1.1035 0.3631  0.2221  0.0716  419 VAL C N   
13183 C CA  . VAL C 419 ? 0.9318 0.8360 1.1269 0.3669  0.2092  0.0699  419 VAL C CA  
13184 C C   . VAL C 419 ? 1.0582 0.9847 1.2855 0.3633  0.2032  0.0784  419 VAL C C   
13185 O O   . VAL C 419 ? 1.0908 1.0057 1.3145 0.3633  0.1915  0.0785  419 VAL C O   
13186 C CB  . VAL C 419 ? 0.8989 0.7646 1.0611 0.3612  0.1991  0.0608  419 VAL C CB  
13187 C CG1 . VAL C 419 ? 0.7613 0.6076 0.8948 0.3657  0.2034  0.0515  419 VAL C CG1 
13188 C CG2 . VAL C 419 ? 0.7912 0.6497 0.9516 0.3462  0.1951  0.0612  419 VAL C CG2 
13189 N N   . VAL C 420 ? 0.9552 0.9140 1.2147 0.3605  0.2110  0.0860  420 VAL C N   
13190 C CA  . VAL C 420 ? 0.8011 0.7857 1.0892 0.3488  0.1993  0.0908  420 VAL C CA  
13191 C C   . VAL C 420 ? 0.8979 0.9153 1.2180 0.3621  0.2032  0.0989  420 VAL C C   
13192 O O   . VAL C 420 ? 0.9336 0.9680 1.2669 0.3707  0.2184  0.1035  420 VAL C O   
13193 C CB  . VAL C 420 ? 0.6623 0.6599 0.9639 0.3284  0.1987  0.0913  420 VAL C CB  
13194 C CG1 . VAL C 420 ? 0.6491 0.6698 0.9766 0.3163  0.1843  0.0933  420 VAL C CG1 
13195 C CG2 . VAL C 420 ? 0.9312 0.8982 1.2016 0.3176  0.1972  0.0839  420 VAL C CG2 
13196 N N   . ASN C 421 ? 0.8220 0.8496 1.1543 0.3642  0.1902  0.1015  421 ASN C N   
13197 C CA  . ASN C 421 ? 0.8985 0.9608 1.2643 0.3767  0.1921  0.1097  421 ASN C CA  
13198 C C   . ASN C 421 ? 0.8581 0.9587 1.2625 0.3622  0.1917  0.1149  421 ASN C C   
13199 O O   . ASN C 421 ? 0.8802 0.9815 1.2873 0.3435  0.1794  0.1115  421 ASN C O   
13200 C CB  . ASN C 421 ? 0.8952 0.9563 1.2609 0.3848  0.1778  0.1115  421 ASN C CB  
13201 C CG  . ASN C 421 ? 0.9747 1.0689 1.3717 0.4012  0.1806  0.1199  421 ASN C CG  
13202 O OD1 . ASN C 421 ? 1.1162 1.2486 1.5493 0.3945  0.1783  0.1253  421 ASN C OD1 
13203 N ND2 . ASN C 421 ? 0.9215 1.0005 1.3020 0.4178  0.1825  0.1189  421 ASN C ND2 
13204 N N   . THR C 422 ? 0.7364 0.8679 1.1704 0.3709  0.2046  0.1229  422 THR C N   
13205 C CA  . THR C 422 ? 0.8514 1.0199 1.3268 0.3560  0.2054  0.1290  422 THR C CA  
13206 C C   . THR C 422 ? 0.9462 1.1395 1.4488 0.3479  0.1862  0.1299  422 THR C C   
13207 O O   . THR C 422 ? 0.9792 1.1872 1.5030 0.3282  0.1782  0.1288  422 THR C O   
13208 C CB  . THR C 422 ? 0.7964 0.9948 1.2993 0.3688  0.2246  0.1394  422 THR C CB  
13209 O OG1 . THR C 422 ? 0.9666 1.1412 1.4399 0.3772  0.2416  0.1375  422 THR C OG1 
13210 C CG2 . THR C 422 ? 1.1162 1.3530 1.6656 0.3529  0.2263  0.1474  422 THR C CG2 
13211 N N   . GLN C 423 ? 0.8971 1.0942 1.3987 0.3629  0.1784  0.1316  423 GLN C N   
13212 C CA  . GLN C 423 ? 0.9109 1.1364 1.4395 0.3581  0.1599  0.1334  423 GLN C CA  
13213 C C   . GLN C 423 ? 0.9372 1.1405 1.4407 0.3451  0.1411  0.1249  423 GLN C C   
13214 O O   . GLN C 423 ? 0.9253 1.1518 1.4490 0.3376  0.1244  0.1245  423 GLN C O   
13215 C CB  . GLN C 423 ? 0.6655 0.9048 1.2026 0.3811  0.1593  0.1400  423 GLN C CB  
13216 C CG  . GLN C 423 ? 0.6716 0.9363 1.2342 0.3968  0.1781  0.1489  423 GLN C CG  
13217 C CD  . GLN C 423 ? 0.7951 1.1122 1.4117 0.3910  0.1745  0.1570  423 GLN C CD  
13218 O OE1 . GLN C 423 ? 1.0197 1.3586 1.6551 0.3914  0.1580  0.1586  423 GLN C OE1 
13219 N NE2 . GLN C 423 ? 0.9896 1.3282 1.6325 0.3855  0.1896  0.1630  423 GLN C NE2 
13220 N N   . ILE C 424 ? 0.9025 1.0647 1.3647 0.3433  0.1437  0.1186  424 ILE C N   
13221 C CA  . ILE C 424 ? 0.9077 1.0491 1.3440 0.3338  0.1272  0.1121  424 ILE C CA  
13222 C C   . ILE C 424 ? 0.9019 1.0207 1.3188 0.3161  0.1292  0.1044  424 ILE C C   
13223 O O   . ILE C 424 ? 0.9076 1.0401 1.3394 0.2994  0.1202  0.1005  424 ILE C O   
13224 C CB  . ILE C 424 ? 0.8947 1.0060 1.2985 0.3496  0.1265  0.1129  424 ILE C CB  
13225 C CG1 . ILE C 424 ? 1.4282 1.5536 1.8469 0.3718  0.1319  0.1208  424 ILE C CG1 
13226 C CG2 . ILE C 424 ? 1.0056 1.1066 1.3912 0.3436  0.1089  0.1107  424 ILE C CG2 
13227 C CD1 . ILE C 424 ? 1.3931 1.4837 1.7804 0.3877  0.1334  0.1212  424 ILE C CD1 
13228 N N   . GLY C 425 ? 1.2557 1.3408 1.6409 0.3202  0.1398  0.1017  425 GLY C N   
13229 C CA  . GLY C 425 ? 1.2023 1.2634 1.5652 0.3052  0.1414  0.0947  425 GLY C CA  
13230 C C   . GLY C 425 ? 1.0075 1.0852 1.3932 0.2898  0.1458  0.0938  425 GLY C C   
13231 O O   . GLY C 425 ? 1.0197 1.1225 1.4354 0.2933  0.1554  0.1001  425 GLY C O   
13232 N N   . PRO C 426 ? 1.1521 1.2165 1.5256 0.2735  0.1396  0.0870  426 PRO C N   
13233 C CA  . PRO C 426 ? 1.0082 1.0824 1.4012 0.2586  0.1441  0.0860  426 PRO C CA  
13234 C C   . PRO C 426 ? 0.9756 1.0321 1.3539 0.2616  0.1626  0.0880  426 PRO C C   
13235 O O   . PRO C 426 ? 1.1303 1.1638 1.4792 0.2727  0.1682  0.0869  426 PRO C O   
13236 C CB  . PRO C 426 ? 0.6038 0.6633 0.9799 0.2440  0.1305  0.0769  426 PRO C CB  
13237 C CG  . PRO C 426 ? 0.9359 0.9670 1.2726 0.2520  0.1279  0.0743  426 PRO C CG  
13238 C CD  . PRO C 426 ? 1.0992 1.1387 1.4403 0.2691  0.1286  0.0806  426 PRO C CD  
13239 N N   . MET C 427 ? 0.8070 0.8736 1.2053 0.2518  0.1712  0.0909  427 MET C N   
13240 C CA  . MET C 427 ? 0.7218 0.7753 1.1065 0.2570  0.1900  0.0946  427 MET C CA  
13241 C C   . MET C 427 ? 0.7938 0.8276 1.1638 0.2429  0.1913  0.0902  427 MET C C   
13242 O O   . MET C 427 ? 0.8096 0.8464 1.1907 0.2278  0.1795  0.0856  427 MET C O   
13243 C CB  . MET C 427 ? 0.7415 0.8253 1.1621 0.2615  0.2041  0.1058  427 MET C CB  
13244 C CG  . MET C 427 ? 0.9000 0.9979 1.3262 0.2814  0.2099  0.1111  427 MET C CG  
13245 S SD  . MET C 427 ? 0.9931 1.0556 1.3700 0.3007  0.2180  0.1062  427 MET C SD  
13246 C CE  . MET C 427 ? 0.7445 0.8295 1.1384 0.3235  0.2237  0.1129  427 MET C CE  
13247 N N   . GLN C 428 ? 0.7882 0.8028 1.1335 0.2488  0.2047  0.0911  428 GLN C N   
13248 C CA  . GLN C 428 ? 0.7322 0.7283 1.0625 0.2378  0.2075  0.0882  428 GLN C CA  
13249 C C   . GLN C 428 ? 0.7808 0.7570 1.0899 0.2276  0.1917  0.0778  428 GLN C C   
13250 O O   . GLN C 428 ? 0.9280 0.9002 1.2416 0.2140  0.1878  0.0750  428 GLN C O   
13251 C CB  . GLN C 428 ? 0.7545 0.7691 1.1187 0.2264  0.2144  0.0956  428 GLN C CB  
13252 C CG  . GLN C 428 ? 0.6537 0.6846 1.0325 0.2366  0.2342  0.1078  428 GLN C CG  
13253 C CD  . GLN C 428 ? 0.8302 0.8391 1.1742 0.2456  0.2474  0.1082  428 GLN C CD  
13254 O OE1 . GLN C 428 ? 0.8756 0.8718 1.2112 0.2370  0.2510  0.1087  428 GLN C OE1 
13255 N NE2 . GLN C 428 ? 0.8440 0.8472 1.1663 0.2636  0.2541  0.1074  428 GLN C NE2 
13256 N N   . THR C 429 ? 0.7808 0.7442 1.0671 0.2349  0.1834  0.0729  429 THR C N   
13257 C CA  . THR C 429 ? 0.6547 0.6006 0.9189 0.2275  0.1701  0.0648  429 THR C CA  
13258 C C   . THR C 429 ? 0.8940 0.8145 1.1233 0.2371  0.1721  0.0623  429 THR C C   
13259 O O   . THR C 429 ? 1.0571 0.9754 1.2817 0.2501  0.1806  0.0653  429 THR C O   
13260 C CB  . THR C 429 ? 0.7477 0.7087 1.0258 0.2243  0.1541  0.0625  429 THR C CB  
13261 O OG1 . THR C 429 ? 1.0345 0.9961 1.3062 0.2376  0.1518  0.0650  429 THR C OG1 
13262 C CG2 . THR C 429 ? 0.7880 0.7774 1.1055 0.2167  0.1511  0.0649  429 THR C CG2 
13263 N N   . VAL C 430 ? 0.9564 0.8581 1.1621 0.2309  0.1642  0.0566  430 VAL C N   
13264 C CA  . VAL C 430 ? 0.8015 0.6791 0.9771 0.2378  0.1644  0.0543  430 VAL C CA  
13265 C C   . VAL C 430 ? 0.8476 0.7242 1.0198 0.2450  0.1553  0.0554  430 VAL C C   
13266 O O   . VAL C 430 ? 0.9845 0.8404 1.1342 0.2488  0.1531  0.0539  430 VAL C O   
13267 C CB  . VAL C 430 ? 0.8888 0.7475 1.0416 0.2287  0.1618  0.0493  430 VAL C CB  
13268 C CG1 . VAL C 430 ? 0.8292 0.6871 0.9840 0.2239  0.1718  0.0495  430 VAL C CG1 
13269 C CG2 . VAL C 430 ? 0.8808 0.7432 1.0335 0.2192  0.1488  0.0463  430 VAL C CG2 
13270 N N   . LYS C 431 ? 0.8051 0.7039 1.0004 0.2470  0.1497  0.0586  431 LYS C N   
13271 C CA  . LYS C 431 ? 0.8583 0.7572 1.0506 0.2543  0.1406  0.0611  431 LYS C CA  
13272 C C   . LYS C 431 ? 0.8671 0.7462 1.0432 0.2677  0.1455  0.0627  431 LYS C C   
13273 O O   . LYS C 431 ? 1.0146 0.8772 1.1736 0.2689  0.1385  0.0630  431 LYS C O   
13274 C CB  . LYS C 431 ? 0.7664 0.6946 0.9879 0.2567  0.1348  0.0648  431 LYS C CB  
13275 C CG  . LYS C 431 ? 0.9096 0.8415 1.1269 0.2585  0.1207  0.0664  431 LYS C CG  
13276 C CD  . LYS C 431 ? 0.8999 0.8624 1.1460 0.2621  0.1138  0.0698  431 LYS C CD  
13277 C CE  . LYS C 431 ? 0.9186 0.8847 1.1710 0.2785  0.1164  0.0765  431 LYS C CE  
13278 N NZ  . LYS C 431 ? 0.8742 0.8288 1.1092 0.2853  0.1071  0.0800  431 LYS C NZ  
13279 N N   . PRO C 432 ? 0.7698 0.6488 0.9499 0.2782  0.1571  0.0636  432 PRO C N   
13280 C CA  . PRO C 432 ? 0.8575 0.7145 1.0201 0.2916  0.1601  0.0629  432 PRO C CA  
13281 C C   . PRO C 432 ? 0.9141 0.7409 1.0482 0.2865  0.1567  0.0581  432 PRO C C   
13282 O O   . PRO C 432 ? 0.9243 0.7326 1.0464 0.2926  0.1518  0.0585  432 PRO C O   
13283 C CB  . PRO C 432 ? 0.7406 0.6032 0.9085 0.3018  0.1745  0.0628  432 PRO C CB  
13284 C CG  . PRO C 432 ? 0.8654 0.7603 1.0635 0.2971  0.1775  0.0676  432 PRO C CG  
13285 C CD  . PRO C 432 ? 0.9828 0.8812 1.1829 0.2794  0.1684  0.0657  432 PRO C CD  
13286 N N   . LEU C 433 ? 0.8793 0.7014 1.0042 0.2752  0.1588  0.0544  433 LEU C N   
13287 C CA  . LEU C 433 ? 0.8662 0.6631 0.9666 0.2696  0.1553  0.0503  433 LEU C CA  
13288 C C   . LEU C 433 ? 1.0288 0.8239 1.1263 0.2619  0.1434  0.0531  433 LEU C C   
13289 O O   . LEU C 433 ? 1.1651 0.9402 1.2483 0.2630  0.1387  0.0536  433 LEU C O   
13290 C CB  . LEU C 433 ? 0.8680 0.6633 0.9610 0.2607  0.1609  0.0464  433 LEU C CB  
13291 C CG  . LEU C 433 ? 0.8438 0.6168 0.9137 0.2542  0.1572  0.0422  433 LEU C CG  
13292 C CD1 . LEU C 433 ? 0.6772 0.4269 0.7308 0.2638  0.1582  0.0385  433 LEU C CD1 
13293 C CD2 . LEU C 433 ? 0.8236 0.5986 0.8887 0.2465  0.1628  0.0395  433 LEU C CD2 
13294 N N   . ALA C 434 ? 0.9195 0.7355 1.0306 0.2546  0.1384  0.0552  434 ALA C N   
13295 C CA  . ALA C 434 ? 0.8540 0.6720 0.9609 0.2489  0.1276  0.0581  434 ALA C CA  
13296 C C   . ALA C 434 ? 1.0437 0.8576 1.1514 0.2588  0.1223  0.0644  434 ALA C C   
13297 O O   . ALA C 434 ? 1.1030 0.9044 1.1982 0.2570  0.1163  0.0681  434 ALA C O   
13298 C CB  . ALA C 434 ? 0.7608 0.6034 0.8831 0.2418  0.1227  0.0573  434 ALA C CB  
13299 N N   . ASP C 435 ? 0.9886 0.8135 1.1120 0.2696  0.1251  0.0666  435 ASP C N   
13300 C CA  . ASP C 435 ? 0.8845 0.7065 1.0111 0.2812  0.1207  0.0730  435 ASP C CA  
13301 C C   . ASP C 435 ? 0.9431 0.7331 1.0519 0.2867  0.1219  0.0732  435 ASP C C   
13302 O O   . ASP C 435 ? 0.9744 0.7539 1.0778 0.2892  0.1152  0.0796  435 ASP C O   
13303 C CB  . ASP C 435 ? 0.9332 0.7740 1.0810 0.2928  0.1256  0.0745  435 ASP C CB  
13304 C CG  . ASP C 435 ? 1.1535 1.0277 1.3242 0.2888  0.1208  0.0763  435 ASP C CG  
13305 O OD1 . ASP C 435 ? 1.1405 1.0223 1.3088 0.2771  0.1137  0.0747  435 ASP C OD1 
13306 O OD2 . ASP C 435 ? 1.1799 1.0731 1.3714 0.2976  0.1239  0.0788  435 ASP C OD2 
13307 N N   . VAL C 436 ? 0.8657 0.6402 0.9657 0.2885  0.1300  0.0663  436 VAL C N   
13308 C CA  . VAL C 436 ? 0.9901 0.7328 1.0736 0.2933  0.1302  0.0637  436 VAL C CA  
13309 C C   . VAL C 436 ? 1.1237 0.8505 1.1931 0.2809  0.1235  0.0653  436 VAL C C   
13310 O O   . VAL C 436 ? 1.1394 0.8432 1.2011 0.2832  0.1192  0.0680  436 VAL C O   
13311 C CB  . VAL C 436 ? 0.9400 0.6732 1.0158 0.2987  0.1399  0.0546  436 VAL C CB  
13312 C CG1 . VAL C 436 ? 1.0874 0.7867 1.1447 0.3018  0.1380  0.0493  436 VAL C CG1 
13313 C CG2 . VAL C 436 ? 1.0151 0.7635 1.1048 0.3133  0.1477  0.0548  436 VAL C CG2 
13314 N N   . LEU C 437 ? 1.0271 0.7661 1.0944 0.2682  0.1229  0.0641  437 LEU C N   
13315 C CA  . LEU C 437 ? 0.8922 0.6206 0.9475 0.2569  0.1178  0.0662  437 LEU C CA  
13316 C C   . LEU C 437 ? 1.0036 0.7378 1.0614 0.2558  0.1099  0.0768  437 LEU C C   
13317 O O   . LEU C 437 ? 1.0154 0.7326 1.0652 0.2526  0.1060  0.0822  437 LEU C O   
13318 C CB  . LEU C 437 ? 0.7878 0.5282 0.8399 0.2457  0.1203  0.0614  437 LEU C CB  
13319 C CG  . LEU C 437 ? 1.0175 0.7486 1.0622 0.2450  0.1277  0.0526  437 LEU C CG  
13320 C CD1 . LEU C 437 ? 0.7333 0.4820 0.7818 0.2376  0.1315  0.0493  437 LEU C CD1 
13321 C CD2 . LEU C 437 ? 0.8851 0.5926 0.9144 0.2403  0.1253  0.0503  437 LEU C CD2 
13322 N N   . VAL C 438 ? 0.9284 0.6869 0.9978 0.2586  0.1073  0.0803  438 VAL C N   
13323 C CA  . VAL C 438 ? 0.9767 0.7441 1.0466 0.2593  0.0994  0.0908  438 VAL C CA  
13324 C C   . VAL C 438 ? 1.0464 0.7969 1.1177 0.2700  0.0973  0.0988  438 VAL C C   
13325 O O   . VAL C 438 ? 1.0979 0.8397 1.1630 0.2683  0.0927  0.1088  438 VAL C O   
13326 C CB  . VAL C 438 ? 0.8476 0.6458 0.9297 0.2606  0.0957  0.0907  438 VAL C CB  
13327 C CG1 . VAL C 438 ? 0.9817 0.7894 1.0673 0.2684  0.0881  0.1016  438 VAL C CG1 
13328 C CG2 . VAL C 438 ? 0.9421 0.7540 1.0196 0.2492  0.0942  0.0856  438 VAL C CG2 
13329 N N   . SER C 439 ? 1.0486 0.7947 1.1281 0.2810  0.1012  0.0953  439 SER C N   
13330 C CA  . SER C 439 ? 1.0032 0.7323 1.0849 0.2931  0.0993  0.1019  439 SER C CA  
13331 C C   . SER C 439 ? 0.9964 0.6916 1.0659 0.2892  0.0982  0.1034  439 SER C C   
13332 O O   . SER C 439 ? 1.1490 0.8301 1.2184 0.2932  0.0936  0.1138  439 SER C O   
13333 C CB  . SER C 439 ? 0.9319 0.6619 1.0230 0.3064  0.1052  0.0958  439 SER C CB  
13334 O OG  . SER C 439 ? 1.0682 0.7797 1.1506 0.3057  0.1117  0.0851  439 SER C OG  
13335 N N   . GLY C 440 ? 0.9241 0.6068 0.9846 0.2813  0.1018  0.0937  440 GLY C N   
13336 C CA  . GLY C 440 ? 0.9285 0.5806 0.9794 0.2760  0.0997  0.0932  440 GLY C CA  
13337 C C   . GLY C 440 ? 1.0337 0.6612 1.0802 0.2841  0.1027  0.0820  440 GLY C C   
13338 O O   . GLY C 440 ? 1.1582 0.7582 1.1974 0.2800  0.0997  0.0793  440 GLY C O   
13339 N N   . VAL C 441 ? 1.0736 0.7114 1.1245 0.2960  0.1087  0.0751  441 VAL C N   
13340 C CA  . VAL C 441 ? 1.0826 0.7043 1.1271 0.3030  0.1108  0.0624  441 VAL C CA  
13341 C C   . VAL C 441 ? 1.0051 0.6159 1.0362 0.2934  0.1123  0.0524  441 VAL C C   
13342 O O   . VAL C 441 ? 1.0389 0.6251 1.0609 0.2920  0.1077  0.0446  441 VAL C O   
13343 C CB  . VAL C 441 ? 1.1463 0.7913 1.1991 0.3142  0.1173  0.0580  441 VAL C CB  
13344 C CG1 . VAL C 441 ? 1.0634 0.6991 1.1063 0.3186  0.1202  0.0436  441 VAL C CG1 
13345 C CG2 . VAL C 441 ? 0.8160 0.4685 0.8818 0.3253  0.1145  0.0667  441 VAL C CG2 
13346 N N   . LEU C 442 ? 1.0654 0.6953 1.0962 0.2860  0.1172  0.0527  442 LEU C N   
13347 C CA  . LEU C 442 ? 1.0335 0.6578 1.0527 0.2756  0.1180  0.0450  442 LEU C CA  
13348 C C   . LEU C 442 ? 1.0932 0.7198 1.1128 0.2607  0.1119  0.0533  442 LEU C C   
13349 O O   . LEU C 442 ? 1.0500 0.6994 1.0768 0.2560  0.1118  0.0608  442 LEU C O   
13350 C CB  . LEU C 442 ? 0.8513 0.4991 0.8708 0.2745  0.1263  0.0401  442 LEU C CB  
13351 C CG  . LEU C 442 ? 0.9329 0.5823 0.9481 0.2849  0.1332  0.0306  442 LEU C CG  
13352 C CD1 . LEU C 442 ? 0.8084 0.4816 0.8276 0.2832  0.1424  0.0301  442 LEU C CD1 
13353 C CD2 . LEU C 442 ? 1.1843 0.8107 1.1825 0.2841  0.1296  0.0196  442 LEU C CD2 
13354 N N   . ARG C 443 ? 0.9992 0.6031 1.0116 0.2535  0.1065  0.0518  443 ARG C N   
13355 C CA  . ARG C 443 ? 1.0241 0.6306 1.0378 0.2396  0.1015  0.0608  443 ARG C CA  
13356 C C   . ARG C 443 ? 1.0391 0.6702 1.0503 0.2304  0.1052  0.0600  443 ARG C C   
13357 O O   . ARG C 443 ? 1.0196 0.6645 1.0338 0.2227  0.1033  0.0691  443 ARG C O   
13358 C CB  . ARG C 443 ? 1.0294 0.6077 1.0383 0.2330  0.0953  0.0580  443 ARG C CB  
13359 C CG  . ARG C 443 ? 0.9176 0.4687 0.9312 0.2395  0.0898  0.0616  443 ARG C CG  
13360 C CD  . ARG C 443 ? 1.1124 0.6669 1.1359 0.2346  0.0863  0.0794  443 ARG C CD  
13361 N NE  . ARG C 443 ? 1.1216 0.6948 1.1508 0.2445  0.0893  0.0869  443 ARG C NE  
13362 C CZ  . ARG C 443 ? 1.1784 0.7665 1.2134 0.2421  0.0879  0.1022  443 ARG C CZ  
13363 N NH1 . ARG C 443 ? 1.3025 0.8897 1.3386 0.2303  0.0849  0.1128  443 ARG C NH1 
13364 N NH2 . ARG C 443 ? 1.2590 0.8647 1.2990 0.2520  0.0894  0.1073  443 ARG C NH2 
13365 N N   . GLY C 444 ? 1.0130 0.6491 1.0184 0.2323  0.1106  0.0494  444 GLY C N   
13366 C CA  . GLY C 444 ? 0.9471 0.6036 0.9506 0.2248  0.1145  0.0480  444 GLY C CA  
13367 C C   . GLY C 444 ? 0.8744 0.5321 0.8711 0.2287  0.1209  0.0374  444 GLY C C   
13368 O O   . GLY C 444 ? 1.0249 0.6708 1.0178 0.2388  0.1234  0.0310  444 GLY C O   
13369 N N   . ALA C 445 ? 0.9166 0.5884 0.9109 0.2217  0.1242  0.0360  445 ALA C N   
13370 C CA  . ALA C 445 ? 0.8922 0.5666 0.8798 0.2249  0.1310  0.0282  445 ALA C CA  
13371 C C   . ALA C 445 ? 0.9608 0.6335 0.9395 0.2156  0.1293  0.0259  445 ALA C C   
13372 O O   . ALA C 445 ? 0.9965 0.6807 0.9785 0.2069  0.1276  0.0308  445 ALA C O   
13373 C CB  . ALA C 445 ? 0.6751 0.3713 0.6727 0.2272  0.1380  0.0299  445 ALA C CB  
13374 N N   . ALA C 446 ? 0.9033 0.5625 0.8699 0.2182  0.1292  0.0182  446 ALA C N   
13375 C CA  . ALA C 446 ? 0.8170 0.4753 0.7753 0.2106  0.1269  0.0156  446 ALA C CA  
13376 C C   . ALA C 446 ? 0.9395 0.6035 0.8888 0.2158  0.1345  0.0101  446 ALA C C   
13377 O O   . ALA C 446 ? 0.9589 0.6212 0.9050 0.2264  0.1403  0.0064  446 ALA C O   
13378 C CB  . ALA C 446 ? 0.8861 0.5237 0.8383 0.2081  0.1181  0.0115  446 ALA C CB  
13379 N N   . ALA C 447 ? 0.8958 0.5674 0.8412 0.2091  0.1349  0.0106  447 ALA C N   
13380 C CA  . ALA C 447 ? 0.9098 0.5870 0.8465 0.2136  0.1420  0.0073  447 ALA C CA  
13381 C C   . ALA C 447 ? 0.9202 0.5890 0.8437 0.2113  0.1365  0.0020  447 ALA C C   
13382 O O   . ALA C 447 ? 0.9530 0.6274 0.8785 0.2025  0.1329  0.0049  447 ALA C O   
13383 C CB  . ALA C 447 ? 0.7555 0.4500 0.7006 0.2087  0.1477  0.0130  447 ALA C CB  
13384 N N   . VAL C 448 ? 0.9157 0.5723 0.8258 0.2200  0.1354  -0.0061 448 VAL C N   
13385 C CA  . VAL C 448 ? 0.8987 0.5480 0.7958 0.2185  0.1285  -0.0126 448 VAL C CA  
13386 C C   . VAL C 448 ? 0.9360 0.5958 0.8223 0.2244  0.1365  -0.0128 448 VAL C C   
13387 O O   . VAL C 448 ? 0.9798 0.6390 0.8562 0.2361  0.1437  -0.0157 448 VAL C O   
13388 C CB  . VAL C 448 ? 1.0078 0.6364 0.8948 0.2245  0.1203  -0.0230 448 VAL C CB  
13389 C CG1 . VAL C 448 ? 0.9518 0.5746 0.8266 0.2222  0.1114  -0.0306 448 VAL C CG1 
13390 C CG2 . VAL C 448 ? 1.0395 0.6562 0.9391 0.2186  0.1129  -0.0209 448 VAL C CG2 
13391 N N   . VAL C 449 ? 1.0769 0.7469 0.9653 0.2168  0.1358  -0.0086 449 VAL C N   
13392 C CA  . VAL C 449 ? 1.0745 0.7538 0.9534 0.2219  0.1432  -0.0071 449 VAL C CA  
13393 C C   . VAL C 449 ? 1.0046 0.6831 0.8750 0.2179  0.1341  -0.0107 449 VAL C C   
13394 O O   . VAL C 449 ? 1.1519 0.8244 1.0278 0.2098  0.1235  -0.0131 449 VAL C O   
13395 C CB  . VAL C 449 ? 0.9784 0.6714 0.8702 0.2186  0.1526  0.0021  449 VAL C CB  
13396 C CG1 . VAL C 449 ? 1.1098 0.8044 1.0122 0.2219  0.1592  0.0048  449 VAL C CG1 
13397 C CG2 . VAL C 449 ? 0.6658 0.3648 0.5686 0.2068  0.1472  0.0061  449 VAL C CG2 
13398 N N   . GLY C 450 ? 0.8394 0.5245 0.6983 0.2233  0.1380  -0.0103 450 GLY C N   
13399 C CA  . GLY C 450 ? 0.9137 0.6011 0.7666 0.2194  0.1286  -0.0131 450 GLY C CA  
13400 C C   . GLY C 450 ? 1.0123 0.6994 0.8442 0.2303  0.1282  -0.0185 450 GLY C C   
13401 O O   . GLY C 450 ? 1.0939 0.7789 0.9143 0.2421  0.1366  -0.0194 450 GLY C O   
13402 N N   . CYS C 451 ? 0.9835 0.6744 0.8105 0.2273  0.1186  -0.0213 451 CYS C N   
13403 C CA  . CYS C 451 ? 1.1117 0.8049 0.9171 0.2384  0.1170  -0.0260 451 CYS C CA  
13404 C C   . CYS C 451 ? 0.9545 0.6371 0.7494 0.2391  0.1013  -0.0396 451 CYS C C   
13405 O O   . CYS C 451 ? 0.9685 0.6376 0.7695 0.2349  0.0951  -0.0459 451 CYS C O   
13406 C CB  . CYS C 451 ? 1.0559 0.7637 0.8630 0.2361  0.1174  -0.0191 451 CYS C CB  
13407 S SG  . CYS C 451 ? 0.8703 0.5879 0.7008 0.2257  0.1265  -0.0062 451 CYS C SG  
13408 N N   . ASN C 452 ? 1.0622 0.7505 0.8422 0.2445  0.0944  -0.0441 452 ASN C N   
13409 C CA  . ASN C 452 ? 1.1036 0.7825 0.8738 0.2447  0.0769  -0.0587 452 ASN C CA  
13410 C C   . ASN C 452 ? 1.0918 0.7839 0.8708 0.2356  0.0660  -0.0569 452 ASN C C   
13411 O O   . ASN C 452 ? 1.3085 1.0159 1.0831 0.2401  0.0725  -0.0488 452 ASN C O   
13412 C CB  . ASN C 452 ? 1.1318 0.8050 0.8720 0.2627  0.0769  -0.0688 452 ASN C CB  
13413 C CG  . ASN C 452 ? 1.1686 0.8252 0.9016 0.2705  0.0813  -0.0758 452 ASN C CG  
13414 O OD1 . ASN C 452 ? 1.2999 0.9566 1.0126 0.2867  0.0910  -0.0770 452 ASN C OD1 
13415 N ND2 . ASN C 452 ? 1.2472 0.8904 0.9972 0.2599  0.0746  -0.0794 452 ASN C ND2 
13416 N N   . ASN C 453 ? 1.0411 0.7280 0.8339 0.2232  0.0504  -0.0633 453 ASN C N   
13417 C CA  . ASN C 453 ? 0.9672 0.6694 0.7730 0.2134  0.0403  -0.0602 453 ASN C CA  
13418 C C   . ASN C 453 ? 1.0217 0.7172 0.8236 0.2107  0.0195  -0.0750 453 ASN C C   
13419 O O   . ASN C 453 ? 1.2525 0.9293 1.0592 0.2055  0.0110  -0.0839 453 ASN C O   
13420 C CB  . ASN C 453 ? 1.0387 0.7470 0.8735 0.1975  0.0426  -0.0490 453 ASN C CB  
13421 C CG  . ASN C 453 ? 1.0308 0.7614 0.8789 0.1910  0.0402  -0.0405 453 ASN C CG  
13422 O OD1 . ASN C 453 ? 1.0247 0.7636 0.8702 0.1908  0.0278  -0.0458 453 ASN C OD1 
13423 N ND2 . ASN C 453 ? 0.9107 0.6521 0.7730 0.1862  0.0514  -0.0276 453 ASN C ND2 
13424 N N   . PRO C 454 ? 0.9942 0.7036 0.7885 0.2137  0.0098  -0.0784 454 PRO C N   
13425 C CA  . PRO C 454 ? 0.9997 0.7025 0.7920 0.2101  -0.0123 -0.0942 454 PRO C CA  
13426 C C   . PRO C 454 ? 1.0014 0.7013 0.8258 0.1896  -0.0250 -0.0937 454 PRO C C   
13427 O O   . PRO C 454 ? 1.1307 0.8221 0.9582 0.1841  -0.0443 -0.1069 454 PRO C O   
13428 C CB  . PRO C 454 ? 1.0325 0.7562 0.8129 0.2175  -0.0183 -0.0945 454 PRO C CB  
13429 C CG  . PRO C 454 ? 1.1341 0.8700 0.9040 0.2286  0.0018  -0.0806 454 PRO C CG  
13430 C CD  . PRO C 454 ? 1.0980 0.8293 0.8859 0.2209  0.0172  -0.0686 454 PRO C CD  
13431 N N   . LYS C 455 ? 0.9755 0.6822 0.8239 0.1785  -0.0147 -0.0785 455 LYS C N   
13432 C CA  . LYS C 455 ? 1.0309 0.7359 0.9105 0.1595  -0.0241 -0.0747 455 LYS C CA  
13433 C C   . LYS C 455 ? 1.1059 0.7813 0.9865 0.1567  -0.0270 -0.0824 455 LYS C C   
13434 O O   . LYS C 455 ? 1.1750 0.8416 1.0779 0.1423  -0.0387 -0.0835 455 LYS C O   
13435 C CB  . LYS C 455 ? 0.9749 0.6988 0.8764 0.1511  -0.0108 -0.0552 455 LYS C CB  
13436 C CG  . LYS C 455 ? 1.0938 0.8440 0.9913 0.1573  -0.0037 -0.0466 455 LYS C CG  
13437 C CD  . LYS C 455 ? 0.8228 0.5912 0.7424 0.1491  0.0072  -0.0295 455 LYS C CD  
13438 C CE  . LYS C 455 ? 0.8897 0.6854 0.8135 0.1514  0.0073  -0.0227 455 LYS C CE  
13439 N NZ  . LYS C 455 ? 1.0439 0.8551 0.9791 0.1503  0.0223  -0.0075 455 LYS C NZ  
13440 N N   . VAL C 456 ? 1.1035 0.7645 0.9615 0.1710  -0.0159 -0.0868 456 VAL C N   
13441 C CA  . VAL C 456 ? 0.9762 0.6100 0.8311 0.1728  -0.0162 -0.0941 456 VAL C CA  
13442 C C   . VAL C 456 ? 1.0992 0.7174 0.9227 0.1895  -0.0219 -0.1127 456 VAL C C   
13443 O O   . VAL C 456 ? 1.0555 0.6855 0.8563 0.2034  -0.0153 -0.1139 456 VAL C O   
13444 C CB  . VAL C 456 ? 0.8498 0.4843 0.7066 0.1764  0.0040  -0.0813 456 VAL C CB  
13445 C CG1 . VAL C 456 ? 1.0191 0.6275 0.8763 0.1780  0.0038  -0.0869 456 VAL C CG1 
13446 C CG2 . VAL C 456 ? 0.8180 0.4717 0.6998 0.1636  0.0112  -0.0632 456 VAL C CG2 
13447 N N   . VAL C 457 ? 1.2065 0.7980 1.0282 0.1892  -0.0334 -0.1267 457 VAL C N   
13448 C CA  . VAL C 457 ? 1.0425 0.6176 0.8314 0.2077  -0.0378 -0.1456 457 VAL C CA  
13449 C C   . VAL C 457 ? 1.1713 0.7507 0.9415 0.2243  -0.0156 -0.1386 457 VAL C C   
13450 O O   . VAL C 457 ? 1.2478 0.8239 1.0323 0.2203  -0.0034 -0.1274 457 VAL C O   
13451 C CB  . VAL C 457 ? 1.0041 0.5468 0.7953 0.2053  -0.0528 -0.1618 457 VAL C CB  
13452 C CG1 . VAL C 457 ? 1.2254 0.7512 0.9806 0.2269  -0.0552 -0.1814 457 VAL C CG1 
13453 C CG2 . VAL C 457 ? 1.0183 0.5567 0.8316 0.1874  -0.0756 -0.1683 457 VAL C CG2 
13454 N N   . GLN C 458 ? 1.0804 0.6677 0.8208 0.2421  -0.0107 -0.1442 458 GLN C N   
13455 C CA  . GLN C 458 ? 1.2037 0.7989 0.9297 0.2568  0.0117  -0.1346 458 GLN C CA  
13456 C C   . GLN C 458 ? 1.1796 0.7553 0.9072 0.2616  0.0191  -0.1367 458 GLN C C   
13457 O O   . GLN C 458 ? 1.1663 0.7199 0.8811 0.2688  0.0085  -0.1537 458 GLN C O   
13458 C CB  . GLN C 458 ? 1.2114 0.8144 0.9029 0.2770  0.0142  -0.1419 458 GLN C CB  
13459 C CG  . GLN C 458 ? 1.0430 0.6657 0.7276 0.2865  0.0364  -0.1252 458 GLN C CG  
13460 C CD  . GLN C 458 ? 1.3814 0.9981 1.0427 0.3065  0.0500  -0.1281 458 GLN C CD  
13461 O OE1 . GLN C 458 ? 1.4001 1.0029 1.0381 0.3196  0.0422  -0.1449 458 GLN C OE1 
13462 N NE2 . GLN C 458 ? 1.4365 1.0641 1.1046 0.3094  0.0705  -0.1119 458 GLN C NE2 
13463 N N   . ASP C 459 ? 1.0421 0.6255 0.7848 0.2583  0.0358  -0.1207 459 ASP C N   
13464 C CA  . ASP C 459 ? 1.1391 0.7081 0.8840 0.2645  0.0447  -0.1207 459 ASP C CA  
13465 C C   . ASP C 459 ? 1.1908 0.7380 0.9552 0.2520  0.0321  -0.1254 459 ASP C C   
13466 O O   . ASP C 459 ? 1.2376 0.7754 1.0102 0.2540  0.0396  -0.1215 459 ASP C O   
13467 C CB  . ASP C 459 ? 1.3602 0.9218 1.0744 0.2872  0.0500  -0.1322 459 ASP C CB  
13468 C CG  . ASP C 459 ? 1.3857 0.9690 1.0812 0.3000  0.0636  -0.1251 459 ASP C CG  
13469 O OD1 . ASP C 459 ? 1.2012 0.8034 0.9108 0.2922  0.0740  -0.1087 459 ASP C OD1 
13470 O OD2 . ASP C 459 ? 1.5107 1.0914 1.1771 0.3182  0.0638  -0.1359 459 ASP C OD2 
13471 N N   . SER C 460 ? 1.1665 0.7066 0.9400 0.2395  0.0136  -0.1326 460 SER C N   
13472 C CA  . SER C 460 ? 1.0997 0.6169 0.8923 0.2279  0.0016  -0.1364 460 SER C CA  
13473 C C   . SER C 460 ? 1.0929 0.6156 0.9119 0.2165  0.0120  -0.1178 460 SER C C   
13474 O O   . SER C 460 ? 1.1483 0.6542 0.9723 0.2195  0.0148  -0.1178 460 SER C O   
13475 C CB  . SER C 460 ? 1.1291 0.6428 0.9334 0.2131  -0.0190 -0.1433 460 SER C CB  
13476 O OG  . SER C 460 ? 1.5113 1.0036 1.3387 0.1997  -0.0297 -0.1437 460 SER C OG  
13477 N N   . ALA C 461 ? 1.0718 0.6181 0.9065 0.2049  0.0175  -0.1024 461 ALA C N   
13478 C CA  . ALA C 461 ? 1.0698 0.6235 0.9274 0.1948  0.0266  -0.0854 461 ALA C CA  
13479 C C   . ALA C 461 ? 1.0765 0.6343 0.9276 0.2065  0.0439  -0.0792 461 ALA C C   
13480 O O   . ALA C 461 ? 1.1862 0.7398 1.0521 0.2024  0.0482  -0.0707 461 ALA C O   
13481 C CB  . ALA C 461 ? 1.0787 0.6575 0.9509 0.1824  0.0287  -0.0722 461 ALA C CB  
13482 N N   . HIS C 462 ? 1.1357 0.7028 0.9661 0.2211  0.0536  -0.0826 462 HIS C N   
13483 C CA  . HIS C 462 ? 1.0281 0.6013 0.8549 0.2319  0.0702  -0.0762 462 HIS C CA  
13484 C C   . HIS C 462 ? 1.0854 0.6370 0.9094 0.2408  0.0694  -0.0835 462 HIS C C   
13485 O O   . HIS C 462 ? 0.9610 0.5136 0.7980 0.2403  0.0771  -0.0748 462 HIS C O   
13486 C CB  . HIS C 462 ? 1.1114 0.6976 0.9166 0.2463  0.0804  -0.0780 462 HIS C CB  
13487 C CG  . HIS C 462 ? 1.0397 0.6488 0.8490 0.2406  0.0869  -0.0671 462 HIS C CG  
13488 N ND1 . HIS C 462 ? 1.1573 0.7800 0.9849 0.2325  0.0963  -0.0529 462 HIS C ND1 
13489 C CD2 . HIS C 462 ? 0.9878 0.6072 0.7839 0.2436  0.0850  -0.0690 462 HIS C CD2 
13490 C CE1 . HIS C 462 ? 1.1109 0.7501 0.9366 0.2306  0.0999  -0.0471 462 HIS C CE1 
13491 N NE2 . HIS C 462 ? 1.0100 0.6483 0.8173 0.2372  0.0937  -0.0556 462 HIS C NE2 
13492 N N   . ILE C 463 ? 1.0860 0.6181 0.8929 0.2498  0.0594  -0.1002 463 ILE C N   
13493 C CA  . ILE C 463 ? 1.0992 0.6086 0.9011 0.2607  0.0580  -0.1091 463 ILE C CA  
13494 C C   . ILE C 463 ? 1.1803 0.6722 1.0052 0.2473  0.0486  -0.1054 463 ILE C C   
13495 O O   . ILE C 463 ? 1.2541 0.7399 1.0877 0.2512  0.0548  -0.1000 463 ILE C O   
13496 C CB  . ILE C 463 ? 0.9838 0.4762 0.7583 0.2753  0.0490  -0.1298 463 ILE C CB  
13497 C CG1 . ILE C 463 ? 1.1409 0.6524 0.8909 0.2912  0.0608  -0.1310 463 ILE C CG1 
13498 C CG2 . ILE C 463 ? 1.1345 0.6001 0.9041 0.2868  0.0460  -0.1407 463 ILE C CG2 
13499 C CD1 . ILE C 463 ? 1.0603 0.5894 0.8112 0.3017  0.0823  -0.1183 463 ILE C CD1 
13500 N N   . GLU C 464 ? 1.1453 0.6310 0.9815 0.2317  0.0341  -0.1068 464 GLU C N   
13501 C CA  . GLU C 464 ? 1.0610 0.5305 0.9212 0.2178  0.0252  -0.1010 464 GLU C CA  
13502 C C   . GLU C 464 ? 0.9925 0.4787 0.8713 0.2117  0.0377  -0.0810 464 GLU C C   
13503 O O   . GLU C 464 ? 1.0272 0.4992 0.9181 0.2107  0.0373  -0.0760 464 GLU C O   
13504 C CB  . GLU C 464 ? 1.1304 0.5981 1.0032 0.2004  0.0097  -0.1021 464 GLU C CB  
13505 C CG  . GLU C 464 ? 1.2612 0.7099 1.1181 0.2050  -0.0062 -0.1234 464 GLU C CG  
13506 C CD  . GLU C 464 ? 1.6059 1.0195 1.4560 0.2145  -0.0143 -0.1380 464 GLU C CD  
13507 O OE1 . GLU C 464 ? 1.6665 1.0646 1.5359 0.2078  -0.0157 -0.1303 464 GLU C OE1 
13508 O OE2 . GLU C 464 ? 1.7138 1.1155 1.5385 0.2296  -0.0192 -0.1570 464 GLU C OE2 
13509 N N   . THR C 465 ? 1.0713 0.5858 0.9515 0.2083  0.0479  -0.0704 465 THR C N   
13510 C CA  . THR C 465 ? 1.0591 0.5908 0.9556 0.2025  0.0583  -0.0531 465 THR C CA  
13511 C C   . THR C 465 ? 1.0600 0.5911 0.9521 0.2163  0.0698  -0.0518 465 THR C C   
13512 O O   . THR C 465 ? 1.0159 0.5430 0.9215 0.2144  0.0714  -0.0434 465 THR C O   
13513 C CB  . THR C 465 ? 0.9882 0.5479 0.8856 0.1968  0.0653  -0.0447 465 THR C CB  
13514 O OG1 . THR C 465 ? 1.0656 0.6281 0.9712 0.1834  0.0548  -0.0438 465 THR C OG1 
13515 C CG2 . THR C 465 ? 0.9739 0.5515 0.8842 0.1932  0.0762  -0.0297 465 THR C CG2 
13516 N N   . ILE C 466 ? 1.1119 0.6485 0.9858 0.2309  0.0779  -0.0592 466 ILE C N   
13517 C CA  . ILE C 466 ? 1.0925 0.6322 0.9642 0.2446  0.0896  -0.0573 466 ILE C CA  
13518 C C   . ILE C 466 ? 1.0413 0.5554 0.9148 0.2512  0.0838  -0.0633 466 ILE C C   
13519 O O   . ILE C 466 ? 1.2360 0.7516 1.1222 0.2528  0.0886  -0.0547 466 ILE C O   
13520 C CB  . ILE C 466 ? 1.0201 0.5699 0.8718 0.2596  0.0995  -0.0636 466 ILE C CB  
13521 C CG1 . ILE C 466 ? 0.9223 0.4973 0.7751 0.2533  0.1070  -0.0549 466 ILE C CG1 
13522 C CG2 . ILE C 466 ? 0.9726 0.5254 0.8241 0.2744  0.1112  -0.0619 466 ILE C CG2 
13523 C CD1 . ILE C 466 ? 1.0371 0.6209 0.8693 0.2660  0.1146  -0.0601 466 ILE C CD1 
13524 N N   . LYS C 467 ? 1.0739 0.5640 0.9353 0.2551  0.0723  -0.0782 467 LYS C N   
13525 C CA  . LYS C 467 ? 1.0417 0.5029 0.9036 0.2621  0.0651  -0.0860 467 LYS C CA  
13526 C C   . LYS C 467 ? 1.1133 0.5670 0.9994 0.2499  0.0609  -0.0732 467 LYS C C   
13527 O O   . LYS C 467 ? 1.3123 0.7580 1.2042 0.2582  0.0647  -0.0697 467 LYS C O   
13528 C CB  . LYS C 467 ? 1.0724 0.5079 0.9206 0.2632  0.0497  -0.1044 467 LYS C CB  
13529 C CG  . LYS C 467 ? 0.9970 0.4296 0.8163 0.2829  0.0526  -0.1211 467 LYS C CG  
13530 C CD  . LYS C 467 ? 1.1915 0.5931 1.0014 0.2879  0.0372  -0.1403 467 LYS C CD  
13531 C CE  . LYS C 467 ? 1.2244 0.6286 1.0068 0.2999  0.0344  -0.1576 467 LYS C CE  
13532 N NZ  . LYS C 467 ? 1.5940 0.9670 1.3690 0.2965  0.0134  -0.1763 467 LYS C NZ  
13533 N N   . GLY C 468 ? 1.0835 0.5411 0.9834 0.2314  0.0535  -0.0654 468 GLY C N   
13534 C CA  . GLY C 468 ? 1.0286 0.4810 0.9509 0.2193  0.0498  -0.0513 468 GLY C CA  
13535 C C   . GLY C 468 ? 0.9632 0.4367 0.8956 0.2208  0.0619  -0.0355 468 GLY C C   
13536 O O   . GLY C 468 ? 1.0523 0.5170 0.9978 0.2198  0.0608  -0.0262 468 GLY C O   
13537 N N   . LEU C 469 ? 1.0588 0.5598 0.9860 0.2233  0.0728  -0.0321 469 LEU C N   
13538 C CA  . LEU C 469 ? 1.0091 0.5317 0.9463 0.2243  0.0831  -0.0187 469 LEU C CA  
13539 C C   . LEU C 469 ? 1.0408 0.5582 0.9755 0.2408  0.0893  -0.0214 469 LEU C C   
13540 O O   . LEU C 469 ? 1.0838 0.6024 1.0308 0.2418  0.0906  -0.0116 469 LEU C O   
13541 C CB  . LEU C 469 ? 0.9973 0.5485 0.9309 0.2214  0.0919  -0.0154 469 LEU C CB  
13542 C CG  . LEU C 469 ? 0.9441 0.5062 0.8822 0.2060  0.0876  -0.0103 469 LEU C CG  
13543 C CD1 . LEU C 469 ? 0.9917 0.5744 0.9210 0.2071  0.0952  -0.0121 469 LEU C CD1 
13544 C CD2 . LEU C 469 ? 0.8537 0.4265 0.8082 0.1957  0.0875  0.0049  469 LEU C CD2 
13545 N N   . ILE C 470 ? 1.0396 0.5526 0.9582 0.2549  0.0934  -0.0340 470 ILE C N   
13546 C CA  . ILE C 470 ? 1.0949 0.6112 1.0138 0.2690  0.0988  -0.0365 470 ILE C CA  
13547 C C   . ILE C 470 ? 1.1165 0.6079 1.0420 0.2714  0.0894  -0.0387 470 ILE C C   
13548 O O   . ILE C 470 ? 1.1524 0.6512 1.0881 0.2775  0.0924  -0.0334 470 ILE C O   
13549 C CB  . ILE C 470 ? 1.0052 0.5329 0.9083 0.2802  0.1046  -0.0479 470 ILE C CB  
13550 C CG1 . ILE C 470 ? 1.0605 0.5653 0.9453 0.2830  0.0953  -0.0640 470 ILE C CG1 
13551 C CG2 . ILE C 470 ? 1.0569 0.6126 0.9586 0.2782  0.1158  -0.0415 470 ILE C CG2 
13552 C CD1 . ILE C 470 ? 1.0491 0.5622 0.9171 0.2970  0.1002  -0.0754 470 ILE C CD1 
13553 N N   . LYS C 471 ? 1.1234 0.5851 1.0450 0.2664  0.0778  -0.0459 471 LYS C N   
13554 C CA  . LYS C 471 ? 1.0392 0.4740 0.9692 0.2672  0.0680  -0.0475 471 LYS C CA  
13555 C C   . LYS C 471 ? 1.0582 0.4948 1.0073 0.2604  0.0689  -0.0286 471 LYS C C   
13556 O O   . LYS C 471 ? 1.1178 0.5443 1.0764 0.2650  0.0656  -0.0256 471 LYS C O   
13557 C CB  . LYS C 471 ? 0.9940 0.3959 0.9180 0.2606  0.0543  -0.0585 471 LYS C CB  
13558 C CG  . LYS C 471 ? 1.1468 0.5176 1.0825 0.2594  0.0432  -0.0599 471 LYS C CG  
13559 C CD  . LYS C 471 ? 1.4850 0.8316 1.4094 0.2652  0.0330  -0.0814 471 LYS C CD  
13560 C CE  . LYS C 471 ? 1.4575 0.7802 1.3936 0.2693  0.0266  -0.0840 471 LYS C CE  
13561 N NZ  . LYS C 471 ? 1.3976 0.7235 1.3212 0.2861  0.0302  -0.0997 471 LYS C NZ  
13562 N N   . ASN C 472 ? 1.0618 0.5161 1.0176 0.2484  0.0725  -0.0157 472 ASN C N   
13563 C CA  . ASN C 472 ? 1.1053 0.5692 1.0784 0.2406  0.0730  0.0028  472 ASN C CA  
13564 C C   . ASN C 472 ? 1.1002 0.5926 1.0770 0.2485  0.0841  0.0111  472 ASN C C   
13565 O O   . ASN C 472 ? 1.1692 0.6802 1.1566 0.2406  0.0857  0.0252  472 ASN C O   
13566 C CB  . ASN C 472 ? 0.8740 0.3489 0.8549 0.2214  0.0690  0.0121  472 ASN C CB  
13567 C CG  . ASN C 472 ? 0.9482 0.3960 0.9353 0.2108  0.0568  0.0106  472 ASN C CG  
13568 O OD1 . ASN C 472 ? 1.2239 0.6662 1.2261 0.2018  0.0529  0.0249  472 ASN C OD1 
13569 N ND2 . ASN C 472 ? 1.0181 0.4489 0.9945 0.2117  0.0503  -0.0060 472 ASN C ND2 
13570 N N   . ASP C 473 ? 0.9930 0.4935 0.9629 0.2622  0.0901  0.0021  473 ASP C N   
13571 C CA  . ASP C 473 ? 0.9674 0.4974 0.9442 0.2685  0.0992  0.0087  473 ASP C CA  
13572 C C   . ASP C 473 ? 1.0842 0.6391 1.0623 0.2614  0.1065  0.0153  473 ASP C C   
13573 O O   . ASP C 473 ? 1.0462 0.6223 1.0353 0.2600  0.1097  0.0256  473 ASP C O   
13574 C CB  . ASP C 473 ? 1.0454 0.5746 1.0360 0.2720  0.0969  0.0205  473 ASP C CB  
13575 C CG  . ASP C 473 ? 1.2505 0.7644 1.2419 0.2827  0.0923  0.0136  473 ASP C CG  
13576 O OD1 . ASP C 473 ? 1.1785 0.6934 1.1609 0.2908  0.0944  0.0001  473 ASP C OD1 
13577 O OD2 . ASP C 473 ? 1.3528 0.8546 1.3538 0.2839  0.0870  0.0222  473 ASP C OD2 
13578 N N   . VAL C 474 ? 1.0601 0.6176 1.0282 0.2547  0.1069  0.0082  474 VAL C N   
13579 C CA  . VAL C 474 ? 1.0137 0.5977 0.9835 0.2457  0.1119  0.0127  474 VAL C CA  
13580 C C   . VAL C 474 ? 0.9820 0.5753 0.9419 0.2544  0.1207  0.0039  474 VAL C C   
13581 O O   . VAL C 474 ? 1.0335 0.6141 0.9793 0.2566  0.1190  -0.0063 474 VAL C O   
13582 C CB  . VAL C 474 ? 0.9760 0.5575 0.9442 0.2302  0.1055  0.0146  474 VAL C CB  
13583 C CG1 . VAL C 474 ? 0.9582 0.5653 0.9267 0.2229  0.1110  0.0179  474 VAL C CG1 
13584 C CG2 . VAL C 474 ? 0.9275 0.5009 0.9066 0.2221  0.0981  0.0256  474 VAL C CG2 
13585 N N   . ILE C 475 ? 0.9551 0.5707 0.9226 0.2597  0.1297  0.0081  475 ILE C N   
13586 C CA  . ILE C 475 ? 0.9463 0.5753 0.9073 0.2661  0.1385  0.0025  475 ILE C CA  
13587 C C   . ILE C 475 ? 0.9803 0.6129 0.9326 0.2577  0.1399  0.0008  475 ILE C C   
13588 O O   . ILE C 475 ? 0.9938 0.6367 0.9532 0.2454  0.1373  0.0072  475 ILE C O   
13589 C CB  . ILE C 475 ? 0.9039 0.5584 0.8798 0.2709  0.1471  0.0089  475 ILE C CB  
13590 C CG1 . ILE C 475 ? 0.8477 0.5156 0.8179 0.2780  0.1563  0.0044  475 ILE C CG1 
13591 C CG2 . ILE C 475 ? 0.8805 0.5522 0.8690 0.2609  0.1483  0.0177  475 ILE C CG2 
13592 C CD1 . ILE C 475 ? 0.7413 0.4310 0.7272 0.2855  0.1644  0.0098  475 ILE C CD1 
13593 N N   . VAL C 476 ? 0.9126 0.5396 0.8490 0.2628  0.1418  -0.0081 476 VAL C N   
13594 C CA  . VAL C 476 ? 0.8515 0.4818 0.7786 0.2561  0.1423  -0.0098 476 VAL C CA  
13595 C C   . VAL C 476 ? 0.9413 0.5901 0.8655 0.2614  0.1540  -0.0085 476 VAL C C   
13596 O O   . VAL C 476 ? 1.1496 0.8035 1.0683 0.2710  0.1587  -0.0121 476 VAL C O   
13597 C CB  . VAL C 476 ? 0.9656 0.5740 0.8760 0.2568  0.1334  -0.0205 476 VAL C CB  
13598 C CG1 . VAL C 476 ? 0.8706 0.4859 0.7710 0.2509  0.1333  -0.0224 476 VAL C CG1 
13599 C CG2 . VAL C 476 ? 0.9844 0.5758 0.9018 0.2480  0.1212  -0.0195 476 VAL C CG2 
13600 N N   . VAL C 477 ? 0.8959 0.5586 0.8252 0.2523  0.1571  -0.0028 477 VAL C N   
13601 C CA  . VAL C 477 ? 0.8502 0.5284 0.7787 0.2558  0.1683  0.0003  477 VAL C CA  
13602 C C   . VAL C 477 ? 0.8930 0.5668 0.8057 0.2522  0.1656  -0.0035 477 VAL C C   
13603 O O   . VAL C 477 ? 1.0204 0.6888 0.9327 0.2419  0.1564  -0.0042 477 VAL C O   
13604 C CB  . VAL C 477 ? 0.8192 0.5170 0.7681 0.2483  0.1734  0.0096  477 VAL C CB  
13605 C CG1 . VAL C 477 ? 0.6913 0.3961 0.6561 0.2534  0.1758  0.0132  477 VAL C CG1 
13606 C CG2 . VAL C 477 ? 0.8500 0.5495 0.8043 0.2342  0.1654  0.0123  477 VAL C CG2 
13607 N N   . VAL C 478 ? 0.9631 0.6401 0.8628 0.2616  0.1736  -0.0053 478 VAL C N   
13608 C CA  . VAL C 478 ? 0.8666 0.5403 0.7496 0.2605  0.1706  -0.0090 478 VAL C CA  
13609 C C   . VAL C 478 ? 0.9747 0.6631 0.8567 0.2630  0.1821  -0.0020 478 VAL C C   
13610 O O   . VAL C 478 ? 1.0582 0.7590 0.9485 0.2677  0.1925  0.0041  478 VAL C O   
13611 C CB  . VAL C 478 ? 0.8088 0.4665 0.6695 0.2716  0.1654  -0.0208 478 VAL C CB  
13612 C CG1 . VAL C 478 ? 0.8558 0.4952 0.7180 0.2663  0.1515  -0.0279 478 VAL C CG1 
13613 C CG2 . VAL C 478 ? 0.9427 0.6084 0.7980 0.2838  0.1732  -0.0218 478 VAL C CG2 
13614 N N   . THR C 479 ? 0.8656 0.5546 0.7392 0.2578  0.1788  -0.0020 479 THR C N   
13615 C CA  . THR C 479 ? 0.8932 0.5938 0.7643 0.2604  0.1890  0.0054  479 THR C CA  
13616 C C   . THR C 479 ? 0.9954 0.6919 0.8465 0.2623  0.1834  0.0008  479 THR C C   
13617 O O   . THR C 479 ? 1.1653 0.8520 1.0108 0.2574  0.1706  -0.0070 479 THR C O   
13618 C CB  . THR C 479 ? 0.8790 0.5901 0.7712 0.2490  0.1923  0.0143  479 THR C CB  
13619 O OG1 . THR C 479 ? 0.9227 0.6311 0.8147 0.2386  0.1826  0.0125  479 THR C OG1 
13620 C CG2 . THR C 479 ? 0.9194 0.6350 0.8323 0.2449  0.1936  0.0172  479 THR C CG2 
13621 N N   . GLY C 480 ? 0.9580 0.6621 0.7998 0.2692  0.1924  0.0064  480 GLY C N   
13622 C CA  . GLY C 480 ? 1.1244 0.8275 0.9469 0.2727  0.1879  0.0035  480 GLY C CA  
13623 C C   . GLY C 480 ? 0.9259 0.6184 0.7256 0.2816  0.1786  -0.0092 480 GLY C C   
13624 O O   . GLY C 480 ? 1.2292 0.9168 1.0205 0.2923  0.1816  -0.0143 480 GLY C O   
13625 N N   . CYS C 481 ? 0.8900 0.5795 0.6800 0.2778  0.1668  -0.0150 481 CYS C N   
13626 C CA  . CYS C 481 ? 1.0459 0.7248 0.8149 0.2849  0.1552  -0.0288 481 CYS C CA  
13627 C C   . CYS C 481 ? 1.1090 0.7726 0.8836 0.2812  0.1456  -0.0387 481 CYS C C   
13628 O O   . CYS C 481 ? 1.1929 0.8450 0.9499 0.2910  0.1394  -0.0508 481 CYS C O   
13629 C CB  . CYS C 481 ? 1.1719 0.8535 0.9346 0.2795  0.1437  -0.0316 481 CYS C CB  
13630 S SG  . CYS C 481 ? 1.1029 0.7999 0.8519 0.2887  0.1536  -0.0215 481 CYS C SG  
13631 N N   . ALA C 482 ? 0.9963 0.6589 0.7943 0.2680  0.1439  -0.0340 482 ALA C N   
13632 C CA  . ALA C 482 ? 1.0159 0.6636 0.8210 0.2645  0.1356  -0.0410 482 ALA C CA  
13633 C C   . ALA C 482 ? 1.1160 0.7595 0.9151 0.2786  0.1449  -0.0433 482 ALA C C   
13634 O O   . ALA C 482 ? 1.0474 0.6753 0.8364 0.2857  0.1381  -0.0545 482 ALA C O   
13635 C CB  . ALA C 482 ? 0.9887 0.6398 0.8188 0.2493  0.1341  -0.0329 482 ALA C CB  
13636 N N   . ALA C 483 ? 1.0689 0.7266 0.8750 0.2832  0.1604  -0.0325 483 ALA C N   
13637 C CA  . ALA C 483 ? 0.9833 0.6432 0.7872 0.2961  0.1707  -0.0320 483 ALA C CA  
13638 C C   . ALA C 483 ? 1.0298 0.6875 0.8067 0.3110  0.1704  -0.0409 483 ALA C C   
13639 O O   . ALA C 483 ? 1.2207 0.8737 0.9916 0.3188  0.1687  -0.0479 483 ALA C O   
13640 C CB  . ALA C 483 ? 0.9407 0.6216 0.7607 0.2937  0.1853  -0.0172 483 ALA C CB  
13641 N N   . GLN C 484 ? 1.0988 0.7604 0.8585 0.3161  0.1716  -0.0407 484 GLN C N   
13642 C CA  . GLN C 484 ? 1.1593 0.8204 0.8902 0.3315  0.1709  -0.0490 484 GLN C CA  
13643 C C   . GLN C 484 ? 1.0784 0.7165 0.7951 0.3345  0.1538  -0.0681 484 GLN C C   
13644 O O   . GLN C 484 ? 1.0620 0.6959 0.7632 0.3456  0.1517  -0.0775 484 GLN C O   
13645 C CB  . GLN C 484 ? 0.9462 0.6182 0.6635 0.3363  0.1765  -0.0424 484 GLN C CB  
13646 C CG  . GLN C 484 ? 1.0408 0.7331 0.7731 0.3345  0.1940  -0.0234 484 GLN C CG  
13647 C CD  . GLN C 484 ? 1.1920 0.8949 0.9122 0.3400  0.2011  -0.0144 484 GLN C CD  
13648 O OE1 . GLN C 484 ? 1.2810 0.9976 1.0139 0.3383  0.2149  0.0014  484 GLN C OE1 
13649 N NE2 . GLN C 484 ? 1.2553 0.9524 0.9519 0.3466  0.1916  -0.0236 484 GLN C NE2 
13650 N N   . ALA C 485 ? 1.0707 0.6982 0.7972 0.3199  0.1394  -0.0725 485 ALA C N   
13651 C CA  . ALA C 485 ? 1.1859 0.7919 0.9052 0.3180  0.1211  -0.0892 485 ALA C CA  
13652 C C   . ALA C 485 ? 1.1845 0.7741 0.9051 0.3259  0.1216  -0.0965 485 ALA C C   
13653 O O   . ALA C 485 ? 1.0814 0.6548 0.7837 0.3359  0.1124  -0.1123 485 ALA C O   
13654 C CB  . ALA C 485 ? 1.2170 0.8198 0.9573 0.2966  0.1080  -0.0871 485 ALA C CB  
13655 N N   . ALA C 486 ? 1.1986 0.7955 0.9426 0.3199  0.1312  -0.0845 486 ALA C N   
13656 C CA  . ALA C 486 ? 1.0897 0.6815 0.8430 0.3222  0.1312  -0.0869 486 ALA C CA  
13657 C C   . ALA C 486 ? 0.9984 0.6028 0.7360 0.3379  0.1403  -0.0889 486 ALA C C   
13658 O O   . ALA C 486 ? 1.1680 0.7606 0.8969 0.3461  0.1347  -0.1002 486 ALA C O   
13659 C CB  . ALA C 486 ? 1.0429 0.6456 0.8251 0.3116  0.1390  -0.0722 486 ALA C CB  
13660 N N   . ALA C 487 ? 1.0771 0.7045 0.8111 0.3424  0.1544  -0.0773 487 ALA C N   
13661 C CA  . ALA C 487 ? 1.2330 0.8747 0.9520 0.3579  0.1650  -0.0760 487 ALA C CA  
13662 C C   . ALA C 487 ? 1.1249 0.7540 0.8117 0.3714  0.1552  -0.0934 487 ALA C C   
13663 O O   . ALA C 487 ? 1.2537 0.8840 0.9285 0.3843  0.1578  -0.0990 487 ALA C O   
13664 C CB  . ALA C 487 ? 0.9240 0.5894 0.6442 0.3590  0.1804  -0.0597 487 ALA C CB  
13665 N N   . LYS C 488 ? 1.1425 0.7601 0.8153 0.3690  0.1437  -0.1021 488 LYS C N   
13666 C CA  . LYS C 488 ? 1.2090 0.8140 0.8506 0.3811  0.1316  -0.1203 488 LYS C CA  
13667 C C   . LYS C 488 ? 1.0504 0.6295 0.6915 0.3811  0.1165  -0.1380 488 LYS C C   
13668 O O   . LYS C 488 ? 1.2037 0.7755 0.8219 0.3943  0.1105  -0.1522 488 LYS C O   
13669 C CB  . LYS C 488 ? 1.3533 0.9526 0.9839 0.3771  0.1215  -0.1250 488 LYS C CB  
13670 C CG  . LYS C 488 ? 1.1129 0.7355 0.7398 0.3791  0.1349  -0.1091 488 LYS C CG  
13671 C CD  . LYS C 488 ? 1.1834 0.8012 0.7913 0.3812  0.1237  -0.1172 488 LYS C CD  
13672 C CE  . LYS C 488 ? 1.1279 0.7356 0.7579 0.3602  0.1091  -0.1190 488 LYS C CE  
13673 N NZ  . LYS C 488 ? 1.1811 0.7931 0.7996 0.3564  0.0950  -0.1248 488 LYS C NZ  
13674 N N   . TYR C 489 ? 1.1061 0.6707 0.7723 0.3666  0.1099  -0.1369 489 TYR C N   
13675 C CA  . TYR C 489 ? 1.2262 0.7641 0.8966 0.3645  0.0956  -0.1514 489 TYR C CA  
13676 C C   . TYR C 489 ? 1.1215 0.6638 0.7977 0.3729  0.1040  -0.1498 489 TYR C C   
13677 O O   . TYR C 489 ? 1.3402 0.8643 1.0066 0.3801  0.0946  -0.1649 489 TYR C O   
13678 C CB  . TYR C 489 ? 1.2439 0.7665 0.9401 0.3465  0.0875  -0.1471 489 TYR C CB  
13679 C CG  . TYR C 489 ? 1.1012 0.5920 0.8015 0.3426  0.0701  -0.1619 489 TYR C CG  
13680 C CD1 . TYR C 489 ? 1.2154 0.6837 0.9014 0.3416  0.0511  -0.1795 489 TYR C CD1 
13681 C CD2 . TYR C 489 ? 1.1617 0.6448 0.8817 0.3396  0.0716  -0.1582 489 TYR C CD2 
13682 C CE1 . TYR C 489 ? 1.2976 0.7352 0.9904 0.3362  0.0342  -0.1926 489 TYR C CE1 
13683 C CE2 . TYR C 489 ? 1.4044 0.8571 1.1301 0.3356  0.0560  -0.1703 489 TYR C CE2 
13684 C CZ  . TYR C 489 ? 1.4050 0.8342 1.1178 0.3332  0.0373  -0.1874 489 TYR C CZ  
13685 O OH  . TYR C 489 ? 1.5244 0.9223 1.2456 0.3276  0.0213  -0.1989 489 TYR C OH  
13686 N N   . GLY C 490 ? 1.1390 0.7046 0.8319 0.3717  0.1208  -0.1320 490 GLY C N   
13687 C CA  . GLY C 490 ? 1.1136 0.6873 0.8142 0.3800  0.1301  -0.1283 490 GLY C CA  
13688 C C   . GLY C 490 ? 1.1796 0.7527 0.9118 0.3688  0.1321  -0.1182 490 GLY C C   
13689 O O   . GLY C 490 ? 1.3691 0.9418 1.1090 0.3751  0.1349  -0.1188 490 GLY C O   
13690 N N   . LEU C 491 ? 1.0051 0.5790 0.7551 0.3533  0.1306  -0.1087 491 LEU C N   
13691 C CA  . LEU C 491 ? 1.0596 0.6342 0.8381 0.3430  0.1319  -0.0983 491 LEU C CA  
13692 C C   . LEU C 491 ? 1.1609 0.7649 0.9542 0.3445  0.1487  -0.0821 491 LEU C C   
13693 O O   . LEU C 491 ? 1.3086 0.9166 1.1230 0.3410  0.1509  -0.0748 491 LEU C O   
13694 C CB  . LEU C 491 ? 1.0385 0.6027 0.8295 0.3265  0.1239  -0.0941 491 LEU C CB  
13695 C CG  . LEU C 491 ? 1.1354 0.6712 0.9147 0.3227  0.1070  -0.1083 491 LEU C CG  
13696 C CD1 . LEU C 491 ? 1.2518 0.7834 1.0428 0.3077  0.1027  -0.1007 491 LEU C CD1 
13697 C CD2 . LEU C 491 ? 1.0857 0.5959 0.8692 0.3242  0.0956  -0.1186 491 LEU C CD2 
13698 N N   . LEU C 492 ? 1.2105 0.8348 0.9938 0.3498  0.1601  -0.0758 492 LEU C N   
13699 C CA  . LEU C 492 ? 1.1807 0.8319 0.9795 0.3507  0.1760  -0.0601 492 LEU C CA  
13700 C C   . LEU C 492 ? 1.1557 0.8168 0.9487 0.3666  0.1844  -0.0611 492 LEU C C   
13701 O O   . LEU C 492 ? 1.1717 0.8524 0.9582 0.3750  0.1973  -0.0536 492 LEU C O   
13702 C CB  . LEU C 492 ? 1.0901 0.7571 0.8839 0.3479  0.1848  -0.0505 492 LEU C CB  
13703 C CG  . LEU C 492 ? 1.1022 0.7678 0.9111 0.3314  0.1814  -0.0438 492 LEU C CG  
13704 C CD1 . LEU C 492 ? 0.8853 0.5561 0.6804 0.3307  0.1844  -0.0410 492 LEU C CD1 
13705 C CD2 . LEU C 492 ? 1.2358 0.9176 1.0733 0.3234  0.1897  -0.0298 492 LEU C CD2 
13706 N N   . GLN C 493 ? 1.1045 0.7515 0.9007 0.3710  0.1772  -0.0697 493 GLN C N   
13707 C CA  . GLN C 493 ? 1.2357 0.8897 1.0275 0.3866  0.1839  -0.0721 493 GLN C CA  
13708 C C   . GLN C 493 ? 1.2371 0.8890 1.0528 0.3843  0.1820  -0.0688 493 GLN C C   
13709 O O   . GLN C 493 ? 1.2273 0.8625 1.0546 0.3732  0.1710  -0.0708 493 GLN C O   
13710 C CB  . GLN C 493 ? 1.1509 0.7848 0.9147 0.3987  0.1748  -0.0905 493 GLN C CB  
13711 C CG  . GLN C 493 ? 1.1641 0.8038 0.9003 0.4062  0.1780  -0.0937 493 GLN C CG  
13712 C CD  . GLN C 493 ? 1.2923 0.9093 1.0004 0.4164  0.1656  -0.1141 493 GLN C CD  
13713 O OE1 . GLN C 493 ? 1.3769 0.9695 1.0875 0.4150  0.1528  -0.1266 493 GLN C OE1 
13714 N NE2 . GLN C 493 ? 1.3037 0.9276 0.9845 0.4271  0.1687  -0.1176 493 GLN C NE2 
13715 N N   . LYS C 494 ? 1.1551 0.8241 0.9779 0.3957  0.1926  -0.0634 494 LYS C N   
13716 C CA  . LYS C 494 ? 0.9605 0.6301 0.8061 0.3956  0.1915  -0.0596 494 LYS C CA  
13717 C C   . LYS C 494 ? 1.0071 0.6460 0.8455 0.3986  0.1769  -0.0747 494 LYS C C   
13718 O O   . LYS C 494 ? 1.2078 0.8363 1.0640 0.3916  0.1695  -0.0727 494 LYS C O   
13719 C CB  . LYS C 494 ? 0.9668 0.6614 0.8203 0.4092  0.2060  -0.0515 494 LYS C CB  
13720 C CG  . LYS C 494 ? 1.0348 0.7593 0.8916 0.4106  0.2224  -0.0374 494 LYS C CG  
13721 C CD  . LYS C 494 ? 1.1193 0.8597 1.0036 0.3958  0.2266  -0.0225 494 LYS C CD  
13722 C CE  . LYS C 494 ? 1.1212 0.8828 1.0334 0.3988  0.2345  -0.0115 494 LYS C CE  
13723 N NZ  . LYS C 494 ? 1.1038 0.8924 1.0184 0.4107  0.2515  -0.0018 494 LYS C NZ  
13724 N N   . GLU C 495 ? 1.1488 0.7728 0.9613 0.4092  0.1726  -0.0894 495 GLU C N   
13725 C CA  . GLU C 495 ? 1.2440 0.8366 1.0486 0.4128  0.1585  -0.1055 495 GLU C CA  
13726 C C   . GLU C 495 ? 1.1783 0.7446 0.9851 0.3972  0.1431  -0.1112 495 GLU C C   
13727 O O   . GLU C 495 ? 1.3654 0.9040 1.1719 0.3973  0.1309  -0.1221 495 GLU C O   
13728 C CB  . GLU C 495 ? 1.1472 0.7322 0.9224 0.4298  0.1584  -0.1205 495 GLU C CB  
13729 C CG  . GLU C 495 ? 1.3180 0.9150 1.0697 0.4330  0.1637  -0.1213 495 GLU C CG  
13730 C CD  . GLU C 495 ? 1.4654 1.0950 1.2144 0.4449  0.1823  -0.1092 495 GLU C CD  
13731 O OE1 . GLU C 495 ? 1.4929 1.1251 1.2266 0.4625  0.1871  -0.1154 495 GLU C OE1 
13732 O OE2 . GLU C 495 ? 1.5389 1.1910 1.3016 0.4367  0.1922  -0.0931 495 GLU C OE2 
13733 N N   . ALA C 496 ? 1.1787 0.7528 0.9890 0.3839  0.1436  -0.1034 496 ALA C N   
13734 C CA  . ALA C 496 ? 1.2151 0.7665 1.0288 0.3692  0.1299  -0.1070 496 ALA C CA  
13735 C C   . ALA C 496 ? 1.2059 0.7498 1.0456 0.3593  0.1252  -0.0983 496 ALA C C   
13736 O O   . ALA C 496 ? 1.2946 0.8156 1.1389 0.3487  0.1131  -0.1013 496 ALA C O   
13737 C CB  . ALA C 496 ? 1.1056 0.6690 0.9149 0.3595  0.1329  -0.1006 496 ALA C CB  
13738 N N   . ALA C 497 ? 1.2438 0.8072 1.1008 0.3631  0.1344  -0.0869 497 ALA C N   
13739 C CA  . ALA C 497 ? 1.1516 0.7105 1.0317 0.3559  0.1303  -0.0777 497 ALA C CA  
13740 C C   . ALA C 497 ? 1.1336 0.6625 1.0143 0.3603  0.1188  -0.0876 497 ALA C C   
13741 O O   . ALA C 497 ? 1.2563 0.7648 1.1464 0.3497  0.1084  -0.0858 497 ALA C O   
13742 C CB  . ALA C 497 ? 1.0354 0.6232 0.9322 0.3611  0.1424  -0.0647 497 ALA C CB  
13743 N N   . GLU C 498 ? 1.1010 0.6261 0.9720 0.3758  0.1209  -0.0976 498 GLU C N   
13744 C CA  . GLU C 498 ? 1.2675 0.7623 1.1395 0.3805  0.1102  -0.1078 498 GLU C CA  
13745 C C   . GLU C 498 ? 1.2769 0.7407 1.1366 0.3727  0.0965  -0.1209 498 GLU C C   
13746 O O   . GLU C 498 ? 1.3285 0.7645 1.1980 0.3664  0.0850  -0.1234 498 GLU C O   
13747 C CB  . GLU C 498 ? 1.3221 0.8196 1.1830 0.4001  0.1159  -0.1172 498 GLU C CB  
13748 C CG  . GLU C 498 ? 1.5871 1.1000 1.4658 0.4092  0.1234  -0.1073 498 GLU C CG  
13749 C CD  . GLU C 498 ? 1.9399 1.4481 1.8083 0.4287  0.1266  -0.1181 498 GLU C CD  
13750 O OE1 . GLU C 498 ? 1.7887 1.2949 1.6333 0.4375  0.1286  -0.1304 498 GLU C OE1 
13751 O OE2 . GLU C 498 ? 2.1150 1.6219 1.9983 0.4360  0.1272  -0.1140 498 GLU C OE2 
13752 N N   . LYS C 499 ? 1.2684 0.7369 1.1075 0.3731  0.0974  -0.1287 499 LYS C N   
13753 C CA  . LYS C 499 ? 1.1967 0.6382 1.0221 0.3668  0.0841  -0.1425 499 LYS C CA  
13754 C C   . LYS C 499 ? 1.2812 0.7108 1.1202 0.3477  0.0753  -0.1350 499 LYS C C   
13755 O O   . LYS C 499 ? 1.3473 0.7463 1.1868 0.3409  0.0614  -0.1439 499 LYS C O   
13756 C CB  . LYS C 499 ? 1.2433 0.6973 1.0416 0.3739  0.0881  -0.1513 499 LYS C CB  
13757 C CG  . LYS C 499 ? 1.4422 0.9019 1.2213 0.3937  0.0943  -0.1617 499 LYS C CG  
13758 C CD  . LYS C 499 ? 1.4159 0.8894 1.1672 0.4010  0.0985  -0.1680 499 LYS C CD  
13759 C CE  . LYS C 499 ? 2.0755 1.5554 1.8050 0.4218  0.1049  -0.1776 499 LYS C CE  
13760 N NZ  . LYS C 499 ? 1.9846 1.4792 1.6864 0.4293  0.1093  -0.1815 499 LYS C NZ  
13761 N N   . TYR C 500 ? 1.1745 0.6272 1.0243 0.3390  0.0830  -0.1190 500 TYR C N   
13762 C CA  . TYR C 500 ? 1.2729 0.7162 1.1333 0.3219  0.0760  -0.1111 500 TYR C CA  
13763 C C   . TYR C 500 ? 1.1552 0.6100 1.0389 0.3133  0.0803  -0.0920 500 TYR C C   
13764 O O   . TYR C 500 ? 1.3188 0.7582 1.2131 0.3007  0.0725  -0.0856 500 TYR C O   
13765 C CB  . TYR C 500 ? 1.1076 0.5641 0.9538 0.3175  0.0787  -0.1120 500 TYR C CB  
13766 C CG  . TYR C 500 ? 1.1180 0.5665 0.9383 0.3264  0.0743  -0.1300 500 TYR C CG  
13767 C CD1 . TYR C 500 ? 1.1599 0.5785 0.9722 0.3217  0.0583  -0.1440 500 TYR C CD1 
13768 C CD2 . TYR C 500 ? 1.0414 0.5130 0.8451 0.3393  0.0857  -0.1322 500 TYR C CD2 
13769 C CE1 . TYR C 500 ? 1.2138 0.6258 1.0005 0.3304  0.0528  -0.1614 500 TYR C CE1 
13770 C CE2 . TYR C 500 ? 1.2896 0.7553 1.0670 0.3487  0.0816  -0.1479 500 TYR C CE2 
13771 C CZ  . TYR C 500 ? 1.3358 0.7719 1.1038 0.3446  0.0647  -0.1632 500 TYR C CZ  
13772 O OH  . TYR C 500 ? 1.3642 0.7950 1.1047 0.3545  0.0591  -0.1799 500 TYR C OH  
13773 N N   . ALA C 501 ? 1.1312 0.6131 1.0225 0.3198  0.0923  -0.0823 501 ALA C N   
13774 C CA  . ALA C 501 ? 1.1969 0.6917 1.1084 0.3126  0.0959  -0.0649 501 ALA C CA  
13775 C C   . ALA C 501 ? 1.1499 0.6242 1.0765 0.3112  0.0876  -0.0604 501 ALA C C   
13776 O O   . ALA C 501 ? 1.0951 0.5514 1.0198 0.3198  0.0826  -0.0698 501 ALA C O   
13777 C CB  . ALA C 501 ? 1.1252 0.6532 1.0419 0.3203  0.1095  -0.0570 501 ALA C CB  
13778 N N   . GLY C 502 ? 1.1039 0.5815 1.0448 0.3010  0.0868  -0.0453 502 GLY C N   
13779 C CA  . GLY C 502 ? 1.0964 0.5571 1.0523 0.2990  0.0799  -0.0369 502 GLY C CA  
13780 C C   . GLY C 502 ? 1.1304 0.6048 1.0956 0.3111  0.0851  -0.0321 502 GLY C C   
13781 O O   . GLY C 502 ? 1.2923 0.7880 1.2528 0.3212  0.0940  -0.0363 502 GLY C O   
13782 N N   . PRO C 503 ? 1.0504 0.5140 1.0296 0.3108  0.0801  -0.0219 503 PRO C N   
13783 C CA  . PRO C 503 ? 1.0632 0.5398 1.0516 0.3236  0.0844  -0.0173 503 PRO C CA  
13784 C C   . PRO C 503 ? 1.0533 0.5675 1.0473 0.3263  0.0956  -0.0078 503 PRO C C   
13785 O O   . PRO C 503 ? 1.0652 0.5967 1.0597 0.3383  0.1027  -0.0113 503 PRO C O   
13786 C CB  . PRO C 503 ? 1.0405 0.4968 1.0422 0.3206  0.0758  -0.0061 503 PRO C CB  
13787 C CG  . PRO C 503 ? 1.3907 0.8177 1.3897 0.3079  0.0662  -0.0086 503 PRO C CG  
13788 C CD  . PRO C 503 ? 1.2676 0.7065 1.2552 0.2996  0.0704  -0.0133 503 PRO C CD  
13789 N N   . GLY C 504 ? 1.0971 0.6236 1.0964 0.3155  0.0972  0.0042  504 GLY C N   
13790 C CA  . GLY C 504 ? 1.1274 0.6878 1.1344 0.3165  0.1065  0.0131  504 GLY C CA  
13791 C C   . GLY C 504 ? 1.1054 0.6855 1.1045 0.3173  0.1156  0.0056  504 GLY C C   
13792 O O   . GLY C 504 ? 1.0631 0.6675 1.0684 0.3254  0.1239  0.0071  504 GLY C O   
13793 N N   . LEU C 505 ? 1.1079 0.6784 1.0941 0.3090  0.1143  -0.0014 505 LEU C N   
13794 C CA  . LEU C 505 ? 1.0816 0.6695 1.0589 0.3095  0.1228  -0.0072 505 LEU C CA  
13795 C C   . LEU C 505 ? 1.1239 0.7151 1.0939 0.3234  0.1275  -0.0172 505 LEU C C   
13796 O O   . LEU C 505 ? 1.1695 0.7852 1.1406 0.3282  0.1378  -0.0159 505 LEU C O   
13797 C CB  . LEU C 505 ? 1.0235 0.5984 0.9876 0.2991  0.1193  -0.0128 505 LEU C CB  
13798 C CG  . LEU C 505 ? 1.0855 0.6745 1.0374 0.3002  0.1270  -0.0192 505 LEU C CG  
13799 C CD1 . LEU C 505 ? 0.8883 0.5071 0.8505 0.2971  0.1372  -0.0094 505 LEU C CD1 
13800 C CD2 . LEU C 505 ? 1.1946 0.7673 1.1332 0.2917  0.1214  -0.0254 505 LEU C CD2 
13801 N N   . ALA C 506 ? 1.1097 0.6769 1.0734 0.3304  0.1203  -0.0266 506 ALA C N   
13802 C CA  . ALA C 506 ? 1.1002 0.6701 1.0558 0.3452  0.1250  -0.0366 506 ALA C CA  
13803 C C   . ALA C 506 ? 1.1019 0.6967 1.0723 0.3553  0.1335  -0.0281 506 ALA C C   
13804 O O   . ALA C 506 ? 1.0984 0.7116 1.0655 0.3654  0.1432  -0.0306 506 ALA C O   
13805 C CB  . ALA C 506 ? 0.9597 0.4971 0.9082 0.3504  0.1147  -0.0483 506 ALA C CB  
13806 N N   . THR C 507 ? 0.9834 0.5799 0.9707 0.3531  0.1299  -0.0171 507 THR C N   
13807 C CA  . THR C 507 ? 0.9677 0.5884 0.9715 0.3623  0.1364  -0.0082 507 THR C CA  
13808 C C   . THR C 507 ? 1.0913 0.7452 1.1028 0.3589  0.1475  -0.0010 507 THR C C   
13809 O O   . THR C 507 ? 1.1466 0.8227 1.1642 0.3688  0.1570  0.0003  507 THR C O   
13810 C CB  . THR C 507 ? 0.9371 0.5511 0.9554 0.3598  0.1288  0.0025  507 THR C CB  
13811 O OG1 . THR C 507 ? 0.9863 0.5689 0.9997 0.3637  0.1193  -0.0037 507 THR C OG1 
13812 C CG2 . THR C 507 ? 0.8900 0.5315 0.9270 0.3686  0.1344  0.0127  507 THR C CG2 
13813 N N   . VAL C 508 ? 1.0903 0.7469 1.1023 0.3450  0.1464  0.0040  508 VAL C N   
13814 C CA  . VAL C 508 ? 1.0219 0.7066 1.0428 0.3402  0.1558  0.0106  508 VAL C CA  
13815 C C   . VAL C 508 ? 1.1083 0.8017 1.1173 0.3446  0.1652  0.0039  508 VAL C C   
13816 O O   . VAL C 508 ? 1.1492 0.8689 1.1692 0.3484  0.1758  0.0094  508 VAL C O   
13817 C CB  . VAL C 508 ? 0.9727 0.6546 0.9945 0.3250  0.1519  0.0158  508 VAL C CB  
13818 C CG1 . VAL C 508 ? 0.7734 0.4813 0.8043 0.3200  0.1613  0.0210  508 VAL C CG1 
13819 C CG2 . VAL C 508 ? 1.0355 0.7129 1.0691 0.3223  0.1442  0.0249  508 VAL C CG2 
13820 N N   . CYS C 509 ? 1.0331 0.7049 1.0205 0.3446  0.1613  -0.0073 509 CYS C N   
13821 C CA  . CYS C 509 ? 1.0666 0.7452 1.0391 0.3504  0.1695  -0.0138 509 CYS C CA  
13822 C C   . CYS C 509 ? 1.0883 0.7815 1.0642 0.3664  0.1779  -0.0142 509 CYS C C   
13823 O O   . CYS C 509 ? 1.1614 0.8759 1.1372 0.3712  0.1897  -0.0109 509 CYS C O   
13824 C CB  . CYS C 509 ? 0.9605 0.6116 0.9095 0.3492  0.1614  -0.0269 509 CYS C CB  
13825 S SG  . CYS C 509 ? 1.2280 0.8661 1.1714 0.3313  0.1540  -0.0263 509 CYS C SG  
13826 N N   . LYS C 510 ? 0.9753 0.6566 0.9544 0.3751  0.1722  -0.0175 510 LYS C N   
13827 C CA  . LYS C 510 ? 0.9624 0.6565 0.9448 0.3915  0.1797  -0.0182 510 LYS C CA  
13828 C C   . LYS C 510 ? 1.0398 0.7676 1.0474 0.3932  0.1895  -0.0043 510 LYS C C   
13829 O O   . LYS C 510 ? 1.1931 0.9433 1.2037 0.4026  0.2015  -0.0013 510 LYS C O   
13830 C CB  . LYS C 510 ? 0.9594 0.6300 0.9404 0.3998  0.1702  -0.0251 510 LYS C CB  
13831 C CG  . LYS C 510 ? 1.0872 0.7624 1.0624 0.4184  0.1766  -0.0313 510 LYS C CG  
13832 C CD  . LYS C 510 ? 1.0955 0.7443 1.0698 0.4265  0.1667  -0.0388 510 LYS C CD  
13833 C CE  . LYS C 510 ? 1.1832 0.8234 1.1404 0.4431  0.1699  -0.0516 510 LYS C CE  
13834 N NZ  . LYS C 510 ? 1.3037 0.9183 1.2631 0.4516  0.1607  -0.0583 510 LYS C NZ  
13835 N N   . LEU C 511 ? 1.0605 0.7930 1.0869 0.3846  0.1843  0.0047  511 LEU C N   
13836 C CA  . LEU C 511 ? 0.9982 0.7626 1.0516 0.3859  0.1915  0.0174  511 LEU C CA  
13837 C C   . LEU C 511 ? 1.0148 0.8032 1.0752 0.3795  0.2028  0.0236  511 LEU C C   
13838 O O   . LEU C 511 ? 1.0734 0.8891 1.1492 0.3866  0.2139  0.0304  511 LEU C O   
13839 C CB  . LEU C 511 ? 0.8918 0.6541 0.9610 0.3782  0.1820  0.0248  511 LEU C CB  
13840 C CG  . LEU C 511 ? 0.8552 0.5983 0.9240 0.3851  0.1719  0.0231  511 LEU C CG  
13841 C CD1 . LEU C 511 ? 0.8345 0.5689 0.9103 0.3750  0.1618  0.0300  511 LEU C CD1 
13842 C CD2 . LEU C 511 ? 1.0812 0.8445 1.1669 0.4000  0.1767  0.0278  511 LEU C CD2 
13843 N N   . VAL C 512 ? 0.9916 0.7700 1.0423 0.3663  0.2001  0.0221  512 VAL C N   
13844 C CA  . VAL C 512 ? 0.9532 0.7506 1.0104 0.3593  0.2101  0.0281  512 VAL C CA  
13845 C C   . VAL C 512 ? 1.0110 0.8097 1.0490 0.3661  0.2197  0.0237  512 VAL C C   
13846 O O   . VAL C 512 ? 1.0466 0.8647 1.0922 0.3637  0.2307  0.0309  512 VAL C O   
13847 C CB  . VAL C 512 ? 0.9270 0.7135 0.9822 0.3433  0.2033  0.0287  512 VAL C CB  
13848 C CG1 . VAL C 512 ? 1.0181 0.8227 1.0824 0.3359  0.2132  0.0352  512 VAL C CG1 
13849 C CG2 . VAL C 512 ? 0.8419 0.6281 0.9139 0.3385  0.1942  0.0338  512 VAL C CG2 
13850 N N   . ASP C 513 ? 0.9493 0.7279 0.9636 0.3750  0.2155  0.0125  513 ASP C N   
13851 C CA  . ASP C 513 ? 0.9450 0.7232 0.9374 0.3837  0.2231  0.0069  513 ASP C CA  
13852 C C   . ASP C 513 ? 1.1253 0.8984 1.1041 0.3734  0.2240  0.0063  513 ASP C C   
13853 O O   . ASP C 513 ? 1.1782 0.9707 1.1608 0.3732  0.2360  0.0144  513 ASP C O   
13854 C CB  . ASP C 513 ? 1.0016 0.8097 1.0063 0.3956  0.2385  0.0157  513 ASP C CB  
13855 C CG  . ASP C 513 ? 1.2061 1.0129 1.1854 0.4082  0.2459  0.0098  513 ASP C CG  
13856 O OD1 . ASP C 513 ? 1.2201 1.0027 1.1761 0.4149  0.2375  -0.0039 513 ASP C OD1 
13857 O OD2 . ASP C 513 ? 1.4326 1.2624 1.4158 0.4117  0.2601  0.0193  513 ASP C OD2 
13858 N N   . ILE C 514 ? 1.1718 0.9187 1.1359 0.3648  0.2113  -0.0025 514 ILE C N   
13859 C CA  . ILE C 514 ? 1.0156 0.7552 0.9664 0.3547  0.2100  -0.0041 514 ILE C CA  
13860 C C   . ILE C 514 ? 1.0100 0.7194 0.9371 0.3539  0.1971  -0.0181 514 ILE C C   
13861 O O   . ILE C 514 ? 1.1501 0.8423 1.0770 0.3567  0.1877  -0.0247 514 ILE C O   
13862 C CB  . ILE C 514 ? 1.0570 0.8018 1.0271 0.3390  0.2075  0.0046  514 ILE C CB  
13863 C CG1 . ILE C 514 ? 0.9207 0.6533 0.9021 0.3346  0.1959  0.0039  514 ILE C CG1 
13864 C CG2 . ILE C 514 ? 1.0583 0.8322 1.0512 0.3378  0.2205  0.0177  514 ILE C CG2 
13865 C CD1 . ILE C 514 ? 0.9179 0.6534 0.9148 0.3209  0.1919  0.0110  514 ILE C CD1 
13866 N N   . PRO C 515 ? 1.0653 0.7670 0.9742 0.3494  0.1957  -0.0224 515 PRO C N   
13867 C CA  . PRO C 515 ? 1.1132 0.7864 1.0032 0.3473  0.1823  -0.0358 515 PRO C CA  
13868 C C   . PRO C 515 ? 1.0133 0.6730 0.9155 0.3326  0.1716  -0.0335 515 PRO C C   
13869 O O   . PRO C 515 ? 0.9939 0.6677 0.9152 0.3245  0.1752  -0.0224 515 PRO C O   
13870 C CB  . PRO C 515 ? 1.0861 0.7606 0.9553 0.3476  0.1855  -0.0388 515 PRO C CB  
13871 C CG  . PRO C 515 ? 1.1634 0.8663 1.0408 0.3503  0.2015  -0.0259 515 PRO C CG  
13872 C CD  . PRO C 515 ? 1.0242 0.7418 0.9306 0.3457  0.2057  -0.0150 515 PRO C CD  
13873 N N   . PRO C 516 ? 1.0324 0.6652 0.9248 0.3290  0.1585  -0.0433 516 PRO C N   
13874 C CA  . PRO C 516 ? 1.0497 0.6712 0.9539 0.3153  0.1498  -0.0387 516 PRO C CA  
13875 C C   . PRO C 516 ? 1.0573 0.6845 0.9599 0.3037  0.1512  -0.0340 516 PRO C C   
13876 O O   . PRO C 516 ? 1.0231 0.6485 0.9375 0.2928  0.1475  -0.0271 516 PRO C O   
13877 C CB  . PRO C 516 ? 1.0436 0.6341 0.9387 0.3162  0.1364  -0.0502 516 PRO C CB  
13878 C CG  . PRO C 516 ? 1.1923 0.7768 1.0649 0.3265  0.1366  -0.0633 516 PRO C CG  
13879 C CD  . PRO C 516 ? 1.1673 0.7786 1.0380 0.3370  0.1510  -0.0586 516 PRO C CD  
13880 N N   . VAL C 517 ? 0.9800 0.6146 0.8674 0.3071  0.1569  -0.0370 517 VAL C N   
13881 C CA  . VAL C 517 ? 0.9439 0.5848 0.8285 0.2983  0.1592  -0.0328 517 VAL C CA  
13882 C C   . VAL C 517 ? 1.0740 0.7411 0.9642 0.3014  0.1736  -0.0235 517 VAL C C   
13883 O O   . VAL C 517 ? 1.2137 0.8891 1.0951 0.3130  0.1808  -0.0253 517 VAL C O   
13884 C CB  . VAL C 517 ? 1.0266 0.6518 0.8877 0.3005  0.1526  -0.0441 517 VAL C CB  
13885 C CG1 . VAL C 517 ? 0.9705 0.6009 0.8297 0.2915  0.1540  -0.0393 517 VAL C CG1 
13886 C CG2 . VAL C 517 ? 1.0735 0.6702 0.9298 0.2992  0.1382  -0.0546 517 VAL C CG2 
13887 N N   . LEU C 518 ? 1.0014 0.6813 0.9068 0.2917  0.1780  -0.0134 518 LEU C N   
13888 C CA  . LEU C 518 ? 1.0556 0.7585 0.9708 0.2932  0.1915  -0.0037 518 LEU C CA  
13889 C C   . LEU C 518 ? 1.0933 0.7999 1.0004 0.2885  0.1954  -0.0008 518 LEU C C   
13890 O O   . LEU C 518 ? 1.1273 0.8301 1.0397 0.2778  0.1910  0.0012  518 LEU C O   
13891 C CB  . LEU C 518 ? 1.0026 0.7181 0.9448 0.2867  0.1939  0.0056  518 LEU C CB  
13892 C CG  . LEU C 518 ? 1.0353 0.7631 0.9919 0.2952  0.1991  0.0091  518 LEU C CG  
13893 C CD1 . LEU C 518 ? 1.0944 0.8066 1.0414 0.3028  0.1910  0.0004  518 LEU C CD1 
13894 C CD2 . LEU C 518 ? 0.7614 0.5011 0.7445 0.2885  0.1997  0.0175  518 LEU C CD2 
13895 N N   . HIS C 519 ? 1.1393 0.8541 1.0334 0.2973  0.2043  0.0003  519 HIS C N   
13896 C CA  . HIS C 519 ? 0.9721 0.6907 0.8579 0.2947  0.2089  0.0044  519 HIS C CA  
13897 C C   . HIS C 519 ? 0.9910 0.7264 0.9004 0.2881  0.2191  0.0174  519 HIS C C   
13898 O O   . HIS C 519 ? 0.9390 0.6897 0.8599 0.2935  0.2302  0.0250  519 HIS C O   
13899 C CB  . HIS C 519 ? 0.9264 0.6481 0.7891 0.3081  0.2152  0.0023  519 HIS C CB  
13900 C CG  . HIS C 519 ? 0.9757 0.6969 0.8236 0.3077  0.2168  0.0040  519 HIS C CG  
13901 N ND1 . HIS C 519 ? 1.0467 0.7753 0.9084 0.2985  0.2220  0.0140  519 HIS C ND1 
13902 C CD2 . HIS C 519 ? 1.0355 0.7497 0.8561 0.3164  0.2136  -0.0033 519 HIS C CD2 
13903 C CE1 . HIS C 519 ? 1.1109 0.8369 0.9538 0.3020  0.2223  0.0134  519 HIS C CE1 
13904 N NE2 . HIS C 519 ? 1.0890 0.8071 0.9065 0.3129  0.2172  0.0032  519 HIS C NE2 
13905 N N   . MET C 520 ? 0.9466 0.6790 0.8644 0.2765  0.2151  0.0196  520 MET C N   
13906 C CA  . MET C 520 ? 0.9333 0.6789 0.8758 0.2694  0.2229  0.0301  520 MET C CA  
13907 C C   . MET C 520 ? 1.0604 0.8107 0.9987 0.2693  0.2315  0.0370  520 MET C C   
13908 O O   . MET C 520 ? 1.0757 0.8351 1.0349 0.2639  0.2388  0.0457  520 MET C O   
13909 C CB  . MET C 520 ? 0.8757 0.6159 0.8316 0.2578  0.2137  0.0286  520 MET C CB  
13910 C CG  . MET C 520 ? 0.8241 0.5595 0.7856 0.2584  0.2059  0.0242  520 MET C CG  
13911 S SD  . MET C 520 ? 1.2427 0.9850 1.2274 0.2441  0.1977  0.0273  520 MET C SD  
13912 C CE  . MET C 520 ? 1.0290 0.7929 1.0398 0.2431  0.2089  0.0366  520 MET C CE  
13913 N N   . GLY C 521 ? 0.9899 0.7336 0.9031 0.2753  0.2304  0.0332  521 GLY C N   
13914 C CA  . GLY C 521 ? 0.9702 0.7191 0.8781 0.2775  0.2397  0.0414  521 GLY C CA  
13915 C C   . GLY C 521 ? 1.0380 0.7762 0.9285 0.2749  0.2319  0.0365  521 GLY C C   
13916 O O   . GLY C 521 ? 1.0535 0.7803 0.9294 0.2754  0.2203  0.0256  521 GLY C O   
13917 N N   . SER C 522 ? 0.9785 0.7205 0.8730 0.2719  0.2378  0.0448  522 SER C N   
13918 C CA  . SER C 522 ? 0.8616 0.5975 0.7411 0.2690  0.2306  0.0420  522 SER C CA  
13919 C C   . SER C 522 ? 0.9377 0.6690 0.8286 0.2545  0.2184  0.0373  522 SER C C   
13920 O O   . SER C 522 ? 1.0672 0.7997 0.9755 0.2476  0.2158  0.0362  522 SER C O   
13921 C CB  . SER C 522 ? 1.1537 0.8960 1.0345 0.2715  0.2416  0.0540  522 SER C CB  
13922 O OG  . SER C 522 ? 1.1942 0.9421 1.1026 0.2619  0.2473  0.0624  522 SER C OG  
13923 N N   . CYS C 523 ? 0.9879 0.7161 0.8695 0.2509  0.2117  0.0354  523 CYS C N   
13924 C CA  . CYS C 523 ? 1.1182 0.8445 1.0102 0.2383  0.2016  0.0323  523 CYS C CA  
13925 C C   . CYS C 523 ? 0.9477 0.6793 0.8614 0.2307  0.2071  0.0392  523 CYS C C   
13926 O O   . CYS C 523 ? 0.9680 0.6999 0.8945 0.2219  0.2008  0.0364  523 CYS C O   
13927 C CB  . CYS C 523 ? 0.8432 0.5676 0.7215 0.2374  0.1942  0.0295  523 CYS C CB  
13928 S SG  . CYS C 523 ? 1.6638 1.3809 1.5320 0.2345  0.1787  0.0180  523 CYS C SG  
13929 N N   . VAL C 524 ? 0.9410 0.6762 0.8590 0.2342  0.2179  0.0480  524 VAL C N   
13930 C CA  . VAL C 524 ? 0.9112 0.6498 0.8528 0.2265  0.2226  0.0539  524 VAL C CA  
13931 C C   . VAL C 524 ? 1.0119 0.7551 0.9698 0.2237  0.2228  0.0525  524 VAL C C   
13932 O O   . VAL C 524 ? 0.9445 0.6899 0.9208 0.2147  0.2193  0.0516  524 VAL C O   
13933 C CB  . VAL C 524 ? 0.9724 0.7130 0.9179 0.2309  0.2351  0.0652  524 VAL C CB  
13934 C CG1 . VAL C 524 ? 0.8897 0.6330 0.8629 0.2228  0.2398  0.0709  524 VAL C CG1 
13935 C CG2 . VAL C 524 ? 0.9834 0.7197 0.9147 0.2337  0.2342  0.0674  524 VAL C CG2 
13936 N N   . ASP C 525 ? 1.0558 0.8008 1.0063 0.2322  0.2263  0.0517  525 ASP C N   
13937 C CA  . ASP C 525 ? 1.0088 0.7591 0.9744 0.2314  0.2268  0.0508  525 ASP C CA  
13938 C C   . ASP C 525 ? 0.9016 0.6476 0.8678 0.2253  0.2138  0.0420  525 ASP C C   
13939 O O   . ASP C 525 ? 0.9356 0.6856 0.9130 0.2254  0.2127  0.0410  525 ASP C O   
13940 C CB  . ASP C 525 ? 1.0919 0.8457 1.0490 0.2445  0.2355  0.0528  525 ASP C CB  
13941 C CG  . ASP C 525 ? 1.2329 0.9949 1.1945 0.2507  0.2507  0.0647  525 ASP C CG  
13942 O OD1 . ASP C 525 ? 1.1697 0.9356 1.1500 0.2429  0.2547  0.0722  525 ASP C OD1 
13943 O OD2 . ASP C 525 ? 1.2697 1.0342 1.2161 0.2639  0.2585  0.0666  525 ASP C OD2 
13944 N N   . ILE C 526 ? 0.9590 0.6983 0.9145 0.2203  0.2044  0.0370  526 ILE C N   
13945 C CA  . ILE C 526 ? 0.9437 0.6804 0.9015 0.2139  0.1932  0.0313  526 ILE C CA  
13946 C C   . ILE C 526 ? 0.8637 0.6079 0.8427 0.2059  0.1919  0.0332  526 ILE C C   
13947 O O   . ILE C 526 ? 0.8717 0.6171 0.8563 0.2023  0.1848  0.0305  526 ILE C O   
13948 C CB  . ILE C 526 ? 0.8253 0.5563 0.7697 0.2101  0.1847  0.0274  526 ILE C CB  
13949 C CG1 . ILE C 526 ? 0.8486 0.5719 0.7736 0.2173  0.1823  0.0231  526 ILE C CG1 
13950 C CG2 . ILE C 526 ? 0.6241 0.3556 0.5750 0.2021  0.1751  0.0249  526 ILE C CG2 
13951 C CD1 . ILE C 526 ? 0.7500 0.4702 0.6633 0.2144  0.1750  0.0203  526 ILE C CD1 
13952 N N   . SER C 527 ? 0.7849 0.5337 0.7758 0.2035  0.1984  0.0379  527 SER C N   
13953 C CA  . SER C 527 ? 0.8489 0.6043 0.8608 0.1961  0.1965  0.0385  527 SER C CA  
13954 C C   . SER C 527 ? 0.8381 0.6014 0.8643 0.1978  0.1974  0.0395  527 SER C C   
13955 O O   . SER C 527 ? 1.0091 0.7784 1.0493 0.1922  0.1912  0.0374  527 SER C O   
13956 C CB  . SER C 527 ? 0.8398 0.5961 0.8630 0.1939  0.2040  0.0438  527 SER C CB  
13957 O OG  . SER C 527 ? 0.9755 0.7336 0.9980 0.2010  0.2155  0.0511  527 SER C OG  
13958 N N   . ARG C 528 ? 0.7858 0.5501 0.8076 0.2067  0.2046  0.0423  528 ARG C N   
13959 C CA  . ARG C 528 ? 0.8786 0.6511 0.9132 0.2106  0.2063  0.0436  528 ARG C CA  
13960 C C   . ARG C 528 ? 0.8810 0.6495 0.9098 0.2098  0.1953  0.0377  528 ARG C C   
13961 O O   . ARG C 528 ? 0.9746 0.7511 1.0183 0.2087  0.1920  0.0380  528 ARG C O   
13962 C CB  . ARG C 528 ? 0.8368 0.6100 0.8630 0.2226  0.2166  0.0468  528 ARG C CB  
13963 C CG  . ARG C 528 ? 0.9831 0.7624 1.0151 0.2257  0.2298  0.0556  528 ARG C CG  
13964 C CD  . ARG C 528 ? 0.8718 0.6564 0.8984 0.2393  0.2404  0.0593  528 ARG C CD  
13965 N NE  . ARG C 528 ? 0.7961 0.5806 0.8106 0.2465  0.2517  0.0657  528 ARG C NE  
13966 C CZ  . ARG C 528 ? 0.9864 0.7816 1.0175 0.2461  0.2637  0.0773  528 ARG C CZ  
13967 N NH1 . ARG C 528 ? 0.8459 0.6526 0.9084 0.2375  0.2651  0.0826  528 ARG C NH1 
13968 N NH2 . ARG C 528 ? 1.0238 0.8185 1.0408 0.2541  0.2741  0.0841  528 ARG C NH2 
13969 N N   . ILE C 529 ? 0.8499 0.6066 0.8584 0.2104  0.1896  0.0332  529 ILE C N   
13970 C CA  . ILE C 529 ? 0.7071 0.4584 0.7105 0.2089  0.1796  0.0295  529 ILE C CA  
13971 C C   . ILE C 529 ? 0.7752 0.5332 0.7892 0.2000  0.1725  0.0295  529 ILE C C   
13972 O O   . ILE C 529 ? 0.8476 0.6098 0.8693 0.1995  0.1670  0.0296  529 ILE C O   
13973 C CB  . ILE C 529 ? 0.7736 0.5116 0.7560 0.2101  0.1752  0.0256  529 ILE C CB  
13974 C CG1 . ILE C 529 ? 0.6539 0.3850 0.6238 0.2208  0.1808  0.0236  529 ILE C CG1 
13975 C CG2 . ILE C 529 ? 0.6347 0.3672 0.6151 0.2065  0.1649  0.0238  529 ILE C CG2 
13976 C CD1 . ILE C 529 ? 0.8140 0.5335 0.7642 0.2221  0.1766  0.0189  529 ILE C CD1 
13977 N N   . LEU C 530 ? 0.6879 0.4473 0.7020 0.1941  0.1725  0.0292  530 LEU C N   
13978 C CA  . LEU C 530 ? 0.7762 0.5421 0.7984 0.1871  0.1656  0.0276  530 LEU C CA  
13979 C C   . LEU C 530 ? 0.8751 0.6525 0.9185 0.1861  0.1656  0.0286  530 LEU C C   
13980 O O   . LEU C 530 ? 0.9012 0.6851 0.9504 0.1838  0.1579  0.0271  530 LEU C O   
13981 C CB  . LEU C 530 ? 0.8416 0.6061 0.8614 0.1827  0.1668  0.0263  530 LEU C CB  
13982 C CG  . LEU C 530 ? 0.8341 0.5916 0.8361 0.1823  0.1646  0.0252  530 LEU C CG  
13983 C CD1 . LEU C 530 ? 0.8110 0.5669 0.8123 0.1804  0.1679  0.0248  530 LEU C CD1 
13984 C CD2 . LEU C 530 ? 0.8337 0.5936 0.8305 0.1794  0.1559  0.0238  530 LEU C CD2 
13985 N N   . ASP C 531 ? 0.7977 0.5791 0.8531 0.1882  0.1743  0.0319  531 ASP C N   
13986 C CA  . ASP C 531 ? 0.7765 0.5710 0.8561 0.1867  0.1751  0.0340  531 ASP C CA  
13987 C C   . ASP C 531 ? 0.8863 0.6868 0.9700 0.1919  0.1717  0.0347  531 ASP C C   
13988 O O   . ASP C 531 ? 1.0021 0.8138 1.1011 0.1892  0.1653  0.0339  531 ASP C O   
13989 C CB  . ASP C 531 ? 0.7845 0.5825 0.8758 0.1887  0.1873  0.0399  531 ASP C CB  
13990 C CG  . ASP C 531 ? 0.9619 0.7753 1.0829 0.1855  0.1888  0.0433  531 ASP C CG  
13991 O OD1 . ASP C 531 ? 0.9015 0.7206 1.0355 0.1780  0.1797  0.0392  531 ASP C OD1 
13992 O OD2 . ASP C 531 ? 0.9972 0.8180 1.1287 0.1907  0.1989  0.0500  531 ASP C OD2 
13993 N N   . LEU C 532 ? 0.9478 0.7403 1.0177 0.1999  0.1751  0.0357  532 LEU C N   
13994 C CA  . LEU C 532 ? 0.8017 0.5969 0.8744 0.2064  0.1722  0.0364  532 LEU C CA  
13995 C C   . LEU C 532 ? 0.8583 0.6516 0.9256 0.2028  0.1605  0.0344  532 LEU C C   
13996 O O   . LEU C 532 ? 1.0012 0.8052 1.0813 0.2033  0.1552  0.0355  532 LEU C O   
13997 C CB  . LEU C 532 ? 0.7656 0.5486 0.8220 0.2162  0.1778  0.0361  532 LEU C CB  
13998 C CG  . LEU C 532 ? 0.7945 0.5768 0.8527 0.2253  0.1763  0.0366  532 LEU C CG  
13999 C CD1 . LEU C 532 ? 0.8520 0.6515 0.9318 0.2307  0.1833  0.0411  532 LEU C CD1 
14000 C CD2 . LEU C 532 ? 0.6390 0.4039 0.6763 0.2338  0.1785  0.0332  532 LEU C CD2 
14001 N N   . VAL C 533 ? 0.7927 0.5744 0.8419 0.1996  0.1567  0.0322  533 VAL C N   
14002 C CA  . VAL C 533 ? 0.8258 0.6068 0.8693 0.1967  0.1470  0.0323  533 VAL C CA  
14003 C C   . VAL C 533 ? 0.9359 0.7310 0.9906 0.1912  0.1411  0.0310  533 VAL C C   
14004 O O   . VAL C 533 ? 0.9602 0.7611 1.0157 0.1916  0.1335  0.0324  533 VAL C O   
14005 C CB  . VAL C 533 ? 0.7689 0.5375 0.7937 0.1937  0.1451  0.0314  533 VAL C CB  
14006 C CG1 . VAL C 533 ? 0.6734 0.4440 0.6935 0.1904  0.1367  0.0336  533 VAL C CG1 
14007 C CG2 . VAL C 533 ? 0.6680 0.4221 0.6821 0.1991  0.1481  0.0310  533 VAL C CG2 
14008 N N   . GLY C 534 ? 0.8394 0.6394 0.9025 0.1868  0.1442  0.0284  534 GLY C N   
14009 C CA  . GLY C 534 ? 0.8663 0.6776 0.9405 0.1816  0.1376  0.0250  534 GLY C CA  
14010 C C   . GLY C 534 ? 0.8477 0.6737 0.9421 0.1833  0.1341  0.0261  534 GLY C C   
14011 O O   . GLY C 534 ? 0.8142 0.6499 0.9119 0.1822  0.1246  0.0240  534 GLY C O   
14012 N N   . ARG C 535 ? 0.8752 0.7045 0.9831 0.1868  0.1419  0.0297  535 ARG C N   
14013 C CA  . ARG C 535 ? 0.7768 0.6226 0.9072 0.1891  0.1398  0.0319  535 ARG C CA  
14014 C C   . ARG C 535 ? 0.8897 0.7380 1.0143 0.1954  0.1328  0.0341  535 ARG C C   
14015 O O   . ARG C 535 ? 0.9104 0.7737 1.0481 0.1955  0.1246  0.0338  535 ARG C O   
14016 C CB  . ARG C 535 ? 0.9016 0.7507 1.0448 0.1939  0.1517  0.0370  535 ARG C CB  
14017 C CG  . ARG C 535 ? 0.7141 0.5657 0.8710 0.1878  0.1591  0.0378  535 ARG C CG  
14018 C CD  . ARG C 535 ? 0.8961 0.7461 1.0538 0.1949  0.1733  0.0440  535 ARG C CD  
14019 N NE  . ARG C 535 ? 1.1363 0.9891 1.3076 0.1899  0.1820  0.0475  535 ARG C NE  
14020 C CZ  . ARG C 535 ? 1.1109 0.9802 1.3122 0.1867  0.1860  0.0526  535 ARG C CZ  
14021 N NH1 . ARG C 535 ? 0.6947 0.5816 0.9164 0.1884  0.1814  0.0538  535 ARG C NH1 
14022 N NH2 . ARG C 535 ? 1.1555 1.0248 1.3684 0.1818  0.1946  0.0573  535 ARG C NH2 
14023 N N   . VAL C 536 ? 0.7805 0.6139 0.8860 0.2007  0.1352  0.0364  536 VAL C N   
14024 C CA  . VAL C 536 ? 0.7816 0.6134 0.8810 0.2068  0.1292  0.0399  536 VAL C CA  
14025 C C   . VAL C 536 ? 0.8716 0.7091 0.9644 0.2026  0.1185  0.0389  536 VAL C C   
14026 O O   . VAL C 536 ? 0.8958 0.7440 0.9943 0.2062  0.1112  0.0416  536 VAL C O   
14027 C CB  . VAL C 536 ? 0.7232 0.5346 0.8042 0.2114  0.1333  0.0417  536 VAL C CB  
14028 C CG1 . VAL C 536 ? 0.7635 0.5697 0.8374 0.2158  0.1263  0.0463  536 VAL C CG1 
14029 C CG2 . VAL C 536 ? 0.8109 0.6181 0.8962 0.2188  0.1431  0.0420  536 VAL C CG2 
14030 N N   . ALA C 537 ? 0.8275 0.6590 0.9078 0.1962  0.1178  0.0353  537 ALA C N   
14031 C CA  . ALA C 537 ? 0.7389 0.5765 0.8104 0.1936  0.1090  0.0340  537 ALA C CA  
14032 C C   . ALA C 537 ? 0.7507 0.6069 0.8380 0.1919  0.1013  0.0295  537 ALA C C   
14033 O O   . ALA C 537 ? 0.8428 0.7097 0.9289 0.1952  0.0926  0.0311  537 ALA C O   
14034 C CB  . ALA C 537 ? 0.7457 0.5746 0.8026 0.1881  0.1112  0.0304  537 ALA C CB  
14035 N N   . ASN C 538 ? 0.6586 0.5190 0.7617 0.1870  0.1040  0.0243  538 ASN C N   
14036 C CA  . ASN C 538 ? 0.8416 0.7187 0.9632 0.1837  0.0957  0.0187  538 ASN C CA  
14037 C C   . ASN C 538 ? 0.7657 0.6586 0.9036 0.1892  0.0910  0.0229  538 ASN C C   
14038 O O   . ASN C 538 ? 0.8688 0.7768 1.0127 0.1894  0.0796  0.0196  538 ASN C O   
14039 C CB  . ASN C 538 ? 0.8000 0.6766 0.9395 0.1768  0.1011  0.0147  538 ASN C CB  
14040 C CG  . ASN C 538 ? 0.8579 0.7242 0.9868 0.1708  0.1010  0.0079  538 ASN C CG  
14041 O OD1 . ASN C 538 ? 0.9903 0.8574 1.1056 0.1705  0.0925  0.0022  538 ASN C OD1 
14042 N ND2 . ASN C 538 ? 0.9043 0.7613 1.0390 0.1671  0.1107  0.0086  538 ASN C ND2 
14043 N N   . LEU C 539 ? 0.7413 0.6314 0.8859 0.1946  0.0994  0.0297  539 LEU C N   
14044 C CA  . LEU C 539 ? 0.8917 0.7967 1.0527 0.2015  0.0964  0.0346  539 LEU C CA  
14045 C C   . LEU C 539 ? 0.8191 0.7261 0.9661 0.2081  0.0876  0.0385  539 LEU C C   
14046 O O   . LEU C 539 ? 0.8423 0.7670 1.0019 0.2121  0.0792  0.0399  539 LEU C O   
14047 C CB  . LEU C 539 ? 0.8184 0.7169 0.9850 0.2079  0.1087  0.0405  539 LEU C CB  
14048 C CG  . LEU C 539 ? 0.6042 0.5192 0.7916 0.2161  0.1085  0.0457  539 LEU C CG  
14049 C CD1 . LEU C 539 ? 0.8018 0.7406 1.0201 0.2106  0.1049  0.0434  539 LEU C CD1 
14050 C CD2 . LEU C 539 ? 0.6689 0.5740 0.8551 0.2242  0.1212  0.0502  539 LEU C CD2 
14051 N N   . LEU C 540 ? 0.8711 0.7613 0.9935 0.2091  0.0892  0.0411  540 LEU C N   
14052 C CA  . LEU C 540 ? 0.7366 0.6275 0.8452 0.2150  0.0821  0.0471  540 LEU C CA  
14053 C C   . LEU C 540 ? 0.8253 0.7257 0.9224 0.2119  0.0722  0.0429  540 LEU C C   
14054 O O   . LEU C 540 ? 0.9056 0.8099 0.9909 0.2172  0.0663  0.0489  540 LEU C O   
14055 C CB  . LEU C 540 ? 0.7139 0.5825 0.8044 0.2173  0.0888  0.0534  540 LEU C CB  
14056 C CG  . LEU C 540 ? 0.6886 0.5459 0.7856 0.2234  0.0968  0.0571  540 LEU C CG  
14057 C CD1 . LEU C 540 ? 0.6554 0.4887 0.7353 0.2223  0.1029  0.0588  540 LEU C CD1 
14058 C CD2 . LEU C 540 ? 0.8978 0.7616 1.0023 0.2335  0.0924  0.0645  540 LEU C CD2 
14059 N N   . GLY C 541 ? 0.7531 0.6568 0.8534 0.2043  0.0708  0.0331  541 GLY C N   
14060 C CA  . GLY C 541 ? 0.7701 0.6819 0.8587 0.2024  0.0614  0.0265  541 GLY C CA  
14061 C C   . GLY C 541 ? 0.8108 0.7115 0.8731 0.2031  0.0641  0.0298  541 GLY C C   
14062 O O   . GLY C 541 ? 0.8921 0.8016 0.9400 0.2061  0.0567  0.0289  541 GLY C O   
14063 N N   . VAL C 542 ? 0.7300 0.6128 0.7859 0.2007  0.0746  0.0338  542 VAL C N   
14064 C CA  . VAL C 542 ? 0.7204 0.5933 0.7550 0.2003  0.0780  0.0383  542 VAL C CA  
14065 C C   . VAL C 542 ? 0.8118 0.6730 0.8428 0.1937  0.0852  0.0320  542 VAL C C   
14066 O O   . VAL C 542 ? 0.8624 0.7219 0.9069 0.1899  0.0879  0.0254  542 VAL C O   
14067 C CB  . VAL C 542 ? 0.7369 0.5990 0.7669 0.2042  0.0823  0.0507  542 VAL C CB  
14068 C CG1 . VAL C 542 ? 0.8343 0.7073 0.8681 0.2119  0.0754  0.0581  542 VAL C CG1 
14069 C CG2 . VAL C 542 ? 0.7696 0.6165 0.8088 0.2026  0.0907  0.0506  542 VAL C CG2 
14070 N N   . ASP C 543 ? 0.7820 0.6364 0.7961 0.1928  0.0885  0.0351  543 ASP C N   
14071 C CA  . ASP C 543 ? 0.8278 0.6717 0.8373 0.1878  0.0951  0.0306  543 ASP C CA  
14072 C C   . ASP C 543 ? 0.8572 0.6857 0.8681 0.1865  0.1029  0.0364  543 ASP C C   
14073 O O   . ASP C 543 ? 0.9062 0.7313 0.9183 0.1896  0.1025  0.0440  543 ASP C O   
14074 C CB  . ASP C 543 ? 0.9260 0.7733 0.9177 0.1884  0.0945  0.0313  543 ASP C CB  
14075 C CG  . ASP C 543 ? 0.9511 0.7923 0.9388 0.1847  0.0989  0.0239  543 ASP C CG  
14076 O OD1 . ASP C 543 ? 0.9263 0.7579 0.9236 0.1811  0.1038  0.0204  543 ASP C OD1 
14077 O OD2 . ASP C 543 ? 0.9936 0.8402 0.9682 0.1865  0.0979  0.0222  543 ASP C OD2 
14078 N N   . MET C 544 ? 0.7947 0.6135 0.8048 0.1828  0.1092  0.0325  544 MET C N   
14079 C CA  . MET C 544 ? 0.8162 0.6209 0.8256 0.1824  0.1155  0.0361  544 MET C CA  
14080 C C   . MET C 544 ? 0.8612 0.6596 0.8596 0.1821  0.1151  0.0439  544 MET C C   
14081 O O   . MET C 544 ? 0.8142 0.6009 0.8131 0.1828  0.1171  0.0473  544 MET C O   
14082 C CB  . MET C 544 ? 0.7721 0.5698 0.7816 0.1793  0.1218  0.0306  544 MET C CB  
14083 C CG  . MET C 544 ? 0.8003 0.6014 0.8246 0.1791  0.1240  0.0258  544 MET C CG  
14084 S SD  . MET C 544 ? 0.9714 0.7666 0.9967 0.1756  0.1308  0.0206  544 MET C SD  
14085 C CE  . MET C 544 ? 0.9432 0.7246 0.9587 0.1777  0.1381  0.0245  544 MET C CE  
14086 N N   . SER C 545 ? 0.8963 0.7029 0.8857 0.1814  0.1123  0.0468  545 SER C N   
14087 C CA  . SER C 545 ? 0.8853 0.6889 0.8674 0.1803  0.1123  0.0562  545 SER C CA  
14088 C C   . SER C 545 ? 1.0723 0.8753 1.0573 0.1836  0.1086  0.0655  545 SER C C   
14089 O O   . SER C 545 ? 1.1105 0.9063 1.0937 0.1819  0.1088  0.0744  545 SER C O   
14090 C CB  . SER C 545 ? 0.7894 0.6049 0.7613 0.1799  0.1119  0.0577  545 SER C CB  
14091 O OG  . SER C 545 ? 0.8699 0.6991 0.8397 0.1839  0.1075  0.0536  545 SER C OG  
14092 N N   . ASP C 546 ? 0.9961 0.8067 0.9870 0.1882  0.1047  0.0641  546 ASP C N   
14093 C CA  . ASP C 546 ? 0.9766 0.7877 0.9704 0.1929  0.1010  0.0734  546 ASP C CA  
14094 C C   . ASP C 546 ? 0.9766 0.7719 0.9792 0.1949  0.1027  0.0742  546 ASP C C   
14095 O O   . ASP C 546 ? 0.9874 0.7778 0.9921 0.1988  0.1003  0.0830  546 ASP C O   
14096 C CB  . ASP C 546 ? 0.8980 0.7266 0.8943 0.1981  0.0950  0.0713  546 ASP C CB  
14097 C CG  . ASP C 546 ? 1.0178 0.8616 1.0036 0.1980  0.0922  0.0678  546 ASP C CG  
14098 O OD1 . ASP C 546 ? 1.2585 1.1049 1.2331 0.1976  0.0936  0.0753  546 ASP C OD1 
14099 O OD2 . ASP C 546 ? 1.1014 0.9546 1.0908 0.1985  0.0887  0.0575  546 ASP C OD2 
14100 N N   . LEU C 547 ? 0.9487 0.7359 0.9557 0.1935  0.1071  0.0656  547 LEU C N   
14101 C CA  . LEU C 547 ? 0.7928 0.5660 0.8059 0.1974  0.1094  0.0649  547 LEU C CA  
14102 C C   . LEU C 547 ? 0.8656 0.6191 0.8729 0.1949  0.1106  0.0676  547 LEU C C   
14103 O O   . LEU C 547 ? 0.9365 0.6881 0.9370 0.1887  0.1117  0.0671  547 LEU C O   
14104 C CB  . LEU C 547 ? 0.7690 0.5434 0.7883 0.1980  0.1145  0.0554  547 LEU C CB  
14105 C CG  . LEU C 547 ? 0.8694 0.6619 0.8992 0.1990  0.1132  0.0514  547 LEU C CG  
14106 C CD1 . LEU C 547 ? 0.7937 0.5862 0.8296 0.1973  0.1196  0.0441  547 LEU C CD1 
14107 C CD2 . LEU C 547 ? 0.6954 0.4952 0.7360 0.2060  0.1096  0.0553  547 LEU C CD2 
14108 N N   . PRO C 548 ? 0.8585 0.5968 0.8690 0.1998  0.1100  0.0696  548 PRO C N   
14109 C CA  . PRO C 548 ? 0.8691 0.5866 0.8750 0.1968  0.1095  0.0700  548 PRO C CA  
14110 C C   . PRO C 548 ? 0.9265 0.6362 0.9283 0.1968  0.1140  0.0591  548 PRO C C   
14111 O O   . PRO C 548 ? 0.9920 0.6893 0.9940 0.2033  0.1156  0.0541  548 PRO C O   
14112 C CB  . PRO C 548 ? 0.7933 0.4971 0.8042 0.2036  0.1066  0.0751  548 PRO C CB  
14113 C CG  . PRO C 548 ? 0.7965 0.5120 0.8144 0.2121  0.1084  0.0725  548 PRO C CG  
14114 C CD  . PRO C 548 ? 0.6610 0.4001 0.6801 0.2087  0.1092  0.0708  548 PRO C CD  
14115 N N   . VAL C 549 ? 0.8297 0.5478 0.8268 0.1910  0.1164  0.0555  549 VAL C N   
14116 C CA  . VAL C 549 ? 0.8325 0.5457 0.8244 0.1913  0.1209  0.0467  549 VAL C CA  
14117 C C   . VAL C 549 ? 0.9793 0.6883 0.9640 0.1840  0.1194  0.0463  549 VAL C C   
14118 O O   . VAL C 549 ? 0.9963 0.7124 0.9813 0.1781  0.1167  0.0526  549 VAL C O   
14119 C CB  . VAL C 549 ? 0.7936 0.5222 0.7893 0.1928  0.1262  0.0426  549 VAL C CB  
14120 C CG1 . VAL C 549 ? 0.8423 0.5759 0.8480 0.2002  0.1280  0.0425  549 VAL C CG1 
14121 C CG2 . VAL C 549 ? 0.9008 0.6449 0.8971 0.1873  0.1246  0.0451  549 VAL C CG2 
14122 N N   . ALA C 550 ? 0.9593 0.6581 0.9374 0.1851  0.1211  0.0391  550 ALA C N   
14123 C CA  . ALA C 550 ? 0.9118 0.6076 0.8839 0.1787  0.1188  0.0379  550 ALA C CA  
14124 C C   . ALA C 550 ? 0.9983 0.6909 0.9619 0.1823  0.1228  0.0293  550 ALA C C   
14125 O O   . ALA C 550 ? 1.0698 0.7578 1.0313 0.1902  0.1269  0.0246  550 ALA C O   
14126 C CB  . ALA C 550 ? 0.6667 0.3468 0.6401 0.1751  0.1116  0.0404  550 ALA C CB  
14127 N N   . GLY C 551 ? 0.8623 0.5590 0.8211 0.1775  0.1222  0.0284  551 GLY C N   
14128 C CA  . GLY C 551 ? 0.8077 0.5025 0.7570 0.1810  0.1254  0.0217  551 GLY C CA  
14129 C C   . GLY C 551 ? 0.8039 0.4896 0.7479 0.1770  0.1182  0.0188  551 GLY C C   
14130 O O   . GLY C 551 ? 0.8243 0.5123 0.7745 0.1690  0.1128  0.0241  551 GLY C O   
14131 N N   . VAL C 552 ? 0.6857 0.3619 0.6189 0.1827  0.1177  0.0107  552 VAL C N   
14132 C CA  . VAL C 552 ? 0.8131 0.4807 0.7415 0.1790  0.1089  0.0060  552 VAL C CA  
14133 C C   . VAL C 552 ? 0.8803 0.5510 0.7954 0.1842  0.1108  -0.0001 552 VAL C C   
14134 O O   . VAL C 552 ? 1.0553 0.7250 0.9612 0.1939  0.1177  -0.0037 552 VAL C O   
14135 C CB  . VAL C 552 ? 0.9211 0.5676 0.8484 0.1811  0.1013  0.0002  552 VAL C CB  
14136 C CG1 . VAL C 552 ? 0.9942 0.6328 0.9238 0.1727  0.0896  -0.0025 552 VAL C CG1 
14137 C CG2 . VAL C 552 ? 0.9293 0.5714 0.8676 0.1804  0.1018  0.0065  552 VAL C CG2 
14138 N N   . ALA C 553 ? 0.8993 0.5749 0.8140 0.1782  0.1047  -0.0002 553 ALA C N   
14139 C CA  . ALA C 553 ? 0.9478 0.6274 0.8497 0.1830  0.1047  -0.0053 553 ALA C CA  
14140 C C   . ALA C 553 ? 0.9314 0.6012 0.8312 0.1789  0.0914  -0.0124 553 ALA C C   
14141 O O   . ALA C 553 ? 0.8746 0.5533 0.7815 0.1708  0.0852  -0.0096 553 ALA C O   
14142 C CB  . ALA C 553 ? 0.8369 0.5345 0.7428 0.1795  0.1091  0.0017  553 ALA C CB  
14143 N N   . PRO C 554 ? 0.8584 0.5099 0.7502 0.1844  0.0862  -0.0219 554 PRO C N   
14144 C CA  . PRO C 554 ? 0.9184 0.5575 0.8096 0.1798  0.0716  -0.0305 554 PRO C CA  
14145 C C   . PRO C 554 ? 0.9842 0.6323 0.8668 0.1801  0.0654  -0.0353 554 PRO C C   
14146 O O   . PRO C 554 ? 0.9931 0.6410 0.8847 0.1706  0.0532  -0.0372 554 PRO C O   
14147 C CB  . PRO C 554 ? 0.9746 0.5923 0.8536 0.1902  0.0696  -0.0416 554 PRO C CB  
14148 C CG  . PRO C 554 ? 0.9949 0.6144 0.8768 0.1958  0.0820  -0.0352 554 PRO C CG  
14149 C CD  . PRO C 554 ? 1.0480 0.6890 0.9319 0.1953  0.0930  -0.0257 554 PRO C CD  
14150 N N   . GLU C 555 ? 1.0153 0.6716 0.8815 0.1911  0.0735  -0.0368 555 GLU C N   
14151 C CA  . GLU C 555 ? 0.9296 0.5959 0.7852 0.1939  0.0687  -0.0404 555 GLU C CA  
14152 C C   . GLU C 555 ? 1.0546 0.7376 0.9078 0.1987  0.0829  -0.0306 555 GLU C C   
14153 O O   . GLU C 555 ? 1.2161 0.8969 1.0625 0.2073  0.0945  -0.0287 555 GLU C O   
14154 C CB  . GLU C 555 ? 0.8709 0.5247 0.7034 0.2061  0.0627  -0.0548 555 GLU C CB  
14155 C CG  . GLU C 555 ? 0.9417 0.5723 0.7736 0.2066  0.0548  -0.0651 555 GLU C CG  
14156 C CD  . GLU C 555 ? 1.1364 0.7532 0.9441 0.2195  0.0472  -0.0815 555 GLU C CD  
14157 O OE1 . GLU C 555 ? 1.2230 0.8493 1.0138 0.2271  0.0455  -0.0856 555 GLU C OE1 
14158 O OE2 . GLU C 555 ? 0.9862 0.5823 0.7908 0.2231  0.0429  -0.0905 555 GLU C OE2 
14159 N N   . TRP C 556 ? 0.8725 0.5719 0.7335 0.1930  0.0822  -0.0238 556 TRP C N   
14160 C CA  . TRP C 556 ? 0.9182 0.6309 0.7779 0.1975  0.0949  -0.0149 556 TRP C CA  
14161 C C   . TRP C 556 ? 0.9651 0.6931 0.8242 0.1968  0.0909  -0.0123 556 TRP C C   
14162 O O   . TRP C 556 ? 1.0761 0.8088 0.9443 0.1886  0.0793  -0.0140 556 TRP C O   
14163 C CB  . TRP C 556 ? 0.8802 0.5973 0.7560 0.1910  0.1033  -0.0056 556 TRP C CB  
14164 C CG  . TRP C 556 ? 0.8624 0.5891 0.7556 0.1791  0.0974  -0.0001 556 TRP C CG  
14165 C CD1 . TRP C 556 ? 0.7955 0.5167 0.7014 0.1695  0.0899  0.0003  556 TRP C CD1 
14166 C CD2 . TRP C 556 ? 0.8424 0.5866 0.7422 0.1763  0.0990  0.0068  556 TRP C CD2 
14167 N NE1 . TRP C 556 ? 0.8310 0.5670 0.7514 0.1607  0.0874  0.0079  556 TRP C NE1 
14168 C CE2 . TRP C 556 ? 0.7880 0.5386 0.7045 0.1652  0.0929  0.0114  556 TRP C CE2 
14169 C CE3 . TRP C 556 ? 0.8167 0.5714 0.7101 0.1830  0.1055  0.0102  556 TRP C CE3 
14170 C CZ2 . TRP C 556 ? 0.8618 0.6309 0.7883 0.1612  0.0935  0.0188  556 TRP C CZ2 
14171 C CZ3 . TRP C 556 ? 0.8186 0.5896 0.7217 0.1792  0.1053  0.0165  556 TRP C CZ3 
14172 C CH2 . TRP C 556 ? 0.8346 0.6136 0.7538 0.1688  0.0997  0.0206  556 TRP C CH2 
14173 N N   . MET C 557 ? 0.8303 0.5664 0.6805 0.2054  0.1004  -0.0073 557 MET C N   
14174 C CA  . MET C 557 ? 0.9773 0.7285 0.8265 0.2068  0.0976  -0.0039 557 MET C CA  
14175 C C   . MET C 557 ? 0.8451 0.6036 0.6971 0.2106  0.1112  0.0061  557 MET C C   
14176 O O   . MET C 557 ? 0.9172 0.6872 0.7814 0.2054  0.1117  0.0120  557 MET C O   
14177 C CB  . MET C 557 ? 0.9180 0.6690 0.7481 0.2158  0.0895  -0.0116 557 MET C CB  
14178 C CG  . MET C 557 ? 0.9483 0.6881 0.7573 0.2289  0.0964  -0.0159 557 MET C CG  
14179 S SD  . MET C 557 ? 1.0917 0.8372 0.8916 0.2408  0.1148  -0.0043 557 MET C SD  
14180 C CE  . MET C 557 ? 0.9276 0.6865 0.7144 0.2487  0.1085  -0.0034 557 MET C CE  
14181 N N   . SER C 558 ? 0.8947 0.6468 0.7364 0.2196  0.1222  0.0081  558 SER C N   
14182 C CA  . SER C 558 ? 0.8512 0.6078 0.6953 0.2238  0.1343  0.0170  558 SER C CA  
14183 C C   . SER C 558 ? 0.9038 0.6648 0.7660 0.2150  0.1372  0.0217  558 SER C C   
14184 O O   . SER C 558 ? 0.9493 0.7065 0.8213 0.2071  0.1348  0.0197  558 SER C O   
14185 C CB  . SER C 558 ? 0.9999 0.7476 0.8369 0.2313  0.1459  0.0192  558 SER C CB  
14186 O OG  . SER C 558 ? 0.9560 0.6960 0.8025 0.2256  0.1476  0.0168  558 SER C OG  
14187 N N   . GLU C 559 ? 0.9478 0.7165 0.8133 0.2175  0.1422  0.0280  559 GLU C N   
14188 C CA  . GLU C 559 ? 0.7977 0.5703 0.6773 0.2118  0.1458  0.0315  559 GLU C CA  
14189 C C   . GLU C 559 ? 0.8636 0.6259 0.7486 0.2099  0.1534  0.0316  559 GLU C C   
14190 O O   . GLU C 559 ? 0.8830 0.6469 0.7789 0.2040  0.1540  0.0320  559 GLU C O   
14191 C CB  . GLU C 559 ? 0.7585 0.5377 0.6379 0.2178  0.1507  0.0372  559 GLU C CB  
14192 C CG  . GLU C 559 ? 1.0573 0.8512 0.9369 0.2183  0.1429  0.0381  559 GLU C CG  
14193 C CD  . GLU C 559 ? 1.1844 0.9840 1.0600 0.2277  0.1473  0.0438  559 GLU C CD  
14194 O OE1 . GLU C 559 ? 1.1800 0.9719 1.0455 0.2360  0.1536  0.0467  559 GLU C OE1 
14195 O OE2 . GLU C 559 ? 0.8514 0.6639 0.7344 0.2274  0.1450  0.0462  559 GLU C OE2 
14196 N N   . LYS C 560 ? 0.8541 0.6077 0.7315 0.2154  0.1588  0.0313  560 LYS C N   
14197 C CA  . LYS C 560 ? 0.8924 0.6386 0.7768 0.2138  0.1655  0.0317  560 LYS C CA  
14198 C C   . LYS C 560 ? 0.8855 0.6297 0.7761 0.2065  0.1590  0.0268  560 LYS C C   
14199 O O   . LYS C 560 ? 0.9795 0.7228 0.8811 0.2019  0.1612  0.0273  560 LYS C O   
14200 C CB  . LYS C 560 ? 0.7686 0.5090 0.6434 0.2222  0.1727  0.0333  560 LYS C CB  
14201 C CG  . LYS C 560 ? 1.0126 0.7532 0.8847 0.2293  0.1822  0.0411  560 LYS C CG  
14202 C CD  . LYS C 560 ? 0.9264 0.6633 0.7908 0.2377  0.1911  0.0448  560 LYS C CD  
14203 C CE  . LYS C 560 ? 0.9870 0.7244 0.8315 0.2454  0.1863  0.0402  560 LYS C CE  
14204 N NZ  . LYS C 560 ? 1.0471 0.7839 0.8803 0.2569  0.1968  0.0461  560 LYS C NZ  
14205 N N   . ALA C 561 ? 0.8110 0.5540 0.6951 0.2056  0.1504  0.0221  561 ALA C N   
14206 C CA  . ALA C 561 ? 0.8860 0.6251 0.7764 0.1988  0.1437  0.0184  561 ALA C CA  
14207 C C   . ALA C 561 ? 0.8602 0.6072 0.7635 0.1902  0.1407  0.0215  561 ALA C C   
14208 O O   . ALA C 561 ? 0.8302 0.5748 0.7415 0.1853  0.1394  0.0216  561 ALA C O   
14209 C CB  . ALA C 561 ? 0.8698 0.6049 0.7518 0.1990  0.1338  0.0124  561 ALA C CB  
14210 N N   . VAL C 562 ? 0.8505 0.6078 0.7550 0.1898  0.1401  0.0247  562 VAL C N   
14211 C CA  . VAL C 562 ? 0.6723 0.4397 0.5872 0.1838  0.1386  0.0282  562 VAL C CA  
14212 C C   . VAL C 562 ? 0.8143 0.5804 0.7342 0.1845  0.1457  0.0294  562 VAL C C   
14213 O O   . VAL C 562 ? 0.8974 0.6658 0.8244 0.1798  0.1442  0.0302  562 VAL C O   
14214 C CB  . VAL C 562 ? 0.6772 0.4575 0.5922 0.1851  0.1368  0.0312  562 VAL C CB  
14215 C CG1 . VAL C 562 ? 0.7280 0.5204 0.6528 0.1807  0.1367  0.0353  562 VAL C CG1 
14216 C CG2 . VAL C 562 ? 0.8030 0.5861 0.7148 0.1837  0.1280  0.0292  562 VAL C CG2 
14217 N N   . ALA C 563 ? 0.8379 0.6001 0.7546 0.1903  0.1528  0.0298  563 ALA C N   
14218 C CA  . ALA C 563 ? 0.8313 0.5910 0.7547 0.1903  0.1584  0.0298  563 ALA C CA  
14219 C C   . ALA C 563 ? 0.9137 0.6679 0.8423 0.1873  0.1582  0.0280  563 ALA C C   
14220 O O   . ALA C 563 ? 0.8264 0.5827 0.7624 0.1841  0.1577  0.0273  563 ALA C O   
14221 C CB  . ALA C 563 ? 0.7782 0.5325 0.6993 0.1963  0.1659  0.0316  563 ALA C CB  
14222 N N   . ILE C 564 ? 0.9560 0.7036 0.8798 0.1894  0.1581  0.0268  564 ILE C N   
14223 C CA  . ILE C 564 ? 0.8115 0.5540 0.7397 0.1884  0.1582  0.0253  564 ILE C CA  
14224 C C   . ILE C 564 ? 0.9120 0.6572 0.8452 0.1823  0.1511  0.0251  564 ILE C C   
14225 O O   . ILE C 564 ? 0.9394 0.6866 0.8807 0.1800  0.1512  0.0255  564 ILE C O   
14226 C CB  . ILE C 564 ? 0.7768 0.5119 0.6959 0.1942  0.1596  0.0234  564 ILE C CB  
14227 C CG1 . ILE C 564 ? 0.8101 0.5437 0.7273 0.2008  0.1694  0.0262  564 ILE C CG1 
14228 C CG2 . ILE C 564 ? 0.7611 0.4907 0.6836 0.1934  0.1569  0.0210  564 ILE C CG2 
14229 C CD1 . ILE C 564 ? 0.7723 0.5020 0.6751 0.2091  0.1717  0.0254  564 ILE C CD1 
14230 N N   . GLY C 565 ? 0.7451 0.4917 0.6748 0.1796  0.1447  0.0252  565 GLY C N   
14231 C CA  . GLY C 565 ? 0.7874 0.5369 0.7232 0.1735  0.1386  0.0274  565 GLY C CA  
14232 C C   . GLY C 565 ? 0.8023 0.5621 0.7439 0.1713  0.1401  0.0305  565 GLY C C   
14233 O O   . GLY C 565 ? 0.8707 0.6316 0.8175 0.1692  0.1387  0.0321  565 GLY C O   
14234 N N   . THR C 566 ? 0.7831 0.5502 0.7226 0.1731  0.1429  0.0310  566 THR C N   
14235 C CA  . THR C 566 ? 0.7995 0.5760 0.7419 0.1729  0.1442  0.0323  566 THR C CA  
14236 C C   . THR C 566 ? 0.8744 0.6478 0.8209 0.1739  0.1464  0.0293  566 THR C C   
14237 O O   . THR C 566 ? 0.7929 0.5726 0.7420 0.1724  0.1440  0.0303  566 THR C O   
14238 C CB  . THR C 566 ? 0.6929 0.4753 0.6319 0.1766  0.1473  0.0321  566 THR C CB  
14239 O OG1 . THR C 566 ? 0.8227 0.6102 0.7597 0.1755  0.1443  0.0350  566 THR C OG1 
14240 C CG2 . THR C 566 ? 0.5871 0.3794 0.5268 0.1779  0.1480  0.0324  566 THR C CG2 
14241 N N   . TYR C 567 ? 0.8694 0.6347 0.8173 0.1765  0.1507  0.0264  567 TYR C N   
14242 C CA  . TYR C 567 ? 0.9148 0.6787 0.8703 0.1763  0.1519  0.0238  567 TYR C CA  
14243 C C   . TYR C 567 ? 0.8443 0.6072 0.8043 0.1746  0.1488  0.0248  567 TYR C C   
14244 O O   . TYR C 567 ? 0.7080 0.4747 0.6745 0.1738  0.1470  0.0234  567 TYR C O   
14245 C CB  . TYR C 567 ? 0.8480 0.6054 0.8077 0.1788  0.1580  0.0223  567 TYR C CB  
14246 C CG  . TYR C 567 ? 0.9414 0.6921 0.9004 0.1813  0.1625  0.0241  567 TYR C CG  
14247 C CD1 . TYR C 567 ? 0.8774 0.6267 0.8417 0.1812  0.1623  0.0242  567 TYR C CD1 
14248 C CD2 . TYR C 567 ? 0.9151 0.6616 0.8687 0.1852  0.1678  0.0260  567 TYR C CD2 
14249 C CE1 . TYR C 567 ? 0.8542 0.5985 0.8170 0.1853  0.1674  0.0256  567 TYR C CE1 
14250 C CE2 . TYR C 567 ? 0.8995 0.6414 0.8509 0.1892  0.1729  0.0280  567 TYR C CE2 
14251 C CZ  . TYR C 567 ? 0.8633 0.6042 0.8188 0.1895  0.1729  0.0275  567 TYR C CZ  
14252 O OH  . TYR C 567 ? 0.8682 0.6057 0.8200 0.1952  0.1787  0.0294  567 TYR C OH  
14253 N N   . VAL C 568 ? 0.7868 0.5447 0.7433 0.1745  0.1473  0.0266  568 VAL C N   
14254 C CA  . VAL C 568 ? 0.8108 0.5657 0.7712 0.1739  0.1443  0.0277  568 VAL C CA  
14255 C C   . VAL C 568 ? 0.8236 0.5861 0.7853 0.1706  0.1390  0.0313  568 VAL C C   
14256 O O   . VAL C 568 ? 0.8626 0.6285 0.8295 0.1708  0.1370  0.0321  568 VAL C O   
14257 C CB  . VAL C 568 ? 0.7710 0.5158 0.7263 0.1756  0.1434  0.0272  568 VAL C CB  
14258 C CG1 . VAL C 568 ? 0.7035 0.4434 0.6624 0.1752  0.1392  0.0287  568 VAL C CG1 
14259 C CG2 . VAL C 568 ? 0.7481 0.4876 0.7012 0.1809  0.1498  0.0245  568 VAL C CG2 
14260 N N   . VAL C 569 ? 0.8480 0.6153 0.8053 0.1682  0.1371  0.0344  569 VAL C N   
14261 C CA  . VAL C 569 ? 0.7447 0.5214 0.7030 0.1658  0.1336  0.0400  569 VAL C CA  
14262 C C   . VAL C 569 ? 0.7502 0.5371 0.7079 0.1681  0.1344  0.0381  569 VAL C C   
14263 O O   . VAL C 569 ? 0.8268 0.6201 0.7855 0.1684  0.1316  0.0412  569 VAL C O   
14264 C CB  . VAL C 569 ? 0.7517 0.5339 0.7082 0.1625  0.1322  0.0450  569 VAL C CB  
14265 C CG1 . VAL C 569 ? 0.8698 0.6629 0.8285 0.1603  0.1299  0.0533  569 VAL C CG1 
14266 C CG2 . VAL C 569 ? 0.8024 0.5736 0.7597 0.1598  0.1293  0.0449  569 VAL C CG2 
14267 N N   . THR C 570 ? 0.7760 0.5638 0.7316 0.1704  0.1377  0.0327  570 THR C N   
14268 C CA  . THR C 570 ? 0.7917 0.5865 0.7465 0.1730  0.1373  0.0283  570 THR C CA  
14269 C C   . THR C 570 ? 0.8505 0.6432 0.8125 0.1731  0.1350  0.0247  570 THR C C   
14270 O O   . THR C 570 ? 0.8017 0.6019 0.7631 0.1747  0.1315  0.0221  570 THR C O   
14271 C CB  . THR C 570 ? 0.7704 0.5627 0.7228 0.1754  0.1410  0.0232  570 THR C CB  
14272 O OG1 . THR C 570 ? 0.9038 0.6989 0.8513 0.1756  0.1429  0.0271  570 THR C OG1 
14273 C CG2 . THR C 570 ? 0.5921 0.3903 0.5419 0.1787  0.1395  0.0173  570 THR C CG2 
14274 N N   . SER C 571 ? 0.7711 0.5549 0.7396 0.1722  0.1369  0.0245  571 SER C N   
14275 C CA  . SER C 571 ? 0.7333 0.5174 0.7115 0.1725  0.1352  0.0222  571 SER C CA  
14276 C C   . SER C 571 ? 0.8638 0.6528 0.8426 0.1729  0.1302  0.0270  571 SER C C   
14277 O O   . SER C 571 ? 0.9392 0.7321 0.9259 0.1739  0.1274  0.0255  571 SER C O   
14278 C CB  . SER C 571 ? 0.8552 0.6307 0.8401 0.1730  0.1402  0.0218  571 SER C CB  
14279 O OG  . SER C 571 ? 0.7777 0.5492 0.7636 0.1730  0.1451  0.0188  571 SER C OG  
14280 N N   . GLY C 572 ? 0.8508 0.6403 0.8229 0.1721  0.1290  0.0333  572 GLY C N   
14281 C CA  . GLY C 572 ? 0.7568 0.5495 0.7295 0.1726  0.1248  0.0401  572 GLY C CA  
14282 C C   . GLY C 572 ? 0.8348 0.6158 0.8101 0.1717  0.1249  0.0443  572 GLY C C   
14283 O O   . GLY C 572 ? 1.0878 0.8682 1.0654 0.1726  0.1216  0.0502  572 GLY C O   
14284 N N   . ILE C 573 ? 0.7973 0.5680 0.7715 0.1709  0.1282  0.0413  573 ILE C N   
14285 C CA  . ILE C 573 ? 0.7985 0.5559 0.7733 0.1711  0.1274  0.0428  573 ILE C CA  
14286 C C   . ILE C 573 ? 0.8927 0.6457 0.8630 0.1668  0.1256  0.0459  573 ILE C C   
14287 O O   . ILE C 573 ? 0.8940 0.6483 0.8600 0.1658  0.1279  0.0428  573 ILE C O   
14288 C CB  . ILE C 573 ? 0.6782 0.4279 0.6541 0.1748  0.1319  0.0365  573 ILE C CB  
14289 C CG1 . ILE C 573 ? 0.8165 0.5723 0.8014 0.1782  0.1335  0.0347  573 ILE C CG1 
14290 C CG2 . ILE C 573 ? 0.7748 0.5099 0.7480 0.1768  0.1308  0.0357  573 ILE C CG2 
14291 C CD1 . ILE C 573 ? 0.7682 0.5233 0.7564 0.1806  0.1399  0.0301  573 ILE C CD1 
14292 N N   . ASP C 574 ? 0.7581 0.5058 0.7309 0.1643  0.1213  0.0524  574 ASP C N   
14293 C CA  . ASP C 574 ? 0.7098 0.4538 0.6825 0.1587  0.1184  0.0559  574 ASP C CA  
14294 C C   . ASP C 574 ? 0.8454 0.5774 0.8138 0.1594  0.1183  0.0478  574 ASP C C   
14295 O O   . ASP C 574 ? 0.9320 0.6539 0.8985 0.1645  0.1196  0.0420  574 ASP C O   
14296 C CB  . ASP C 574 ? 0.7813 0.5174 0.7602 0.1557  0.1136  0.0642  574 ASP C CB  
14297 C CG  . ASP C 574 ? 0.9376 0.6862 0.9192 0.1559  0.1136  0.0743  574 ASP C CG  
14298 O OD1 . ASP C 574 ? 0.9735 0.7359 0.9547 0.1526  0.1146  0.0809  574 ASP C OD1 
14299 O OD2 . ASP C 574 ? 0.9319 0.6778 0.9154 0.1603  0.1127  0.0759  574 ASP C OD2 
14300 N N   . THR C 575 ? 0.8280 0.5627 0.7948 0.1553  0.1168  0.0477  575 THR C N   
14301 C CA  . THR C 575 ? 0.7732 0.4982 0.7340 0.1568  0.1157  0.0399  575 THR C CA  
14302 C C   . THR C 575 ? 0.7713 0.4911 0.7356 0.1503  0.1084  0.0413  575 THR C C   
14303 O O   . THR C 575 ? 0.8662 0.5977 0.8367 0.1442  0.1069  0.0484  575 THR C O   
14304 C CB  . THR C 575 ? 0.7961 0.5306 0.7506 0.1599  0.1211  0.0363  575 THR C CB  
14305 O OG1 . THR C 575 ? 0.8239 0.5620 0.7784 0.1646  0.1270  0.0350  575 THR C OG1 
14306 C CG2 . THR C 575 ? 0.8724 0.5987 0.8185 0.1633  0.1206  0.0290  575 THR C CG2 
14307 N N   . TRP C 576 ? 0.8889 0.5917 0.8496 0.1518  0.1036  0.0343  576 TRP C N   
14308 C CA  . TRP C 576 ? 0.9098 0.6051 0.8748 0.1452  0.0946  0.0332  576 TRP C CA  
14309 C C   . TRP C 576 ? 0.9081 0.6048 0.8632 0.1481  0.0932  0.0246  576 TRP C C   
14310 O O   . TRP C 576 ? 0.9780 0.6697 0.9211 0.1569  0.0974  0.0171  576 TRP C O   
14311 C CB  . TRP C 576 ? 0.7818 0.4546 0.7487 0.1457  0.0882  0.0294  576 TRP C CB  
14312 C CG  . TRP C 576 ? 0.8412 0.5112 0.8220 0.1389  0.0852  0.0404  576 TRP C CG  
14313 C CD1 . TRP C 576 ? 0.8638 0.5270 0.8568 0.1292  0.0768  0.0453  576 TRP C CD1 
14314 C CD2 . TRP C 576 ? 0.9825 0.6569 0.9670 0.1414  0.0903  0.0487  576 TRP C CD2 
14315 N NE1 . TRP C 576 ? 0.8340 0.4966 0.8378 0.1258  0.0776  0.0576  576 TRP C NE1 
14316 C CE2 . TRP C 576 ? 0.9246 0.5942 0.9221 0.1339  0.0855  0.0595  576 TRP C CE2 
14317 C CE3 . TRP C 576 ? 0.8620 0.5443 0.8411 0.1492  0.0979  0.0484  576 TRP C CE3 
14318 C CZ2 . TRP C 576 ? 0.8824 0.5556 0.8850 0.1353  0.0885  0.0703  576 TRP C CZ2 
14319 C CZ3 . TRP C 576 ? 0.8561 0.5423 0.8410 0.1500  0.0995  0.0575  576 TRP C CZ3 
14320 C CH2 . TRP C 576 ? 0.9499 0.6319 0.9452 0.1438  0.0951  0.0685  576 TRP C CH2 
14321 N N   . LEU C 577 ? 0.8897 0.5949 0.8504 0.1411  0.0877  0.0267  577 LEU C N   
14322 C CA  . LEU C 577 ? 0.7840 0.4927 0.7359 0.1439  0.0850  0.0195  577 LEU C CA  
14323 C C   . LEU C 577 ? 0.9750 0.6717 0.9299 0.1386  0.0720  0.0130  577 LEU C C   
14324 O O   . LEU C 577 ? 1.0058 0.7044 0.9767 0.1280  0.0653  0.0192  577 LEU C O   
14325 C CB  . LEU C 577 ? 0.7622 0.4934 0.7183 0.1415  0.0887  0.0264  577 LEU C CB  
14326 C CG  . LEU C 577 ? 0.8147 0.5570 0.7682 0.1463  0.1000  0.0314  577 LEU C CG  
14327 C CD1 . LEU C 577 ? 0.6314 0.3942 0.5889 0.1449  0.1026  0.0372  577 LEU C CD1 
14328 C CD2 . LEU C 577 ? 0.6417 0.3768 0.5815 0.1564  0.1067  0.0245  577 LEU C CD2 
14329 N N   . GLY C 578 ? 0.8520 0.5366 0.7919 0.1463  0.0685  0.0008  578 GLY C N   
14330 C CA  . GLY C 578 ? 0.8963 0.5675 0.8354 0.1432  0.0547  -0.0090 578 GLY C CA  
14331 C C   . GLY C 578 ? 0.9265 0.6128 0.8688 0.1385  0.0476  -0.0096 578 GLY C C   
14332 O O   . GLY C 578 ? 1.0055 0.6864 0.9568 0.1305  0.0342  -0.0139 578 GLY C O   
14333 N N   . VAL C 579 ? 0.8167 0.5219 0.7528 0.1436  0.0559  -0.0054 579 VAL C N   
14334 C CA  . VAL C 579 ? 0.9751 0.6985 0.9142 0.1411  0.0510  -0.0043 579 VAL C CA  
14335 C C   . VAL C 579 ? 0.9516 0.6956 0.9074 0.1344  0.0579  0.0101  579 VAL C C   
14336 O O   . VAL C 579 ? 0.9621 0.7098 0.9148 0.1387  0.0698  0.0159  579 VAL C O   
14337 C CB  . VAL C 579 ? 0.8048 0.5330 0.7225 0.1543  0.0559  -0.0099 579 VAL C CB  
14338 C CG1 . VAL C 579 ? 0.8354 0.5844 0.7569 0.1529  0.0516  -0.0071 579 VAL C CG1 
14339 C CG2 . VAL C 579 ? 0.8711 0.5806 0.7699 0.1629  0.0500  -0.0239 579 VAL C CG2 
14340 N N   . ALA C 580 ? 0.9166 0.6743 0.8904 0.1240  0.0503  0.0158  580 ALA C N   
14341 C CA  . ALA C 580 ? 0.8499 0.6291 0.8390 0.1189  0.0572  0.0298  580 ALA C CA  
14342 C C   . ALA C 580 ? 0.8143 0.6122 0.7950 0.1276  0.0655  0.0322  580 ALA C C   
14343 O O   . ALA C 580 ? 0.9683 0.7740 0.9450 0.1304  0.0599  0.0277  580 ALA C O   
14344 C CB  . ALA C 580 ? 1.0177 0.8080 1.0308 0.1055  0.0471  0.0363  580 ALA C CB  
14345 N N   . PRO C 581 ? 0.8890 0.6941 0.8671 0.1322  0.0779  0.0389  581 PRO C N   
14346 C CA  . PRO C 581 ? 0.8320 0.6526 0.8032 0.1406  0.0853  0.0410  581 PRO C CA  
14347 C C   . PRO C 581 ? 0.8949 0.7408 0.8821 0.1359  0.0826  0.0492  581 PRO C C   
14348 O O   . PRO C 581 ? 0.8705 0.7234 0.8757 0.1253  0.0772  0.0557  581 PRO C O   
14349 C CB  . PRO C 581 ? 0.7336 0.5522 0.6997 0.1455  0.0974  0.0444  581 PRO C CB  
14350 C CG  . PRO C 581 ? 0.8152 0.6286 0.7915 0.1376  0.0962  0.0492  581 PRO C CG  
14351 C CD  . PRO C 581 ? 0.9643 0.7641 0.9456 0.1305  0.0849  0.0446  581 PRO C CD  
14352 N N   . PRO C 582 ? 0.8685 0.7291 0.8509 0.1438  0.0864  0.0503  582 PRO C N   
14353 C CA  . PRO C 582 ? 0.8468 0.7340 0.8456 0.1405  0.0842  0.0587  582 PRO C CA  
14354 C C   . PRO C 582 ? 0.9210 0.8234 0.9296 0.1396  0.0937  0.0696  582 PRO C C   
14355 O O   . PRO C 582 ? 0.8426 0.7585 0.8476 0.1482  0.1018  0.0729  582 PRO C O   
14356 C CB  . PRO C 582 ? 0.8041 0.6989 0.7918 0.1516  0.0854  0.0555  582 PRO C CB  
14357 C CG  . PRO C 582 ? 0.7449 0.6210 0.7124 0.1615  0.0944  0.0501  582 PRO C CG  
14358 C CD  . PRO C 582 ? 0.7130 0.5672 0.6765 0.1564  0.0932  0.0452  582 PRO C CD  
14359 N N   . VAL C 583 ? 0.8340 0.7335 0.8538 0.1302  0.0927  0.0752  583 VAL C N   
14360 C CA  . VAL C 583 ? 0.6044 0.5185 0.6318 0.1297  0.1015  0.0862  583 VAL C CA  
14361 C C   . VAL C 583 ? 0.7104 0.6420 0.7623 0.1179  0.0974  0.0987  583 VAL C C   
14362 O O   . VAL C 583 ? 0.8497 0.7999 0.9089 0.1187  0.1051  0.1099  583 VAL C O   
14363 C CB  . VAL C 583 ? 0.6019 0.4983 0.6175 0.1324  0.1078  0.0841  583 VAL C CB  
14364 C CG1 . VAL C 583 ? 0.7956 0.6794 0.7911 0.1438  0.1136  0.0743  583 VAL C CG1 
14365 C CG2 . VAL C 583 ? 0.7141 0.5897 0.7332 0.1236  0.1005  0.0817  583 VAL C CG2 
14366 N N   . THR C 584 ? 0.7251 0.6512 0.7901 0.1072  0.0852  0.0969  584 THR C N   
14367 C CA  . THR C 584 ? 0.6403 0.5805 0.7326 0.0937  0.0796  0.1089  584 THR C CA  
14368 C C   . THR C 584 ? 0.7959 0.7720 0.9047 0.0943  0.0867  0.1237  584 THR C C   
14369 O O   . THR C 584 ? 0.7994 0.7879 0.9246 0.0874  0.0906  0.1380  584 THR C O   
14370 C CB  . THR C 584 ? 0.8215 0.7541 0.9247 0.0843  0.0636  0.1014  584 THR C CB  
14371 O OG1 . THR C 584 ? 0.9502 0.8508 1.0344 0.0870  0.0583  0.0866  584 THR C OG1 
14372 C CG2 . THR C 584 ? 0.9534 0.8930 1.0872 0.0677  0.0558  0.1125  584 THR C CG2 
14373 N N   . GLY C 585 ? 0.7678 0.7609 0.8721 0.1033  0.0888  0.1210  585 GLY C N   
14374 C CA  . GLY C 585 ? 0.6044 0.6330 0.7237 0.1061  0.0956  0.1340  585 GLY C CA  
14375 C C   . GLY C 585 ? 0.6708 0.7106 0.7809 0.1160  0.1109  0.1418  585 GLY C C   
14376 O O   . GLY C 585 ? 0.7119 0.7823 0.8353 0.1184  0.1176  0.1544  585 GLY C O   
14377 N N   . GLY C 586 ? 0.6892 0.7056 0.7768 0.1224  0.1159  0.1341  586 GLY C N   
14378 C CA  . GLY C 586 ? 0.7360 0.7594 0.8114 0.1325  0.1286  0.1384  586 GLY C CA  
14379 C C   . GLY C 586 ? 0.6532 0.6698 0.7314 0.1260  0.1308  0.1464  586 GLY C C   
14380 O O   . GLY C 586 ? 0.6957 0.6866 0.7592 0.1267  0.1297  0.1382  586 GLY C O   
14381 N N   . PRO C 587 ? 0.6636 0.7038 0.7611 0.1201  0.1344  0.1638  587 PRO C N   
14382 C CA  . PRO C 587 ? 0.6042 0.6379 0.7043 0.1145  0.1368  0.1735  587 PRO C CA  
14383 C C   . PRO C 587 ? 0.7229 0.7462 0.7975 0.1262  0.1444  0.1681  587 PRO C C   
14384 O O   . PRO C 587 ? 0.8157 0.8185 0.8847 0.1227  0.1420  0.1667  587 PRO C O   
14385 C CB  . PRO C 587 ? 0.6080 0.6756 0.7317 0.1097  0.1424  0.1948  587 PRO C CB  
14386 C CG  . PRO C 587 ? 0.6052 0.6916 0.7463 0.1066  0.1379  0.1952  587 PRO C CG  
14387 C CD  . PRO C 587 ? 0.6585 0.7336 0.7780 0.1183  0.1367  0.1768  587 PRO C CD  
14388 N N   . GLU C 588 ? 0.7259 0.7632 0.7857 0.1406  0.1530  0.1646  588 GLU C N   
14389 C CA  . GLU C 588 ? 0.7030 0.7312 0.7390 0.1520  0.1587  0.1576  588 GLU C CA  
14390 C C   . GLU C 588 ? 0.6744 0.6694 0.6960 0.1520  0.1525  0.1401  588 GLU C C   
14391 O O   . GLU C 588 ? 0.7105 0.6904 0.7216 0.1530  0.1523  0.1368  588 GLU C O   
14392 C CB  . GLU C 588 ? 0.8124 0.8604 0.8363 0.1676  0.1677  0.1552  588 GLU C CB  
14393 C CG  . GLU C 588 ? 0.9136 0.9571 0.9147 0.1795  0.1732  0.1493  588 GLU C CG  
14394 C CD  . GLU C 588 ? 1.0051 1.0644 0.9925 0.1960  0.1810  0.1443  588 GLU C CD  
14395 O OE1 . GLU C 588 ? 0.9572 1.0381 0.9551 0.1990  0.1846  0.1503  588 GLU C OE1 
14396 O OE2 . GLU C 588 ? 0.9279 0.9777 0.8947 0.2063  0.1830  0.1339  588 GLU C OE2 
14397 N N   . VAL C 589 ? 0.7269 0.7123 0.7488 0.1514  0.1475  0.1300  589 VAL C N   
14398 C CA  . VAL C 589 ? 0.6825 0.6388 0.6916 0.1521  0.1429  0.1150  589 VAL C CA  
14399 C C   . VAL C 589 ? 0.7722 0.7090 0.7872 0.1413  0.1358  0.1156  589 VAL C C   
14400 O O   . VAL C 589 ? 0.8159 0.7324 0.8194 0.1433  0.1351  0.1075  589 VAL C O   
14401 C CB  . VAL C 589 ? 0.6110 0.5636 0.6184 0.1550  0.1398  0.1062  589 VAL C CB  
14402 C CG1 . VAL C 589 ? 0.5875 0.5116 0.5820 0.1561  0.1363  0.0927  589 VAL C CG1 
14403 C CG2 . VAL C 589 ? 0.6388 0.6084 0.6398 0.1673  0.1471  0.1054  589 VAL C CG2 
14404 N N   . VAL C 590 ? 0.8172 0.7599 0.8513 0.1300  0.1306  0.1252  590 VAL C N   
14405 C CA  . VAL C 590 ? 0.7355 0.6579 0.7763 0.1200  0.1234  0.1259  590 VAL C CA  
14406 C C   . VAL C 590 ? 0.7838 0.7036 0.8196 0.1218  0.1281  0.1328  590 VAL C C   
14407 O O   . VAL C 590 ? 0.8012 0.6989 0.8302 0.1212  0.1250  0.1268  590 VAL C O   
14408 C CB  . VAL C 590 ? 0.6115 0.5410 0.6765 0.1068  0.1160  0.1353  590 VAL C CB  
14409 C CG1 . VAL C 590 ? 0.6815 0.5895 0.7545 0.0971  0.1094  0.1378  590 VAL C CG1 
14410 C CG2 . VAL C 590 ? 0.6109 0.5398 0.6791 0.1052  0.1087  0.1260  590 VAL C CG2 
14411 N N   . ASP C 591 ? 0.7239 0.6676 0.7622 0.1253  0.1357  0.1454  591 ASP C N   
14412 C CA  . ASP C 591 ? 0.6679 0.6126 0.6995 0.1287  0.1402  0.1529  591 ASP C CA  
14413 C C   . ASP C 591 ? 0.7840 0.7154 0.7934 0.1391  0.1419  0.1387  591 ASP C C   
14414 O O   . ASP C 591 ? 0.8438 0.7615 0.8479 0.1392  0.1402  0.1380  591 ASP C O   
14415 C CB  . ASP C 591 ? 0.6165 0.5925 0.6519 0.1330  0.1490  0.1686  591 ASP C CB  
14416 C CG  . ASP C 591 ? 0.8288 0.8079 0.8577 0.1364  0.1531  0.1788  591 ASP C CG  
14417 O OD1 . ASP C 591 ? 0.8852 0.8490 0.9222 0.1283  0.1485  0.1848  591 ASP C OD1 
14418 O OD2 . ASP C 591 ? 0.9334 0.9297 0.9481 0.1480  0.1606  0.1805  591 ASP C OD2 
14419 N N   . ILE C 592 ? 0.7890 0.7241 0.7871 0.1478  0.1449  0.1278  592 ILE C N   
14420 C CA  . ILE C 592 ? 0.7542 0.6767 0.7343 0.1566  0.1460  0.1142  592 ILE C CA  
14421 C C   . ILE C 592 ? 0.7651 0.6605 0.7446 0.1518  0.1397  0.1047  592 ILE C C   
14422 O O   . ILE C 592 ? 0.8232 0.7079 0.7976 0.1528  0.1384  0.1026  592 ILE C O   
14423 C CB  . ILE C 592 ? 0.5977 0.5273 0.5681 0.1663  0.1502  0.1050  592 ILE C CB  
14424 C CG1 . ILE C 592 ? 0.6505 0.6068 0.6176 0.1745  0.1574  0.1130  592 ILE C CG1 
14425 C CG2 . ILE C 592 ? 0.7266 0.6383 0.6829 0.1726  0.1496  0.0900  592 ILE C CG2 
14426 C CD1 . ILE C 592 ? 0.7360 0.7037 0.7010 0.1821  0.1612  0.1087  592 ILE C CD1 
14427 N N   . LEU C 593 ? 0.8045 0.6903 0.7888 0.1477  0.1358  0.0990  593 LEU C N   
14428 C CA  . LEU C 593 ? 0.8194 0.6810 0.8012 0.1452  0.1308  0.0894  593 LEU C CA  
14429 C C   . LEU C 593 ? 0.7734 0.6224 0.7617 0.1387  0.1263  0.0942  593 LEU C C   
14430 O O   . LEU C 593 ? 0.8586 0.6921 0.8409 0.1410  0.1253  0.0878  593 LEU C O   
14431 C CB  . LEU C 593 ? 0.7251 0.5814 0.7098 0.1426  0.1269  0.0838  593 LEU C CB  
14432 C CG  . LEU C 593 ? 0.7216 0.5843 0.6984 0.1503  0.1309  0.0774  593 LEU C CG  
14433 C CD1 . LEU C 593 ? 0.6233 0.4849 0.6042 0.1477  0.1260  0.0747  593 LEU C CD1 
14434 C CD2 . LEU C 593 ? 0.7591 0.6079 0.7233 0.1575  0.1342  0.0671  593 LEU C CD2 
14435 N N   . THR C 594 ? 0.8163 0.6717 0.8185 0.1306  0.1235  0.1058  594 THR C N   
14436 C CA  . THR C 594 ? 0.9071 0.7481 0.9174 0.1241  0.1187  0.1113  594 THR C CA  
14437 C C   . THR C 594 ? 0.8119 0.6628 0.8249 0.1244  0.1222  0.1253  594 THR C C   
14438 O O   . THR C 594 ? 0.9048 0.7466 0.9286 0.1177  0.1184  0.1338  594 THR C O   
14439 C CB  . THR C 594 ? 0.8323 0.6683 0.8584 0.1134  0.1114  0.1145  594 THR C CB  
14440 O OG1 . THR C 594 ? 0.7146 0.5735 0.7546 0.1083  0.1137  0.1291  594 THR C OG1 
14441 C CG2 . THR C 594 ? 0.6235 0.4521 0.6453 0.1141  0.1071  0.1012  594 THR C CG2 
14442 N N   . ASN C 595 ? 0.8520 0.7203 0.8549 0.1326  0.1289  0.1276  595 ASN C N   
14443 C CA  . ASN C 595 ? 0.7667 0.6461 0.7693 0.1348  0.1322  0.1411  595 ASN C CA  
14444 C C   . ASN C 595 ? 0.8788 0.7711 0.8640 0.1466  0.1375  0.1368  595 ASN C C   
14445 O O   . ASN C 595 ? 0.8568 0.7406 0.8337 0.1511  0.1359  0.1324  595 ASN C O   
14446 C CB  . ASN C 595 ? 0.7256 0.6235 0.7438 0.1282  0.1347  0.1596  595 ASN C CB  
14447 C CG  . ASN C 595 ? 0.8379 0.7501 0.8544 0.1318  0.1396  0.1758  595 ASN C CG  
14448 O OD1 . ASN C 595 ? 0.9297 0.8305 0.9410 0.1341  0.1377  0.1772  595 ASN C OD1 
14449 N ND2 . ASN C 595 ? 1.0291 0.9682 1.0493 0.1335  0.1465  0.1891  595 ASN C ND2 
14450 N N   . LYS C 596 ? 0.8846 0.7976 0.8647 0.1522  0.1430  0.1376  596 LYS C N   
14451 C CA  . LYS C 596 ? 0.7525 0.6772 0.7154 0.1640  0.1470  0.1322  596 LYS C CA  
14452 C C   . LYS C 596 ? 0.8294 0.7366 0.7815 0.1685  0.1435  0.1144  596 LYS C C   
14453 O O   . LYS C 596 ? 0.8961 0.8059 0.8370 0.1755  0.1431  0.1108  596 LYS C O   
14454 C CB  . LYS C 596 ? 0.6216 0.5674 0.5808 0.1702  0.1532  0.1326  596 LYS C CB  
14455 C CG  . LYS C 596 ? 0.6814 0.6463 0.6248 0.1824  0.1584  0.1347  596 LYS C CG  
14456 C CD  . LYS C 596 ? 0.8251 0.8129 0.7665 0.1893  0.1654  0.1376  596 LYS C CD  
14457 C CE  . LYS C 596 ? 0.9543 0.9647 0.8802 0.2021  0.1714  0.1430  596 LYS C CE  
14458 N NZ  . LYS C 596 ? 0.8259 0.8333 0.7320 0.2147  0.1711  0.1245  596 LYS C NZ  
14459 N N   . MET C 597 ? 0.7671 0.6575 0.7233 0.1644  0.1407  0.1040  597 MET C N   
14460 C CA  . MET C 597 ? 0.8637 0.7380 0.8132 0.1675  0.1384  0.0889  597 MET C CA  
14461 C C   . MET C 597 ? 0.9042 0.7706 0.8519 0.1684  0.1348  0.0884  597 MET C C   
14462 O O   . MET C 597 ? 0.8818 0.7454 0.8223 0.1737  0.1337  0.0785  597 MET C O   
14463 C CB  . MET C 597 ? 0.8475 0.7051 0.8035 0.1619  0.1361  0.0826  597 MET C CB  
14464 C CG  . MET C 597 ? 0.6824 0.5279 0.6326 0.1658  0.1362  0.0688  597 MET C CG  
14465 S SD  . MET C 597 ? 1.1497 0.9817 1.1042 0.1619  0.1354  0.0637  597 MET C SD  
14466 C CE  . MET C 597 ? 1.1915 1.0120 1.1400 0.1674  0.1375  0.0508  597 MET C CE  
14467 N N   . GLU C 598 ? 0.8565 0.7191 0.8121 0.1632  0.1326  0.0994  598 GLU C N   
14468 C CA  . GLU C 598 ? 0.7623 0.6182 0.7175 0.1646  0.1292  0.1013  598 GLU C CA  
14469 C C   . GLU C 598 ? 0.8983 0.7695 0.8418 0.1733  0.1298  0.1011  598 GLU C C   
14470 O O   . GLU C 598 ? 0.9261 0.7925 0.8662 0.1770  0.1262  0.0945  598 GLU C O   
14471 C CB  . GLU C 598 ? 0.8634 0.7159 0.8289 0.1586  0.1278  0.1165  598 GLU C CB  
14472 C CG  . GLU C 598 ? 0.9789 0.8224 0.9455 0.1604  0.1241  0.1201  598 GLU C CG  
14473 C CD  . GLU C 598 ? 1.2224 1.0597 1.2004 0.1544  0.1227  0.1357  598 GLU C CD  
14474 O OE1 . GLU C 598 ? 1.2978 1.1443 1.2824 0.1492  0.1252  0.1468  598 GLU C OE1 
14475 O OE2 . GLU C 598 ? 1.2597 1.0829 1.2413 0.1548  0.1190  0.1372  598 GLU C OE2 
14476 N N   . ASP C 599 ? 0.8878 0.7783 0.8247 0.1773  0.1340  0.1078  599 ASP C N   
14477 C CA  . ASP C 599 ? 0.6819 0.5883 0.6045 0.1873  0.1343  0.1067  599 ASP C CA  
14478 C C   . ASP C 599 ? 0.7428 0.6462 0.6563 0.1930  0.1324  0.0879  599 ASP C C   
14479 O O   . ASP C 599 ? 0.8627 0.7739 0.7649 0.2007  0.1295  0.0824  599 ASP C O   
14480 C CB  . ASP C 599 ? 0.7974 0.7265 0.7150 0.1913  0.1406  0.1192  599 ASP C CB  
14481 C CG  . ASP C 599 ? 1.0040 0.9390 0.9317 0.1860  0.1428  0.1403  599 ASP C CG  
14482 O OD1 . ASP C 599 ? 1.0604 0.9838 0.9939 0.1825  0.1388  0.1454  599 ASP C OD1 
14483 O OD2 . ASP C 599 ? 1.0506 1.0021 0.9818 0.1854  0.1489  0.1523  599 ASP C OD2 
14484 N N   . TRP C 600 ? 0.7340 0.6260 0.6524 0.1895  0.1334  0.0782  600 TRP C N   
14485 C CA  . TRP C 600 ? 0.8316 0.7183 0.7441 0.1939  0.1320  0.0617  600 TRP C CA  
14486 C C   . TRP C 600 ? 0.8887 0.7585 0.8086 0.1902  0.1274  0.0523  600 TRP C C   
14487 O O   . TRP C 600 ? 1.0023 0.8713 0.9184 0.1941  0.1234  0.0418  600 TRP C O   
14488 C CB  . TRP C 600 ? 0.8758 0.7603 0.7895 0.1934  0.1365  0.0576  600 TRP C CB  
14489 C CG  . TRP C 600 ? 0.8390 0.7415 0.7490 0.1967  0.1420  0.0669  600 TRP C CG  
14490 C CD1 . TRP C 600 ? 0.9454 0.8672 0.8481 0.2021  0.1443  0.0769  600 TRP C CD1 
14491 C CD2 . TRP C 600 ? 0.6469 0.5517 0.5610 0.1956  0.1463  0.0680  600 TRP C CD2 
14492 N NE1 . TRP C 600 ? 0.8115 0.7482 0.7151 0.2039  0.1504  0.0847  600 TRP C NE1 
14493 C CE2 . TRP C 600 ? 0.6341 0.5609 0.5452 0.1999  0.1513  0.0791  600 TRP C CE2 
14494 C CE3 . TRP C 600 ? 0.6819 0.5738 0.6020 0.1922  0.1467  0.0616  600 TRP C CE3 
14495 C CZ2 . TRP C 600 ? 0.8390 0.7758 0.7547 0.2004  0.1560  0.0834  600 TRP C CZ2 
14496 C CZ3 . TRP C 600 ? 0.6148 0.5157 0.5377 0.1931  0.1507  0.0655  600 TRP C CZ3 
14497 C CH2 . TRP C 600 ? 0.7665 0.6899 0.6882 0.1969  0.1551  0.0760  600 TRP C CH2 
14498 N N   . VAL C 601 ? 0.7791 0.6357 0.7099 0.1831  0.1277  0.0557  601 VAL C N   
14499 C CA  . VAL C 601 ? 0.7419 0.5840 0.6804 0.1806  0.1251  0.0479  601 VAL C CA  
14500 C C   . VAL C 601 ? 0.8896 0.7259 0.8352 0.1780  0.1222  0.0546  601 VAL C C   
14501 O O   . VAL C 601 ? 0.8942 0.7204 0.8469 0.1768  0.1209  0.0492  601 VAL C O   
14502 C CB  . VAL C 601 ? 0.8078 0.6376 0.7509 0.1772  0.1286  0.0426  601 VAL C CB  
14503 C CG1 . VAL C 601 ? 0.7829 0.6170 0.7196 0.1809  0.1315  0.0363  601 VAL C CG1 
14504 C CG2 . VAL C 601 ? 0.7485 0.5731 0.6960 0.1721  0.1302  0.0509  601 VAL C CG2 
14505 N N   . GLY C 602 ? 0.8448 0.6876 0.7893 0.1776  0.1217  0.0668  602 GLY C N   
14506 C CA  . GLY C 602 ? 0.7830 0.6187 0.7343 0.1761  0.1189  0.0739  602 GLY C CA  
14507 C C   . GLY C 602 ? 0.8160 0.6348 0.7758 0.1703  0.1197  0.0758  602 GLY C C   
14508 O O   . GLY C 602 ? 0.9432 0.7527 0.9088 0.1698  0.1172  0.0798  602 GLY C O   
14509 N N   . ALA C 603 ? 0.8564 0.6713 0.8165 0.1668  0.1225  0.0724  603 ALA C N   
14510 C CA  . ALA C 603 ? 0.7613 0.5610 0.7272 0.1620  0.1222  0.0722  603 ALA C CA  
14511 C C   . ALA C 603 ? 0.8654 0.6701 0.8313 0.1579  0.1240  0.0755  603 ALA C C   
14512 O O   . ALA C 603 ? 0.9444 0.7632 0.9053 0.1600  0.1268  0.0757  603 ALA C O   
14513 C CB  . ALA C 603 ? 0.7016 0.4902 0.6681 0.1638  0.1234  0.0609  603 ALA C CB  
14514 N N   . LYS C 604 ? 0.7396 0.5334 0.7112 0.1525  0.1219  0.0774  604 LYS C N   
14515 C CA  . LYS C 604 ? 0.8321 0.6321 0.8065 0.1479  0.1222  0.0808  604 LYS C CA  
14516 C C   . LYS C 604 ? 0.8855 0.6702 0.8623 0.1445  0.1190  0.0745  604 LYS C C   
14517 O O   . LYS C 604 ? 0.8294 0.5982 0.8050 0.1462  0.1172  0.0683  604 LYS C O   
14518 C CB  . LYS C 604 ? 0.7527 0.5627 0.7347 0.1431  0.1214  0.0957  604 LYS C CB  
14519 C CG  . LYS C 604 ? 0.9134 0.7104 0.9023 0.1402  0.1174  0.1026  604 LYS C CG  
14520 C CD  . LYS C 604 ? 0.9320 0.7381 0.9308 0.1346  0.1171  0.1196  604 LYS C CD  
14521 C CE  . LYS C 604 ? 1.0904 0.8863 1.1026 0.1248  0.1123  0.1230  604 LYS C CE  
14522 N NZ  . LYS C 604 ? 1.0166 0.8200 1.0421 0.1183  0.1122  0.1414  604 LYS C NZ  
14523 N N   . PHE C 605 ? 0.7682 0.5591 0.7478 0.1407  0.1182  0.0756  605 PHE C N   
14524 C CA  . PHE C 605 ? 0.7307 0.5093 0.7114 0.1378  0.1137  0.0692  605 PHE C CA  
14525 C C   . PHE C 605 ? 0.8438 0.6151 0.8362 0.1295  0.1070  0.0761  605 PHE C C   
14526 O O   . PHE C 605 ? 0.9648 0.7465 0.9662 0.1249  0.1073  0.0882  605 PHE C O   
14527 C CB  . PHE C 605 ? 0.7376 0.5278 0.7162 0.1383  0.1151  0.0668  605 PHE C CB  
14528 C CG  . PHE C 605 ? 0.7345 0.5231 0.7020 0.1460  0.1199  0.0576  605 PHE C CG  
14529 C CD1 . PHE C 605 ? 0.6726 0.4466 0.6338 0.1490  0.1187  0.0488  605 PHE C CD1 
14530 C CD2 . PHE C 605 ? 0.6914 0.4930 0.6549 0.1508  0.1257  0.0580  605 PHE C CD2 
14531 C CE1 . PHE C 605 ? 0.7703 0.5434 0.7231 0.1557  0.1241  0.0427  605 PHE C CE1 
14532 C CE2 . PHE C 605 ? 0.6650 0.4631 0.6206 0.1570  0.1299  0.0505  605 PHE C CE2 
14533 C CZ  . PHE C 605 ? 0.7820 0.5662 0.7331 0.1591  0.1294  0.0439  605 PHE C CZ  
14534 N N   . PHE C 606 ? 0.7837 0.5368 0.7761 0.1278  0.1009  0.0685  606 PHE C N   
14535 C CA  . PHE C 606 ? 0.8175 0.5592 0.8219 0.1194  0.0927  0.0725  606 PHE C CA  
14536 C C   . PHE C 606 ? 0.8377 0.5719 0.8402 0.1176  0.0859  0.0623  606 PHE C C   
14537 O O   . PHE C 606 ? 0.8350 0.5570 0.8249 0.1245  0.0858  0.0505  606 PHE C O   
14538 C CB  . PHE C 606 ? 0.9400 0.6607 0.9442 0.1215  0.0904  0.0712  606 PHE C CB  
14539 C CG  . PHE C 606 ? 0.9408 0.6670 0.9477 0.1235  0.0949  0.0819  606 PHE C CG  
14540 C CD1 . PHE C 606 ? 1.0225 0.7554 1.0195 0.1319  0.1014  0.0790  606 PHE C CD1 
14541 C CD2 . PHE C 606 ? 0.7448 0.4678 0.7645 0.1171  0.0919  0.0946  606 PHE C CD2 
14542 C CE1 . PHE C 606 ? 0.9084 0.6470 0.9069 0.1345  0.1041  0.0877  606 PHE C CE1 
14543 C CE2 . PHE C 606 ? 0.7402 0.4686 0.7605 0.1203  0.0958  0.1049  606 PHE C CE2 
14544 C CZ  . PHE C 606 ? 0.8587 0.5953 0.8675 0.1294  0.1014  0.1008  606 PHE C CZ  
14545 N N   . ILE C 607 ? 0.9138 0.6568 0.9286 0.1088  0.0803  0.0670  607 ILE C N   
14546 C CA  . ILE C 607 ? 0.8151 0.5527 0.8284 0.1070  0.0719  0.0567  607 ILE C CA  
14547 C C   . ILE C 607 ? 0.9981 0.7146 1.0218 0.0993  0.0604  0.0541  607 ILE C C   
14548 O O   . ILE C 607 ? 1.1123 0.8318 1.1550 0.0888  0.0567  0.0654  607 ILE C O   
14549 C CB  . ILE C 607 ? 0.8200 0.5822 0.8411 0.1030  0.0718  0.0619  607 ILE C CB  
14550 C CG1 . ILE C 607 ? 0.7167 0.4957 0.7256 0.1125  0.0829  0.0623  607 ILE C CG1 
14551 C CG2 . ILE C 607 ? 0.8881 0.6455 0.9089 0.1007  0.0609  0.0514  607 ILE C CG2 
14552 C CD1 . ILE C 607 ? 0.6377 0.4435 0.6559 0.1101  0.0861  0.0717  607 ILE C CD1 
14553 N N   . GLU C 608 ? 0.9377 0.6322 0.9490 0.1048  0.0550  0.0397  608 GLU C N   
14554 C CA  . GLU C 608 ? 0.9644 0.6348 0.9832 0.0991  0.0430  0.0341  608 GLU C CA  
14555 C C   . GLU C 608 ? 1.0734 0.7299 1.0763 0.1056  0.0353  0.0157  608 GLU C C   
14556 O O   . GLU C 608 ? 1.1282 0.7762 1.1117 0.1180  0.0407  0.0067  608 GLU C O   
14557 C CB  . GLU C 608 ? 0.7413 0.3931 0.7611 0.1017  0.0456  0.0376  608 GLU C CB  
14558 C CG  . GLU C 608 ? 0.8838 0.5083 0.9137 0.0955  0.0333  0.0332  608 GLU C CG  
14559 C CD  . GLU C 608 ? 1.0635 0.6920 1.1183 0.0794  0.0239  0.0423  608 GLU C CD  
14560 O OE1 . GLU C 608 ? 1.0355 0.6726 1.1073 0.0720  0.0280  0.0600  608 GLU C OE1 
14561 O OE2 . GLU C 608 ? 1.2509 0.8749 1.3087 0.0744  0.0123  0.0321  608 GLU C OE2 
14562 N N   . THR C 609 ? 1.0305 0.6859 1.0419 0.0976  0.0225  0.0105  609 THR C N   
14563 C CA  . THR C 609 ? 0.9335 0.5771 0.9289 0.1039  0.0131  -0.0077 609 THR C CA  
14564 C C   . THR C 609 ? 1.0646 0.6750 1.0548 0.1068  0.0045  -0.0197 609 THR C C   
14565 O O   . THR C 609 ? 1.3015 0.8993 1.2698 0.1187  0.0024  -0.0351 609 THR C O   
14566 C CB  . THR C 609 ? 0.8833 0.5408 0.8907 0.0944  0.0013  -0.0092 609 THR C CB  
14567 O OG1 . THR C 609 ? 1.0953 0.7445 1.1288 0.0790  -0.0098 -0.0038 609 THR C OG1 
14568 C CG2 . THR C 609 ? 0.8055 0.4958 0.8174 0.0936  0.0102  0.0024  609 THR C CG2 
14569 N N   . ASP C 610 ? 1.0518 0.6477 1.0612 0.0971  0.0002  -0.0123 610 ASP C N   
14570 C CA  . ASP C 610 ? 1.0627 0.6249 1.0692 0.1000  -0.0081 -0.0229 610 ASP C CA  
14571 C C   . ASP C 610 ? 1.1077 0.6619 1.0986 0.1141  0.0049  -0.0225 610 ASP C C   
14572 O O   . ASP C 610 ? 1.0679 0.6308 1.0683 0.1120  0.0146  -0.0073 610 ASP C O   
14573 C CB  . ASP C 610 ? 1.1358 0.6861 1.1713 0.0840  -0.0166 -0.0123 610 ASP C CB  
14574 C CG  . ASP C 610 ? 1.1155 0.6278 1.1512 0.0857  -0.0270 -0.0231 610 ASP C CG  
14575 O OD1 . ASP C 610 ? 1.2021 0.6989 1.2160 0.1012  -0.0226 -0.0341 610 ASP C OD1 
14576 O OD2 . ASP C 610 ? 1.1588 0.6568 1.2176 0.0717  -0.0393 -0.0202 610 ASP C OD2 
14577 N N   . PRO C 611 ? 1.1391 0.6789 1.1063 0.1292  0.0054  -0.0386 611 PRO C N   
14578 C CA  . PRO C 611 ? 1.0843 0.6202 1.0399 0.1423  0.0182  -0.0370 611 PRO C CA  
14579 C C   . PRO C 611 ? 1.0943 0.6088 1.0618 0.1410  0.0169  -0.0315 611 PRO C C   
14580 O O   . PRO C 611 ? 1.0186 0.5382 0.9855 0.1472  0.0281  -0.0230 611 PRO C O   
14581 C CB  . PRO C 611 ? 1.0332 0.5598 0.9621 0.1584  0.0181  -0.0551 611 PRO C CB  
14582 C CG  . PRO C 611 ? 1.1705 0.6828 1.0978 0.1538  0.0010  -0.0691 611 PRO C CG  
14583 C CD  . PRO C 611 ? 0.9893 0.5181 0.9388 0.1359  -0.0052 -0.0584 611 PRO C CD  
14584 N N   . HIS C 612 ? 1.1830 0.6737 1.1624 0.1328  0.0028  -0.0360 612 HIS C N   
14585 C CA  . HIS C 612 ? 1.1177 0.5852 1.1097 0.1314  0.0007  -0.0300 612 HIS C CA  
14586 C C   . HIS C 612 ? 1.1295 0.6141 1.1429 0.1203  0.0076  -0.0064 612 HIS C C   
14587 O O   . HIS C 612 ? 1.1731 0.6515 1.1906 0.1246  0.0137  0.0030  612 HIS C O   
14588 C CB  . HIS C 612 ? 1.2284 0.6638 1.2290 0.1247  -0.0172 -0.0413 612 HIS C CB  
14589 C CG  . HIS C 612 ? 1.3795 0.7973 1.3562 0.1375  -0.0248 -0.0659 612 HIS C CG  
14590 N ND1 . HIS C 612 ? 1.6163 1.0410 1.5856 0.1343  -0.0345 -0.0783 612 HIS C ND1 
14591 C CD2 . HIS C 612 ? 1.5265 0.9226 1.4841 0.1549  -0.0233 -0.0795 612 HIS C CD2 
14592 C CE1 . HIS C 612 ? 1.7084 1.1149 1.6531 0.1498  -0.0389 -0.0992 612 HIS C CE1 
14593 N NE2 . HIS C 612 ? 1.7775 1.1665 1.7144 0.1628  -0.0319 -0.1006 612 HIS C NE2 
14594 N N   . LYS C 613 ? 1.0687 0.5764 1.0949 0.1073  0.0069  0.0033  613 LYS C N   
14595 C CA  . LYS C 613 ? 1.0337 0.5611 1.0776 0.0984  0.0144  0.0258  613 LYS C CA  
14596 C C   . LYS C 613 ? 0.9799 0.5310 1.0099 0.1089  0.0299  0.0311  613 LYS C C   
14597 O O   . LYS C 613 ? 1.0662 0.6250 1.1027 0.1092  0.0374  0.0458  613 LYS C O   
14598 C CB  . LYS C 613 ? 0.9872 0.5338 1.0493 0.0826  0.0095  0.0344  613 LYS C CB  
14599 C CG  . LYS C 613 ? 0.9610 0.4859 1.0444 0.0689  -0.0062 0.0332  613 LYS C CG  
14600 C CD  . LYS C 613 ? 1.0528 0.5993 1.1551 0.0537  -0.0120 0.0396  613 LYS C CD  
14601 C CE  . LYS C 613 ? 1.2861 0.8548 1.4117 0.0427  -0.0044 0.0655  613 LYS C CE  
14602 N NZ  . LYS C 613 ? 1.1709 0.7183 1.3225 0.0306  -0.0118 0.0770  613 LYS C NZ  
14603 N N   . ALA C 614 ? 0.9465 0.5086 0.9578 0.1177  0.0342  0.0194  614 ALA C N   
14604 C CA  . ALA C 614 ? 0.9849 0.5677 0.9846 0.1268  0.0477  0.0229  614 ALA C CA  
14605 C C   . ALA C 614 ? 0.9532 0.5253 0.9480 0.1374  0.0537  0.0240  614 ALA C C   
14606 O O   . ALA C 614 ? 1.0130 0.6008 1.0107 0.1389  0.0623  0.0352  614 ALA C O   
14607 C CB  . ALA C 614 ? 0.7742 0.3655 0.7558 0.1345  0.0502  0.0100  614 ALA C CB  
14608 N N   . VAL C 615 ? 0.9694 0.5158 0.9567 0.1456  0.0489  0.0119  615 VAL C N   
14609 C CA  . VAL C 615 ? 1.0263 0.5637 1.0103 0.1569  0.0546  0.0130  615 VAL C CA  
14610 C C   . VAL C 615 ? 1.0632 0.5964 1.0644 0.1506  0.0536  0.0293  615 VAL C C   
14611 O O   . VAL C 615 ? 1.0373 0.5782 1.0389 0.1572  0.0609  0.0370  615 VAL C O   
14612 C CB  . VAL C 615 ? 0.8625 0.3744 0.8332 0.1697  0.0510  -0.0037 615 VAL C CB  
14613 C CG1 . VAL C 615 ? 1.0582 0.5779 1.0097 0.1778  0.0540  -0.0176 615 VAL C CG1 
14614 C CG2 . VAL C 615 ? 1.1148 0.5962 1.0929 0.1641  0.0371  -0.0095 615 VAL C CG2 
14615 N N   . GLU C 616 ? 1.0252 0.5479 1.0417 0.1377  0.0446  0.0356  616 GLU C N   
14616 C CA  . GLU C 616 ? 1.0049 0.5244 1.0387 0.1313  0.0443  0.0538  616 GLU C CA  
14617 C C   . GLU C 616 ? 0.9893 0.5414 1.0255 0.1291  0.0543  0.0694  616 GLU C C   
14618 O O   . GLU C 616 ? 1.0418 0.5982 1.0813 0.1332  0.0591  0.0813  616 GLU C O   
14619 C CB  . GLU C 616 ? 0.9237 0.4291 0.9761 0.1161  0.0333  0.0589  616 GLU C CB  
14620 C CG  . GLU C 616 ? 1.2883 0.7559 1.3422 0.1176  0.0215  0.0457  616 GLU C CG  
14621 C CD  . GLU C 616 ? 1.6231 1.0745 1.7002 0.1013  0.0099  0.0529  616 GLU C CD  
14622 O OE1 . GLU C 616 ? 1.3945 0.8678 1.4865 0.0880  0.0110  0.0669  616 GLU C OE1 
14623 O OE2 . GLU C 616 ? 1.6527 1.0695 1.7343 0.1019  -0.0003 0.0446  616 GLU C OE2 
14624 N N   . GLN C 617 ? 0.9553 0.5302 0.9889 0.1237  0.0569  0.0687  617 GLN C N   
14625 C CA  . GLN C 617 ? 0.9560 0.5616 0.9901 0.1223  0.0658  0.0809  617 GLN C CA  
14626 C C   . GLN C 617 ? 0.9305 0.5472 0.9511 0.1347  0.0744  0.0769  617 GLN C C   
14627 O O   . GLN C 617 ? 0.9944 0.6271 1.0166 0.1365  0.0799  0.0883  617 GLN C O   
14628 C CB  . GLN C 617 ? 0.8432 0.4678 0.8772 0.1151  0.0659  0.0789  617 GLN C CB  
14629 C CG  . GLN C 617 ? 0.8568 0.4779 0.9086 0.1011  0.0578  0.0858  617 GLN C CG  
14630 C CD  . GLN C 617 ? 0.9542 0.5884 1.0044 0.0963  0.0552  0.0781  617 GLN C CD  
14631 O OE1 . GLN C 617 ? 1.0191 0.6727 1.0575 0.1018  0.0621  0.0744  617 GLN C OE1 
14632 N NE2 . GLN C 617 ? 0.9732 0.5969 1.0364 0.0860  0.0445  0.0758  617 GLN C NE2 
14633 N N   . ILE C 618 ? 0.9932 0.6025 1.0010 0.1435  0.0754  0.0612  618 ILE C N   
14634 C CA  . ILE C 618 ? 0.9268 0.5470 0.9250 0.1544  0.0835  0.0575  618 ILE C CA  
14635 C C   . ILE C 618 ? 1.0155 0.6284 1.0185 0.1607  0.0842  0.0645  618 ILE C C   
14636 O O   . ILE C 618 ? 0.9812 0.6113 0.9846 0.1642  0.0894  0.0714  618 ILE C O   
14637 C CB  . ILE C 618 ? 0.8742 0.4873 0.8592 0.1628  0.0851  0.0410  618 ILE C CB  
14638 C CG1 . ILE C 618 ? 0.8138 0.4385 0.7927 0.1583  0.0855  0.0355  618 ILE C CG1 
14639 C CG2 . ILE C 618 ? 0.7227 0.3451 0.7026 0.1738  0.0933  0.0389  618 ILE C CG2 
14640 C CD1 . ILE C 618 ? 0.7331 0.3468 0.6991 0.1647  0.0840  0.0205  618 ILE C CD1 
14641 N N   . VAL C 619 ? 0.9628 0.5498 0.9696 0.1625  0.0781  0.0624  619 VAL C N   
14642 C CA  . VAL C 619 ? 0.9188 0.4962 0.9307 0.1698  0.0782  0.0694  619 VAL C CA  
14643 C C   . VAL C 619 ? 1.0595 0.6498 1.0815 0.1637  0.0789  0.0886  619 VAL C C   
14644 O O   . VAL C 619 ? 1.0720 0.6747 1.0939 0.1704  0.0829  0.0956  619 VAL C O   
14645 C CB  . VAL C 619 ? 0.9341 0.4778 0.9481 0.1730  0.0708  0.0627  619 VAL C CB  
14646 C CG1 . VAL C 619 ? 1.0694 0.6022 1.0907 0.1799  0.0704  0.0727  619 VAL C CG1 
14647 C CG2 . VAL C 619 ? 0.9135 0.4469 0.9140 0.1830  0.0714  0.0436  619 VAL C CG2 
14648 N N   . ASN C 620 ? 1.0210 0.6108 1.0521 0.1514  0.0752  0.0976  620 ASN C N   
14649 C CA  . ASN C 620 ? 0.9491 0.5530 0.9891 0.1462  0.0770  0.1176  620 ASN C CA  
14650 C C   . ASN C 620 ? 1.0237 0.6596 1.0558 0.1492  0.0844  0.1211  620 ASN C C   
14651 O O   . ASN C 620 ? 0.9715 0.6192 1.0043 0.1534  0.0870  0.1332  620 ASN C O   
14652 C CB  . ASN C 620 ? 0.8479 0.4495 0.9005 0.1320  0.0729  0.1265  620 ASN C CB  
14653 C CG  . ASN C 620 ? 1.1190 0.6886 1.1840 0.1271  0.0644  0.1280  620 ASN C CG  
14654 O OD1 . ASN C 620 ? 1.2117 0.7631 1.2792 0.1338  0.0628  0.1319  620 ASN C OD1 
14655 N ND2 . ASN C 620 ? 1.2339 0.7955 1.3079 0.1155  0.0581  0.1247  620 ASN C ND2 
14656 N N   . ARG C 621 ? 0.9510 0.6003 0.9754 0.1477  0.0872  0.1104  621 ARG C N   
14657 C CA  . ARG C 621 ? 0.8694 0.5462 0.8862 0.1505  0.0934  0.1111  621 ARG C CA  
14658 C C   . ARG C 621 ? 0.9625 0.6437 0.9737 0.1616  0.0959  0.1066  621 ARG C C   
14659 O O   . ARG C 621 ? 0.9433 0.6427 0.9526 0.1649  0.0983  0.1139  621 ARG C O   
14660 C CB  . ARG C 621 ? 0.8667 0.5519 0.8771 0.1473  0.0954  0.0996  621 ARG C CB  
14661 C CG  . ARG C 621 ? 0.7884 0.4977 0.7907 0.1510  0.1012  0.0974  621 ARG C CG  
14662 C CD  . ARG C 621 ? 0.8336 0.5631 0.8375 0.1482  0.1034  0.1112  621 ARG C CD  
14663 N NE  . ARG C 621 ? 0.8853 0.6352 0.8806 0.1509  0.1079  0.1062  621 ARG C NE  
14664 C CZ  . ARG C 621 ? 0.9620 0.7320 0.9549 0.1501  0.1108  0.1145  621 ARG C CZ  
14665 N NH1 . ARG C 621 ? 1.1033 0.8782 1.1025 0.1462  0.1105  0.1301  621 ARG C NH1 
14666 N NH2 . ARG C 621 ? 1.0392 0.8244 1.0237 0.1537  0.1142  0.1075  621 ARG C NH2 
14667 N N   . MET C 622 ? 0.8084 0.4742 0.8173 0.1679  0.0953  0.0946  622 MET C N   
14668 C CA  . MET C 622 ? 0.7813 0.4523 0.7883 0.1783  0.0978  0.0906  622 MET C CA  
14669 C C   . MET C 622 ? 0.8885 0.5603 0.9012 0.1825  0.0957  0.1038  622 MET C C   
14670 O O   . MET C 622 ? 0.9186 0.6089 0.9304 0.1874  0.0973  0.1070  622 MET C O   
14671 C CB  . MET C 622 ? 0.8263 0.4796 0.8310 0.1852  0.0980  0.0777  622 MET C CB  
14672 C CG  . MET C 622 ? 0.9631 0.6230 0.9604 0.1856  0.1023  0.0652  622 MET C CG  
14673 S SD  . MET C 622 ? 0.9094 0.5475 0.9012 0.1943  0.1028  0.0515  622 MET C SD  
14674 C CE  . MET C 622 ? 0.9504 0.6042 0.9345 0.1955  0.1100  0.0420  622 MET C CE  
14675 N N   . ASN C 623 ? 0.8709 0.5226 0.8899 0.1805  0.0916  0.1116  623 ASN C N   
14676 C CA  . ASN C 623 ? 0.9493 0.5997 0.9740 0.1849  0.0897  0.1263  623 ASN C CA  
14677 C C   . ASN C 623 ? 1.0156 0.6916 1.0383 0.1822  0.0917  0.1395  623 ASN C C   
14678 O O   . ASN C 623 ? 0.9205 0.6095 0.9420 0.1898  0.0917  0.1460  623 ASN C O   
14679 C CB  . ASN C 623 ? 1.0303 0.6517 1.0634 0.1819  0.0848  0.1325  623 ASN C CB  
14680 C CG  . ASN C 623 ? 1.0863 0.6827 1.1189 0.1893  0.0825  0.1190  623 ASN C CG  
14681 O OD1 . ASN C 623 ? 1.1451 0.7446 1.1753 0.2008  0.0846  0.1136  623 ASN C OD1 
14682 N ND2 . ASN C 623 ? 1.2268 0.7990 1.2617 0.1834  0.0780  0.1127  623 ASN C ND2 
14683 N N   . GLU C 624 ? 0.9743 0.6593 0.9961 0.1725  0.0931  0.1430  624 GLU C N   
14684 C CA  . GLU C 624 ? 0.8933 0.6040 0.9110 0.1714  0.0959  0.1545  624 GLU C CA  
14685 C C   . GLU C 624 ? 0.8240 0.5562 0.8325 0.1792  0.0976  0.1465  624 GLU C C   
14686 O O   . GLU C 624 ? 0.9588 0.7072 0.9636 0.1848  0.0973  0.1557  624 GLU C O   
14687 C CB  . GLU C 624 ? 0.8407 0.5599 0.8587 0.1612  0.0982  0.1559  624 GLU C CB  
14688 C CG  . GLU C 624 ? 1.1197 0.8241 1.1500 0.1517  0.0960  0.1679  624 GLU C CG  
14689 C CD  . GLU C 624 ? 1.4542 1.1662 1.4874 0.1415  0.0973  0.1663  624 GLU C CD  
14690 O OE1 . GLU C 624 ? 1.2005 0.9346 1.2248 0.1427  0.1015  0.1621  624 GLU C OE1 
14691 O OE2 . GLU C 624 ? 1.4355 1.1309 1.4806 0.1324  0.0935  0.1688  624 GLU C OE2 
14692 N N   . LYS C 625 ? 0.7949 0.5272 0.8002 0.1797  0.0989  0.1297  625 LYS C N   
14693 C CA  . LYS C 625 ? 0.8924 0.6428 0.8924 0.1855  0.0999  0.1209  625 LYS C CA  
14694 C C   . LYS C 625 ? 0.9972 0.7472 1.0014 0.1949  0.0972  0.1216  625 LYS C C   
14695 O O   . LYS C 625 ? 0.9459 0.7147 0.9476 0.2000  0.0958  0.1202  625 LYS C O   
14696 C CB  . LYS C 625 ? 0.8267 0.5754 0.8247 0.1830  0.1027  0.1049  625 LYS C CB  
14697 C CG  . LYS C 625 ? 0.8839 0.6397 0.8767 0.1757  0.1052  0.1036  625 LYS C CG  
14698 C CD  . LYS C 625 ? 1.0122 0.7714 1.0017 0.1753  0.1082  0.0893  625 LYS C CD  
14699 C CE  . LYS C 625 ? 0.8327 0.6037 0.8163 0.1706  0.1107  0.0886  625 LYS C CE  
14700 N NZ  . LYS C 625 ? 1.0152 0.7884 0.9960 0.1710  0.1137  0.0758  625 LYS C NZ  
14701 N N   . ARG C 626 ? 1.0092 0.7380 1.0200 0.1978  0.0957  0.1233  626 ARG C N   
14702 C CA  . ARG C 626 ? 0.8506 0.5784 0.8667 0.2080  0.0934  0.1253  626 ARG C CA  
14703 C C   . ARG C 626 ? 0.9056 0.6437 0.9208 0.2116  0.0905  0.1418  626 ARG C C   
14704 O O   . ARG C 626 ? 0.9524 0.7070 0.9677 0.2193  0.0880  0.1431  626 ARG C O   
14705 C CB  . ARG C 626 ? 0.9707 0.6708 0.9927 0.2113  0.0927  0.1234  626 ARG C CB  
14706 C CG  . ARG C 626 ? 0.8001 0.4900 0.8214 0.2113  0.0957  0.1072  626 ARG C CG  
14707 C CD  . ARG C 626 ? 0.8857 0.5497 0.9109 0.2180  0.0945  0.1046  626 ARG C CD  
14708 N NE  . ARG C 626 ? 1.0280 0.6972 1.0594 0.2300  0.0939  0.1075  626 ARG C NE  
14709 C CZ  . ARG C 626 ? 1.0518 0.7316 1.0864 0.2377  0.0971  0.0987  626 ARG C CZ  
14710 N NH1 . ARG C 626 ? 0.8111 0.4959 0.8424 0.2347  0.1017  0.0867  626 ARG C NH1 
14711 N NH2 . ARG C 626 ? 1.0647 0.7510 1.1069 0.2486  0.0960  0.1028  626 ARG C NH2 
14712 N N   . LYS C 627 ? 0.8538 0.5837 0.8688 0.2061  0.0906  0.1550  627 LYS C N   
14713 C CA  . LYS C 627 ? 0.9341 0.6734 0.9478 0.2103  0.0889  0.1740  627 LYS C CA  
14714 C C   . LYS C 627 ? 0.8429 0.6132 0.8460 0.2127  0.0890  0.1742  627 LYS C C   
14715 O O   . LYS C 627 ? 1.0634 0.8477 1.0635 0.2216  0.0858  0.1818  627 LYS C O   
14716 C CB  . LYS C 627 ? 0.8673 0.5915 0.8857 0.2025  0.0900  0.1891  627 LYS C CB  
14717 C CG  . LYS C 627 ? 1.2542 0.9456 1.2827 0.1982  0.0884  0.1851  627 LYS C CG  
14718 C CD  . LYS C 627 ? 1.2369 0.9074 1.2741 0.2029  0.0855  0.1993  627 LYS C CD  
14719 C CE  . LYS C 627 ? 1.2995 0.9351 1.3457 0.1990  0.0828  0.1926  627 LYS C CE  
14720 N NZ  . LYS C 627 ? 1.3657 0.9960 1.4078 0.2001  0.0831  0.1699  627 LYS C NZ  
14721 N N   . LYS C 628 ? 0.7994 0.5798 0.7963 0.2059  0.0919  0.1656  628 LYS C N   
14722 C CA  . LYS C 628 ? 0.8110 0.6184 0.7965 0.2089  0.0915  0.1629  628 LYS C CA  
14723 C C   . LYS C 628 ? 0.7988 0.6179 0.7846 0.2166  0.0869  0.1515  628 LYS C C   
14724 O O   . LYS C 628 ? 0.8657 0.7052 0.8440 0.2233  0.0832  0.1543  628 LYS C O   
14725 C CB  . LYS C 628 ? 0.8277 0.6395 0.8083 0.2009  0.0955  0.1534  628 LYS C CB  
14726 C CG  . LYS C 628 ? 1.0076 0.8446 0.9755 0.2043  0.0952  0.1490  628 LYS C CG  
14727 C CD  . LYS C 628 ? 1.0328 0.8722 0.9965 0.1974  0.0997  0.1408  628 LYS C CD  
14728 C CE  . LYS C 628 ? 1.1833 1.0452 1.1336 0.2022  0.0989  0.1345  628 LYS C CE  
14729 N NZ  . LYS C 628 ? 1.1969 1.0610 1.1431 0.1970  0.1036  0.1273  628 LYS C NZ  
14730 N N   . LEU C 629 ? 0.9180 0.7255 0.9129 0.2160  0.0870  0.1389  629 LEU C N   
14731 C CA  . LEU C 629 ? 0.8053 0.6245 0.8052 0.2219  0.0832  0.1286  629 LEU C CA  
14732 C C   . LEU C 629 ? 0.8725 0.6928 0.8790 0.2318  0.0787  0.1374  629 LEU C C   
14733 O O   . LEU C 629 ? 0.9855 0.8226 0.9956 0.2379  0.0738  0.1325  629 LEU C O   
14734 C CB  . LEU C 629 ? 0.8006 0.6085 0.8086 0.2179  0.0868  0.1139  629 LEU C CB  
14735 C CG  . LEU C 629 ? 0.8051 0.6262 0.8215 0.2212  0.0845  0.1022  629 LEU C CG  
14736 C CD1 . LEU C 629 ? 0.8061 0.6482 0.8163 0.2195  0.0809  0.0957  629 LEU C CD1 
14737 C CD2 . LEU C 629 ? 0.6785 0.4873 0.7023 0.2178  0.0901  0.0913  629 LEU C CD2 
14738 N N   . GLY C 630 ? 1.0152 0.8176 1.0244 0.2335  0.0798  0.1503  630 GLY C N   
14739 C CA  . GLY C 630 ? 0.9319 0.7319 0.9473 0.2437  0.0761  0.1603  630 GLY C CA  
14740 C C   . GLY C 630 ? 0.9435 0.7288 0.9713 0.2479  0.0770  0.1519  630 GLY C C   
14741 O O   . GLY C 630 ? 1.0039 0.7969 1.0391 0.2579  0.0735  0.1538  630 GLY C O   
14742 N N   . ILE C 631 ? 1.0496 0.8153 1.0796 0.2415  0.0819  0.1427  631 ILE C N   
14743 C CA  . ILE C 631 ? 0.9841 0.7355 1.0233 0.2465  0.0840  0.1338  631 ILE C CA  
14744 C C   . ILE C 631 ? 1.0556 0.7747 1.0945 0.2443  0.0860  0.1360  631 ILE C C   
14745 O O   . ILE C 631 ? 1.1669 0.8748 1.2034 0.2412  0.0844  0.1485  631 ILE C O   
14746 C CB  . ILE C 631 ? 0.8272 0.5884 0.8688 0.2430  0.0876  0.1174  631 ILE C CB  
14747 C CG1 . ILE C 631 ? 0.8844 0.6362 0.9178 0.2317  0.0916  0.1108  631 ILE C CG1 
14748 C CG2 . ILE C 631 ? 0.7807 0.5717 0.8250 0.2442  0.0840  0.1144  631 ILE C CG2 
14749 C CD1 . ILE C 631 ? 0.8506 0.6024 0.8865 0.2296  0.0966  0.0962  631 ILE C CD1 
14750 N N   . MET D 1   ? 1.2724 0.9172 1.3430 0.3584  0.2222  0.0482  1   MET D N   
14751 C CA  . MET D 1   ? 1.1529 0.8134 1.2637 0.3577  0.2157  0.0635  1   MET D CA  
14752 C C   . MET D 1   ? 1.1560 0.8208 1.2758 0.3496  0.1933  0.0658  1   MET D C   
14753 O O   . MET D 1   ? 1.1275 0.7850 1.2226 0.3457  0.1838  0.0585  1   MET D O   
14754 C CB  . MET D 1   ? 0.9700 0.6431 1.0814 0.3572  0.2177  0.0745  1   MET D CB  
14755 C CG  . MET D 1   ? 1.1606 0.8330 1.2342 0.3524  0.2085  0.0720  1   MET D CG  
14756 S SD  . MET D 1   ? 1.4547 1.1401 1.5366 0.3494  0.2051  0.0870  1   MET D SD  
14757 C CE  . MET D 1   ? 1.1023 0.7881 1.1933 0.3565  0.2322  0.0934  1   MET D CE  
14758 N N   . ASN D 2   ? 1.1384 0.8180 1.2925 0.3449  0.1837  0.0754  2   ASN D N   
14759 C CA  . ASN D 2   ? 1.1105 0.7931 1.2716 0.3383  0.1642  0.0792  2   ASN D CA  
14760 C C   . ASN D 2   ? 1.0939 0.7808 1.2394 0.3337  0.1524  0.0821  2   ASN D C   
14761 O O   . ASN D 2   ? 0.9857 0.6762 1.1215 0.3352  0.1574  0.0840  2   ASN D O   
14762 C CB  . ASN D 2   ? 1.0785 0.7754 1.2768 0.3369  0.1571  0.0899  2   ASN D CB  
14763 C CG  . ASN D 2   ? 1.1833 0.8983 1.4028 0.3360  0.1565  0.0997  2   ASN D CG  
14764 O OD1 . ASN D 2   ? 1.1807 0.8967 1.3902 0.3371  0.1659  0.0992  2   ASN D OD1 
14765 N ND2 . ASN D 2   ? 1.3561 1.0848 1.6060 0.3346  0.1455  0.1095  2   ASN D ND2 
14766 N N   . LEU D 3   ? 1.0950 0.7802 1.2380 0.3286  0.1381  0.0831  3   LEU D N   
14767 C CA  . LEU D 3   ? 0.9415 0.6300 1.0706 0.3239  0.1274  0.0846  3   LEU D CA  
14768 C C   . LEU D 3   ? 1.0475 0.7485 1.1889 0.3223  0.1250  0.0929  3   LEU D C   
14769 O O   . LEU D 3   ? 1.1161 0.8194 1.2423 0.3196  0.1235  0.0916  3   LEU D O   
14770 C CB  . LEU D 3   ? 0.9169 0.6031 1.0468 0.3182  0.1145  0.0863  3   LEU D CB  
14771 C CG  . LEU D 3   ? 0.8855 0.5756 0.9986 0.3106  0.1040  0.0846  3   LEU D CG  
14772 C CD1 . LEU D 3   ? 0.7854 0.4728 0.8750 0.3098  0.1069  0.0747  3   LEU D CD1 
14773 C CD2 . LEU D 3   ? 0.8132 0.4997 0.9267 0.3054  0.0947  0.0873  3   LEU D CD2 
14774 N N   . PHE D 4   ? 0.9477 0.6589 1.1179 0.3219  0.1233  0.1007  4   PHE D N   
14775 C CA  . PHE D 4   ? 0.8190 0.5409 1.0055 0.3198  0.1212  0.1080  4   PHE D CA  
14776 C C   . PHE D 4   ? 1.0320 0.7540 1.2135 0.3225  0.1355  0.1077  4   PHE D C   
14777 O O   . PHE D 4   ? 1.0026 0.7243 1.1728 0.3190  0.1339  0.1082  4   PHE D O   
14778 C CB  . PHE D 4   ? 1.0216 0.7560 1.2443 0.3201  0.1164  0.1167  4   PHE D CB  
14779 C CG  . PHE D 4   ? 1.0627 0.8000 1.2882 0.3152  0.0982  0.1208  4   PHE D CG  
14780 C CD1 . PHE D 4   ? 1.0761 0.8053 1.2961 0.3178  0.0938  0.1213  4   PHE D CD1 
14781 C CD2 . PHE D 4   ? 0.9641 0.7106 1.1937 0.3067  0.0860  0.1232  4   PHE D CD2 
14782 C CE1 . PHE D 4   ? 0.8942 0.6255 1.1116 0.3127  0.0776  0.1263  4   PHE D CE1 
14783 C CE2 . PHE D 4   ? 0.9090 0.6578 1.1342 0.3011  0.0692  0.1259  4   PHE D CE2 
14784 C CZ  . PHE D 4   ? 0.9196 0.6612 1.1378 0.3044  0.0652  0.1284  4   PHE D CZ  
14785 N N   . GLN D 5   ? 1.0534 0.7753 1.2410 0.3278  0.1502  0.1067  5   GLN D N   
14786 C CA  . GLN D 5   ? 0.9948 0.7148 1.1752 0.3319  0.1666  0.1085  5   GLN D CA  
14787 C C   . GLN D 5   ? 0.9526 0.6614 1.0934 0.3334  0.1674  0.1031  5   GLN D C   
14788 O O   . GLN D 5   ? 0.9775 0.6860 1.1085 0.3337  0.1741  0.1073  5   GLN D O   
14789 C CB  . GLN D 5   ? 0.9287 0.6493 1.1211 0.3382  0.1847  0.1079  5   GLN D CB  
14790 C CG  . GLN D 5   ? 1.0008 0.7374 1.2382 0.3369  0.1841  0.1149  5   GLN D CG  
14791 C CD  . GLN D 5   ? 1.1615 0.9110 1.4264 0.3319  0.1781  0.1244  5   GLN D CD  
14792 O OE1 . GLN D 5   ? 1.0554 0.8024 1.3144 0.3311  0.1862  0.1280  5   GLN D OE1 
14793 N NE2 . GLN D 5   ? 1.1345 0.8969 1.4308 0.3288  0.1639  0.1295  5   GLN D NE2 
14794 N N   . THR D 6   ? 0.9816 0.6833 1.1010 0.3326  0.1591  0.0944  6   THR D N   
14795 C CA  . THR D 6   ? 1.0167 0.7135 1.1019 0.3321  0.1557  0.0887  6   THR D CA  
14796 C C   . THR D 6   ? 0.9955 0.6974 1.0801 0.3270  0.1448  0.0936  6   THR D C   
14797 O O   . THR D 6   ? 1.0637 0.7645 1.1296 0.3288  0.1464  0.0954  6   THR D O   
14798 C CB  . THR D 6   ? 1.0239 0.7139 1.0939 0.3306  0.1490  0.0777  6   THR D CB  
14799 O OG1 . THR D 6   ? 1.1887 0.8709 1.2629 0.3353  0.1605  0.0726  6   THR D OG1 
14800 C CG2 . THR D 6   ? 0.8325 0.5208 0.8702 0.3300  0.1446  0.0711  6   THR D CG2 
14801 N N   . VAL D 7   ? 0.9238 0.6304 1.0275 0.3213  0.1341  0.0959  7   VAL D N   
14802 C CA  . VAL D 7   ? 0.9558 0.6648 1.0591 0.3162  0.1255  0.0984  7   VAL D CA  
14803 C C   . VAL D 7   ? 1.0005 0.7112 1.1168 0.3163  0.1338  0.1064  7   VAL D C   
14804 O O   . VAL D 7   ? 1.0278 0.7352 1.1331 0.3168  0.1353  0.1090  7   VAL D O   
14805 C CB  . VAL D 7   ? 0.9425 0.6547 1.0575 0.3093  0.1124  0.0974  7   VAL D CB  
14806 C CG1 . VAL D 7   ? 1.0242 0.7375 1.1418 0.3035  0.1065  0.0991  7   VAL D CG1 
14807 C CG2 . VAL D 7   ? 0.8781 0.5868 0.9779 0.3082  0.1057  0.0906  7   VAL D CG2 
14808 N N   . PHE D 8   ? 0.8899 0.6059 1.0322 0.3161  0.1400  0.1112  8   PHE D N   
14809 C CA  . PHE D 8   ? 0.9143 0.6325 1.0738 0.3146  0.1493  0.1189  8   PHE D CA  
14810 C C   . PHE D 8   ? 1.0170 0.7278 1.1555 0.3211  0.1641  0.1227  8   PHE D C   
14811 O O   . PHE D 8   ? 1.2061 0.9133 1.3459 0.3196  0.1690  0.1291  8   PHE D O   
14812 C CB  . PHE D 8   ? 0.8530 0.5816 1.0483 0.3139  0.1545  0.1234  8   PHE D CB  
14813 C CG  . PHE D 8   ? 0.9513 0.6895 1.1690 0.3079  0.1386  0.1225  8   PHE D CG  
14814 C CD1 . PHE D 8   ? 0.8301 0.5682 1.0445 0.2994  0.1237  0.1200  8   PHE D CD1 
14815 C CD2 . PHE D 8   ? 0.9742 0.7212 1.2160 0.3114  0.1391  0.1248  8   PHE D CD2 
14816 C CE1 . PHE D 8   ? 0.8330 0.5799 1.0628 0.2937  0.1084  0.1198  8   PHE D CE1 
14817 C CE2 . PHE D 8   ? 0.8693 0.6260 1.1302 0.3068  0.1228  0.1264  8   PHE D CE2 
14818 C CZ  . PHE D 8   ? 0.8696 0.6264 1.1222 0.2975  0.1070  0.1239  8   PHE D CZ  
14819 N N   . THR D 9   ? 0.9203 0.6274 1.0374 0.3281  0.1710  0.1189  9   THR D N   
14820 C CA  . THR D 9   ? 0.9551 0.6554 1.0457 0.3345  0.1838  0.1226  9   THR D CA  
14821 C C   . THR D 9   ? 1.0886 0.7846 1.1555 0.3350  0.1751  0.1241  9   THR D C   
14822 O O   . THR D 9   ? 1.2281 0.9194 1.2886 0.3373  0.1829  0.1335  9   THR D O   
14823 C CB  . THR D 9   ? 0.9916 0.6881 1.0611 0.3405  0.1911  0.1150  9   THR D CB  
14824 O OG1 . THR D 9   ? 0.9973 0.6970 1.0926 0.3421  0.2030  0.1154  9   THR D OG1 
14825 C CG2 . THR D 9   ? 1.0865 0.7761 1.1199 0.3468  0.2015  0.1176  9   THR D CG2 
14826 N N   . GLY D 10  ? 0.9491 0.6468 1.0056 0.3332  0.1601  0.1159  10  GLY D N   
14827 C CA  . GLY D 10  ? 0.9938 0.6904 1.0330 0.3345  0.1512  0.1169  10  GLY D CA  
14828 C C   . GLY D 10  ? 1.0607 0.7549 1.1169 0.3310  0.1496  0.1233  10  GLY D C   
14829 O O   . GLY D 10  ? 1.0916 0.7817 1.1368 0.3350  0.1498  0.1294  10  GLY D O   
14830 N N   . SER D 11  ? 1.0633 0.7595 1.1464 0.3235  0.1474  0.1219  11  SER D N   
14831 C CA  . SER D 11  ? 0.9889 0.6811 1.0884 0.3179  0.1458  0.1251  11  SER D CA  
14832 C C   . SER D 11  ? 1.0830 0.7686 1.1898 0.3197  0.1607  0.1363  11  SER D C   
14833 O O   . SER D 11  ? 1.0910 0.7677 1.1973 0.3201  0.1630  0.1415  11  SER D O   
14834 C CB  . SER D 11  ? 0.8811 0.5787 1.0044 0.3085  0.1378  0.1198  11  SER D CB  
14835 O OG  . SER D 11  ? 1.0471 0.7476 1.1617 0.3061  0.1250  0.1113  11  SER D OG  
14836 N N   . LYS D 12  ? 1.0384 0.7272 1.1527 0.3213  0.1724  0.1404  12  LYS D N   
14837 C CA  . LYS D 12  ? 1.1134 0.7960 1.2344 0.3227  0.1896  0.1523  12  LYS D CA  
14838 C C   . LYS D 12  ? 1.0861 0.7594 1.1738 0.3324  0.1952  0.1603  12  LYS D C   
14839 O O   . LYS D 12  ? 1.0066 0.6698 1.0957 0.3335  0.2046  0.1715  12  LYS D O   
14840 C CB  . LYS D 12  ? 1.1467 0.8363 1.2821 0.3235  0.2030  0.1545  12  LYS D CB  
14841 C CG  . LYS D 12  ? 1.1084 0.8071 1.2875 0.3139  0.2030  0.1543  12  LYS D CG  
14842 C CD  . LYS D 12  ? 1.0579 0.7697 1.2541 0.3149  0.2026  0.1494  12  LYS D CD  
14843 C CE  . LYS D 12  ? 1.0892 0.8019 1.2854 0.3219  0.2241  0.1549  12  LYS D CE  
14844 N NZ  . LYS D 12  ? 1.3615 1.0848 1.5742 0.3249  0.2243  0.1493  12  LYS D NZ  
14845 N N   . GLN D 13  ? 1.0978 0.7745 1.1561 0.3389  0.1885  0.1548  13  GLN D N   
14846 C CA  . GLN D 13  ? 1.1687 0.8405 1.1934 0.3482  0.1891  0.1617  13  GLN D CA  
14847 C C   . GLN D 13  ? 1.0575 0.7246 1.0852 0.3490  0.1800  0.1653  13  GLN D C   
14848 O O   . GLN D 13  ? 0.9865 0.6450 1.0030 0.3555  0.1860  0.1783  13  GLN D O   
14849 C CB  . GLN D 13  ? 1.0237 0.7028 1.0210 0.3521  0.1799  0.1514  13  GLN D CB  
14850 C CG  . GLN D 13  ? 1.1856 0.8652 1.1723 0.3538  0.1917  0.1475  13  GLN D CG  
14851 C CD  . GLN D 13  ? 1.3919 1.0759 1.3527 0.3557  0.1824  0.1347  13  GLN D CD  
14852 O OE1 . GLN D 13  ? 1.2373 0.9264 1.1900 0.3552  0.1661  0.1288  13  GLN D OE1 
14853 N NE2 . GLN D 13  ? 1.3763 1.0579 1.3251 0.3575  0.1937  0.1291  13  GLN D NE2 
14854 N N   . ALA D 14  ? 1.0443 0.7159 1.0869 0.3430  0.1669  0.1546  14  ALA D N   
14855 C CA  . ALA D 14  ? 0.9544 0.6212 1.0024 0.3437  0.1600  0.1556  14  ALA D CA  
14856 C C   . ALA D 14  ? 1.1084 0.7620 1.1758 0.3397  0.1706  0.1642  14  ALA D C   
14857 O O   . ALA D 14  ? 1.1086 0.7554 1.1734 0.3422  0.1708  0.1704  14  ALA D O   
14858 C CB  . ALA D 14  ? 0.9132 0.5868 0.9721 0.3366  0.1470  0.1415  14  ALA D CB  
14859 N N   . LEU D 15  ? 1.0646 0.7165 1.1540 0.3318  0.1786  0.1638  15  LEU D N   
14860 C CA  . LEU D 15  ? 0.9175 0.5564 1.0288 0.3262  0.1894  0.1710  15  LEU D CA  
14861 C C   . LEU D 15  ? 0.9403 0.5689 1.0377 0.3349  0.2047  0.1887  15  LEU D C   
14862 O O   . LEU D 15  ? 1.0708 0.6869 1.1711 0.3345  0.2092  0.1964  15  LEU D O   
14863 C CB  . LEU D 15  ? 0.8687 0.5138 1.0098 0.3144  0.1926  0.1664  15  LEU D CB  
14864 C CG  . LEU D 15  ? 0.8831 0.5166 1.0508 0.3068  0.2057  0.1740  15  LEU D CG  
14865 C CD1 . LEU D 15  ? 1.0574 0.6780 1.2369 0.2999  0.1999  0.1677  15  LEU D CD1 
14866 C CD2 . LEU D 15  ? 0.8971 0.5429 1.0951 0.2968  0.2092  0.1713  15  LEU D CD2 
14867 N N   . ALA D 16  ? 1.0296 0.6641 1.1092 0.3408  0.2123  0.1939  16  ALA D N   
14868 C CA  . ALA D 16  ? 1.1187 0.7435 1.1780 0.3496  0.2277  0.2116  16  ALA D CA  
14869 C C   . ALA D 16  ? 1.1483 0.7661 1.1825 0.3611  0.2212  0.2207  16  ALA D C   
14870 O O   . ALA D 16  ? 1.0203 0.6230 1.0505 0.3665  0.2325  0.2378  16  ALA D O   
14871 C CB  . ALA D 16  ? 0.9591 0.5931 0.9966 0.3537  0.2344  0.2109  16  ALA D CB  
14872 N N   . ALA D 17  ? 1.0576 0.6868 1.0776 0.3650  0.2033  0.2105  17  ALA D N   
14873 C CA  . ALA D 17  ? 1.0804 0.7083 1.0817 0.3764  0.1945  0.2183  17  ALA D CA  
14874 C C   . ALA D 17  ? 1.0976 0.7182 1.1216 0.3695  0.1930  0.2192  17  ALA D C   
14875 O O   . ALA D 17  ? 1.0338 0.6468 1.0494 0.3769  0.1957  0.2336  17  ALA D O   
14876 C CB  . ALA D 17  ? 0.9761 0.6219 0.9656 0.3778  0.1755  0.2041  17  ALA D CB  
14877 N N   . ALA D 18  ? 1.1065 0.7282 1.1577 0.3559  0.1890  0.2040  18  ALA D N   
14878 C CA  . ALA D 18  ? 1.0509 0.6622 1.1226 0.3490  0.1890  0.2016  18  ALA D CA  
14879 C C   . ALA D 18  ? 1.1537 0.7459 1.2372 0.3463  0.2068  0.2155  18  ALA D C   
14880 O O   . ALA D 18  ? 1.2551 0.8347 1.3457 0.3466  0.2101  0.2211  18  ALA D O   
14881 C CB  . ALA D 18  ? 0.9176 0.5318 1.0099 0.3367  0.1817  0.1825  18  ALA D CB  
14882 N N   . GLU D 19  ? 1.0919 0.6813 1.1796 0.3438  0.2196  0.2213  19  GLU D N   
14883 C CA  . GLU D 19  ? 0.9984 0.5700 1.0998 0.3406  0.2391  0.2358  19  GLU D CA  
14884 C C   . GLU D 19  ? 1.1687 0.7308 1.2448 0.3537  0.2481  0.2578  19  GLU D C   
14885 O O   . GLU D 19  ? 1.2281 0.7726 1.3146 0.3518  0.2607  0.2701  19  GLU D O   
14886 C CB  . GLU D 19  ? 1.1877 0.7618 1.3001 0.3371  0.2524  0.2383  19  GLU D CB  
14887 C CG  . GLU D 19  ? 1.1829 0.7621 1.3304 0.3230  0.2485  0.2224  19  GLU D CG  
14888 C CD  . GLU D 19  ? 1.3069 0.8968 1.4685 0.3190  0.2586  0.2232  19  GLU D CD  
14889 O OE1 . GLU D 19  ? 1.4221 1.0138 1.5634 0.3271  0.2710  0.2351  19  GLU D OE1 
14890 O OE2 . GLU D 19  ? 1.3827 0.9825 1.5746 0.3060  0.2531  0.2108  19  GLU D OE2 
14891 N N   . GLY D 20  ? 1.1552 0.7279 1.1978 0.3672  0.2413  0.2631  20  GLY D N   
14892 C CA  . GLY D 20  ? 1.2887 0.8541 1.3009 0.3820  0.2471  0.2853  20  GLY D CA  
14893 C C   . GLY D 20  ? 1.1634 0.7272 1.1763 0.3865  0.2366  0.2894  20  GLY D C   
14894 O O   . GLY D 20  ? 1.2922 0.8412 1.3021 0.3912  0.2468  0.3078  20  GLY D O   
14895 N N   . ILE D 21  ? 1.2030 0.7816 1.2211 0.3858  0.2173  0.2732  21  ILE D N   
14896 C CA  . ILE D 21  ? 1.2370 0.8163 1.2602 0.3911  0.2076  0.2757  21  ILE D CA  
14897 C C   . ILE D 21  ? 1.1552 0.7160 1.2093 0.3805  0.2167  0.2725  21  ILE D C   
14898 O O   . ILE D 21  ? 1.2684 0.8202 1.3258 0.3867  0.2182  0.2835  21  ILE D O   
14899 C CB  . ILE D 21  ? 1.1680 0.7688 1.1903 0.3937  0.1869  0.2597  21  ILE D CB  
14900 C CG1 . ILE D 21  ? 1.0546 0.6599 1.0780 0.4046  0.1774  0.2678  21  ILE D CG1 
14901 C CG2 . ILE D 21  ? 1.1771 0.7803 1.2244 0.3786  0.1832  0.2359  21  ILE D CG2 
14902 C CD1 . ILE D 21  ? 1.1620 0.7907 1.1818 0.4107  0.1584  0.2579  21  ILE D CD1 
14903 N N   . VAL D 22  ? 1.2060 0.7605 1.2825 0.3655  0.2226  0.2582  22  VAL D N   
14904 C CA  . VAL D 22  ? 1.1493 0.6833 1.2547 0.3547  0.2316  0.2534  22  VAL D CA  
14905 C C   . VAL D 22  ? 1.2306 0.7439 1.3375 0.3566  0.2509  0.2752  22  VAL D C   
14906 O O   . VAL D 22  ? 1.3017 0.7973 1.4226 0.3557  0.2568  0.2793  22  VAL D O   
14907 C CB  . VAL D 22  ? 1.2501 0.7827 1.3780 0.3388  0.2317  0.2336  22  VAL D CB  
14908 C CG1 . VAL D 22  ? 1.6709 1.1974 1.8081 0.3320  0.2467  0.2409  22  VAL D CG1 
14909 C CG2 . VAL D 22  ? 1.0607 0.5761 1.2125 0.3296  0.2330  0.2209  22  VAL D CG2 
14910 N N   . LYS D 23  ? 1.1896 0.7037 1.2825 0.3594  0.2618  0.2889  23  LYS D N   
14911 C CA  . LYS D 23  ? 1.4107 0.9052 1.5024 0.3617  0.2824  0.3117  23  LYS D CA  
14912 C C   . LYS D 23  ? 1.4124 0.9032 1.4830 0.3772  0.2795  0.3306  23  LYS D C   
14913 O O   . LYS D 23  ? 1.3045 0.7752 1.3851 0.3772  0.2919  0.3441  23  LYS D O   
14914 C CB  . LYS D 23  ? 1.3370 0.8345 1.4139 0.3637  0.2958  0.3227  23  LYS D CB  
14915 C CG  . LYS D 23  ? 1.5173 0.9933 1.5982 0.3626  0.3219  0.3454  23  LYS D CG  
14916 C CD  . LYS D 23  ? 1.6644 1.1200 1.7879 0.3464  0.3349  0.3415  23  LYS D CD  
14917 C CE  . LYS D 23  ? 1.7481 1.2083 1.9068 0.3295  0.3326  0.3191  23  LYS D CE  
14918 N NZ  . LYS D 23  ? 1.4564 0.9085 1.6400 0.3195  0.3220  0.3003  23  LYS D NZ  
14919 N N   . GLN D 24  ? 1.2450 0.7553 1.2889 0.3901  0.2623  0.3313  24  GLN D N   
14920 C CA  . GLN D 24  ? 1.2052 0.7168 1.2303 0.4061  0.2555  0.3491  24  GLN D CA  
14921 C C   . GLN D 24  ? 1.2999 0.8015 1.3524 0.4040  0.2524  0.3440  24  GLN D C   
14922 O O   . GLN D 24  ? 1.4591 0.9482 1.5098 0.4125  0.2581  0.3629  24  GLN D O   
14923 C CB  . GLN D 24  ? 1.2307 0.7680 1.2289 0.4181  0.2347  0.3458  24  GLN D CB  
14924 C CG  . GLN D 24  ? 1.4628 1.0049 1.4362 0.4364  0.2264  0.3679  24  GLN D CG  
14925 C CD  . GLN D 24  ? 1.5975 1.1651 1.5437 0.4478  0.2058  0.3649  24  GLN D CD  
14926 O OE1 . GLN D 24  ? 1.5781 1.1564 1.5156 0.4437  0.2018  0.3503  24  GLN D OE1 
14927 N NE2 . GLN D 24  ? 1.2395 0.8174 1.1732 0.4627  0.1919  0.3791  24  GLN D NE2 
14928 N N   . ALA D 25  ? 1.3056 0.8113 1.3822 0.3932  0.2446  0.3191  25  ALA D N   
14929 C CA  . ALA D 25  ? 1.3301 0.8241 1.4317 0.3911  0.2437  0.3113  25  ALA D CA  
14930 C C   . ALA D 25  ? 1.4071 0.8706 1.5299 0.3816  0.2641  0.3167  25  ALA D C   
14931 O O   . ALA D 25  ? 1.3254 0.7728 1.4605 0.3858  0.2690  0.3234  25  ALA D O   
14932 C CB  . ALA D 25  ? 1.1427 0.6475 1.2591 0.3820  0.2321  0.2833  25  ALA D CB  
14933 N N   . VAL D 26  ? 1.3805 0.8359 1.5104 0.3689  0.2765  0.3139  26  VAL D N   
14934 C CA  . VAL D 26  ? 1.3185 0.7455 1.4719 0.3580  0.2967  0.3187  26  VAL D CA  
14935 C C   . VAL D 26  ? 1.3835 0.7971 1.5240 0.3692  0.3101  0.3487  26  VAL D C   
14936 O O   . VAL D 26  ? 1.4475 0.8381 1.6043 0.3686  0.3208  0.3559  26  VAL D O   
14937 C CB  . VAL D 26  ? 1.2130 0.6388 1.3800 0.3423  0.3062  0.3101  26  VAL D CB  
14938 C CG1 . VAL D 26  ? 1.2466 0.6453 1.4360 0.3325  0.3297  0.3217  26  VAL D CG1 
14939 C CG2 . VAL D 26  ? 1.2575 0.6899 1.4421 0.3299  0.2944  0.2810  26  VAL D CG2 
14940 N N   . ASP D 27  ? 1.3804 0.8072 1.4900 0.3800  0.3099  0.3662  27  ASP D N   
14941 C CA  . ASP D 27  ? 1.5134 0.9286 1.6039 0.3917  0.3223  0.3965  27  ASP D CA  
14942 C C   . ASP D 27  ? 1.4733 0.8890 1.5543 0.4082  0.3115  0.4094  27  ASP D C   
14943 O O   . ASP D 27  ? 1.5163 0.9133 1.5960 0.4144  0.3241  0.4315  27  ASP D O   
14944 C CB  . ASP D 27  ? 1.6588 1.0873 1.7136 0.3992  0.3250  0.4101  27  ASP D CB  
14945 C CG  . ASP D 27  ? 1.6131 1.0406 1.6787 0.3853  0.3389  0.4017  27  ASP D CG  
14946 O OD1 . ASP D 27  ? 1.6527 1.0670 1.7549 0.3690  0.3485  0.3895  27  ASP D OD1 
14947 O OD2 . ASP D 27  ? 1.5582 0.9980 1.5963 0.3910  0.3400  0.4072  27  ASP D OD2 
14948 N N   . GLU D 28  ? 1.3311 0.7684 1.4075 0.4155  0.2891  0.3970  28  GLU D N   
14949 C CA  . GLU D 28  ? 1.3543 0.7957 1.4261 0.4320  0.2776  0.4095  28  GLU D CA  
14950 C C   . GLU D 28  ? 1.3549 0.7831 1.4607 0.4288  0.2776  0.3969  28  GLU D C   
14951 O O   . GLU D 28  ? 1.5922 1.0060 1.7046 0.4384  0.2824  0.4134  28  GLU D O   
14952 C CB  . GLU D 28  ? 1.3319 0.8057 1.3809 0.4437  0.2536  0.4062  28  GLU D CB  
14953 C CG  . GLU D 28  ? 1.5910 1.0759 1.5987 0.4530  0.2520  0.4243  28  GLU D CG  
14954 C CD  . GLU D 28  ? 1.7216 1.2375 1.7071 0.4641  0.2278  0.4202  28  GLU D CD  
14955 O OE1 . GLU D 28  ? 1.7018 1.2312 1.7036 0.4695  0.2116  0.4122  28  GLU D OE1 
14956 O OE2 . GLU D 28  ? 1.6099 1.1360 1.5622 0.4676  0.2258  0.4248  28  GLU D OE2 
14957 N N   . LYS D 29  ? 1.3161 0.7487 1.4416 0.4165  0.2722  0.3683  29  LYS D N   
14958 C CA  . LYS D 29  ? 1.3179 0.7376 1.4720 0.4137  0.2728  0.3537  29  LYS D CA  
14959 C C   . LYS D 29  ? 1.3377 0.7274 1.5175 0.3960  0.2909  0.3409  29  LYS D C   
14960 O O   . LYS D 29  ? 1.3386 0.7112 1.5403 0.3943  0.2952  0.3310  29  LYS D O   
14961 C CB  . LYS D 29  ? 1.2761 0.7203 1.4333 0.4139  0.2542  0.3304  29  LYS D CB  
14962 C CG  . LYS D 29  ? 1.2689 0.7435 1.4066 0.4305  0.2349  0.3405  29  LYS D CG  
14963 C CD  . LYS D 29  ? 1.2986 0.7722 1.4470 0.4468  0.2305  0.3536  29  LYS D CD  
14964 C CE  . LYS D 29  ? 1.3449 0.8514 1.4802 0.4621  0.2092  0.3604  29  LYS D CE  
14965 N NZ  . LYS D 29  ? 1.3592 0.8679 1.5137 0.4768  0.2036  0.3681  29  LYS D NZ  
14966 N N   . GLY D 30  ? 1.3202 0.7036 1.4987 0.3832  0.3017  0.3408  30  GLY D N   
14967 C CA  . GLY D 30  ? 1.3286 0.6853 1.5338 0.3652  0.3179  0.3288  30  GLY D CA  
14968 C C   . GLY D 30  ? 1.4095 0.7716 1.6276 0.3510  0.3097  0.2974  30  GLY D C   
14969 O O   . GLY D 30  ? 1.4700 0.8529 1.6798 0.3562  0.2929  0.2841  30  GLY D O   
14970 N N   . ARG D 31  ? 1.3711 0.7144 1.6107 0.3327  0.3214  0.2854  31  ARG D N   
14971 C CA  . ARG D 31  ? 1.3794 0.7253 1.6307 0.3184  0.3138  0.2561  31  ARG D CA  
14972 C C   . ARG D 31  ? 1.4103 0.7419 1.6731 0.3174  0.3109  0.2362  31  ARG D C   
14973 O O   . ARG D 31  ? 1.2900 0.6248 1.5568 0.3081  0.3031  0.2117  31  ARG D O   
14974 C CB  . ARG D 31  ? 1.2654 0.5961 1.5387 0.2989  0.3264  0.2502  31  ARG D CB  
14975 C CG  . ARG D 31  ? 1.3450 0.6901 1.6099 0.2992  0.3318  0.2680  31  ARG D CG  
14976 C CD  . ARG D 31  ? 1.2714 0.6299 1.5458 0.2861  0.3264  0.2524  31  ARG D CD  
14977 N NE  . ARG D 31  ? 1.3180 0.6914 1.5833 0.2890  0.3329  0.2699  31  ARG D NE  
14978 C CZ  . ARG D 31  ? 1.3872 0.7481 1.6702 0.2809  0.3525  0.2835  31  ARG D CZ  
14979 N NH1 . ARG D 31  ? 1.5131 0.8460 1.8258 0.2680  0.3668  0.2817  31  ARG D NH1 
14980 N NH2 . ARG D 31  ? 1.3843 0.7598 1.6563 0.2852  0.3593  0.2987  31  ARG D NH2 
14981 N N   . ASP D 32  ? 1.4208 0.7359 1.6886 0.3274  0.3180  0.2465  32  ASP D N   
14982 C CA  . ASP D 32  ? 1.3319 0.6318 1.6113 0.3278  0.3182  0.2283  32  ASP D CA  
14983 C C   . ASP D 32  ? 1.3435 0.6664 1.6103 0.3457  0.3042  0.2294  32  ASP D C   
14984 O O   . ASP D 32  ? 1.3105 0.6248 1.5861 0.3473  0.3044  0.2134  32  ASP D O   
14985 C CB  . ASP D 32  ? 1.3873 0.6506 1.6866 0.3262  0.3371  0.2359  32  ASP D CB  
14986 C CG  . ASP D 32  ? 1.6772 0.9162 1.9946 0.3066  0.3520  0.2329  32  ASP D CG  
14987 O OD1 . ASP D 32  ? 1.7021 0.9461 2.0233 0.2912  0.3474  0.2146  32  ASP D OD1 
14988 O OD2 . ASP D 32  ? 1.6317 0.8469 1.9615 0.3065  0.3684  0.2494  32  ASP D OD2 
14989 N N   . TYR D 33  ? 1.4621 0.8139 1.7095 0.3587  0.2928  0.2473  33  TYR D N   
14990 C CA  . TYR D 33  ? 1.2824 0.6587 1.5212 0.3749  0.2784  0.2492  33  TYR D CA  
14991 C C   . TYR D 33  ? 1.3304 0.7211 1.5686 0.3685  0.2679  0.2218  33  TYR D C   
14992 O O   . TYR D 33  ? 1.3725 0.7712 1.6038 0.3566  0.2635  0.2098  33  TYR D O   
14993 C CB  . TYR D 33  ? 1.2626 0.6661 1.4791 0.3871  0.2675  0.2714  33  TYR D CB  
14994 C CG  . TYR D 33  ? 1.2586 0.6860 1.4700 0.4051  0.2531  0.2782  33  TYR D CG  
14995 C CD1 . TYR D 33  ? 1.2955 0.7163 1.5125 0.4208  0.2557  0.2988  33  TYR D CD1 
14996 C CD2 . TYR D 33  ? 1.3447 0.8022 1.5473 0.4066  0.2366  0.2655  33  TYR D CD2 
14997 C CE1 . TYR D 33  ? 1.2933 0.7379 1.5094 0.4376  0.2414  0.3059  33  TYR D CE1 
14998 C CE2 . TYR D 33  ? 1.2528 0.7338 1.4549 0.4224  0.2233  0.2719  33  TYR D CE2 
14999 C CZ  . TYR D 33  ? 1.2745 0.7499 1.4841 0.4380  0.2252  0.2921  33  TYR D CZ  
15000 O OH  . TYR D 33  ? 1.3649 0.8652 1.5777 0.4540  0.2109  0.2990  33  TYR D OH  
15001 N N   . LYS D 34  ? 1.4506 0.8439 1.6970 0.3768  0.2652  0.2124  34  LYS D N   
15002 C CA  . LYS D 34  ? 1.3047 0.7092 1.5502 0.3715  0.2581  0.1871  34  LYS D CA  
15003 C C   . LYS D 34  ? 1.1862 0.6288 1.4156 0.3766  0.2403  0.1880  34  LYS D C   
15004 O O   . LYS D 34  ? 1.1708 0.6342 1.3951 0.3909  0.2314  0.2051  34  LYS D O   
15005 C CB  . LYS D 34  ? 1.3712 0.7652 1.6321 0.3791  0.2642  0.1770  34  LYS D CB  
15006 C CG  . LYS D 34  ? 1.4650 0.8182 1.7424 0.3728  0.2829  0.1711  34  LYS D CG  
15007 C CD  . LYS D 34  ? 1.6250 0.9567 1.9031 0.3534  0.2895  0.1429  34  LYS D CD  
15008 C CE  . LYS D 34  ? 1.6217 0.9127 1.9141 0.3424  0.3067  0.1398  34  LYS D CE  
15009 N NZ  . LYS D 34  ? 1.5616 0.8435 1.8516 0.3232  0.3074  0.1320  34  LYS D NZ  
15010 N N   . VAL D 35  ? 1.2292 0.6795 1.4508 0.3647  0.2350  0.1694  35  VAL D N   
15011 C CA  . VAL D 35  ? 1.1611 0.6445 1.3684 0.3673  0.2194  0.1671  35  VAL D CA  
15012 C C   . VAL D 35  ? 1.1047 0.5941 1.3160 0.3660  0.2172  0.1453  35  VAL D C   
15013 O O   . VAL D 35  ? 1.0986 0.5668 1.3142 0.3554  0.2257  0.1266  35  VAL D O   
15014 C CB  . VAL D 35  ? 1.1282 0.6176 1.3225 0.3564  0.2155  0.1668  35  VAL D CB  
15015 C CG1 . VAL D 35  ? 1.3018 0.7785 1.4951 0.3558  0.2236  0.1865  35  VAL D CG1 
15016 C CG2 . VAL D 35  ? 1.1479 0.6238 1.3454 0.3407  0.2188  0.1440  35  VAL D CG2 
15017 N N   . ALA D 36  ? 1.1751 0.6920 1.3855 0.3769  0.2071  0.1476  36  ALA D N   
15018 C CA  . ALA D 36  ? 1.0810 0.6058 1.2960 0.3769  0.2069  0.1289  36  ALA D CA  
15019 C C   . ALA D 36  ? 1.1375 0.6981 1.3507 0.3869  0.1932  0.1344  36  ALA D C   
15020 O O   . ALA D 36  ? 1.0394 0.6157 1.2518 0.3972  0.1848  0.1533  36  ALA D O   
15021 C CB  . ALA D 36  ? 1.0946 0.5999 1.3273 0.3824  0.2199  0.1232  36  ALA D CB  
15022 N N   . PHE D 37  ? 1.2000 0.7724 1.4123 0.3837  0.1916  0.1181  37  PHE D N   
15023 C CA  . PHE D 37  ? 1.0573 0.6631 1.2715 0.3918  0.1799  0.1212  37  PHE D CA  
15024 C C   . PHE D 37  ? 1.2066 0.8198 1.4426 0.4027  0.1856  0.1177  37  PHE D C   
15025 O O   . PHE D 37  ? 1.0776 0.6694 1.3210 0.4002  0.1997  0.1052  37  PHE D O   
15026 C CB  . PHE D 37  ? 1.0525 0.6684 1.2522 0.3815  0.1750  0.1078  37  PHE D CB  
15027 C CG  . PHE D 37  ? 1.1402 0.7657 1.3224 0.3767  0.1640  0.1158  37  PHE D CG  
15028 C CD1 . PHE D 37  ? 1.1300 0.7756 1.3094 0.3860  0.1529  0.1327  37  PHE D CD1 
15029 C CD2 . PHE D 37  ? 1.1218 0.7366 1.2902 0.3637  0.1649  0.1060  37  PHE D CD2 
15030 C CE1 . PHE D 37  ? 1.1381 0.7907 1.2998 0.3821  0.1450  0.1387  37  PHE D CE1 
15031 C CE2 . PHE D 37  ? 0.9199 0.5440 1.0744 0.3602  0.1563  0.1131  37  PHE D CE2 
15032 C CZ  . PHE D 37  ? 0.9336 0.5756 1.0840 0.3692  0.1474  0.1287  37  PHE D CZ  
15033 N N   . PRO D 38  ? 1.2739 0.9169 1.5219 0.4152  0.1753  0.1282  38  PRO D N   
15034 C CA  . PRO D 38  ? 1.1808 0.8331 1.4545 0.4266  0.1813  0.1258  38  PRO D CA  
15035 C C   . PRO D 38  ? 1.2269 0.8758 1.5054 0.4209  0.1939  0.1041  38  PRO D C   
15036 O O   . PRO D 38  ? 1.1130 0.7814 1.3879 0.4174  0.1896  0.0968  38  PRO D O   
15037 C CB  . PRO D 38  ? 1.0316 0.7211 1.3162 0.4388  0.1650  0.1398  38  PRO D CB  
15038 C CG  . PRO D 38  ? 1.0471 0.7404 1.3103 0.4366  0.1519  0.1529  38  PRO D CG  
15039 C CD  . PRO D 38  ? 1.2372 0.9065 1.4771 0.4202  0.1582  0.1425  38  PRO D CD  
15040 N N   . ASP D 39  ? 1.3206 0.9437 1.6069 0.4205  0.2108  0.0942  39  ASP D N   
15041 C CA  . ASP D 39  ? 1.2006 0.8161 1.4894 0.4162  0.2262  0.0733  39  ASP D CA  
15042 C C   . ASP D 39  ? 1.2125 0.8213 1.4754 0.4009  0.2270  0.0574  39  ASP D C   
15043 O O   . ASP D 39  ? 1.1505 0.7821 1.4117 0.4000  0.2226  0.0540  39  ASP D O   
15044 C CB  . ASP D 39  ? 1.1742 0.8208 1.4892 0.4288  0.2265  0.0755  39  ASP D CB  
15045 C CG  . ASP D 39  ? 1.4512 1.0920 1.7728 0.4272  0.2458  0.0559  39  ASP D CG  
15046 O OD1 . ASP D 39  ? 1.5305 1.1392 1.8345 0.4170  0.2597  0.0394  39  ASP D OD1 
15047 O OD2 . ASP D 39  ? 1.4236 1.0917 1.7679 0.4359  0.2475  0.0568  39  ASP D OD2 
15048 N N   . THR D 40  ? 1.2578 0.8347 1.5022 0.3890  0.2330  0.0478  40  THR D N   
15049 C CA  . THR D 40  ? 1.1687 0.7353 1.3882 0.3750  0.2339  0.0328  40  THR D CA  
15050 C C   . THR D 40  ? 1.3300 0.8568 1.5379 0.3647  0.2468  0.0170  40  THR D C   
15051 O O   . THR D 40  ? 1.2532 0.7615 1.4651 0.3632  0.2471  0.0234  40  THR D O   
15052 C CB  . THR D 40  ? 1.0926 0.6742 1.2983 0.3699  0.2164  0.0435  40  THR D CB  
15053 O OG1 . THR D 40  ? 0.9855 0.5595 1.1696 0.3586  0.2176  0.0296  40  THR D OG1 
15054 C CG2 . THR D 40  ? 1.3594 0.9278 1.5627 0.3675  0.2107  0.0559  40  THR D CG2 
15055 N N   . ALA D 41  ? 1.2727 0.7851 1.4652 0.3573  0.2582  -0.0040 41  ALA D N   
15056 C CA  . ALA D 41  ? 1.3727 0.8457 1.5509 0.3462  0.2705  -0.0232 41  ALA D CA  
15057 C C   . ALA D 41  ? 1.2655 0.7251 1.4218 0.3326  0.2619  -0.0279 41  ALA D C   
15058 O O   . ALA D 41  ? 1.3311 0.7577 1.4737 0.3215  0.2703  -0.0459 41  ALA D O   
15059 C CB  . ALA D 41  ? 1.4995 0.9611 1.6673 0.3447  0.2881  -0.0453 41  ALA D CB  
15060 N N   . TYR D 42  ? 1.2691 0.7531 1.4228 0.3331  0.2455  -0.0128 42  TYR D N   
15061 C CA  . TYR D 42  ? 1.2699 0.7448 1.4067 0.3220  0.2370  -0.0150 42  TYR D CA  
15062 C C   . TYR D 42  ? 1.2210 0.7029 1.3685 0.3217  0.2253  0.0042  42  TYR D C   
15063 O O   . TYR D 42  ? 1.2028 0.6900 1.3414 0.3160  0.2153  0.0085  42  TYR D O   
15064 C CB  . TYR D 42  ? 1.1459 0.6398 1.2658 0.3217  0.2304  -0.0164 42  TYR D CB  
15065 C CG  . TYR D 42  ? 1.2615 0.7501 1.3660 0.3191  0.2424  -0.0352 42  TYR D CG  
15066 C CD1 . TYR D 42  ? 1.3704 0.8764 1.4881 0.3312  0.2508  -0.0326 42  TYR D CD1 
15067 C CD2 . TYR D 42  ? 1.1604 0.6319 1.2364 0.3008  0.2428  -0.0558 42  TYR D CD2 
15068 C CE1 . TYR D 42  ? 1.3123 0.8110 1.4168 0.3300  0.2663  -0.0497 42  TYR D CE1 
15069 C CE2 . TYR D 42  ? 1.2397 0.7062 1.2962 0.2970  0.2545  -0.0732 42  TYR D CE2 
15070 C CZ  . TYR D 42  ? 1.2425 0.7220 1.3134 0.3118  0.2678  -0.0700 42  TYR D CZ  
15071 O OH  . TYR D 42  ? 1.1721 0.6467 1.2241 0.3082  0.2824  -0.0867 42  TYR D OH  
15072 N N   . SER D 43  ? 1.3453 0.8258 1.5110 0.3284  0.2279  0.0161  43  SER D N   
15073 C CA  . SER D 43  ? 1.2246 0.7089 1.3981 0.3288  0.2203  0.0352  43  SER D CA  
15074 C C   . SER D 43  ? 1.2041 0.7200 1.3696 0.3311  0.2046  0.0480  43  SER D C   
15075 O O   . SER D 43  ? 1.2864 0.8281 1.4546 0.3406  0.1990  0.0550  43  SER D O   
15076 C CB  . SER D 43  ? 1.1934 0.6459 1.3666 0.3159  0.2259  0.0278  43  SER D CB  
15077 O OG  . SER D 43  ? 1.4634 0.9185 1.6449 0.3161  0.2218  0.0466  43  SER D OG  
15078 N N   . LEU D 44  ? 1.2215 0.7354 1.3792 0.3225  0.1983  0.0502  44  LEU D N   
15079 C CA  . LEU D 44  ? 1.1309 0.6718 1.2806 0.3242  0.1850  0.0612  44  LEU D CA  
15080 C C   . LEU D 44  ? 1.2887 0.8299 1.4247 0.3182  0.1827  0.0469  44  LEU D C   
15081 O O   . LEU D 44  ? 1.2362 0.7605 1.3672 0.3085  0.1835  0.0390  44  LEU D O   
15082 C CB  . LEU D 44  ? 1.1451 0.6830 1.2966 0.3196  0.1819  0.0735  44  LEU D CB  
15083 C CG  . LEU D 44  ? 0.9688 0.5019 1.1302 0.3253  0.1862  0.0899  44  LEU D CG  
15084 C CD1 . LEU D 44  ? 1.0137 0.5488 1.1737 0.3215  0.1841  0.1028  44  LEU D CD1 
15085 C CD2 . LEU D 44  ? 0.9650 0.5193 1.1276 0.3390  0.1814  0.1014  44  LEU D CD2 
15086 N N   . PRO D 45  ? 1.2824 0.8410 1.4129 0.3236  0.1807  0.0431  45  PRO D N   
15087 C CA  . PRO D 45  ? 1.2732 0.8326 1.3867 0.3158  0.1788  0.0295  45  PRO D CA  
15088 C C   . PRO D 45  ? 1.1989 0.7669 1.3002 0.3015  0.1650  0.0292  45  PRO D C   
15089 O O   . PRO D 45  ? 1.2934 0.8532 1.3818 0.2874  0.1625  0.0156  45  PRO D O   
15090 C CB  . PRO D 45  ? 1.2963 0.8817 1.4110 0.3253  0.1757  0.0344  45  PRO D CB  
15091 C CG  . PRO D 45  ? 1.2365 0.8283 1.3700 0.3359  0.1804  0.0414  45  PRO D CG  
15092 C CD  . PRO D 45  ? 1.2451 0.8270 1.3853 0.3347  0.1783  0.0517  45  PRO D CD  
15093 N N   . VAL D 46  ? 1.1262 0.7103 1.2313 0.3058  0.1566  0.0439  46  VAL D N   
15094 C CA  . VAL D 46  ? 1.2783 0.8728 1.3752 0.2943  0.1446  0.0441  46  VAL D CA  
15095 C C   . VAL D 46  ? 1.2478 0.8251 1.3494 0.2820  0.1453  0.0386  46  VAL D C   
15096 O O   . VAL D 46  ? 1.1264 0.7054 1.2188 0.2683  0.1371  0.0289  46  VAL D O   
15097 C CB  . VAL D 46  ? 1.1877 0.8005 1.2876 0.3016  0.1380  0.0594  46  VAL D CB  
15098 C CG1 . VAL D 46  ? 0.8415 0.4650 0.9353 0.2909  0.1273  0.0588  46  VAL D CG1 
15099 C CG2 . VAL D 46  ? 1.1119 0.7418 1.2097 0.3126  0.1364  0.0637  46  VAL D CG2 
15100 N N   . ILE D 47  ? 1.1425 0.7035 1.2591 0.2865  0.1545  0.0454  47  ILE D N   
15101 C CA  . ILE D 47  ? 1.0825 0.6264 1.2085 0.2738  0.1564  0.0402  47  ILE D CA  
15102 C C   . ILE D 47  ? 1.0751 0.6011 1.1928 0.2624  0.1591  0.0195  47  ILE D C   
15103 O O   . ILE D 47  ? 1.2146 0.7372 1.3306 0.2462  0.1519  0.0092  47  ILE D O   
15104 C CB  . ILE D 47  ? 1.0145 0.5426 1.1589 0.2818  0.1681  0.0541  47  ILE D CB  
15105 C CG1 . ILE D 47  ? 1.0112 0.5574 1.1585 0.2890  0.1644  0.0729  47  ILE D CG1 
15106 C CG2 . ILE D 47  ? 1.0910 0.5964 1.2487 0.2673  0.1733  0.0459  47  ILE D CG2 
15107 C CD1 . ILE D 47  ? 1.1833 0.7255 1.3371 0.3000  0.1725  0.0895  47  ILE D CD1 
15108 N N   . PHE D 48  ? 1.1435 0.6590 1.2560 0.2707  0.1691  0.0129  48  PHE D N   
15109 C CA  . PHE D 48  ? 1.2059 0.7023 1.3064 0.2607  0.1743  -0.0085 48  PHE D CA  
15110 C C   . PHE D 48  ? 1.1918 0.7033 1.2675 0.2484  0.1612  -0.0196 48  PHE D C   
15111 O O   . PHE D 48  ? 1.3248 0.8236 1.3868 0.2337  0.1588  -0.0370 48  PHE D O   
15112 C CB  . PHE D 48  ? 1.1807 0.6644 1.2837 0.2747  0.1903  -0.0118 48  PHE D CB  
15113 C CG  . PHE D 48  ? 1.2209 0.6823 1.3090 0.2651  0.1990  -0.0356 48  PHE D CG  
15114 C CD1 . PHE D 48  ? 1.1810 0.6135 1.2726 0.2533  0.2045  -0.0487 48  PHE D CD1 
15115 C CD2 . PHE D 48  ? 1.1922 0.6608 1.2615 0.2667  0.2022  -0.0457 48  PHE D CD2 
15116 C CE1 . PHE D 48  ? 1.1404 0.5507 1.2140 0.2433  0.2124  -0.0731 48  PHE D CE1 
15117 C CE2 . PHE D 48  ? 1.1700 0.6168 1.2208 0.2577  0.2116  -0.0685 48  PHE D CE2 
15118 C CZ  . PHE D 48  ? 1.2442 0.6616 1.2958 0.2461  0.2163  -0.0828 48  PHE D CZ  
15119 N N   . ALA D 49  ? 1.1779 0.7153 1.2468 0.2540  0.1524  -0.0098 49  ALA D N   
15120 C CA  . ALA D 49  ? 1.1206 0.6714 1.1665 0.2437  0.1406  -0.0168 49  ALA D CA  
15121 C C   . ALA D 49  ? 1.1594 0.7176 1.2067 0.2301  0.1250  -0.0159 49  ALA D C   
15122 O O   . ALA D 49  ? 1.2482 0.8045 1.2777 0.2164  0.1162  -0.0279 49  ALA D O   
15123 C CB  . ALA D 49  ? 1.0418 0.6155 1.0839 0.2536  0.1374  -0.0059 49  ALA D CB  
15124 N N   . ALA D 50  ? 1.1628 0.7301 1.2314 0.2340  0.1217  -0.0014 50  ALA D N   
15125 C CA  . ALA D 50  ? 1.0870 0.6648 1.1644 0.2229  0.1083  0.0016  50  ALA D CA  
15126 C C   . ALA D 50  ? 1.2049 0.7663 1.2924 0.2084  0.1079  -0.0096 50  ALA D C   
15127 O O   . ALA D 50  ? 1.4259 0.9946 1.5099 0.1942  0.0938  -0.0165 50  ALA D O   
15128 C CB  . ALA D 50  ? 0.8962 0.4880 0.9931 0.2323  0.1086  0.0200  50  ALA D CB  
15129 N N   . THR D 51  ? 1.1468 0.6863 1.2482 0.2117  0.1226  -0.0109 51  THR D N   
15130 C CA  . THR D 51  ? 1.2030 0.7236 1.3179 0.1973  0.1244  -0.0217 51  THR D CA  
15131 C C   . THR D 51  ? 1.2060 0.6994 1.3052 0.1907  0.1325  -0.0429 51  THR D C   
15132 O O   . THR D 51  ? 1.2743 0.7547 1.3756 0.1736  0.1286  -0.0582 51  THR D O   
15133 C CB  . THR D 51  ? 1.3879 0.8982 1.5317 0.2044  0.1374  -0.0076 51  THR D CB  
15134 O OG1 . THR D 51  ? 1.2101 0.7025 1.3521 0.2199  0.1540  -0.0039 51  THR D OG1 
15135 C CG2 . THR D 51  ? 1.1114 0.6460 1.2690 0.2114  0.1327  0.0127  51  THR D CG2 
15136 N N   . GLY D 52  ? 1.2206 0.7057 1.3066 0.2038  0.1446  -0.0445 52  GLY D N   
15137 C CA  . GLY D 52  ? 1.2803 0.7376 1.3525 0.2006  0.1569  -0.0644 52  GLY D CA  
15138 C C   . GLY D 52  ? 1.3127 0.7403 1.4090 0.2038  0.1738  -0.0646 52  GLY D C   
15139 O O   . GLY D 52  ? 1.3076 0.7065 1.3981 0.1970  0.1842  -0.0838 52  GLY D O   
15140 N N   . LYS D 53  ? 1.3248 0.7574 1.4469 0.2145  0.1778  -0.0431 53  LYS D N   
15141 C CA  . LYS D 53  ? 1.4451 0.8501 1.5916 0.2190  0.1942  -0.0377 53  LYS D CA  
15142 C C   . LYS D 53  ? 1.3800 0.7852 1.5344 0.2437  0.2066  -0.0191 53  LYS D C   
15143 O O   . LYS D 53  ? 1.2384 0.6712 1.3880 0.2549  0.1992  -0.0042 53  LYS D O   
15144 C CB  . LYS D 53  ? 1.4806 0.8908 1.6509 0.2097  0.1890  -0.0262 53  LYS D CB  
15145 C CG  . LYS D 53  ? 1.5306 0.9516 1.6987 0.1860  0.1718  -0.0406 53  LYS D CG  
15146 C CD  . LYS D 53  ? 1.8204 1.2107 1.9886 0.1675  0.1759  -0.0657 53  LYS D CD  
15147 C CE  . LYS D 53  ? 1.7358 1.1408 1.8944 0.1445  0.1549  -0.0826 53  LYS D CE  
15148 N NZ  . LYS D 53  ? 1.5122 0.8889 1.6543 0.1285  0.1571  -0.1120 53  LYS D NZ  
15149 N N   . LYS D 54  ? 1.4083 0.7828 1.5757 0.2520  0.2249  -0.0199 54  LYS D N   
15150 C CA  . LYS D 54  ? 1.3483 0.7273 1.5246 0.2744  0.2336  -0.0013 54  LYS D CA  
15151 C C   . LYS D 54  ? 1.3899 0.7721 1.5842 0.2763  0.2343  0.0207  54  LYS D C   
15152 O O   . LYS D 54  ? 1.3539 0.7098 1.5622 0.2659  0.2423  0.0172  54  LYS D O   
15153 C CB  . LYS D 54  ? 1.1427 0.5046 1.3175 0.2784  0.2461  -0.0146 54  LYS D CB  
15154 C CG  . LYS D 54  ? 1.3782 0.7403 1.5320 0.2786  0.2479  -0.0343 54  LYS D CG  
15155 C CD  . LYS D 54  ? 1.2473 0.5981 1.4016 0.2848  0.2616  -0.0455 54  LYS D CD  
15156 C CE  . LYS D 54  ? 1.3428 0.7185 1.4863 0.2956  0.2609  -0.0461 54  LYS D CE  
15157 N NZ  . LYS D 54  ? 1.6010 0.9633 1.7450 0.2999  0.2767  -0.0606 54  LYS D NZ  
15158 N N   . ILE D 55  ? 1.4180 0.8310 1.6106 0.2887  0.2265  0.0427  55  ILE D N   
15159 C CA  . ILE D 55  ? 1.2463 0.6636 1.4494 0.2924  0.2279  0.0653  55  ILE D CA  
15160 C C   . ILE D 55  ? 1.3465 0.7610 1.5552 0.3045  0.2346  0.0746  55  ILE D C   
15161 O O   . ILE D 55  ? 1.4113 0.8467 1.6138 0.3162  0.2292  0.0775  55  ILE D O   
15162 C CB  . ILE D 55  ? 1.0389 0.4891 1.2329 0.2979  0.2157  0.0816  55  ILE D CB  
15163 C CG1 . ILE D 55  ? 1.0816 0.5357 1.2731 0.2875  0.2091  0.0732  55  ILE D CG1 
15164 C CG2 . ILE D 55  ? 1.1085 0.5623 1.3079 0.3030  0.2189  0.1049  55  ILE D CG2 
15165 C CD1 . ILE D 55  ? 1.1611 0.5906 1.3706 0.2728  0.2162  0.0685  55  ILE D CD1 
15166 N N   . THR D 56  ? 1.1878 0.5761 1.4108 0.3017  0.2467  0.0792  56  THR D N   
15167 C CA  . THR D 56  ? 1.1761 0.5574 1.4072 0.3135  0.2544  0.0886  56  THR D CA  
15168 C C   . THR D 56  ? 1.2964 0.6799 1.5335 0.3212  0.2570  0.1160  56  THR D C   
15169 O O   . THR D 56  ? 1.3704 0.7581 1.6113 0.3351  0.2587  0.1286  56  THR D O   
15170 C CB  . THR D 56  ? 1.4280 0.7724 1.6698 0.3058  0.2688  0.0699  56  THR D CB  
15171 O OG1 . THR D 56  ? 1.4794 0.7979 1.7323 0.2913  0.2766  0.0690  56  THR D OG1 
15172 C CG2 . THR D 56  ? 1.3887 0.7280 1.6204 0.2996  0.2684  0.0423  56  THR D CG2 
15173 N N   . ASN D 57  ? 1.2174 0.5974 1.4561 0.3129  0.2585  0.1257  57  ASN D N   
15174 C CA  . ASN D 57  ? 1.2101 0.5902 1.4512 0.3200  0.2635  0.1522  57  ASN D CA  
15175 C C   . ASN D 57  ? 1.2398 0.6418 1.4694 0.3191  0.2564  0.1654  57  ASN D C   
15176 O O   . ASN D 57  ? 1.3768 0.7906 1.6014 0.3110  0.2487  0.1533  57  ASN D O   
15177 C CB  . ASN D 57  ? 1.4194 0.7629 1.6794 0.3112  0.2809  0.1541  57  ASN D CB  
15178 C CG  . ASN D 57  ? 1.3585 0.6831 1.6299 0.2908  0.2859  0.1366  57  ASN D CG  
15179 O OD1 . ASN D 57  ? 1.6063 0.9197 1.8794 0.2820  0.2847  0.1117  57  ASN D OD1 
15180 N ND2 . ASN D 57  ? 1.2223 0.5418 1.5028 0.2826  0.2924  0.1487  57  ASN D ND2 
15181 N N   . VAL D 58  ? 1.2599 0.6666 1.4845 0.3281  0.2599  0.1904  58  VAL D N   
15182 C CA  . VAL D 58  ? 1.3824 0.8078 1.5939 0.3287  0.2561  0.2041  58  VAL D CA  
15183 C C   . VAL D 58  ? 1.4246 0.8390 1.6488 0.3118  0.2634  0.1968  58  VAL D C   
15184 O O   . VAL D 58  ? 1.4204 0.8534 1.6370 0.3089  0.2569  0.1956  58  VAL D O   
15185 C CB  . VAL D 58  ? 1.2263 0.6526 1.4283 0.3418  0.2617  0.2327  58  VAL D CB  
15186 C CG1 . VAL D 58  ? 1.1599 0.5966 1.3496 0.3404  0.2644  0.2466  58  VAL D CG1 
15187 C CG2 . VAL D 58  ? 1.1649 0.6108 1.3536 0.3593  0.2493  0.2403  58  VAL D CG2 
15188 N N   . GLY D 59  ? 1.2750 0.6594 1.5208 0.3006  0.2769  0.1915  59  GLY D N   
15189 C CA  . GLY D 59  ? 1.3225 0.6950 1.5873 0.2831  0.2840  0.1836  59  GLY D CA  
15190 C C   . GLY D 59  ? 1.3477 0.7302 1.6130 0.2743  0.2716  0.1601  59  GLY D C   
15191 O O   . GLY D 59  ? 1.2396 0.6320 1.5119 0.2663  0.2695  0.1588  59  GLY D O   
15192 N N   . GLU D 60  ? 1.2633 0.6436 1.5216 0.2765  0.2641  0.1421  60  GLU D N   
15193 C CA  . GLU D 60  ? 1.2669 0.6550 1.5214 0.2697  0.2529  0.1200  60  GLU D CA  
15194 C C   . GLU D 60  ? 1.2706 0.6943 1.5057 0.2788  0.2388  0.1266  60  GLU D C   
15195 O O   . GLU D 60  ? 1.1454 0.5789 1.3814 0.2722  0.2313  0.1170  60  GLU D O   
15196 C CB  . GLU D 60  ? 1.1873 0.5620 1.4368 0.2709  0.2520  0.1003  60  GLU D CB  
15197 C CG  . GLU D 60  ? 1.1590 0.4956 1.4270 0.2576  0.2647  0.0854  60  GLU D CG  
15198 C CD  . GLU D 60  ? 1.3861 0.7071 1.6472 0.2587  0.2666  0.0643  60  GLU D CD  
15199 O OE1 . GLU D 60  ? 1.5362 0.8770 1.7799 0.2679  0.2575  0.0588  60  GLU D OE1 
15200 O OE2 . GLU D 60  ? 1.2972 0.5856 1.5709 0.2499  0.2784  0.0528  60  GLU D OE2 
15201 N N   . LEU D 61  ? 1.2765 0.7184 1.4952 0.2938  0.2352  0.1428  61  LEU D N   
15202 C CA  . LEU D 61  ? 1.1578 0.6316 1.3576 0.3022  0.2227  0.1493  61  LEU D CA  
15203 C C   . LEU D 61  ? 1.2302 0.7112 1.4331 0.2976  0.2259  0.1598  61  LEU D C   
15204 O O   . LEU D 61  ? 1.2801 0.7818 1.4742 0.2980  0.2166  0.1569  61  LEU D O   
15205 C CB  . LEU D 61  ? 1.1328 0.6196 1.3181 0.3182  0.2196  0.1650  61  LEU D CB  
15206 C CG  . LEU D 61  ? 1.1386 0.6566 1.3038 0.3271  0.2061  0.1694  61  LEU D CG  
15207 C CD1 . LEU D 61  ? 1.2202 0.7511 1.3813 0.3276  0.1948  0.1518  61  LEU D CD1 
15208 C CD2 . LEU D 61  ? 1.0622 0.5889 1.2154 0.3418  0.2051  0.1895  61  LEU D CD2 
15209 N N   . GLU D 62  ? 1.2409 0.7043 1.4580 0.2932  0.2405  0.1721  62  GLU D N   
15210 C CA  . GLU D 62  ? 1.2114 0.6795 1.4364 0.2885  0.2476  0.1828  62  GLU D CA  
15211 C C   . GLU D 62  ? 1.2354 0.7034 1.4809 0.2747  0.2438  0.1662  62  GLU D C   
15212 O O   . GLU D 62  ? 1.2667 0.7526 1.5132 0.2743  0.2405  0.1686  62  GLU D O   
15213 C CB  . GLU D 62  ? 1.1628 0.6088 1.4021 0.2858  0.2667  0.1995  62  GLU D CB  
15214 C CG  . GLU D 62  ? 1.2444 0.6980 1.4851 0.2863  0.2774  0.2171  62  GLU D CG  
15215 C CD  . GLU D 62  ? 1.3557 0.7864 1.6123 0.2824  0.2986  0.2343  62  GLU D CD  
15216 O OE1 . GLU D 62  ? 1.2595 0.6665 1.5418 0.2704  0.3059  0.2262  62  GLU D OE1 
15217 O OE2 . GLU D 62  ? 1.3477 0.7826 1.5900 0.2911  0.3087  0.2557  62  GLU D OE2 
15218 N N   . GLY D 63  ? 1.1792 0.6262 1.4412 0.2641  0.2444  0.1491  63  GLY D N   
15219 C CA  . GLY D 63  ? 1.1150 0.5612 1.3961 0.2494  0.2382  0.1313  63  GLY D CA  
15220 C C   . GLY D 63  ? 1.1735 0.6494 1.4345 0.2509  0.2187  0.1196  63  GLY D C   
15221 O O   . GLY D 63  ? 1.2812 0.7784 1.5499 0.2386  0.2077  0.1116  63  GLY D O   
15222 N N   . ALA D 64  ? 1.1047 0.5828 1.3423 0.2661  0.2144  0.1196  64  ALA D N   
15223 C CA  . ALA D 64  ? 1.0773 0.5814 1.2953 0.2683  0.1978  0.1100  64  ALA D CA  
15224 C C   . ALA D 64  ? 1.2396 0.7709 1.4527 0.2718  0.1924  0.1208  64  ALA D C   
15225 O O   . ALA D 64  ? 1.3288 0.8813 1.5321 0.2691  0.1787  0.1122  64  ALA D O   
15226 C CB  . ALA D 64  ? 1.1083 0.6134 1.3063 0.2827  0.1957  0.1100  64  ALA D CB  
15227 N N   . LEU D 65  ? 1.1682 0.6966 1.3878 0.2772  0.2044  0.1391  65  LEU D N   
15228 C CA  . LEU D 65  ? 1.2266 0.7781 1.4409 0.2808  0.2027  0.1485  65  LEU D CA  
15229 C C   . LEU D 65  ? 1.2776 0.8458 1.5112 0.2646  0.1943  0.1375  65  LEU D C   
15230 O O   . LEU D 65  ? 1.2633 0.8538 1.4903 0.2671  0.1868  0.1377  65  LEU D O   
15231 C CB  . LEU D 65  ? 1.2135 0.7569 1.4296 0.2868  0.2195  0.1690  65  LEU D CB  
15232 C CG  . LEU D 65  ? 1.0504 0.6017 1.2350 0.3005  0.2184  0.1807  65  LEU D CG  
15233 C CD1 . LEU D 65  ? 1.3277 0.8765 1.5081 0.3058  0.2339  0.2010  65  LEU D CD1 
15234 C CD2 . LEU D 65  ? 1.0168 0.5909 1.1795 0.3071  0.2031  0.1734  65  LEU D CD2 
15235 N N   . ASP D 66  ? 1.2787 0.8365 1.5365 0.2486  0.1949  0.1282  66  ASP D N   
15236 C CA  . ASP D 66  ? 1.2984 0.8743 1.5783 0.2325  0.1847  0.1185  66  ASP D CA  
15237 C C   . ASP D 66  ? 1.2299 0.8226 1.4935 0.2304  0.1643  0.1039  66  ASP D C   
15238 O O   . ASP D 66  ? 1.2917 0.9063 1.5668 0.2235  0.1536  0.1008  66  ASP D O   
15239 C CB  . ASP D 66  ? 1.2317 0.7922 1.5404 0.2144  0.1882  0.1101  66  ASP D CB  
15240 C CG  . ASP D 66  ? 1.3488 0.8993 1.6828 0.2123  0.2080  0.1256  66  ASP D CG  
15241 O OD1 . ASP D 66  ? 1.2679 0.8384 1.6184 0.2113  0.2115  0.1348  66  ASP D OD1 
15242 O OD2 . ASP D 66  ? 1.5856 1.1074 1.9239 0.2120  0.2215  0.1292  66  ASP D OD2 
15243 N N   . ILE D 67  ? 1.0909 0.6740 1.3294 0.2369  0.1601  0.0964  67  ILE D N   
15244 C CA  . ILE D 67  ? 0.9934 0.5899 1.2133 0.2357  0.1436  0.0843  67  ILE D CA  
15245 C C   . ILE D 67  ? 1.1085 0.7265 1.3177 0.2467  0.1397  0.0937  67  ILE D C   
15246 O O   . ILE D 67  ? 1.1326 0.7683 1.3411 0.2423  0.1269  0.0888  67  ILE D O   
15247 C CB  . ILE D 67  ? 1.0781 0.6583 1.2761 0.2413  0.1445  0.0756  67  ILE D CB  
15248 C CG1 . ILE D 67  ? 1.2346 0.7886 1.4424 0.2312  0.1513  0.0649  67  ILE D CG1 
15249 C CG2 . ILE D 67  ? 1.1654 0.7591 1.3427 0.2400  0.1300  0.0647  67  ILE D CG2 
15250 C CD1 . ILE D 67  ? 1.3980 0.9535 1.6199 0.2101  0.1412  0.0500  67  ILE D CD1 
15251 N N   . VAL D 68  ? 1.1756 0.7910 1.3759 0.2609  0.1507  0.1072  68  VAL D N   
15252 C CA  . VAL D 68  ? 1.1110 0.7435 1.2992 0.2711  0.1489  0.1146  68  VAL D CA  
15253 C C   . VAL D 68  ? 1.1407 0.7882 1.3506 0.2649  0.1492  0.1184  68  VAL D C   
15254 O O   . VAL D 68  ? 1.0755 0.7395 1.2828 0.2659  0.1405  0.1162  68  VAL D O   
15255 C CB  . VAL D 68  ? 1.0426 0.6683 1.2154 0.2862  0.1604  0.1282  68  VAL D CB  
15256 C CG1 . VAL D 68  ? 0.9143 0.5560 1.0725 0.2949  0.1587  0.1331  68  VAL D CG1 
15257 C CG2 . VAL D 68  ? 0.9712 0.5854 1.1283 0.2939  0.1594  0.1260  68  VAL D CG2 
15258 N N   . ARG D 69  ? 1.0235 0.6651 1.2579 0.2585  0.1600  0.1244  69  ARG D N   
15259 C CA  . ARG D 69  ? 1.0422 0.6994 1.3043 0.2524  0.1627  0.1287  69  ARG D CA  
15260 C C   . ARG D 69  ? 1.0674 0.7412 1.3456 0.2406  0.1447  0.1175  69  ARG D C   
15261 O O   . ARG D 69  ? 1.1543 0.8475 1.4439 0.2420  0.1404  0.1200  69  ARG D O   
15262 C CB  . ARG D 69  ? 1.0948 0.7412 1.3837 0.2452  0.1782  0.1362  69  ARG D CB  
15263 C CG  . ARG D 69  ? 1.1378 0.7694 1.4133 0.2571  0.1980  0.1519  69  ARG D CG  
15264 C CD  . ARG D 69  ? 1.2063 0.8254 1.5105 0.2485  0.2146  0.1603  69  ARG D CD  
15265 N NE  . ARG D 69  ? 1.1447 0.7361 1.4363 0.2532  0.2248  0.1666  69  ARG D NE  
15266 C CZ  . ARG D 69  ? 1.2032 0.7832 1.4723 0.2677  0.2383  0.1826  69  ARG D CZ  
15267 N NH1 . ARG D 69  ? 1.3235 0.9167 1.5767 0.2781  0.2438  0.1920  69  ARG D NH1 
15268 N NH2 . ARG D 69  ? 1.2052 0.7599 1.4667 0.2724  0.2463  0.1894  69  ARG D NH2 
15269 N N   . SER D 70  ? 0.8940 0.5596 1.1725 0.2293  0.1345  0.1054  70  SER D N   
15270 C CA  . SER D 70  ? 1.0163 0.6967 1.3052 0.2171  0.1154  0.0947  70  SER D CA  
15271 C C   . SER D 70  ? 1.0532 0.7461 1.3195 0.2242  0.1022  0.0925  70  SER D C   
15272 O O   . SER D 70  ? 1.0896 0.8015 1.3693 0.2197  0.0893  0.0919  70  SER D O   
15273 C CB  . SER D 70  ? 0.9576 0.6223 1.2428 0.2039  0.1088  0.0805  70  SER D CB  
15274 O OG  . SER D 70  ? 1.2043 0.8547 1.4548 0.2105  0.1073  0.0737  70  SER D OG  
15275 N N   . LEU D 71  ? 0.9562 0.6391 1.1910 0.2352  0.1054  0.0922  71  LEU D N   
15276 C CA  . LEU D 71  ? 1.0167 0.7090 1.2307 0.2410  0.0949  0.0902  71  LEU D CA  
15277 C C   . LEU D 71  ? 1.1246 0.8311 1.3454 0.2505  0.0983  0.0998  71  LEU D C   
15278 O O   . LEU D 71  ? 1.1161 0.8318 1.3282 0.2531  0.0887  0.0988  71  LEU D O   
15279 C CB  . LEU D 71  ? 1.0166 0.6957 1.1997 0.2486  0.0977  0.0861  71  LEU D CB  
15280 C CG  . LEU D 71  ? 1.0141 0.6839 1.1809 0.2410  0.0896  0.0733  71  LEU D CG  
15281 C CD1 . LEU D 71  ? 1.1025 0.7616 1.2833 0.2281  0.0897  0.0657  71  LEU D CD1 
15282 C CD2 . LEU D 71  ? 0.9381 0.5965 1.0828 0.2505  0.0968  0.0716  71  LEU D CD2 
15283 N N   . ILE D 72  ? 1.0839 0.7907 1.3191 0.2555  0.1131  0.1091  72  ILE D N   
15284 C CA  . ILE D 72  ? 0.9890 0.7073 1.2297 0.2645  0.1190  0.1165  72  ILE D CA  
15285 C C   . ILE D 72  ? 0.9312 0.6672 1.2096 0.2583  0.1161  0.1198  72  ILE D C   
15286 O O   . ILE D 72  ? 0.9392 0.6772 1.2435 0.2540  0.1263  0.1248  72  ILE D O   
15287 C CB  . ILE D 72  ? 0.9655 0.6752 1.1955 0.2749  0.1378  0.1249  72  ILE D CB  
15288 C CG1 . ILE D 72  ? 1.0794 0.7767 1.2743 0.2826  0.1375  0.1225  72  ILE D CG1 
15289 C CG2 . ILE D 72  ? 0.8454 0.5658 1.0815 0.2830  0.1457  0.1302  72  ILE D CG2 
15290 C CD1 . ILE D 72  ? 1.0046 0.6917 1.1861 0.2914  0.1528  0.1314  72  ILE D CD1 
15291 N N   . VAL D 73  ? 0.8945 0.6439 1.1779 0.2581  0.1022  0.1182  73  VAL D N   
15292 C CA  . VAL D 73  ? 0.8468 0.6168 1.1679 0.2544  0.0963  0.1225  73  VAL D CA  
15293 C C   . VAL D 73  ? 0.9163 0.6923 1.2358 0.2672  0.1011  0.1275  73  VAL D C   
15294 O O   . VAL D 73  ? 0.9992 0.7733 1.2989 0.2707  0.0908  0.1249  73  VAL D O   
15295 C CB  . VAL D 73  ? 0.8602 0.6397 1.1869 0.2431  0.0730  0.1167  73  VAL D CB  
15296 C CG1 . VAL D 73  ? 0.8693 0.6740 1.2388 0.2402  0.0643  0.1229  73  VAL D CG1 
15297 C CG2 . VAL D 73  ? 0.8724 0.6409 1.1938 0.2301  0.0692  0.1081  73  VAL D CG2 
15298 N N   . GLU D 74  ? 0.7631 0.5440 1.1021 0.2740  0.1187  0.1343  74  GLU D N   
15299 C CA  . GLU D 74  ? 0.7612 0.5441 1.0975 0.2864  0.1267  0.1372  74  GLU D CA  
15300 C C   . GLU D 74  ? 0.9418 0.7433 1.3099 0.2881  0.1157  0.1412  74  GLU D C   
15301 O O   . GLU D 74  ? 0.9774 0.7915 1.3792 0.2931  0.1266  0.1473  74  GLU D O   
15302 C CB  . GLU D 74  ? 0.9634 0.7426 1.3038 0.2938  0.1518  0.1421  74  GLU D CB  
15303 C CG  . GLU D 74  ? 0.8933 0.6532 1.1961 0.2956  0.1617  0.1404  74  GLU D CG  
15304 C CD  . GLU D 74  ? 1.1637 0.9180 1.4604 0.3040  0.1860  0.1458  74  GLU D CD  
15305 O OE1 . GLU D 74  ? 1.3199 1.0734 1.6070 0.3135  0.1940  0.1443  74  GLU D OE1 
15306 O OE2 . GLU D 74  ? 1.1620 0.9111 1.4621 0.3009  0.1980  0.1515  74  GLU D OE2 
15307 N N   . GLU D 75  ? 0.9504 0.7533 1.3072 0.2847  0.0951  0.1386  75  GLU D N   
15308 C CA  . GLU D 75  ? 0.8934 0.7123 1.2750 0.2871  0.0814  0.1443  75  GLU D CA  
15309 C C   . GLU D 75  ? 0.8320 0.6377 1.1807 0.2931  0.0751  0.1421  75  GLU D C   
15310 O O   . GLU D 75  ? 0.9044 0.6970 1.2178 0.2882  0.0686  0.1356  75  GLU D O   
15311 C CB  . GLU D 75  ? 0.8611 0.6960 1.2616 0.2743  0.0595  0.1448  75  GLU D CB  
15312 C CG  . GLU D 75  ? 0.8369 0.6884 1.2799 0.2671  0.0645  0.1474  75  GLU D CG  
15313 C CD  . GLU D 75  ? 1.0988 0.9678 1.5623 0.2528  0.0410  0.1462  75  GLU D CD  
15314 O OE1 . GLU D 75  ? 1.1058 0.9809 1.5598 0.2517  0.0198  0.1474  75  GLU D OE1 
15315 O OE2 . GLU D 75  ? 1.1841 1.0600 1.6720 0.2419  0.0439  0.1439  75  GLU D OE2 
15316 N N   . GLU D 76  ? 0.8961 0.7042 1.2580 0.3037  0.0785  0.1475  76  GLU D N   
15317 C CA  . GLU D 76  ? 0.9627 0.7560 1.2965 0.3090  0.0751  0.1458  76  GLU D CA  
15318 C C   . GLU D 76  ? 1.0240 0.8216 1.3516 0.3040  0.0521  0.1502  76  GLU D C   
15319 O O   . GLU D 76  ? 0.9539 0.7593 1.3020 0.3100  0.0446  0.1595  76  GLU D O   
15320 C CB  . GLU D 76  ? 1.1073 0.8962 1.4553 0.3224  0.0902  0.1486  76  GLU D CB  
15321 C CG  . GLU D 76  ? 1.0854 0.8685 1.4285 0.3258  0.1133  0.1426  76  GLU D CG  
15322 C CD  . GLU D 76  ? 1.1615 0.9328 1.4852 0.3302  0.1258  0.1347  76  GLU D CD  
15323 O OE1 . GLU D 76  ? 1.2804 1.0484 1.6054 0.3327  0.1192  0.1356  76  GLU D OE1 
15324 O OE2 . GLU D 76  ? 1.1259 0.8896 1.4331 0.3316  0.1427  0.1280  76  GLU D OE2 
15325 N N   . MET D 77  ? 0.9072 0.6985 1.2048 0.2936  0.0419  0.1439  77  MET D N   
15326 C CA  . MET D 77  ? 0.8855 0.6773 1.1653 0.2872  0.0220  0.1460  77  MET D CA  
15327 C C   . MET D 77  ? 0.9086 0.6822 1.1455 0.2817  0.0250  0.1356  77  MET D C   
15328 O O   . MET D 77  ? 0.8804 0.6492 1.1100 0.2786  0.0343  0.1278  77  MET D O   
15329 C CB  . MET D 77  ? 0.8656 0.6763 1.1642 0.2771  0.0044  0.1482  77  MET D CB  
15330 C CG  . MET D 77  ? 0.8997 0.7327 1.2425 0.2822  -0.0042 0.1605  77  MET D CG  
15331 S SD  . MET D 77  ? 1.1035 0.9370 1.4425 0.2905  -0.0190 0.1743  77  MET D SD  
15332 C CE  . MET D 77  ? 1.0340 0.8866 1.3708 0.2774  -0.0498 0.1778  77  MET D CE  
15333 N N   . LEU D 78  ? 0.9884 0.7523 1.1992 0.2811  0.0185  0.1365  78  LEU D N   
15334 C CA  . LEU D 78  ? 0.9470 0.6960 1.1219 0.2767  0.0229  0.1271  78  LEU D CA  
15335 C C   . LEU D 78  ? 0.9319 0.6807 1.0960 0.2675  0.0216  0.1179  78  LEU D C   
15336 O O   . LEU D 78  ? 1.0829 0.8227 1.2339 0.2681  0.0328  0.1104  78  LEU D O   
15337 C CB  . LEU D 78  ? 1.0562 0.7975 1.2073 0.2748  0.0147  0.1308  78  LEU D CB  
15338 C CG  . LEU D 78  ? 0.7912 0.5195 0.9088 0.2698  0.0200  0.1217  78  LEU D CG  
15339 C CD1 . LEU D 78  ? 0.7797 0.4996 0.8949 0.2754  0.0355  0.1154  78  LEU D CD1 
15340 C CD2 . LEU D 78  ? 0.8075 0.5290 0.9039 0.2672  0.0132  0.1274  78  LEU D CD2 
15341 N N   . ASP D 79  ? 0.9100 0.6683 1.0796 0.2589  0.0078  0.1183  79  ASP D N   
15342 C CA  . ASP D 79  ? 1.0074 0.7623 1.1674 0.2493  0.0071  0.1080  79  ASP D CA  
15343 C C   . ASP D 79  ? 0.9271 0.6803 1.1039 0.2514  0.0215  0.1045  79  ASP D C   
15344 O O   . ASP D 79  ? 1.0171 0.7603 1.1809 0.2473  0.0275  0.0962  79  ASP D O   
15345 C CB  . ASP D 79  ? 0.9371 0.7036 1.1036 0.2385  -0.0115 0.1079  79  ASP D CB  
15346 C CG  . ASP D 79  ? 1.0522 0.8378 1.2610 0.2383  -0.0167 0.1144  79  ASP D CG  
15347 O OD1 . ASP D 79  ? 1.2471 1.0421 1.4778 0.2477  -0.0162 0.1253  79  ASP D OD1 
15348 O OD2 . ASP D 79  ? 1.0114 0.8022 1.2336 0.2286  -0.0203 0.1083  79  ASP D OD2 
15349 N N   . LYS D 80  ? 0.9393 0.7012 1.1445 0.2585  0.0285  0.1116  80  LYS D N   
15350 C CA  . LYS D 80  ? 0.9390 0.6993 1.1591 0.2609  0.0437  0.1107  80  LYS D CA  
15351 C C   . LYS D 80  ? 0.8889 0.6354 1.0865 0.2692  0.0581  0.1079  80  LYS D C   
15352 O O   . LYS D 80  ? 1.0217 0.7606 1.2136 0.2692  0.0679  0.1048  80  LYS D O   
15353 C CB  . LYS D 80  ? 0.8702 0.6453 1.1283 0.2658  0.0482  0.1193  80  LYS D CB  
15354 C CG  . LYS D 80  ? 0.8691 0.6635 1.1552 0.2603  0.0311  0.1248  80  LYS D CG  
15355 C CD  . LYS D 80  ? 0.9841 0.7871 1.2903 0.2478  0.0252  0.1212  80  LYS D CD  
15356 C CE  . LYS D 80  ? 1.0213 0.8470 1.3558 0.2417  0.0050  0.1263  80  LYS D CE  
15357 N NZ  . LYS D 80  ? 1.1594 0.9848 1.4788 0.2267  -0.0127 0.1175  80  LYS D NZ  
15358 N N   . LEU D 81  ? 0.8164 0.5597 1.0023 0.2760  0.0590  0.1095  81  LEU D N   
15359 C CA  . LEU D 81  ? 0.9277 0.6599 1.0916 0.2824  0.0699  0.1054  81  LEU D CA  
15360 C C   . LEU D 81  ? 1.0372 0.7615 1.1782 0.2775  0.0678  0.0984  81  LEU D C   
15361 O O   . LEU D 81  ? 1.0840 0.8027 1.2169 0.2806  0.0768  0.0960  81  LEU D O   
15362 C CB  . LEU D 81  ? 0.7863 0.5153 0.9421 0.2874  0.0691  0.1063  81  LEU D CB  
15363 C CG  . LEU D 81  ? 0.9508 0.6707 1.0859 0.2921  0.0778  0.1005  81  LEU D CG  
15364 C CD1 . LEU D 81  ? 0.9045 0.6212 1.0444 0.2991  0.0843  0.1014  81  LEU D CD1 
15365 C CD2 . LEU D 81  ? 1.0411 0.7556 1.1540 0.2875  0.0723  0.0953  81  LEU D CD2 
15366 N N   . LEU D 82  ? 1.0423 0.7661 1.1728 0.2708  0.0569  0.0961  82  LEU D N   
15367 C CA  . LEU D 82  ? 0.9151 0.6307 1.0239 0.2669  0.0572  0.0886  82  LEU D CA  
15368 C C   . LEU D 82  ? 1.0183 0.7299 1.1324 0.2638  0.0617  0.0850  82  LEU D C   
15369 O O   . LEU D 82  ? 1.0520 0.7561 1.1550 0.2664  0.0688  0.0809  82  LEU D O   
15370 C CB  . LEU D 82  ? 0.9680 0.6829 1.0623 0.2596  0.0462  0.0868  82  LEU D CB  
15371 C CG  . LEU D 82  ? 0.9775 0.6932 1.0657 0.2622  0.0424  0.0922  82  LEU D CG  
15372 C CD1 . LEU D 82  ? 0.8817 0.5975 0.9558 0.2549  0.0306  0.0937  82  LEU D CD1 
15373 C CD2 . LEU D 82  ? 0.8414 0.5510 0.9167 0.2665  0.0512  0.0889  82  LEU D CD2 
15374 N N   . ASN D 83  ? 1.0388 0.7556 1.1728 0.2585  0.0580  0.0870  83  ASN D N   
15375 C CA  . ASN D 83  ? 0.9437 0.6545 1.0865 0.2544  0.0636  0.0840  83  ASN D CA  
15376 C C   . ASN D 83  ? 1.0092 0.7164 1.1570 0.2637  0.0782  0.0892  83  ASN D C   
15377 O O   . ASN D 83  ? 0.9975 0.6943 1.1403 0.2649  0.0860  0.0875  83  ASN D O   
15378 C CB  . ASN D 83  ? 1.0693 0.7890 1.2371 0.2454  0.0561  0.0852  83  ASN D CB  
15379 C CG  . ASN D 83  ? 1.0205 0.7413 1.1793 0.2339  0.0409  0.0780  83  ASN D CG  
15380 O OD1 . ASN D 83  ? 1.0158 0.7265 1.1482 0.2316  0.0394  0.0704  83  ASN D OD1 
15381 N ND2 . ASN D 83  ? 1.0158 0.7500 1.1965 0.2264  0.0294  0.0801  83  ASN D ND2 
15382 N N   . SER D 84  ? 1.0636 0.7782 1.2196 0.2708  0.0824  0.0959  84  SER D N   
15383 C CA  . SER D 84  ? 0.9981 0.7092 1.1524 0.2797  0.0961  0.1008  84  SER D CA  
15384 C C   . SER D 84  ? 1.0309 0.7348 1.1599 0.2857  0.0984  0.0976  84  SER D C   
15385 O O   . SER D 84  ? 1.0130 0.7110 1.1363 0.2911  0.1070  0.1007  84  SER D O   
15386 C CB  . SER D 84  ? 0.9427 0.6618 1.1067 0.2858  0.1004  0.1059  84  SER D CB  
15387 O OG  . SER D 84  ? 0.9881 0.7041 1.1511 0.2928  0.1149  0.1109  84  SER D OG  
15388 N N   . GLY D 85  ? 1.0096 0.7149 1.1252 0.2847  0.0905  0.0925  85  GLY D N   
15389 C CA  . GLY D 85  ? 0.9367 0.6390 1.0338 0.2890  0.0914  0.0888  85  GLY D CA  
15390 C C   . GLY D 85  ? 0.9549 0.6496 1.0488 0.2877  0.0936  0.0861  85  GLY D C   
15391 O O   . GLY D 85  ? 1.0189 0.7115 1.1053 0.2944  0.0982  0.0871  85  GLY D O   
15392 N N   . LEU D 86  ? 1.0199 0.7104 1.1198 0.2790  0.0899  0.0822  86  LEU D N   
15393 C CA  . LEU D 86  ? 0.9234 0.6031 1.0215 0.2769  0.0936  0.0776  86  LEU D CA  
15394 C C   . LEU D 86  ? 1.0269 0.6992 1.1364 0.2808  0.1033  0.0841  86  LEU D C   
15395 O O   . LEU D 86  ? 0.9923 0.6545 1.0994 0.2847  0.1096  0.0838  86  LEU D O   
15396 C CB  . LEU D 86  ? 0.8306 0.5063 0.9289 0.2650  0.0866  0.0695  86  LEU D CB  
15397 C CG  . LEU D 86  ? 0.9883 0.6672 1.0699 0.2607  0.0789  0.0635  86  LEU D CG  
15398 C CD1 . LEU D 86  ? 1.0742 0.7515 1.1539 0.2486  0.0696  0.0574  86  LEU D CD1 
15399 C CD2 . LEU D 86  ? 0.8886 0.5614 0.9567 0.2646  0.0852  0.0578  86  LEU D CD2 
15400 N N   . ALA D 87  ? 1.0287 0.7054 1.1518 0.2804  0.1059  0.0910  87  ALA D N   
15401 C CA  . ALA D 87  ? 0.9384 0.6078 1.0716 0.2840  0.1174  0.0994  87  ALA D CA  
15402 C C   . ALA D 87  ? 0.9581 0.6259 1.0757 0.2968  0.1235  0.1060  87  ALA D C   
15403 O O   . ALA D 87  ? 1.0291 0.6863 1.1469 0.3018  0.1315  0.1119  87  ALA D O   
15404 C CB  . ALA D 87  ? 0.9640 0.6415 1.1144 0.2819  0.1206  0.1057  87  ALA D CB  
15405 N N   . THR D 88  ? 0.8903 0.5685 0.9947 0.3019  0.1188  0.1051  88  THR D N   
15406 C CA  . THR D 88  ? 0.9236 0.6042 1.0118 0.3126  0.1207  0.1094  88  THR D CA  
15407 C C   . THR D 88  ? 1.0177 0.6939 1.1020 0.3159  0.1190  0.1068  88  THR D C   
15408 O O   . THR D 88  ? 1.0296 0.7037 1.1089 0.3239  0.1228  0.1140  88  THR D O   
15409 C CB  . THR D 88  ? 0.9131 0.6048 0.9905 0.3139  0.1145  0.1049  88  THR D CB  
15410 O OG1 . THR D 88  ? 1.0800 0.7743 1.1634 0.3126  0.1184  0.1074  88  THR D OG1 
15411 C CG2 . THR D 88  ? 0.7902 0.4870 0.8506 0.3228  0.1133  0.1068  88  THR D CG2 
15412 N N   . ALA D 89  ? 0.9775 0.6537 1.0639 0.3091  0.1135  0.0970  89  ALA D N   
15413 C CA  . ALA D 89  ? 0.8971 0.5692 0.9823 0.3118  0.1142  0.0928  89  ALA D CA  
15414 C C   . ALA D 89  ? 0.9766 0.6322 1.0713 0.3136  0.1231  0.0966  89  ALA D C   
15415 O O   . ALA D 89  ? 1.0755 0.7299 1.1702 0.3209  0.1261  0.1005  89  ALA D O   
15416 C CB  . ALA D 89  ? 0.7927 0.4662 0.8753 0.3029  0.1089  0.0813  89  ALA D CB  
15417 N N   . VAL D 90  ? 0.9827 0.6286 1.0873 0.3045  0.1258  0.0949  90  VAL D N   
15418 C CA  . VAL D 90  ? 0.9819 0.6091 1.0976 0.3042  0.1353  0.0976  90  VAL D CA  
15419 C C   . VAL D 90  ? 0.9810 0.6082 1.0961 0.3126  0.1417  0.1123  90  VAL D C   
15420 O O   . VAL D 90  ? 1.0218 0.6407 1.1391 0.3160  0.1468  0.1163  90  VAL D O   
15421 C CB  . VAL D 90  ? 1.0330 0.6530 1.1617 0.2898  0.1351  0.0918  90  VAL D CB  
15422 C CG1 . VAL D 90  ? 0.9908 0.5896 1.1334 0.2886  0.1466  0.0953  90  VAL D CG1 
15423 C CG2 . VAL D 90  ? 0.9326 0.5539 1.0558 0.2789  0.1263  0.0763  90  VAL D CG2 
15424 N N   . ALA D 91  ? 0.9656 0.6036 1.0756 0.3146  0.1410  0.1198  91  ALA D N   
15425 C CA  . ALA D 91  ? 1.0368 0.6762 1.1395 0.3216  0.1468  0.1337  91  ALA D CA  
15426 C C   . ALA D 91  ? 1.0643 0.7122 1.1534 0.3314  0.1415  0.1370  91  ALA D C   
15427 O O   . ALA D 91  ? 1.0625 0.7047 1.1499 0.3376  0.1463  0.1476  91  ALA D O   
15428 C CB  . ALA D 91  ? 0.8453 0.4936 0.9421 0.3229  0.1484  0.1384  91  ALA D CB  
15429 N N   . ALA D 92  ? 0.9831 0.6445 1.0651 0.3333  0.1319  0.1288  92  ALA D N   
15430 C CA  . ALA D 92  ? 1.0629 0.7352 1.1375 0.3430  0.1258  0.1314  92  ALA D CA  
15431 C C   . ALA D 92  ? 1.0758 0.7407 1.1619 0.3447  0.1287  0.1315  92  ALA D C   
15432 O O   . ALA D 92  ? 1.1092 0.7786 1.1936 0.3545  0.1275  0.1410  92  ALA D O   
15433 C CB  . ALA D 92  ? 0.8853 0.5710 0.9559 0.3427  0.1171  0.1212  92  ALA D CB  
15434 N N   . GLU D 93  ? 1.0134 0.6659 1.1109 0.3365  0.1329  0.1212  93  GLU D N   
15435 C CA  . GLU D 93  ? 1.0868 0.7283 1.1953 0.3381  0.1382  0.1191  93  GLU D CA  
15436 C C   . GLU D 93  ? 1.2360 0.8631 1.3492 0.3401  0.1466  0.1316  93  GLU D C   
15437 O O   . GLU D 93  ? 1.2773 0.9016 1.3960 0.3475  0.1489  0.1379  93  GLU D O   
15438 C CB  . GLU D 93  ? 1.0223 0.6494 1.1374 0.3292  0.1424  0.1041  93  GLU D CB  
15439 C CG  . GLU D 93  ? 1.2336 0.8477 1.3589 0.3315  0.1499  0.0994  93  GLU D CG  
15440 C CD  . GLU D 93  ? 1.4126 1.0124 1.5388 0.3250  0.1547  0.0824  93  GLU D CD  
15441 O OE1 . GLU D 93  ? 1.3767 0.9587 1.5037 0.3164  0.1583  0.0764  93  GLU D OE1 
15442 O OE2 . GLU D 93  ? 1.4141 1.0197 1.5406 0.3291  0.1558  0.0752  93  GLU D OE2 
15443 N N   . ILE D 94  ? 1.1679 0.7857 1.2813 0.3341  0.1519  0.1361  94  ILE D N   
15444 C CA  . ILE D 94  ? 1.0865 0.6888 1.2048 0.3354  0.1623  0.1493  94  ILE D CA  
15445 C C   . ILE D 94  ? 1.1291 0.7414 1.2344 0.3483  0.1604  0.1664  94  ILE D C   
15446 O O   . ILE D 94  ? 1.0618 0.6643 1.1709 0.3543  0.1658  0.1773  94  ILE D O   
15447 C CB  . ILE D 94  ? 0.9692 0.5624 1.0937 0.3262  0.1695  0.1508  94  ILE D CB  
15448 C CG1 . ILE D 94  ? 1.0263 0.6033 1.1677 0.3147  0.1726  0.1362  94  ILE D CG1 
15449 C CG2 . ILE D 94  ? 1.0089 0.5903 1.1346 0.3293  0.1814  0.1687  94  ILE D CG2 
15450 C CD1 . ILE D 94  ? 1.1236 0.6992 1.2749 0.3057  0.1743  0.1335  94  ILE D CD1 
15451 N N   . ILE D 95  ? 1.0756 0.7058 1.1648 0.3533  0.1526  0.1689  95  ILE D N   
15452 C CA  . ILE D 95  ? 1.0510 0.6904 1.1233 0.3670  0.1492  0.1846  95  ILE D CA  
15453 C C   . ILE D 95  ? 1.1733 0.8214 1.2515 0.3761  0.1416  0.1860  95  ILE D C   
15454 O O   . ILE D 95  ? 1.1258 0.7716 1.2007 0.3866  0.1427  0.2017  95  ILE D O   
15455 C CB  . ILE D 95  ? 0.9959 0.6503 1.0489 0.3703  0.1425  0.1833  95  ILE D CB  
15456 C CG1 . ILE D 95  ? 0.9858 0.6315 1.0346 0.3643  0.1529  0.1858  95  ILE D CG1 
15457 C CG2 . ILE D 95  ? 1.1384 0.8036 1.1713 0.3863  0.1358  0.1971  95  ILE D CG2 
15458 C CD1 . ILE D 95  ? 0.9188 0.5756 0.9577 0.3627  0.1481  0.1768  95  ILE D CD1 
15459 N N   . GLU D 96  ? 1.1367 0.7948 1.2246 0.3729  0.1347  0.1707  96  GLU D N   
15460 C CA  . GLU D 96  ? 0.9981 0.6667 1.0970 0.3816  0.1290  0.1708  96  GLU D CA  
15461 C C   . GLU D 96  ? 1.0690 0.7198 1.1843 0.3821  0.1384  0.1737  96  GLU D C   
15462 O O   . GLU D 96  ? 1.1980 0.8544 1.3214 0.3932  0.1358  0.1824  96  GLU D O   
15463 C CB  . GLU D 96  ? 1.0098 0.6917 1.1160 0.3776  0.1230  0.1538  96  GLU D CB  
15464 C CG  . GLU D 96  ? 1.1102 0.8116 1.2031 0.3807  0.1125  0.1525  96  GLU D CG  
15465 C CD  . GLU D 96  ? 1.1120 0.8302 1.1981 0.3960  0.1029  0.1662  96  GLU D CD  
15466 O OE1 . GLU D 96  ? 1.0943 0.8188 1.1948 0.4047  0.1007  0.1725  96  GLU D OE1 
15467 O OE2 . GLU D 96  ? 1.1442 0.8693 1.2104 0.4003  0.0973  0.1707  96  GLU D OE2 
15468 N N   . ALA D 97  ? 1.0870 0.7161 1.2087 0.3709  0.1490  0.1666  97  ALA D N   
15469 C CA  . ALA D 97  ? 1.0760 0.6838 1.2127 0.3707  0.1595  0.1678  97  ALA D CA  
15470 C C   . ALA D 97  ? 1.1346 0.7339 1.2672 0.3789  0.1644  0.1897  97  ALA D C   
15471 O O   . ALA D 97  ? 1.1353 0.7284 1.2782 0.3875  0.1674  0.1979  97  ALA D O   
15472 C CB  . ALA D 97  ? 1.1814 0.7675 1.3248 0.3564  0.1688  0.1544  97  ALA D CB  
15473 N N   . ALA D 98  ? 1.1261 0.7249 1.2435 0.3774  0.1662  0.1999  98  ALA D N   
15474 C CA  . ALA D 98  ? 1.0946 0.6846 1.2034 0.3855  0.1726  0.2223  98  ALA D CA  
15475 C C   . ALA D 98  ? 1.1375 0.7460 1.2351 0.4024  0.1614  0.2371  98  ALA D C   
15476 O O   . ALA D 98  ? 1.1916 0.7921 1.2864 0.4121  0.1653  0.2563  98  ALA D O   
15477 C CB  . ALA D 98  ? 1.1573 0.7435 1.2518 0.3802  0.1789  0.2283  98  ALA D CB  
15478 N N   . LYS D 99  ? 1.0510 0.6835 1.1434 0.4059  0.1475  0.2288  99  LYS D N   
15479 C CA  . LYS D 99  ? 1.1025 0.7557 1.1872 0.4223  0.1343  0.2418  99  LYS D CA  
15480 C C   . LYS D 99  ? 1.1596 0.8106 1.2668 0.4303  0.1343  0.2467  99  LYS D C   
15481 O O   . LYS D 99  ? 1.3109 0.9663 1.4132 0.4443  0.1297  0.2666  99  LYS D O   
15482 C CB  . LYS D 99  ? 1.2024 0.8807 1.2832 0.4227  0.1205  0.2290  99  LYS D CB  
15483 C CG  . LYS D 99  ? 1.1028 0.7913 1.1542 0.4270  0.1140  0.2347  99  LYS D CG  
15484 C CD  . LYS D 99  ? 1.2531 0.9693 1.3006 0.4368  0.0966  0.2325  99  LYS D CD  
15485 C CE  . LYS D 99  ? 1.1243 0.8487 1.1659 0.4287  0.0930  0.2146  99  LYS D CE  
15486 N NZ  . LYS D 99  ? 1.4147 1.1653 1.4537 0.4389  0.0764  0.2127  99  LYS D NZ  
15487 N N   . TYR D 100 ? 1.1448 0.7890 1.2746 0.4226  0.1396  0.2295  100 TYR D N   
15488 C CA  . TYR D 100 ? 1.2583 0.8983 1.4116 0.4303  0.1424  0.2314  100 TYR D CA  
15489 C C   . TYR D 100 ? 1.1803 0.7926 1.3376 0.4322  0.1556  0.2454  100 TYR D C   
15490 O O   . TYR D 100 ? 1.3991 1.0082 1.5717 0.4430  0.1569  0.2548  100 TYR D O   
15491 C CB  . TYR D 100 ? 1.2275 0.8645 1.3995 0.4215  0.1473  0.2078  100 TYR D CB  
15492 C CG  . TYR D 100 ? 1.1195 0.7852 1.2981 0.4250  0.1357  0.1979  100 TYR D CG  
15493 C CD1 . TYR D 100 ? 1.0935 0.7727 1.2581 0.4176  0.1287  0.1882  100 TYR D CD1 
15494 C CD2 . TYR D 100 ? 1.0970 0.7761 1.2983 0.4361  0.1328  0.1987  100 TYR D CD2 
15495 C CE1 . TYR D 100 ? 1.2434 0.9478 1.4156 0.4206  0.1195  0.1798  100 TYR D CE1 
15496 C CE2 . TYR D 100 ? 1.1530 0.8595 1.3641 0.4393  0.1236  0.1903  100 TYR D CE2 
15497 C CZ  . TYR D 100 ? 1.2804 0.9990 1.4766 0.4311  0.1172  0.1808  100 TYR D CZ  
15498 O OH  . TYR D 100 ? 1.2440 0.9887 1.4515 0.4340  0.1094  0.1730  100 TYR D OH  
15499 N N   . VAL D 101 ? 1.1901 0.7824 1.3358 0.4219  0.1662  0.2473  101 VAL D N   
15500 C CA  . VAL D 101 ? 1.4102 0.9746 1.5603 0.4220  0.1809  0.2607  101 VAL D CA  
15501 C C   . VAL D 101 ? 1.3723 0.9411 1.5059 0.4365  0.1776  0.2888  101 VAL D C   
15502 O O   . VAL D 101 ? 1.1831 0.7410 1.3260 0.4465  0.1818  0.3039  101 VAL D O   
15503 C CB  . VAL D 101 ? 1.2518 0.7957 1.3992 0.4051  0.1936  0.2523  101 VAL D CB  
15504 C CG1 . VAL D 101 ? 1.1793 0.6964 1.3284 0.4052  0.2092  0.2700  101 VAL D CG1 
15505 C CG2 . VAL D 101 ? 1.2706 0.8047 1.4346 0.3920  0.1977  0.2266  101 VAL D CG2 
15506 N N   . LEU D 102 ? 1.3214 0.9052 1.4289 0.4384  0.1702  0.2959  102 LEU D N   
15507 C CA  . LEU D 102 ? 1.3901 0.9778 1.4739 0.4521  0.1670  0.3225  102 LEU D CA  
15508 C C   . LEU D 102 ? 1.3588 0.9721 1.4400 0.4696  0.1481  0.3335  102 LEU D C   
15509 O O   . LEU D 102 ? 1.4011 1.0195 1.4590 0.4821  0.1427  0.3561  102 LEU D O   
15510 C CB  . LEU D 102 ? 1.2554 0.8470 1.3096 0.4477  0.1684  0.3244  102 LEU D CB  
15511 C CG  . LEU D 102 ? 1.1634 0.7310 1.2199 0.4329  0.1878  0.3205  102 LEU D CG  
15512 C CD1 . LEU D 102 ? 1.1417 0.7183 1.1779 0.4269  0.1873  0.3134  102 LEU D CD1 
15513 C CD2 . LEU D 102 ? 1.3498 0.8945 1.4006 0.4375  0.2034  0.3447  102 LEU D CD2 
15514 N N   . SER D 103 ? 1.2064 0.8361 1.3109 0.4712  0.1382  0.3189  103 SER D N   
15515 C CA  . SER D 103 ? 1.2542 0.9111 1.3627 0.4876  0.1197  0.3290  103 SER D CA  
15516 C C   . SER D 103 ? 1.3573 1.0187 1.5029 0.4908  0.1189  0.3187  103 SER D C   
15517 O O   . SER D 103 ? 1.4623 1.1192 1.6240 0.4791  0.1256  0.2958  103 SER D O   
15518 C CB  . SER D 103 ? 1.1540 0.8398 1.2453 0.4884  0.1032  0.3217  103 SER D CB  
15519 O OG  . SER D 103 ? 1.2844 0.9991 1.3816 0.5040  0.0837  0.3317  103 SER D OG  
15520 N N   . ASP D 104 ? 1.2157 0.8859 1.3741 0.5073  0.1111  0.3362  104 ASP D N   
15521 C CA  . ASP D 104 ? 1.1930 0.8683 1.3884 0.5131  0.1114  0.3284  104 ASP D CA  
15522 C C   . ASP D 104 ? 1.3058 1.0127 1.5139 0.5116  0.0988  0.3103  104 ASP D C   
15523 O O   . ASP D 104 ? 1.4946 1.1991 1.7259 0.5052  0.1068  0.2905  104 ASP D O   
15524 C CB  . ASP D 104 ? 1.2348 0.9163 1.4414 0.5331  0.1035  0.3534  104 ASP D CB  
15525 C CG  . ASP D 104 ? 1.4598 1.1097 1.6554 0.5364  0.1166  0.3741  104 ASP D CG  
15526 O OD1 . ASP D 104 ? 1.7349 1.3531 1.9359 0.5248  0.1368  0.3646  104 ASP D OD1 
15527 O OD2 . ASP D 104 ? 1.5317 1.1887 1.7133 0.5506  0.1064  0.4001  104 ASP D OD2 
15528 N N   . ALA D 105 ? 1.2712 1.0071 1.4626 0.5175  0.0798  0.3174  105 ALA D N   
15529 C CA  . ALA D 105 ? 1.2712 1.0392 1.4736 0.5165  0.0667  0.3025  105 ALA D CA  
15530 C C   . ALA D 105 ? 1.1672 0.9409 1.3352 0.5083  0.0609  0.2977  105 ALA D C   
15531 O O   . ALA D 105 ? 1.1518 0.9448 1.2987 0.5177  0.0446  0.3118  105 ALA D O   
15532 C CB  . ALA D 105 ? 1.3208 1.1230 1.5412 0.5346  0.0463  0.3170  105 ALA D CB  
15533 N N   . PRO D 106 ? 1.1876 0.9443 1.3475 0.4913  0.0737  0.2784  106 PRO D N   
15534 C CA  . PRO D 106 ? 1.2536 1.0137 1.3817 0.4847  0.0696  0.2742  106 PRO D CA  
15535 C C   . PRO D 106 ? 1.2100 1.0028 1.3394 0.4878  0.0529  0.2655  106 PRO D C   
15536 O O   . PRO D 106 ? 1.1745 0.9746 1.2743 0.4890  0.0447  0.2679  106 PRO D O   
15537 C CB  . PRO D 106 ? 1.1781 0.9123 1.3054 0.4662  0.0874  0.2558  106 PRO D CB  
15538 C CG  . PRO D 106 ? 1.2278 0.9580 1.3879 0.4628  0.0948  0.2426  106 PRO D CG  
15539 C CD  . PRO D 106 ? 1.2307 0.9641 1.4080 0.4781  0.0918  0.2600  106 PRO D CD  
15540 N N   . TYR D 107 ? 1.2388 1.0506 1.4022 0.4895  0.0490  0.2551  107 TYR D N   
15541 C CA  . TYR D 107 ? 1.1410 0.9849 1.3116 0.4919  0.0346  0.2463  107 TYR D CA  
15542 C C   . TYR D 107 ? 1.3068 1.1862 1.4981 0.5089  0.0149  0.2597  107 TYR D C   
15543 O O   . TYR D 107 ? 1.1819 1.0638 1.4018 0.5163  0.0167  0.2667  107 TYR D O   
15544 C CB  . TYR D 107 ? 1.0564 0.8985 1.2501 0.4795  0.0457  0.2228  107 TYR D CB  
15545 C CG  . TYR D 107 ? 1.1033 0.9251 1.2728 0.4637  0.0555  0.2083  107 TYR D CG  
15546 C CD1 . TYR D 107 ? 1.3315 1.1658 1.4826 0.4621  0.0465  0.2026  107 TYR D CD1 
15547 C CD2 . TYR D 107 ? 1.1912 0.9812 1.3555 0.4514  0.0725  0.2015  107 TYR D CD2 
15548 C CE1 . TYR D 107 ? 1.3427 1.1581 1.4728 0.4487  0.0551  0.1906  107 TYR D CE1 
15549 C CE2 . TYR D 107 ? 1.2476 1.0217 1.3922 0.4374  0.0795  0.1897  107 TYR D CE2 
15550 C CZ  . TYR D 107 ? 1.2727 1.0595 1.4009 0.4361  0.0711  0.1846  107 TYR D CZ  
15551 O OH  . TYR D 107 ? 1.2785 1.0505 1.3898 0.4231  0.0776  0.1736  107 TYR D OH  
15552 N N   . ALA D 108 ? 1.5647 1.4726 1.7415 0.5154  -0.0047 0.2627  108 ALA D N   
15553 C CA  . ALA D 108 ? 1.6323 1.5813 1.8271 0.5308  -0.0284 0.2748  108 ALA D CA  
15554 C C   . ALA D 108 ? 1.6209 1.6030 1.8444 0.5287  -0.0364 0.2584  108 ALA D C   
15555 O O   . ALA D 108 ? 1.4271 1.4010 1.6362 0.5095  -0.0302 0.2371  108 ALA D O   
15556 C CB  . ALA D 108 ? 1.6913 1.6501 1.8423 0.5405  -0.0477 0.2915  108 ALA D CB  
15557 N N   . GLU D 109 ? 1.5811 1.6011 1.8452 0.5389  -0.0507 0.2637  109 GLU D N   
15558 C CA  . GLU D 109 ? 1.4978 1.5522 1.7938 0.5279  -0.0582 0.2445  109 GLU D CA  
15559 C C   . GLU D 109 ? 1.5644 1.6350 1.8271 0.5083  -0.0768 0.2289  109 GLU D C   
15560 O O   . GLU D 109 ? 1.6230 1.6942 1.8455 0.5104  -0.0924 0.2381  109 GLU D O   
15561 C CB  . GLU D 109 ? 1.4699 1.5670 1.8184 0.5449  -0.0724 0.2568  109 GLU D CB  
15562 C CG  . GLU D 109 ? 1.6280 1.7127 2.0201 0.5480  -0.0505 0.2540  109 GLU D CG  
15563 C CD  . GLU D 109 ? 1.7495 1.8347 2.1682 0.5363  -0.0318 0.2317  109 GLU D CD  
15564 O OE1 . GLU D 109 ? 1.8079 1.9317 2.2519 0.5300  -0.0434 0.2219  109 GLU D OE1 
15565 O OE2 . GLU D 109 ? 1.5680 1.6139 1.9777 0.5262  -0.0068 0.2202  109 GLU D OE2 
15566 N N   . PRO D 110 ? 1.5218 1.6035 1.7989 0.4890  -0.0742 0.2050  110 PRO D N   
15567 C CA  . PRO D 110 ? 1.2603 1.3416 1.5792 0.4837  -0.0550 0.1922  110 PRO D CA  
15568 C C   . PRO D 110 ? 1.3158 1.3513 1.6168 0.4755  -0.0271 0.1829  110 PRO D C   
15569 O O   . PRO D 110 ? 1.4205 1.4518 1.7481 0.4701  -0.0101 0.1716  110 PRO D O   
15570 C CB  . PRO D 110 ? 1.1757 1.2897 1.5089 0.4649  -0.0682 0.1727  110 PRO D CB  
15571 C CG  . PRO D 110 ? 1.3902 1.5131 1.6812 0.4570  -0.0920 0.1708  110 PRO D CG  
15572 C CD  . PRO D 110 ? 1.3936 1.4871 1.6416 0.4696  -0.0900 0.1884  110 PRO D CD  
15573 N N   . CYS D 111 ? 1.3707 1.3731 1.6270 0.4742  -0.0224 0.1877  111 CYS D N   
15574 C CA  . CYS D 111 ? 1.2223 1.1834 1.4609 0.4656  0.0008  0.1795  111 CYS D CA  
15575 C C   . CYS D 111 ? 1.1242 1.0667 1.3911 0.4765  0.0217  0.1842  111 CYS D C   
15576 O O   . CYS D 111 ? 1.3091 1.2568 1.5949 0.4917  0.0197  0.1994  111 CYS D O   
15577 C CB  . CYS D 111 ? 1.1311 1.0654 1.3231 0.4647  0.0010  0.1869  111 CYS D CB  
15578 S SG  . CYS D 111 ? 1.5076 1.4577 1.6607 0.4512  -0.0195 0.1781  111 CYS D SG  
15579 N N   . VAL D 112 ? 1.0597 0.9795 1.3265 0.4642  0.0407  0.1685  112 VAL D N   
15580 C CA  . VAL D 112 ? 1.1833 1.0833 1.4685 0.4624  0.0597  0.1635  112 VAL D CA  
15581 C C   . VAL D 112 ? 1.1185 0.9784 1.3743 0.4529  0.0712  0.1625  112 VAL D C   
15582 O O   . VAL D 112 ? 1.2267 1.0710 1.4901 0.4555  0.0792  0.1670  112 VAL D O   
15583 C CB  . VAL D 112 ? 0.9824 0.8870 1.2868 0.4538  0.0726  0.1458  112 VAL D CB  
15584 C CG1 . VAL D 112 ? 1.2396 1.1243 1.5574 0.4501  0.0918  0.1377  112 VAL D CG1 
15585 C CG2 . VAL D 112 ? 1.1707 1.1186 1.5072 0.4569  0.0607  0.1446  112 VAL D CG2 
15586 N N   . GLY D 113 ? 0.9866 0.8309 1.2121 0.4423  0.0723  0.1566  113 GLY D N   
15587 C CA  . GLY D 113 ? 1.1751 0.9858 1.3772 0.4322  0.0825  0.1552  113 GLY D CA  
15588 C C   . GLY D 113 ? 1.2087 1.0002 1.4167 0.4200  0.0986  0.1388  113 GLY D C   
15589 O O   . GLY D 113 ? 1.2614 1.0588 1.4720 0.4137  0.1016  0.1263  113 GLY D O   
15590 N N   . PHE D 114 ? 1.1873 0.9548 1.3962 0.4174  0.1095  0.1390  114 PHE D N   
15591 C CA  . PHE D 114 ? 1.1421 0.8895 1.3530 0.4069  0.1246  0.1230  114 PHE D CA  
15592 C C   . PHE D 114 ? 0.9113 0.6728 1.1470 0.4111  0.1310  0.1140  114 PHE D C   
15593 O O   . PHE D 114 ? 1.1568 0.9349 1.4162 0.4234  0.1284  0.1218  114 PHE D O   
15594 C CB  . PHE D 114 ? 1.0135 0.7328 1.2232 0.4051  0.1348  0.1252  114 PHE D CB  
15595 C CG  . PHE D 114 ? 1.0334 0.7291 1.2401 0.3940  0.1493  0.1080  114 PHE D CG  
15596 C CD1 . PHE D 114 ? 1.1435 0.8251 1.3300 0.3810  0.1506  0.0993  114 PHE D CD1 
15597 C CD2 . PHE D 114 ? 0.9255 0.6134 1.1496 0.3976  0.1617  0.1002  114 PHE D CD2 
15598 C CE1 . PHE D 114 ? 1.0482 0.7079 1.2301 0.3719  0.1626  0.0837  114 PHE D CE1 
15599 C CE2 . PHE D 114 ? 0.9527 0.6170 1.1700 0.3880  0.1755  0.0834  114 PHE D CE2 
15600 C CZ  . PHE D 114 ? 1.0330 0.6833 1.2285 0.3753  0.1752  0.0753  114 PHE D CZ  
15601 N N   . ILE D 115 ? 1.0451 0.7999 1.2757 0.4015  0.1403  0.0984  115 ILE D N   
15602 C CA  . ILE D 115 ? 1.0652 0.8313 1.3169 0.4042  0.1505  0.0889  115 ILE D CA  
15603 C C   . ILE D 115 ? 1.0646 0.8045 1.3177 0.4013  0.1683  0.0785  115 ILE D C   
15604 O O   . ILE D 115 ? 0.9889 0.7027 1.2200 0.3906  0.1747  0.0696  115 ILE D O   
15605 C CB  . ILE D 115 ? 0.9816 0.7552 1.2238 0.3962  0.1514  0.0794  115 ILE D CB  
15606 C CG1 . ILE D 115 ? 0.9291 0.7249 1.1680 0.3988  0.1342  0.0884  115 ILE D CG1 
15607 C CG2 . ILE D 115 ? 1.1122 0.8974 1.3763 0.3985  0.1650  0.0702  115 ILE D CG2 
15608 C CD1 . ILE D 115 ? 0.8305 0.6599 1.0978 0.4129  0.1231  0.0996  115 ILE D CD1 
15609 N N   . SER D 116 ? 1.0536 0.8002 1.3332 0.4114  0.1761  0.0794  116 SER D N   
15610 C CA  . SER D 116 ? 1.0636 0.7843 1.3457 0.4102  0.1943  0.0689  116 SER D CA  
15611 C C   . SER D 116 ? 1.0977 0.8051 1.3677 0.4007  0.2107  0.0497  116 SER D C   
15612 O O   . SER D 116 ? 1.1521 0.8778 1.4246 0.3991  0.2115  0.0458  116 SER D O   
15613 C CB  . SER D 116 ? 1.1908 0.9245 1.5063 0.4247  0.1990  0.0752  116 SER D CB  
15614 O OG  . SER D 116 ? 1.1834 0.9403 1.5212 0.4288  0.2066  0.0687  116 SER D OG  
15615 N N   . ASP D 117 ? 1.0822 0.7566 1.3388 0.3947  0.2248  0.0376  117 ASP D N   
15616 C CA  . ASP D 117 ? 1.1343 0.7911 1.3736 0.3859  0.2415  0.0184  117 ASP D CA  
15617 C C   . ASP D 117 ? 1.1546 0.8308 1.4135 0.3918  0.2551  0.0123  117 ASP D C   
15618 O O   . ASP D 117 ? 1.1574 0.8362 1.4029 0.3856  0.2617  0.0036  117 ASP D O   
15619 C CB  . ASP D 117 ? 1.2198 0.8380 1.4455 0.3803  0.2551  0.0054  117 ASP D CB  
15620 C CG  . ASP D 117 ? 1.2548 0.8496 1.4544 0.3691  0.2471  0.0039  117 ASP D CG  
15621 O OD1 . ASP D 117 ? 1.2735 0.8822 1.4702 0.3683  0.2299  0.0174  117 ASP D OD1 
15622 O OD2 . ASP D 117 ? 1.2859 0.8484 1.4688 0.3611  0.2586  -0.0115 117 ASP D OD2 
15623 N N   . PRO D 118 ? 1.1682 0.8588 1.4600 0.4040  0.2603  0.0174  118 PRO D N   
15624 C CA  . PRO D 118 ? 1.1522 0.8642 1.4667 0.4091  0.2744  0.0119  118 PRO D CA  
15625 C C   . PRO D 118 ? 1.2460 0.9908 1.5686 0.4083  0.2647  0.0182  118 PRO D C   
15626 O O   . PRO D 118 ? 1.2897 1.0438 1.6173 0.4060  0.2794  0.0096  118 PRO D O   
15627 C CB  . PRO D 118 ? 1.0006 0.7262 1.3528 0.4241  0.2754  0.0213  118 PRO D CB  
15628 C CG  . PRO D 118 ? 1.1137 0.8123 1.4556 0.4248  0.2704  0.0258  118 PRO D CG  
15629 C CD  . PRO D 118 ? 1.0495 0.7382 1.3608 0.4142  0.2547  0.0293  118 PRO D CD  
15630 N N   . ILE D 119 ? 1.1457 0.9068 1.4691 0.4098  0.2415  0.0326  119 ILE D N   
15631 C CA  . ILE D 119 ? 1.0033 0.7935 1.3345 0.4087  0.2317  0.0378  119 ILE D CA  
15632 C C   . ILE D 119 ? 1.1555 0.9274 1.4524 0.3954  0.2386  0.0270  119 ILE D C   
15633 O O   . ILE D 119 ? 1.2187 1.0062 1.5222 0.3926  0.2450  0.0239  119 ILE D O   
15634 C CB  . ILE D 119 ? 1.0556 0.8648 1.3921 0.4139  0.2059  0.0546  119 ILE D CB  
15635 C CG1 . ILE D 119 ? 1.0897 0.9222 1.4628 0.4291  0.1989  0.0668  119 ILE D CG1 
15636 C CG2 . ILE D 119 ? 1.1099 0.9423 1.4481 0.4104  0.1965  0.0571  119 ILE D CG2 
15637 C CD1 . ILE D 119 ? 1.1583 0.9976 1.5269 0.4350  0.1761  0.0832  119 ILE D CD1 
15638 N N   . ILE D 120 ? 1.1681 0.9070 1.4297 0.3870  0.2376  0.0217  120 ILE D N   
15639 C CA  . ILE D 120 ? 1.0845 0.8045 1.3094 0.3732  0.2410  0.0118  120 ILE D CA  
15640 C C   . ILE D 120 ? 1.1560 0.8699 1.3745 0.3677  0.2635  -0.0032 120 ILE D C   
15641 O O   . ILE D 120 ? 1.1869 0.9081 1.3868 0.3542  0.2632  -0.0077 120 ILE D O   
15642 C CB  . ILE D 120 ? 1.0220 0.7084 1.2164 0.3665  0.2365  0.0083  120 ILE D CB  
15643 C CG1 . ILE D 120 ? 1.1455 0.8372 1.3451 0.3702  0.2165  0.0233  120 ILE D CG1 
15644 C CG2 . ILE D 120 ? 1.0586 0.7347 1.2134 0.3466  0.2319  -0.0011 120 ILE D CG2 
15645 C CD1 . ILE D 120 ? 1.1309 0.8476 1.3340 0.3712  0.1994  0.0348  120 ILE D CD1 
15646 N N   . ARG D 121 ? 1.0820 0.7819 1.3148 0.3774  0.2834  -0.0105 121 ARG D N   
15647 C CA  . ARG D 121 ? 1.0859 0.7766 1.3136 0.3754  0.3099  -0.0257 121 ARG D CA  
15648 C C   . ARG D 121 ? 1.3046 1.0324 1.5635 0.3783  0.3157  -0.0211 121 ARG D C   
15649 O O   . ARG D 121 ? 1.4225 1.1514 1.6660 0.3680  0.3299  -0.0304 121 ARG D O   
15650 C CB  . ARG D 121 ? 1.2531 0.9275 1.4903 0.3802  0.3231  -0.0338 121 ARG D CB  
15651 C CG  . ARG D 121 ? 1.3308 0.9719 1.5450 0.3757  0.3160  -0.0377 121 ARG D CG  
15652 C CD  . ARG D 121 ? 1.3985 1.0142 1.6121 0.3770  0.3352  -0.0519 121 ARG D CD  
15653 N NE  . ARG D 121 ? 1.5020 1.0816 1.6716 0.3650  0.3497  -0.0728 121 ARG D NE  
15654 C CZ  . ARG D 121 ? 1.4277 0.9752 1.5689 0.3564  0.3440  -0.0804 121 ARG D CZ  
15655 N NH1 . ARG D 121 ? 1.2564 0.8033 1.4096 0.3579  0.3255  -0.0679 121 ARG D NH1 
15656 N NH2 . ARG D 121 ? 1.2868 0.8024 1.3861 0.3455  0.3571  -0.1011 121 ARG D NH2 
15657 N N   . SER D 122 ? 1.2787 1.0388 1.5799 0.3898  0.3027  -0.0065 122 SER D N   
15658 C CA  . SER D 122 ? 1.2394 1.0383 1.5806 0.3948  0.3065  -0.0009 122 SER D CA  
15659 C C   . SER D 122 ? 1.1021 0.9153 1.4225 0.3761  0.2942  -0.0003 122 SER D C   
15660 O O   . SER D 122 ? 1.2160 1.0475 1.5492 0.3702  0.3065  -0.0037 122 SER D O   
15661 C CB  . SER D 122 ? 1.1062 0.9372 1.4882 0.4066  0.2858  0.0147  122 SER D CB  
15662 O OG  . SER D 122 ? 1.2467 1.1182 1.6676 0.4099  0.2829  0.0213  122 SER D OG  
15663 N N   . LEU D 123 ? 1.2153 1.0199 1.5063 0.3672  0.2716  0.0045  123 LEU D N   
15664 C CA  . LEU D 123 ? 1.3768 1.1912 1.6481 0.3505  0.2591  0.0060  123 LEU D CA  
15665 C C   . LEU D 123 ? 1.2481 1.0353 1.4715 0.3343  0.2686  -0.0043 123 LEU D C   
15666 O O   . LEU D 123 ? 1.1493 0.9428 1.3577 0.3210  0.2633  -0.0029 123 LEU D O   
15667 C CB  . LEU D 123 ? 0.9978 0.8169 1.2619 0.3496  0.2313  0.0162  123 LEU D CB  
15668 C CG  . LEU D 123 ? 1.2257 1.0723 1.5292 0.3644  0.2175  0.0278  123 LEU D CG  
15669 C CD1 . LEU D 123 ? 1.1561 0.9970 1.4417 0.3646  0.1946  0.0363  123 LEU D CD1 
15670 C CD2 . LEU D 123 ? 1.4200 1.3054 1.7587 0.3621  0.2142  0.0304  123 LEU D CD2 
15671 N N   . GLY D 124 ? 1.2236 0.9805 1.4232 0.3355  0.2819  -0.0142 124 GLY D N   
15672 C CA  . GLY D 124 ? 1.0778 0.8089 1.2289 0.3207  0.2889  -0.0243 124 GLY D CA  
15673 C C   . GLY D 124 ? 1.1559 0.8934 1.2996 0.3123  0.3082  -0.0295 124 GLY D C   
15674 O O   . GLY D 124 ? 1.2910 1.0225 1.4014 0.2979  0.3040  -0.0290 124 GLY D O   
15675 N N   . VAL D 125 ? 1.2129 0.9621 1.3882 0.3217  0.3307  -0.0336 125 VAL D N   
15676 C CA  . VAL D 125 ? 1.2060 0.9617 1.3766 0.3141  0.3534  -0.0384 125 VAL D CA  
15677 C C   . VAL D 125 ? 1.2093 0.9935 1.3966 0.3051  0.3424  -0.0270 125 VAL D C   
15678 O O   . VAL D 125 ? 1.3242 1.1006 1.4790 0.2907  0.3460  -0.0269 125 VAL D O   
15679 C CB  . VAL D 125 ? 1.2278 0.9905 1.4330 0.3271  0.3828  -0.0458 125 VAL D CB  
15680 C CG1 . VAL D 125 ? 1.0405 0.8083 1.2374 0.3180  0.4091  -0.0507 125 VAL D CG1 
15681 C CG2 . VAL D 125 ? 1.2290 0.9586 1.4164 0.3353  0.3944  -0.0585 125 VAL D CG2 
15682 N N   . PRO D 126 ? 1.1543 0.9699 1.3894 0.3126  0.3281  -0.0173 126 PRO D N   
15683 C CA  . PRO D 126 ? 1.1795 1.0196 1.4295 0.3020  0.3176  -0.0090 126 PRO D CA  
15684 C C   . PRO D 126 ? 1.2264 1.0497 1.4340 0.2882  0.2984  -0.0049 126 PRO D C   
15685 O O   . PRO D 126 ? 1.3640 1.1964 1.5710 0.2762  0.2971  -0.0004 126 PRO D O   
15686 C CB  . PRO D 126 ? 1.1855 1.0590 1.4891 0.3136  0.3017  -0.0014 126 PRO D CB  
15687 C CG  . PRO D 126 ? 1.1666 1.0271 1.4707 0.3288  0.2961  -0.0018 126 PRO D CG  
15688 C CD  . PRO D 126 ? 1.2957 1.1258 1.5725 0.3305  0.3203  -0.0131 126 PRO D CD  
15689 N N   . LEU D 127 ? 1.1526 0.9517 1.3278 0.2896  0.2843  -0.0060 127 LEU D N   
15690 C CA  . LEU D 127 ? 1.2216 1.0055 1.3595 0.2780  0.2667  -0.0017 127 LEU D CA  
15691 C C   . LEU D 127 ? 1.2673 1.0309 1.3625 0.2656  0.2809  -0.0054 127 LEU D C   
15692 O O   . LEU D 127 ? 1.1618 0.9240 1.2405 0.2544  0.2747  0.0011  127 LEU D O   
15693 C CB  . LEU D 127 ? 0.9901 0.7554 1.1088 0.2829  0.2499  -0.0020 127 LEU D CB  
15694 C CG  . LEU D 127 ? 1.0197 0.8001 1.1641 0.2909  0.2287  0.0058  127 LEU D CG  
15695 C CD1 . LEU D 127 ? 0.8669 0.6276 0.9964 0.2971  0.2197  0.0048  127 LEU D CD1 
15696 C CD2 . LEU D 127 ? 1.0039 0.7926 1.1439 0.2815  0.2118  0.0130  127 LEU D CD2 
15697 N N   . VAL D 128 ? 1.2955 1.0422 1.3716 0.2679  0.3004  -0.0157 128 VAL D N   
15698 C CA  . VAL D 128 ? 1.2794 1.0054 1.3088 0.2568  0.3149  -0.0203 128 VAL D CA  
15699 C C   . VAL D 128 ? 1.2032 0.9439 1.2433 0.2495  0.3328  -0.0155 128 VAL D C   
15700 O O   . VAL D 128 ? 1.2130 0.9452 1.2224 0.2376  0.3310  -0.0090 128 VAL D O   
15701 C CB  . VAL D 128 ? 1.2372 0.9413 1.2446 0.2613  0.3330  -0.0353 128 VAL D CB  
15702 C CG1 . VAL D 128 ? 1.0834 0.7682 1.0403 0.2498  0.3505  -0.0409 128 VAL D CG1 
15703 C CG2 . VAL D 128 ? 1.2029 0.8886 1.1955 0.2649  0.3151  -0.0399 128 VAL D CG2 
15704 N N   . THR D 129 ? 1.2268 0.9902 1.3127 0.2569  0.3503  -0.0176 129 THR D N   
15705 C CA  . THR D 129 ? 1.3204 1.1004 1.4238 0.2494  0.3696  -0.0132 129 THR D CA  
15706 C C   . THR D 129 ? 1.3683 1.1658 1.4921 0.2408  0.3520  -0.0010 129 THR D C   
15707 O O   . THR D 129 ? 1.2930 1.0987 1.4237 0.2309  0.3659  0.0041  129 THR D O   
15708 C CB  . THR D 129 ? 1.2772 1.0796 1.4297 0.2598  0.3939  -0.0190 129 THR D CB  
15709 O OG1 . THR D 129 ? 1.6917 1.5128 1.8660 0.2511  0.4121  -0.0139 129 THR D OG1 
15710 C CG2 . THR D 129 ? 1.2317 1.0591 1.4386 0.2740  0.3783  -0.0171 129 THR D CG2 
15711 N N   . GLY D 130 ? 1.2460 1.0474 1.3784 0.2439  0.3236  0.0032  130 GLY D N   
15712 C CA  . GLY D 130 ? 1.0764 0.8909 1.2257 0.2360  0.3067  0.0122  130 GLY D CA  
15713 C C   . GLY D 130 ? 1.2433 1.0935 1.4532 0.2405  0.3017  0.0131  130 GLY D C   
15714 O O   . GLY D 130 ? 1.3211 1.1834 1.5482 0.2323  0.2899  0.0183  130 GLY D O   
15715 N N   . ASP D 131 ? 1.3378 1.2049 1.5812 0.2537  0.3096  0.0080  131 ASP D N   
15716 C CA  . ASP D 131 ? 1.3167 1.2215 1.6201 0.2596  0.3022  0.0097  131 ASP D CA  
15717 C C   . ASP D 131 ? 1.2736 1.1831 1.5791 0.2621  0.2702  0.0137  131 ASP D C   
15718 O O   . ASP D 131 ? 1.3083 1.2432 1.6468 0.2579  0.2574  0.0162  131 ASP D O   
15719 C CB  . ASP D 131 ? 1.3427 1.2618 1.6792 0.2761  0.3161  0.0052  131 ASP D CB  
15720 C CG  . ASP D 131 ? 1.6315 1.5499 1.9728 0.2748  0.3508  0.0001  131 ASP D CG  
15721 O OD1 . ASP D 131 ? 1.6345 1.5437 1.9541 0.2601  0.3644  0.0012  131 ASP D OD1 
15722 O OD2 . ASP D 131 ? 1.8355 1.7613 2.2017 0.2889  0.3656  -0.0045 131 ASP D OD2 
15723 N N   . ILE D 132 ? 1.1179 1.0024 1.3874 0.2680  0.2582  0.0134  132 ILE D N   
15724 C CA  . ILE D 132 ? 1.0131 0.8966 1.2762 0.2703  0.2310  0.0172  132 ILE D CA  
15725 C C   . ILE D 132 ? 1.0843 0.9414 1.3037 0.2573  0.2262  0.0193  132 ILE D C   
15726 O O   . ILE D 132 ? 1.1468 0.9773 1.3279 0.2579  0.2285  0.0181  132 ILE D O   
15727 C CB  . ILE D 132 ? 1.0218 0.8954 1.2781 0.2855  0.2233  0.0169  132 ILE D CB  
15728 C CG1 . ILE D 132 ? 0.9573 0.8584 1.2610 0.3001  0.2264  0.0176  132 ILE D CG1 
15729 C CG2 . ILE D 132 ? 0.9964 0.8628 1.2358 0.2857  0.1984  0.0213  132 ILE D CG2 
15730 C CD1 . ILE D 132 ? 0.8257 0.7131 1.1253 0.3157  0.2274  0.0175  132 ILE D CD1 
15731 N N   . PRO D 133 ? 0.9855 0.8490 1.2108 0.2452  0.2205  0.0224  133 PRO D N   
15732 C CA  . PRO D 133 ? 0.9145 0.7520 1.1006 0.2346  0.2170  0.0263  133 PRO D CA  
15733 C C   . PRO D 133 ? 0.9061 0.7276 1.0676 0.2387  0.1964  0.0284  133 PRO D C   
15734 O O   . PRO D 133 ? 1.0194 0.8172 1.1452 0.2344  0.1949  0.0314  133 PRO D O   
15735 C CB  . PRO D 133 ? 1.0060 0.8553 1.2132 0.2219  0.2169  0.0288  133 PRO D CB  
15736 C CG  . PRO D 133 ? 0.8908 0.7736 1.1475 0.2239  0.2231  0.0251  133 PRO D CG  
15737 C CD  . PRO D 133 ? 0.9420 0.8358 1.2110 0.2402  0.2166  0.0224  133 PRO D CD  
15738 N N   . GLY D 134 ? 0.8734 0.7092 1.0545 0.2470  0.1809  0.0275  134 GLY D N   
15739 C CA  . GLY D 134 ? 0.9743 0.7973 1.1358 0.2513  0.1634  0.0296  134 GLY D CA  
15740 C C   . GLY D 134 ? 0.9561 0.7932 1.1353 0.2640  0.1521  0.0292  134 GLY D C   
15741 O O   . GLY D 134 ? 0.9932 0.8539 1.2043 0.2695  0.1541  0.0280  134 GLY D O   
15742 N N   . VAL D 135 ? 0.9731 0.7958 1.1322 0.2693  0.1409  0.0316  135 VAL D N   
15743 C CA  . VAL D 135 ? 0.9668 0.8007 1.1386 0.2814  0.1296  0.0336  135 VAL D CA  
15744 C C   . VAL D 135 ? 0.9686 0.8007 1.1304 0.2789  0.1135  0.0354  135 VAL D C   
15745 O O   . VAL D 135 ? 0.9316 0.7433 1.0687 0.2772  0.1105  0.0373  135 VAL D O   
15746 C CB  . VAL D 135 ? 0.7735 0.5939 0.9365 0.2921  0.1342  0.0349  135 VAL D CB  
15747 C CG1 . VAL D 135 ? 0.8529 0.6658 1.0149 0.2916  0.1528  0.0304  135 VAL D CG1 
15748 C CG2 . VAL D 135 ? 0.9542 0.7525 1.0896 0.2919  0.1269  0.0374  135 VAL D CG2 
15749 N N   . ALA D 136 ? 0.9631 0.8164 1.1443 0.2779  0.1040  0.0339  136 ALA D N   
15750 C CA  . ALA D 136 ? 0.8904 0.7430 1.0622 0.2752  0.0898  0.0331  136 ALA D CA  
15751 C C   . ALA D 136 ? 0.8843 0.7382 1.0490 0.2877  0.0801  0.0377  136 ALA D C   
15752 O O   . ALA D 136 ? 1.1367 1.0109 1.3195 0.2961  0.0747  0.0399  136 ALA D O   
15753 C CB  . ALA D 136 ? 0.8804 0.7557 1.0750 0.2675  0.0832  0.0277  136 ALA D CB  
15754 N N   . VAL D 137 ? 0.7514 0.5848 0.8915 0.2894  0.0780  0.0405  137 VAL D N   
15755 C CA  . VAL D 137 ? 0.8691 0.7010 1.0002 0.3004  0.0712  0.0461  137 VAL D CA  
15756 C C   . VAL D 137 ? 0.8876 0.7239 1.0088 0.2981  0.0595  0.0435  137 VAL D C   
15757 O O   . VAL D 137 ? 1.0469 0.8666 1.1505 0.2938  0.0600  0.0422  137 VAL D O   
15758 C CB  . VAL D 137 ? 1.0100 0.8181 1.1234 0.3034  0.0777  0.0505  137 VAL D CB  
15759 C CG1 . VAL D 137 ? 0.8248 0.6305 0.9314 0.3147  0.0734  0.0579  137 VAL D CG1 
15760 C CG2 . VAL D 137 ? 0.9765 0.7777 1.0954 0.3031  0.0895  0.0497  137 VAL D CG2 
15761 N N   . ILE D 138 ? 0.8287 0.6878 0.9617 0.3008  0.0490  0.0423  138 ILE D N   
15762 C CA  . ILE D 138 ? 0.9088 0.7726 1.0295 0.2975  0.0373  0.0373  138 ILE D CA  
15763 C C   . ILE D 138 ? 0.9577 0.8173 1.0582 0.3090  0.0320  0.0450  138 ILE D C   
15764 O O   . ILE D 138 ? 0.9976 0.8682 1.1052 0.3202  0.0288  0.0535  138 ILE D O   
15765 C CB  . ILE D 138 ? 0.8674 0.7593 1.0100 0.2918  0.0268  0.0304  138 ILE D CB  
15766 C CG1 . ILE D 138 ? 0.9603 0.8514 1.1204 0.2780  0.0352  0.0230  138 ILE D CG1 
15767 C CG2 . ILE D 138 ? 0.7920 0.6891 0.9180 0.2886  0.0128  0.0237  138 ILE D CG2 
15768 C CD1 . ILE D 138 ? 0.9518 0.8714 1.1426 0.2718  0.0294  0.0175  138 ILE D CD1 
15769 N N   . LEU D 139 ? 1.0375 0.8802 1.1138 0.3067  0.0325  0.0427  139 LEU D N   
15770 C CA  . LEU D 139 ? 1.0432 0.8788 1.0973 0.3164  0.0307  0.0501  139 LEU D CA  
15771 C C   . LEU D 139 ? 1.0314 0.8655 1.0634 0.3120  0.0239  0.0419  139 LEU D C   
15772 O O   . LEU D 139 ? 1.0696 0.8949 1.1003 0.3017  0.0265  0.0314  139 LEU D O   
15773 C CB  . LEU D 139 ? 0.8974 0.7092 0.9443 0.3185  0.0437  0.0562  139 LEU D CB  
15774 C CG  . LEU D 139 ? 1.0597 0.8608 1.0873 0.3278  0.0467  0.0657  139 LEU D CG  
15775 C CD1 . LEU D 139 ? 1.0823 0.8691 1.1166 0.3318  0.0573  0.0742  139 LEU D CD1 
15776 C CD2 . LEU D 139 ? 0.9388 0.7275 0.9461 0.3239  0.0494  0.0604  139 LEU D CD2 
15777 N N   . GLY D 140 ? 0.9973 0.8381 1.0106 0.3202  0.0162  0.0467  140 GLY D N   
15778 C CA  . GLY D 140 ? 1.2288 1.0667 1.2151 0.3167  0.0106  0.0380  140 GLY D CA  
15779 C C   . GLY D 140 ? 1.2782 1.1404 1.2612 0.3143  -0.0076 0.0311  140 GLY D C   
15780 O O   . GLY D 140 ? 1.0681 0.9517 1.0629 0.3217  -0.0179 0.0397  140 GLY D O   
15781 N N   . GLU D 141 ? 1.2107 1.0694 1.1780 0.3039  -0.0122 0.0151  141 GLU D N   
15782 C CA  . GLU D 141 ? 1.1739 1.0547 1.1347 0.2985  -0.0312 0.0047  141 GLU D CA  
15783 C C   . GLU D 141 ? 1.1491 1.0256 1.1184 0.2811  -0.0321 -0.0160 141 GLU D C   
15784 O O   . GLU D 141 ? 1.3069 1.1576 1.2634 0.2760  -0.0197 -0.0240 141 GLU D O   
15785 C CB  . GLU D 141 ? 1.2582 1.1350 1.1753 0.3052  -0.0365 0.0060  141 GLU D CB  
15786 C CG  . GLU D 141 ? 1.4467 1.3498 1.3517 0.3021  -0.0599 -0.0014 141 GLU D CG  
15787 C CD  . GLU D 141 ? 1.6216 1.5167 1.4754 0.3056  -0.0640 -0.0044 141 GLU D CD  
15788 O OE1 . GLU D 141 ? 1.6152 1.4824 1.4448 0.3030  -0.0483 -0.0121 141 GLU D OE1 
15789 O OE2 . GLU D 141 ? 1.5867 1.5040 1.4243 0.3114  -0.0827 0.0014  141 GLU D OE2 
15790 N N   . CYS D 142 ? 1.1681 1.0701 1.1615 0.2721  -0.0464 -0.0241 142 CYS D N   
15791 C CA  . CYS D 142 ? 1.2254 1.1251 1.2314 0.2540  -0.0481 -0.0437 142 CYS D CA  
15792 C C   . CYS D 142 ? 1.3187 1.2198 1.2932 0.2466  -0.0616 -0.0609 142 CYS D C   
15793 O O   . CYS D 142 ? 1.2832 1.1972 1.2321 0.2554  -0.0742 -0.0557 142 CYS D O   
15794 C CB  . CYS D 142 ? 1.1580 1.0862 1.2083 0.2469  -0.0559 -0.0441 142 CYS D CB  
15795 S SG  . CYS D 142 ? 1.2255 1.1432 1.3101 0.2473  -0.0354 -0.0334 142 CYS D SG  
15796 N N   . PRO D 143 ? 1.2330 1.1203 1.2071 0.2302  -0.0597 -0.0815 143 PRO D N   
15797 C CA  . PRO D 143 ? 1.3344 1.2218 1.2758 0.2221  -0.0728 -0.1007 143 PRO D CA  
15798 C C   . PRO D 143 ? 1.4102 1.3380 1.3566 0.2196  -0.1002 -0.1030 143 PRO D C   
15799 O O   . PRO D 143 ? 1.4456 1.3791 1.3540 0.2212  -0.1140 -0.1094 143 PRO D O   
15800 C CB  . PRO D 143 ? 1.2359 1.1020 1.1891 0.2037  -0.0646 -0.1217 143 PRO D CB  
15801 C CG  . PRO D 143 ? 1.1848 1.0534 1.1836 0.2002  -0.0547 -0.1126 143 PRO D CG  
15802 C CD  . PRO D 143 ? 1.1416 1.0106 1.1424 0.2184  -0.0454 -0.0883 143 PRO D CD  
15803 N N   . ASP D 144 ? 1.3717 1.3280 1.3648 0.2166  -0.1075 -0.0968 144 ASP D N   
15804 C CA  . ASP D 144 ? 1.4458 1.4463 1.4549 0.2148  -0.1346 -0.0972 144 ASP D CA  
15805 C C   . ASP D 144 ? 1.4221 1.4483 1.4796 0.2234  -0.1332 -0.0783 144 ASP D C   
15806 O O   . ASP D 144 ? 1.4435 1.4515 1.5218 0.2244  -0.1119 -0.0716 144 ASP D O   
15807 C CB  . ASP D 144 ? 1.5231 1.5350 1.5458 0.1916  -0.1485 -0.1230 144 ASP D CB  
15808 C CG  . ASP D 144 ? 1.4906 1.4895 1.5541 0.1767  -0.1321 -0.1309 144 ASP D CG  
15809 O OD1 . ASP D 144 ? 1.5691 1.5900 1.6786 0.1775  -0.1300 -0.1199 144 ASP D OD1 
15810 O OD2 . ASP D 144 ? 1.5065 1.4723 1.5551 0.1649  -0.1202 -0.1472 144 ASP D OD2 
15811 N N   . SER D 145 ? 1.2619 1.3287 1.3364 0.2297  -0.1549 -0.0702 145 SER D N   
15812 C CA  . SER D 145 ? 1.1754 1.2677 1.2983 0.2391  -0.1526 -0.0531 145 SER D CA  
15813 C C   . SER D 145 ? 1.2681 1.3746 1.4442 0.2224  -0.1478 -0.0632 145 SER D C   
15814 O O   . SER D 145 ? 1.3150 1.4312 1.5287 0.2288  -0.1363 -0.0508 145 SER D O   
15815 C CB  . SER D 145 ? 1.2322 1.3643 1.3610 0.2527  -0.1770 -0.0397 145 SER D CB  
15816 O OG  . SER D 145 ? 1.4696 1.6408 1.6237 0.2392  -0.2022 -0.0529 145 SER D OG  
15817 N N   . GLU D 146 ? 1.3082 1.4144 1.4872 0.2007  -0.1548 -0.0859 146 GLU D N   
15818 C CA  . GLU D 146 ? 1.1801 1.2982 1.4099 0.1829  -0.1487 -0.0954 146 GLU D CA  
15819 C C   . GLU D 146 ? 1.1347 1.2161 1.3695 0.1826  -0.1177 -0.0899 146 GLU D C   
15820 O O   . GLU D 146 ? 0.9777 1.0704 1.2540 0.1814  -0.1060 -0.0825 146 GLU D O   
15821 C CB  . GLU D 146 ? 1.2679 1.3882 1.4965 0.1586  -0.1622 -0.1220 146 GLU D CB  
15822 C CG  . GLU D 146 ? 1.3207 1.4850 1.5534 0.1548  -0.1961 -0.1295 146 GLU D CG  
15823 C CD  . GLU D 146 ? 1.6027 1.7667 1.8272 0.1299  -0.2111 -0.1586 146 GLU D CD  
15824 O OE1 . GLU D 146 ? 1.6386 1.7626 1.8495 0.1164  -0.1935 -0.1734 146 GLU D OE1 
15825 O OE2 . GLU D 146 ? 1.5685 1.7721 1.8007 0.1237  -0.2411 -0.1667 146 GLU D OE2 
15826 N N   . THR D 147 ? 1.3125 1.3508 1.5047 0.1841  -0.1043 -0.0930 147 THR D N   
15827 C CA  . THR D 147 ? 1.3189 1.3219 1.5117 0.1845  -0.0774 -0.0869 147 THR D CA  
15828 C C   . THR D 147 ? 1.1902 1.1952 1.3898 0.2033  -0.0661 -0.0648 147 THR D C   
15829 O O   . THR D 147 ? 1.2078 1.2043 1.4294 0.2016  -0.0486 -0.0584 147 THR D O   
15830 C CB  . THR D 147 ? 1.1511 1.1110 1.2999 0.1833  -0.0675 -0.0948 147 THR D CB  
15831 O OG1 . THR D 147 ? 1.2944 1.2499 1.4022 0.1985  -0.0744 -0.0889 147 THR D OG1 
15832 C CG2 . THR D 147 ? 1.0541 1.0031 1.2003 0.1625  -0.0720 -0.1186 147 THR D CG2 
15833 N N   . ALA D 148 ? 1.0992 1.1138 1.2789 0.2209  -0.0754 -0.0530 148 ALA D N   
15834 C CA  . ALA D 148 ? 1.0030 1.0170 1.1893 0.2385  -0.0645 -0.0333 148 ALA D CA  
15835 C C   . ALA D 148 ? 1.0777 1.1227 1.3147 0.2381  -0.0632 -0.0279 148 ALA D C   
15836 O O   . ALA D 148 ? 1.0109 1.0447 1.2621 0.2411  -0.0444 -0.0202 148 ALA D O   
15837 C CB  . ALA D 148 ? 0.9472 0.9669 1.1059 0.2563  -0.0756 -0.0216 148 ALA D CB  
15838 N N   . ALA D 149 ? 1.0052 1.0898 1.2698 0.2338  -0.0829 -0.0327 149 ALA D N   
15839 C CA  . ALA D 149 ? 0.9957 1.1142 1.3140 0.2339  -0.0817 -0.0278 149 ALA D CA  
15840 C C   . ALA D 149 ? 1.1773 1.2878 1.5238 0.2166  -0.0636 -0.0361 149 ALA D C   
15841 O O   . ALA D 149 ? 1.1039 1.2238 1.4827 0.2202  -0.0490 -0.0280 149 ALA D O   
15842 C CB  . ALA D 149 ? 0.8586 1.0233 1.2017 0.2316  -0.1092 -0.0320 149 ALA D CB  
15843 N N   . LYS D 150 ? 1.0609 1.1525 1.3948 0.1980  -0.0631 -0.0516 150 LYS D N   
15844 C CA  . LYS D 150 ? 0.9531 1.0336 1.3117 0.1812  -0.0451 -0.0577 150 LYS D CA  
15845 C C   . LYS D 150 ? 1.0190 1.0664 1.3627 0.1891  -0.0194 -0.0457 150 LYS D C   
15846 O O   . LYS D 150 ? 0.8519 0.9026 1.2236 0.1849  -0.0027 -0.0414 150 LYS D O   
15847 C CB  . LYS D 150 ? 0.9622 1.0227 1.3063 0.1613  -0.0488 -0.0761 150 LYS D CB  
15848 C CG  . LYS D 150 ? 0.9897 1.0844 1.3575 0.1466  -0.0723 -0.0920 150 LYS D CG  
15849 C CD  . LYS D 150 ? 1.3584 1.4325 1.7281 0.1223  -0.0689 -0.1113 150 LYS D CD  
15850 C CE  . LYS D 150 ? 1.2667 1.3567 1.6900 0.1050  -0.0581 -0.1141 150 LYS D CE  
15851 N NZ  . LYS D 150 ? 1.1570 1.2212 1.5818 0.0815  -0.0522 -0.1315 150 LYS D NZ  
15852 N N   . ILE D 151 ? 0.9585 0.9750 1.2580 0.2003  -0.0163 -0.0404 151 ILE D N   
15853 C CA  . ILE D 151 ? 0.9474 0.9329 1.2294 0.2077  0.0045  -0.0297 151 ILE D CA  
15854 C C   . ILE D 151 ? 1.0414 1.0427 1.3407 0.2223  0.0115  -0.0164 151 ILE D C   
15855 O O   . ILE D 151 ? 1.0033 0.9946 1.3114 0.2215  0.0302  -0.0111 151 ILE D O   
15856 C CB  . ILE D 151 ? 0.8349 0.7879 1.0701 0.2155  0.0041  -0.0280 151 ILE D CB  
15857 C CG1 . ILE D 151 ? 0.8266 0.7562 1.0462 0.2010  0.0042  -0.0412 151 ILE D CG1 
15858 C CG2 . ILE D 151 ? 0.7947 0.7232 1.0145 0.2256  0.0212  -0.0154 151 ILE D CG2 
15859 C CD1 . ILE D 151 ? 0.8383 0.7463 1.0174 0.2078  -0.0009 -0.0438 151 ILE D CD1 
15860 N N   . ILE D 152 ? 1.0011 1.0243 1.3026 0.2364  -0.0023 -0.0107 152 ILE D N   
15861 C CA  . ILE D 152 ? 0.9275 0.9642 1.2491 0.2514  0.0057  0.0015  152 ILE D CA  
15862 C C   . ILE D 152 ? 0.9619 1.0246 1.3312 0.2433  0.0143  -0.0008 152 ILE D C   
15863 O O   . ILE D 152 ? 0.9572 1.0091 1.3337 0.2452  0.0351  0.0040  152 ILE D O   
15864 C CB  . ILE D 152 ? 0.8730 0.9308 1.1936 0.2682  -0.0117 0.0096  152 ILE D CB  
15865 C CG1 . ILE D 152 ? 0.7858 0.8140 1.0606 0.2793  -0.0122 0.0162  152 ILE D CG1 
15866 C CG2 . ILE D 152 ? 1.0204 1.1020 1.3782 0.2810  -0.0056 0.0195  152 ILE D CG2 
15867 C CD1 . ILE D 152 ? 0.8032 0.8437 1.0592 0.2847  -0.0342 0.0167  152 ILE D CD1 
15868 N N   . LYS D 153 ? 0.9347 1.0309 1.3353 0.2340  -0.0010 -0.0085 153 LYS D N   
15869 C CA  . LYS D 153 ? 0.9447 1.0708 1.3974 0.2266  0.0072  -0.0100 153 LYS D CA  
15870 C C   . LYS D 153 ? 0.9637 1.0660 1.4175 0.2123  0.0316  -0.0131 153 LYS D C   
15871 O O   . LYS D 153 ? 1.0226 1.1382 1.5090 0.2117  0.0485  -0.0097 153 LYS D O   
15872 C CB  . LYS D 153 ? 1.0171 1.1831 1.5037 0.2153  -0.0153 -0.0197 153 LYS D CB  
15873 C CG  . LYS D 153 ? 0.9554 1.1529 1.4478 0.2311  -0.0401 -0.0135 153 LYS D CG  
15874 C CD  . LYS D 153 ? 1.2125 1.4604 1.7527 0.2220  -0.0614 -0.0205 153 LYS D CD  
15875 C CE  . LYS D 153 ? 1.2310 1.4780 1.7542 0.2027  -0.0810 -0.0374 153 LYS D CE  
15876 N NZ  . LYS D 153 ? 1.2107 1.5080 1.7653 0.2002  -0.1115 -0.0418 153 LYS D NZ  
15877 N N   . ASP D 154 ? 0.9928 1.0598 1.4111 0.2019  0.0348  -0.0185 154 ASP D N   
15878 C CA  . ASP D 154 ? 1.0414 1.0832 1.4568 0.1893  0.0570  -0.0188 154 ASP D CA  
15879 C C   . ASP D 154 ? 1.0104 1.0294 1.4043 0.2017  0.0764  -0.0076 154 ASP D C   
15880 O O   . ASP D 154 ? 1.0672 1.0851 1.4761 0.1972  0.0966  -0.0044 154 ASP D O   
15881 C CB  . ASP D 154 ? 0.9895 0.9995 1.3749 0.1767  0.0540  -0.0264 154 ASP D CB  
15882 C CG  . ASP D 154 ? 0.9568 0.9448 1.3462 0.1613  0.0742  -0.0264 154 ASP D CG  
15883 O OD1 . ASP D 154 ? 1.1008 1.1044 1.5219 0.1562  0.0890  -0.0231 154 ASP D OD1 
15884 O OD2 . ASP D 154 ? 0.9410 0.8961 1.3027 0.1548  0.0762  -0.0287 154 ASP D OD2 
15885 N N   . TYR D 155 ? 0.9152 0.9161 1.2739 0.2164  0.0709  -0.0022 155 TYR D N   
15886 C CA  . TYR D 155 ? 0.8794 0.8586 1.2171 0.2271  0.0872  0.0064  155 TYR D CA  
15887 C C   . TYR D 155 ? 1.0393 1.0438 1.4104 0.2364  0.0970  0.0105  155 TYR D C   
15888 O O   . TYR D 155 ? 1.0997 1.0939 1.4705 0.2361  0.1177  0.0134  155 TYR D O   
15889 C CB  . TYR D 155 ? 0.8678 0.8275 1.1689 0.2406  0.0780  0.0109  155 TYR D CB  
15890 C CG  . TYR D 155 ? 0.9183 0.8461 1.1828 0.2347  0.0756  0.0092  155 TYR D CG  
15891 C CD1 . TYR D 155 ? 1.0119 0.9145 1.2622 0.2255  0.0897  0.0104  155 TYR D CD1 
15892 C CD2 . TYR D 155 ? 0.9530 0.8747 1.1957 0.2403  0.0606  0.0080  155 TYR D CD2 
15893 C CE1 . TYR D 155 ? 1.0010 0.8756 1.2220 0.2221  0.0876  0.0103  155 TYR D CE1 
15894 C CE2 . TYR D 155 ? 0.9940 0.8872 1.2067 0.2364  0.0605  0.0067  155 TYR D CE2 
15895 C CZ  . TYR D 155 ? 0.9915 0.8618 1.1956 0.2277  0.0735  0.0080  155 TYR D CZ  
15896 O OH  . TYR D 155 ? 0.8874 0.7309 1.0663 0.2255  0.0733  0.0078  155 TYR D OH  
15897 N N   . GLN D 156 ? 1.0387 1.0754 1.4368 0.2453  0.0821  0.0111  156 GLN D N   
15898 C CA  . GLN D 156 ? 0.9131 0.9767 1.3497 0.2562  0.0910  0.0156  156 GLN D CA  
15899 C C   . GLN D 156 ? 1.0096 1.0879 1.4812 0.2426  0.1085  0.0117  156 GLN D C   
15900 O O   . GLN D 156 ? 1.1766 1.2557 1.6616 0.2484  0.1298  0.0149  156 GLN D O   
15901 C CB  . GLN D 156 ? 1.0386 1.1381 1.5022 0.2668  0.0686  0.0180  156 GLN D CB  
15902 C CG  . GLN D 156 ? 1.0939 1.2329 1.6143 0.2725  0.0746  0.0205  156 GLN D CG  
15903 C CD  . GLN D 156 ? 1.1250 1.2972 1.6686 0.2877  0.0521  0.0268  156 GLN D CD  
15904 O OE1 . GLN D 156 ? 0.8335 1.0193 1.3712 0.2836  0.0271  0.0241  156 GLN D OE1 
15905 N NE2 . GLN D 156 ? 1.2623 1.4468 1.8314 0.3059  0.0611  0.0355  156 GLN D NE2 
15906 N N   . SER D 157 ? 0.9381 1.0258 1.4232 0.2247  0.1013  0.0045  157 SER D N   
15907 C CA  . SER D 157 ? 0.8386 0.9397 1.3591 0.2094  0.1190  0.0014  157 SER D CA  
15908 C C   . SER D 157 ? 0.9817 1.0474 1.4727 0.2062  0.1463  0.0053  157 SER D C   
15909 O O   . SER D 157 ? 0.9580 1.0341 1.4744 0.2040  0.1686  0.0071  157 SER D O   
15910 C CB  . SER D 157 ? 0.7825 0.8914 1.3163 0.1892  0.1069  -0.0076 157 SER D CB  
15911 O OG  . SER D 157 ? 1.3197 1.3879 1.8147 0.1777  0.1152  -0.0089 157 SER D OG  
15912 N N   . LYS D 158 ? 1.0830 1.1096 1.5224 0.2064  0.1446  0.0070  158 LYS D N   
15913 C CA  . LYS D 158 ? 1.0064 0.9988 1.4124 0.2035  0.1670  0.0117  158 LYS D CA  
15914 C C   . LYS D 158 ? 1.0342 1.0227 1.4311 0.2198  0.1794  0.0157  158 LYS D C   
15915 O O   . LYS D 158 ? 1.0722 1.0369 1.4434 0.2181  0.1991  0.0184  158 LYS D O   
15916 C CB  . LYS D 158 ? 1.1330 1.0885 1.4916 0.1996  0.1589  0.0129  158 LYS D CB  
15917 C CG  . LYS D 158 ? 0.9729 0.9297 1.3364 0.1881  0.1419  0.0069  158 LYS D CG  
15918 C CD  . LYS D 158 ? 0.8261 0.7583 1.1783 0.1717  0.1528  0.0079  158 LYS D CD  
15919 C CE  . LYS D 158 ? 0.8570 0.7928 1.2236 0.1583  0.1391  -0.0008 158 LYS D CE  
15920 N NZ  . LYS D 158 ? 1.2075 1.1623 1.6164 0.1417  0.1492  -0.0044 158 LYS D NZ  
15921 N N   . GLY D 159 ? 1.0409 1.0503 1.4565 0.2350  0.1682  0.0160  159 GLY D N   
15922 C CA  . GLY D 159 ? 0.9797 0.9843 1.3912 0.2512  0.1808  0.0189  159 GLY D CA  
15923 C C   . GLY D 159 ? 0.8963 0.8674 1.2594 0.2595  0.1742  0.0213  159 GLY D C   
15924 O O   . GLY D 159 ? 1.0415 1.0044 1.3983 0.2725  0.1828  0.0226  159 GLY D O   
15925 N N   . LEU D 160 ? 1.0316 0.9849 1.3655 0.2521  0.1598  0.0213  160 LEU D N   
15926 C CA  . LEU D 160 ? 1.0053 0.9300 1.2977 0.2592  0.1518  0.0238  160 LEU D CA  
15927 C C   . LEU D 160 ? 0.9795 0.9175 1.2830 0.2753  0.1383  0.0266  160 LEU D C   
15928 O O   . LEU D 160 ? 0.8783 0.8437 1.2085 0.2766  0.1237  0.0264  160 LEU D O   
15929 C CB  . LEU D 160 ? 0.8282 0.7379 1.0977 0.2489  0.1388  0.0232  160 LEU D CB  
15930 C CG  . LEU D 160 ? 0.9799 0.8606 1.2188 0.2381  0.1494  0.0247  160 LEU D CG  
15931 C CD1 . LEU D 160 ? 0.8520 0.7404 1.1098 0.2237  0.1607  0.0234  160 LEU D CD1 
15932 C CD2 . LEU D 160 ? 1.0608 0.9206 1.2710 0.2363  0.1356  0.0261  160 LEU D CD2 
15933 N N   . LEU D 161 ? 0.8548 0.7739 1.1384 0.2865  0.1425  0.0293  161 LEU D N   
15934 C CA  . LEU D 161 ? 0.8163 0.7433 1.1070 0.3021  0.1301  0.0344  161 LEU D CA  
15935 C C   . LEU D 161 ? 0.9678 0.8902 1.2382 0.3002  0.1097  0.0363  161 LEU D C   
15936 O O   . LEU D 161 ? 1.0300 0.9281 1.2691 0.2923  0.1095  0.0348  161 LEU D O   
15937 C CB  . LEU D 161 ? 0.9033 0.8060 1.1764 0.3122  0.1417  0.0359  161 LEU D CB  
15938 C CG  . LEU D 161 ? 1.0850 0.9854 1.3567 0.3274  0.1309  0.0430  161 LEU D CG  
15939 C CD1 . LEU D 161 ? 1.0019 0.9356 1.3133 0.3392  0.1232  0.0484  161 LEU D CD1 
15940 C CD2 . LEU D 161 ? 0.7802 0.6534 1.0364 0.3346  0.1444  0.0427  161 LEU D CD2 
15941 N N   . THR D 162 ? 0.9225 0.8675 1.2092 0.3079  0.0935  0.0398  162 THR D N   
15942 C CA  . THR D 162 ? 0.9354 0.8756 1.1993 0.3058  0.0756  0.0403  162 THR D CA  
15943 C C   . THR D 162 ? 1.0008 0.9383 1.2559 0.3221  0.0676  0.0495  162 THR D C   
15944 O O   . THR D 162 ? 1.1530 1.1136 1.4342 0.3336  0.0627  0.0551  162 THR D O   
15945 C CB  . THR D 162 ? 1.0273 0.9919 1.3081 0.2951  0.0625  0.0341  162 THR D CB  
15946 O OG1 . THR D 162 ? 1.3524 1.3097 1.6362 0.2799  0.0745  0.0275  162 THR D OG1 
15947 C CG2 . THR D 162 ? 1.0868 1.0468 1.3430 0.2930  0.0452  0.0325  162 THR D CG2 
15948 N N   . CYS D 163 ? 0.9634 0.8741 1.1853 0.3233  0.0671  0.0520  163 CYS D N   
15949 C CA  . CYS D 163 ? 0.9673 0.8702 1.1786 0.3377  0.0630  0.0619  163 CYS D CA  
15950 C C   . CYS D 163 ? 0.9683 0.8710 1.1569 0.3362  0.0480  0.0631  163 CYS D C   
15951 O O   . CYS D 163 ? 1.0847 0.9716 1.2521 0.3258  0.0487  0.0573  163 CYS D O   
15952 C CB  . CYS D 163 ? 0.7642 0.6363 0.9582 0.3397  0.0771  0.0635  163 CYS D CB  
15953 S SG  . CYS D 163 ? 1.1289 0.9959 1.3408 0.3391  0.0972  0.0585  163 CYS D SG  
15954 N N   . LEU D 164 ? 0.8594 0.7794 1.0516 0.3468  0.0348  0.0707  164 LEU D N   
15955 C CA  . LEU D 164 ? 0.9114 0.8319 1.0780 0.3454  0.0208  0.0709  164 LEU D CA  
15956 C C   . LEU D 164 ? 0.8823 0.7861 1.0248 0.3572  0.0210  0.0829  164 LEU D C   
15957 O O   . LEU D 164 ? 0.9881 0.8930 1.1409 0.3708  0.0234  0.0946  164 LEU D O   
15958 C CB  . LEU D 164 ? 0.9061 0.8610 1.0876 0.3469  0.0019  0.0704  164 LEU D CB  
15959 C CG  . LEU D 164 ? 0.9228 0.9049 1.1421 0.3391  0.0002  0.0624  164 LEU D CG  
15960 C CD1 . LEU D 164 ? 0.9306 0.9481 1.1634 0.3399  -0.0218 0.0618  164 LEU D CD1 
15961 C CD2 . LEU D 164 ? 0.9548 0.9253 1.1718 0.3209  0.0087  0.0488  164 LEU D CD2 
15962 N N   . VAL D 165 ? 1.0090 0.8967 1.1209 0.3517  0.0198  0.0800  165 VAL D N   
15963 C CA  . VAL D 165 ? 1.0488 0.9191 1.1361 0.3613  0.0223  0.0915  165 VAL D CA  
15964 C C   . VAL D 165 ? 1.0029 0.8731 1.0601 0.3574  0.0131  0.0877  165 VAL D C   
15965 O O   . VAL D 165 ? 0.9852 0.8463 1.0333 0.3454  0.0159  0.0757  165 VAL D O   
15966 C CB  . VAL D 165 ? 0.8377 0.6793 0.9205 0.3593  0.0391  0.0927  165 VAL D CB  
15967 C CG1 . VAL D 165 ? 1.0634 0.8944 1.1417 0.3447  0.0443  0.0801  165 VAL D CG1 
15968 C CG2 . VAL D 165 ? 0.9387 0.7629 0.9996 0.3670  0.0433  0.1040  165 VAL D CG2 
15969 N N   . GLY D 166 ? 0.9126 0.7917 0.9539 0.3676  0.0030  0.0978  166 GLY D N   
15970 C CA  . GLY D 166 ? 1.0115 0.8906 1.0193 0.3650  -0.0055 0.0940  166 GLY D CA  
15971 C C   . GLY D 166 ? 1.0743 0.9835 1.0824 0.3646  -0.0266 0.0901  166 GLY D C   
15972 O O   . GLY D 166 ? 1.0954 1.0275 1.1298 0.3716  -0.0356 0.0969  166 GLY D O   
15973 N N   . LYS D 167 ? 1.0944 1.0044 1.0749 0.3562  -0.0348 0.0783  167 LYS D N   
15974 C CA  . LYS D 167 ? 1.1750 1.1138 1.1519 0.3532  -0.0573 0.0717  167 LYS D CA  
15975 C C   . LYS D 167 ? 1.0853 1.0473 1.1025 0.3425  -0.0649 0.0595  167 LYS D C   
15976 O O   . LYS D 167 ? 0.9678 0.9604 0.9953 0.3413  -0.0849 0.0568  167 LYS D O   
15977 C CB  . LYS D 167 ? 1.2672 1.1968 1.2021 0.3450  -0.0619 0.0586  167 LYS D CB  
15978 C CG  . LYS D 167 ? 1.4397 1.3533 1.3312 0.3563  -0.0573 0.0715  167 LYS D CG  
15979 C CD  . LYS D 167 ? 1.6141 1.5383 1.4646 0.3540  -0.0745 0.0642  167 LYS D CD  
15980 C CE  . LYS D 167 ? 1.6939 1.5909 1.4964 0.3559  -0.0610 0.0642  167 LYS D CE  
15981 N NZ  . LYS D 167 ? 1.6432 1.5488 1.4018 0.3518  -0.0769 0.0535  167 LYS D NZ  
15982 N N   . VAL D 168 ? 1.0091 0.9583 1.0497 0.3344  -0.0495 0.0529  168 VAL D N   
15983 C CA  . VAL D 168 ? 0.9701 0.9395 1.0496 0.3240  -0.0529 0.0430  168 VAL D CA  
15984 C C   . VAL D 168 ? 1.0503 1.0507 1.1641 0.3351  -0.0621 0.0547  168 VAL D C   
15985 O O   . VAL D 168 ? 1.1209 1.1484 1.2670 0.3278  -0.0709 0.0474  168 VAL D O   
15986 C CB  . VAL D 168 ? 0.8809 0.8291 0.9756 0.3151  -0.0332 0.0372  168 VAL D CB  
15987 C CG1 . VAL D 168 ? 0.9333 0.8593 1.0059 0.3016  -0.0280 0.0229  168 VAL D CG1 
15988 C CG2 . VAL D 168 ? 0.9932 0.9210 1.0871 0.3262  -0.0168 0.0507  168 VAL D CG2 
15989 N N   . ILE D 169 ? 0.9764 0.9728 1.0859 0.3527  -0.0592 0.0731  169 ILE D N   
15990 C CA  . ILE D 169 ? 0.9091 0.9325 1.0523 0.3660  -0.0665 0.0860  169 ILE D CA  
15991 C C   . ILE D 169 ? 1.1021 1.1608 1.2451 0.3670  -0.0937 0.0859  169 ILE D C   
15992 O O   . ILE D 169 ? 1.1234 1.2160 1.3062 0.3662  -0.1045 0.0843  169 ILE D O   
15993 C CB  . ILE D 169 ? 0.8898 0.8950 1.0256 0.3847  -0.0559 0.1061  169 ILE D CB  
15994 C CG1 . ILE D 169 ? 0.9843 0.9584 1.1259 0.3820  -0.0309 0.1040  169 ILE D CG1 
15995 C CG2 . ILE D 169 ? 1.1206 1.1539 1.2898 0.4010  -0.0654 0.1212  169 ILE D CG2 
15996 C CD1 . ILE D 169 ? 0.9764 0.9229 1.0998 0.3942  -0.0188 0.1187  169 ILE D CD1 
15997 N N   . ASP D 170 ? 1.0990 1.1509 1.1970 0.3681  -0.1046 0.0870  170 ASP D N   
15998 C CA  . ASP D 170 ? 1.0776 1.1611 1.1653 0.3682  -0.1325 0.0861  170 ASP D CA  
15999 C C   . ASP D 170 ? 1.1882 1.2922 1.2927 0.3475  -0.1443 0.0628  170 ASP D C   
16000 O O   . ASP D 170 ? 1.2324 1.3750 1.3586 0.3460  -0.1672 0.0611  170 ASP D O   
16001 C CB  . ASP D 170 ? 1.1139 1.1789 1.1415 0.3718  -0.1372 0.0897  170 ASP D CB  
16002 C CG  . ASP D 170 ? 1.1971 1.2443 1.2061 0.3920  -0.1280 0.1146  170 ASP D CG  
16003 O OD1 . ASP D 170 ? 1.2085 1.2726 1.2461 0.4074  -0.1326 0.1326  170 ASP D OD1 
16004 O OD2 . ASP D 170 ? 1.4549 1.4709 1.4225 0.3924  -0.1153 0.1163  170 ASP D OD2 
16005 N N   . GLN D 171 ? 1.0968 1.1752 1.1931 0.3314  -0.1290 0.0455  171 GLN D N   
16006 C CA  . GLN D 171 ? 1.2394 1.3299 1.3513 0.3103  -0.1363 0.0231  171 GLN D CA  
16007 C C   . GLN D 171 ? 1.1761 1.2949 1.3484 0.3060  -0.1357 0.0220  171 GLN D C   
16008 O O   . GLN D 171 ? 1.2036 1.3532 1.4004 0.2939  -0.1526 0.0103  171 GLN D O   
16009 C CB  . GLN D 171 ? 1.1139 1.1654 1.2038 0.2971  -0.1169 0.0086  171 GLN D CB  
16010 C CG  . GLN D 171 ? 1.1918 1.2198 1.2257 0.2969  -0.1184 0.0035  171 GLN D CG  
16011 C CD  . GLN D 171 ? 1.0712 1.0637 1.0905 0.2846  -0.0997 -0.0108 171 GLN D CD  
16012 O OE1 . GLN D 171 ? 1.1975 1.1696 1.2306 0.2859  -0.0796 -0.0058 171 GLN D OE1 
16013 N NE2 . GLN D 171 ? 1.2596 1.2437 1.2505 0.2727  -0.1062 -0.0290 171 GLN D NE2 
16014 N N   . ALA D 172 ? 1.1867 1.2947 1.3829 0.3149  -0.1154 0.0332  172 ALA D N   
16015 C CA  . ALA D 172 ? 1.0098 1.1415 1.2616 0.3124  -0.1097 0.0332  172 ALA D CA  
16016 C C   . ALA D 172 ? 1.0656 1.2435 1.3511 0.3234  -0.1312 0.0433  172 ALA D C   
16017 O O   . ALA D 172 ? 1.0473 1.2587 1.3782 0.3148  -0.1383 0.0365  172 ALA D O   
16018 C CB  . ALA D 172 ? 0.8714 0.9773 1.1316 0.3205  -0.0829 0.0422  172 ALA D CB  
16019 N N   . ILE D 173 ? 1.0979 1.2783 1.3633 0.3427  -0.1411 0.0608  173 ILE D N   
16020 C CA  . ILE D 173 ? 1.0062 1.2300 1.3008 0.3561  -0.1635 0.0739  173 ILE D CA  
16021 C C   . ILE D 173 ? 1.0959 1.3555 1.3951 0.3411  -0.1924 0.0595  173 ILE D C   
16022 O O   . ILE D 173 ? 1.0778 1.3804 1.4282 0.3390  -0.2057 0.0586  173 ILE D O   
16023 C CB  . ILE D 173 ? 0.9609 1.1739 1.2228 0.3790  -0.1685 0.0966  173 ILE D CB  
16024 C CG1 . ILE D 173 ? 0.9093 1.0939 1.1812 0.3947  -0.1413 0.1115  173 ILE D CG1 
16025 C CG2 . ILE D 173 ? 1.0102 1.2688 1.2898 0.3916  -0.1987 0.1100  173 ILE D CG2 
16026 C CD1 . ILE D 173 ? 1.0586 1.2691 1.3921 0.4085  -0.1358 0.1229  173 ILE D CD1 
16027 N N   . GLU D 174 ? 1.2635 1.5050 1.5103 0.3299  -0.2014 0.0471  174 GLU D N   
16028 C CA  . GLU D 174 ? 1.3295 1.5987 1.5710 0.3134  -0.2289 0.0298  174 GLU D CA  
16029 C C   . GLU D 174 ? 1.3537 1.6368 1.6400 0.2905  -0.2249 0.0092  174 GLU D C   
16030 O O   . GLU D 174 ? 1.4906 1.8158 1.8092 0.2806  -0.2480 0.0007  174 GLU D O   
16031 C CB  . GLU D 174 ? 1.3987 1.6361 1.5710 0.3058  -0.2321 0.0185  174 GLU D CB  
16032 C CG  . GLU D 174 ? 1.7064 1.9363 1.8308 0.3257  -0.2408 0.0378  174 GLU D CG  
16033 C CD  . GLU D 174 ? 1.9900 2.1846 2.0453 0.3195  -0.2376 0.0274  174 GLU D CD  
16034 O OE1 . GLU D 174 ? 1.6717 1.8408 1.7166 0.3018  -0.2240 0.0062  174 GLU D OE1 
16035 O OE2 . GLU D 174 ? 2.1374 2.3293 2.1490 0.3331  -0.2476 0.0413  174 GLU D OE2 
16036 N N   . GLY D 175 ? 1.2177 1.4663 1.5066 0.2821  -0.1961 0.0021  175 GLY D N   
16037 C CA  . GLY D 175 ? 1.0942 1.3495 1.4229 0.2608  -0.1876 -0.0150 175 GLY D CA  
16038 C C   . GLY D 175 ? 1.1303 1.4174 1.5257 0.2654  -0.1802 -0.0063 175 GLY D C   
16039 O O   . GLY D 175 ? 1.1534 1.4379 1.5809 0.2507  -0.1637 -0.0159 175 GLY D O   
16040 N N   . LYS D 176 ? 1.1394 1.4557 1.5567 0.2864  -0.1906 0.0129  176 LYS D N   
16041 C CA  . LYS D 176 ? 1.0158 1.3651 1.4987 0.2945  -0.1836 0.0227  176 LYS D CA  
16042 C C   . LYS D 176 ? 1.0679 1.3946 1.5741 0.2952  -0.1484 0.0249  176 LYS D C   
16043 O O   . LYS D 176 ? 1.1258 1.4739 1.6824 0.2844  -0.1394 0.0183  176 LYS D O   
16044 C CB  . LYS D 176 ? 0.9859 1.3884 1.5222 0.2794  -0.2054 0.0116  176 LYS D CB  
16045 C CG  . LYS D 176 ? 1.2113 1.6454 1.7305 0.2786  -0.2447 0.0093  176 LYS D CG  
16046 C CD  . LYS D 176 ? 1.2271 1.6845 1.7475 0.3067  -0.2615 0.0342  176 LYS D CD  
16047 C CE  . LYS D 176 ? 1.4044 1.8959 1.9063 0.3051  -0.3023 0.0325  176 LYS D CE  
16048 N NZ  . LYS D 176 ? 1.3824 1.8665 1.8429 0.3309  -0.3132 0.0557  176 LYS D NZ  
16049 N N   . VAL D 177 ? 1.0106 1.2935 1.4784 0.3069  -0.1282 0.0336  177 VAL D N   
16050 C CA  . VAL D 177 ? 0.9459 1.2052 1.4294 0.3082  -0.0953 0.0357  177 VAL D CA  
16051 C C   . VAL D 177 ? 0.9849 1.2593 1.5012 0.3316  -0.0877 0.0535  177 VAL D C   
16052 O O   . VAL D 177 ? 0.9892 1.2700 1.4931 0.3500  -0.1023 0.0678  177 VAL D O   
16053 C CB  . VAL D 177 ? 0.8071 1.0112 1.2374 0.3055  -0.0757 0.0332  177 VAL D CB  
16054 C CG1 . VAL D 177 ? 0.8173 1.0037 1.2121 0.2862  -0.0837 0.0173  177 VAL D CG1 
16055 C CG2 . VAL D 177 ? 0.9136 1.0953 1.3099 0.3265  -0.0741 0.0489  177 VAL D CG2 
16056 N N   . LYS D 178 ? 0.8392 1.1172 1.3946 0.3309  -0.0644 0.0528  178 LYS D N   
16057 C CA  . LYS D 178 ? 0.9201 1.2079 1.5089 0.3525  -0.0517 0.0673  178 LYS D CA  
16058 C C   . LYS D 178 ? 0.9701 1.2078 1.5200 0.3624  -0.0279 0.0727  178 LYS D C   
16059 O O   . LYS D 178 ? 1.1258 1.3373 1.6675 0.3524  -0.0039 0.0645  178 LYS D O   
16060 C CB  . LYS D 178 ? 0.8832 1.2005 1.5343 0.3467  -0.0361 0.0625  178 LYS D CB  
16061 C CG  . LYS D 178 ? 0.7835 1.1561 1.4834 0.3373  -0.0602 0.0578  178 LYS D CG  
16062 C CD  . LYS D 178 ? 0.8869 1.2935 1.6572 0.3360  -0.0430 0.0569  178 LYS D CD  
16063 C CE  . LYS D 178 ? 1.0628 1.5331 1.8946 0.3375  -0.0689 0.0597  178 LYS D CE  
16064 N NZ  . LYS D 178 ? 1.0959 1.5980 1.9947 0.3543  -0.0530 0.0699  178 LYS D NZ  
16065 N N   . MET D 179 ? 0.8585 1.0826 1.3839 0.3813  -0.0348 0.0869  179 MET D N   
16066 C CA  . MET D 179 ? 0.8928 1.0700 1.3828 0.3897  -0.0141 0.0917  179 MET D CA  
16067 C C   . MET D 179 ? 1.0005 1.1759 1.5219 0.4091  0.0046  0.1021  179 MET D C   
16068 O O   . MET D 179 ? 1.0938 1.3026 1.6565 0.4245  -0.0045 0.1130  179 MET D O   
16069 C CB  . MET D 179 ? 1.0377 1.1939 1.4783 0.3967  -0.0287 0.1002  179 MET D CB  
16070 C CG  . MET D 179 ? 1.0351 1.1839 1.4379 0.3783  -0.0422 0.0884  179 MET D CG  
16071 S SD  . MET D 179 ? 1.1558 1.2673 1.4949 0.3850  -0.0470 0.0965  179 MET D SD  
16072 C CE  . MET D 179 ? 1.1598 1.2893 1.4753 0.3705  -0.0736 0.0858  179 MET D CE  
16073 N N   . GLY D 180 ? 0.9418 1.0777 1.4429 0.4085  0.0302  0.0983  180 GLY D N   
16074 C CA  . GLY D 180 ? 0.8851 1.0098 1.4087 0.4248  0.0521  0.1044  180 GLY D CA  
16075 C C   . GLY D 180 ? 0.9797 1.0675 1.4825 0.4146  0.0800  0.0925  180 GLY D C   
16076 O O   . GLY D 180 ? 0.9192 1.0014 1.4062 0.3950  0.0834  0.0803  180 GLY D O   
16077 N N   . LEU D 181 ? 1.1315 1.1931 1.6335 0.4275  0.0999  0.0958  181 LEU D N   
16078 C CA  . LEU D 181 ? 0.8091 0.8351 1.2880 0.4181  0.1255  0.0839  181 LEU D CA  
16079 C C   . LEU D 181 ? 1.0036 1.0475 1.5091 0.4067  0.1412  0.0727  181 LEU D C   
16080 O O   . LEU D 181 ? 0.9949 1.0192 1.4727 0.3898  0.1516  0.0620  181 LEU D O   
16081 C CB  . LEU D 181 ? 1.1619 1.1592 1.6410 0.4346  0.1439  0.0881  181 LEU D CB  
16082 C CG  . LEU D 181 ? 1.0291 0.9914 1.4872 0.4265  0.1713  0.0744  181 LEU D CG  
16083 C CD1 . LEU D 181 ? 0.8149 0.7467 1.2197 0.4088  0.1675  0.0671  181 LEU D CD1 
16084 C CD2 . LEU D 181 ? 1.1229 1.0605 1.5822 0.4383  0.1856  0.0754  181 LEU D CD2 
16085 N N   . ASP D 182 ? 1.0564 1.1382 1.6167 0.4162  0.1431  0.0765  182 ASP D N   
16086 C CA  . ASP D 182 ? 0.9814 1.0834 1.5724 0.4055  0.1599  0.0670  182 ASP D CA  
16087 C C   . ASP D 182 ? 0.9044 1.0256 1.4912 0.3843  0.1438  0.0613  182 ASP D C   
16088 O O   . ASP D 182 ? 0.9248 1.0408 1.5070 0.3679  0.1591  0.0516  182 ASP D O   
16089 C CB  . ASP D 182 ? 1.0132 1.1538 1.6705 0.4221  0.1666  0.0732  182 ASP D CB  
16090 C CG  . ASP D 182 ? 1.3494 1.4682 2.0172 0.4368  0.1973  0.0715  182 ASP D CG  
16091 O OD1 . ASP D 182 ? 1.3295 1.4325 1.9888 0.4267  0.2240  0.0595  182 ASP D OD1 
16092 O OD2 . ASP D 182 ? 1.7237 1.8394 2.4064 0.4583  0.1953  0.0821  182 ASP D OD2 
16093 N N   . LEU D 183 ? 0.8462 0.9870 1.4318 0.3843  0.1139  0.0671  183 LEU D N   
16094 C CA  . LEU D 183 ? 0.8393 0.9949 1.4187 0.3640  0.0974  0.0601  183 LEU D CA  
16095 C C   . LEU D 183 ? 0.8903 1.0043 1.4108 0.3485  0.0997  0.0528  183 LEU D C   
16096 O O   . LEU D 183 ? 0.9540 1.0727 1.4645 0.3317  0.0882  0.0464  183 LEU D O   
16097 C CB  . LEU D 183 ? 0.8414 1.0292 1.4334 0.3692  0.0645  0.0671  183 LEU D CB  
16098 C CG  . LEU D 183 ? 0.8261 1.0667 1.4841 0.3791  0.0559  0.0732  183 LEU D CG  
16099 C CD1 . LEU D 183 ? 0.8750 1.1364 1.5351 0.3945  0.0262  0.0861  183 LEU D CD1 
16100 C CD2 . LEU D 183 ? 0.7607 1.0345 1.4533 0.3588  0.0523  0.0626  183 LEU D CD2 
16101 N N   . ARG D 184 ? 0.8102 0.8841 1.2943 0.3540  0.1142  0.0536  184 ARG D N   
16102 C CA  . ARG D 184 ? 0.8088 0.8442 1.2410 0.3415  0.1175  0.0482  184 ARG D CA  
16103 C C   . ARG D 184 ? 0.9554 0.9848 1.3570 0.3374  0.0937  0.0500  184 ARG D C   
16104 O O   . ARG D 184 ? 1.2508 1.2604 1.6219 0.3231  0.0930  0.0441  184 ARG D O   
16105 C CB  . ARG D 184 ? 1.0185 1.0497 1.4498 0.3229  0.1331  0.0388  184 ARG D CB  
16106 C CG  . ARG D 184 ? 1.0054 1.0429 1.4648 0.3265  0.1593  0.0365  184 ARG D CG  
16107 C CD  . ARG D 184 ? 0.9585 0.9770 1.3986 0.3101  0.1794  0.0292  184 ARG D CD  
16108 N NE  . ARG D 184 ? 1.0193 1.0342 1.4726 0.3156  0.2074  0.0265  184 ARG D NE  
16109 C CZ  . ARG D 184 ? 1.0735 1.0729 1.5109 0.3040  0.2296  0.0212  184 ARG D CZ  
16110 N NH1 . ARG D 184 ? 0.9940 0.9799 1.4039 0.2867  0.2264  0.0197  184 ARG D NH1 
16111 N NH2 . ARG D 184 ? 1.2226 1.2186 1.6702 0.3102  0.2560  0.0178  184 ARG D NH2 
16112 N N   . VAL D 185 ? 0.8574 0.9036 1.2674 0.3506  0.0753  0.0587  185 VAL D N   
16113 C CA  . VAL D 185 ? 1.0133 1.0528 1.3903 0.3484  0.0541  0.0608  185 VAL D CA  
16114 C C   . VAL D 185 ? 0.9601 0.9904 1.3264 0.3679  0.0491  0.0739  185 VAL D C   
16115 O O   . VAL D 185 ? 0.9744 1.0327 1.3695 0.3814  0.0384  0.0831  185 VAL D O   
16116 C CB  . VAL D 185 ? 1.0244 1.0993 1.4201 0.3405  0.0322  0.0572  185 VAL D CB  
16117 C CG1 . VAL D 185 ? 0.7718 0.8389 1.1305 0.3396  0.0120  0.0584  185 VAL D CG1 
16118 C CG2 . VAL D 185 ? 1.0179 1.1002 1.4280 0.3204  0.0389  0.0447  185 VAL D CG2 
16119 N N   . ILE D 186 ? 0.8913 0.8846 1.2202 0.3693  0.0566  0.0757  186 ILE D N   
16120 C CA  . ILE D 186 ? 0.9282 0.9082 1.2484 0.3872  0.0558  0.0890  186 ILE D CA  
16121 C C   . ILE D 186 ? 0.9067 0.8733 1.1881 0.3862  0.0417  0.0935  186 ILE D C   
16122 O O   . ILE D 186 ? 0.9878 0.9287 1.2387 0.3750  0.0472  0.0869  186 ILE D O   
16123 C CB  . ILE D 186 ? 0.8400 0.7878 1.1540 0.3909  0.0787  0.0877  186 ILE D CB  
16124 C CG1 . ILE D 186 ? 1.1177 1.0774 1.4679 0.3933  0.0954  0.0827  186 ILE D CG1 
16125 C CG2 . ILE D 186 ? 0.9004 0.8293 1.2040 0.4068  0.0792  0.1007  186 ILE D CG2 
16126 C CD1 . ILE D 186 ? 0.8170 0.7460 1.1507 0.3852  0.1177  0.0727  186 ILE D CD1 
16127 N N   . PRO D 187 ? 0.9054 0.8887 1.1864 0.3978  0.0244  0.1052  187 PRO D N   
16128 C CA  . PRO D 187 ? 0.9329 0.9015 1.1742 0.3982  0.0143  0.1105  187 PRO D CA  
16129 C C   . PRO D 187 ? 0.9975 0.9340 1.2232 0.4094  0.0271  0.1217  187 PRO D C   
16130 O O   . PRO D 187 ? 1.1128 1.0527 1.3579 0.4254  0.0296  0.1341  187 PRO D O   
16131 C CB  . PRO D 187 ? 0.8313 0.8331 1.0807 0.4073  -0.0087 0.1197  187 PRO D CB  
16132 C CG  . PRO D 187 ? 1.0567 1.0818 1.3528 0.4208  -0.0065 0.1275  187 PRO D CG  
16133 C CD  . PRO D 187 ? 0.8718 0.8903 1.1901 0.4111  0.0136  0.1144  187 PRO D CD  
16134 N N   . LEU D 188 ? 0.8181 0.7246 1.0126 0.4009  0.0354  0.1175  188 LEU D N   
16135 C CA  . LEU D 188 ? 0.8361 0.7115 1.0194 0.4088  0.0488  0.1265  188 LEU D CA  
16136 C C   . LEU D 188 ? 1.0582 0.9300 1.2197 0.4195  0.0398  0.1423  188 LEU D C   
16137 O O   . LEU D 188 ? 1.2641 1.1298 1.4353 0.4349  0.0436  0.1572  188 LEU D O   
16138 C CB  . LEU D 188 ? 0.9209 0.7690 1.0844 0.3945  0.0607  0.1155  188 LEU D CB  
16139 C CG  . LEU D 188 ? 0.8676 0.7152 1.0453 0.3835  0.0706  0.1013  188 LEU D CG  
16140 C CD1 . LEU D 188 ? 1.0560 0.8985 1.2143 0.3669  0.0684  0.0901  188 LEU D CD1 
16141 C CD2 . LEU D 188 ? 1.0932 0.9156 1.2752 0.3858  0.0880  0.1003  188 LEU D CD2 
16142 N N   . GLY D 189 ? 1.1050 0.9786 1.2374 0.4120  0.0300  0.1394  189 GLY D N   
16143 C CA  . GLY D 189 ? 1.1615 1.0296 1.2669 0.4210  0.0236  0.1539  189 GLY D CA  
16144 C C   . GLY D 189 ? 1.1562 1.0260 1.2288 0.4107  0.0150  0.1462  189 GLY D C   
16145 O O   . GLY D 189 ? 1.2174 1.0858 1.2880 0.3961  0.0168  0.1299  189 GLY D O   
16146 N N   . TYR D 190 ? 1.1242 0.9951 1.1694 0.4186  0.0069  0.1581  190 TYR D N   
16147 C CA  . TYR D 190 ? 1.0662 0.9370 1.0763 0.4101  0.0002  0.1503  190 TYR D CA  
16148 C C   . TYR D 190 ? 1.2650 1.1052 1.2536 0.4040  0.0173  0.1485  190 TYR D C   
16149 O O   . TYR D 190 ? 1.3580 1.1945 1.3277 0.3933  0.0172  0.1357  190 TYR D O   
16150 C CB  . TYR D 190 ? 1.1931 1.0791 1.1785 0.4208  -0.0160 0.1633  190 TYR D CB  
16151 C CG  . TYR D 190 ? 1.1589 1.0808 1.1674 0.4249  -0.0365 0.1632  190 TYR D CG  
16152 C CD1 . TYR D 190 ? 1.2425 1.1867 1.2522 0.4121  -0.0513 0.1452  190 TYR D CD1 
16153 C CD2 . TYR D 190 ? 1.0343 0.9680 1.0684 0.4412  -0.0404 0.1808  190 TYR D CD2 
16154 C CE1 . TYR D 190 ? 1.1492 1.1296 1.1857 0.4145  -0.0706 0.1446  190 TYR D CE1 
16155 C CE2 . TYR D 190 ? 1.3269 1.2971 1.3885 0.4455  -0.0594 0.1814  190 TYR D CE2 
16156 C CZ  . TYR D 190 ? 1.1850 1.1801 1.2486 0.4316  -0.0750 0.1631  190 TYR D CZ  
16157 O OH  . TYR D 190 ? 1.2389 1.2733 1.3343 0.4348  -0.0945 0.1635  190 TYR D OH  
16158 N N   . ASP D 191 ? 1.2258 1.0442 1.2198 0.4107  0.0322  0.1607  191 ASP D N   
16159 C CA  . ASP D 191 ? 1.3284 1.1208 1.3084 0.4046  0.0483  0.1597  191 ASP D CA  
16160 C C   . ASP D 191 ? 1.2320 1.0182 1.2283 0.3905  0.0549  0.1424  191 ASP D C   
16161 O O   . ASP D 191 ? 1.1333 0.9279 1.1544 0.3878  0.0528  0.1355  191 ASP D O   
16162 C CB  . ASP D 191 ? 1.1877 0.9591 1.1734 0.4139  0.0620  0.1770  191 ASP D CB  
16163 C CG  . ASP D 191 ? 1.3436 1.1137 1.3061 0.4275  0.0596  0.1975  191 ASP D CG  
16164 O OD1 . ASP D 191 ? 1.3857 1.1686 1.3197 0.4282  0.0485  0.1972  191 ASP D OD1 
16165 O OD2 . ASP D 191 ? 1.5196 1.2744 1.4909 0.4370  0.0691  0.2138  191 ASP D OD2 
16166 N N   . VAL D 192 ? 1.2224 0.9944 1.2051 0.3822  0.0634  0.1364  192 VAL D N   
16167 C CA  . VAL D 192 ? 1.2229 0.9889 1.2192 0.3698  0.0685  0.1224  192 VAL D CA  
16168 C C   . VAL D 192 ? 1.1764 0.9311 1.1960 0.3694  0.0774  0.1247  192 VAL D C   
16169 O O   . VAL D 192 ? 1.1261 0.8841 1.1615 0.3625  0.0766  0.1146  192 VAL D O   
16170 C CB  . VAL D 192 ? 1.0717 0.8253 1.0520 0.3634  0.0764  0.1182  192 VAL D CB  
16171 C CG1 . VAL D 192 ? 0.8737 0.6198 0.8701 0.3526  0.0815  0.1078  192 VAL D CG1 
16172 C CG2 . VAL D 192 ? 1.1348 0.8975 1.0913 0.3620  0.0686  0.1111  192 VAL D CG2 
16173 N N   . THR D 193 ? 1.1574 0.8976 1.1778 0.3763  0.0864  0.1375  193 THR D N   
16174 C CA  . THR D 193 ? 1.1118 0.8377 1.1523 0.3753  0.0957  0.1384  193 THR D CA  
16175 C C   . THR D 193 ? 1.0610 0.7963 1.1210 0.3785  0.0920  0.1343  193 THR D C   
16176 O O   . THR D 193 ? 1.0832 0.8097 1.1573 0.3712  0.0982  0.1274  193 THR D O   
16177 C CB  . THR D 193 ? 1.1559 0.8663 1.1944 0.3800  0.1051  0.1528  193 THR D CB  
16178 O OG1 . THR D 193 ? 1.1242 0.8417 1.1528 0.3948  0.1000  0.1673  193 THR D OG1 
16179 C CG2 . THR D 193 ? 1.0127 0.7109 1.0400 0.3751  0.1139  0.1555  193 THR D CG2 
16180 N N   . SER D 194 ? 1.0271 0.7831 1.0884 0.3858  0.0811  0.1366  194 SER D N   
16181 C CA  . SER D 194 ? 1.1138 0.8821 1.1985 0.3896  0.0788  0.1333  194 SER D CA  
16182 C C   . SER D 194 ? 1.1062 0.8765 1.2004 0.3767  0.0812  0.1167  194 SER D C   
16183 O O   . SER D 194 ? 1.0594 0.8321 1.1727 0.3780  0.0858  0.1127  194 SER D O   
16184 C CB  . SER D 194 ? 1.0608 0.8561 1.1476 0.3978  0.0642  0.1380  194 SER D CB  
16185 O OG  . SER D 194 ? 1.2581 1.0524 1.3305 0.4100  0.0603  0.1547  194 SER D OG  
16186 N N   . VAL D 195 ? 1.0087 0.7757 1.0892 0.3650  0.0799  0.1083  195 VAL D N   
16187 C CA  . VAL D 195 ? 1.0082 0.7755 1.0944 0.3527  0.0819  0.0949  195 VAL D CA  
16188 C C   . VAL D 195 ? 1.0962 0.8443 1.1884 0.3493  0.0932  0.0922  195 VAL D C   
16189 O O   . VAL D 195 ? 1.0216 0.7694 1.1180 0.3411  0.0960  0.0826  195 VAL D O   
16190 C CB  . VAL D 195 ? 0.9429 0.7091 1.0139 0.3428  0.0780  0.0887  195 VAL D CB  
16191 C CG1 . VAL D 195 ? 0.8610 0.6079 0.9234 0.3390  0.0849  0.0908  195 VAL D CG1 
16192 C CG2 . VAL D 195 ? 0.8822 0.6554 0.9592 0.3324  0.0764  0.0775  195 VAL D CG2 
16193 N N   . ILE D 196 ? 1.1942 0.9261 1.2856 0.3547  0.0996  0.1001  196 ILE D N   
16194 C CA  . ILE D 196 ? 1.0889 0.8009 1.1848 0.3488  0.1094  0.0952  196 ILE D CA  
16195 C C   . ILE D 196 ? 1.0483 0.7613 1.1586 0.3516  0.1151  0.0898  196 ILE D C   
16196 O O   . ILE D 196 ? 1.1212 0.8207 1.2312 0.3449  0.1224  0.0804  196 ILE D O   
16197 C CB  . ILE D 196 ? 0.9961 0.6947 1.0904 0.3475  0.1133  0.1030  196 ILE D CB  
16198 C CG1 . ILE D 196 ? 1.0458 0.7248 1.1423 0.3376  0.1206  0.0958  196 ILE D CG1 
16199 C CG2 . ILE D 196 ? 0.8854 0.5862 0.9884 0.3569  0.1146  0.1122  196 ILE D CG2 
16200 C CD1 . ILE D 196 ? 1.0714 0.7488 1.1611 0.3297  0.1184  0.0871  196 ILE D CD1 
16201 N N   . HIS D 197 ? 0.9693 0.6975 1.0918 0.3619  0.1123  0.0955  197 HIS D N   
16202 C CA  . HIS D 197 ? 1.1618 0.8917 1.3025 0.3658  0.1199  0.0910  197 HIS D CA  
16203 C C   . HIS D 197 ? 1.1455 0.8827 1.2893 0.3612  0.1234  0.0796  197 HIS D C   
16204 O O   . HIS D 197 ? 1.3363 1.0673 1.4898 0.3618  0.1346  0.0724  197 HIS D O   
16205 C CB  . HIS D 197 ? 1.1211 0.8678 1.2779 0.3789  0.1149  0.1019  197 HIS D CB  
16206 C CG  . HIS D 197 ? 1.0782 0.8182 1.2279 0.3831  0.1112  0.1151  197 HIS D CG  
16207 N ND1 . HIS D 197 ? 1.2104 0.9269 1.3553 0.3773  0.1192  0.1158  197 HIS D ND1 
16208 C CD2 . HIS D 197 ? 0.9751 0.7280 1.1212 0.3932  0.1015  0.1288  197 HIS D CD2 
16209 C CE1 . HIS D 197 ? 1.1103 0.8252 1.2495 0.3834  0.1158  0.1303  197 HIS D CE1 
16210 N NE2 . HIS D 197 ? 1.1766 0.9131 1.3144 0.3934  0.1049  0.1386  197 HIS D NE2 
16211 N N   . VAL D 198 ? 1.0665 0.8179 1.2011 0.3529  0.1138  0.0767  198 VAL D N   
16212 C CA  . VAL D 198 ? 1.0512 0.8096 1.1857 0.3422  0.1164  0.0657  198 VAL D CA  
16213 C C   . VAL D 198 ? 1.0813 0.8179 1.1974 0.3308  0.1216  0.0585  198 VAL D C   
16214 O O   . VAL D 198 ? 0.9951 0.7264 1.1094 0.3252  0.1304  0.0499  198 VAL D O   
16215 C CB  . VAL D 198 ? 0.8862 0.6643 1.0189 0.3367  0.1052  0.0651  198 VAL D CB  
16216 C CG1 . VAL D 198 ? 0.8374 0.6147 0.9635 0.3234  0.1085  0.0560  198 VAL D CG1 
16217 C CG2 . VAL D 198 ? 0.9874 0.7914 1.1413 0.3455  0.0990  0.0692  198 VAL D CG2 
16218 N N   . VAL D 199 ? 0.9859 0.7117 1.0890 0.3275  0.1165  0.0622  199 VAL D N   
16219 C CA  . VAL D 199 ? 0.9952 0.7034 1.0841 0.3168  0.1185  0.0566  199 VAL D CA  
16220 C C   . VAL D 199 ? 1.0950 0.7863 1.1862 0.3174  0.1299  0.0502  199 VAL D C   
16221 O O   . VAL D 199 ? 1.1146 0.7964 1.1939 0.3078  0.1334  0.0408  199 VAL D O   
16222 C CB  . VAL D 199 ? 0.9954 0.6968 1.0783 0.3158  0.1129  0.0632  199 VAL D CB  
16223 C CG1 . VAL D 199 ? 0.9052 0.5896 0.9804 0.3063  0.1146  0.0583  199 VAL D CG1 
16224 C CG2 . VAL D 199 ? 0.7770 0.4910 0.8541 0.3134  0.1039  0.0661  199 VAL D CG2 
16225 N N   . THR D 200 ? 1.0295 0.7163 1.1349 0.3291  0.1358  0.0552  200 THR D N   
16226 C CA  . THR D 200 ? 1.0525 0.7205 1.1628 0.3312  0.1486  0.0486  200 THR D CA  
16227 C C   . THR D 200 ? 1.1263 0.8003 1.2404 0.3312  0.1578  0.0391  200 THR D C   
16228 O O   . THR D 200 ? 1.2015 0.8580 1.3101 0.3275  0.1690  0.0282  200 THR D O   
16229 C CB  . THR D 200 ? 1.1827 0.8451 1.3091 0.3437  0.1523  0.0585  200 THR D CB  
16230 O OG1 . THR D 200 ? 1.4035 1.0911 1.5436 0.3530  0.1462  0.0670  200 THR D OG1 
16231 C CG2 . THR D 200 ? 0.9810 0.6348 1.1016 0.3396  0.1464  0.0663  200 THR D CG2 
16232 N N   . ILE D 201 ? 1.0939 0.7922 1.2174 0.3344  0.1540  0.0421  201 ILE D N   
16233 C CA  . ILE D 201 ? 1.0465 0.7532 1.1766 0.3336  0.1643  0.0340  201 ILE D CA  
16234 C C   . ILE D 201 ? 1.0455 0.7408 1.1492 0.3181  0.1670  0.0233  201 ILE D C   
16235 O O   . ILE D 201 ? 1.0213 0.7055 1.1183 0.3153  0.1804  0.0129  201 ILE D O   
16236 C CB  . ILE D 201 ? 0.9111 0.6483 1.0587 0.3372  0.1577  0.0396  201 ILE D CB  
16237 C CG1 . ILE D 201 ? 0.9159 0.6675 1.0898 0.3535  0.1540  0.0504  201 ILE D CG1 
16238 C CG2 . ILE D 201 ? 0.8265 0.5730 0.9793 0.3323  0.1691  0.0312  201 ILE D CG2 
16239 C CD1 . ILE D 201 ? 0.9113 0.6943 1.1011 0.3555  0.1428  0.0557  201 ILE D CD1 
16240 N N   . ALA D 202 ? 0.9506 0.6482 1.0383 0.3087  0.1544  0.0263  202 ALA D N   
16241 C CA  . ALA D 202 ? 1.0044 0.6930 1.0666 0.2950  0.1535  0.0196  202 ALA D CA  
16242 C C   . ALA D 202 ? 1.1085 0.7733 1.1541 0.2892  0.1562  0.0117  202 ALA D C   
16243 O O   . ALA D 202 ? 1.2295 0.8839 1.2549 0.2808  0.1623  0.0020  202 ALA D O   
16244 C CB  . ALA D 202 ? 0.8241 0.5211 0.8789 0.2890  0.1393  0.0266  202 ALA D CB  
16245 N N   . ILE D 203 ? 0.9973 0.6531 1.0503 0.2929  0.1520  0.0155  203 ILE D N   
16246 C CA  . ILE D 203 ? 0.9705 0.6039 1.0119 0.2858  0.1538  0.0072  203 ILE D CA  
16247 C C   . ILE D 203 ? 1.1416 0.7592 1.1838 0.2890  0.1707  -0.0045 203 ILE D C   
16248 O O   . ILE D 203 ? 1.2460 0.8477 1.2671 0.2789  0.1750  -0.0176 203 ILE D O   
16249 C CB  . ILE D 203 ? 0.8728 0.5008 0.9260 0.2885  0.1472  0.0154  203 ILE D CB  
16250 C CG1 . ILE D 203 ? 0.9342 0.5736 0.9818 0.2822  0.1323  0.0230  203 ILE D CG1 
16251 C CG2 . ILE D 203 ? 0.9742 0.5777 1.0242 0.2826  0.1526  0.0059  203 ILE D CG2 
16252 C CD1 . ILE D 203 ? 1.1319 0.7738 1.1938 0.2881  0.1279  0.0345  203 ILE D CD1 
16253 N N   . ARG D 204 ? 1.0028 0.6248 1.0688 0.3032  0.1802  0.0000  204 ARG D N   
16254 C CA  . ARG D 204 ? 1.0897 0.6965 1.1611 0.3086  0.1985  -0.0107 204 ARG D CA  
16255 C C   . ARG D 204 ? 1.1710 0.7815 1.2266 0.3028  0.2083  -0.0215 204 ARG D C   
16256 O O   . ARG D 204 ? 1.1830 0.7742 1.2274 0.3003  0.2229  -0.0358 204 ARG D O   
16257 C CB  . ARG D 204 ? 1.0168 0.6309 1.1212 0.3272  0.2055  -0.0008 204 ARG D CB  
16258 C CG  . ARG D 204 ? 1.1443 0.7418 1.2602 0.3333  0.2042  0.0064  204 ARG D CG  
16259 C CD  . ARG D 204 ? 1.2188 0.8299 1.3638 0.3483  0.2056  0.0186  204 ARG D CD  
16260 N NE  . ARG D 204 ? 1.2587 0.8993 1.4114 0.3527  0.1899  0.0338  204 ARG D NE  
16261 C CZ  . ARG D 204 ? 1.2078 0.8707 1.3818 0.3626  0.1844  0.0451  204 ARG D CZ  
16262 N NH1 . ARG D 204 ? 0.9430 0.6038 1.1358 0.3700  0.1931  0.0448  204 ARG D NH1 
16263 N NH2 . ARG D 204 ? 1.1738 0.8604 1.3504 0.3658  0.1700  0.0566  204 ARG D NH2 
16264 N N   . ALA D 205 ? 1.0661 0.6991 1.1190 0.3000  0.2018  -0.0153 205 ALA D N   
16265 C CA  . ALA D 205 ? 1.0761 0.7122 1.1128 0.2935  0.2124  -0.0235 205 ALA D CA  
16266 C C   . ALA D 205 ? 1.2593 0.8750 1.2563 0.2783  0.2111  -0.0353 205 ALA D C   
16267 O O   . ALA D 205 ? 1.2893 0.8947 1.2669 0.2739  0.2258  -0.0473 205 ALA D O   
16268 C CB  . ALA D 205 ? 0.9150 0.5765 0.9572 0.2916  0.2043  -0.0134 205 ALA D CB  
16269 N N   . ALA D 206 ? 1.1003 0.7112 1.0851 0.2703  0.1935  -0.0318 206 ALA D N   
16270 C CA  . ALA D 206 ? 1.1169 0.7119 1.0665 0.2557  0.1876  -0.0417 206 ALA D CA  
16271 C C   . ALA D 206 ? 1.3156 0.8843 1.2578 0.2535  0.1983  -0.0580 206 ALA D C   
16272 O O   . ALA D 206 ? 1.4286 0.9824 1.3383 0.2429  0.2026  -0.0722 206 ALA D O   
16273 C CB  . ALA D 206 ? 1.1063 0.7072 1.0542 0.2494  0.1659  -0.0323 206 ALA D CB  
16274 N N   . LEU D 207 ? 1.3537 0.9151 1.3241 0.2633  0.2028  -0.0563 207 LEU D N   
16275 C CA  . LEU D 207 ? 1.3596 0.8928 1.3276 0.2618  0.2144  -0.0716 207 LEU D CA  
16276 C C   . LEU D 207 ? 1.3273 0.8509 1.2944 0.2689  0.2388  -0.0835 207 LEU D C   
16277 O O   . LEU D 207 ? 1.4404 0.9403 1.3834 0.2610  0.2498  -0.1026 207 LEU D O   
16278 C CB  . LEU D 207 ? 1.2321 0.7592 1.2326 0.2712  0.2130  -0.0628 207 LEU D CB  
16279 C CG  . LEU D 207 ? 1.0104 0.5442 1.0153 0.2648  0.1930  -0.0520 207 LEU D CG  
16280 C CD1 . LEU D 207 ? 1.0482 0.5822 1.0858 0.2777  0.1942  -0.0379 207 LEU D CD1 
16281 C CD2 . LEU D 207 ? 1.2838 0.7983 1.2693 0.2478  0.1863  -0.0659 207 LEU D CD2 
16282 N N   . ILE D 208 ? 1.2007 0.7435 1.1948 0.2834  0.2474  -0.0730 208 ILE D N   
16283 C CA  . ILE D 208 ? 1.2502 0.7892 1.2531 0.2926  0.2719  -0.0818 208 ILE D CA  
16284 C C   . ILE D 208 ? 1.2506 0.7924 1.2202 0.2827  0.2807  -0.0914 208 ILE D C   
16285 O O   . ILE D 208 ? 1.4752 0.9943 1.4201 0.2774  0.2969  -0.1100 208 ILE D O   
16286 C CB  . ILE D 208 ? 1.1363 0.6996 1.1850 0.3116  0.2756  -0.0657 208 ILE D CB  
16287 C CG1 . ILE D 208 ? 1.1184 0.6715 1.1962 0.3237  0.2735  -0.0578 208 ILE D CG1 
16288 C CG2 . ILE D 208 ? 1.0611 0.6295 1.1229 0.3206  0.3000  -0.0726 208 ILE D CG2 
16289 C CD1 . ILE D 208 ? 1.1623 0.7430 1.2776 0.3396  0.2659  -0.0374 208 ILE D CD1 
16290 N N   . PHE D 209 ? 1.2627 0.8302 1.2303 0.2799  0.2714  -0.0792 209 PHE D N   
16291 C CA  . PHE D 209 ? 1.2233 0.7943 1.1614 0.2712  0.2811  -0.0847 209 PHE D CA  
16292 C C   . PHE D 209 ? 1.2945 0.8519 1.1832 0.2536  0.2682  -0.0910 209 PHE D C   
16293 O O   . PHE D 209 ? 1.4454 0.9875 1.2972 0.2453  0.2808  -0.1049 209 PHE D O   
16294 C CB  . PHE D 209 ? 1.2137 0.8160 1.1728 0.2750  0.2780  -0.0687 209 PHE D CB  
16295 C CG  . PHE D 209 ? 1.2547 0.8762 1.2653 0.2919  0.2839  -0.0600 209 PHE D CG  
16296 C CD1 . PHE D 209 ? 1.2277 0.8494 1.2595 0.3023  0.3084  -0.0672 209 PHE D CD1 
16297 C CD2 . PHE D 209 ? 1.2602 0.8996 1.2978 0.2979  0.2647  -0.0448 209 PHE D CD2 
16298 C CE1 . PHE D 209 ? 1.1139 0.7562 1.1958 0.3187  0.3114  -0.0577 209 PHE D CE1 
16299 C CE2 . PHE D 209 ? 1.0693 0.7276 1.1514 0.3133  0.2674  -0.0362 209 PHE D CE2 
16300 C CZ  . PHE D 209 ? 1.0682 0.7287 1.1734 0.3239  0.2896  -0.0421 209 PHE D CZ  
16301 N N   . GLY D 210 ? 1.1760 0.7401 1.0639 0.2482  0.2433  -0.0805 210 GLY D N   
16302 C CA  . GLY D 210 ? 1.2113 0.7669 1.0582 0.2326  0.2273  -0.0838 210 GLY D CA  
16303 C C   . GLY D 210 ? 1.2882 0.8160 1.1087 0.2237  0.2299  -0.1038 210 GLY D C   
16304 O O   . GLY D 210 ? 1.3115 0.8303 1.0893 0.2100  0.2225  -0.1117 210 GLY D O   
16305 N N   . GLY D 211 ? 1.1721 0.6860 1.0175 0.2313  0.2397  -0.1118 211 GLY D N   
16306 C CA  . GLY D 211 ? 1.2545 0.7390 1.0799 0.2226  0.2436  -0.1326 211 GLY D CA  
16307 C C   . GLY D 211 ? 1.3024 0.7847 1.1193 0.2098  0.2178  -0.1317 211 GLY D C   
16308 O O   . GLY D 211 ? 1.4848 0.9475 1.2715 0.1960  0.2140  -0.1494 211 GLY D O   
16309 N N   . ILE D 212 ? 1.2169 0.7200 1.0613 0.2139  0.2002  -0.1119 212 ILE D N   
16310 C CA  . ILE D 212 ? 1.2090 0.7143 1.0533 0.2032  0.1767  -0.1086 212 ILE D CA  
16311 C C   . ILE D 212 ? 1.3807 0.8685 1.2533 0.2057  0.1812  -0.1145 212 ILE D C   
16312 O O   . ILE D 212 ? 1.5121 0.9963 1.4139 0.2202  0.1965  -0.1101 212 ILE D O   
16313 C CB  . ILE D 212 ? 1.3374 0.8709 1.1989 0.2070  0.1586  -0.0854 212 ILE D CB  
16314 C CG1 . ILE D 212 ? 1.1672 0.7168 1.0100 0.2085  0.1596  -0.0766 212 ILE D CG1 
16315 C CG2 . ILE D 212 ? 1.3901 0.9280 1.2490 0.1950  0.1349  -0.0828 212 ILE D CG2 
16316 C CD1 . ILE D 212 ? 1.4021 0.9459 1.1964 0.1948  0.1543  -0.0849 212 ILE D CD1 
16317 N N   . LYS D 213 ? 1.3802 0.8572 1.2457 0.1914  0.1679  -0.1237 213 LYS D N   
16318 C CA  . LYS D 213 ? 1.4504 0.9080 1.3425 0.1911  0.1727  -0.1296 213 LYS D CA  
16319 C C   . LYS D 213 ? 1.3393 0.8142 1.2663 0.1952  0.1591  -0.1091 213 LYS D C   
16320 O O   . LYS D 213 ? 1.3250 0.8235 1.2494 0.1922  0.1412  -0.0965 213 LYS D O   
16321 C CB  . LYS D 213 ? 1.3566 0.7918 1.2244 0.1713  0.1670  -0.1531 213 LYS D CB  
16322 C CG  . LYS D 213 ? 1.5363 0.9522 1.3615 0.1653  0.1805  -0.1758 213 LYS D CG  
16323 C CD  . LYS D 213 ? 1.6895 1.0732 1.5250 0.1725  0.2080  -0.1920 213 LYS D CD  
16324 C CE  . LYS D 213 ? 1.6049 0.9717 1.3999 0.1701  0.2262  -0.2128 213 LYS D CE  
16325 N NZ  . LYS D 213 ? 1.7227 1.1029 1.5263 0.1886  0.2444  -0.2011 213 LYS D NZ  
16326 N N   . GLY D 214 ? 1.2850 0.7466 1.2439 0.2027  0.1689  -0.1056 214 GLY D N   
16327 C CA  . GLY D 214 ? 1.2329 0.7075 1.2235 0.2070  0.1598  -0.0865 214 GLY D CA  
16328 C C   . GLY D 214 ? 1.2986 0.7799 1.2880 0.1895  0.1399  -0.0887 214 GLY D C   
16329 O O   . GLY D 214 ? 1.2930 0.7583 1.2673 0.1735  0.1363  -0.1079 214 GLY D O   
16330 N N   . GLY D 215 ? 1.1485 0.6541 1.1540 0.1923  0.1268  -0.0702 215 GLY D N   
16331 C CA  . GLY D 215 ? 1.2106 0.7281 1.2218 0.1776  0.1076  -0.0694 215 GLY D CA  
16332 C C   . GLY D 215 ? 1.2958 0.8357 1.2832 0.1722  0.0897  -0.0668 215 GLY D C   
16333 O O   . GLY D 215 ? 1.2768 0.8359 1.2760 0.1666  0.0731  -0.0577 215 GLY D O   
16334 N N   . GLN D 216 ? 1.2707 0.8081 1.2258 0.1743  0.0942  -0.0736 216 GLN D N   
16335 C CA  . GLN D 216 ? 1.3792 0.9347 1.3083 0.1702  0.0794  -0.0693 216 GLN D CA  
16336 C C   . GLN D 216 ? 1.2862 0.8621 1.2297 0.1849  0.0799  -0.0482 216 GLN D C   
16337 O O   . GLN D 216 ? 1.3379 0.9160 1.2672 0.1929  0.0888  -0.0457 216 GLN D O   
16338 C CB  . GLN D 216 ? 1.2834 0.8258 1.1707 0.1661  0.0871  -0.0846 216 GLN D CB  
16339 C CG  . GLN D 216 ? 1.3805 0.8984 1.2485 0.1515  0.0894  -0.1091 216 GLN D CG  
16340 C CD  . GLN D 216 ? 1.5425 1.0669 1.4118 0.1342  0.0662  -0.1139 216 GLN D CD  
16341 O OE1 . GLN D 216 ? 1.7048 1.2489 1.5596 0.1283  0.0460  -0.1065 216 GLN D OE1 
16342 N NE2 . GLN D 216 ? 1.4465 0.9551 1.3361 0.1258  0.0683  -0.1256 216 GLN D NE2 
16343 N N   . LEU D 217 ? 1.1704 0.7608 1.1432 0.1878  0.0715  -0.0342 217 LEU D N   
16344 C CA  . LEU D 217 ? 1.1715 0.7792 1.1587 0.2009  0.0721  -0.0161 217 LEU D CA  
16345 C C   . LEU D 217 ? 1.3332 0.9550 1.2995 0.2005  0.0624  -0.0096 217 LEU D C   
16346 O O   . LEU D 217 ? 1.2470 0.8740 1.2103 0.2102  0.0699  -0.0027 217 LEU D O   
16347 C CB  . LEU D 217 ? 1.0875 0.7059 1.1071 0.2023  0.0660  -0.0045 217 LEU D CB  
16348 C CG  . LEU D 217 ? 1.0620 0.6952 1.0971 0.2156  0.0682  0.0124  217 LEU D CG  
16349 C CD1 . LEU D 217 ? 0.8807 0.5079 0.9162 0.2287  0.0838  0.0146  217 LEU D CD1 
16350 C CD2 . LEU D 217 ? 1.1769 0.8176 1.2418 0.2159  0.0655  0.0217  217 LEU D CD2 
16351 N N   . ASN D 218 ? 1.1606 0.7888 1.1134 0.1892  0.0454  -0.0112 218 ASN D N   
16352 C CA  . ASN D 218 ? 1.2045 0.8439 1.1367 0.1891  0.0359  -0.0027 218 ASN D CA  
16353 C C   . ASN D 218 ? 1.3255 0.9548 1.2255 0.1905  0.0480  -0.0091 218 ASN D C   
16354 O O   . ASN D 218 ? 1.3835 1.0202 1.2767 0.1963  0.0499  0.0011  218 ASN D O   
16355 C CB  . ASN D 218 ? 1.3181 0.9657 1.2400 0.1768  0.0143  -0.0033 218 ASN D CB  
16356 C CG  . ASN D 218 ? 1.4896 1.1531 1.4480 0.1765  0.0020  0.0064  218 ASN D CG  
16357 O OD1 . ASN D 218 ? 1.4770 1.1458 1.4648 0.1865  0.0098  0.0159  218 ASN D OD1 
16358 N ND2 . ASN D 218 ? 1.7572 1.4295 1.7146 0.1649  -0.0175 0.0041  218 ASN D ND2 
16359 N N   . ASP D 219 ? 1.2979 0.9096 1.1800 0.1850  0.0578  -0.0263 219 ASP D N   
16360 C CA  . ASP D 219 ? 1.3041 0.9057 1.1571 0.1863  0.0725  -0.0336 219 ASP D CA  
16361 C C   . ASP D 219 ? 1.2539 0.8569 1.1278 0.2005  0.0912  -0.0287 219 ASP D C   
16362 O O   . ASP D 219 ? 1.3628 0.9683 1.2234 0.2041  0.1006  -0.0261 219 ASP D O   
16363 C CB  . ASP D 219 ? 1.4249 1.0057 1.2523 0.1762  0.0787  -0.0553 219 ASP D CB  
16364 C CG  . ASP D 219 ? 1.6205 1.2016 1.4217 0.1606  0.0582  -0.0617 219 ASP D CG  
16365 O OD1 . ASP D 219 ? 1.6361 1.2223 1.4042 0.1564  0.0506  -0.0573 219 ASP D OD1 
16366 O OD2 . ASP D 219 ? 1.6511 1.2279 1.4656 0.1523  0.0493  -0.0703 219 ASP D OD2 
16367 N N   . ILE D 220 ? 1.2658 0.8684 1.1726 0.2081  0.0961  -0.0265 220 ILE D N   
16368 C CA  . ILE D 220 ? 1.1660 0.7726 1.0941 0.2220  0.1105  -0.0207 220 ILE D CA  
16369 C C   . ILE D 220 ? 1.2197 0.8457 1.1579 0.2279  0.1037  -0.0045 220 ILE D C   
16370 O O   . ILE D 220 ? 1.0849 0.7173 1.0244 0.2342  0.1128  -0.0012 220 ILE D O   
16371 C CB  . ILE D 220 ? 0.9497 0.5486 0.9063 0.2286  0.1165  -0.0213 220 ILE D CB  
16372 C CG1 . ILE D 220 ? 1.1604 0.7360 1.1083 0.2245  0.1285  -0.0388 220 ILE D CG1 
16373 C CG2 . ILE D 220 ? 1.0052 0.6143 0.9854 0.2437  0.1253  -0.0107 220 ILE D CG2 
16374 C CD1 . ILE D 220 ? 1.2991 0.8620 1.2704 0.2256  0.1310  -0.0404 220 ILE D CD1 
16375 N N   . LEU D 221 ? 1.1585 0.7936 1.1054 0.2253  0.0885  0.0047  221 LEU D N   
16376 C CA  . LEU D 221 ? 1.0754 0.7255 1.0315 0.2305  0.0826  0.0187  221 LEU D CA  
16377 C C   . LEU D 221 ? 1.2107 0.8633 1.1428 0.2263  0.0814  0.0213  221 LEU D C   
16378 O O   . LEU D 221 ? 1.2579 0.9190 1.1966 0.2312  0.0831  0.0299  221 LEU D O   
16379 C CB  . LEU D 221 ? 1.0219 0.6799 0.9935 0.2289  0.0686  0.0271  221 LEU D CB  
16380 C CG  . LEU D 221 ? 0.9246 0.5811 0.9216 0.2331  0.0711  0.0277  221 LEU D CG  
16381 C CD1 . LEU D 221 ? 1.1139 0.7782 1.1251 0.2289  0.0583  0.0341  221 LEU D CD1 
16382 C CD2 . LEU D 221 ? 0.8381 0.4998 0.8512 0.2453  0.0800  0.0344  221 LEU D CD2 
16383 N N   . LYS D 222 ? 1.2255 0.8695 1.1285 0.2168  0.0787  0.0138  222 LYS D N   
16384 C CA  . LYS D 222 ? 1.2041 0.8478 1.0791 0.2124  0.0793  0.0173  222 LYS D CA  
16385 C C   . LYS D 222 ? 1.2656 0.9065 1.1378 0.2168  0.0993  0.0125  222 LYS D C   
16386 O O   . LYS D 222 ? 1.1802 0.8266 1.0493 0.2181  0.1038  0.0205  222 LYS D O   
16387 C CB  . LYS D 222 ? 1.1877 0.8221 1.0274 0.2008  0.0715  0.0092  222 LYS D CB  
16388 C CG  . LYS D 222 ? 1.2716 0.9138 1.1047 0.1953  0.0495  0.0195  222 LYS D CG  
16389 C CD  . LYS D 222 ? 1.7190 1.3541 1.5075 0.1844  0.0422  0.0149  222 LYS D CD  
16390 C CE  . LYS D 222 ? 1.6466 1.2698 1.4181 0.1750  0.0416  -0.0048 222 LYS D CE  
16391 N NZ  . LYS D 222 ? 1.5680 1.1985 1.3573 0.1692  0.0216  -0.0058 222 LYS D NZ  
16392 N N   . TYR D 223 ? 1.1888 0.8211 1.0651 0.2191  0.1121  -0.0003 223 TYR D N   
16393 C CA  . TYR D 223 ? 1.0599 0.6916 0.9395 0.2245  0.1319  -0.0052 223 TYR D CA  
16394 C C   . TYR D 223 ? 1.1364 0.7841 1.0478 0.2340  0.1343  0.0051  223 TYR D C   
16395 O O   . TYR D 223 ? 1.1964 0.8509 1.1078 0.2346  0.1433  0.0084  223 TYR D O   
16396 C CB  . TYR D 223 ? 1.0879 0.7067 0.9725 0.2274  0.1444  -0.0198 223 TYR D CB  
16397 C CG  . TYR D 223 ? 1.0591 0.6781 0.9493 0.2337  0.1662  -0.0255 223 TYR D CG  
16398 C CD1 . TYR D 223 ? 1.0732 0.7056 0.9991 0.2455  0.1727  -0.0195 223 TYR D CD1 
16399 C CD2 . TYR D 223 ? 1.0706 0.6780 0.9306 0.2279  0.1802  -0.0365 223 TYR D CD2 
16400 C CE1 . TYR D 223 ? 1.1286 0.7651 1.0657 0.2518  0.1920  -0.0238 223 TYR D CE1 
16401 C CE2 . TYR D 223 ? 1.1641 0.7734 1.0333 0.2342  0.2023  -0.0414 223 TYR D CE2 
16402 C CZ  . TYR D 223 ? 1.1801 0.8052 1.0908 0.2463  0.2079  -0.0347 223 TYR D CZ  
16403 O OH  . TYR D 223 ? 1.1735 0.8041 1.0992 0.2531  0.2291  -0.0389 223 TYR D OH  
16404 N N   . THR D 224 ? 1.1437 0.7975 1.0814 0.2405  0.1267  0.0100  224 THR D N   
16405 C CA  . THR D 224 ? 1.0598 0.7286 1.0241 0.2490  0.1272  0.0183  224 THR D CA  
16406 C C   . THR D 224 ? 1.1042 0.7810 1.0640 0.2452  0.1206  0.0278  224 THR D C   
16407 O O   . THR D 224 ? 1.0214 0.7081 0.9928 0.2475  0.1266  0.0307  224 THR D O   
16408 C CB  . THR D 224 ? 0.9175 0.5890 0.9034 0.2559  0.1199  0.0223  224 THR D CB  
16409 O OG1 . THR D 224 ? 1.0351 0.7033 1.0144 0.2504  0.1066  0.0263  224 THR D OG1 
16410 C CG2 . THR D 224 ? 0.9536 0.6159 0.9485 0.2612  0.1284  0.0152  224 THR D CG2 
16411 N N   . ALA D 225 ? 1.0725 0.7449 1.0177 0.2392  0.1083  0.0328  225 ALA D N   
16412 C CA  . ALA D 225 ? 0.9625 0.6388 0.9039 0.2364  0.1019  0.0432  225 ALA D CA  
16413 C C   . ALA D 225 ? 1.0764 0.7499 0.9988 0.2308  0.1113  0.0443  225 ALA D C   
16414 O O   . ALA D 225 ? 1.2331 0.9114 1.1631 0.2306  0.1133  0.0514  225 ALA D O   
16415 C CB  . ALA D 225 ? 0.9831 0.6562 0.9158 0.2327  0.0864  0.0492  225 ALA D CB  
16416 N N   . GLU D 226 ? 1.0275 0.6919 0.9245 0.2257  0.1184  0.0368  226 GLU D N   
16417 C CA  . GLU D 226 ? 1.0767 0.7368 0.9509 0.2200  0.1297  0.0384  226 GLU D CA  
16418 C C   . GLU D 226 ? 1.0845 0.7487 0.9691 0.2225  0.1502  0.0306  226 GLU D C   
16419 O O   . GLU D 226 ? 1.1792 0.8449 1.0584 0.2189  0.1614  0.0347  226 GLU D O   
16420 C CB  . GLU D 226 ? 1.0731 0.7203 0.9067 0.2120  0.1261  0.0349  226 GLU D CB  
16421 C CG  . GLU D 226 ? 1.2898 0.9357 1.1133 0.2089  0.1046  0.0433  226 GLU D CG  
16422 C CD  . GLU D 226 ? 1.5433 1.1788 1.3255 0.2002  0.0979  0.0390  226 GLU D CD  
16423 O OE1 . GLU D 226 ? 1.6476 1.2741 1.4078 0.1965  0.1109  0.0260  226 GLU D OE1 
16424 O OE2 . GLU D 226 ? 1.7515 1.3886 1.5239 0.1972  0.0793  0.0483  226 GLU D OE2 
16425 N N   . ARG D 227 ? 1.0345 0.7002 0.9354 0.2287  0.1562  0.0204  227 ARG D N   
16426 C CA  . ARG D 227 ? 1.0474 0.7182 0.9618 0.2327  0.1759  0.0131  227 ARG D CA  
16427 C C   . ARG D 227 ? 1.0541 0.7426 1.0110 0.2422  0.1772  0.0150  227 ARG D C   
16428 O O   . ARG D 227 ? 1.2485 0.9483 1.2224 0.2438  0.1906  0.0143  227 ARG D O   
16429 C CB  . ARG D 227 ? 1.1072 0.7644 1.0076 0.2337  0.1856  -0.0009 227 ARG D CB  
16430 C CG  . ARG D 227 ? 1.1570 0.7963 1.0120 0.2236  0.1822  -0.0061 227 ARG D CG  
16431 C CD  . ARG D 227 ? 1.3188 0.9526 1.1445 0.2173  0.1990  -0.0079 227 ARG D CD  
16432 N NE  . ARG D 227 ? 1.5982 1.2185 1.3771 0.2070  0.1896  -0.0072 227 ARG D NE  
16433 C CZ  . ARG D 227 ? 1.7638 1.3772 1.5068 0.1998  0.1996  -0.0048 227 ARG D CZ  
16434 N NH1 . ARG D 227 ? 1.7565 1.3753 1.5078 0.2013  0.2216  -0.0034 227 ARG D NH1 
16435 N NH2 . ARG D 227 ? 1.6273 1.2296 1.3263 0.1911  0.1875  -0.0030 227 ARG D NH2 
16436 N N   . VAL D 228 ? 1.0297 0.7218 1.0038 0.2483  0.1638  0.0175  228 VAL D N   
16437 C CA  . VAL D 228 ? 0.8798 0.5890 0.8897 0.2576  0.1631  0.0198  228 VAL D CA  
16438 C C   . VAL D 228 ? 0.9067 0.6278 0.9269 0.2545  0.1546  0.0282  228 VAL D C   
16439 O O   . VAL D 228 ? 0.9839 0.7013 0.9988 0.2532  0.1412  0.0335  228 VAL D O   
16440 C CB  . VAL D 228 ? 0.9424 0.6490 0.9638 0.2660  0.1549  0.0196  228 VAL D CB  
16441 C CG1 . VAL D 228 ? 0.8488 0.5740 0.9024 0.2759  0.1525  0.0238  228 VAL D CG1 
16442 C CG2 . VAL D 228 ? 0.9568 0.6482 0.9699 0.2683  0.1648  0.0101  228 VAL D CG2 
16443 N N   . PRO D 229 ? 0.9035 0.6392 0.9420 0.2533  0.1628  0.0288  229 PRO D N   
16444 C CA  . PRO D 229 ? 0.9409 0.6852 0.9894 0.2483  0.1560  0.0347  229 PRO D CA  
16445 C C   . PRO D 229 ? 0.9559 0.7141 1.0284 0.2551  0.1438  0.0358  229 PRO D C   
16446 O O   . PRO D 229 ? 1.0035 0.7794 1.1003 0.2550  0.1449  0.0350  229 PRO D O   
16447 C CB  . PRO D 229 ? 0.8635 0.6190 0.9258 0.2437  0.1713  0.0332  229 PRO D CB  
16448 C CG  . PRO D 229 ? 0.9114 0.6758 0.9901 0.2523  0.1820  0.0266  229 PRO D CG  
16449 C CD  . PRO D 229 ? 0.9441 0.6895 0.9985 0.2563  0.1798  0.0232  229 PRO D CD  
16450 N N   . ALA D 230 ? 0.9370 0.6873 1.0011 0.2596  0.1324  0.0379  230 ALA D N   
16451 C CA  . ALA D 230 ? 0.9250 0.6863 1.0054 0.2666  0.1217  0.0394  230 ALA D CA  
16452 C C   . ALA D 230 ? 0.9776 0.7340 1.0515 0.2626  0.1114  0.0429  230 ALA D C   
16453 O O   . ALA D 230 ? 0.9507 0.6928 1.0071 0.2571  0.1105  0.0460  230 ALA D O   
16454 C CB  . ALA D 230 ? 0.8027 0.5585 0.8813 0.2757  0.1193  0.0397  230 ALA D CB  
16455 N N   . PHE D 231 ? 0.9125 0.6807 0.9996 0.2657  0.1039  0.0423  231 PHE D N   
16456 C CA  . PHE D 231 ? 0.8931 0.6558 0.9749 0.2632  0.0957  0.0436  231 PHE D CA  
16457 C C   . PHE D 231 ? 0.8828 0.6569 0.9724 0.2703  0.0874  0.0422  231 PHE D C   
16458 O O   . PHE D 231 ? 0.9534 0.7436 1.0568 0.2752  0.0866  0.0408  231 PHE D O   
16459 C CB  . PHE D 231 ? 0.8443 0.6062 0.9302 0.2531  0.0981  0.0423  231 PHE D CB  
16460 C CG  . PHE D 231 ? 0.8723 0.6532 0.9798 0.2495  0.1001  0.0372  231 PHE D CG  
16461 C CD1 . PHE D 231 ? 0.9195 0.7142 1.0392 0.2508  0.0910  0.0325  231 PHE D CD1 
16462 C CD2 . PHE D 231 ? 0.9432 0.7291 1.0590 0.2440  0.1110  0.0368  231 PHE D CD2 
16463 C CE1 . PHE D 231 ? 1.0071 0.8227 1.1503 0.2465  0.0906  0.0275  231 PHE D CE1 
16464 C CE2 . PHE D 231 ? 0.9745 0.7810 1.1160 0.2401  0.1132  0.0323  231 PHE D CE2 
16465 C CZ  . PHE D 231 ? 1.0076 0.8298 1.1643 0.2411  0.1019  0.0276  231 PHE D CZ  
16466 N N   . VAL D 232 ? 0.8795 0.6459 0.9599 0.2716  0.0815  0.0432  232 VAL D N   
16467 C CA  . VAL D 232 ? 0.8843 0.6594 0.9652 0.2781  0.0742  0.0420  232 VAL D CA  
16468 C C   . VAL D 232 ? 0.9870 0.7656 1.0695 0.2719  0.0693  0.0354  232 VAL D C   
16469 O O   . VAL D 232 ? 0.9447 0.7116 1.0248 0.2645  0.0721  0.0337  232 VAL D O   
16470 C CB  . VAL D 232 ? 0.7756 0.5392 0.8438 0.2850  0.0736  0.0473  232 VAL D CB  
16471 C CG1 . VAL D 232 ? 0.7893 0.5608 0.8532 0.2924  0.0677  0.0477  232 VAL D CG1 
16472 C CG2 . VAL D 232 ? 0.8312 0.5885 0.8987 0.2886  0.0786  0.0520  232 VAL D CG2 
16473 N N   . ASN D 233 ? 0.8943 0.6889 0.9812 0.2748  0.0615  0.0316  233 ASN D N   
16474 C CA  . ASN D 233 ? 0.8698 0.6680 0.9563 0.2679  0.0553  0.0225  233 ASN D CA  
16475 C C   . ASN D 233 ? 1.0293 0.8303 1.1000 0.2755  0.0477  0.0218  233 ASN D C   
16476 O O   . ASN D 233 ? 1.1184 0.9388 1.1935 0.2799  0.0392  0.0218  233 ASN D O   
16477 C CB  . ASN D 233 ? 0.8408 0.6593 0.9490 0.2604  0.0517  0.0163  233 ASN D CB  
16478 C CG  . ASN D 233 ? 0.9862 0.7969 1.1052 0.2491  0.0606  0.0146  233 ASN D CG  
16479 O OD1 . ASN D 233 ? 1.1754 0.9695 1.2869 0.2492  0.0693  0.0208  233 ASN D OD1 
16480 N ND2 . ASN D 233 ? 0.7811 0.6039 0.9177 0.2388  0.0581  0.0067  233 ASN D ND2 
16481 N N   . ALA D 234 ? 0.9748 0.7579 1.0283 0.2775  0.0512  0.0221  234 ALA D N   
16482 C CA  . ALA D 234 ? 0.9084 0.6910 0.9428 0.2849  0.0475  0.0223  234 ALA D CA  
16483 C C   . ALA D 234 ? 1.0174 0.8012 1.0417 0.2787  0.0413  0.0094  234 ALA D C   
16484 O O   . ALA D 234 ? 1.1151 0.8831 1.1372 0.2721  0.0465  0.0022  234 ALA D O   
16485 C CB  . ALA D 234 ? 0.9260 0.6900 0.9495 0.2904  0.0565  0.0290  234 ALA D CB  
16486 N N   . PHE D 235 ? 1.0107 0.8129 1.0288 0.2808  0.0298  0.0062  235 PHE D N   
16487 C CA  . PHE D 235 ? 1.1146 0.9199 1.1201 0.2737  0.0214  -0.0083 235 PHE D CA  
16488 C C   . PHE D 235 ? 1.1222 0.9224 1.0951 0.2816  0.0198  -0.0081 235 PHE D C   
16489 O O   . PHE D 235 ? 1.0639 0.8671 1.0279 0.2931  0.0208  0.0050  235 PHE D O   
16490 C CB  . PHE D 235 ? 1.1228 0.9562 1.1453 0.2683  0.0068  -0.0135 235 PHE D CB  
16491 C CG  . PHE D 235 ? 1.1160 0.9553 1.1707 0.2588  0.0102  -0.0152 235 PHE D CG  
16492 C CD1 . PHE D 235 ? 1.0233 0.8480 1.0849 0.2459  0.0160  -0.0257 235 PHE D CD1 
16493 C CD2 . PHE D 235 ? 1.1785 1.0364 1.2564 0.2632  0.0093  -0.0059 235 PHE D CD2 
16494 C CE1 . PHE D 235 ? 1.1273 0.9562 1.2164 0.2370  0.0210  -0.0256 235 PHE D CE1 
16495 C CE2 . PHE D 235 ? 0.9954 0.8582 1.1008 0.2544  0.0151  -0.0074 235 PHE D CE2 
16496 C CZ  . PHE D 235 ? 1.0348 0.8833 1.1448 0.2411  0.0208  -0.0166 235 PHE D CZ  
16497 N N   . GLY D 236 ? 1.0923 0.8830 1.0468 0.2750  0.0187  -0.0230 236 GLY D N   
16498 C CA  . GLY D 236 ? 1.1129 0.8967 1.0315 0.2812  0.0192  -0.0253 236 GLY D CA  
16499 C C   . GLY D 236 ? 1.0851 0.8466 0.9939 0.2895  0.0369  -0.0169 236 GLY D C   
16500 O O   . GLY D 236 ? 1.1598 0.9131 1.0901 0.2906  0.0462  -0.0085 236 GLY D O   
16501 N N   . PRO D 237 ? 1.1034 0.8556 0.9797 0.2953  0.0422  -0.0186 237 PRO D N   
16502 C CA  . PRO D 237 ? 1.1771 0.9103 1.0490 0.3030  0.0606  -0.0102 237 PRO D CA  
16503 C C   . PRO D 237 ? 1.0720 0.8087 0.9643 0.3105  0.0654  0.0093  237 PRO D C   
16504 O O   . PRO D 237 ? 1.1955 0.9473 1.0900 0.3154  0.0569  0.0198  237 PRO D O   
16505 C CB  . PRO D 237 ? 1.1221 0.8513 0.9536 0.3090  0.0637  -0.0123 237 PRO D CB  
16506 C CG  . PRO D 237 ? 1.1294 0.8674 0.9419 0.3007  0.0486  -0.0294 237 PRO D CG  
16507 C CD  . PRO D 237 ? 1.0075 0.7666 0.8492 0.2946  0.0321  -0.0284 237 PRO D CD  
16508 N N   . LEU D 238 ? 1.0366 0.7590 0.9451 0.3115  0.0787  0.0137  238 LEU D N   
16509 C CA  . LEU D 238 ? 1.1342 0.8579 1.0626 0.3164  0.0833  0.0295  238 LEU D CA  
16510 C C   . LEU D 238 ? 1.1032 0.8179 1.0216 0.3246  0.0970  0.0390  238 LEU D C   
16511 O O   . LEU D 238 ? 1.3020 1.0041 1.2172 0.3251  0.1087  0.0342  238 LEU D O   
16512 C CB  . LEU D 238 ? 1.1555 0.8722 1.1112 0.3105  0.0864  0.0286  238 LEU D CB  
16513 C CG  . LEU D 238 ? 1.2418 0.9687 1.2165 0.3044  0.0768  0.0288  238 LEU D CG  
16514 C CD1 . LEU D 238 ? 1.1000 0.8366 1.0699 0.2976  0.0661  0.0168  238 LEU D CD1 
16515 C CD2 . LEU D 238 ? 1.0253 0.7425 1.0199 0.2995  0.0814  0.0299  238 LEU D CD2 
16516 N N   . SER D 239 ? 0.9780 0.6984 0.8942 0.3312  0.0971  0.0528  239 SER D N   
16517 C CA  . SER D 239 ? 1.0025 0.7147 0.9124 0.3381  0.1115  0.0635  239 SER D CA  
16518 C C   . SER D 239 ? 1.1835 0.8907 1.1249 0.3364  0.1189  0.0702  239 SER D C   
16519 O O   . SER D 239 ? 1.2323 0.9428 1.1942 0.3310  0.1115  0.0680  239 SER D O   
16520 C CB  . SER D 239 ? 1.0972 0.8154 0.9928 0.3455  0.1088  0.0768  239 SER D CB  
16521 O OG  . SER D 239 ? 1.0942 0.8188 1.0125 0.3455  0.1022  0.0848  239 SER D OG  
16522 N N   . GLU D 240 ? 1.1722 0.8727 1.1176 0.3404  0.1334  0.0785  240 GLU D N   
16523 C CA  . GLU D 240 ? 1.0952 0.7938 1.0722 0.3379  0.1385  0.0847  240 GLU D CA  
16524 C C   . GLU D 240 ? 1.0973 0.8010 1.0882 0.3360  0.1300  0.0920  240 GLU D C   
16525 O O   . GLU D 240 ? 0.8932 0.5980 0.9061 0.3306  0.1255  0.0911  240 GLU D O   
16526 C CB  . GLU D 240 ? 1.0965 0.7900 1.0783 0.3421  0.1559  0.0931  240 GLU D CB  
16527 C CG  . GLU D 240 ? 1.0172 0.7043 0.9888 0.3448  0.1682  0.0855  240 GLU D CG  
16528 C CD  . GLU D 240 ? 1.2871 0.9696 1.2208 0.3505  0.1764  0.0849  240 GLU D CD  
16529 O OE1 . GLU D 240 ? 1.3663 1.0522 1.2802 0.3530  0.1700  0.0915  240 GLU D OE1 
16530 O OE2 . GLU D 240 ? 1.3584 1.0336 1.2812 0.3530  0.1896  0.0779  240 GLU D OE2 
16531 N N   . LEU D 241 ? 0.9926 0.6983 0.9691 0.3409  0.1280  0.0991  241 LEU D N   
16532 C CA  . LEU D 241 ? 0.9621 0.6702 0.9509 0.3407  0.1222  0.1055  241 LEU D CA  
16533 C C   . LEU D 241 ? 1.0322 0.7474 1.0288 0.3356  0.1093  0.0965  241 LEU D C   
16534 O O   . LEU D 241 ? 1.1084 0.8230 1.1228 0.3315  0.1069  0.0970  241 LEU D O   
16535 C CB  . LEU D 241 ? 0.9422 0.6511 0.9124 0.3491  0.1221  0.1155  241 LEU D CB  
16536 C CG  . LEU D 241 ? 0.8531 0.5609 0.8368 0.3513  0.1195  0.1238  241 LEU D CG  
16537 C CD1 . LEU D 241 ? 1.0049 0.7011 1.0028 0.3508  0.1322  0.1338  241 LEU D CD1 
16538 C CD2 . LEU D 241 ? 0.9472 0.6606 0.9132 0.3604  0.1132  0.1314  241 LEU D CD2 
16539 N N   . VAL D 242 ? 1.0684 0.7901 1.0511 0.3349  0.1017  0.0877  242 VAL D N   
16540 C CA  . VAL D 242 ? 1.0138 0.7432 1.0052 0.3293  0.0912  0.0793  242 VAL D CA  
16541 C C   . VAL D 242 ? 0.9931 0.7170 1.0008 0.3217  0.0929  0.0744  242 VAL D C   
16542 O O   . VAL D 242 ? 0.9628 0.6891 0.9827 0.3172  0.0884  0.0730  242 VAL D O   
16543 C CB  . VAL D 242 ? 0.9817 0.7197 0.9568 0.3286  0.0828  0.0702  242 VAL D CB  
16544 C CG1 . VAL D 242 ? 0.9019 0.6465 0.8901 0.3205  0.0749  0.0606  242 VAL D CG1 
16545 C CG2 . VAL D 242 ? 1.0475 0.7952 1.0086 0.3363  0.0766  0.0768  242 VAL D CG2 
16546 N N   . VAL D 243 ? 1.0326 0.7490 1.0402 0.3211  0.0998  0.0726  243 VAL D N   
16547 C CA  . VAL D 243 ? 0.9416 0.6533 0.9656 0.3156  0.1003  0.0705  243 VAL D CA  
16548 C C   . VAL D 243 ? 1.0275 0.7390 1.0681 0.3137  0.1005  0.0781  243 VAL D C   
16549 O O   . VAL D 243 ? 1.0981 0.8094 1.1485 0.3081  0.0957  0.0768  243 VAL D O   
16550 C CB  . VAL D 243 ? 0.8817 0.5860 0.9060 0.3173  0.1087  0.0680  243 VAL D CB  
16551 C CG1 . VAL D 243 ? 0.7903 0.4911 0.8353 0.3136  0.1085  0.0697  243 VAL D CG1 
16552 C CG2 . VAL D 243 ? 0.8175 0.5193 0.8244 0.3168  0.1079  0.0569  243 VAL D CG2 
16553 N N   . SER D 244 ? 0.9730 0.6833 1.0149 0.3176  0.1062  0.0857  244 SER D N   
16554 C CA  . SER D 244 ? 0.9116 0.6202 0.9690 0.3143  0.1063  0.0909  244 SER D CA  
16555 C C   . SER D 244 ? 1.0664 0.7768 1.1228 0.3116  0.0994  0.0882  244 SER D C   
16556 O O   . SER D 244 ? 0.9691 0.6779 1.0347 0.3056  0.0961  0.0868  244 SER D O   
16557 C CB  . SER D 244 ? 0.8459 0.5511 0.9052 0.3187  0.1155  0.0995  244 SER D CB  
16558 O OG  . SER D 244 ? 1.2253 0.9295 1.2884 0.3208  0.1243  0.1020  244 SER D OG  
16559 N N   . ALA D 245 ? 0.9916 0.7062 1.0368 0.3161  0.0972  0.0871  245 ALA D N   
16560 C CA  . ALA D 245 ? 0.9557 0.6737 1.0029 0.3150  0.0926  0.0843  245 ALA D CA  
16561 C C   . ALA D 245 ? 0.9625 0.6831 1.0122 0.3074  0.0875  0.0768  245 ALA D C   
16562 O O   . ALA D 245 ? 0.9590 0.6785 1.0132 0.3031  0.0864  0.0745  245 ALA D O   
16563 C CB  . ALA D 245 ? 0.7766 0.5027 0.8152 0.3221  0.0899  0.0856  245 ALA D CB  
16564 N N   . GLY D 246 ? 0.9137 0.6356 0.9592 0.3057  0.0859  0.0731  246 GLY D N   
16565 C CA  . GLY D 246 ? 0.9445 0.6660 0.9924 0.2988  0.0825  0.0681  246 GLY D CA  
16566 C C   . GLY D 246 ? 1.0176 0.7330 1.0723 0.2940  0.0823  0.0711  246 GLY D C   
16567 O O   . GLY D 246 ? 1.0851 0.7997 1.1395 0.2883  0.0796  0.0693  246 GLY D O   
16568 N N   . ALA D 247 ? 0.9591 0.6712 1.0200 0.2960  0.0849  0.0762  247 ALA D N   
16569 C CA  . ALA D 247 ? 0.9496 0.6592 1.0195 0.2912  0.0821  0.0794  247 ALA D CA  
16570 C C   . ALA D 247 ? 0.9824 0.6906 1.0505 0.2873  0.0805  0.0778  247 ALA D C   
16571 O O   . ALA D 247 ? 1.0239 0.7303 1.0905 0.2809  0.0757  0.0768  247 ALA D O   
16572 C CB  . ALA D 247 ? 0.8428 0.5524 0.9248 0.2940  0.0860  0.0848  247 ALA D CB  
16573 N N   . GLY D 248 ? 0.8783 0.5859 0.9448 0.2915  0.0848  0.0776  248 GLY D N   
16574 C CA  . GLY D 248 ? 0.8875 0.5909 0.9532 0.2891  0.0859  0.0749  248 GLY D CA  
16575 C C   . GLY D 248 ? 0.8846 0.5898 0.9423 0.2860  0.0843  0.0691  248 GLY D C   
16576 O O   . GLY D 248 ? 0.9242 0.6246 0.9778 0.2803  0.0839  0.0652  248 GLY D O   
16577 N N   . ALA D 249 ? 0.8148 0.5270 0.8700 0.2888  0.0840  0.0680  249 ALA D N   
16578 C CA  . ALA D 249 ? 0.8103 0.5263 0.8619 0.2853  0.0842  0.0632  249 ALA D CA  
16579 C C   . ALA D 249 ? 0.9880 0.6993 1.0333 0.2772  0.0811  0.0632  249 ALA D C   
16580 O O   . ALA D 249 ? 1.0448 0.7537 1.0831 0.2722  0.0828  0.0602  249 ALA D O   
16581 C CB  . ALA D 249 ? 0.7527 0.4784 0.8064 0.2883  0.0831  0.0618  249 ALA D CB  
16582 N N   . ILE D 250 ? 0.9494 0.6590 0.9969 0.2767  0.0773  0.0673  250 ILE D N   
16583 C CA  . ILE D 250 ? 0.9531 0.6585 0.9964 0.2709  0.0729  0.0705  250 ILE D CA  
16584 C C   . ILE D 250 ? 0.9847 0.6864 1.0229 0.2661  0.0694  0.0707  250 ILE D C   
16585 O O   . ILE D 250 ? 0.9509 0.6494 0.9776 0.2602  0.0664  0.0713  250 ILE D O   
16586 C CB  . ILE D 250 ? 0.9499 0.6544 1.0016 0.2738  0.0707  0.0755  250 ILE D CB  
16587 C CG1 . ILE D 250 ? 0.9997 0.7044 1.0516 0.2754  0.0737  0.0726  250 ILE D CG1 
16588 C CG2 . ILE D 250 ? 0.7681 0.4692 0.8196 0.2700  0.0643  0.0819  250 ILE D CG2 
16589 C CD1 . ILE D 250 ? 0.7757 0.4777 0.8349 0.2799  0.0750  0.0742  250 ILE D CD1 
16590 N N   . ALA D 251 ? 0.9444 0.6455 0.9894 0.2678  0.0698  0.0699  251 ALA D N   
16591 C CA  . ALA D 251 ? 0.8981 0.5949 0.9395 0.2616  0.0660  0.0675  251 ALA D CA  
16592 C C   . ALA D 251 ? 0.9465 0.6379 0.9720 0.2575  0.0701  0.0600  251 ALA D C   
16593 O O   . ALA D 251 ? 1.0218 0.7086 1.0347 0.2500  0.0656  0.0569  251 ALA D O   
16594 C CB  . ALA D 251 ? 0.8697 0.5652 0.9244 0.2639  0.0686  0.0675  251 ALA D CB  
16595 N N   . LEU D 252 ? 0.9762 0.6689 1.0022 0.2623  0.0784  0.0568  252 LEU D N   
16596 C CA  . LEU D 252 ? 1.0284 0.7172 1.0432 0.2598  0.0853  0.0496  252 LEU D CA  
16597 C C   . LEU D 252 ? 0.9365 0.6272 0.9389 0.2553  0.0859  0.0507  252 LEU D C   
16598 O O   . LEU D 252 ? 0.9866 0.6755 0.9802 0.2532  0.0939  0.0454  252 LEU D O   
16599 C CB  . LEU D 252 ? 0.9997 0.6921 1.0257 0.2681  0.0941  0.0472  252 LEU D CB  
16600 C CG  . LEU D 252 ? 1.0125 0.7025 1.0513 0.2748  0.0954  0.0493  252 LEU D CG  
16601 C CD1 . LEU D 252 ? 0.9268 0.6241 0.9765 0.2845  0.1010  0.0507  252 LEU D CD1 
16602 C CD2 . LEU D 252 ? 0.8963 0.5730 0.9319 0.2707  0.0981  0.0436  252 LEU D CD2 
16603 N N   . GLY D 253 ? 0.9650 0.6583 0.9683 0.2541  0.0793  0.0579  253 GLY D N   
16604 C CA  . GLY D 253 ? 0.9977 0.6903 0.9910 0.2498  0.0804  0.0613  253 GLY D CA  
16605 C C   . GLY D 253 ? 0.9605 0.6599 0.9647 0.2524  0.0871  0.0604  253 GLY D C   
16606 O O   . GLY D 253 ? 1.0522 0.7505 1.0504 0.2479  0.0913  0.0621  253 GLY D O   
16607 N N   . PHE D 254 ? 0.9897 0.6963 1.0097 0.2591  0.0878  0.0582  254 PHE D N   
16608 C CA  . PHE D 254 ? 0.9793 0.6951 1.0108 0.2609  0.0913  0.0562  254 PHE D CA  
16609 C C   . PHE D 254 ? 0.9223 0.6380 0.9597 0.2615  0.0862  0.0594  254 PHE D C   
16610 O O   . PHE D 254 ? 0.8321 0.5473 0.8731 0.2666  0.0821  0.0609  254 PHE D O   
16611 C CB  . PHE D 254 ? 0.8615 0.5864 0.9048 0.2684  0.0935  0.0525  254 PHE D CB  
16612 C CG  . PHE D 254 ? 0.8915 0.6144 0.9330 0.2701  0.1002  0.0486  254 PHE D CG  
16613 C CD1 . PHE D 254 ? 1.0053 0.7225 1.0350 0.2638  0.1068  0.0455  254 PHE D CD1 
16614 C CD2 . PHE D 254 ? 0.8231 0.5480 0.8736 0.2782  0.1014  0.0480  254 PHE D CD2 
16615 C CE1 . PHE D 254 ? 1.0408 0.7538 1.0678 0.2655  0.1151  0.0398  254 PHE D CE1 
16616 C CE2 . PHE D 254 ? 0.8305 0.5507 0.8813 0.2804  0.1094  0.0437  254 PHE D CE2 
16617 C CZ  . PHE D 254 ? 0.9312 0.6451 0.9703 0.2739  0.1165  0.0385  254 PHE D CZ  
16618 N N   . PRO D 255 ? 0.9189 0.6336 0.9577 0.2562  0.0881  0.0599  255 PRO D N   
16619 C CA  . PRO D 255 ? 0.7747 0.4862 0.8194 0.2569  0.0848  0.0609  255 PRO D CA  
16620 C C   . PRO D 255 ? 0.7663 0.4878 0.8200 0.2617  0.0830  0.0547  255 PRO D C   
16621 O O   . PRO D 255 ? 0.9609 0.6942 1.0203 0.2630  0.0842  0.0507  255 PRO D O   
16622 C CB  . PRO D 255 ? 0.8682 0.5747 0.9136 0.2490  0.0890  0.0620  255 PRO D CB  
16623 C CG  . PRO D 255 ? 0.9672 0.6748 1.0050 0.2444  0.0949  0.0631  255 PRO D CG  
16624 C CD  . PRO D 255 ? 0.9930 0.7079 1.0289 0.2493  0.0952  0.0594  255 PRO D CD  
16625 N N   . VAL D 256 ? 0.9013 0.6184 0.9557 0.2649  0.0802  0.0544  256 VAL D N   
16626 C CA  . VAL D 256 ? 0.8804 0.6052 0.9369 0.2693  0.0778  0.0487  256 VAL D CA  
16627 C C   . VAL D 256 ? 0.8881 0.6081 0.9470 0.2646  0.0778  0.0427  256 VAL D C   
16628 O O   . VAL D 256 ? 1.1373 0.8440 1.1949 0.2645  0.0797  0.0449  256 VAL D O   
16629 C CB  . VAL D 256 ? 0.8080 0.5298 0.8600 0.2773  0.0771  0.0522  256 VAL D CB  
16630 C CG1 . VAL D 256 ? 0.9023 0.6305 0.9504 0.2819  0.0752  0.0472  256 VAL D CG1 
16631 C CG2 . VAL D 256 ? 0.8233 0.5471 0.8748 0.2806  0.0777  0.0572  256 VAL D CG2 
16632 N N   . LEU D 257 ? 0.9174 0.6482 0.9820 0.2604  0.0756  0.0349  257 LEU D N   
16633 C CA  . LEU D 257 ? 0.8760 0.6014 0.9434 0.2539  0.0753  0.0266  257 LEU D CA  
16634 C C   . LEU D 257 ? 1.0325 0.7665 1.0938 0.2572  0.0694  0.0181  257 LEU D C   
16635 O O   . LEU D 257 ? 1.1457 0.8971 1.2079 0.2609  0.0641  0.0178  257 LEU D O   
16636 C CB  . LEU D 257 ? 0.7919 0.5231 0.8723 0.2435  0.0772  0.0233  257 LEU D CB  
16637 C CG  . LEU D 257 ? 0.8729 0.5964 0.9547 0.2397  0.0841  0.0325  257 LEU D CG  
16638 C CD1 . LEU D 257 ? 0.8531 0.5924 0.9391 0.2411  0.0855  0.0348  257 LEU D CD1 
16639 C CD2 . LEU D 257 ? 0.9227 0.6366 1.0131 0.2286  0.0895  0.0309  257 LEU D CD2 
16640 N N   . THR D 258 ? 0.9413 0.6627 0.9952 0.2566  0.0706  0.0114  258 THR D N   
16641 C CA  . THR D 258 ? 1.0542 0.7813 1.0953 0.2595  0.0656  0.0025  258 THR D CA  
16642 C C   . THR D 258 ? 1.0726 0.7903 1.1118 0.2508  0.0653  -0.0119 258 THR D C   
16643 O O   . THR D 258 ? 1.0353 0.7354 1.0818 0.2454  0.0720  -0.0132 258 THR D O   
16644 C CB  . THR D 258 ? 1.0369 0.7561 1.0640 0.2703  0.0699  0.0085  258 THR D CB  
16645 O OG1 . THR D 258 ? 1.1631 0.8846 1.1724 0.2729  0.0669  -0.0002 258 THR D OG1 
16646 C CG2 . THR D 258 ? 0.8240 0.5228 0.8544 0.2717  0.0790  0.0123  258 THR D CG2 
16647 N N   . ASP D 259 ? 1.0895 0.8179 1.1176 0.2495  0.0572  -0.0228 259 ASP D N   
16648 C CA  . ASP D 259 ? 1.0166 0.7356 1.0394 0.2401  0.0560  -0.0400 259 ASP D CA  
16649 C C   . ASP D 259 ? 1.1132 0.8111 1.1150 0.2464  0.0643  -0.0449 259 ASP D C   
16650 O O   . ASP D 259 ? 1.2789 0.9611 1.2753 0.2395  0.0674  -0.0596 259 ASP D O   
16651 C CB  . ASP D 259 ? 1.1289 0.8714 1.1484 0.2344  0.0413  -0.0510 259 ASP D CB  
16652 C CG  . ASP D 259 ? 1.1405 0.8987 1.1392 0.2453  0.0332  -0.0465 259 ASP D CG  
16653 O OD1 . ASP D 259 ? 1.2240 0.9750 1.2126 0.2570  0.0404  -0.0344 259 ASP D OD1 
16654 O OD2 . ASP D 259 ? 1.0804 0.8586 1.0741 0.2420  0.0193  -0.0542 259 ASP D OD2 
16655 N N   . GLN D 260 ? 0.9934 0.6901 0.9852 0.2590  0.0694  -0.0331 260 GLN D N   
16656 C CA  . GLN D 260 ? 1.1747 0.8543 1.1496 0.2663  0.0797  -0.0358 260 GLN D CA  
16657 C C   . GLN D 260 ? 1.1860 0.8452 1.1766 0.2689  0.0922  -0.0292 260 GLN D C   
16658 O O   . GLN D 260 ? 1.0961 0.7575 1.1055 0.2684  0.0918  -0.0173 260 GLN D O   
16659 C CB  . GLN D 260 ? 1.0117 0.7016 0.9716 0.2779  0.0800  -0.0250 260 GLN D CB  
16660 C CG  . GLN D 260 ? 0.9513 0.6615 0.8941 0.2782  0.0671  -0.0278 260 GLN D CG  
16661 C CD  . GLN D 260 ? 1.2108 0.9164 1.1262 0.2747  0.0645  -0.0449 260 GLN D CD  
16662 O OE1 . GLN D 260 ? 1.4713 1.1619 1.3663 0.2800  0.0754  -0.0486 260 GLN D OE1 
16663 N NE2 . GLN D 260 ? 1.3497 1.0689 1.2640 0.2651  0.0502  -0.0566 260 GLN D NE2 
16664 N N   . VAL D 261 ? 1.2305 0.8702 1.2130 0.2725  0.1034  -0.0365 261 VAL D N   
16665 C CA  . VAL D 261 ? 1.1224 0.7435 1.1226 0.2771  0.1152  -0.0294 261 VAL D CA  
16666 C C   . VAL D 261 ? 1.1535 0.7827 1.1605 0.2881  0.1188  -0.0122 261 VAL D C   
16667 O O   . VAL D 261 ? 1.1580 0.7911 1.1506 0.2952  0.1235  -0.0118 261 VAL D O   
16668 C CB  . VAL D 261 ? 0.9582 0.5554 0.9507 0.2782  0.1279  -0.0440 261 VAL D CB  
16669 C CG1 . VAL D 261 ? 1.0636 0.6447 1.0773 0.2869  0.1408  -0.0337 261 VAL D CG1 
16670 C CG2 . VAL D 261 ? 1.0951 0.6807 1.0861 0.2651  0.1247  -0.0617 261 VAL D CG2 
16671 N N   . VAL D 262 ? 1.1063 0.7377 1.1341 0.2886  0.1167  0.0021  262 VAL D N   
16672 C CA  . VAL D 262 ? 1.1551 0.7949 1.1928 0.2967  0.1181  0.0176  262 VAL D CA  
16673 C C   . VAL D 262 ? 1.1085 0.7390 1.1692 0.2988  0.1209  0.0285  262 VAL D C   
16674 O O   . VAL D 262 ? 1.1177 0.7366 1.1849 0.2934  0.1204  0.0264  262 VAL D O   
16675 C CB  . VAL D 262 ? 0.9950 0.6541 1.0301 0.2946  0.1077  0.0252  262 VAL D CB  
16676 C CG1 . VAL D 262 ? 1.1683 0.8381 1.1827 0.2947  0.1037  0.0180  262 VAL D CG1 
16677 C CG2 . VAL D 262 ? 0.8303 0.4918 0.8744 0.2864  0.1001  0.0280  262 VAL D CG2 
16678 N N   . PRO D 263 ? 1.0651 0.7012 1.1397 0.3062  0.1231  0.0411  263 PRO D N   
16679 C CA  . PRO D 263 ? 1.1110 0.7416 1.2077 0.3085  0.1224  0.0531  263 PRO D CA  
16680 C C   . PRO D 263 ? 1.1122 0.7495 1.2082 0.3010  0.1106  0.0605  263 PRO D C   
16681 O O   . PRO D 263 ? 1.0915 0.7428 1.1869 0.3003  0.1038  0.0675  263 PRO D O   
16682 C CB  . PRO D 263 ? 1.0089 0.6491 1.1210 0.3171  0.1260  0.0630  263 PRO D CB  
16683 C CG  . PRO D 263 ? 1.0393 0.6847 1.1356 0.3197  0.1329  0.0552  263 PRO D CG  
16684 C CD  . PRO D 263 ? 1.0003 0.6486 1.0731 0.3121  0.1257  0.0461  263 PRO D CD  
16685 N N   . GLU D 264 ? 1.1238 0.7496 1.2187 0.2947  0.1097  0.0580  264 GLU D N   
16686 C CA  . GLU D 264 ? 0.9466 0.5768 1.0383 0.2869  0.1017  0.0641  264 GLU D CA  
16687 C C   . GLU D 264 ? 1.0613 0.6958 1.1618 0.2895  0.0955  0.0806  264 GLU D C   
16688 O O   . GLU D 264 ? 1.0729 0.7033 1.1884 0.2968  0.0970  0.0890  264 GLU D O   
16689 C CB  . GLU D 264 ? 1.1141 0.7287 1.2061 0.2795  0.1048  0.0593  264 GLU D CB  
16690 C CG  . GLU D 264 ? 1.0993 0.7146 1.1812 0.2725  0.1063  0.0420  264 GLU D CG  
16691 C CD  . GLU D 264 ? 1.1695 0.7692 1.2557 0.2632  0.1098  0.0365  264 GLU D CD  
16692 O OE1 . GLU D 264 ? 1.2301 0.8353 1.3162 0.2548  0.1065  0.0397  264 GLU D OE1 
16693 O OE2 . GLU D 264 ? 1.2910 0.8719 1.3815 0.2638  0.1174  0.0286  264 GLU D OE2 
16694 N N   . VAL D 265 ? 1.1114 0.7551 1.2026 0.2833  0.0883  0.0845  265 VAL D N   
16695 C CA  . VAL D 265 ? 0.9815 0.6298 1.0735 0.2830  0.0804  0.0981  265 VAL D CA  
16696 C C   . VAL D 265 ? 0.9611 0.6048 1.0406 0.2741  0.0795  0.0997  265 VAL D C   
16697 O O   . VAL D 265 ? 1.0122 0.6641 1.0816 0.2686  0.0795  0.0923  265 VAL D O   
16698 C CB  . VAL D 265 ? 0.8979 0.5624 0.9874 0.2839  0.0747  0.0986  265 VAL D CB  
16699 C CG1 . VAL D 265 ? 0.8036 0.4725 0.8895 0.2811  0.0650  0.1097  265 VAL D CG1 
16700 C CG2 . VAL D 265 ? 0.8220 0.4915 0.9255 0.2919  0.0779  0.0979  265 VAL D CG2 
16701 N N   . PRO D 266 ? 0.9333 0.5640 1.0144 0.2729  0.0797  0.1103  266 PRO D N   
16702 C CA  . PRO D 266 ? 0.9896 0.6141 1.0587 0.2639  0.0819  0.1127  266 PRO D CA  
16703 C C   . PRO D 266 ? 1.0985 0.7364 1.1514 0.2581  0.0784  0.1108  266 PRO D C   
16704 O O   . PRO D 266 ? 1.0923 0.7396 1.1407 0.2608  0.0710  0.1146  266 PRO D O   
16705 C CB  . PRO D 266 ? 0.9189 0.5309 0.9892 0.2665  0.0792  0.1305  266 PRO D CB  
16706 C CG  . PRO D 266 ? 0.9218 0.5266 1.0126 0.2765  0.0808  0.1324  266 PRO D CG  
16707 C CD  . PRO D 266 ? 1.0406 0.6614 1.1363 0.2808  0.0791  0.1219  266 PRO D CD  
16708 N N   . THR D 267 ? 1.1577 0.7963 1.2050 0.2502  0.0846  0.1040  267 THR D N   
16709 C CA  . THR D 267 ? 1.0839 0.7335 1.1175 0.2451  0.0848  0.1013  267 THR D CA  
16710 C C   . THR D 267 ? 0.9684 0.6323 1.0019 0.2496  0.0801  0.0939  267 THR D C   
16711 O O   . THR D 267 ? 1.1647 0.8351 1.1867 0.2471  0.0795  0.0929  267 THR D O   
16712 C CB  . THR D 267 ? 1.1589 0.8018 1.1750 0.2415  0.0835  0.1143  267 THR D CB  
16713 O OG1 . THR D 267 ? 1.0023 0.6497 1.0127 0.2465  0.0729  0.1203  267 THR D OG1 
16714 C CG2 . THR D 267 ? 1.4443 1.0698 1.4621 0.2396  0.0874  0.1258  267 THR D CG2 
16715 N N   . LEU D 268 ? 1.0511 0.7180 1.0961 0.2558  0.0785  0.0889  268 LEU D N   
16716 C CA  . LEU D 268 ? 0.9948 0.6737 1.0406 0.2601  0.0760  0.0828  268 LEU D CA  
16717 C C   . LEU D 268 ? 0.9992 0.6822 1.0525 0.2632  0.0789  0.0732  268 LEU D C   
16718 O O   . LEU D 268 ? 1.0870 0.7793 1.1391 0.2617  0.0802  0.0660  268 LEU D O   
16719 C CB  . LEU D 268 ? 1.0656 0.7452 1.1146 0.2651  0.0697  0.0900  268 LEU D CB  
16720 C CG  . LEU D 268 ? 0.9411 0.6217 0.9787 0.2613  0.0636  0.0966  268 LEU D CG  
16721 C CD1 . LEU D 268 ? 0.8999 0.5855 0.9457 0.2651  0.0559  0.1014  268 LEU D CD1 
16722 C CD2 . LEU D 268 ? 0.8759 0.5614 0.9013 0.2568  0.0666  0.0893  268 LEU D CD2 
16723 N N   . LEU D 269 ? 1.1292 0.8059 1.1897 0.2680  0.0799  0.0731  269 LEU D N   
16724 C CA  . LEU D 269 ? 0.9687 0.6476 1.0307 0.2707  0.0826  0.0630  269 LEU D CA  
16725 C C   . LEU D 269 ? 0.9430 0.6102 1.0085 0.2665  0.0866  0.0576  269 LEU D C   
16726 O O   . LEU D 269 ? 1.0638 0.7177 1.1354 0.2692  0.0894  0.0620  269 LEU D O   
16727 C CB  . LEU D 269 ? 0.8850 0.5640 0.9505 0.2791  0.0838  0.0649  269 LEU D CB  
16728 C CG  . LEU D 269 ? 0.9695 0.6480 1.0311 0.2826  0.0879  0.0553  269 LEU D CG  
16729 C CD1 . LEU D 269 ? 0.8408 0.5311 0.8936 0.2803  0.0847  0.0481  269 LEU D CD1 
16730 C CD2 . LEU D 269 ? 0.7895 0.4686 0.8541 0.2908  0.0917  0.0588  269 LEU D CD2 
16731 N N   . LEU D 270 ? 0.8600 0.5322 0.9246 0.2600  0.0868  0.0484  270 LEU D N   
16732 C CA  . LEU D 270 ? 1.0303 0.6908 1.0998 0.2536  0.0905  0.0412  270 LEU D CA  
16733 C C   . LEU D 270 ? 1.0073 0.6732 1.0738 0.2520  0.0890  0.0263  270 LEU D C   
16734 O O   . LEU D 270 ? 1.0366 0.7191 1.0977 0.2547  0.0841  0.0229  270 LEU D O   
16735 C CB  . LEU D 270 ? 0.9933 0.6541 1.0673 0.2436  0.0922  0.0436  270 LEU D CB  
16736 C CG  . LEU D 270 ? 0.8228 0.4802 0.8930 0.2438  0.0929  0.0580  270 LEU D CG  
16737 C CD1 . LEU D 270 ? 0.9496 0.6125 1.0208 0.2346  0.0964  0.0587  270 LEU D CD1 
16738 C CD2 . LEU D 270 ? 1.1075 0.7450 1.1801 0.2462  0.0955  0.0681  270 LEU D CD2 
16739 N N   . THR D 271 ? 0.9528 0.6038 1.0222 0.2475  0.0930  0.0174  271 THR D N   
16740 C CA  . THR D 271 ? 1.0882 0.7422 1.1516 0.2441  0.0907  0.0009  271 THR D CA  
16741 C C   . THR D 271 ? 1.0867 0.7384 1.1584 0.2306  0.0900  -0.0112 271 THR D C   
16742 O O   . THR D 271 ? 1.2208 0.8510 1.2989 0.2255  0.0968  -0.0149 271 THR D O   
16743 C CB  . THR D 271 ? 0.9490 0.5843 1.0060 0.2497  0.0974  -0.0054 271 THR D CB  
16744 O OG1 . THR D 271 ? 1.6382 1.2506 1.7069 0.2476  0.1053  -0.0015 271 THR D OG1 
16745 C CG2 . THR D 271 ? 0.8655 0.5044 0.9153 0.2625  0.0993  0.0027  271 THR D CG2 
16746 N N   . GLN D 272 ? 1.0051 0.6793 1.0799 0.2248  0.0821  -0.0168 272 GLN D N   
16747 C CA  . GLN D 272 ? 1.0538 0.7309 1.1409 0.2103  0.0799  -0.0295 272 GLN D CA  
16748 C C   . GLN D 272 ? 1.0991 0.7881 1.1781 0.2063  0.0703  -0.0474 272 GLN D C   
16749 O O   . GLN D 272 ? 1.1571 0.8719 1.2330 0.2099  0.0603  -0.0470 272 GLN D O   
16750 C CB  . GLN D 272 ? 1.0182 0.7147 1.1207 0.2056  0.0787  -0.0214 272 GLN D CB  
16751 C CG  . GLN D 272 ? 1.1836 0.8899 1.3056 0.1901  0.0767  -0.0324 272 GLN D CG  
16752 C CD  . GLN D 272 ? 1.0655 0.7454 1.1937 0.1792  0.0839  -0.0406 272 GLN D CD  
16753 O OE1 . GLN D 272 ? 1.2759 0.9454 1.3960 0.1766  0.0812  -0.0553 272 GLN D OE1 
16754 N NE2 . GLN D 272 ? 0.9974 0.6641 1.1385 0.1726  0.0942  -0.0312 272 GLN D NE2 
16755 N N   . LYS D 273 ? 1.0410 0.7109 1.1157 0.1994  0.0730  -0.0623 273 LYS D N   
16756 C CA  . LYS D 273 ? 1.0692 0.7478 1.1309 0.1944  0.0632  -0.0814 273 LYS D CA  
16757 C C   . LYS D 273 ? 1.2097 0.9093 1.2906 0.1788  0.0530  -0.0920 273 LYS D C   
16758 O O   . LYS D 273 ? 1.4038 1.1252 1.4768 0.1764  0.0390  -0.1027 273 LYS D O   
16759 C CB  . LYS D 273 ? 1.0407 0.6886 1.0887 0.1927  0.0715  -0.0958 273 LYS D CB  
16760 C CG  . LYS D 273 ? 1.1942 0.8242 1.2283 0.2086  0.0825  -0.0853 273 LYS D CG  
16761 C CD  . LYS D 273 ? 1.2901 0.9055 1.2986 0.2121  0.0861  -0.1012 273 LYS D CD  
16762 C CE  . LYS D 273 ? 1.5233 1.1167 1.5280 0.2258  0.1013  -0.0923 273 LYS D CE  
16763 N NZ  . LYS D 273 ? 1.3861 0.9472 1.4058 0.2220  0.1145  -0.0964 273 LYS D NZ  
16764 N N   . ASP D 274 ? 1.1710 0.8654 1.2776 0.1682  0.0597  -0.0882 274 ASP D N   
16765 C CA  . ASP D 274 ? 1.0834 0.7991 1.2147 0.1523  0.0521  -0.0973 274 ASP D CA  
16766 C C   . ASP D 274 ? 1.1477 0.8989 1.2913 0.1582  0.0449  -0.0851 274 ASP D C   
16767 O O   . ASP D 274 ? 1.1444 0.8948 1.2960 0.1636  0.0540  -0.0684 274 ASP D O   
16768 C CB  . ASP D 274 ? 1.1081 0.8029 1.2629 0.1385  0.0651  -0.0966 274 ASP D CB  
16769 C CG  . ASP D 274 ? 1.1415 0.8528 1.3244 0.1184  0.0593  -0.1107 274 ASP D CG  
16770 O OD1 . ASP D 274 ? 1.2924 1.0372 1.4800 0.1158  0.0431  -0.1193 274 ASP D OD1 
16771 O OD2 . ASP D 274 ? 1.0798 0.7710 1.2815 0.1052  0.0706  -0.1123 274 ASP D OD2 
16772 N N   . TYR D 275 ? 1.2099 0.9915 1.3538 0.1576  0.0284  -0.0933 275 TYR D N   
16773 C CA  . TYR D 275 ? 1.0600 0.8761 1.2183 0.1646  0.0210  -0.0825 275 TYR D CA  
16774 C C   . TYR D 275 ? 1.0283 0.8601 1.2251 0.1526  0.0260  -0.0801 275 TYR D C   
16775 O O   . TYR D 275 ? 1.1166 0.9650 1.3266 0.1597  0.0298  -0.0667 275 TYR D O   
16776 C CB  . TYR D 275 ? 0.9843 0.8286 1.1334 0.1677  0.0008  -0.0910 275 TYR D CB  
16777 C CG  . TYR D 275 ? 1.1158 0.9458 1.2247 0.1807  -0.0019 -0.0909 275 TYR D CG  
16778 C CD1 . TYR D 275 ? 1.1425 0.9715 1.2371 0.1984  0.0025  -0.0738 275 TYR D CD1 
16779 C CD2 . TYR D 275 ? 1.2377 1.0534 1.3229 0.1746  -0.0068 -0.1085 275 TYR D CD2 
16780 C CE1 . TYR D 275 ? 1.1813 0.9976 1.2415 0.2097  0.0023  -0.0727 275 TYR D CE1 
16781 C CE2 . TYR D 275 ? 1.1312 0.9336 1.1789 0.1866  -0.0063 -0.1082 275 TYR D CE2 
16782 C CZ  . TYR D 275 ? 1.0946 0.8979 1.1309 0.2041  -0.0014 -0.0894 275 TYR D CZ  
16783 O OH  . TYR D 275 ? 1.1616 0.9521 1.1630 0.2152  0.0010  -0.0884 275 TYR D OH  
16784 N N   . ASP D 276 ? 0.9587 0.7834 1.1738 0.1339  0.0279  -0.0932 276 ASP D N   
16785 C CA  . ASP D 276 ? 1.0977 0.9356 1.3513 0.1205  0.0353  -0.0912 276 ASP D CA  
16786 C C   . ASP D 276 ? 1.0687 0.8833 1.3231 0.1236  0.0566  -0.0738 276 ASP D C   
16787 O O   . ASP D 276 ? 1.0310 0.8557 1.3133 0.1149  0.0662  -0.0684 276 ASP D O   
16788 C CB  . ASP D 276 ? 1.0449 0.8776 1.3175 0.0983  0.0326  -0.1104 276 ASP D CB  
16789 C CG  . ASP D 276 ? 1.1532 1.0135 1.4273 0.0921  0.0095  -0.1290 276 ASP D CG  
16790 O OD1 . ASP D 276 ? 1.2742 1.1756 1.5684 0.0950  -0.0032 -0.1261 276 ASP D OD1 
16791 O OD2 . ASP D 276 ? 1.3429 1.1838 1.5978 0.0847  0.0040  -0.1463 276 ASP D OD2 
16792 N N   . LYS D 277 ? 1.0841 0.8691 1.3081 0.1356  0.0637  -0.0647 277 LYS D N   
16793 C CA  . LYS D 277 ? 1.0294 0.7927 1.2483 0.1399  0.0805  -0.0475 277 LYS D CA  
16794 C C   . LYS D 277 ? 1.0216 0.7921 1.2221 0.1582  0.0799  -0.0335 277 LYS D C   
16795 O O   . LYS D 277 ? 1.0970 0.8598 1.2952 0.1616  0.0913  -0.0196 277 LYS D O   
16796 C CB  . LYS D 277 ? 1.0215 0.7445 1.2292 0.1356  0.0900  -0.0484 277 LYS D CB  
16797 C CG  . LYS D 277 ? 1.0698 0.7809 1.3022 0.1162  0.0991  -0.0543 277 LYS D CG  
16798 C CD  . LYS D 277 ? 1.1702 0.8381 1.3926 0.1154  0.1121  -0.0481 277 LYS D CD  
16799 C CE  . LYS D 277 ? 1.2984 0.9447 1.5056 0.1174  0.1074  -0.0626 277 LYS D CE  
16800 N NZ  . LYS D 277 ? 1.3184 0.9235 1.5283 0.1118  0.1213  -0.0604 277 LYS D NZ  
16801 N N   . MET D 278 ? 1.0006 0.7847 1.1871 0.1691  0.0671  -0.0374 278 MET D N   
16802 C CA  . MET D 278 ? 0.9559 0.7442 1.1259 0.1858  0.0670  -0.0247 278 MET D CA  
16803 C C   . MET D 278 ? 0.9742 0.7747 1.1565 0.1883  0.0756  -0.0132 278 MET D C   
16804 O O   . MET D 278 ? 0.8806 0.6664 1.0469 0.1963  0.0830  -0.0018 278 MET D O   
16805 C CB  . MET D 278 ? 0.8899 0.6976 1.0502 0.1954  0.0523  -0.0296 278 MET D CB  
16806 C CG  . MET D 278 ? 1.2025 1.0118 1.3476 0.2117  0.0531  -0.0171 278 MET D CG  
16807 S SD  . MET D 278 ? 0.9898 0.7648 1.1110 0.2187  0.0638  -0.0070 278 MET D SD  
16808 C CE  . MET D 278 ? 0.9033 0.6707 1.0008 0.2266  0.0560  -0.0135 278 MET D CE  
16809 N N   . VAL D 279 ? 0.8984 0.7254 1.1089 0.1815  0.0748  -0.0168 279 VAL D N   
16810 C CA  . VAL D 279 ? 0.9227 0.7621 1.1456 0.1846  0.0851  -0.0075 279 VAL D CA  
16811 C C   . VAL D 279 ? 0.9698 0.7842 1.1848 0.1787  0.1020  0.0014  279 VAL D C   
16812 O O   . VAL D 279 ? 0.9308 0.7367 1.1297 0.1867  0.1096  0.0114  279 VAL D O   
16813 C CB  . VAL D 279 ? 1.0166 0.8912 1.2771 0.1781  0.0823  -0.0133 279 VAL D CB  
16814 C CG1 . VAL D 279 ? 0.8232 0.7080 1.0978 0.1809  0.0974  -0.0046 279 VAL D CG1 
16815 C CG2 . VAL D 279 ? 0.9103 0.8110 1.1754 0.1866  0.0635  -0.0189 279 VAL D CG2 
16816 N N   . LYS D 280 ? 0.9769 0.7783 1.2017 0.1645  0.1076  -0.0021 280 LYS D N   
16817 C CA  . LYS D 280 ? 0.8793 0.6557 1.0959 0.1587  0.1236  0.0086  280 LYS D CA  
16818 C C   . LYS D 280 ? 1.0106 0.7595 1.1933 0.1692  0.1237  0.0186  280 LYS D C   
16819 O O   . LYS D 280 ? 1.0753 0.8122 1.2441 0.1710  0.1339  0.0307  280 LYS D O   
16820 C CB  . LYS D 280 ? 0.9204 0.6841 1.1541 0.1419  0.1289  0.0032  280 LYS D CB  
16821 C CG  . LYS D 280 ? 0.8692 0.6593 1.1410 0.1283  0.1331  -0.0038 280 LYS D CG  
16822 C CD  . LYS D 280 ? 1.0547 0.8263 1.3427 0.1102  0.1437  -0.0055 280 LYS D CD  
16823 C CE  . LYS D 280 ? 1.4168 1.2168 1.7477 0.0950  0.1478  -0.0132 280 LYS D CE  
16824 N NZ  . LYS D 280 ? 1.2974 1.0792 1.6475 0.0755  0.1557  -0.0183 280 LYS D NZ  
16825 N N   . THR D 281 ? 1.0733 0.8141 1.2436 0.1758  0.1125  0.0133  281 THR D N   
16826 C CA  . THR D 281 ? 1.0975 0.8159 1.2415 0.1862  0.1118  0.0225  281 THR D CA  
16827 C C   . THR D 281 ? 1.0796 0.8084 1.2105 0.1976  0.1105  0.0297  281 THR D C   
16828 O O   . THR D 281 ? 1.0747 0.7892 1.1891 0.2008  0.1156  0.0410  281 THR D O   
16829 C CB  . THR D 281 ? 0.8645 0.5743 1.0011 0.1909  0.1025  0.0141  281 THR D CB  
16830 O OG1 . THR D 281 ? 1.4043 1.1328 1.5347 0.2011  0.0928  0.0105  281 THR D OG1 
16831 C CG2 . THR D 281 ? 0.8589 0.5663 1.0105 0.1791  0.1008  0.0001  281 THR D CG2 
16832 N N   . SER D 282 ? 0.8690 0.6211 1.0070 0.2031  0.1034  0.0234  282 SER D N   
16833 C CA  . SER D 282 ? 0.9075 0.6673 1.0354 0.2139  0.1029  0.0287  282 SER D CA  
16834 C C   . SER D 282 ? 0.9457 0.7046 1.0716 0.2112  0.1150  0.0357  282 SER D C   
16835 O O   . SER D 282 ? 1.0564 0.8057 1.1632 0.2170  0.1171  0.0425  282 SER D O   
16836 C CB  . SER D 282 ? 0.9049 0.6899 1.0454 0.2199  0.0946  0.0221  282 SER D CB  
16837 O OG  . SER D 282 ? 0.9535 0.7379 1.0877 0.2237  0.0835  0.0164  282 SER D OG  
16838 N N   . LEU D 283 ? 0.8803 0.6494 1.0255 0.2015  0.1237  0.0336  283 LEU D N   
16839 C CA  . LEU D 283 ? 0.9520 0.7201 1.0937 0.1985  0.1382  0.0398  283 LEU D CA  
16840 C C   . LEU D 283 ? 1.0156 0.7563 1.1318 0.1953  0.1440  0.0505  283 LEU D C   
16841 O O   . LEU D 283 ? 1.0540 0.7872 1.1490 0.1987  0.1493  0.0568  283 LEU D O   
16842 C CB  . LEU D 283 ? 0.8334 0.6192 1.0052 0.1881  0.1480  0.0358  283 LEU D CB  
16843 C CG  . LEU D 283 ? 0.8487 0.6665 1.0510 0.1912  0.1411  0.0266  283 LEU D CG  
16844 C CD1 . LEU D 283 ? 0.8179 0.6540 1.0549 0.1786  0.1495  0.0225  283 LEU D CD1 
16845 C CD2 . LEU D 283 ? 0.8144 0.6438 1.0141 0.2038  0.1432  0.0277  283 LEU D CD2 
16846 N N   . GLU D 284 ? 0.9868 0.7118 1.1043 0.1892  0.1422  0.0525  284 GLU D N   
16847 C CA  . GLU D 284 ? 0.9448 0.6439 1.0405 0.1876  0.1463  0.0651  284 GLU D CA  
16848 C C   . GLU D 284 ? 0.9891 0.6797 1.0611 0.1988  0.1364  0.0702  284 GLU D C   
16849 O O   . GLU D 284 ? 1.0332 0.7117 1.0826 0.1999  0.1391  0.0807  284 GLU D O   
16850 C CB  . GLU D 284 ? 0.8774 0.5600 0.9834 0.1806  0.1463  0.0654  284 GLU D CB  
16851 C CG  . GLU D 284 ? 1.0397 0.6953 1.1266 0.1798  0.1512  0.0812  284 GLU D CG  
16852 C CD  . GLU D 284 ? 1.2304 0.8656 1.3293 0.1735  0.1537  0.0825  284 GLU D CD  
16853 O OE1 . GLU D 284 ? 1.3953 1.0356 1.5179 0.1628  0.1589  0.0731  284 GLU D OE1 
16854 O OE2 . GLU D 284 ? 1.2591 0.8733 1.3458 0.1793  0.1504  0.0926  284 GLU D OE2 
16855 N N   . ALA D 285 ? 1.0330 0.7306 1.1097 0.2066  0.1250  0.0629  285 ALA D N   
16856 C CA  . ALA D 285 ? 1.0129 0.7047 1.0731 0.2164  0.1162  0.0670  285 ALA D CA  
16857 C C   . ALA D 285 ? 0.8730 0.5705 0.9183 0.2201  0.1178  0.0689  285 ALA D C   
16858 O O   . ALA D 285 ? 1.1333 0.8223 1.1615 0.2243  0.1126  0.0751  285 ALA D O   
16859 C CB  . ALA D 285 ? 0.9569 0.6567 1.0260 0.2232  0.1069  0.0584  285 ALA D CB  
16860 N N   . ARG D 286 ? 0.9329 0.6452 0.9865 0.2183  0.1250  0.0630  286 ARG D N   
16861 C CA  . ARG D 286 ? 1.0109 0.7262 1.0509 0.2217  0.1290  0.0625  286 ARG D CA  
16862 C C   . ARG D 286 ? 1.0646 0.7774 1.0958 0.2143  0.1438  0.0654  286 ARG D C   
16863 O O   . ARG D 286 ? 1.0852 0.8043 1.1125 0.2161  0.1516  0.0611  286 ARG D O   
16864 C CB  . ARG D 286 ? 0.8128 0.5458 0.8690 0.2289  0.1266  0.0536  286 ARG D CB  
16865 C CG  . ARG D 286 ? 0.9251 0.6576 0.9692 0.2346  0.1292  0.0515  286 ARG D CG  
16866 C CD  . ARG D 286 ? 0.9191 0.6359 0.9388 0.2358  0.1225  0.0562  286 ARG D CD  
16867 N NE  . ARG D 286 ? 0.8858 0.6025 0.8995 0.2414  0.1224  0.0514  286 ARG D NE  
16868 C CZ  . ARG D 286 ? 0.9332 0.6381 0.9254 0.2403  0.1191  0.0524  286 ARG D CZ  
16869 N NH1 . ARG D 286 ? 1.0251 0.7197 0.9990 0.2351  0.1141  0.0598  286 ARG D NH1 
16870 N NH2 . ARG D 286 ? 1.1076 0.8110 1.0974 0.2443  0.1202  0.0464  286 ARG D NH2 
16871 N N   . ASN D 287 ? 1.0821 0.7838 1.1098 0.2063  0.1493  0.0732  287 ASN D N   
16872 C CA  . ASN D 287 ? 1.0128 0.7096 1.0297 0.1984  0.1652  0.0784  287 ASN D CA  
16873 C C   . ASN D 287 ? 1.1208 0.8362 1.1562 0.1967  0.1789  0.0698  287 ASN D C   
16874 O O   . ASN D 287 ? 1.3262 1.0392 1.3449 0.1949  0.1922  0.0707  287 ASN D O   
16875 C CB  . ASN D 287 ? 1.0297 0.7109 1.0079 0.1992  0.1648  0.0866  287 ASN D CB  
16876 C CG  . ASN D 287 ? 1.4002 1.0680 1.3589 0.1906  0.1780  0.0979  287 ASN D CG  
16877 O OD1 . ASN D 287 ? 1.5855 1.2431 1.5502 0.1858  0.1792  0.1072  287 ASN D OD1 
16878 N ND2 . ASN D 287 ? 1.7162 1.3819 1.6499 0.1885  0.1897  0.0975  287 ASN D ND2 
16879 N N   . ILE D 288 ? 1.0923 0.8269 1.1620 0.1976  0.1758  0.0615  288 ILE D N   
16880 C CA  . ILE D 288 ? 1.0680 0.8245 1.1633 0.1973  0.1872  0.0543  288 ILE D CA  
16881 C C   . ILE D 288 ? 1.1990 0.9605 1.3155 0.1850  0.1998  0.0564  288 ILE D C   
16882 O O   . ILE D 288 ? 1.1050 0.8709 1.2432 0.1797  0.1925  0.0543  288 ILE D O   
16883 C CB  . ILE D 288 ? 0.9115 0.6893 1.0333 0.2058  0.1748  0.0454  288 ILE D CB  
16884 C CG1 . ILE D 288 ? 0.9878 0.7591 1.0899 0.2175  0.1657  0.0442  288 ILE D CG1 
16885 C CG2 . ILE D 288 ? 0.9395 0.7435 1.0953 0.2057  0.1853  0.0396  288 ILE D CG2 
16886 C CD1 . ILE D 288 ? 1.0999 0.8827 1.2170 0.2257  0.1498  0.0399  288 ILE D CD1 
16887 N N   . LYS D 289 ? 1.3052 1.0648 1.4147 0.1797  0.2199  0.0601  289 LYS D N   
16888 C CA  . LYS D 289 ? 1.3239 1.0875 1.4543 0.1670  0.2354  0.0635  289 LYS D CA  
16889 C C   . LYS D 289 ? 1.3599 1.1543 1.5307 0.1669  0.2465  0.0549  289 LYS D C   
16890 O O   . LYS D 289 ? 1.1705 0.9706 1.3353 0.1725  0.2595  0.0526  289 LYS D O   
16891 C CB  . LYS D 289 ? 1.3674 1.1078 1.4624 0.1607  0.2524  0.0755  289 LYS D CB  
16892 C CG  . LYS D 289 ? 1.4227 1.1350 1.4806 0.1620  0.2398  0.0861  289 LYS D CG  
16893 C CD  . LYS D 289 ? 1.7267 1.4166 1.7489 0.1556  0.2546  0.1006  289 LYS D CD  
16894 C CE  . LYS D 289 ? 1.7633 1.4289 1.7507 0.1592  0.2397  0.1123  289 LYS D CE  
16895 N NZ  . LYS D 289 ? 2.1663 1.8105 2.1153 0.1537  0.2522  0.1286  289 LYS D NZ  
16896 N N   . ILE D 290 ? 1.3659 1.1808 1.5791 0.1606  0.2407  0.0493  290 ILE D N   
16897 C CA  . ILE D 290 ? 1.3674 1.2169 1.6269 0.1605  0.2477  0.0418  290 ILE D CA  
16898 C C   . ILE D 290 ? 1.4878 1.3428 1.7682 0.1468  0.2722  0.0457  290 ILE D C   
16899 O O   . ILE D 290 ? 1.4063 1.2544 1.6980 0.1331  0.2734  0.0486  290 ILE D O   
16900 C CB  . ILE D 290 ? 1.1483 1.0210 1.4435 0.1604  0.2259  0.0331  290 ILE D CB  
16901 C CG1 . ILE D 290 ? 1.1277 0.9937 1.4006 0.1737  0.2031  0.0304  290 ILE D CG1 
16902 C CG2 . ILE D 290 ? 1.3450 1.2577 1.6919 0.1609  0.2305  0.0266  290 ILE D CG2 
16903 C CD1 . ILE D 290 ? 1.1968 1.0677 1.4588 0.1897  0.2035  0.0296  290 ILE D CD1 
16904 N N   . LYS D 291 ? 1.6519 1.5186 1.9392 0.1503  0.2934  0.0455  291 LYS D N   
16905 C CA  . LYS D 291 ? 1.7159 1.5903 2.0252 0.1380  0.3205  0.0494  291 LYS D CA  
16906 C C   . LYS D 291 ? 1.6383 1.5526 2.0145 0.1322  0.3171  0.0416  291 LYS D C   
16907 O O   . LYS D 291 ? 1.5412 1.4856 1.9511 0.1405  0.3221  0.0358  291 LYS D O   
16908 C CB  . LYS D 291 ? 1.7907 1.6623 2.0808 0.1446  0.3460  0.0506  291 LYS D CB  
16909 C CG  . LYS D 291 ? 1.8039 1.6364 2.0260 0.1463  0.3509  0.0587  291 LYS D CG  
16910 C CD  . LYS D 291 ? 1.8666 1.6946 2.0657 0.1512  0.3772  0.0575  291 LYS D CD  
16911 C CE  . LYS D 291 ? 1.9346 1.7253 2.0644 0.1503  0.3809  0.0656  291 LYS D CE  
16912 N NZ  . LYS D 291 ? 1.8715 1.6558 1.9739 0.1536  0.4077  0.0625  291 LYS D NZ  
16913 N N   . ILE D 292 ? 1.5882 1.5026 1.9847 0.1181  0.3076  0.0411  292 ILE D N   
16914 C CA  . ILE D 292 ? 1.7108 1.6627 2.1699 0.1095  0.3002  0.0325  292 ILE D CA  
16915 C C   . ILE D 292 ? 1.8958 1.8673 2.3954 0.0978  0.3293  0.0351  292 ILE D C   
16916 O O   . ILE D 292 ? 1.8868 1.8344 2.3690 0.0860  0.3510  0.0444  292 ILE D O   
16917 C CB  . ILE D 292 ? 1.5700 1.5113 2.0338 0.0969  0.2804  0.0287  292 ILE D CB  
16918 C CG1 . ILE D 292 ? 1.6077 1.5283 2.0302 0.1090  0.2544  0.0265  292 ILE D CG1 
16919 C CG2 . ILE D 292 ? 1.5708 1.5532 2.0982 0.0870  0.2692  0.0174  292 ILE D CG2 
16920 C CD1 . ILE D 292 ? 1.4399 1.3340 1.8485 0.0982  0.2428  0.0258  292 ILE D CD1 
16921 N N   . THR D 293 ? 1.9908 2.0065 2.5459 0.1013  0.3303  0.0282  293 THR D N   
16922 C CA  . THR D 293 ? 1.9419 1.9833 2.5458 0.0909  0.3583  0.0298  293 THR D CA  
16923 C C   . THR D 293 ? 1.8707 1.9351 2.5301 0.0702  0.3504  0.0244  293 THR D C   
16924 O O   . THR D 293 ? 1.9180 1.9884 2.6072 0.0542  0.3754  0.0285  293 THR D O   
16925 C CB  . THR D 293 ? 1.8284 1.9064 2.4670 0.1072  0.3657  0.0258  293 THR D CB  
16926 O OG1 . THR D 293 ? 1.7528 1.8071 2.3389 0.1264  0.3661  0.0275  293 THR D OG1 
16927 C CG2 . THR D 293 ? 1.8031 1.9020 2.4829 0.0996  0.4021  0.0290  293 THR D CG2 
16928 N N   . GLU D 294 ? 1.6596 1.7358 2.3314 0.0695  0.3164  0.0149  294 GLU D N   
16929 C CA  . GLU D 294 ? 1.7135 1.8104 2.4342 0.0493  0.3039  0.0064  294 GLU D CA  
16930 C C   . GLU D 294 ? 1.5500 1.6988 2.3499 0.0392  0.3133  0.0018  294 GLU D C   
16931 O O   . GLU D 294 ? 1.4803 1.6324 2.3142 0.0172  0.3275  0.0016  294 GLU D O   
16932 C CB  . GLU D 294 ? 1.8222 1.8773 2.5187 0.0299  0.3138  0.0110  294 GLU D CB  
16933 C CG  . GLU D 294 ? 1.7952 1.8209 2.4550 0.0292  0.2864  0.0053  294 GLU D CG  
16934 C CD  . GLU D 294 ? 1.9401 1.9163 2.5653 0.0165  0.2992  0.0137  294 GLU D CD  
16935 O OE1 . GLU D 294 ? 1.8851 1.8539 2.5257 0.0024  0.3273  0.0224  294 GLU D OE1 
16936 O OE2 . GLU D 294 ? 2.0574 2.0021 2.6413 0.0211  0.2821  0.0126  294 GLU D OE2 
16937 N N   . ILE D 295 ? 1.3641 1.5537 2.1963 0.0555  0.3056  -0.0011 295 ILE D N   
16938 C CA  . ILE D 295 ? 1.3586 1.6034 2.2719 0.0488  0.3125  -0.0048 295 ILE D CA  
16939 C C   . ILE D 295 ? 1.2571 1.5358 2.2206 0.0324  0.2821  -0.0174 295 ILE D C   
16940 O O   . ILE D 295 ? 1.1141 1.3941 2.0585 0.0397  0.2478  -0.0244 295 ILE D O   
16941 C CB  . ILE D 295 ? 1.2686 1.5440 2.1995 0.0744  0.3143  -0.0025 295 ILE D CB  
16942 C CG1 . ILE D 295 ? 1.3175 1.5530 2.1878 0.0906  0.3403  0.0066  295 ILE D CG1 
16943 C CG2 . ILE D 295 ? 0.9720 1.3030 1.9885 0.0694  0.3296  -0.0034 295 ILE D CG2 
16944 C CD1 . ILE D 295 ? 0.9318 1.1840 1.8041 0.1176  0.3378  0.0074  295 ILE D CD1 
16945 N N   . PRO D 296 ? 1.1624 1.4679 2.1885 0.0093  0.2937  -0.0209 296 PRO D N   
16946 C CA  . PRO D 296 ? 1.1490 1.4868 2.2219 -0.0083 0.2627  -0.0352 296 PRO D CA  
16947 C C   . PRO D 296 ? 1.0829 1.4829 2.2095 0.0045  0.2362  -0.0407 296 PRO D C   
16948 O O   . PRO D 296 ? 0.9460 1.3965 2.1485 -0.0028 0.2438  -0.0419 296 PRO D O   
16949 C CB  . PRO D 296 ? 1.0889 1.4334 2.2123 -0.0371 0.2881  -0.0357 296 PRO D CB  
16950 C CG  . PRO D 296 ? 0.9131 1.2591 2.0459 -0.0292 0.3299  -0.0219 296 PRO D CG  
16951 C CD  . PRO D 296 ? 0.9063 1.2139 1.9630 -0.0029 0.3357  -0.0126 296 PRO D CD  
16952 N N   . ILE D 297 ? 1.1122 1.5091 2.2006 0.0240  0.2053  -0.0430 297 ILE D N   
16953 C CA  . ILE D 297 ? 1.1009 1.5520 2.2301 0.0397  0.1774  -0.0453 297 ILE D CA  
16954 C C   . ILE D 297 ? 0.9961 1.4426 2.0905 0.0417  0.1340  -0.0552 297 ILE D C   
16955 O O   . ILE D 297 ? 0.9327 1.3278 1.9572 0.0432  0.1303  -0.0561 297 ILE D O   
16956 C CB  . ILE D 297 ? 1.0797 1.5340 2.1985 0.0705  0.1932  -0.0324 297 ILE D CB  
16957 C CG1 . ILE D 297 ? 1.1649 1.5552 2.1942 0.0841  0.2041  -0.0259 297 ILE D CG1 
16958 C CG2 . ILE D 297 ? 0.9351 1.4157 2.1113 0.0694  0.2311  -0.0257 297 ILE D CG2 
16959 C CD1 . ILE D 297 ? 0.9833 1.3710 1.9930 0.1136  0.2119  -0.0166 297 ILE D CD1 
16960 N N   . PRO D 298 ? 0.8731 1.3733 2.0142 0.0421  0.1007  -0.0622 298 PRO D N   
16961 C CA  . PRO D 298 ? 1.0678 1.5634 2.1714 0.0434  0.0601  -0.0720 298 PRO D CA  
16962 C C   . PRO D 298 ? 1.2153 1.7004 2.2696 0.0744  0.0453  -0.0626 298 PRO D C   
16963 O O   . PRO D 298 ? 1.3114 1.7886 2.3275 0.0770  0.0146  -0.0692 298 PRO D O   
16964 C CB  . PRO D 298 ? 0.8484 1.4096 2.0250 0.0300  0.0314  -0.0824 298 PRO D CB  
16965 C CG  . PRO D 298 ? 0.8818 1.4898 2.1279 0.0406  0.0500  -0.0712 298 PRO D CG  
16966 C CD  . PRO D 298 ? 0.9271 1.4961 2.1577 0.0412  0.0979  -0.0614 298 PRO D CD  
16967 N N   . VAL D 299 ? 1.1424 1.6263 2.1972 0.0973  0.0676  -0.0480 299 VAL D N   
16968 C CA  . VAL D 299 ? 0.9925 1.4646 2.0047 0.1266  0.0567  -0.0383 299 VAL D CA  
16969 C C   . VAL D 299 ? 1.0582 1.4707 2.0073 0.1364  0.0863  -0.0305 299 VAL D C   
16970 O O   . VAL D 299 ? 1.1241 1.5160 2.0750 0.1254  0.1179  -0.0293 299 VAL D O   
16971 C CB  . VAL D 299 ? 0.9424 1.4676 2.0121 0.1483  0.0522  -0.0282 299 VAL D CB  
16972 C CG1 . VAL D 299 ? 1.0671 1.5857 2.0974 0.1757  0.0309  -0.0194 299 VAL D CG1 
16973 C CG2 . VAL D 299 ? 0.9148 1.5057 2.0634 0.1348  0.0303  -0.0350 299 VAL D CG2 
16974 N N   . SER D 300 ? 0.9668 1.3520 1.8601 0.1565  0.0757  -0.0249 300 SER D N   
16975 C CA  . SER D 300 ? 0.9396 1.2706 1.7726 0.1659  0.0991  -0.0183 300 SER D CA  
16976 C C   . SER D 300 ? 0.9558 1.2890 1.8088 0.1785  0.1324  -0.0091 300 SER D C   
16977 O O   . SER D 300 ? 1.0873 1.4650 2.0000 0.1860  0.1353  -0.0061 300 SER D O   
16978 C CB  . SER D 300 ? 1.0886 1.3963 1.8662 0.1841  0.0788  -0.0146 300 SER D CB  
16979 O OG  . SER D 300 ? 1.2371 1.4910 1.9542 0.1879  0.0967  -0.0109 300 SER D OG  
16980 N N   . PHE D 301 ? 0.8466 1.1322 1.6496 0.1807  0.1576  -0.0053 301 PHE D N   
16981 C CA  . PHE D 301 ? 0.7843 1.0639 1.5943 0.1909  0.1914  0.0012  301 PHE D CA  
16982 C C   . PHE D 301 ? 0.8435 1.0703 1.5818 0.2020  0.2014  0.0053  301 PHE D C   
16983 O O   . PHE D 301 ? 0.9746 1.1630 1.6687 0.1896  0.2099  0.0044  301 PHE D O   
16984 C CB  . PHE D 301 ? 0.7933 1.0759 1.6309 0.1703  0.2196  -0.0007 301 PHE D CB  
16985 C CG  . PHE D 301 ? 0.9176 1.2014 1.7715 0.1776  0.2575  0.0044  301 PHE D CG  
16986 C CD1 . PHE D 301 ? 0.8270 1.0637 1.6232 0.1807  0.2823  0.0079  301 PHE D CD1 
16987 C CD2 . PHE D 301 ? 0.8537 1.1861 1.7814 0.1793  0.2693  0.0048  301 PHE D CD2 
16988 C CE1 . PHE D 301 ? 0.8318 1.0678 1.6384 0.1860  0.3186  0.0108  301 PHE D CE1 
16989 C CE2 . PHE D 301 ? 0.8170 1.1491 1.7591 0.1855  0.3074  0.0083  301 PHE D CE2 
16990 C CZ  . PHE D 301 ? 0.8323 1.1148 1.7113 0.1886  0.3324  0.0107  301 PHE D CZ  
16991 N N   . ALA D 302 ? 0.9025 1.1275 1.6309 0.2249  0.1999  0.0101  302 ALA D N   
16992 C CA  . ALA D 302 ? 0.9485 1.1261 1.6127 0.2351  0.2074  0.0129  302 ALA D CA  
16993 C C   . ALA D 302 ? 1.0653 1.2454 1.7368 0.2585  0.2183  0.0173  302 ALA D C   
16994 O O   . ALA D 302 ? 0.9564 1.1753 1.6795 0.2705  0.2122  0.0199  302 ALA D O   
16995 C CB  . ALA D 302 ? 0.7718 0.9293 1.3930 0.2353  0.1782  0.0122  302 ALA D CB  
16996 N N   . ALA D 303 ? 1.0620 1.2003 1.6828 0.2652  0.2340  0.0179  303 ALA D N   
16997 C CA  . ALA D 303 ? 0.9634 1.0952 1.5844 0.2862  0.2466  0.0201  303 ALA D CA  
16998 C C   . ALA D 303 ? 0.9850 1.1284 1.6138 0.3042  0.2203  0.0255  303 ALA D C   
16999 O O   . ALA D 303 ? 1.1876 1.3361 1.8350 0.3232  0.2284  0.0288  303 ALA D O   
17000 C CB  . ALA D 303 ? 0.9423 1.0244 1.5010 0.2858  0.2638  0.0178  303 ALA D CB  
17001 N N   . ALA D 304 ? 0.9437 1.0892 1.5568 0.2989  0.1904  0.0266  304 ALA D N   
17002 C CA  . ALA D 304 ? 1.0528 1.2086 1.6681 0.3150  0.1651  0.0331  304 ALA D CA  
17003 C C   . ALA D 304 ? 1.0669 1.2745 1.7490 0.3260  0.1558  0.0381  304 ALA D C   
17004 O O   . ALA D 304 ? 1.0360 1.2524 1.7283 0.3457  0.1443  0.0464  304 ALA D O   
17005 C CB  . ALA D 304 ? 1.0368 1.1833 1.6182 0.3048  0.1378  0.0318  304 ALA D CB  
17006 N N   . PHE D 305 ? 1.0316 1.2739 1.7611 0.3134  0.1606  0.0340  305 PHE D N   
17007 C CA  . PHE D 305 ? 1.0808 1.3778 1.8807 0.3222  0.1508  0.0385  305 PHE D CA  
17008 C C   . PHE D 305 ? 1.0972 1.4070 1.9406 0.3369  0.1809  0.0414  305 PHE D C   
17009 O O   . PHE D 305 ? 1.0697 1.4276 1.9805 0.3410  0.1803  0.0441  305 PHE D O   
17010 C CB  . PHE D 305 ? 1.0198 1.3518 1.8553 0.3002  0.1389  0.0319  305 PHE D CB  
17011 C CG  . PHE D 305 ? 1.0389 1.3534 1.8302 0.2838  0.1142  0.0262  305 PHE D CG  
17012 C CD1 . PHE D 305 ? 1.0182 1.3375 1.7902 0.2922  0.0820  0.0299  305 PHE D CD1 
17013 C CD2 . PHE D 305 ? 0.9684 1.2590 1.7354 0.2609  0.1249  0.0177  305 PHE D CD2 
17014 C CE1 . PHE D 305 ? 0.8135 1.1148 1.5436 0.2777  0.0621  0.0233  305 PHE D CE1 
17015 C CE2 . PHE D 305 ? 0.9793 1.2517 1.7076 0.2471  0.1042  0.0119  305 PHE D CE2 
17016 C CZ  . PHE D 305 ? 0.9268 1.2048 1.6370 0.2555  0.0735  0.0137  305 PHE D CZ  
17017 N N   . GLU D 306 ? 1.1646 1.4315 1.9693 0.3440  0.2067  0.0400  306 GLU D N   
17018 C CA  . GLU D 306 ? 1.0958 1.3680 1.9351 0.3594  0.2381  0.0409  306 GLU D CA  
17019 C C   . GLU D 306 ? 1.1442 1.4301 2.0088 0.3866  0.2253  0.0515  306 GLU D C   
17020 O O   . GLU D 306 ? 1.2110 1.4788 2.0384 0.3929  0.2014  0.0569  306 GLU D O   
17021 C CB  . GLU D 306 ? 1.1542 1.3738 1.9384 0.3565  0.2687  0.0338  306 GLU D CB  
17022 C CG  . GLU D 306 ? 1.2437 1.4608 2.0291 0.3375  0.2967  0.0262  306 GLU D CG  
17023 C CD  . GLU D 306 ? 1.4306 1.6013 2.1671 0.3373  0.3294  0.0195  306 GLU D CD  
17024 O OE1 . GLU D 306 ? 1.2703 1.3995 1.9468 0.3387  0.3224  0.0181  306 GLU D OE1 
17025 O OE2 . GLU D 306 ? 1.5794 1.7565 2.3378 0.3354  0.3620  0.0153  306 GLU D OE2 
17026 N N   . GLY D 307 ? 1.1192 1.4357 2.0459 0.4025  0.2416  0.0554  307 GLY D N   
17027 C CA  . GLY D 307 ? 1.3055 1.6353 2.2623 0.4304  0.2321  0.0675  307 GLY D CA  
17028 C C   . GLY D 307 ? 1.1325 1.4989 2.1080 0.4339  0.1891  0.0782  307 GLY D C   
17029 O O   . GLY D 307 ? 1.1984 1.5566 2.1610 0.4520  0.1713  0.0895  307 GLY D O   
17030 N N   . GLU D 308 ? 1.1176 1.5224 2.1204 0.4150  0.1728  0.0743  308 GLU D N   
17031 C CA  . GLU D 308 ? 1.2057 1.6487 2.2248 0.4149  0.1297  0.0818  308 GLU D CA  
17032 C C   . GLU D 308 ? 1.2366 1.7252 2.3235 0.4412  0.1199  0.0967  308 GLU D C   
17033 O O   . GLU D 308 ? 1.2453 1.7597 2.3930 0.4488  0.1442  0.0969  308 GLU D O   
17034 C CB  . GLU D 308 ? 1.2028 1.6772 2.2428 0.3875  0.1178  0.0718  308 GLU D CB  
17035 C CG  . GLU D 308 ? 1.2270 1.6713 2.2006 0.3669  0.0980  0.0639  308 GLU D CG  
17036 C CD  . GLU D 308 ? 1.2859 1.7617 2.2826 0.3406  0.0818  0.0541  308 GLU D CD  
17037 O OE1 . GLU D 308 ? 1.3390 1.8053 2.3388 0.3213  0.1052  0.0442  308 GLU D OE1 
17038 O OE2 . GLU D 308 ? 1.2737 1.7824 2.2837 0.3391  0.0460  0.0562  308 GLU D OE2 
17039 N N   . ARG D 309 ? 1.2761 1.7749 2.3530 0.4549  0.0859  0.1097  309 ARG D N   
17040 C CA  . ARG D 309 ? 1.4147 1.9568 2.5538 0.4824  0.0725  0.1275  309 ARG D CA  
17041 C C   . ARG D 309 ? 1.3563 1.9640 2.5440 0.4737  0.0356  0.1301  309 ARG D C   
17042 O O   . ARG D 309 ? 1.4665 2.0871 2.6364 0.4805  -0.0014 0.1407  309 ARG D O   
17043 C CB  . ARG D 309 ? 1.6430 2.1533 2.7403 0.5051  0.0600  0.1429  309 ARG D CB  
17044 C CG  . ARG D 309 ? 1.7675 2.2110 2.8101 0.5090  0.0936  0.1368  309 ARG D CG  
17045 C CD  . ARG D 309 ? 1.7712 2.2146 2.8442 0.5161  0.1230  0.1323  309 ARG D CD  
17046 N NE  . ARG D 309 ? 1.8336 2.2140 2.8534 0.5175  0.1521  0.1247  309 ARG D NE  
17047 C CZ  . ARG D 309 ? 1.6070 1.9750 2.6404 0.5218  0.1822  0.1181  309 ARG D CZ  
17048 N NH1 . ARG D 309 ? 1.5414 1.9554 2.6396 0.5270  0.1868  0.1200  309 ARG D NH1 
17049 N NH2 . ARG D 309 ? 1.6188 1.9301 2.6027 0.5205  0.2069  0.1093  309 ARG D NH2 
17050 N N   . ILE D 310 ? 1.0431 1.6905 2.2891 0.4586  0.0458  0.1206  310 ILE D N   
17051 C CA  . ILE D 310 ? 0.9548 1.6671 2.2537 0.4474  0.0120  0.1206  310 ILE D CA  
17052 C C   . ILE D 310 ? 1.1008 1.8637 2.4686 0.4774  -0.0038 0.1408  310 ILE D C   
17053 O O   . ILE D 310 ? 1.0581 1.8419 2.4788 0.4854  0.0196  0.1417  310 ILE D O   
17054 C CB  . ILE D 310 ? 0.7698 1.5066 2.1131 0.4210  0.0316  0.1044  310 ILE D CB  
17055 C CG1 . ILE D 310 ? 0.7631 1.4430 2.0355 0.3944  0.0518  0.0873  310 ILE D CG1 
17056 C CG2 . ILE D 310 ? 0.7693 1.5739 2.1695 0.4064  -0.0048 0.1024  310 ILE D CG2 
17057 C CD1 . ILE D 310 ? 0.9796 1.6305 2.1769 0.3791  0.0213  0.0814  310 ILE D CD1 
17058 N N   . ARG D 311 ? 1.2489 2.0220 2.5948 0.4902  -0.0430 0.1547  311 ARG D N   
17059 C CA  . ARG D 311 ? 1.3217 2.1290 2.7029 0.5159  -0.0604 0.1730  311 ARG D CA  
17060 C C   . ARG D 311 ? 1.2947 2.1825 2.7480 0.5084  -0.0951 0.1748  311 ARG D C   
17061 O O   . ARG D 311 ? 1.2485 2.1611 2.7170 0.4832  -0.1109 0.1624  311 ARG D O   
17062 C CB  . ARG D 311 ? 1.4117 2.1875 2.7296 0.5346  -0.0838 0.1889  311 ARG D CB  
17063 C CG  . ARG D 311 ? 1.4227 2.1196 2.6672 0.5393  -0.0539 0.1865  311 ARG D CG  
17064 C CD  . ARG D 311 ? 1.7388 2.4020 2.9846 0.5512  -0.0141 0.1838  311 ARG D CD  
17065 N NE  . ARG D 311 ? 1.8390 2.4365 3.0176 0.5632  -0.0017 0.1885  311 ARG D NE  
17066 C CZ  . ARG D 311 ? 1.8642 2.4114 3.0187 0.5642  0.0368  0.1795  311 ARG D CZ  
17067 N NH1 . ARG D 311 ? 2.0889 2.6443 3.2806 0.5576  0.0679  0.1674  311 ARG D NH1 
17068 N NH2 . ARG D 311 ? 1.5877 2.0767 2.6801 0.5705  0.0436  0.1823  311 ARG D NH2 
17069 N N   . LYS D 312 ? 1.2208 2.1439 2.7105 0.5273  -0.1071 0.1874  312 LYS D N   
17070 C CA  . LYS D 312 ? 1.2259 2.2292 2.7877 0.5212  -0.1396 0.1893  312 LYS D CA  
17071 C C   . LYS D 312 ? 1.1881 2.2245 2.7429 0.5037  -0.1878 0.1871  312 LYS D C   
17072 O O   . LYS D 312 ? 1.1380 2.2167 2.7427 0.4781  -0.1962 0.1727  312 LYS D O   
17073 C CB  . LYS D 312 ? 1.3533 2.3811 2.9368 0.5493  -0.1537 0.2073  312 LYS D CB  
17074 C CG  . LYS D 312 ? 1.4528 2.4291 2.9681 0.5743  -0.1588 0.2230  312 LYS D CG  
17075 C CD  . LYS D 312 ? 1.4839 2.4050 2.9828 0.5903  -0.1132 0.2232  312 LYS D CD  
17076 C CE  . LYS D 312 ? 1.6170 2.4939 3.0614 0.6148  -0.1207 0.2396  312 LYS D CE  
17077 N NZ  . LYS D 312 ? 1.5731 2.4262 3.0346 0.6342  -0.0890 0.2433  312 LYS D NZ  
17078 N N   . ASN D 313 ? 1.2718 2.2888 2.7669 0.5154  -0.2182 0.1996  313 ASN D N   
17079 C CA  . ASN D 313 ? 1.3817 2.4327 2.8676 0.4985  -0.2674 0.1965  313 ASN D CA  
17080 C C   . ASN D 313 ? 1.3693 2.3863 2.8072 0.4593  -0.2554 0.1665  313 ASN D C   
17081 O O   . ASN D 313 ? 1.2336 2.2902 2.6927 0.4328  -0.2806 0.1511  313 ASN D O   
17082 C CB  . ASN D 313 ? 1.4625 2.4876 2.8743 0.5165  -0.2965 0.2142  313 ASN D CB  
17083 C CG  . ASN D 313 ? 1.5273 2.5912 2.9169 0.5015  -0.3507 0.2108  313 ASN D CG  
17084 O OD1 . ASN D 313 ? 1.3693 2.4921 2.8141 0.4820  -0.3733 0.1989  313 ASN D OD1 
17085 N ND2 . ASN D 313 ? 1.6647 2.6960 2.9722 0.5094  -0.3723 0.2205  313 ASN D ND2 
17086 N N   . ASP D 314 ? 1.3331 2.2775 2.7083 0.4552  -0.2178 0.1582  314 ASP D N   
17087 C CA  . ASP D 314 ? 1.3453 2.2520 2.6727 0.4208  -0.2038 0.1323  314 ASP D CA  
17088 C C   . ASP D 314 ? 1.2288 2.1568 2.6209 0.4005  -0.1746 0.1167  314 ASP D C   
17089 O O   . ASP D 314 ? 1.0653 1.9631 2.4246 0.3722  -0.1605 0.0968  314 ASP D O   
17090 C CB  . ASP D 314 ? 1.3969 2.2213 2.6378 0.4248  -0.1747 0.1307  314 ASP D CB  
17091 C CG  . ASP D 314 ? 1.5258 2.3209 2.6914 0.4372  -0.2003 0.1418  314 ASP D CG  
17092 O OD1 . ASP D 314 ? 1.7283 2.5485 2.8748 0.4267  -0.2402 0.1388  314 ASP D OD1 
17093 O OD2 . ASP D 314 ? 1.4593 2.2054 2.5839 0.4563  -0.1797 0.1528  314 ASP D OD2 
17094 N N   . MET D 315 ? 2.1241 2.2014 1.9910 0.1246  -0.0479 -0.3839 315 MET D N   
17095 C CA  . MET D 315 ? 1.9103 1.9638 1.8331 0.1100  -0.0517 -0.3806 315 MET D CA  
17096 C C   . MET D 315 ? 1.7447 1.7898 1.6811 0.0946  -0.0765 -0.4112 315 MET D C   
17097 O O   . MET D 315 ? 1.7905 1.8598 1.6964 0.0939  -0.0962 -0.4254 315 MET D O   
17098 C CB  . MET D 315 ? 1.9270 1.9984 1.8796 0.1028  -0.0490 -0.3433 315 MET D CB  
17099 C CG  . MET D 315 ? 1.9699 2.0594 1.9448 0.0875  -0.0720 -0.3428 315 MET D CG  
17100 S SD  . MET D 315 ? 1.7400 1.8452 1.7526 0.0818  -0.0621 -0.3015 315 MET D SD  
17101 C CE  . MET D 315 ? 1.6492 1.7873 1.6794 0.0709  -0.0909 -0.3027 315 MET D CE  
17102 N N   . LEU D 316 ? 1.5625 1.5744 1.5424 0.0823  -0.0757 -0.4203 316 LEU D N   
17103 C CA  . LEU D 316 ? 1.5427 1.5429 1.5454 0.0642  -0.0969 -0.4509 316 LEU D CA  
17104 C C   . LEU D 316 ? 1.6392 1.6464 1.6972 0.0439  -0.1033 -0.4323 316 LEU D C   
17105 O O   . LEU D 316 ? 1.7888 1.8208 1.8612 0.0306  -0.1265 -0.4436 316 LEU D O   
17106 C CB  . LEU D 316 ? 1.5447 1.4950 1.5563 0.0643  -0.0889 -0.4803 316 LEU D CB  
17107 C CG  . LEU D 316 ? 1.5961 1.5261 1.6380 0.0425  -0.1081 -0.5150 316 LEU D CG  
17108 C CD1 . LEU D 316 ? 1.8718 1.8313 1.8789 0.0401  -0.1349 -0.5484 316 LEU D CD1 
17109 C CD2 . LEU D 316 ? 1.6421 1.5144 1.6975 0.0438  -0.0955 -0.5377 316 LEU D CD2 
17110 N N   . ALA D 317 ? 1.5810 1.5693 1.6698 0.0419  -0.0829 -0.4044 317 ALA D N   
17111 C CA  . ALA D 317 ? 1.5380 1.5321 1.6782 0.0227  -0.0835 -0.3860 317 ALA D CA  
17112 C C   . ALA D 317 ? 1.4153 1.4287 1.5591 0.0293  -0.0675 -0.3457 317 ALA D C   
17113 O O   . ALA D 317 ? 1.4156 1.4194 1.5366 0.0451  -0.0498 -0.3298 317 ALA D O   
17114 C CB  . ALA D 317 ? 1.4884 1.4354 1.6664 0.0083  -0.0737 -0.3934 317 ALA D CB  
17115 N N   . GLU D 318 ? 1.3566 1.3977 1.5333 0.0166  -0.0744 -0.3322 318 GLU D N   
17116 C CA  . GLU D 318 ? 1.1195 1.1796 1.3033 0.0210  -0.0599 -0.2970 318 GLU D CA  
17117 C C   . GLU D 318 ? 1.1275 1.1826 1.3643 0.0014  -0.0517 -0.2854 318 GLU D C   
17118 O O   . GLU D 318 ? 1.1629 1.2229 1.4349 -0.0162 -0.0653 -0.3031 318 GLU D O   
17119 C CB  . GLU D 318 ? 1.0451 1.1486 1.2129 0.0289  -0.0742 -0.2897 318 GLU D CB  
17120 C CG  . GLU D 318 ? 1.0161 1.1371 1.1894 0.0345  -0.0596 -0.2571 318 GLU D CG  
17121 C CD  . GLU D 318 ? 1.2586 1.4130 1.4065 0.0466  -0.0711 -0.2479 318 GLU D CD  
17122 O OE1 . GLU D 318 ? 1.3884 1.5616 1.5307 0.0460  -0.0951 -0.2636 318 GLU D OE1 
17123 O OE2 . GLU D 318 ? 1.2372 1.3976 1.3703 0.0565  -0.0568 -0.2251 318 GLU D OE2 
17124 N N   . PHE D 319 ? 1.0904 1.1377 1.3323 0.0036  -0.0299 -0.2581 319 PHE D N   
17125 C CA  . PHE D 319 ? 1.0557 1.0984 1.3410 -0.0141 -0.0171 -0.2441 319 PHE D CA  
17126 C C   . PHE D 319 ? 0.9982 1.0611 1.2794 -0.0069 -0.0021 -0.2156 319 PHE D C   
17127 O O   . PHE D 319 ? 1.0472 1.1079 1.2932 0.0096  0.0054  -0.2043 319 PHE D O   
17128 C CB  . PHE D 319 ? 0.9531 0.9471 1.2454 -0.0215 -0.0019 -0.2425 319 PHE D CB  
17129 C CG  . PHE D 319 ? 1.1318 1.0929 1.4143 -0.0210 -0.0117 -0.2699 319 PHE D CG  
17130 C CD1 . PHE D 319 ? 1.2511 1.1950 1.4922 -0.0002 -0.0105 -0.2754 319 PHE D CD1 
17131 C CD2 . PHE D 319 ? 1.1651 1.1122 1.4831 -0.0421 -0.0206 -0.2917 319 PHE D CD2 
17132 C CE1 . PHE D 319 ? 1.3166 1.2289 1.5494 0.0015  -0.0179 -0.3034 319 PHE D CE1 
17133 C CE2 . PHE D 319 ? 1.0569 0.9705 1.3664 -0.0422 -0.0292 -0.3201 319 PHE D CE2 
17134 C CZ  . PHE D 319 ? 1.0832 0.9785 1.3491 -0.0195 -0.0274 -0.3260 319 PHE D CZ  
17135 N N   . GLY D 320 ? 0.9103 0.9924 1.2306 -0.0204 0.0035  -0.2061 320 GLY D N   
17136 C CA  . GLY D 320 ? 1.0117 1.1124 1.3310 -0.0149 0.0186  -0.1825 320 GLY D CA  
17137 C C   . GLY D 320 ? 0.9575 1.0926 1.2645 -0.0014 0.0055  -0.1812 320 GLY D C   
17138 O O   . GLY D 320 ? 0.9615 1.1115 1.2681 0.0005  -0.0167 -0.1975 320 GLY D O   
17139 N N   . GLY D 321 ? 0.9704 1.1162 1.2664 0.0073  0.0184  -0.1624 321 GLY D N   
17140 C CA  . GLY D 321 ? 0.9126 1.0853 1.1968 0.0203  0.0087  -0.1573 321 GLY D CA  
17141 C C   . GLY D 321 ? 1.1743 1.3778 1.5010 0.0149  -0.0028 -0.1600 321 GLY D C   
17142 O O   . GLY D 321 ? 1.2123 1.4188 1.5804 -0.0009 -0.0008 -0.1669 321 GLY D O   
17143 N N   . ASN D 322 ? 1.2770 1.5028 1.5961 0.0277  -0.0139 -0.1538 322 ASN D N   
17144 C CA  . ASN D 322 ? 1.4485 1.7070 1.8104 0.0268  -0.0288 -0.1558 322 ASN D CA  
17145 C C   . ASN D 322 ? 1.4670 1.7348 1.8315 0.0231  -0.0567 -0.1767 322 ASN D C   
17146 O O   . ASN D 322 ? 1.5068 1.7978 1.8659 0.0339  -0.0798 -0.1777 322 ASN D O   
17147 C CB  . ASN D 322 ? 1.7398 2.0139 2.0902 0.0438  -0.0329 -0.1402 322 ASN D CB  
17148 C CG  . ASN D 322 ? 2.1139 2.4176 2.5181 0.0444  -0.0369 -0.1363 322 ASN D CG  
17149 O OD1 . ASN D 322 ? 1.9937 2.2998 2.4331 0.0358  -0.0169 -0.1334 322 ASN D OD1 
17150 N ND2 . ASN D 322 ? 2.0552 2.3827 2.4654 0.0558  -0.0625 -0.1362 322 ASN D ND2 
17151 N N   . LYS D 323 ? 1.1972 1.4458 1.5681 0.0086  -0.0552 -0.1926 323 LYS D N   
17152 C CA  . LYS D 323 ? 1.0881 1.3424 1.4606 0.0031  -0.0814 -0.2170 323 LYS D CA  
17153 C C   . LYS D 323 ? 1.0946 1.3448 1.5196 -0.0205 -0.0774 -0.2313 323 LYS D C   
17154 O O   . LYS D 323 ? 1.2035 1.4822 1.6703 -0.0298 -0.0973 -0.2463 323 LYS D O   
17155 C CB  . LYS D 323 ? 0.9987 1.2267 1.3139 0.0109  -0.0864 -0.2282 323 LYS D CB  
17156 C CG  . LYS D 323 ? 1.2651 1.4979 1.5269 0.0320  -0.0891 -0.2155 323 LYS D CG  
17157 C CD  . LYS D 323 ? 1.4354 1.7028 1.6952 0.0414  -0.1163 -0.2157 323 LYS D CD  
17158 C CE  . LYS D 323 ? 1.5016 1.7690 1.7044 0.0608  -0.1168 -0.2009 323 LYS D CE  
17159 N NZ  . LYS D 323 ? 1.5956 1.8938 1.7919 0.0718  -0.1440 -0.1966 323 LYS D NZ  
17160 N N   . THR D 324 ? 0.9944 1.2098 1.4183 -0.0305 -0.0524 -0.2260 324 THR D N   
17161 C CA  . THR D 324 ? 0.9597 1.1641 1.4303 -0.0545 -0.0436 -0.2355 324 THR D CA  
17162 C C   . THR D 324 ? 0.9310 1.1117 1.4052 -0.0609 -0.0099 -0.2141 324 THR D C   
17163 O O   . THR D 324 ? 1.0715 1.2386 1.5059 -0.0466 0.0036  -0.1968 324 THR D O   
17164 C CB  . THR D 324 ? 0.9542 1.1305 1.4141 -0.0633 -0.0564 -0.2603 324 THR D CB  
17165 O OG1 . THR D 324 ? 1.3155 1.4827 1.8279 -0.0892 -0.0488 -0.2697 324 THR D OG1 
17166 C CG2 . THR D 324 ? 0.8771 1.0091 1.2838 -0.0522 -0.0439 -0.2555 324 THR D CG2 
17167 N N   . LYS D 325 ? 0.9095 1.0872 1.4309 -0.0830 0.0038  -0.2153 325 LYS D N   
17168 C CA  . LYS D 325 ? 0.7497 0.9061 1.2717 -0.0905 0.0362  -0.1942 325 LYS D CA  
17169 C C   . LYS D 325 ? 0.9216 1.0247 1.4060 -0.0909 0.0469  -0.1896 325 LYS D C   
17170 O O   . LYS D 325 ? 1.0841 1.1627 1.5794 -0.1028 0.0396  -0.2053 325 LYS D O   
17171 C CB  . LYS D 325 ? 0.9659 1.1401 1.5522 -0.1149 0.0500  -0.1957 325 LYS D CB  
17172 C CG  . LYS D 325 ? 1.0886 1.3179 1.7182 -0.1117 0.0431  -0.1979 325 LYS D CG  
17173 C CD  . LYS D 325 ? 1.2817 1.5345 1.9828 -0.1366 0.0565  -0.2031 325 LYS D CD  
17174 C CE  . LYS D 325 ? 1.4446 1.7546 2.1936 -0.1301 0.0491  -0.2061 325 LYS D CE  
17175 N NZ  . LYS D 325 ? 1.0307 1.3693 1.8551 -0.1542 0.0649  -0.2121 325 LYS D NZ  
17176 N N   . ALA D 326 ? 1.0333 1.1184 1.4756 -0.0773 0.0630  -0.1690 326 ALA D N   
17177 C CA  . ALA D 326 ? 1.0030 1.0401 1.4097 -0.0732 0.0723  -0.1613 326 ALA D CA  
17178 C C   . ALA D 326 ? 1.0285 1.0531 1.4167 -0.0718 0.0981  -0.1346 326 ALA D C   
17179 O O   . ALA D 326 ? 0.9279 0.9804 1.3119 -0.0655 0.1054  -0.1244 326 ALA D O   
17180 C CB  . ALA D 326 ? 0.9070 0.9369 1.2690 -0.0510 0.0565  -0.1689 326 ALA D CB  
17181 N N   . TRP D 327 ? 0.9742 0.9550 1.3496 -0.0771 0.1113  -0.1234 327 TRP D N   
17182 C CA  . TRP D 327 ? 0.9359 0.9029 1.2878 -0.0758 0.1341  -0.0970 327 TRP D CA  
17183 C C   . TRP D 327 ? 1.1777 1.0930 1.4986 -0.0694 0.1390  -0.0845 327 TRP D C   
17184 O O   . TRP D 327 ? 1.3250 1.2109 1.6504 -0.0696 0.1282  -0.0975 327 TRP D O   
17185 C CB  . TRP D 327 ? 1.1130 1.0916 1.5011 -0.0988 0.1556  -0.0884 327 TRP D CB  
17186 C CG  . TRP D 327 ? 1.1991 1.1557 1.6276 -0.1228 0.1596  -0.0961 327 TRP D CG  
17187 C CD1 . TRP D 327 ? 1.1240 1.1049 1.6041 -0.1381 0.1482  -0.1185 327 TRP D CD1 
17188 C CD2 . TRP D 327 ? 1.3086 1.2157 1.7325 -0.1359 0.1772  -0.0804 327 TRP D CD2 
17189 N NE1 . TRP D 327 ? 1.1087 1.0588 1.6194 -0.1618 0.1578  -0.1204 327 TRP D NE1 
17190 C CE2 . TRP D 327 ? 1.1664 1.0679 1.6425 -0.1610 0.1769  -0.0959 327 TRP D CE2 
17191 C CE3 . TRP D 327 ? 1.3689 1.2352 1.7494 -0.1285 0.1920  -0.0539 327 TRP D CE3 
17192 C CZ2 . TRP D 327 ? 1.2042 1.0568 1.6911 -0.1801 0.1935  -0.0853 327 TRP D CZ2 
17193 C CZ3 . TRP D 327 ? 1.2615 1.0787 1.6491 -0.1448 0.2071  -0.0410 327 TRP D CZ3 
17194 C CH2 . TRP D 327 ? 1.2553 1.0638 1.6959 -0.1712 0.2092  -0.0563 327 TRP D CH2 
17195 N N   . GLU D 328 ? 1.0617 0.9660 1.3504 -0.0627 0.1544  -0.0598 328 GLU D N   
17196 C CA  . GLU D 328 ? 1.0548 0.9118 1.3124 -0.0536 0.1589  -0.0425 328 GLU D CA  
17197 C C   . GLU D 328 ? 1.1641 1.0105 1.4047 -0.0619 0.1826  -0.0138 328 GLU D C   
17198 O O   . GLU D 328 ? 1.2133 1.0949 1.4540 -0.0667 0.1930  -0.0096 328 GLU D O   
17199 C CB  . GLU D 328 ? 1.0285 0.8883 1.2500 -0.0255 0.1440  -0.0444 328 GLU D CB  
17200 C CG  . GLU D 328 ? 1.2396 1.1364 1.4364 -0.0141 0.1466  -0.0352 328 GLU D CG  
17201 C CD  . GLU D 328 ? 1.2303 1.1362 1.4003 0.0108  0.1323  -0.0400 328 GLU D CD  
17202 O OE1 . GLU D 328 ? 1.0748 0.9697 1.2488 0.0197  0.1191  -0.0563 328 GLU D OE1 
17203 O OE2 . GLU D 328 ? 1.2115 1.1374 1.3576 0.0205  0.1352  -0.0291 328 GLU D OE2 
17204 N N   . LEU D 329 ? 1.2321 1.0287 1.4565 -0.0633 0.1917  0.0061  329 LEU D N   
17205 C CA  . LEU D 329 ? 1.1494 0.9319 1.3501 -0.0712 0.2146  0.0363  329 LEU D CA  
17206 C C   . LEU D 329 ? 1.2766 1.0004 1.4477 -0.0624 0.2174  0.0611  329 LEU D C   
17207 O O   . LEU D 329 ? 1.4708 1.1556 1.6577 -0.0616 0.2094  0.0537  329 LEU D O   
17208 C CB  . LEU D 329 ? 1.1818 0.9716 1.4222 -0.1023 0.2362  0.0360  329 LEU D CB  
17209 C CG  . LEU D 329 ? 1.3569 1.1259 1.5770 -0.1166 0.2655  0.0672  329 LEU D CG  
17210 C CD1 . LEU D 329 ? 1.2855 1.0936 1.4737 -0.1101 0.2756  0.0760  329 LEU D CD1 
17211 C CD2 . LEU D 329 ? 1.4842 1.2472 1.7538 -0.1492 0.2862  0.0647  329 LEU D CD2 
17212 N N   . VAL D 330 ? 1.3127 1.0292 1.4399 -0.0551 0.2284  0.0902  330 VAL D N   
17213 C CA  . VAL D 330 ? 1.4572 1.1188 1.5511 -0.0448 0.2314  0.1202  330 VAL D CA  
17214 C C   . VAL D 330 ? 1.6682 1.3161 1.7433 -0.0646 0.2601  0.1499  330 VAL D C   
17215 O O   . VAL D 330 ? 1.6211 1.3084 1.6761 -0.0678 0.2701  0.1539  330 VAL D O   
17216 C CB  . VAL D 330 ? 1.5083 1.1763 1.5596 -0.0116 0.2124  0.1288  330 VAL D CB  
17217 C CG1 . VAL D 330 ? 1.5547 1.1710 1.5671 -0.0002 0.2168  0.1659  330 VAL D CG1 
17218 C CG2 . VAL D 330 ? 1.5497 1.2236 1.6203 0.0073  0.1884  0.1014  330 VAL D CG2 
17219 N N   . MET D 331 ? 1.7678 1.3590 1.8494 -0.0788 0.2750  0.1697  331 MET D N   
17220 C CA  . MET D 331 ? 1.7577 1.3303 1.8219 -0.1004 0.3061  0.2003  331 MET D CA  
17221 C C   . MET D 331 ? 1.9130 1.4269 1.9257 -0.0874 0.3107  0.2422  331 MET D C   
17222 O O   . MET D 331 ? 1.9200 1.3903 1.9303 -0.0688 0.2937  0.2468  331 MET D O   
17223 C CB  . MET D 331 ? 1.6324 1.1880 1.7537 -0.1350 0.3257  0.1909  331 MET D CB  
17224 C CG  . MET D 331 ? 1.5806 1.1978 1.7521 -0.1518 0.3270  0.1566  331 MET D CG  
17225 S SD  . MET D 331 ? 1.8877 1.4906 2.1346 -0.1922 0.3457  0.1425  331 MET D SD  
17226 C CE  . MET D 331 ? 1.9779 1.5609 2.2015 -0.2165 0.3899  0.1828  331 MET D CE  
17227 N N   . CYS D 332 ? 1.9678 1.4804 1.9390 -0.0970 0.3346  0.2731  332 CYS D N   
17228 C CA  . CYS D 332 ? 1.9413 1.4003 1.8560 -0.0870 0.3422  0.3188  332 CYS D CA  
17229 C C   . CYS D 332 ? 1.9278 1.3360 1.8639 -0.1195 0.3748  0.3394  332 CYS D C   
17230 O O   . CYS D 332 ? 1.9002 1.3358 1.8585 -0.1491 0.4019  0.3332  332 CYS D O   
17231 C CB  . CYS D 332 ? 2.0105 1.5044 1.8605 -0.0780 0.3480  0.3379  332 CYS D CB  
17232 S SG  . CYS D 332 ? 2.2865 1.7244 2.0544 -0.0556 0.3462  0.3944  332 CYS D SG  
17233 N N   . ALA D 333 ? 2.2126 1.5472 2.1471 -0.1147 0.3734  0.3624  333 ALA D N   
17234 C CA  . ALA D 333 ? 2.3384 1.6172 2.2971 -0.1472 0.4047  0.3825  333 ALA D CA  
17235 C C   . ALA D 333 ? 2.4796 1.6740 2.3942 -0.1336 0.4081  0.4309  333 ALA D C   
17236 O O   . ALA D 333 ? 2.5847 1.7634 2.4644 -0.0966 0.3805  0.4414  333 ALA D O   
17237 C CB  . ALA D 333 ? 2.3951 1.6685 2.4350 -0.1666 0.3997  0.3429  333 ALA D CB  
17238 N N   . ASP D 334 ? 2.5040 1.6445 2.4225 -0.1632 0.4424  0.4614  334 ASP D N   
17239 C CA  . ASP D 334 ? 2.4761 1.5291 2.3536 -0.1529 0.4493  0.5120  334 ASP D CA  
17240 C C   . ASP D 334 ? 2.5410 1.5302 2.4640 -0.1427 0.4304  0.4988  334 ASP D C   
17241 O O   . ASP D 334 ? 2.5057 1.5173 2.4941 -0.1527 0.4188  0.4509  334 ASP D O   
17242 C CB  . ASP D 334 ? 2.5359 1.5530 2.4040 -0.1916 0.4967  0.5491  334 ASP D CB  
17243 C CG  . ASP D 334 ? 2.6752 1.6255 2.4649 -0.1778 0.5085  0.6138  334 ASP D CG  
17244 O OD1 . ASP D 334 ? 2.7265 1.6896 2.4511 -0.1397 0.4837  0.6318  334 ASP D OD1 
17245 O OD2 . ASP D 334 ? 2.4696 1.3556 2.2633 -0.2056 0.5426  0.6472  334 ASP D OD2 
17246 N N   . GLN D 335 ? 2.8110 1.7203 2.6981 -0.1216 0.4269  0.5408  335 GLN D N   
17247 C CA  . GLN D 335 ? 2.8350 1.6757 2.7610 -0.1084 0.4105  0.5307  335 GLN D CA  
17248 C C   . GLN D 335 ? 2.8067 1.6109 2.8094 -0.1507 0.4313  0.5057  335 GLN D C   
17249 O O   . GLN D 335 ? 2.7921 1.5604 2.8401 -0.1435 0.4143  0.4772  335 GLN D O   
17250 C CB  . GLN D 335 ? 2.9421 1.6988 2.8143 -0.0786 0.4069  0.5870  335 GLN D CB  
17251 C CG  . GLN D 335 ? 2.9565 1.7443 2.7647 -0.0289 0.3751  0.6046  335 GLN D CG  
17252 C CD  . GLN D 335 ? 3.1609 1.8672 2.9169 0.0005  0.3712  0.6633  335 GLN D CD  
17253 O OE1 . GLN D 335 ? 3.1180 1.7489 2.8620 -0.0198 0.4002  0.7053  335 GLN D OE1 
17254 N NE2 . GLN D 335 ? 3.3342 2.0532 3.0604 0.0494  0.3352  0.6687  335 GLN D NE2 
17255 N N   . GLY D 336 ? 2.7550 1.5709 2.7733 -0.1943 0.4677  0.5142  336 GLY D N   
17256 C CA  . GLY D 336 ? 2.6823 1.4713 2.7772 -0.2386 0.4890  0.4908  336 GLY D CA  
17257 C C   . GLY D 336 ? 2.6618 1.5208 2.8249 -0.2503 0.4704  0.4242  336 GLY D C   
17258 O O   . GLY D 336 ? 2.6541 1.4830 2.8811 -0.2689 0.4669  0.3924  336 GLY D O   
17259 N N   . GLU D 337 ? 2.5216 1.4729 2.6707 -0.2397 0.4578  0.4024  337 GLU D N   
17260 C CA  . GLU D 337 ? 2.5107 1.5327 2.7179 -0.2478 0.4388  0.3429  337 GLU D CA  
17261 C C   . GLU D 337 ? 2.4781 1.4956 2.6925 -0.2129 0.3983  0.3099  337 GLU D C   
17262 O O   . GLU D 337 ? 2.4011 1.4370 2.6723 -0.2238 0.3838  0.2628  337 GLU D O   
17263 C CB  . GLU D 337 ? 2.5794 1.6960 2.7670 -0.2459 0.4400  0.3337  337 GLU D CB  
17264 C CG  . GLU D 337 ? 2.6150 1.7491 2.8002 -0.2805 0.4816  0.3584  337 GLU D CG  
17265 C CD  . GLU D 337 ? 2.6886 1.9165 2.8679 -0.2812 0.4840  0.3406  337 GLU D CD  
17266 O OE1 . GLU D 337 ? 2.5564 1.8399 2.7550 -0.2643 0.4543  0.3008  337 GLU D OE1 
17267 O OE2 . GLU D 337 ? 2.6982 1.9420 2.8527 -0.2985 0.5170  0.3667  337 GLU D OE2 
17268 N N   . VAL D 338 ? 2.3637 1.3601 2.5205 -0.1708 0.3801  0.3339  338 VAL D N   
17269 C CA  . VAL D 338 ? 2.3091 1.3043 2.4685 -0.1341 0.3444  0.3057  338 VAL D CA  
17270 C C   . VAL D 338 ? 2.4302 1.3299 2.6065 -0.1265 0.3418  0.3121  338 VAL D C   
17271 O O   . VAL D 338 ? 2.4948 1.3260 2.6378 -0.1194 0.3552  0.3598  338 VAL D O   
17272 C CB  . VAL D 338 ? 2.2370 1.2693 2.3330 -0.0919 0.3248  0.3244  338 VAL D CB  
17273 C CG1 . VAL D 338 ? 2.2208 1.2556 2.3221 -0.0538 0.2907  0.2961  338 VAL D CG1 
17274 C CG2 . VAL D 338 ? 2.2187 1.3415 2.3002 -0.1001 0.3279  0.3146  338 VAL D CG2 
17275 N N   . GLU D 339 ? 2.5383 1.4321 2.7641 -0.1269 0.3242  0.2639  339 GLU D N   
17276 C CA  . GLU D 339 ? 2.6755 1.4804 2.9239 -0.1195 0.3204  0.2597  339 GLU D CA  
17277 C C   . GLU D 339 ? 2.6483 1.4578 2.8808 -0.0710 0.2881  0.2397  339 GLU D C   
17278 O O   . GLU D 339 ? 2.6909 1.4813 2.9609 -0.0674 0.2744  0.1974  339 GLU D O   
17279 C CB  . GLU D 339 ? 2.6943 1.4857 3.0141 -0.1598 0.3266  0.2155  339 GLU D CB  
17280 C CG  . GLU D 339 ? 2.8317 1.6224 3.1792 -0.2101 0.3595  0.2309  339 GLU D CG  
17281 C CD  . GLU D 339 ? 2.9068 1.6742 3.3290 -0.2503 0.3649  0.1897  339 GLU D CD  
17282 O OE1 . GLU D 339 ? 2.7584 1.5510 3.2111 -0.2437 0.3390  0.1366  339 GLU D OE1 
17283 O OE2 . GLU D 339 ? 2.8256 1.5510 3.2753 -0.2892 0.3953  0.2100  339 GLU D OE2 
17284 N N   . ASP D 340 ? 2.4273 1.2650 2.6052 -0.0341 0.2764  0.2682  340 ASP D N   
17285 C CA  . ASP D 340 ? 2.3310 1.1829 2.4930 0.0136  0.2475  0.2538  340 ASP D CA  
17286 C C   . ASP D 340 ? 2.3208 1.2185 2.5224 0.0147  0.2284  0.1897  340 ASP D C   
17287 O O   . ASP D 340 ? 2.3845 1.3487 2.6017 -0.0096 0.2291  0.1636  340 ASP D O   
17288 C CB  . ASP D 340 ? 2.4195 1.1785 2.5700 0.0432  0.2454  0.2843  340 ASP D CB  
17289 C CG  . ASP D 340 ? 2.3278 1.1086 2.4475 0.0965  0.2196  0.2906  340 ASP D CG  
17290 O OD1 . ASP D 340 ? 2.1962 1.0157 2.2685 0.1127  0.2152  0.3245  340 ASP D OD1 
17291 O OD2 . ASP D 340 ? 2.3855 1.1472 2.5300 0.1215  0.2040  0.2594  340 ASP D OD2 
17292 N N   . HIS D 341 ? 2.2635 1.1281 2.4798 0.0433  0.2120  0.1646  341 HIS D N   
17293 C CA  . HIS D 341 ? 2.1638 1.0706 2.4100 0.0448  0.1954  0.1050  341 HIS D CA  
17294 C C   . HIS D 341 ? 2.1086 1.0045 2.4017 -0.0013 0.2057  0.0722  341 HIS D C   
17295 O O   . HIS D 341 ? 2.1767 0.9966 2.4992 -0.0144 0.2141  0.0656  341 HIS D O   
17296 C CB  . HIS D 341 ? 2.1364 1.0017 2.3887 0.0838  0.1804  0.0858  341 HIS D CB  
17297 C CG  . HIS D 341 ? 2.0323 0.9490 2.3021 0.0921  0.1632  0.0281  341 HIS D CG  
17298 N ND1 . HIS D 341 ? 2.0968 1.1057 2.3573 0.0851  0.1549  0.0096  341 HIS D ND1 
17299 C CD2 . HIS D 341 ? 1.9962 0.8817 2.2888 0.1072  0.1545  -0.0127 341 HIS D CD2 
17300 C CE1 . HIS D 341 ? 2.0883 1.1191 2.3634 0.0955  0.1414  -0.0391 341 HIS D CE1 
17301 N NE2 . HIS D 341 ? 1.9870 0.9474 2.2808 0.1088  0.1410  -0.0556 341 HIS D NE2 
17302 N N   . LYS D 342 ? 2.0003 0.9724 2.3028 -0.0258 0.2047  0.0524  342 LYS D N   
17303 C CA  . LYS D 342 ? 2.0414 1.0195 2.3913 -0.0696 0.2115  0.0209  342 LYS D CA  
17304 C C   . LYS D 342 ? 1.9806 1.0506 2.3376 -0.0729 0.1942  -0.0194 342 LYS D C   
17305 O O   . LYS D 342 ? 1.9426 1.0774 2.2773 -0.0706 0.1946  -0.0042 342 LYS D O   
17306 C CB  . LYS D 342 ? 2.0193 0.9829 2.3753 -0.1053 0.2390  0.0593  342 LYS D CB  
17307 C CG  . LYS D 342 ? 2.0047 1.0126 2.4066 -0.1505 0.2466  0.0333  342 LYS D CG  
17308 C CD  . LYS D 342 ? 2.0232 0.9688 2.4794 -0.1846 0.2560  0.0120  342 LYS D CD  
17309 C CE  . LYS D 342 ? 1.8780 0.8772 2.3856 -0.2276 0.2595  -0.0176 342 LYS D CE  
17310 N NZ  . LYS D 342 ? 1.8648 0.8894 2.3727 -0.2533 0.2866  0.0200  342 LYS D NZ  
17311 N N   . ILE D 343 ? 2.0459 1.1196 2.4315 -0.0771 0.1788  -0.0706 343 ILE D N   
17312 C CA  . ILE D 343 ? 2.0376 1.1930 2.4277 -0.0789 0.1607  -0.1089 343 ILE D CA  
17313 C C   . ILE D 343 ? 2.0233 1.1885 2.4637 -0.1206 0.1599  -0.1433 343 ILE D C   
17314 O O   . ILE D 343 ? 2.1384 1.2568 2.6067 -0.1306 0.1551  -0.1751 343 ILE D O   
17315 C CB  . ILE D 343 ? 2.1125 1.2764 2.4841 -0.0433 0.1401  -0.1415 343 ILE D CB  
17316 C CG1 . ILE D 343 ? 2.0412 1.1853 2.3733 -0.0009 0.1406  -0.1096 343 ILE D CG1 
17317 C CG2 . ILE D 343 ? 1.9267 1.1765 2.2929 -0.0425 0.1228  -0.1728 343 ILE D CG2 
17318 C CD1 . ILE D 343 ? 1.8609 1.0601 2.1576 0.0119  0.1433  -0.0718 343 ILE D CD1 
17319 N N   . GLU D 344 ? 2.0474 1.2745 2.5019 -0.1442 0.1639  -0.1388 344 GLU D N   
17320 C CA  . GLU D 344 ? 2.0565 1.3058 2.5639 -0.1835 0.1615  -0.1701 344 GLU D CA  
17321 C C   . GLU D 344 ? 1.9378 1.2772 2.4439 -0.1800 0.1410  -0.1965 344 GLU D C   
17322 O O   . GLU D 344 ? 1.8831 1.2755 2.3732 -0.1755 0.1462  -0.1733 344 GLU D O   
17323 C CB  . GLU D 344 ? 2.1131 1.3498 2.6489 -0.2184 0.1892  -0.1375 344 GLU D CB  
17324 C CG  . GLU D 344 ? 2.0552 1.3388 2.6492 -0.2586 0.1886  -0.1635 344 GLU D CG  
17325 C CD  . GLU D 344 ? 2.2164 1.4743 2.8584 -0.2815 0.1748  -0.2115 344 GLU D CD  
17326 O OE1 . GLU D 344 ? 2.2055 1.3834 2.8637 -0.2935 0.1870  -0.2087 344 GLU D OE1 
17327 O OE2 . GLU D 344 ? 2.2222 1.5390 2.8855 -0.2877 0.1511  -0.2520 344 GLU D OE2 
17328 N N   . VAL D 345 ? 1.7577 1.1123 2.2784 -0.1812 0.1178  -0.2449 345 VAL D N   
17329 C CA  . VAL D 345 ? 1.6694 1.1047 2.1865 -0.1767 0.0961  -0.2700 345 VAL D CA  
17330 C C   . VAL D 345 ? 1.7238 1.1963 2.2975 -0.2150 0.0911  -0.2919 345 VAL D C   
17331 O O   . VAL D 345 ? 1.8336 1.3058 2.4336 -0.2288 0.0727  -0.3349 345 VAL D O   
17332 C CB  . VAL D 345 ? 1.8110 1.2486 2.3001 -0.1510 0.0727  -0.3078 345 VAL D CB  
17333 C CG1 . VAL D 345 ? 1.7199 1.2381 2.2017 -0.1471 0.0503  -0.3310 345 VAL D CG1 
17334 C CG2 . VAL D 345 ? 1.7495 1.1588 2.1894 -0.1120 0.0785  -0.2859 345 VAL D CG2 
17335 N N   . ILE D 346 ? 1.7651 1.2719 2.3584 -0.2317 0.1072  -0.2641 346 ILE D N   
17336 C CA  . ILE D 346 ? 1.7337 1.2851 2.3871 -0.2667 0.1045  -0.2815 346 ILE D CA  
17337 C C   . ILE D 346 ? 1.6720 1.2982 2.3215 -0.2552 0.0738  -0.3115 346 ILE D C   
17338 O O   . ILE D 346 ? 1.6426 1.3020 2.2475 -0.2261 0.0681  -0.2983 346 ILE D O   
17339 C CB  . ILE D 346 ? 1.5601 1.1288 2.2326 -0.2843 0.1342  -0.2416 346 ILE D CB  
17340 C CG1 . ILE D 346 ? 1.5235 1.0177 2.2167 -0.3087 0.1637  -0.2191 346 ILE D CG1 
17341 C CG2 . ILE D 346 ? 1.3945 1.0377 2.1218 -0.3081 0.1275  -0.2583 346 ILE D CG2 
17342 C CD1 . ILE D 346 ? 1.4699 0.9519 2.1392 -0.3075 0.1967  -0.1666 346 ILE D CD1 
17343 N N   . GLY D 347 ? 1.6077 1.2587 2.3033 -0.2782 0.0539  -0.3510 347 GLY D N   
17344 C CA  . GLY D 347 ? 1.6256 1.3455 2.3180 -0.2684 0.0221  -0.3797 347 GLY D CA  
17345 C C   . GLY D 347 ? 1.7516 1.4534 2.4071 -0.2499 -0.0032 -0.4159 347 GLY D C   
17346 O O   . GLY D 347 ? 1.8058 1.4408 2.4423 -0.2439 0.0047  -0.4205 347 GLY D O   
17347 N N   . PRO D 348 ? 1.8353 1.5948 2.4782 -0.2394 -0.0334 -0.4423 348 PRO D N   
17348 C CA  . PRO D 348 ? 1.8012 1.5458 2.4037 -0.2221 -0.0560 -0.4787 348 PRO D CA  
17349 C C   . PRO D 348 ? 1.8669 1.5806 2.4027 -0.1854 -0.0454 -0.4607 348 PRO D C   
17350 O O   . PRO D 348 ? 1.8810 1.5974 2.3971 -0.1705 -0.0261 -0.4199 348 PRO D O   
17351 C CB  . PRO D 348 ? 1.7033 1.5238 2.3038 -0.2186 -0.0886 -0.5015 348 PRO D CB  
17352 C CG  . PRO D 348 ? 1.7438 1.6139 2.4015 -0.2399 -0.0853 -0.4848 348 PRO D CG  
17353 C CD  . PRO D 348 ? 1.7834 1.6227 2.4471 -0.2418 -0.0482 -0.4401 348 PRO D CD  
17354 N N   . ASP D 349 ? 1.7155 1.4022 2.2179 -0.1709 -0.0580 -0.4932 349 ASP D N   
17355 C CA  . ASP D 349 ? 1.5865 1.2479 2.0311 -0.1355 -0.0487 -0.4817 349 ASP D CA  
17356 C C   . ASP D 349 ? 1.5865 1.2945 1.9835 -0.1135 -0.0713 -0.5051 349 ASP D C   
17357 O O   . ASP D 349 ? 1.7507 1.5010 2.1575 -0.1259 -0.0960 -0.5328 349 ASP D O   
17358 C CB  . ASP D 349 ? 1.7088 1.2900 2.1544 -0.1339 -0.0378 -0.4976 349 ASP D CB  
17359 C CG  . ASP D 349 ? 1.8064 1.3517 2.2137 -0.1017 -0.0180 -0.4682 349 ASP D CG  
17360 O OD1 . ASP D 349 ? 1.8195 1.3814 2.1811 -0.0729 -0.0242 -0.4780 349 ASP D OD1 
17361 O OD2 . ASP D 349 ? 1.9474 1.4495 2.3706 -0.1055 0.0036  -0.4351 349 ASP D OD2 
17362 N N   . ILE D 350 ? 1.5159 1.2183 1.8616 -0.0812 -0.0629 -0.4930 350 ILE D N   
17363 C CA  . ILE D 350 ? 1.6941 1.4371 1.9896 -0.0594 -0.0787 -0.5106 350 ILE D CA  
17364 C C   . ILE D 350 ? 1.9125 1.6477 2.1981 -0.0655 -0.1004 -0.5652 350 ILE D C   
17365 O O   . ILE D 350 ? 1.9422 1.7203 2.1905 -0.0553 -0.1188 -0.5831 350 ILE D O   
17366 C CB  . ILE D 350 ? 1.6348 1.3688 1.8845 -0.0255 -0.0611 -0.4883 350 ILE D CB  
17367 C CG1 . ILE D 350 ? 1.6957 1.4781 1.8934 -0.0048 -0.0731 -0.4989 350 ILE D CG1 
17368 C CG2 . ILE D 350 ? 1.8273 1.4950 2.0734 -0.0140 -0.0476 -0.5016 350 ILE D CG2 
17369 C CD1 . ILE D 350 ? 1.5667 1.4093 1.7608 -0.0070 -0.0815 -0.4750 350 ILE D CD1 
17370 N N   . ASP D 351 ? 1.8200 1.5002 2.1368 -0.0824 -0.0984 -0.5919 351 ASP D N   
17371 C CA  . ASP D 351 ? 1.8407 1.5108 2.1502 -0.0906 -0.1192 -0.6482 351 ASP D CA  
17372 C C   . ASP D 351 ? 1.8934 1.6214 2.2231 -0.1139 -0.1494 -0.6687 351 ASP D C   
17373 O O   . ASP D 351 ? 1.9508 1.7050 2.2484 -0.1102 -0.1733 -0.7067 351 ASP D O   
17374 C CB  . ASP D 351 ? 2.0631 1.6570 2.4102 -0.1069 -0.1090 -0.6704 351 ASP D CB  
17375 C CG  . ASP D 351 ? 2.1840 1.7176 2.5135 -0.0814 -0.0825 -0.6532 351 ASP D CG  
17376 O OD1 . ASP D 351 ? 2.2343 1.7655 2.5166 -0.0532 -0.0817 -0.6710 351 ASP D OD1 
17377 O OD2 . ASP D 351 ? 2.1862 1.6765 2.5491 -0.0888 -0.0623 -0.6213 351 ASP D OD2 
17378 N N   . THR D 352 ? 1.9868 1.7372 2.3695 -0.1368 -0.1483 -0.6435 352 THR D N   
17379 C CA  . THR D 352 ? 1.9255 1.7357 2.3402 -0.1587 -0.1764 -0.6586 352 THR D CA  
17380 C C   . THR D 352 ? 1.8394 1.7172 2.2046 -0.1369 -0.1972 -0.6534 352 THR D C   
17381 O O   . THR D 352 ? 1.7356 1.6625 2.1113 -0.1480 -0.2278 -0.6758 352 THR D O   
17382 C CB  . THR D 352 ? 1.6046 1.4263 2.0855 -0.1826 -0.1633 -0.6255 352 THR D CB  
17383 O OG1 . THR D 352 ? 1.6267 1.3794 2.1427 -0.1988 -0.1381 -0.6200 352 THR D OG1 
17384 C CG2 . THR D 352 ? 1.5151 1.3920 2.0476 -0.2098 -0.1911 -0.6471 352 THR D CG2 
17385 N N   . ILE D 353 ? 1.8652 1.7456 2.1782 -0.1063 -0.1812 -0.6232 353 ILE D N   
17386 C CA  . ILE D 353 ? 1.7701 1.7070 2.0334 -0.0850 -0.1960 -0.6127 353 ILE D CA  
17387 C C   . ILE D 353 ? 1.8198 1.7681 2.0338 -0.0779 -0.2216 -0.6588 353 ILE D C   
17388 O O   . ILE D 353 ? 1.8406 1.7443 2.0435 -0.0793 -0.2184 -0.6939 353 ILE D O   
17389 C CB  . ILE D 353 ? 1.7192 1.6506 1.9425 -0.0565 -0.1688 -0.5706 353 ILE D CB  
17390 C CG1 . ILE D 353 ? 1.6675 1.6585 1.8722 -0.0445 -0.1768 -0.5397 353 ILE D CG1 
17391 C CG2 . ILE D 353 ? 1.9146 1.8171 2.0796 -0.0329 -0.1600 -0.5895 353 ILE D CG2 
17392 C CD1 . ILE D 353 ? 1.4906 1.4782 1.6841 -0.0273 -0.1482 -0.4926 353 ILE D CD1 
17393 N N   . ASP D 354 ? 1.9460 1.9525 2.1291 -0.0697 -0.2466 -0.6584 354 ASP D N   
17394 C CA  . ASP D 354 ? 2.0523 2.0767 2.1792 -0.0618 -0.2724 -0.6986 354 ASP D CA  
17395 C C   . ASP D 354 ? 2.1069 2.1753 2.1693 -0.0353 -0.2772 -0.6730 354 ASP D C   
17396 O O   . ASP D 354 ? 2.0650 2.1268 2.0605 -0.0161 -0.2729 -0.6868 354 ASP D O   
17397 C CB  . ASP D 354 ? 1.8479 1.9014 2.0112 -0.0875 -0.3102 -0.7367 354 ASP D CB  
17398 C CG  . ASP D 354 ? 2.0718 2.1421 2.1744 -0.0812 -0.3392 -0.7830 354 ASP D CG  
17399 O OD1 . ASP D 354 ? 2.1662 2.1984 2.2198 -0.0683 -0.3252 -0.8061 354 ASP D OD1 
17400 O OD2 . ASP D 354 ? 2.1595 2.2823 2.2633 -0.0883 -0.3760 -0.7966 354 ASP D OD2 
17401 N N   . LYS D 355 ? 2.1405 2.2520 2.2241 -0.0345 -0.2840 -0.6358 355 LYS D N   
17402 C CA  . LYS D 355 ? 2.1715 2.3212 2.2009 -0.0110 -0.2874 -0.6061 355 LYS D CA  
17403 C C   . LYS D 355 ? 2.1513 2.2741 2.1532 0.0086  -0.2489 -0.5727 355 LYS D C   
17404 O O   . LYS D 355 ? 2.0933 2.1815 2.1350 0.0027  -0.2236 -0.5591 355 LYS D O   
17405 C CB  . LYS D 355 ? 2.1558 2.3531 2.2282 -0.0164 -0.3039 -0.5766 355 LYS D CB  
17406 C CG  . LYS D 355 ? 2.1011 2.3439 2.1208 0.0038  -0.3227 -0.5571 355 LYS D CG  
17407 C CD  . LYS D 355 ? 2.0678 2.3442 2.1328 0.0048  -0.3247 -0.5164 355 LYS D CD  
17408 C CE  . LYS D 355 ? 2.0942 2.4040 2.1066 0.0280  -0.3351 -0.4874 355 LYS D CE  
17409 N NZ  . LYS D 355 ? 2.1754 2.5127 2.2372 0.0300  -0.3348 -0.4497 355 LYS D NZ  
17410 N N   . ALA D 356 ? 2.0813 2.2205 2.0158 0.0313  -0.2442 -0.5593 356 ALA D N   
17411 C CA  . ALA D 356 ? 1.9421 2.0614 1.8532 0.0490  -0.2088 -0.5305 356 ALA D CA  
17412 C C   . ALA D 356 ? 2.0517 2.1743 2.0086 0.0473  -0.1904 -0.4843 356 ALA D C   
17413 O O   . ALA D 356 ? 2.1103 2.1997 2.0905 0.0473  -0.1645 -0.4740 356 ALA D O   
17414 C CB  . ALA D 356 ? 1.6994 1.8394 1.5328 0.0705  -0.2066 -0.5249 356 ALA D CB  
17415 N N   . PRO D 357 ? 2.0513 2.2116 2.0231 0.0467  -0.2029 -0.4567 357 PRO D N   
17416 C CA  . PRO D 357 ? 1.9461 2.1067 1.9599 0.0450  -0.1832 -0.4175 357 PRO D CA  
17417 C C   . PRO D 357 ? 1.9969 2.1581 2.0848 0.0229  -0.1895 -0.4188 357 PRO D C   
17418 O O   . PRO D 357 ? 2.0924 2.2814 2.2128 0.0200  -0.1939 -0.3953 357 PRO D O   
17419 C CB  . PRO D 357 ? 2.0058 2.2039 1.9917 0.0587  -0.1909 -0.3884 357 PRO D CB  
17420 C CG  . PRO D 357 ? 2.0731 2.2996 2.0313 0.0590  -0.2267 -0.4124 357 PRO D CG  
17421 C CD  . PRO D 357 ? 2.0766 2.2805 2.0269 0.0494  -0.2353 -0.4588 357 PRO D CD  
17422 N N   . GLY D 358 ? 1.7049 1.8345 1.8204 0.0074  -0.1883 -0.4464 358 GLY D N   
17423 C CA  . GLY D 358 ? 1.6261 1.7528 1.8127 -0.0166 -0.1907 -0.4491 358 GLY D CA  
17424 C C   . GLY D 358 ? 1.6351 1.7464 1.8537 -0.0185 -0.1608 -0.4133 358 GLY D C   
17425 O O   . GLY D 358 ? 1.4724 1.5523 1.6674 -0.0074 -0.1365 -0.4001 358 GLY D O   
17426 N N   . ARG D 359 ? 1.6792 1.8152 1.9519 -0.0322 -0.1632 -0.3990 359 ARG D N   
17427 C CA  . ARG D 359 ? 1.3401 1.4657 1.6407 -0.0348 -0.1345 -0.3651 359 ARG D CA  
17428 C C   . ARG D 359 ? 1.3085 1.4231 1.6751 -0.0618 -0.1283 -0.3708 359 ARG D C   
17429 O O   . ARG D 359 ? 1.3339 1.4756 1.7395 -0.0774 -0.1504 -0.3914 359 ARG D O   
17430 C CB  . ARG D 359 ? 0.9865 1.1530 1.2868 -0.0230 -0.1354 -0.3366 359 ARG D CB  
17431 C CG  . ARG D 359 ? 1.1637 1.3520 1.4077 -0.0015 -0.1512 -0.3356 359 ARG D CG  
17432 C CD  . ARG D 359 ? 1.2804 1.5014 1.5290 0.0095  -0.1499 -0.3054 359 ARG D CD  
17433 N NE  . ARG D 359 ? 1.5331 1.7527 1.7231 0.0308  -0.1426 -0.2888 359 ARG D NE  
17434 C CZ  . ARG D 359 ? 1.6730 1.9049 1.8136 0.0434  -0.1606 -0.2976 359 ARG D CZ  
17435 N NH1 . ARG D 359 ? 1.6383 1.8849 1.7774 0.0380  -0.1895 -0.3252 359 ARG D NH1 
17436 N NH2 . ARG D 359 ? 1.6055 1.8355 1.6973 0.0605  -0.1490 -0.2790 359 ARG D NH2 
17437 N N   . MET D 360 ? 1.2439 1.3217 1.6222 -0.0671 -0.0995 -0.3526 360 MET D N   
17438 C CA  . MET D 360 ? 1.3174 1.3792 1.7541 -0.0935 -0.0875 -0.3527 360 MET D CA  
17439 C C   . MET D 360 ? 1.2305 1.2797 1.6757 -0.0934 -0.0556 -0.3159 360 MET D C   
17440 O O   . MET D 360 ? 1.2566 1.2947 1.6586 -0.0733 -0.0430 -0.2960 360 MET D O   
17441 C CB  . MET D 360 ? 1.2797 1.2889 1.7176 -0.1051 -0.0857 -0.3773 360 MET D CB  
17442 C CG  . MET D 360 ? 1.5400 1.5595 1.9819 -0.1134 -0.1163 -0.4198 360 MET D CG  
17443 S SD  . MET D 360 ? 2.2842 2.3569 2.7991 -0.1409 -0.1396 -0.4378 360 MET D SD  
17444 C CE  . MET D 360 ? 1.7343 1.7618 2.3118 -0.1744 -0.1145 -0.4374 360 MET D CE  
17445 N N   . PRO D 361 ? 1.2296 1.2811 1.7284 -0.1159 -0.0413 -0.3070 361 PRO D N   
17446 C CA  . PRO D 361 ? 1.1390 1.1773 1.6369 -0.1152 -0.0103 -0.2730 361 PRO D CA  
17447 C C   . PRO D 361 ? 1.2467 1.2248 1.7138 -0.1112 0.0083  -0.2625 361 PRO D C   
17448 O O   . PRO D 361 ? 1.3993 1.3423 1.8611 -0.1145 0.0004  -0.2831 361 PRO D O   
17449 C CB  . PRO D 361 ? 1.1197 1.1761 1.6839 -0.1427 0.0002  -0.2711 361 PRO D CB  
17450 C CG  . PRO D 361 ? 1.2896 1.3769 1.8936 -0.1559 -0.0282 -0.3034 361 PRO D CG  
17451 C CD  . PRO D 361 ? 1.4321 1.4992 1.9943 -0.1440 -0.0509 -0.3279 361 PRO D CD  
17452 N N   . LEU D 362 ? 1.1630 1.1287 1.6104 -0.1033 0.0319  -0.2315 362 LEU D N   
17453 C CA  . LEU D 362 ? 1.1131 1.0245 1.5310 -0.0962 0.0475  -0.2180 362 LEU D CA  
17454 C C   . LEU D 362 ? 1.1152 1.0156 1.5305 -0.0998 0.0749  -0.1841 362 LEU D C   
17455 O O   . LEU D 362 ? 1.0587 0.9875 1.4557 -0.0879 0.0811  -0.1672 362 LEU D O   
17456 C CB  . LEU D 362 ? 0.9859 0.8928 1.3511 -0.0672 0.0381  -0.2209 362 LEU D CB  
17457 C CG  . LEU D 362 ? 1.0741 0.9304 1.4090 -0.0537 0.0500  -0.2089 362 LEU D CG  
17458 C CD1 . LEU D 362 ? 1.1058 0.9128 1.4559 -0.0639 0.0468  -0.2289 362 LEU D CD1 
17459 C CD2 . LEU D 362 ? 1.0226 0.8898 1.3125 -0.0251 0.0435  -0.2095 362 LEU D CD2 
17460 N N   . GLY D 363 ? 1.0809 0.9381 1.5121 -0.1163 0.0914  -0.1747 363 GLY D N   
17461 C CA  . GLY D 363 ? 1.1502 0.9908 1.5731 -0.1211 0.1183  -0.1415 363 GLY D CA  
17462 C C   . GLY D 363 ? 1.3415 1.1220 1.7313 -0.1101 0.1263  -0.1262 363 GLY D C   
17463 O O   . GLY D 363 ? 1.4277 1.1676 1.8269 -0.1143 0.1197  -0.1415 363 GLY D O   
17464 N N   . MET D 364 ? 1.3541 1.1283 1.7055 -0.0947 0.1390  -0.0973 364 MET D N   
17465 C CA  . MET D 364 ? 1.3871 1.1073 1.7061 -0.0801 0.1445  -0.0792 364 MET D CA  
17466 C C   . MET D 364 ? 1.3186 1.0170 1.6243 -0.0884 0.1693  -0.0429 364 MET D C   
17467 O O   . MET D 364 ? 1.2418 0.9611 1.5148 -0.0751 0.1749  -0.0234 364 MET D O   
17468 C CB  . MET D 364 ? 1.2794 1.0129 1.5572 -0.0474 0.1311  -0.0801 364 MET D CB  
17469 C CG  . MET D 364 ? 1.1831 0.9308 1.4652 -0.0374 0.1093  -0.1138 364 MET D CG  
17470 S SD  . MET D 364 ? 1.3800 1.1316 1.6185 -0.0004 0.0983  -0.1151 364 MET D SD  
17471 C CE  . MET D 364 ? 1.5341 1.3559 1.7650 0.0042  0.0906  -0.1217 364 MET D CE  
17472 N N   . LEU D 365 ? 1.3437 0.9992 1.6730 -0.1110 0.1846  -0.0342 365 LEU D N   
17473 C CA  . LEU D 365 ? 1.4691 1.0986 1.7821 -0.1208 0.2106  0.0026  365 LEU D CA  
17474 C C   . LEU D 365 ? 1.5273 1.0912 1.8077 -0.1041 0.2116  0.0245  365 LEU D C   
17475 O O   . LEU D 365 ? 1.5384 1.0568 1.8372 -0.1062 0.2051  0.0116  365 LEU D O   
17476 C CB  . LEU D 365 ? 1.4408 1.0641 1.8017 -0.1581 0.2308  0.0026  365 LEU D CB  
17477 C CG  . LEU D 365 ? 1.3257 0.9383 1.6711 -0.1727 0.2628  0.0396  365 LEU D CG  
17478 C CD1 . LEU D 365 ? 1.3895 1.0373 1.7869 -0.2059 0.2813  0.0313  365 LEU D CD1 
17479 C CD2 . LEU D 365 ? 1.5329 1.0687 1.8601 -0.1761 0.2768  0.0682  365 LEU D CD2 
17480 N N   . ILE D 366 ? 1.6423 1.2014 1.8752 -0.0866 0.2186  0.0566  366 ILE D N   
17481 C CA  . ILE D 366 ? 1.7365 1.2379 1.9355 -0.0658 0.2174  0.0818  366 ILE D CA  
17482 C C   . ILE D 366 ? 1.7446 1.2192 1.9134 -0.0744 0.2415  0.1252  366 ILE D C   
17483 O O   . ILE D 366 ? 1.7179 1.2329 1.8608 -0.0742 0.2496  0.1385  366 ILE D O   
17484 C CB  . ILE D 366 ? 1.5295 1.0567 1.6947 -0.0290 0.1957  0.0773  366 ILE D CB  
17485 C CG1 . ILE D 366 ? 1.3886 0.9355 1.5787 -0.0198 0.1742  0.0356  366 ILE D CG1 
17486 C CG2 . ILE D 366 ? 1.6496 1.1261 1.7792 -0.0039 0.1935  0.1071  366 ILE D CG2 
17487 C CD1 . ILE D 366 ? 1.1295 0.7480 1.3227 -0.0180 0.1644  0.0140  366 ILE D CD1 
17488 N N   . LYS D 367 ? 1.6906 1.0951 1.8600 -0.0818 0.2536  0.1474  367 LYS D N   
17489 C CA  . LYS D 367 ? 1.7909 1.1633 1.9260 -0.0899 0.2778  0.1926  367 LYS D CA  
17490 C C   . LYS D 367 ? 1.8865 1.2179 1.9711 -0.0553 0.2668  0.2234  367 LYS D C   
17491 O O   . LYS D 367 ? 1.8897 1.1901 1.9824 -0.0337 0.2482  0.2119  367 LYS D O   
17492 C CB  . LYS D 367 ? 2.0346 1.3554 2.2053 -0.1249 0.3027  0.2017  367 LYS D CB  
17493 C CG  . LYS D 367 ? 1.9050 1.2708 2.1328 -0.1594 0.3124  0.1707  367 LYS D CG  
17494 C CD  . LYS D 367 ? 2.0200 1.3400 2.2862 -0.1974 0.3400  0.1814  367 LYS D CD  
17495 C CE  . LYS D 367 ? 1.7616 1.1311 2.0933 -0.2298 0.3452  0.1465  367 LYS D CE  
17496 N NZ  . LYS D 367 ? 2.0560 1.3823 2.4340 -0.2689 0.3711  0.1528  367 LYS D NZ  
17497 N N   . VAL D 368 ? 1.9838 1.3173 2.0168 -0.0498 0.2783  0.2615  368 VAL D N   
17498 C CA  . VAL D 368 ? 2.1767 1.4762 2.1584 -0.0151 0.2655  0.2947  368 VAL D CA  
17499 C C   . VAL D 368 ? 2.3363 1.5787 2.2827 -0.0268 0.2905  0.3448  368 VAL D C   
17500 O O   . VAL D 368 ? 2.3723 1.6277 2.3193 -0.0583 0.3180  0.3536  368 VAL D O   
17501 C CB  . VAL D 368 ? 2.1541 1.5183 2.0971 0.0104  0.2473  0.2922  368 VAL D CB  
17502 C CG1 . VAL D 368 ? 2.2567 1.5950 2.1590 0.0493  0.2272  0.3184  368 VAL D CG1 
17503 C CG2 . VAL D 368 ? 1.9987 1.4249 1.9763 0.0136  0.2300  0.2449  368 VAL D CG2 
17504 N N   . SER D 369 ? 2.3529 1.5347 2.2699 -0.0013 0.2821  0.3772  369 SER D N   
17505 C CA  . SER D 369 ? 2.3576 1.4772 2.2344 -0.0089 0.3046  0.4304  369 SER D CA  
17506 C C   . SER D 369 ? 2.4886 1.6347 2.2906 0.0099  0.3016  0.4662  369 SER D C   
17507 O O   . SER D 369 ? 2.3676 1.5615 2.1487 0.0398  0.2745  0.4552  369 SER D O   
17508 C CB  . SER D 369 ? 2.4003 1.4311 2.2844 0.0088  0.2982  0.4506  369 SER D CB  
17509 O OG  . SER D 369 ? 2.3752 1.3567 2.3165 -0.0211 0.3149  0.4345  369 SER D OG  
17510 N N   . GLY D 370 ? 2.7440 1.8585 2.5063 -0.0089 0.3302  0.5086  370 GLY D N   
17511 C CA  . GLY D 370 ? 2.9007 2.0355 2.5849 0.0044  0.3312  0.5451  370 GLY D CA  
17512 C C   . GLY D 370 ? 3.1055 2.2011 2.7401 0.0468  0.3057  0.5825  370 GLY D C   
17513 O O   . GLY D 370 ? 3.1400 2.1553 2.7606 0.0508  0.3144  0.6224  370 GLY D O   
17514 N N   . THR D 371 ? 3.1905 2.3447 2.8024 0.0784  0.2736  0.5685  371 THR D N   
17515 C CA  . THR D 371 ? 3.2419 2.3761 2.8095 0.1232  0.2433  0.6000  371 THR D CA  
17516 C C   . THR D 371 ? 3.2033 2.4218 2.7319 0.1410  0.2206  0.5874  371 THR D C   
17517 O O   . THR D 371 ? 3.1559 2.4230 2.7195 0.1596  0.1942  0.5491  371 THR D O   
17518 C CB  . THR D 371 ? 3.2096 2.3107 2.8287 0.1511  0.2189  0.5826  371 THR D CB  
17519 O OG1 . THR D 371 ? 3.2393 2.2586 2.8928 0.1319  0.2412  0.5931  371 THR D OG1 
17520 C CG2 . THR D 371 ? 3.2458 2.3341 2.8290 0.1997  0.1863  0.6114  371 THR D CG2 
17521 N N   . ASN D 372 ? 2.8852 2.1212 2.3447 0.1337  0.2319  0.6163  372 ASN D N   
17522 C CA  . ASN D 372 ? 2.8426 2.1574 2.2614 0.1460  0.2127  0.6029  372 ASN D CA  
17523 C C   . ASN D 372 ? 2.8124 2.1998 2.2867 0.1327  0.2089  0.5426  372 ASN D C   
17524 O O   . ASN D 372 ? 2.6706 2.1172 2.1439 0.1528  0.1811  0.5190  372 ASN D O   
17525 C CB  . ASN D 372 ? 2.6855 2.0053 2.0675 0.1927  0.1720  0.6247  372 ASN D CB  
17526 C CG  . ASN D 372 ? 2.7104 2.0247 2.1510 0.2233  0.1423  0.6033  372 ASN D CG  
17527 O OD1 . ASN D 372 ? 2.6613 2.0358 2.1439 0.2285  0.1256  0.5578  372 ASN D OD1 
17528 N ND2 . ASN D 372 ? 2.7195 1.9603 2.1640 0.2449  0.1362  0.6358  372 ASN D ND2 
17529 N N   . MET D 373 ? 2.7610 2.1403 2.2846 0.0984  0.2372  0.5203  373 MET D N   
17530 C CA  . MET D 373 ? 2.5436 1.9861 2.1207 0.0839  0.2361  0.4662  373 MET D CA  
17531 C C   . MET D 373 ? 2.4117 1.8783 1.9843 0.0460  0.2715  0.4591  373 MET D C   
17532 O O   . MET D 373 ? 2.3931 1.8124 1.9613 0.0228  0.3019  0.4844  373 MET D O   
17533 C CB  . MET D 373 ? 2.5031 1.9216 2.1548 0.0814  0.2318  0.4380  373 MET D CB  
17534 C CG  . MET D 373 ? 2.3828 1.8618 2.0866 0.0683  0.2292  0.3862  373 MET D CG  
17535 S SD  . MET D 373 ? 2.5204 1.9759 2.2999 0.0726  0.2167  0.3521  373 MET D SD  
17536 C CE  . MET D 373 ? 2.2484 1.7792 2.0717 0.0527  0.2188  0.3006  373 MET D CE  
17537 N N   . GLN D 374 ? 2.4317 1.9681 2.0076 0.0401  0.2690  0.4262  374 GLN D N   
17538 C CA  . GLN D 374 ? 2.4492 2.0168 2.0247 0.0080  0.3011  0.4143  374 GLN D CA  
17539 C C   . GLN D 374 ? 2.2306 1.8391 1.8787 -0.0075 0.3031  0.3660  374 GLN D C   
17540 O O   . GLN D 374 ? 2.1894 1.8119 1.8755 0.0086  0.2771  0.3405  374 GLN D O   
17541 C CB  . GLN D 374 ? 2.3600 1.9747 1.8702 0.0148  0.2980  0.4172  374 GLN D CB  
17542 C CG  . GLN D 374 ? 2.5633 2.1448 1.9926 0.0309  0.2939  0.4655  374 GLN D CG  
17543 C CD  . GLN D 374 ? 2.6387 2.2699 2.0028 0.0345  0.2913  0.4634  374 GLN D CD  
17544 O OE1 . GLN D 374 ? 2.2721 1.9613 1.6488 0.0419  0.2725  0.4273  374 GLN D OE1 
17545 N NE2 . GLN D 374 ? 2.8130 2.4218 2.1042 0.0286  0.3108  0.5016  374 GLN D NE2 
17546 N N   . LYS D 375 ? 2.0527 1.6822 1.7191 -0.0377 0.3344  0.3539  375 LYS D N   
17547 C CA  . LYS D 375 ? 1.9245 1.5954 1.6580 -0.0516 0.3361  0.3106  375 LYS D CA  
17548 C C   . LYS D 375 ? 1.8847 1.6132 1.6160 -0.0331 0.3105  0.2802  375 LYS D C   
17549 O O   . LYS D 375 ? 1.9357 1.6906 1.7200 -0.0335 0.2993  0.2470  375 LYS D O   
17550 C CB  . LYS D 375 ? 1.8830 1.5727 1.6328 -0.0841 0.3745  0.3052  375 LYS D CB  
17551 C CG  . LYS D 375 ? 1.8415 1.4858 1.6273 -0.1098 0.4006  0.3202  375 LYS D CG  
17552 C CD  . LYS D 375 ? 1.9032 1.5791 1.7198 -0.1411 0.4368  0.3074  375 LYS D CD  
17553 C CE  . LYS D 375 ? 1.9262 1.5601 1.7782 -0.1698 0.4659  0.3241  375 LYS D CE  
17554 N NZ  . LYS D 375 ? 1.9405 1.6114 1.8260 -0.1997 0.5028  0.3115  375 LYS D NZ  
17555 N N   . ASP D 376 ? 1.8932 1.6407 1.5631 -0.0178 0.3010  0.2916  376 ASP D N   
17556 C CA  . ASP D 376 ? 1.8202 1.6205 1.4873 -0.0021 0.2775  0.2638  376 ASP D CA  
17557 C C   . ASP D 376 ? 1.7798 1.5779 1.4736 0.0229  0.2430  0.2533  376 ASP D C   
17558 O O   . ASP D 376 ? 1.8059 1.6473 1.5134 0.0328  0.2250  0.2263  376 ASP D O   
17559 C CB  . ASP D 376 ? 1.9422 1.7617 1.5356 0.0069  0.2744  0.2786  376 ASP D CB  
17560 C CG  . ASP D 376 ? 2.0770 1.9068 1.6392 -0.0164 0.3097  0.2834  376 ASP D CG  
17561 O OD1 . ASP D 376 ? 2.0437 1.8807 1.6516 -0.0392 0.3352  0.2670  376 ASP D OD1 
17562 O OD2 . ASP D 376 ? 2.1192 1.9521 1.6114 -0.0114 0.3117  0.3029  376 ASP D OD2 
17563 N N   . PHE D 377 ? 1.8156 1.5630 1.5181 0.0327  0.2356  0.2736  377 PHE D N   
17564 C CA  . PHE D 377 ? 1.7556 1.4985 1.4852 0.0571  0.2063  0.2628  377 PHE D CA  
17565 C C   . PHE D 377 ? 1.7652 1.5060 1.5616 0.0464  0.2080  0.2334  377 PHE D C   
17566 O O   . PHE D 377 ? 1.6897 1.4434 1.5121 0.0634  0.1864  0.2138  377 PHE D O   
17567 C CB  . PHE D 377 ? 1.8130 1.5001 1.5180 0.0770  0.1959  0.2982  377 PHE D CB  
17568 C CG  . PHE D 377 ? 2.0060 1.6900 1.6423 0.0936  0.1875  0.3317  377 PHE D CG  
17569 C CD1 . PHE D 377 ? 2.0371 1.7743 1.6370 0.0948  0.1821  0.3232  377 PHE D CD1 
17570 C CD2 . PHE D 377 ? 2.2612 1.8886 1.8689 0.1092  0.1831  0.3711  377 PHE D CD2 
17571 C CE1 . PHE D 377 ? 2.1651 1.9023 1.6985 0.1103  0.1714  0.3525  377 PHE D CE1 
17572 C CE2 . PHE D 377 ? 2.3376 1.9635 1.8788 0.1264  0.1724  0.4040  377 PHE D CE2 
17573 C CZ  . PHE D 377 ? 2.2380 1.9209 1.7411 0.1268  0.1658  0.3939  377 PHE D CZ  
17574 N N   . GLU D 378 ? 1.6723 1.4003 1.4965 0.0186  0.2331  0.2295  378 GLU D N   
17575 C CA  . GLU D 378 ? 1.6085 1.3367 1.4946 0.0075  0.2326  0.2013  378 GLU D CA  
17576 C C   . GLU D 378 ? 1.5891 1.3709 1.5007 0.0154  0.2157  0.1658  378 GLU D C   
17577 O O   . GLU D 378 ? 1.5467 1.3250 1.4922 0.0231  0.2011  0.1468  378 GLU D O   
17578 C CB  . GLU D 378 ? 1.7971 1.5194 1.7126 -0.0252 0.2617  0.1991  378 GLU D CB  
17579 C CG  . GLU D 378 ? 1.9529 1.6213 1.8518 -0.0399 0.2844  0.2329  378 GLU D CG  
17580 C CD  . GLU D 378 ? 1.9928 1.6731 1.9119 -0.0725 0.3173  0.2318  378 GLU D CD  
17581 O OE1 . GLU D 378 ? 1.9732 1.7019 1.8844 -0.0781 0.3266  0.2198  378 GLU D OE1 
17582 O OE2 . GLU D 378 ? 1.9174 1.5591 1.8636 -0.0928 0.3348  0.2416  378 GLU D OE2 
17583 N N   . PRO D 379 ? 1.6308 1.4603 1.5269 0.0133  0.2184  0.1556  379 PRO D N   
17584 C CA  . PRO D 379 ? 1.5160 1.3902 1.4380 0.0198  0.2039  0.1243  379 PRO D CA  
17585 C C   . PRO D 379 ? 1.4243 1.3028 1.3447 0.0459  0.1772  0.1181  379 PRO D C   
17586 O O   . PRO D 379 ? 1.5586 1.4572 1.5109 0.0494  0.1670  0.0938  379 PRO D O   
17587 C CB  . PRO D 379 ? 1.5561 1.4707 1.4534 0.0142  0.2127  0.1196  379 PRO D CB  
17588 C CG  . PRO D 379 ? 1.5420 1.4376 1.4132 -0.0020 0.2376  0.1415  379 PRO D CG  
17589 C CD  . PRO D 379 ? 1.7317 1.5750 1.5854 0.0045  0.2356  0.1705  379 PRO D CD  
17590 N N   . VAL D 380 ? 1.2610 1.1225 1.1452 0.0642  0.1666  0.1403  380 VAL D N   
17591 C CA  . VAL D 380 ? 1.5229 1.3921 1.4094 0.0913  0.1416  0.1350  380 VAL D CA  
17592 C C   . VAL D 380 ? 1.4867 1.3199 1.4068 0.0969  0.1369  0.1284  380 VAL D C   
17593 O O   . VAL D 380 ? 1.3687 1.2210 1.3128 0.1091  0.1234  0.1066  380 VAL D O   
17594 C CB  . VAL D 380 ? 1.3706 1.2312 1.2119 0.1109  0.1302  0.1624  380 VAL D CB  
17595 C CG1 . VAL D 380 ? 1.5377 1.4101 1.3883 0.1399  0.1050  0.1567  380 VAL D CG1 
17596 C CG2 . VAL D 380 ? 1.3226 1.2177 1.1251 0.1037  0.1347  0.1668  380 VAL D CG2 
17597 N N   . LEU D 381 ? 1.4700 1.2527 1.3916 0.0871  0.1491  0.1456  381 LEU D N   
17598 C CA  . LEU D 381 ? 1.5028 1.2443 1.4550 0.0907  0.1456  0.1386  381 LEU D CA  
17599 C C   . LEU D 381 ? 1.4313 1.1944 1.4253 0.0754  0.1475  0.1052  381 LEU D C   
17600 O O   . LEU D 381 ? 1.4797 1.2403 1.4961 0.0865  0.1354  0.0851  381 LEU D O   
17601 C CB  . LEU D 381 ? 1.6341 1.3151 1.5808 0.0775  0.1619  0.1644  381 LEU D CB  
17602 C CG  . LEU D 381 ? 1.7707 1.4077 1.6804 0.0965  0.1580  0.2013  381 LEU D CG  
17603 C CD1 . LEU D 381 ? 1.8524 1.4810 1.7678 0.1296  0.1348  0.1967  381 LEU D CD1 
17604 C CD2 . LEU D 381 ? 1.8186 1.4782 1.6784 0.0977  0.1616  0.2255  381 LEU D CD2 
17605 N N   . GLU D 382 ? 1.3694 1.1548 1.3731 0.0510  0.1626  0.0992  382 GLU D N   
17606 C CA  . GLU D 382 ? 1.2898 1.0983 1.3327 0.0367  0.1632  0.0704  382 GLU D CA  
17607 C C   . GLU D 382 ? 1.3331 1.1861 1.3806 0.0509  0.1477  0.0481  382 GLU D C   
17608 O O   . GLU D 382 ? 1.3172 1.1765 1.3906 0.0513  0.1395  0.0255  382 GLU D O   
17609 C CB  . GLU D 382 ? 1.3995 1.2261 1.4529 0.0106  0.1832  0.0714  382 GLU D CB  
17610 C CG  . GLU D 382 ? 1.3606 1.1960 1.4609 -0.0074 0.1853  0.0481  382 GLU D CG  
17611 C CD  . GLU D 382 ? 1.4219 1.2930 1.5394 -0.0267 0.2007  0.0425  382 GLU D CD  
17612 O OE1 . GLU D 382 ? 1.3966 1.2641 1.4966 -0.0373 0.2202  0.0611  382 GLU D OE1 
17613 O OE2 . GLU D 382 ? 1.4385 1.3412 1.5861 -0.0301 0.1937  0.0197  382 GLU D OE2 
17614 N N   . ARG D 383 ? 1.2602 1.1440 1.2818 0.0615  0.1439  0.0540  383 ARG D N   
17615 C CA  . ARG D 383 ? 1.1481 1.0737 1.1751 0.0727  0.1319  0.0348  383 ARG D CA  
17616 C C   . ARG D 383 ? 1.1628 1.0794 1.1964 0.0941  0.1165  0.0259  383 ARG D C   
17617 O O   . ARG D 383 ? 1.2369 1.1757 1.2874 0.0975  0.1101  0.0048  383 ARG D O   
17618 C CB  . ARG D 383 ? 1.1180 1.0763 1.1177 0.0775  0.1314  0.0422  383 ARG D CB  
17619 C CG  . ARG D 383 ? 1.0942 1.0942 1.1001 0.0882  0.1200  0.0245  383 ARG D CG  
17620 C CD  . ARG D 383 ? 1.0087 1.0342 1.0386 0.0751  0.1253  0.0048  383 ARG D CD  
17621 N NE  . ARG D 383 ? 0.9655 0.9776 1.0208 0.0740  0.1217  -0.0083 383 ARG D NE  
17622 C CZ  . ARG D 383 ? 1.0431 1.0744 1.1190 0.0667  0.1219  -0.0246 383 ARG D CZ  
17623 N NH1 . ARG D 383 ? 1.1160 1.1774 1.1939 0.0601  0.1268  -0.0293 383 ARG D NH1 
17624 N NH2 . ARG D 383 ? 1.0172 1.0364 1.1108 0.0665  0.1163  -0.0366 383 ARG D NH2 
17625 N N   . ARG D 384 ? 1.1941 1.0777 1.2140 0.1095  0.1114  0.0424  384 ARG D N   
17626 C CA  . ARG D 384 ? 1.2545 1.1288 1.2829 0.1326  0.0983  0.0334  384 ARG D CA  
17627 C C   . ARG D 384 ? 1.2095 1.0596 1.2642 0.1285  0.0981  0.0130  384 ARG D C   
17628 O O   . ARG D 384 ? 1.1670 1.0168 1.2300 0.1467  0.0892  -0.0012 384 ARG D O   
17629 C CB  . ARG D 384 ? 1.3630 1.2053 1.3725 0.1527  0.0921  0.0579  384 ARG D CB  
17630 C CG  . ARG D 384 ? 1.2873 1.1655 1.2783 0.1725  0.0800  0.0665  384 ARG D CG  
17631 C CD  . ARG D 384 ? 1.1407 1.0574 1.1515 0.1883  0.0697  0.0429  384 ARG D CD  
17632 N NE  . ARG D 384 ? 1.5554 1.4903 1.5595 0.2147  0.0552  0.0522  384 ARG D NE  
17633 C CZ  . ARG D 384 ? 1.6417 1.6201 1.6623 0.2287  0.0469  0.0353  384 ARG D CZ  
17634 N NH1 . ARG D 384 ? 1.4889 1.4933 1.5280 0.2188  0.0528  0.0105  384 ARG D NH1 
17635 N NH2 . ARG D 384 ? 1.7004 1.6979 1.7199 0.2527  0.0326  0.0441  384 ARG D NH2 
17636 N N   . LEU D 385 ? 1.2168 1.0500 1.2854 0.1051  0.1077  0.0092  385 LEU D N   
17637 C CA  . LEU D 385 ? 1.1306 0.9434 1.2244 0.0989  0.1051  -0.0136 385 LEU D CA  
17638 C C   . LEU D 385 ? 1.1511 1.0018 1.2512 0.1081  0.0957  -0.0395 385 LEU D C   
17639 O O   . LEU D 385 ? 1.1818 1.0161 1.2905 0.1179  0.0892  -0.0578 385 LEU D O   
17640 C CB  . LEU D 385 ? 1.1883 0.9948 1.3007 0.0699  0.1155  -0.0155 385 LEU D CB  
17641 C CG  . LEU D 385 ? 1.2889 1.0550 1.3970 0.0569  0.1292  0.0099  385 LEU D CG  
17642 C CD1 . LEU D 385 ? 1.1815 0.9521 1.3152 0.0271  0.1412  0.0050  385 LEU D CD1 
17643 C CD2 . LEU D 385 ? 1.1587 0.8669 1.2687 0.0669  0.1268  0.0153  385 LEU D CD2 
17644 N N   . HIS D 386 ? 1.0637 0.9609 1.1585 0.1050  0.0962  -0.0412 386 HIS D N   
17645 C CA  . HIS D 386 ? 0.9562 0.8893 1.0543 0.1114  0.0899  -0.0615 386 HIS D CA  
17646 C C   . HIS D 386 ? 1.1693 1.1044 1.2610 0.1366  0.0834  -0.0670 386 HIS D C   
17647 O O   . HIS D 386 ? 1.2300 1.1662 1.3268 0.1443  0.0793  -0.0874 386 HIS D O   
17648 C CB  . HIS D 386 ? 0.8115 0.7880 0.9046 0.1044  0.0936  -0.0574 386 HIS D CB  
17649 C CG  . HIS D 386 ? 0.9406 0.9518 1.0340 0.1116  0.0894  -0.0726 386 HIS D CG  
17650 N ND1 . HIS D 386 ? 1.0916 1.1239 1.1927 0.0998  0.0899  -0.0822 386 HIS D ND1 
17651 C CD2 . HIS D 386 ? 1.1771 1.2049 1.2648 0.1294  0.0857  -0.0781 386 HIS D CD2 
17652 C CE1 . HIS D 386 ? 1.1975 1.2551 1.2931 0.1098  0.0876  -0.0910 386 HIS D CE1 
17653 N NE2 . HIS D 386 ? 1.2589 1.3163 1.3479 0.1267  0.0861  -0.0899 386 HIS D NE2 
17654 N N   . TYR D 387 ? 1.1511 1.0889 1.2317 0.1500  0.0822  -0.0495 387 TYR D N   
17655 C CA  . TYR D 387 ? 1.0614 1.0063 1.1416 0.1759  0.0757  -0.0525 387 TYR D CA  
17656 C C   . TYR D 387 ? 1.1506 1.0515 1.2396 0.1884  0.0732  -0.0617 387 TYR D C   
17657 O O   . TYR D 387 ? 1.2446 1.1548 1.3405 0.2041  0.0707  -0.0804 387 TYR D O   
17658 C CB  . TYR D 387 ? 0.9953 0.9491 1.0627 0.1865  0.0720  -0.0293 387 TYR D CB  
17659 C CG  . TYR D 387 ? 1.3450 1.3037 1.4168 0.2155  0.0632  -0.0282 387 TYR D CG  
17660 C CD1 . TYR D 387 ? 1.4162 1.4233 1.4969 0.2267  0.0600  -0.0402 387 TYR D CD1 
17661 C CD2 . TYR D 387 ? 1.5949 1.5114 1.6639 0.2318  0.0585  -0.0127 387 TYR D CD2 
17662 C CE1 . TYR D 387 ? 1.4862 1.5044 1.5774 0.2541  0.0520  -0.0399 387 TYR D CE1 
17663 C CE2 . TYR D 387 ? 1.4998 1.4233 1.5772 0.2614  0.0491  -0.0108 387 TYR D CE2 
17664 C CZ  . TYR D 387 ? 1.4416 1.4188 1.5317 0.2727  0.0456  -0.0254 387 TYR D CZ  
17665 O OH  . TYR D 387 ? 1.5041 1.4944 1.6091 0.3026  0.0366  -0.0252 387 TYR D OH  
17666 N N   . PHE D 388 ? 1.1900 1.0421 1.2794 0.1806  0.0757  -0.0498 388 PHE D N   
17667 C CA  . PHE D 388 ? 1.1943 0.9965 1.2940 0.1908  0.0743  -0.0586 388 PHE D CA  
17668 C C   . PHE D 388 ? 1.2180 1.0166 1.3296 0.1814  0.0741  -0.0905 388 PHE D C   
17669 O O   . PHE D 388 ? 1.2950 1.0803 1.4125 0.1982  0.0714  -0.1101 388 PHE D O   
17670 C CB  . PHE D 388 ? 1.2303 0.9779 1.3285 0.1805  0.0793  -0.0360 388 PHE D CB  
17671 C CG  . PHE D 388 ? 1.3517 1.0936 1.4309 0.1896  0.0790  -0.0016 388 PHE D CG  
17672 C CD1 . PHE D 388 ? 1.4691 1.2328 1.5412 0.2173  0.0698  0.0062  388 PHE D CD1 
17673 C CD2 . PHE D 388 ? 1.2739 0.9898 1.3425 0.1707  0.0879  0.0228  388 PHE D CD2 
17674 C CE1 . PHE D 388 ? 1.5072 1.2682 1.5586 0.2265  0.0662  0.0376  388 PHE D CE1 
17675 C CE2 . PHE D 388 ? 1.4497 1.1602 1.4934 0.1796  0.0873  0.0552  388 PHE D CE2 
17676 C CZ  . PHE D 388 ? 1.4773 1.2104 1.5111 0.2079  0.0748  0.0623  388 PHE D CZ  
17677 N N   . LEU D 389 ? 1.1216 0.9347 1.2362 0.1562  0.0764  -0.0967 389 LEU D N   
17678 C CA  . LEU D 389 ? 1.1231 0.9332 1.2470 0.1462  0.0730  -0.1267 389 LEU D CA  
17679 C C   . LEU D 389 ? 1.0565 0.9081 1.1711 0.1593  0.0696  -0.1467 389 LEU D C   
17680 O O   . LEU D 389 ? 1.1268 0.9683 1.2420 0.1640  0.0662  -0.1733 389 LEU D O   
17681 C CB  . LEU D 389 ? 1.2147 1.0345 1.3480 0.1174  0.0746  -0.1253 389 LEU D CB  
17682 C CG  . LEU D 389 ? 1.2063 0.9835 1.3531 0.0998  0.0811  -0.1106 389 LEU D CG  
17683 C CD1 . LEU D 389 ? 1.1915 0.9851 1.3558 0.0721  0.0824  -0.1160 389 LEU D CD1 
17684 C CD2 . LEU D 389 ? 1.2068 0.9286 1.3637 0.1051  0.0795  -0.1223 389 LEU D CD2 
17685 N N   . ASN D 390 ? 1.0295 0.9253 1.1352 0.1639  0.0715  -0.1355 390 ASN D N   
17686 C CA  . ASN D 390 ? 1.1719 1.1083 1.2690 0.1727  0.0714  -0.1519 390 ASN D CA  
17687 C C   . ASN D 390 ? 1.1935 1.1234 1.2910 0.1987  0.0724  -0.1646 390 ASN D C   
17688 O O   . ASN D 390 ? 1.1947 1.1465 1.2848 0.2057  0.0743  -0.1850 390 ASN D O   
17689 C CB  . ASN D 390 ? 1.0152 0.9967 1.1069 0.1685  0.0747  -0.1371 390 ASN D CB  
17690 C CG  . ASN D 390 ? 1.0056 1.0113 1.0933 0.1513  0.0742  -0.1433 390 ASN D CG  
17691 O OD1 . ASN D 390 ? 1.1827 1.1876 1.2652 0.1496  0.0705  -0.1626 390 ASN D OD1 
17692 N ND2 . ASN D 390 ? 1.1363 1.1631 1.2253 0.1396  0.0771  -0.1276 390 ASN D ND2 
17693 N N   . TYR D 391 ? 1.0408 0.9423 1.1463 0.2135  0.0718  -0.1523 391 TYR D N   
17694 C CA  . TYR D 391 ? 1.1256 1.0196 1.2379 0.2414  0.0725  -0.1635 391 TYR D CA  
17695 C C   . TYR D 391 ? 1.1765 1.0386 1.2899 0.2445  0.0730  -0.1944 391 TYR D C   
17696 O O   . TYR D 391 ? 1.1657 1.0325 1.2822 0.2662  0.0765  -0.2129 391 TYR D O   
17697 C CB  . TYR D 391 ? 1.1845 1.0473 1.3053 0.2570  0.0693  -0.1402 391 TYR D CB  
17698 C CG  . TYR D 391 ? 1.1880 1.0902 1.3111 0.2735  0.0669  -0.1223 391 TYR D CG  
17699 C CD1 . TYR D 391 ? 1.3068 1.2570 1.4225 0.2603  0.0676  -0.1128 391 TYR D CD1 
17700 C CD2 . TYR D 391 ? 1.0987 0.9895 1.2340 0.3024  0.0626  -0.1153 391 TYR D CD2 
17701 C CE1 . TYR D 391 ? 1.2412 1.2293 1.3613 0.2731  0.0639  -0.0994 391 TYR D CE1 
17702 C CE2 . TYR D 391 ? 1.0975 1.0293 1.2381 0.3174  0.0573  -0.1002 391 TYR D CE2 
17703 C CZ  . TYR D 391 ? 1.1949 1.1761 1.3276 0.3013  0.0578  -0.0933 391 TYR D CZ  
17704 O OH  . TYR D 391 ? 1.2806 1.3046 1.4206 0.3139  0.0512  -0.0816 391 TYR D OH  
17705 N N   . ILE D 392 ? 1.1921 1.0240 1.3049 0.2229  0.0698  -0.2021 392 ILE D N   
17706 C CA  . ILE D 392 ? 1.1249 0.9266 1.2380 0.2223  0.0681  -0.2345 392 ILE D CA  
17707 C C   . ILE D 392 ? 1.2148 1.0592 1.3097 0.2229  0.0692  -0.2587 392 ILE D C   
17708 O O   . ILE D 392 ? 1.3486 1.2304 1.4329 0.2079  0.0677  -0.2508 392 ILE D O   
17709 C CB  . ILE D 392 ? 1.1406 0.9074 1.2616 0.1949  0.0630  -0.2370 392 ILE D CB  
17710 C CG1 . ILE D 392 ? 1.1995 0.9203 1.3358 0.1906  0.0651  -0.2102 392 ILE D CG1 
17711 C CG2 . ILE D 392 ? 1.2309 0.9715 1.3517 0.1921  0.0589  -0.2755 392 ILE D CG2 
17712 C CD1 . ILE D 392 ? 1.1564 0.8642 1.3029 0.1577  0.0638  -0.2019 392 ILE D CD1 
17713 N N   . GLU D 393 ? 1.2227 1.0598 1.3124 0.2402  0.0727  -0.2878 393 GLU D N   
17714 C CA  . GLU D 393 ? 1.3988 1.2735 1.4649 0.2411  0.0756  -0.3112 393 GLU D CA  
17715 C C   . GLU D 393 ? 1.6076 1.4714 1.6613 0.2181  0.0650  -0.3300 393 GLU D C   
17716 O O   . GLU D 393 ? 1.7309 1.5495 1.7964 0.2105  0.0589  -0.3438 393 GLU D O   
17717 C CB  . GLU D 393 ? 1.5693 1.4398 1.6331 0.2677  0.0850  -0.3385 393 GLU D CB  
17718 C CG  . GLU D 393 ? 1.5263 1.4231 1.5593 0.2672  0.0890  -0.3689 393 GLU D CG  
17719 C CD  . GLU D 393 ? 1.5470 1.4479 1.5773 0.2941  0.1027  -0.3955 393 GLU D CD  
17720 O OE1 . GLU D 393 ? 1.5007 1.3638 1.5546 0.3122  0.1050  -0.4032 393 GLU D OE1 
17721 O OE2 . GLU D 393 ? 1.5463 1.4874 1.5511 0.2977  0.1124  -0.4082 393 GLU D OE2 
17722 N N   . GLY D 394 ? 1.7193 1.6241 1.7512 0.2070  0.0623  -0.3299 394 GLY D N   
17723 C CA  . GLY D 394 ? 1.6807 1.5850 1.7004 0.1870  0.0491  -0.3464 394 GLY D CA  
17724 C C   . GLY D 394 ? 1.5584 1.4710 1.5929 0.1644  0.0406  -0.3220 394 GLY D C   
17725 O O   . GLY D 394 ? 1.5773 1.5126 1.5997 0.1508  0.0304  -0.3266 394 GLY D O   
17726 N N   . VAL D 395 ? 1.2901 1.1857 1.3499 0.1610  0.0447  -0.2958 395 VAL D N   
17727 C CA  . VAL D 395 ? 1.3321 1.2364 1.4074 0.1399  0.0400  -0.2737 395 VAL D CA  
17728 C C   . VAL D 395 ? 1.3627 1.3026 1.4345 0.1435  0.0479  -0.2444 395 VAL D C   
17729 O O   . VAL D 395 ? 1.4244 1.3739 1.4907 0.1611  0.0569  -0.2371 395 VAL D O   
17730 C CB  . VAL D 395 ? 1.4349 1.2943 1.5388 0.1271  0.0395  -0.2661 395 VAL D CB  
17731 C CG1 . VAL D 395 ? 1.3637 1.1788 1.4738 0.1277  0.0350  -0.2961 395 VAL D CG1 
17732 C CG2 . VAL D 395 ? 1.2647 1.1117 1.3769 0.1365  0.0502  -0.2361 395 VAL D CG2 
17733 N N   . MET D 396 ? 1.2238 1.1842 1.3022 0.1265  0.0441  -0.2302 396 MET D N   
17734 C CA  . MET D 396 ? 1.1240 1.1162 1.2009 0.1269  0.0515  -0.2049 396 MET D CA  
17735 C C   . MET D 396 ? 1.0529 1.0424 1.1507 0.1082  0.0510  -0.1872 396 MET D C   
17736 O O   . MET D 396 ? 1.1148 1.1119 1.2211 0.0939  0.0425  -0.1941 396 MET D O   
17737 C CB  . MET D 396 ? 1.1469 1.1770 1.2032 0.1289  0.0502  -0.2083 396 MET D CB  
17738 C CG  . MET D 396 ? 1.4032 1.4619 1.4621 0.1251  0.0569  -0.1848 396 MET D CG  
17739 S SD  . MET D 396 ? 1.1163 1.2039 1.1655 0.1154  0.0492  -0.1836 396 MET D SD  
17740 C CE  . MET D 396 ? 1.0496 1.1248 1.1294 0.0962  0.0398  -0.1804 396 MET D CE  
17741 N N   . HIS D 397 ? 0.9076 0.8889 1.0132 0.1089  0.0596  -0.1662 397 HIS D N   
17742 C CA  . HIS D 397 ? 0.9143 0.8935 1.0366 0.0921  0.0634  -0.1489 397 HIS D CA  
17743 C C   . HIS D 397 ? 1.0081 1.0217 1.1249 0.0921  0.0696  -0.1325 397 HIS D C   
17744 O O   . HIS D 397 ? 0.9775 1.0017 1.0826 0.1049  0.0743  -0.1248 397 HIS D O   
17745 C CB  . HIS D 397 ? 0.9596 0.9012 1.0887 0.0920  0.0696  -0.1358 397 HIS D CB  
17746 C CG  . HIS D 397 ? 0.9797 0.9200 1.1208 0.0753  0.0776  -0.1163 397 HIS D CG  
17747 N ND1 . HIS D 397 ? 0.8522 0.8173 0.9848 0.0761  0.0847  -0.0987 397 HIS D ND1 
17748 C CD2 . HIS D 397 ? 1.0950 1.0130 1.2562 0.0569  0.0809  -0.1139 397 HIS D CD2 
17749 C CE1 . HIS D 397 ? 0.9500 0.9073 1.0944 0.0597  0.0929  -0.0864 397 HIS D CE1 
17750 N NE2 . HIS D 397 ? 1.1309 1.0608 1.2940 0.0473  0.0918  -0.0939 397 HIS D NE2 
17751 N N   . VAL D 398 ? 1.0384 1.0703 1.1671 0.0779  0.0693  -0.1287 398 VAL D N   
17752 C CA  . VAL D 398 ? 0.8879 0.9485 1.0146 0.0764  0.0759  -0.1157 398 VAL D CA  
17753 C C   . VAL D 398 ? 0.8396 0.9014 0.9869 0.0600  0.0815  -0.1066 398 VAL D C   
17754 O O   . VAL D 398 ? 0.9327 0.9928 1.0991 0.0493  0.0759  -0.1145 398 VAL D O   
17755 C CB  . VAL D 398 ? 0.6915 0.7791 0.8098 0.0805  0.0705  -0.1230 398 VAL D CB  
17756 C CG1 . VAL D 398 ? 0.7977 0.9094 0.9178 0.0777  0.0783  -0.1102 398 VAL D CG1 
17757 C CG2 . VAL D 398 ? 1.1160 1.2052 1.2130 0.0958  0.0686  -0.1331 398 VAL D CG2 
17758 N N   . GLY D 399 ? 0.7545 0.8218 0.8989 0.0579  0.0923  -0.0918 399 GLY D N   
17759 C CA  . GLY D 399 ? 0.8186 0.8897 0.9803 0.0431  0.1016  -0.0837 399 GLY D CA  
17760 C C   . GLY D 399 ? 0.8997 0.9469 1.0573 0.0375  0.1118  -0.0707 399 GLY D C   
17761 O O   . GLY D 399 ? 0.9735 1.0014 1.1131 0.0475  0.1103  -0.0652 399 GLY D O   
17762 N N   . GLN D 400 ? 0.9096 0.9585 1.0839 0.0223  0.1230  -0.0647 400 GLN D N   
17763 C CA  . GLN D 400 ? 0.8962 0.9226 1.0632 0.0145  0.1361  -0.0493 400 GLN D CA  
17764 C C   . GLN D 400 ? 0.9294 0.9572 1.1263 -0.0056 0.1483  -0.0487 400 GLN D C   
17765 O O   . GLN D 400 ? 0.9468 1.0002 1.1702 -0.0112 0.1465  -0.0593 400 GLN D O   
17766 C CB  . GLN D 400 ? 0.7833 0.8209 0.9226 0.0206  0.1440  -0.0370 400 GLN D CB  
17767 C CG  . GLN D 400 ? 0.8863 0.9573 1.0333 0.0167  0.1501  -0.0423 400 GLN D CG  
17768 C CD  . GLN D 400 ? 0.8905 0.9823 1.0364 0.0281  0.1385  -0.0529 400 GLN D CD  
17769 O OE1 . GLN D 400 ? 0.8917 0.9807 1.0206 0.0409  0.1294  -0.0536 400 GLN D OE1 
17770 N NE2 . GLN D 400 ? 0.9022 1.0154 1.0677 0.0242  0.1398  -0.0605 400 GLN D NE2 
17771 N N   . ARG D 401 ? 0.8099 0.8110 1.0038 -0.0159 0.1612  -0.0351 401 ARG D N   
17772 C CA  . ARG D 401 ? 0.9596 0.9617 1.1833 -0.0371 0.1773  -0.0328 401 ARG D CA  
17773 C C   . ARG D 401 ? 0.9693 0.9843 1.2390 -0.0471 0.1674  -0.0521 401 ARG D C   
17774 O O   . ARG D 401 ? 0.9960 0.9905 1.2712 -0.0458 0.1540  -0.0612 401 ARG D O   
17775 C CB  . ARG D 401 ? 1.0044 1.0328 1.2232 -0.0419 0.1951  -0.0263 401 ARG D CB  
17776 C CG  . ARG D 401 ? 1.1040 1.1189 1.2771 -0.0366 0.2058  -0.0072 401 ARG D CG  
17777 C CD  . ARG D 401 ? 0.9302 0.9703 1.0991 -0.0437 0.2250  -0.0053 401 ARG D CD  
17778 N NE  . ARG D 401 ? 0.9857 1.0132 1.1075 -0.0413 0.2358  0.0130  401 ARG D NE  
17779 C CZ  . ARG D 401 ? 1.0824 1.1275 1.1879 -0.0467 0.2537  0.0152  401 ARG D CZ  
17780 N NH1 . ARG D 401 ? 0.8678 0.9423 1.0049 -0.0541 0.2643  0.0001  401 ARG D NH1 
17781 N NH2 . ARG D 401 ? 1.2351 1.2687 1.2918 -0.0436 0.2604  0.0318  401 ARG D NH2 
17782 N N   . ASN D 402 ? 0.9490 0.9980 1.2523 -0.0561 0.1729  -0.0598 402 ASN D N   
17783 C CA  . ASN D 402 ? 0.8828 0.9490 1.2315 -0.0645 0.1604  -0.0778 402 ASN D CA  
17784 C C   . ASN D 402 ? 0.8119 0.9055 1.1606 -0.0491 0.1392  -0.0910 402 ASN D C   
17785 O O   . ASN D 402 ? 0.9201 1.0393 1.3058 -0.0534 0.1288  -0.1038 402 ASN D O   
17786 C CB  . ASN D 402 ? 0.8813 0.9691 1.2755 -0.0837 0.1780  -0.0783 402 ASN D CB  
17787 C CG  . ASN D 402 ? 1.0132 1.1379 1.4168 -0.0782 0.1865  -0.0787 402 ASN D CG  
17788 O OD1 . ASN D 402 ? 1.2873 1.4437 1.7251 -0.0751 0.1748  -0.0914 402 ASN D OD1 
17789 N ND2 . ASN D 402 ? 1.2080 1.3285 1.5810 -0.0759 0.2060  -0.0653 402 ASN D ND2 
17790 N N   . LEU D 403 ? 0.8306 0.9198 1.1389 -0.0313 0.1327  -0.0871 403 LEU D N   
17791 C CA  . LEU D 403 ? 0.9371 1.0476 1.2391 -0.0170 0.1155  -0.0961 403 LEU D CA  
17792 C C   . LEU D 403 ? 0.9121 1.0031 1.1789 -0.0034 0.1033  -0.0991 403 LEU D C   
17793 O O   . LEU D 403 ? 0.7438 0.8434 0.9851 0.0104  0.1002  -0.0967 403 LEU D O   
17794 C CB  . LEU D 403 ? 0.7759 0.9084 1.0706 -0.0100 0.1248  -0.0891 403 LEU D CB  
17795 C CG  . LEU D 403 ? 0.6628 0.8195 0.9958 -0.0194 0.1363  -0.0899 403 LEU D CG  
17796 C CD1 . LEU D 403 ? 0.8248 0.9920 1.1441 -0.0139 0.1505  -0.0833 403 LEU D CD1 
17797 C CD2 . LEU D 403 ? 0.8664 1.0482 1.2335 -0.0167 0.1190  -0.1011 403 LEU D CD2 
17798 N N   . THR D 404 ? 0.8803 0.9447 1.1490 -0.0080 0.0976  -0.1057 404 THR D N   
17799 C CA  . THR D 404 ? 0.7212 0.7647 0.9615 0.0053  0.0875  -0.1116 404 THR D CA  
17800 C C   . THR D 404 ? 0.7809 0.8383 1.0228 0.0106  0.0678  -0.1308 404 THR D C   
17801 O O   . THR D 404 ? 0.9500 1.0291 1.2184 0.0025  0.0595  -0.1390 404 THR D O   
17802 C CB  . THR D 404 ? 0.8411 0.8436 1.0818 -0.0009 0.0925  -0.1094 404 THR D CB  
17803 O OG1 . THR D 404 ? 0.8788 0.8757 1.1548 -0.0188 0.0887  -0.1214 404 THR D OG1 
17804 C CG2 . THR D 404 ? 1.0484 1.0352 1.2770 -0.0035 0.1110  -0.0869 404 THR D CG2 
17805 N N   . TRP D 405 ? 0.9309 0.9783 1.1440 0.0252  0.0602  -0.1382 405 TRP D N   
17806 C CA  . TRP D 405 ? 0.9236 0.9827 1.1276 0.0318  0.0428  -0.1564 405 TRP D CA  
17807 C C   . TRP D 405 ? 0.9784 1.0115 1.1585 0.0430  0.0396  -0.1682 405 TRP D C   
17808 O O   . TRP D 405 ? 1.0783 1.1117 1.2334 0.0578  0.0456  -0.1621 405 TRP D O   
17809 C CB  . TRP D 405 ? 0.7626 0.8532 0.9508 0.0422  0.0406  -0.1500 405 TRP D CB  
17810 C CG  . TRP D 405 ? 0.9519 1.0568 1.1249 0.0490  0.0234  -0.1647 405 TRP D CG  
17811 C CD1 . TRP D 405 ? 0.9808 1.0848 1.1627 0.0431  0.0064  -0.1841 405 TRP D CD1 
17812 C CD2 . TRP D 405 ? 1.1745 1.2979 1.3191 0.0621  0.0216  -0.1604 405 TRP D CD2 
17813 N NE1 . TRP D 405 ? 0.9860 1.1071 1.1412 0.0533  -0.0069 -0.1922 405 TRP D NE1 
17814 C CE2 . TRP D 405 ? 1.1095 1.2415 1.2412 0.0649  0.0035  -0.1762 405 TRP D CE2 
17815 C CE3 . TRP D 405 ? 1.2453 1.3786 1.3738 0.0704  0.0340  -0.1451 405 TRP D CE3 
17816 C CZ2 . TRP D 405 ? 1.3938 1.5421 1.4931 0.0765  -0.0009 -0.1740 405 TRP D CZ2 
17817 C CZ3 . TRP D 405 ? 1.3852 1.5336 1.4872 0.0804  0.0307  -0.1438 405 TRP D CZ3 
17818 C CH2 . TRP D 405 ? 1.6444 1.7993 1.7301 0.0837  0.0142  -0.1566 405 TRP D CH2 
17819 N N   . VAL D 406 ? 0.8929 0.9041 1.0844 0.0355  0.0309  -0.1867 406 VAL D N   
17820 C CA  . VAL D 406 ? 1.0822 1.0646 1.2553 0.0462  0.0283  -0.2020 406 VAL D CA  
17821 C C   . VAL D 406 ? 1.2582 1.2549 1.4150 0.0509  0.0113  -0.2275 406 VAL D C   
17822 O O   . VAL D 406 ? 1.0741 1.0890 1.2460 0.0395  -0.0024 -0.2379 406 VAL D O   
17823 C CB  . VAL D 406 ? 1.0029 0.9423 1.1985 0.0343  0.0326  -0.2054 406 VAL D CB  
17824 C CG1 . VAL D 406 ? 1.1950 1.1000 1.3755 0.0465  0.0298  -0.2240 406 VAL D CG1 
17825 C CG2 . VAL D 406 ? 0.8118 0.7375 1.0147 0.0307  0.0498  -0.1771 406 VAL D CG2 
17826 N N   . ARG D 407 ? 1.3125 1.3041 1.4382 0.0686  0.0123  -0.2376 407 ARG D N   
17827 C CA  . ARG D 407 ? 1.1778 1.1818 1.2783 0.0750  -0.0009 -0.2618 407 ARG D CA  
17828 C C   . ARG D 407 ? 1.3283 1.3001 1.4150 0.0860  0.0018  -0.2835 407 ARG D C   
17829 O O   . ARG D 407 ? 1.5236 1.4895 1.5971 0.1022  0.0148  -0.2757 407 ARG D O   
17830 C CB  . ARG D 407 ? 1.1582 1.1970 1.2287 0.0877  0.0022  -0.2504 407 ARG D CB  
17831 C CG  . ARG D 407 ? 1.3449 1.4143 1.4269 0.0795  -0.0024 -0.2324 407 ARG D CG  
17832 C CD  . ARG D 407 ? 1.5045 1.6024 1.5547 0.0910  -0.0008 -0.2230 407 ARG D CD  
17833 N NE  . ARG D 407 ? 1.4857 1.6058 1.5270 0.0880  -0.0192 -0.2286 407 ARG D NE  
17834 C CZ  . ARG D 407 ? 1.6274 1.7701 1.6398 0.0965  -0.0206 -0.2188 407 ARG D CZ  
17835 N NH1 . ARG D 407 ? 1.8555 2.0027 1.8482 0.1062  -0.0028 -0.2047 407 ARG D NH1 
17836 N NH2 . ARG D 407 ? 1.5952 1.7567 1.5992 0.0952  -0.0402 -0.2222 407 ARG D NH2 
17837 N N   . ILE D 408 ? 1.3665 1.3184 1.4591 0.0777  -0.0106 -0.3123 408 ILE D N   
17838 C CA  . ILE D 408 ? 1.3277 1.2449 1.4092 0.0884  -0.0077 -0.3371 408 ILE D CA  
17839 C C   . ILE D 408 ? 1.3098 1.2471 1.3508 0.1000  -0.0154 -0.3630 408 ILE D C   
17840 O O   . ILE D 408 ? 1.4966 1.4607 1.5261 0.0917  -0.0316 -0.3727 408 ILE D O   
17841 C CB  . ILE D 408 ? 1.3337 1.2089 1.4477 0.0713  -0.0136 -0.3545 408 ILE D CB  
17842 C CG1 . ILE D 408 ? 1.3747 1.2271 1.5219 0.0619  -0.0009 -0.3245 408 ILE D CG1 
17843 C CG2 . ILE D 408 ? 1.3030 1.1390 1.4057 0.0831  -0.0116 -0.3849 408 ILE D CG2 
17844 C CD1 . ILE D 408 ? 1.2791 1.0947 1.4630 0.0397  -0.0041 -0.3349 408 ILE D CD1 
17845 N N   . GLY D 409 ? 1.5203 1.4463 1.5396 0.1200  -0.0035 -0.3732 409 GLY D N   
17846 C CA  . GLY D 409 ? 1.7215 1.6653 1.6983 0.1328  -0.0051 -0.3976 409 GLY D CA  
17847 C C   . GLY D 409 ? 1.7412 1.6603 1.7093 0.1289  -0.0172 -0.4404 409 GLY D C   
17848 O O   . GLY D 409 ? 1.7412 1.6191 1.7396 0.1206  -0.0194 -0.4531 409 GLY D O   
17849 N N   . LYS D 410 ? 1.6971 1.6396 1.6214 0.1344  -0.0244 -0.4633 410 LYS D N   
17850 C CA  . LYS D 410 ? 1.8048 1.7281 1.7132 0.1310  -0.0373 -0.5091 410 LYS D CA  
17851 C C   . LYS D 410 ? 1.8670 1.7499 1.7779 0.1475  -0.0205 -0.5322 410 LYS D C   
17852 O O   . LYS D 410 ? 1.7996 1.6444 1.7242 0.1409  -0.0277 -0.5652 410 LYS D O   
17853 C CB  . LYS D 410 ? 1.8783 1.8394 1.7299 0.1354  -0.0477 -0.5256 410 LYS D CB  
17854 C CG  . LYS D 410 ? 1.7533 1.7548 1.5994 0.1234  -0.0659 -0.5020 410 LYS D CG  
17855 C CD  . LYS D 410 ? 1.7103 1.7446 1.4950 0.1286  -0.0789 -0.5181 410 LYS D CD  
17856 C CE  . LYS D 410 ? 1.5322 1.5685 1.3125 0.1135  -0.1105 -0.5524 410 LYS D CE  
17857 N NZ  . LYS D 410 ? 1.6812 1.7616 1.4307 0.1108  -0.1327 -0.5390 410 LYS D NZ  
17858 N N   . GLU D 411 ? 1.8767 1.7685 1.7785 0.1690  0.0017  -0.5159 411 GLU D N   
17859 C CA  . GLU D 411 ? 1.9832 1.8421 1.8914 0.1893  0.0187  -0.5350 411 GLU D CA  
17860 C C   . GLU D 411 ? 2.0039 1.8105 1.9622 0.1849  0.0195  -0.5279 411 GLU D C   
17861 O O   . GLU D 411 ? 2.0334 1.7966 2.0016 0.1936  0.0238  -0.5565 411 GLU D O   
17862 C CB  . GLU D 411 ? 2.1458 2.0340 2.0430 0.2120  0.0412  -0.5139 411 GLU D CB  
17863 C CG  . GLU D 411 ? 2.2135 2.1477 2.0588 0.2182  0.0466  -0.5215 411 GLU D CG  
17864 C CD  . GLU D 411 ? 2.2667 2.2300 2.1059 0.2390  0.0716  -0.5058 411 GLU D CD  
17865 O OE1 . GLU D 411 ? 2.2439 2.1884 2.1146 0.2553  0.0850  -0.5042 411 GLU D OE1 
17866 O OE2 . GLU D 411 ? 2.2259 2.2311 2.0303 0.2389  0.0778  -0.4946 411 GLU D OE2 
17867 N N   . ALA D 412 ? 1.8833 1.6919 1.8717 0.1720  0.0169  -0.4897 412 ALA D N   
17868 C CA  . ALA D 412 ? 1.5884 1.3479 1.6199 0.1665  0.0193  -0.4767 412 ALA D CA  
17869 C C   . ALA D 412 ? 1.6695 1.3866 1.7190 0.1467  0.0061  -0.5077 412 ALA D C   
17870 O O   . ALA D 412 ? 1.7590 1.4216 1.8325 0.1507  0.0120  -0.5174 412 ALA D O   
17871 C CB  . ALA D 412 ? 1.5957 1.3722 1.6481 0.1543  0.0196  -0.4318 412 ALA D CB  
17872 N N   . PHE D 413 ? 1.6606 1.4019 1.7013 0.1254  -0.0123 -0.5233 413 PHE D N   
17873 C CA  . PHE D 413 ? 1.6566 1.3646 1.7181 0.1033  -0.0271 -0.5560 413 PHE D CA  
17874 C C   . PHE D 413 ? 1.8562 1.5294 1.9008 0.1158  -0.0252 -0.6040 413 PHE D C   
17875 O O   . PHE D 413 ? 1.9091 1.5281 1.9827 0.1062  -0.0263 -0.6256 413 PHE D O   
17876 C CB  . PHE D 413 ? 1.6843 1.4365 1.7381 0.0813  -0.0500 -0.5640 413 PHE D CB  
17877 C CG  . PHE D 413 ? 1.7298 1.4577 1.8100 0.0553  -0.0684 -0.5993 413 PHE D CG  
17878 C CD1 . PHE D 413 ? 1.6981 1.3854 1.8313 0.0350  -0.0653 -0.5897 413 PHE D CD1 
17879 C CD2 . PHE D 413 ? 1.6993 1.4475 1.7513 0.0495  -0.0891 -0.6414 413 PHE D CD2 
17880 C CE1 . PHE D 413 ? 1.7303 1.3970 1.8934 0.0081  -0.0814 -0.6233 413 PHE D CE1 
17881 C CE2 . PHE D 413 ? 1.7894 1.5189 1.8695 0.0237  -0.1081 -0.6766 413 PHE D CE2 
17882 C CZ  . PHE D 413 ? 1.8261 1.5152 1.9646 0.0023  -0.1037 -0.6679 413 PHE D CZ  
17883 N N   . GLU D 414 ? 1.8678 1.5704 1.8662 0.1368  -0.0202 -0.6209 414 GLU D N   
17884 C CA  . GLU D 414 ? 1.8413 1.5154 1.8191 0.1515  -0.0154 -0.6689 414 GLU D CA  
17885 C C   . GLU D 414 ? 1.8604 1.4796 1.8686 0.1712  0.0045  -0.6647 414 GLU D C   
17886 O O   . GLU D 414 ? 1.8584 1.4261 1.8781 0.1728  0.0053  -0.7020 414 GLU D O   
17887 C CB  . GLU D 414 ? 1.9597 1.6822 1.8797 0.1707  -0.0095 -0.6818 414 GLU D CB  
17888 C CG  . GLU D 414 ? 2.0356 1.7960 1.9148 0.1551  -0.0318 -0.7062 414 GLU D CG  
17889 C CD  . GLU D 414 ? 2.1872 2.0102 2.0204 0.1633  -0.0298 -0.6823 414 GLU D CD  
17890 O OE1 . GLU D 414 ? 2.2886 2.1265 2.1060 0.1859  -0.0067 -0.6671 414 GLU D OE1 
17891 O OE2 . GLU D 414 ? 2.1185 1.9758 1.9340 0.1471  -0.0514 -0.6783 414 GLU D OE2 
17892 N N   . LYS D 415 ? 1.8500 1.4787 1.8721 0.1866  0.0191  -0.6200 415 LYS D N   
17893 C CA  . LYS D 415 ? 1.6795 1.2601 1.7311 0.2082  0.0353  -0.6097 415 LYS D CA  
17894 C C   . LYS D 415 ? 1.7467 1.2616 1.8423 0.1902  0.0307  -0.6047 415 LYS D C   
17895 O O   . LYS D 415 ? 1.9425 1.4021 2.0609 0.2065  0.0411  -0.6084 415 LYS D O   
17896 C CB  . LYS D 415 ? 1.6108 1.2238 1.6672 0.2259  0.0476  -0.5614 415 LYS D CB  
17897 C CG  . LYS D 415 ? 1.6666 1.3318 1.6899 0.2498  0.0598  -0.5667 415 LYS D CG  
17898 C CD  . LYS D 415 ? 1.6128 1.2742 1.6559 0.2812  0.0770  -0.5473 415 LYS D CD  
17899 C CE  . LYS D 415 ? 1.6013 1.3276 1.6216 0.2971  0.0891  -0.5364 415 LYS D CE  
17900 N NZ  . LYS D 415 ? 1.7216 1.4738 1.7012 0.3021  0.0948  -0.5766 415 LYS D NZ  
17901 N N   . GLY D 416 ? 1.8254 1.3471 1.9344 0.1576  0.0165  -0.5951 416 GLY D N   
17902 C CA  . GLY D 416 ? 1.8176 1.2829 1.9694 0.1348  0.0137  -0.5890 416 GLY D CA  
17903 C C   . GLY D 416 ? 1.7363 1.2122 1.9104 0.1208  0.0162  -0.5360 416 GLY D C   
17904 O O   . GLY D 416 ? 1.7916 1.2162 2.0001 0.1078  0.0209  -0.5201 416 GLY D O   
17905 N N   . PHE D 417 ? 1.7153 1.2553 1.8696 0.1226  0.0145  -0.5084 417 PHE D N   
17906 C CA  . PHE D 417 ? 1.6189 1.1734 1.7909 0.1103  0.0181  -0.4605 417 PHE D CA  
17907 C C   . PHE D 417 ? 1.6562 1.2159 1.8532 0.0737  0.0065  -0.4627 417 PHE D C   
17908 O O   . PHE D 417 ? 1.6352 1.2310 1.8218 0.0607  -0.0092 -0.4884 417 PHE D O   
17909 C CB  . PHE D 417 ? 1.2873 0.9063 1.4323 0.1240  0.0207  -0.4341 417 PHE D CB  
17910 C CG  . PHE D 417 ? 1.3425 0.9731 1.5018 0.1175  0.0274  -0.3860 417 PHE D CG  
17911 C CD1 . PHE D 417 ? 1.4217 1.0267 1.5877 0.1355  0.0400  -0.3566 417 PHE D CD1 
17912 C CD2 . PHE D 417 ? 1.3921 1.0607 1.5574 0.0948  0.0207  -0.3711 417 PHE D CD2 
17913 C CE1 . PHE D 417 ? 1.3745 0.9913 1.5476 0.1294  0.0456  -0.3143 417 PHE D CE1 
17914 C CE2 . PHE D 417 ? 1.4433 1.1222 1.6195 0.0890  0.0287  -0.3300 417 PHE D CE2 
17915 C CZ  . PHE D 417 ? 1.4932 1.1462 1.6708 0.1056  0.0411  -0.3025 417 PHE D CZ  
17916 N N   . ARG D 418 ? 1.6333 1.1587 1.8634 0.0576  0.0143  -0.4348 418 ARG D N   
17917 C CA  . ARG D 418 ? 1.6691 1.1986 1.9323 0.0218  0.0078  -0.4330 418 ARG D CA  
17918 C C   . ARG D 418 ? 1.7490 1.2856 2.0253 0.0153  0.0211  -0.3821 418 ARG D C   
17919 O O   . ARG D 418 ? 1.6175 1.1455 1.8778 0.0379  0.0331  -0.3523 418 ARG D O   
17920 C CB  . ARG D 418 ? 1.6229 1.0875 1.9196 0.0023  0.0071  -0.4608 418 ARG D CB  
17921 C CG  . ARG D 418 ? 1.7186 1.1626 2.0002 0.0125  -0.0026 -0.5134 418 ARG D CG  
17922 C CD  . ARG D 418 ? 1.6928 1.1856 1.9659 -0.0040 -0.0254 -0.5520 418 ARG D CD  
17923 N NE  . ARG D 418 ? 1.8854 1.3582 2.1380 0.0058  -0.0339 -0.6043 418 ARG D NE  
17924 C CZ  . ARG D 418 ? 1.8899 1.3903 2.0956 0.0331  -0.0353 -0.6211 418 ARG D CZ  
17925 N NH1 . ARG D 418 ? 1.7470 1.2963 1.9235 0.0529  -0.0295 -0.5889 418 ARG D NH1 
17926 N NH2 . ARG D 418 ? 1.8612 1.3404 2.0492 0.0398  -0.0412 -0.6714 418 ARG D NH2 
17927 N N   . LEU D 419 ? 1.7889 1.3438 2.0946 -0.0148 0.0189  -0.3733 419 LEU D N   
17928 C CA  . LEU D 419 ? 1.7332 1.2968 2.0493 -0.0226 0.0334  -0.3278 419 LEU D CA  
17929 C C   . LEU D 419 ? 1.7330 1.2310 2.0551 -0.0171 0.0519  -0.3000 419 LEU D C   
17930 O O   . LEU D 419 ? 1.7086 1.2123 2.0201 -0.0102 0.0643  -0.2602 419 LEU D O   
17931 C CB  . LEU D 419 ? 1.6077 1.1977 1.9622 -0.0574 0.0304  -0.3279 419 LEU D CB  
17932 C CG  . LEU D 419 ? 1.3580 1.0223 1.7087 -0.0613 0.0145  -0.3372 419 LEU D CG  
17933 C CD1 . LEU D 419 ? 1.2484 0.9528 1.5673 -0.0402 0.0208  -0.3063 419 LEU D CD1 
17934 C CD2 . LEU D 419 ? 1.4378 1.1188 1.7739 -0.0561 -0.0078 -0.3808 419 LEU D CD2 
17935 N N   . LYS D 420 ? 1.8100 1.2443 2.1470 -0.0193 0.0532  -0.3206 420 LYS D N   
17936 C CA  . LYS D 420 ? 1.9358 1.2999 2.2783 -0.0121 0.0697  -0.2935 420 LYS D CA  
17937 C C   . LYS D 420 ? 1.9229 1.2909 2.2294 0.0267  0.0744  -0.2670 420 LYS D C   
17938 O O   . LYS D 420 ? 1.9124 1.2489 2.2146 0.0342  0.0871  -0.2277 420 LYS D O   
17939 C CB  . LYS D 420 ? 1.9277 1.2226 2.2901 -0.0154 0.0681  -0.3272 420 LYS D CB  
17940 C CG  . LYS D 420 ? 2.0060 1.2885 2.4104 -0.0557 0.0630  -0.3570 420 LYS D CG  
17941 C CD  . LYS D 420 ? 2.0874 1.3037 2.5266 -0.0804 0.0813  -0.3325 420 LYS D CD  
17942 C CE  . LYS D 420 ? 2.0508 1.2686 2.5381 -0.1240 0.0769  -0.3605 420 LYS D CE  
17943 N NZ  . LYS D 420 ? 1.9880 1.1469 2.5108 -0.1518 0.0986  -0.3324 420 LYS D NZ  
17944 N N   . HIS D 421 ? 1.9346 1.3431 2.2156 0.0507  0.0641  -0.2881 421 HIS D N   
17945 C CA  . HIS D 421 ? 1.8490 1.2647 2.1026 0.0879  0.0680  -0.2678 421 HIS D CA  
17946 C C   . HIS D 421 ? 1.7420 1.2068 1.9799 0.0889  0.0723  -0.2281 421 HIS D C   
17947 O O   . HIS D 421 ? 1.7363 1.1944 1.9596 0.1119  0.0780  -0.1984 421 HIS D O   
17948 C CB  . HIS D 421 ? 1.7783 1.2209 2.0127 0.1110  0.0592  -0.3044 421 HIS D CB  
17949 C CG  . HIS D 421 ? 1.8043 1.2016 2.0517 0.1076  0.0548  -0.3482 421 HIS D CG  
17950 N ND1 . HIS D 421 ? 1.7459 1.1681 1.9920 0.0909  0.0425  -0.3895 421 HIS D ND1 
17951 C CD2 . HIS D 421 ? 1.8171 1.1449 2.0785 0.1190  0.0604  -0.3584 421 HIS D CD2 
17952 C CE1 . HIS D 421 ? 1.7467 1.1169 2.0047 0.0909  0.0409  -0.4259 421 HIS D CE1 
17953 N NE2 . HIS D 421 ? 1.7996 1.1100 2.0686 0.1079  0.0526  -0.4079 421 HIS D NE2 
17954 N N   . PHE D 422 ? 1.7023 1.2155 1.9443 0.0655  0.0689  -0.2289 422 PHE D N   
17955 C CA  . PHE D 422 ? 1.7047 1.2660 1.9323 0.0658  0.0735  -0.1959 422 PHE D CA  
17956 C C   . PHE D 422 ? 1.7609 1.2845 1.9870 0.0672  0.0870  -0.1547 422 PHE D C   
17957 O O   . PHE D 422 ? 1.7189 1.2625 1.9223 0.0867  0.0894  -0.1291 422 PHE D O   
17958 C CB  . PHE D 422 ? 1.5397 1.1451 1.7815 0.0377  0.0700  -0.2017 422 PHE D CB  
17959 C CG  . PHE D 422 ? 1.4732 1.1426 1.6973 0.0459  0.0595  -0.2152 422 PHE D CG  
17960 C CD1 . PHE D 422 ? 1.5867 1.2955 1.7894 0.0598  0.0634  -0.1921 422 PHE D CD1 
17961 C CD2 . PHE D 422 ? 1.4149 1.1038 1.6425 0.0392  0.0455  -0.2508 422 PHE D CD2 
17962 C CE1 . PHE D 422 ? 1.6096 1.3718 1.7970 0.0661  0.0556  -0.2025 422 PHE D CE1 
17963 C CE2 . PHE D 422 ? 1.2053 0.9492 1.4128 0.0473  0.0367  -0.2593 422 PHE D CE2 
17964 C CZ  . PHE D 422 ? 1.4613 1.2398 1.6499 0.0604  0.0428  -0.2342 422 PHE D CZ  
17965 N N   . GLY D 423 ? 2.1028 1.5736 2.3519 0.0462  0.0953  -0.1487 423 GLY D N   
17966 C CA  . GLY D 423 ? 2.1448 1.5748 2.3883 0.0454  0.1098  -0.1065 423 GLY D CA  
17967 C C   . GLY D 423 ? 2.1725 1.5593 2.3997 0.0791  0.1089  -0.0932 423 GLY D C   
17968 O O   . GLY D 423 ? 2.1937 1.5750 2.3996 0.0920  0.1146  -0.0549 423 GLY D O   
17969 N N   . GLU D 424 ? 1.8922 1.2510 2.1288 0.0939  0.1014  -0.1247 424 GLU D N   
17970 C CA  . GLU D 424 ? 1.8981 1.2136 2.1262 0.1283  0.1006  -0.1150 424 GLU D CA  
17971 C C   . GLU D 424 ? 1.9059 1.2716 2.1066 0.1578  0.0955  -0.0946 424 GLU D C   
17972 O O   . GLU D 424 ? 1.8993 1.2380 2.0890 0.1805  0.0969  -0.0638 424 GLU D O   
17973 C CB  . GLU D 424 ? 1.9982 1.2879 2.2403 0.1412  0.0938  -0.1598 424 GLU D CB  
17974 C CG  . GLU D 424 ? 2.1173 1.3384 2.3888 0.1177  0.0987  -0.1782 424 GLU D CG  
17975 C CD  . GLU D 424 ? 2.0763 1.2127 2.3564 0.1274  0.1085  -0.1503 424 GLU D CD  
17976 O OE1 . GLU D 424 ? 1.9899 1.1218 2.2504 0.1527  0.1105  -0.1112 424 GLU D OE1 
17977 O OE2 . GLU D 424 ? 2.0277 1.1010 2.3343 0.1096  0.1134  -0.1674 424 GLU D OE2 
17978 N N   . VAL D 425 ? 1.8242 1.2621 2.0147 0.1572  0.0891  -0.1103 425 VAL D N   
17979 C CA  . VAL D 425 ? 1.6605 1.1490 1.8295 0.1815  0.0848  -0.0938 425 VAL D CA  
17980 C C   . VAL D 425 ? 1.6391 1.1383 1.7921 0.1718  0.0904  -0.0521 425 VAL D C   
17981 O O   . VAL D 425 ? 1.7133 1.2209 1.8496 0.1945  0.0875  -0.0267 425 VAL D O   
17982 C CB  . VAL D 425 ? 1.4680 1.0269 1.6302 0.1838  0.0784  -0.1208 425 VAL D CB  
17983 C CG1 . VAL D 425 ? 1.5299 1.0802 1.7025 0.1856  0.0744  -0.1646 425 VAL D CG1 
17984 C CG2 . VAL D 425 ? 1.4408 1.0460 1.5981 0.1564  0.0801  -0.1142 425 VAL D CG2 
17985 N N   . ILE D 426 ? 1.6653 1.1671 1.8236 0.1384  0.0983  -0.0463 426 ILE D N   
17986 C CA  . ILE D 426 ? 1.7686 1.2817 1.9098 0.1268  0.1068  -0.0099 426 ILE D CA  
17987 C C   . ILE D 426 ? 1.8325 1.2834 1.9631 0.1369  0.1129  0.0255  426 ILE D C   
17988 O O   . ILE D 426 ? 1.8011 1.2630 1.9054 0.1543  0.1107  0.0549  426 ILE D O   
17989 C CB  . ILE D 426 ? 1.5332 1.0629 1.6889 0.0892  0.1163  -0.0146 426 ILE D CB  
17990 C CG1 . ILE D 426 ? 1.4239 1.0202 1.5845 0.0836  0.1084  -0.0425 426 ILE D CG1 
17991 C CG2 . ILE D 426 ? 1.5325 1.0634 1.6701 0.0766  0.1296  0.0234  426 ILE D CG2 
17992 C CD1 . ILE D 426 ? 1.5048 1.1126 1.6925 0.0514  0.1116  -0.0609 426 ILE D CD1 
17993 N N   . TYR D 427 ? 1.8616 1.2461 2.0120 0.1269  0.1194  0.0228  427 TYR D N   
17994 C CA  . TYR D 427 ? 1.7761 1.0925 1.9167 0.1362  0.1264  0.0589  427 TYR D CA  
17995 C C   . TYR D 427 ? 1.7822 1.0917 1.9071 0.1798  0.1136  0.0709  427 TYR D C   
17996 O O   . TYR D 427 ? 1.8656 1.1566 1.9651 0.1939  0.1141  0.1110  427 TYR D O   
17997 C CB  . TYR D 427 ? 1.8276 1.0712 1.9988 0.1184  0.1350  0.0467  427 TYR D CB  
17998 C CG  . TYR D 427 ? 2.0666 1.2295 2.2303 0.1302  0.1424  0.0833  427 TYR D CG  
17999 C CD1 . TYR D 427 ? 2.0723 1.2143 2.2126 0.1176  0.1563  0.1295  427 TYR D CD1 
18000 C CD2 . TYR D 427 ? 2.0436 1.1485 2.2227 0.1541  0.1367  0.0718  427 TYR D CD2 
18001 C CE1 . TYR D 427 ? 2.0453 1.1096 2.1748 0.1287  0.1635  0.1671  427 TYR D CE1 
18002 C CE2 . TYR D 427 ? 2.0345 1.0603 2.2077 0.1667  0.1432  0.1077  427 TYR D CE2 
18003 C CZ  . TYR D 427 ? 2.1465 1.1512 2.2937 0.1538  0.1562  0.1570  427 TYR D CZ  
18004 O OH  . TYR D 427 ? 2.2051 1.1282 2.3428 0.1667  0.1628  0.1963  427 TYR D OH  
18005 N N   . ALA D 428 ? 1.7641 1.0914 1.9035 0.2016  0.1022  0.0367  428 ALA D N   
18006 C CA  . ALA D 428 ? 1.8135 1.1408 1.9469 0.2441  0.0905  0.0438  428 ALA D CA  
18007 C C   . ALA D 428 ? 1.8784 1.2725 1.9860 0.2587  0.0819  0.0635  428 ALA D C   
18008 O O   . ALA D 428 ? 1.9723 1.3555 2.0649 0.2854  0.0746  0.0936  428 ALA D O   
18009 C CB  . ALA D 428 ? 1.6942 1.0298 1.8507 0.2610  0.0842  -0.0013 428 ALA D CB  
18010 N N   . LYS D 429 ? 1.7970 1.2593 1.9002 0.2420  0.0815  0.0465  429 LYS D N   
18011 C CA  . LYS D 429 ? 1.8467 1.3730 1.9288 0.2526  0.0738  0.0604  429 LYS D CA  
18012 C C   . LYS D 429 ? 1.8858 1.4083 1.9377 0.2386  0.0794  0.0997  429 LYS D C   
18013 O O   . LYS D 429 ? 1.9436 1.4997 1.9733 0.2545  0.0705  0.1194  429 LYS D O   
18014 C CB  . LYS D 429 ? 1.6554 1.2505 1.7437 0.2401  0.0729  0.0292  429 LYS D CB  
18015 C CG  . LYS D 429 ? 1.4644 1.0757 1.5737 0.2570  0.0677  -0.0084 429 LYS D CG  
18016 C CD  . LYS D 429 ? 1.4883 1.1160 1.6024 0.2961  0.0575  -0.0067 429 LYS D CD  
18017 C CE  . LYS D 429 ? 1.3966 1.0879 1.4974 0.3044  0.0501  0.0076  429 LYS D CE  
18018 N NZ  . LYS D 429 ? 1.5974 1.3130 1.7126 0.3409  0.0401  0.0024  429 LYS D NZ  
18019 N N   . MET D 430 ? 1.7992 1.2834 1.8503 0.2087  0.0943  0.1102  430 MET D N   
18020 C CA  . MET D 430 ? 1.8985 1.3771 1.9186 0.1937  0.1038  0.1472  430 MET D CA  
18021 C C   . MET D 430 ? 2.0346 1.4684 2.0291 0.2191  0.0985  0.1876  430 MET D C   
18022 O O   . MET D 430 ? 2.1672 1.6130 2.1250 0.2184  0.0997  0.2190  430 MET D O   
18023 C CB  . MET D 430 ? 1.8263 1.2731 1.8580 0.1554  0.1238  0.1481  430 MET D CB  
18024 C CG  . MET D 430 ? 1.9275 1.4286 1.9759 0.1288  0.1288  0.1189  430 MET D CG  
18025 S SD  . MET D 430 ? 1.8478 1.4098 1.8639 0.1171  0.1348  0.1359  430 MET D SD  
18026 C CE  . MET D 430 ? 2.0416 1.5588 2.0513 0.0846  0.1606  0.1647  430 MET D CE  
18027 N N   . LEU D 431 ? 2.0879 1.4695 2.0998 0.2426  0.0924  0.1869  431 LEU D N   
18028 C CA  . LEU D 431 ? 2.1559 1.4906 2.1469 0.2713  0.0852  0.2262  431 LEU D CA  
18029 C C   . LEU D 431 ? 2.1925 1.5700 2.1839 0.3127  0.0622  0.2222  431 LEU D C   
18030 O O   . LEU D 431 ? 2.2702 1.6486 2.2330 0.3353  0.0506  0.2566  431 LEU D O   
18031 C CB  . LEU D 431 ? 2.0581 1.3035 2.0718 0.2741  0.0929  0.2298  431 LEU D CB  
18032 C CG  . LEU D 431 ? 2.0691 1.2696 2.0953 0.2318  0.1157  0.2273  431 LEU D CG  
18033 C CD1 . LEU D 431 ? 2.1043 1.2184 2.1587 0.2364  0.1211  0.2238  431 LEU D CD1 
18034 C CD2 . LEU D 431 ? 2.0685 1.2581 2.0571 0.2100  0.1305  0.2701  431 LEU D CD2 
18035 N N   . ASP D 432 ? 2.0992 1.5143 2.1229 0.3226  0.0556  0.1806  432 ASP D N   
18036 C CA  . ASP D 432 ? 2.0858 1.5472 2.1186 0.3598  0.0366  0.1725  432 ASP D CA  
18037 C C   . ASP D 432 ? 2.0391 1.5778 2.0478 0.3578  0.0271  0.1799  432 ASP D C   
18038 O O   . ASP D 432 ? 2.0837 1.6506 2.0865 0.3879  0.0094  0.1940  432 ASP D O   
18039 C CB  . ASP D 432 ? 2.0329 1.5151 2.1045 0.3662  0.0370  0.1246  432 ASP D CB  
18040 C CG  . ASP D 432 ? 2.2153 1.7425 2.3049 0.4049  0.0213  0.1132  432 ASP D CG  
18041 O OD1 . ASP D 432 ? 2.2336 1.7467 2.3181 0.4363  0.0081  0.1415  432 ASP D OD1 
18042 O OD2 . ASP D 432 ? 2.1683 1.7460 2.2780 0.4041  0.0224  0.0768  432 ASP D OD2 
18043 N N   . GLU D 433 ? 1.9919 1.5655 1.9898 0.3231  0.0381  0.1693  433 GLU D N   
18044 C CA  . GLU D 433 ? 2.0480 1.6916 2.0246 0.3175  0.0314  0.1718  433 GLU D CA  
18045 C C   . GLU D 433 ? 2.0295 1.6602 1.9611 0.3035  0.0359  0.2092  433 GLU D C   
18046 O O   . GLU D 433 ? 1.9739 1.6418 1.8795 0.3163  0.0223  0.2255  433 GLU D O   
18047 C CB  . GLU D 433 ? 2.0650 1.7565 2.0575 0.2904  0.0408  0.1363  433 GLU D CB  
18048 C CG  . GLU D 433 ? 2.0195 1.7881 2.0059 0.2914  0.0319  0.1265  433 GLU D CG  
18049 C CD  . GLU D 433 ? 2.0077 1.8220 2.0260 0.3091  0.0236  0.0959  433 GLU D CD  
18050 O OE1 . GLU D 433 ? 1.8420 1.6313 1.8863 0.3193  0.0263  0.0774  433 GLU D OE1 
18051 O OE2 . GLU D 433 ? 2.0345 1.9100 2.0518 0.3116  0.0157  0.0894  433 GLU D OE2 
18052 N N   . PHE D 434 ? 2.2694 1.8504 2.1916 0.2764  0.0553  0.2214  434 PHE D N   
18053 C CA  . PHE D 434 ? 2.3318 1.8999 2.2098 0.2600  0.0649  0.2560  434 PHE D CA  
18054 C C   . PHE D 434 ? 2.3915 1.8790 2.2511 0.2654  0.0718  0.2951  434 PHE D C   
18055 O O   . PHE D 434 ? 2.4049 1.8612 2.2436 0.2388  0.0919  0.3153  434 PHE D O   
18056 C CB  . PHE D 434 ? 2.2999 1.8881 2.1806 0.2197  0.0858  0.2399  434 PHE D CB  
18057 C CG  . PHE D 434 ? 2.3211 1.9843 2.2148 0.2140  0.0800  0.2068  434 PHE D CG  
18058 C CD1 . PHE D 434 ? 2.4593 2.1742 2.3235 0.2172  0.0719  0.2129  434 PHE D CD1 
18059 C CD2 . PHE D 434 ? 2.2638 1.9438 2.1977 0.2053  0.0824  0.1698  434 PHE D CD2 
18060 C CE1 . PHE D 434 ? 2.4557 2.2343 2.3344 0.2107  0.0680  0.1830  434 PHE D CE1 
18061 C CE2 . PHE D 434 ? 2.2720 2.0161 2.2160 0.2001  0.0784  0.1432  434 PHE D CE2 
18062 C CZ  . PHE D 434 ? 2.4123 2.2035 2.3307 0.2024  0.0719  0.1502  434 PHE D CZ  
18063 N N   . GLY D 435 ? 2.1856 1.6398 2.0541 0.3001  0.0564  0.3066  435 GLY D N   
18064 C CA  . GLY D 435 ? 2.1419 1.5140 1.9937 0.3096  0.0614  0.3464  435 GLY D CA  
18065 C C   . GLY D 435 ? 2.2618 1.6305 2.0533 0.3150  0.0580  0.3940  435 GLY D C   
18066 O O   . GLY D 435 ? 2.3705 1.6703 2.1370 0.3128  0.0689  0.4330  435 GLY D O   
18067 N N   . SER D 436 ? 2.2775 1.7194 2.0433 0.3213  0.0431  0.3909  436 SER D N   
18068 C CA  . SER D 436 ? 2.3526 1.8028 2.0554 0.3270  0.0366  0.4310  436 SER D CA  
18069 C C   . SER D 436 ? 2.4095 1.8296 2.0750 0.2893  0.0667  0.4530  436 SER D C   
18070 O O   . SER D 436 ? 2.6078 1.9952 2.2194 0.2940  0.0689  0.4979  436 SER D O   
18071 C CB  . SER D 436 ? 2.1046 1.6449 1.7950 0.3346  0.0166  0.4121  436 SER D CB  
18072 O OG  . SER D 436 ? 2.2280 1.7806 1.8536 0.3382  0.0094  0.4466  436 SER D OG  
18073 N N   . VAL D 437 ? 2.3977 1.8307 2.0913 0.2526  0.0900  0.4226  437 VAL D N   
18074 C CA  . VAL D 437 ? 2.4577 1.8688 2.1257 0.2152  0.1212  0.4389  437 VAL D CA  
18075 C C   . VAL D 437 ? 2.4743 1.8351 2.1894 0.1875  0.1459  0.4255  437 VAL D C   
18076 O O   . VAL D 437 ? 2.5470 1.9004 2.2566 0.1528  0.1734  0.4298  437 VAL D O   
18077 C CB  . VAL D 437 ? 2.3743 1.8590 2.0238 0.1934  0.1280  0.4184  437 VAL D CB  
18078 C CG1 . VAL D 437 ? 2.3317 1.8628 1.9308 0.2171  0.1043  0.4321  437 VAL D CG1 
18079 C CG2 . VAL D 437 ? 2.2497 1.7838 1.9555 0.1814  0.1268  0.3662  437 VAL D CG2 
18080 N N   . VAL D 438 ? 2.3847 1.7126 2.1469 0.2021  0.1365  0.4078  438 VAL D N   
18081 C CA  . VAL D 438 ? 2.3866 1.6672 2.1952 0.1763  0.1563  0.3910  438 VAL D CA  
18082 C C   . VAL D 438 ? 2.5400 1.7376 2.3619 0.1970  0.1522  0.4105  438 VAL D C   
18083 O O   . VAL D 438 ? 2.4888 1.6861 2.3175 0.2346  0.1283  0.4076  438 VAL D O   
18084 C CB  . VAL D 438 ? 2.2589 1.5887 2.1198 0.1662  0.1515  0.3355  438 VAL D CB  
18085 C CG1 . VAL D 438 ? 2.1261 1.4071 2.0348 0.1421  0.1671  0.3160  438 VAL D CG1 
18086 C CG2 . VAL D 438 ? 2.2061 1.6103 2.0578 0.1445  0.1578  0.3175  438 VAL D CG2 
18087 N N   . ASP D 439 ? 2.6559 1.7833 2.4854 0.1720  0.1767  0.4293  439 ASP D N   
18088 C CA  . ASP D 439 ? 2.5474 1.5851 2.3924 0.1865  0.1774  0.4483  439 ASP D CA  
18089 C C   . ASP D 439 ? 2.4634 1.4709 2.3709 0.1610  0.1896  0.4086  439 ASP D C   
18090 O O   . ASP D 439 ? 2.4384 1.4135 2.3798 0.1817  0.1772  0.3881  439 ASP D O   
18091 C CB  . ASP D 439 ? 2.6152 1.5859 2.4145 0.1780  0.1968  0.5077  439 ASP D CB  
18092 C CG  . ASP D 439 ? 2.7706 1.7469 2.5066 0.2138  0.1786  0.5528  439 ASP D CG  
18093 O OD1 . ASP D 439 ? 2.6743 1.7210 2.4002 0.2391  0.1528  0.5364  439 ASP D OD1 
18094 O OD2 . ASP D 439 ? 2.8749 1.7858 2.5714 0.2158  0.1900  0.6050  439 ASP D OD2 
18095 N N   . LYS D 440 ? 2.4410 1.4624 2.3649 0.1166  0.2132  0.3958  440 LYS D N   
18096 C CA  . LYS D 440 ? 2.4040 1.4050 2.3873 0.0876  0.2239  0.3569  440 LYS D CA  
18097 C C   . LYS D 440 ? 2.2655 1.3505 2.2717 0.0641  0.2240  0.3143  440 LYS D C   
18098 O O   . LYS D 440 ? 2.2399 1.3817 2.2165 0.0569  0.2285  0.3240  440 LYS D O   
18099 C CB  . LYS D 440 ? 2.5096 1.4382 2.5019 0.0523  0.2546  0.3838  440 LYS D CB  
18100 C CG  . LYS D 440 ? 2.3901 1.2408 2.3400 0.0694  0.2617  0.4433  440 LYS D CG  
18101 C CD  . LYS D 440 ? 2.3858 1.1647 2.3470 0.0300  0.2962  0.4701  440 LYS D CD  
18102 C CE  . LYS D 440 ? 2.4483 1.1610 2.4719 0.0144  0.3016  0.4427  440 LYS D CE  
18103 N NZ  . LYS D 440 ? 2.5184 1.1734 2.5469 0.0565  0.2800  0.4435  440 LYS D NZ  
18104 N N   . CYS D 441 ? 2.2067 1.2983 2.2643 0.0528  0.2189  0.2672  441 CYS D N   
18105 C CA  . CYS D 441 ? 2.1768 1.3443 2.2587 0.0328  0.2165  0.2269  441 CYS D CA  
18106 C C   . CYS D 441 ? 1.9916 1.1421 2.1301 0.0113  0.2166  0.1838  441 CYS D C   
18107 O O   . CYS D 441 ? 2.0703 1.1684 2.2266 0.0254  0.2085  0.1716  441 CYS D O   
18108 C CB  . CYS D 441 ? 2.2228 1.4587 2.2866 0.0637  0.1928  0.2095  441 CYS D CB  
18109 S SG  . CYS D 441 ? 2.0818 1.3990 2.1792 0.0477  0.1845  0.1559  441 CYS D SG  
18110 N N   . GLU D 442 ? 1.9488 1.1444 2.1163 -0.0218 0.2246  0.1592  442 GLU D N   
18111 C CA  . GLU D 442 ? 1.8878 1.0772 2.1086 -0.0440 0.2216  0.1159  442 GLU D CA  
18112 C C   . GLU D 442 ? 1.9223 1.1958 2.1604 -0.0548 0.2119  0.0804  442 GLU D C   
18113 O O   . GLU D 442 ? 1.9617 1.2858 2.1855 -0.0635 0.2202  0.0935  442 GLU D O   
18114 C CB  . GLU D 442 ? 2.0355 1.1695 2.2887 -0.0824 0.2457  0.1268  442 GLU D CB  
18115 C CG  . GLU D 442 ? 1.9905 1.1567 2.2439 -0.1142 0.2699  0.1483  442 GLU D CG  
18116 C CD  . GLU D 442 ? 2.2434 1.3618 2.5380 -0.1557 0.2953  0.1544  442 GLU D CD  
18117 O OE1 . GLU D 442 ? 2.3817 1.4269 2.6966 -0.1584 0.2961  0.1516  442 GLU D OE1 
18118 O OE2 . GLU D 442 ? 2.1235 1.2776 2.4330 -0.1859 0.3156  0.1610  442 GLU D OE2 
18119 N N   . VAL D 443 ? 1.8155 1.1025 2.0825 -0.0529 0.1944  0.0357  443 VAL D N   
18120 C CA  . VAL D 443 ? 1.6309 0.9931 1.9130 -0.0602 0.1823  0.0021  443 VAL D CA  
18121 C C   . VAL D 443 ? 1.6496 1.0134 1.9841 -0.0958 0.1843  -0.0288 443 VAL D C   
18122 O O   . VAL D 443 ? 1.7268 1.0345 2.0869 -0.1062 0.1851  -0.0423 443 VAL D O   
18123 C CB  . VAL D 443 ? 1.5684 0.9565 1.8348 -0.0274 0.1587  -0.0247 443 VAL D CB  
18124 C CG1 . VAL D 443 ? 1.5676 1.0308 1.8439 -0.0335 0.1466  -0.0543 443 VAL D CG1 
18125 C CG2 . VAL D 443 ? 1.5997 0.9889 1.8218 0.0076  0.1555  0.0040  443 VAL D CG2 
18126 N N   . THR D 444 ? 1.7101 1.1389 2.0631 -0.1139 0.1840  -0.0412 444 THR D N   
18127 C CA  . THR D 444 ? 1.6286 1.0732 2.0353 -0.1470 0.1826  -0.0715 444 THR D CA  
18128 C C   . THR D 444 ? 1.6281 1.1481 2.0409 -0.1413 0.1618  -0.1022 444 THR D C   
18129 O O   . THR D 444 ? 1.6377 1.2113 2.0475 -0.1441 0.1669  -0.0916 444 THR D O   
18130 C CB  . THR D 444 ? 1.5077 0.9515 1.9409 -0.1808 0.2098  -0.0478 444 THR D CB  
18131 O OG1 . THR D 444 ? 1.7266 1.1053 2.1357 -0.1794 0.2308  -0.0079 444 THR D OG1 
18132 C CG2 . THR D 444 ? 1.5422 0.9873 2.0399 -0.2179 0.2105  -0.0772 444 THR D CG2 
18133 N N   . ILE D 445 ? 1.5515 1.0739 1.9705 -0.1325 0.1391  -0.1399 445 ILE D N   
18134 C CA  . ILE D 445 ? 1.4956 1.0847 1.9153 -0.1258 0.1180  -0.1677 445 ILE D CA  
18135 C C   . ILE D 445 ? 1.5081 1.1294 1.9818 -0.1587 0.1139  -0.1905 445 ILE D C   
18136 O O   . ILE D 445 ? 1.5819 1.1665 2.0925 -0.1827 0.1171  -0.2044 445 ILE D O   
18137 C CB  . ILE D 445 ? 1.3680 0.9469 1.7655 -0.1016 0.0967  -0.1978 445 ILE D CB  
18138 C CG1 . ILE D 445 ? 1.2364 0.7850 1.5887 -0.0679 0.1011  -0.1765 445 ILE D CG1 
18139 C CG2 . ILE D 445 ? 1.2111 0.8561 1.6037 -0.0948 0.0757  -0.2235 445 ILE D CG2 
18140 C CD1 . ILE D 445 ? 1.3230 0.9152 1.6402 -0.0479 0.1049  -0.1488 445 ILE D CD1 
18141 N N   . ILE D 446 ? 1.3630 1.0524 1.8450 -0.1600 0.1066  -0.1945 446 ILE D N   
18142 C CA  . ILE D 446 ? 1.4317 1.1609 1.9691 -0.1882 0.1003  -0.2156 446 ILE D CA  
18143 C C   . ILE D 446 ? 1.3685 1.1555 1.9033 -0.1764 0.0711  -0.2441 446 ILE D C   
18144 O O   . ILE D 446 ? 1.3405 1.1676 1.8482 -0.1569 0.0681  -0.2321 446 ILE D O   
18145 C CB  . ILE D 446 ? 1.4796 1.2370 2.0419 -0.2057 0.1244  -0.1884 446 ILE D CB  
18146 C CG1 . ILE D 446 ? 1.3850 1.0841 1.9390 -0.2161 0.1558  -0.1540 446 ILE D CG1 
18147 C CG2 . ILE D 446 ? 1.3846 1.1845 2.0140 -0.2352 0.1185  -0.2113 446 ILE D CG2 
18148 C CD1 . ILE D 446 ? 1.3156 1.0221 1.8254 -0.1995 0.1750  -0.1155 446 ILE D CD1 
18149 N N   . THR D 447 ? 1.4530 1.2435 2.0152 -0.1889 0.0496  -0.2817 447 THR D N   
18150 C CA  . THR D 447 ? 1.5486 1.3925 2.1066 -0.1791 0.0195  -0.3095 447 THR D CA  
18151 C C   . THR D 447 ? 1.5967 1.4895 2.2182 -0.2061 0.0078  -0.3280 447 THR D C   
18152 O O   . THR D 447 ? 1.5455 1.4894 2.1684 -0.1987 -0.0180 -0.3467 447 THR D O   
18153 C CB  . THR D 447 ? 1.6080 1.4230 2.1360 -0.1664 -0.0003 -0.3412 447 THR D CB  
18154 O OG1 . THR D 447 ? 1.7201 1.4896 2.2006 -0.1428 0.0136  -0.3229 447 THR D OG1 
18155 C CG2 . THR D 447 ? 1.4294 1.2961 1.9345 -0.1507 -0.0297 -0.3645 447 THR D CG2 
18156 N N   . ASP D 448 ? 1.5582 1.4374 2.2331 -0.2366 0.0269  -0.3215 448 ASP D N   
18157 C CA  . ASP D 448 ? 1.6044 1.5331 2.3489 -0.2637 0.0186  -0.3386 448 ASP D CA  
18158 C C   . ASP D 448 ? 1.6598 1.6481 2.4148 -0.2557 0.0268  -0.3153 448 ASP D C   
18159 O O   . ASP D 448 ? 1.6887 1.6624 2.4303 -0.2534 0.0568  -0.2819 448 ASP D O   
18160 C CB  . ASP D 448 ? 1.7203 1.6117 2.5195 -0.3004 0.0418  -0.3374 448 ASP D CB  
18161 C CG  . ASP D 448 ? 1.6912 1.6365 2.5718 -0.3313 0.0367  -0.3549 448 ASP D CG  
18162 O OD1 . ASP D 448 ? 1.6920 1.6657 2.6014 -0.3398 0.0047  -0.3935 448 ASP D OD1 
18163 O OD2 . ASP D 448 ? 1.5998 1.5616 2.5157 -0.3468 0.0647  -0.3311 448 ASP D OD2 
18164 N N   . PRO D 449 ? 1.5808 1.6347 2.3584 -0.2506 0.0011  -0.3318 449 PRO D N   
18165 C CA  . PRO D 449 ? 1.5826 1.6885 2.3729 -0.2411 0.0106  -0.3099 449 PRO D CA  
18166 C C   . PRO D 449 ? 1.4682 1.5824 2.3132 -0.2661 0.0438  -0.2922 449 PRO D C   
18167 O O   . PRO D 449 ? 1.3598 1.4872 2.1925 -0.2561 0.0661  -0.2651 449 PRO D O   
18168 C CB  . PRO D 449 ? 1.2774 1.4474 2.0949 -0.2353 -0.0263 -0.3350 449 PRO D CB  
18169 C CG  . PRO D 449 ? 1.2579 1.4078 2.0484 -0.2322 -0.0560 -0.3656 449 PRO D CG  
18170 C CD  . PRO D 449 ? 1.4551 1.5383 2.2451 -0.2512 -0.0384 -0.3706 449 PRO D CD  
18171 N N   . GLY D 450 ? 1.3530 1.4606 2.2581 -0.2992 0.0478  -0.3090 450 GLY D N   
18172 C CA  . GLY D 450 ? 1.4141 1.5304 2.3761 -0.3271 0.0817  -0.2942 450 GLY D CA  
18173 C C   . GLY D 450 ? 1.4313 1.4897 2.3535 -0.3288 0.1219  -0.2583 450 GLY D C   
18174 O O   . GLY D 450 ? 1.3762 1.4530 2.2998 -0.3276 0.1495  -0.2330 450 GLY D O   
18175 N N   . LYS D 451 ? 1.4422 1.4302 2.3277 -0.3303 0.1250  -0.2560 451 LYS D N   
18176 C CA  . LYS D 451 ? 1.3985 1.3269 2.2428 -0.3301 0.1597  -0.2200 451 LYS D CA  
18177 C C   . LYS D 451 ? 1.4528 1.3829 2.2259 -0.2953 0.1648  -0.1931 451 LYS D C   
18178 O O   . LYS D 451 ? 1.4833 1.3959 2.2341 -0.2960 0.1958  -0.1610 451 LYS D O   
18179 C CB  . LYS D 451 ? 1.3357 1.1872 2.1618 -0.3370 0.1585  -0.2254 451 LYS D CB  
18180 C CG  . LYS D 451 ? 1.4503 1.2846 2.3474 -0.3783 0.1660  -0.2436 451 LYS D CG  
18181 C CD  . LYS D 451 ? 1.7311 1.4865 2.6109 -0.3827 0.1616  -0.2535 451 LYS D CD  
18182 C CE  . LYS D 451 ? 1.3545 1.0942 2.3079 -0.4242 0.1627  -0.2801 451 LYS D CE  
18183 N NZ  . LYS D 451 ? 1.3266 0.9896 2.2625 -0.4250 0.1537  -0.2968 451 LYS D NZ  
18184 N N   . ALA D 452 ? 1.3826 1.3343 2.1197 -0.2663 0.1355  -0.2060 452 ALA D N   
18185 C CA  . ALA D 452 ? 1.3151 1.2714 1.9902 -0.2351 0.1390  -0.1836 452 ALA D CA  
18186 C C   . ALA D 452 ? 1.2606 1.2667 1.9544 -0.2362 0.1573  -0.1682 452 ALA D C   
18187 O O   . ALA D 452 ? 1.2444 1.2399 1.8981 -0.2250 0.1783  -0.1414 452 ALA D O   
18188 C CB  . ALA D 452 ? 1.2177 1.1925 1.8601 -0.2082 0.1053  -0.2027 452 ALA D CB  
18189 N N   . GLU D 453 ? 1.1761 1.2373 1.9316 -0.2488 0.1486  -0.1867 453 GLU D N   
18190 C CA  . GLU D 453 ? 1.0840 1.1958 1.8675 -0.2493 0.1657  -0.1767 453 GLU D CA  
18191 C C   . GLU D 453 ? 1.1492 1.2426 1.9470 -0.2721 0.2081  -0.1538 453 GLU D C   
18192 O O   . GLU D 453 ? 1.1523 1.2583 1.9291 -0.2640 0.2311  -0.1339 453 GLU D O   
18193 C CB  . GLU D 453 ? 1.0576 1.2320 1.9129 -0.2581 0.1444  -0.2035 453 GLU D CB  
18194 C CG  . GLU D 453 ? 1.2147 1.4452 2.1095 -0.2569 0.1608  -0.1969 453 GLU D CG  
18195 C CD  . GLU D 453 ? 1.5729 1.8685 2.5405 -0.2608 0.1361  -0.2223 453 GLU D CD  
18196 O OE1 . GLU D 453 ? 1.4215 1.7204 2.4135 -0.2700 0.1070  -0.2466 453 GLU D OE1 
18197 O OE2 . GLU D 453 ? 1.7385 2.0828 2.7396 -0.2539 0.1453  -0.2190 453 GLU D OE2 
18198 N N   . GLU D 454 ? 1.3319 1.3941 2.1636 -0.3013 0.2195  -0.1570 454 GLU D N   
18199 C CA  . GLU D 454 ? 1.1974 1.2381 2.0422 -0.3261 0.2620  -0.1334 454 GLU D CA  
18200 C C   . GLU D 454 ? 1.2493 1.2343 2.0134 -0.3111 0.2812  -0.0998 454 GLU D C   
18201 O O   . GLU D 454 ? 1.3444 1.3371 2.0881 -0.3106 0.3106  -0.0766 454 GLU D O   
18202 C CB  . GLU D 454 ? 1.2517 1.2653 2.1516 -0.3620 0.2686  -0.1445 454 GLU D CB  
18203 C CG  . GLU D 454 ? 1.3177 1.3875 2.3040 -0.3809 0.2485  -0.1797 454 GLU D CG  
18204 C CD  . GLU D 454 ? 1.6502 1.6854 2.6821 -0.4133 0.2455  -0.1972 454 GLU D CD  
18205 O OE1 . GLU D 454 ? 1.5645 1.5393 2.5827 -0.4314 0.2751  -0.1754 454 GLU D OE1 
18206 O OE2 . GLU D 454 ? 1.7629 1.8299 2.8431 -0.4205 0.2131  -0.2326 454 GLU D OE2 
18207 N N   . LEU D 455 ? 1.2674 1.1983 1.9857 -0.2981 0.2639  -0.0984 455 LEU D N   
18208 C CA  . LEU D 455 ? 1.2745 1.1532 1.9189 -0.2811 0.2766  -0.0674 455 LEU D CA  
18209 C C   . LEU D 455 ? 1.4394 1.3482 2.0339 -0.2527 0.2759  -0.0554 455 LEU D C   
18210 O O   . LEU D 455 ? 1.5450 1.4286 2.0885 -0.2450 0.2956  -0.0267 455 LEU D O   
18211 C CB  . LEU D 455 ? 1.3491 1.1736 1.9630 -0.2680 0.2532  -0.0748 455 LEU D CB  
18212 C CG  . LEU D 455 ? 1.3694 1.1364 2.0123 -0.2942 0.2621  -0.0760 455 LEU D CG  
18213 C CD1 . LEU D 455 ? 1.4407 1.1848 2.0883 -0.2866 0.2296  -0.1066 455 LEU D CD1 
18214 C CD2 . LEU D 455 ? 1.3412 1.0433 1.9373 -0.2933 0.2885  -0.0369 455 LEU D CD2 
18215 N N   . GLU D 456 ? 1.3962 1.3575 2.0045 -0.2376 0.2530  -0.0767 456 GLU D N   
18216 C CA  . GLU D 456 ? 1.3039 1.2936 1.8718 -0.2126 0.2520  -0.0684 456 GLU D CA  
18217 C C   . GLU D 456 ? 1.3419 1.3547 1.9169 -0.2236 0.2867  -0.0518 456 GLU D C   
18218 O O   . GLU D 456 ? 1.4173 1.4197 1.9391 -0.2111 0.3005  -0.0316 456 GLU D O   
18219 C CB  . GLU D 456 ? 1.2797 1.3184 1.8685 -0.1973 0.2221  -0.0937 456 GLU D CB  
18220 C CG  . GLU D 456 ? 1.1873 1.2438 1.7293 -0.1695 0.2161  -0.0870 456 GLU D CG  
18221 C CD  . GLU D 456 ? 1.2989 1.4059 1.8668 -0.1570 0.1939  -0.1063 456 GLU D CD  
18222 O OE1 . GLU D 456 ? 1.4693 1.5910 2.0745 -0.1622 0.1714  -0.1272 456 GLU D OE1 
18223 O OE2 . GLU D 456 ? 1.0816 1.2121 1.6316 -0.1418 0.1984  -0.1005 456 GLU D OE2 
18224 N N   . GLY D 457 ? 1.3541 1.4002 1.9953 -0.2470 0.3006  -0.0621 457 GLY D N   
18225 C CA  . GLY D 457 ? 1.2689 1.3411 1.9241 -0.2590 0.3366  -0.0500 457 GLY D CA  
18226 C C   . GLY D 457 ? 1.3414 1.3694 1.9723 -0.2787 0.3723  -0.0220 457 GLY D C   
18227 O O   . GLY D 457 ? 1.5322 1.5716 2.1455 -0.2827 0.4038  -0.0062 457 GLY D O   
18228 N N   . LYS D 458 ? 1.3545 1.3297 1.9823 -0.2909 0.3686  -0.0154 458 LYS D N   
18229 C CA  . LYS D 458 ? 1.4684 1.3935 2.0721 -0.3098 0.4020  0.0150  458 LYS D CA  
18230 C C   . LYS D 458 ? 1.5911 1.4824 2.1051 -0.2879 0.4095  0.0452  458 LYS D C   
18231 O O   . LYS D 458 ? 1.6204 1.5131 2.1078 -0.2952 0.4423  0.0673  458 LYS D O   
18232 C CB  . LYS D 458 ? 1.6192 1.4905 2.2446 -0.3269 0.3940  0.0133  458 LYS D CB  
18233 C CG  . LYS D 458 ? 1.5740 1.4709 2.2902 -0.3592 0.3970  -0.0109 458 LYS D CG  
18234 C CD  . LYS D 458 ? 1.6426 1.4782 2.3759 -0.3779 0.3921  -0.0123 458 LYS D CD  
18235 C CE  . LYS D 458 ? 1.5130 1.3766 2.3399 -0.4112 0.3908  -0.0408 458 LYS D CE  
18236 N NZ  . LYS D 458 ? 1.3814 1.1869 2.2250 -0.4255 0.3769  -0.0517 458 LYS D NZ  
18237 N N   . TYR D 459 ? 1.5683 1.4317 2.0360 -0.2612 0.3794  0.0455  459 TYR D N   
18238 C CA  . TYR D 459 ? 1.6062 1.4404 1.9934 -0.2392 0.3815  0.0725  459 TYR D CA  
18239 C C   . TYR D 459 ? 1.5453 1.4086 1.8976 -0.2073 0.3549  0.0608  459 TYR D C   
18240 O O   . TYR D 459 ? 1.6261 1.4882 1.9215 -0.1927 0.3616  0.0786  459 TYR D O   
18241 C CB  . TYR D 459 ? 1.7393 1.5021 2.0969 -0.2363 0.3756  0.0920  459 TYR D CB  
18242 C CG  . TYR D 459 ? 2.1072 1.8281 2.4852 -0.2672 0.4063  0.1124  459 TYR D CG  
18243 C CD1 . TYR D 459 ? 2.2255 1.9341 2.5679 -0.2781 0.4418  0.1452  459 TYR D CD1 
18244 C CD2 . TYR D 459 ? 1.9654 1.6553 2.3943 -0.2859 0.4002  0.0993  459 TYR D CD2 
18245 C CE1 . TYR D 459 ? 2.1408 1.8073 2.4993 -0.3076 0.4728  0.1674  459 TYR D CE1 
18246 C CE2 . TYR D 459 ? 1.9828 1.6299 2.4329 -0.3164 0.4298  0.1188  459 TYR D CE2 
18247 C CZ  . TYR D 459 ? 2.1622 1.7971 2.5771 -0.3274 0.4672  0.1545  459 TYR D CZ  
18248 O OH  . TYR D 459 ? 2.1891 1.7795 2.6230 -0.3590 0.4997  0.1769  459 TYR D OH  
18249 N N   . ALA D 460 ? 1.3561 1.2445 1.7392 -0.1969 0.3251  0.0319  460 ALA D N   
18250 C CA  . ALA D 460 ? 1.2873 1.2006 1.6387 -0.1684 0.3019  0.0223  460 ALA D CA  
18251 C C   . ALA D 460 ? 1.3035 1.2672 1.6532 -0.1645 0.3141  0.0184  460 ALA D C   
18252 O O   . ALA D 460 ? 1.3579 1.3221 1.6557 -0.1490 0.3166  0.0302  460 ALA D O   
18253 C CB  . ALA D 460 ? 1.1410 1.0654 1.5211 -0.1592 0.2692  -0.0051 460 ALA D CB  
18254 N N   . VAL D 461 ? 1.3099 1.3159 1.7174 -0.1781 0.3216  0.0010  461 VAL D N   
18255 C CA  . VAL D 461 ? 1.1100 1.1615 1.5214 -0.1728 0.3338  -0.0053 461 VAL D CA  
18256 C C   . VAL D 461 ? 1.2963 1.3400 1.6669 -0.1795 0.3680  0.0164  461 VAL D C   
18257 O O   . VAL D 461 ? 1.2792 1.3372 1.6107 -0.1646 0.3698  0.0174  461 VAL D O   
18258 C CB  . VAL D 461 ? 1.1635 1.2630 1.6508 -0.1835 0.3343  -0.0279 461 VAL D CB  
18259 C CG1 . VAL D 461 ? 1.1019 1.2438 1.5936 -0.1752 0.3479  -0.0346 461 VAL D CG1 
18260 C CG2 . VAL D 461 ? 1.0432 1.1525 1.5596 -0.1740 0.2973  -0.0487 461 VAL D CG2 
18261 N N   . PRO D 462 ? 1.3283 1.3484 1.7032 -0.2022 0.3958  0.0339  462 PRO D N   
18262 C CA  . PRO D 462 ? 1.3844 1.3975 1.7111 -0.2075 0.4286  0.0558  462 PRO D CA  
18263 C C   . PRO D 462 ? 1.4519 1.4329 1.6960 -0.1871 0.4176  0.0756  462 PRO D C   
18264 O O   . PRO D 462 ? 1.4704 1.4607 1.6677 -0.1826 0.4342  0.0848  462 PRO D O   
18265 C CB  . PRO D 462 ? 1.2164 1.2036 1.5659 -0.2366 0.4578  0.0728  462 PRO D CB  
18266 C CG  . PRO D 462 ? 1.2144 1.2117 1.6411 -0.2495 0.4430  0.0519  462 PRO D CG  
18267 C CD  . PRO D 462 ? 1.3144 1.3122 1.7357 -0.2252 0.4001  0.0348  462 PRO D CD  
18268 N N   . ARG D 463 ? 1.2134 1.1594 1.4407 -0.1741 0.3894  0.0805  463 ARG D N   
18269 C CA  . ARG D 463 ? 1.3133 1.2325 1.4700 -0.1528 0.3758  0.0985  463 ARG D CA  
18270 C C   . ARG D 463 ? 1.3735 1.3294 1.5101 -0.1314 0.3583  0.0818  463 ARG D C   
18271 O O   . ARG D 463 ? 1.3916 1.3491 1.4730 -0.1216 0.3626  0.0931  463 ARG D O   
18272 C CB  . ARG D 463 ? 1.4617 1.3366 1.6147 -0.1430 0.3511  0.1047  463 ARG D CB  
18273 C CG  . ARG D 463 ? 1.5826 1.4028 1.7244 -0.1575 0.3681  0.1329  463 ARG D CG  
18274 C CD  . ARG D 463 ? 1.6254 1.4121 1.6924 -0.1431 0.3706  0.1658  463 ARG D CD  
18275 N NE  . ARG D 463 ? 1.8431 1.5668 1.9010 -0.1447 0.3697  0.1895  463 ARG D NE  
18276 C CZ  . ARG D 463 ? 1.7780 1.4656 1.8451 -0.1688 0.3974  0.2107  463 ARG D CZ  
18277 N NH1 . ARG D 463 ? 1.5136 1.2265 1.6002 -0.1941 0.4297  0.2107  463 ARG D NH1 
18278 N NH2 . ARG D 463 ? 1.8892 1.5143 1.9482 -0.1679 0.3945  0.2319  463 ARG D NH2 
18279 N N   . TYR D 464 ? 1.3383 1.3234 1.5184 -0.1249 0.3387  0.0552  464 TYR D N   
18280 C CA  . TYR D 464 ? 1.3383 1.3550 1.5042 -0.1065 0.3236  0.0397  464 TYR D CA  
18281 C C   . TYR D 464 ? 1.3517 1.3977 1.5052 -0.1118 0.3486  0.0368  464 TYR D C   
18282 O O   . TYR D 464 ? 1.2971 1.3539 1.4107 -0.0988 0.3437  0.0347  464 TYR D O   
18283 C CB  . TYR D 464 ? 1.2742 1.3160 1.4906 -0.1008 0.3021  0.0145  464 TYR D CB  
18284 C CG  . TYR D 464 ? 1.1150 1.1330 1.3491 -0.0976 0.2790  0.0109  464 TYR D CG  
18285 C CD1 . TYR D 464 ? 1.1435 1.1219 1.3405 -0.0887 0.2690  0.0262  464 TYR D CD1 
18286 C CD2 . TYR D 464 ? 1.0687 1.1049 1.3559 -0.1018 0.2662  -0.0090 464 TYR D CD2 
18287 C CE1 . TYR D 464 ? 1.1948 1.1498 1.4081 -0.0851 0.2496  0.0196  464 TYR D CE1 
18288 C CE2 . TYR D 464 ? 1.0355 1.0505 1.3352 -0.0994 0.2451  -0.0158 464 TYR D CE2 
18289 C CZ  . TYR D 464 ? 1.1379 1.1113 1.4009 -0.0913 0.2381  -0.0026 464 TYR D CZ  
18290 O OH  . TYR D 464 ? 1.1512 1.1023 1.4270 -0.0882 0.2189  -0.0126 464 TYR D OH  
18291 N N   . LYS D 465 ? 1.3144 1.3739 1.5036 -0.1314 0.3761  0.0348  465 LYS D N   
18292 C CA  . LYS D 465 ? 1.3068 1.3943 1.4880 -0.1373 0.4042  0.0297  465 LYS D CA  
18293 C C   . LYS D 465 ? 1.3829 1.4485 1.4907 -0.1384 0.4213  0.0529  465 LYS D C   
18294 O O   . LYS D 465 ? 1.5052 1.5884 1.5763 -0.1318 0.4289  0.0469  465 LYS D O   
18295 C CB  . LYS D 465 ? 1.1007 1.2100 1.3444 -0.1581 0.4309  0.0220  465 LYS D CB  
18296 C CG  . LYS D 465 ? 1.3842 1.5233 1.7004 -0.1550 0.4126  -0.0022 465 LYS D CG  
18297 C CD  . LYS D 465 ? 1.3080 1.4763 1.6919 -0.1744 0.4378  -0.0115 465 LYS D CD  
18298 C CE  . LYS D 465 ? 1.1808 1.3829 1.6345 -0.1681 0.4162  -0.0350 465 LYS D CE  
18299 N NZ  . LYS D 465 ? 1.2894 1.5194 1.8181 -0.1881 0.4347  -0.0432 465 LYS D NZ  
18300 N N   . GLU D 466 ? 1.4351 1.4607 1.5202 -0.1465 0.4263  0.0794  466 GLU D N   
18301 C CA  . GLU D 466 ? 1.5617 1.5613 1.5732 -0.1466 0.4403  0.1072  466 GLU D CA  
18302 C C   . GLU D 466 ? 1.4730 1.4703 1.4276 -0.1224 0.4123  0.1088  466 GLU D C   
18303 O O   . GLU D 466 ? 1.4609 1.4662 1.3592 -0.1185 0.4215  0.1144  466 GLU D O   
18304 C CB  . GLU D 466 ? 1.5338 1.4842 1.5404 -0.1578 0.4466  0.1365  466 GLU D CB  
18305 C CG  . GLU D 466 ? 1.6778 1.5944 1.6053 -0.1557 0.4582  0.1714  466 GLU D CG  
18306 C CD  . GLU D 466 ? 1.9068 1.7684 1.8306 -0.1664 0.4659  0.2028  466 GLU D CD  
18307 O OE1 . GLU D 466 ? 1.8814 1.7238 1.8537 -0.1675 0.4490  0.1962  466 GLU D OE1 
18308 O OE2 . GLU D 466 ? 1.9035 1.7392 1.7736 -0.1738 0.4891  0.2340  466 GLU D OE2 
18309 N N   . ARG D 467 ? 1.4673 1.4564 1.4380 -0.1069 0.3788  0.1020  467 ARG D N   
18310 C CA  . ARG D 467 ? 1.4162 1.4067 1.3418 -0.0840 0.3512  0.1024  467 ARG D CA  
18311 C C   . ARG D 467 ? 1.3822 1.4154 1.3068 -0.0787 0.3500  0.0765  467 ARG D C   
18312 O O   . ARG D 467 ? 1.5018 1.5428 1.3729 -0.0704 0.3467  0.0796  467 ARG D O   
18313 C CB  . ARG D 467 ? 1.2905 1.2657 1.2411 -0.0700 0.3198  0.0984  467 ARG D CB  
18314 C CG  . ARG D 467 ? 1.4853 1.4142 1.4424 -0.0746 0.3199  0.1198  467 ARG D CG  
18315 C CD  . ARG D 467 ? 1.4706 1.3935 1.4789 -0.0708 0.2995  0.1034  467 ARG D CD  
18316 N NE  . ARG D 467 ? 1.5558 1.4344 1.5507 -0.0603 0.2846  0.1201  467 ARG D NE  
18317 C CZ  . ARG D 467 ? 1.5987 1.4576 1.6324 -0.0608 0.2725  0.1107  467 ARG D CZ  
18318 N NH1 . ARG D 467 ? 1.6528 1.5366 1.7380 -0.0706 0.2704  0.0853  467 ARG D NH1 
18319 N NH2 . ARG D 467 ? 1.7078 1.5228 1.7296 -0.0511 0.2620  0.1253  467 ARG D NH2 
18320 N N   . ASP D 468 ? 1.3578 1.4169 1.3399 -0.0830 0.3516  0.0518  468 ASP D N   
18321 C CA  . ASP D 468 ? 1.3969 1.4908 1.3841 -0.0771 0.3500  0.0269  468 ASP D CA  
18322 C C   . ASP D 468 ? 1.4299 1.5382 1.3817 -0.0853 0.3779  0.0247  468 ASP D C   
18323 O O   . ASP D 468 ? 1.6798 1.8073 1.6083 -0.0781 0.3736  0.0092  468 ASP D O   
18324 C CB  . ASP D 468 ? 1.2889 1.4044 1.3459 -0.0797 0.3486  0.0049  468 ASP D CB  
18325 C CG  . ASP D 468 ? 1.3097 1.4205 1.3928 -0.0677 0.3176  -0.0008 468 ASP D CG  
18326 O OD1 . ASP D 468 ? 1.1798 1.2757 1.2296 -0.0554 0.2971  0.0078  468 ASP D OD1 
18327 O OD2 . ASP D 468 ? 1.3327 1.4566 1.4694 -0.0697 0.3136  -0.0141 468 ASP D OD2 
18328 N N   . ALA D 469 ? 1.4062 1.5054 1.3534 -0.1014 0.4077  0.0388  469 ALA D N   
18329 C CA  . ALA D 469 ? 1.3966 1.5096 1.3063 -0.1102 0.4383  0.0366  469 ALA D CA  
18330 C C   . ALA D 469 ? 1.4429 1.5324 1.2713 -0.1086 0.4404  0.0642  469 ALA D C   
18331 O O   . ALA D 469 ? 1.8152 1.9055 1.6085 -0.1203 0.4712  0.0729  469 ALA D O   
18332 C CB  . ALA D 469 ? 1.3864 1.5090 1.3407 -0.1295 0.4739  0.0348  469 ALA D CB  
18333 N N   . ARG D 470 ? 1.4719 1.5418 1.2693 -0.0932 0.4084  0.0784  470 ARG D N   
18334 C CA  . ARG D 470 ? 1.6809 1.7286 1.4016 -0.0880 0.4057  0.1070  470 ARG D CA  
18335 C C   . ARG D 470 ? 1.9203 1.9934 1.5825 -0.0859 0.4126  0.0949  470 ARG D C   
18336 O O   . ARG D 470 ? 2.1767 2.2397 1.7773 -0.0915 0.4308  0.1149  470 ARG D O   
18337 C CB  . ARG D 470 ? 1.5232 1.5490 1.2329 -0.0689 0.3678  0.1218  470 ARG D CB  
18338 C CG  . ARG D 470 ? 1.8981 1.9015 1.5305 -0.0585 0.3585  0.1534  470 ARG D CG  
18339 C CD  . ARG D 470 ? 2.2066 2.1724 1.8100 -0.0713 0.3853  0.1890  470 ARG D CD  
18340 N NE  . ARG D 470 ? 2.2390 2.1812 1.7666 -0.0577 0.3723  0.2221  470 ARG D NE  
18341 C CZ  . ARG D 470 ? 2.3259 2.2368 1.8029 -0.0660 0.3949  0.2575  470 ARG D CZ  
18342 N NH1 . ARG D 470 ? 2.3965 2.2972 1.8937 -0.0903 0.4344  0.2632  470 ARG D NH1 
18343 N NH2 . ARG D 470 ? 2.4490 2.3394 1.8559 -0.0500 0.3783  0.2885  470 ARG D NH2 
18344 N N   . LEU D 471 ? 1.6152 1.7197 1.2949 -0.0790 0.3994  0.0620  471 LEU D N   
18345 C CA  . LEU D 471 ? 1.7456 1.8742 1.3736 -0.0782 0.4047  0.0447  471 LEU D CA  
18346 C C   . LEU D 471 ? 1.8155 1.9748 1.4902 -0.0791 0.4069  0.0040  471 LEU D C   
18347 O O   . LEU D 471 ? 1.8336 2.0046 1.5219 -0.0682 0.3792  -0.0126 471 LEU D O   
18348 C CB  . LEU D 471 ? 1.6277 1.7540 1.1969 -0.0621 0.3711  0.0562  471 LEU D CB  
18349 C CG  . LEU D 471 ? 1.8133 1.9621 1.3142 -0.0612 0.3716  0.0428  471 LEU D CG  
18350 C CD1 . LEU D 471 ? 1.7954 1.9390 1.2440 -0.0751 0.4097  0.0546  471 LEU D CD1 
18351 C CD2 . LEU D 471 ? 1.5779 1.7253 1.0287 -0.0441 0.3344  0.0586  471 LEU D CD2 
18352 N N   . GLU D 472 ? 1.7784 1.9507 1.4780 -0.0918 0.4414  -0.0118 472 GLU D N   
18353 C CA  . GLU D 472 ? 1.6440 1.8412 1.3946 -0.0910 0.4452  -0.0493 472 GLU D CA  
18354 C C   . GLU D 472 ? 1.7100 1.9266 1.4128 -0.0930 0.4582  -0.0744 472 GLU D C   
18355 O O   . GLU D 472 ? 1.8856 2.1195 1.6255 -0.0959 0.4759  -0.1046 472 GLU D O   
18356 C CB  . GLU D 472 ? 1.5584 1.7612 1.3793 -0.1005 0.4713  -0.0550 472 GLU D CB  
18357 C CG  . GLU D 472 ? 1.9106 2.1168 1.7105 -0.1154 0.5136  -0.0487 472 GLU D CG  
18358 C CD  . GLU D 472 ? 2.0220 2.2378 1.8988 -0.1253 0.5382  -0.0529 472 GLU D CD  
18359 O OE1 . GLU D 472 ? 1.7899 2.0151 1.7344 -0.1188 0.5233  -0.0681 472 GLU D OE1 
18360 O OE2 . GLU D 472 ? 2.2785 2.4935 2.1470 -0.1397 0.5719  -0.0401 472 GLU D OE2 
18361 N N   . SER D 473 ? 1.7121 1.9256 1.3360 -0.0906 0.4489  -0.0632 473 SER D N   
18362 C CA  . SER D 473 ? 1.7469 1.9797 1.3188 -0.0926 0.4569  -0.0895 473 SER D CA  
18363 C C   . SER D 473 ? 1.7712 2.0124 1.3066 -0.0820 0.4180  -0.0977 473 SER D C   
18364 O O   . SER D 473 ? 1.7697 2.0293 1.2749 -0.0839 0.4188  -0.1276 473 SER D O   
18365 C CB  . SER D 473 ? 1.7119 1.9411 1.2126 -0.1020 0.4869  -0.0733 473 SER D CB  
18366 O OG  . SER D 473 ? 1.7973 2.0042 1.2493 -0.0978 0.4716  -0.0316 473 SER D OG  
18367 N N   . LEU D 474 ? 1.6198 1.8493 1.1603 -0.0711 0.3845  -0.0741 474 LEU D N   
18368 C CA  . LEU D 474 ? 1.3809 1.6231 0.8946 -0.0607 0.3473  -0.0812 474 LEU D CA  
18369 C C   . LEU D 474 ? 1.4549 1.7131 1.0264 -0.0596 0.3348  -0.1159 474 LEU D C   
18370 O O   . LEU D 474 ? 1.4417 1.6924 1.0805 -0.0595 0.3390  -0.1185 474 LEU D O   
18371 C CB  . LEU D 474 ? 1.1825 1.4077 0.6897 -0.0479 0.3183  -0.0452 474 LEU D CB  
18372 C CG  . LEU D 474 ? 1.2292 1.4707 0.7071 -0.0350 0.2787  -0.0467 474 LEU D CG  
18373 C CD1 . LEU D 474 ? 1.2693 1.5260 0.6634 -0.0362 0.2768  -0.0496 474 LEU D CD1 
18374 C CD2 . LEU D 474 ? 1.1823 1.4045 0.6660 -0.0204 0.2543  -0.0117 474 LEU D CD2 
18375 N N   . VAL D 475 ? 1.4886 1.7681 1.0327 -0.0596 0.3194  -0.1424 475 VAL D N   
18376 C CA  . VAL D 475 ? 1.4433 1.7358 1.0378 -0.0605 0.3080  -0.1755 475 VAL D CA  
18377 C C   . VAL D 475 ? 1.4339 1.7415 1.0192 -0.0521 0.2683  -0.1748 475 VAL D C   
18378 O O   . VAL D 475 ? 1.4476 1.7621 0.9763 -0.0461 0.2505  -0.1580 475 VAL D O   
18379 C CB  . VAL D 475 ? 1.3387 1.6433 0.9263 -0.0713 0.3303  -0.2166 475 VAL D CB  
18380 C CG1 . VAL D 475 ? 1.2140 1.5075 0.8261 -0.0776 0.3706  -0.2195 475 VAL D CG1 
18381 C CG2 . VAL D 475 ? 1.3970 1.7190 0.9036 -0.0747 0.3243  -0.2284 475 VAL D CG2 
18382 N N   . ASP D 476 ? 1.3255 1.6393 0.9675 -0.0514 0.2547  -0.1921 476 ASP D N   
18383 C CA  . ASP D 476 ? 1.2641 1.5968 0.9093 -0.0448 0.2195  -0.1942 476 ASP D CA  
18384 C C   . ASP D 476 ? 1.3229 1.6831 0.9187 -0.0500 0.2055  -0.2192 476 ASP D C   
18385 O O   . ASP D 476 ? 1.3129 1.6943 0.8990 -0.0435 0.1743  -0.2170 476 ASP D O   
18386 C CB  . ASP D 476 ? 1.1575 1.4904 0.8741 -0.0461 0.2141  -0.2091 476 ASP D CB  
18387 C CG  . ASP D 476 ? 1.2420 1.5519 1.0070 -0.0404 0.2228  -0.1873 476 ASP D CG  
18388 O OD1 . ASP D 476 ? 1.4958 1.7897 1.2443 -0.0355 0.2304  -0.1601 476 ASP D OD1 
18389 O OD2 . ASP D 476 ? 1.1411 1.4486 0.9594 -0.0413 0.2217  -0.1973 476 ASP D OD2 
18390 N N   . GLU D 477 ? 1.3873 1.7494 0.9535 -0.0612 0.2281  -0.2448 477 GLU D N   
18391 C CA  . GLU D 477 ? 1.3797 1.7679 0.8957 -0.0679 0.2163  -0.2737 477 GLU D CA  
18392 C C   . GLU D 477 ? 1.4384 1.8356 0.8716 -0.0606 0.2037  -0.2496 477 GLU D C   
18393 O O   . GLU D 477 ? 1.3946 1.8198 0.7879 -0.0603 0.1775  -0.2635 477 GLU D O   
18394 C CB  . GLU D 477 ? 1.3662 1.7505 0.8800 -0.0820 0.2476  -0.3125 477 GLU D CB  
18395 C CG  . GLU D 477 ? 1.3609 1.7326 0.9539 -0.0879 0.2608  -0.3356 477 GLU D CG  
18396 C CD  . GLU D 477 ? 1.4740 1.8189 1.1083 -0.0851 0.2914  -0.3198 477 GLU D CD  
18397 O OE1 . GLU D 477 ? 1.3483 1.6819 1.0118 -0.0762 0.2843  -0.2865 477 GLU D OE1 
18398 O OE2 . GLU D 477 ? 1.7447 2.0817 1.3842 -0.0917 0.3222  -0.3426 477 GLU D OE2 
18399 N N   . LYS D 478 ? 1.4636 1.8374 0.8714 -0.0549 0.2213  -0.2131 478 LYS D N   
18400 C CA  . LYS D 478 ? 1.3660 1.7408 0.6924 -0.0474 0.2130  -0.1840 478 LYS D CA  
18401 C C   . LYS D 478 ? 1.4017 1.7702 0.7309 -0.0297 0.1833  -0.1425 478 LYS D C   
18402 O O   . LYS D 478 ? 1.4753 1.8295 0.7497 -0.0217 0.1834  -0.1068 478 LYS D O   
18403 C CB  . LYS D 478 ? 1.3985 1.7493 0.6908 -0.0539 0.2539  -0.1681 478 LYS D CB  
18404 C CG  . LYS D 478 ? 1.4129 1.7711 0.6933 -0.0692 0.2864  -0.2088 478 LYS D CG  
18405 C CD  . LYS D 478 ? 1.4809 1.8604 0.6690 -0.0729 0.2818  -0.2244 478 LYS D CD  
18406 C CE  . LYS D 478 ? 1.6881 2.0535 0.7988 -0.0715 0.3020  -0.1888 478 LYS D CE  
18407 N NZ  . LYS D 478 ? 1.6477 2.0326 0.6692 -0.0783 0.3093  -0.2117 478 LYS D NZ  
18408 N N   . VAL D 479 ? 1.4186 1.7961 0.8104 -0.0231 0.1595  -0.1466 479 VAL D N   
18409 C CA  . VAL D 479 ? 1.3124 1.6854 0.7147 -0.0046 0.1319  -0.1118 479 VAL D CA  
18410 C C   . VAL D 479 ? 1.4255 1.8368 0.8469 0.0021  0.0931  -0.1296 479 VAL D C   
18411 O O   . VAL D 479 ? 1.5197 1.9521 0.9758 -0.0099 0.0922  -0.1676 479 VAL D O   
18412 C CB  . VAL D 479 ? 1.3201 1.6626 0.7875 -0.0019 0.1461  -0.0940 479 VAL D CB  
18413 C CG1 . VAL D 479 ? 1.4574 1.7934 0.9374 0.0178  0.1192  -0.0620 479 VAL D CG1 
18414 C CG2 . VAL D 479 ? 1.3839 1.6937 0.8386 -0.0100 0.1833  -0.0778 479 VAL D CG2 
18415 N N   . ASP D 480 ? 1.5750 1.9955 0.9773 0.0213  0.0617  -0.1022 480 ASP D N   
18416 C CA  . ASP D 480 ? 1.5822 2.0447 1.0066 0.0297  0.0233  -0.1167 480 ASP D CA  
18417 C C   . ASP D 480 ? 1.4654 1.9246 0.9547 0.0446  0.0091  -0.0998 480 ASP D C   
18418 O O   . ASP D 480 ? 1.3463 1.8414 0.8754 0.0476  -0.0150 -0.1176 480 ASP D O   
18419 C CB  . ASP D 480 ? 1.6535 2.1416 1.0050 0.0422  -0.0073 -0.1047 480 ASP D CB  
18420 C CG  . ASP D 480 ? 1.7577 2.2182 1.0674 0.0640  -0.0150 -0.0533 480 ASP D CG  
18421 O OD1 . ASP D 480 ? 1.7369 2.1524 1.0578 0.0642  0.0118  -0.0278 480 ASP D OD1 
18422 O OD2 . ASP D 480 ? 1.6059 2.0895 0.8725 0.0808  -0.0484 -0.0384 480 ASP D OD2 
18423 N N   . THR D 481 ? 1.5112 1.9291 1.0120 0.0531  0.0246  -0.0675 481 THR D N   
18424 C CA  . THR D 481 ? 1.4066 1.8180 0.9640 0.0678  0.0136  -0.0528 481 THR D CA  
18425 C C   . THR D 481 ? 1.4095 1.7881 1.0178 0.0584  0.0427  -0.0540 481 THR D C   
18426 O O   . THR D 481 ? 1.4266 1.7693 1.0176 0.0528  0.0678  -0.0385 481 THR D O   
18427 C CB  . THR D 481 ? 1.4638 1.8559 0.9886 0.0917  -0.0028 -0.0106 481 THR D CB  
18428 O OG1 . THR D 481 ? 1.5787 1.9994 1.0467 0.1011  -0.0297 -0.0063 481 THR D OG1 
18429 C CG2 . THR D 481 ? 1.3821 1.7739 0.9630 0.1103  -0.0188 0.0004  481 THR D CG2 
18430 N N   . PHE D 482 ? 1.3020 1.6950 0.9733 0.0568  0.0388  -0.0718 482 PHE D N   
18431 C CA  . PHE D 482 ? 1.1564 1.5231 0.8770 0.0505  0.0609  -0.0730 482 PHE D CA  
18432 C C   . PHE D 482 ? 1.2444 1.5986 0.9911 0.0700  0.0483  -0.0496 482 PHE D C   
18433 O O   . PHE D 482 ? 1.3323 1.6995 1.0620 0.0877  0.0242  -0.0351 482 PHE D O   
18434 C CB  . PHE D 482 ? 1.0031 1.3914 0.7713 0.0358  0.0662  -0.1068 482 PHE D CB  
18435 C CG  . PHE D 482 ? 1.1146 1.5060 0.8699 0.0158  0.0844  -0.1335 482 PHE D CG  
18436 C CD1 . PHE D 482 ? 1.3134 1.6914 1.0160 0.0106  0.0981  -0.1287 482 PHE D CD1 
18437 C CD2 . PHE D 482 ? 1.0188 1.4241 0.8153 0.0021  0.0899  -0.1633 482 PHE D CD2 
18438 C CE1 . PHE D 482 ? 1.3776 1.7588 1.0701 -0.0065 0.1166  -0.1563 482 PHE D CE1 
18439 C CE2 . PHE D 482 ? 1.0853 1.4896 0.8729 -0.0149 0.1074  -0.1895 482 PHE D CE2 
18440 C CZ  . PHE D 482 ? 1.2230 1.6161 0.9592 -0.0184 0.1207  -0.1872 482 PHE D CZ  
18441 N N   . TYR D 483 ? 1.2505 1.5798 1.0372 0.0685  0.0634  -0.0463 483 TYR D N   
18442 C CA  . TYR D 483 ? 1.1315 1.4469 0.9421 0.0865  0.0534  -0.0282 483 TYR D CA  
18443 C C   . TYR D 483 ? 1.1488 1.4704 1.0153 0.0838  0.0582  -0.0436 483 TYR D C   
18444 O O   . TYR D 483 ? 1.0649 1.3870 0.9510 0.0675  0.0743  -0.0611 483 TYR D O   
18445 C CB  . TYR D 483 ? 1.0676 1.3364 0.8576 0.0908  0.0655  -0.0003 483 TYR D CB  
18446 C CG  . TYR D 483 ? 1.1730 1.4327 0.9047 0.0978  0.0586  0.0223  483 TYR D CG  
18447 C CD1 . TYR D 483 ? 1.2228 1.4857 0.9392 0.1205  0.0339  0.0418  483 TYR D CD1 
18448 C CD2 . TYR D 483 ? 1.3225 1.5736 1.0132 0.0828  0.0763  0.0235  483 TYR D CD2 
18449 C CE1 . TYR D 483 ? 1.5067 1.7607 1.1648 0.1285  0.0258  0.0656  483 TYR D CE1 
18450 C CE2 . TYR D 483 ? 1.5034 1.7468 1.1333 0.0889  0.0708  0.0456  483 TYR D CE2 
18451 C CZ  . TYR D 483 ? 1.6722 1.9161 1.2841 0.1119  0.0446  0.0680  483 TYR D CZ  
18452 O OH  . TYR D 483 ? 1.5567 1.7911 1.1043 0.1195  0.0377  0.0935  483 TYR D OH  
18453 N N   . SER D 484 ? 0.9643 1.2906 0.8554 0.1010  0.0445  -0.0367 484 SER D N   
18454 C CA  . SER D 484 ? 0.8474 1.1806 0.7859 0.1003  0.0492  -0.0493 484 SER D CA  
18455 C C   . SER D 484 ? 1.0672 1.3692 1.0169 0.1148  0.0502  -0.0331 484 SER D C   
18456 O O   . SER D 484 ? 1.1581 1.4525 1.0952 0.1334  0.0366  -0.0165 484 SER D O   
18457 C CB  . SER D 484 ? 1.0056 1.3854 0.9702 0.1052  0.0331  -0.0649 484 SER D CB  
18458 O OG  . SER D 484 ? 0.9922 1.3856 0.9512 0.1275  0.0113  -0.0522 484 SER D OG  
18459 N N   . CYS D 485 ? 0.9587 1.2416 0.9314 0.1071  0.0654  -0.0382 485 CYS D N   
18460 C CA  . CYS D 485 ? 0.8620 1.1150 0.8462 0.1183  0.0670  -0.0280 485 CYS D CA  
18461 C C   . CYS D 485 ? 0.9802 1.2495 1.0002 0.1219  0.0676  -0.0422 485 CYS D C   
18462 O O   . CYS D 485 ? 1.0610 1.3434 1.0969 0.1081  0.0772  -0.0560 485 CYS D O   
18463 C CB  . CYS D 485 ? 0.9424 1.1580 0.9188 0.1062  0.0832  -0.0210 485 CYS D CB  
18464 S SG  . CYS D 485 ? 0.9930 1.1691 0.9832 0.1164  0.0844  -0.0121 485 CYS D SG  
18465 N N   . ASN D 486 ? 0.9088 1.1759 0.9407 0.1412  0.0587  -0.0383 486 ASN D N   
18466 C CA  . ASN D 486 ? 0.8248 1.1078 0.8870 0.1464  0.0613  -0.0513 486 ASN D CA  
18467 C C   . ASN D 486 ? 0.8373 1.0849 0.9038 0.1534  0.0666  -0.0488 486 ASN D C   
18468 O O   . ASN D 486 ? 0.9721 1.2289 1.0574 0.1634  0.0672  -0.0578 486 ASN D O   
18469 C CB  . ASN D 486 ? 0.7616 1.0815 0.8407 0.1638  0.0475  -0.0552 486 ASN D CB  
18470 C CG  . ASN D 486 ? 0.9423 1.2461 1.0154 0.1884  0.0343  -0.0414 486 ASN D CG  
18471 O OD1 . ASN D 486 ? 0.9774 1.2388 1.0292 0.1916  0.0350  -0.0264 486 ASN D OD1 
18472 N ND2 . ASN D 486 ? 0.9789 1.3163 1.0741 0.2067  0.0225  -0.0459 486 ASN D ND2 
18473 N N   . LEU D 487 ? 0.8505 1.0592 0.9005 0.1473  0.0714  -0.0384 487 LEU D N   
18474 C CA  . LEU D 487 ? 0.7700 0.9439 0.8249 0.1513  0.0750  -0.0383 487 LEU D CA  
18475 C C   . LEU D 487 ? 0.7925 0.9753 0.8637 0.1441  0.0828  -0.0541 487 LEU D C   
18476 O O   . LEU D 487 ? 0.7769 0.9523 0.8569 0.1548  0.0820  -0.0617 487 LEU D O   
18477 C CB  . LEU D 487 ? 0.8464 0.9827 0.8855 0.1399  0.0809  -0.0259 487 LEU D CB  
18478 C CG  . LEU D 487 ? 0.7517 0.8486 0.7971 0.1415  0.0833  -0.0258 487 LEU D CG  
18479 C CD1 . LEU D 487 ? 0.8759 0.9491 0.9183 0.1625  0.0744  -0.0169 487 LEU D CD1 
18480 C CD2 . LEU D 487 ? 0.9565 1.0269 0.9954 0.1233  0.0928  -0.0176 487 LEU D CD2 
18481 N N   . CYS D 488 ? 0.8027 1.0005 0.8760 0.1271  0.0905  -0.0589 488 CYS D N   
18482 C CA  . CYS D 488 ? 0.7463 0.9508 0.8309 0.1206  0.0973  -0.0698 488 CYS D CA  
18483 C C   . CYS D 488 ? 0.8624 1.0990 0.9595 0.1271  0.0984  -0.0793 488 CYS D C   
18484 O O   . CYS D 488 ? 1.0037 1.2481 1.1061 0.1204  0.1055  -0.0856 488 CYS D O   
18485 C CB  . CYS D 488 ? 0.5722 0.7766 0.6574 0.1023  0.1053  -0.0697 488 CYS D CB  
18486 S SG  . CYS D 488 ? 0.9069 1.0776 0.9855 0.0928  0.1082  -0.0611 488 CYS D SG  
18487 N N   . GLN D 489 ? 0.7945 1.0507 0.8973 0.1405  0.0917  -0.0795 489 GLN D N   
18488 C CA  . GLN D 489 ? 0.7767 1.0676 0.8972 0.1460  0.0949  -0.0895 489 GLN D CA  
18489 C C   . GLN D 489 ? 0.9101 1.1923 1.0334 0.1577  0.0991  -0.0973 489 GLN D C   
18490 O O   . GLN D 489 ? 0.9026 1.2106 1.0376 0.1589  0.1071  -0.1059 489 GLN D O   
18491 C CB  . GLN D 489 ? 0.7927 1.1136 0.9245 0.1574  0.0851  -0.0891 489 GLN D CB  
18492 C CG  . GLN D 489 ? 0.8556 1.1991 0.9872 0.1430  0.0826  -0.0886 489 GLN D CG  
18493 C CD  . GLN D 489 ? 0.9814 1.3684 1.1326 0.1516  0.0732  -0.0939 489 GLN D CD  
18494 O OE1 . GLN D 489 ? 0.9859 1.3768 1.1382 0.1710  0.0601  -0.0885 489 GLN D OE1 
18495 N NE2 . GLN D 489 ? 1.0107 1.4317 1.1808 0.1376  0.0791  -0.1045 489 GLN D NE2 
18496 N N   . SER D 490 ? 0.9762 1.2222 1.0887 0.1649  0.0951  -0.0956 490 SER D N   
18497 C CA  . SER D 490 ? 1.0604 1.2946 1.1718 0.1753  0.0984  -0.1066 490 SER D CA  
18498 C C   . SER D 490 ? 1.1608 1.4015 1.2656 0.1627  0.1078  -0.1127 490 SER D C   
18499 O O   . SER D 490 ? 1.3543 1.6084 1.4592 0.1693  0.1150  -0.1229 490 SER D O   
18500 C CB  . SER D 490 ? 1.0276 1.2177 1.1296 0.1801  0.0921  -0.1047 490 SER D CB  
18501 O OG  . SER D 490 ? 1.2921 1.4702 1.3958 0.1907  0.0837  -0.0936 490 SER D OG  
18502 N N   . PHE D 491 ? 1.1510 1.3829 1.2495 0.1455  0.1084  -0.1058 491 PHE D N   
18503 C CA  . PHE D 491 ? 1.0174 1.2534 1.1094 0.1349  0.1151  -0.1076 491 PHE D CA  
18504 C C   . PHE D 491 ? 1.0742 1.3406 1.1760 0.1261  0.1243  -0.1046 491 PHE D C   
18505 O O   . PHE D 491 ? 1.2904 1.5743 1.3920 0.1273  0.1335  -0.1087 491 PHE D O   
18506 C CB  . PHE D 491 ? 0.9615 1.1731 1.0478 0.1231  0.1105  -0.1025 491 PHE D CB  
18507 C CG  . PHE D 491 ? 1.7079 1.8902 1.7885 0.1280  0.1026  -0.1077 491 PHE D CG  
18508 C CD1 . PHE D 491 ? 1.7463 1.9213 1.8164 0.1314  0.1004  -0.1184 491 PHE D CD1 
18509 C CD2 . PHE D 491 ? 1.6803 1.8412 1.7648 0.1275  0.0976  -0.1019 491 PHE D CD2 
18510 C CE1 . PHE D 491 ? 1.3383 1.4856 1.4060 0.1333  0.0923  -0.1263 491 PHE D CE1 
18511 C CE2 . PHE D 491 ? 1.4203 1.5511 1.5033 0.1291  0.0918  -0.1070 491 PHE D CE2 
18512 C CZ  . PHE D 491 ? 1.2250 1.3494 1.3017 0.1314  0.0886  -0.1206 491 PHE D CZ  
18513 N N   . ALA D 492 ? 1.0053 1.2772 1.1150 0.1163  0.1231  -0.0984 492 ALA D N   
18514 C CA  . ALA D 492 ? 0.7865 1.0838 0.9085 0.1054  0.1312  -0.0981 492 ALA D CA  
18515 C C   . ALA D 492 ? 0.8665 1.1923 1.0037 0.1113  0.1281  -0.1021 492 ALA D C   
18516 O O   . ALA D 492 ? 0.9324 1.2580 1.0693 0.1103  0.1198  -0.0994 492 ALA D O   
18517 C CB  . ALA D 492 ? 0.8111 1.0978 0.9332 0.0908  0.1318  -0.0929 492 ALA D CB  
18518 N N   . PRO D 493 ? 0.8539 1.2068 1.0044 0.1180  0.1341  -0.1087 493 PRO D N   
18519 C CA  . PRO D 493 ? 0.9396 1.3252 1.1106 0.1255  0.1283  -0.1135 493 PRO D CA  
18520 C C   . PRO D 493 ? 0.9398 1.3467 1.1233 0.1120  0.1249  -0.1145 493 PRO D C   
18521 O O   . PRO D 493 ? 0.9462 1.3713 1.1375 0.1199  0.1124  -0.1159 493 PRO D O   
18522 C CB  . PRO D 493 ? 0.9673 1.3812 1.1548 0.1316  0.1402  -0.1215 493 PRO D CB  
18523 C CG  . PRO D 493 ? 1.0590 1.4609 1.2343 0.1189  0.1549  -0.1187 493 PRO D CG  
18524 C CD  . PRO D 493 ? 0.8641 1.2248 1.0136 0.1164  0.1481  -0.1115 493 PRO D CD  
18525 N N   . ALA D 494 ? 0.7469 1.1510 0.9319 0.0926  0.1347  -0.1144 494 ALA D N   
18526 C CA  . ALA D 494 ? 0.7117 1.1342 0.9090 0.0779  0.1326  -0.1196 494 ALA D CA  
18527 C C   . ALA D 494 ? 0.7126 1.1108 0.8900 0.0721  0.1254  -0.1158 494 ALA D C   
18528 O O   . ALA D 494 ? 0.7674 1.1802 0.9496 0.0616  0.1217  -0.1225 494 ALA D O   
18529 C CB  . ALA D 494 ? 0.7008 1.1313 0.9140 0.0595  0.1490  -0.1230 494 ALA D CB  
18530 N N   . HIS D 495 ? 0.7654 1.1289 0.9215 0.0778  0.1239  -0.1069 495 HIS D N   
18531 C CA  . HIS D 495 ? 0.7956 1.1376 0.9349 0.0717  0.1208  -0.1030 495 HIS D CA  
18532 C C   . HIS D 495 ? 0.8128 1.1611 0.9395 0.0797  0.1073  -0.1006 495 HIS D C   
18533 O O   . HIS D 495 ? 0.7366 1.0846 0.8598 0.0962  0.0982  -0.0953 495 HIS D O   
18534 C CB  . HIS D 495 ? 0.6156 0.9227 0.7419 0.0739  0.1238  -0.0949 495 HIS D CB  
18535 C CG  . HIS D 495 ? 0.7432 1.0308 0.8560 0.0679  0.1232  -0.0908 495 HIS D CG  
18536 N ND1 . HIS D 495 ? 0.8091 1.0956 0.9251 0.0537  0.1313  -0.0953 495 HIS D ND1 
18537 C CD2 . HIS D 495 ? 0.9550 1.2239 1.0521 0.0741  0.1176  -0.0829 495 HIS D CD2 
18538 C CE1 . HIS D 495 ? 0.8617 1.1322 0.9635 0.0519  0.1312  -0.0910 495 HIS D CE1 
18539 N NE2 . HIS D 495 ? 0.8545 1.1135 0.9442 0.0629  0.1234  -0.0822 495 HIS D NE2 
18540 N N   . VAL D 496 ? 0.8726 1.2241 0.9900 0.0687  0.1063  -0.1041 496 VAL D N   
18541 C CA  . VAL D 496 ? 0.8361 1.1925 0.9331 0.0743  0.0939  -0.1001 496 VAL D CA  
18542 C C   . VAL D 496 ? 0.9774 1.3111 1.0538 0.0624  0.1018  -0.0984 496 VAL D C   
18543 O O   . VAL D 496 ? 1.0111 1.3467 1.0957 0.0474  0.1119  -0.1090 496 VAL D O   
18544 C CB  . VAL D 496 ? 0.7130 1.1109 0.8201 0.0723  0.0833  -0.1116 496 VAL D CB  
18545 C CG1 . VAL D 496 ? 0.8003 1.2041 0.8809 0.0825  0.0667  -0.1042 496 VAL D CG1 
18546 C CG2 . VAL D 496 ? 0.7488 1.1757 0.8871 0.0799  0.0810  -0.1170 496 VAL D CG2 
18547 N N   . CYS D 497 ? 0.9228 1.2338 0.9746 0.0688  0.0990  -0.0853 497 CYS D N   
18548 C CA  . CYS D 497 ? 0.7233 1.0152 0.7564 0.0576  0.1094  -0.0833 497 CYS D CA  
18549 C C   . CYS D 497 ? 0.8647 1.1683 0.8681 0.0554  0.1034  -0.0838 497 CYS D C   
18550 O O   . CYS D 497 ? 1.1346 1.4354 1.1162 0.0675  0.0920  -0.0703 497 CYS D O   
18551 C CB  . CYS D 497 ? 0.8065 1.0646 0.8297 0.0626  0.1135  -0.0677 497 CYS D CB  
18552 S SG  . CYS D 497 ? 0.8454 1.0823 0.8907 0.0528  0.1288  -0.0705 497 CYS D SG  
18553 N N   . ILE D 498 ? 0.8602 1.1753 0.8606 0.0409  0.1108  -0.0991 498 ILE D N   
18554 C CA  . ILE D 498 ? 0.8277 1.1553 0.7945 0.0371  0.1060  -0.1032 498 ILE D CA  
18555 C C   . ILE D 498 ? 0.9303 1.2323 0.8719 0.0300  0.1223  -0.0966 498 ILE D C   
18556 O O   . ILE D 498 ? 0.9008 1.1973 0.8518 0.0172  0.1388  -0.1097 498 ILE D O   
18557 C CB  . ILE D 498 ? 0.7914 1.1482 0.7711 0.0245  0.1044  -0.1283 498 ILE D CB  
18558 C CG1 . ILE D 498 ? 0.7845 1.1693 0.7967 0.0296  0.0913  -0.1344 498 ILE D CG1 
18559 C CG2 . ILE D 498 ? 0.7221 1.0950 0.6633 0.0199  0.0973  -0.1366 498 ILE D CG2 
18560 C CD1 . ILE D 498 ? 0.7858 1.1914 0.7888 0.0472  0.0691  -0.1235 498 ILE D CD1 
18561 N N   . VAL D 499 ? 0.7659 1.0517 0.6771 0.0387  0.1189  -0.0758 499 VAL D N   
18562 C CA  . VAL D 499 ? 0.8765 1.1370 0.7660 0.0311  0.1376  -0.0664 499 VAL D CA  
18563 C C   . VAL D 499 ? 1.0756 1.3478 0.9213 0.0241  0.1409  -0.0723 499 VAL D C   
18564 O O   . VAL D 499 ? 1.1223 1.4055 0.9341 0.0331  0.1239  -0.0631 499 VAL D O   
18565 C CB  . VAL D 499 ? 0.8986 1.1307 0.7787 0.0416  0.1353  -0.0398 499 VAL D CB  
18566 C CG1 . VAL D 499 ? 1.1107 1.3182 0.9701 0.0324  0.1555  -0.0278 499 VAL D CG1 
18567 C CG2 . VAL D 499 ? 0.9329 1.1540 0.8530 0.0481  0.1319  -0.0381 499 VAL D CG2 
18568 N N   . THR D 500 ? 1.0343 1.3049 0.8799 0.0097  0.1617  -0.0877 500 THR D N   
18569 C CA  . THR D 500 ? 1.0029 1.2831 0.8021 0.0021  0.1687  -0.0961 500 THR D CA  
18570 C C   . THR D 500 ? 1.1379 1.3952 0.9251 -0.0057 0.1959  -0.0866 500 THR D C   
18571 O O   . THR D 500 ? 1.0995 1.3399 0.9250 -0.0070 0.2069  -0.0811 500 THR D O   
18572 C CB  . THR D 500 ? 1.0076 1.3107 0.8182 -0.0087 0.1705  -0.1294 500 THR D CB  
18573 O OG1 . THR D 500 ? 1.1327 1.4226 0.9709 -0.0189 0.1958  -0.1421 500 THR D OG1 
18574 C CG2 . THR D 500 ? 1.1837 1.5061 1.0306 -0.0053 0.1513  -0.1404 500 THR D CG2 
18575 N N   . PRO D 501 ? 1.1858 1.4435 0.9219 -0.0111 0.2071  -0.0842 501 PRO D N   
18576 C CA  . PRO D 501 ? 1.2467 1.4846 0.9730 -0.0194 0.2360  -0.0735 501 PRO D CA  
18577 C C   . PRO D 501 ? 1.1263 1.3603 0.9079 -0.0281 0.2575  -0.0900 501 PRO D C   
18578 O O   . PRO D 501 ? 1.1985 1.4152 0.9998 -0.0309 0.2726  -0.0757 501 PRO D O   
18579 C CB  . PRO D 501 ? 1.2154 1.4662 0.8826 -0.0264 0.2460  -0.0837 501 PRO D CB  
18580 C CG  . PRO D 501 ? 1.2770 1.5454 0.9070 -0.0161 0.2143  -0.0806 501 PRO D CG  
18581 C CD  . PRO D 501 ? 1.2315 1.5109 0.9156 -0.0097 0.1928  -0.0916 501 PRO D CD  
18582 N N   . GLU D 502 ? 1.1646 1.4140 0.9716 -0.0320 0.2578  -0.1189 502 GLU D N   
18583 C CA  . GLU D 502 ? 1.1756 1.4215 1.0347 -0.0374 0.2764  -0.1345 502 GLU D CA  
18584 C C   . GLU D 502 ? 1.1821 1.4226 1.0942 -0.0307 0.2622  -0.1306 502 GLU D C   
18585 O O   . GLU D 502 ? 1.1720 1.4040 1.1252 -0.0316 0.2737  -0.1293 502 GLU D O   
18586 C CB  . GLU D 502 ? 1.2211 1.4805 1.0784 -0.0450 0.2876  -0.1677 502 GLU D CB  
18587 C CG  . GLU D 502 ? 1.3295 1.5948 1.1317 -0.0521 0.3051  -0.1744 502 GLU D CG  
18588 C CD  . GLU D 502 ? 1.3604 1.6366 1.1601 -0.0601 0.3196  -0.2111 502 GLU D CD  
18589 O OE1 . GLU D 502 ? 1.4312 1.7024 1.2652 -0.0637 0.3448  -0.2247 502 GLU D OE1 
18590 O OE2 . GLU D 502 ? 1.2797 1.5702 1.0454 -0.0625 0.3052  -0.2277 502 GLU D OE2 
18591 N N   . ARG D 503 ? 1.0869 1.3347 0.9982 -0.0237 0.2374  -0.1287 503 ARG D N   
18592 C CA  . ARG D 503 ? 0.8980 1.1420 0.8521 -0.0172 0.2248  -0.1246 503 ARG D CA  
18593 C C   . ARG D 503 ? 1.0286 1.2625 0.9740 -0.0072 0.2097  -0.0997 503 ARG D C   
18594 O O   . ARG D 503 ? 1.0805 1.3236 1.0124 0.0006  0.1901  -0.0953 503 ARG D O   
18595 C CB  . ARG D 503 ? 1.0129 1.2729 0.9796 -0.0176 0.2120  -0.1425 503 ARG D CB  
18596 C CG  . ARG D 503 ? 1.0360 1.2927 1.0436 -0.0121 0.2027  -0.1387 503 ARG D CG  
18597 C CD  . ARG D 503 ? 1.0964 1.3714 1.1109 -0.0129 0.1887  -0.1510 503 ARG D CD  
18598 N NE  . ARG D 503 ? 1.1068 1.3773 1.1604 -0.0171 0.1951  -0.1618 503 ARG D NE  
18599 C CZ  . ARG D 503 ? 1.1391 1.4060 1.2189 -0.0117 0.1890  -0.1531 503 ARG D CZ  
18600 N NH1 . ARG D 503 ? 0.9496 1.2179 1.0236 -0.0015 0.1763  -0.1366 503 ARG D NH1 
18601 N NH2 . ARG D 503 ? 1.1492 1.4092 1.2592 -0.0158 0.1963  -0.1606 503 ARG D NH2 
18602 N N   . LEU D 504 ? 1.1014 1.3172 1.0594 -0.0075 0.2190  -0.0852 504 LEU D N   
18603 C CA  . LEU D 504 ? 0.9923 1.1924 0.9434 0.0012  0.2068  -0.0629 504 LEU D CA  
18604 C C   . LEU D 504 ? 0.8755 1.0757 0.8600 0.0096  0.1914  -0.0642 504 LEU D C   
18605 O O   . LEU D 504 ? 0.9801 1.1917 0.9905 0.0077  0.1917  -0.0794 504 LEU D O   
18606 C CB  . LEU D 504 ? 0.8864 1.0668 0.8425 -0.0054 0.2238  -0.0497 504 LEU D CB  
18607 C CG  . LEU D 504 ? 0.8242 0.9994 0.8301 -0.0081 0.2288  -0.0539 504 LEU D CG  
18608 C CD1 . LEU D 504 ? 0.8947 1.0515 0.9065 -0.0151 0.2415  -0.0393 504 LEU D CD1 
18609 C CD2 . LEU D 504 ? 0.9219 1.1123 0.9548 -0.0140 0.2415  -0.0740 504 LEU D CD2 
18610 N N   . GLY D 505 ? 0.8494 1.0353 0.8317 0.0187  0.1798  -0.0486 505 GLY D N   
18611 C CA  . GLY D 505 ? 0.8607 1.0464 0.8687 0.0276  0.1665  -0.0502 505 GLY D CA  
18612 C C   . GLY D 505 ? 0.8743 1.0581 0.9191 0.0225  0.1734  -0.0586 505 GLY D C   
18613 O O   . GLY D 505 ? 0.8496 1.0271 0.9057 0.0137  0.1874  -0.0590 505 GLY D O   
18614 N N   . LEU D 506 ? 0.9636 1.1547 1.0273 0.0285  0.1638  -0.0647 506 LEU D N   
18615 C CA  . LEU D 506 ? 0.8202 1.0102 0.9147 0.0262  0.1669  -0.0706 506 LEU D CA  
18616 C C   . LEU D 506 ? 0.8666 1.0396 0.9737 0.0266  0.1652  -0.0634 506 LEU D C   
18617 O O   . LEU D 506 ? 0.6833 0.8559 0.8149 0.0217  0.1705  -0.0667 506 LEU D O   
18618 C CB  . LEU D 506 ? 0.8068 1.0078 0.9112 0.0323  0.1581  -0.0762 506 LEU D CB  
18619 C CG  . LEU D 506 ? 0.6967 0.9161 0.7933 0.0309  0.1574  -0.0843 506 LEU D CG  
18620 C CD1 . LEU D 506 ? 0.8298 1.0580 0.9412 0.0343  0.1532  -0.0882 506 LEU D CD1 
18621 C CD2 . LEU D 506 ? 0.8726 1.0968 0.9704 0.0203  0.1700  -0.0942 506 LEU D CD2 
18622 N N   . CYS D 507 ? 0.9067 1.0658 0.9995 0.0327  0.1571  -0.0545 507 CYS D N   
18623 C CA  . CYS D 507 ? 0.8493 0.9888 0.9537 0.0314  0.1551  -0.0496 507 CYS D CA  
18624 C C   . CYS D 507 ? 0.7527 0.8850 0.8653 0.0183  0.1701  -0.0455 507 CYS D C   
18625 O O   . CYS D 507 ? 1.0302 1.1563 1.1680 0.0124  0.1714  -0.0473 507 CYS D O   
18626 C CB  . CYS D 507 ? 0.8483 0.9700 0.9349 0.0413  0.1453  -0.0412 507 CYS D CB  
18627 S SG  . CYS D 507 ? 0.9058 1.0232 0.9562 0.0445  0.1477  -0.0273 507 CYS D SG  
18628 N N   . GLY D 508 ? 0.7454 0.8810 0.8370 0.0134  0.1817  -0.0410 508 GLY D N   
18629 C CA  . GLY D 508 ? 0.9580 1.0890 1.0534 0.0006  0.2002  -0.0367 508 GLY D CA  
18630 C C   . GLY D 508 ? 1.0039 1.1100 1.0771 -0.0022 0.2044  -0.0194 508 GLY D C   
18631 O O   . GLY D 508 ? 1.0818 1.1827 1.1522 -0.0141 0.2227  -0.0128 508 GLY D O   
18632 N N   . ALA D 509 ? 0.8073 0.8964 0.8653 0.0089  0.1891  -0.0111 509 ALA D N   
18633 C CA  . ALA D 509 ? 0.9355 0.9942 0.9723 0.0090  0.1912  0.0080  509 ALA D CA  
18634 C C   . ALA D 509 ? 1.2282 1.2853 1.2208 0.0206  0.1844  0.0207  509 ALA D C   
18635 O O   . ALA D 509 ? 1.2621 1.2911 1.2343 0.0254  0.1824  0.0393  509 ALA D O   
18636 C CB  . ALA D 509 ? 1.1512 1.1869 1.2070 0.0145  0.1789  0.0077  509 ALA D CB  
18637 N N   . VAL D 510 ? 1.1026 1.1887 1.0815 0.0252  0.1799  0.0110  510 VAL D N   
18638 C CA  . VAL D 510 ? 0.9021 0.9945 0.8416 0.0360  0.1700  0.0201  510 VAL D CA  
18639 C C   . VAL D 510 ? 1.1003 1.2168 1.0177 0.0275  0.1802  0.0123  510 VAL D C   
18640 O O   . VAL D 510 ? 1.0144 1.1579 0.9419 0.0280  0.1754  -0.0060 510 VAL D O   
18641 C CB  . VAL D 510 ? 0.7792 0.8862 0.7264 0.0530  0.1483  0.0127  510 VAL D CB  
18642 C CG1 . VAL D 510 ? 0.9299 1.0503 0.8420 0.0645  0.1356  0.0205  510 VAL D CG1 
18643 C CG2 . VAL D 510 ? 1.1886 1.2705 1.1543 0.0628  0.1396  0.0177  510 VAL D CG2 
18644 N N   . SER D 511 ? 1.1371 1.2424 1.0235 0.0190  0.1957  0.0255  511 SER D N   
18645 C CA  . SER D 511 ? 1.0117 1.1377 0.8701 0.0108  0.2074  0.0170  511 SER D CA  
18646 C C   . SER D 511 ? 1.1970 1.3337 1.0086 0.0224  0.1902  0.0243  511 SER D C   
18647 O O   . SER D 511 ? 1.3346 1.4608 1.1393 0.0373  0.1713  0.0387  511 SER D O   
18648 C CB  . SER D 511 ? 1.1619 1.2731 1.0064 -0.0041 0.2345  0.0277  511 SER D CB  
18649 O OG  . SER D 511 ? 1.2248 1.3123 1.0238 -0.0005 0.2348  0.0553  511 SER D OG  
18650 N N   . TRP D 512 ? 1.2736 1.4323 1.0539 0.0165  0.1956  0.0132  512 TRP D N   
18651 C CA  . TRP D 512 ? 1.3615 1.5354 1.0958 0.0269  0.1766  0.0183  512 TRP D CA  
18652 C C   . TRP D 512 ? 1.3813 1.5273 1.0715 0.0353  0.1736  0.0527  512 TRP D C   
18653 O O   . TRP D 512 ? 1.2984 1.4493 0.9638 0.0516  0.1499  0.0648  512 TRP D O   
18654 C CB  . TRP D 512 ? 1.1747 1.3747 0.8799 0.0162  0.1855  -0.0024 512 TRP D CB  
18655 C CG  . TRP D 512 ? 1.3261 1.5469 0.9830 0.0256  0.1635  -0.0004 512 TRP D CG  
18656 C CD1 . TRP D 512 ? 1.4133 1.6653 1.0812 0.0328  0.1388  -0.0176 512 TRP D CD1 
18657 C CD2 . TRP D 512 ? 1.3569 1.5705 0.9473 0.0289  0.1630  0.0211  512 TRP D CD2 
18658 N NE1 . TRP D 512 ? 1.4174 1.6856 1.0324 0.0408  0.1206  -0.0104 512 TRP D NE1 
18659 C CE2 . TRP D 512 ? 1.3751 1.6190 0.9385 0.0396  0.1343  0.0146  512 TRP D CE2 
18660 C CE3 . TRP D 512 ? 1.3410 1.5262 0.8918 0.0232  0.1844  0.0462  512 TRP D CE3 
18661 C CZ2 . TRP D 512 ? 1.4502 1.6968 0.9447 0.0468  0.1237  0.0329  512 TRP D CZ2 
18662 C CZ3 . TRP D 512 ? 1.3702 1.5547 0.8505 0.0295  0.1771  0.0662  512 TRP D CZ3 
18663 C CH2 . TRP D 512 ? 1.5053 1.7203 0.9560 0.0421  0.1456  0.0598  512 TRP D CH2 
18664 N N   . LEU D 513 ? 1.3509 1.4676 1.0350 0.0244  0.1979  0.0690  513 LEU D N   
18665 C CA  . LEU D 513 ? 1.4989 1.5816 1.1426 0.0294  0.2003  0.1045  513 LEU D CA  
18666 C C   . LEU D 513 ? 1.5138 1.5684 1.1865 0.0438  0.1841  0.1202  513 LEU D C   
18667 O O   . LEU D 513 ? 1.4926 1.5292 1.1346 0.0599  0.1683  0.1452  513 LEU D O   
18668 C CB  . LEU D 513 ? 1.4791 1.5409 1.1153 0.0095  0.2356  0.1145  513 LEU D CB  
18669 C CG  . LEU D 513 ? 1.5374 1.6253 1.1487 -0.0057 0.2583  0.0960  513 LEU D CG  
18670 C CD1 . LEU D 513 ? 1.4412 1.5414 1.1115 -0.0208 0.2792  0.0695  513 LEU D CD1 
18671 C CD2 . LEU D 513 ? 1.4397 1.5079 0.9921 -0.0144 0.2816  0.1223  513 LEU D CD2 
18672 N N   . ASP D 514 ? 1.4754 1.5261 1.2063 0.0391  0.1873  0.1050  514 ASP D N   
18673 C CA  . ASP D 514 ? 1.3074 1.3322 1.0686 0.0514  0.1739  0.1137  514 ASP D CA  
18674 C C   . ASP D 514 ? 1.3212 1.3662 1.0848 0.0738  0.1440  0.1080  514 ASP D C   
18675 O O   . ASP D 514 ? 1.3897 1.4114 1.1552 0.0907  0.1299  0.1236  514 ASP D O   
18676 C CB  . ASP D 514 ? 1.2041 1.2263 1.0228 0.0400  0.1835  0.0949  514 ASP D CB  
18677 C CG  . ASP D 514 ? 1.4050 1.4167 1.2338 0.0175  0.2124  0.0959  514 ASP D CG  
18678 O OD1 . ASP D 514 ? 1.5887 1.5751 1.3860 0.0109  0.2272  0.1196  514 ASP D OD1 
18679 O OD2 . ASP D 514 ? 1.0502 1.0799 0.9192 0.0070  0.2206  0.0740  514 ASP D OD2 
18680 N N   . ALA D 515 ? 1.2471 1.3351 1.0145 0.0737  0.1354  0.0847  515 ALA D N   
18681 C CA  . ALA D 515 ? 1.2415 1.3562 1.0167 0.0923  0.1090  0.0767  515 ALA D CA  
18682 C C   . ALA D 515 ? 1.4595 1.5739 1.1875 0.1090  0.0914  0.0993  515 ALA D C   
18683 O O   . ALA D 515 ? 1.3729 1.4885 1.1094 0.1303  0.0700  0.1069  515 ALA D O   
18684 C CB  . ALA D 515 ? 1.2466 1.4053 1.0376 0.0839  0.1072  0.0467  515 ALA D CB  
18685 N N   . LYS D 516 ? 1.5502 1.6638 1.2276 0.1005  0.1004  0.1103  516 LYS D N   
18686 C CA  . LYS D 516 ? 1.4768 1.5897 1.1005 0.1161  0.0832  0.1346  516 LYS D CA  
18687 C C   . LYS D 516 ? 1.5599 1.6225 1.1765 0.1305  0.0812  0.1694  516 LYS D C   
18688 O O   . LYS D 516 ? 1.5935 1.6551 1.1986 0.1548  0.0566  0.1858  516 LYS D O   
18689 C CB  . LYS D 516 ? 1.5289 1.6475 1.0952 0.1011  0.0985  0.1385  516 LYS D CB  
18690 C CG  . LYS D 516 ? 1.6706 1.7905 1.1709 0.1169  0.0798  0.1649  516 LYS D CG  
18691 C CD  . LYS D 516 ? 1.6265 1.7168 1.0657 0.1047  0.1042  0.1904  516 LYS D CD  
18692 C CE  . LYS D 516 ? 1.5097 1.6320 0.9125 0.0866  0.1180  0.1682  516 LYS D CE  
18693 N NZ  . LYS D 516 ? 1.5887 1.7367 0.9252 0.0988  0.0940  0.1758  516 LYS D NZ  
18694 N N   . ALA D 517 ? 1.5996 1.6207 1.2272 0.1158  0.1068  0.1795  517 ALA D N   
18695 C CA  . ALA D 517 ? 1.5536 1.5202 1.1792 0.1252  0.1090  0.2106  517 ALA D CA  
18696 C C   . ALA D 517 ? 1.6291 1.5899 1.2996 0.1466  0.0883  0.2046  517 ALA D C   
18697 O O   . ALA D 517 ? 1.6074 1.5352 1.2673 0.1669  0.0761  0.2303  517 ALA D O   
18698 C CB  . ALA D 517 ? 1.4520 1.3838 1.0944 0.1008  0.1409  0.2138  517 ALA D CB  
18699 N N   . THR D 518 ? 1.5547 1.5463 1.2742 0.1430  0.0853  0.1713  518 THR D N   
18700 C CA  . THR D 518 ? 1.4607 1.4527 1.2228 0.1620  0.0689  0.1610  518 THR D CA  
18701 C C   . THR D 518 ? 1.5874 1.6030 1.3353 0.1902  0.0402  0.1696  518 THR D C   
18702 O O   . THR D 518 ? 1.7162 1.7082 1.4761 0.2131  0.0273  0.1826  518 THR D O   
18703 C CB  . THR D 518 ? 1.3287 1.3554 1.1362 0.1510  0.0727  0.1251  518 THR D CB  
18704 O OG1 . THR D 518 ? 1.4477 1.4563 1.2698 0.1269  0.0965  0.1178  518 THR D OG1 
18705 C CG2 . THR D 518 ? 1.2830 1.3126 1.1315 0.1692  0.0593  0.1126  518 THR D CG2 
18706 N N   . LEU D 519 ? 1.4873 1.5502 1.2123 0.1888  0.0296  0.1609  519 LEU D N   
18707 C CA  . LEU D 519 ? 1.5203 1.6159 1.2343 0.2138  -0.0003 0.1662  519 LEU D CA  
18708 C C   . LEU D 519 ? 1.6594 1.7184 1.3280 0.2335  -0.0112 0.2066  519 LEU D C   
18709 O O   . LEU D 519 ? 1.6097 1.6752 1.2852 0.2625  -0.0360 0.2176  519 LEU D O   
18710 C CB  . LEU D 519 ? 1.3122 1.4642 1.0084 0.2025  -0.0074 0.1458  519 LEU D CB  
18711 C CG  . LEU D 519 ? 1.3165 1.5141 1.0038 0.2243  -0.0403 0.1459  519 LEU D CG  
18712 C CD1 . LEU D 519 ? 1.5665 1.7908 1.3134 0.2422  -0.0556 0.1292  519 LEU D CD1 
18713 C CD2 . LEU D 519 ? 1.2493 1.4955 0.9142 0.2077  -0.0441 0.1241  519 LEU D CD2 
18714 N N   . GLU D 520 ? 1.7209 1.7414 1.3445 0.2187  0.0082  0.2298  520 GLU D N   
18715 C CA  . GLU D 520 ? 1.8085 1.7875 1.3829 0.2351  0.0015  0.2728  520 GLU D CA  
18716 C C   . GLU D 520 ? 1.8091 1.7344 1.4146 0.2534  0.0002  0.2902  520 GLU D C   
18717 O O   . GLU D 520 ? 1.7760 1.6864 1.3694 0.2832  -0.0217 0.3152  520 GLU D O   
18718 C CB  . GLU D 520 ? 1.7974 1.7453 1.3199 0.2107  0.0295  0.2926  520 GLU D CB  
18719 C CG  . GLU D 520 ? 1.8031 1.7969 1.2818 0.1957  0.0313  0.2797  520 GLU D CG  
18720 C CD  . GLU D 520 ? 2.1114 2.1346 1.5387 0.2176  0.0003  0.2949  520 GLU D CD  
18721 O OE1 . GLU D 520 ? 2.2253 2.2142 1.6209 0.2401  -0.0130 0.3336  520 GLU D OE1 
18722 O OE2 . GLU D 520 ? 2.1328 2.2126 1.5520 0.2123  -0.0117 0.2679  520 GLU D OE2 
18723 N N   . LEU D 521 ? 1.7597 1.6562 1.4062 0.2364  0.0225  0.2759  521 LEU D N   
18724 C CA  . LEU D 521 ? 1.7222 1.5642 1.3999 0.2493  0.0245  0.2867  521 LEU D CA  
18725 C C   . LEU D 521 ? 1.7926 1.6581 1.5190 0.2758  0.0026  0.2663  521 LEU D C   
18726 O O   . LEU D 521 ? 2.0164 1.8408 1.7589 0.2979  -0.0043 0.2802  521 LEU D O   
18727 C CB  . LEU D 521 ? 1.6645 1.4725 1.3685 0.2197  0.0545  0.2751  521 LEU D CB  
18728 C CG  . LEU D 521 ? 1.8447 1.6280 1.5091 0.1920  0.0811  0.2947  521 LEU D CG  
18729 C CD1 . LEU D 521 ? 1.7990 1.5780 1.5006 0.1610  0.1070  0.2708  521 LEU D CD1 
18730 C CD2 . LEU D 521 ? 1.9800 1.6973 1.6099 0.2004  0.0861  0.3394  521 LEU D CD2 
18731 N N   . ASN D 522 ? 1.7758 1.7054 1.5270 0.2736  -0.0063 0.2334  522 ASN D N   
18732 C CA  . ASN D 522 ? 1.7225 1.6809 1.5210 0.2969  -0.0238 0.2128  522 ASN D CA  
18733 C C   . ASN D 522 ? 1.7357 1.7690 1.5366 0.3010  -0.0423 0.1944  522 ASN D C   
18734 O O   . ASN D 522 ? 1.7298 1.8011 1.5486 0.2799  -0.0332 0.1653  522 ASN D O   
18735 C CB  . ASN D 522 ? 1.6780 1.6279 1.5243 0.2839  -0.0072 0.1834  522 ASN D CB  
18736 C CG  . ASN D 522 ? 1.8800 1.8473 1.7723 0.3093  -0.0202 0.1652  522 ASN D CG  
18737 O OD1 . ASN D 522 ? 1.8496 1.8347 1.7457 0.3389  -0.0419 0.1747  522 ASN D OD1 
18738 N ND2 . ASN D 522 ? 1.9293 1.8944 1.8578 0.2991  -0.0072 0.1382  522 ASN D ND2 
18739 N N   . PRO D 523 ? 1.6890 1.7447 1.4737 0.3279  -0.0693 0.2108  523 PRO D N   
18740 C CA  . PRO D 523 ? 1.6509 1.7816 1.4423 0.3299  -0.0887 0.1907  523 PRO D CA  
18741 C C   . PRO D 523 ? 1.5349 1.7094 1.3884 0.3289  -0.0875 0.1534  523 PRO D C   
18742 O O   . PRO D 523 ? 1.3622 1.5908 1.2261 0.3137  -0.0895 0.1289  523 PRO D O   
18743 C CB  . PRO D 523 ? 1.7319 1.8728 1.5047 0.3649  -0.1205 0.2169  523 PRO D CB  
18744 C CG  . PRO D 523 ? 1.7673 1.8338 1.5015 0.3739  -0.1140 0.2571  523 PRO D CG  
18745 C CD  . PRO D 523 ? 1.6879 1.7026 1.4496 0.3578  -0.0848 0.2486  523 PRO D CD  
18746 N N   . THR D 524 ? 1.5620 1.7110 1.4554 0.3441  -0.0827 0.1490  524 THR D N   
18747 C CA  . THR D 524 ? 1.5467 1.7317 1.4955 0.3443  -0.0782 0.1159  524 THR D CA  
18748 C C   . THR D 524 ? 1.6294 1.7830 1.5881 0.3179  -0.0499 0.1001  524 THR D C   
18749 O O   . THR D 524 ? 1.5754 1.7170 1.5688 0.3248  -0.0419 0.0856  524 THR D O   
18750 C CB  . THR D 524 ? 1.5382 1.7198 1.5235 0.3810  -0.0917 0.1187  524 THR D CB  
18751 O OG1 . THR D 524 ? 1.4282 1.5364 1.4073 0.3882  -0.0803 0.1347  524 THR D OG1 
18752 C CG2 . THR D 524 ? 1.4828 1.6948 1.4604 0.4106  -0.1227 0.1373  524 THR D CG2 
18753 N N   . GLY D 525 ? 1.5610 1.7037 1.4890 0.2891  -0.0356 0.1021  525 GLY D N   
18754 C CA  . GLY D 525 ? 1.4387 1.5554 1.3750 0.2638  -0.0112 0.0890  525 GLY D CA  
18755 C C   . GLY D 525 ? 1.3103 1.4726 1.2661 0.2427  -0.0028 0.0605  525 GLY D C   
18756 O O   . GLY D 525 ? 1.3144 1.5288 1.2821 0.2465  -0.0145 0.0482  525 GLY D O   
18757 N N   . PRO D 526 ? 1.0765 1.2203 1.0382 0.2201  0.0171  0.0495  526 PRO D N   
18758 C CA  . PRO D 526 ? 1.1329 1.3147 1.1125 0.2011  0.0257  0.0251  526 PRO D CA  
18759 C C   . PRO D 526 ? 1.2747 1.4836 1.2306 0.1848  0.0257  0.0238  526 PRO D C   
18760 O O   . PRO D 526 ? 1.3059 1.5559 1.2780 0.1761  0.0252  0.0047  526 PRO D O   
18761 C CB  . PRO D 526 ? 1.2263 1.3757 1.2152 0.1846  0.0441  0.0182  526 PRO D CB  
18762 C CG  . PRO D 526 ? 1.2858 1.3832 1.2682 0.1949  0.0448  0.0347  526 PRO D CG  
18763 C CD  . PRO D 526 ? 1.0964 1.1851 1.0517 0.2105  0.0319  0.0587  526 PRO D CD  
18764 N N   . CYS D 527 ? 1.2702 1.4547 1.1873 0.1796  0.0280  0.0431  527 CYS D N   
18765 C CA  . CYS D 527 ? 1.1408 1.3479 1.0292 0.1644  0.0297  0.0405  527 CYS D CA  
18766 C C   . CYS D 527 ? 1.3399 1.5781 1.2076 0.1804  0.0062  0.0478  527 CYS D C   
18767 O O   . CYS D 527 ? 1.2307 1.4489 1.0789 0.2001  -0.0063 0.0714  527 CYS D O   
18768 C CB  . CYS D 527 ? 0.9675 1.1367 0.8233 0.1491  0.0473  0.0559  527 CYS D CB  
18769 S SG  . CYS D 527 ? 1.2030 1.3414 1.0877 0.1301  0.0719  0.0467  527 CYS D SG  
18770 N N   . GLN D 528 ? 1.2677 1.5543 1.1406 0.1718  -0.0007 0.0275  528 GLN D N   
18771 C CA  . GLN D 528 ? 1.2552 1.5812 1.1114 0.1840  -0.0256 0.0288  528 GLN D CA  
18772 C C   . GLN D 528 ? 1.3098 1.6576 1.1347 0.1630  -0.0222 0.0159  528 GLN D C   
18773 O O   . GLN D 528 ? 1.3034 1.6490 1.1386 0.1407  -0.0021 -0.0020 528 GLN D O   
18774 C CB  . GLN D 528 ? 1.2902 1.6632 1.1952 0.1958  -0.0412 0.0106  528 GLN D CB  
18775 C CG  . GLN D 528 ? 1.4248 1.7815 1.3598 0.2205  -0.0462 0.0208  528 GLN D CG  
18776 C CD  . GLN D 528 ? 1.4173 1.7457 1.3226 0.2456  -0.0617 0.0516  528 GLN D CD  
18777 O OE1 . GLN D 528 ? 1.4209 1.6953 1.3157 0.2508  -0.0510 0.0700  528 GLN D OE1 
18778 N NE2 . GLN D 528 ? 1.3818 1.7448 1.2736 0.2617  -0.0880 0.0584  528 GLN D NE2 
18779 N N   . ALA D 529 ? 1.3971 1.7655 1.1826 0.1714  -0.0424 0.0244  529 ALA D N   
18780 C CA  . ALA D 529 ? 1.2016 1.5912 0.9507 0.1528  -0.0406 0.0103  529 ALA D CA  
18781 C C   . ALA D 529 ? 1.0507 1.4930 0.8353 0.1403  -0.0481 -0.0254 529 ALA D C   
18782 O O   . ALA D 529 ? 1.1621 1.6381 0.9883 0.1519  -0.0651 -0.0339 529 ALA D O   
18783 C CB  . ALA D 529 ? 1.1760 1.5702 0.8656 0.1667  -0.0615 0.0319  529 ALA D CB  
18784 N N   . VAL D 530 ? 1.1457 1.5942 0.9158 0.1160  -0.0335 -0.0470 530 VAL D N   
18785 C CA  . VAL D 530 ? 1.1999 1.6908 1.0008 0.0994  -0.0366 -0.0824 530 VAL D CA  
18786 C C   . VAL D 530 ? 1.2225 1.7283 0.9731 0.0855  -0.0394 -0.0967 530 VAL D C   
18787 O O   . VAL D 530 ? 1.2623 1.7404 0.9889 0.0699  -0.0148 -0.1007 530 VAL D O   
18788 C CB  . VAL D 530 ? 1.1551 1.6291 1.0007 0.0813  -0.0091 -0.0991 530 VAL D CB  
18789 C CG1 . VAL D 530 ? 1.0705 1.5834 0.9510 0.0636  -0.0111 -0.1337 530 VAL D CG1 
18790 C CG2 . VAL D 530 ? 1.0463 1.5009 0.9308 0.0945  -0.0042 -0.0845 530 VAL D CG2 
18791 N N   . PRO D 531 ? 1.1251 1.6759 0.8587 0.0911  -0.0688 -0.1062 531 PRO D N   
18792 C CA  . PRO D 531 ? 1.2101 1.7747 0.8902 0.0771  -0.0713 -0.1230 531 PRO D CA  
18793 C C   . PRO D 531 ? 1.2647 1.8399 0.9730 0.0490  -0.0535 -0.1633 531 PRO D C   
18794 O O   . PRO D 531 ? 1.3634 1.9644 1.1304 0.0421  -0.0577 -0.1842 531 PRO D O   
18795 C CB  . PRO D 531 ? 1.3709 1.9845 1.0326 0.0928  -0.1120 -0.1224 531 PRO D CB  
18796 C CG  . PRO D 531 ? 1.1792 1.8194 0.9090 0.1063  -0.1277 -0.1224 531 PRO D CG  
18797 C CD  . PRO D 531 ? 1.0966 1.6907 0.8600 0.1103  -0.1015 -0.1044 531 PRO D CD  
18798 N N   . LYS D 532 ? 1.2909 1.8443 0.9589 0.0331  -0.0314 -0.1736 532 LYS D N   
18799 C CA  . LYS D 532 ? 1.0710 1.6261 0.7626 0.0078  -0.0116 -0.2112 532 LYS D CA  
18800 C C   . LYS D 532 ? 1.3177 1.9222 1.0064 -0.0037 -0.0348 -0.2473 532 LYS D C   
18801 O O   . LYS D 532 ? 1.4465 2.0561 1.0869 -0.0148 -0.0323 -0.2668 532 LYS D O   
18802 C CB  . LYS D 532 ? 1.0338 1.5511 0.6824 -0.0023 0.0196  -0.2102 532 LYS D CB  
18803 C CG  . LYS D 532 ? 1.0019 1.4988 0.6923 -0.0214 0.0502  -0.2348 532 LYS D CG  
18804 C CD  . LYS D 532 ? 1.3332 1.8195 0.9818 -0.0363 0.0718  -0.2566 532 LYS D CD  
18805 C CE  . LYS D 532 ? 1.2294 1.6845 0.8290 -0.0300 0.0919  -0.2291 532 LYS D CE  
18806 N NZ  . LYS D 532 ? 1.4087 1.8589 0.9653 -0.0439 0.1144  -0.2527 532 LYS D NZ  
18807 N N   . GLU D 533 ? 1.4288 2.0713 1.1712 -0.0020 -0.0562 -0.2584 533 GLU D N   
18808 C CA  . GLU D 533 ? 1.4813 2.1767 1.2324 -0.0138 -0.0814 -0.2938 533 GLU D CA  
18809 C C   . GLU D 533 ? 1.3281 2.0333 1.1510 -0.0362 -0.0692 -0.3265 533 GLU D C   
18810 O O   . GLU D 533 ? 1.2554 1.9398 1.1284 -0.0352 -0.0518 -0.3149 533 GLU D O   
18811 C CB  . GLU D 533 ? 1.4522 2.1946 1.2065 0.0078  -0.1219 -0.2795 533 GLU D CB  
18812 C CG  . GLU D 533 ? 1.5071 2.2268 1.2165 0.0368  -0.1300 -0.2331 533 GLU D CG  
18813 C CD  . GLU D 533 ? 1.6848 2.4483 1.3961 0.0619  -0.1709 -0.2173 533 GLU D CD  
18814 O OE1 . GLU D 533 ? 1.8021 2.6108 1.5766 0.0614  -0.1880 -0.2345 533 GLU D OE1 
18815 O OE2 . GLU D 533 ? 1.5831 2.3355 1.2346 0.0827  -0.1851 -0.1863 533 GLU D OE2 
18816 N N   . GLY D 534 ? 1.3312 2.0671 1.1565 -0.0568 -0.0786 -0.3671 534 GLY D N   
18817 C CA  . GLY D 534 ? 1.1414 1.8858 1.0328 -0.0811 -0.0674 -0.4003 534 GLY D CA  
18818 C C   . GLY D 534 ? 1.1297 1.8208 1.0286 -0.0969 -0.0281 -0.4100 534 GLY D C   
18819 O O   . GLY D 534 ? 1.2736 1.9436 1.2272 -0.1027 -0.0083 -0.4058 534 GLY D O   
18820 N N   . VAL D 535 ? 1.1739 1.8426 1.0150 -0.1012 -0.0161 -0.4195 535 VAL D N   
18821 C CA  . VAL D 535 ? 1.0629 1.6809 0.9112 -0.1129 0.0222  -0.4282 535 VAL D CA  
18822 C C   . VAL D 535 ? 1.1669 1.7881 1.0695 -0.1387 0.0307  -0.4685 535 VAL D C   
18823 O O   . VAL D 535 ? 1.3825 2.0408 1.2825 -0.1529 0.0108  -0.5029 535 VAL D O   
18824 C CB  . VAL D 535 ? 1.0498 1.6484 0.8265 -0.1124 0.0350  -0.4333 535 VAL D CB  
18825 C CG1 . VAL D 535 ? 1.1128 1.7448 0.8529 -0.1269 0.0178  -0.4746 535 VAL D CG1 
18826 C CG2 . VAL D 535 ? 1.1613 1.7097 0.9511 -0.1192 0.0747  -0.4367 535 VAL D CG2 
18827 N N   . VAL D 536 ? 1.1566 1.7385 1.1049 -0.1447 0.0591  -0.4645 536 VAL D N   
18828 C CA  . VAL D 536 ? 1.3156 1.8907 1.3165 -0.1697 0.0711  -0.5000 536 VAL D CA  
18829 C C   . VAL D 536 ? 1.2647 1.7861 1.2651 -0.1751 0.1061  -0.5082 536 VAL D C   
18830 O O   . VAL D 536 ? 1.3950 1.9075 1.4039 -0.1947 0.1157  -0.5478 536 VAL D O   
18831 C CB  . VAL D 536 ? 1.1073 1.6917 1.1757 -0.1725 0.0693  -0.4870 536 VAL D CB  
18832 C CG1 . VAL D 536 ? 1.2583 1.8261 1.3786 -0.1986 0.0863  -0.5185 536 VAL D CG1 
18833 C CG2 . VAL D 536 ? 1.2591 1.9030 1.3361 -0.1685 0.0351  -0.4863 536 VAL D CG2 
18834 N N   . ASP D 537 ? 0.9673 1.4553 0.9613 -0.1581 0.1237  -0.4738 537 ASP D N   
18835 C CA  . ASP D 537 ? 1.1320 1.5745 1.1257 -0.1604 0.1552  -0.4813 537 ASP D CA  
18836 C C   . ASP D 537 ? 0.9337 1.3593 0.8888 -0.1402 0.1649  -0.4481 537 ASP D C   
18837 O O   . ASP D 537 ? 1.0524 1.4708 1.0231 -0.1263 0.1634  -0.4125 537 ASP D O   
18838 C CB  . ASP D 537 ? 1.0220 1.4318 1.0804 -0.1668 0.1741  -0.4778 537 ASP D CB  
18839 C CG  . ASP D 537 ? 1.1973 1.5632 1.2677 -0.1720 0.2041  -0.4956 537 ASP D CG  
18840 O OD1 . ASP D 537 ? 1.2792 1.6322 1.3135 -0.1623 0.2171  -0.4929 537 ASP D OD1 
18841 O OD2 . ASP D 537 ? 1.2183 1.5623 1.3363 -0.1852 0.2157  -0.5114 537 ASP D OD2 
18842 N N   . GLU D 538 ? 1.0030 1.4230 0.9082 -0.1396 0.1757  -0.4603 538 GLU D N   
18843 C CA  . GLU D 538 ? 1.0131 1.4176 0.8839 -0.1235 0.1879  -0.4296 538 GLU D CA  
18844 C C   . GLU D 538 ? 1.0554 1.4197 0.9603 -0.1203 0.2191  -0.4231 538 GLU D C   
18845 O O   . GLU D 538 ? 1.0400 1.3914 0.9340 -0.1076 0.2290  -0.3942 538 GLU D O   
18846 C CB  . GLU D 538 ? 1.2408 1.6594 1.0389 -0.1236 0.1872  -0.4408 538 GLU D CB  
18847 C CG  . GLU D 538 ? 1.2693 1.7252 1.0241 -0.1169 0.1539  -0.4276 538 GLU D CG  
18848 C CD  . GLU D 538 ? 1.5829 2.0507 1.2574 -0.1144 0.1525  -0.4304 538 GLU D CD  
18849 O OE1 . GLU D 538 ? 1.6113 2.0630 1.2621 -0.1216 0.1787  -0.4517 538 GLU D OE1 
18850 O OE2 . GLU D 538 ? 1.6526 2.1456 1.2869 -0.1043 0.1257  -0.4105 538 GLU D OE2 
18851 N N   . ASN D 539 ? 1.1761 1.5206 1.1247 -0.1314 0.2340  -0.4494 539 ASN D N   
18852 C CA  . ASN D 539 ? 1.1960 1.5038 1.1821 -0.1259 0.2609  -0.4426 539 ASN D CA  
18853 C C   . ASN D 539 ? 1.1479 1.4456 1.1770 -0.1167 0.2544  -0.4082 539 ASN D C   
18854 O O   . ASN D 539 ? 1.0393 1.3201 1.0790 -0.1041 0.2653  -0.3829 539 ASN D O   
18855 C CB  . ASN D 539 ? 1.1550 1.4411 1.1719 -0.1389 0.2784  -0.4813 539 ASN D CB  
18856 C CG  . ASN D 539 ? 1.4618 1.7512 1.4373 -0.1456 0.2921  -0.5168 539 ASN D CG  
18857 O OD1 . ASN D 539 ? 1.4984 1.7925 1.4332 -0.1371 0.3026  -0.5076 539 ASN D OD1 
18858 N ND2 . ASN D 539 ? 1.7788 2.0654 1.7631 -0.1620 0.2939  -0.5593 539 ASN D ND2 
18859 N N   . LEU D 540 ? 1.0253 1.3359 1.0791 -0.1235 0.2369  -0.4084 540 LEU D N   
18860 C CA  . LEU D 540 ? 0.9216 1.2260 1.0111 -0.1157 0.2308  -0.3778 540 LEU D CA  
18861 C C   . LEU D 540 ? 0.9290 1.2557 0.9907 -0.1022 0.2121  -0.3474 540 LEU D C   
18862 O O   . LEU D 540 ? 0.9722 1.2879 1.0491 -0.0903 0.2124  -0.3182 540 LEU D O   
18863 C CB  . LEU D 540 ? 0.9433 1.2547 1.0709 -0.1298 0.2229  -0.3905 540 LEU D CB  
18864 C CG  . LEU D 540 ? 0.9285 1.2046 1.1020 -0.1395 0.2427  -0.4042 540 LEU D CG  
18865 C CD1 . LEU D 540 ? 1.0127 1.3000 1.2160 -0.1596 0.2359  -0.4257 540 LEU D CD1 
18866 C CD2 . LEU D 540 ? 0.8864 1.1355 1.0887 -0.1265 0.2518  -0.3712 540 LEU D CD2 
18867 N N   . GLY D 541 ? 0.8547 1.2114 0.8757 -0.1034 0.1950  -0.3549 541 GLY D N   
18868 C CA  . GLY D 541 ? 0.8285 1.2043 0.8218 -0.0894 0.1762  -0.3269 541 GLY D CA  
18869 C C   . GLY D 541 ? 0.7974 1.2008 0.8142 -0.0893 0.1541  -0.3224 541 GLY D C   
18870 O O   . GLY D 541 ? 0.9024 1.3018 0.9407 -0.0789 0.1508  -0.2973 541 GLY D O   
18871 N N   . ILE D 542 ? 0.8549 1.2888 0.8694 -0.1014 0.1393  -0.3490 542 ILE D N   
18872 C CA  . ILE D 542 ? 0.8702 1.3384 0.9131 -0.1033 0.1185  -0.3495 542 ILE D CA  
18873 C C   . ILE D 542 ? 1.0038 1.5143 1.0094 -0.0987 0.0903  -0.3550 542 ILE D C   
18874 O O   . ILE D 542 ? 0.9464 1.4708 0.9255 -0.1099 0.0850  -0.3829 542 ILE D O   
18875 C CB  . ILE D 542 ? 0.8101 1.2793 0.9016 -0.1252 0.1262  -0.3781 542 ILE D CB  
18876 C CG1 . ILE D 542 ? 0.7592 1.1829 0.8842 -0.1277 0.1535  -0.3700 542 ILE D CG1 
18877 C CG2 . ILE D 542 ? 0.8495 1.3583 0.9767 -0.1283 0.1075  -0.3780 542 ILE D CG2 
18878 C CD1 . ILE D 542 ? 0.7751 1.1847 0.9380 -0.1497 0.1670  -0.3993 542 ILE D CD1 
18879 N N   . TRP D 543 ? 1.0023 1.5329 1.0056 -0.0813 0.0715  -0.3290 543 TRP D N   
18880 C CA  . TRP D 543 ? 0.9318 1.5034 0.9038 -0.0720 0.0413  -0.3282 543 TRP D CA  
18881 C C   . TRP D 543 ? 0.9731 1.5802 0.9904 -0.0659 0.0231  -0.3221 543 TRP D C   
18882 O O   . TRP D 543 ? 1.0063 1.5980 1.0517 -0.0559 0.0320  -0.2997 543 TRP D O   
18883 C CB  . TRP D 543 ? 0.9350 1.4907 0.8527 -0.0512 0.0375  -0.2968 543 TRP D CB  
18884 C CG  . TRP D 543 ? 0.9729 1.5027 0.8407 -0.0568 0.0544  -0.3028 543 TRP D CG  
18885 C CD1 . TRP D 543 ? 0.9777 1.5243 0.7914 -0.0603 0.0442  -0.3176 543 TRP D CD1 
18886 C CD2 . TRP D 543 ? 0.8662 1.3515 0.7340 -0.0589 0.0852  -0.2947 543 TRP D CD2 
18887 N NE1 . TRP D 543 ? 1.1946 1.7089 0.9738 -0.0651 0.0698  -0.3195 543 TRP D NE1 
18888 C CE2 . TRP D 543 ? 0.9972 1.4749 0.8125 -0.0641 0.0949  -0.3058 543 TRP D CE2 
18889 C CE3 . TRP D 543 ? 0.8205 1.2743 0.7275 -0.0565 0.1047  -0.2798 543 TRP D CE3 
18890 C CZ2 . TRP D 543 ? 1.0688 1.5106 0.8763 -0.0669 0.1251  -0.3031 543 TRP D CZ2 
18891 C CZ3 . TRP D 543 ? 0.8928 1.3118 0.7915 -0.0586 0.1310  -0.2765 543 TRP D CZ3 
18892 C CH2 . TRP D 543 ? 0.9185 1.3325 0.7713 -0.0639 0.1418  -0.2886 543 TRP D CH2 
18893 N N   . GLU D 544 ? 0.9527 1.6098 0.9784 -0.0715 -0.0023 -0.3430 544 GLU D N   
18894 C CA  . GLU D 544 ? 0.9923 1.6910 1.0679 -0.0662 -0.0190 -0.3404 544 GLU D CA  
18895 C C   . GLU D 544 ? 0.9540 1.6537 1.0179 -0.0363 -0.0310 -0.3038 544 GLU D C   
18896 O O   . GLU D 544 ? 1.0898 1.7944 1.1970 -0.0290 -0.0265 -0.2917 544 GLU D O   
18897 C CB  . GLU D 544 ? 0.9673 1.7253 1.0542 -0.0772 -0.0474 -0.3712 544 GLU D CB  
18898 C CG  . GLU D 544 ? 1.0446 1.8027 1.1508 -0.1091 -0.0365 -0.4120 544 GLU D CG  
18899 C CD  . GLU D 544 ? 1.3938 2.2123 1.5121 -0.1226 -0.0661 -0.4466 544 GLU D CD  
18900 O OE1 . GLU D 544 ? 1.4063 2.2717 1.5176 -0.1051 -0.0980 -0.4376 544 GLU D OE1 
18901 O OE2 . GLU D 544 ? 1.5628 2.3817 1.6992 -0.1504 -0.0583 -0.4837 544 GLU D OE2 
18902 N N   . LYS D 545 ? 0.9520 1.6448 0.9572 -0.0192 -0.0445 -0.2862 545 LYS D N   
18903 C CA  . LYS D 545 ? 1.0400 1.7274 1.0332 0.0096  -0.0556 -0.2510 545 LYS D CA  
18904 C C   . LYS D 545 ? 1.0441 1.6814 1.0493 0.0154  -0.0284 -0.2282 545 LYS D C   
18905 O O   . LYS D 545 ? 1.0467 1.6845 1.0741 0.0334  -0.0323 -0.2086 545 LYS D O   
18906 C CB  . LYS D 545 ? 1.0107 1.6943 0.9340 0.0247  -0.0731 -0.2346 545 LYS D CB  
18907 C CG  . LYS D 545 ? 1.0524 1.7244 0.9618 0.0553  -0.0850 -0.1966 545 LYS D CG  
18908 C CD  . LYS D 545 ? 1.1630 1.8887 1.1036 0.0735  -0.1179 -0.1955 545 LYS D CD  
18909 C CE  . LYS D 545 ? 1.3158 2.0251 1.2707 0.1020  -0.1210 -0.1633 545 LYS D CE  
18910 N NZ  . LYS D 545 ? 1.3783 2.1339 1.4005 0.1105  -0.1332 -0.1726 545 LYS D NZ  
18911 N N   . VAL D 546 ? 0.9868 1.5829 0.9795 0.0008  -0.0017 -0.2325 546 VAL D N   
18912 C CA  . VAL D 546 ? 1.0744 1.6261 1.0795 0.0049  0.0221  -0.2134 546 VAL D CA  
18913 C C   . VAL D 546 ? 0.8892 1.4525 0.9539 -0.0001 0.0293  -0.2196 546 VAL D C   
18914 O O   . VAL D 546 ? 0.9450 1.4986 1.0260 0.0143  0.0319  -0.2006 546 VAL D O   
18915 C CB  . VAL D 546 ? 0.9357 1.4474 0.9202 -0.0092 0.0475  -0.2191 546 VAL D CB  
18916 C CG1 . VAL D 546 ? 0.9593 1.4333 0.9680 -0.0073 0.0695  -0.2042 546 VAL D CG1 
18917 C CG2 . VAL D 546 ? 0.9693 1.4667 0.8930 -0.0030 0.0454  -0.2081 546 VAL D CG2 
18918 N N   . ASN D 547 ? 0.8549 1.4386 0.9504 -0.0212 0.0332  -0.2469 547 ASN D N   
18919 C CA  . ASN D 547 ? 0.8411 1.4367 0.9930 -0.0294 0.0430  -0.2527 547 ASN D CA  
18920 C C   . ASN D 547 ? 0.8365 1.4713 1.0126 -0.0119 0.0249  -0.2433 547 ASN D C   
18921 O O   . ASN D 547 ? 0.8391 1.4700 1.0467 -0.0073 0.0365  -0.2335 547 ASN D O   
18922 C CB  . ASN D 547 ? 0.7111 1.3246 0.8931 -0.0565 0.0482  -0.2844 547 ASN D CB  
18923 C CG  . ASN D 547 ? 0.7955 1.3651 0.9718 -0.0733 0.0727  -0.2939 547 ASN D CG  
18924 O OD1 . ASN D 547 ? 0.9465 1.4781 1.0907 -0.0652 0.0833  -0.2796 547 ASN D OD1 
18925 N ND2 . ASN D 547 ? 0.8605 1.4350 1.0712 -0.0967 0.0822  -0.3184 547 ASN D ND2 
18926 N N   . GLU D 548 ? 0.7901 1.4622 0.9514 -0.0013 -0.0026 -0.2461 548 GLU D N   
18927 C CA  . GLU D 548 ? 0.6793 1.3938 0.8683 0.0175  -0.0221 -0.2393 548 GLU D CA  
18928 C C   . GLU D 548 ? 0.7734 1.4592 0.9468 0.0446  -0.0206 -0.2086 548 GLU D C   
18929 O O   . GLU D 548 ? 0.8813 1.5819 1.0911 0.0562  -0.0186 -0.2027 548 GLU D O   
18930 C CB  . GLU D 548 ? 0.8609 1.6230 1.0355 0.0236  -0.0553 -0.2496 548 GLU D CB  
18931 C CG  . GLU D 548 ? 1.0335 1.8395 1.2389 -0.0022 -0.0626 -0.2848 548 GLU D CG  
18932 C CD  . GLU D 548 ? 1.2699 2.1133 1.4433 0.0002  -0.0949 -0.2976 548 GLU D CD  
18933 O OE1 . GLU D 548 ? 1.2692 2.1332 1.4246 0.0268  -0.1204 -0.2795 548 GLU D OE1 
18934 O OE2 . GLU D 548 ? 1.2276 2.0785 1.3924 -0.0239 -0.0951 -0.3258 548 GLU D OE2 
18935 N N   . THR D 549 ? 0.7753 1.4205 0.8964 0.0542  -0.0202 -0.1903 549 THR D N   
18936 C CA  . THR D 549 ? 0.7440 1.3569 0.8506 0.0778  -0.0182 -0.1624 549 THR D CA  
18937 C C   . THR D 549 ? 0.7841 1.3661 0.9147 0.0729  0.0077  -0.1584 549 THR D C   
18938 O O   . THR D 549 ? 0.7341 1.3084 0.8779 0.0905  0.0088  -0.1452 549 THR D O   
18939 C CB  . THR D 549 ? 0.8216 1.3972 0.8688 0.0847  -0.0207 -0.1442 549 THR D CB  
18940 O OG1 . THR D 549 ? 1.0662 1.6712 1.0843 0.0847  -0.0429 -0.1509 549 THR D OG1 
18941 C CG2 . THR D 549 ? 0.7810 1.3277 0.8148 0.1103  -0.0245 -0.1157 549 THR D CG2 
18942 N N   . VAL D 550 ? 0.8684 1.4324 1.0039 0.0500  0.0278  -0.1704 550 VAL D N   
18943 C CA  . VAL D 550 ? 0.8594 1.3956 1.0145 0.0449  0.0506  -0.1660 550 VAL D CA  
18944 C C   . VAL D 550 ? 0.8623 1.4333 1.0648 0.0454  0.0526  -0.1736 550 VAL D C   
18945 O O   . VAL D 550 ? 0.8397 1.3986 1.0531 0.0561  0.0615  -0.1631 550 VAL D O   
18946 C CB  . VAL D 550 ? 0.5888 1.0984 0.7393 0.0224  0.0698  -0.1760 550 VAL D CB  
18947 C CG1 . VAL D 550 ? 0.6362 1.1268 0.8126 0.0162  0.0903  -0.1730 550 VAL D CG1 
18948 C CG2 . VAL D 550 ? 0.7191 1.1920 0.8270 0.0243  0.0734  -0.1660 550 VAL D CG2 
18949 N N   . SER D 551 ? 0.7434 1.3591 0.9744 0.0332  0.0450  -0.1932 551 SER D N   
18950 C CA  . SER D 551 ? 0.7466 1.4011 1.0275 0.0314  0.0489  -0.2015 551 SER D CA  
18951 C C   . SER D 551 ? 0.8096 1.4862 1.1003 0.0596  0.0352  -0.1904 551 SER D C   
18952 O O   . SER D 551 ? 0.8159 1.5051 1.1376 0.0650  0.0465  -0.1893 551 SER D O   
18953 C CB  . SER D 551 ? 0.6937 1.3955 1.0058 0.0118  0.0404  -0.2264 551 SER D CB  
18954 O OG  . SER D 551 ? 1.0154 1.6943 1.3145 -0.0123 0.0500  -0.2392 551 SER D OG  
18955 N N   . LYS D 552 ? 0.7947 1.4746 1.0581 0.0782  0.0120  -0.1817 552 LYS D N   
18956 C CA  . LYS D 552 ? 0.7220 1.4178 0.9941 0.1080  -0.0028 -0.1699 552 LYS D CA  
18957 C C   . LYS D 552 ? 0.6742 1.3219 0.9305 0.1229  0.0117  -0.1519 552 LYS D C   
18958 O O   . LYS D 552 ? 0.7911 1.4514 1.0757 0.1369  0.0171  -0.1513 552 LYS D O   
18959 C CB  . LYS D 552 ? 0.7497 1.4554 0.9909 0.1238  -0.0320 -0.1620 552 LYS D CB  
18960 C CG  . LYS D 552 ? 0.7703 1.4836 1.0173 0.1581  -0.0485 -0.1461 552 LYS D CG  
18961 C CD  . LYS D 552 ? 0.9439 1.6701 1.1603 0.1744  -0.0792 -0.1360 552 LYS D CD  
18962 C CE  . LYS D 552 ? 1.3435 2.0892 1.5804 0.2095  -0.0983 -0.1236 552 LYS D CE  
18963 N NZ  . LYS D 552 ? 1.4784 2.2383 1.6842 0.2275  -0.1309 -0.1108 552 LYS D NZ  
18964 N N   . ILE D 553 ? 0.6748 1.2698 0.8880 0.1195  0.0184  -0.1393 553 ILE D N   
18965 C CA  . ILE D 553 ? 0.7958 1.3449 0.9937 0.1314  0.0299  -0.1244 553 ILE D CA  
18966 C C   . ILE D 553 ? 0.8137 1.3548 1.0324 0.1200  0.0534  -0.1308 553 ILE D C   
18967 O O   . ILE D 553 ? 0.8344 1.3634 1.0593 0.1340  0.0600  -0.1259 553 ILE D O   
18968 C CB  . ILE D 553 ? 0.7163 1.2163 0.8673 0.1289  0.0304  -0.1101 553 ILE D CB  
18969 C CG1 . ILE D 553 ? 0.6376 1.1433 0.7618 0.1427  0.0079  -0.0994 553 ILE D CG1 
18970 C CG2 . ILE D 553 ? 0.8325 1.2870 0.9731 0.1383  0.0415  -0.0976 553 ILE D CG2 
18971 C CD1 . ILE D 553 ? 0.7161 1.1841 0.7942 0.1344  0.0107  -0.0883 553 ILE D CD1 
18972 N N   . SER D 554 ? 0.7698 1.3163 0.9977 0.0953  0.0661  -0.1416 554 SER D N   
18973 C CA  . SER D 554 ? 0.7361 1.2737 0.9798 0.0842  0.0883  -0.1443 554 SER D CA  
18974 C C   . SER D 554 ? 0.8730 1.4529 1.1570 0.0881  0.0939  -0.1530 554 SER D C   
18975 O O   . SER D 554 ? 0.9688 1.5434 1.2632 0.0804  0.1135  -0.1534 554 SER D O   
18976 C CB  . SER D 554 ? 0.6491 1.1794 0.8949 0.0576  0.1001  -0.1524 554 SER D CB  
18977 O OG  . SER D 554 ? 1.1809 1.6840 1.3960 0.0519  0.0952  -0.1497 554 SER D OG  
18978 N N   . GLN D 555 ? 0.8792 1.5034 1.1867 0.0998  0.0775  -0.1596 555 GLN D N   
18979 C CA  . GLN D 555 ? 0.8439 1.5167 1.1975 0.1034  0.0832  -0.1699 555 GLN D CA  
18980 C C   . GLN D 555 ? 0.8635 1.5574 1.2454 0.0740  0.1002  -0.1824 555 GLN D C   
18981 O O   . GLN D 555 ? 0.9025 1.6131 1.3112 0.0690  0.1198  -0.1857 555 GLN D O   
18982 C CB  . GLN D 555 ? 0.9693 1.6285 1.3234 0.1216  0.0965  -0.1637 555 GLN D CB  
18983 C CG  . GLN D 555 ? 0.9172 1.5564 1.2519 0.1513  0.0802  -0.1537 555 GLN D CG  
18984 C CD  . GLN D 555 ? 1.1371 1.8220 1.4997 0.1703  0.0582  -0.1579 555 GLN D CD  
18985 O OE1 . GLN D 555 ? 1.1365 1.8769 1.5444 0.1673  0.0591  -0.1711 555 GLN D OE1 
18986 N NE2 . GLN D 555 ? 1.1657 1.8293 1.5037 0.1904  0.0378  -0.1458 555 GLN D NE2 
18987 N N   . GLY D 556 ? 0.7485 1.4393 1.1230 0.0543  0.0940  -0.1893 556 GLY D N   
18988 C CA  . GLY D 556 ? 0.6718 1.3761 1.0730 0.0247  0.1084  -0.2025 556 GLY D CA  
18989 C C   . GLY D 556 ? 0.6263 1.2840 1.0118 0.0086  0.1333  -0.1944 556 GLY D C   
18990 O O   . GLY D 556 ? 0.7887 1.4520 1.1979 -0.0158 0.1479  -0.2030 556 GLY D O   
18991 N N   . ALA D 557 ? 0.6599 1.2713 1.0078 0.0216  0.1378  -0.1779 557 ALA D N   
18992 C CA  . ALA D 557 ? 0.5842 1.1531 0.9168 0.0094  0.1583  -0.1685 557 ALA D CA  
18993 C C   . ALA D 557 ? 0.6999 1.2421 1.0203 -0.0082 0.1580  -0.1728 557 ALA D C   
18994 O O   . ALA D 557 ? 0.8144 1.3411 1.1456 -0.0270 0.1749  -0.1737 557 ALA D O   
18995 C CB  . ALA D 557 ? 0.6904 1.2234 0.9896 0.0283  0.1599  -0.1526 557 ALA D CB  
18996 N N   . VAL D 558 ? 0.7952 1.3305 1.0926 -0.0017 0.1402  -0.1752 558 VAL D N   
18997 C CA  . VAL D 558 ? 0.8051 1.3175 1.0886 -0.0162 0.1403  -0.1822 558 VAL D CA  
18998 C C   . VAL D 558 ? 0.8151 1.3649 1.1084 -0.0233 0.1234  -0.2010 558 VAL D C   
18999 O O   . VAL D 558 ? 0.8634 1.4341 1.1451 -0.0071 0.1041  -0.1993 558 VAL D O   
19000 C CB  . VAL D 558 ? 0.5914 1.0636 0.8354 -0.0041 0.1366  -0.1692 558 VAL D CB  
19001 C CG1 . VAL D 558 ? 0.6332 1.0827 0.8655 -0.0185 0.1407  -0.1777 558 VAL D CG1 
19002 C CG2 . VAL D 558 ? 0.6805 1.1227 0.9158 0.0050  0.1481  -0.1522 558 VAL D CG2 
19003 N N   . THR D 559 ? 0.8434 1.4011 1.1577 -0.0470 0.1297  -0.2192 559 THR D N   
19004 C CA  . THR D 559 ? 0.9348 1.5310 1.2589 -0.0563 0.1123  -0.2413 559 THR D CA  
19005 C C   . THR D 559 ? 0.9499 1.5217 1.2464 -0.0675 0.1106  -0.2538 559 THR D C   
19006 O O   . THR D 559 ? 0.9992 1.5838 1.2677 -0.0598 0.0917  -0.2586 559 THR D O   
19007 C CB  . THR D 559 ? 0.6712 1.3068 1.0478 -0.0761 0.1182  -0.2586 559 THR D CB  
19008 O OG1 . THR D 559 ? 0.9561 1.5596 1.3477 -0.0983 0.1421  -0.2621 559 THR D OG1 
19009 C CG2 . THR D 559 ? 0.5589 1.2268 0.9637 -0.0638 0.1203  -0.2489 559 THR D CG2 
19010 N N   . SER D 560 ? 0.9470 1.4834 1.2502 -0.0844 0.1308  -0.2585 560 SER D N   
19011 C CA  . SER D 560 ? 0.8856 1.3976 1.1670 -0.0948 0.1331  -0.2732 560 SER D CA  
19012 C C   . SER D 560 ? 0.8627 1.3281 1.1114 -0.0819 0.1429  -0.2545 560 SER D C   
19013 O O   . SER D 560 ? 0.9537 1.3928 1.2100 -0.0768 0.1566  -0.2364 560 SER D O   
19014 C CB  . SER D 560 ? 0.9187 1.4197 1.2331 -0.1212 0.1493  -0.2934 560 SER D CB  
19015 O OG  . SER D 560 ? 1.3562 1.8308 1.6934 -0.1241 0.1701  -0.2768 560 SER D OG  
19016 N N   . VAL D 561 ? 0.8148 1.2730 1.0274 -0.0776 0.1357  -0.2599 561 VAL D N   
19017 C CA  . VAL D 561 ? 0.8211 1.2407 1.0048 -0.0657 0.1445  -0.2430 561 VAL D CA  
19018 C C   . VAL D 561 ? 0.8837 1.2882 1.0446 -0.0742 0.1503  -0.2604 561 VAL D C   
19019 O O   . VAL D 561 ? 0.8827 1.3124 1.0332 -0.0832 0.1396  -0.2821 561 VAL D O   
19020 C CB  . VAL D 561 ? 0.6290 1.0558 0.7858 -0.0442 0.1305  -0.2215 561 VAL D CB  
19021 C CG1 . VAL D 561 ? 0.9660 1.3632 1.0887 -0.0362 0.1359  -0.2108 561 VAL D CG1 
19022 C CG2 . VAL D 561 ? 0.7323 1.1600 0.9078 -0.0327 0.1310  -0.2026 561 VAL D CG2 
19023 N N   . THR D 562 ? 0.6918 1.0597 0.8458 -0.0710 0.1664  -0.2529 562 THR D N   
19024 C CA  . THR D 562 ? 0.6746 1.0264 0.8081 -0.0764 0.1763  -0.2681 562 THR D CA  
19025 C C   . THR D 562 ? 0.8489 1.1830 0.9578 -0.0609 0.1799  -0.2458 562 THR D C   
19026 O O   . THR D 562 ? 0.9993 1.3131 1.1247 -0.0531 0.1870  -0.2273 562 THR D O   
19027 C CB  . THR D 562 ? 0.7681 1.0922 0.9315 -0.0889 0.1961  -0.2834 562 THR D CB  
19028 O OG1 . THR D 562 ? 1.0929 1.3925 1.2805 -0.0814 0.2054  -0.2613 562 THR D OG1 
19029 C CG2 . THR D 562 ? 0.8107 1.1497 0.9984 -0.1082 0.1942  -0.3096 562 THR D CG2 
19030 N N   . LEU D 563 ? 0.9173 1.2597 0.9863 -0.0572 0.1747  -0.2466 563 LEU D N   
19031 C CA  . LEU D 563 ? 0.9318 1.2575 0.9791 -0.0453 0.1798  -0.2253 563 LEU D CA  
19032 C C   . LEU D 563 ? 0.8669 1.1660 0.9230 -0.0483 0.2025  -0.2303 563 LEU D C   
19033 O O   . LEU D 563 ? 0.9720 1.2565 1.0258 -0.0399 0.2088  -0.2121 563 LEU D O   
19034 C CB  . LEU D 563 ? 0.8779 1.2187 0.8769 -0.0405 0.1687  -0.2207 563 LEU D CB  
19035 C CG  . LEU D 563 ? 0.7042 1.0734 0.6919 -0.0330 0.1435  -0.2134 563 LEU D CG  
19036 C CD1 . LEU D 563 ? 0.7386 1.1128 0.6757 -0.0245 0.1343  -0.2007 563 LEU D CD1 
19037 C CD2 . LEU D 563 ? 0.7471 1.1139 0.7628 -0.0216 0.1366  -0.1933 563 LEU D CD2 
19038 N N   . TYR D 564 ? 0.6912 0.9844 0.7606 -0.0600 0.2149  -0.2558 564 TYR D N   
19039 C CA  . TYR D 564 ? 0.7607 1.0307 0.8428 -0.0606 0.2371  -0.2625 564 TYR D CA  
19040 C C   . TYR D 564 ? 0.8269 1.0762 0.9548 -0.0643 0.2477  -0.2706 564 TYR D C   
19041 O O   . TYR D 564 ? 0.8942 1.1279 1.0346 -0.0681 0.2652  -0.2884 564 TYR D O   
19042 C CB  . TYR D 564 ? 0.9890 1.2646 1.0389 -0.0684 0.2476  -0.2869 564 TYR D CB  
19043 C CG  . TYR D 564 ? 0.9833 1.2805 0.9805 -0.0668 0.2350  -0.2813 564 TYR D CG  
19044 C CD1 . TYR D 564 ? 0.9798 1.2765 0.9587 -0.0556 0.2290  -0.2514 564 TYR D CD1 
19045 C CD2 . TYR D 564 ? 0.9748 1.2907 0.9390 -0.0762 0.2293  -0.3059 564 TYR D CD2 
19046 C CE1 . TYR D 564 ? 1.0072 1.3187 0.9366 -0.0526 0.2178  -0.2425 564 TYR D CE1 
19047 C CE2 . TYR D 564 ? 1.0758 1.4110 0.9874 -0.0728 0.2160  -0.2979 564 TYR D CE2 
19048 C CZ  . TYR D 564 ? 1.0774 1.4086 0.9714 -0.0603 0.2108  -0.2644 564 TYR D CZ  
19049 O OH  . TYR D 564 ? 0.8790 1.2247 0.7196 -0.0555 0.1980  -0.2529 564 TYR D OH  
19050 N N   . SER D 565 ? 0.8230 1.0705 0.9755 -0.0623 0.2389  -0.2567 565 SER D N   
19051 C CA  . SER D 565 ? 0.6617 0.8862 0.8539 -0.0653 0.2490  -0.2591 565 SER D CA  
19052 C C   . SER D 565 ? 0.7955 1.0132 1.0050 -0.0555 0.2425  -0.2310 565 SER D C   
19053 O O   . SER D 565 ? 0.8981 1.1337 1.0943 -0.0512 0.2284  -0.2171 565 SER D O   
19054 C CB  . SER D 565 ? 0.8250 1.0544 1.0292 -0.0818 0.2485  -0.2828 565 SER D CB  
19055 O OG  . SER D 565 ? 0.6766 0.8821 0.9183 -0.0855 0.2571  -0.2791 565 SER D OG  
19056 N N   . ILE D 566 ? 0.7483 0.9398 0.9865 -0.0507 0.2527  -0.2231 566 ILE D N   
19057 C CA  . ILE D 566 ? 0.8060 0.9891 1.0569 -0.0412 0.2472  -0.1971 566 ILE D CA  
19058 C C   . ILE D 566 ? 0.7615 0.9315 1.0350 -0.0494 0.2516  -0.1959 566 ILE D C   
19059 O O   . ILE D 566 ? 0.8890 1.0557 1.1663 -0.0435 0.2471  -0.1747 566 ILE D O   
19060 C CB  . ILE D 566 ? 0.6366 0.8030 0.9003 -0.0272 0.2514  -0.1830 566 ILE D CB  
19061 C CG1 . ILE D 566 ? 0.8027 0.9421 1.0969 -0.0271 0.2667  -0.1922 566 ILE D CG1 
19062 C CG2 . ILE D 566 ? 0.8462 1.0259 1.0910 -0.0225 0.2503  -0.1845 566 ILE D CG2 
19063 C CD1 . ILE D 566 ? 1.0588 1.1852 1.3733 -0.0116 0.2684  -0.1772 566 ILE D CD1 
19064 N N   . LEU D 567 ? 0.6896 0.8512 0.9770 -0.0639 0.2613  -0.2188 567 LEU D N   
19065 C CA  . LEU D 567 ? 0.7043 0.8501 1.0164 -0.0749 0.2684  -0.2183 567 LEU D CA  
19066 C C   . LEU D 567 ? 0.9617 1.1359 1.2716 -0.0914 0.2618  -0.2318 567 LEU D C   
19067 O O   . LEU D 567 ? 0.8819 1.0628 1.2000 -0.0945 0.2601  -0.2175 567 LEU D O   
19068 C CB  . LEU D 567 ? 0.6882 0.8003 1.0256 -0.0812 0.2851  -0.2358 567 LEU D CB  
19069 C CG  . LEU D 567 ? 0.8164 0.8980 1.1689 -0.0643 0.2929  -0.2213 567 LEU D CG  
19070 C CD1 . LEU D 567 ? 0.9919 1.0464 1.3664 -0.0685 0.3091  -0.2462 567 LEU D CD1 
19071 C CD2 . LEU D 567 ? 0.8630 0.9230 1.2290 -0.0571 0.2929  -0.1908 567 LEU D CD2 
19072 N N   . GLN D 568 ? 0.9504 1.1437 1.2499 -0.1020 0.2583  -0.2599 568 GLN D N   
19073 C CA  . GLN D 568 ? 1.0152 1.2409 1.3167 -0.1174 0.2491  -0.2756 568 GLN D CA  
19074 C C   . GLN D 568 ? 0.9626 1.2254 1.2403 -0.1069 0.2309  -0.2620 568 GLN D C   
19075 O O   . GLN D 568 ? 0.9364 1.2104 1.1844 -0.0972 0.2224  -0.2627 568 GLN D O   
19076 C CB  . GLN D 568 ? 1.0370 1.2710 1.3334 -0.1321 0.2494  -0.3125 568 GLN D CB  
19077 C CG  . GLN D 568 ? 1.1196 1.3934 1.4207 -0.1484 0.2361  -0.3316 568 GLN D CG  
19078 C CD  . GLN D 568 ? 1.0960 1.3754 1.3949 -0.1657 0.2362  -0.3713 568 GLN D CD  
19079 O OE1 . GLN D 568 ? 1.3508 1.5960 1.6593 -0.1714 0.2523  -0.3880 568 GLN D OE1 
19080 N NE2 . GLN D 568 ? 1.2044 1.5281 1.4909 -0.1736 0.2174  -0.3888 568 GLN D NE2 
19081 N N   . ASP D 569 ? 0.8884 1.1687 1.1795 -0.1085 0.2266  -0.2493 569 ASP D N   
19082 C CA  . ASP D 569 ? 0.6543 0.9694 0.9295 -0.0973 0.2102  -0.2371 569 ASP D CA  
19083 C C   . ASP D 569 ? 0.8071 1.1177 1.0489 -0.0778 0.2021  -0.2231 569 ASP D C   
19084 O O   . ASP D 569 ? 0.8385 1.1713 1.0568 -0.0735 0.1890  -0.2295 569 ASP D O   
19085 C CB  . ASP D 569 ? 0.6432 1.0004 0.9212 -0.1084 0.1965  -0.2598 569 ASP D CB  
19086 C CG  . ASP D 569 ? 1.0217 1.3844 1.3372 -0.1318 0.2050  -0.2787 569 ASP D CG  
19087 O OD1 . ASP D 569 ? 0.9504 1.3069 1.2912 -0.1362 0.2158  -0.2653 569 ASP D OD1 
19088 O OD2 . ASP D 569 ? 1.1776 1.5503 1.4962 -0.1468 0.2016  -0.3076 569 ASP D OD2 
19089 N N   . PRO D 570 ? 0.8179 1.0995 1.0574 -0.0664 0.2097  -0.2038 570 PRO D N   
19090 C CA  . PRO D 570 ? 0.7727 1.0497 0.9862 -0.0512 0.2036  -0.1925 570 PRO D CA  
19091 C C   . PRO D 570 ? 0.8184 1.1171 1.0143 -0.0390 0.1886  -0.1793 570 PRO D C   
19092 O O   . PRO D 570 ? 0.8375 1.1535 1.0435 -0.0383 0.1840  -0.1746 570 PRO D O   
19093 C CB  . PRO D 570 ? 0.8273 1.0729 1.0517 -0.0434 0.2135  -0.1764 570 PRO D CB  
19094 C CG  . PRO D 570 ? 0.8485 1.0885 1.0937 -0.0484 0.2191  -0.1687 570 PRO D CG  
19095 C CD  . PRO D 570 ? 0.6544 0.9063 0.9148 -0.0668 0.2230  -0.1907 570 PRO D CD  
19096 N N   . MET D 571 ? 0.9069 1.2034 1.0781 -0.0294 0.1828  -0.1734 571 MET D N   
19097 C CA  . MET D 571 ? 0.9317 1.2409 1.0854 -0.0162 0.1693  -0.1600 571 MET D CA  
19098 C C   . MET D 571 ? 0.9887 1.2844 1.1507 -0.0061 0.1704  -0.1422 571 MET D C   
19099 O O   . MET D 571 ? 1.1578 1.4312 1.3293 -0.0063 0.1796  -0.1367 571 MET D O   
19100 C CB  . MET D 571 ? 1.0969 1.3992 1.2222 -0.0108 0.1666  -0.1564 571 MET D CB  
19101 C CG  . MET D 571 ? 0.9866 1.3114 1.0887 -0.0130 0.1562  -0.1661 571 MET D CG  
19102 S SD  . MET D 571 ? 1.2465 1.5938 1.3395 0.0021  0.1359  -0.1532 571 MET D SD  
19103 C CE  . MET D 571 ? 1.1265 1.4470 1.1940 0.0149  0.1360  -0.1317 571 MET D CE  
19104 N N   . THR D 572 ? 0.8968 1.2068 1.0552 0.0038  0.1606  -0.1340 572 THR D N   
19105 C CA  . THR D 572 ? 0.7878 1.0867 0.9492 0.0134  0.1613  -0.1203 572 THR D CA  
19106 C C   . THR D 572 ? 0.7785 1.0570 0.9249 0.0228  0.1577  -0.1100 572 THR D C   
19107 O O   . THR D 572 ? 0.8337 1.1108 0.9650 0.0244  0.1535  -0.1103 572 THR D O   
19108 C CB  . THR D 572 ? 0.7242 1.0461 0.8891 0.0211  0.1545  -0.1186 572 THR D CB  
19109 O OG1 . THR D 572 ? 0.8782 1.2145 1.0301 0.0294  0.1415  -0.1198 572 THR D OG1 
19110 C CG2 . THR D 572 ? 0.5673 0.9102 0.7547 0.0099  0.1612  -0.1273 572 THR D CG2 
19111 N N   . SER D 573 ? 0.8628 1.1261 1.0130 0.0282  0.1595  -0.1008 573 SER D N   
19112 C CA  . SER D 573 ? 0.8184 1.0645 0.9605 0.0352  0.1552  -0.0931 573 SER D CA  
19113 C C   . SER D 573 ? 0.9373 1.1828 1.0730 0.0464  0.1477  -0.0871 573 SER D C   
19114 O O   . SER D 573 ? 0.8644 1.1169 1.0040 0.0479  0.1501  -0.0862 573 SER D O   
19115 C CB  . SER D 573 ? 0.8271 1.0570 0.9815 0.0316  0.1619  -0.0909 573 SER D CB  
19116 O OG  . SER D 573 ? 0.8895 1.1175 1.0507 0.0228  0.1709  -0.0988 573 SER D OG  
19117 N N   . CYS D 574 ? 0.7690 1.0051 0.8945 0.0536  0.1402  -0.0836 574 CYS D N   
19118 C CA  . CYS D 574 ? 0.6530 0.8855 0.7721 0.0646  0.1331  -0.0815 574 CYS D CA  
19119 C C   . CYS D 574 ? 0.7183 0.9362 0.8392 0.0656  0.1312  -0.0789 574 CYS D C   
19120 O O   . CYS D 574 ? 0.9068 1.1284 1.0298 0.0652  0.1342  -0.0776 574 CYS D O   
19121 C CB  . CYS D 574 ? 0.5257 0.7517 0.6344 0.0723  0.1256  -0.0797 574 CYS D CB  
19122 S SG  . CYS D 574 ? 0.8015 1.0083 0.9058 0.0652  0.1272  -0.0743 574 CYS D SG  
19123 N N   . GLY D 575 ? 0.5210 0.7234 0.6414 0.0664  0.1259  -0.0777 575 GLY D N   
19124 C CA  . GLY D 575 ? 0.6704 0.8637 0.7954 0.0670  0.1207  -0.0776 575 GLY D CA  
19125 C C   . GLY D 575 ? 0.7566 0.9360 0.8899 0.0632  0.1168  -0.0778 575 GLY D C   
19126 O O   . GLY D 575 ? 0.8726 1.0478 1.0138 0.0628  0.1100  -0.0797 575 GLY D O   
19127 N N   . CYS D 576 ? 0.6243 0.7973 0.7557 0.0596  0.1209  -0.0754 576 CYS D N   
19128 C CA  . CYS D 576 ? 0.5441 0.7025 0.6842 0.0533  0.1211  -0.0738 576 CYS D CA  
19129 C C   . CYS D 576 ? 0.7377 0.9015 0.8944 0.0430  0.1314  -0.0723 576 CYS D C   
19130 O O   . CYS D 576 ? 0.9082 1.0651 1.0799 0.0359  0.1336  -0.0719 576 CYS D O   
19131 C CB  . CYS D 576 ? 0.6573 0.8015 0.7827 0.0561  0.1212  -0.0690 576 CYS D CB  
19132 S SG  . CYS D 576 ? 0.8831 1.0404 0.9905 0.0590  0.1262  -0.0643 576 CYS D SG  
19133 N N   . PHE D 577 ? 0.6823 0.8586 0.8391 0.0413  0.1391  -0.0730 577 PHE D N   
19134 C CA  . PHE D 577 ? 0.6461 0.8276 0.8189 0.0332  0.1510  -0.0746 577 PHE D CA  
19135 C C   . PHE D 577 ? 0.6896 0.8721 0.8915 0.0302  0.1503  -0.0760 577 PHE D C   
19136 O O   . PHE D 577 ? 0.6894 0.8742 0.9005 0.0356  0.1393  -0.0766 577 PHE D O   
19137 C CB  . PHE D 577 ? 0.7819 0.9735 0.9570 0.0334  0.1565  -0.0783 577 PHE D CB  
19138 C CG  . PHE D 577 ? 0.7228 0.9175 0.8965 0.0403  0.1487  -0.0772 577 PHE D CG  
19139 C CD1 . PHE D 577 ? 0.6078 0.8017 0.7966 0.0441  0.1433  -0.0749 577 PHE D CD1 
19140 C CD2 . PHE D 577 ? 0.7988 0.9995 0.9561 0.0432  0.1472  -0.0778 577 PHE D CD2 
19141 C CE1 . PHE D 577 ? 0.6680 0.8632 0.8489 0.0502  0.1377  -0.0713 577 PHE D CE1 
19142 C CE2 . PHE D 577 ? 0.8409 1.0451 0.9960 0.0480  0.1438  -0.0758 577 PHE D CE2 
19143 C CZ  . PHE D 577 ? 0.8182 1.0180 0.9820 0.0514  0.1398  -0.0717 577 PHE D CZ  
19144 N N   . GLU D 578 ? 0.8143 0.9977 1.0306 0.0218  0.1622  -0.0767 578 GLU D N   
19145 C CA  . GLU D 578 ? 0.9073 1.0977 1.1599 0.0185  0.1622  -0.0794 578 GLU D CA  
19146 C C   . GLU D 578 ? 0.8634 1.0657 1.1390 0.0227  0.1660  -0.0830 578 GLU D C   
19147 O O   . GLU D 578 ? 0.9042 1.1146 1.2076 0.0266  0.1568  -0.0838 578 GLU D O   
19148 C CB  . GLU D 578 ? 0.8517 1.0405 1.1150 0.0070  0.1767  -0.0787 578 GLU D CB  
19149 C CG  . GLU D 578 ? 1.0410 1.2360 1.3417 0.0017  0.1722  -0.0814 578 GLU D CG  
19150 C CD  . GLU D 578 ? 1.2058 1.4118 1.5366 -0.0092 0.1917  -0.0838 578 GLU D CD  
19151 O OE1 . GLU D 578 ? 1.2294 1.4270 1.5409 -0.0175 0.2089  -0.0793 578 GLU D OE1 
19152 O OE2 . GLU D 578 ? 1.0278 1.2521 1.4010 -0.0088 0.1898  -0.0897 578 GLU D OE2 
19153 N N   . CYS D 579 ? 0.7271 0.9297 0.9922 0.0222  0.1779  -0.0857 579 CYS D N   
19154 C CA  . CYS D 579 ? 0.7309 0.9387 1.0190 0.0263  0.1837  -0.0896 579 CYS D CA  
19155 C C   . CYS D 579 ? 0.7617 0.9636 1.0320 0.0308  0.1811  -0.0886 579 CYS D C   
19156 O O   . CYS D 579 ? 0.7830 0.9819 1.0241 0.0289  0.1788  -0.0878 579 CYS D O   
19157 C CB  . CYS D 579 ? 0.7432 0.9561 1.0449 0.0196  0.2046  -0.0980 579 CYS D CB  
19158 S SG  . CYS D 579 ? 0.9292 1.1508 1.2528 0.0106  0.2139  -0.0984 579 CYS D SG  
19159 N N   . ILE D 580 ? 0.6310 0.8314 0.9223 0.0368  0.1818  -0.0881 580 ILE D N   
19160 C CA  . ILE D 580 ? 0.6890 0.8809 0.9701 0.0391  0.1827  -0.0863 580 ILE D CA  
19161 C C   . ILE D 580 ? 0.7779 0.9644 1.0858 0.0401  0.1962  -0.0928 580 ILE D C   
19162 O O   . ILE D 580 ? 0.7521 0.9415 1.0912 0.0471  0.1956  -0.0913 580 ILE D O   
19163 C CB  . ILE D 580 ? 0.6852 0.8736 0.9599 0.0480  0.1672  -0.0739 580 ILE D CB  
19164 C CG1 . ILE D 580 ? 0.7851 0.9773 1.0324 0.0479  0.1556  -0.0711 580 ILE D CG1 
19165 C CG2 . ILE D 580 ? 0.7680 0.9454 1.0374 0.0485  0.1729  -0.0702 580 ILE D CG2 
19166 C CD1 . ILE D 580 ? 0.7411 0.9332 0.9821 0.0567  0.1399  -0.0623 580 ILE D CD1 
19167 N N   . THR D 581 ? 0.7611 0.9406 1.0601 0.0336  0.2079  -0.1015 581 THR D N   
19168 C CA  . THR D 581 ? 0.8090 0.9789 1.1329 0.0341  0.2223  -0.1111 581 THR D CA  
19169 C C   . THR D 581 ? 0.8073 0.9600 1.1312 0.0347  0.2228  -0.1065 581 THR D C   
19170 O O   . THR D 581 ? 0.8545 1.0062 1.1586 0.0251  0.2257  -0.1122 581 THR D O   
19171 C CB  . THR D 581 ? 0.7030 0.8778 1.0187 0.0237  0.2386  -0.1300 581 THR D CB  
19172 O OG1 . THR D 581 ? 0.7927 0.9815 1.1035 0.0216  0.2396  -0.1300 581 THR D OG1 
19173 C CG2 . THR D 581 ? 0.6594 0.8241 1.0033 0.0250  0.2554  -0.1439 581 THR D CG2 
19174 N N   . GLY D 582 ? 0.7683 0.9084 1.1158 0.0459  0.2196  -0.0953 582 GLY D N   
19175 C CA  . GLY D 582 ? 0.8366 0.9551 1.1857 0.0470  0.2216  -0.0864 582 GLY D CA  
19176 C C   . GLY D 582 ? 0.8095 0.9070 1.1884 0.0481  0.2373  -0.0962 582 GLY D C   
19177 O O   . GLY D 582 ? 0.8192 0.9190 1.2257 0.0556  0.2428  -0.1039 582 GLY D O   
19178 N N   . ILE D 583 ? 0.8192 0.8956 1.1956 0.0407  0.2452  -0.0960 583 ILE D N   
19179 C CA  . ILE D 583 ? 0.8433 0.8928 1.2487 0.0400  0.2618  -0.1079 583 ILE D CA  
19180 C C   . ILE D 583 ? 0.9615 0.9882 1.3940 0.0587  0.2580  -0.0874 583 ILE D C   
19181 O O   . ILE D 583 ? 1.1152 1.1366 1.5339 0.0653  0.2458  -0.0621 583 ILE D O   
19182 C CB  . ILE D 583 ? 0.7386 0.7731 1.1348 0.0224  0.2718  -0.1168 583 ILE D CB  
19183 C CG1 . ILE D 583 ? 0.8823 0.8801 1.3098 0.0221  0.2879  -0.1252 583 ILE D CG1 
19184 C CG2 . ILE D 583 ? 1.1110 1.1465 1.4847 0.0193  0.2627  -0.0947 583 ILE D CG2 
19185 C CD1 . ILE D 583 ? 1.2367 1.2343 1.6853 0.0235  0.3009  -0.1528 583 ILE D CD1 
19186 N N   . MET D 584 ? 0.9181 0.9325 1.3867 0.0682  0.2683  -0.0983 584 MET D N   
19187 C CA  . MET D 584 ? 0.9222 0.9139 1.4224 0.0888  0.2646  -0.0799 584 MET D CA  
19188 C C   . MET D 584 ? 0.9985 0.9511 1.5241 0.0859  0.2848  -0.0928 584 MET D C   
19189 O O   . MET D 584 ? 0.9874 0.9386 1.5410 0.0887  0.2987  -0.1167 584 MET D O   
19190 C CB  . MET D 584 ? 0.9242 0.9399 1.4546 0.1058  0.2583  -0.0826 584 MET D CB  
19191 C CG  . MET D 584 ? 1.1174 1.1177 1.6809 0.1308  0.2479  -0.0603 584 MET D CG  
19192 S SD  . MET D 584 ? 1.1241 1.1620 1.7319 0.1500  0.2388  -0.0654 584 MET D SD  
19193 C CE  . MET D 584 ? 1.0815 1.0893 1.7353 0.1797  0.2330  -0.0448 584 MET D CE  
19194 N N   . PRO D 585 ? 0.8573 0.7773 1.3736 0.0785  0.2888  -0.0795 585 PRO D N   
19195 C CA  . PRO D 585 ? 0.8260 0.7040 1.3689 0.0733  0.3089  -0.0935 585 PRO D CA  
19196 C C   . PRO D 585 ? 0.8566 0.7100 1.4453 0.0973  0.3136  -0.0911 585 PRO D C   
19197 O O   . PRO D 585 ? 0.9079 0.7354 1.5244 0.0948  0.3324  -0.1151 585 PRO D O   
19198 C CB  . PRO D 585 ? 0.8518 0.7004 1.3775 0.0632  0.3098  -0.0702 585 PRO D CB  
19199 C CG  . PRO D 585 ? 0.8167 0.7001 1.3016 0.0568  0.2944  -0.0556 585 PRO D CG  
19200 C CD  . PRO D 585 ? 0.7843 0.7026 1.2673 0.0738  0.2776  -0.0519 585 PRO D CD  
19201 N N   . GLU D 586 ? 0.9802 0.8433 1.5782 0.1211  0.2957  -0.0641 586 GLU D N   
19202 C CA  . GLU D 586 ? 0.9893 0.8350 1.6350 0.1481  0.2960  -0.0582 586 GLU D CA  
19203 C C   . GLU D 586 ? 1.0309 0.8973 1.7093 0.1505  0.3103  -0.0945 586 GLU D C   
19204 O O   . GLU D 586 ? 1.0477 0.8867 1.7682 0.1629  0.3250  -0.1069 586 GLU D O   
19205 C CB  . GLU D 586 ? 0.9530 0.8188 1.5990 0.1717  0.2691  -0.0248 586 GLU D CB  
19206 C CG  . GLU D 586 ? 0.9829 0.8298 1.5912 0.1719  0.2550  0.0129  586 GLU D CG  
19207 C CD  . GLU D 586 ? 1.1595 1.0447 1.7192 0.1586  0.2399  0.0191  586 GLU D CD  
19208 O OE1 . GLU D 586 ? 1.2085 1.1103 1.7469 0.1351  0.2499  -0.0038 586 GLU D OE1 
19209 O OE2 . GLU D 586 ? 1.3134 1.2118 1.8558 0.1727  0.2172  0.0463  586 GLU D OE2 
19210 N N   . ALA D 587 ? 1.0382 0.9510 1.6969 0.1390  0.3079  -0.1113 587 ALA D N   
19211 C CA  . ALA D 587 ? 1.0475 0.9849 1.7301 0.1391  0.3234  -0.1441 587 ALA D CA  
19212 C C   . ALA D 587 ? 1.0645 1.0022 1.7213 0.1131  0.3434  -0.1790 587 ALA D C   
19213 O O   . ALA D 587 ? 1.0065 0.9689 1.6693 0.1097  0.3566  -0.2055 587 ALA D O   
19214 C CB  . ALA D 587 ? 0.9213 0.9091 1.6017 0.1441  0.3086  -0.1381 587 ALA D CB  
19215 N N   . ASN D 588 ? 1.0996 1.0128 1.7277 0.0943  0.3455  -0.1792 588 ASN D N   
19216 C CA  . ASN D 588 ? 1.0215 0.9372 1.6241 0.0692  0.3600  -0.2121 588 ASN D CA  
19217 C C   . ASN D 588 ? 1.0952 1.0588 1.6670 0.0593  0.3574  -0.2255 588 ASN D C   
19218 O O   . ASN D 588 ? 1.1537 1.1266 1.7155 0.0476  0.3728  -0.2577 588 ASN D O   
19219 C CB  . ASN D 588 ? 1.0921 0.9772 1.7268 0.0698  0.3843  -0.2447 588 ASN D CB  
19220 C CG  . ASN D 588 ? 1.2489 1.1216 1.8603 0.0430  0.3958  -0.2744 588 ASN D CG  
19221 O OD1 . ASN D 588 ? 1.1294 0.9810 1.7292 0.0293  0.3912  -0.2641 588 ASN D OD1 
19222 N ND2 . ASN D 588 ? 1.2623 1.1507 1.8658 0.0340  0.4111  -0.3125 588 ASN D ND2 
19223 N N   . GLY D 589 ? 1.0976 1.0887 1.6525 0.0641  0.3382  -0.2003 589 GLY D N   
19224 C CA  . GLY D 589 ? 1.0615 1.0931 1.5885 0.0562  0.3342  -0.2065 589 GLY D CA  
19225 C C   . GLY D 589 ? 0.9145 0.9642 1.4200 0.0588  0.3107  -0.1768 589 GLY D C   
19226 O O   . GLY D 589 ? 0.9364 0.9692 1.4441 0.0659  0.2984  -0.1528 589 GLY D O   
19227 N N   . VAL D 590 ? 0.8077 0.8900 1.2906 0.0530  0.3056  -0.1782 590 VAL D N   
19228 C CA  . VAL D 590 ? 0.7940 0.8938 1.2544 0.0540  0.2844  -0.1551 590 VAL D CA  
19229 C C   . VAL D 590 ? 0.7336 0.8564 1.2141 0.0662  0.2743  -0.1437 590 VAL D C   
19230 O O   . VAL D 590 ? 0.8423 0.9789 1.3477 0.0691  0.2866  -0.1571 590 VAL D O   
19231 C CB  . VAL D 590 ? 0.7433 0.8594 1.1601 0.0361  0.2852  -0.1660 590 VAL D CB  
19232 C CG1 . VAL D 590 ? 0.8331 0.9331 1.2333 0.0226  0.2921  -0.1792 590 VAL D CG1 
19233 C CG2 . VAL D 590 ? 0.6568 0.7931 1.0709 0.0315  0.2984  -0.1835 590 VAL D CG2 
19234 N N   . VAL D 591 ? 0.6460 0.7749 1.1160 0.0720  0.2527  -0.1209 591 VAL D N   
19235 C CA  . VAL D 591 ? 0.6122 0.7649 1.1004 0.0810  0.2394  -0.1116 591 VAL D CA  
19236 C C   . VAL D 591 ? 0.7493 0.9196 1.2012 0.0688  0.2312  -0.1101 591 VAL D C   
19237 O O   . VAL D 591 ? 0.8029 0.9657 1.2173 0.0599  0.2278  -0.1073 591 VAL D O   
19238 C CB  . VAL D 591 ? 0.5938 0.7419 1.0999 0.0989  0.2188  -0.0890 591 VAL D CB  
19239 C CG1 . VAL D 591 ? 0.7032 0.8237 1.2365 0.1114  0.2261  -0.0856 591 VAL D CG1 
19240 C CG2 . VAL D 591 ? 0.5876 0.7325 1.0525 0.0961  0.2003  -0.0713 591 VAL D CG2 
19241 N N   . MET D 592 ? 0.6546 0.8479 1.1210 0.0682  0.2289  -0.1121 592 MET D N   
19242 C CA  . MET D 592 ? 0.6632 0.8682 1.0988 0.0573  0.2221  -0.1100 592 MET D CA  
19243 C C   . MET D 592 ? 0.7745 0.9943 1.2246 0.0635  0.2016  -0.0987 592 MET D C   
19244 O O   . MET D 592 ? 0.8466 1.0785 1.3390 0.0735  0.1975  -0.0979 592 MET D O   
19245 C CB  . MET D 592 ? 0.6481 0.8640 1.0814 0.0455  0.2421  -0.1246 592 MET D CB  
19246 C CG  . MET D 592 ? 0.6621 0.8775 1.0494 0.0331  0.2402  -0.1230 592 MET D CG  
19247 S SD  . MET D 592 ? 0.8886 1.1134 1.2636 0.0198  0.2643  -0.1359 592 MET D SD  
19248 C CE  . MET D 592 ? 0.8929 1.1084 1.2667 0.0191  0.2838  -0.1547 592 MET D CE  
19249 N N   . VAL D 593 ? 0.6882 0.9078 1.1051 0.0583  0.1879  -0.0917 593 VAL D N   
19250 C CA  . VAL D 593 ? 0.5498 0.7822 0.9766 0.0627  0.1665  -0.0844 593 VAL D CA  
19251 C C   . VAL D 593 ? 0.7717 1.0055 1.1710 0.0510  0.1638  -0.0861 593 VAL D C   
19252 O O   . VAL D 593 ? 0.8449 1.0664 1.2060 0.0457  0.1678  -0.0855 593 VAL D O   
19253 C CB  . VAL D 593 ? 0.5215 0.7462 0.9364 0.0751  0.1466  -0.0708 593 VAL D CB  
19254 C CG1 . VAL D 593 ? 0.9482 1.1557 1.3164 0.0713  0.1472  -0.0657 593 VAL D CG1 
19255 C CG2 . VAL D 593 ? 0.7155 0.9556 1.1387 0.0799  0.1229  -0.0666 593 VAL D CG2 
19256 N N   . ASN D 594 ? 0.6434 0.8919 1.0654 0.0471  0.1570  -0.0885 594 ASN D N   
19257 C CA  . ASN D 594 ? 0.7031 0.9479 1.1035 0.0361  0.1546  -0.0895 594 ASN D CA  
19258 C C   . ASN D 594 ? 0.7809 1.0255 1.1706 0.0414  0.1292  -0.0857 594 ASN D C   
19259 O O   . ASN D 594 ? 0.7684 1.0221 1.1741 0.0520  0.1136  -0.0826 594 ASN D O   
19260 C CB  . ASN D 594 ? 0.6760 0.9328 1.1061 0.0242  0.1681  -0.0958 594 ASN D CB  
19261 C CG  . ASN D 594 ? 0.8079 1.0891 1.2932 0.0270  0.1612  -0.1001 594 ASN D CG  
19262 O OD1 . ASN D 594 ? 1.1369 1.4271 1.6371 0.0241  0.1442  -0.1014 594 ASN D OD1 
19263 N ND2 . ASN D 594 ? 0.7136 1.0074 1.2334 0.0330  0.1735  -0.1041 594 ASN D ND2 
19264 N N   . ARG D 595 ? 0.7780 1.0112 1.1382 0.0353  0.1247  -0.0860 595 ARG D N   
19265 C CA  . ARG D 595 ? 0.6434 0.8742 0.9878 0.0396  0.1028  -0.0862 595 ARG D CA  
19266 C C   . ARG D 595 ? 0.7526 1.0017 1.1335 0.0398  0.0855  -0.0918 595 ARG D C   
19267 O O   . ARG D 595 ? 0.7290 0.9829 1.1011 0.0487  0.0647  -0.0912 595 ARG D O   
19268 C CB  . ARG D 595 ? 0.7080 0.9215 1.0224 0.0328  0.1044  -0.0881 595 ARG D CB  
19269 C CG  . ARG D 595 ? 0.9255 1.1310 1.2084 0.0404  0.0875  -0.0892 595 ARG D CG  
19270 C CD  . ARG D 595 ? 0.9877 1.1744 1.2413 0.0377  0.0923  -0.0901 595 ARG D CD  
19271 N NE  . ARG D 595 ? 0.8521 1.0343 1.0811 0.0414  0.1042  -0.0838 595 ARG D NE  
19272 C CZ  . ARG D 595 ? 0.9185 1.1018 1.1243 0.0501  0.1011  -0.0814 595 ARG D CZ  
19273 N NH1 . ARG D 595 ? 1.0286 1.2154 1.2261 0.0574  0.0873  -0.0830 595 ARG D NH1 
19274 N NH2 . ARG D 595 ? 0.8352 1.0178 1.0257 0.0509  0.1119  -0.0777 595 ARG D NH2 
19275 N N   . GLU D 596 ? 0.7550 1.0168 1.1765 0.0296  0.0939  -0.0976 596 GLU D N   
19276 C CA  . GLU D 596 ? 0.6813 0.9663 1.1463 0.0275  0.0774  -0.1052 596 GLU D CA  
19277 C C   . GLU D 596 ? 0.9238 1.2305 1.4160 0.0428  0.0639  -0.1019 596 GLU D C   
19278 O O   . GLU D 596 ? 1.0934 1.4183 1.6039 0.0472  0.0395  -0.1062 596 GLU D O   
19279 C CB  . GLU D 596 ? 0.8848 1.1802 1.3913 0.0110  0.0947  -0.1116 596 GLU D CB  
19280 C CG  . GLU D 596 ? 1.0108 1.2824 1.4941 -0.0042 0.1056  -0.1124 596 GLU D CG  
19281 C CD  . GLU D 596 ? 1.2098 1.4673 1.6754 -0.0108 0.1347  -0.1055 596 GLU D CD  
19282 O OE1 . GLU D 596 ? 1.1423 1.3961 1.5858 -0.0013 0.1429  -0.1003 596 GLU D OE1 
19283 O OE2 . GLU D 596 ? 1.3447 1.5940 1.8172 -0.0262 0.1494  -0.1052 596 GLU D OE2 
19284 N N   . PHE D 597 ? 0.8967 1.2007 1.3917 0.0513  0.0787  -0.0947 597 PHE D N   
19285 C CA  . PHE D 597 ? 0.8641 1.1827 1.3858 0.0680  0.0682  -0.0889 597 PHE D CA  
19286 C C   . PHE D 597 ? 0.8466 1.1572 1.3314 0.0817  0.0443  -0.0789 597 PHE D C   
19287 O O   . PHE D 597 ? 0.8913 1.1788 1.3326 0.0852  0.0511  -0.0704 597 PHE D O   
19288 C CB  . PHE D 597 ? 0.9030 1.2120 1.4313 0.0726  0.0926  -0.0852 597 PHE D CB  
19289 C CG  . PHE D 597 ? 0.8609 1.1843 1.4314 0.0895  0.0870  -0.0809 597 PHE D CG  
19290 C CD1 . PHE D 597 ? 0.8509 1.2037 1.4835 0.0901  0.0903  -0.0895 597 PHE D CD1 
19291 C CD2 . PHE D 597 ? 0.8957 1.2028 1.4462 0.1053  0.0796  -0.0675 597 PHE D CD2 
19292 C CE1 . PHE D 597 ? 0.7873 1.1539 1.4630 0.1087  0.0844  -0.0854 597 PHE D CE1 
19293 C CE2 . PHE D 597 ? 0.8940 1.2099 1.4841 0.1231  0.0741  -0.0613 597 PHE D CE2 
19294 C CZ  . PHE D 597 ? 0.9221 1.2682 1.5753 0.1261  0.0755  -0.0706 597 PHE D CZ  
19295 N N   . GLY D 598 ? 0.8658 1.1975 1.3681 0.0888  0.0168  -0.0803 598 GLY D N   
19296 C CA  . GLY D 598 ? 0.9629 1.2900 1.4264 0.1018  -0.0074 -0.0709 598 GLY D CA  
19297 C C   . GLY D 598 ? 0.9918 1.3210 1.4623 0.1224  -0.0168 -0.0541 598 GLY D C   
19298 O O   . GLY D 598 ? 1.0446 1.3648 1.4738 0.1333  -0.0325 -0.0419 598 GLY D O   
19299 N N   . ALA D 599 ? 0.9613 1.3010 1.4827 0.1286  -0.0066 -0.0526 599 ALA D N   
19300 C CA  . ALA D 599 ? 0.8490 1.1872 1.3839 0.1503  -0.0150 -0.0356 599 ALA D CA  
19301 C C   . ALA D 599 ? 0.8682 1.1691 1.3683 0.1538  0.0066  -0.0218 599 ALA D C   
19302 O O   . ALA D 599 ? 0.9967 1.2797 1.4728 0.1390  0.0294  -0.0285 599 ALA D O   
19303 C CB  . ALA D 599 ? 0.8703 1.2352 1.4795 0.1569  -0.0115 -0.0421 599 ALA D CB  
19304 N N   . THR D 600 ? 0.9626 1.2516 1.4608 0.1731  -0.0015 -0.0021 600 THR D N   
19305 C CA  . THR D 600 ? 0.9093 1.1615 1.3809 0.1756  0.0187  0.0115  600 THR D CA  
19306 C C   . THR D 600 ? 0.8889 1.1333 1.4014 0.1712  0.0475  0.0003  600 THR D C   
19307 O O   . THR D 600 ? 0.8340 1.1026 1.3993 0.1726  0.0497  -0.0124 600 THR D O   
19308 C CB  . THR D 600 ? 0.8763 1.1151 1.3337 0.1974  0.0009  0.0382  600 THR D CB  
19309 O OG1 . THR D 600 ? 1.2098 1.4544 1.6168 0.1985  -0.0220 0.0461  600 THR D OG1 
19310 C CG2 . THR D 600 ? 0.8838 1.0815 1.3226 0.1994  0.0230  0.0535  600 THR D CG2 
19311 N N   . THR D 601 ? 0.8871 1.0999 1.3756 0.1646  0.0704  0.0032  601 THR D N   
19312 C CA  . THR D 601 ? 0.8939 1.0958 1.4114 0.1589  0.0986  -0.0102 601 THR D CA  
19313 C C   . THR D 601 ? 0.9102 1.0808 1.4389 0.1726  0.1072  0.0035  601 THR D C   
19314 O O   . THR D 601 ? 0.9775 1.1330 1.4859 0.1852  0.0922  0.0265  601 THR D O   
19315 C CB  . THR D 601 ? 0.7928 0.9862 1.2751 0.1369  0.1180  -0.0235 601 THR D CB  
19316 O OG1 . THR D 601 ? 0.8861 1.0534 1.3241 0.1338  0.1206  -0.0111 601 THR D OG1 
19317 C CG2 . THR D 601 ? 0.9819 1.1989 1.4509 0.1248  0.1095  -0.0338 601 THR D CG2 
19318 N N   . PRO D 602 ? 0.8120 0.9696 1.3706 0.1704  0.1320  -0.0100 602 PRO D N   
19319 C CA  . PRO D 602 ? 0.9221 1.0443 1.4943 0.1831  0.1409  0.0018  602 PRO D CA  
19320 C C   . PRO D 602 ? 0.9881 1.0752 1.5120 0.1755  0.1457  0.0174  602 PRO D C   
19321 O O   . PRO D 602 ? 0.9781 1.0321 1.5085 0.1865  0.1495  0.0336  602 PRO D O   
19322 C CB  . PRO D 602 ? 1.0627 1.1808 1.6712 0.1775  0.1689  -0.0235 602 PRO D CB  
19323 C CG  . PRO D 602 ? 0.9096 1.0677 1.5353 0.1690  0.1700  -0.0427 602 PRO D CG  
19324 C CD  . PRO D 602 ? 0.8358 1.0076 1.4153 0.1567  0.1540  -0.0365 602 PRO D CD  
19325 N N   . LEU D 603 ? 0.8959 0.9896 1.3742 0.1571  0.1466  0.0133  603 LEU D N   
19326 C CA  . LEU D 603 ? 0.8148 0.8821 1.2503 0.1485  0.1522  0.0270  603 LEU D CA  
19327 C C   . LEU D 603 ? 0.8795 0.9484 1.2805 0.1591  0.1294  0.0535  603 LEU D C   
19328 O O   . LEU D 603 ? 0.9520 1.0049 1.3133 0.1514  0.1339  0.0659  603 LEU D O   
19329 C CB  . LEU D 603 ? 0.6937 0.7697 1.1002 0.1253  0.1650  0.0087  603 LEU D CB  
19330 C CG  . LEU D 603 ? 0.8239 0.9002 1.2519 0.1128  0.1866  -0.0181 603 LEU D CG  
19331 C CD1 . LEU D 603 ? 0.6626 0.7528 1.0583 0.0933  0.1923  -0.0324 603 LEU D CD1 
19332 C CD2 . LEU D 603 ? 0.9945 1.0358 1.4408 0.1121  0.2050  -0.0196 603 LEU D CD2 
19333 N N   . GLY D 604 ? 0.7900 0.8802 1.2063 0.1760  0.1056  0.0610  604 GLY D N   
19334 C CA  . GLY D 604 ? 1.0072 1.1026 1.3884 0.1873  0.0810  0.0838  604 GLY D CA  
19335 C C   . GLY D 604 ? 0.9230 1.0368 1.2583 0.1733  0.0750  0.0762  604 GLY D C   
19336 O O   . GLY D 604 ? 1.0502 1.1578 1.3400 0.1759  0.0661  0.0935  604 GLY D O   
19337 N N   . MET D 605 ? 0.9705 1.1057 1.3164 0.1591  0.0809  0.0507  605 MET D N   
19338 C CA  . MET D 605 ? 0.9694 1.1196 1.2775 0.1468  0.0765  0.0410  605 MET D CA  
19339 C C   . MET D 605 ? 0.9806 1.1593 1.3127 0.1407  0.0695  0.0195  605 MET D C   
19340 O O   . MET D 605 ? 0.8993 1.0847 1.2738 0.1391  0.0789  0.0075  605 MET D O   
19341 C CB  . MET D 605 ? 0.9642 1.0997 1.2502 0.1295  0.1005  0.0338  605 MET D CB  
19342 C CG  . MET D 605 ? 1.0113 1.1238 1.2628 0.1294  0.1079  0.0533  605 MET D CG  
19343 S SD  . MET D 605 ? 0.9160 1.0185 1.1568 0.1081  0.1354  0.0407  605 MET D SD  
19344 C CE  . MET D 605 ? 0.7123 0.7903 0.9973 0.1073  0.1534  0.0377  605 MET D CE  
19345 N N   . THR D 606 ? 0.9923 1.1860 1.2967 0.1364  0.0555  0.0137  606 THR D N   
19346 C CA  . THR D 606 ? 0.9969 1.2132 1.3203 0.1280  0.0496  -0.0058 606 THR D CA  
19347 C C   . THR D 606 ? 0.9289 1.1381 1.2327 0.1114  0.0687  -0.0185 606 THR D C   
19348 O O   . THR D 606 ? 0.9291 1.1223 1.2039 0.1079  0.0809  -0.0129 606 THR D O   
19349 C CB  . THR D 606 ? 0.9071 1.1402 1.2120 0.1330  0.0223  -0.0064 606 THR D CB  
19350 O OG1 . THR D 606 ? 0.7997 1.0208 1.0496 0.1317  0.0220  -0.0004 606 THR D OG1 
19351 C CG2 . THR D 606 ? 0.8396 1.0854 1.1652 0.1506  -0.0011 0.0056  606 THR D CG2 
19352 N N   . PHE D 607 ? 0.9149 1.1366 1.2353 0.1012  0.0710  -0.0345 607 PHE D N   
19353 C CA  . PHE D 607 ? 0.8183 1.0333 1.1193 0.0878  0.0865  -0.0442 607 PHE D CA  
19354 C C   . PHE D 607 ? 0.7938 1.0012 1.0484 0.0875  0.0821  -0.0412 607 PHE D C   
19355 O O   . PHE D 607 ? 0.9445 1.1431 1.1804 0.0816  0.0964  -0.0422 607 PHE D O   
19356 C CB  . PHE D 607 ? 0.8400 1.0668 1.1612 0.0782  0.0865  -0.0577 607 PHE D CB  
19357 C CG  . PHE D 607 ? 0.6832 0.9014 0.9831 0.0667  0.1004  -0.0646 607 PHE D CG  
19358 C CD1 . PHE D 607 ? 0.5253 0.7381 0.7933 0.0650  0.0930  -0.0668 607 PHE D CD1 
19359 C CD2 . PHE D 607 ? 0.6343 0.8500 0.9451 0.0590  0.1202  -0.0693 607 PHE D CD2 
19360 C CE1 . PHE D 607 ? 0.5394 0.7443 0.7898 0.0574  0.1038  -0.0712 607 PHE D CE1 
19361 C CE2 . PHE D 607 ? 0.8136 1.0226 1.1018 0.0502  0.1301  -0.0735 607 PHE D CE2 
19362 C CZ  . PHE D 607 ? 0.8043 1.0078 1.0640 0.0502  0.1211  -0.0732 607 PHE D CZ  
19363 N N   . GLY D 608 ? 0.7140 0.9273 0.9515 0.0941  0.0626  -0.0391 608 GLY D N   
19364 C CA  . GLY D 608 ? 0.8466 1.0547 1.0401 0.0952  0.0597  -0.0382 608 GLY D CA  
19365 C C   . GLY D 608 ? 0.8652 1.0620 1.0357 0.0987  0.0710  -0.0238 608 GLY D C   
19366 O O   . GLY D 608 ? 0.9898 1.1826 1.1349 0.0947  0.0814  -0.0255 608 GLY D O   
19367 N N   . GLU D 609 ? 0.9210 1.1124 1.1036 0.1064  0.0696  -0.0092 609 GLU D N   
19368 C CA  . GLU D 609 ? 1.0007 1.1766 1.1654 0.1084  0.0820  0.0071  609 GLU D CA  
19369 C C   . GLU D 609 ? 0.8818 1.0492 1.0602 0.0967  0.1052  0.0011  609 GLU D C   
19370 O O   . GLU D 609 ? 0.8694 1.0304 1.0276 0.0914  0.1181  0.0051  609 GLU D O   
19371 C CB  . GLU D 609 ? 0.9393 1.1071 1.1178 0.1208  0.0739  0.0254  609 GLU D CB  
19372 C CG  . GLU D 609 ? 1.0422 1.2193 1.1981 0.1337  0.0488  0.0346  609 GLU D CG  
19373 C CD  . GLU D 609 ? 1.2084 1.3763 1.3724 0.1490  0.0388  0.0572  609 GLU D CD  
19374 O OE1 . GLU D 609 ? 1.1497 1.3247 1.3579 0.1558  0.0308  0.0553  609 GLU D OE1 
19375 O OE2 . GLU D 609 ? 1.2434 1.3972 1.3702 0.1549  0.0398  0.0779  609 GLU D OE2 
19376 N N   . LEU D 610 ? 0.9140 1.0838 1.1266 0.0922  0.1107  -0.0097 610 LEU D N   
19377 C CA  . LEU D 610 ? 0.8460 1.0103 1.0698 0.0810  0.1304  -0.0187 610 LEU D CA  
19378 C C   . LEU D 610 ? 0.8191 0.9923 1.0216 0.0723  0.1344  -0.0298 610 LEU D C   
19379 O O   . LEU D 610 ? 0.8290 0.9998 1.0259 0.0643  0.1476  -0.0329 610 LEU D O   
19380 C CB  . LEU D 610 ? 0.6542 0.8215 0.9149 0.0793  0.1354  -0.0291 610 LEU D CB  
19381 C CG  . LEU D 610 ? 0.7715 0.9264 1.0622 0.0865  0.1405  -0.0223 610 LEU D CG  
19382 C CD1 . LEU D 610 ? 0.7925 0.9591 1.1212 0.0900  0.1388  -0.0314 610 LEU D CD1 
19383 C CD2 . LEU D 610 ? 0.7228 0.8611 1.0176 0.0779  0.1608  -0.0264 610 LEU D CD2 
19384 N N   . ALA D 611 ? 0.7459 0.9292 0.9392 0.0740  0.1223  -0.0362 611 ALA D N   
19385 C CA  . ALA D 611 ? 0.6678 0.8569 0.8430 0.0691  0.1243  -0.0456 611 ALA D CA  
19386 C C   . ALA D 611 ? 0.8287 1.0190 0.9776 0.0701  0.1287  -0.0412 611 ALA D C   
19387 O O   . ALA D 611 ? 0.8056 1.0017 0.9482 0.0653  0.1363  -0.0478 611 ALA D O   
19388 C CB  . ALA D 611 ? 0.8008 0.9945 0.9731 0.0716  0.1103  -0.0522 611 ALA D CB  
19389 N N   . SER D 612 ? 0.8284 1.0152 0.9618 0.0767  0.1242  -0.0297 612 SER D N   
19390 C CA  . SER D 612 ? 0.9037 1.0927 1.0118 0.0769  0.1321  -0.0243 612 SER D CA  
19391 C C   . SER D 612 ? 0.9824 1.1679 1.1029 0.0673  0.1506  -0.0210 612 SER D C   
19392 O O   . SER D 612 ? 0.9736 1.1674 1.0838 0.0630  0.1607  -0.0224 612 SER D O   
19393 C CB  . SER D 612 ? 0.8149 0.9991 0.8994 0.0858  0.1241  -0.0102 612 SER D CB  
19394 O OG  . SER D 612 ? 1.0750 1.2462 1.1737 0.0882  0.1244  0.0044  612 SER D OG  
19395 N N   . MET D 613 ? 0.9718 1.1462 1.1175 0.0635  0.1554  -0.0189 613 MET D N   
19396 C CA  . MET D 613 ? 0.9098 1.0776 1.0707 0.0528  0.1721  -0.0191 613 MET D CA  
19397 C C   . MET D 613 ? 1.0018 1.1801 1.1773 0.0431  0.1775  -0.0371 613 MET D C   
19398 O O   . MET D 613 ? 0.9504 1.1275 1.1376 0.0325  0.1900  -0.0418 613 MET D O   
19399 C CB  . MET D 613 ? 0.7548 0.9017 0.9364 0.0548  0.1752  -0.0100 613 MET D CB  
19400 C CG  . MET D 613 ? 0.9606 1.0959 1.1295 0.0670  0.1663  0.0102  613 MET D CG  
19401 S SD  . MET D 613 ? 0.9448 1.0490 1.1339 0.0683  0.1770  0.0273  613 MET D SD  
19402 C CE  . MET D 613 ? 0.7783 0.8808 1.0089 0.0666  0.1795  0.0088  613 MET D CE  
19403 N N   . THR D 614 ? 0.7156 0.9029 0.8902 0.0459  0.1684  -0.0469 614 THR D N   
19404 C CA  . THR D 614 ? 0.7419 0.9382 0.9241 0.0380  0.1725  -0.0612 614 THR D CA  
19405 C C   . THR D 614 ? 0.8377 1.0504 1.0042 0.0396  0.1670  -0.0673 614 THR D C   
19406 O O   . THR D 614 ? 0.9338 1.1587 1.1021 0.0331  0.1712  -0.0759 614 THR D O   
19407 C CB  . THR D 614 ? 0.7447 0.9355 0.9403 0.0388  0.1704  -0.0662 614 THR D CB  
19408 O OG1 . THR D 614 ? 1.0504 1.2435 1.2386 0.0464  0.1581  -0.0635 614 THR D OG1 
19409 C CG2 . THR D 614 ? 0.6078 0.7839 0.8245 0.0402  0.1757  -0.0616 614 THR D CG2 
19410 N N   . GLY D 615 ? 0.7593 0.9721 0.9123 0.0487  0.1566  -0.0641 615 GLY D N   
19411 C CA  . GLY D 615 ? 0.7199 0.9434 0.8601 0.0532  0.1510  -0.0696 615 GLY D CA  
19412 C C   . GLY D 615 ? 0.6882 0.9255 0.8205 0.0551  0.1555  -0.0697 615 GLY D C   
19413 O O   . GLY D 615 ? 0.8171 1.0544 0.9507 0.0515  0.1640  -0.0637 615 GLY D O   
19414 N N   . GLY D 616 ? 0.6823 0.9307 0.8081 0.0612  0.1509  -0.0757 616 GLY D N   
19415 C CA  . GLY D 616 ? 0.8322 1.0989 0.9550 0.0651  0.1557  -0.0784 616 GLY D CA  
19416 C C   . GLY D 616 ? 0.6865 0.9762 0.8235 0.0610  0.1588  -0.0856 616 GLY D C   
19417 O O   . GLY D 616 ? 0.8357 1.1461 0.9777 0.0634  0.1642  -0.0889 616 GLY D O   
19418 N N   . GLY D 617 ? 0.6386 0.9280 0.7826 0.0548  0.1554  -0.0892 617 GLY D N   
19419 C CA  . GLY D 617 ? 0.6581 0.9720 0.8139 0.0506  0.1547  -0.0974 617 GLY D CA  
19420 C C   . GLY D 617 ? 0.7362 1.0639 0.9104 0.0366  0.1665  -0.1013 617 GLY D C   
19421 O O   . GLY D 617 ? 0.7132 1.0695 0.9024 0.0340  0.1676  -0.1087 617 GLY D O   
19422 N N   . VAL D 618 ? 0.9084 1.2160 1.0851 0.0274  0.1753  -0.0964 618 VAL D N   
19423 C CA  . VAL D 618 ? 0.7107 1.0222 0.9058 0.0126  0.1886  -0.0984 618 VAL D CA  
19424 C C   . VAL D 618 ? 0.8265 1.1230 1.0298 0.0015  0.1910  -0.1048 618 VAL D C   
19425 O O   . VAL D 618 ? 0.9424 1.2172 1.1367 0.0061  0.1879  -0.1006 618 VAL D O   
19426 C CB  . VAL D 618 ? 0.6222 0.9181 0.8115 0.0135  0.1992  -0.0842 618 VAL D CB  
19427 C CG1 . VAL D 618 ? 0.9375 1.2322 1.1464 -0.0030 0.2154  -0.0832 618 VAL D CG1 
19428 C CG2 . VAL D 618 ? 0.6970 1.0070 0.8731 0.0254  0.1982  -0.0806 618 VAL D CG2 
19429 N N   . GLN D 619 ? 0.9027 1.2121 1.1254 -0.0135 0.1971  -0.1170 619 GLN D N   
19430 C CA  . GLN D 619 ? 0.8368 1.1316 1.0675 -0.0248 0.2010  -0.1276 619 GLN D CA  
19431 C C   . GLN D 619 ? 0.8252 1.0871 1.0629 -0.0275 0.2134  -0.1164 619 GLN D C   
19432 O O   . GLN D 619 ? 0.8030 1.0610 1.0540 -0.0359 0.2248  -0.1111 619 GLN D O   
19433 C CB  . GLN D 619 ? 0.6791 0.9973 0.9297 -0.0413 0.2030  -0.1467 619 GLN D CB  
19434 C CG  . GLN D 619 ? 0.5338 0.8854 0.7763 -0.0368 0.1871  -0.1577 619 GLN D CG  
19435 C CD  . GLN D 619 ? 0.6028 0.9791 0.8634 -0.0534 0.1852  -0.1797 619 GLN D CD  
19436 O OE1 . GLN D 619 ? 0.6965 1.1026 0.9801 -0.0609 0.1854  -0.1862 619 GLN D OE1 
19437 N NE2 . GLN D 619 ? 0.8245 1.1920 1.0762 -0.0602 0.1834  -0.1938 619 GLN D NE2 
19438 N N   . THR D 620 ? 0.7059 0.9448 0.9358 -0.0197 0.2112  -0.1115 620 THR D N   
19439 C CA  . THR D 620 ? 0.6815 0.8897 0.9187 -0.0175 0.2193  -0.0990 620 THR D CA  
19440 C C   . THR D 620 ? 0.7115 0.8996 0.9653 -0.0243 0.2273  -0.1102 620 THR D C   
19441 O O   . THR D 620 ? 0.8493 1.0292 1.1006 -0.0165 0.2240  -0.1116 620 THR D O   
19442 C CB  . THR D 620 ? 0.8343 1.0348 1.0550 -0.0008 0.2095  -0.0840 620 THR D CB  
19443 O OG1 . THR D 620 ? 0.8408 1.0491 1.0536 0.0041  0.2006  -0.0924 620 THR D OG1 
19444 C CG2 . THR D 620 ? 0.8551 1.0676 1.0594 0.0064  0.2050  -0.0726 620 THR D CG2 
19445 N N   . PRO D 621 ? 0.6995 0.8784 0.9731 -0.0391 0.2394  -0.1192 621 PRO D N   
19446 C CA  . PRO D 621 ? 0.6608 0.8169 0.9514 -0.0446 0.2484  -0.1327 621 PRO D CA  
19447 C C   . PRO D 621 ? 0.6422 0.7700 0.9384 -0.0303 0.2502  -0.1179 621 PRO D C   
19448 O O   . PRO D 621 ? 0.8080 0.9220 1.1028 -0.0223 0.2498  -0.0955 621 PRO D O   
19449 C CB  . PRO D 621 ? 0.6302 0.7752 0.9432 -0.0625 0.2617  -0.1396 621 PRO D CB  
19450 C CG  . PRO D 621 ? 0.6572 0.8339 0.9656 -0.0700 0.2577  -0.1394 621 PRO D CG  
19451 C CD  . PRO D 621 ? 0.8484 1.0368 1.1332 -0.0526 0.2471  -0.1193 621 PRO D CD  
19452 N N   . GLY D 622 ? 0.7197 0.8419 1.0216 -0.0265 0.2518  -0.1307 622 GLY D N   
19453 C CA  . GLY D 622 ? 0.7246 0.8257 1.0399 -0.0123 0.2533  -0.1205 622 GLY D CA  
19454 C C   . GLY D 622 ? 0.7740 0.8898 1.0770 0.0020  0.2407  -0.1104 622 GLY D C   
19455 O O   . GLY D 622 ? 0.8264 0.9338 1.1450 0.0123  0.2415  -0.1087 622 GLY D O   
19456 N N   . PHE D 623 ? 0.7780 0.9159 1.0571 0.0026  0.2294  -0.1047 623 PHE D N   
19457 C CA  . PHE D 623 ? 0.8026 0.9520 1.0711 0.0141  0.2173  -0.0963 623 PHE D CA  
19458 C C   . PHE D 623 ? 0.7709 0.9429 1.0174 0.0098  0.2113  -0.1050 623 PHE D C   
19459 O O   . PHE D 623 ? 0.8412 1.0250 1.0757 0.0032  0.2097  -0.1085 623 PHE D O   
19460 C CB  . PHE D 623 ? 0.6560 0.8021 0.9157 0.0240  0.2072  -0.0749 623 PHE D CB  
19461 C CG  . PHE D 623 ? 0.7952 0.9176 1.0698 0.0300  0.2110  -0.0603 623 PHE D CG  
19462 C CD1 . PHE D 623 ? 0.7345 0.8440 1.0078 0.0228  0.2198  -0.0533 623 PHE D CD1 
19463 C CD2 . PHE D 623 ? 0.8918 1.0056 1.1825 0.0432  0.2053  -0.0518 623 PHE D CD2 
19464 C CE1 . PHE D 623 ? 0.8120 0.8947 1.0961 0.0290  0.2239  -0.0361 623 PHE D CE1 
19465 C CE2 . PHE D 623 ? 0.9455 1.0359 1.2486 0.0515  0.2068  -0.0355 623 PHE D CE2 
19466 C CZ  . PHE D 623 ? 0.9191 0.9915 1.2165 0.0446  0.2164  -0.0265 623 PHE D CZ  
19467 N N   . MET D 624 ? 0.7922 0.9705 1.0355 0.0139  0.2082  -0.1075 624 MET D N   
19468 C CA  . MET D 624 ? 0.8093 1.0037 1.0298 0.0113  0.2027  -0.1121 624 MET D CA  
19469 C C   . MET D 624 ? 0.8235 1.0196 1.0405 0.0186  0.1953  -0.1039 624 MET D C   
19470 O O   . MET D 624 ? 0.7638 0.9540 1.0004 0.0228  0.1976  -0.1015 624 MET D O   
19471 C CB  . MET D 624 ? 0.7870 0.9866 1.0020 0.0016  0.2123  -0.1300 624 MET D CB  
19472 C CG  . MET D 624 ? 0.8734 1.0684 1.0980 0.0022  0.2225  -0.1361 624 MET D CG  
19473 S SD  . MET D 624 ? 0.9178 1.1221 1.1215 -0.0083 0.2335  -0.1563 624 MET D SD  
19474 C CE  . MET D 624 ? 1.0058 1.2248 1.1732 -0.0070 0.2192  -0.1460 624 MET D CE  
19475 N N   . GLY D 625 ? 0.8387 1.0431 1.0345 0.0200  0.1865  -0.1005 625 GLY D N   
19476 C CA  . GLY D 625 ? 0.8227 1.0259 1.0146 0.0245  0.1799  -0.0939 625 GLY D CA  
19477 C C   . GLY D 625 ? 0.7994 1.0057 0.9767 0.0190  0.1855  -0.0983 625 GLY D C   
19478 O O   . GLY D 625 ? 0.8134 1.0267 0.9732 0.0149  0.1872  -0.1043 625 GLY D O   
19479 N N   . HIS D 626 ? 0.8193 1.0216 1.0033 0.0181  0.1886  -0.0951 626 HIS D N   
19480 C CA  . HIS D 626 ? 0.8611 1.0637 1.0278 0.0120  0.1970  -0.0961 626 HIS D CA  
19481 C C   . HIS D 626 ? 0.8526 1.0499 1.0324 0.0098  0.2005  -0.0900 626 HIS D C   
19482 O O   . HIS D 626 ? 0.8873 1.0846 1.0950 0.0126  0.1966  -0.0889 626 HIS D O   
19483 C CB  . HIS D 626 ? 0.8082 1.0159 0.9756 0.0051  0.2127  -0.1090 626 HIS D CB  
19484 C CG  . HIS D 626 ? 0.6656 0.8720 0.8683 0.0055  0.2225  -0.1150 626 HIS D CG  
19485 N ND1 . HIS D 626 ? 0.8587 1.0674 1.0774 0.0021  0.2363  -0.1177 626 HIS D ND1 
19486 C CD2 . HIS D 626 ? 0.8079 1.0111 1.0339 0.0101  0.2205  -0.1174 626 HIS D CD2 
19487 C CE1 . HIS D 626 ? 0.7752 0.9843 1.0294 0.0063  0.2408  -0.1229 626 HIS D CE1 
19488 N NE2 . HIS D 626 ? 0.7913 0.9947 1.0492 0.0116  0.2311  -0.1217 626 HIS D NE2 
19489 N N   . GLY D 627 ? 0.8749 1.0684 1.0347 0.0043  0.2078  -0.0858 627 GLY D N   
19490 C CA  . GLY D 627 ? 0.9719 1.1597 1.1451 -0.0013 0.2151  -0.0798 627 GLY D CA  
19491 C C   . GLY D 627 ? 1.0834 1.2811 1.2840 -0.0076 0.2337  -0.0885 627 GLY D C   
19492 O O   . GLY D 627 ? 1.1107 1.3157 1.3132 -0.0070 0.2417  -0.0994 627 GLY D O   
19493 N N   . ARG D 628 ? 0.9676 1.1663 1.1932 -0.0139 0.2418  -0.0855 628 ARG D N   
19494 C CA  . ARG D 628 ? 0.8100 1.0227 1.0691 -0.0187 0.2610  -0.0948 628 ARG D CA  
19495 C C   . ARG D 628 ? 0.9261 1.1409 1.1598 -0.0274 0.2855  -0.0983 628 ARG D C   
19496 O O   . ARG D 628 ? 1.0469 1.2743 1.3035 -0.0299 0.3043  -0.1099 628 ARG D O   
19497 C CB  . ARG D 628 ? 0.7771 0.9968 1.0804 -0.0230 0.2604  -0.0925 628 ARG D CB  
19498 C CG  . ARG D 628 ? 1.1181 1.3332 1.4180 -0.0369 0.2768  -0.0849 628 ARG D CG  
19499 C CD  . ARG D 628 ? 1.2914 1.5070 1.6275 -0.0422 0.2669  -0.0813 628 ARG D CD  
19500 N NE  . ARG D 628 ? 1.3251 1.5641 1.7172 -0.0380 0.2614  -0.0918 628 ARG D NE  
19501 C CZ  . ARG D 628 ? 1.3560 1.6014 1.7824 -0.0384 0.2438  -0.0931 628 ARG D CZ  
19502 N NH1 . ARG D 628 ? 1.4086 1.6357 1.8202 -0.0438 0.2317  -0.0867 628 ARG D NH1 
19503 N NH2 . ARG D 628 ? 1.2812 1.5512 1.7572 -0.0325 0.2370  -0.1017 628 ARG D NH2 
19504 N N   . GLN D 629 ? 0.9212 1.1243 1.1070 -0.0307 0.2852  -0.0886 629 GLN D N   
19505 C CA  . GLN D 629 ? 1.0649 1.2696 1.2163 -0.0386 0.3066  -0.0900 629 GLN D CA  
19506 C C   . GLN D 629 ? 0.9660 1.1785 1.0951 -0.0352 0.3081  -0.1060 629 GLN D C   
19507 O O   . GLN D 629 ? 1.0834 1.3025 1.1944 -0.0412 0.3286  -0.1156 629 GLN D O   
19508 C CB  . GLN D 629 ? 1.0942 1.2820 1.2006 -0.0420 0.3037  -0.0704 629 GLN D CB  
19509 C CG  . GLN D 629 ? 1.2474 1.4206 1.3745 -0.0458 0.2988  -0.0553 629 GLN D CG  
19510 C CD  . GLN D 629 ? 1.2410 1.4007 1.3619 -0.0352 0.2708  -0.0481 629 GLN D CD  
19511 O OE1 . GLN D 629 ? 1.1559 1.3231 1.2993 -0.0269 0.2551  -0.0573 629 GLN D OE1 
19512 N NE2 . GLN D 629 ? 1.1026 1.2409 1.1922 -0.0346 0.2653  -0.0308 629 GLN D NE2 
19513 N N   . PHE D 630 ? 0.9955 1.2072 1.1262 -0.0267 0.2879  -0.1102 630 PHE D N   
19514 C CA  . PHE D 630 ? 1.0689 1.2868 1.1849 -0.0254 0.2876  -0.1268 630 PHE D CA  
19515 C C   . PHE D 630 ? 0.9768 1.2007 1.1323 -0.0250 0.3019  -0.1454 630 PHE D C   
19516 O O   . PHE D 630 ? 0.9457 1.1718 1.0932 -0.0260 0.3062  -0.1626 630 PHE D O   
19517 C CB  . PHE D 630 ? 1.0970 1.3126 1.2071 -0.0181 0.2630  -0.1233 630 PHE D CB  
19518 C CG  . PHE D 630 ? 0.9925 1.2147 1.0936 -0.0189 0.2601  -0.1402 630 PHE D CG  
19519 C CD1 . PHE D 630 ? 1.0812 1.3109 1.1422 -0.0241 0.2627  -0.1489 630 PHE D CD1 
19520 C CD2 . PHE D 630 ? 0.8965 1.1171 1.0277 -0.0150 0.2535  -0.1465 630 PHE D CD2 
19521 C CE1 . PHE D 630 ? 1.0009 1.2382 1.0572 -0.0270 0.2586  -0.1673 630 PHE D CE1 
19522 C CE2 . PHE D 630 ? 0.8822 1.1068 1.0088 -0.0184 0.2520  -0.1622 630 PHE D CE2 
19523 C CZ  . PHE D 630 ? 1.0024 1.2362 1.0940 -0.0251 0.2543  -0.1742 630 PHE D CZ  
19524 N N   . ILE D 631 ? 0.9874 1.2139 1.1879 -0.0230 0.3085  -0.1431 631 ILE D N   
19525 C CA  . ILE D 631 ? 0.8666 1.0983 1.1102 -0.0189 0.3205  -0.1586 631 ILE D CA  
19526 C C   . ILE D 631 ? 0.9109 1.1490 1.1439 -0.0250 0.3475  -0.1778 631 ILE D C   
19527 O O   . ILE D 631 ? 0.9776 1.2131 1.2202 -0.0223 0.3537  -0.1962 631 ILE D O   
19528 C CB  . ILE D 631 ? 0.8517 1.0907 1.1476 -0.0145 0.3195  -0.1512 631 ILE D CB  
19529 C CG1 . ILE D 631 ? 0.7734 1.0060 1.0780 -0.0071 0.2916  -0.1368 631 ILE D CG1 
19530 C CG2 . ILE D 631 ? 0.7900 1.0366 1.1338 -0.0078 0.3335  -0.1667 631 ILE D CG2 
19531 C CD1 . ILE D 631 ? 1.0042 1.2451 1.3460 -0.0062 0.2852  -0.1278 631 ILE D CD1 
19532 N N   . ALA D 632 ? 0.9665 1.2110 1.1790 -0.0336 0.3651  -0.1742 632 ALA D N   
19533 C CA  . ALA D 632 ? 0.9878 1.2401 1.1843 -0.0400 0.3938  -0.1928 632 ALA D CA  
19534 C C   . ALA D 632 ? 1.0679 1.3165 1.2020 -0.0450 0.3919  -0.2021 632 ALA D C   
19535 O O   . ALA D 632 ? 1.0574 1.3117 1.1744 -0.0495 0.4134  -0.2228 632 ALA D O   
19536 C CB  . ALA D 632 ? 0.9354 1.1968 1.1324 -0.0485 0.4158  -0.1835 632 ALA D CB  
19537 N N   . SER D 633 ? 1.2047 1.4463 1.3060 -0.0438 0.3662  -0.1887 633 SER D N   
19538 C CA  . SER D 633 ? 1.1806 1.4238 1.2255 -0.0476 0.3585  -0.1961 633 SER D CA  
19539 C C   . SER D 633 ? 1.0058 1.2521 1.0518 -0.0498 0.3671  -0.2276 633 SER D C   
19540 O O   . SER D 633 ? 0.9184 1.1592 1.0099 -0.0451 0.3665  -0.2391 633 SER D O   
19541 C CB  . SER D 633 ? 1.1730 1.4118 1.2050 -0.0425 0.3273  -0.1806 633 SER D CB  
19542 O OG  . SER D 633 ? 1.1278 1.3734 1.1155 -0.0450 0.3162  -0.1902 633 SER D OG  
19543 N N   . LYS D 634 ? 1.0421 1.2955 1.0356 -0.0568 0.3741  -0.2415 634 LYS D N   
19544 C CA  . LYS D 634 ? 0.9622 1.2179 0.9516 -0.0609 0.3819  -0.2758 634 LYS D CA  
19545 C C   . LYS D 634 ? 0.9707 1.2237 0.9681 -0.0601 0.3552  -0.2815 634 LYS D C   
19546 O O   . LYS D 634 ? 1.0233 1.2725 1.0365 -0.0636 0.3592  -0.3087 634 LYS D O   
19547 C CB  . LYS D 634 ? 1.0235 1.2900 0.9479 -0.0693 0.3947  -0.2907 634 LYS D CB  
19548 C CG  . LYS D 634 ? 1.3116 1.5820 1.2111 -0.0720 0.4183  -0.2754 634 LYS D CG  
19549 C CD  . LYS D 634 ? 1.4083 1.6888 1.2473 -0.0802 0.4386  -0.2963 634 LYS D CD  
19550 C CE  . LYS D 634 ? 1.5548 1.8385 1.3678 -0.0844 0.4659  -0.2787 634 LYS D CE  
19551 N NZ  . LYS D 634 ? 1.4946 1.7712 1.2895 -0.0827 0.4502  -0.2372 634 LYS D NZ  
19552 N N   . LYS D 635 ? 0.9264 1.1812 0.9154 -0.0561 0.3298  -0.2568 635 LYS D N   
19553 C CA  . LYS D 635 ? 0.9931 1.2496 0.9919 -0.0556 0.3059  -0.2593 635 LYS D CA  
19554 C C   . LYS D 635 ? 1.0019 1.2456 1.0565 -0.0488 0.3002  -0.2485 635 LYS D C   
19555 O O   . LYS D 635 ? 0.8832 1.1277 0.9495 -0.0486 0.2831  -0.2474 635 LYS D O   
19556 C CB  . LYS D 635 ? 0.8493 1.1177 0.8079 -0.0532 0.2823  -0.2401 635 LYS D CB  
19557 C CG  . LYS D 635 ? 1.1447 1.4269 1.0415 -0.0584 0.2828  -0.2478 635 LYS D CG  
19558 C CD  . LYS D 635 ? 1.1346 1.4266 1.0194 -0.0684 0.2864  -0.2849 635 LYS D CD  
19559 C CE  . LYS D 635 ? 1.1837 1.4957 1.0041 -0.0722 0.2742  -0.2915 635 LYS D CE  
19560 N NZ  . LYS D 635 ? 0.9720 1.2884 0.7624 -0.0819 0.2937  -0.3240 635 LYS D NZ  
19561 N N   . PHE D 636 ? 0.9583 1.1925 1.0473 -0.0433 0.3143  -0.2409 636 PHE D N   
19562 C CA  . PHE D 636 ? 0.9093 1.1322 1.0464 -0.0354 0.3077  -0.2297 636 PHE D CA  
19563 C C   . PHE D 636 ? 0.9748 1.1864 1.1411 -0.0372 0.3135  -0.2507 636 PHE D C   
19564 O O   . PHE D 636 ? 1.1437 1.3494 1.3271 -0.0376 0.3336  -0.2692 636 PHE D O   
19565 C CB  . PHE D 636 ? 0.9425 1.1632 1.1093 -0.0292 0.3198  -0.2182 636 PHE D CB  
19566 C CG  . PHE D 636 ? 0.9180 1.1299 1.1307 -0.0195 0.3104  -0.2052 636 PHE D CG  
19567 C CD1 . PHE D 636 ? 0.9269 1.1389 1.1379 -0.0149 0.2908  -0.1828 636 PHE D CD1 
19568 C CD2 . PHE D 636 ? 0.9074 1.1106 1.1632 -0.0138 0.3209  -0.2153 636 PHE D CD2 
19569 C CE1 . PHE D 636 ? 0.9678 1.1732 1.2144 -0.0059 0.2812  -0.1713 636 PHE D CE1 
19570 C CE2 . PHE D 636 ? 0.9061 1.1018 1.1993 -0.0034 0.3101  -0.2007 636 PHE D CE2 
19571 C CZ  . PHE D 636 ? 0.9929 1.1908 1.2788 0.0000  0.2900  -0.1790 636 PHE D CZ  
19572 N N   . MET D 637 ? 0.8926 1.1007 1.0649 -0.0388 0.2979  -0.2487 637 MET D N   
19573 C CA  . MET D 637 ? 0.8636 1.0556 1.0660 -0.0422 0.3037  -0.2659 637 MET D CA  
19574 C C   . MET D 637 ? 0.9554 1.1487 1.1412 -0.0532 0.3171  -0.2996 637 MET D C   
19575 O O   . MET D 637 ? 1.0978 1.2727 1.3131 -0.0538 0.3320  -0.3182 637 MET D O   
19576 C CB  . MET D 637 ? 0.8342 1.0075 1.0828 -0.0313 0.3141  -0.2593 637 MET D CB  
19577 C CG  . MET D 637 ? 0.9619 1.1369 1.2237 -0.0201 0.3014  -0.2291 637 MET D CG  
19578 S SD  . MET D 637 ? 0.8504 1.0018 1.1616 -0.0085 0.3000  -0.2171 637 MET D SD  
19579 C CE  . MET D 637 ? 0.9469 1.0818 1.2582 -0.0202 0.3015  -0.2328 637 MET D CE  
19580 N N   . LYS D 638 ? 0.9474 1.1607 1.0868 -0.0607 0.3111  -0.3075 638 LYS D N   
19581 C CA  . LYS D 638 ? 1.0276 1.2455 1.1434 -0.0719 0.3213  -0.3417 638 LYS D CA  
19582 C C   . LYS D 638 ? 0.9877 1.1932 1.1286 -0.0820 0.3206  -0.3662 638 LYS D C   
19583 O O   . LYS D 638 ? 0.9901 1.1828 1.1402 -0.0873 0.3380  -0.3960 638 LYS D O   
19584 C CB  . LYS D 638 ? 0.8916 1.1355 0.9493 -0.0774 0.3081  -0.3421 638 LYS D CB  
19585 C CG  . LYS D 638 ? 1.0636 1.3153 1.0844 -0.0867 0.3212  -0.3749 638 LYS D CG  
19586 C CD  . LYS D 638 ? 1.1303 1.4082 1.0902 -0.0904 0.3041  -0.3721 638 LYS D CD  
19587 C CE  . LYS D 638 ? 1.0253 1.3132 0.9432 -0.1009 0.3133  -0.4078 638 LYS D CE  
19588 N NZ  . LYS D 638 ? 1.1332 1.4492 0.9939 -0.1044 0.2897  -0.4067 638 LYS D NZ  
19589 N N   . GLY D 639 ? 0.9231 1.1317 1.0766 -0.0851 0.3024  -0.3545 639 GLY D N   
19590 C CA  . GLY D 639 ? 1.0032 1.2002 1.1837 -0.0973 0.3019  -0.3743 639 GLY D CA  
19591 C C   . GLY D 639 ? 1.0138 1.1742 1.2427 -0.0935 0.3189  -0.3763 639 GLY D C   
19592 O O   . GLY D 639 ? 1.0799 1.2229 1.3319 -0.1050 0.3245  -0.3977 639 GLY D O   
19593 N N   . GLU D 640 ? 0.8738 1.0218 1.1206 -0.0773 0.3265  -0.3541 640 GLU D N   
19594 C CA  . GLU D 640 ? 0.9632 1.0774 1.2567 -0.0691 0.3401  -0.3514 640 GLU D CA  
19595 C C   . GLU D 640 ? 1.1288 1.2326 1.4342 -0.0613 0.3625  -0.3699 640 GLU D C   
19596 O O   . GLU D 640 ? 1.2116 1.2873 1.5586 -0.0522 0.3744  -0.3704 640 GLU D O   
19597 C CB  . GLU D 640 ? 0.7480 0.8576 1.0599 -0.0548 0.3298  -0.3123 640 GLU D CB  
19598 C CG  . GLU D 640 ? 0.9891 1.0970 1.3050 -0.0609 0.3152  -0.2955 640 GLU D CG  
19599 C CD  . GLU D 640 ? 1.0572 1.1980 1.3388 -0.0654 0.2967  -0.2852 640 GLU D CD  
19600 O OE1 . GLU D 640 ? 1.0029 1.1582 1.2680 -0.0546 0.2888  -0.2654 640 GLU D OE1 
19601 O OE2 . GLU D 640 ? 0.9723 1.1244 1.2470 -0.0796 0.2898  -0.2973 640 GLU D OE2 
19602 N N   . GLY D 641 ? 1.0370 1.1632 1.3068 -0.0639 0.3688  -0.3842 641 GLY D N   
19603 C CA  . GLY D 641 ? 1.1003 1.2220 1.3792 -0.0573 0.3931  -0.4035 641 GLY D CA  
19604 C C   . GLY D 641 ? 1.0447 1.1873 1.3132 -0.0471 0.3975  -0.3839 641 GLY D C   
19605 O O   . GLY D 641 ? 1.1436 1.2830 1.4376 -0.0375 0.4176  -0.3908 641 GLY D O   
19606 N N   . GLY D 642 ? 0.9798 1.1435 1.2144 -0.0493 0.3796  -0.3603 642 GLY D N   
19607 C CA  . GLY D 642 ? 1.1015 1.2829 1.3244 -0.0428 0.3829  -0.3404 642 GLY D CA  
19608 C C   . GLY D 642 ? 1.0430 1.2185 1.3133 -0.0282 0.3820  -0.3163 642 GLY D C   
19609 O O   . GLY D 642 ? 0.8934 1.0500 1.2037 -0.0208 0.3774  -0.3113 642 GLY D O   
19610 N N   . LEU D 643 ? 1.0146 1.2068 1.2801 -0.0247 0.3862  -0.3007 643 LEU D N   
19611 C CA  . LEU D 643 ? 1.0183 1.2124 1.3279 -0.0123 0.3833  -0.2792 643 LEU D CA  
19612 C C   . LEU D 643 ? 1.0106 1.1934 1.3781 -0.0001 0.3978  -0.2907 643 LEU D C   
19613 O O   . LEU D 643 ? 0.9495 1.1330 1.3579 0.0122  0.3897  -0.2727 643 LEU D O   
19614 C CB  . LEU D 643 ? 0.8825 1.0969 1.1767 -0.0148 0.3876  -0.2645 643 LEU D CB  
19615 C CG  . LEU D 643 ? 0.9671 1.1947 1.2440 -0.0214 0.4163  -0.2823 643 LEU D CG  
19616 C CD1 . LEU D 643 ? 0.9721 1.2049 1.3062 -0.0120 0.4386  -0.2935 643 LEU D CD1 
19617 C CD2 . LEU D 643 ? 1.0683 1.3096 1.3070 -0.0292 0.4158  -0.2635 643 LEU D CD2 
19618 N N   . GLY D 644 ? 0.9176 1.0899 1.2890 -0.0023 0.4174  -0.3207 644 GLY D N   
19619 C CA  . GLY D 644 ? 0.9314 1.0905 1.3595 0.0114  0.4329  -0.3335 644 GLY D CA  
19620 C C   . GLY D 644 ? 1.1177 1.2546 1.5841 0.0236  0.4145  -0.3143 644 GLY D C   
19621 O O   . GLY D 644 ? 1.1207 1.2459 1.6387 0.0391  0.4225  -0.3171 644 GLY D O   
19622 N N   . ARG D 645 ? 1.0134 1.1447 1.4543 0.0179  0.3903  -0.2938 645 ARG D N   
19623 C CA  . ARG D 645 ? 0.9354 1.0461 1.4015 0.0276  0.3728  -0.2720 645 ARG D CA  
19624 C C   . ARG D 645 ? 0.9098 1.0351 1.3973 0.0408  0.3568  -0.2426 645 ARG D C   
19625 O O   . ARG D 645 ? 0.8492 0.9591 1.3590 0.0520  0.3432  -0.2237 645 ARG D O   
19626 C CB  . ARG D 645 ? 0.8266 0.9287 1.2561 0.0145  0.3569  -0.2650 645 ARG D CB  
19627 C CG  . ARG D 645 ? 0.9464 1.0349 1.3588 -0.0003 0.3680  -0.2944 645 ARG D CG  
19628 C CD  . ARG D 645 ? 0.7832 0.8347 1.2326 0.0040  0.3756  -0.3021 645 ARG D CD  
19629 N NE  . ARG D 645 ? 0.9340 0.9731 1.3655 -0.0144 0.3812  -0.3287 645 ARG D NE  
19630 C CZ  . ARG D 645 ? 0.9879 0.9920 1.4466 -0.0168 0.3922  -0.3450 645 ARG D CZ  
19631 N NH1 . ARG D 645 ? 1.0355 1.0110 1.5398 0.0006  0.3990  -0.3348 645 ARG D NH1 
19632 N NH2 . ARG D 645 ? 0.9232 0.9202 1.3656 -0.0363 0.3957  -0.3717 645 ARG D NH2 
19633 N N   . ILE D 646 ? 0.9692 1.1232 1.4489 0.0387  0.3579  -0.2384 646 ILE D N   
19634 C CA  . ILE D 646 ? 0.8412 1.0109 1.3433 0.0488  0.3416  -0.2144 646 ILE D CA  
19635 C C   . ILE D 646 ? 0.7941 0.9625 1.3575 0.0678  0.3466  -0.2149 646 ILE D C   
19636 O O   . ILE D 646 ? 0.8751 1.0544 1.4655 0.0707  0.3685  -0.2336 646 ILE D O   
19637 C CB  . ILE D 646 ? 0.6869 0.8848 1.1715 0.0398  0.3446  -0.2118 646 ILE D CB  
19638 C CG1 . ILE D 646 ? 0.6410 0.8385 1.0647 0.0242  0.3375  -0.2089 646 ILE D CG1 
19639 C CG2 . ILE D 646 ? 0.7771 0.9909 1.2907 0.0489  0.3268  -0.1908 646 ILE D CG2 
19640 C CD1 . ILE D 646 ? 0.8258 1.0426 1.2248 0.0136  0.3482  -0.2106 646 ILE D CD1 
19641 N N   . VAL D 647 ? 0.7589 0.9147 1.3435 0.0818  0.3270  -0.1943 647 VAL D N   
19642 C CA  . VAL D 647 ? 0.8300 0.9837 1.4739 0.1035  0.3274  -0.1912 647 VAL D CA  
19643 C C   . VAL D 647 ? 0.8292 1.0082 1.4993 0.1154  0.3049  -0.1697 647 VAL D C   
19644 O O   . VAL D 647 ? 0.9477 1.1362 1.6721 0.1339  0.3040  -0.1684 647 VAL D O   
19645 C CB  . VAL D 647 ? 0.8221 0.9355 1.4765 0.1137  0.3253  -0.1859 647 VAL D CB  
19646 C CG1 . VAL D 647 ? 0.7861 0.8752 1.4245 0.1013  0.3486  -0.2128 647 VAL D CG1 
19647 C CG2 . VAL D 647 ? 0.8724 0.9713 1.4966 0.1132  0.3003  -0.1577 647 VAL D CG2 
19648 N N   . TRP D 648 ? 0.8006 0.9912 1.4354 0.1059  0.2859  -0.1545 648 TRP D N   
19649 C CA  . TRP D 648 ? 0.7999 1.0145 1.4561 0.1149  0.2627  -0.1375 648 TRP D CA  
19650 C C   . TRP D 648 ? 0.8097 1.0392 1.4260 0.0981  0.2533  -0.1327 648 TRP D C   
19651 O O   . TRP D 648 ? 0.7997 1.0131 1.3661 0.0869  0.2510  -0.1296 648 TRP D O   
19652 C CB  . TRP D 648 ? 0.7586 0.9547 1.4164 0.1313  0.2384  -0.1143 648 TRP D CB  
19653 C CG  . TRP D 648 ? 0.6406 0.8621 1.3235 0.1439  0.2118  -0.0987 648 TRP D CG  
19654 C CD1 . TRP D 648 ? 0.7722 1.0066 1.5101 0.1655  0.2021  -0.0933 648 TRP D CD1 
19655 C CD2 . TRP D 648 ? 0.6608 0.8970 1.3141 0.1368  0.1891  -0.0872 648 TRP D CD2 
19656 N NE1 . TRP D 648 ? 0.9054 1.1650 1.6491 0.1711  0.1733  -0.0799 648 TRP D NE1 
19657 C CE2 . TRP D 648 ? 0.8272 1.0868 1.5186 0.1530  0.1656  -0.0770 648 TRP D CE2 
19658 C CE3 . TRP D 648 ? 0.7686 1.0007 1.3685 0.1194  0.1856  -0.0857 648 TRP D CE3 
19659 C CZ2 . TRP D 648 ? 0.8127 1.0910 1.4881 0.1502  0.1396  -0.0682 648 TRP D CZ2 
19660 C CZ3 . TRP D 648 ? 0.8268 1.0750 1.4131 0.1179  0.1619  -0.0764 648 TRP D CZ3 
19661 C CH2 . TRP D 648 ? 0.7326 1.0028 1.3549 0.1322  0.1394  -0.0688 648 TRP D CH2 
19662 N N   . MET D 649 ? 0.7327 0.9927 1.3742 0.0965  0.2484  -0.1328 649 MET D N   
19663 C CA  . MET D 649 ? 0.8188 1.0896 1.4283 0.0814  0.2392  -0.1279 649 MET D CA  
19664 C C   . MET D 649 ? 0.7365 1.0395 1.3909 0.0844  0.2268  -0.1256 649 MET D C   
19665 O O   . MET D 649 ? 0.7943 1.1176 1.5038 0.0927  0.2363  -0.1339 649 MET D O   
19666 C CB  . MET D 649 ? 0.7308 0.9994 1.3069 0.0627  0.2629  -0.1403 649 MET D CB  
19667 C CG  . MET D 649 ? 0.7665 1.0579 1.3782 0.0576  0.2874  -0.1548 649 MET D CG  
19668 S SD  . MET D 649 ? 1.1116 1.3940 1.6770 0.0403  0.3188  -0.1703 649 MET D SD  
19669 C CE  . MET D 649 ? 0.9789 1.2612 1.4977 0.0239  0.3079  -0.1566 649 MET D CE  
19670 N N   . PRO D 650 ? 0.7155 1.0256 1.3525 0.0781  0.2056  -0.1165 650 PRO D N   
19671 C CA  . PRO D 650 ? 0.6808 1.0235 1.3652 0.0790  0.1925  -0.1175 650 PRO D CA  
19672 C C   . PRO D 650 ? 0.8899 1.2579 1.6170 0.0687  0.2184  -0.1318 650 PRO D C   
19673 O O   . PRO D 650 ? 0.9774 1.3359 1.6781 0.0547  0.2440  -0.1387 650 PRO D O   
19674 C CB  . PRO D 650 ? 0.8034 1.1416 1.4499 0.0679  0.1731  -0.1106 650 PRO D CB  
19675 C CG  . PRO D 650 ? 0.7615 1.0686 1.3502 0.0709  0.1669  -0.1013 650 PRO D CG  
19676 C CD  . PRO D 650 ? 0.7962 1.0867 1.3739 0.0701  0.1927  -0.1074 650 PRO D CD  
19677 N N   . LYS D 651 ? 1.0058 1.4085 1.7991 0.0759  0.2116  -0.1361 651 LYS D N   
19678 C CA  . LYS D 651 ? 0.8919 1.3250 1.7354 0.0660  0.2373  -0.1499 651 LYS D CA  
19679 C C   . LYS D 651 ? 0.9373 1.3684 1.7522 0.0401  0.2481  -0.1504 651 LYS D C   
19680 O O   . LYS D 651 ? 1.0136 1.4480 1.8278 0.0267  0.2803  -0.1584 651 LYS D O   
19681 C CB  . LYS D 651 ? 0.9289 1.4049 1.8519 0.0780  0.2206  -0.1532 651 LYS D CB  
19682 C CG  . LYS D 651 ? 1.0494 1.5652 2.0348 0.0655  0.2454  -0.1676 651 LYS D CG  
19683 C CD  . LYS D 651 ? 1.1328 1.6565 2.1509 0.0738  0.2805  -0.1809 651 LYS D CD  
19684 C CE  . LYS D 651 ? 0.9698 1.5421 2.0676 0.0706  0.2958  -0.1938 651 LYS D CE  
19685 N NZ  . LYS D 651 ? 1.0134 1.6017 2.1128 0.0417  0.3061  -0.1954 651 LYS D NZ  
19686 N N   . GLU D 652 ? 0.8166 1.2389 1.6035 0.0336  0.2221  -0.1415 652 GLU D N   
19687 C CA  . GLU D 652 ? 0.9528 1.3663 1.7121 0.0108  0.2297  -0.1400 652 GLU D CA  
19688 C C   . GLU D 652 ? 0.9943 1.3776 1.6932 0.0016  0.2553  -0.1377 652 GLU D C   
19689 O O   . GLU D 652 ? 1.0928 1.4783 1.7892 -0.0150 0.2812  -0.1402 652 GLU D O   
19690 C CB  . GLU D 652 ? 1.1755 1.5765 1.9065 0.0096  0.1964  -0.1324 652 GLU D CB  
19691 C CG  . GLU D 652 ? 1.3339 1.7668 2.1186 0.0144  0.1684  -0.1365 652 GLU D CG  
19692 C CD  . GLU D 652 ? 1.7812 2.2010 2.5335 0.0108  0.1384  -0.1331 652 GLU D CD  
19693 O OE1 . GLU D 652 ? 1.3196 1.7097 2.0130 0.0186  0.1284  -0.1245 652 GLU D OE1 
19694 O OE2 . GLU D 652 ? 1.9016 2.3417 2.6892 -0.0007 0.1259  -0.1407 652 GLU D OE2 
19695 N N   . LEU D 653 ? 0.8770 1.2336 1.5274 0.0120  0.2478  -0.1325 653 LEU D N   
19696 C CA  . LEU D 653 ? 0.8245 1.1558 1.4175 0.0049  0.2666  -0.1316 653 LEU D CA  
19697 C C   . LEU D 653 ? 0.9318 1.2720 1.5396 0.0038  0.2994  -0.1438 653 LEU D C   
19698 O O   . LEU D 653 ? 0.9537 1.2870 1.5298 -0.0093 0.3223  -0.1456 653 LEU D O   
19699 C CB  . LEU D 653 ? 0.7670 1.0734 1.3154 0.0159  0.2491  -0.1253 653 LEU D CB  
19700 C CG  . LEU D 653 ? 0.7470 1.0292 1.2324 0.0084  0.2578  -0.1227 653 LEU D CG  
19701 C CD1 . LEU D 653 ? 1.0243 1.2964 1.4786 -0.0029 0.2500  -0.1135 653 LEU D CD1 
19702 C CD2 . LEU D 653 ? 0.7556 1.0203 1.2131 0.0192  0.2446  -0.1198 653 LEU D CD2 
19703 N N   . LYS D 654 ? 0.8827 1.2375 1.5375 0.0186  0.3018  -0.1524 654 LYS D N   
19704 C CA  . LYS D 654 ? 0.7858 1.1495 1.4603 0.0200  0.3338  -0.1678 654 LYS D CA  
19705 C C   . LYS D 654 ? 1.0621 1.4491 1.7586 0.0035  0.3616  -0.1737 654 LYS D C   
19706 O O   . LYS D 654 ? 1.1388 1.5213 1.8073 -0.0057 0.3912  -0.1817 654 LYS D O   
19707 C CB  . LYS D 654 ? 0.8155 1.1925 1.5492 0.0412  0.3286  -0.1746 654 LYS D CB  
19708 C CG  . LYS D 654 ? 0.8917 1.2761 1.6504 0.0456  0.3624  -0.1939 654 LYS D CG  
19709 C CD  . LYS D 654 ? 0.9205 1.2877 1.6943 0.0668  0.3573  -0.1989 654 LYS D CD  
19710 C CE  . LYS D 654 ? 1.0015 1.3894 1.8459 0.0879  0.3391  -0.1948 654 LYS D CE  
19711 N NZ  . LYS D 654 ? 0.8379 1.2508 1.7428 0.0960  0.3629  -0.2117 654 LYS D NZ  
19712 N N   . ASP D 655 ? 1.1323 1.5449 1.8776 -0.0015 0.3524  -0.1702 655 ASP D N   
19713 C CA  . ASP D 655 ? 1.0830 1.5191 1.8563 -0.0197 0.3796  -0.1743 655 ASP D CA  
19714 C C   . ASP D 655 ? 1.0744 1.4851 1.7810 -0.0398 0.3913  -0.1637 655 ASP D C   
19715 O O   . ASP D 655 ? 1.3192 1.7337 2.0131 -0.0529 0.4253  -0.1672 655 ASP D O   
19716 C CB  . ASP D 655 ? 1.1547 1.6227 1.9953 -0.0230 0.3621  -0.1730 655 ASP D CB  
19717 C CG  . ASP D 655 ? 1.0771 1.5808 1.9962 -0.0038 0.3544  -0.1836 655 ASP D CG  
19718 O OD1 . ASP D 655 ? 0.9794 1.4869 1.9121 0.0086  0.3743  -0.1944 655 ASP D OD1 
19719 O OD2 . ASP D 655 ? 1.0676 1.5943 2.0330 -0.0005 0.3267  -0.1815 655 ASP D OD2 
19720 N N   . PHE D 656 ? 0.8265 1.2109 1.4892 -0.0412 0.3639  -0.1501 656 PHE D N   
19721 C CA  . PHE D 656 ? 0.7884 1.1459 1.3892 -0.0566 0.3703  -0.1376 656 PHE D CA  
19722 C C   . PHE D 656 ? 0.8795 1.2208 1.4224 -0.0572 0.3928  -0.1402 656 PHE D C   
19723 O O   . PHE D 656 ? 1.0898 1.4263 1.6037 -0.0719 0.4180  -0.1354 656 PHE D O   
19724 C CB  . PHE D 656 ? 0.9713 1.3042 1.5386 -0.0522 0.3352  -0.1258 656 PHE D CB  
19725 C CG  . PHE D 656 ? 1.1239 1.4287 1.6369 -0.0655 0.3377  -0.1116 656 PHE D CG  
19726 C CD1 . PHE D 656 ? 1.0552 1.3374 1.5027 -0.0643 0.3448  -0.1062 656 PHE D CD1 
19727 C CD2 . PHE D 656 ? 1.1814 1.4814 1.7100 -0.0784 0.3307  -0.1041 656 PHE D CD2 
19728 C CE1 . PHE D 656 ? 1.1653 1.4215 1.5641 -0.0733 0.3448  -0.0910 656 PHE D CE1 
19729 C CE2 . PHE D 656 ? 1.3970 1.6661 1.8769 -0.0885 0.3328  -0.0894 656 PHE D CE2 
19730 C CZ  . PHE D 656 ? 1.4894 1.7369 1.9045 -0.0846 0.3394  -0.0817 656 PHE D CZ  
19731 N N   . VAL D 657 ? 0.8816 1.2147 1.4073 -0.0420 0.3841  -0.1480 657 VAL D N   
19732 C CA  . VAL D 657 ? 0.9197 1.2393 1.3917 -0.0429 0.4019  -0.1546 657 VAL D CA  
19733 C C   . VAL D 657 ? 0.8717 1.2095 1.3717 -0.0394 0.4319  -0.1752 657 VAL D C   
19734 O O   . VAL D 657 ? 0.9339 1.2611 1.3975 -0.0363 0.4415  -0.1867 657 VAL D O   
19735 C CB  . VAL D 657 ? 0.9281 1.2237 1.3543 -0.0333 0.3770  -0.1516 657 VAL D CB  
19736 C CG1 . VAL D 657 ? 0.8100 1.0888 1.2072 -0.0364 0.3516  -0.1330 657 VAL D CG1 
19737 C CG2 . VAL D 657 ? 0.9199 1.2178 1.3821 -0.0164 0.3625  -0.1604 657 VAL D CG2 
19738 N N   . ALA D 658 ? 0.8584 1.2247 1.4243 -0.0400 0.4465  -0.1818 658 ALA D N   
19739 C CA  . ALA D 658 ? 0.9106 1.2943 1.5091 -0.0333 0.4729  -0.2025 658 ALA D CA  
19740 C C   . ALA D 658 ? 1.1009 1.4726 1.6356 -0.0434 0.4991  -0.2090 658 ALA D C   
19741 O O   . ALA D 658 ? 1.1142 1.4730 1.6237 -0.0350 0.5015  -0.2238 658 ALA D O   
19742 C CB  . ALA D 658 ? 0.9811 1.3939 1.6470 -0.0344 0.4771  -0.2031 658 ALA D CB  
19743 N N   . GLU D 659 ? 1.2970 1.6722 1.8065 -0.0612 0.5181  -0.1985 659 GLU D N   
19744 C CA  . GLU D 659 ? 1.4113 1.7790 1.8592 -0.0702 0.5443  -0.2034 659 GLU D CA  
19745 C C   . GLU D 659 ? 1.4942 1.8385 1.8662 -0.0712 0.5384  -0.2028 659 GLU D C   
19746 O O   . GLU D 659 ? 1.4797 1.8179 1.8170 -0.0670 0.5464  -0.2199 659 GLU D O   
19747 C CB  . GLU D 659 ? 1.3357 1.7110 1.7748 -0.0892 0.5661  -0.1877 659 GLU D CB  
19748 C CG  . GLU D 659 ? 1.4529 1.8534 1.9715 -0.0920 0.5668  -0.1854 659 GLU D CG  
19749 C CD  . GLU D 659 ? 1.7534 2.1679 2.2743 -0.1075 0.5978  -0.1814 659 GLU D CD  
19750 O OE1 . GLU D 659 ? 1.8783 2.2784 2.3330 -0.1200 0.6171  -0.1710 659 GLU D OE1 
19751 O OE2 . GLU D 659 ? 1.8166 2.2576 2.4053 -0.1066 0.6024  -0.1879 659 GLU D OE2 
19752 N N   . LYS D 660 ? 1.3054 1.6352 1.6501 -0.0759 0.5204  -0.1838 660 LYS D N   
19753 C CA  . LYS D 660 ? 1.1562 1.4625 1.4220 -0.0756 0.5056  -0.1790 660 LYS D CA  
19754 C C   . LYS D 660 ? 1.2664 1.5695 1.5303 -0.0632 0.4974  -0.2025 660 LYS D C   
19755 O O   . LYS D 660 ? 1.3171 1.6115 1.5209 -0.0656 0.4998  -0.2108 660 LYS D O   
19756 C CB  . LYS D 660 ? 1.0249 1.3115 1.2718 -0.0752 0.4719  -0.1541 660 LYS D CB  
19757 C CG  . LYS D 660 ? 1.1816 1.4572 1.3935 -0.0890 0.4798  -0.1296 660 LYS D CG  
19758 C CD  . LYS D 660 ? 1.4752 1.7263 1.6193 -0.0870 0.4567  -0.1126 660 LYS D CD  
19759 C CE  . LYS D 660 ? 1.2908 1.5232 1.4222 -0.0952 0.4512  -0.0845 660 LYS D CE  
19760 N NZ  . LYS D 660 ? 1.3722 1.6034 1.4764 -0.1105 0.4850  -0.0729 660 LYS D NZ  
19761 N N   . LEU D 661 ? 1.2124 1.5216 1.5393 -0.0507 0.4878  -0.2128 661 LEU D N   
19762 C CA  . LEU D 661 ? 1.2361 1.5355 1.5648 -0.0394 0.4792  -0.2327 661 LEU D CA  
19763 C C   . LEU D 661 ? 1.3761 1.6817 1.7185 -0.0363 0.5043  -0.2582 661 LEU D C   
19764 O O   . LEU D 661 ? 1.4653 1.7597 1.7667 -0.0372 0.5077  -0.2758 661 LEU D O   
19765 C CB  . LEU D 661 ? 1.0535 1.3489 1.4357 -0.0256 0.4519  -0.2260 661 LEU D CB  
19766 C CG  . LEU D 661 ? 1.2209 1.4987 1.6015 -0.0155 0.4381  -0.2385 661 LEU D CG  
19767 C CD1 . LEU D 661 ? 1.1765 1.4424 1.5684 -0.0075 0.4035  -0.2200 661 LEU D CD1 
19768 C CD2 . LEU D 661 ? 1.2220 1.5046 1.6540 -0.0048 0.4576  -0.2615 661 LEU D CD2 
19769 N N   . ASN D 662 ? 1.3349 1.6556 1.7305 -0.0323 0.5149  -0.2591 662 ASN D N   
19770 C CA  . ASN D 662 ? 1.3793 1.7033 1.7897 -0.0272 0.5335  -0.2805 662 ASN D CA  
19771 C C   . ASN D 662 ? 1.4441 1.7638 1.7821 -0.0390 0.5529  -0.2906 662 ASN D C   
19772 O O   . ASN D 662 ? 1.5244 1.8368 1.8497 -0.0353 0.5624  -0.3141 662 ASN D O   
19773 C CB  . ASN D 662 ? 1.2608 1.6083 1.7312 -0.0251 0.5449  -0.2764 662 ASN D CB  
19774 C CG  . ASN D 662 ? 1.1988 1.5536 1.7424 -0.0107 0.5242  -0.2704 662 ASN D CG  
19775 O OD1 . ASN D 662 ? 1.1266 1.4660 1.6842 0.0023  0.5075  -0.2755 662 ASN D OD1 
19776 N ND2 . ASN D 662 ? 1.2363 1.6149 1.8283 -0.0128 0.5245  -0.2592 662 ASN D ND2 
19777 N N   . LYS D 663 ? 1.3176 1.6398 1.6057 -0.0526 0.5575  -0.2728 663 LYS D N   
19778 C CA  . LYS D 663 ? 1.4541 1.7741 1.6657 -0.0635 0.5751  -0.2777 663 LYS D CA  
19779 C C   . LYS D 663 ? 1.5022 1.8067 1.6605 -0.0628 0.5613  -0.2923 663 LYS D C   
19780 O O   . LYS D 663 ? 1.5003 1.8038 1.5991 -0.0686 0.5727  -0.3046 663 LYS D O   
19781 C CB  . LYS D 663 ? 1.4071 1.7311 1.5847 -0.0772 0.5828  -0.2497 663 LYS D CB  
19782 C CG  . LYS D 663 ? 1.5622 1.8838 1.6559 -0.0881 0.6001  -0.2467 663 LYS D CG  
19783 C CD  . LYS D 663 ? 1.5315 1.8439 1.5744 -0.0986 0.5952  -0.2176 663 LYS D CD  
19784 C CE  . LYS D 663 ? 1.7189 2.0274 1.6711 -0.1068 0.6085  -0.2132 663 LYS D CE  
19785 N NZ  . LYS D 663 ? 1.9655 2.2649 1.8795 -0.1185 0.6153  -0.1782 663 LYS D NZ  
19786 N N   . THR D 664 ? 1.5170 1.8117 1.6951 -0.0564 0.5372  -0.2914 664 THR D N   
19787 C CA  . THR D 664 ? 1.4417 1.7247 1.5769 -0.0573 0.5229  -0.3060 664 THR D CA  
19788 C C   . THR D 664 ? 1.4843 1.7559 1.6744 -0.0457 0.5131  -0.3239 664 THR D C   
19789 O O   . THR D 664 ? 1.6274 1.8887 1.8097 -0.0448 0.4960  -0.3300 664 THR D O   
19790 C CB  . THR D 664 ? 1.2468 1.5256 1.3449 -0.0614 0.4996  -0.2850 664 THR D CB  
19791 O OG1 . THR D 664 ? 1.3146 1.5882 1.4649 -0.0534 0.4773  -0.2648 664 THR D OG1 
19792 C CG2 . THR D 664 ? 1.2924 1.5754 1.3321 -0.0715 0.5062  -0.2629 664 THR D CG2 
19793 N N   . ALA D 665 ? 1.4475 1.7208 1.6937 -0.0369 0.5245  -0.3317 665 ALA D N   
19794 C CA  . ALA D 665 ? 1.4758 1.7344 1.7741 -0.0245 0.5169  -0.3462 665 ALA D CA  
19795 C C   . ALA D 665 ? 1.7662 2.0111 2.0359 -0.0275 0.5259  -0.3782 665 ALA D C   
19796 O O   . ALA D 665 ? 1.8336 2.0797 2.1172 -0.0244 0.5447  -0.3954 665 ALA D O   
19797 C CB  . ALA D 665 ? 1.4095 1.6768 1.7775 -0.0126 0.5247  -0.3426 665 ALA D CB  
19798 N N   . LYS D 666 ? 1.8369 2.0711 2.0670 -0.0345 0.5127  -0.3877 666 LYS D N   
19799 C CA  . LYS D 666 ? 1.6789 1.9011 1.8778 -0.0407 0.5176  -0.4205 666 LYS D CA  
19800 C C   . LYS D 666 ? 1.7654 2.0014 1.9110 -0.0488 0.5367  -0.4306 666 LYS D C   
19801 O O   . LYS D 666 ? 1.8318 2.0619 1.9752 -0.0488 0.5515  -0.4577 666 LYS D O   
19802 C CB  . LYS D 666 ? 1.3874 1.5880 1.6434 -0.0306 0.5234  -0.4411 666 LYS D CB  
19803 C CG  . LYS D 666 ? 1.3752 1.5603 1.6896 -0.0193 0.5082  -0.4270 666 LYS D CG  
19804 C CD  . LYS D 666 ? 1.1632 1.3330 1.4618 -0.0264 0.4917  -0.4339 666 LYS D CD  
19805 C CE  . LYS D 666 ? 0.9507 1.1283 1.2544 -0.0243 0.4731  -0.4044 666 LYS D CE  
19806 N NZ  . LYS D 666 ? 1.1568 1.3576 1.4051 -0.0339 0.4655  -0.3873 666 LYS D NZ  
19807 N N   . GLU D 667 ? 1.7742 2.0273 1.8766 -0.0554 0.5372  -0.4077 667 GLU D N   
19808 C CA  . GLU D 667 ? 1.4587 1.7251 1.5056 -0.0628 0.5560  -0.4089 667 GLU D CA  
19809 C C   . GLU D 667 ? 1.7169 1.9922 1.8043 -0.0572 0.5809  -0.4065 667 GLU D C   
19810 O O   . GLU D 667 ? 2.2002 2.4847 2.2500 -0.0619 0.6016  -0.4144 667 GLU D O   
19811 C CB  . GLU D 667 ? 1.4782 1.7408 1.4676 -0.0702 0.5576  -0.4405 667 GLU D CB  
19812 C CG  . GLU D 667 ? 1.8217 2.0843 1.7625 -0.0781 0.5329  -0.4420 667 GLU D CG  
19813 C CD  . GLU D 667 ? 2.0959 2.3724 1.9841 -0.0832 0.5255  -0.4110 667 GLU D CD  
19814 O OE1 . GLU D 667 ? 1.7815 2.0669 1.6350 -0.0857 0.5432  -0.3975 667 GLU D OE1 
19815 O OE2 . GLU D 667 ? 2.1600 2.4377 2.0422 -0.0845 0.5032  -0.3996 667 GLU D OE2 
19816 N N   . LEU D 668 ? 1.7206 1.9952 1.8834 -0.0468 0.5777  -0.3961 668 LEU D N   
19817 C CA  . LEU D 668 ? 1.9486 2.2369 2.1613 -0.0406 0.5982  -0.3929 668 LEU D CA  
19818 C C   . LEU D 668 ? 2.3315 2.6141 2.5591 -0.0347 0.6161  -0.4260 668 LEU D C   
19819 O O   . LEU D 668 ? 2.5321 2.8167 2.8279 -0.0227 0.6221  -0.4301 668 LEU D O   
19820 C CB  . LEU D 668 ? 2.0460 2.3535 2.2260 -0.0508 0.6131  -0.3705 668 LEU D CB  
19821 C CG  . LEU D 668 ? 2.0830 2.4096 2.3111 -0.0478 0.6364  -0.3681 668 LEU D CG  
19822 C CD1 . LEU D 668 ? 2.0456 2.3774 2.3587 -0.0370 0.6237  -0.3566 668 LEU D CD1 
19823 C CD2 . LEU D 668 ? 1.9358 2.2778 2.1230 -0.0610 0.6540  -0.3468 668 LEU D CD2 
19824 N N   . TYR D 669 ? 2.4352 2.7114 2.6024 -0.0421 0.6233  -0.4494 669 TYR D N   
19825 C CA  . TYR D 669 ? 2.4966 2.7652 2.6762 -0.0371 0.6408  -0.4842 669 TYR D CA  
19826 C C   . TYR D 669 ? 2.4424 2.6892 2.6894 -0.0247 0.6305  -0.4981 669 TYR D C   
19827 O O   . TYR D 669 ? 2.1403 2.3864 2.4374 -0.0137 0.6462  -0.5121 669 TYR D O   
19828 C CB  . TYR D 669 ? 2.4559 2.7198 2.5566 -0.0481 0.6441  -0.5083 669 TYR D CB  
19829 C CG  . TYR D 669 ? 2.5067 2.7487 2.5974 -0.0513 0.6222  -0.5272 669 TYR D CG  
19830 C CD1 . TYR D 669 ? 2.3615 2.6019 2.4255 -0.0579 0.5971  -0.5106 669 TYR D CD1 
19831 C CD2 . TYR D 669 ? 2.4093 2.6325 2.5205 -0.0484 0.6275  -0.5625 669 TYR D CD2 
19832 C CE1 . TYR D 669 ? 2.2339 2.4575 2.2929 -0.0624 0.5779  -0.5287 669 TYR D CE1 
19833 C CE2 . TYR D 669 ? 2.3511 2.5538 2.4575 -0.0538 0.6086  -0.5806 669 TYR D CE2 
19834 C CZ  . TYR D 669 ? 2.1413 2.3457 2.2222 -0.0613 0.5838  -0.5638 669 TYR D CZ  
19835 O OH  . TYR D 669 ? 1.8839 2.0710 1.9637 -0.0682 0.5661  -0.5826 669 TYR D OH  
19836 N N   . ASN D 670 ? 2.5373 2.7664 2.7869 -0.0257 0.6059  -0.4939 670 ASN D N   
19837 C CA  . ASN D 670 ? 2.4022 2.6056 2.7119 -0.0143 0.5980  -0.5064 670 ASN D CA  
19838 C C   . ASN D 670 ? 2.2625 2.4728 2.6481 0.0021  0.5977  -0.4856 670 ASN D C   
19839 O O   . ASN D 670 ? 2.1018 2.3014 2.5389 0.0150  0.6072  -0.5003 670 ASN D O   
19840 C CB  . ASN D 670 ? 2.2930 2.4761 2.5895 -0.0201 0.5745  -0.5072 670 ASN D CB  
19841 C CG  . ASN D 670 ? 2.2983 2.4517 2.6561 -0.0089 0.5685  -0.5157 670 ASN D CG  
19842 O OD1 . ASN D 670 ? 2.3291 2.4719 2.7277 0.0016  0.5828  -0.5317 670 ASN D OD1 
19843 N ND2 . ASN D 670 ? 2.0985 2.2377 2.4634 -0.0104 0.5483  -0.5044 670 ASN D ND2 
19844 N N   . ILE D 671 ? 1.9395 2.1673 2.3326 0.0019  0.5864  -0.4537 671 ILE D N   
19845 C CA  . ILE D 671 ? 1.7396 1.9768 2.2069 0.0175  0.5817  -0.4347 671 ILE D CA  
19846 C C   . ILE D 671 ? 1.6905 1.9590 2.1539 0.0116  0.5858  -0.4107 671 ILE D C   
19847 O O   . ILE D 671 ? 1.4558 1.7297 1.8655 -0.0019 0.5803  -0.3973 671 ILE D O   
19848 C CB  . ILE D 671 ? 1.5543 1.7726 2.0549 0.0265  0.5562  -0.4202 671 ILE D CB  
19849 C CG1 . ILE D 671 ? 1.5324 1.7177 2.0590 0.0356  0.5561  -0.4418 671 ILE D CG1 
19850 C CG2 . ILE D 671 ? 1.1755 1.4116 1.7347 0.0390  0.5453  -0.3938 671 ILE D CG2 
19851 C CD1 . ILE D 671 ? 1.5401 1.7006 2.0341 0.0267  0.5416  -0.4464 671 ILE D CD1 
19852 N N   . ASP D 672 ? 1.6907 1.9789 2.2115 0.0214  0.5951  -0.4056 672 ASP D N   
19853 C CA  . ASP D 672 ? 1.6697 1.9882 2.1967 0.0141  0.6005  -0.3841 672 ASP D CA  
19854 C C   . ASP D 672 ? 1.4948 1.8249 2.0933 0.0267  0.5816  -0.3645 672 ASP D C   
19855 O O   . ASP D 672 ? 1.3829 1.7030 2.0326 0.0442  0.5732  -0.3714 672 ASP D O   
19856 C CB  . ASP D 672 ? 1.7331 2.0724 2.2593 0.0104  0.6317  -0.3971 672 ASP D CB  
19857 C CG  . ASP D 672 ? 1.7865 2.1139 2.2462 0.0018  0.6500  -0.4210 672 ASP D CG  
19858 O OD1 . ASP D 672 ? 1.7997 2.1043 2.2596 0.0087  0.6478  -0.4439 672 ASP D OD1 
19859 O OD2 . ASP D 672 ? 1.5411 1.8816 1.9488 -0.0121 0.6663  -0.4162 672 ASP D OD2 
19860 N N   . ASN D 673 ? 1.8253 2.1750 2.4265 0.0181  0.5746  -0.3411 673 ASN D N   
19861 C CA  . ASN D 673 ? 1.7944 2.1587 2.4609 0.0286  0.5537  -0.3232 673 ASN D CA  
19862 C C   . ASN D 673 ? 1.7687 2.1085 2.4458 0.0416  0.5275  -0.3191 673 ASN D C   
19863 O O   . ASN D 673 ? 1.8105 2.1533 2.5489 0.0599  0.5152  -0.3169 673 ASN D O   
19864 C CB  . ASN D 673 ? 1.8127 2.2020 2.5507 0.0408  0.5637  -0.3302 673 ASN D CB  
19865 C CG  . ASN D 673 ? 1.9348 2.3564 2.7197 0.0378  0.5546  -0.3115 673 ASN D CG  
19866 O OD1 . ASN D 673 ? 1.9310 2.3528 2.6993 0.0283  0.5386  -0.2931 673 ASN D OD1 
19867 N ND2 . ASN D 673 ? 1.9412 2.3910 2.7868 0.0453  0.5647  -0.3176 673 ASN D ND2 
19868 N N   . PHE D 674 ? 1.4051 1.7228 2.0247 0.0328  0.5196  -0.3173 674 PHE D N   
19869 C CA  . PHE D 674 ? 1.3362 1.6296 1.9620 0.0430  0.4974  -0.3132 674 PHE D CA  
19870 C C   . PHE D 674 ? 1.2108 1.5182 1.8857 0.0533  0.4740  -0.2904 674 PHE D C   
19871 O O   . PHE D 674 ? 1.2666 1.5618 1.9799 0.0707  0.4590  -0.2871 674 PHE D O   
19872 C CB  . PHE D 674 ? 1.2633 1.5391 1.8199 0.0291  0.4928  -0.3135 674 PHE D CB  
19873 C CG  . PHE D 674 ? 1.1188 1.3720 1.6787 0.0365  0.4724  -0.3082 674 PHE D CG  
19874 C CD1 . PHE D 674 ? 1.2291 1.4623 1.8306 0.0526  0.4687  -0.3159 674 PHE D CD1 
19875 C CD2 . PHE D 674 ? 1.1150 1.3658 1.6369 0.0276  0.4585  -0.2950 674 PHE D CD2 
19876 C CE1 . PHE D 674 ? 1.2675 1.4781 1.8719 0.0586  0.4528  -0.3092 674 PHE D CE1 
19877 C CE2 . PHE D 674 ? 1.1677 1.3972 1.6893 0.0332  0.4384  -0.2878 674 PHE D CE2 
19878 C CZ  . PHE D 674 ? 1.2175 1.4271 1.7806 0.0481  0.4373  -0.2949 674 PHE D CZ  
19879 N N   . ALA D 675 ? 1.0459 1.3769 1.7191 0.0426  0.4713  -0.2753 675 ALA D N   
19880 C CA  . ALA D 675 ? 0.9818 1.3296 1.7005 0.0502  0.4478  -0.2559 675 ALA D CA  
19881 C C   . ALA D 675 ? 1.0958 1.4528 1.8857 0.0724  0.4393  -0.2581 675 ALA D C   
19882 O O   . ALA D 675 ? 1.1147 1.4662 1.9315 0.0874  0.4157  -0.2466 675 ALA D O   
19883 C CB  . ALA D 675 ? 0.8644 1.2385 1.5841 0.0344  0.4525  -0.2455 675 ALA D CB  
19884 N N   . ASP D 676 ? 1.2039 1.5752 2.0226 0.0753  0.4580  -0.2715 676 ASP D N   
19885 C CA  . ASP D 676 ? 1.3298 1.7132 2.2192 0.0978  0.4503  -0.2735 676 ASP D CA  
19886 C C   . ASP D 676 ? 1.2945 1.6448 2.1931 0.1179  0.4377  -0.2740 676 ASP D C   
19887 O O   . ASP D 676 ? 1.3405 1.6969 2.2958 0.1398  0.4236  -0.2685 676 ASP D O   
19888 C CB  . ASP D 676 ? 1.5750 1.9743 2.4866 0.0977  0.4774  -0.2918 676 ASP D CB  
19889 C CG  . ASP D 676 ? 1.7237 2.1587 2.6430 0.0807  0.4908  -0.2893 676 ASP D CG  
19890 O OD1 . ASP D 676 ? 1.6134 2.0523 2.5006 0.0633  0.4856  -0.2763 676 ASP D OD1 
19891 O OD2 . ASP D 676 ? 1.6431 2.1013 2.6022 0.0846  0.5077  -0.3003 676 ASP D OD2 
19892 N N   . MET D 677 ? 1.1798 1.4954 2.0242 0.1106  0.4424  -0.2799 677 MET D N   
19893 C CA  . MET D 677 ? 1.0644 1.3436 1.9141 0.1258  0.4338  -0.2805 677 MET D CA  
19894 C C   . MET D 677 ? 1.0085 1.2785 1.8498 0.1296  0.4082  -0.2585 677 MET D C   
19895 O O   . MET D 677 ? 1.0965 1.3420 1.9586 0.1470  0.3963  -0.2508 677 MET D O   
19896 C CB  . MET D 677 ? 1.0890 1.3364 1.8884 0.1141  0.4538  -0.3026 677 MET D CB  
19897 C CG  . MET D 677 ? 1.2505 1.5060 2.0484 0.1090  0.4805  -0.3263 677 MET D CG  
19898 S SD  . MET D 677 ? 1.3505 1.5675 2.0970 0.0985  0.4995  -0.3555 677 MET D SD  
19899 C CE  . MET D 677 ? 1.0695 1.2586 1.8766 0.1235  0.4995  -0.3637 677 MET D CE  
19900 N N   . ILE D 678 ? 1.0377 1.3249 1.8480 0.1139  0.4011  -0.2478 678 ILE D N   
19901 C CA  . ILE D 678 ? 0.9652 1.2413 1.7519 0.1141  0.3721  -0.2246 678 ILE D CA  
19902 C C   . ILE D 678 ? 0.9621 1.2588 1.7998 0.1316  0.3451  -0.2053 678 ILE D C   
19903 O O   . ILE D 678 ? 1.0699 1.4044 1.9553 0.1339  0.3497  -0.2094 678 ILE D O   
19904 C CB  . ILE D 678 ? 0.7688 1.0498 1.4930 0.0900  0.3688  -0.2184 678 ILE D CB  
19905 C CG1 . ILE D 678 ? 0.7557 1.0171 1.4252 0.0746  0.3904  -0.2363 678 ILE D CG1 
19906 C CG2 . ILE D 678 ? 0.7412 1.0102 1.4348 0.0896  0.3344  -0.1930 678 ILE D CG2 
19907 C CD1 . ILE D 678 ? 0.7730 1.0446 1.3892 0.0534  0.3945  -0.2333 678 ILE D CD1 
19908 N N   . CYS D 679 ? 0.7474 1.0213 1.5752 0.1434  0.3172  -0.1847 679 CYS D N   
19909 C CA  . CYS D 679 ? 0.9222 1.2140 1.7896 0.1615  0.2873  -0.1650 679 CYS D CA  
19910 C C   . CYS D 679 ? 0.9487 1.2587 1.7857 0.1481  0.2633  -0.1503 679 CYS D C   
19911 O O   . CYS D 679 ? 0.9276 1.2264 1.7079 0.1281  0.2672  -0.1507 679 CYS D O   
19912 C CB  . CYS D 679 ? 0.8660 1.1223 1.7333 0.1814  0.2706  -0.1482 679 CYS D CB  
19913 S SG  . CYS D 679 ? 0.9220 1.1994 1.8402 0.2097  0.2335  -0.1239 679 CYS D SG  
19914 N N   . ASP D 680 ? 1.0165 1.3552 1.8926 0.1599  0.2376  -0.1388 680 ASP D N   
19915 C CA  . ASP D 680 ? 0.9672 1.3228 1.8200 0.1484  0.2131  -0.1279 680 ASP D CA  
19916 C C   . ASP D 680 ? 0.9541 1.3251 1.8347 0.1684  0.1760  -0.1107 680 ASP D C   
19917 O O   . ASP D 680 ? 0.9833 1.3539 1.9051 0.1920  0.1703  -0.1057 680 ASP D O   
19918 C CB  . ASP D 680 ? 0.9348 1.3243 1.8072 0.1290  0.2289  -0.1423 680 ASP D CB  
19919 C CG  . ASP D 680 ? 1.0755 1.5062 2.0299 0.1383  0.2393  -0.1547 680 ASP D CG  
19920 O OD1 . ASP D 680 ? 1.0653 1.5089 2.0677 0.1619  0.2203  -0.1485 680 ASP D OD1 
19921 O OD2 . ASP D 680 ? 1.1907 1.6419 2.1617 0.1223  0.2666  -0.1698 680 ASP D OD2 
19922 N N   . GLU D 681 ? 0.8265 1.2095 1.6828 0.1601  0.1502  -0.1019 681 GLU D N   
19923 C CA  . GLU D 681 ? 0.8430 1.2424 1.7157 0.1775  0.1122  -0.0868 681 GLU D CA  
19924 C C   . GLU D 681 ? 0.8893 1.3326 1.8467 0.1944  0.1035  -0.0927 681 GLU D C   
19925 O O   . GLU D 681 ? 0.8165 1.2693 1.7936 0.2168  0.0735  -0.0785 681 GLU D O   
19926 C CB  . GLU D 681 ? 0.6685 1.0752 1.5003 0.1625  0.0889  -0.0829 681 GLU D CB  
19927 C CG  . GLU D 681 ? 0.9037 1.3505 1.7735 0.1461  0.0879  -0.0982 681 GLU D CG  
19928 C CD  . GLU D 681 ? 0.9601 1.3982 1.8068 0.1194  0.1181  -0.1107 681 GLU D CD  
19929 O OE1 . GLU D 681 ? 1.0019 1.4199 1.8363 0.1163  0.1485  -0.1156 681 GLU D OE1 
19930 O OE2 . GLU D 681 ? 0.8736 1.3238 1.7137 0.1018  0.1109  -0.1158 681 GLU D OE2 
19931 N N   . THR D 682 ? 0.8405 1.3124 1.8480 0.1844  0.1296  -0.1128 682 THR D N   
19932 C CA  . THR D 682 ? 0.8861 1.4061 1.9825 0.1995  0.1244  -0.1210 682 THR D CA  
19933 C C   . THR D 682 ? 1.0452 1.5529 2.1801 0.2276  0.1347  -0.1191 682 THR D C   
19934 O O   . THR D 682 ? 1.0561 1.5939 2.2545 0.2519  0.1150  -0.1152 682 THR D O   
19935 C CB  . THR D 682 ? 0.7185 1.2753 1.8567 0.1773  0.1514  -0.1428 682 THR D CB  
19936 O OG1 . THR D 682 ? 0.8442 1.3816 1.9751 0.1706  0.1947  -0.1557 682 THR D OG1 
19937 C CG2 . THR D 682 ? 0.8011 1.3614 1.9005 0.1486  0.1444  -0.1440 682 THR D CG2 
19938 N N   . ILE D 683 ? 0.9575 1.4215 2.0569 0.2251  0.1642  -0.1228 683 ILE D N   
19939 C CA  . ILE D 683 ? 0.9147 1.3585 2.0478 0.2504  0.1767  -0.1232 683 ILE D CA  
19940 C C   . ILE D 683 ? 0.9891 1.3974 2.0919 0.2719  0.1460  -0.0951 683 ILE D C   
19941 O O   . ILE D 683 ? 0.9105 1.3296 2.0631 0.3011  0.1268  -0.0840 683 ILE D O   
19942 C CB  . ILE D 683 ? 0.8361 1.2470 1.9430 0.2372  0.2202  -0.1418 683 ILE D CB  
19943 C CG1 . ILE D 683 ? 0.7583 1.2051 1.8956 0.2190  0.2521  -0.1675 683 ILE D CG1 
19944 C CG2 . ILE D 683 ? 0.7587 1.1364 1.8910 0.2627  0.2308  -0.1416 683 ILE D CG2 
19945 C CD1 . ILE D 683 ? 0.8726 1.2913 1.9526 0.1949  0.2874  -0.1831 683 ILE D CD1 
19946 N N   . ALA D 684 ? 1.0645 1.4318 2.0866 0.2579  0.1419  -0.0825 684 ALA D N   
19947 C CA  . ALA D 684 ? 1.1062 1.4367 2.0888 0.2736  0.1174  -0.0542 684 ALA D CA  
19948 C C   . ALA D 684 ? 1.1712 1.4675 2.0680 0.2508  0.1196  -0.0469 684 ALA D C   
19949 O O   . ALA D 684 ? 1.2251 1.5132 2.0955 0.2276  0.1456  -0.0642 684 ALA D O   
19950 C CB  . ALA D 684 ? 1.1545 1.4479 2.1630 0.2965  0.1307  -0.0488 684 ALA D CB  
19951 N N   . THR D 685 ? 1.2138 1.4919 2.0670 0.2584  0.0925  -0.0212 685 THR D N   
19952 C CA  . THR D 685 ? 1.1665 1.4151 1.9424 0.2393  0.0940  -0.0134 685 THR D CA  
19953 C C   . THR D 685 ? 1.2230 1.4206 1.9671 0.2493  0.0969  0.0082  685 THR D C   
19954 O O   . THR D 685 ? 1.1528 1.3212 1.8489 0.2317  0.1129  0.0070  685 THR D O   
19955 C CB  . THR D 685 ? 1.1037 1.3765 1.8463 0.2335  0.0636  -0.0047 685 THR D CB  
19956 O OG1 . THR D 685 ? 1.5573 1.8392 2.3130 0.2586  0.0310  0.0170  685 THR D OG1 
19957 C CG2 . THR D 685 ? 0.9856 1.3016 1.7535 0.2175  0.0639  -0.0266 685 THR D CG2 
19958 N N   . GLU D 686 ? 1.2794 1.4663 2.0511 0.2772  0.0813  0.0289  686 GLU D N   
19959 C CA  . GLU D 686 ? 1.2006 1.3347 1.9445 0.2870  0.0850  0.0530  686 GLU D CA  
19960 C C   . GLU D 686 ? 1.1642 1.2614 1.9199 0.2777  0.1219  0.0362  686 GLU D C   
19961 O O   . GLU D 686 ? 1.1737 1.2830 1.9824 0.2819  0.1391  0.0137  686 GLU D O   
19962 C CB  . GLU D 686 ? 1.2528 1.3825 2.0293 0.3217  0.0605  0.0798  686 GLU D CB  
19963 C CG  . GLU D 686 ? 1.4408 1.5910 2.1829 0.3318  0.0214  0.1048  686 GLU D CG  
19964 C CD  . GLU D 686 ? 1.4991 1.6042 2.1944 0.3455  0.0106  0.1430  686 GLU D CD  
19965 O OE1 . GLU D 686 ? 1.4449 1.5084 2.1625 0.3615  0.0229  0.1570  686 GLU D OE1 
19966 O OE2 . GLU D 686 ? 1.3388 1.4488 1.9745 0.3402  -0.0088 0.1591  686 GLU D OE2 
19967 N N   . SER D 687 ? 1.1653 1.2192 1.8728 0.2645  0.1346  0.0456  687 SER D N   
19968 C CA  . SER D 687 ? 1.1824 1.1996 1.8955 0.2523  0.1677  0.0279  687 SER D CA  
19969 C C   . SER D 687 ? 1.1708 1.1656 1.9451 0.2748  0.1796  0.0239  687 SER D C   
19970 O O   . SER D 687 ? 1.1339 1.1239 1.9345 0.2667  0.2064  -0.0059 687 SER D O   
19971 C CB  . SER D 687 ? 1.1667 1.1410 1.8266 0.2385  0.1744  0.0449  687 SER D CB  
19972 O OG  . SER D 687 ? 1.3615 1.3549 1.9695 0.2147  0.1721  0.0397  687 SER D OG  
19973 N N   . GLU D 688 ? 1.1309 1.1110 1.9263 0.3038  0.1601  0.0531  688 GLU D N   
19974 C CA  . GLU D 688 ? 1.3637 1.3198 2.2214 0.3294  0.1699  0.0514  688 GLU D CA  
19975 C C   . GLU D 688 ? 1.3676 1.3713 2.2893 0.3384  0.1755  0.0220  688 GLU D C   
19976 O O   . GLU D 688 ? 1.3969 1.3856 2.3623 0.3433  0.2015  -0.0016 688 GLU D O   
19977 C CB  . GLU D 688 ? 1.5782 1.5126 2.4433 0.3617  0.1430  0.0933  688 GLU D CB  
19978 C CG  . GLU D 688 ? 1.6626 1.5332 2.4813 0.3573  0.1487  0.1226  688 GLU D CG  
19979 C CD  . GLU D 688 ? 1.8804 1.7298 2.6937 0.3883  0.1207  0.1691  688 GLU D CD  
19980 O OE1 . GLU D 688 ? 1.9224 1.7954 2.7866 0.4199  0.1004  0.1761  688 GLU D OE1 
19981 O OE2 . GLU D 688 ? 1.9994 1.8102 2.7574 0.3813  0.1190  0.1993  688 GLU D OE2 
19982 N N   . GLU D 689 ? 1.3889 1.4496 2.3164 0.3392  0.1530  0.0216  689 GLU D N   
19983 C CA  . GLU D 689 ? 1.2573 1.3691 2.2497 0.3458  0.1592  -0.0054 689 GLU D CA  
19984 C C   . GLU D 689 ? 1.1921 1.3123 2.1724 0.3156  0.1933  -0.0422 689 GLU D C   
19985 O O   . GLU D 689 ? 1.2496 1.3822 2.2818 0.3206  0.2171  -0.0689 689 GLU D O   
19986 C CB  . GLU D 689 ? 1.3159 1.4854 2.3171 0.3510  0.1253  0.0041  689 GLU D CB  
19987 C CG  . GLU D 689 ? 1.4241 1.5957 2.4483 0.3854  0.0895  0.0367  689 GLU D CG  
19988 C CD  . GLU D 689 ? 1.6542 1.7958 2.6063 0.3849  0.0653  0.0721  689 GLU D CD  
19989 O OE1 . GLU D 689 ? 1.7601 1.8446 2.6729 0.3790  0.0814  0.0841  689 GLU D OE1 
19990 O OE2 . GLU D 689 ? 1.6972 1.8734 2.6329 0.3895  0.0312  0.0863  689 GLU D OE2 
19991 N N   . VAL D 690 ? 1.1595 1.2736 2.0729 0.2867  0.1957  -0.0433 690 VAL D N   
19992 C CA  . VAL D 690 ? 1.0911 1.2153 1.9850 0.2585  0.2235  -0.0746 690 VAL D CA  
19993 C C   . VAL D 690 ? 1.1092 1.1930 2.0128 0.2557  0.2564  -0.0956 690 VAL D C   
19994 O O   . VAL D 690 ? 1.0919 1.1919 2.0173 0.2480  0.2821  -0.1265 690 VAL D O   
19995 C CB  . VAL D 690 ? 0.9204 1.0458 1.7418 0.2315  0.2157  -0.0686 690 VAL D CB  
19996 C CG1 . VAL D 690 ? 0.9499 1.0767 1.7454 0.2045  0.2440  -0.0976 690 VAL D CG1 
19997 C CG2 . VAL D 690 ? 0.8427 1.0116 1.6592 0.2314  0.1876  -0.0572 690 VAL D CG2 
19998 N N   . VAL D 691 ? 1.0179 1.0487 1.9056 0.2613  0.2569  -0.0801 691 VAL D N   
19999 C CA  . VAL D 691 ? 0.9733 0.9621 1.8725 0.2573  0.2873  -0.1026 691 VAL D CA  
20000 C C   . VAL D 691 ? 1.2131 1.2072 2.1864 0.2823  0.3018  -0.1203 691 VAL D C   
20001 O O   . VAL D 691 ? 1.3281 1.3102 2.3157 0.2751  0.3321  -0.1534 691 VAL D O   
20002 C CB  . VAL D 691 ? 1.0027 0.9305 1.8736 0.2551  0.2873  -0.0831 691 VAL D CB  
20003 C CG1 . VAL D 691 ? 1.1071 1.0345 1.9084 0.2284  0.2784  -0.0715 691 VAL D CG1 
20004 C CG2 . VAL D 691 ? 1.1071 1.0099 2.0064 0.2869  0.2672  -0.0474 691 VAL D CG2 
20005 N N   . LYS D 692 ? 1.2586 1.2739 2.2797 0.3119  0.2802  -0.1003 692 LYS D N   
20006 C CA  . LYS D 692 ? 1.2575 1.2843 2.3571 0.3389  0.2923  -0.1162 692 LYS D CA  
20007 C C   . LYS D 692 ? 1.2055 1.2851 2.3115 0.3209  0.3085  -0.1489 692 LYS D C   
20008 O O   . LYS D 692 ? 1.2175 1.2922 2.3367 0.3174  0.3312  -0.1755 692 LYS D O   
20009 C CB  . LYS D 692 ? 1.2590 1.3035 2.4013 0.3729  0.2586  -0.0844 692 LYS D CB  
20010 C CG  . LYS D 692 ? 1.3764 1.3612 2.5181 0.3960  0.2456  -0.0511 692 LYS D CG  
20011 C CD  . LYS D 692 ? 1.5169 1.5242 2.6951 0.4304  0.2089  -0.0195 692 LYS D CD  
20012 C CE  . LYS D 692 ? 1.7387 1.6869 2.9026 0.4522  0.1924  0.0221  692 LYS D CE  
20013 N NZ  . LYS D 692 ? 1.8425 1.8153 3.0341 0.4863  0.1530  0.0539  692 LYS D NZ  
20014 N N   . PHE D 693 ? 1.1702 1.2982 2.2639 0.3085  0.2973  -0.1460 693 PHE D N   
20015 C CA  . PHE D 693 ? 1.1623 1.3375 2.2553 0.2885  0.3122  -0.1716 693 PHE D CA  
20016 C C   . PHE D 693 ? 1.0854 1.2393 2.1331 0.2612  0.3452  -0.2010 693 PHE D C   
20017 O O   . PHE D 693 ? 1.1723 1.3442 2.2248 0.2514  0.3659  -0.2257 693 PHE D O   
20018 C CB  . PHE D 693 ? 1.0284 1.2500 2.1115 0.2780  0.2931  -0.1601 693 PHE D CB  
20019 C CG  . PHE D 693 ? 1.0694 1.3294 2.1378 0.2516  0.3113  -0.1829 693 PHE D CG  
20020 C CD1 . PHE D 693 ? 1.0177 1.3193 2.1282 0.2543  0.3139  -0.1927 693 PHE D CD1 
20021 C CD2 . PHE D 693 ? 1.1970 1.4505 2.2088 0.2242  0.3264  -0.1928 693 PHE D CD2 
20022 C CE1 . PHE D 693 ? 0.9072 1.2394 2.0022 0.2294  0.3326  -0.2101 693 PHE D CE1 
20023 C CE2 . PHE D 693 ? 1.1710 1.4549 2.1648 0.2009  0.3428  -0.2093 693 PHE D CE2 
20024 C CZ  . PHE D 693 ? 0.8431 1.1642 1.8779 0.2032  0.3467  -0.2170 693 PHE D CZ  
20025 N N   . LEU D 694 ? 1.0446 1.1623 2.0480 0.2490  0.3497  -0.1984 694 LEU D N   
20026 C CA  . LEU D 694 ? 0.9941 1.0929 1.9514 0.2230  0.3767  -0.2264 694 LEU D CA  
20027 C C   . LEU D 694 ? 1.0932 1.1549 2.0663 0.2286  0.3960  -0.2470 694 LEU D C   
20028 O O   . LEU D 694 ? 1.2016 1.2662 2.1534 0.2114  0.4188  -0.2766 694 LEU D O   
20029 C CB  . LEU D 694 ? 0.8586 0.9296 1.7488 0.2027  0.3654  -0.2129 694 LEU D CB  
20030 C CG  . LEU D 694 ? 0.8625 0.9650 1.7108 0.1885  0.3417  -0.1923 694 LEU D CG  
20031 C CD1 . LEU D 694 ? 0.9149 0.9872 1.7090 0.1772  0.3247  -0.1712 694 LEU D CD1 
20032 C CD2 . LEU D 694 ? 0.9639 1.0993 1.7846 0.1656  0.3581  -0.2139 694 LEU D CD2 
20033 N N   . GLU D 695 ? 1.0936 1.1196 2.1024 0.2530  0.3867  -0.2309 695 GLU D N   
20034 C CA  . GLU D 695 ? 1.1427 1.1304 2.1723 0.2605  0.4038  -0.2492 695 GLU D CA  
20035 C C   . GLU D 695 ? 1.1779 1.2021 2.2438 0.2688  0.4133  -0.2670 695 GLU D C   
20036 O O   . GLU D 695 ? 1.1534 1.1656 2.2171 0.2613  0.4371  -0.2969 695 GLU D O   
20037 C CB  . GLU D 695 ? 1.1058 1.0465 2.1662 0.2869  0.3890  -0.2215 695 GLU D CB  
20038 C CG  . GLU D 695 ? 1.2238 1.1106 2.2511 0.2766  0.3905  -0.2108 695 GLU D CG  
20039 C CD  . GLU D 695 ? 1.4144 1.2501 2.4667 0.3015  0.3767  -0.1781 695 GLU D CD  
20040 O OE1 . GLU D 695 ? 1.3450 1.1978 2.4318 0.3295  0.3543  -0.1515 695 GLU D OE1 
20041 O OE2 . GLU D 695 ? 1.6018 1.3800 2.6378 0.2923  0.3875  -0.1781 695 GLU D OE2 
20042 N N   . GLU D 696 ? 1.2460 1.3161 2.3461 0.2839  0.3947  -0.2496 696 GLU D N   
20043 C CA  . GLU D 696 ? 1.2949 1.4054 2.4353 0.2920  0.4029  -0.2642 696 GLU D CA  
20044 C C   . GLU D 696 ? 1.1548 1.2906 2.2602 0.2636  0.4293  -0.2942 696 GLU D C   
20045 O O   . GLU D 696 ? 1.3007 1.4346 2.4161 0.2627  0.4526  -0.3203 696 GLU D O   
20046 C CB  . GLU D 696 ? 1.3501 1.5105 2.5292 0.3078  0.3756  -0.2404 696 GLU D CB  
20047 C CG  . GLU D 696 ? 1.4639 1.6091 2.6857 0.3418  0.3478  -0.2113 696 GLU D CG  
20048 C CD  . GLU D 696 ? 1.4949 1.6915 2.7468 0.3546  0.3161  -0.1881 696 GLU D CD  
20049 O OE1 . GLU D 696 ? 1.4325 1.6813 2.6907 0.3399  0.3199  -0.1996 696 GLU D OE1 
20050 O OE2 . GLU D 696 ? 1.6225 1.8066 2.8905 0.3788  0.2868  -0.1579 696 GLU D OE2 
20051 N N   . LYS D 697 ? 0.9980 1.1560 2.0602 0.2412  0.4258  -0.2897 697 LYS D N   
20052 C CA  . LYS D 697 ? 1.0045 1.1856 2.0266 0.2146  0.4482  -0.3124 697 LYS D CA  
20053 C C   . LYS D 697 ? 1.0953 1.2390 2.0668 0.1964  0.4698  -0.3375 697 LYS D C   
20054 O O   . LYS D 697 ? 1.0648 1.2233 2.0049 0.1784  0.4906  -0.3594 697 LYS D O   
20055 C CB  . LYS D 697 ? 0.8418 1.0555 1.8336 0.1975  0.4361  -0.2972 697 LYS D CB  
20056 C CG  . LYS D 697 ? 0.8684 1.1253 1.9081 0.2105  0.4147  -0.2767 697 LYS D CG  
20057 C CD  . LYS D 697 ? 1.0896 1.3896 2.1557 0.2056  0.4303  -0.2902 697 LYS D CD  
20058 C CE  . LYS D 697 ? 1.0072 1.3481 2.1357 0.2227  0.4083  -0.2738 697 LYS D CE  
20059 N NZ  . LYS D 697 ? 1.0471 1.4269 2.2129 0.2213  0.4264  -0.2891 697 LYS D NZ  
20060 N N   . GLY D 698 ? 1.1415 1.2380 2.1050 0.2005  0.4645  -0.3342 698 GLY D N   
20061 C CA  . GLY D 698 ? 1.0862 1.1478 2.0058 0.1821  0.4822  -0.3596 698 GLY D CA  
20062 C C   . GLY D 698 ? 1.0429 1.1194 1.8988 0.1551  0.4826  -0.3621 698 GLY D C   
20063 O O   . GLY D 698 ? 1.0195 1.1038 1.8346 0.1361  0.5002  -0.3865 698 GLY D O   
20064 N N   . HIS D 699 ? 0.8831 0.9645 1.7294 0.1548  0.4622  -0.3357 699 HIS D N   
20065 C CA  . HIS D 699 ? 0.8493 0.9460 1.6390 0.1323  0.4592  -0.3335 699 HIS D CA  
20066 C C   . HIS D 699 ? 1.0441 1.1128 1.7854 0.1124  0.4717  -0.3579 699 HIS D C   
20067 O O   . HIS D 699 ? 1.0747 1.1024 1.8280 0.1166  0.4733  -0.3641 699 HIS D O   
20068 C CB  . HIS D 699 ? 0.9209 1.0198 1.7153 0.1390  0.4355  -0.3021 699 HIS D CB  
20069 C CG  . HIS D 699 ? 1.0094 1.1380 1.7594 0.1208  0.4295  -0.2944 699 HIS D CG  
20070 N ND1 . HIS D 699 ? 1.1194 1.2356 1.8066 0.0985  0.4288  -0.3009 699 HIS D ND1 
20071 C CD2 . HIS D 699 ? 0.8145 0.9811 1.5695 0.1202  0.4184  -0.2780 699 HIS D CD2 
20072 C CE1 . HIS D 699 ? 1.1126 1.2574 1.7668 0.0868  0.4172  -0.2864 699 HIS D CE1 
20073 N NE2 . HIS D 699 ? 1.0423 1.2156 1.7348 0.0982  0.4114  -0.2727 699 HIS D NE2 
20074 N N   . PRO D 700 ? 1.0904 1.1795 1.7769 0.0904  0.4798  -0.3717 700 PRO D N   
20075 C CA  . PRO D 700 ? 1.1260 1.1932 1.7662 0.0714  0.4883  -0.3968 700 PRO D CA  
20076 C C   . PRO D 700 ? 1.2901 1.3314 1.9209 0.0669  0.4759  -0.3880 700 PRO D C   
20077 O O   . PRO D 700 ? 1.2248 1.2403 1.8357 0.0542  0.4822  -0.4103 700 PRO D O   
20078 C CB  . PRO D 700 ? 1.2175 1.3178 1.8001 0.0523  0.4937  -0.4039 700 PRO D CB  
20079 C CG  . PRO D 700 ? 1.0792 1.2131 1.6753 0.0586  0.4849  -0.3768 700 PRO D CG  
20080 C CD  . PRO D 700 ? 1.0729 1.2044 1.7371 0.0818  0.4810  -0.3646 700 PRO D CD  
20081 N N   . ALA D 701 ? 1.3523 1.4008 1.9937 0.0751  0.4552  -0.3539 701 ALA D N   
20082 C CA  . ALA D 701 ? 1.4520 1.4771 2.0709 0.0675  0.4326  -0.3323 701 ALA D CA  
20083 C C   . ALA D 701 ? 1.4688 1.4457 2.1225 0.0767  0.4358  -0.3338 701 ALA D C   
20084 O O   . ALA D 701 ? 1.4355 1.3867 2.0675 0.0622  0.4310  -0.3355 701 ALA D O   
20085 C CB  . ALA D 701 ? 1.3422 1.3861 1.9585 0.0745  0.4062  -0.2927 701 ALA D CB  
20086 N N   . LEU D 702 ? 1.1861 1.1508 1.8968 0.1007  0.4440  -0.3325 702 LEU D N   
20087 C CA  . LEU D 702 ? 1.1199 1.0335 1.8674 0.1127  0.4478  -0.3309 702 LEU D CA  
20088 C C   . LEU D 702 ? 1.1363 1.0203 1.8795 0.0988  0.4724  -0.3738 702 LEU D C   
20089 O O   . LEU D 702 ? 1.2851 1.1241 2.0325 0.0927  0.4726  -0.3743 702 LEU D O   
20090 C CB  . LEU D 702 ? 1.0723 0.9829 1.8848 0.1452  0.4495  -0.3193 702 LEU D CB  
20091 C CG  . LEU D 702 ? 1.0672 1.0109 1.8919 0.1611  0.4240  -0.2811 702 LEU D CG  
20092 C CD1 . LEU D 702 ? 0.9113 0.8559 1.8045 0.1933  0.4257  -0.2753 702 LEU D CD1 
20093 C CD2 . LEU D 702 ? 0.9226 0.8480 1.7190 0.1578  0.3971  -0.2429 702 LEU D CD2 
20094 N N   . LYS D 703 ? 1.1601 1.0698 1.8849 0.0892  0.4871  -0.4045 703 LYS D N   
20095 C CA  . LYS D 703 ? 1.2778 1.1657 1.9856 0.0724  0.5029  -0.4431 703 LYS D CA  
20096 C C   . LYS D 703 ? 1.3054 1.2129 1.9520 0.0442  0.5024  -0.4627 703 LYS D C   
20097 O O   . LYS D 703 ? 1.4311 1.3608 2.0431 0.0315  0.5112  -0.4885 703 LYS D O   
20098 C CB  . LYS D 703 ? 1.2908 1.1920 2.0132 0.0803  0.5174  -0.4630 703 LYS D CB  
20099 C CG  . LYS D 703 ? 1.2046 1.0839 1.9909 0.1085  0.5178  -0.4480 703 LYS D CG  
20100 C CD  . LYS D 703 ? 1.2411 1.1166 2.0460 0.1139  0.5368  -0.4774 703 LYS D CD  
20101 C CE  . LYS D 703 ? 1.3177 1.1441 2.1753 0.1323  0.5401  -0.4758 703 LYS D CE  
20102 N NZ  . LYS D 703 ? 1.4397 1.2748 2.3316 0.1489  0.5544  -0.4917 703 LYS D NZ  
20103 N N   . MET D 704 ? 1.2746 1.1750 1.9052 0.0349  0.4883  -0.4459 704 MET D N   
20104 C CA  . MET D 704 ? 1.1638 1.0861 1.7345 0.0076  0.4787  -0.4566 704 MET D CA  
20105 C C   . MET D 704 ? 1.1690 1.0609 1.7384 -0.0064 0.4649  -0.4456 704 MET D C   
20106 O O   . MET D 704 ? 1.2895 1.1528 1.8926 0.0065  0.4580  -0.4157 704 MET D O   
20107 C CB  . MET D 704 ? 1.0228 0.9916 1.5583 0.0070  0.4613  -0.4283 704 MET D CB  
20108 C CG  . MET D 704 ? 1.1431 1.1487 1.6335 -0.0042 0.4709  -0.4521 704 MET D CG  
20109 S SD  . MET D 704 ? 1.2631 1.3128 1.7054 -0.0102 0.4473  -0.4177 704 MET D SD  
20110 C CE  . MET D 704 ? 0.8440 0.9029 1.3331 0.0147  0.4443  -0.3835 704 MET D CE  
20111 N N   . ASP D 705 ? 1.1044 1.0024 1.6379 -0.0319 0.4618  -0.4694 705 ASP D N   
20112 C CA  . ASP D 705 ? 1.2784 1.1487 1.8180 -0.0482 0.4524  -0.4631 705 ASP D CA  
20113 C C   . ASP D 705 ? 1.3004 1.1757 1.8415 -0.0402 0.4319  -0.4119 705 ASP D C   
20114 O O   . ASP D 705 ? 1.3332 1.2477 1.8477 -0.0342 0.4185  -0.3908 705 ASP D O   
20115 C CB  . ASP D 705 ? 1.3950 1.2861 1.8949 -0.0768 0.4464  -0.4929 705 ASP D CB  
20116 C CG  . ASP D 705 ? 1.6839 1.6298 2.1310 -0.0806 0.4337  -0.4901 705 ASP D CG  
20117 O OD1 . ASP D 705 ? 1.6750 1.6428 2.1121 -0.0706 0.4186  -0.4519 705 ASP D OD1 
20118 O OD2 . ASP D 705 ? 1.7909 1.7554 2.2059 -0.0935 0.4388  -0.5263 705 ASP D OD2 
20119 N N   . PRO D 706 ? 1.2692 1.1023 1.8413 -0.0388 0.4316  -0.3922 706 PRO D N   
20120 C CA  . PRO D 706 ? 1.2403 1.0738 1.8113 -0.0311 0.4145  -0.3446 706 PRO D CA  
20121 C C   . PRO D 706 ? 1.1521 1.0329 1.6781 -0.0448 0.3961  -0.3350 706 PRO D C   
20122 O O   . PRO D 706 ? 1.3497 1.2425 1.8567 -0.0677 0.3948  -0.3577 706 PRO D O   
20123 C CB  . PRO D 706 ? 1.1954 0.9790 1.7918 -0.0418 0.4209  -0.3385 706 PRO D CB  
20124 C CG  . PRO D 706 ? 1.1100 0.8525 1.7419 -0.0384 0.4429  -0.3723 706 PRO D CG  
20125 C CD  . PRO D 706 ? 1.2122 0.9913 1.8203 -0.0449 0.4490  -0.4142 706 PRO D CD  
20126 N N   . ILE D 707 ? 0.9376 0.8431 1.4507 -0.0299 0.3814  -0.3023 707 ILE D N   
20127 C CA  . ILE D 707 ? 1.0871 1.0362 1.5586 -0.0403 0.3647  -0.2944 707 ILE D CA  
20128 C C   . ILE D 707 ? 1.1330 1.0753 1.6000 -0.0545 0.3565  -0.2780 707 ILE D C   
20129 O O   . ILE D 707 ? 1.1966 1.1664 1.6393 -0.0724 0.3493  -0.2903 707 ILE D O   
20130 C CB  . ILE D 707 ? 1.0458 1.0215 1.5065 -0.0217 0.3524  -0.2676 707 ILE D CB  
20131 C CG1 . ILE D 707 ? 0.9867 1.0004 1.4067 -0.0320 0.3362  -0.2604 707 ILE D CG1 
20132 C CG2 . ILE D 707 ? 0.7887 0.7423 1.2733 -0.0032 0.3461  -0.2321 707 ILE D CG2 
20133 C CD1 . ILE D 707 ? 0.9314 0.9749 1.3348 -0.0192 0.3264  -0.2450 707 ILE D CD1 
20134 N N   . MET D 708 ? 1.2447 1.1534 1.7344 -0.0462 0.3580  -0.2501 708 MET D N   
20135 C CA  . MET D 708 ? 1.0806 0.9815 1.5669 -0.0600 0.3543  -0.2314 708 MET D CA  
20136 C C   . MET D 708 ? 1.0719 0.9246 1.5906 -0.0733 0.3717  -0.2436 708 MET D C   
20137 O O   . MET D 708 ? 1.2395 1.0508 1.7858 -0.0578 0.3811  -0.2344 708 MET D O   
20138 C CB  . MET D 708 ? 0.9154 0.8127 1.3958 -0.0425 0.3436  -0.1869 708 MET D CB  
20139 C CG  . MET D 708 ? 0.8789 0.8219 1.3269 -0.0343 0.3256  -0.1744 708 MET D CG  
20140 S SD  . MET D 708 ? 1.1693 1.1127 1.6008 -0.0243 0.3131  -0.1290 708 MET D SD  
20141 C CE  . MET D 708 ? 1.0234 0.9495 1.4606 -0.0497 0.3252  -0.1287 708 MET D CE  
# 
