data_9JI1
# 
_entry.id   9JI1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9JI1         pdb_00009ji1 10.2210/pdb9ji1/pdb 
WWPDB D_1300051407 ?            ?                   
# 
_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       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9JI1 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-11 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        '9JHW is the same protein complexed with Diclofenac (DIF)' 
_pdbx_database_related.db_id          9JHW 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yasukawa.kiyoshi.7v@kyoto-u.ac.jp 
_pdbx_contact_author.name_first         Kiyoshi 
_pdbx_contact_author.name_last          Yasukawa 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7748-6043 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Mikami, B.'   1 0000-0003-0638-8619 
'Takita, T.'   2 0000-0001-9333-2335 
'Sakaki, T.'   3 0000-0001-7064-8185 
'Yasuda, K.'   4 0000-0003-3495-3216 
'Wada, M.'     5 0009-0005-3017-1104 
'Yasukawa, K.' 6 0000-0001-7748-6043 
# 
loop_
_citation.abstract 
_citation.abstract_id_CAS 
_citation.book_id_ISBN 
_citation.book_publisher 
_citation.book_publisher_city 
_citation.book_title 
_citation.coordinate_linkage 
_citation.country 
_citation.database_id_Medline 
_citation.details 
_citation.id 
_citation.journal_abbrev 
_citation.journal_id_ASTM 
_citation.journal_id_CSD 
_citation.journal_id_ISSN 
_citation.journal_full 
_citation.journal_issue 
_citation.journal_volume 
_citation.language 
_citation.page_first 
_citation.page_last 
_citation.title 
_citation.year 
_citation.database_id_CSD 
_citation.pdbx_database_id_DOI 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_patent 
_citation.unpublished_flag 
? ? ? ? ? ? ? US ? ? primary Biochemistry                                     BICHAW 0033 0006-2960 ? ? 64 ? 468 478 
'Structure-Function Analysis of Streptomyces griseolus CYP105A1 in the Metabolism of Nonsteroidal Anti-inflammatory Drugs.' 2025 ? 
10.1021/acs.biochem.4c00652 39752145 ? ? 
? ? ? ? ? ? ? DK ? ? 1       'Acta Crystallogr., Sect. D: Biol. Crystallogr.' ABCRE6 0766 0907-4449 ? ? 75 ? 861 877 
'Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix'                2019 ? 
10.1107/S2059798319011471   31588918 ? ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Takita, T.'        1  ?                   
primary 'Wada, M.'          2  ?                   
primary 'Yamagata, M.'      3  ?                   
primary 'Kamata, S.'        4  ?                   
primary 'Mizutani, K.'      5  ?                   
primary 'Yogo, Y.'          6  ?                   
primary 'Hamada, M.'        7  ?                   
primary 'Yasuda, K.'        8  ?                   
primary 'Mikami, B.'        9  ?                   
primary 'Sakaki, T.'        10 0000-0001-7064-8185 
primary 'Yasukawa, K.'      11 0000-0001-7748-6043 
1       'Liebschner, D.'    12 0000-0003-3921-3209 
1       'Afonine, P.V.'     13 0000-0002-5052-991X 
1       'Baker, M.L.'       14 ?                   
1       'Bunkoczi, G.'      15 ?                   
1       'Chen, V.B.'        16 0000-0003-2492-979X 
1       'Croll, T.I.'       17 ?                   
1       'Hintze, B.'        18 0000-0002-4871-2096 
1       'Hung, L.W.'        19 0000-0001-6690-8458 
1       'Jain, S.'          20 ?                   
1       'McCoy, A.J.'       21 ?                   
1       'Moriarty, N.W.'    22 0000-0001-8857-9464 
1       'Oeffner, R.D.'     23 0000-0003-3107-2202 
1       'Poon, B.K.'        24 0000-0001-9633-6067 
1       'Prisant, M.G.'     25 ?                   
1       'Read, R.J.'        26 0000-0001-8273-0047 
1       'Richardson, J.S.'  27 0000-0002-3311-2944 
1       'Richardson, D.C.'  28 ?                   
1       'Sammito, M.D.'     29 0000-0002-8346-9247 
1       'Sobolev, O.V.'     30 0000-0002-0623-3214 
1       'Stockwell, D.H.'   31 ?                   
1       'Terwilliger, T.C.' 32 0000-0001-6384-0320 
1       'Urzhumtsev, A.G.'  33 ?                   
1       'Videau, L.L.'      34 ?                   
1       'Williams, C.J.'    35 ?                   
1       'Adams, P.D.'       36 0000-0001-9333-8219 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Vitamin D3 dihydroxylase'                          45077.855 1   1.14.15.22 ? ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                   616.487   1   ?          ? ? ? 
3 non-polymer syn 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL            122.143   1   ?          ? ? ? 
4 non-polymer syn '2-[[3-(TRIFLUOROMETHYL)PHENYL]AMINO] BENZOIC ACID' 281.230   1   ?          ? ? ? 
5 non-polymer syn 1,2-ETHANEDIOL                                      62.068    5   ?          ? ? ? 
6 water       nat water                                               18.015    406 ?          ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'CYP105A1,Cytochrome P450-CVA1,Cytochrome P450-SU1,Vitamin D3 hydroxylase,VD3 hydroxylase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MTDTATTPQTTDAPAFPSNRSCPYQLPDGYAQLRDTPGPLHRVTLYDGRQAWVVTKHEAARKLLGDPRLSSNRTDDNFPA
TSPRFEAVRESPQAFIGLDPPEHGTRRRMTISEFTVKRIKGMRPEVEEVVHGFLDEMLAAGPTADLVSQFALPVPSMVIC
RLLGVPYADHEFFQDASKRLVQSTDAQSALTARNDLAGYLDGLITQFQTEPGAGLVGALVADQLANGEIDREELISTAML
LLIAGHETTASMTSLSVITLLDHPEQYAALRADRSLVPGAVEELLRYLAIADIAGGRVATADIEVEGQLIRAGEGVIVVN
SIANRDGTVYEDPDALDIHRSARHHLAFGFGVHQCLGQNLARLELEVILNALMDRVPTLRLAVPVEQLVLRPGTTIQGVN
ELPVTWHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTDTATTPQTTDAPAFPSNRSCPYQLPDGYAQLRDTPGPLHRVTLYDGRQAWVVTKHEAARKLLGDPRLSSNRTDDNFPA
TSPRFEAVRESPQAFIGLDPPEHGTRRRMTISEFTVKRIKGMRPEVEEVVHGFLDEMLAAGPTADLVSQFALPVPSMVIC
RLLGVPYADHEFFQDASKRLVQSTDAQSALTARNDLAGYLDGLITQFQTEPGAGLVGALVADQLANGEIDREELISTAML
LLIAGHETTASMTSLSVITLLDHPEQYAALRADRSLVPGAVEELLRYLAIADIAGGRVATADIEVEGQLIRAGEGVIVVN
SIANRDGTVYEDPDALDIHRSARHHLAFGFGVHQCLGQNLARLELEVILNALMDRVPTLRLAVPVEQLVLRPGTTIQGVN
ELPVTWHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'PROTOPORPHYRIN IX CONTAINING FE'                   HEM 
3 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL            TRS 
4 '2-[[3-(TRIFLUOROMETHYL)PHENYL]AMINO] BENZOIC ACID' FLF 
5 1,2-ETHANEDIOL                                      EDO 
6 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   THR n 
1 3   ASP n 
1 4   THR n 
1 5   ALA n 
1 6   THR n 
1 7   THR n 
1 8   PRO n 
1 9   GLN n 
1 10  THR n 
1 11  THR n 
1 12  ASP n 
1 13  ALA n 
1 14  PRO n 
1 15  ALA n 
1 16  PHE n 
1 17  PRO n 
1 18  SER n 
1 19  ASN n 
1 20  ARG n 
1 21  SER n 
1 22  CYS n 
1 23  PRO n 
1 24  TYR n 
1 25  GLN n 
1 26  LEU n 
1 27  PRO n 
1 28  ASP n 
1 29  GLY n 
1 30  TYR n 
1 31  ALA n 
1 32  GLN n 
1 33  LEU n 
1 34  ARG n 
1 35  ASP n 
1 36  THR n 
1 37  PRO n 
1 38  GLY n 
1 39  PRO n 
1 40  LEU n 
1 41  HIS n 
1 42  ARG n 
1 43  VAL n 
1 44  THR n 
1 45  LEU n 
1 46  TYR n 
1 47  ASP n 
1 48  GLY n 
1 49  ARG n 
1 50  GLN n 
1 51  ALA n 
1 52  TRP n 
1 53  VAL n 
1 54  VAL n 
1 55  THR n 
1 56  LYS n 
1 57  HIS n 
1 58  GLU n 
1 59  ALA n 
1 60  ALA n 
1 61  ARG n 
1 62  LYS n 
1 63  LEU n 
1 64  LEU n 
1 65  GLY n 
1 66  ASP n 
1 67  PRO n 
1 68  ARG n 
1 69  LEU n 
1 70  SER n 
1 71  SER n 
1 72  ASN n 
1 73  ARG n 
1 74  THR n 
1 75  ASP n 
1 76  ASP n 
1 77  ASN n 
1 78  PHE n 
1 79  PRO n 
1 80  ALA n 
1 81  THR n 
1 82  SER n 
1 83  PRO n 
1 84  ARG n 
1 85  PHE n 
1 86  GLU n 
1 87  ALA n 
1 88  VAL n 
1 89  ARG n 
1 90  GLU n 
1 91  SER n 
1 92  PRO n 
1 93  GLN n 
1 94  ALA n 
1 95  PHE n 
1 96  ILE n 
1 97  GLY n 
1 98  LEU n 
1 99  ASP n 
1 100 PRO n 
1 101 PRO n 
1 102 GLU n 
1 103 HIS n 
1 104 GLY n 
1 105 THR n 
1 106 ARG n 
1 107 ARG n 
1 108 ARG n 
1 109 MET n 
1 110 THR n 
1 111 ILE n 
1 112 SER n 
1 113 GLU n 
1 114 PHE n 
1 115 THR n 
1 116 VAL n 
1 117 LYS n 
1 118 ARG n 
1 119 ILE n 
1 120 LYS n 
1 121 GLY n 
1 122 MET n 
1 123 ARG n 
1 124 PRO n 
1 125 GLU n 
1 126 VAL n 
1 127 GLU n 
1 128 GLU n 
1 129 VAL n 
1 130 VAL n 
1 131 HIS n 
1 132 GLY n 
1 133 PHE n 
1 134 LEU n 
1 135 ASP n 
1 136 GLU n 
1 137 MET n 
1 138 LEU n 
1 139 ALA n 
1 140 ALA n 
1 141 GLY n 
1 142 PRO n 
1 143 THR n 
1 144 ALA n 
1 145 ASP n 
1 146 LEU n 
1 147 VAL n 
1 148 SER n 
1 149 GLN n 
1 150 PHE n 
1 151 ALA n 
1 152 LEU n 
1 153 PRO n 
1 154 VAL n 
1 155 PRO n 
1 156 SER n 
1 157 MET n 
1 158 VAL n 
1 159 ILE n 
1 160 CYS n 
1 161 ARG n 
1 162 LEU n 
1 163 LEU n 
1 164 GLY n 
1 165 VAL n 
1 166 PRO n 
1 167 TYR n 
1 168 ALA n 
1 169 ASP n 
1 170 HIS n 
1 171 GLU n 
1 172 PHE n 
1 173 PHE n 
1 174 GLN n 
1 175 ASP n 
1 176 ALA n 
1 177 SER n 
1 178 LYS n 
1 179 ARG n 
1 180 LEU n 
1 181 VAL n 
1 182 GLN n 
1 183 SER n 
1 184 THR n 
1 185 ASP n 
1 186 ALA n 
1 187 GLN n 
1 188 SER n 
1 189 ALA n 
1 190 LEU n 
1 191 THR n 
1 192 ALA n 
1 193 ARG n 
1 194 ASN n 
1 195 ASP n 
1 196 LEU n 
1 197 ALA n 
1 198 GLY n 
1 199 TYR n 
1 200 LEU n 
1 201 ASP n 
1 202 GLY n 
1 203 LEU n 
1 204 ILE n 
1 205 THR n 
1 206 GLN n 
1 207 PHE n 
1 208 GLN n 
1 209 THR n 
1 210 GLU n 
1 211 PRO n 
1 212 GLY n 
1 213 ALA n 
1 214 GLY n 
1 215 LEU n 
1 216 VAL n 
1 217 GLY n 
1 218 ALA n 
1 219 LEU n 
1 220 VAL n 
1 221 ALA n 
1 222 ASP n 
1 223 GLN n 
1 224 LEU n 
1 225 ALA n 
1 226 ASN n 
1 227 GLY n 
1 228 GLU n 
1 229 ILE n 
1 230 ASP n 
1 231 ARG n 
1 232 GLU n 
1 233 GLU n 
1 234 LEU n 
1 235 ILE n 
1 236 SER n 
1 237 THR n 
1 238 ALA n 
1 239 MET n 
1 240 LEU n 
1 241 LEU n 
1 242 LEU n 
1 243 ILE n 
1 244 ALA n 
1 245 GLY n 
1 246 HIS n 
1 247 GLU n 
1 248 THR n 
1 249 THR n 
1 250 ALA n 
1 251 SER n 
1 252 MET n 
1 253 THR n 
1 254 SER n 
1 255 LEU n 
1 256 SER n 
1 257 VAL n 
1 258 ILE n 
1 259 THR n 
1 260 LEU n 
1 261 LEU n 
1 262 ASP n 
1 263 HIS n 
1 264 PRO n 
1 265 GLU n 
1 266 GLN n 
1 267 TYR n 
1 268 ALA n 
1 269 ALA n 
1 270 LEU n 
1 271 ARG n 
1 272 ALA n 
1 273 ASP n 
1 274 ARG n 
1 275 SER n 
1 276 LEU n 
1 277 VAL n 
1 278 PRO n 
1 279 GLY n 
1 280 ALA n 
1 281 VAL n 
1 282 GLU n 
1 283 GLU n 
1 284 LEU n 
1 285 LEU n 
1 286 ARG n 
1 287 TYR n 
1 288 LEU n 
1 289 ALA n 
1 290 ILE n 
1 291 ALA n 
1 292 ASP n 
1 293 ILE n 
1 294 ALA n 
1 295 GLY n 
1 296 GLY n 
1 297 ARG n 
1 298 VAL n 
1 299 ALA n 
1 300 THR n 
1 301 ALA n 
1 302 ASP n 
1 303 ILE n 
1 304 GLU n 
1 305 VAL n 
1 306 GLU n 
1 307 GLY n 
1 308 GLN n 
1 309 LEU n 
1 310 ILE n 
1 311 ARG n 
1 312 ALA n 
1 313 GLY n 
1 314 GLU n 
1 315 GLY n 
1 316 VAL n 
1 317 ILE n 
1 318 VAL n 
1 319 VAL n 
1 320 ASN n 
1 321 SER n 
1 322 ILE n 
1 323 ALA n 
1 324 ASN n 
1 325 ARG n 
1 326 ASP n 
1 327 GLY n 
1 328 THR n 
1 329 VAL n 
1 330 TYR n 
1 331 GLU n 
1 332 ASP n 
1 333 PRO n 
1 334 ASP n 
1 335 ALA n 
1 336 LEU n 
1 337 ASP n 
1 338 ILE n 
1 339 HIS n 
1 340 ARG n 
1 341 SER n 
1 342 ALA n 
1 343 ARG n 
1 344 HIS n 
1 345 HIS n 
1 346 LEU n 
1 347 ALA n 
1 348 PHE n 
1 349 GLY n 
1 350 PHE n 
1 351 GLY n 
1 352 VAL n 
1 353 HIS n 
1 354 GLN n 
1 355 CYS n 
1 356 LEU n 
1 357 GLY n 
1 358 GLN n 
1 359 ASN n 
1 360 LEU n 
1 361 ALA n 
1 362 ARG n 
1 363 LEU n 
1 364 GLU n 
1 365 LEU n 
1 366 GLU n 
1 367 VAL n 
1 368 ILE n 
1 369 LEU n 
1 370 ASN n 
1 371 ALA n 
1 372 LEU n 
1 373 MET n 
1 374 ASP n 
1 375 ARG n 
1 376 VAL n 
1 377 PRO n 
1 378 THR n 
1 379 LEU n 
1 380 ARG n 
1 381 LEU n 
1 382 ALA n 
1 383 VAL n 
1 384 PRO n 
1 385 VAL n 
1 386 GLU n 
1 387 GLN n 
1 388 LEU n 
1 389 VAL n 
1 390 LEU n 
1 391 ARG n 
1 392 PRO n 
1 393 GLY n 
1 394 THR n 
1 395 THR n 
1 396 ILE n 
1 397 GLN n 
1 398 GLY n 
1 399 VAL n 
1 400 ASN n 
1 401 GLU n 
1 402 LEU n 
1 403 PRO n 
1 404 VAL n 
1 405 THR n 
1 406 TRP n 
1 407 HIS n 
1 408 HIS n 
1 409 HIS n 
1 410 HIS n 
1 411 HIS n 
1 412 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   412 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'cyp105A1, suaC' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Streptomyces griseolus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1909 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 11796 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               JM109 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 53323 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                             ?                 'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                                            ?                 'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                                          ?                 'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                     ?                 'C4 H7 N O4'       133.103 
CYS 'L-peptide linking' y CYSTEINE                                            ?                 'C3 H7 N O2 S'     121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                      'ETHYLENE GLYCOL' 'C2 H6 O2'         62.068  
FLF non-polymer         . '2-[[3-(TRIFLUOROMETHYL)PHENYL]AMINO] BENZOIC ACID' 'FLUFENAMIC ACID' 'C14 H10 F3 N O2'  281.230 
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  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE'                   HEME              'C34 H32 Fe N4 O4' 616.487 
HIS 'L-peptide linking' y HISTIDINE                                           ?                 'C6 H10 N3 O2 1'   156.162 
HOH non-polymer         . WATER                                               ?                 'H2 O'             18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                          ?                 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking' y LEUCINE                                             ?                 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking' y LYSINE                                              ?                 'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking' y METHIONINE                                          ?                 'C5 H11 N O2 S'    149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                       ?                 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking' y PROLINE                                             ?                 'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                                              ?                 'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                                           ?                 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                          ?                 'C11 H12 N2 O2'    204.225 
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 
# 
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   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   ASP 3   3   ?   ?   ?   A . n 
A 1 4   THR 4   4   4   THR THR A . n 
A 1 5   ALA 5   5   5   ALA ALA A . n 
A 1 6   THR 6   6   6   THR THR A . n 
A 1 7   THR 7   7   7   THR THR A . n 
A 1 8   PRO 8   8   8   PRO PRO A . n 
A 1 9   GLN 9   9   9   GLN GLN A . n 
A 1 10  THR 10  10  10  THR THR A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  PHE 16  16  16  PHE PHE A . n 
A 1 17  PRO 17  17  17  PRO PRO A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  PRO 27  27  27  PRO PRO A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  TYR 30  30  30  TYR TYR A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  GLN 32  32  32  GLN GLN A . n 
A 1 33  LEU 33  33  33  LEU LEU A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  THR 36  36  36  THR THR A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  LEU 40  40  40  LEU LEU A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  ARG 42  42  42  ARG ARG A . n 
A 1 43  VAL 43  43  43  VAL VAL A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  TYR 46  46  46  TYR TYR A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  GLN 50  50  50  GLN GLN A . n 
A 1 51  ALA 51  51  51  ALA ALA A . n 
A 1 52  TRP 52  52  52  TRP TRP A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  VAL 54  54  54  VAL VAL A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  HIS 57  57  57  HIS HIS A . n 
A 1 58  GLU 58  58  58  GLU GLU A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  LYS 62  62  62  LYS LYS A . n 
A 1 63  LEU 63  63  63  LEU LEU A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  PRO 67  67  67  PRO PRO A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  SER 71  71  71  SER SER A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  ASN 77  77  77  ASN ASN A . n 
A 1 78  PHE 78  78  78  PHE PHE A . n 
A 1 79  PRO 79  79  79  PRO PRO A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  SER 82  82  82  SER SER A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  PHE 85  85  85  PHE PHE A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  GLU 90  90  90  GLU GLU A . n 
A 1 91  SER 91  91  91  SER SER A . n 
A 1 92  PRO 92  92  92  PRO PRO A . n 
A 1 93  GLN 93  93  93  GLN GLN A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 PRO 101 101 101 PRO PRO A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 HIS 103 103 103 HIS HIS A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 THR 105 105 105 THR THR A . n 
A 1 106 ARG 106 106 106 ARG ARG A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 MET 109 109 109 MET MET A . n 
A 1 110 THR 110 110 110 THR THR A . n 
A 1 111 ILE 111 111 111 ILE ILE A . n 
A 1 112 SER 112 112 112 SER SER A . n 
A 1 113 GLU 113 113 113 GLU GLU A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 THR 115 115 115 THR THR A . n 
A 1 116 VAL 116 116 116 VAL VAL A . n 
A 1 117 LYS 117 117 117 LYS LYS A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 ILE 119 119 119 ILE ILE A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 MET 122 122 122 MET MET A . n 
A 1 123 ARG 123 123 123 ARG ARG A . n 
A 1 124 PRO 124 124 124 PRO PRO A . n 
A 1 125 GLU 125 125 125 GLU GLU A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 GLU 128 128 128 GLU GLU A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 HIS 131 131 131 HIS HIS A . n 
A 1 132 GLY 132 132 132 GLY GLY A . n 
A 1 133 PHE 133 133 133 PHE PHE A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 MET 137 137 137 MET MET A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 ALA 139 139 139 ALA ALA A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 PRO 142 142 142 PRO PRO A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 GLN 149 149 149 GLN GLN A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ALA 151 151 151 ALA ALA A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 VAL 154 154 154 VAL VAL A . n 
A 1 155 PRO 155 155 155 PRO PRO A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 MET 157 157 157 MET MET A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 ARG 161 161 161 ARG ARG A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 GLY 164 164 164 GLY GLY A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 PRO 166 166 166 PRO PRO A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 ASP 169 169 169 ASP ASP A . n 
A 1 170 HIS 170 170 170 HIS HIS A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 PHE 172 172 172 PHE PHE A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 GLN 174 174 174 GLN GLN A . n 
A 1 175 ASP 175 175 175 ASP ASP A . n 
A 1 176 ALA 176 176 176 ALA ALA A . n 
A 1 177 SER 177 177 177 SER SER A . n 
A 1 178 LYS 178 178 178 LYS LYS A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 LEU 180 180 180 LEU LEU A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 GLN 182 182 182 GLN GLN A . n 
A 1 183 SER 183 183 183 SER SER A . n 
A 1 184 THR 184 184 184 THR THR A . n 
A 1 185 ASP 185 185 185 ASP ASP A . n 
A 1 186 ALA 186 186 186 ALA ALA A . n 
A 1 187 GLN 187 187 187 GLN GLN A . n 
A 1 188 SER 188 188 188 SER SER A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 THR 191 191 191 THR THR A . n 
A 1 192 ALA 192 192 192 ALA ALA A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 ASN 194 194 194 ASN ASN A . n 
A 1 195 ASP 195 195 195 ASP ASP A . n 
A 1 196 LEU 196 196 196 LEU LEU A . n 
A 1 197 ALA 197 197 197 ALA ALA A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 TYR 199 199 199 TYR TYR A . n 
A 1 200 LEU 200 200 200 LEU LEU A . n 
A 1 201 ASP 201 201 201 ASP ASP A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 LEU 203 203 203 LEU LEU A . n 
A 1 204 ILE 204 204 204 ILE ILE A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 GLN 206 206 206 GLN GLN A . n 
A 1 207 PHE 207 207 207 PHE PHE A . n 
A 1 208 GLN 208 208 208 GLN GLN A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 PRO 211 211 211 PRO PRO A . n 
A 1 212 GLY 212 212 212 GLY GLY A . n 
A 1 213 ALA 213 213 213 ALA ALA A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 VAL 216 216 216 VAL VAL A . n 
A 1 217 GLY 217 217 217 GLY GLY A . n 
A 1 218 ALA 218 218 218 ALA ALA A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 VAL 220 220 220 VAL VAL A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 ASP 222 222 222 ASP ASP A . n 
A 1 223 GLN 223 223 223 GLN GLN A . n 
A 1 224 LEU 224 224 224 LEU LEU A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 ASN 226 226 226 ASN ASN A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 GLU 228 228 228 GLU GLU A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 ASP 230 230 230 ASP ASP A . n 
A 1 231 ARG 231 231 231 ARG ARG A . n 
A 1 232 GLU 232 232 232 GLU GLU A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 LEU 234 234 234 LEU LEU A . n 
A 1 235 ILE 235 235 235 ILE ILE A . n 
A 1 236 SER 236 236 236 SER SER A . n 
A 1 237 THR 237 237 237 THR THR A . n 
A 1 238 ALA 238 238 238 ALA ALA A . n 
A 1 239 MET 239 239 239 MET MET A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 GLY 245 245 245 GLY GLY A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 THR 248 248 248 THR THR A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 SER 251 251 251 SER SER A . n 
A 1 252 MET 252 252 252 MET MET A . n 
A 1 253 THR 253 253 253 THR THR A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 LEU 255 255 255 LEU LEU A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 LEU 260 260 260 LEU LEU A . n 
A 1 261 LEU 261 261 261 LEU LEU A . n 
A 1 262 ASP 262 262 262 ASP ASP A . n 
A 1 263 HIS 263 263 263 HIS HIS A . n 
A 1 264 PRO 264 264 264 PRO PRO A . n 
A 1 265 GLU 265 265 265 GLU GLU A . n 
A 1 266 GLN 266 266 266 GLN GLN A . n 
A 1 267 TYR 267 267 267 TYR TYR A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 LEU 270 270 270 LEU LEU A . n 
A 1 271 ARG 271 271 271 ARG ARG A . n 
A 1 272 ALA 272 272 272 ALA ALA A . n 
A 1 273 ASP 273 273 273 ASP ASP A . n 
A 1 274 ARG 274 274 274 ARG ARG A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 VAL 277 277 277 VAL VAL A . n 
A 1 278 PRO 278 278 278 PRO PRO A . n 
A 1 279 GLY 279 279 279 GLY GLY A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 VAL 281 281 281 VAL VAL A . n 
A 1 282 GLU 282 282 282 GLU GLU A . n 
A 1 283 GLU 283 283 283 GLU GLU A . n 
A 1 284 LEU 284 284 284 LEU LEU A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 ARG 286 286 286 ARG ARG A . n 
A 1 287 TYR 287 287 287 TYR TYR A . n 
A 1 288 LEU 288 288 288 LEU LEU A . n 
A 1 289 ALA 289 289 289 ALA ALA A . n 
A 1 290 ILE 290 290 290 ILE ILE A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 ASP 292 292 292 ASP ASP A . n 
A 1 293 ILE 293 293 293 ILE ILE A . n 
A 1 294 ALA 294 294 294 ALA ALA A . n 
A 1 295 GLY 295 295 295 GLY GLY A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 ARG 297 297 297 ARG ARG A . n 
A 1 298 VAL 298 298 298 VAL VAL A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 THR 300 300 300 THR THR A . n 
A 1 301 ALA 301 301 301 ALA ALA A . n 
A 1 302 ASP 302 302 302 ASP ASP A . n 
A 1 303 ILE 303 303 303 ILE ILE A . n 
A 1 304 GLU 304 304 304 GLU GLU A . n 
A 1 305 VAL 305 305 305 VAL VAL 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 GLN 308 308 308 GLN GLN A . n 
A 1 309 LEU 309 309 309 LEU LEU A . n 
A 1 310 ILE 310 310 310 ILE ILE A . n 
A 1 311 ARG 311 311 311 ARG ARG A . n 
A 1 312 ALA 312 312 312 ALA ALA A . n 
A 1 313 GLY 313 313 313 GLY GLY A . n 
A 1 314 GLU 314 314 314 GLU GLU A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 ILE 317 317 317 ILE ILE A . n 
A 1 318 VAL 318 318 318 VAL VAL A . n 
A 1 319 VAL 319 319 319 VAL VAL A . n 
A 1 320 ASN 320 320 320 ASN ASN A . n 
A 1 321 SER 321 321 321 SER SER A . n 
A 1 322 ILE 322 322 322 ILE ILE A . n 
A 1 323 ALA 323 323 323 ALA ALA A . n 
A 1 324 ASN 324 324 324 ASN ASN A . n 
A 1 325 ARG 325 325 325 ARG ARG A . n 
A 1 326 ASP 326 326 326 ASP ASP A . n 
A 1 327 GLY 327 327 327 GLY GLY A . n 
A 1 328 THR 328 328 328 THR THR A . n 
A 1 329 VAL 329 329 329 VAL VAL A . n 
A 1 330 TYR 330 330 330 TYR TYR A . n 
A 1 331 GLU 331 331 331 GLU GLU A . n 
A 1 332 ASP 332 332 332 ASP ASP A . n 
A 1 333 PRO 333 333 333 PRO PRO A . n 
A 1 334 ASP 334 334 334 ASP ASP A . n 
A 1 335 ALA 335 335 335 ALA ALA A . n 
A 1 336 LEU 336 336 336 LEU LEU A . n 
A 1 337 ASP 337 337 337 ASP ASP A . n 
A 1 338 ILE 338 338 338 ILE ILE A . n 
A 1 339 HIS 339 339 339 HIS HIS A . n 
A 1 340 ARG 340 340 340 ARG ARG A . n 
A 1 341 SER 341 341 341 SER SER A . n 
A 1 342 ALA 342 342 342 ALA ALA A . n 
A 1 343 ARG 343 343 343 ARG ARG A . n 
A 1 344 HIS 344 344 344 HIS HIS A . n 
A 1 345 HIS 345 345 345 HIS HIS A . n 
A 1 346 LEU 346 346 346 LEU LEU A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 PHE 348 348 348 PHE PHE A . n 
A 1 349 GLY 349 349 349 GLY GLY A . n 
A 1 350 PHE 350 350 350 PHE PHE A . n 
A 1 351 GLY 351 351 351 GLY GLY A . n 
A 1 352 VAL 352 352 352 VAL VAL A . n 
A 1 353 HIS 353 353 353 HIS HIS A . n 
A 1 354 GLN 354 354 354 GLN GLN A . n 
A 1 355 CYS 355 355 355 CYS CYS A . n 
A 1 356 LEU 356 356 356 LEU LEU A . n 
A 1 357 GLY 357 357 357 GLY GLY A . n 
A 1 358 GLN 358 358 358 GLN GLN A . n 
A 1 359 ASN 359 359 359 ASN ASN A . n 
A 1 360 LEU 360 360 360 LEU LEU A . n 
A 1 361 ALA 361 361 361 ALA ALA A . n 
A 1 362 ARG 362 362 362 ARG ARG A . n 
A 1 363 LEU 363 363 363 LEU LEU A . n 
A 1 364 GLU 364 364 364 GLU GLU A . n 
A 1 365 LEU 365 365 365 LEU LEU A . n 
A 1 366 GLU 366 366 366 GLU GLU A . n 
A 1 367 VAL 367 367 367 VAL VAL A . n 
A 1 368 ILE 368 368 368 ILE ILE A . n 
A 1 369 LEU 369 369 369 LEU LEU A . n 
A 1 370 ASN 370 370 370 ASN ASN A . n 
A 1 371 ALA 371 371 371 ALA ALA A . n 
A 1 372 LEU 372 372 372 LEU LEU A . n 
A 1 373 MET 373 373 373 MET MET A . n 
A 1 374 ASP 374 374 374 ASP ASP A . n 
A 1 375 ARG 375 375 375 ARG ARG A . n 
A 1 376 VAL 376 376 376 VAL VAL A . n 
A 1 377 PRO 377 377 377 PRO PRO A . n 
A 1 378 THR 378 378 378 THR THR A . n 
A 1 379 LEU 379 379 379 LEU LEU A . n 
A 1 380 ARG 380 380 380 ARG ARG A . n 
A 1 381 LEU 381 381 381 LEU LEU A . n 
A 1 382 ALA 382 382 382 ALA ALA A . n 
A 1 383 VAL 383 383 383 VAL VAL A . n 
A 1 384 PRO 384 384 384 PRO PRO A . n 
A 1 385 VAL 385 385 385 VAL VAL A . n 
A 1 386 GLU 386 386 386 GLU GLU A . n 
A 1 387 GLN 387 387 387 GLN GLN A . n 
A 1 388 LEU 388 388 388 LEU LEU A . n 
A 1 389 VAL 389 389 389 VAL VAL A . n 
A 1 390 LEU 390 390 390 LEU LEU A . n 
A 1 391 ARG 391 391 391 ARG ARG A . n 
A 1 392 PRO 392 392 392 PRO PRO A . n 
A 1 393 GLY 393 393 393 GLY GLY A . n 
A 1 394 THR 394 394 394 THR THR A . n 
A 1 395 THR 395 395 395 THR THR A . n 
A 1 396 ILE 396 396 396 ILE ILE A . n 
A 1 397 GLN 397 397 397 GLN GLN A . n 
A 1 398 GLY 398 398 398 GLY GLY A . n 
A 1 399 VAL 399 399 399 VAL VAL A . n 
A 1 400 ASN 400 400 400 ASN ASN A . n 
A 1 401 GLU 401 401 401 GLU GLU A . n 
A 1 402 LEU 402 402 402 LEU LEU A . n 
A 1 403 PRO 403 403 403 PRO PRO A . n 
A 1 404 VAL 404 404 404 VAL VAL A . n 
A 1 405 THR 405 405 405 THR THR A . n 
A 1 406 TRP 406 406 406 TRP TRP A . n 
A 1 407 HIS 407 407 407 HIS HIS A . n 
A 1 408 HIS 408 408 408 HIS HIS A . n 
A 1 409 HIS 409 409 ?   ?   ?   A . n 
A 1 410 HIS 410 410 ?   ?   ?   A . n 
A 1 411 HIS 411 411 ?   ?   ?   A . n 
A 1 412 HIS 412 412 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HEM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HEM 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
B 2 HEM 1   501  413 HEM HEM A . 
C 3 TRS 1   502  501 TRS TRS A . 
D 4 FLF 1   503  1   FLF FLF A . 
E 5 EDO 1   504  1   EDO EDO A . 
F 5 EDO 1   505  2   EDO EDO A . 
G 5 EDO 1   506  3   EDO EDO A . 
H 5 EDO 1   507  7   EDO EDO A . 
I 5 EDO 1   508  9   EDO EDO A . 
J 6 HOH 1   601  317 HOH HOH A . 
J 6 HOH 2   602  427 HOH HOH A . 
J 6 HOH 3   603  266 HOH HOH A . 
J 6 HOH 4   604  340 HOH HOH A . 
J 6 HOH 5   605  339 HOH HOH A . 
J 6 HOH 6   606  166 HOH HOH A . 
J 6 HOH 7   607  175 HOH HOH A . 
J 6 HOH 8   608  224 HOH HOH A . 
J 6 HOH 9   609  355 HOH HOH A . 
J 6 HOH 10  610  198 HOH HOH A . 
J 6 HOH 11  611  107 HOH HOH A . 
J 6 HOH 12  612  424 HOH HOH A . 
J 6 HOH 13  613  41  HOH HOH A . 
J 6 HOH 14  614  143 HOH HOH A . 
J 6 HOH 15  615  8   HOH HOH A . 
J 6 HOH 16  616  55  HOH HOH A . 
J 6 HOH 17  617  303 HOH HOH A . 
J 6 HOH 18  618  3   HOH HOH A . 
J 6 HOH 19  619  120 HOH HOH A . 
J 6 HOH 20  620  81  HOH HOH A . 
J 6 HOH 21  621  104 HOH HOH A . 
J 6 HOH 22  622  393 HOH HOH A . 
J 6 HOH 23  623  141 HOH HOH A . 
J 6 HOH 24  624  347 HOH HOH A . 
J 6 HOH 25  625  232 HOH HOH A . 
J 6 HOH 26  626  243 HOH HOH A . 
J 6 HOH 27  627  106 HOH HOH A . 
J 6 HOH 28  628  171 HOH HOH A . 
J 6 HOH 29  629  111 HOH HOH A . 
J 6 HOH 30  630  258 HOH HOH A . 
J 6 HOH 31  631  201 HOH HOH A . 
J 6 HOH 32  632  394 HOH HOH A . 
J 6 HOH 33  633  194 HOH HOH A . 
J 6 HOH 34  634  117 HOH HOH A . 
J 6 HOH 35  635  119 HOH HOH A . 
J 6 HOH 36  636  309 HOH HOH A . 
J 6 HOH 37  637  96  HOH HOH A . 
J 6 HOH 38  638  447 HOH HOH A . 
J 6 HOH 39  639  76  HOH HOH A . 
J 6 HOH 40  640  219 HOH HOH A . 
J 6 HOH 41  641  346 HOH HOH A . 
J 6 HOH 42  642  20  HOH HOH A . 
J 6 HOH 43  643  95  HOH HOH A . 
J 6 HOH 44  644  136 HOH HOH A . 
J 6 HOH 45  645  176 HOH HOH A . 
J 6 HOH 46  646  291 HOH HOH A . 
J 6 HOH 47  647  268 HOH HOH A . 
J 6 HOH 48  648  279 HOH HOH A . 
J 6 HOH 49  649  227 HOH HOH A . 
J 6 HOH 50  650  33  HOH HOH A . 
J 6 HOH 51  651  350 HOH HOH A . 
J 6 HOH 52  652  52  HOH HOH A . 
J 6 HOH 53  653  69  HOH HOH A . 
J 6 HOH 54  654  150 HOH HOH A . 
J 6 HOH 55  655  193 HOH HOH A . 
J 6 HOH 56  656  26  HOH HOH A . 
J 6 HOH 57  657  125 HOH HOH A . 
J 6 HOH 58  658  182 HOH HOH A . 
J 6 HOH 59  659  70  HOH HOH A . 
J 6 HOH 60  660  299 HOH HOH A . 
J 6 HOH 61  661  73  HOH HOH A . 
J 6 HOH 62  662  122 HOH HOH A . 
J 6 HOH 63  663  29  HOH HOH A . 
J 6 HOH 64  664  297 HOH HOH A . 
J 6 HOH 65  665  110 HOH HOH A . 
J 6 HOH 66  666  288 HOH HOH A . 
J 6 HOH 67  667  4   HOH HOH A . 
J 6 HOH 68  668  62  HOH HOH A . 
J 6 HOH 69  669  407 HOH HOH A . 
J 6 HOH 70  670  487 HOH HOH A . 
J 6 HOH 71  671  13  HOH HOH A . 
J 6 HOH 72  672  47  HOH HOH A . 
J 6 HOH 73  673  158 HOH HOH A . 
J 6 HOH 74  674  230 HOH HOH A . 
J 6 HOH 75  675  11  HOH HOH A . 
J 6 HOH 76  676  138 HOH HOH A . 
J 6 HOH 77  677  15  HOH HOH A . 
J 6 HOH 78  678  196 HOH HOH A . 
J 6 HOH 79  679  7   HOH HOH A . 
J 6 HOH 80  680  126 HOH HOH A . 
J 6 HOH 81  681  239 HOH HOH A . 
J 6 HOH 82  682  103 HOH HOH A . 
J 6 HOH 83  683  2   HOH HOH A . 
J 6 HOH 84  684  148 HOH HOH A . 
J 6 HOH 85  685  10  HOH HOH A . 
J 6 HOH 86  686  423 HOH HOH A . 
J 6 HOH 87  687  411 HOH HOH A . 
J 6 HOH 88  688  272 HOH HOH A . 
J 6 HOH 89  689  352 HOH HOH A . 
J 6 HOH 90  690  374 HOH HOH A . 
J 6 HOH 91  691  83  HOH HOH A . 
J 6 HOH 92  692  78  HOH HOH A . 
J 6 HOH 93  693  280 HOH HOH A . 
J 6 HOH 94  694  1   HOH HOH A . 
J 6 HOH 95  695  180 HOH HOH A . 
J 6 HOH 96  696  246 HOH HOH A . 
J 6 HOH 97  697  486 HOH HOH A . 
J 6 HOH 98  698  30  HOH HOH A . 
J 6 HOH 99  699  46  HOH HOH A . 
J 6 HOH 100 700  289 HOH HOH A . 
J 6 HOH 101 701  174 HOH HOH A . 
J 6 HOH 102 702  82  HOH HOH A . 
J 6 HOH 103 703  74  HOH HOH A . 
J 6 HOH 104 704  28  HOH HOH A . 
J 6 HOH 105 705  286 HOH HOH A . 
J 6 HOH 106 706  250 HOH HOH A . 
J 6 HOH 107 707  97  HOH HOH A . 
J 6 HOH 108 708  93  HOH HOH A . 
J 6 HOH 109 709  306 HOH HOH A . 
J 6 HOH 110 710  395 HOH HOH A . 
J 6 HOH 111 711  439 HOH HOH A . 
J 6 HOH 112 712  249 HOH HOH A . 
J 6 HOH 113 713  130 HOH HOH A . 
J 6 HOH 114 714  145 HOH HOH A . 
J 6 HOH 115 715  99  HOH HOH A . 
J 6 HOH 116 716  318 HOH HOH A . 
J 6 HOH 117 717  80  HOH HOH A . 
J 6 HOH 118 718  181 HOH HOH A . 
J 6 HOH 119 719  214 HOH HOH A . 
J 6 HOH 120 720  191 HOH HOH A . 
J 6 HOH 121 721  53  HOH HOH A . 
J 6 HOH 122 722  124 HOH HOH A . 
J 6 HOH 123 723  21  HOH HOH A . 
J 6 HOH 124 724  307 HOH HOH A . 
J 6 HOH 125 725  121 HOH HOH A . 
J 6 HOH 126 726  397 HOH HOH A . 
J 6 HOH 127 727  118 HOH HOH A . 
J 6 HOH 128 728  100 HOH HOH A . 
J 6 HOH 129 729  281 HOH HOH A . 
J 6 HOH 130 730  71  HOH HOH A . 
J 6 HOH 131 731  123 HOH HOH A . 
J 6 HOH 132 732  57  HOH HOH A . 
J 6 HOH 133 733  133 HOH HOH A . 
J 6 HOH 134 734  152 HOH HOH A . 
J 6 HOH 135 735  398 HOH HOH A . 
J 6 HOH 136 736  197 HOH HOH A . 
J 6 HOH 137 737  267 HOH HOH A . 
J 6 HOH 138 738  173 HOH HOH A . 
J 6 HOH 139 739  16  HOH HOH A . 
J 6 HOH 140 740  172 HOH HOH A . 
J 6 HOH 141 741  157 HOH HOH A . 
J 6 HOH 142 742  86  HOH HOH A . 
J 6 HOH 143 743  329 HOH HOH A . 
J 6 HOH 144 744  231 HOH HOH A . 
J 6 HOH 145 745  101 HOH HOH A . 
J 6 HOH 146 746  292 HOH HOH A . 
J 6 HOH 147 747  51  HOH HOH A . 
J 6 HOH 148 748  186 HOH HOH A . 
J 6 HOH 149 749  56  HOH HOH A . 
J 6 HOH 150 750  149 HOH HOH A . 
J 6 HOH 151 751  242 HOH HOH A . 
J 6 HOH 152 752  35  HOH HOH A . 
J 6 HOH 153 753  44  HOH HOH A . 
J 6 HOH 154 754  315 HOH HOH A . 
J 6 HOH 155 755  221 HOH HOH A . 
J 6 HOH 156 756  301 HOH HOH A . 
J 6 HOH 157 757  132 HOH HOH A . 
J 6 HOH 158 758  168 HOH HOH A . 
J 6 HOH 159 759  226 HOH HOH A . 
J 6 HOH 160 760  417 HOH HOH A . 
J 6 HOH 161 761  179 HOH HOH A . 
J 6 HOH 162 762  432 HOH HOH A . 
J 6 HOH 163 763  264 HOH HOH A . 
J 6 HOH 164 764  38  HOH HOH A . 
J 6 HOH 165 765  420 HOH HOH A . 
J 6 HOH 166 766  418 HOH HOH A . 
J 6 HOH 167 767  154 HOH HOH A . 
J 6 HOH 168 768  259 HOH HOH A . 
J 6 HOH 169 769  188 HOH HOH A . 
J 6 HOH 170 770  112 HOH HOH A . 
J 6 HOH 171 771  189 HOH HOH A . 
J 6 HOH 172 772  156 HOH HOH A . 
J 6 HOH 173 773  105 HOH HOH A . 
J 6 HOH 174 774  200 HOH HOH A . 
J 6 HOH 175 775  108 HOH HOH A . 
J 6 HOH 176 776  382 HOH HOH A . 
J 6 HOH 177 777  241 HOH HOH A . 
J 6 HOH 178 778  127 HOH HOH A . 
J 6 HOH 179 779  199 HOH HOH A . 
J 6 HOH 180 780  12  HOH HOH A . 
J 6 HOH 181 781  362 HOH HOH A . 
J 6 HOH 182 782  43  HOH HOH A . 
J 6 HOH 183 783  68  HOH HOH A . 
J 6 HOH 184 784  410 HOH HOH A . 
J 6 HOH 185 785  204 HOH HOH A . 
J 6 HOH 186 786  391 HOH HOH A . 
J 6 HOH 187 787  275 HOH HOH A . 
J 6 HOH 188 788  327 HOH HOH A . 
J 6 HOH 189 789  18  HOH HOH A . 
J 6 HOH 190 790  87  HOH HOH A . 
J 6 HOH 191 791  257 HOH HOH A . 
J 6 HOH 192 792  431 HOH HOH A . 
J 6 HOH 193 793  155 HOH HOH A . 
J 6 HOH 194 794  54  HOH HOH A . 
J 6 HOH 195 795  333 HOH HOH A . 
J 6 HOH 196 796  162 HOH HOH A . 
J 6 HOH 197 797  45  HOH HOH A . 
J 6 HOH 198 798  381 HOH HOH A . 
J 6 HOH 199 799  72  HOH HOH A . 
J 6 HOH 200 800  116 HOH HOH A . 
J 6 HOH 201 801  109 HOH HOH A . 
J 6 HOH 202 802  17  HOH HOH A . 
J 6 HOH 203 803  5   HOH HOH A . 
J 6 HOH 204 804  220 HOH HOH A . 
J 6 HOH 205 805  58  HOH HOH A . 
J 6 HOH 206 806  437 HOH HOH A . 
J 6 HOH 207 807  98  HOH HOH A . 
J 6 HOH 208 808  248 HOH HOH A . 
J 6 HOH 209 809  336 HOH HOH A . 
J 6 HOH 210 810  178 HOH HOH A . 
J 6 HOH 211 811  282 HOH HOH A . 
J 6 HOH 212 812  326 HOH HOH A . 
J 6 HOH 213 813  25  HOH HOH A . 
J 6 HOH 214 814  255 HOH HOH A . 
J 6 HOH 215 815  302 HOH HOH A . 
J 6 HOH 216 816  169 HOH HOH A . 
J 6 HOH 217 817  42  HOH HOH A . 
J 6 HOH 218 818  27  HOH HOH A . 
J 6 HOH 219 819  85  HOH HOH A . 
J 6 HOH 220 820  229 HOH HOH A . 
J 6 HOH 221 821  134 HOH HOH A . 
J 6 HOH 222 822  185 HOH HOH A . 
J 6 HOH 223 823  159 HOH HOH A . 
J 6 HOH 224 824  369 HOH HOH A . 
J 6 HOH 225 825  160 HOH HOH A . 
J 6 HOH 226 826  206 HOH HOH A . 
J 6 HOH 227 827  211 HOH HOH A . 
J 6 HOH 228 828  468 HOH HOH A . 
J 6 HOH 229 829  320 HOH HOH A . 
J 6 HOH 230 830  376 HOH HOH A . 
J 6 HOH 231 831  177 HOH HOH A . 
J 6 HOH 232 832  240 HOH HOH A . 
J 6 HOH 233 833  389 HOH HOH A . 
J 6 HOH 234 834  419 HOH HOH A . 
J 6 HOH 235 835  405 HOH HOH A . 
J 6 HOH 236 836  238 HOH HOH A . 
J 6 HOH 237 837  449 HOH HOH A . 
J 6 HOH 238 838  19  HOH HOH A . 
J 6 HOH 239 839  331 HOH HOH A . 
J 6 HOH 240 840  479 HOH HOH A . 
J 6 HOH 241 841  164 HOH HOH A . 
J 6 HOH 242 842  142 HOH HOH A . 
J 6 HOH 243 843  14  HOH HOH A . 
J 6 HOH 244 844  37  HOH HOH A . 
J 6 HOH 245 845  79  HOH HOH A . 
J 6 HOH 246 846  167 HOH HOH A . 
J 6 HOH 247 847  335 HOH HOH A . 
J 6 HOH 248 848  184 HOH HOH A . 
J 6 HOH 249 849  483 HOH HOH A . 
J 6 HOH 250 850  210 HOH HOH A . 
J 6 HOH 251 851  385 HOH HOH A . 
J 6 HOH 252 852  470 HOH HOH A . 
J 6 HOH 253 853  413 HOH HOH A . 
J 6 HOH 254 854  406 HOH HOH A . 
J 6 HOH 255 855  113 HOH HOH A . 
J 6 HOH 256 856  484 HOH HOH A . 
J 6 HOH 257 857  213 HOH HOH A . 
J 6 HOH 258 858  436 HOH HOH A . 
J 6 HOH 259 859  456 HOH HOH A . 
J 6 HOH 260 860  296 HOH HOH A . 
J 6 HOH 261 861  294 HOH HOH A . 
J 6 HOH 262 862  480 HOH HOH A . 
J 6 HOH 263 863  115 HOH HOH A . 
J 6 HOH 264 864  364 HOH HOH A . 
J 6 HOH 265 865  161 HOH HOH A . 
J 6 HOH 266 866  270 HOH HOH A . 
J 6 HOH 267 867  422 HOH HOH A . 
J 6 HOH 268 868  300 HOH HOH A . 
J 6 HOH 269 869  32  HOH HOH A . 
J 6 HOH 270 870  359 HOH HOH A . 
J 6 HOH 271 871  31  HOH HOH A . 
J 6 HOH 272 872  337 HOH HOH A . 
J 6 HOH 273 873  290 HOH HOH A . 
J 6 HOH 274 874  6   HOH HOH A . 
J 6 HOH 275 875  287 HOH HOH A . 
J 6 HOH 276 876  426 HOH HOH A . 
J 6 HOH 277 877  245 HOH HOH A . 
J 6 HOH 278 878  358 HOH HOH A . 
J 6 HOH 279 879  310 HOH HOH A . 
J 6 HOH 280 880  345 HOH HOH A . 
J 6 HOH 281 881  222 HOH HOH A . 
J 6 HOH 282 882  9   HOH HOH A . 
J 6 HOH 283 883  39  HOH HOH A . 
J 6 HOH 284 884  462 HOH HOH A . 
J 6 HOH 285 885  485 HOH HOH A . 
J 6 HOH 286 886  195 HOH HOH A . 
J 6 HOH 287 887  415 HOH HOH A . 
J 6 HOH 288 888  75  HOH HOH A . 
J 6 HOH 289 889  445 HOH HOH A . 
J 6 HOH 290 890  61  HOH HOH A . 
J 6 HOH 291 891  129 HOH HOH A . 
J 6 HOH 292 892  372 HOH HOH A . 
J 6 HOH 293 893  207 HOH HOH A . 
J 6 HOH 294 894  375 HOH HOH A . 
J 6 HOH 295 895  343 HOH HOH A . 
J 6 HOH 296 896  351 HOH HOH A . 
J 6 HOH 297 897  403 HOH HOH A . 
J 6 HOH 298 898  458 HOH HOH A . 
J 6 HOH 299 899  383 HOH HOH A . 
J 6 HOH 300 900  65  HOH HOH A . 
J 6 HOH 301 901  64  HOH HOH A . 
J 6 HOH 302 902  312 HOH HOH A . 
J 6 HOH 303 903  452 HOH HOH A . 
J 6 HOH 304 904  265 HOH HOH A . 
J 6 HOH 305 905  276 HOH HOH A . 
J 6 HOH 306 906  416 HOH HOH A . 
J 6 HOH 307 907  467 HOH HOH A . 
J 6 HOH 308 908  278 HOH HOH A . 
J 6 HOH 309 909  341 HOH HOH A . 
J 6 HOH 310 910  91  HOH HOH A . 
J 6 HOH 311 911  316 HOH HOH A . 
J 6 HOH 312 912  396 HOH HOH A . 
J 6 HOH 313 913  22  HOH HOH A . 
J 6 HOH 314 914  408 HOH HOH A . 
J 6 HOH 315 915  446 HOH HOH A . 
J 6 HOH 316 916  478 HOH HOH A . 
J 6 HOH 317 917  380 HOH HOH A . 
J 6 HOH 318 918  298 HOH HOH A . 
J 6 HOH 319 919  370 HOH HOH A . 
J 6 HOH 320 920  349 HOH HOH A . 
J 6 HOH 321 921  144 HOH HOH A . 
J 6 HOH 322 922  84  HOH HOH A . 
J 6 HOH 323 923  293 HOH HOH A . 
J 6 HOH 324 924  464 HOH HOH A . 
J 6 HOH 325 925  400 HOH HOH A . 
J 6 HOH 326 926  466 HOH HOH A . 
J 6 HOH 327 927  274 HOH HOH A . 
J 6 HOH 328 928  390 HOH HOH A . 
J 6 HOH 329 929  319 HOH HOH A . 
J 6 HOH 330 930  283 HOH HOH A . 
J 6 HOH 331 931  137 HOH HOH A . 
J 6 HOH 332 932  441 HOH HOH A . 
J 6 HOH 333 933  92  HOH HOH A . 
J 6 HOH 334 934  330 HOH HOH A . 
J 6 HOH 335 935  334 HOH HOH A . 
J 6 HOH 336 936  34  HOH HOH A . 
J 6 HOH 337 937  114 HOH HOH A . 
J 6 HOH 338 938  313 HOH HOH A . 
J 6 HOH 339 939  311 HOH HOH A . 
J 6 HOH 340 940  402 HOH HOH A . 
J 6 HOH 341 941  388 HOH HOH A . 
J 6 HOH 342 942  251 HOH HOH A . 
J 6 HOH 343 943  233 HOH HOH A . 
J 6 HOH 344 944  151 HOH HOH A . 
J 6 HOH 345 945  147 HOH HOH A . 
J 6 HOH 346 946  304 HOH HOH A . 
J 6 HOH 347 947  469 HOH HOH A . 
J 6 HOH 348 948  308 HOH HOH A . 
J 6 HOH 349 949  252 HOH HOH A . 
J 6 HOH 350 950  344 HOH HOH A . 
J 6 HOH 351 951  66  HOH HOH A . 
J 6 HOH 352 952  254 HOH HOH A . 
J 6 HOH 353 953  338 HOH HOH A . 
J 6 HOH 354 954  477 HOH HOH A . 
J 6 HOH 355 955  218 HOH HOH A . 
J 6 HOH 356 956  247 HOH HOH A . 
J 6 HOH 357 957  90  HOH HOH A . 
J 6 HOH 358 958  454 HOH HOH A . 
J 6 HOH 359 959  94  HOH HOH A . 
J 6 HOH 360 960  128 HOH HOH A . 
J 6 HOH 361 961  371 HOH HOH A . 
J 6 HOH 362 962  203 HOH HOH A . 
J 6 HOH 363 963  321 HOH HOH A . 
J 6 HOH 364 964  474 HOH HOH A . 
J 6 HOH 365 965  324 HOH HOH A . 
J 6 HOH 366 966  228 HOH HOH A . 
J 6 HOH 367 967  88  HOH HOH A . 
J 6 HOH 368 968  256 HOH HOH A . 
J 6 HOH 369 969  353 HOH HOH A . 
J 6 HOH 370 970  363 HOH HOH A . 
J 6 HOH 371 971  360 HOH HOH A . 
J 6 HOH 372 972  263 HOH HOH A . 
J 6 HOH 373 973  295 HOH HOH A . 
J 6 HOH 374 974  332 HOH HOH A . 
J 6 HOH 375 975  135 HOH HOH A . 
J 6 HOH 376 976  212 HOH HOH A . 
J 6 HOH 377 977  63  HOH HOH A . 
J 6 HOH 378 978  357 HOH HOH A . 
J 6 HOH 379 979  386 HOH HOH A . 
J 6 HOH 380 980  183 HOH HOH A . 
J 6 HOH 381 981  48  HOH HOH A . 
J 6 HOH 382 982  192 HOH HOH A . 
J 6 HOH 383 983  139 HOH HOH A . 
J 6 HOH 384 984  146 HOH HOH A . 
J 6 HOH 385 985  425 HOH HOH A . 
J 6 HOH 386 986  67  HOH HOH A . 
J 6 HOH 387 987  50  HOH HOH A . 
J 6 HOH 388 988  378 HOH HOH A . 
J 6 HOH 389 989  217 HOH HOH A . 
J 6 HOH 390 990  377 HOH HOH A . 
J 6 HOH 391 991  475 HOH HOH A . 
J 6 HOH 392 992  440 HOH HOH A . 
J 6 HOH 393 993  216 HOH HOH A . 
J 6 HOH 394 994  225 HOH HOH A . 
J 6 HOH 395 995  342 HOH HOH A . 
J 6 HOH 396 996  89  HOH HOH A . 
J 6 HOH 397 997  322 HOH HOH A . 
J 6 HOH 398 998  260 HOH HOH A . 
J 6 HOH 399 999  49  HOH HOH A . 
J 6 HOH 400 1000 262 HOH HOH A . 
J 6 HOH 401 1001 325 HOH HOH A . 
J 6 HOH 402 1002 451 HOH HOH A . 
J 6 HOH 403 1003 314 HOH HOH A . 
J 6 HOH 404 1004 465 HOH HOH A . 
J 6 HOH 405 1005 209 HOH HOH A . 
J 6 HOH 406 1006 412 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? 1.21.1_5286 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9JI1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.994 
_cell.length_a_esd                 ? 
_cell.length_b                     53.578 
_cell.length_b_esd                 ? 
_cell.length_c                     139.097 
_cell.length_c_esd                 ? 
_cell.volume                       394939.845 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9JI1 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9JI1 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.24 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.2 
_exptl_crystal.description                  'red rectangle 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              6.1 
_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    
;12-20% PEG4000, 10% MPD, 0.2 M NaCl, and 0.1 M Bis-Tris (pH 6.1)
Flufenamic Acid (FLF) is introduced by three times soaking the crystal to the mother liqure containing 11 mM FLF.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER R 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-02-14 
_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   1.000 
_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                        'SPRING-8 BEAMLINE BL26B1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL26B1 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          22.52 
_reflns.entry_id                                       9JI1 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.47 
_reflns.d_resolution_low                               50 
_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                                     66980 
_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                           97.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.37 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          24.12 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.047 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.044 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.47 
_reflns_shell.d_res_low                                     1.56 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.08 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             9337 
_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                               5.75 
_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                               0.650 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.853 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          85.3 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.583 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               29.86 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9JI1 
_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                            1.47 
_refine.ls_d_res_low                             42.15 
_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                     66969 
_refine.ls_number_reflns_R_free                  3349 
_refine.ls_number_reflns_R_work                  63620 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.60 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1522 
_refine.ls_R_factor_R_free                       0.1900 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1502 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 18.8476 
_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                            0.2143 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.47 
_refine_hist.d_res_low                        42.15 
_refine_hist.number_atoms_solvent             406 
_refine_hist.number_atoms_total               3603 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3106 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         91 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0055  ? 3397 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8742  ? 4661 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0781  ? 523  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0096  ? 617  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.8703 ? 1282 ? f_dihedral_angle_d ? ? 
# 
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' 1.47 1.49  . . 109 2080 77.32  . . . . 0.5666 . . . . . . . . . . . 0.5385 
'X-RAY DIFFRACTION' 1.49 1.51  . . 116 2201 82.46  . . . . 0.4073 . . . . . . . . . . . 0.4273 
'X-RAY DIFFRACTION' 1.51 1.53  . . 125 2378 88.73  . . . . 0.3248 . . . . . . . . . . . 0.3393 
'X-RAY DIFFRACTION' 1.53 1.56  . . 132 2507 94.28  . . . . 0.2492 . . . . . . . . . . . 0.2964 
'X-RAY DIFFRACTION' 1.56 1.59  . . 141 2669 99.61  . . . . 0.2003 . . . . . . . . . . . 0.2737 
'X-RAY DIFFRACTION' 1.59 1.62  . . 141 2689 99.82  . . . . 0.1719 . . . . . . . . . . . 0.2298 
'X-RAY DIFFRACTION' 1.62 1.65  . . 140 2664 99.82  . . . . 0.1530 . . . . . . . . . . . 0.2089 
'X-RAY DIFFRACTION' 1.65 1.68  . . 143 2700 99.93  . . . . 0.1430 . . . . . . . . . . . 0.1996 
'X-RAY DIFFRACTION' 1.68 1.72  . . 142 2699 99.96  . . . . 0.1384 . . . . . . . . . . . 0.2127 
'X-RAY DIFFRACTION' 1.72 1.76  . . 141 2682 100.00 . . . . 0.1397 . . . . . . . . . . . 0.1989 
'X-RAY DIFFRACTION' 1.76 1.80  . . 142 2691 100.00 . . . . 0.1488 . . . . . . . . . . . 0.2039 
'X-RAY DIFFRACTION' 1.80 1.85  . . 141 2685 100.00 . . . . 0.1738 . . . . . . . . . . . 0.2471 
'X-RAY DIFFRACTION' 1.85 1.90  . . 142 2710 100.00 . . . . 0.1900 . . . . . . . . . . . 0.2546 
'X-RAY DIFFRACTION' 1.90 1.96  . . 143 2703 99.96  . . . . 0.1988 . . . . . . . . . . . 0.2804 
'X-RAY DIFFRACTION' 1.96 2.03  . . 142 2695 100.00 . . . . 0.1467 . . . . . . . . . . . 0.1944 
'X-RAY DIFFRACTION' 2.03 2.12  . . 142 2715 100.00 . . . . 0.1414 . . . . . . . . . . . 0.1981 
'X-RAY DIFFRACTION' 2.12 2.21  . . 144 2724 100.00 . . . . 0.1338 . . . . . . . . . . . 0.1888 
'X-RAY DIFFRACTION' 2.21 2.33  . . 143 2721 100.00 . . . . 0.1395 . . . . . . . . . . . 0.1911 
'X-RAY DIFFRACTION' 2.33 2.48  . . 143 2709 100.00 . . . . 0.1391 . . . . . . . . . . . 0.2045 
'X-RAY DIFFRACTION' 2.48 2.67  . . 144 2743 100.00 . . . . 0.1452 . . . . . . . . . . . 0.2053 
'X-RAY DIFFRACTION' 2.67 2.93  . . 145 2746 100.00 . . . . 0.1489 . . . . . . . . . . . 0.1951 
'X-RAY DIFFRACTION' 2.93 3.36  . . 145 2773 100.00 . . . . 0.1421 . . . . . . . . . . . 0.1727 
'X-RAY DIFFRACTION' 3.36 4.23  . . 148 2795 100.00 . . . . 0.1253 . . . . . . . . . . . 0.1484 
'X-RAY DIFFRACTION' 4.23 42.15 . . 155 2941 99.81  . . . . 0.1405 . . . . . . . . . . . 0.1434 
# 
_struct.entry_id                     9JI1 
_struct.title                        'CYP105A1 complexed with flufenamic acid (FLF)' 
_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        9JI1 
_struct_keywords.text            
'P450, CYP105A1, nonsteroidal anti-inflammatory drugs, diclofenac, flufenamic acid, 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 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
G N N 5 ? 
H N N 5 ? 
I N N 5 ? 
J N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CPXE_STRGO 
_struct_ref.pdbx_db_accession          P18326 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTDTATTPQTTDAPAFPSNRSCPYQLPDGYAQLRDTPGPLHRVTLYDGRQAWVVTKHEAARKLLGDPRLSSNRTDDNFPA
TSPRFEAVRESPQAFIGLDPPEHGTRRRMTISEFTVKRIKGMRPEVEEVVHGFLDEMLAAGPTADLVSQFALPVPSMVIC
RLLGVPYADHEFFQDASKRLVQSTDAQSALTARNDLAGYLDGLITQFQTEPGAGLVGALVADQLANGEIDREELISTAML
LLIAGHETTASMTSLSVITLLDHPEQYAALRADRSLVPGAVEELLRYLAIADIAGGRVATADIEVEGHLIRAGEGVIVVN
SIANRDGTVYEDPDALDIHRSARHHLAFGFGVHQCLGQNLARLELEVILNALMDRVPTLRLAVPVEQLVLRPGTTIQGVN
ELPVTW
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9JI1 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 406 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P18326 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  406 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       406 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9JI1 GLN A 308 ? UNP P18326 HIS 308 conflict         308 1 
1 9JI1 HIS A 407 ? UNP P18326 ?   ?   'expression tag' 407 2 
1 9JI1 HIS A 408 ? UNP P18326 ?   ?   'expression tag' 408 3 
1 9JI1 HIS A 409 ? UNP P18326 ?   ?   'expression tag' 409 4 
1 9JI1 HIS A 410 ? UNP P18326 ?   ?   'expression tag' 410 5 
1 9JI1 HIS A 411 ? UNP P18326 ?   ?   'expression tag' 411 6 
1 9JI1 HIS A 412 ? UNP P18326 ?   ?   'expression tag' 412 7 
# 
_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   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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 
# 
_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                'monomer in solution' 
# 
_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 PRO A 27  ? THR A 36  ? PRO A 27  THR A 36  1 ? 10 
HELX_P HELX_P2  AA2 LYS A 56  ? GLY A 65  ? LYS A 56  GLY A 65  1 ? 10 
HELX_P HELX_P3  AA3 ARG A 84  ? ARG A 89  ? ARG A 84  ARG A 89  5 ? 6  
HELX_P HELX_P4  AA4 ALA A 94  ? LEU A 98  ? ALA A 94  LEU A 98  5 ? 5  
HELX_P HELX_P5  AA5 PRO A 101 ? ARG A 108 ? PRO A 101 ARG A 108 1 ? 8  
HELX_P HELX_P6  AA6 MET A 109 ? PHE A 114 ? MET A 109 PHE A 114 5 ? 6  
HELX_P HELX_P7  AA7 THR A 115 ? MET A 122 ? THR A 115 MET A 122 1 ? 8  
HELX_P HELX_P8  AA8 MET A 122 ? GLY A 141 ? MET A 122 GLY A 141 1 ? 20 
HELX_P HELX_P9  AA9 LEU A 146 ? PHE A 150 ? LEU A 146 PHE A 150 1 ? 5  
HELX_P HELX_P10 AB1 LEU A 152 ? GLY A 164 ? LEU A 152 GLY A 164 1 ? 13 
HELX_P HELX_P11 AB2 PRO A 166 ? ALA A 168 ? PRO A 166 ALA A 168 5 ? 3  
HELX_P HELX_P12 AB3 ASP A 169 ? GLN A 182 ? ASP A 169 GLN A 182 1 ? 14 
HELX_P HELX_P13 AB4 ASP A 185 ? GLU A 210 ? ASP A 185 GLU A 210 1 ? 26 
HELX_P HELX_P14 AB5 GLY A 214 ? ASP A 222 ? GLY A 214 ASP A 222 1 ? 9  
HELX_P HELX_P15 AB6 ASP A 230 ? ASP A 262 ? ASP A 230 ASP A 262 1 ? 33 
HELX_P HELX_P16 AB7 HIS A 263 ? ASP A 273 ? HIS A 263 ASP A 273 1 ? 11 
HELX_P HELX_P17 AB8 LEU A 276 ? ALA A 289 ? LEU A 276 ALA A 289 1 ? 14 
HELX_P HELX_P18 AB9 ALA A 291 ? ALA A 294 ? ALA A 291 ALA A 294 5 ? 4  
HELX_P HELX_P19 AC1 VAL A 319 ? ASN A 324 ? VAL A 319 ASN A 324 1 ? 6  
HELX_P HELX_P20 AC2 GLY A 357 ? VAL A 376 ? GLY A 357 VAL A 376 1 ? 20 
HELX_P HELX_P21 AC3 PRO A 384 ? LEU A 388 ? PRO A 384 LEU A 388 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            metalc1 
_struct_conn.conn_type_id                  metalc 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            355 
_struct_conn.ptnr1_label_atom_id           SG 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           B 
_struct_conn.ptnr2_label_comp_id           HEM 
_struct_conn.ptnr2_label_seq_id            . 
_struct_conn.ptnr2_label_atom_id           FE 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             355 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            HEM 
_struct_conn.ptnr2_auth_seq_id             501 
_struct_conn.ptnr2_symmetry                1_555 
_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               2.359 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_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  SG ? A CYS 355 ? A CYS 355 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 NA ? B HEM . ? A HEM 501 ? 1_555 105.1 ? 
2  SG ? A CYS 355 ? A CYS 355 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 NB ? B HEM . ? A HEM 501 ? 1_555 93.2  ? 
3  NA ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 NB ? B HEM . ? A HEM 501 ? 1_555 88.8  ? 
4  SG ? A CYS 355 ? A CYS 355 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 NC ? B HEM . ? A HEM 501 ? 1_555 88.2  ? 
5  NA ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 NC ? B HEM . ? A HEM 501 ? 1_555 166.8 ? 
6  NB ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 NC ? B HEM . ? A HEM 501 ? 1_555 90.0  ? 
7  SG ? A CYS 355 ? A CYS 355 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 ND ? B HEM . ? A HEM 501 ? 1_555 101.6 ? 
8  NA ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 ND ? B HEM . ? A HEM 501 ? 1_555 88.1  ? 
9  NB ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 ND ? B HEM . ? A HEM 501 ? 1_555 165.2 ? 
10 NC ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 ND ? B HEM . ? A HEM 501 ? 1_555 89.7  ? 
# 
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 PHE 16  A . ? PHE 16  A PRO 17  A ? PRO 17  A 1 1.14 
2 PRO 100 A . ? PRO 100 A PRO 101 A ? PRO 101 A 1 5.93 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 3 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 40  ? THR A 44  ? LEU A 40  THR A 44  
AA1 2 GLN A 50  ? VAL A 54  ? GLN A 50  VAL A 54  
AA1 3 GLY A 315 ? VAL A 318 ? GLY A 315 VAL A 318 
AA1 4 GLY A 296 ? ALA A 299 ? GLY A 296 ALA A 299 
AA1 5 LEU A 69  ? SER A 70  ? LEU A 69  SER A 70  
AA2 1 THR A 143 ? ASP A 145 ? THR A 143 ASP A 145 
AA2 2 PRO A 403 ? THR A 405 ? PRO A 403 THR A 405 
AA2 3 ARG A 380 ? LEU A 381 ? ARG A 380 LEU A 381 
AA3 1 ILE A 303 ? VAL A 305 ? ILE A 303 VAL A 305 
AA3 2 GLN A 308 ? ILE A 310 ? GLN A 308 ILE A 310 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 43  ? N VAL A 43  O ALA A 51  ? O ALA A 51  
AA1 2 3 N TRP A 52  ? N TRP A 52  O ILE A 317 ? O ILE A 317 
AA1 3 4 O VAL A 316 ? O VAL A 316 N ARG A 297 ? N ARG A 297 
AA1 4 5 O VAL A 298 ? O VAL A 298 N SER A 70  ? N SER A 70  
AA2 1 2 N ALA A 144 ? N ALA A 144 O VAL A 404 ? O VAL A 404 
AA2 2 3 O THR A 405 ? O THR A 405 N ARG A 380 ? N ARG A 380 
AA3 1 2 N VAL A 305 ? N VAL A 305 O GLN A 308 ? O GLN A 308 
# 
_pdbx_entry_details.entry_id                   9JI1 
_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 PHE A 150 ? ? -148.74 -54.67 
2 1 ASP A 222 ? ? -108.40 -78.86 
3 1 ALA A 289 ? ? 28.41   72.85  
4 1 CYS A 355 ? ? -37.55  118.88 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 1001 ? 5.88 . 
2 1 O ? A HOH 1002 ? 5.89 . 
3 1 O ? A HOH 1003 ? 5.99 . 
4 1 O ? A HOH 1004 ? 6.60 . 
5 1 O ? A HOH 1005 ? 6.97 . 
6 1 O ? A HOH 1006 ? 7.26 . 
# 
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 MET 1   ? A MET 1   
2 1 Y 1 A THR 2   ? A THR 2   
3 1 Y 1 A ASP 3   ? A ASP 3   
4 1 Y 1 A HIS 409 ? A HIS 409 
5 1 Y 1 A HIS 410 ? A HIS 410 
6 1 Y 1 A HIS 411 ? A HIS 411 
7 1 Y 1 A HIS 412 ? A HIS 412 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N     N  N N 1   
ALA CA    C  N S 2   
ALA C     C  N N 3   
ALA O     O  N N 4   
ALA CB    C  N N 5   
ALA OXT   O  N N 6   
ALA H     H  N N 7   
ALA H2    H  N N 8   
ALA HA    H  N N 9   
ALA HB1   H  N N 10  
ALA HB2   H  N N 11  
ALA HB3   H  N N 12  
ALA HXT   H  N N 13  
ARG N     N  N N 14  
ARG CA    C  N S 15  
ARG C     C  N N 16  
ARG O     O  N N 17  
ARG CB    C  N N 18  
ARG CG    C  N N 19  
ARG CD    C  N N 20  
ARG NE    N  N N 21  
ARG CZ    C  N N 22  
ARG NH1   N  N N 23  
ARG NH2   N  N N 24  
ARG OXT   O  N N 25  
ARG H     H  N N 26  
ARG H2    H  N N 27  
ARG HA    H  N N 28  
ARG HB2   H  N N 29  
ARG HB3   H  N N 30  
ARG HG2   H  N N 31  
ARG HG3   H  N N 32  
ARG HD2   H  N N 33  
ARG HD3   H  N N 34  
ARG HE    H  N N 35  
ARG HH11  H  N N 36  
ARG HH12  H  N N 37  
ARG HH21  H  N N 38  
ARG HH22  H  N N 39  
ARG HXT   H  N N 40  
ASN N     N  N N 41  
ASN CA    C  N S 42  
ASN C     C  N N 43  
ASN O     O  N N 44  
ASN CB    C  N N 45  
ASN CG    C  N N 46  
ASN OD1   O  N N 47  
ASN ND2   N  N N 48  
ASN OXT   O  N N 49  
ASN H     H  N N 50  
ASN H2    H  N N 51  
ASN HA    H  N N 52  
ASN HB2   H  N N 53  
ASN HB3   H  N N 54  
ASN HD21  H  N N 55  
ASN HD22  H  N N 56  
ASN HXT   H  N N 57  
ASP N     N  N N 58  
ASP CA    C  N S 59  
ASP C     C  N N 60  
ASP O     O  N N 61  
ASP CB    C  N N 62  
ASP CG    C  N N 63  
ASP OD1   O  N N 64  
ASP OD2   O  N N 65  
ASP OXT   O  N N 66  
ASP H     H  N N 67  
ASP H2    H  N N 68  
ASP HA    H  N N 69  
ASP HB2   H  N N 70  
ASP HB3   H  N N 71  
ASP HD2   H  N N 72  
ASP HXT   H  N N 73  
CYS N     N  N N 74  
CYS CA    C  N R 75  
CYS C     C  N N 76  
CYS O     O  N N 77  
CYS CB    C  N N 78  
CYS SG    S  N N 79  
CYS OXT   O  N N 80  
CYS H     H  N N 81  
CYS H2    H  N N 82  
CYS HA    H  N N 83  
CYS HB2   H  N N 84  
CYS HB3   H  N N 85  
CYS HG    H  N N 86  
CYS HXT   H  N N 87  
EDO C1    C  N N 88  
EDO O1    O  N N 89  
EDO C2    C  N N 90  
EDO O2    O  N N 91  
EDO H11   H  N N 92  
EDO H12   H  N N 93  
EDO HO1   H  N N 94  
EDO H21   H  N N 95  
EDO H22   H  N N 96  
EDO HO2   H  N N 97  
FLF C1    C  Y N 98  
FLF O1    O  N N 99  
FLF C2    C  Y N 100 
FLF C3    C  Y N 101 
FLF O2    O  N N 102 
FLF C4    C  Y N 103 
FLF C5    C  Y N 104 
FLF C6    C  Y N 105 
FLF C7    C  N N 106 
FLF N     N  N N 107 
FLF "C1'" C  Y N 108 
FLF "C2'" C  Y N 109 
FLF "C3'" C  Y N 110 
FLF "C4'" C  Y N 111 
FLF "C5'" C  Y N 112 
FLF "C6'" C  Y N 113 
FLF "C7'" C  N N 114 
FLF F1    F  N N 115 
FLF F2    F  N N 116 
FLF F3    F  N N 117 
FLF H2    H  N N 118 
FLF H3    H  N N 119 
FLF HO2   H  N N 120 
FLF H4    H  N N 121 
FLF H5    H  N N 122 
FLF HN1   H  N N 123 
FLF "H2'" H  N N 124 
FLF "H4'" H  N N 125 
FLF "H5'" H  N N 126 
FLF "H6'" H  N N 127 
GLN N     N  N N 128 
GLN CA    C  N S 129 
GLN C     C  N N 130 
GLN O     O  N N 131 
GLN CB    C  N N 132 
GLN CG    C  N N 133 
GLN CD    C  N N 134 
GLN OE1   O  N N 135 
GLN NE2   N  N N 136 
GLN OXT   O  N N 137 
GLN H     H  N N 138 
GLN H2    H  N N 139 
GLN HA    H  N N 140 
GLN HB2   H  N N 141 
GLN HB3   H  N N 142 
GLN HG2   H  N N 143 
GLN HG3   H  N N 144 
GLN HE21  H  N N 145 
GLN HE22  H  N N 146 
GLN HXT   H  N N 147 
GLU N     N  N N 148 
GLU CA    C  N S 149 
GLU C     C  N N 150 
GLU O     O  N N 151 
GLU CB    C  N N 152 
GLU CG    C  N N 153 
GLU CD    C  N N 154 
GLU OE1   O  N N 155 
GLU OE2   O  N N 156 
GLU OXT   O  N N 157 
GLU H     H  N N 158 
GLU H2    H  N N 159 
GLU HA    H  N N 160 
GLU HB2   H  N N 161 
GLU HB3   H  N N 162 
GLU HG2   H  N N 163 
GLU HG3   H  N N 164 
GLU HE2   H  N N 165 
GLU HXT   H  N N 166 
GLY N     N  N N 167 
GLY CA    C  N N 168 
GLY C     C  N N 169 
GLY O     O  N N 170 
GLY OXT   O  N N 171 
GLY H     H  N N 172 
GLY H2    H  N N 173 
GLY HA2   H  N N 174 
GLY HA3   H  N N 175 
GLY HXT   H  N N 176 
HEM CHA   C  N N 177 
HEM CHB   C  N N 178 
HEM CHC   C  N N 179 
HEM CHD   C  N N 180 
HEM C1A   C  Y N 181 
HEM C2A   C  Y N 182 
HEM C3A   C  Y N 183 
HEM C4A   C  Y N 184 
HEM CMA   C  N N 185 
HEM CAA   C  N N 186 
HEM CBA   C  N N 187 
HEM CGA   C  N N 188 
HEM O1A   O  N N 189 
HEM O2A   O  N N 190 
HEM C1B   C  N N 191 
HEM C2B   C  N N 192 
HEM C3B   C  N N 193 
HEM C4B   C  N N 194 
HEM CMB   C  N N 195 
HEM CAB   C  N N 196 
HEM CBB   C  N N 197 
HEM C1C   C  Y N 198 
HEM C2C   C  Y N 199 
HEM C3C   C  Y N 200 
HEM C4C   C  Y N 201 
HEM CMC   C  N N 202 
HEM CAC   C  N N 203 
HEM CBC   C  N N 204 
HEM C1D   C  N N 205 
HEM C2D   C  N N 206 
HEM C3D   C  N N 207 
HEM C4D   C  N N 208 
HEM CMD   C  N N 209 
HEM CAD   C  N N 210 
HEM CBD   C  N N 211 
HEM CGD   C  N N 212 
HEM O1D   O  N N 213 
HEM O2D   O  N N 214 
HEM NA    N  Y N 215 
HEM NB    N  N N 216 
HEM NC    N  Y N 217 
HEM ND    N  N N 218 
HEM FE    FE N N 219 
HEM HHB   H  N N 220 
HEM HHC   H  N N 221 
HEM HHD   H  N N 222 
HEM HMA   H  N N 223 
HEM HMAA  H  N N 224 
HEM HMAB  H  N N 225 
HEM HAA   H  N N 226 
HEM HAAA  H  N N 227 
HEM HBA   H  N N 228 
HEM HBAA  H  N N 229 
HEM HMB   H  N N 230 
HEM HMBA  H  N N 231 
HEM HMBB  H  N N 232 
HEM HAB   H  N N 233 
HEM HBB   H  N N 234 
HEM HBBA  H  N N 235 
HEM HMC   H  N N 236 
HEM HMCA  H  N N 237 
HEM HMCB  H  N N 238 
HEM HAC   H  N N 239 
HEM HBC   H  N N 240 
HEM HBCA  H  N N 241 
HEM HMD   H  N N 242 
HEM HMDA  H  N N 243 
HEM HMDB  H  N N 244 
HEM HAD   H  N N 245 
HEM HADA  H  N N 246 
HEM HBD   H  N N 247 
HEM HBDA  H  N N 248 
HEM H2A   H  N N 249 
HEM H2D   H  N N 250 
HEM HHA   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 
PHE N     N  N N 365 
PHE CA    C  N S 366 
PHE C     C  N N 367 
PHE O     O  N N 368 
PHE CB    C  N N 369 
PHE CG    C  Y N 370 
PHE CD1   C  Y N 371 
PHE CD2   C  Y N 372 
PHE CE1   C  Y N 373 
PHE CE2   C  Y N 374 
PHE CZ    C  Y N 375 
PHE OXT   O  N N 376 
PHE H     H  N N 377 
PHE H2    H  N N 378 
PHE HA    H  N N 379 
PHE HB2   H  N N 380 
PHE HB3   H  N N 381 
PHE HD1   H  N N 382 
PHE HD2   H  N N 383 
PHE HE1   H  N N 384 
PHE HE2   H  N N 385 
PHE HZ    H  N N 386 
PHE HXT   H  N N 387 
PRO N     N  N N 388 
PRO CA    C  N S 389 
PRO C     C  N N 390 
PRO O     O  N N 391 
PRO CB    C  N N 392 
PRO CG    C  N N 393 
PRO CD    C  N N 394 
PRO OXT   O  N N 395 
PRO H     H  N N 396 
PRO HA    H  N N 397 
PRO HB2   H  N N 398 
PRO HB3   H  N N 399 
PRO HG2   H  N N 400 
PRO HG3   H  N N 401 
PRO HD2   H  N N 402 
PRO HD3   H  N N 403 
PRO HXT   H  N N 404 
SER N     N  N N 405 
SER CA    C  N S 406 
SER C     C  N N 407 
SER O     O  N N 408 
SER CB    C  N N 409 
SER OG    O  N N 410 
SER OXT   O  N N 411 
SER H     H  N N 412 
SER H2    H  N N 413 
SER HA    H  N N 414 
SER HB2   H  N N 415 
SER HB3   H  N N 416 
SER HG    H  N N 417 
SER HXT   H  N N 418 
THR N     N  N N 419 
THR CA    C  N S 420 
THR C     C  N N 421 
THR O     O  N N 422 
THR CB    C  N R 423 
THR OG1   O  N N 424 
THR CG2   C  N N 425 
THR OXT   O  N N 426 
THR H     H  N N 427 
THR H2    H  N N 428 
THR HA    H  N N 429 
THR HB    H  N N 430 
THR HG1   H  N N 431 
THR HG21  H  N N 432 
THR HG22  H  N N 433 
THR HG23  H  N N 434 
THR HXT   H  N N 435 
TRP N     N  N N 436 
TRP CA    C  N S 437 
TRP C     C  N N 438 
TRP O     O  N N 439 
TRP CB    C  N N 440 
TRP CG    C  Y N 441 
TRP CD1   C  Y N 442 
TRP CD2   C  Y N 443 
TRP NE1   N  Y N 444 
TRP CE2   C  Y N 445 
TRP CE3   C  Y N 446 
TRP CZ2   C  Y N 447 
TRP CZ3   C  Y N 448 
TRP CH2   C  Y N 449 
TRP OXT   O  N N 450 
TRP H     H  N N 451 
TRP H2    H  N N 452 
TRP HA    H  N N 453 
TRP HB2   H  N N 454 
TRP HB3   H  N N 455 
TRP HD1   H  N N 456 
TRP HE1   H  N N 457 
TRP HE3   H  N N 458 
TRP HZ2   H  N N 459 
TRP HZ3   H  N N 460 
TRP HH2   H  N N 461 
TRP HXT   H  N N 462 
TRS C     C  N N 463 
TRS C1    C  N N 464 
TRS C2    C  N N 465 
TRS C3    C  N N 466 
TRS N     N  N N 467 
TRS O1    O  N N 468 
TRS O2    O  N N 469 
TRS O3    O  N N 470 
TRS H11   H  N N 471 
TRS H12   H  N N 472 
TRS H21   H  N N 473 
TRS H22   H  N N 474 
TRS H31   H  N N 475 
TRS H32   H  N N 476 
TRS HN1   H  N N 477 
TRS HN2   H  N N 478 
TRS HN3   H  N N 479 
TRS HO1   H  N N 480 
TRS HO2   H  N N 481 
TRS HO3   H  N N 482 
TYR N     N  N N 483 
TYR CA    C  N S 484 
TYR C     C  N N 485 
TYR O     O  N N 486 
TYR CB    C  N N 487 
TYR CG    C  Y N 488 
TYR CD1   C  Y N 489 
TYR CD2   C  Y N 490 
TYR CE1   C  Y N 491 
TYR CE2   C  Y N 492 
TYR CZ    C  Y N 493 
TYR OH    O  N N 494 
TYR OXT   O  N N 495 
TYR H     H  N N 496 
TYR H2    H  N N 497 
TYR HA    H  N N 498 
TYR HB2   H  N N 499 
TYR HB3   H  N N 500 
TYR HD1   H  N N 501 
TYR HD2   H  N N 502 
TYR HE1   H  N N 503 
TYR HE2   H  N N 504 
TYR HH    H  N N 505 
TYR HXT   H  N N 506 
VAL N     N  N N 507 
VAL CA    C  N S 508 
VAL C     C  N N 509 
VAL O     O  N N 510 
VAL CB    C  N N 511 
VAL CG1   C  N N 512 
VAL CG2   C  N N 513 
VAL OXT   O  N N 514 
VAL H     H  N N 515 
VAL H2    H  N N 516 
VAL HA    H  N N 517 
VAL HB    H  N N 518 
VAL HG11  H  N N 519 
VAL HG12  H  N N 520 
VAL HG13  H  N N 521 
VAL HG21  H  N N 522 
VAL HG22  H  N N 523 
VAL HG23  H  N N 524 
VAL HXT   H  N N 525 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N     CA    sing N N 1   
ALA N     H     sing N N 2   
ALA N     H2    sing N N 3   
ALA CA    C     sing N N 4   
ALA CA    CB    sing N N 5   
ALA CA    HA    sing N N 6   
ALA C     O     doub N N 7   
ALA C     OXT   sing N N 8   
ALA CB    HB1   sing N N 9   
ALA CB    HB2   sing N N 10  
ALA CB    HB3   sing N N 11  
ALA OXT   HXT   sing N N 12  
ARG N     CA    sing N N 13  
ARG N     H     sing N N 14  
ARG N     H2    sing N N 15  
ARG CA    C     sing N N 16  
ARG CA    CB    sing N N 17  
ARG CA    HA    sing N N 18  
ARG C     O     doub N N 19  
ARG C     OXT   sing N N 20  
ARG CB    CG    sing N N 21  
ARG CB    HB2   sing N N 22  
ARG CB    HB3   sing N N 23  
ARG CG    CD    sing N N 24  
ARG CG    HG2   sing N N 25  
ARG CG    HG3   sing N N 26  
ARG CD    NE    sing N N 27  
ARG CD    HD2   sing N N 28  
ARG CD    HD3   sing N N 29  
ARG NE    CZ    sing N N 30  
ARG NE    HE    sing N N 31  
ARG CZ    NH1   sing N N 32  
ARG CZ    NH2   doub N N 33  
ARG NH1   HH11  sing N N 34  
ARG NH1   HH12  sing N N 35  
ARG NH2   HH21  sing N N 36  
ARG NH2   HH22  sing N N 37  
ARG OXT   HXT   sing N N 38  
ASN N     CA    sing N N 39  
ASN N     H     sing N N 40  
ASN N     H2    sing N N 41  
ASN CA    C     sing N N 42  
ASN CA    CB    sing N N 43  
ASN CA    HA    sing N N 44  
ASN C     O     doub N N 45  
ASN C     OXT   sing N N 46  
ASN CB    CG    sing N N 47  
ASN CB    HB2   sing N N 48  
ASN CB    HB3   sing N N 49  
ASN CG    OD1   doub N N 50  
ASN CG    ND2   sing N N 51  
ASN ND2   HD21  sing N N 52  
ASN ND2   HD22  sing N N 53  
ASN OXT   HXT   sing N N 54  
ASP N     CA    sing N N 55  
ASP N     H     sing N N 56  
ASP N     H2    sing N N 57  
ASP CA    C     sing N N 58  
ASP CA    CB    sing N N 59  
ASP CA    HA    sing N N 60  
ASP C     O     doub N N 61  
ASP C     OXT   sing N N 62  
ASP CB    CG    sing N N 63  
ASP CB    HB2   sing N N 64  
ASP CB    HB3   sing N N 65  
ASP CG    OD1   doub N N 66  
ASP CG    OD2   sing N N 67  
ASP OD2   HD2   sing N N 68  
ASP OXT   HXT   sing N N 69  
CYS N     CA    sing N N 70  
CYS N     H     sing N N 71  
CYS N     H2    sing N N 72  
CYS CA    C     sing N N 73  
CYS CA    CB    sing N N 74  
CYS CA    HA    sing N N 75  
CYS C     O     doub N N 76  
CYS C     OXT   sing N N 77  
CYS CB    SG    sing N N 78  
CYS CB    HB2   sing N N 79  
CYS CB    HB3   sing N N 80  
CYS SG    HG    sing N N 81  
CYS OXT   HXT   sing N N 82  
EDO C1    O1    sing N N 83  
EDO C1    C2    sing N N 84  
EDO C1    H11   sing N N 85  
EDO C1    H12   sing N N 86  
EDO O1    HO1   sing N N 87  
EDO C2    O2    sing N N 88  
EDO C2    H21   sing N N 89  
EDO C2    H22   sing N N 90  
EDO O2    HO2   sing N N 91  
FLF C1    C2    doub Y N 92  
FLF C1    C6    sing Y N 93  
FLF C1    C7    sing N N 94  
FLF O1    C7    doub N N 95  
FLF C2    C3    sing Y N 96  
FLF C2    H2    sing N N 97  
FLF C3    C4    doub Y N 98  
FLF C3    H3    sing N N 99  
FLF O2    C7    sing N N 100 
FLF O2    HO2   sing N N 101 
FLF C4    C5    sing Y N 102 
FLF C4    H4    sing N N 103 
FLF C5    C6    doub Y N 104 
FLF C5    H5    sing N N 105 
FLF C6    N     sing N N 106 
FLF N     "C1'" sing N N 107 
FLF N     HN1   sing N N 108 
FLF "C1'" "C2'" doub Y N 109 
FLF "C1'" "C6'" sing Y N 110 
FLF "C2'" "C3'" sing Y N 111 
FLF "C2'" "H2'" sing N N 112 
FLF "C3'" "C4'" doub Y N 113 
FLF "C3'" "C7'" sing N N 114 
FLF "C4'" "C5'" sing Y N 115 
FLF "C4'" "H4'" sing N N 116 
FLF "C5'" "C6'" doub Y N 117 
FLF "C5'" "H5'" sing N N 118 
FLF "C6'" "H6'" sing N N 119 
FLF "C7'" F1    sing N N 120 
FLF "C7'" F2    sing N N 121 
FLF "C7'" F3    sing N N 122 
GLN N     CA    sing N N 123 
GLN N     H     sing N N 124 
GLN N     H2    sing N N 125 
GLN CA    C     sing N N 126 
GLN CA    CB    sing N N 127 
GLN CA    HA    sing N N 128 
GLN C     O     doub N N 129 
GLN C     OXT   sing N N 130 
GLN CB    CG    sing N N 131 
GLN CB    HB2   sing N N 132 
GLN CB    HB3   sing N N 133 
GLN CG    CD    sing N N 134 
GLN CG    HG2   sing N N 135 
GLN CG    HG3   sing N N 136 
GLN CD    OE1   doub N N 137 
GLN CD    NE2   sing N N 138 
GLN NE2   HE21  sing N N 139 
GLN NE2   HE22  sing N N 140 
GLN OXT   HXT   sing N N 141 
GLU N     CA    sing N N 142 
GLU N     H     sing N N 143 
GLU N     H2    sing N N 144 
GLU CA    C     sing N N 145 
GLU CA    CB    sing N N 146 
GLU CA    HA    sing N N 147 
GLU C     O     doub N N 148 
GLU C     OXT   sing N N 149 
GLU CB    CG    sing N N 150 
GLU CB    HB2   sing N N 151 
GLU CB    HB3   sing N N 152 
GLU CG    CD    sing N N 153 
GLU CG    HG2   sing N N 154 
GLU CG    HG3   sing N N 155 
GLU CD    OE1   doub N N 156 
GLU CD    OE2   sing N N 157 
GLU OE2   HE2   sing N N 158 
GLU OXT   HXT   sing N N 159 
GLY N     CA    sing N N 160 
GLY N     H     sing N N 161 
GLY N     H2    sing N N 162 
GLY CA    C     sing N N 163 
GLY CA    HA2   sing N N 164 
GLY CA    HA3   sing N N 165 
GLY C     O     doub N N 166 
GLY C     OXT   sing N N 167 
GLY OXT   HXT   sing N N 168 
HEM CHA   C1A   sing N N 169 
HEM CHA   C4D   doub N N 170 
HEM CHA   HHA   sing N N 171 
HEM CHB   C4A   sing N N 172 
HEM CHB   C1B   doub N N 173 
HEM CHB   HHB   sing N N 174 
HEM CHC   C4B   sing N N 175 
HEM CHC   C1C   doub N N 176 
HEM CHC   HHC   sing N N 177 
HEM CHD   C4C   doub N N 178 
HEM CHD   C1D   sing N N 179 
HEM CHD   HHD   sing N N 180 
HEM C1A   C2A   doub Y N 181 
HEM C1A   NA    sing Y N 182 
HEM C2A   C3A   sing Y N 183 
HEM C2A   CAA   sing N N 184 
HEM C3A   C4A   doub Y N 185 
HEM C3A   CMA   sing N N 186 
HEM C4A   NA    sing Y N 187 
HEM CMA   HMA   sing N N 188 
HEM CMA   HMAA  sing N N 189 
HEM CMA   HMAB  sing N N 190 
HEM CAA   CBA   sing N N 191 
HEM CAA   HAA   sing N N 192 
HEM CAA   HAAA  sing N N 193 
HEM CBA   CGA   sing N N 194 
HEM CBA   HBA   sing N N 195 
HEM CBA   HBAA  sing N N 196 
HEM CGA   O1A   doub N N 197 
HEM CGA   O2A   sing N N 198 
HEM C1B   C2B   sing N N 199 
HEM C1B   NB    sing N N 200 
HEM C2B   C3B   doub N N 201 
HEM C2B   CMB   sing N N 202 
HEM C3B   C4B   sing N N 203 
HEM C3B   CAB   sing N N 204 
HEM C4B   NB    doub N N 205 
HEM CMB   HMB   sing N N 206 
HEM CMB   HMBA  sing N N 207 
HEM CMB   HMBB  sing N N 208 
HEM CAB   CBB   doub N N 209 
HEM CAB   HAB   sing N N 210 
HEM CBB   HBB   sing N N 211 
HEM CBB   HBBA  sing N N 212 
HEM C1C   C2C   sing Y N 213 
HEM C1C   NC    sing Y N 214 
HEM C2C   C3C   doub Y N 215 
HEM C2C   CMC   sing N N 216 
HEM C3C   C4C   sing Y N 217 
HEM C3C   CAC   sing N N 218 
HEM C4C   NC    sing Y N 219 
HEM CMC   HMC   sing N N 220 
HEM CMC   HMCA  sing N N 221 
HEM CMC   HMCB  sing N N 222 
HEM CAC   CBC   doub N N 223 
HEM CAC   HAC   sing N N 224 
HEM CBC   HBC   sing N N 225 
HEM CBC   HBCA  sing N N 226 
HEM C1D   C2D   sing N N 227 
HEM C1D   ND    doub N N 228 
HEM C2D   C3D   doub N N 229 
HEM C2D   CMD   sing N N 230 
HEM C3D   C4D   sing N N 231 
HEM C3D   CAD   sing N N 232 
HEM C4D   ND    sing N N 233 
HEM CMD   HMD   sing N N 234 
HEM CMD   HMDA  sing N N 235 
HEM CMD   HMDB  sing N N 236 
HEM CAD   CBD   sing N N 237 
HEM CAD   HAD   sing N N 238 
HEM CAD   HADA  sing N N 239 
HEM CBD   CGD   sing N N 240 
HEM CBD   HBD   sing N N 241 
HEM CBD   HBDA  sing N N 242 
HEM CGD   O1D   doub N N 243 
HEM CGD   O2D   sing N N 244 
HEM O2A   H2A   sing N N 245 
HEM O2D   H2D   sing N N 246 
HEM FE    NA    sing N N 247 
HEM FE    NB    sing N N 248 
HEM FE    NC    sing N N 249 
HEM FE    ND    sing N N 250 
HIS N     CA    sing N N 251 
HIS N     H     sing N N 252 
HIS N     H2    sing N N 253 
HIS CA    C     sing N N 254 
HIS CA    CB    sing N N 255 
HIS CA    HA    sing N N 256 
HIS C     O     doub N N 257 
HIS C     OXT   sing N N 258 
HIS CB    CG    sing N N 259 
HIS CB    HB2   sing N N 260 
HIS CB    HB3   sing N N 261 
HIS CG    ND1   sing Y N 262 
HIS CG    CD2   doub Y N 263 
HIS ND1   CE1   doub Y N 264 
HIS ND1   HD1   sing N N 265 
HIS CD2   NE2   sing Y N 266 
HIS CD2   HD2   sing N N 267 
HIS CE1   NE2   sing Y N 268 
HIS CE1   HE1   sing N N 269 
HIS NE2   HE2   sing N N 270 
HIS OXT   HXT   sing N N 271 
HOH O     H1    sing N N 272 
HOH O     H2    sing N N 273 
ILE N     CA    sing N N 274 
ILE N     H     sing N N 275 
ILE N     H2    sing N N 276 
ILE CA    C     sing N N 277 
ILE CA    CB    sing N N 278 
ILE CA    HA    sing N N 279 
ILE C     O     doub N N 280 
ILE C     OXT   sing N N 281 
ILE CB    CG1   sing N N 282 
ILE CB    CG2   sing N N 283 
ILE CB    HB    sing N N 284 
ILE CG1   CD1   sing N N 285 
ILE CG1   HG12  sing N N 286 
ILE CG1   HG13  sing N N 287 
ILE CG2   HG21  sing N N 288 
ILE CG2   HG22  sing N N 289 
ILE CG2   HG23  sing N N 290 
ILE CD1   HD11  sing N N 291 
ILE CD1   HD12  sing N N 292 
ILE CD1   HD13  sing N N 293 
ILE OXT   HXT   sing N N 294 
LEU N     CA    sing N N 295 
LEU N     H     sing N N 296 
LEU N     H2    sing N N 297 
LEU CA    C     sing N N 298 
LEU CA    CB    sing N N 299 
LEU CA    HA    sing N N 300 
LEU C     O     doub N N 301 
LEU C     OXT   sing N N 302 
LEU CB    CG    sing N N 303 
LEU CB    HB2   sing N N 304 
LEU CB    HB3   sing N N 305 
LEU CG    CD1   sing N N 306 
LEU CG    CD2   sing N N 307 
LEU CG    HG    sing N N 308 
LEU CD1   HD11  sing N N 309 
LEU CD1   HD12  sing N N 310 
LEU CD1   HD13  sing N N 311 
LEU CD2   HD21  sing N N 312 
LEU CD2   HD22  sing N N 313 
LEU CD2   HD23  sing N N 314 
LEU OXT   HXT   sing N N 315 
LYS N     CA    sing N N 316 
LYS N     H     sing N N 317 
LYS N     H2    sing N N 318 
LYS CA    C     sing N N 319 
LYS CA    CB    sing N N 320 
LYS CA    HA    sing N N 321 
LYS C     O     doub N N 322 
LYS C     OXT   sing N N 323 
LYS CB    CG    sing N N 324 
LYS CB    HB2   sing N N 325 
LYS CB    HB3   sing N N 326 
LYS CG    CD    sing N N 327 
LYS CG    HG2   sing N N 328 
LYS CG    HG3   sing N N 329 
LYS CD    CE    sing N N 330 
LYS CD    HD2   sing N N 331 
LYS CD    HD3   sing N N 332 
LYS CE    NZ    sing N N 333 
LYS CE    HE2   sing N N 334 
LYS CE    HE3   sing N N 335 
LYS NZ    HZ1   sing N N 336 
LYS NZ    HZ2   sing N N 337 
LYS NZ    HZ3   sing N N 338 
LYS OXT   HXT   sing N N 339 
MET N     CA    sing N N 340 
MET N     H     sing N N 341 
MET N     H2    sing N N 342 
MET CA    C     sing N N 343 
MET CA    CB    sing N N 344 
MET CA    HA    sing N N 345 
MET C     O     doub N N 346 
MET C     OXT   sing N N 347 
MET CB    CG    sing N N 348 
MET CB    HB2   sing N N 349 
MET CB    HB3   sing N N 350 
MET CG    SD    sing N N 351 
MET CG    HG2   sing N N 352 
MET CG    HG3   sing N N 353 
MET SD    CE    sing N N 354 
MET CE    HE1   sing N N 355 
MET CE    HE2   sing N N 356 
MET CE    HE3   sing N N 357 
MET OXT   HXT   sing N N 358 
PHE N     CA    sing N N 359 
PHE N     H     sing N N 360 
PHE N     H2    sing N N 361 
PHE CA    C     sing N N 362 
PHE CA    CB    sing N N 363 
PHE CA    HA    sing N N 364 
PHE C     O     doub N N 365 
PHE C     OXT   sing N N 366 
PHE CB    CG    sing N N 367 
PHE CB    HB2   sing N N 368 
PHE CB    HB3   sing N N 369 
PHE CG    CD1   doub Y N 370 
PHE CG    CD2   sing Y N 371 
PHE CD1   CE1   sing Y N 372 
PHE CD1   HD1   sing N N 373 
PHE CD2   CE2   doub Y N 374 
PHE CD2   HD2   sing N N 375 
PHE CE1   CZ    doub Y N 376 
PHE CE1   HE1   sing N N 377 
PHE CE2   CZ    sing Y N 378 
PHE CE2   HE2   sing N N 379 
PHE CZ    HZ    sing N N 380 
PHE OXT   HXT   sing N N 381 
PRO N     CA    sing N N 382 
PRO N     CD    sing N N 383 
PRO N     H     sing N N 384 
PRO CA    C     sing N N 385 
PRO CA    CB    sing N N 386 
PRO CA    HA    sing N N 387 
PRO C     O     doub N N 388 
PRO C     OXT   sing N N 389 
PRO CB    CG    sing N N 390 
PRO CB    HB2   sing N N 391 
PRO CB    HB3   sing N N 392 
PRO CG    CD    sing N N 393 
PRO CG    HG2   sing N N 394 
PRO CG    HG3   sing N N 395 
PRO CD    HD2   sing N N 396 
PRO CD    HD3   sing N N 397 
PRO OXT   HXT   sing N N 398 
SER N     CA    sing N N 399 
SER N     H     sing N N 400 
SER N     H2    sing N N 401 
SER CA    C     sing N N 402 
SER CA    CB    sing N N 403 
SER CA    HA    sing N N 404 
SER C     O     doub N N 405 
SER C     OXT   sing N N 406 
SER CB    OG    sing N N 407 
SER CB    HB2   sing N N 408 
SER CB    HB3   sing N N 409 
SER OG    HG    sing N N 410 
SER OXT   HXT   sing N N 411 
THR N     CA    sing N N 412 
THR N     H     sing N N 413 
THR N     H2    sing N N 414 
THR CA    C     sing N N 415 
THR CA    CB    sing N N 416 
THR CA    HA    sing N N 417 
THR C     O     doub N N 418 
THR C     OXT   sing N N 419 
THR CB    OG1   sing N N 420 
THR CB    CG2   sing N N 421 
THR CB    HB    sing N N 422 
THR OG1   HG1   sing N N 423 
THR CG2   HG21  sing N N 424 
THR CG2   HG22  sing N N 425 
THR CG2   HG23  sing N N 426 
THR OXT   HXT   sing N N 427 
TRP N     CA    sing N N 428 
TRP N     H     sing N N 429 
TRP N     H2    sing N N 430 
TRP CA    C     sing N N 431 
TRP CA    CB    sing N N 432 
TRP CA    HA    sing N N 433 
TRP C     O     doub N N 434 
TRP C     OXT   sing N N 435 
TRP CB    CG    sing N N 436 
TRP CB    HB2   sing N N 437 
TRP CB    HB3   sing N N 438 
TRP CG    CD1   doub Y N 439 
TRP CG    CD2   sing Y N 440 
TRP CD1   NE1   sing Y N 441 
TRP CD1   HD1   sing N N 442 
TRP CD2   CE2   doub Y N 443 
TRP CD2   CE3   sing Y N 444 
TRP NE1   CE2   sing Y N 445 
TRP NE1   HE1   sing N N 446 
TRP CE2   CZ2   sing Y N 447 
TRP CE3   CZ3   doub Y N 448 
TRP CE3   HE3   sing N N 449 
TRP CZ2   CH2   doub Y N 450 
TRP CZ2   HZ2   sing N N 451 
TRP CZ3   CH2   sing Y N 452 
TRP CZ3   HZ3   sing N N 453 
TRP CH2   HH2   sing N N 454 
TRP OXT   HXT   sing N N 455 
TRS C     C1    sing N N 456 
TRS C     C2    sing N N 457 
TRS C     C3    sing N N 458 
TRS C     N     sing N N 459 
TRS C1    O1    sing N N 460 
TRS C1    H11   sing N N 461 
TRS C1    H12   sing N N 462 
TRS C2    O2    sing N N 463 
TRS C2    H21   sing N N 464 
TRS C2    H22   sing N N 465 
TRS C3    O3    sing N N 466 
TRS C3    H31   sing N N 467 
TRS C3    H32   sing N N 468 
TRS N     HN1   sing N N 469 
TRS N     HN2   sing N N 470 
TRS N     HN3   sing N N 471 
TRS O1    HO1   sing N N 472 
TRS O2    HO2   sing N N 473 
TRS O3    HO3   sing N N 474 
TYR N     CA    sing N N 475 
TYR N     H     sing N N 476 
TYR N     H2    sing N N 477 
TYR CA    C     sing N N 478 
TYR CA    CB    sing N N 479 
TYR CA    HA    sing N N 480 
TYR C     O     doub N N 481 
TYR C     OXT   sing N N 482 
TYR CB    CG    sing N N 483 
TYR CB    HB2   sing N N 484 
TYR CB    HB3   sing N N 485 
TYR CG    CD1   doub Y N 486 
TYR CG    CD2   sing Y N 487 
TYR CD1   CE1   sing Y N 488 
TYR CD1   HD1   sing N N 489 
TYR CD2   CE2   doub Y N 490 
TYR CD2   HD2   sing N N 491 
TYR CE1   CZ    doub Y N 492 
TYR CE1   HE1   sing N N 493 
TYR CE2   CZ    sing Y N 494 
TYR CE2   HE2   sing N N 495 
TYR CZ    OH    sing N N 496 
TYR OH    HH    sing N N 497 
TYR OXT   HXT   sing N N 498 
VAL N     CA    sing N N 499 
VAL N     H     sing N N 500 
VAL N     H2    sing N N 501 
VAL CA    C     sing N N 502 
VAL CA    CB    sing N N 503 
VAL CA    HA    sing N N 504 
VAL C     O     doub N N 505 
VAL C     OXT   sing N N 506 
VAL CB    CG1   sing N N 507 
VAL CB    CG2   sing N N 508 
VAL CB    HB    sing N N 509 
VAL CG1   HG11  sing N N 510 
VAL CG1   HG12  sing N N 511 
VAL CG1   HG13  sing N N 512 
VAL CG2   HG21  sing N N 513 
VAL CG2   HG22  sing N N 514 
VAL CG2   HG23  sing N N 515 
VAL OXT   HXT   sing N N 516 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Japan Society for the Promotion of Science (JSPS)' Japan 22K05441 1 
'Japan Society for the Promotion of Science (JSPS)' Japan 25292062 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   2ZBX 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9JI1 
_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]   0.018870 
_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]   0.018664 
_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]   0.007189 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F  ? ? 4.90428  4.07044 ? ? 12.99538 1.63651  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
FE ? ? 20.90327 4.99816 ? ? 2.55100  38.46870 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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     . THR A 1 4   ? -10.22700 -28.45800 32.41200  1.000 52.16152  ? 4    THR A N     1 
ATOM   2    C  CA    . THR A 1 4   ? -9.19500  -27.43400 32.27500  1.000 51.72725  ? 4    THR A CA    1 
ATOM   3    C  C     . THR A 1 4   ? -7.87700  -28.04900 31.81500  1.000 50.59554  ? 4    THR A C     1 
ATOM   4    O  O     . THR A 1 4   ? -7.75300  -29.27000 31.71800  1.000 50.00863  ? 4    THR A O     1 
ATOM   5    C  CB    . THR A 1 4   ? -8.95900  -26.66500 33.59600  1.000 51.54039  ? 4    THR A CB    1 
ATOM   6    O  OG1   . THR A 1 4   ? -8.42600  -27.55400 34.58400  1.000 52.68526  ? 4    THR A OG1   1 
ATOM   7    C  CG2   . THR A 1 4   ? -10.26400 -26.04800 34.10600  1.000 48.12156  ? 4    THR A CG2   1 
ATOM   8    N  N     . ALA A 1 5   ? -6.89300  -27.19200 31.54400  1.000 48.05050  ? 5    ALA A N     1 
ATOM   9    C  CA    . ALA A 1 5   ? -5.62200  -27.63400 30.98300  1.000 45.40018  ? 5    ALA A CA    1 
ATOM   10   C  C     . ALA A 1 5   ? -4.73700  -28.24200 32.06600  1.000 44.17635  ? 5    ALA A C     1 
ATOM   11   O  O     . ALA A 1 5   ? -4.46700  -27.60700 33.09100  1.000 42.95515  ? 5    ALA A O     1 
ATOM   12   C  CB    . ALA A 1 5   ? -4.90700  -26.45800 30.31600  1.000 44.03949  ? 5    ALA A CB    1 
ATOM   13   N  N     . THR A 1 6   ? -4.27100  -29.47000 31.82700  1.000 46.12922  ? 6    THR A N     1 
ATOM   14   C  CA    . THR A 1 6   ? -3.45800  -30.19900 32.79200  1.000 49.08483  ? 6    THR A CA    1 
ATOM   15   C  C     . THR A 1 6   ? -2.05700  -30.53300 32.29000  1.000 50.54553  ? 6    THR A C     1 
ATOM   16   O  O     . THR A 1 6   ? -1.26800  -31.11700 33.04100  1.000 53.39588  ? 6    THR A O     1 
ATOM   17   C  CB    . THR A 1 6   ? -4.17600  -31.48700 33.22300  1.000 50.70871  ? 6    THR A CB    1 
ATOM   18   O  OG1   . THR A 1 6   ? -4.54100  -32.24400 32.06000  1.000 51.92465  ? 6    THR A OG1   1 
ATOM   19   C  CG2   . THR A 1 6   ? -5.42800  -31.15600 34.02400  1.000 50.35341  ? 6    THR A CG2   1 
ATOM   20   N  N     . THR A 1 7   ? -1.72500  -30.17800 31.06400  1.000 46.28186  ? 7    THR A N     1 
ATOM   21   C  CA    . THR A 1 7   ? -0.46100  -30.51200 30.42900  1.000 41.85765  ? 7    THR A CA    1 
ATOM   22   C  C     . THR A 1 7   ? 0.45500   -29.29600 30.42400  1.000 36.93601  ? 7    THR A C     1 
ATOM   23   O  O     . THR A 1 7   ? 0.01100   -28.17000 30.66400  1.000 35.73323  ? 7    THR A O     1 
ATOM   24   C  CB    . THR A 1 7   ? -0.73900  -30.97600 29.00000  1.000 44.12371  ? 7    THR A CB    1 
ATOM   25   O  OG1   . THR A 1 7   ? -1.56200  -30.00500 28.34500  1.000 43.73419  ? 7    THR A OG1   1 
ATOM   26   C  CG2   . THR A 1 7   ? -1.45800  -32.32400 29.01500  1.000 44.41322  ? 7    THR A CG2   1 
ATOM   27   N  N     . PRO A 1 8   ? 1.75800   -29.48200 30.16500  1.000 34.12251  ? 8    PRO A N     1 
ATOM   28   C  CA    . PRO A 1 8   ? 2.66800   -28.32700 30.14100  1.000 31.66695  ? 8    PRO A CA    1 
ATOM   29   C  C     . PRO A 1 8   ? 2.23600   -27.29200 29.11300  1.000 30.77211  ? 8    PRO A C     1 
ATOM   30   O  O     . PRO A 1 8   ? 1.63600   -27.61700 28.08700  1.000 31.21953  ? 8    PRO A O     1 
ATOM   31   C  CB    . PRO A 1 8   ? 4.02200   -28.93800 29.76700  1.000 33.30662  ? 8    PRO A CB    1 
ATOM   32   C  CG    . PRO A 1 8   ? 3.91900   -30.37200 30.14700  1.000 34.49098  ? 8    PRO A CG    1 
ATOM   33   C  CD    . PRO A 1 8   ? 2.48000   -30.75800 29.99100  1.000 33.34874  ? 8    PRO A CD    1 
ATOM   34   N  N     . GLN A 1 9   ? 2.57000   -26.03400 29.40000  1.000 29.98254  ? 9    GLN A N     1 
ATOM   35   C  CA    . GLN A 1 9   ? 2.06600   -24.88900 28.65300  1.000 29.91411  ? 9    GLN A CA    1 
ATOM   36   C  C     . GLN A 1 9   ? 3.09900   -24.23700 27.74200  1.000 28.67712  ? 9    GLN A C     1 
ATOM   37   O  O     . GLN A 1 9   ? 2.78500   -23.22000 27.11200  1.000 31.23006  ? 9    GLN A O     1 
ATOM   38   C  CB    . GLN A 1 9   ? 1.49200   -23.84700 29.62000  1.000 32.15649  ? 9    GLN A CB    1 
ATOM   39   C  CG    . GLN A 1 9   ? 0.31800   -24.36300 30.43300  1.000 39.21786  ? 9    GLN A CG    1 
ATOM   40   C  CD    . GLN A 1 9   ? -0.87700  -24.71100 29.56500  1.000 43.89474  ? 9    GLN A CD    1 
ATOM   41   O  OE1   . GLN A 1 9   ? -1.58100  -23.82600 29.07800  1.000 47.71362  ? 9    GLN A OE1   1 
ATOM   42   N  NE2   . GLN A 1 9   ? -1.09900  -26.00300 29.34900  1.000 42.88146  ? 9    GLN A NE2   1 
ATOM   43   N  N     . THR A 1 10  ? 4.31600   -24.77900 27.66700  1.000 27.94546  ? 10   THR A N     1 
ATOM   44   C  CA    . THR A 1 10  ? 5.34000   -24.26800 26.75700  1.000 27.21379  ? 10   THR A CA    1 
ATOM   45   C  C     . THR A 1 10  ? 4.78700   -24.16600 25.33900  1.000 25.59254  ? 10   THR A C     1 
ATOM   46   O  O     . THR A 1 10  ? 4.04300   -25.03600 24.88500  1.000 24.83982  ? 10   THR A O     1 
ATOM   47   C  CB    . THR A 1 10  ? 6.53400   -25.23600 26.76600  1.000 27.81386  ? 10   THR A CB    1 
ATOM   48   O  OG1   . THR A 1 10  ? 7.25800   -25.11700 28.00100  1.000 30.59051  ? 10   THR A OG1   1 
ATOM   49   C  CG2   . THR A 1 10  ? 7.48600   -24.98200 25.59200  1.000 27.73227  ? 10   THR A CG2   1 
ATOM   50   N  N     . THR A 1 11  ? 5.14600   -23.08800 24.63900  1.000 25.69782  ? 11   THR A N     1 
ATOM   51   C  CA    . THR A 1 11  ? 4.78000   -22.91600 23.24200  1.000 26.21893  ? 11   THR A CA    1 
ATOM   52   C  C     . THR A 1 11  ? 6.02300   -22.57900 22.43200  1.000 27.07430  ? 11   THR A C     1 
ATOM   53   O  O     . THR A 1 11  ? 7.00800   -22.06800 22.96900  1.000 30.06939  ? 11   THR A O     1 
ATOM   54   C  CB    . THR A 1 11  ? 3.74800   -21.79400 23.07600  1.000 27.41908  ? 11   THR A CB    1 
ATOM   55   O  OG1   . THR A 1 11  ? 3.43300   -21.63100 21.68700  1.000 28.25865  ? 11   THR A OG1   1 
ATOM   56   C  CG2   . THR A 1 11  ? 4.28400   -20.47000 23.63600  1.000 30.31153  ? 11   THR A CG2   1 
ATOM   57   N  N     . ASP A 1 12  ? 5.98000   -22.88600 21.13500  1.000 26.62688  ? 12   ASP A N     1 
ATOM   58   C  CA    . ASP A 1 12  ? 7.00700   -22.43800 20.20300  1.000 28.36393  ? 12   ASP A CA    1 
ATOM   59   C  C     . ASP A 1 12  ? 6.59100   -21.18600 19.43600  1.000 29.81410  ? 12   ASP A C     1 
ATOM   60   O  O     . ASP A 1 12  ? 7.28700   -20.78100 18.49900  1.000 31.59589  ? 12   ASP A O     1 
ATOM   61   C  CB    . ASP A 1 12  ? 7.42600   -23.56600 19.25000  1.000 29.41142  ? 12   ASP A CB    1 
ATOM   62   C  CG    . ASP A 1 12  ? 6.30800   -24.00000 18.31200  1.000 26.43475  ? 12   ASP A CG    1 
ATOM   63   O  OD1   . ASP A 1 12  ? 5.15200   -23.57500 18.51700  1.000 28.48763  ? 12   ASP A OD1   1 
ATOM   64   O  OD2   . ASP A 1 12  ? 6.59000   -24.76900 17.36100  1.000 27.51119  ? 12   ASP A OD2   1 
ATOM   65   N  N     . ALA A 1 13  ? 5.47000   -20.56800 19.81300  1.000 28.85346  ? 13   ALA A N     1 
ATOM   66   C  CA    . ALA A 1 13  ? 5.00000   -19.32900 19.19200  1.000 29.36405  ? 13   ALA A CA    1 
ATOM   67   C  C     . ALA A 1 13  ? 4.52600   -18.40000 20.29700  1.000 30.22994  ? 13   ALA A C     1 
ATOM   68   O  O     . ALA A 1 13  ? 3.32000   -18.22600 20.51600  1.000 31.30902  ? 13   ALA A O     1 
ATOM   69   C  CB    . ALA A 1 13  ? 3.88300   -19.60500 18.18400  1.000 29.09823  ? 13   ALA A CB    1 
ATOM   70   N  N     . PRO A 1 14  ? 5.45600   -17.78100 21.02100  1.000 29.99570  ? 14   PRO A N     1 
ATOM   71   C  CA    . PRO A 1 14  ? 5.07600   -16.98800 22.19500  1.000 30.23520  ? 14   PRO A CA    1 
ATOM   72   C  C     . PRO A 1 14  ? 4.23000   -15.77500 21.83700  1.000 30.05360  ? 14   PRO A C     1 
ATOM   73   O  O     . PRO A 1 14  ? 4.27500   -15.24400 20.72400  1.000 29.23772  ? 14   PRO A O     1 
ATOM   74   C  CB    . PRO A 1 14  ? 6.42500   -16.55800 22.78300  1.000 30.76948  ? 14   PRO A CB    1 
ATOM   75   C  CG    . PRO A 1 14  ? 7.38600   -16.66700 21.64900  1.000 32.00121  ? 14   PRO A CG    1 
ATOM   76   C  CD    . PRO A 1 14  ? 6.91300   -17.82900 20.83500  1.000 30.30363  ? 14   PRO A CD    1 
ATOM   77   N  N     . ALA A 1 15  ? 3.44700   -15.33600 22.82300  1.000 30.19046  ? 15   ALA A N     1 
ATOM   78   C  CA    . ALA A 1 15  ? 2.62700   -14.14800 22.65100  1.000 28.17706  ? 15   ALA A CA    1 
ATOM   79   C  C     . ALA A 1 15  ? 3.51200   -12.93900 22.39000  1.000 25.57149  ? 15   ALA A C     1 
ATOM   80   O  O     . ALA A 1 15  ? 4.55000   -12.75700 23.03200  1.000 28.11653  ? 15   ALA A O     1 
ATOM   81   C  CB    . ALA A 1 15  ? 1.78000   -13.90900 23.89900  1.000 28.90610  ? 15   ALA A CB    1 
ATOM   82   N  N     . PHE A 1 16  ? 3.09200   -12.11000 21.43600  1.000 24.34239  ? 16   PHE A N     1 
ATOM   83   C  CA    . PHE A 1 16  ? 3.84500   -10.92700 21.05400  1.000 22.92643  ? 16   PHE A CA    1 
ATOM   84   C  C     . PHE A 1 16  ? 2.85300   -9.79000  20.85100  1.000 24.28712  ? 16   PHE A C     1 
ATOM   85   O  O     . PHE A 1 16  ? 1.76600   -10.01300 20.30300  1.000 25.31883  ? 16   PHE A O     1 
ATOM   86   C  CB    . PHE A 1 16  ? 4.61800   -11.17500 19.75000  1.000 24.84772  ? 16   PHE A CB    1 
ATOM   87   C  CG    . PHE A 1 16  ? 5.42100   -9.99600  19.29700  1.000 22.66324  ? 16   PHE A CG    1 
ATOM   88   C  CD1   . PHE A 1 16  ? 4.84800   -9.00300  18.50300  1.000 21.97106  ? 16   PHE A CD1   1 
ATOM   89   C  CD2   . PHE A 1 16  ? 6.74900   -9.86500  19.66800  1.000 22.38953  ? 16   PHE A CD2   1 
ATOM   90   C  CE1   . PHE A 1 16  ? 5.58500   -7.90400  18.09600  1.000 23.19489  ? 16   PHE A CE1   1 
ATOM   91   C  CE2   . PHE A 1 16  ? 7.48800   -8.76800  19.26900  1.000 23.31859  ? 16   PHE A CE2   1 
ATOM   92   C  CZ    . PHE A 1 16  ? 6.90700   -7.78900  18.48200  1.000 24.32134  ? 16   PHE A CZ    1 
ATOM   93   N  N     . PRO A 1 17  ? 3.20200   -8.55700  21.24600  1.000 25.00037  ? 17   PRO A N     1 
ATOM   94   C  CA    . PRO A 1 17  ? 4.46400   -8.11600  21.85300  1.000 25.23197  ? 17   PRO A CA    1 
ATOM   95   C  C     . PRO A 1 17  ? 4.54300   -8.40100  23.34000  1.000 25.30303  ? 17   PRO A C     1 
ATOM   96   O  O     . PRO A 1 17  ? 3.59500   -8.87900  23.95400  1.000 27.77438  ? 17   PRO A O     1 
ATOM   97   C  CB    . PRO A 1 17  ? 4.43000   -6.59600  21.63700  1.000 25.37673  ? 17   PRO A CB    1 
ATOM   98   C  CG    . PRO A 1 17  ? 2.97300   -6.26600  21.71800  1.000 26.30315  ? 17   PRO A CG    1 
ATOM   99   C  CD    . PRO A 1 17  ? 2.28900   -7.42100  21.01600  1.000 27.09799  ? 17   PRO A CD    1 
ATOM   100  N  N     . SER A 1 18  ? 5.69500   -8.10400  23.92900  1.000 27.14273  ? 18   SER A N     1 
ATOM   101  C  CA    . SER A 1 18  ? 5.89600   -8.14900  25.36600  1.000 26.81374  ? 18   SER A CA    1 
ATOM   102  C  C     . SER A 1 18  ? 6.04000   -6.72800  25.89400  1.000 27.51119  ? 18   SER A C     1 
ATOM   103  O  O     . SER A 1 18  ? 6.31500   -5.78700  25.14700  1.000 27.39276  ? 18   SER A O     1 
ATOM   104  C  CB    . SER A 1 18  ? 7.14800   -8.95900  25.72300  1.000 28.16917  ? 18   SER A CB    1 
ATOM   105  O  OG    . SER A 1 18  ? 7.05800   -10.29400 25.24600  1.000 33.02501  ? 18   SER A OG    1 
ATOM   106  N  N     . ASN A 1 19  ? 5.84700   -6.57300  27.19900  1.000 27.92177  ? 19   ASN A N     1 
ATOM   107  C  CA    . ASN A 1 19  ? 5.98400   -5.27400  27.84100  1.000 26.89796  ? 19   ASN A CA    1 
ATOM   108  C  C     . ASN A 1 19  ? 7.34700   -5.16600  28.50900  1.000 26.70057  ? 19   ASN A C     1 
ATOM   109  O  O     . ASN A 1 19  ? 7.82900   -6.12400  29.11900  1.000 28.69291  ? 19   ASN A O     1 
ATOM   110  C  CB    . ASN A 1 19  ? 4.89600   -5.05600  28.89200  1.000 28.10074  ? 19   ASN A CB    1 
ATOM   111  C  CG    . ASN A 1 19  ? 3.50100   -5.19400  28.32600  1.000 30.46155  ? 19   ASN A CG    1 
ATOM   112  O  OD1   . ASN A 1 19  ? 3.25900   -4.90500  27.15200  1.000 29.75620  ? 19   ASN A OD1   1 
ATOM   113  N  ND2   . ASN A 1 19  ? 2.56900   -5.63200  29.16400  1.000 34.03566  ? 19   ASN A ND2   1 
ATOM   114  N  N     . ARG A 1 20  ? 7.95800   -3.99100  28.40200  1.000 25.03721  ? 20   ARG A N     1 
ATOM   115  C  CA    . ARG A 1 20  ? 9.18300   -3.72400  29.14300  1.000 26.72162  ? 20   ARG A CA    1 
ATOM   116  C  C     . ARG A 1 20  ? 8.89800   -3.60900  30.63000  1.000 30.21941  ? 20   ARG A C     1 
ATOM   117  O  O     . ARG A 1 20  ? 7.89100   -3.03100  31.04700  1.000 32.66181  ? 20   ARG A O     1 
ATOM   118  C  CB    . ARG A 1 20  ? 9.81000   -2.41800  28.68100  1.000 25.83204  ? 20   ARG A CB    1 
ATOM   119  C  CG    . ARG A 1 20  ? 10.47900  -2.56400  27.37600  1.000 24.30555  ? 20   ARG A CG    1 
ATOM   120  C  CD    . ARG A 1 20  ? 11.19800  -1.30800  26.95200  1.000 22.81326  ? 20   ARG A CD    1 
ATOM   121  N  NE    . ARG A 1 20  ? 11.49200  -1.42400  25.53200  1.000 21.78419  ? 20   ARG A NE    1 
ATOM   122  C  CZ    . ARG A 1 20  ? 12.05700  -0.47900  24.79900  1.000 18.97333  ? 20   ARG A CZ    1 
ATOM   123  N  NH1   . ARG A 1 20  ? 12.50600  0.64000   25.34300  1.000 19.83922  ? 20   ARG A NH1   1 
ATOM   124  N  NH2   . ARG A 1 20  ? 12.16100  -0.65700  23.48600  1.000 20.08136  ? 20   ARG A NH2   1 
ATOM   125  N  N     . SER A 1 21  ? 9.79900   -4.17200  31.42900  1.000 30.17204  ? 21   SER A N     1 
ATOM   126  C  CA    . SER A 1 21  ? 9.81300   -3.93000  32.86100  1.000 32.24597  ? 21   SER A CA    1 
ATOM   127  C  C     . SER A 1 21  ? 10.88300  -2.93000  33.26300  1.000 30.07992  ? 21   SER A C     1 
ATOM   128  O  O     . SER A 1 21  ? 10.77000  -2.31600  34.32900  1.000 33.88827  ? 21   SER A O     1 
ATOM   129  C  CB    . SER A 1 21  ? 10.03100  -5.24200  33.61800  1.000 34.83576  ? 21   SER A CB    1 
ATOM   130  O  OG    . SER A 1 21  ? 11.15300  -5.93100  33.10000  1.000 37.57293  ? 21   SER A OG    1 
ATOM   131  N  N     . CYS A 1 22  ? 11.90800  -2.75200  32.43100  1.000 26.50844  ? 22   CYS A N     1 
ATOM   132  C  CA    . CYS A 1 22  ? 12.94000  -1.75400  32.63500  1.000 27.12430  ? 22   CYS A CA    1 
ATOM   133  C  C     . CYS A 1 22  ? 12.98500  -0.92600  31.35700  1.000 26.53476  ? 22   CYS A C     1 
ATOM   134  O  O     . CYS A 1 22  ? 12.97900  -1.50000  30.25400  1.000 26.44528  ? 22   CYS A O     1 
ATOM   135  C  CB    . CYS A 1 22  ? 14.29900  -2.41600  32.87400  1.000 29.31404  ? 22   CYS A CB    1 
ATOM   136  S  SG    . CYS A 1 22  ? 15.70500  -1.27800  32.78300  1.000 31.19585  ? 22   CYS A SG    1 
ATOM   137  N  N     . PRO A 1 23  ? 13.02300  0.40600   31.45200  1.000 27.56646  ? 23   PRO A N     1 
ATOM   138  C  CA    . PRO A 1 23  ? 12.88100  1.23000   30.24000  1.000 28.53237  ? 23   PRO A CA    1 
ATOM   139  C  C     . PRO A 1 23  ? 13.94800  0.98700   29.18900  1.000 26.70320  ? 23   PRO A C     1 
ATOM   140  O  O     . PRO A 1 23  ? 13.69100  1.23400   28.00400  1.000 27.95598  ? 23   PRO A O     1 
ATOM   141  C  CB    . PRO A 1 23  ? 12.92000  2.67000   30.77700  1.000 30.34838  ? 23   PRO A CB    1 
ATOM   142  C  CG    . PRO A 1 23  ? 13.47700  2.56500   32.15000  1.000 32.47495  ? 23   PRO A CG    1 
ATOM   143  C  CD    . PRO A 1 23  ? 13.06200  1.22600   32.67500  1.000 31.19848  ? 23   PRO A CD    1 
ATOM   144  N  N     . TYR A 1 24  ? 15.12200  0.48300   29.56600  1.000 23.66336  ? 24   TYR A N     1 
ATOM   145  C  CA    . TYR A 1 24  ? 16.23400  0.36200   28.63000  1.000 23.94761  ? 24   TYR A CA    1 
ATOM   146  C  C     . TYR A 1 24  ? 16.73300  -1.07200  28.48500  1.000 24.01341  ? 24   TYR A C     1 
ATOM   147  O  O     . TYR A 1 24  ? 17.84800  -1.29000  27.99300  1.000 26.50844  ? 24   TYR A O     1 
ATOM   148  C  CB    . TYR A 1 24  ? 17.37300  1.32000   28.99100  1.000 24.14763  ? 24   TYR A CB    1 
ATOM   149  C  CG    . TYR A 1 24  ? 17.81600  1.19100   30.42400  1.000 24.75297  ? 24   TYR A CG    1 
ATOM   150  C  CD1   . TYR A 1 24  ? 18.74800  0.23100   30.78900  1.000 25.93995  ? 24   TYR A CD1   1 
ATOM   151  C  CD2   . TYR A 1 24  ? 17.29900  2.02500   31.41100  1.000 25.90574  ? 24   TYR A CD2   1 
ATOM   152  C  CE1   . TYR A 1 24  ? 19.15400  0.08900   32.10600  1.000 27.44803  ? 24   TYR A CE1   1 
ATOM   153  C  CE2   . TYR A 1 24  ? 17.70100  1.89200   32.74000  1.000 26.77426  ? 24   TYR A CE2   1 
ATOM   154  C  CZ    . TYR A 1 24  ? 18.62900  0.92300   33.07800  1.000 28.85346  ? 24   TYR A CZ    1 
ATOM   155  O  OH    . TYR A 1 24  ? 19.03600  0.78500   34.38900  1.000 33.54876  ? 24   TYR A OH    1 
ATOM   156  N  N     . GLN A 1 25  ? 15.93700  -2.06200  28.87300  1.000 23.92655  ? 25   GLN A N     1 
ATOM   157  C  CA    A GLN A 1 25  ? 16.34000  -3.42800  28.60700  0.510 25.80573  ? 25   GLN A CA    1 
ATOM   158  C  CA    B GLN A 1 25  ? 16.28500  -3.47500  28.74600  0.490 25.03458  ? 25   GLN A CA    1 
ATOM   159  C  C     . GLN A 1 25  ? 15.24300  -4.19700  27.89300  1.000 25.90311  ? 25   GLN A C     1 
ATOM   160  O  O     . GLN A 1 25  ? 14.06000  -3.84800  27.93300  1.000 26.11366  ? 25   GLN A O     1 
ATOM   161  C  CB    A GLN A 1 25  ? 16.92100  -4.17100  29.81800  0.510 28.28760  ? 25   GLN A CB    1 
ATOM   162  C  CB    B GLN A 1 25  ? 16.34200  -4.15000  30.13200  0.490 27.10062  ? 25   GLN A CB    1 
ATOM   163  C  CG    A GLN A 1 25  ? 18.44100  -3.99100  29.94600  0.510 27.43224  ? 25   GLN A CG    1 
ATOM   164  C  CG    B GLN A 1 25  ? 17.50000  -3.69000  31.01200  0.490 26.85322  ? 25   GLN A CG    1 
ATOM   165  C  CD    A GLN A 1 25  ? 19.21200  -4.31800  28.65700  0.510 26.81374  ? 25   GLN A CD    1 
ATOM   166  C  CD    B GLN A 1 25  ? 17.48100  -4.30400  32.41000  0.490 30.14572  ? 25   GLN A CD    1 
ATOM   167  O  OE1   A GLN A 1 25  ? 20.19000  -3.65000  28.32800  0.510 30.94582  ? 25   GLN A OE1   1 
ATOM   168  O  OE1   B GLN A 1 25  ? 16.51500  -4.95900  32.80900  0.490 32.67234  ? 25   GLN A OE1   1 
ATOM   169  N  NE2   A GLN A 1 25  ? 18.78700  -5.35900  27.94500  0.510 28.62712  ? 25   GLN A NE2   1 
ATOM   170  N  NE2   B GLN A 1 25  ? 18.55700  -4.09300  33.15700  0.490 30.26942  ? 25   GLN A NE2   1 
ATOM   171  N  N     . LEU A 1 26  ? 15.68400  -5.21300  27.15700  1.000 26.08471  ? 26   LEU A N     1 
ATOM   172  C  CA    . LEU A 1 26  ? 14.75800  -6.05800  26.42300  1.000 29.05612  ? 26   LEU A CA    1 
ATOM   173  C  C     . LEU A 1 26  ? 13.81400  -6.74600  27.40400  1.000 31.42482  ? 26   LEU A C     1 
ATOM   174  O  O     . LEU A 1 26  ? 14.24200  -7.16600  28.48600  1.000 32.47495  ? 26   LEU A O     1 
ATOM   175  C  CB    . LEU A 1 26  ? 15.52600  -7.14400  25.66500  1.000 31.08004  ? 26   LEU A CB    1 
ATOM   176  C  CG    . LEU A 1 26  ? 16.42300  -6.74500  24.49500  1.000 30.59577  ? 26   LEU A CG    1 
ATOM   177  C  CD1   . LEU A 1 26  ? 17.11900  -7.97400  23.91600  1.000 30.28784  ? 26   LEU A CD1   1 
ATOM   178  C  CD2   . LEU A 1 26  ? 15.61800  -6.04700  23.42100  1.000 31.42219  ? 26   LEU A CD2   1 
ATOM   179  N  N     . PRO A 1 27  ? 12.53000  -6.86400  27.07200  1.000 30.12466  ? 27   PRO A N     1 
ATOM   180  C  CA    . PRO A 1 27  ? 11.66700  -7.78600  27.81500  1.000 32.00384  ? 27   PRO A CA    1 
ATOM   181  C  C     . PRO A 1 27  ? 12.27300  -9.18400  27.79300  1.000 35.06473  ? 27   PRO A C     1 
ATOM   182  O  O     . PRO A 1 27  ? 12.91000  -9.58600  26.81600  1.000 33.75931  ? 27   PRO A O     1 
ATOM   183  C  CB    . PRO A 1 27  ? 10.35100  -7.73900  27.03200  1.000 32.73024  ? 27   PRO A CB    1 
ATOM   184  C  CG    . PRO A 1 27  ? 10.36700  -6.39400  26.34200  1.000 30.75106  ? 27   PRO A CG    1 
ATOM   185  C  CD    . PRO A 1 27  ? 11.80600  -6.13400  26.01500  1.000 30.00097  ? 27   PRO A CD    1 
ATOM   186  N  N     . ASP A 1 28  ? 12.08300  -9.91900  28.89600  1.000 39.78635  ? 28   ASP A N     1 
ATOM   187  C  CA    . ASP A 1 28  ? 12.69800  -11.23800 29.03500  1.000 43.51838  ? 28   ASP A CA    1 
ATOM   188  C  C     . ASP A 1 28  ? 12.45800  -12.11200 27.80700  1.000 40.74699  ? 28   ASP A C     1 
ATOM   189  O  O     . ASP A 1 28  ? 13.38800  -12.73200 27.27900  1.000 41.01018  ? 28   ASP A O     1 
ATOM   190  C  CB    . ASP A 1 28  ? 12.19500  -11.93300 30.30500  1.000 50.16917  ? 28   ASP A CB    1 
ATOM   191  C  CG    . ASP A 1 28  ? 12.77100  -11.32500 31.57600  1.000 56.96999  ? 28   ASP A CG    1 
ATOM   192  O  OD1   . ASP A 1 28  ? 13.85200  -10.70200 31.49600  1.000 58.77284  ? 28   ASP A OD1   1 
ATOM   193  O  OD2   . ASP A 1 28  ? 12.14000  -11.46100 32.65100  1.000 59.66242  ? 28   ASP A OD2   1 
ATOM   194  N  N     . GLY A 1 29  ? 11.21300  -12.15900 27.32800  1.000 38.89151  ? 29   GLY A N     1 
ATOM   195  C  CA    . GLY A 1 29  ? 10.91600  -12.93800 26.13700  1.000 36.34383  ? 29   GLY A CA    1 
ATOM   196  C  C     . GLY A 1 29  ? 11.67500  -12.48400 24.90300  1.000 34.27253  ? 29   GLY A C     1 
ATOM   197  O  O     . GLY A 1 29  ? 11.95900  -13.29300 24.01500  1.000 31.29059  ? 29   GLY A O     1 
ATOM   198  N  N     . TYR A 1 30  ? 12.01600  -11.19200 24.82300  1.000 30.00097  ? 30   TYR A N     1 
ATOM   199  C  CA    . TYR A 1 30  ? 12.72000  -10.69500 23.64100  1.000 29.67461  ? 30   TYR A CA    1 
ATOM   200  C  C     . TYR A 1 30  ? 14.17700  -11.13200 23.62200  1.000 32.16175  ? 30   TYR A C     1 
ATOM   201  O  O     . TYR A 1 30  ? 14.75100  -11.32000 22.54200  1.000 31.19321  ? 30   TYR A O     1 
ATOM   202  C  CB    . TYR A 1 30  ? 12.65300  -9.16800  23.55000  1.000 29.15350  ? 30   TYR A CB    1 
ATOM   203  C  CG    . TYR A 1 30  ? 11.32600  -8.60300  23.09900  1.000 28.81135  ? 30   TYR A CG    1 
ATOM   204  C  CD1   . TYR A 1 30  ? 10.17800  -9.39100  23.07400  1.000 28.32182  ? 30   TYR A CD1   1 
ATOM   205  C  CD2   . TYR A 1 30  ? 11.21800  -7.27000  22.70400  1.000 26.23736  ? 30   TYR A CD2   1 
ATOM   206  C  CE1   . TYR A 1 30  ? 8.96800   -8.86800  22.67000  1.000 27.91387  ? 30   TYR A CE1   1 
ATOM   207  C  CE2   . TYR A 1 30  ? 10.01200  -6.74300  22.30100  1.000 24.84508  ? 30   TYR A CE2   1 
ATOM   208  C  CZ    . TYR A 1 30  ? 8.89500   -7.54600  22.28000  1.000 25.79520  ? 30   TYR A CZ    1 
ATOM   209  O  OH    . TYR A 1 30  ? 7.69700   -7.01700  21.88500  1.000 25.53201  ? 30   TYR A OH    1 
ATOM   210  N  N     . ALA A 1 31  ? 14.80400  -11.26000 24.79500  1.000 33.44875  ? 31   ALA A N     1 
ATOM   211  C  CA    . ALA A 1 31  ? 16.17000  -11.76700 24.84000  1.000 35.49373  ? 31   ALA A CA    1 
ATOM   212  C  C     . ALA A 1 31  ? 16.22700  -13.19500 24.31700  1.000 35.69112  ? 31   ALA A C     1 
ATOM   213  O  O     . ALA A 1 31  ? 17.17900  -13.57600 23.62500  1.000 34.93314  ? 31   ALA A O     1 
ATOM   214  C  CB    . ALA A 1 31  ? 16.71000  -11.69000 26.26900  1.000 36.90179  ? 31   ALA A CB    1 
ATOM   215  N  N     . GLN A 1 32  ? 15.20500  -13.99400 24.63300  1.000 37.77032  ? 32   GLN A N     1 
ATOM   216  C  CA    . GLN A 1 32  ? 15.10400  -15.34400 24.08900  1.000 39.60738  ? 32   GLN A CA    1 
ATOM   217  C  C     . GLN A 1 32  ? 15.01400  -15.31500 22.56800  1.000 35.13053  ? 32   GLN A C     1 
ATOM   218  O  O     . GLN A 1 32  ? 15.73100  -16.05100 21.87800  1.000 35.48847  ? 32   GLN A O     1 
ATOM   219  C  CB    . GLN A 1 32  ? 13.88900  -16.05100 24.69400  1.000 47.10038  ? 32   GLN A CB    1 
ATOM   220  C  CG    . GLN A 1 32  ? 13.47000  -17.31600 23.96300  1.000 55.06713  ? 32   GLN A CG    1 
ATOM   221  C  CD    . GLN A 1 32  ? 14.04800  -18.57000 24.58500  1.000 62.17324  ? 32   GLN A CD    1 
ATOM   222  O  OE1   . GLN A 1 32  ? 13.72200  -18.92400 25.72100  1.000 63.36286  ? 32   GLN A OE1   1 
ATOM   223  N  NE2   . GLN A 1 32  ? 14.91200  -19.25200 23.84200  1.000 65.88948  ? 32   GLN A NE2   1 
ATOM   224  N  N     . LEU A 1 33  ? 14.13600  -14.46400 22.02600  1.000 31.80118  ? 33   LEU A N     1 
ATOM   225  C  CA    . LEU A 1 33  ? 14.05500  -14.31800 20.57700  1.000 28.50605  ? 33   LEU A CA    1 
ATOM   226  C  C     . LEU A 1 33  ? 15.39300  -13.87800 19.99900  1.000 29.12718  ? 33   LEU A C     1 
ATOM   227  O  O     . LEU A 1 33  ? 15.83600  -14.40000 18.96900  1.000 29.39563  ? 33   LEU A O     1 
ATOM   228  C  CB    . LEU A 1 33  ? 12.94500  -13.32700 20.20800  1.000 27.28222  ? 33   LEU A CB    1 
ATOM   229  C  CG    . LEU A 1 33  ? 11.51400  -13.74400 20.57200  1.000 27.35328  ? 33   LEU A CG    1 
ATOM   230  C  CD1   . LEU A 1 33  ? 10.52900  -12.58800 20.42000  1.000 28.16654  ? 33   LEU A CD1   1 
ATOM   231  C  CD2   . LEU A 1 33  ? 11.06600  -14.94400 19.74000  1.000 28.15074  ? 33   LEU A CD2   1 
ATOM   232  N  N     . ARG A 1 34  ? 16.06100  -12.93000 20.66600  1.000 27.65332  ? 34   ARG A N     1 
ATOM   233  C  CA    . ARG A 1 34  ? 17.36000  -12.45100 20.19500  1.000 28.03494  ? 34   ARG A CA    1 
ATOM   234  C  C     . ARG A 1 34  ? 18.37200  -13.58900 20.10600  1.000 29.66671  ? 34   ARG A C     1 
ATOM   235  O  O     . ARG A 1 34  ? 19.17500  -13.64700 19.16600  1.000 31.12215  ? 34   ARG A O     1 
ATOM   236  C  CB    . ARG A 1 34  ? 17.86600  -11.34900 21.13200  1.000 26.81901  ? 34   ARG A CB    1 
ATOM   237  C  CG    . ARG A 1 34  ? 19.07900  -10.55700 20.63600  1.000 26.14524  ? 34   ARG A CG    1 
ATOM   238  C  CD    . ARG A 1 34  ? 20.39800  -11.08600 21.20100  1.000 26.75584  ? 34   ARG A CD    1 
ATOM   239  N  NE    . ARG A 1 34  ? 20.38300  -11.16400 22.65700  1.000 28.02968  ? 34   ARG A NE    1 
ATOM   240  C  CZ    . ARG A 1 34  ? 20.60700  -10.13800 23.47000  1.000 27.34012  ? 34   ARG A CZ    1 
ATOM   241  N  NH1   . ARG A 1 34  ? 20.88500  -8.93200  23.00300  1.000 26.19788  ? 34   ARG A NH1   1 
ATOM   242  N  NH2   . ARG A 1 34  ? 20.53300  -10.32300 24.78500  1.000 30.59841  ? 34   ARG A NH2   1 
ATOM   243  N  N     . ASP A 1 35  ? 18.33200  -14.51800 21.06100  1.000 31.54589  ? 35   ASP A N     1 
ATOM   244  C  CA    . ASP A 1 35  ? 19.34700  -15.56600 21.14200  1.000 33.99355  ? 35   ASP A CA    1 
ATOM   245  C  C     . ASP A 1 35  ? 19.06400  -16.74700 20.21800  1.000 35.21212  ? 35   ASP A C     1 
ATOM   246  O  O     . ASP A 1 35  ? 20.00000  -17.46900 19.85100  1.000 37.01233  ? 35   ASP A O     1 
ATOM   247  C  CB    . ASP A 1 35  ? 19.49000  -16.06200 22.58400  1.000 37.39133  ? 35   ASP A CB    1 
ATOM   248  C  CG    . ASP A 1 35  ? 20.00300  -14.98800 23.52900  1.000 40.03112  ? 35   ASP A CG    1 
ATOM   249  O  OD1   . ASP A 1 35  ? 20.54900  -13.96900 23.04300  1.000 41.33390  ? 35   ASP A OD1   1 
ATOM   250  O  OD2   . ASP A 1 35  ? 19.86100  -15.16500 24.75700  1.000 40.00216  ? 35   ASP A OD2   1 
ATOM   251  N  N     . THR A 1 36  ? 17.80800  -16.97500 19.85100  1.000 34.17252  ? 36   THR A N     1 
ATOM   252  C  CA    . THR A 1 36  ? 17.47300  -18.13900 19.03200  1.000 36.47279  ? 36   THR A CA    1 
ATOM   253  C  C     . THR A 1 36  ? 18.03300  -17.96000 17.62600  1.000 36.07011  ? 36   THR A C     1 
ATOM   254  O  O     . THR A 1 36  ? 17.84300  -16.90000 17.02000  1.000 37.20972  ? 36   THR A O     1 
ATOM   255  C  CB    . THR A 1 36  ? 15.95800  -18.32800 18.96000  1.000 40.10744  ? 36   THR A CB    1 
ATOM   256  O  OG1   . THR A 1 36  ? 15.42600  -18.43500 20.28300  1.000 41.36549  ? 36   THR A OG1   1 
ATOM   257  C  CG2   . THR A 1 36  ? 15.60800  -19.59900 18.18700  1.000 40.03901  ? 36   THR A CG2   1 
ATOM   258  N  N     . PRO A 1 37  ? 18.72600  -18.95700 17.08000  1.000 33.13029  ? 37   PRO A N     1 
ATOM   259  C  CA    . PRO A 1 37  ? 19.28900  -18.81500 15.73500  1.000 32.20912  ? 37   PRO A CA    1 
ATOM   260  C  C     . PRO A 1 37  ? 18.20300  -18.63300 14.68500  1.000 31.58800  ? 37   PRO A C     1 
ATOM   261  O  O     . PRO A 1 37  ? 17.05300  -19.05700 14.84400  1.000 30.65104  ? 37   PRO A O     1 
ATOM   262  C  CB    . PRO A 1 37  ? 20.03600  -20.13900 15.51900  1.000 32.83552  ? 37   PRO A CB    1 
ATOM   263  C  CG    . PRO A 1 37  ? 20.32000  -20.64700 16.88600  1.000 34.02250  ? 37   PRO A CG    1 
ATOM   264  C  CD    . PRO A 1 37  ? 19.15100  -20.20800 17.72800  1.000 33.85143  ? 37   PRO A CD    1 
ATOM   265  N  N     . GLY A 1 38  ? 18.59200  -18.00000 13.58400  1.000 30.52208  ? 38   GLY A N     1 
ATOM   266  C  CA    . GLY A 1 38  ? 17.68900  -17.78900 12.48100  1.000 29.56933  ? 38   GLY A CA    1 
ATOM   267  C  C     . GLY A 1 38  ? 17.13000  -16.38400 12.46700  1.000 27.75070  ? 38   GLY A C     1 
ATOM   268  O  O     . GLY A 1 38  ? 16.95600  -15.74300 13.50700  1.000 29.04296  ? 38   GLY A O     1 
ATOM   269  N  N     . PRO A 1 39  ? 16.84400  -15.87800 11.26800  1.000 25.35567  ? 39   PRO A N     1 
ATOM   270  C  CA    . PRO A 1 39  ? 16.30700  -14.51600 11.15000  1.000 24.03183  ? 39   PRO A CA    1 
ATOM   271  C  C     . PRO A 1 39  ? 14.88200  -14.36600 11.65200  1.000 22.44216  ? 39   PRO A C     1 
ATOM   272  O  O     . PRO A 1 39  ? 14.50400  -13.25200 12.03400  1.000 21.59206  ? 39   PRO A O     1 
ATOM   273  C  CB    . PRO A 1 39  ? 16.39000  -14.24500 9.64400   1.000 26.44001  ? 39   PRO A CB    1 
ATOM   274  C  CG    . PRO A 1 39  ? 16.38600  -15.59500 9.01500   1.000 28.07705  ? 39   PRO A CG    1 
ATOM   275  C  CD    . PRO A 1 39  ? 17.14600  -16.47100 9.95700   1.000 27.45592  ? 39   PRO A CD    1 
ATOM   276  N  N     . LEU A 1 40  ? 14.08500  -15.43500 11.66600  1.000 23.89234  ? 40   LEU A N     1 
ATOM   277  C  CA    . LEU A 1 40  ? 12.65600  -15.34700 11.92800  1.000 22.55534  ? 40   LEU A CA    1 
ATOM   278  C  C     . LEU A 1 40  ? 12.26500  -16.23100 13.10100  1.000 25.35567  ? 40   LEU A C     1 
ATOM   279  O  O     . LEU A 1 40  ? 12.89800  -17.26000 13.36600  1.000 26.21630  ? 40   LEU A O     1 
ATOM   280  C  CB    . LEU A 1 40  ? 11.84600  -15.81600 10.71100  1.000 23.62652  ? 40   LEU A CB    1 
ATOM   281  C  CG    . LEU A 1 40  ? 12.17700  -15.16100 9.37600   1.000 24.76086  ? 40   LEU A CG    1 
ATOM   282  C  CD1   . LEU A 1 40  ? 11.28300  -15.73300 8.28700   1.000 28.12442  ? 40   LEU A CD1   1 
ATOM   283  C  CD2   . LEU A 1 40  ? 12.01100  -13.64900 9.47400   1.000 25.59781  ? 40   LEU A CD2   1 
ATOM   284  N  N     . HIS A 1 41  ? 11.18800  -15.83700 13.78200  1.000 23.72653  ? 41   HIS A N     1 
ATOM   285  C  CA    . HIS A 1 41  ? 10.58900  -16.67400 14.81100  1.000 25.05827  ? 41   HIS A CA    1 
ATOM   286  C  C     . HIS A 1 41  ? 9.07700   -16.51500 14.78800  1.000 23.94498  ? 41   HIS A C     1 
ATOM   287  O  O     . HIS A 1 41  ? 8.56500   -15.40400 14.61600  1.000 23.27121  ? 41   HIS A O     1 
ATOM   288  C  CB    . HIS A 1 41  ? 11.13000  -16.34200 16.20600  1.000 23.92655  ? 41   HIS A CB    1 
ATOM   289  C  CG    . HIS A 1 41  ? 10.96200  -17.45700 17.19400  1.000 23.65547  ? 41   HIS A CG    1 
ATOM   290  N  ND1   . HIS A 1 41  ? 9.74200   -17.79900 17.73900  1.000 25.85047  ? 41   HIS A ND1   1 
ATOM   291  C  CD2   . HIS A 1 41  ? 11.86600  -18.30800 17.73600  1.000 25.60307  ? 41   HIS A CD2   1 
ATOM   292  C  CE1   . HIS A 1 41  ? 9.90100   -18.82100 18.56300  1.000 27.27695  ? 41   HIS A CE1   1 
ATOM   293  N  NE2   . HIS A 1 41  ? 11.18200  -19.14500 18.58400  1.000 26.11892  ? 41   HIS A NE2   1 
ATOM   294  N  N     . ARG A 1 42  ? 8.36800   -17.62900 14.95300  1.000 24.74770  ? 42   ARG A N     1 
ATOM   295  C  CA    . ARG A 1 42  ? 6.91700   -17.57400 15.03900  1.000 24.25817  ? 42   ARG A CA    1 
ATOM   296  C  C     . ARG A 1 42  ? 6.49200   -16.91200 16.34600  1.000 25.06353  ? 42   ARG A C     1 
ATOM   297  O  O     . ARG A 1 42  ? 7.15300   -17.04500 17.38000  1.000 26.07418  ? 42   ARG A O     1 
ATOM   298  C  CB    . ARG A 1 42  ? 6.32500   -18.98300 14.97100  1.000 25.69782  ? 42   ARG A CB    1 
ATOM   299  C  CG    . ARG A 1 42  ? 6.59600   -19.69200 13.65900  1.000 28.22970  ? 42   ARG A CG    1 
ATOM   300  C  CD    . ARG A 1 42  ? 5.94800   -21.06900 13.62400  1.000 33.18556  ? 42   ARG A CD    1 
ATOM   301  N  NE    . ARG A 1 42  ? 6.28200   -21.79800 12.40500  1.000 37.55187  ? 42   ARG A NE    1 
ATOM   302  C  CZ    . ARG A 1 42  ? 7.32000   -22.61400 12.28600  1.000 44.23162  ? 42   ARG A CZ    1 
ATOM   303  N  NH1   . ARG A 1 42  ? 8.12900   -22.85500 13.30700  1.000 46.93457  ? 42   ARG A NH1   1 
ATOM   304  N  NH2   . ARG A 1 42  ? 7.55700   -23.19600 11.11300  1.000 45.90814  ? 42   ARG A NH2   1 
ATOM   305  N  N     . VAL A 1 43  ? 5.38200   -16.17100 16.28600  1.000 24.87930  ? 43   VAL A N     1 
ATOM   306  C  CA    . VAL A 1 43  ? 4.75200   -15.57300 17.45800  1.000 24.40293  ? 43   VAL A CA    1 
ATOM   307  C  C     . VAL A 1 43  ? 3.24300   -15.67300 17.29100  1.000 24.98984  ? 43   VAL A C     1 
ATOM   308  O  O     . VAL A 1 43  ? 2.73100   -15.91900 16.19700  1.000 26.07944  ? 43   VAL A O     1 
ATOM   309  C  CB    . VAL A 1 43  ? 5.14100   -14.09100 17.68400  1.000 25.40831  ? 43   VAL A CB    1 
ATOM   310  C  CG1   . VAL A 1 43  ? 6.63000   -13.93800 17.92700  1.000 25.45042  ? 43   VAL A CG1   1 
ATOM   311  C  CG2   . VAL A 1 43  ? 4.66200   -13.21600 16.52200  1.000 25.33725  ? 43   VAL A CG2   1 
ATOM   312  N  N     . THR A 1 44  ? 2.53200   -15.45100 18.39400  1.000 25.80046  ? 44   THR A N     1 
ATOM   313  C  CA    . THR A 1 44  ? 1.07500   -15.43200 18.41800  1.000 26.31895  ? 44   THR A CA    1 
ATOM   314  C  C     . THR A 1 44  ? 0.61300   -14.03600 18.81000  1.000 27.39276  ? 44   THR A C     1 
ATOM   315  O  O     . THR A 1 44  ? 1.03400   -13.51200 19.84500  1.000 28.21917  ? 44   THR A O     1 
ATOM   316  C  CB    . THR A 1 44  ? 0.54100   -16.44700 19.43300  1.000 28.03757  ? 44   THR A CB    1 
ATOM   317  O  OG1   . THR A 1 44  ? 1.03300   -17.75700 19.11300  1.000 29.58776  ? 44   THR A OG1   1 
ATOM   318  C  CG2   . THR A 1 44  ? -0.97700  -16.46300 19.42200  1.000 30.84054  ? 44   THR A CG2   1 
ATOM   319  N  N     . LEU A 1 45  ? -0.25200  -13.43900 17.98800  1.000 27.50330  ? 45   LEU A N     1 
ATOM   320  C  CA    . LEU A 1 45  ? -0.73900  -12.09200 18.24800  1.000 28.31392  ? 45   LEU A CA    1 
ATOM   321  C  C     . LEU A 1 45  ? -1.96600  -12.13600 19.15800  1.000 30.64841  ? 45   LEU A C     1 
ATOM   322  O  O     . LEU A 1 45  ? -2.47800  -13.20400 19.50200  1.000 30.92739  ? 45   LEU A O     1 
ATOM   323  C  CB    . LEU A 1 45  ? -1.02200  -11.35900 16.93800  1.000 27.27959  ? 45   LEU A CB    1 
ATOM   324  C  CG    . LEU A 1 45  ? 0.16000   -11.32100 15.96900  1.000 26.44264  ? 45   LEU A CG    1 
ATOM   325  C  CD1   . LEU A 1 45  ? -0.19800  -10.51500 14.73700  1.000 27.90335  ? 45   LEU A CD1   1 
ATOM   326  C  CD2   . LEU A 1 45  ? 1.40600   -10.76000 16.64900  1.000 27.31643  ? 45   LEU A CD2   1 
ATOM   327  N  N     . TYR A 1 46  ? -2.46000  -10.94900 19.53100  1.000 31.40377  ? 46   TYR A N     1 
ATOM   328  C  CA    . TYR A 1 46  ? -3.46900  -10.83800 20.58500  1.000 32.47758  ? 46   TYR A CA    1 
ATOM   329  C  C     . TYR A 1 46  ? -4.74500  -11.60500 20.25400  1.000 35.75955  ? 46   TYR A C     1 
ATOM   330  O  O     . TYR A 1 46  ? -5.43500  -12.07600 21.16600  1.000 37.98613  ? 46   TYR A O     1 
ATOM   331  C  CB    . TYR A 1 46  ? -3.79100  -9.36400  20.84800  1.000 31.39587  ? 46   TYR A CB    1 
ATOM   332  C  CG    . TYR A 1 46  ? -4.70200  -8.75100  19.81100  1.000 32.06963  ? 46   TYR A CG    1 
ATOM   333  C  CD1   . TYR A 1 46  ? -4.21200  -8.36100  18.57100  1.000 32.11964  ? 46   TYR A CD1   1 
ATOM   334  C  CD2   . TYR A 1 46  ? -6.05600  -8.56500  20.06900  1.000 32.27492  ? 46   TYR A CD2   1 
ATOM   335  C  CE1   . TYR A 1 46  ? -5.04700  -7.80400  17.61600  1.000 30.58261  ? 46   TYR A CE1   1 
ATOM   336  C  CE2   . TYR A 1 46  ? -6.89400  -8.01200  19.12400  1.000 33.62508  ? 46   TYR A CE2   1 
ATOM   337  C  CZ    . TYR A 1 46  ? -6.38600  -7.62900  17.89900  1.000 33.15661  ? 46   TYR A CZ    1 
ATOM   338  O  OH    . TYR A 1 46  ? -7.22900  -7.07900  16.95900  1.000 37.98087  ? 46   TYR A OH    1 
ATOM   339  N  N     . ASP A 1 47  ? -5.08300  -11.73400 18.97100  1.000 35.74639  ? 47   ASP A N     1 
ATOM   340  C  CA    . ASP A 1 47  ? -6.29200  -12.42900 18.55100  1.000 35.69112  ? 47   ASP A CA    1 
ATOM   341  C  C     . ASP A 1 47  ? -6.06000  -13.90400 18.25100  1.000 35.15158  ? 47   ASP A C     1 
ATOM   342  O  O     . ASP A 1 47  ? -6.97900  -14.57900 17.77500  1.000 39.18891  ? 47   ASP A O     1 
ATOM   343  C  CB    . ASP A 1 47  ? -6.93700  -11.73100 17.34700  1.000 37.75189  ? 47   ASP A CB    1 
ATOM   344  C  CG    . ASP A 1 47  ? -5.99700  -11.61300 16.15600  1.000 39.77056  ? 47   ASP A CG    1 
ATOM   345  O  OD1   . ASP A 1 47  ? -4.80500  -11.96700 16.28200  1.000 37.28605  ? 47   ASP A OD1   1 
ATOM   346  O  OD2   . ASP A 1 47  ? -6.46000  -11.16300 15.08300  1.000 41.53393  ? 47   ASP A OD2   1 
ATOM   347  N  N     . GLY A 1 48  ? -4.86400  -14.42200 18.52600  1.000 34.85681  ? 48   GLY A N     1 
ATOM   348  C  CA    . GLY A 1 48  ? -4.56100  -15.81100 18.26500  1.000 33.70667  ? 48   GLY A CA    1 
ATOM   349  C  C     . GLY A 1 48  ? -3.93000  -16.09100 16.91900  1.000 36.14118  ? 48   GLY A C     1 
ATOM   350  O  O     . GLY A 1 48  ? -3.54000  -17.23700 16.66300  1.000 37.49660  ? 48   GLY A O     1 
ATOM   351  N  N     . ARG A 1 49  ? -3.81500  -15.09100 16.05200  1.000 33.94881  ? 49   ARG A N     1 
ATOM   352  C  CA    . ARG A 1 49  ? -3.21500  -15.30600 14.74600  1.000 34.87787  ? 49   ARG A CA    1 
ATOM   353  C  C     . ARG A 1 49  ? -1.70100  -15.39900 14.86200  1.000 31.48535  ? 49   ARG A C     1 
ATOM   354  O  O     . ARG A 1 49  ? -1.07200  -14.67300 15.63800  1.000 30.31679  ? 49   ARG A O     1 
ATOM   355  C  CB    . ARG A 1 49  ? -3.61000  -14.19200 13.77800  1.000 40.28904  ? 49   ARG A CB    1 
ATOM   356  C  CG    . ARG A 1 49  ? -5.07900  -14.23700 13.39600  1.000 47.32936  ? 49   ARG A CG    1 
ATOM   357  C  CD    . ARG A 1 49  ? -5.29000  -13.83500 11.95700  1.000 54.98817  ? 49   ARG A CD    1 
ATOM   358  N  NE    . ARG A 1 49  ? -5.22700  -12.39100 11.77400  1.000 63.03387  ? 49   ARG A NE    1 
ATOM   359  C  CZ    . ARG A 1 49  ? -5.20900  -11.79300 10.59100  1.000 68.95037  ? 49   ARG A CZ    1 
ATOM   360  N  NH1   . ARG A 1 49  ? -5.21200  -12.48900 9.46500   1.000 71.75071  ? 49   ARG A NH1   1 
ATOM   361  N  NH2   . ARG A 1 49  ? -5.18600  -10.46400 10.53500  1.000 70.33738  ? 49   ARG A NH2   1 
ATOM   362  N  N     . GLN A 1 50  ? -1.12200  -16.30900 14.09000  1.000 31.95909  ? 50   GLN A N     1 
ATOM   363  C  CA    . GLN A 1 50  ? 0.31800   -16.48700 14.06100  1.000 31.36429  ? 50   GLN A CA    1 
ATOM   364  C  C     . GLN A 1 50  ? 0.94400   -15.52700 13.05900  1.000 31.59853  ? 50   GLN A C     1 
ATOM   365  O  O     . GLN A 1 50  ? 0.37100   -15.24100 12.00300  1.000 33.49612  ? 50   GLN A O     1 
ATOM   366  C  CB    . GLN A 1 50  ? 0.67600   -17.92700 13.68900  1.000 36.56754  ? 50   GLN A CB    1 
ATOM   367  C  CG    . GLN A 1 50  ? 2.16300   -18.24700 13.81000  1.000 41.60499  ? 50   GLN A CG    1 
ATOM   368  C  CD    . GLN A 1 50  ? 2.54900   -19.50400 13.06800  1.000 46.80561  ? 50   GLN A CD    1 
ATOM   369  O  OE1   . GLN A 1 50  ? 2.14100   -20.60600 13.44000  1.000 44.57640  ? 50   GLN A OE1   1 
ATOM   370  N  NE2   . GLN A 1 50  ? 3.33600   -19.34800 12.00400  1.000 48.38475  ? 50   GLN A NE2   1 
ATOM   371  N  N     . ALA A 1 51  ? 2.12700   -15.03300 13.40100  1.000 26.80321  ? 51   ALA A N     1 
ATOM   372  C  CA    . ALA A 1 51  ? 2.88800   -14.16100 12.52500  1.000 24.15816  ? 51   ALA A CA    1 
ATOM   373  C  C     . ALA A 1 51  ? 4.36000   -14.46800 12.72400  1.000 25.26092  ? 51   ALA A C     1 
ATOM   374  O  O     . ALA A 1 51  ? 4.74200   -15.19500 13.64200  1.000 26.59793  ? 51   ALA A O     1 
ATOM   375  C  CB    . ALA A 1 51  ? 2.61600   -12.68600 12.82800  1.000 26.70847  ? 51   ALA A CB    1 
ATOM   376  N  N     . TRP A 1 52  ? 5.18600   -13.91700 11.84300  1.000 23.66073  ? 52   TRP A N     1 
ATOM   377  C  CA    . TRP A 1 52  ? 6.62800   -13.99000 11.99800  1.000 21.66049  ? 52   TRP A CA    1 
ATOM   378  C  C     . TRP A 1 52  ? 7.12500   -12.68100 12.58600  1.000 21.18149  ? 52   TRP A C     1 
ATOM   379  O  O     . TRP A 1 52  ? 6.59800   -11.60900 12.27400  1.000 24.26607  ? 52   TRP A O     1 
ATOM   380  C  CB    . TRP A 1 52  ? 7.33400   -14.16100 10.65300  1.000 23.00276  ? 52   TRP A CB    1 
ATOM   381  C  CG    . TRP A 1 52  ? 7.10600   -15.45600 9.95100   1.000 22.47112  ? 52   TRP A CG    1 
ATOM   382  C  CD1   . TRP A 1 52  ? 6.31800   -15.66100 8.85600   1.000 23.22121  ? 52   TRP A CD1   1 
ATOM   383  C  CD2   . TRP A 1 52  ? 7.69200   -16.72400 10.26900  1.000 22.49743  ? 52   TRP A CD2   1 
ATOM   384  N  NE1   . TRP A 1 52  ? 6.37600   -16.97800 8.47100   1.000 23.61862  ? 52   TRP A NE1   1 
ATOM   385  C  CE2   . TRP A 1 52  ? 7.21300   -17.65300 9.32200   1.000 23.49755  ? 52   TRP A CE2   1 
ATOM   386  C  CE3   . TRP A 1 52  ? 8.58400   -17.16300 11.25400  1.000 23.18436  ? 52   TRP A CE3   1 
ATOM   387  C  CZ2   . TRP A 1 52  ? 7.58400   -19.00100 9.34100   1.000 25.71098  ? 52   TRP A CZ2   1 
ATOM   388  C  CZ3   . TRP A 1 52  ? 8.95400   -18.50200 11.27400  1.000 24.09236  ? 52   TRP A CZ3   1 
ATOM   389  C  CH2   . TRP A 1 52  ? 8.45500   -19.40400 10.31900  1.000 25.87415  ? 52   TRP A CH2   1 
ATOM   390  N  N     . VAL A 1 53  ? 8.16200   -12.77000 13.41600  1.000 20.92619  ? 53   VAL A N     1 
ATOM   391  C  CA    . VAL A 1 53  ? 8.96300   -11.61600 13.80600  1.000 20.20505  ? 53   VAL A CA    1 
ATOM   392  C  C     . VAL A 1 53  ? 10.36700  -11.78600 13.24600  1.000 20.83671  ? 53   VAL A C     1 
ATOM   393  O  O     . VAL A 1 53  ? 10.88900  -12.90500 13.18500  1.000 20.60773  ? 53   VAL A O     1 
ATOM   394  C  CB    . VAL A 1 53  ? 9.00700   -11.38800 15.33200  1.000 22.19213  ? 53   VAL A CB    1 
ATOM   395  C  CG1   . VAL A 1 53  ? 7.65300   -10.92800 15.84500  1.000 22.72904  ? 53   VAL A CG1   1 
ATOM   396  C  CG2   . VAL A 1 53  ? 9.50800   -12.63500 16.07400  1.000 23.23700  ? 53   VAL A CG2   1 
ATOM   397  N  N     . VAL A 1 54  ? 10.97400  -10.67400 12.83000  1.000 20.42613  ? 54   VAL A N     1 
ATOM   398  C  CA    . VAL A 1 54  ? 12.36700  -10.64500 12.39800  1.000 20.14452  ? 54   VAL A CA    1 
ATOM   399  C  C     . VAL A 1 54  ? 13.20400  -10.18400 13.57900  1.000 20.30507  ? 54   VAL A C     1 
ATOM   400  O  O     . VAL A 1 54  ? 12.92500  -9.13400  14.16900  1.000 21.67365  ? 54   VAL A O     1 
ATOM   401  C  CB    . VAL A 1 54  ? 12.56600  -9.70000  11.20300  1.000 19.79448  ? 54   VAL A CB    1 
ATOM   402  C  CG1   . VAL A 1 54  ? 13.96500  -9.85400  10.63600  1.000 21.19465  ? 54   VAL A CG1   1 
ATOM   403  C  CG2   . VAL A 1 54  ? 11.53100  -9.94800  10.14100  1.000 19.65499  ? 54   VAL A CG2   1 
ATOM   404  N  N     . THR A 1 55  ? 14.23800  -10.95600 13.91700  1.000 19.98397  ? 55   THR A N     1 
ATOM   405  C  CA    . THR A 1 55  ? 14.97800  -10.76200 15.15600  1.000 21.91579  ? 55   THR A CA    1 
ATOM   406  C  C     . THR A 1 55  ? 16.46500  -10.49400 14.96300  1.000 23.55809  ? 55   THR A C     1 
ATOM   407  O  O     . THR A 1 55  ? 17.18700  -10.38500 15.96200  1.000 28.95874  ? 55   THR A O     1 
ATOM   408  C  CB    . THR A 1 55  ? 14.82900  -11.99800 16.04800  1.000 24.74770  ? 55   THR A CB    1 
ATOM   409  O  OG1   . THR A 1 55  ? 15.43500  -13.11700 15.38700  1.000 26.73478  ? 55   THR A OG1   1 
ATOM   410  C  CG2   . THR A 1 55  ? 13.34900  -12.29700 16.32700  1.000 25.77677  ? 55   THR A CG2   1 
ATOM   411  N  N     . LYS A 1 56  ? 16.95100  -10.40700 13.72900  1.000 20.99462  ? 56   LYS A N     1 
ATOM   412  C  CA    . LYS A 1 56  ? 18.36800  -10.20900 13.45600  1.000 18.40747  ? 56   LYS A CA    1 
ATOM   413  C  C     . LYS A 1 56  ? 18.54700  -8.99600  12.54900  1.000 18.24692  ? 56   LYS A C     1 
ATOM   414  O  O     . LYS A 1 56  ? 17.67200  -8.67400  11.74100  1.000 19.50497  ? 56   LYS A O     1 
ATOM   415  C  CB    . LYS A 1 56  ? 18.97100  -11.45800 12.78400  1.000 21.18149  ? 56   LYS A CB    1 
ATOM   416  C  CG    . LYS A 1 56  ? 18.76400  -12.75700 13.55900  1.000 23.75285  ? 56   LYS A CG    1 
ATOM   417  C  CD    . LYS A 1 56  ? 19.40900  -12.71100 14.93300  1.000 26.32947  ? 56   LYS A CD    1 
ATOM   418  C  CE    . LYS A 1 56  ? 19.28400  -14.04900 15.65700  1.000 27.34012  ? 56   LYS A CE    1 
ATOM   419  N  NZ    . LYS A 1 56  ? 17.88400  -14.41900 15.99800  1.000 31.28533  ? 56   LYS A NZ    1 
ATOM   420  N  N     . HIS A 1 57  ? 19.72100  -8.35800  12.65900  1.000 17.43367  ? 57   HIS A N     1 
ATOM   421  C  CA    . HIS A 1 57  ? 19.93100  -7.02100  12.10000  1.000 17.48631  ? 57   HIS A CA    1 
ATOM   422  C  C     . HIS A 1 57  ? 19.94300  -7.01500  10.56800  1.000 17.27839  ? 57   HIS A C     1 
ATOM   423  O  O     . HIS A 1 57  ? 19.18300  -6.27100  9.93200   1.000 19.35758  ? 57   HIS A O     1 
ATOM   424  C  CB    . HIS A 1 57  ? 21.22300  -6.43700  12.65600  1.000 17.73634  ? 57   HIS A CB    1 
ATOM   425  C  CG    . HIS A 1 57  ? 21.46400  -5.01400  12.26700  1.000 16.19668  ? 57   HIS A CG    1 
ATOM   426  N  ND1   . HIS A 1 57  ? 22.11600  -4.66000  11.10200  1.000 17.96268  ? 57   HIS A ND1   1 
ATOM   427  C  CD2   . HIS A 1 57  ? 21.17900  -3.85500  12.90800  1.000 16.75990  ? 57   HIS A CD2   1 
ATOM   428  C  CE1   . HIS A 1 57  ? 22.20000  -3.34200  11.03500  1.000 17.68370  ? 57   HIS A CE1   1 
ATOM   429  N  NE2   . HIS A 1 57  ? 21.63500  -2.83000  12.11600  1.000 18.56012  ? 57   HIS A NE2   1 
ATOM   430  N  N     . GLU A 1 58  ? 20.82900  -7.80100  9.94700   1.000 20.09188  ? 58   GLU A N     1 
ATOM   431  C  CA    . GLU A 1 58  ? 20.90800  -7.74800  8.48600   1.000 20.72880  ? 58   GLU A CA    1 
ATOM   432  C  C     . GLU A 1 58  ? 19.64200  -8.30000  7.84400   1.000 20.79723  ? 58   GLU A C     1 
ATOM   433  O  O     . GLU A 1 58  ? 19.17200  -7.76500  6.83300   1.000 20.32349  ? 58   GLU A O     1 
ATOM   434  C  CB    . GLU A 1 58  ? 22.16700  -8.45000  7.96600   1.000 24.49767  ? 58   GLU A CB    1 
ATOM   435  C  CG    . GLU A 1 58  ? 22.35200  -8.40700  6.43400   1.000 25.29777  ? 58   GLU A CG    1 
ATOM   436  C  CD    . GLU A 1 58  ? 22.53700  -6.99600  5.86600   1.000 27.23748  ? 58   GLU A CD    1 
ATOM   437  O  OE1   . GLU A 1 58  ? 22.89800  -6.06500  6.62100   1.000 26.55055  ? 58   GLU A OE1   1 
ATOM   438  O  OE2   . GLU A 1 58  ? 22.32300  -6.81700  4.64400   1.000 28.96400  ? 58   GLU A OE2   1 
ATOM   439  N  N     . ALA A 1 59  ? 19.05900  -9.35000  8.43100   1.000 19.79185  ? 59   ALA A N     1 
ATOM   440  C  CA    . ALA A 1 59  ? 17.78700  -9.85800  7.92000   1.000 21.81314  ? 59   ALA A CA    1 
ATOM   441  C  C     . ALA A 1 59  ? 16.69400  -8.79500  7.99200   1.000 19.99977  ? 59   ALA A C     1 
ATOM   442  O  O     . ALA A 1 59  ? 15.83700  -8.71500  7.10300   1.000 21.50521  ? 59   ALA A O     1 
ATOM   443  C  CB    . ALA A 1 59  ? 17.36400  -11.10800 8.68700   1.000 22.67903  ? 59   ALA A CB    1 
ATOM   444  N  N     . ALA A 1 60  ? 16.71100  -7.96500  9.04200   1.000 18.17060  ? 60   ALA A N     1 
ATOM   445  C  CA    . ALA A 1 60  ? 15.73400  -6.88300  9.14900   1.000 18.15744  ? 60   ALA A CA    1 
ATOM   446  C  C     . ALA A 1 60  ? 15.90500  -5.86000  8.02800   1.000 18.05216  ? 60   ALA A C     1 
ATOM   447  O  O     . ALA A 1 60  ? 14.91300  -5.42300  7.43400   1.000 18.12586  ? 60   ALA A O     1 
ATOM   448  C  CB    . ALA A 1 60  ? 15.82900  -6.21900  10.51900  1.000 18.70751  ? 60   ALA A CB    1 
ATOM   449  N  N     . ARG A 1 61  ? 17.15000  -5.47400  7.71700   1.000 17.58106  ? 61   ARG A N     1 
ATOM   450  C  CA    . ARG A 1 61  ? 17.37700  -4.57500  6.58600   1.000 18.17323  ? 61   ARG A CA    1 
ATOM   451  C  C     . ARG A 1 61  ? 16.91900  -5.21400  5.28600   1.000 18.56012  ? 61   ARG A C     1 
ATOM   452  O  O     . ARG A 1 61  ? 16.29300  -4.55700  4.44300   1.000 19.91291  ? 61   ARG A O     1 
ATOM   453  C  CB    . ARG A 1 61  ? 18.85400  -4.20700  6.46700   1.000 16.05982  ? 61   ARG A CB    1 
ATOM   454  C  CG    . ARG A 1 61  ? 19.35500  -3.29500  7.55200   1.000 18.34957  ? 61   ARG A CG    1 
ATOM   455  C  CD    . ARG A 1 61  ? 20.86700  -3.14400  7.46600   1.000 17.50473  ? 61   ARG A CD    1 
ATOM   456  N  NE    . ARG A 1 61  ? 21.34400  -2.55000  6.21600   1.000 20.16558  ? 61   ARG A NE    1 
ATOM   457  C  CZ    . ARG A 1 61  ? 21.96000  -1.37200  6.13600   1.000 19.46286  ? 61   ARG A CZ    1 
ATOM   458  N  NH1   . ARG A 1 61  ? 22.03200  -0.55800  7.18000   1.000 17.69686  ? 61   ARG A NH1   1 
ATOM   459  N  NH2   . ARG A 1 61  ? 22.55400  -1.01900  4.98900   1.000 19.03386  ? 61   ARG A NH2   1 
ATOM   460  N  N     . LYS A 1 62  ? 17.23400  -6.49400  5.09700   1.000 19.07071  ? 62   LYS A N     1 
ATOM   461  C  CA    . LYS A 1 62  ? 16.85200  -7.14700  3.85200   1.000 19.49181  ? 62   LYS A CA    1 
ATOM   462  C  C     . LYS A 1 62  ? 15.34000  -7.15800  3.68800   1.000 19.54708  ? 62   LYS A C     1 
ATOM   463  O  O     . LYS A 1 62  ? 14.82100  -6.89000  2.59600   1.000 23.15541  ? 62   LYS A O     1 
ATOM   464  C  CB    . LYS A 1 62  ? 17.41400  -8.56800  3.79600   1.000 23.98709  ? 62   LYS A CB    1 
ATOM   465  C  CG    . LYS A 1 62  ? 17.03200  -9.32300  2.52800   1.000 30.15888  ? 62   LYS A CG    1 
ATOM   466  C  CD    . LYS A 1 62  ? 17.71900  -10.68500 2.43100   1.000 38.32565  ? 62   LYS A CD    1 
ATOM   467  C  CE    . LYS A 1 62  ? 17.33900  -11.37800 1.12700   1.000 41.79712  ? 62   LYS A CE    1 
ATOM   468  N  NZ    . LYS A 1 62  ? 18.44500  -12.19900 0.55000   1.000 45.57915  ? 62   LYS A NZ    1 
ATOM   469  N  N     . LEU A 1 63  ? 14.60900  -7.45800  4.76500   1.000 17.30997  ? 63   LEU A N     1 
ATOM   470  C  CA    . LEU A 1 63  ? 13.16100  -7.57400  4.64300   1.000 17.07047  ? 63   LEU A CA    1 
ATOM   471  C  C     . LEU A 1 63  ? 12.48300  -6.20800  4.56000   1.000 17.98374  ? 63   LEU A C     1 
ATOM   472  O  O     . LEU A 1 63  ? 11.50200  -6.05400  3.82400   1.000 18.77330  ? 63   LEU A O     1 
ATOM   473  C  CB    . LEU A 1 63  ? 12.59400  -8.45900  5.75400   1.000 18.46274  ? 63   LEU A CB    1 
ATOM   474  C  CG    . LEU A 1 63  ? 12.91300  -9.94700  5.52600   1.000 19.59445  ? 63   LEU A CG    1 
ATOM   475  C  CD1   . LEU A 1 63  ? 12.63600  -10.77000 6.77600   1.000 19.61551  ? 63   LEU A CD1   1 
ATOM   476  C  CD2   . LEU A 1 63  ? 12.12500  -10.51700 4.34900   1.000 21.10516  ? 63   LEU A CD2   1 
ATOM   477  N  N     . LEU A 1 64  ? 12.99300  -5.20500  5.29600   1.000 16.88624  ? 64   LEU A N     1 
ATOM   478  C  CA    . LEU A 1 64  ? 12.48800  -3.84400  5.13700   1.000 17.35998  ? 64   LEU A CA    1 
ATOM   479  C  C     . LEU A 1 64  ? 12.74500  -3.30900  3.73200   1.000 18.58381  ? 64   LEU A C     1 
ATOM   480  O  O     . LEU A 1 64  ? 11.99000  -2.46100  3.24200   1.000 19.28915  ? 64   LEU A O     1 
ATOM   481  C  CB    . LEU A 1 64  ? 13.10900  -2.91900  6.18700   1.000 17.56000  ? 64   LEU A CB    1 
ATOM   482  C  CG    . LEU A 1 64  ? 12.55300  -3.08200  7.60700   1.000 17.65212  ? 64   LEU A CG    1 
ATOM   483  C  CD1   . LEU A 1 64  ? 13.41400  -2.31500  8.60300   1.000 20.21032  ? 64   LEU A CD1   1 
ATOM   484  C  CD2   . LEU A 1 64  ? 11.07900  -2.64700  7.72100   1.000 18.84700  ? 64   LEU A CD2   1 
ATOM   485  N  N     . GLY A 1 65  ? 13.80000  -3.78900  3.07000   1.000 17.79161  ? 65   GLY A N     1 
ATOM   486  C  CA    . GLY A 1 65  ? 14.07800  -3.41200  1.69500   1.000 19.59972  ? 65   GLY A CA    1 
ATOM   487  C  C     . GLY A 1 65  ? 13.36400  -4.22700  0.63800   1.000 18.28640  ? 65   GLY A C     1 
ATOM   488  O  O     . GLY A 1 65  ? 13.46600  -3.89500  -0.54700  1.000 22.10528  ? 65   GLY A O     1 
ATOM   489  N  N     . ASP A 1 66  ? 12.62400  -5.26300  1.03000   1.000 18.36010  ? 66   ASP A N     1 
ATOM   490  C  CA    . ASP A 1 66  ? 12.03400  -6.18500  0.06600   1.000 19.52603  ? 66   ASP A CA    1 
ATOM   491  C  C     . ASP A 1 66  ? 10.63800  -5.70200  -0.30600  1.000 18.78120  ? 66   ASP A C     1 
ATOM   492  O  O     . ASP A 1 66  ? 9.75600   -5.67500  0.56000   1.000 20.06556  ? 66   ASP A O     1 
ATOM   493  C  CB    . ASP A 1 66  ? 11.94400  -7.57100  0.68400   1.000 20.89987  ? 66   ASP A CB    1 
ATOM   494  C  CG    . ASP A 1 66  ? 11.63200  -8.65800  -0.32900  1.000 20.99989  ? 66   ASP A CG    1 
ATOM   495  O  OD1   . ASP A 1 66  ? 10.92300  -8.38100  -1.31300  1.000 22.61061  ? 66   ASP A OD1   1 
ATOM   496  O  OD2   . ASP A 1 66  ? 12.09500  -9.80600  -0.13100  1.000 26.53476  ? 66   ASP A OD2   1 
ATOM   497  N  N     . PRO A 1 67  ? 10.37900  -5.32600  -1.56200  1.000 20.52615  ? 67   PRO A N     1 
ATOM   498  C  CA    . PRO A 1 67  ? 9.03900   -4.83000  -1.90500  1.000 21.92631  ? 67   PRO A CA    1 
ATOM   499  C  C     . PRO A 1 67  ? 7.94700   -5.87800  -1.79300  1.000 22.18950  ? 67   PRO A C     1 
ATOM   500  O  O     . PRO A 1 67  ? 6.76200   -5.52100  -1.83800  1.000 21.57364  ? 67   PRO A O     1 
ATOM   501  C  CB    . PRO A 1 67  ? 9.19800   -4.32300  -3.34200  1.000 25.83204  ? 67   PRO A CB    1 
ATOM   502  C  CG    . PRO A 1 67  ? 10.38400  -5.02900  -3.86900  1.000 27.93756  ? 67   PRO A CG    1 
ATOM   503  C  CD    . PRO A 1 67  ? 11.30300  -5.27000  -2.71000  1.000 23.62125  ? 67   PRO A CD    1 
ATOM   504  N  N     . ARG A 1 68  ? 8.30100   -7.15400  -1.63800  1.000 19.93660  ? 68   ARG A N     1 
ATOM   505  C  CA    . ARG A 1 68  ? 7.29300   -8.17700  -1.40100  1.000 20.14715  ? 68   ARG A CA    1 
ATOM   506  C  C     . ARG A 1 68  ? 6.69100   -8.10100  -0.00300  1.000 19.91291  ? 68   ARG A C     1 
ATOM   507  O  O     . ARG A 1 68  ? 5.70500   -8.79400  0.26100   1.000 21.31835  ? 68   ARG A O     1 
ATOM   508  C  CB    . ARG A 1 68  ? 7.87600   -9.57100  -1.65000  1.000 23.73179  ? 68   ARG A CB    1 
ATOM   509  C  CG    . ARG A 1 68  ? 8.29600   -9.79800  -3.09700  1.000 25.07669  ? 68   ARG A CG    1 
ATOM   510  C  CD    . ARG A 1 68  ? 9.05300   -11.10600 -3.29000  1.000 24.90035  ? 68   ARG A CD    1 
ATOM   511  N  NE    . ARG A 1 68  ? 10.31800  -11.09500 -2.56900  1.000 25.98206  ? 68   ARG A NE    1 
ATOM   512  C  CZ    . ARG A 1 68  ? 11.22900  -12.05400 -2.64200  1.000 26.26631  ? 68   ARG A CZ    1 
ATOM   513  N  NH1   . ARG A 1 68  ? 11.03400  -13.13600 -3.37800  1.000 29.79041  ? 68   ARG A NH1   1 
ATOM   514  N  NH2   . ARG A 1 68  ? 12.36600  -11.92000 -1.96500  1.000 25.83468  ? 68   ARG A NH2   1 
ATOM   515  N  N     . LEU A 1 69  ? 7.25600   -7.29900  0.89600   1.000 19.48392  ? 69   LEU A N     1 
ATOM   516  C  CA    . LEU A 1 69  ? 6.65900   -7.05600  2.20700   1.000 19.92607  ? 69   LEU A CA    1 
ATOM   517  C  C     . LEU A 1 69  ? 5.94700   -5.71200  2.14500   1.000 19.19704  ? 69   LEU A C     1 
ATOM   518  O  O     . LEU A 1 69  ? 6.58600   -4.65700  2.16300   1.000 19.80764  ? 69   LEU A O     1 
ATOM   519  C  CB    . LEU A 1 69  ? 7.71100   -7.08300  3.30700   1.000 21.24465  ? 69   LEU A CB    1 
ATOM   520  C  CG    . LEU A 1 69  ? 8.14600   -8.45400  3.83000   1.000 21.44468  ? 69   LEU A CG    1 
ATOM   521  C  CD1   . LEU A 1 69  ? 8.98500   -8.27000  5.08300   1.000 24.58716  ? 69   LEU A CD1   1 
ATOM   522  C  CD2   . LEU A 1 69  ? 6.95400   -9.35100  4.13100   1.000 21.75787  ? 69   LEU A CD2   1 
ATOM   523  N  N     . SER A 1 70  ? 4.62100   -5.76300  2.09000   1.000 18.96280  ? 70   SER A N     1 
ATOM   524  C  CA    . SER A 1 70  ? 3.78600   -4.58200  1.92000   1.000 20.77354  ? 70   SER A CA    1 
ATOM   525  C  C     . SER A 1 70  ? 3.50500   -3.92100  3.26500   1.000 19.69447  ? 70   SER A C     1 
ATOM   526  O  O     . SER A 1 70  ? 3.46000   -4.58300  4.30700   1.000 20.17610  ? 70   SER A O     1 
ATOM   527  C  CB    . SER A 1 70  ? 2.45900   -4.99600  1.27700   1.000 22.66061  ? 70   SER A CB    1 
ATOM   528  O  OG    . SER A 1 70  ? 1.49900   -3.95200  1.31000   1.000 24.28712  ? 70   SER A OG    1 
ATOM   529  N  N     . SER A 1 71  ? 3.31700   -2.59700  3.23400   1.000 20.52878  ? 71   SER A N     1 
ATOM   530  C  CA    . SER A 1 71  ? 2.94900   -1.80600  4.40800   1.000 19.34442  ? 71   SER A CA    1 
ATOM   531  C  C     . SER A 1 71  ? 1.44900   -1.52600  4.48900   1.000 21.46310  ? 71   SER A C     1 
ATOM   532  O  O     . SER A 1 71  ? 1.02700   -0.68600  5.29000   1.000 22.87643  ? 71   SER A O     1 
ATOM   533  C  CB    . SER A 1 71  ? 3.73700   -0.48800  4.43600   1.000 19.69973  ? 71   SER A CB    1 
ATOM   534  O  OG    . SER A 1 71  ? 5.12100   -0.71300  4.65600   1.000 19.18125  ? 71   SER A OG    1 
ATOM   535  N  N     . ASN A 1 72  ? 0.64000   -2.20900  3.68600   1.000 23.26858  ? 72   ASN A N     1 
ATOM   536  C  CA    . ASN A 1 72  ? -0.79200  -1.91900  3.55500   1.000 23.23963  ? 72   ASN A CA    1 
ATOM   537  C  C     . ASN A 1 72  ? -1.55900  -2.38900  4.79000   1.000 26.82953  ? 72   ASN A C     1 
ATOM   538  O  O     . ASN A 1 72  ? -1.86200  -3.57300  4.93600   1.000 29.50091  ? 72   ASN A O     1 
ATOM   539  C  CB    . ASN A 1 72  ? -1.32300  -2.59900  2.30000   1.000 24.03709  ? 72   ASN A CB    1 
ATOM   540  C  CG    . ASN A 1 72  ? -2.79900  -2.32800  2.05900   1.000 25.48990  ? 72   ASN A CG    1 
ATOM   541  O  OD1   . ASN A 1 72  ? -3.42100  -1.51200  2.73800   1.000 27.35591  ? 72   ASN A OD1   1 
ATOM   542  N  ND2   . ASN A 1 72  ? -3.36200  -3.01000  1.06600   1.000 28.99032  ? 72   ASN A ND2   1 
ATOM   543  N  N     . ARG A 1 73  ? -1.92900  -1.44400  5.66100   1.000 27.97441  ? 73   ARG A N     1 
ATOM   544  C  CA    A ARG A 1 73  ? -2.67200  -1.76900  6.87600   0.400 31.02214  ? 73   ARG A CA    1 
ATOM   545  C  CA    B ARG A 1 73  ? -2.66200  -1.79000  6.87400   0.600 29.70093  ? 73   ARG A CA    1 
ATOM   546  C  C     . ARG A 1 73  ? -4.06900  -2.30400  6.58900   1.000 31.83803  ? 73   ARG A C     1 
ATOM   547  O  O     . ARG A 1 73  ? -4.64500  -2.98400  7.44400   1.000 34.17515  ? 73   ARG A O     1 
ATOM   548  C  CB    A ARG A 1 73  ? -2.79700  -0.53100  7.76700   0.400 32.76182  ? 73   ARG A CB    1 
ATOM   549  C  CB    B ARG A 1 73  ? -2.73400  -0.59300  7.82900   0.600 29.12191  ? 73   ARG A CB    1 
ATOM   550  C  CG    A ARG A 1 73  ? -1.99700  -0.58300  9.05700   0.400 35.73323  ? 73   ARG A CG    1 
ATOM   551  C  CG    B ARG A 1 73  ? -1.49200  -0.38100  8.69500   0.600 30.34838  ? 73   ARG A CG    1 
ATOM   552  C  CD    A ARG A 1 73  ? -0.86900  0.43500   9.05600   0.400 36.78073  ? 73   ARG A CD    1 
ATOM   553  C  CD    B ARG A 1 73  ? -0.35500  0.25400   7.91900   0.600 31.26427  ? 73   ARG A CD    1 
ATOM   554  N  NE    A ARG A 1 73  ? 0.33200   -0.06600  8.39700   0.400 37.23868  ? 73   ARG A NE    1 
ATOM   555  N  NE    B ARG A 1 73  ? 0.70300   0.74800   8.79800   0.600 32.74340  ? 73   ARG A NE    1 
ATOM   556  C  CZ    A ARG A 1 73  ? 1.51300   0.53800   8.43800   0.400 33.68035  ? 73   ARG A CZ    1 
ATOM   557  C  CZ    B ARG A 1 73  ? 0.64000   1.89000   9.46800   0.600 30.77474  ? 73   ARG A CZ    1 
ATOM   558  N  NH1   A ARG A 1 73  ? 1.68300   1.67900   9.08700   0.400 35.67796  ? 73   ARG A NH1   1 
ATOM   559  N  NH1   B ARG A 1 73  ? -0.42700  2.67200   9.40100   0.600 35.32002  ? 73   ARG A NH1   1 
ATOM   560  N  NH2   A ARG A 1 73  ? 2.55000   -0.02000  7.81800   0.400 29.65882  ? 73   ARG A NH2   1 
ATOM   561  N  NH2   B ARG A 1 73  ? 1.67100   2.25600   10.22600  0.600 27.96388  ? 73   ARG A NH2   1 
ATOM   562  N  N     . THR A 1 74  ? -4.63600  -1.99800  5.42000   1.000 33.21188  ? 74   THR A N     1 
ATOM   563  C  CA    . THR A 1 74  ? -5.98300  -2.46200  5.10000   1.000 35.76481  ? 74   THR A CA    1 
ATOM   564  C  C     . THR A 1 74  ? -6.02000  -3.92000  4.66200   1.000 34.26727  ? 74   THR A C     1 
ATOM   565  O  O     . THR A 1 74  ? -7.11300  -4.48300  4.54300   1.000 36.90179  ? 74   THR A O     1 
ATOM   566  C  CB    . THR A 1 74  ? -6.63900  -1.57500  4.03200   1.000 37.74663  ? 74   THR A CB    1 
ATOM   567  O  OG1   . THR A 1 74  ? -6.01600  -1.79600  2.75800   1.000 37.73347  ? 74   THR A OG1   1 
ATOM   568  C  CG2   . THR A 1 74  ? -6.52200  -0.10000  4.41100   1.000 39.82583  ? 74   THR A CG2   1 
ATOM   569  N  N     . ASP A 1 75  ? -4.86600  -4.54200  4.42300   1.000 33.63298  ? 75   ASP A N     1 
ATOM   570  C  CA    . ASP A 1 75  ? -4.84400  -5.95300  4.06400   1.000 33.68562  ? 75   ASP A CA    1 
ATOM   571  C  C     . ASP A 1 75  ? -5.39000  -6.78900  5.21300   1.000 35.94642  ? 75   ASP A C     1 
ATOM   572  O  O     . ASP A 1 75  ? -5.04900  -6.56300  6.37800   1.000 34.20147  ? 75   ASP A O     1 
ATOM   573  C  CB    . ASP A 1 75  ? -3.41100  -6.38800  3.75600   1.000 34.49098  ? 75   ASP A CB    1 
ATOM   574  C  CG    . ASP A 1 75  ? -3.34300  -7.75900  3.11500   1.000 38.87045  ? 75   ASP A CG    1 
ATOM   575  O  OD1   . ASP A 1 75  ? -3.49100  -8.76900  3.83000   1.000 40.15481  ? 75   ASP A OD1   1 
ATOM   576  O  OD2   . ASP A 1 75  ? -3.14900  -7.82400  1.88600   1.000 43.53154  ? 75   ASP A OD2   1 
ATOM   577  N  N     . ASP A 1 76  ? -6.23900  -7.76600  4.86900   1.000 38.42040  ? 76   ASP A N     1 
ATOM   578  C  CA    . ASP A 1 76  ? -6.85700  -8.62800  5.87500   1.000 42.14716  ? 76   ASP A CA    1 
ATOM   579  C  C     . ASP A 1 76  ? -5.82300  -9.30700  6.76000   1.000 39.47842  ? 76   ASP A C     1 
ATOM   580  O  O     . ASP A 1 76  ? -6.10300  -9.60500  7.92700   1.000 40.16797  ? 76   ASP A O     1 
ATOM   581  C  CB    . ASP A 1 76  ? -7.71100  -9.70300  5.19500   1.000 50.27708  ? 76   ASP A CB    1 
ATOM   582  C  CG    . ASP A 1 76  ? -8.87600  -9.12600  4.41500   1.000 57.93326  ? 76   ASP A CG    1 
ATOM   583  O  OD1   . ASP A 1 76  ? -9.18400  -7.92700  4.58500   1.000 61.92321  ? 76   ASP A OD1   1 
ATOM   584  O  OD2   . ASP A 1 76  ? -9.48400  -9.87900  3.62500   1.000 59.68347  ? 76   ASP A OD2   1 
ATOM   585  N  N     . ASN A 1 77  ? -4.62900  -9.55900  6.23400   1.000 35.78850  ? 77   ASN A N     1 
ATOM   586  C  CA    . ASN A 1 77  ? -3.61800  -10.32100 6.94900   1.000 34.48835  ? 77   ASN A CA    1 
ATOM   587  C  C     . ASN A 1 77  ? -2.53800  -9.45400  7.58300   1.000 30.20889  ? 77   ASN A C     1 
ATOM   588  O  O     . ASN A 1 77  ? -1.53200  -9.99200  8.05800   1.000 32.75919  ? 77   ASN A O     1 
ATOM   589  C  CB    . ASN A 1 77  ? -2.99900  -11.36800 6.02500   1.000 38.32302  ? 77   ASN A CB    1 
ATOM   590  C  CG    . ASN A 1 77  ? -3.99300  -12.43300 5.62000   1.000 42.21822  ? 77   ASN A CG    1 
ATOM   591  O  OD1   . ASN A 1 77  ? -4.81500  -12.86000 6.42600   1.000 44.40269  ? 77   ASN A OD1   1 
ATOM   592  N  ND2   . ASN A 1 77  ? -3.93600  -12.85700 4.36400   1.000 44.24478  ? 77   ASN A ND2   1 
ATOM   593  N  N     . PHE A 1 78  ? -2.71400  -8.13500  7.60500   1.000 28.93768  ? 78   PHE A N     1 
ATOM   594  C  CA    . PHE A 1 78  ? -1.71600  -7.28700  8.24100   1.000 26.87691  ? 78   PHE A CA    1 
ATOM   595  C  C     . PHE A 1 78  ? -1.61100  -7.63300  9.72800   1.000 27.08483  ? 78   PHE A C     1 
ATOM   596  O  O     . PHE A 1 78  ? -2.63600  -7.81000  10.40200  1.000 29.96675  ? 78   PHE A O     1 
ATOM   597  C  CB    . PHE A 1 78  ? -2.06300  -5.80400  8.07300   1.000 28.59817  ? 78   PHE A CB    1 
ATOM   598  C  CG    . PHE A 1 78  ? -0.96400  -4.88000  8.51800   1.000 27.90071  ? 78   PHE A CG    1 
ATOM   599  C  CD1   . PHE A 1 78  ? 0.02000   -4.47400  7.62900   1.000 28.31129  ? 78   PHE A CD1   1 
ATOM   600  C  CD2   . PHE A 1 78  ? -0.89800  -4.43700  9.82900   1.000 27.67437  ? 78   PHE A CD2   1 
ATOM   601  C  CE1   . PHE A 1 78  ? 1.04700   -3.62700  8.03600   1.000 28.36919  ? 78   PHE A CE1   1 
ATOM   602  C  CE2   . PHE A 1 78  ? 0.12600   -3.59700  10.24400  1.000 30.41944  ? 78   PHE A CE2   1 
ATOM   603  C  CZ    . PHE A 1 78  ? 1.09900   -3.19100  9.34400   1.000 29.82200  ? 78   PHE A CZ    1 
ATOM   604  N  N     . PRO A 1 79  ? -0.39000  -7.73900  10.27400  1.000 25.57675  ? 79   PRO A N     1 
ATOM   605  C  CA    . PRO A 1 79  ? -0.18600  -8.23700  11.65700  1.000 27.15852  ? 79   PRO A CA    1 
ATOM   606  C  C     . PRO A 1 79  ? -0.47900  -7.22100  12.75800  1.000 30.02202  ? 79   PRO A C     1 
ATOM   607  O  O     . PRO A 1 79  ? 0.40800   -6.63600  13.38900  1.000 31.84329  ? 79   PRO A O     1 
ATOM   608  C  CB    . PRO A 1 79  ? 1.28800   -8.64900  11.64800  1.000 25.66887  ? 79   PRO A CB    1 
ATOM   609  C  CG    . PRO A 1 79  ? 1.92000   -7.68700  10.67200  1.000 23.36596  ? 79   PRO A CG    1 
ATOM   610  C  CD    . PRO A 1 79  ? 0.88800   -7.51100  9.57400   1.000 23.23173  ? 79   PRO A CD    1 
ATOM   611  N  N     . ALA A 1 80  ? -1.76800  -7.03200  13.02300  1.000 28.81924  ? 80   ALA A N     1 
ATOM   612  C  CA    . ALA A 1 80  ? -2.20200  -6.09300  14.05000  1.000 29.48248  ? 80   ALA A CA    1 
ATOM   613  C  C     . ALA A 1 80  ? -1.86700  -6.63400  15.43400  1.000 27.76649  ? 80   ALA A C     1 
ATOM   614  O  O     . ALA A 1 80  ? -2.13200  -7.80200  15.73800  1.000 28.47447  ? 80   ALA A O     1 
ATOM   615  C  CB    . ALA A 1 80  ? -3.70700  -5.86000  13.93900  1.000 31.76433  ? 80   ALA A CB    1 
ATOM   616  N  N     . THR A 1 81  ? -1.28400  -5.78000  16.27600  1.000 26.30579  ? 81   THR A N     1 
ATOM   617  C  CA    . THR A 1 81  ? -0.86900  -6.19700  17.60900  1.000 25.31883  ? 81   THR A CA    1 
ATOM   618  C  C     . THR A 1 81  ? -1.87400  -5.85000  18.70000  1.000 28.84030  ? 81   THR A C     1 
ATOM   619  O  O     . THR A 1 81  ? -1.70500  -6.31000  19.83300  1.000 29.87200  ? 81   THR A O     1 
ATOM   620  C  CB    . THR A 1 81  ? 0.50800   -5.62000  17.95600  1.000 26.71110  ? 81   THR A CB    1 
ATOM   621  O  OG1   . THR A 1 81  ? 0.50300   -4.20300  17.73900  1.000 29.24824  ? 81   THR A OG1   1 
ATOM   622  C  CG2   . THR A 1 81  ? 1.58400   -6.26400  17.09300  1.000 26.30842  ? 81   THR A CG2   1 
ATOM   623  N  N     . SER A 1 82  ? -2.90500  -5.06900  18.39000  1.000 31.33534  ? 82   SER A N     1 
ATOM   624  C  CA    . SER A 1 82  ? -3.93400  -4.71500  19.36000  1.000 33.81984  ? 82   SER A CA    1 
ATOM   625  C  C     . SER A 1 82  ? -5.18300  -4.30400  18.59200  1.000 35.61743  ? 82   SER A C     1 
ATOM   626  O  O     . SER A 1 82  ? -5.12300  -4.07000  17.37500  1.000 33.30136  ? 82   SER A O     1 
ATOM   627  C  CB    . SER A 1 82  ? -3.46300  -3.58600  20.29500  1.000 35.65164  ? 82   SER A CB    1 
ATOM   628  O  OG    . SER A 1 82  ? -3.55600  -2.31900  19.66800  1.000 37.24920  ? 82   SER A OG    1 
ATOM   629  N  N     . PRO A 1 83  ? -6.33500  -4.22000  19.26900  1.000 37.90981  ? 83   PRO A N     1 
ATOM   630  C  CA    . PRO A 1 83  ? -7.56900  -3.80000  18.58200  1.000 41.58657  ? 83   PRO A CA    1 
ATOM   631  C  C     . PRO A 1 83  ? -7.53000  -2.39200  18.00600  1.000 43.53154  ? 83   PRO A C     1 
ATOM   632  O  O     . PRO A 1 83  ? -8.41200  -2.06600  17.19900  1.000 45.31859  ? 83   PRO A O     1 
ATOM   633  C  CB    . PRO A 1 83  ? -8.64200  -3.92400  19.67200  1.000 42.16295  ? 83   PRO A CB    1 
ATOM   634  C  CG    . PRO A 1 83  ? -8.09600  -4.92400  20.62400  1.000 41.45760  ? 83   PRO A CG    1 
ATOM   635  C  CD    . PRO A 1 83  ? -6.61100  -4.72800  20.62500  1.000 40.49170  ? 83   PRO A CD    1 
ATOM   636  N  N     . ARG A 1 84  ? -6.56000  -1.55700  18.39500  1.000 47.22145  ? 84   ARG A N     1 
ATOM   637  C  CA    . ARG A 1 84  ? -6.45100  -0.21000  17.83500  1.000 50.38499  ? 84   ARG A CA    1 
ATOM   638  C  C     . ARG A 1 84  ? -6.48800  -0.23300  16.31300  1.000 56.94893  ? 84   ARG A C     1 
ATOM   639  O  O     . ARG A 1 84  ? -7.10800  0.63400   15.68500  1.000 56.30938  ? 84   ARG A O     1 
ATOM   640  C  CB    . ARG A 1 84  ? -5.15200  0.45300   18.30400  1.000 50.00336  ? 84   ARG A CB    1 
ATOM   641  C  CG    . ARG A 1 84  ? -4.79100  1.72200   17.52400  1.000 48.66636  ? 84   ARG A CG    1 
ATOM   642  C  CD    . ARG A 1 84  ? -3.45000  2.31700   17.93600  1.000 45.46598  ? 84   ARG A CD    1 
ATOM   643  N  NE    . ARG A 1 84  ? -3.21500  2.18400   19.36800  1.000 43.77630  ? 84   ARG A NE    1 
ATOM   644  C  CZ    . ARG A 1 84  ? -2.18200  1.54800   19.90000  1.000 42.44456  ? 84   ARG A CZ    1 
ATOM   645  N  NH1   . ARG A 1 84  ? -1.21400  1.04900   19.14900  1.000 41.59446  ? 84   ARG A NH1   1 
ATOM   646  N  NH2   . ARG A 1 84  ? -2.11400  1.41500   21.22100  1.000 42.79460  ? 84   ARG A NH2   1 
ATOM   647  N  N     . PHE A 1 85  ? -5.84000  -1.23000  15.70500  1.000 64.38930  ? 85   PHE A N     1 
ATOM   648  C  CA    . PHE A 1 85  ? -5.71100  -1.26600  14.25100  1.000 72.09549  ? 85   PHE A CA    1 
ATOM   649  C  C     . PHE A 1 85  ? -7.07100  -1.34600  13.56400  1.000 79.69113  ? 85   PHE A C     1 
ATOM   650  O  O     . PHE A 1 85  ? -7.34000  -0.60000  12.61600  1.000 83.44422  ? 85   PHE A O     1 
ATOM   651  C  CB    . PHE A 1 85  ? -4.81000  -2.42800  13.83200  1.000 72.10338  ? 85   PHE A CB    1 
ATOM   652  C  CG    . PHE A 1 85  ? -3.33900  -2.13100  13.95600  1.000 73.10087  ? 85   PHE A CG    1 
ATOM   653  C  CD1   . PHE A 1 85  ? -2.70200  -2.19900  15.18800  1.000 74.47998  ? 85   PHE A CD1   1 
ATOM   654  C  CD2   . PHE A 1 85  ? -2.59300  -1.78600  12.83800  1.000 72.35341  ? 85   PHE A CD2   1 
ATOM   655  C  CE1   . PHE A 1 85  ? -1.35000  -1.92400  15.30400  1.000 74.70106  ? 85   PHE A CE1   1 
ATOM   656  C  CE2   . PHE A 1 85  ? -1.24000  -1.51100  12.94700  1.000 73.53513  ? 85   PHE A CE2   1 
ATOM   657  C  CZ    . PHE A 1 85  ? -0.61700  -1.58100  14.18100  1.000 74.75633  ? 85   PHE A CZ    1 
ATOM   658  N  N     . GLU A 1 86  ? -7.95100  -2.23200  14.04200  1.000 81.49398  ? 86   GLU A N     1 
ATOM   659  C  CA    . GLU A 1 86  ? -9.23500  -2.46500  13.38400  1.000 82.69676  ? 86   GLU A CA    1 
ATOM   660  C  C     . GLU A 1 86  ? -10.08000 -1.20600  13.24700  1.000 84.18641  ? 86   GLU A C     1 
ATOM   661  O  O     . GLU A 1 86  ? -11.06700 -1.22200  12.50300  1.000 83.58371  ? 86   GLU A O     1 
ATOM   662  C  CB    . GLU A 1 86  ? -10.05900 -3.49100  14.16300  1.000 82.77045  ? 86   GLU A CB    1 
ATOM   663  C  CG    . GLU A 1 86  ? -9.27800  -4.66200  14.72100  1.000 84.76016  ? 86   GLU A CG    1 
ATOM   664  C  CD    . GLU A 1 86  ? -10.11200 -5.48800  15.68200  1.000 87.15519  ? 86   GLU A CD    1 
ATOM   665  O  OE1   . GLU A 1 86  ? -11.35500 -5.47700  15.54600  1.000 89.32387  ? 86   GLU A OE1   1 
ATOM   666  O  OE2   . GLU A 1 86  ? -9.53200  -6.13600  16.58000  1.000 87.03675  ? 86   GLU A OE2   1 
ATOM   667  N  N     . ALA A 1 87  ? -9.72000  -0.12200  13.93500  1.000 86.77093  ? 87   ALA A N     1 
ATOM   668  C  CA    . ALA A 1 87  ? -10.59300 1.04300   14.01800  1.000 89.71339  ? 87   ALA A CA    1 
ATOM   669  C  C     . ALA A 1 87  ? -10.55300 1.89500   12.75300  1.000 93.94284  ? 87   ALA A C     1 
ATOM   670  O  O     . ALA A 1 87  ? -11.60000 2.34900   12.27700  1.000 95.49040  ? 87   ALA A O     1 
ATOM   671  C  CB    . ALA A 1 87  ? -10.20500 1.88900   15.23000  1.000 87.96318  ? 87   ALA A CB    1 
ATOM   672  N  N     . VAL A 1 88  ? -9.36500  2.11400   12.19300  1.000 94.85874  ? 88   VAL A N     1 
ATOM   673  C  CA    . VAL A 1 88  ? -9.14700  3.18600   11.22600  1.000 95.13509  ? 88   VAL A CA    1 
ATOM   674  C  C     . VAL A 1 88  ? -9.36100  2.72900   9.78500   1.000 96.44841  ? 88   VAL A C     1 
ATOM   675  O  O     . VAL A 1 88  ? -8.78300  3.30000   8.85200   1.000 97.25377  ? 88   VAL A O     1 
ATOM   676  C  CB    . VAL A 1 88  ? -7.74800  3.80000   11.42300  1.000 93.84809  ? 88   VAL A CB    1 
ATOM   677  C  CG1   . VAL A 1 88  ? -7.58700  4.28500   12.85700  1.000 93.11380  ? 88   VAL A CG1   1 
ATOM   678  C  CG2   . VAL A 1 88  ? -6.66400  2.78200   11.08300  1.000 92.79007  ? 88   VAL A CG2   1 
ATOM   679  N  N     . ARG A 1 89  ? -10.21500 1.72200   9.58800   1.000 96.10100  ? 89   ARG A N     1 
ATOM   680  C  CA    . ARG A 1 89  ? -10.38300 1.13800   8.25900   1.000 95.16667  ? 89   ARG A CA    1 
ATOM   681  C  C     . ARG A 1 89  ? -10.97000 2.13800   7.26700   1.000 94.19814  ? 89   ARG A C     1 
ATOM   682  O  O     . ARG A 1 89  ? -10.48700 2.25700   6.13500   1.000 94.44290  ? 89   ARG A O     1 
ATOM   683  C  CB    . ARG A 1 89  ? -11.27200 -0.10200  8.33800   1.000 94.94033  ? 89   ARG A CB    1 
ATOM   684  C  CG    . ARG A 1 89  ? -11.60000 -0.70400  6.98200   1.000 94.75610  ? 89   ARG A CG    1 
ATOM   685  C  CD    . ARG A 1 89  ? -10.64400 -1.83100  6.62800   1.000 94.24288  ? 89   ARG A CD    1 
ATOM   686  N  NE    . ARG A 1 89  ? -10.63900 -2.12400  5.19900   1.000 93.22697  ? 89   ARG A NE    1 
ATOM   687  C  CZ    . ARG A 1 89  ? -10.18900 -3.25200  4.66700   1.000 91.88470  ? 89   ARG A CZ    1 
ATOM   688  N  NH1   . ARG A 1 89  ? -9.73800  -4.24100  5.42200   1.000 91.28200  ? 89   ARG A NH1   1 
ATOM   689  N  NH2   . ARG A 1 89  ? -10.19700 -3.39400  3.34300   1.000 91.37938  ? 89   ARG A NH2   1 
ATOM   690  N  N     . GLU A 1 90  ? -12.01200 2.86600   7.67500   1.000 92.95062  ? 90   GLU A N     1 
ATOM   691  C  CA    . GLU A 1 90  ? -12.77900 3.69400   6.74700   1.000 90.98459  ? 90   GLU A CA    1 
ATOM   692  C  C     . GLU A 1 90  ? -11.95600 4.82400   6.13500   1.000 86.00242  ? 90   GLU A C     1 
ATOM   693  O  O     . GLU A 1 90  ? -12.28900 5.29300   5.04100   1.000 85.87345  ? 90   GLU A O     1 
ATOM   694  C  CB    . GLU A 1 90  ? -14.00500 4.25800   7.47000   1.000 92.67690  ? 90   GLU A CB    1 
ATOM   695  C  CG    . GLU A 1 90  ? -15.08000 4.84400   6.56600   1.000 93.88757  ? 90   GLU A CG    1 
ATOM   696  C  CD    . GLU A 1 90  ? -16.39100 5.06700   7.30000   1.000 94.88243  ? 90   GLU A CD    1 
ATOM   697  O  OE1   . GLU A 1 90  ? -16.64900 4.34300   8.28600   1.000 96.08257  ? 90   GLU A OE1   1 
ATOM   698  O  OE2   . GLU A 1 90  ? -17.15900 5.96600   6.89800   1.000 94.20866  ? 90   GLU A OE2   1 
ATOM   699  N  N     . SER A 1 91  ? -10.88700 5.26100   6.80300   1.000 80.11750  ? 91   SER A N     1 
ATOM   700  C  CA    . SER A 1 91  ? -10.09400 6.41800   6.40200   1.000 72.85347  ? 91   SER A CA    1 
ATOM   701  C  C     . SER A 1 91  ? -8.98300  5.99900   5.44600   1.000 65.61839  ? 91   SER A C     1 
ATOM   702  O  O     . SER A 1 91  ? -8.38200  4.93400   5.62200   1.000 64.25770  ? 91   SER A O     1 
ATOM   703  C  CB    . SER A 1 91  ? -9.45300  7.06000   7.62400   1.000 73.27194  ? 91   SER A CB    1 
ATOM   704  O  OG    . SER A 1 91  ? -10.40100 7.24700   8.65800   1.000 74.66685  ? 91   SER A OG    1 
ATOM   705  N  N     . PRO A 1 92  ? -8.68600  6.82400   4.44200   1.000 59.21763  ? 92   PRO A N     1 
ATOM   706  C  CA    . PRO A 1 92  ? -7.53600  6.53300   3.58100   1.000 52.19047  ? 92   PRO A CA    1 
ATOM   707  C  C     . PRO A 1 92  ? -6.25700  6.59300   4.39500   1.000 43.13412  ? 92   PRO A C     1 
ATOM   708  O  O     . PRO A 1 92  ? -6.11900  7.39800   5.31700   1.000 43.18413  ? 92   PRO A O     1 
ATOM   709  C  CB    . PRO A 1 92  ? -7.58600  7.64800   2.52900   1.000 56.08304  ? 92   PRO A CB    1 
ATOM   710  C  CG    . PRO A 1 92  ? -8.29200  8.76600   3.20800   1.000 58.65440  ? 92   PRO A CG    1 
ATOM   711  C  CD    . PRO A 1 92  ? -9.32300  8.10700   4.09700   1.000 59.63610  ? 92   PRO A CD    1 
ATOM   712  N  N     . GLN A 1 93  ? -5.32300  5.72100   4.05800   1.000 36.01484  ? 93   GLN A N     1 
ATOM   713  C  CA    A GLN A 1 93  ? -4.08600  5.65500   4.81100   0.640 31.25112  ? 93   GLN A CA    1 
ATOM   714  C  CA    B GLN A 1 93  ? -4.07300  5.64200   4.79500   0.360 32.85657  ? 93   GLN A CA    1 
ATOM   715  C  C     . GLN A 1 93  ? -3.18100  6.83100   4.46500   1.000 30.70105  ? 93   GLN A C     1 
ATOM   716  O  O     . GLN A 1 93  ? -3.23000  7.38200   3.36200   1.000 33.71720  ? 93   GLN A O     1 
ATOM   717  C  CB    A GLN A 1 93  ? -3.36000  4.35000   4.50000   0.640 32.08806  ? 93   GLN A CB    1 
ATOM   718  C  CB    B GLN A 1 93  ? -3.33400  4.36000   4.41600   0.360 34.01197  ? 93   GLN A CB    1 
ATOM   719  C  CG    A GLN A 1 93  ? -4.16800  3.10900   4.80400   0.640 33.03554  ? 93   GLN A CG    1 
ATOM   720  C  CG    B GLN A 1 93  ? -4.09100  3.09400   4.74400   0.360 35.42793  ? 93   GLN A CG    1 
ATOM   721  C  CD    A GLN A 1 93  ? -3.38600  1.84400   4.52200   0.640 30.73526  ? 93   GLN A CD    1 
ATOM   722  C  CD    B GLN A 1 93  ? -4.23500  2.88500   6.23300   0.360 36.18065  ? 93   GLN A CD    1 
ATOM   723  O  OE1   A GLN A 1 93  ? -2.57600  1.40500   5.33900   0.640 30.52734  ? 93   GLN A OE1   1 
ATOM   724  O  OE1   B GLN A 1 93  ? -5.34400  2.74100   6.74600   0.360 36.74125  ? 93   GLN A OE1   1 
ATOM   725  N  NE2   A GLN A 1 93  ? -3.61100  1.25900   3.35000   0.640 33.64877  ? 93   GLN A NE2   1 
ATOM   726  N  NE2   B GLN A 1 93  ? -3.10900  2.86700   6.94000   0.360 36.71756  ? 93   GLN A NE2   1 
ATOM   727  N  N     . ALA A 1 94  ? -2.36300  7.22800   5.43700   1.000 26.71110  ? 94   ALA A N     1 
ATOM   728  C  CA    . ALA A 1 94  ? -1.24900  8.10500   5.12700   1.000 26.45844  ? 94   ALA A CA    1 
ATOM   729  C  C     . ALA A 1 94  ? -0.15200  7.27200   4.46700   1.000 24.55294  ? 94   ALA A C     1 
ATOM   730  O  O     . ALA A 1 94  ? -0.25400  6.04200   4.36100   1.000 24.92667  ? 94   ALA A O     1 
ATOM   731  C  CB    . ALA A 1 94  ? -0.73900  8.80700   6.38500   1.000 27.23221  ? 94   ALA A CB    1 
ATOM   732  N  N     . PHE A 1 95  ? 0.90900   7.94200   4.00400   1.000 22.96854  ? 95   PHE A N     1 
ATOM   733  C  CA    . PHE A 1 95  ? 1.87600   7.22800   3.17100   1.000 21.27887  ? 95   PHE A CA    1 
ATOM   734  C  C     . PHE A 1 95  ? 2.63500   6.13900   3.92100   1.000 20.26559  ? 95   PHE A C     1 
ATOM   735  O  O     . PHE A 1 95  ? 3.19900   5.25000   3.27500   1.000 21.34203  ? 95   PHE A O     1 
ATOM   736  C  CB    . PHE A 1 95  ? 2.79300   8.16500   2.37000   1.000 23.23173  ? 95   PHE A CB    1 
ATOM   737  C  CG    . PHE A 1 95  ? 3.60500   9.11200   3.19900   1.000 21.08674  ? 95   PHE A CG    1 
ATOM   738  C  CD1   . PHE A 1 95  ? 4.80800   8.71300   3.76800   1.000 21.25781  ? 95   PHE A CD1   1 
ATOM   739  C  CD2   . PHE A 1 95  ? 3.18400   10.42500  3.37300   1.000 22.83432  ? 95   PHE A CD2   1 
ATOM   740  C  CE1   . PHE A 1 95  ? 5.56800   9.60200   4.50900   1.000 20.51825  ? 95   PHE A CE1   1 
ATOM   741  C  CE2   . PHE A 1 95  ? 3.93100   11.32200  4.11800   1.000 22.41321  ? 95   PHE A CE2   1 
ATOM   742  C  CZ    . PHE A 1 95  ? 5.12600   10.91700  4.68300   1.000 21.88947  ? 95   PHE A CZ    1 
ATOM   743  N  N     . ILE A 1 96  ? 2.63500   6.16400   5.25700   1.000 20.96567  ? 96   ILE A N     1 
ATOM   744  C  CA    . ILE A 1 96  ? 3.24900   5.08300   6.02200   1.000 19.33916  ? 96   ILE A CA    1 
ATOM   745  C  C     . ILE A 1 96  ? 2.57500   3.74100   5.74000   1.000 19.41812  ? 96   ILE A C     1 
ATOM   746  O  O     . ILE A 1 96  ? 3.20000   2.69200   5.91100   1.000 20.47877  ? 96   ILE A O     1 
ATOM   747  C  CB    . ILE A 1 96  ? 3.26800   5.44100   7.52700   1.000 19.38127  ? 96   ILE A CB    1 
ATOM   748  C  CG1   . ILE A 1 96  ? 4.17900   4.50100   8.31800   1.000 18.88647  ? 96   ILE A CG1   1 
ATOM   749  C  CG2   . ILE A 1 96  ? 1.84500   5.47100   8.10500   1.000 18.57591  ? 96   ILE A CG2   1 
ATOM   750  C  CD1   . ILE A 1 96  ? 4.36400   4.96700   9.76100   1.000 19.76816  ? 96   ILE A CD1   1 
ATOM   751  N  N     . GLY A 1 97  ? 1.31600   3.75200   5.29700   1.000 19.34706  ? 97   GLY A N     1 
ATOM   752  C  CA    . GLY A 1 97  ? 0.57400   2.56500   4.92800   1.000 19.86028  ? 97   GLY A CA    1 
ATOM   753  C  C     . GLY A 1 97  ? 0.47700   2.31700   3.43800   1.000 21.06832  ? 97   GLY A C     1 
ATOM   754  O  O     . GLY A 1 97  ? -0.29200  1.44100   3.01700   1.000 25.92942  ? 97   GLY A O     1 
ATOM   755  N  N     . LEU A 1 98  ? 1.22900   3.05100   2.62300   1.000 21.85525  ? 98   LEU A N     1 
ATOM   756  C  CA    . LEU A 1 98  ? 1.20400   2.88100   1.17700   1.000 21.25255  ? 98   LEU A CA    1 
ATOM   757  C  C     . LEU A 1 98  ? 2.45300   2.14700   0.70900   1.000 21.31045  ? 98   LEU A C     1 
ATOM   758  O  O     . LEU A 1 98  ? 3.47800   2.11400   1.39400   1.000 22.70009  ? 98   LEU A O     1 
ATOM   759  C  CB    . LEU A 1 98  ? 1.11800   4.24000   0.47600   1.000 22.99749  ? 98   LEU A CB    1 
ATOM   760  C  CG    . LEU A 1 98  ? -0.15100  5.05200   0.75600   1.000 21.74998  ? 98   LEU A CG    1 
ATOM   761  C  CD1   . LEU A 1 98  ? -0.10400  6.39500   0.04500   1.000 22.88432  ? 98   LEU A CD1   1 
ATOM   762  C  CD2   . LEU A 1 98  ? -1.38600  4.26100   0.35700   1.000 23.78969  ? 98   LEU A CD2   1 
ATOM   763  N  N     . ASP A 1 99  ? 2.34300   1.53500   -0.46300  1.000 23.10277  ? 99   ASP A N     1 
ATOM   764  C  CA    . ASP A 1 99  ? 3.46000   0.91300   -1.14900  1.000 23.15278  ? 99   ASP A CA    1 
ATOM   765  C  C     . ASP A 1 99  ? 3.79100   1.69900   -2.41300  1.000 25.85310  ? 99   ASP A C     1 
ATOM   766  O  O     . ASP A 1 99  ? 2.96300   2.47000   -2.90900  1.000 24.48188  ? 99   ASP A O     1 
ATOM   767  C  CB    . ASP A 1 99  ? 3.09400   -0.52400  -1.55200  1.000 23.86076  ? 99   ASP A CB    1 
ATOM   768  C  CG    . ASP A 1 99  ? 2.83700   -1.41900  -0.35900  1.000 23.64494  ? 99   ASP A CG    1 
ATOM   769  O  OD1   . ASP A 1 99  ? 3.51000   -1.24700  0.68200   1.000 24.28712  ? 99   ASP A OD1   1 
ATOM   770  O  OD2   . ASP A 1 99  ? 1.95800   -2.29600  -0.46300  1.000 27.69279  ? 99   ASP A OD2   1 
ATOM   771  N  N     . PRO A 1 100 ? 5.00300   1.54800   -2.94800  1.000 27.51119  ? 100  PRO A N     1 
ATOM   772  C  CA    . PRO A 1 100 ? 5.31200   2.12700   -4.25900  1.000 29.41932  ? 100  PRO A CA    1 
ATOM   773  C  C     . PRO A 1 100 ? 4.32400   1.62100   -5.29300  1.000 31.91172  ? 100  PRO A C     1 
ATOM   774  O  O     . PRO A 1 100 ? 3.91500   0.45100   -5.24300  1.000 36.01221  ? 100  PRO A O     1 
ATOM   775  C  CB    . PRO A 1 100 ? 6.73000   1.60100   -4.53900  1.000 30.03781  ? 100  PRO A CB    1 
ATOM   776  C  CG    . PRO A 1 100 ? 7.31800   1.41700   -3.16600  1.000 31.20901  ? 100  PRO A CG    1 
ATOM   777  C  CD    . PRO A 1 100 ? 6.18000   0.89800   -2.33800  1.000 30.02992  ? 100  PRO A CD    1 
ATOM   778  N  N     . PRO A 1 101 ? 3.90400   2.47000   -6.24400  1.000 29.47195  ? 101  PRO A N     1 
ATOM   779  C  CA    . PRO A 1 101 ? 4.36500   3.84100   -6.51000  1.000 29.47722  ? 101  PRO A CA    1 
ATOM   780  C  C     . PRO A 1 101 ? 3.62500   4.91700   -5.71800  1.000 27.40592  ? 101  PRO A C     1 
ATOM   781  O  O     . PRO A 1 101 ? 4.06100   6.06400   -5.66800  1.000 27.77965  ? 101  PRO A O     1 
ATOM   782  C  CB    . PRO A 1 101 ? 4.04700   4.00100   -7.99900  1.000 32.04595  ? 101  PRO A CB    1 
ATOM   783  C  CG    . PRO A 1 101 ? 2.75400   3.23400   -8.15800  1.000 31.69591  ? 101  PRO A CG    1 
ATOM   784  C  CD    . PRO A 1 101 ? 2.89600   2.04000   -7.23500  1.000 32.83288  ? 101  PRO A CD    1 
ATOM   785  N  N     . GLU A 1 102 ? 2.48800   4.58900   -5.10600  1.000 28.55079  ? 102  GLU A N     1 
ATOM   786  C  CA    . GLU A 1 102 ? 1.71400   5.61300   -4.41600  1.000 27.50330  ? 102  GLU A CA    1 
ATOM   787  C  C     . GLU A 1 102 ? 2.48100   6.18100   -3.22900  1.000 25.26882  ? 102  GLU A C     1 
ATOM   788  O  O     . GLU A 1 102 ? 2.37800   7.37900   -2.93600  1.000 27.53488  ? 102  GLU A O     1 
ATOM   789  C  CB    . GLU A 1 102 ? 0.36000   5.04700   -3.97700  1.000 29.16402  ? 102  GLU A CB    1 
ATOM   790  C  CG    . GLU A 1 102 ? -0.54700  4.61000   -5.12800  1.000 32.05384  ? 102  GLU A CG    1 
ATOM   791  C  CD    . GLU A 1 102 ? -0.18500  3.24200   -5.68200  1.000 38.88624  ? 102  GLU A CD    1 
ATOM   792  O  OE1   . GLU A 1 102 ? 0.41100   2.43000   -4.93400  1.000 40.99176  ? 102  GLU A OE1   1 
ATOM   793  O  OE2   . GLU A 1 102 ? -0.49500  2.98300   -6.86700  1.000 42.64722  ? 102  GLU A OE2   1 
ATOM   794  N  N     . HIS A 1 103 ? 3.26200   5.34600   -2.54700  1.000 23.03434  ? 103  HIS A N     1 
ATOM   795  C  CA    . HIS A 1 103 ? 4.02100   5.81500   -1.39400  1.000 22.16845  ? 103  HIS A CA    1 
ATOM   796  C  C     . HIS A 1 103 ? 4.89000   7.01300   -1.75100  1.000 19.52076  ? 103  HIS A C     1 
ATOM   797  O  O     . HIS A 1 103 ? 4.87500   8.03800   -1.05800  1.000 20.63932  ? 103  HIS A O     1 
ATOM   798  C  CB    . HIS A 1 103 ? 4.89000   4.68800   -0.84800  1.000 22.30004  ? 103  HIS A CB    1 
ATOM   799  C  CG    . HIS A 1 103 ? 5.93200   5.16200   0.10700   1.000 21.48415  ? 103  HIS A CG    1 
ATOM   800  N  ND1   . HIS A 1 103 ? 7.27000   5.22400   -0.21600  1.000 22.42637  ? 103  HIS A ND1   1 
ATOM   801  C  CD2   . HIS A 1 103 ? 5.82300   5.64000   1.36800   1.000 22.15002  ? 103  HIS A CD2   1 
ATOM   802  C  CE1   . HIS A 1 103 ? 7.94600   5.69700   0.81800   1.000 23.49492  ? 103  HIS A CE1   1 
ATOM   803  N  NE2   . HIS A 1 103 ? 7.09100   5.95700   1.79100   1.000 22.21845  ? 103  HIS A NE2   1 
ATOM   804  N  N     . GLY A 1 104 ? 5.65700   6.89900   -2.83500  1.000 21.77630  ? 104  GLY A N     1 
ATOM   805  C  CA    . GLY A 1 104 ? 6.58300   7.96100   -3.19200  1.000 22.30004  ? 104  GLY A CA    1 
ATOM   806  C  C     . GLY A 1 104 ? 5.89500   9.25100   -3.59700  1.000 21.16833  ? 104  GLY A C     1 
ATOM   807  O  O     . GLY A 1 104 ? 6.35800   10.34300  -3.24700  1.000 23.90023  ? 104  GLY A O     1 
ATOM   808  N  N     . THR A 1 105 ? 4.77700   9.15300   -4.32600  1.000 21.55258  ? 105  THR A N     1 
ATOM   809  C  CA    . THR A 1 105 ? 4.09100   10.37300  -4.74900  1.000 23.50808  ? 105  THR A CA    1 
ATOM   810  C  C     . THR A 1 105 ? 3.56800   11.16700  -3.55900  1.000 24.52136  ? 105  THR A C     1 
ATOM   811  O  O     . THR A 1 105 ? 3.54500   12.40200  -3.60100  1.000 24.88193  ? 105  THR A O     1 
ATOM   812  C  CB    . THR A 1 105 ? 2.95500   10.07700  -5.73400  1.000 26.50581  ? 105  THR A CB    1 
ATOM   813  O  OG1   . THR A 1 105 ? 1.85100   9.47900   -5.04400  1.000 27.59015  ? 105  THR A OG1   1 
ATOM   814  C  CG2   . THR A 1 105 ? 3.42500   9.16100   -6.85800  1.000 27.82965  ? 105  THR A CG2   1 
ATOM   815  N  N     . ARG A 1 106 ? 3.13700   10.48600  -2.49300  1.000 21.41309  ? 106  ARG A N     1 
ATOM   816  C  CA    . ARG A 1 106 ? 2.67900   11.20700  -1.30900  1.000 21.11306  ? 106  ARG A CA    1 
ATOM   817  C  C     . ARG A 1 106 ? 3.84200   11.65500  -0.43300  1.000 20.26032  ? 106  ARG A C     1 
ATOM   818  O  O     . ARG A 1 106 ? 3.86000   12.79700  0.04000   1.000 21.71839  ? 106  ARG A O     1 
ATOM   819  C  CB    . ARG A 1 106 ? 1.67800   10.37200  -0.50800  1.000 23.77653  ? 106  ARG A CB    1 
ATOM   820  C  CG    . ARG A 1 106 ? 0.23000   10.57300  -0.93300  1.000 28.44025  ? 106  ARG A CG    1 
ATOM   821  C  CD    . ARG A 1 106 ? -0.17300  9.67900   -2.07200  1.000 31.05636  ? 106  ARG A CD    1 
ATOM   822  N  NE    . ARG A 1 106 ? -1.48500  10.06600  -2.57900  1.000 28.22180  ? 106  ARG A NE    1 
ATOM   823  C  CZ    . ARG A 1 106 ? -1.68800  10.75400  -3.69400  1.000 25.36094  ? 106  ARG A CZ    1 
ATOM   824  N  NH1   . ARG A 1 106 ? -0.68400  11.12000  -4.47600  1.000 24.12131  ? 106  ARG A NH1   1 
ATOM   825  N  NH2   . ARG A 1 106 ? -2.93000  11.07000  -4.03900  1.000 23.46334  ? 106  ARG A NH2   1 
ATOM   826  N  N     . ARG A 1 107 ? 4.81600   10.77100  -0.18800  1.000 18.49432  ? 107  ARG A N     1 
ATOM   827  C  CA    . ARG A 1 107 ? 5.96000   11.15400  0.63300   1.000 18.30219  ? 107  ARG A CA    1 
ATOM   828  C  C     . ARG A 1 107 ? 6.66800   12.37100  0.04800   1.000 20.16031  ? 107  ARG A C     1 
ATOM   829  O  O     . ARG A 1 107 ? 7.03700   13.29200  0.78400   1.000 21.36309  ? 107  ARG A O     1 
ATOM   830  C  CB    . ARG A 1 107 ? 6.92100   9.97600   0.80800   1.000 20.43666  ? 107  ARG A CB    1 
ATOM   831  C  CG    . ARG A 1 107 ? 8.20500   10.32100  1.57700   1.000 21.03410  ? 107  ARG A CG    1 
ATOM   832  C  CD    . ARG A 1 107 ? 9.01300   9.08500   1.95500   1.000 21.87368  ? 107  ARG A CD    1 
ATOM   833  N  NE    . ARG A 1 107 ? 10.34800  9.42100   2.42600   1.000 22.90538  ? 107  ARG A NE    1 
ATOM   834  C  CZ    . ARG A 1 107 ? 10.87800  9.03200   3.58300   1.000 24.06078  ? 107  ARG A CZ    1 
ATOM   835  N  NH1   . ARG A 1 107 ? 10.19900  8.29100   4.44800   1.000 20.83145  ? 107  ARG A NH1   1 
ATOM   836  N  NH2   . ARG A 1 107 ? 12.12200  9.39700   3.88300   1.000 29.07191  ? 107  ARG A NH2   1 
ATOM   837  N  N     . ARG A 1 108 ? 6.83300   12.41200  -1.28100  1.000 20.41824  ? 108  ARG A N     1 
ATOM   838  C  CA    . ARG A 1 108 ? 7.53800   13.53500  -1.88800  1.000 23.07382  ? 108  ARG A CA    1 
ATOM   839  C  C     . ARG A 1 108 ? 6.79600   14.85300  -1.71600  1.000 23.05540  ? 108  ARG A C     1 
ATOM   840  O  O     . ARG A 1 108 ? 7.40700   15.91500  -1.87500  1.000 25.29251  ? 108  ARG A O     1 
ATOM   841  C  CB    . ARG A 1 108 ? 7.82800   13.27700  -3.36900  1.000 28.31655  ? 108  ARG A CB    1 
ATOM   842  C  CG    . ARG A 1 108 ? 8.97200   12.30600  -3.61400  1.000 35.79377  ? 108  ARG A CG    1 
ATOM   843  C  CD    . ARG A 1 108 ? 9.35300   12.21500  -5.08900  1.000 40.92070  ? 108  ARG A CD    1 
ATOM   844  N  NE    . ARG A 1 108 ? 8.28200   11.66900  -5.91600  1.000 43.88421  ? 108  ARG A NE    1 
ATOM   845  C  CZ    . ARG A 1 108 ? 8.07400   10.37300  -6.10900  1.000 45.32122  ? 108  ARG A CZ    1 
ATOM   846  N  NH1   . ARG A 1 108 ? 8.83600   9.45800   -5.53200  1.000 47.20303  ? 108  ARG A NH1   1 
ATOM   847  N  NH2   . ARG A 1 108 ? 7.08100   9.98600   -6.90400  1.000 44.23951  ? 108  ARG A NH2   1 
ATOM   848  N  N     . MET A 1 109 ? 5.50300   14.81900  -1.39000  1.000 19.45760  ? 109  MET A N     1 
ATOM   849  C  CA    . MET A 1 109 ? 4.79900   16.06300  -1.10600  1.000 17.75213  ? 109  MET A CA    1 
ATOM   850  C  C     . MET A 1 109 ? 5.23400   16.69400  0.20400   1.000 18.69171  ? 109  MET A C     1 
ATOM   851  O  O     . MET A 1 109 ? 4.91300   17.86600  0.44100   1.000 21.39467  ? 109  MET A O     1 
ATOM   852  C  CB    . MET A 1 109 ? 3.29900   15.81200  -1.05200  1.000 20.96041  ? 109  MET A CB    1 
ATOM   853  C  CG    . MET A 1 109 ? 2.74100   15.29500  -2.36600  1.000 21.20781  ? 109  MET A CG    1 
ATOM   854  S  SD    . MET A 1 109 ? 0.98700   14.96900  -2.20700  1.000 22.76062  ? 109  MET A SD    1 
ATOM   855  C  CE    . MET A 1 109 ? 0.59900   14.31700  -3.84200  1.000 24.52662  ? 109  MET A CE    1 
ATOM   856  N  N     . THR A 1 110 ? 5.94100   15.95200  1.06000   1.000 19.04965  ? 110  THR A N     1 
ATOM   857  C  CA    . THR A 1 110 ? 6.32200   16.45200  2.37000   1.000 17.82319  ? 110  THR A CA    1 
ATOM   858  C  C     . THR A 1 110 ? 7.82600   16.57400  2.58400   1.000 18.48380  ? 110  THR A C     1 
ATOM   859  O  O     . THR A 1 110 ? 8.23500   17.20000  3.56900   1.000 18.65487  ? 110  THR A O     1 
ATOM   860  C  CB    . THR A 1 110 ? 5.75400   15.55700  3.48500   1.000 18.16270  ? 110  THR A CB    1 
ATOM   861  O  OG1   . THR A 1 110 ? 6.46300   14.31600  3.50600   1.000 20.23664  ? 110  THR A OG1   1 
ATOM   862  C  CG2   . THR A 1 110 ? 4.27700   15.26600  3.26200   1.000 19.56287  ? 110  THR A CG2   1 
ATOM   863  N  N     . ILE A 1 111 ? 8.65800   16.00500  1.70300   1.000 20.30243  ? 111  ILE A N     1 
ATOM   864  C  CA    . ILE A 1 111 ? 10.09100  15.87500  1.98900   1.000 20.18663  ? 111  ILE A CA    1 
ATOM   865  C  C     . ILE A 1 111 ? 10.77500  17.22400  2.10300   1.000 21.32098  ? 111  ILE A C     1 
ATOM   866  O  O     . ILE A 1 111 ? 11.78800  17.35100  2.80000   1.000 22.68693  ? 111  ILE A O     1 
ATOM   867  C  CB    . ILE A 1 111 ? 10.81100  15.00100  0.94500   1.000 25.23460  ? 111  ILE A CB    1 
ATOM   868  C  CG1   . ILE A 1 111 ? 10.64100  15.61000  -0.45400  1.000 28.25339  ? 111  ILE A CG1   1 
ATOM   869  C  CG2   . ILE A 1 111 ? 10.32500  13.58000  1.03300   1.000 26.95586  ? 111  ILE A CG2   1 
ATOM   870  C  CD1   . ILE A 1 111 ? 11.64600  15.14400  -1.47200  1.000 31.17216  ? 111  ILE A CD1   1 
ATOM   871  N  N     . SER A 1 112 ? 10.26800  18.24100  1.40200   1.000 22.78694  ? 112  SER A N     1 
ATOM   872  C  CA    . SER A 1 112 ? 10.95200  19.52700  1.36300   1.000 23.46597  ? 112  SER A CA    1 
ATOM   873  C  C     . SER A 1 112 ? 11.02100  20.18700  2.72800   1.000 22.76589  ? 112  SER A C     1 
ATOM   874  O  O     . SER A 1 112 ? 11.88900  21.03400  2.94700   1.000 24.95299  ? 112  SER A O     1 
ATOM   875  C  CB    . SER A 1 112 ? 10.26800  20.46600  0.37100   1.000 30.20889  ? 112  SER A CB    1 
ATOM   876  O  OG    . SER A 1 112 ? 8.98400   20.84300  0.83600   1.000 33.12766  ? 112  SER A OG    1 
ATOM   877  N  N     . GLU A 1 113 ? 10.14800  19.80800  3.65700   1.000 20.42877  ? 113  GLU A N     1 
ATOM   878  C  CA    A GLU A 1 113 ? 10.15400  20.37300  4.99900   0.510 19.33916  ? 113  GLU A CA    1 
ATOM   879  C  CA    B GLU A 1 113 ? 10.19700  20.41400  4.97600   0.490 20.50246  ? 113  GLU A CA    1 
ATOM   880  C  C     . GLU A 1 113 ? 11.19900  19.73800  5.90200   1.000 19.48392  ? 113  GLU A C     1 
ATOM   881  O  O     . GLU A 1 113 ? 11.43000  20.23500  7.00400   1.000 21.31308  ? 113  GLU A O     1 
ATOM   882  C  CB    A GLU A 1 113 ? 8.78400   20.17600  5.65200   0.510 20.21558  ? 113  GLU A CB    1 
ATOM   883  C  CB    B GLU A 1 113 ? 8.79800   20.44600  5.59800   0.490 23.32648  ? 113  GLU A CB    1 
ATOM   884  C  CG    A GLU A 1 113 ? 7.62700   20.79100  4.89400   0.510 22.57113  ? 113  GLU A CG    1 
ATOM   885  C  CG    B GLU A 1 113 ? 7.78100   21.16900  4.72600   0.490 27.34012  ? 113  GLU A CG    1 
ATOM   886  C  CD    A GLU A 1 113 ? 7.48400   22.27700  5.14100   0.510 23.76601  ? 113  GLU A CD    1 
ATOM   887  C  CD    B GLU A 1 113 ? 8.24900   22.55400  4.31500   0.490 32.25650  ? 113  GLU A CD    1 
ATOM   888  O  OE1   A GLU A 1 113 ? 8.22000   22.81900  5.99700   0.510 24.11342  ? 113  GLU A OE1   1 
ATOM   889  O  OE1   B GLU A 1 113 ? 8.45400   23.39900  5.20900   0.490 34.52519  ? 113  GLU A OE1   1 
ATOM   890  O  OE2   A GLU A 1 113 ? 6.62500   22.89900  4.47900   0.510 25.28461  ? 113  GLU A OE2   1 
ATOM   891  O  OE2   B GLU A 1 113 ? 8.42200   22.79400  3.09800   0.490 34.74890  ? 113  GLU A OE2   1 
ATOM   892  N  N     . PHE A 1 114 ? 11.82400  18.64600  5.46900   1.000 17.61001  ? 114  PHE A N     1 
ATOM   893  C  CA    . PHE A 1 114 ? 12.71000  17.86400  6.32000   1.000 18.08112  ? 114  PHE A CA    1 
ATOM   894  C  C     . PHE A 1 114 ? 14.12500  17.74700  5.76600   1.000 18.62329  ? 114  PHE A C     1 
ATOM   895  O  O     . PHE A 1 114 ? 14.90600  16.92900  6.27100   1.000 21.96842  ? 114  PHE A O     1 
ATOM   896  C  CB    . PHE A 1 114 ? 12.09800  16.47900  6.56700   1.000 18.19692  ? 114  PHE A CB    1 
ATOM   897  C  CG    . PHE A 1 114 ? 10.79800  16.52500  7.31400   1.000 18.26008  ? 114  PHE A CG    1 
ATOM   898  C  CD1   . PHE A 1 114 ? 10.78700  16.51200  8.70600   1.000 19.44444  ? 114  PHE A CD1   1 
ATOM   899  C  CD2   . PHE A 1 114 ? 9.58400   16.60800  6.63600   1.000 17.67054  ? 114  PHE A CD2   1 
ATOM   900  C  CE1   . PHE A 1 114 ? 9.59500   16.58100  9.41300   1.000 18.77067  ? 114  PHE A CE1   1 
ATOM   901  C  CE2   . PHE A 1 114 ? 8.38700   16.67600  7.34000   1.000 18.89700  ? 114  PHE A CE2   1 
ATOM   902  C  CZ    . PHE A 1 114 ? 8.39200   16.65500  8.73200   1.000 18.30219  ? 114  PHE A CZ    1 
ATOM   903  N  N     . THR A 1 115 ? 14.47700  18.53600  4.74500   1.000 19.05228  ? 115  THR A N     1 
ATOM   904  C  CA    . THR A 1 115 ? 15.82400  18.49000  4.18700   1.000 20.82618  ? 115  THR A CA    1 
ATOM   905  C  C     . THR A 1 115 ? 16.84000  18.91900  5.23700   1.000 20.54983  ? 115  THR A C     1 
ATOM   906  O  O     . THR A 1 115 ? 16.52400  19.64000  6.18400   1.000 20.79723  ? 115  THR A O     1 
ATOM   907  C  CB    . THR A 1 115 ? 15.97900  19.47100  3.02000   1.000 22.86327  ? 115  THR A CB    1 
ATOM   908  O  OG1   . THR A 1 115 ? 15.86200  20.81200  3.50900   1.000 24.65559  ? 115  THR A OG1   1 
ATOM   909  C  CG2   . THR A 1 115 ? 14.94300  19.23000  1.92800   1.000 21.86578  ? 115  THR A CG2   1 
ATOM   910  N  N     . VAL A 1 116 ? 18.08900  18.49300  5.04200   1.000 20.76302  ? 116  VAL A N     1 
ATOM   911  C  CA    . VAL A 1 116 ? 19.15000  18.92400  5.95400   1.000 22.43164  ? 116  VAL A CA    1 
ATOM   912  C  C     . VAL A 1 116 ? 19.21300  20.44600  6.04400   1.000 25.12406  ? 116  VAL A C     1 
ATOM   913  O  O     . VAL A 1 116 ? 19.44000  21.01000  7.12200   1.000 23.71863  ? 116  VAL A O     1 
ATOM   914  C  CB    . VAL A 1 116 ? 20.49900  18.29600  5.56200   1.000 26.52160  ? 116  VAL A CB    1 
ATOM   915  C  CG1   . VAL A 1 116 ? 20.44200  16.79200  5.74600   1.000 27.37960  ? 116  VAL A CG1   1 
ATOM   916  C  CG2   . VAL A 1 116 ? 20.85600  18.64600  4.12700   1.000 27.76386  ? 116  VAL A CG2   1 
ATOM   917  N  N     . LYS A 1 117 ? 18.96300  21.13400  4.92800   1.000 25.95838  ? 117  LYS A N     1 
ATOM   918  C  CA    . LYS A 1 117 ? 19.03000  22.59200  4.92200   1.000 24.90299  ? 117  LYS A CA    1 
ATOM   919  C  C     . LYS A 1 117 ? 17.90700  23.19700  5.75900   1.000 22.68956  ? 117  LYS A C     1 
ATOM   920  O  O     . LYS A 1 117 ? 18.13800  24.14200  6.52700   1.000 23.96077  ? 117  LYS A O     1 
ATOM   921  C  CB    . LYS A 1 117 ? 19.00800  23.10700  3.48100   1.000 30.82738  ? 117  LYS A CB    1 
ATOM   922  C  CG    . LYS A 1 117 ? 19.33900  24.58000  3.32600   1.000 38.74938  ? 117  LYS A CG    1 
ATOM   923  C  CD    . LYS A 1 117 ? 19.35400  24.97600  1.85300   1.000 44.12634  ? 117  LYS A CD    1 
ATOM   924  C  CE    . LYS A 1 117 ? 19.77100  26.42800  1.66100   1.000 48.92166  ? 117  LYS A CE    1 
ATOM   925  N  NZ    . LYS A 1 117 ? 19.90200  26.79400  0.21600   1.000 50.62449  ? 117  LYS A NZ    1 
ATOM   926  N  N     . ARG A 1 118 ? 16.68800  22.65800  5.64200   1.000 21.74471  ? 118  ARG A N     1 
ATOM   927  C  CA    A ARG A 1 118 ? 15.59400  23.18000  6.45300   0.580 22.17634  ? 118  ARG A CA    1 
ATOM   928  C  CA    B ARG A 1 118 ? 15.58000  23.16000  6.44900   0.420 21.50784  ? 118  ARG A CA    1 
ATOM   929  C  C     . ARG A 1 118 ? 15.80200  22.86500  7.92500   1.000 21.91052  ? 118  ARG A C     1 
ATOM   930  O  O     . ARG A 1 118 ? 15.51500  23.70600  8.78500   1.000 23.52914  ? 118  ARG A O     1 
ATOM   931  C  CB    A ARG A 1 118 ? 14.24300  22.65500  5.96500   0.580 26.66109  ? 118  ARG A CB    1 
ATOM   932  C  CB    B ARG A 1 118 ? 14.26200  22.54500  5.97400   0.420 23.61336  ? 118  ARG A CB    1 
ATOM   933  C  CG    A ARG A 1 118 ? 13.60500  23.52600  4.89100   0.580 34.08303  ? 118  ARG A CG    1 
ATOM   934  C  CG    B ARG A 1 118 ? 13.74600  23.12000  4.66500   0.420 28.43236  ? 118  ARG A CG    1 
ATOM   935  C  CD    A ARG A 1 118 ? 13.54400  24.99800  5.31100   0.580 37.09655  ? 118  ARG A CD    1 
ATOM   936  C  CD    B ARG A 1 118 ? 13.11800  24.49100  4.87800   0.420 30.39049  ? 118  ARG A CD    1 
ATOM   937  N  NE    A ARG A 1 118 ? 12.62800  25.24300  6.42100   0.580 39.26523  ? 118  ARG A NE    1 
ATOM   938  N  NE    B ARG A 1 118 ? 13.12500  25.28800  3.65800   0.420 34.97261  ? 118  ARG A NE    1 
ATOM   939  C  CZ    A ARG A 1 118 ? 12.98000  25.72800  7.60700   0.580 38.87571  ? 118  ARG A CZ    1 
ATOM   940  C  CZ    B ARG A 1 118 ? 12.22200  25.19400  2.69300   0.420 36.62281  ? 118  ARG A CZ    1 
ATOM   941  N  NH1   A ARG A 1 118 ? 14.23600  26.04700  7.88400   0.580 33.59087  ? 118  ARG A NH1   1 
ATOM   942  N  NH1   B ARG A 1 118 ? 11.21600  24.33700  2.76700   0.420 37.61240  ? 118  ARG A NH1   1 
ATOM   943  N  NH2   A ARG A 1 118 ? 12.04600  25.91000  8.53600   0.580 39.24418  ? 118  ARG A NH2   1 
ATOM   944  N  NH2   B ARG A 1 118 ? 12.33100  25.98000  1.62600   0.420 36.85705  ? 118  ARG A NH2   1 
ATOM   945  N  N     . ILE A 1 119 ? 16.30900  21.67100  8.23400   1.000 21.28676  ? 119  ILE A N     1 
ATOM   946  C  CA    . ILE A 1 119 ? 16.54300  21.31700  9.63100   1.000 20.34454  ? 119  ILE A CA    1 
ATOM   947  C  C     . ILE A 1 119 ? 17.56800  22.25900  10.24600  1.000 23.57388  ? 119  ILE A C     1 
ATOM   948  O  O     . ILE A 1 119 ? 17.40200  22.73500  11.37600  1.000 23.51598  ? 119  ILE A O     1 
ATOM   949  C  CB    . ILE A 1 119 ? 16.98800  19.84700  9.74800   1.000 22.37374  ? 119  ILE A CB    1 
ATOM   950  C  CG1   . ILE A 1 119 ? 15.90800  18.89300  9.23400   1.000 25.62939  ? 119  ILE A CG1   1 
ATOM   951  C  CG2   . ILE A 1 119 ? 17.38100  19.51800  11.17500  1.000 21.58417  ? 119  ILE A CG2   1 
ATOM   952  C  CD1   . ILE A 1 119 ? 14.54200  19.15000  9.78100   1.000 25.11880  ? 119  ILE A CD1   1 
ATOM   953  N  N     . LYS A 1 120 ? 18.64500  22.54600  9.51300   1.000 22.74483  ? 120  LYS A N     1 
ATOM   954  C  CA    . LYS A 1 120 ? 19.64000  23.49000  10.01000  1.000 24.05288  ? 120  LYS A CA    1 
ATOM   955  C  C     . LYS A 1 120 ? 19.01200  24.84900  10.28000  1.000 24.61348  ? 120  LYS A C     1 
ATOM   956  O  O     . LYS A 1 120 ? 19.30500  25.48700  11.29800  1.000 26.74531  ? 120  LYS A O     1 
ATOM   957  C  CB    . LYS A 1 120 ? 20.76800  23.63300  8.99300   1.000 24.67401  ? 120  LYS A CB    1 
ATOM   958  C  CG    . LYS A 1 120 ? 21.85400  24.60900  9.41300   1.000 24.83192  ? 120  LYS A CG    1 
ATOM   959  C  CD    . LYS A 1 120 ? 22.93600  24.73200  8.34900   1.000 27.23221  ? 120  LYS A CD    1 
ATOM   960  C  CE    . LYS A 1 120 ? 24.00400  25.72000  8.78400   1.000 32.87763  ? 120  LYS A CE    1 
ATOM   961  N  NZ    . LYS A 1 120 ? 25.04300  25.93400  7.73900   1.000 35.33055  ? 120  LYS A NZ    1 
ATOM   962  N  N     . GLY A 1 121 ? 18.13100  25.30100  9.38300   1.000 25.18460  ? 121  GLY A N     1 
ATOM   963  C  CA    . GLY A 1 121 ? 17.44700  26.56400  9.58500   1.000 25.72151  ? 121  GLY A CA    1 
ATOM   964  C  C     . GLY A 1 121 ? 16.47300  26.56400  10.74600  1.000 24.47925  ? 121  GLY A C     1 
ATOM   965  O  O     . GLY A 1 121 ? 16.06300  27.64000  11.19300  1.000 26.32947  ? 121  GLY A O     1 
ATOM   966  N  N     . MET A 1 122 ? 16.08800  25.38700  11.23700  1.000 23.16594  ? 122  MET A N     1 
ATOM   967  C  CA    . MET A 1 122 ? 15.17700  25.29400  12.36900  1.000 23.25279  ? 122  MET A CA    1 
ATOM   968  C  C     . MET A 1 122 ? 15.87600  25.37700  13.71300  1.000 24.08183  ? 122  MET A C     1 
ATOM   969  O  O     . MET A 1 122 ? 15.18900  25.48500  14.73600  1.000 23.59757  ? 122  MET A O     1 
ATOM   970  C  CB    . MET A 1 122 ? 14.38400  23.98900  12.31000  1.000 23.88444  ? 122  MET A CB    1 
ATOM   971  C  CG    . MET A 1 122 ? 13.43500  23.92800  11.14200  1.000 25.13196  ? 122  MET A CG    1 
ATOM   972  S  SD    . MET A 1 122 ? 12.61700  22.33900  11.08300  1.000 27.72964  ? 122  MET A SD    1 
ATOM   973  C  CE    . MET A 1 122 ? 11.63700  22.46200  12.55500  1.000 27.95598  ? 122  MET A CE    1 
ATOM   974  N  N     . ARG A 1 123 ? 17.20700  25.33900  13.74300  1.000 24.62927  ? 123  ARG A N     1 
ATOM   975  C  CA    . ARG A 1 123 ? 17.91900  25.38100  15.02100  1.000 25.65308  ? 123  ARG A CA    1 
ATOM   976  C  C     . ARG A 1 123 ? 17.51500  26.54700  15.91900  1.000 26.51107  ? 123  ARG A C     1 
ATOM   977  O  O     . ARG A 1 123 ? 17.25400  26.31000  17.10900  1.000 25.54517  ? 123  ARG A O     1 
ATOM   978  C  CB    . ARG A 1 123 ? 19.43900  25.27900  14.83100  1.000 26.03470  ? 123  ARG A CB    1 
ATOM   979  C  CG    . ARG A 1 123 ? 20.18900  25.46400  16.14200  1.000 26.85322  ? 123  ARG A CG    1 
ATOM   980  C  CD    . ARG A 1 123 ? 21.69600  25.35300  15.99100  1.000 27.45329  ? 123  ARG A CD    1 
ATOM   981  N  NE    . ARG A 1 123 ? 22.11400  24.05800  15.47100  1.000 28.10863  ? 123  ARG A NE    1 
ATOM   982  C  CZ    . ARG A 1 123 ? 22.25400  22.96100  16.20300  1.000 27.44540  ? 123  ARG A CZ    1 
ATOM   983  N  NH1   . ARG A 1 123 ? 21.98900  22.95400  17.50000  1.000 28.11127  ? 123  ARG A NH1   1 
ATOM   984  N  NH2   . ARG A 1 123 ? 22.65400  21.83700  15.61500  1.000 26.70583  ? 123  ARG A NH2   1 
ATOM   985  N  N     . PRO A 1 124 ? 17.44500  27.80200  15.44300  1.000 27.82439  ? 124  PRO A N     1 
ATOM   986  C  CA    . PRO A 1 124 ? 17.02300  28.88600  16.34900  1.000 29.50354  ? 124  PRO A CA    1 
ATOM   987  C  C     . PRO A 1 124 ? 15.66500  28.65900  16.98600  1.000 27.29801  ? 124  PRO A C     1 
ATOM   988  O  O     . PRO A 1 124 ? 15.51100  28.90400  18.18900  1.000 30.03518  ? 124  PRO A O     1 
ATOM   989  C  CB    . PRO A 1 124 ? 17.03400  30.12700  15.44600  1.000 29.71409  ? 124  PRO A CB    1 
ATOM   990  C  CG    . PRO A 1 124 ? 18.03000  29.81000  14.39100  1.000 28.20601  ? 124  PRO A CG    1 
ATOM   991  C  CD    . PRO A 1 124 ? 17.89200  28.32900  14.14000  1.000 28.22444  ? 124  PRO A CD    1 
ATOM   992  N  N     . GLU A 1 125 ? 14.67300  28.20200  16.21400  1.000 26.34263  ? 125  GLU A N     1 
ATOM   993  C  CA    . GLU A 1 125 ? 13.35400  27.93700  16.78500  1.000 25.33988  ? 125  GLU A CA    1 
ATOM   994  C  C     . GLU A 1 125 ? 13.42200  26.81900  17.81400  1.000 23.94761  ? 125  GLU A C     1 
ATOM   995  O  O     . GLU A 1 125 ? 12.83200  26.92600  18.89500  1.000 24.67138  ? 125  GLU A O     1 
ATOM   996  C  CB    . GLU A 1 125 ? 12.35100  27.58600  15.67800  1.000 25.77941  ? 125  GLU A CB    1 
ATOM   997  C  CG    . GLU A 1 125 ? 11.07600  26.85600  16.14700  1.000 30.22468  ? 125  GLU A CG    1 
ATOM   998  C  CD    . GLU A 1 125 ? 9.94700   27.79300  16.59200  1.000 34.98051  ? 125  GLU A CD    1 
ATOM   999  O  OE1   . GLU A 1 125 ? 10.14700  29.02300  16.58600  1.000 38.90993  ? 125  GLU A OE1   1 
ATOM   1000 O  OE2   . GLU A 1 125 ? 8.85200   27.29500  16.94700  1.000 34.18831  ? 125  GLU A OE2   1 
ATOM   1001 N  N     . VAL A 1 126 ? 14.13700  25.73700  17.49300  1.000 22.39216  ? 126  VAL A N     1 
ATOM   1002 C  CA    . VAL A 1 126 ? 14.21100  24.60100  18.40600  1.000 21.06568  ? 126  VAL A CA    1 
ATOM   1003 C  C     . VAL A 1 126 ? 14.88400  25.01100  19.70600  1.000 21.41309  ? 126  VAL A C     1 
ATOM   1004 O  O     . VAL A 1 126 ? 14.39700  24.69600  20.79600  1.000 23.26858  ? 126  VAL A O     1 
ATOM   1005 C  CB    . VAL A 1 126 ? 14.90900  23.40300  17.73300  1.000 19.86291  ? 126  VAL A CB    1 
ATOM   1006 C  CG1   . VAL A 1 126 ? 15.06800  22.24700  18.72200  1.000 20.27085  ? 126  VAL A CG1   1 
ATOM   1007 C  CG2   . VAL A 1 126 ? 14.11800  22.96300  16.51400  1.000 20.44719  ? 126  VAL A CG2   1 
ATOM   1008 N  N     . GLU A 1 127 ? 15.99000  25.75300  19.61500  1.000 22.81589  ? 127  GLU A N     1 
ATOM   1009 C  CA    . GLU A 1 127 ? 16.66200  26.19700  20.83100  1.000 22.60271  ? 127  GLU A CA    1 
ATOM   1010 C  C     . GLU A 1 127 ? 15.78000  27.14400  21.63600  1.000 24.03446  ? 127  GLU A C     1 
ATOM   1011 O  O     . GLU A 1 127 ? 15.71200  27.04300  22.86700  1.000 25.72677  ? 127  GLU A O     1 
ATOM   1012 C  CB    . GLU A 1 127 ? 18.01800  26.81700  20.49500  1.000 23.57388  ? 127  GLU A CB    1 
ATOM   1013 C  CG    . GLU A 1 127 ? 18.90300  25.79500  19.80000  1.000 27.28222  ? 127  GLU A CG    1 
ATOM   1014 C  CD    . GLU A 1 127 ? 20.35200  26.19900  19.66700  1.000 35.33582  ? 127  GLU A CD    1 
ATOM   1015 O  OE1   . GLU A 1 127 ? 20.65200  27.40300  19.74100  1.000 36.10170  ? 127  GLU A OE1   1 
ATOM   1016 O  OE2   . GLU A 1 127 ? 21.19600  25.29100  19.48000  1.000 38.56252  ? 127  GLU A OE2   1 
ATOM   1017 N  N     . GLU A 1 128 ? 15.07700  28.05600  20.95900  1.000 24.40556  ? 128  GLU A N     1 
ATOM   1018 C  CA    . GLU A 1 128 ? 14.20100  28.97600  21.68100  1.000 25.34251  ? 128  GLU A CA    1 
ATOM   1019 C  C     . GLU A 1 128 ? 13.07900  28.22700  22.39000  1.000 26.53476  ? 128  GLU A C     1 
ATOM   1020 O  O     . GLU A 1 128 ? 12.78100  28.50300  23.56200  1.000 25.98996  ? 128  GLU A O     1 
ATOM   1021 C  CB    . GLU A 1 128 ? 13.63300  30.04500  20.74600  1.000 29.05085  ? 128  GLU A CB    1 
ATOM   1022 C  CG    . GLU A 1 128 ? 12.60200  30.93900  21.42900  1.000 36.02274  ? 128  GLU A CG    1 
ATOM   1023 C  CD    . GLU A 1 128 ? 12.02100  31.99700  20.51100  1.000 43.68419  ? 128  GLU A CD    1 
ATOM   1024 O  OE1   . GLU A 1 128 ? 12.65800  32.31500  19.48700  1.000 39.97058  ? 128  GLU A OE1   1 
ATOM   1025 O  OE2   . GLU A 1 128 ? 10.91900  32.50600  20.81500  1.000 51.70620  ? 128  GLU A OE2   1 
ATOM   1026 N  N     . VAL A 1 129 ? 12.46800  27.25600  21.70400  1.000 24.06868  ? 129  VAL A N     1 
ATOM   1027 C  CA    . VAL A 1 129 ? 11.36300  26.50000  22.28600  1.000 23.70284  ? 129  VAL A CA    1 
ATOM   1028 C  C     . VAL A 1 129 ? 11.84900  25.68300  23.48000  1.000 23.82391  ? 129  VAL A C     1 
ATOM   1029 O  O     . VAL A 1 129 ? 11.21400  25.66400  24.54200  1.000 24.73454  ? 129  VAL A O     1 
ATOM   1030 C  CB    . VAL A 1 129 ? 10.69400  25.62100  21.21100  1.000 23.03434  ? 129  VAL A CB    1 
ATOM   1031 C  CG1   . VAL A 1 129 ? 9.77700   24.60000  21.85100  1.000 24.33713  ? 129  VAL A CG1   1 
ATOM   1032 C  CG2   . VAL A 1 129 ? 9.91900   26.49300  20.21300  1.000 25.31356  ? 129  VAL A CG2   1 
ATOM   1033 N  N     . VAL A 1 130 ? 12.98000  24.98900  23.31700  1.000 23.53966  ? 130  VAL A N     1 
ATOM   1034 C  CA    . VAL A 1 130 ? 13.52900  24.17900  24.40300  1.000 22.32636  ? 130  VAL A CA    1 
ATOM   1035 C  C     . VAL A 1 130 ? 13.81400  25.03800  25.62400  1.000 24.89772  ? 130  VAL A C     1 
ATOM   1036 O  O     . VAL A 1 130 ? 13.43300  24.69800  26.75100  1.000 26.55845  ? 130  VAL A O     1 
ATOM   1037 C  CB    . VAL A 1 130 ? 14.78900  23.43000  23.93100  1.000 22.92380  ? 130  VAL A CB    1 
ATOM   1038 C  CG1   . VAL A 1 130 ? 15.55300  22.85000  25.12000  1.000 25.38725  ? 130  VAL A CG1   1 
ATOM   1039 C  CG2   . VAL A 1 130 ? 14.41400  22.33700  22.93600  1.000 23.55809  ? 130  VAL A CG2   1 
ATOM   1040 N  N     . HIS A 1 131 ? 14.49700  26.14600  25.42400  1.000 24.85561  ? 131  HIS A N     1 
ATOM   1041 C  CA    . HIS A 1 131 ? 14.90700  26.99300  26.57400  1.000 28.88241  ? 131  HIS A CA    1 
ATOM   1042 C  C     . HIS A 1 131 ? 13.68500  27.65000  27.21900  1.000 30.41680  ? 131  HIS A C     1 
ATOM   1043 O  O     . HIS A 1 131 ? 13.67500  27.80600  28.42700  1.000 33.08818  ? 131  HIS A O     1 
ATOM   1044 C  CB    . HIS A 1 131 ? 15.98800  27.96100  26.13600  1.000 30.42996  ? 131  HIS A CB    1 
ATOM   1045 C  CG    . HIS A 1 131 ? 17.32100  27.32500  25.98500  1.000 35.59901  ? 131  HIS A CG    1 
ATOM   1046 N  ND1   . HIS A 1 131 ? 18.08400  26.95400  27.05400  1.000 37.27552  ? 131  HIS A ND1   1 
ATOM   1047 C  CD2   . HIS A 1 131 ? 18.02700  26.98800  24.89600  1.000 38.80728  ? 131  HIS A CD2   1 
ATOM   1048 C  CE1   . HIS A 1 131 ? 19.19900  26.43100  26.62400  1.000 39.84688  ? 131  HIS A CE1   1 
ATOM   1049 N  NE2   . HIS A 1 131 ? 19.18300  26.42500  25.32300  1.000 39.61791  ? 131  HIS A NE2   1 
ATOM   1050 N  N     . GLY A 1 132 ? 12.67800  27.98500  26.43100  1.000 29.37194  ? 132  GLY A N     1 
ATOM   1051 C  CA    . GLY A 1 132 ? 11.46100  28.59800  26.97800  1.000 28.10600  ? 132  GLY A CA    1 
ATOM   1052 C  C     . GLY A 1 132 ? 10.71200  27.66000  27.88600  1.000 29.12981  ? 132  GLY A C     1 
ATOM   1053 O  O     . GLY A 1 132 ? 10.32100  28.07200  28.95300  1.000 31.45377  ? 132  GLY A O     1 
ATOM   1054 N  N     . PHE A 1 133 ? 10.48200  26.42100  27.46000  1.000 26.26631  ? 133  PHE A N     1 
ATOM   1055 C  CA    . PHE A 1 133 ? 9.72800   25.49300  28.32100  1.000 25.09775  ? 133  PHE A CA    1 
ATOM   1056 C  C     . PHE A 1 133 ? 10.57900  25.17300  29.55400  1.000 28.65607  ? 133  PHE A C     1 
ATOM   1057 O  O     . PHE A 1 133 ? 10.01000  24.88600  30.57600  1.000 30.01676  ? 133  PHE A O     1 
ATOM   1058 C  CB    . PHE A 1 133 ? 9.27000   24.26600  27.52800  1.000 24.34502  ? 133  PHE A CB    1 
ATOM   1059 C  CG    . PHE A 1 133 ? 8.03400   24.50300  26.70000  1.000 23.44492  ? 133  PHE A CG    1 
ATOM   1060 C  CD1   . PHE A 1 133 ? 6.79600   24.62300  27.28100  1.000 24.91615  ? 133  PHE A CD1   1 
ATOM   1061 C  CD2   . PHE A 1 133 ? 8.10600   24.60100  25.32200  1.000 24.56084  ? 133  PHE A CD2   1 
ATOM   1062 C  CE1   . PHE A 1 133 ? 5.66300   24.86100  26.53000  1.000 24.57663  ? 133  PHE A CE1   1 
ATOM   1063 C  CE2   . PHE A 1 133 ? 6.97100   24.83800  24.57600  1.000 23.31595  ? 133  PHE A CE2   1 
ATOM   1064 C  CZ    . PHE A 1 133 ? 5.75200   24.95300  25.16800  1.000 22.42637  ? 133  PHE A CZ    1 
ATOM   1065 N  N     . LEU A 1 134 ? 11.89300  25.23800  29.40400  1.000 30.43786  ? 134  LEU A N     1 
ATOM   1066 C  CA    . LEU A 1 134 ? 12.80600  24.99100  30.54700  1.000 36.13065  ? 134  LEU A CA    1 
ATOM   1067 C  C     . LEU A 1 134 ? 12.73000  26.16900  31.50700  1.000 41.17599  ? 134  LEU A C     1 
ATOM   1068 O  O     . LEU A 1 134 ? 12.47400  25.91000  32.67900  1.000 45.45282  ? 134  LEU A O     1 
ATOM   1069 C  CB    . LEU A 1 134 ? 14.23600  24.84900  30.05000  1.000 38.26248  ? 134  LEU A CB    1 
ATOM   1070 C  CG    . LEU A 1 134 ? 14.69000  23.41800  29.84100  1.000 37.58082  ? 134  LEU A CG    1 
ATOM   1071 C  CD1   . LEU A 1 134 ? 16.13500  23.40100  29.40800  1.000 38.09404  ? 134  LEU A CD1   1 
ATOM   1072 C  CD2   . LEU A 1 134 ? 14.52600  22.61100  31.10600  1.000 37.00707  ? 134  LEU A CD2   1 
ATOM   1073 N  N     . ASP A 1 135 ? 12.93800  27.40000  31.02800  1.000 42.10768  ? 135  ASP A N     1 
ATOM   1074 C  CA    . ASP A 1 135 ? 12.70200  28.62200  31.85100  1.000 43.14465  ? 135  ASP A CA    1 
ATOM   1075 C  C     . ASP A 1 135 ? 11.42700  28.40100  32.67700  1.000 39.93637  ? 135  ASP A C     1 
ATOM   1076 O  O     . ASP A 1 135 ? 11.47900  28.43500  33.90300  1.000 41.22336  ? 135  ASP A O     1 
ATOM   1077 C  CB    . ASP A 1 135 ? 12.46900  29.86600  30.98500  1.000 48.86375  ? 135  ASP A CB    1 
ATOM   1078 C  CG    . ASP A 1 135 ? 13.65200  30.41000  30.21300  1.000 53.16690  ? 135  ASP A CG    1 
ATOM   1079 O  OD1   . ASP A 1 135 ? 14.76600  30.11400  30.57000  1.000 55.51981  ? 135  ASP A OD1   1 
ATOM   1080 O  OD2   . ASP A 1 135 ? 13.42000  31.11700  29.23400  1.000 54.33546  ? 135  ASP A OD2   1 
ATOM   1081 N  N     . GLU A 1 136 ? 10.33200  28.08100  32.00600  1.000 36.85968  ? 136  GLU A N     1 
ATOM   1082 C  CA    . GLU A 1 136 ? 9.01200   27.93900  32.65100  1.000 34.73838  ? 136  GLU A CA    1 
ATOM   1083 C  C     . GLU A 1 136 ? 9.00100   26.84600  33.72100  1.000 35.53847  ? 136  GLU A C     1 
ATOM   1084 O  O     . GLU A 1 136 ? 8.49500   27.10700  34.79400  1.000 37.26763  ? 136  GLU A O     1 
ATOM   1085 C  CB    . GLU A 1 136 ? 7.92800   27.72800  31.60600  1.000 32.73814  ? 136  GLU A CB    1 
ATOM   1086 C  CG    . GLU A 1 136 ? 6.54500   27.71500  32.17600  1.000 30.65631  ? 136  GLU A CG    1 
ATOM   1087 C  CD    . GLU A 1 136 ? 5.44500   27.78800  31.14400  1.000 32.45389  ? 136  GLU A CD    1 
ATOM   1088 O  OE1   . GLU A 1 136 ? 5.75800   27.63700  29.95700  1.000 30.81948  ? 136  GLU A OE1   1 
ATOM   1089 O  OE2   . GLU A 1 136 ? 4.30200   27.96000  31.52100  1.000 33.65930  ? 136  GLU A OE2   1 
ATOM   1090 N  N     . MET A 1 137 ? 9.51300   25.65400  33.42500  1.000 36.35962  ? 137  MET A N     1 
ATOM   1091 C  CA    . MET A 1 137 ? 9.39500   24.52400  34.37600  1.000 35.33845  ? 137  MET A CA    1 
ATOM   1092 C  C     . MET A 1 137 ? 10.21100  24.83100  35.63200  1.000 38.24932  ? 137  MET A C     1 
ATOM   1093 O  O     . MET A 1 137 ? 9.74200   24.52000  36.70800  1.000 40.68119  ? 137  MET A O     1 
ATOM   1094 C  CB    . MET A 1 137 ? 9.93100   23.23200  33.75400  1.000 34.76469  ? 137  MET A CB    1 
ATOM   1095 C  CG    . MET A 1 137 ? 9.56800   21.99000  34.51600  1.000 35.34634  ? 137  MET A CG    1 
ATOM   1096 S  SD    . MET A 1 137 ? 10.44100  20.56600  33.79700  1.000 38.81255  ? 137  MET A SD    1 
ATOM   1097 C  CE    . MET A 1 137 ? 12.10300  21.19100  33.85900  1.000 38.08615  ? 137  MET A CE    1 
ATOM   1098 N  N     . LEU A 1 138 ? 11.39300  25.39200  35.45400  1.000 39.63896  ? 138  LEU A N     1 
ATOM   1099 C  CA    . LEU A 1 138 ? 12.27800  25.64700  36.61100  1.000 43.28940  ? 138  LEU A CA    1 
ATOM   1100 C  C     . LEU A 1 138 ? 11.63700  26.71500  37.49000  1.000 44.62377  ? 138  LEU A C     1 
ATOM   1101 O  O     . LEU A 1 138 ? 11.81000  26.63900  38.68600  1.000 48.02681  ? 138  LEU A O     1 
ATOM   1102 C  CB    . LEU A 1 138 ? 13.62700  26.14700  36.11400  1.000 45.41071  ? 138  LEU A CB    1 
ATOM   1103 C  CG    . LEU A 1 138 ? 14.42500  25.13600  35.30300  1.000 49.11378  ? 138  LEU A CG    1 
ATOM   1104 C  CD1   . LEU A 1 138 ? 15.69000  25.76900  34.77500  1.000 50.23760  ? 138  LEU A CD1   1 
ATOM   1105 C  CD2   . LEU A 1 138 ? 14.72700  23.90100  36.12600  1.000 51.60356  ? 138  LEU A CD2   1 
ATOM   1106 N  N     . ALA A 1 139 ? 10.92000  27.65800  36.89600  1.000 42.64459  ? 139  ALA A N     1 
ATOM   1107 C  CA    . ALA A 1 139 ? 10.30400  28.70900  37.69400  1.000 41.42865  ? 139  ALA A CA    1 
ATOM   1108 C  C     . ALA A 1 139 ? 9.00700   28.27000  38.36300  1.000 42.80513  ? 139  ALA A C     1 
ATOM   1109 O  O     . ALA A 1 139 ? 8.61900   28.86100  39.37700  1.000 46.08974  ? 139  ALA A O     1 
ATOM   1110 C  CB    . ALA A 1 139 ? 10.05600  29.94300  36.82400  1.000 42.00240  ? 139  ALA A CB    1 
ATOM   1111 N  N     . ALA A 1 140 ? 8.33500   27.24600  37.83100  1.000 43.86579  ? 140  ALA A N     1 
ATOM   1112 C  CA    . ALA A 1 140 ? 7.01000   26.87500  38.31100  1.000 45.93182  ? 140  ALA A CA    1 
ATOM   1113 C  C     . ALA A 1 140 ? 7.03500   26.13300  39.64200  1.000 49.50067  ? 140  ALA A C     1 
ATOM   1114 O  O     . ALA A 1 140 ? 6.03500   26.16200  40.36800  1.000 52.96688  ? 140  ALA A O     1 
ATOM   1115 C  CB    . ALA A 1 140 ? 6.27500   26.04400  37.25300  1.000 45.17647  ? 140  ALA A CB    1 
ATOM   1116 N  N     . GLY A 1 141 ? 8.14100   25.48300  39.98900  1.000 48.83743  ? 141  GLY A N     1 
ATOM   1117 C  CA    . GLY A 1 141 ? 8.21700   24.76800  41.23900  1.000 49.04009  ? 141  GLY A CA    1 
ATOM   1118 C  C     . GLY A 1 141 ? 9.53800   24.06000  41.43500  1.000 49.45593  ? 141  GLY A C     1 
ATOM   1119 O  O     . GLY A 1 141 ? 10.38100  24.00900  40.53900  1.000 51.29562  ? 141  GLY A O     1 
ATOM   1120 N  N     . PRO A 1 142 ? 9.75400   23.51900  42.63900  1.000 49.39276  ? 142  PRO A N     1 
ATOM   1121 C  CA    . PRO A 1 142 ? 10.95200  22.70000  42.87000  1.000 46.67928  ? 142  PRO A CA    1 
ATOM   1122 C  C     . PRO A 1 142 ? 10.86600  21.31900  42.25200  1.000 44.89749  ? 142  PRO A C     1 
ATOM   1123 O  O     . PRO A 1 142 ? 11.90800  20.67100  42.08500  1.000 45.90814  ? 142  PRO A O     1 
ATOM   1124 C  CB    . PRO A 1 142 ? 11.03500  22.61700  44.40100  1.000 47.81626  ? 142  PRO A CB    1 
ATOM   1125 C  CG    . PRO A 1 142 ? 9.62400   22.78500  44.85500  1.000 49.44277  ? 142  PRO A CG    1 
ATOM   1126 C  CD    . PRO A 1 142 ? 8.96000   23.71000  43.86300  1.000 49.74544  ? 142  PRO A CD    1 
ATOM   1127 N  N     . THR A 1 143 ? 9.66700   20.84300  41.92400  1.000 41.38391  ? 143  THR A N     1 
ATOM   1128 C  CA    . THR A 1 143 ? 9.49300   19.55700  41.26400  1.000 39.20996  ? 143  THR A CA    1 
ATOM   1129 C  C     . THR A 1 143 ? 8.60200   19.74200  40.04600  1.000 39.06521  ? 143  THR A C     1 
ATOM   1130 O  O     . THR A 1 143 ? 7.91200   20.75400  39.90500  1.000 41.43392  ? 143  THR A O     1 
ATOM   1131 C  CB    . THR A 1 143 ? 8.86200   18.51400  42.19200  1.000 42.56563  ? 143  THR A CB    1 
ATOM   1132 O  OG1   . THR A 1 143 ? 7.53300   18.92300  42.53300  1.000 46.17133  ? 143  THR A OG1   1 
ATOM   1133 C  CG2   . THR A 1 143 ? 9.69000   18.35400  43.46100  1.000 42.83671  ? 143  THR A CG2   1 
ATOM   1134 N  N     . ALA A 1 144 ? 8.62400   18.74600  39.16100  1.000 34.11462  ? 144  ALA A N     1 
ATOM   1135 C  CA    . ALA A 1 144 ? 7.82900   18.82100  37.94600  1.000 33.00133  ? 144  ALA A CA    1 
ATOM   1136 C  C     . ALA A 1 144 ? 7.63500   17.42600  37.37500  1.000 31.14058  ? 144  ALA A C     1 
ATOM   1137 O  O     . ALA A 1 144 ? 8.40800   16.50600  37.65400  1.000 33.12239  ? 144  ALA A O     1 
ATOM   1138 C  CB    . ALA A 1 144 ? 8.50800   19.70500  36.89500  1.000 35.50689  ? 144  ALA A CB    1 
ATOM   1139 N  N     . ASP A 1 145 ? 6.58600   17.29000  36.56400  1.000 27.70069  ? 145  ASP A N     1 
ATOM   1140 C  CA    . ASP A 1 145 ? 6.43900   16.16300  35.64500  1.000 26.88743  ? 145  ASP A CA    1 
ATOM   1141 C  C     . ASP A 1 145 ? 7.16400   16.53600  34.35800  1.000 27.41908  ? 145  ASP A C     1 
ATOM   1142 O  O     . ASP A 1 145 ? 6.70700   17.41000  33.61600  1.000 28.39551  ? 145  ASP A O     1 
ATOM   1143 C  CB    . ASP A 1 145 ? 4.96300   15.89900  35.35700  1.000 29.00348  ? 145  ASP A CB    1 
ATOM   1144 C  CG    . ASP A 1 145 ? 4.75300   14.88900  34.23200  1.000 32.39862  ? 145  ASP A CG    1 
ATOM   1145 O  OD1   . ASP A 1 145 ? 5.65000   14.05900  33.98800  1.000 31.74591  ? 145  ASP A OD1   1 
ATOM   1146 O  OD2   . ASP A 1 145 ? 3.69200   14.93500  33.57300  1.000 36.80178  ? 145  ASP A OD2   1 
ATOM   1147 N  N     . LEU A 1 146 ? 8.29700   15.88000  34.10000  1.000 26.86638  ? 146  LEU A N     1 
ATOM   1148 C  CA    . LEU A 1 146 ? 9.07200   16.20100  32.90500  1.000 24.22922  ? 146  LEU A CA    1 
ATOM   1149 C  C     . LEU A 1 146 ? 8.26500   15.98200  31.63300  1.000 23.07119  ? 146  LEU A C     1 
ATOM   1150 O  O     . LEU A 1 146 ? 8.47800   16.68800  30.64500  1.000 25.57412  ? 146  LEU A O     1 
ATOM   1151 C  CB    . LEU A 1 146 ? 10.35000  15.36500  32.84600  1.000 26.02944  ? 146  LEU A CB    1 
ATOM   1152 C  CG    . LEU A 1 146 ? 11.38800  15.93000  31.87600  1.000 26.88217  ? 146  LEU A CG    1 
ATOM   1153 C  CD1   . LEU A 1 146 ? 11.97200  17.23200  32.42800  1.000 26.66109  ? 146  LEU A CD1   1 
ATOM   1154 C  CD2   . LEU A 1 146 ? 12.48600  14.91600  31.58000  1.000 26.26894  ? 146  LEU A CD2   1 
ATOM   1155 N  N     . VAL A 1 147 ? 7.34500   15.01800  31.63600  1.000 25.46621  ? 147  VAL A N     1 
ATOM   1156 C  CA    . VAL A 1 147 ? 6.59800   14.70000  30.42000  1.000 24.02656  ? 147  VAL A CA    1 
ATOM   1157 C  C     . VAL A 1 147 ? 5.69800   15.86500  30.02400  1.000 24.66612  ? 147  VAL A C     1 
ATOM   1158 O  O     . VAL A 1 147 ? 5.83300   16.43900  28.93400  1.000 25.41094  ? 147  VAL A O     1 
ATOM   1159 C  CB    . VAL A 1 147 ? 5.80800   13.39100  30.58600  1.000 24.70559  ? 147  VAL A CB    1 
ATOM   1160 C  CG1   . VAL A 1 147 ? 5.00500   13.08300  29.32200  1.000 25.49779  ? 147  VAL A CG1   1 
ATOM   1161 C  CG2   . VAL A 1 147 ? 6.74500   12.24700  30.92700  1.000 26.05839  ? 147  VAL A CG2   1 
ATOM   1162 N  N     . SER A 1 148 ? 4.76600   16.23500  30.90500  1.000 25.91100  ? 148  SER A N     1 
ATOM   1163 C  CA    . SER A 1 148 ? 3.78700   17.25500  30.55400  1.000 25.31619  ? 148  SER A CA    1 
ATOM   1164 C  C     . SER A 1 148 ? 4.40000   18.64800  30.49500  1.000 25.20039  ? 148  SER A C     1 
ATOM   1165 O  O     . SER A 1 148 ? 3.89200   19.50500  29.76700  1.000 28.12969  ? 148  SER A O     1 
ATOM   1166 C  CB    . SER A 1 148 ? 2.62100   17.24200  31.54400  1.000 28.09547  ? 148  SER A CB    1 
ATOM   1167 O  OG    . SER A 1 148 ? 3.05600   17.53000  32.86700  1.000 29.50091  ? 148  SER A OG    1 
ATOM   1168 N  N     . GLN A 1 149 ? 5.47200   18.90500  31.24900  1.000 25.82941  ? 149  GLN A N     1 
ATOM   1169 C  CA    A GLN A 1 149 ? 6.04700   20.24300  31.32300  0.410 25.90837  ? 149  GLN A CA    1 
ATOM   1170 C  CA    B GLN A 1 149 ? 6.03300   20.24700  31.31000  0.590 27.10851  ? 149  GLN A CA    1 
ATOM   1171 C  C     . GLN A 1 149 ? 7.18700   20.47500  30.33800  1.000 25.06353  ? 149  GLN A C     1 
ATOM   1172 O  O     . GLN A 1 149 ? 7.58400   21.63000  30.13700  1.000 26.01101  ? 149  GLN A O     1 
ATOM   1173 C  CB    A GLN A 1 149 ? 6.52900   20.55000  32.74800  0.410 25.84257  ? 149  GLN A CB    1 
ATOM   1174 C  CB    B GLN A 1 149 ? 6.43600   20.59800  32.75000  0.590 29.21403  ? 149  GLN A CB    1 
ATOM   1175 C  CG    A GLN A 1 149 ? 5.48700   20.29700  33.82100  0.410 25.03458  ? 149  GLN A CG    1 
ATOM   1176 C  CG    B GLN A 1 149 ? 5.23600   20.73200  33.67600  0.590 30.25100  ? 149  GLN A CG    1 
ATOM   1177 C  CD    A GLN A 1 149 ? 4.17900   21.00500  33.54900  0.410 25.81362  ? 149  GLN A CD    1 
ATOM   1178 C  CD    B GLN A 1 149 ? 5.62200   20.93000  35.12800  0.590 31.48535  ? 149  GLN A CD    1 
ATOM   1179 O  OE1   A GLN A 1 149 ? 3.12100   20.37500  33.48500  0.410 27.45329  ? 149  GLN A OE1   1 
ATOM   1180 O  OE1   B GLN A 1 149 ? 5.37600   20.06500  35.97000  0.590 31.80908  ? 149  GLN A OE1   1 
ATOM   1181 N  NE2   A GLN A 1 149 ? 4.24000   22.32200  33.38900  0.410 24.12395  ? 149  GLN A NE2   1 
ATOM   1182 N  NE2   B GLN A 1 149 ? 6.21900   22.07800  35.43300  0.590 31.55642  ? 149  GLN A NE2   1 
ATOM   1183 N  N     . PHE A 1 150 ? 7.72100   19.42300  29.71300  1.000 24.18448  ? 150  PHE A N     1 
ATOM   1184 C  CA    . PHE A 1 150 ? 8.89000   19.62200  28.86600  1.000 21.98685  ? 150  PHE A CA    1 
ATOM   1185 C  C     . PHE A 1 150 ? 8.95700   18.65300  27.68700  1.000 21.13411  ? 150  PHE A C     1 
ATOM   1186 O  O     . PHE A 1 150 ? 9.06900   19.08100  26.53000  1.000 21.05516  ? 150  PHE A O     1 
ATOM   1187 C  CB    . PHE A 1 150 ? 10.15500  19.53900  29.72600  1.000 22.48427  ? 150  PHE A CB    1 
ATOM   1188 C  CG    . PHE A 1 150 ? 11.43100  19.73800  28.96000  1.000 21.46836  ? 150  PHE A CG    1 
ATOM   1189 C  CD1   . PHE A 1 150 ? 11.75300  20.97900  28.44600  1.000 20.54194  ? 150  PHE A CD1   1 
ATOM   1190 C  CD2   . PHE A 1 150 ? 12.32400  18.68800  28.78200  1.000 22.43427  ? 150  PHE A CD2   1 
ATOM   1191 C  CE1   . PHE A 1 150 ? 12.92600  21.17500  27.75100  1.000 21.78945  ? 150  PHE A CE1   1 
ATOM   1192 C  CE2   . PHE A 1 150 ? 13.50300  18.87700  28.07600  1.000 21.12885  ? 150  PHE A CE2   1 
ATOM   1193 C  CZ    . PHE A 1 150 ? 13.80400  20.12700  27.56300  1.000 24.44240  ? 150  PHE A CZ    1 
ATOM   1194 N  N     . ALA A 1 151 ? 8.89700   17.34600  27.96500  1.000 21.49468  ? 151  ALA A N     1 
ATOM   1195 C  CA    . ALA A 1 151 ? 9.14700   16.36000  26.91300  1.000 19.51287  ? 151  ALA A CA    1 
ATOM   1196 C  C     . ALA A 1 151 ? 8.11000   16.44300  25.80500  1.000 20.14978  ? 151  ALA A C     1 
ATOM   1197 O  O     . ALA A 1 151 ? 8.44200   16.27800  24.62600  1.000 20.26296  ? 151  ALA A O     1 
ATOM   1198 C  CB    . ALA A 1 151 ? 9.18000   14.94700  27.49700  1.000 20.30507  ? 151  ALA A CB    1 
ATOM   1199 N  N     . LEU A 1 152 ? 6.85100   16.68100  26.15300  1.000 19.68394  ? 152  LEU A N     1 
ATOM   1200 C  CA    . LEU A 1 152 ? 5.81100   16.73600  25.12900  1.000 18.59433  ? 152  LEU A CA    1 
ATOM   1201 C  C     . LEU A 1 152 ? 5.64100   18.12000  24.49400  1.000 19.94186  ? 152  LEU A C     1 
ATOM   1202 O  O     . LEU A 1 152 ? 5.57900   18.21700  23.25900  1.000 20.38929  ? 152  LEU A O     1 
ATOM   1203 C  CB    . LEU A 1 152 ? 4.47300   16.21100  25.65900  1.000 23.09224  ? 152  LEU A CB    1 
ATOM   1204 C  CG    . LEU A 1 152 ? 3.37500   16.29400  24.59300  1.000 29.49038  ? 152  LEU A CG    1 
ATOM   1205 C  CD1   . LEU A 1 152 ? 3.54800   15.19100  23.52500  1.000 31.13531  ? 152  LEU A CD1   1 
ATOM   1206 C  CD2   . LEU A 1 152 ? 1.98500   16.28500  25.20000  1.000 36.42542  ? 152  LEU A CD2   1 
ATOM   1207 N  N     . PRO A 1 153 ? 5.55100   19.21100  25.26800  1.000 21.29203  ? 153  PRO A N     1 
ATOM   1208 C  CA    . PRO A 1 153 ? 5.29700   20.51100  24.62100  1.000 22.22635  ? 153  PRO A CA    1 
ATOM   1209 C  C     . PRO A 1 153 ? 6.36900   20.92700  23.63000  1.000 20.40508  ? 153  PRO A C     1 
ATOM   1210 O  O     . PRO A 1 153 ? 6.05400   21.59200  22.63600  1.000 22.06844  ? 153  PRO A O     1 
ATOM   1211 C  CB    . PRO A 1 153 ? 5.22800   21.49600  25.79500  1.000 24.64243  ? 153  PRO A CB    1 
ATOM   1212 C  CG    . PRO A 1 153 ? 5.04700   20.68700  27.00000  1.000 25.65044  ? 153  PRO A CG    1 
ATOM   1213 C  CD    . PRO A 1 153 ? 5.56300   19.32200  26.74100  1.000 23.78443  ? 153  PRO A CD    1 
ATOM   1214 N  N     . VAL A 1 154 ? 7.62700   20.59200  23.88600  1.000 20.57615  ? 154  VAL A N     1 
ATOM   1215 C  CA    . VAL A 1 154 ? 8.71200   21.04100  23.01700  1.000 18.84700  ? 154  VAL A CA    1 
ATOM   1216 C  C     . VAL A 1 154 ? 8.53900   20.51500  21.59100  1.000 17.79161  ? 154  VAL A C     1 
ATOM   1217 O  O     . VAL A 1 154 ? 8.39500   21.32400  20.66100  1.000 18.39431  ? 154  VAL A O     1 
ATOM   1218 C  CB    . VAL A 1 154 ? 10.09400  20.74000  23.62100  1.000 20.83408  ? 154  VAL A CB    1 
ATOM   1219 C  CG1   . VAL A 1 154 ? 11.17300  20.86100  22.56200  1.000 20.71564  ? 154  VAL A CG1   1 
ATOM   1220 C  CG2   . VAL A 1 154 ? 10.37000  21.66000  24.80900  1.000 21.91052  ? 154  VAL A CG2   1 
ATOM   1221 N  N     . PRO A 1 155 ? 8.53500   19.19500  21.35100  1.000 17.66001  ? 155  PRO A N     1 
ATOM   1222 C  CA    . PRO A 1 155 ? 8.34600   18.72100  19.96700  1.000 16.84939  ? 155  PRO A CA    1 
ATOM   1223 C  C     . PRO A 1 155 ? 6.97700   19.05200  19.40800  1.000 17.52579  ? 155  PRO A C     1 
ATOM   1224 O  O     . PRO A 1 155 ? 6.83200   19.16700  18.18000  1.000 17.25996  ? 155  PRO A O     1 
ATOM   1225 C  CB    . PRO A 1 155 ? 8.56500   17.20300  20.07100  1.000 16.81781  ? 155  PRO A CB    1 
ATOM   1226 C  CG    . PRO A 1 155 ? 8.25600   16.88200  21.50700  1.000 17.78897  ? 155  PRO A CG    1 
ATOM   1227 C  CD    . PRO A 1 155 ? 8.73000   18.07300  22.29200  1.000 18.81541  ? 155  PRO A CD    1 
ATOM   1228 N  N     . SER A 1 156 ? 5.97300   19.21000  20.27200  1.000 16.40723  ? 156  SER A N     1 
ATOM   1229 C  CA    . SER A 1 156 ? 4.64600   19.60800  19.81900  1.000 16.76517  ? 156  SER A CA    1 
ATOM   1230 C  C     . SER A 1 156 ? 4.67800   20.99200  19.18400  1.000 16.74938  ? 156  SER A C     1 
ATOM   1231 O  O     . SER A 1 156 ? 4.18900   21.18900  18.06700  1.000 18.98649  ? 156  SER A O     1 
ATOM   1232 C  CB    . SER A 1 156 ? 3.69200   19.59900  21.01300  1.000 19.12335  ? 156  SER A CB    1 
ATOM   1233 O  OG    . SER A 1 156 ? 2.36400   19.84500  20.57300  1.000 24.30028  ? 156  SER A OG    1 
ATOM   1234 N  N     . MET A 1 157 ? 5.25500   21.97000  19.88600  1.000 16.77833  ? 157  MET A N     1 
ATOM   1235 C  CA    . MET A 1 157 ? 5.33200   23.32000  19.33800  1.000 17.28628  ? 157  MET A CA    1 
ATOM   1236 C  C     . MET A 1 157 ? 6.14700   23.34900  18.04700  1.000 16.12299  ? 157  MET A C     1 
ATOM   1237 O  O     . MET A 1 157 ? 5.78200   24.04000  17.08400  1.000 18.88911  ? 157  MET A O     1 
ATOM   1238 C  CB    . MET A 1 157 ? 5.90800   24.27000  20.39200  1.000 18.93122  ? 157  MET A CB    1 
ATOM   1239 C  CG    . MET A 1 157 ? 6.10700   25.69400  19.89500  1.000 20.90777  ? 157  MET A CG    1 
ATOM   1240 S  SD    . MET A 1 157 ? 6.34700   26.85700  21.25200  1.000 22.91064  ? 157  MET A SD    1 
ATOM   1241 C  CE    . MET A 1 157 ? 4.72600   26.82900  22.05200  1.000 24.05288  ? 157  MET A CE    1 
ATOM   1242 N  N     . VAL A 1 158 ? 7.25200   22.59600  18.00600  1.000 17.38103  ? 158  VAL A N     1 
ATOM   1243 C  CA    . VAL A 1 158 ? 8.10800   22.57400  16.82000  1.000 15.69925  ? 158  VAL A CA    1 
ATOM   1244 C  C     . VAL A 1 158 ? 7.35700   22.00600  15.61900  1.000 14.40436  ? 158  VAL A C     1 
ATOM   1245 O  O     . VAL A 1 158 ? 7.35500   22.60200  14.53300  1.000 16.98098  ? 158  VAL A O     1 
ATOM   1246 C  CB    . VAL A 1 158 ? 9.42100   21.81200  17.09600  1.000 17.07047  ? 158  VAL A CB    1 
ATOM   1247 C  CG1   . VAL A 1 158 ? 10.26500  21.69400  15.82200  1.000 17.78108  ? 158  VAL A CG1   1 
ATOM   1248 C  CG2   . VAL A 1 158 ? 10.21500  22.50600  18.19600  1.000 18.69435  ? 158  VAL A CG2   1 
ATOM   1249 N  N     . ILE A 1 159 ? 6.72700   20.84000  15.78200  1.000 14.61228  ? 159  ILE A N     1 
ATOM   1250 C  CA    . ILE A 1 159 ? 6.04600   20.24400  14.63300  1.000 14.92284  ? 159  ILE A CA    1 
ATOM   1251 C  C     . ILE A 1 159 ? 4.83300   21.06900  14.22200  1.000 17.42314  ? 159  ILE A C     1 
ATOM   1252 O  O     . ILE A 1 159 ? 4.51000   21.14800  13.03000  1.000 16.78886  ? 159  ILE A O     1 
ATOM   1253 C  CB    . ILE A 1 159 ? 5.71200   18.75000  14.83900  1.000 15.10181  ? 159  ILE A CB    1 
ATOM   1254 C  CG1   . ILE A 1 159 ? 5.47000   18.06600  13.48100  1.000 16.69411  ? 159  ILE A CG1   1 
ATOM   1255 C  CG2   . ILE A 1 159 ? 4.49600   18.55800  15.74800  1.000 17.16522  ? 159  ILE A CG2   1 
ATOM   1256 C  CD1   . ILE A 1 159 ? 6.71000   17.88400  12.64700  1.000 18.96806  ? 159  ILE A CD1   1 
ATOM   1257 N  N     . CYS A 1 160 ? 4.13500   21.69300  15.17900  1.000 16.44408  ? 160  CYS A N     1 
ATOM   1258 C  CA    . CYS A 1 160 ? 2.99100   22.51100  14.79400  1.000 17.43630  ? 160  CYS A CA    1 
ATOM   1259 C  C     . CYS A 1 160 ? 3.42400   23.68300  13.92500  1.000 17.69949  ? 160  CYS A C     1 
ATOM   1260 O  O     . CYS A 1 160 ? 2.73600   24.03900  12.95900  1.000 18.24429  ? 160  CYS A O     1 
ATOM   1261 C  CB    . CYS A 1 160 ? 2.20000   22.97000  16.02600  1.000 19.15230  ? 160  CYS A CB    1 
ATOM   1262 S  SG    . CYS A 1 160 ? 1.27900   21.61200  16.76000  1.000 22.40532  ? 160  CYS A SG    1 
ATOM   1263 N  N     . ARG A 1 161 ? 4.57200   24.28800  14.23900  1.000 20.04977  ? 161  ARG A N     1 
ATOM   1264 C  CA    . ARG A 1 161 ? 5.06600   25.38100  13.40900  1.000 19.58393  ? 161  ARG A CA    1 
ATOM   1265 C  C     . ARG A 1 161 ? 5.43400   24.88400  12.01600  1.000 18.44695  ? 161  ARG A C     1 
ATOM   1266 O  O     . ARG A 1 161 ? 5.12400   25.53700  11.01100  1.000 20.49983  ? 161  ARG A O     1 
ATOM   1267 C  CB    . ARG A 1 161 ? 6.24700   26.06700  14.09600  1.000 25.04511  ? 161  ARG A CB    1 
ATOM   1268 C  CG    . ARG A 1 161 ? 6.54900   27.45000  13.56500  1.000 29.19561  ? 161  ARG A CG    1 
ATOM   1269 C  CD    . ARG A 1 161 ? 5.29300   28.31200  13.51800  1.000 29.44564  ? 161  ARG A CD    1 
ATOM   1270 N  NE    . ARG A 1 161 ? 5.03400   29.05500  14.74800  1.000 30.27468  ? 161  ARG A NE    1 
ATOM   1271 C  CZ    . ARG A 1 161 ? 4.11000   30.00400  14.85000  1.000 31.14584  ? 161  ARG A CZ    1 
ATOM   1272 N  NH1   . ARG A 1 161 ? 3.33500   30.32600  13.82600  1.000 29.33246  ? 161  ARG A NH1   1 
ATOM   1273 N  NH2   . ARG A 1 161 ? 3.96700   30.65300  16.00200  1.000 30.47471  ? 161  ARG A NH2   1 
ATOM   1274 N  N     . LEU A 1 162 ? 6.06800   23.71300  11.93600  1.000 16.23089  ? 162  LEU A N     1 
ATOM   1275 C  CA    . LEU A 1 162 ? 6.39500   23.14700  10.62800  1.000 16.49935  ? 162  LEU A CA    1 
ATOM   1276 C  C     . LEU A 1 162 ? 5.13100   22.90600  9.81000   1.000 17.28628  ? 162  LEU A C     1 
ATOM   1277 O  O     . LEU A 1 162 ? 5.11000   23.13800  8.59100   1.000 17.90215  ? 162  LEU A O     1 
ATOM   1278 C  CB    . LEU A 1 162 ? 7.17100   21.84300  10.81900  1.000 16.09140  ? 162  LEU A CB    1 
ATOM   1279 C  CG    . LEU A 1 162 ? 7.67300   21.10800  9.57000   1.000 16.07298  ? 162  LEU A CG    1 
ATOM   1280 C  CD1   . LEU A 1 162 ? 8.94000   20.32900  9.87400   1.000 18.22587  ? 162  LEU A CD1   1 
ATOM   1281 C  CD2   . LEU A 1 162 ? 6.61800   20.16200  8.95600   1.000 19.02070  ? 162  LEU A CD2   1 
ATOM   1282 N  N     . LEU A 1 163 ? 4.06800   22.43400  10.46500  1.000 15.47554  ? 163  LEU A N     1 
ATOM   1283 C  CA    . LEU A 1 163 ? 2.83500   22.07200  9.77300   1.000 15.68083  ? 163  LEU A CA    1 
ATOM   1284 C  C     . LEU A 1 163 ? 1.91200   23.25500  9.50700   1.000 15.37553  ? 163  LEU A C     1 
ATOM   1285 O  O     . LEU A 1 163 ? 1.05800   23.15700  8.61600   1.000 16.57304  ? 163  LEU A O     1 
ATOM   1286 C  CB    . LEU A 1 163 ? 2.05800   21.03200  10.58600  1.000 16.75990  ? 163  LEU A CB    1 
ATOM   1287 C  CG    . LEU A 1 163 ? 2.66900   19.63100  10.68200  1.000 15.51765  ? 163  LEU A CG    1 
ATOM   1288 C  CD1   . LEU A 1 163 ? 1.90100   18.79500  11.69400  1.000 15.93349  ? 163  LEU A CD1   1 
ATOM   1289 C  CD2   . LEU A 1 163 ? 2.67700   18.95300  9.29900   1.000 18.98649  ? 163  LEU A CD2   1 
ATOM   1290 N  N     . GLY A 1 164 ? 2.03000   24.34300  10.27000  1.000 15.81242  ? 164  GLY A N     1 
ATOM   1291 C  CA    . GLY A 1 164 ? 1.01800   25.38000  10.22100  1.000 17.27312  ? 164  GLY A CA    1 
ATOM   1292 C  C     . GLY A 1 164 ? -0.20300  25.09200  11.06300  1.000 18.32851  ? 164  GLY A C     1 
ATOM   1293 O  O     . GLY A 1 164 ? -1.28100  25.61300  10.77700  1.000 21.10779  ? 164  GLY A O     1 
ATOM   1294 N  N     . VAL A 1 165 ? -0.06800  24.25500  12.08500  1.000 17.81266  ? 165  VAL A N     1 
ATOM   1295 C  CA    . VAL A 1 165 ? -1.14300  23.98600  13.03500  1.000 18.58644  ? 165  VAL A CA    1 
ATOM   1296 C  C     . VAL A 1 165 ? -1.00900  24.98800  14.17700  1.000 17.83635  ? 165  VAL A C     1 
ATOM   1297 O  O     . VAL A 1 165 ? 0.06800   25.06300  14.79200  1.000 19.48392  ? 165  VAL A O     1 
ATOM   1298 C  CB    . VAL A 1 165 ? -1.03500  22.54600  13.55700  1.000 18.87068  ? 165  VAL A CB    1 
ATOM   1299 C  CG1   . VAL A 1 165 ? -1.97700  22.31200  14.72600  1.000 19.69183  ? 165  VAL A CG1   1 
ATOM   1300 C  CG2   . VAL A 1 165 ? -1.33600  21.55600  12.43000  1.000 18.96017  ? 165  VAL A CG2   1 
ATOM   1301 N  N     . PRO A 1 166 ? -2.04600  25.77200  14.48800  1.000 19.11545  ? 166  PRO A N     1 
ATOM   1302 C  CA    . PRO A 1 166 ? -1.90300  26.80500  15.52800  1.000 19.67078  ? 166  PRO A CA    1 
ATOM   1303 C  C     . PRO A 1 166 ? -1.78900  26.18900  16.91600  1.000 21.25781  ? 166  PRO A C     1 
ATOM   1304 O  O     . PRO A 1 166 ? -2.63800  25.39700  17.33700  1.000 22.56850  ? 166  PRO A O     1 
ATOM   1305 C  CB    . PRO A 1 166 ? -3.17100  27.65700  15.37700  1.000 22.38163  ? 166  PRO A CB    1 
ATOM   1306 C  CG    . PRO A 1 166 ? -4.13500  26.81100  14.66000  1.000 22.69219  ? 166  PRO A CG    1 
ATOM   1307 C  CD    . PRO A 1 166 ? -3.35500  25.84000  13.81100  1.000 20.07872  ? 166  PRO A CD    1 
ATOM   1308 N  N     . TYR A 1 167 ? -0.73300  26.57300  17.63600  1.000 21.26044  ? 167  TYR A N     1 
ATOM   1309 C  CA    . TYR A 1 167 ? -0.49600  25.95600  18.93400  1.000 24.66348  ? 167  TYR A CA    1 
ATOM   1310 C  C     . TYR A 1 167 ? -1.53700  26.34800  19.97700  1.000 25.49516  ? 167  TYR A C     1 
ATOM   1311 O  O     . TYR A 1 167 ? -1.59900  25.70400  21.02800  1.000 26.86112  ? 167  TYR A O     1 
ATOM   1312 C  CB    . TYR A 1 167 ? 0.91600   26.25900  19.43700  1.000 24.38187  ? 167  TYR A CB    1 
ATOM   1313 C  CG    . TYR A 1 167 ? 1.34900   25.36400  20.57600  1.000 24.10026  ? 167  TYR A CG    1 
ATOM   1314 C  CD1   . TYR A 1 167 ? 1.78200   24.07500  20.32700  1.000 23.16330  ? 167  TYR A CD1   1 
ATOM   1315 C  CD2   . TYR A 1 167 ? 1.32000   25.80700  21.90500  1.000 25.27935  ? 167  TYR A CD2   1 
ATOM   1316 C  CE1   . TYR A 1 167 ? 2.17500   23.23800  21.35300  1.000 25.75046  ? 167  TYR A CE1   1 
ATOM   1317 C  CE2   . TYR A 1 167 ? 1.72300   24.97600  22.94600  1.000 25.79783  ? 167  TYR A CE2   1 
ATOM   1318 C  CZ    . TYR A 1 167 ? 2.14300   23.69100  22.66100  1.000 25.38989  ? 167  TYR A CZ    1 
ATOM   1319 O  OH    . TYR A 1 167 ? 2.53900   22.85100  23.67900  1.000 26.33210  ? 167  TYR A OH    1 
ATOM   1320 N  N     . ALA A 1 168 ? -2.35700  27.37100  19.71500  1.000 26.72426  ? 168  ALA A N     1 
ATOM   1321 C  CA    . ALA A 1 168 ? -3.41500  27.73700  20.65400  1.000 29.04822  ? 168  ALA A CA    1 
ATOM   1322 C  C     . ALA A 1 168 ? -4.37900  26.58800  20.92000  1.000 30.17993  ? 168  ALA A C     1 
ATOM   1323 O  O     . ALA A 1 168 ? -5.05700  26.58700  21.95300  1.000 33.45927  ? 168  ALA A O     1 
ATOM   1324 C  CB    . ALA A 1 168 ? -4.18900  28.95500  20.14200  1.000 32.50127  ? 168  ALA A CB    1 
ATOM   1325 N  N     . ASP A 1 169 ? -4.45400  25.60800  20.02100  1.000 27.30327  ? 169  ASP A N     1 
ATOM   1326 C  CA    . ASP A 1 169 ? -5.35200  24.47500  20.17800  1.000 28.02704  ? 169  ASP A CA    1 
ATOM   1327 C  C     . ASP A 1 169 ? -4.65800  23.26100  20.77900  1.000 26.78479  ? 169  ASP A C     1 
ATOM   1328 O  O     . ASP A 1 169 ? -5.18100  22.14700  20.68200  1.000 26.72952  ? 169  ASP A O     1 
ATOM   1329 C  CB    . ASP A 1 169 ? -5.98100  24.12500  18.82900  1.000 28.27971  ? 169  ASP A CB    1 
ATOM   1330 C  CG    . ASP A 1 169 ? -6.72900  25.29900  18.21600  1.000 31.16689  ? 169  ASP A CG    1 
ATOM   1331 O  OD1   . ASP A 1 169 ? -7.40500  26.02900  18.97200  1.000 36.51227  ? 169  ASP A OD1   1 
ATOM   1332 O  OD2   . ASP A 1 169 ? -6.64000  25.49800  16.98200  1.000 30.37206  ? 169  ASP A OD2   1 
ATOM   1333 N  N     . HIS A 1 170 ? -3.50700  23.45900  21.42400  1.000 25.08459  ? 170  HIS A N     1 
ATOM   1334 C  CA    . HIS A 1 170 ? -2.64300  22.33300  21.77200  1.000 24.75297  ? 170  HIS A CA    1 
ATOM   1335 C  C     . HIS A 1 170 ? -3.27200  21.40200  22.80700  1.000 23.14225  ? 170  HIS A C     1 
ATOM   1336 O  O     . HIS A 1 170 ? -3.04600  20.18900  22.76200  1.000 23.80812  ? 170  HIS A O     1 
ATOM   1337 C  CB    . HIS A 1 170 ? -1.26800  22.82300  22.22000  1.000 24.48451  ? 170  HIS A CB    1 
ATOM   1338 C  CG    . HIS A 1 170 ? -1.27100  23.49700  23.55500  1.000 26.90059  ? 170  HIS A CG    1 
ATOM   1339 N  ND1   . HIS A 1 170 ? -1.45600  24.85600  23.70300  1.000 27.74280  ? 170  HIS A ND1   1 
ATOM   1340 C  CD2   . HIS A 1 170 ? -1.11400  22.99900  24.80500  1.000 29.21929  ? 170  HIS A CD2   1 
ATOM   1341 C  CE1   . HIS A 1 170 ? -1.40400  25.16600  24.98600  1.000 30.36154  ? 170  HIS A CE1   1 
ATOM   1342 N  NE2   . HIS A 1 170 ? -1.19600  24.05700  25.67600  1.000 29.34562  ? 170  HIS A NE2   1 
ATOM   1343 N  N     . GLU A 1 171 ? -4.03700  21.92800  23.76400  1.000 26.21367  ? 171  GLU A N     1 
ATOM   1344 C  CA    . GLU A 1 171 ? -4.66300  21.02200  24.72300  1.000 29.50880  ? 171  GLU A CA    1 
ATOM   1345 C  C     . GLU A 1 171 ? -5.58000  20.02500  24.02000  1.000 28.95347  ? 171  GLU A C     1 
ATOM   1346 O  O     . GLU A 1 171 ? -5.57400  18.82900  24.34000  1.000 29.24298  ? 171  GLU A O     1 
ATOM   1347 C  CB    . GLU A 1 171 ? -5.39100  21.80300  25.81700  1.000 32.95658  ? 171  GLU A CB    1 
ATOM   1348 C  CG    . GLU A 1 171 ? -4.42300  22.52600  26.74900  1.000 39.27839  ? 171  GLU A CG    1 
ATOM   1349 C  CD    . GLU A 1 171 ? -5.06500  23.02000  28.03600  1.000 46.31871  ? 171  GLU A CD    1 
ATOM   1350 O  OE1   . GLU A 1 171 ? -6.29100  22.84100  28.21500  1.000 49.39276  ? 171  GLU A OE1   1 
ATOM   1351 O  OE2   . GLU A 1 171 ? -4.33300  23.58800  28.87400  1.000 48.99535  ? 171  GLU A OE2   1 
ATOM   1352 N  N     . PHE A 1 172 ? -6.34000  20.48900  23.02900  1.000 26.69267  ? 172  PHE A N     1 
ATOM   1353 C  CA    . PHE A 1 172 ? -7.20400  19.58800  22.27600  1.000 24.77402  ? 172  PHE A CA    1 
ATOM   1354 C  C     . PHE A 1 172 ? -6.39700  18.54600  21.50400  1.000 23.80285  ? 172  PHE A C     1 
ATOM   1355 O  O     . PHE A 1 172 ? -6.62100  17.33500  21.64700  1.000 24.13447  ? 172  PHE A O     1 
ATOM   1356 C  CB    . PHE A 1 172 ? -8.10400  20.38000  21.32500  1.000 25.84784  ? 172  PHE A CB    1 
ATOM   1357 C  CG    . PHE A 1 172 ? -8.78900  19.52100  20.31000  1.000 27.97441  ? 172  PHE A CG    1 
ATOM   1358 C  CD1   . PHE A 1 172 ? -9.93600  18.82500  20.63700  1.000 32.72498  ? 172  PHE A CD1   1 
ATOM   1359 C  CD2   . PHE A 1 172 ? -8.26400  19.37900  19.03400  1.000 29.85095  ? 172  PHE A CD2   1 
ATOM   1360 C  CE1   . PHE A 1 172 ? -10.55800 18.01800  19.70100  1.000 33.65404  ? 172  PHE A CE1   1 
ATOM   1361 C  CE2   . PHE A 1 172 ? -8.88100  18.57400  18.10600  1.000 33.02764  ? 172  PHE A CE2   1 
ATOM   1362 C  CZ    . PHE A 1 172 ? -10.03200 17.89600  18.44000  1.000 33.89091  ? 172  PHE A CZ    1 
ATOM   1363 N  N     . PHE A 1 173 ? -5.46100  18.98800  20.66000  1.000 22.70009  ? 173  PHE A N     1 
ATOM   1364 C  CA    . PHE A 1 173 ? -4.83400  18.01100  19.77100  1.000 20.30770  ? 173  PHE A CA    1 
ATOM   1365 C  C     . PHE A 1 173 ? -3.79300  17.15100  20.47700  1.000 19.94186  ? 173  PHE A C     1 
ATOM   1366 O  O     . PHE A 1 173 ? -3.56300  16.00800  20.06300  1.000 20.66564  ? 173  PHE A O     1 
ATOM   1367 C  CB    . PHE A 1 173 ? -4.36000  18.61200  18.43200  1.000 20.97357  ? 173  PHE A CB    1 
ATOM   1368 C  CG    . PHE A 1 173 ? -3.32900  19.70700  18.55300  1.000 21.22097  ? 173  PHE A CG    1 
ATOM   1369 C  CD1   . PHE A 1 173 ? -2.03500  19.42700  18.96100  1.000 22.49217  ? 173  PHE A CD1   1 
ATOM   1370 C  CD2   . PHE A 1 173 ? -3.64700  21.01200  18.20500  1.000 23.31859  ? 173  PHE A CD2   1 
ATOM   1371 C  CE1   . PHE A 1 173 ? -1.08100  20.42800  19.04100  1.000 22.67903  ? 173  PHE A CE1   1 
ATOM   1372 C  CE2   . PHE A 1 173 ? -2.70000  22.02300  18.28800  1.000 23.21331  ? 173  PHE A CE2   1 
ATOM   1373 C  CZ    . PHE A 1 173 ? -1.41600  21.72900  18.71200  1.000 24.58716  ? 173  PHE A CZ    1 
ATOM   1374 N  N     . GLN A 1 174 ? -3.18000  17.65100  21.55300  1.000 20.96041  ? 174  GLN A N     1 
ATOM   1375 C  CA    . GLN A 1 174 ? -2.28000  16.79200  22.31900  1.000 21.42099  ? 174  GLN A CA    1 
ATOM   1376 C  C     . GLN A 1 174 ? -3.05200  15.67800  23.01200  1.000 22.10528  ? 174  GLN A C     1 
ATOM   1377 O  O     . GLN A 1 174 ? -2.61900  14.51600  23.00800  1.000 23.85812  ? 174  GLN A O     1 
ATOM   1378 C  CB    . GLN A 1 174 ? -1.48300  17.61600  23.33100  1.000 22.55270  ? 174  GLN A CB    1 
ATOM   1379 C  CG    . GLN A 1 174 ? -0.41400  18.48200  22.68500  1.000 21.02357  ? 174  GLN A CG    1 
ATOM   1380 C  CD    . GLN A 1 174 ? 0.16900   19.49700  23.64800  1.000 25.28461  ? 174  GLN A CD    1 
ATOM   1381 O  OE1   . GLN A 1 174 ? -0.26800  19.60000  24.79600  1.000 25.82152  ? 174  GLN A OE1   1 
ATOM   1382 N  NE2   . GLN A 1 174 ? 1.16600   20.25000  23.18800  1.000 24.05288  ? 174  GLN A NE2   1 
ATOM   1383 N  N     . ASP A 1 175 ? -4.20200  16.01300  23.60400  1.000 22.33426  ? 175  ASP A N     1 
ATOM   1384 C  CA    . ASP A 1 175 ? -5.02700  14.98500  24.22300  1.000 25.51622  ? 175  ASP A CA    1 
ATOM   1385 C  C     . ASP A 1 175 ? -5.51400  13.97300  23.19300  1.000 25.05037  ? 175  ASP A C     1 
ATOM   1386 O  O     . ASP A 1 175 ? -5.50000  12.76300  23.44800  1.000 26.38737  ? 175  ASP A O     1 
ATOM   1387 C  CB    . ASP A 1 175 ? -6.20800  15.62600  24.94700  1.000 27.30064  ? 175  ASP A CB    1 
ATOM   1388 C  CG    . ASP A 1 175 ? -7.15600  14.59800  25.52900  1.000 31.40113  ? 175  ASP A CG    1 
ATOM   1389 O  OD1   . ASP A 1 175 ? -6.82000  13.99000  26.57200  1.000 36.28593  ? 175  ASP A OD1   1 
ATOM   1390 O  OD2   . ASP A 1 175 ? -8.23100  14.39100  24.93400  1.000 32.98290  ? 175  ASP A OD2   1 
ATOM   1391 N  N     . ALA A 1 176 ? -5.95200  14.44400  22.02000  1.000 22.54218  ? 176  ALA A N     1 
ATOM   1392 C  CA    . ALA A 1 176 ? -6.43700  13.51400  21.00600  1.000 22.67377  ? 176  ALA A CA    1 
ATOM   1393 C  C     . ALA A 1 176 ? -5.31300  12.62500  20.49000  1.000 22.13160  ? 176  ALA A C     1 
ATOM   1394 O  O     . ALA A 1 176 ? -5.52200  11.43200  20.24200  1.000 22.96854  ? 176  ALA A O     1 
ATOM   1395 C  CB    . ALA A 1 176 ? -7.12100  14.27000  19.86900  1.000 22.10265  ? 176  ALA A CB    1 
ATOM   1396 N  N     . SER A 1 177 ? -4.11300  13.18600  20.32900  1.000 21.63154  ? 177  SER A N     1 
ATOM   1397 C  CA    . SER A 1 177 ? -2.97300  12.38800  19.89000  1.000 22.53954  ? 177  SER A CA    1 
ATOM   1398 C  C     . SER A 1 177 ? -2.66100  11.29000  20.89700  1.000 24.74770  ? 177  SER A C     1 
ATOM   1399 O  O     . SER A 1 177 ? -2.41900  10.13500  20.52500  1.000 24.55031  ? 177  SER A O     1 
ATOM   1400 C  CB    . SER A 1 177 ? -1.76400  13.30800  19.71500  1.000 22.31057  ? 177  SER A CB    1 
ATOM   1401 O  OG    . SER A 1 177 ? -0.57500  12.60500  19.39100  1.000 23.40544  ? 177  SER A OG    1 
ATOM   1402 N  N     . LYS A 1 178 ? -2.66600  11.63200  22.18200  1.000 24.32134  ? 178  LYS A N     1 
ATOM   1403 C  CA    . LYS A 1 178 ? -2.39900  10.63400  23.21100  1.000 26.58477  ? 178  LYS A CA    1 
ATOM   1404 C  C     . LYS A 1 178 ? -3.44800  9.52800   23.19400  1.000 26.40580  ? 178  LYS A C     1 
ATOM   1405 O  O     . LYS A 1 178 ? -3.11800  8.33800   23.28600  1.000 27.80333  ? 178  LYS A O     1 
ATOM   1406 C  CB    . LYS A 1 178 ? -2.36500  11.31400  24.57600  1.000 28.89031  ? 178  LYS A CB    1 
ATOM   1407 C  CG    . LYS A 1 178 ? -2.08200  10.37400  25.72900  1.000 32.94342  ? 178  LYS A CG    1 
ATOM   1408 C  CD    . LYS A 1 178 ? -2.06600  11.13100  27.03400  1.000 37.89139  ? 178  LYS A CD    1 
ATOM   1409 C  CE    . LYS A 1 178 ? -1.45400  10.29000  28.13500  1.000 44.45270  ? 178  LYS A CE    1 
ATOM   1410 N  NZ    . LYS A 1 178 ? -1.35100  11.05500  29.40700  1.000 47.24777  ? 178  LYS A NZ    1 
ATOM   1411 N  N     . ARG A 1 179 ? -4.72500  9.90500   23.09100  1.000 25.16354  ? 179  ARG A N     1 
ATOM   1412 C  CA    . ARG A 1 179 ? -5.78700  8.90500   23.07600  1.000 25.92942  ? 179  ARG A CA    1 
ATOM   1413 C  C     . ARG A 1 179 ? -5.65600  7.97700   21.87700  1.000 28.79819  ? 179  ARG A C     1 
ATOM   1414 O  O     . ARG A 1 179 ? -5.94800  6.77800   21.97400  1.000 31.50641  ? 179  ARG A O     1 
ATOM   1415 C  CB    . ARG A 1 179 ? -7.15400  9.58800   23.08400  1.000 28.03757  ? 179  ARG A CB    1 
ATOM   1416 C  CG    . ARG A 1 179 ? -7.51000  10.25400  24.40600  1.000 29.95359  ? 179  ARG A CG    1 
ATOM   1417 C  CD    . ARG A 1 179 ? -8.93800  10.79200  24.40300  1.000 29.73778  ? 179  ARG A CD    1 
ATOM   1418 N  NE    . ARG A 1 179 ? -9.08200  12.04800  23.67300  1.000 34.36201  ? 179  ARG A NE    1 
ATOM   1419 C  CZ    . ARG A 1 179 ? -9.83600  12.21800  22.59500  1.000 33.79089  ? 179  ARG A CZ    1 
ATOM   1420 N  NH1   . ARG A 1 179 ? -10.50100 11.21200  22.04700  1.000 35.23054  ? 179  ARG A NH1   1 
ATOM   1421 N  NH2   . ARG A 1 179 ? -9.93400  13.42900  22.05600  1.000 33.62772  ? 179  ARG A NH2   1 
ATOM   1422 N  N     . LEU A 1 180 ? -5.20400  8.50600   20.74000  1.000 27.01377  ? 180  LEU A N     1 
ATOM   1423 C  CA    . LEU A 1 180 ? -5.09000  7.67600   19.54600  1.000 26.95586  ? 180  LEU A CA    1 
ATOM   1424 C  C     . LEU A 1 180 ? -3.92900  6.69000   19.64800  1.000 26.36369  ? 180  LEU A C     1 
ATOM   1425 O  O     . LEU A 1 180 ? -4.10200  5.49000   19.40200  1.000 27.37697  ? 180  LEU A O     1 
ATOM   1426 C  CB    . LEU A 1 180 ? -4.97400  8.55200   18.29700  1.000 25.14249  ? 180  LEU A CB    1 
ATOM   1427 C  CG    . LEU A 1 180 ? -4.88800  7.74200   17.00400  1.000 28.82977  ? 180  LEU A CG    1 
ATOM   1428 C  CD1   . LEU A 1 180 ? -5.99500  6.69400   16.94900  1.000 32.78288  ? 180  LEU A CD1   1 
ATOM   1429 C  CD2   . LEU A 1 180 ? -4.97900  8.67600   15.81600  1.000 31.60642  ? 180  LEU A CD2   1 
ATOM   1430 N  N     . VAL A 1 181 ? -2.73400  7.16700   20.00900  1.000 25.23460  ? 181  VAL A N     1 
ATOM   1431 C  CA    . VAL A 1 181 ? -1.59200  6.25000   20.01400  1.000 23.68705  ? 181  VAL A CA    1 
ATOM   1432 C  C     . VAL A 1 181 ? -1.64400  5.26900   21.17600  1.000 28.80609  ? 181  VAL A C     1 
ATOM   1433 O  O     . VAL A 1 181 ? -1.08100  4.17100   21.08100  1.000 30.20099  ? 181  VAL A O     1 
ATOM   1434 C  CB    . VAL A 1 181 ? -0.24300  6.98300   19.95500  1.000 29.06401  ? 181  VAL A CB    1 
ATOM   1435 C  CG1   . VAL A 1 181 ? -0.24600  7.93000   18.81700  1.000 30.51945  ? 181  VAL A CG1   1 
ATOM   1436 C  CG2   . VAL A 1 181 ? 0.05800   7.68600   21.27900  1.000 33.66983  ? 181  VAL A CG2   1 
ATOM   1437 N  N     . GLN A 1 182 ? -2.29000  5.63300   22.28400  1.000 27.58225  ? 182  GLN A N     1 
ATOM   1438 C  CA    . GLN A 1 182 ? -2.34300  4.77700   23.46300  1.000 30.37469  ? 182  GLN A CA    1 
ATOM   1439 C  C     . GLN A 1 182 ? -3.67800  4.05600   23.62600  1.000 32.12490  ? 182  GLN A C     1 
ATOM   1440 O  O     . GLN A 1 182 ? -3.89400  3.39300   24.64800  1.000 33.52507  ? 182  GLN A O     1 
ATOM   1441 C  CB    . GLN A 1 182 ? -2.00300  5.57900   24.71900  1.000 30.87212  ? 182  GLN A CB    1 
ATOM   1442 C  CG    . GLN A 1 182 ? -0.61000  6.17200   24.69100  1.000 30.46944  ? 182  GLN A CG    1 
ATOM   1443 C  CD    . GLN A 1 182 ? -0.14200  6.61800   26.06200  1.000 34.99104  ? 182  GLN A CD    1 
ATOM   1444 O  OE1   . GLN A 1 182 ? -0.49300  6.01500   27.07200  1.000 36.13328  ? 182  GLN A OE1   1 
ATOM   1445 N  NE2   . GLN A 1 182 ? 0.65500   7.68100   26.10300  1.000 36.88863  ? 182  GLN A NE2   1 
ATOM   1446 N  N     . SER A 1 183 ? -4.56800  4.16700   22.64300  1.000 30.85107  ? 183  SER A N     1 
ATOM   1447 C  CA    . SER A 1 183 ? -5.85400  3.48400   22.69100  1.000 31.91962  ? 183  SER A CA    1 
ATOM   1448 C  C     . SER A 1 183 ? -5.65900  1.98000   22.80900  1.000 32.58022  ? 183  SER A C     1 
ATOM   1449 O  O     . SER A 1 183 ? -4.82900  1.38900   22.11400  1.000 31.99068  ? 183  SER A O     1 
ATOM   1450 C  CB    . SER A 1 183 ? -6.63000  3.77600   21.40900  1.000 34.27779  ? 183  SER A CB    1 
ATOM   1451 O  OG    . SER A 1 183 ? -5.81800  3.53800   20.27000  1.000 36.28593  ? 183  SER A OG    1 
ATOM   1452 N  N     . THR A 1 184 ? -6.44700  1.35600   23.68000  1.000 35.92536  ? 184  THR A N     1 
ATOM   1453 C  CA    . THR A 1 184 ? -6.41800  -0.09100  23.84100  1.000 36.19381  ? 184  THR A CA    1 
ATOM   1454 C  C     . THR A 1 184 ? -7.59400  -0.79100  23.17400  1.000 37.30447  ? 184  THR A C     1 
ATOM   1455 O  O     . THR A 1 184 ? -7.59800  -2.02600  23.09500  1.000 38.01245  ? 184  THR A O     1 
ATOM   1456 C  CB    . THR A 1 184 ? -6.36700  -0.45900  25.32800  1.000 39.16785  ? 184  THR A CB    1 
ATOM   1457 O  OG1   . THR A 1 184 ? -7.46000  0.17000   26.00600  1.000 40.35747  ? 184  THR A OG1   1 
ATOM   1458 C  CG2   . THR A 1 184 ? -5.04900  0.00700   25.94300  1.000 40.03112  ? 184  THR A CG2   1 
ATOM   1459 N  N     . ASP A 1 185 ? -8.58600  -0.04500  22.69600  1.000 36.51490  ? 185  ASP A N     1 
ATOM   1460 C  CA    . ASP A 1 185 ? -9.71300  -0.62000  21.98000  1.000 36.56754  ? 185  ASP A CA    1 
ATOM   1461 C  C     . ASP A 1 185 ? -9.97100  0.17900   20.71100  1.000 36.60702  ? 185  ASP A C     1 
ATOM   1462 O  O     . ASP A 1 185 ? -9.48600  1.30100   20.54500  1.000 36.55965  ? 185  ASP A O     1 
ATOM   1463 C  CB    . ASP A 1 185 ? -10.98200 -0.66200  22.83900  1.000 39.70739  ? 185  ASP A CB    1 
ATOM   1464 C  CG    . ASP A 1 185 ? -11.46300 0.71800   23.23900  1.000 43.82104  ? 185  ASP A CG    1 
ATOM   1465 O  OD1   . ASP A 1 185 ? -10.89800 1.29600   24.18900  1.000 47.17671  ? 185  ASP A OD1   1 
ATOM   1466 O  OD2   . ASP A 1 185 ? -12.40100 1.23100   22.59300  1.000 43.36836  ? 185  ASP A OD2   1 
ATOM   1467 N  N     . ALA A 1 186 ? -10.75800 -0.41900  19.81500  1.000 34.66468  ? 186  ALA A N     1 
ATOM   1468 C  CA    . ALA A 1 186 ? -11.00200 0.19300   18.51500  1.000 33.68035  ? 186  ALA A CA    1 
ATOM   1469 C  C     . ALA A 1 186 ? -11.86600 1.44300   18.63500  1.000 33.44348  ? 186  ALA A C     1 
ATOM   1470 O  O     . ALA A 1 186 ? -11.65300 2.42000   17.90900  1.000 33.61456  ? 186  ALA A O     1 
ATOM   1471 C  CB    . ALA A 1 186 ? -11.64900 -0.82100  17.57300  1.000 34.21726  ? 186  ALA A CB    1 
ATOM   1472 N  N     . GLN A 1 187 ? -12.84900 1.43500   19.53800  1.000 34.04356  ? 187  GLN A N     1 
ATOM   1473 C  CA    . GLN A 1 187 ? -13.77400 2.56200   19.60300  1.000 35.49373  ? 187  GLN A CA    1 
ATOM   1474 C  C     . GLN A 1 187 ? -13.08700 3.82500   20.10500  1.000 33.34610  ? 187  GLN A C     1 
ATOM   1475 O  O     . GLN A 1 187 ? -13.30000 4.91200   19.55500  1.000 34.07514  ? 187  GLN A O     1 
ATOM   1476 C  CB    . GLN A 1 187 ? -14.98400 2.22000   20.47100  1.000 40.92070  ? 187  GLN A CB    1 
ATOM   1477 C  CG    . GLN A 1 187 ? -16.00200 3.34100   20.53200  1.000 49.92967  ? 187  GLN A CG    1 
ATOM   1478 C  CD    . GLN A 1 187 ? -16.48600 3.75300   19.15500  1.000 56.56204  ? 187  GLN A CD    1 
ATOM   1479 O  OE1   . GLN A 1 187 ? -17.07500 2.95200   18.42600  1.000 59.95982  ? 187  GLN A OE1   1 
ATOM   1480 N  NE2   . GLN A 1 187 ? -16.22800 5.00600   18.78500  1.000 56.00935  ? 187  GLN A NE2   1 
ATOM   1481 N  N     . SER A 1 188 ? -12.26000 3.70800   21.14600  1.000 32.69076  ? 188  SER A N     1 
ATOM   1482 C  CA    A SER A 1 188 ? -11.53700 4.87600   21.63900  0.300 31.89067  ? 188  SER A CA    1 
ATOM   1483 C  CA    B SER A 1 188 ? -11.53700 4.87600   21.63900  0.700 32.89605  ? 188  SER A CA    1 
ATOM   1484 C  C     . SER A 1 188 ? -10.57200 5.40900   20.58700  1.000 31.03793  ? 188  SER A C     1 
ATOM   1485 O  O     . SER A 1 188 ? -10.38500 6.62700   20.46200  1.000 29.94570  ? 188  SER A O     1 
ATOM   1486 C  CB    A SER A 1 188 ? -10.79300 4.52600   22.92700  0.300 31.66169  ? 188  SER A CB    1 
ATOM   1487 C  CB    B SER A 1 188 ? -10.79100 4.52400   22.92500  0.700 33.80405  ? 188  SER A CB    1 
ATOM   1488 O  OG    A SER A 1 188 ? -9.82700  3.51800   22.69400  0.300 32.79341  ? 188  SER A OG    1 
ATOM   1489 O  OG    B SER A 1 188 ? -11.68900 4.06800   23.92100  0.700 35.74639  ? 188  SER A OG    1 
ATOM   1490 N  N     . ALA A 1 189 ? -9.95100  4.51100   19.82000  1.000 28.25339  ? 189  ALA A N     1 
ATOM   1491 C  CA    . ALA A 1 189 ? -9.05900  4.93600   18.74800  1.000 28.77713  ? 189  ALA A CA    1 
ATOM   1492 C  C     . ALA A 1 189 ? -9.83000  5.67300   17.66200  1.000 27.53225  ? 189  ALA A C     1 
ATOM   1493 O  O     . ALA A 1 189 ? -9.39300  6.72600   17.17600  1.000 27.88492  ? 189  ALA A O     1 
ATOM   1494 C  CB    . ALA A 1 189 ? -8.35900  3.71900   18.15200  1.000 31.22480  ? 189  ALA A CB    1 
ATOM   1495 N  N     . LEU A 1 190 ? -10.97900 5.12300   17.26600  1.000 26.33474  ? 190  LEU A N     1 
ATOM   1496 C  CA    . LEU A 1 190 ? -11.79000 5.75500   16.23300  1.000 27.03482  ? 190  LEU A CA    1 
ATOM   1497 C  C     . LEU A 1 190 ? -12.25500 7.13600   16.67400  1.000 25.96627  ? 190  LEU A C     1 
ATOM   1498 O  O     . LEU A 1 190 ? -12.24900 8.08300   15.88000  1.000 27.45856  ? 190  LEU A O     1 
ATOM   1499 C  CB    . LEU A 1 190 ? -12.98700 4.86700   15.89400  1.000 29.77462  ? 190  LEU A CB    1 
ATOM   1500 C  CG    . LEU A 1 190 ? -14.02100 5.49000   14.95000  1.000 36.09380  ? 190  LEU A CG    1 
ATOM   1501 C  CD1   . LEU A 1 190 ? -13.39700 5.76300   13.59900  1.000 39.09416  ? 190  LEU A CD1   1 
ATOM   1502 C  CD2   . LEU A 1 190 ? -15.25500 4.60700   14.81300  1.000 40.72067  ? 190  LEU A CD2   1 
ATOM   1503 N  N     . THR A 1 191 ? -12.66300 7.27200   17.93800  1.000 27.41118  ? 191  THR A N     1 
ATOM   1504 C  CA    . THR A 1 191 ? -13.09800 8.57200   18.43800  1.000 26.60056  ? 191  THR A CA    1 
ATOM   1505 C  C     . THR A 1 191 ? -11.96400 9.58700   18.38500  1.000 27.29801  ? 191  THR A C     1 
ATOM   1506 O  O     . THR A 1 191 ? -12.15300 10.72300  17.93000  1.000 27.34802  ? 191  THR A O     1 
ATOM   1507 C  CB    . THR A 1 191 ? -13.62200 8.43800   19.86700  1.000 29.85358  ? 191  THR A CB    1 
ATOM   1508 O  OG1   . THR A 1 191 ? -14.79900 7.61800   19.87700  1.000 32.97764  ? 191  THR A OG1   1 
ATOM   1509 C  CG2   . THR A 1 191 ? -13.96400 9.80400   20.42700  1.000 31.21427  ? 191  THR A CG2   1 
ATOM   1510 N  N     . ALA A 1 192 ? -10.77300 9.19800   18.85000  1.000 26.07944  ? 192  ALA A N     1 
ATOM   1511 C  CA    . ALA A 1 192 ? -9.65100  10.12800  18.83600  1.000 24.62664  ? 192  ALA A CA    1 
ATOM   1512 C  C     . ALA A 1 192 ? -9.27700  10.50800  17.41000  1.000 23.10014  ? 192  ALA A C     1 
ATOM   1513 O  O     . ALA A 1 192 ? -8.97200  11.67400  17.12900  1.000 24.02656  ? 192  ALA A O     1 
ATOM   1514 C  CB    . ALA A 1 192 ? -8.44700  9.52800   19.56400  1.000 25.28987  ? 192  ALA A CB    1 
ATOM   1515 N  N     . ARG A 1 193 ? -9.30400  9.54100   16.49100  1.000 23.82128  ? 193  ARG A N     1 
ATOM   1516 C  CA    . ARG A 1 193 ? -8.96300  9.85100   15.10700  1.000 23.81075  ? 193  ARG A CA    1 
ATOM   1517 C  C     . ARG A 1 193 ? -9.97300  10.81000  14.49800  1.000 23.25279  ? 193  ARG A C     1 
ATOM   1518 O  O     . ARG A 1 193 ? -9.59300  11.76400  13.80600  1.000 25.01353  ? 193  ARG A O     1 
ATOM   1519 C  CB    . ARG A 1 193 ? -8.88000  8.58100   14.26500  1.000 25.29777  ? 193  ARG A CB    1 
ATOM   1520 C  CG    . ARG A 1 193 ? -8.15600  8.84100   12.96700  1.000 27.94546  ? 193  ARG A CG    1 
ATOM   1521 C  CD    . ARG A 1 193 ? -8.49400  7.86900   11.86700  1.000 33.89354  ? 193  ARG A CD    1 
ATOM   1522 N  NE    . ARG A 1 193 ? -7.68400  8.17600   10.69600  1.000 38.72833  ? 193  ARG A NE    1 
ATOM   1523 C  CZ    . ARG A 1 193 ? -8.00500  9.07800   9.77600   1.000 44.02896  ? 193  ARG A CZ    1 
ATOM   1524 N  NH1   . ARG A 1 193 ? -9.15500  9.73100   9.81900   1.000 45.17647  ? 193  ARG A NH1   1 
ATOM   1525 N  NH2   . ARG A 1 193 ? -7.15100  9.32900   8.79000   1.000 44.60535  ? 193  ARG A NH2   1 
ATOM   1526 N  N     . ASN A 1 194 ? -11.26500 10.57100  14.74200  1.000 23.87128  ? 194  ASN A N     1 
ATOM   1527 C  CA    . ASN A 1 194 ? -12.29400 11.46900  14.22200  1.000 25.18723  ? 194  ASN A CA    1 
ATOM   1528 C  C     . ASN A 1 194 ? -12.16100 12.86300  14.82200  1.000 26.20314  ? 194  ASN A C     1 
ATOM   1529 O  O     . ASN A 1 194 ? -12.40600 13.86800  14.13800  1.000 27.10588  ? 194  ASN A O     1 
ATOM   1530 C  CB    . ASN A 1 194 ? -13.68500 10.89800  14.50100  1.000 29.52459  ? 194  ASN A CB    1 
ATOM   1531 C  CG    . ASN A 1 194 ? -13.98000 9.65300   13.68900  1.000 35.23580  ? 194  ASN A CG    1 
ATOM   1532 O  OD1   . ASN A 1 194 ? -13.36600 9.40900   12.64700  1.000 39.68107  ? 194  ASN A OD1   1 
ATOM   1533 N  ND2   . ASN A 1 194 ? -14.93400 8.86100   14.16000  1.000 37.57819  ? 194  ASN A ND2   1 
ATOM   1534 N  N     . ASP A 1 195 ? -11.78000 12.94300  16.10100  1.000 25.72940  ? 195  ASP A N     1 
ATOM   1535 C  CA    . ASP A 1 195 ? -11.54600 14.24200  16.72700  1.000 25.36620  ? 195  ASP A CA    1 
ATOM   1536 C  C     . ASP A 1 195 ? -10.46200 15.01000  15.98000  1.000 23.87128  ? 195  ASP A C     1 
ATOM   1537 O  O     . ASP A 1 195 ? -10.64800 16.17900  15.61700  1.000 25.54517  ? 195  ASP A O     1 
ATOM   1538 C  CB    . ASP A 1 195 ? -11.15200 14.05800  18.19900  1.000 27.75070  ? 195  ASP A CB    1 
ATOM   1539 C  CG    . ASP A 1 195 ? -12.31400 13.60700  19.08300  1.000 31.34060  ? 195  ASP A CG    1 
ATOM   1540 O  OD1   . ASP A 1 195 ? -13.49100 13.76900  18.68600  1.000 32.60391  ? 195  ASP A OD1   1 
ATOM   1541 O  OD2   . ASP A 1 195 ? -12.04100 13.09400  20.19200  1.000 32.56180  ? 195  ASP A OD2   1 
ATOM   1542 N  N     . LEU A 1 196 ? -9.31600  14.36100  15.74200  1.000 22.93696  ? 196  LEU A N     1 
ATOM   1543 C  CA    . LEU A 1 196 ? -8.22500  15.00700  15.01700  1.000 24.02920  ? 196  LEU A CA    1 
ATOM   1544 C  C     . LEU A 1 196 ? -8.61900  15.31400  13.58000  1.000 20.84724  ? 196  LEU A C     1 
ATOM   1545 O  O     . LEU A 1 196 ? -8.26300  16.37300  13.04800  1.000 22.21056  ? 196  LEU A O     1 
ATOM   1546 C  CB    . LEU A 1 196 ? -6.97300  14.12700  15.04600  1.000 25.20829  ? 196  LEU A CB    1 
ATOM   1547 C  CG    . LEU A 1 196 ? -6.19700  14.13900  16.35700  1.000 28.17969  ? 196  LEU A CG    1 
ATOM   1548 C  CD1   . LEU A 1 196 ? -5.13100  13.06700  16.32900  1.000 28.88767  ? 196  LEU A CD1   1 
ATOM   1549 C  CD2   . LEU A 1 196 ? -5.57100  15.50500  16.58500  1.000 29.27456  ? 196  LEU A CD2   1 
ATOM   1550 N  N     . ALA A 1 197 ? -9.34000  14.39400  12.93300  1.000 20.55773  ? 197  ALA A N     1 
ATOM   1551 C  CA    . ALA A 1 197 ? -9.73800  14.60400  11.54600  1.000 20.70775  ? 197  ALA A CA    1 
ATOM   1552 C  C     . ALA A 1 197 ? -10.63800 15.82400  11.40600  1.000 21.71839  ? 197  ALA A C     1 
ATOM   1553 O  O     . ALA A 1 197 ? -10.44700 16.64400  10.50100  1.000 23.72653  ? 197  ALA A O     1 
ATOM   1554 C  CB    . ALA A 1 197 ? -10.42400 13.35200  11.00100  1.000 20.92093  ? 197  ALA A CB    1 
ATOM   1555 N  N     . GLY A 1 198 ? -11.61800 15.96700  12.29800  1.000 23.80022  ? 198  GLY A N     1 
ATOM   1556 C  CA    . GLY A 1 198 ? -12.49800 17.12000  12.22200  1.000 24.39240  ? 198  GLY A CA    1 
ATOM   1557 C  C     . GLY A 1 198 ? -11.75200 18.42000  12.43100  1.000 23.62652  ? 198  GLY A C     1 
ATOM   1558 O  O     . GLY A 1 198 ? -12.03000 19.42200  11.76500  1.000 25.86100  ? 198  GLY A O     1 
ATOM   1559 N  N     . TYR A 1 199 ? -10.78200 18.41600  13.34800  1.000 24.92141  ? 199  TYR A N     1 
ATOM   1560 C  CA    . TYR A 1 199 ? -9.97800  19.60700  13.58700  1.000 23.61862  ? 199  TYR A CA    1 
ATOM   1561 C  C     . TYR A 1 199 ? -9.14900  19.96300  12.35900  1.000 21.76050  ? 199  TYR A C     1 
ATOM   1562 O  O     . TYR A 1 199 ? -9.10300  21.12900  11.94000  1.000 24.57137  ? 199  TYR A O     1 
ATOM   1563 C  CB    . TYR A 1 199 ? -9.07100  19.37600  14.79300  1.000 25.15828  ? 199  TYR A CB    1 
ATOM   1564 C  CG    . TYR A 1 199 ? -8.10500  20.50100  15.00000  1.000 22.81853  ? 199  TYR A CG    1 
ATOM   1565 C  CD1   . TYR A 1 199 ? -8.53400  21.72400  15.49900  1.000 25.66887  ? 199  TYR A CD1   1 
ATOM   1566 C  CD2   . TYR A 1 199 ? -6.76300  20.35200  14.68700  1.000 23.32385  ? 199  TYR A CD2   1 
ATOM   1567 C  CE1   . TYR A 1 199 ? -7.65100  22.76800  15.67500  1.000 26.34000  ? 199  TYR A CE1   1 
ATOM   1568 C  CE2   . TYR A 1 199 ? -5.87700  21.38200  14.86500  1.000 25.13722  ? 199  TYR A CE2   1 
ATOM   1569 C  CZ    . TYR A 1 199 ? -6.32700  22.59400  15.35700  1.000 25.84784  ? 199  TYR A CZ    1 
ATOM   1570 O  OH    . TYR A 1 199 ? -5.44100  23.62600  15.53000  1.000 27.35065  ? 199  TYR A OH    1 
ATOM   1571 N  N     . LEU A 1 200 ? -8.47000  18.97000  11.77500  1.000 22.71851  ? 200  LEU A N     1 
ATOM   1572 C  CA    . LEU A 1 200 ? -7.62800  19.24300  10.61600  1.000 21.57627  ? 200  LEU A CA    1 
ATOM   1573 C  C     . LEU A 1 200 ? -8.46600  19.64400  9.41000   1.000 22.97907  ? 200  LEU A C     1 
ATOM   1574 O  O     . LEU A 1 200 ? -8.02200  20.45600  8.59000   1.000 22.53691  ? 200  LEU A O     1 
ATOM   1575 C  CB    . LEU A 1 200 ? -6.75800  18.02600  10.30500  1.000 20.52088  ? 200  LEU A CB    1 
ATOM   1576 C  CG    . LEU A 1 200 ? -5.72800  17.69600  11.39300  1.000 22.31320  ? 200  LEU A CG    1 
ATOM   1577 C  CD1   . LEU A 1 200 ? -5.14500  16.31400  11.19600  1.000 20.38929  ? 200  LEU A CD1   1 
ATOM   1578 C  CD2   . LEU A 1 200 ? -4.62300  18.74800  11.40600  1.000 22.07633  ? 200  LEU A CD2   1 
ATOM   1579 N  N     . ASP A 1 201 ? -9.67600  19.09200  9.29200   1.000 24.41345  ? 201  ASP A N     1 
ATOM   1580 C  CA    . ASP A 1 201 ? -10.56200 19.48300  8.20200   1.000 24.92141  ? 201  ASP A CA    1 
ATOM   1581 C  C     . ASP A 1 201 ? -10.89300 20.97000  8.26500   1.000 25.16881  ? 201  ASP A C     1 
ATOM   1582 O  O     . ASP A 1 201 ? -10.87800 21.66000  7.23900   1.000 27.19273  ? 201  ASP A O     1 
ATOM   1583 C  CB    . ASP A 1 201 ? -11.84100 18.65100  8.23600   1.000 27.17694  ? 201  ASP A CB    1 
ATOM   1584 C  CG    . ASP A 1 201 ? -12.72800 18.92000  7.04200   1.000 34.17778  ? 201  ASP A CG    1 
ATOM   1585 O  OD1   . ASP A 1 201 ? -12.42300 18.39300  5.95300   1.000 36.08591  ? 201  ASP A OD1   1 
ATOM   1586 O  OD2   . ASP A 1 201 ? -13.71200 19.67800  7.18500   1.000 38.33091  ? 201  ASP A OD2   1 
ATOM   1587 N  N     . GLY A 1 202 ? -11.20100 21.47800  9.46300   1.000 27.36644  ? 202  GLY A N     1 
ATOM   1588 C  CA    . GLY A 1 202 ? -11.46500 22.90300  9.60800   1.000 27.84808  ? 202  GLY A CA    1 
ATOM   1589 C  C     . GLY A 1 202 ? -10.25900 23.74900  9.24900   1.000 27.25327  ? 202  GLY A C     1 
ATOM   1590 O  O     . GLY A 1 202 ? -10.39200 24.82100  8.65000   1.000 28.48763  ? 202  GLY A O     1 
ATOM   1591 N  N     . LEU A 1 203 ? -9.06100  23.26100  9.58200   1.000 27.97441  ? 203  LEU A N     1 
ATOM   1592 C  CA    . LEU A 1 203 ? -7.83800  23.97400  9.23300   1.000 25.80046  ? 203  LEU A CA    1 
ATOM   1593 C  C     . LEU A 1 203 ? -7.66500  24.05600  7.72100   1.000 26.17419  ? 203  LEU A C     1 
ATOM   1594 O  O     . LEU A 1 203 ? -7.21100  25.07700  7.19300   1.000 26.30315  ? 203  LEU A O     1 
ATOM   1595 C  CB    . LEU A 1 203 ? -6.64800  23.25900  9.87300   1.000 28.51658  ? 203  LEU A CB    1 
ATOM   1596 C  CG    . LEU A 1 203 ? -5.31800  23.99000  9.98200   1.000 30.68263  ? 203  LEU A CG    1 
ATOM   1597 C  CD1   . LEU A 1 203 ? -5.47100  25.23500  10.85000  1.000 31.84329  ? 203  LEU A CD1   1 
ATOM   1598 C  CD2   . LEU A 1 203 ? -4.26800  23.05100  10.55900  1.000 30.48787  ? 203  LEU A CD2   1 
ATOM   1599 N  N     . ILE A 1 204 ? -8.03000  22.98600  7.00800   1.000 25.75572  ? 204  ILE A N     1 
ATOM   1600 C  CA    . ILE A 1 204 ? -7.91600  22.97300  5.55000   1.000 25.45568  ? 204  ILE A CA    1 
ATOM   1601 C  C     . ILE A 1 204 ? -8.82400  24.03200  4.92700   1.000 26.83216  ? 204  ILE A C     1 
ATOM   1602 O  O     . ILE A 1 204 ? -8.40200  24.81300  4.06100   1.000 27.57436  ? 204  ILE A O     1 
ATOM   1603 C  CB    . ILE A 1 204 ? -8.22000  21.56500  5.00900   1.000 23.96603  ? 204  ILE A CB    1 
ATOM   1604 C  CG1   . ILE A 1 204 ? -7.04700  20.62400  5.28300   1.000 22.77642  ? 204  ILE A CG1   1 
ATOM   1605 C  CG2   . ILE A 1 204 ? -8.56800  21.61800  3.52400   1.000 27.18747  ? 204  ILE A CG2   1 
ATOM   1606 C  CD1   . ILE A 1 204 ? -7.39000  19.17800  5.05300   1.000 23.15014  ? 204  ILE A CD1   1 
ATOM   1607 N  N     . THR A 1 205 ? -10.08700 24.06600  5.35200   1.000 27.70859  ? 205  THR A N     1 
ATOM   1608 C  CA    . THR A 1 205 ? -11.02100 25.04900  4.81100   1.000 29.11139  ? 205  THR A CA    1 
ATOM   1609 C  C     . THR A 1 205 ? -10.50400 26.46500  5.02200   1.000 29.19561  ? 205  THR A C     1 
ATOM   1610 O  O     . THR A 1 205 ? -10.67100 27.33800  4.15700   1.000 31.31165  ? 205  THR A O     1 
ATOM   1611 C  CB    . THR A 1 205 ? -12.39000 24.86700  5.46600   1.000 32.62496  ? 205  THR A CB    1 
ATOM   1612 O  OG1   . THR A 1 205 ? -12.85300 23.53300  5.23100   1.000 36.03853  ? 205  THR A OG1   1 
ATOM   1613 C  CG2   . THR A 1 205 ? -13.39900 25.85300  4.89000   1.000 33.87775  ? 205  THR A CG2   1 
ATOM   1614 N  N     . GLN A 1 206 ? -9.83800  26.70200  6.15100   1.000 27.63489  ? 206  GLN A N     1 
ATOM   1615 C  CA    . GLN A 1 206 ? -9.34600  28.04000  6.43700   1.000 28.50868  ? 206  GLN A CA    1 
ATOM   1616 C  C     . GLN A 1 206 ? -8.21900  28.43200  5.48700   1.000 27.54541  ? 206  GLN A C     1 
ATOM   1617 O  O     . GLN A 1 206 ? -8.14300  29.58800  5.05400   1.000 26.52160  ? 206  GLN A O     1 
ATOM   1618 C  CB    . GLN A 1 206 ? -8.89700  28.11700  7.89400   1.000 29.26404  ? 206  GLN A CB    1 
ATOM   1619 C  CG    . GLN A 1 206 ? -8.78700  29.53400  8.41500   1.000 40.71278  ? 206  GLN A CG    1 
ATOM   1620 C  CD    . GLN A 1 206 ? -8.31400  29.59000  9.85300   1.000 51.65883  ? 206  GLN A CD    1 
ATOM   1621 O  OE1   . GLN A 1 206 ? -8.45800  28.62700  10.60800  1.000 56.19358  ? 206  GLN A OE1   1 
ATOM   1622 N  NE2   . GLN A 1 206 ? -7.74100  30.72500  10.24000  1.000 55.35927  ? 206  GLN A NE2   1 
ATOM   1623 N  N     . PHE A 1 207 ? -7.34100  27.48100  5.14700   1.000 26.56108  ? 207  PHE A N     1 
ATOM   1624 C  CA    . PHE A 1 207 ? -6.26700  27.75700  4.19700   1.000 25.48463  ? 207  PHE A CA    1 
ATOM   1625 C  C     . PHE A 1 207 ? -6.79800  28.01600  2.78600   1.000 24.78981  ? 207  PHE A C     1 
ATOM   1626 O  O     . PHE A 1 207 ? -6.16200  28.74100  2.01200   1.000 26.22683  ? 207  PHE A O     1 
ATOM   1627 C  CB    . PHE A 1 207 ? -5.25000  26.60600  4.18000   1.000 24.15290  ? 207  PHE A CB    1 
ATOM   1628 C  CG    . PHE A 1 207 ? -4.23600  26.63800  5.31400   1.000 25.02405  ? 207  PHE A CG    1 
ATOM   1629 C  CD1   . PHE A 1 207 ? -3.38200  27.72000  5.47800   1.000 27.46908  ? 207  PHE A CD1   1 
ATOM   1630 C  CD2   . PHE A 1 207 ? -4.09600  25.55100  6.16800   1.000 26.57424  ? 207  PHE A CD2   1 
ATOM   1631 C  CE1   . PHE A 1 207 ? -2.43600  27.73300  6.49700   1.000 26.74268  ? 207  PHE A CE1   1 
ATOM   1632 C  CE2   . PHE A 1 207 ? -3.15300  25.55800  7.19100   1.000 25.37673  ? 207  PHE A CE2   1 
ATOM   1633 C  CZ    . PHE A 1 207 ? -2.32300  26.65100  7.35700   1.000 24.97405  ? 207  PHE A CZ    1 
ATOM   1634 N  N     . GLN A 1 208 ? -7.93200  27.41200  2.41200   1.000 24.84772  ? 208  GLN A N     1 
ATOM   1635 C  CA    . GLN A 1 208 ? -8.49200  27.67800  1.08600   1.000 22.43427  ? 208  GLN A CA    1 
ATOM   1636 C  C     . GLN A 1 208 ? -9.02200  29.09900  0.98000   1.000 23.73706  ? 208  GLN A C     1 
ATOM   1637 O  O     . GLN A 1 208 ? -8.98000  29.70300  -0.10300  1.000 27.59015  ? 208  GLN A O     1 
ATOM   1638 C  CB    . GLN A 1 208 ? -9.57400  26.65400  0.74300   1.000 24.80297  ? 208  GLN A CB    1 
ATOM   1639 C  CG    . GLN A 1 208 ? -8.99500  25.26400  0.55900   1.000 24.03972  ? 208  GLN A CG    1 
ATOM   1640 C  CD    . GLN A 1 208 ? -10.03000 24.19300  0.28800   1.000 23.98182  ? 208  GLN A CD    1 
ATOM   1641 O  OE1   . GLN A 1 208 ? -11.09600 24.18900  0.87500   1.000 25.81099  ? 208  GLN A OE1   1 
ATOM   1642 N  NE2   . GLN A 1 208 ? -9.69700  23.25700  -0.59300  1.000 26.05049  ? 208  GLN A NE2   1 
ATOM   1643 N  N     . THR A 1 209 ? -9.52200  29.63900  2.08800   1.000 19.87870  ? 209  THR A N     1 
ATOM   1644 C  CA    . THR A 1 209 ? -9.97400  31.01800  2.13900   1.000 21.96842  ? 209  THR A CA    1 
ATOM   1645 C  C     . THR A 1 209 ? -8.79600  31.96400  2.29400   1.000 25.65834  ? 209  THR A C     1 
ATOM   1646 O  O     . THR A 1 209 ? -8.70700  32.98300  1.59700   1.000 27.78228  ? 209  THR A O     1 
ATOM   1647 C  CB    . THR A 1 209 ? -10.91500 31.18700  3.33200   1.000 23.87392  ? 209  THR A CB    1 
ATOM   1648 O  OG1   . THR A 1 209 ? -12.00400 30.27000  3.20500   1.000 29.26667  ? 209  THR A OG1   1 
ATOM   1649 C  CG2   . THR A 1 209 ? -11.44900 32.60700  3.38200   1.000 24.71875  ? 209  THR A CG2   1 
ATOM   1650 N  N     . GLU A 1 210 ? -7.88600  31.63800  3.21100   1.000 26.81111  ? 210  GLU A N     1 
ATOM   1651 C  CA    . GLU A 1 210 ? -6.76600  32.50000  3.57400   1.000 30.26679  ? 210  GLU A CA    1 
ATOM   1652 C  C     . GLU A 1 210 ? -5.50500  31.65600  3.48700   1.000 26.78479  ? 210  GLU A C     1 
ATOM   1653 O  O     . GLU A 1 210 ? -5.12200  30.98900  4.45900   1.000 29.10349  ? 210  GLU A O     1 
ATOM   1654 C  CB    . GLU A 1 210 ? -6.93600  33.06000  4.98100   1.000 40.24956  ? 210  GLU A CB    1 
ATOM   1655 C  CG    . GLU A 1 210 ? -6.36800  34.45000  5.12900   1.000 53.14585  ? 210  GLU A CG    1 
ATOM   1656 C  CD    . GLU A 1 210 ? -7.00100  35.42500  4.15200   1.000 64.13927  ? 210  GLU A CD    1 
ATOM   1657 O  OE1   . GLU A 1 210 ? -8.18900  35.77000  4.34100   1.000 67.97657  ? 210  GLU A OE1   1 
ATOM   1658 O  OE2   . GLU A 1 210 ? -6.31900  35.82800  3.18400   1.000 67.48441  ? 210  GLU A OE2   1 
ATOM   1659 N  N     . PRO A 1 211 ? -4.85300  31.63300  2.32800   1.000 27.80070  ? 211  PRO A N     1 
ATOM   1660 C  CA    . PRO A 1 211 ? -3.60700  30.87500  2.19300   1.000 27.22958  ? 211  PRO A CA    1 
ATOM   1661 C  C     . PRO A 1 211 ? -2.61100  31.26100  3.27900   1.000 25.80309  ? 211  PRO A C     1 
ATOM   1662 O  O     . PRO A 1 211 ? -2.54000  32.41400  3.70600   1.000 28.46131  ? 211  PRO A O     1 
ATOM   1663 C  CB    . PRO A 1 211 ? -3.11500  31.26900  0.79700   1.000 30.63262  ? 211  PRO A CB    1 
ATOM   1664 C  CG    . PRO A 1 211 ? -4.38900  31.55200  0.03500   1.000 32.66181  ? 211  PRO A CG    1 
ATOM   1665 C  CD    . PRO A 1 211 ? -5.34100  32.15800  1.03900   1.000 30.01939  ? 211  PRO A CD    1 
ATOM   1666 N  N     . GLY A 1 212 ? -1.86000  30.27800  3.76100   1.000 26.96639  ? 212  GLY A N     1 
ATOM   1667 C  CA    . GLY A 1 212 ? -0.96200  30.56000  4.86000   1.000 26.66636  ? 212  GLY A CA    1 
ATOM   1668 C  C     . GLY A 1 212 ? 0.22700   29.62600  4.88000   1.000 25.16354  ? 212  GLY A C     1 
ATOM   1669 O  O     . GLY A 1 212 ? 0.34300   28.71700  4.05800   1.000 23.35806  ? 212  GLY A O     1 
ATOM   1670 N  N     . ALA A 1 213 ? 1.11800   29.87000  5.84000   1.000 26.52423  ? 213  ALA A N     1 
ATOM   1671 C  CA    . ALA A 1 213 ? 2.38400   29.16600  5.96000   1.000 23.20015  ? 213  ALA A CA    1 
ATOM   1672 C  C     . ALA A 1 213 ? 2.19700   27.78300  6.57700   1.000 21.28939  ? 213  ALA A C     1 
ATOM   1673 O  O     . ALA A 1 213 ? 1.17600   27.46700  7.19500   1.000 25.20565  ? 213  ALA A O     1 
ATOM   1674 C  CB    . ALA A 1 213 ? 3.34900   29.96100  6.83300   1.000 26.45317  ? 213  ALA A CB    1 
ATOM   1675 N  N     . GLY A 1 214 ? 3.23300   26.97200  6.43000   1.000 20.73933  ? 214  GLY A N     1 
ATOM   1676 C  CA    . GLY A 1 214 ? 3.27300   25.63800  6.97900   1.000 18.17850  ? 214  GLY A CA    1 
ATOM   1677 C  C     . GLY A 1 214 ? 2.95800   24.58700  5.93100   1.000 17.45999  ? 214  GLY A C     1 
ATOM   1678 O  O     . GLY A 1 214 ? 2.36500   24.85800  4.88900   1.000 21.58943  ? 214  GLY A O     1 
ATOM   1679 N  N     . LEU A 1 215 ? 3.36700   23.35300  6.22600   1.000 15.76768  ? 215  LEU A N     1 
ATOM   1680 C  CA    . LEU A 1 215 ? 3.18300   22.26100  5.27400   1.000 15.46764  ? 215  LEU A CA    1 
ATOM   1681 C  C     . LEU A 1 215 ? 1.71200   22.04200  4.93600   1.000 16.88887  ? 215  LEU A C     1 
ATOM   1682 O  O     . LEU A 1 215 ? 1.37100   21.78100  3.77600   1.000 18.55749  ? 215  LEU A O     1 
ATOM   1683 C  CB    . LEU A 1 215 ? 3.82600   20.98000  5.81500   1.000 17.09415  ? 215  LEU A CB    1 
ATOM   1684 C  CG    . LEU A 1 215 ? 3.68300   19.71000  4.96900   1.000 17.62843  ? 215  LEU A CG    1 
ATOM   1685 C  CD1   . LEU A 1 215 ? 4.17000   19.95300  3.55100   1.000 19.48392  ? 215  LEU A CD1   1 
ATOM   1686 C  CD2   . LEU A 1 215 ? 4.45800   18.57100  5.58600   1.000 21.48679  ? 215  LEU A CD2   1 
ATOM   1687 N  N     . VAL A 1 216 ? 0.81900   22.13200  5.92800   1.000 17.56526  ? 216  VAL A N     1 
ATOM   1688 C  CA    . VAL A 1 216 ? -0.60300  21.98100  5.61800   1.000 16.79412  ? 216  VAL A CA    1 
ATOM   1689 C  C     . VAL A 1 216 ? -1.05000  23.06300  4.64500   1.000 18.03637  ? 216  VAL A C     1 
ATOM   1690 O  O     . VAL A 1 216 ? -1.75400  22.78100  3.66800   1.000 19.86291  ? 216  VAL A O     1 
ATOM   1691 C  CB    . VAL A 1 216 ? -1.46600  21.93600  6.89300   1.000 17.11784  ? 216  VAL A CB    1 
ATOM   1692 C  CG1   . VAL A 1 216 ? -2.93100  21.87300  6.53100   1.000 18.64960  ? 216  VAL A CG1   1 
ATOM   1693 C  CG2   . VAL A 1 216 ? -1.10000  20.72800  7.75100   1.000 19.32337  ? 216  VAL A CG2   1 
ATOM   1694 N  N     . GLY A 1 217 ? -0.63200  24.31200  4.88000   1.000 17.12574  ? 217  GLY A N     1 
ATOM   1695 C  CA    . GLY A 1 217 ? -0.98000  25.38400  3.95200   1.000 18.37852  ? 217  GLY A CA    1 
ATOM   1696 C  C     . GLY A 1 217 ? -0.43700  25.14900  2.55100   1.000 19.42601  ? 217  GLY A C     1 
ATOM   1697 O  O     . GLY A 1 217 ? -1.10600  25.44500  1.55000   1.000 19.24441  ? 217  GLY A O     1 
ATOM   1698 N  N     . ALA A 1 218 ? 0.77700   24.60000  2.45900   1.000 17.85214  ? 218  ALA A N     1 
ATOM   1699 C  CA    . ALA A 1 218 ? 1.38700   24.35400  1.15400   1.000 18.53117  ? 218  ALA A CA    1 
ATOM   1700 C  C     . ALA A 1 218 ? 0.65700   23.24800  0.40300   1.000 17.12574  ? 218  ALA A C     1 
ATOM   1701 O  O     . ALA A 1 218 ? 0.44100   23.35300  -0.81400  1.000 19.28389  ? 218  ALA A O     1 
ATOM   1702 C  CB    . ALA A 1 218 ? 2.86400   24.01000  1.31900   1.000 17.86530  ? 218  ALA A CB    1 
ATOM   1703 N  N     . LEU A 1 219 ? 0.26600   22.17700  1.10900   1.000 16.43881  ? 219  LEU A N     1 
ATOM   1704 C  CA    . LEU A 1 219 ? -0.46800  21.08700  0.47200   1.000 17.71265  ? 219  LEU A CA    1 
ATOM   1705 C  C     . LEU A 1 219 ? -1.84100  21.54500  0.00100   1.000 16.91782  ? 219  LEU A C     1 
ATOM   1706 O  O     . LEU A 1 219 ? -2.31800  21.11100  -1.05300  1.000 19.93397  ? 219  LEU A O     1 
ATOM   1707 C  CB    . LEU A 1 219 ? -0.61500  19.92000  1.44300   1.000 18.45748  ? 219  LEU A CB    1 
ATOM   1708 C  CG    . LEU A 1 219 ? 0.69000   19.21900  1.79700   1.000 19.54971  ? 219  LEU A CG    1 
ATOM   1709 C  CD1   . LEU A 1 219 ? 0.47300   18.28200  2.96900   1.000 20.45772  ? 219  LEU A CD1   1 
ATOM   1710 C  CD2   . LEU A 1 219 ? 1.21500   18.46100  0.58200   1.000 22.20529  ? 219  LEU A CD2   1 
ATOM   1711 N  N     . VAL A 1 220 ? -2.50100  22.40500  0.77900   1.000 16.41513  ? 220  VAL A N     1 
ATOM   1712 C  CA    . VAL A 1 220 ? -3.79500  22.94500  0.36600   1.000 17.81266  ? 220  VAL A CA    1 
ATOM   1713 C  C     . VAL A 1 220 ? -3.64400  23.78600  -0.89600  1.000 18.31535  ? 220  VAL A C     1 
ATOM   1714 O  O     . VAL A 1 220 ? -4.42300  23.65500  -1.85500  1.000 19.94976  ? 220  VAL A O     1 
ATOM   1715 C  CB    . VAL A 1 220 ? -4.42800  23.75500  1.51300   1.000 17.85214  ? 220  VAL A CB    1 
ATOM   1716 C  CG1   . VAL A 1 220 ? -5.63300  24.54800  0.99600   1.000 18.56012  ? 220  VAL A CG1   1 
ATOM   1717 C  CG2   . VAL A 1 220 ? -4.83400  22.82200  2.63800   1.000 17.10731  ? 220  VAL A CG2   1 
ATOM   1718 N  N     . ALA A 1 221 ? -2.64700  24.67300  -0.91100  1.000 18.75225  ? 221  ALA A N     1 
ATOM   1719 C  CA    . ALA A 1 221 ? -2.53400  25.63600  -2.00200  1.000 19.02597  ? 221  ALA A CA    1 
ATOM   1720 C  C     . ALA A 1 221 ? -2.04900  24.98100  -3.28800  1.000 20.19716  ? 221  ALA A C     1 
ATOM   1721 O  O     . ALA A 1 221 ? -2.35300  25.47100  -4.38600  1.000 20.82092  ? 221  ALA A O     1 
ATOM   1722 C  CB    . ALA A 1 221 ? -1.59500  26.77000  -1.59700  1.000 21.82630  ? 221  ALA A CB    1 
ATOM   1723 N  N     . ASP A 1 222 ? -1.29200  23.89200  -3.17800  1.000 20.73143  ? 222  ASP A N     1 
ATOM   1724 C  CA    . ASP A 1 222 ? -0.67800  23.27600  -4.34700  1.000 18.85752  ? 222  ASP A CA    1 
ATOM   1725 C  C     . ASP A 1 222 ? -1.35100  21.95000  -4.69700  1.000 18.40484  ? 222  ASP A C     1 
ATOM   1726 O  O     . ASP A 1 222 ? -2.19800  21.90100  -5.59200  1.000 19.06281  ? 222  ASP A O     1 
ATOM   1727 C  CB    . ASP A 1 222 ? 0.82200   23.10700  -4.11100  1.000 22.14213  ? 222  ASP A CB    1 
ATOM   1728 C  CG    . ASP A 1 222 ? 1.57200   22.71800  -5.36700  1.000 25.50832  ? 222  ASP A CG    1 
ATOM   1729 O  OD1   . ASP A 1 222 ? 0.91900   22.50800  -6.41200  1.000 25.55306  ? 222  ASP A OD1   1 
ATOM   1730 O  OD2   . ASP A 1 222 ? 2.81900   22.63700  -5.30900  1.000 30.56156  ? 222  ASP A OD2   1 
ATOM   1731 N  N     . GLN A 1 223 ? -1.02200  20.87600  -3.97700  1.000 18.73909  ? 223  GLN A N     1 
ATOM   1732 C  CA    . GLN A 1 223 ? -1.49100  19.55200  -4.38500  1.000 19.27863  ? 223  GLN A CA    1 
ATOM   1733 C  C     . GLN A 1 223 ? -3.01400  19.42700  -4.32800  1.000 18.19955  ? 223  GLN A C     1 
ATOM   1734 O  O     . GLN A 1 223 ? -3.62900  18.85400  -5.23800  1.000 19.31811  ? 223  GLN A O     1 
ATOM   1735 C  CB    . GLN A 1 223 ? -0.81000  18.46100  -3.55600  1.000 19.86291  ? 223  GLN A CB    1 
ATOM   1736 C  CG    . GLN A 1 223 ? 0.63200   18.21100  -3.96100  1.000 20.98409  ? 223  GLN A CG    1 
ATOM   1737 C  CD    . GLN A 1 223 ? 1.62700   19.14300  -3.28900  1.000 22.35005  ? 223  GLN A CD    1 
ATOM   1738 O  OE1   . GLN A 1 223 ? 1.25100   20.07600  -2.57900  1.000 21.61838  ? 223  GLN A OE1   1 
ATOM   1739 N  NE2   . GLN A 1 223 ? 2.91400   18.87800  -3.50100  1.000 24.10026  ? 223  GLN A NE2   1 
ATOM   1740 N  N     . LEU A 1 224 ? -3.64500  19.93300  -3.26900  1.000 18.05216  ? 224  LEU A N     1 
ATOM   1741 C  CA    . LEU A 1 224 ? -5.09900  19.84200  -3.18100  1.000 17.86793  ? 224  LEU A CA    1 
ATOM   1742 C  C     . LEU A 1 224 ? -5.76800  20.61300  -4.32300  1.000 16.82307  ? 224  LEU A C     1 
ATOM   1743 O  O     . LEU A 1 224 ? -6.69600  20.10900  -4.97500  1.000 18.55222  ? 224  LEU A O     1 
ATOM   1744 C  CB    . LEU A 1 224 ? -5.58000  20.34000  -1.81500  1.000 18.58907  ? 224  LEU A CB    1 
ATOM   1745 C  CG    . LEU A 1 224 ? -7.06700  20.12600  -1.54700  1.000 18.77594  ? 224  LEU A CG    1 
ATOM   1746 C  CD1   . LEU A 1 224 ? -7.41300  18.65200  -1.58200  1.000 21.12622  ? 224  LEU A CD1   1 
ATOM   1747 C  CD2   . LEU A 1 224 ? -7.47400  20.76200  -0.22300  1.000 22.18424  ? 224  LEU A CD2   1 
ATOM   1748 N  N     . ALA A 1 225 ? -5.29800  21.84000  -4.58000  1.000 17.23891  ? 225  ALA A N     1 
ATOM   1749 C  CA    . ALA A 1 225 ? -5.86400  22.67100  -5.64000  1.000 16.76780  ? 225  ALA A CA    1 
ATOM   1750 C  C     . ALA A 1 225 ? -5.66300  22.05500  -7.01900  1.000 15.89401  ? 225  ALA A C     1 
ATOM   1751 O  O     . ALA A 1 225 ? -6.40300  22.38300  -7.95600  1.000 17.34418  ? 225  ALA A O     1 
ATOM   1752 C  CB    . ALA A 1 225 ? -5.26200  24.07900  -5.58800  1.000 18.75751  ? 225  ALA A CB    1 
ATOM   1753 N  N     . ASN A 1 226 ? -4.68700  21.16700  -7.17000  1.000 16.22826  ? 226  ASN A N     1 
ATOM   1754 C  CA    . ASN A 1 226 ? -4.48000  20.46900  -8.43200  1.000 18.01005  ? 226  ASN A CA    1 
ATOM   1755 C  C     . ASN A 1 226 ? -5.13100  19.09500  -8.47000  1.000 19.33127  ? 226  ASN A C     1 
ATOM   1756 O  O     . ASN A 1 226 ? -4.97800  18.38300  -9.46800  1.000 21.45520  ? 226  ASN A O     1 
ATOM   1757 C  CB    . ASN A 1 226 ? -2.98700  20.34200  -8.73100  1.000 17.29681  ? 226  ASN A CB    1 
ATOM   1758 C  CG    . ASN A 1 226 ? -2.40400  21.60800  -9.30200  1.000 18.08375  ? 226  ASN A CG    1 
ATOM   1759 O  OD1   . ASN A 1 226 ? -2.43200  21.81200  -10.51300 1.000 21.05516  ? 226  ASN A OD1   1 
ATOM   1760 N  ND2   . ASN A 1 226 ? -1.88200  22.47700  -8.43500  1.000 20.18400  ? 226  ASN A ND2   1 
ATOM   1761 N  N     . GLY A 1 227 ? -5.84100  18.70400  -7.41200  1.000 17.15732  ? 227  GLY A N     1 
ATOM   1762 C  CA    . GLY A 1 227 ? -6.43400  17.38500  -7.33700  1.000 18.78120  ? 227  GLY A CA    1 
ATOM   1763 C  C     . GLY A 1 227 ? -5.43200  16.26000  -7.24000  1.000 19.89186  ? 227  GLY A C     1 
ATOM   1764 O  O     . GLY A 1 227 ? -5.76700  15.11500  -7.56300  1.000 24.95299  ? 227  GLY A O     1 
ATOM   1765 N  N     . GLU A 1 228 ? -4.20300  16.55400  -6.82000  1.000 19.03649  ? 228  GLU A N     1 
ATOM   1766 C  CA    . GLU A 1 228 ? -3.14000  15.56600  -6.72000  1.000 19.17862  ? 228  GLU A CA    1 
ATOM   1767 C  C     . GLU A 1 228 ? -3.13700  14.83500  -5.38400  1.000 19.99713  ? 228  GLU A C     1 
ATOM   1768 O  O     . GLU A 1 228 ? -2.43600  13.82600  -5.23600  1.000 22.67640  ? 228  GLU A O     1 
ATOM   1769 C  CB    . GLU A 1 228 ? -1.79300  16.24800  -6.96300  1.000 21.36835  ? 228  GLU A CB    1 
ATOM   1770 C  CG    . GLU A 1 228 ? -1.68100  16.77600  -8.38500  1.000 23.72916  ? 228  GLU A CG    1 
ATOM   1771 C  CD    . GLU A 1 228 ? -0.45200  17.63400  -8.60800  1.000 28.58237  ? 228  GLU A CD    1 
ATOM   1772 O  OE1   . GLU A 1 228 ? 0.15700   18.09600  -7.61500  1.000 29.87727  ? 228  GLU A OE1   1 
ATOM   1773 O  OE2   . GLU A 1 228 ? -0.10500  17.84700  -9.78400  1.000 31.19321  ? 228  GLU A OE2   1 
ATOM   1774 N  N     . ILE A 1 229 ? -3.89300  15.32500  -4.41300  1.000 20.21295  ? 229  ILE A N     1 
ATOM   1775 C  CA    . ILE A 1 229 ? -4.12900  14.62100  -3.16300  1.000 19.62604  ? 229  ILE A CA    1 
ATOM   1776 C  C     . ILE A 1 229 ? -5.59600  14.81800  -2.82500  1.000 20.96304  ? 229  ILE A C     1 
ATOM   1777 O  O     . ILE A 1 229 ? -6.16400  15.88300  -3.09400  1.000 21.55258  ? 229  ILE A O     1 
ATOM   1778 C  CB    . ILE A 1 229 ? -3.19100  15.12100  -2.03700  1.000 19.48392  ? 229  ILE A CB    1 
ATOM   1779 C  CG1   . ILE A 1 229 ? -3.26600  14.21500  -0.80600  1.000 20.09978  ? 229  ILE A CG1   1 
ATOM   1780 C  CG2   . ILE A 1 229 ? -3.50400  16.55900  -1.65200  1.000 20.00503  ? 229  ILE A CG2   1 
ATOM   1781 C  CD1   . ILE A 1 229 ? -2.18400  14.52400  0.22100   1.000 21.68944  ? 229  ILE A CD1   1 
ATOM   1782 N  N     . ASP A 1 230 ? -6.22800  13.77000  -2.30200  1.000 22.14213  ? 230  ASP A N     1 
ATOM   1783 C  CA    . ASP A 1 230 ? -7.59200  13.89100  -1.81700  1.000 23.81865  ? 230  ASP A CA    1 
ATOM   1784 C  C     . ASP A 1 230 ? -7.59200  14.62400  -0.47300  1.000 22.88432  ? 230  ASP A C     1 
ATOM   1785 O  O     . ASP A 1 230 ? -6.62000  14.57600  0.28300   1.000 19.75763  ? 230  ASP A O     1 
ATOM   1786 C  CB    . ASP A 1 230 ? -8.23600  12.50400  -1.67400  1.000 25.52148  ? 230  ASP A CB    1 
ATOM   1787 C  CG    . ASP A 1 230 ? -8.32800  11.74100  -3.00300  1.000 29.82200  ? 230  ASP A CG    1 
ATOM   1788 O  OD1   . ASP A 1 230 ? -8.40700  12.38300  -4.07900  1.000 35.46478  ? 230  ASP A OD1   1 
ATOM   1789 O  OD2   . ASP A 1 230 ? -8.34200  10.48500  -2.97200  1.000 24.73718  ? 230  ASP A OD2   1 
ATOM   1790 N  N     . ARG A 1 231 ? -8.68500  15.34500  -0.20100  1.000 21.89999  ? 231  ARG A N     1 
ATOM   1791 C  CA    . ARG A 1 231 ? -8.80800  16.07900  1.05500   1.000 22.53954  ? 231  ARG A CA    1 
ATOM   1792 C  C     . ARG A 1 231 ? -8.62000  15.14600  2.24400   1.000 20.04977  ? 231  ARG A C     1 
ATOM   1793 O  O     . ARG A 1 231 ? -7.92700  15.47000  3.21600   1.000 20.90777  ? 231  ARG A O     1 
ATOM   1794 C  CB    . ARG A 1 231 ? -10.18600 16.73500  1.11300   1.000 23.55546  ? 231  ARG A CB    1 
ATOM   1795 C  CG    . ARG A 1 231 ? -10.42300 17.60400  2.32600   1.000 23.68179  ? 231  ARG A CG    1 
ATOM   1796 C  CD    . ARG A 1 231 ? -11.75400 18.35300  2.21700   1.000 26.35053  ? 231  ARG A CD    1 
ATOM   1797 N  NE    . ARG A 1 231 ? -11.95200 19.24000  3.35400   1.000 29.26930  ? 231  ARG A NE    1 
ATOM   1798 C  CZ    . ARG A 1 231 ? -11.91400 20.56500  3.29300   1.000 29.97201  ? 231  ARG A CZ    1 
ATOM   1799 N  NH1   . ARG A 1 231 ? -11.78200 21.20100  2.14000   1.000 28.90873  ? 231  ARG A NH1   1 
ATOM   1800 N  NH2   . ARG A 1 231 ? -12.01800 21.26800  4.41800   1.000 30.08519  ? 231  ARG A NH2   1 
ATOM   1801 N  N     . GLU A 1 232 ? -9.22200  13.97200  2.17500   1.000 20.28664  ? 232  GLU A N     1 
ATOM   1802 C  CA    A GLU A 1 232 ? -9.12400  13.01200  3.25900   0.530 20.10504  ? 232  GLU A CA    1 
ATOM   1803 C  CA    B GLU A 1 232 ? -9.10100  13.04000  3.29400   0.470 19.79974  ? 232  GLU A CA    1 
ATOM   1804 C  C     . GLU A 1 232 ? -7.68900  12.49300  3.41400   1.000 18.21797  ? 232  GLU A C     1 
ATOM   1805 O  O     . GLU A 1 232 ? -7.22600  12.23100  4.53700   1.000 17.50736  ? 232  GLU A O     1 
ATOM   1806 C  CB    A GLU A 1 232 ? -10.14700 11.91600  2.95600   0.530 22.27372  ? 232  GLU A CB    1 
ATOM   1807 C  CB    B GLU A 1 232 ? -10.11800 11.90200  3.19800   0.470 21.47363  ? 232  GLU A CB    1 
ATOM   1808 C  CG    A GLU A 1 232 ? -11.63600 12.43500  2.79900   0.530 27.16905  ? 232  GLU A CG    1 
ATOM   1809 C  CG    B GLU A 1 232 ? -11.55700 12.30600  3.48500   0.470 25.46884  ? 232  GLU A CG    1 
ATOM   1810 C  CD    A GLU A 1 232 ? -11.96800 13.38300  1.58800   0.530 24.72928  ? 232  GLU A CD    1 
ATOM   1811 C  CD    B GLU A 1 232 ? -11.89500 12.37300  4.96700   0.470 27.98230  ? 232  GLU A CD    1 
ATOM   1812 O  OE1   A GLU A 1 232 ? -11.42600 13.23800  0.46400   0.530 16.27827  ? 232  GLU A OE1   1 
ATOM   1813 O  OE1   B GLU A 1 232 ? -11.07000 11.94500  5.80400   0.470 28.83240  ? 232  GLU A OE1   1 
ATOM   1814 O  OE2   A GLU A 1 232 ? -12.83000 14.28400  1.76700   0.530 28.28497  ? 232  GLU A OE2   1 
ATOM   1815 O  OE2   B GLU A 1 232 ? -13.00200 12.84900  5.29300   0.470 31.96699  ? 232  GLU A OE2   1 
ATOM   1816 N  N     . GLU A 1 233 ? -6.97200  12.33900  2.29000   1.000 18.92595  ? 233  GLU A N     1 
ATOM   1817 C  CA    . GLU A 1 233 ? -5.55800  11.96600  2.34900   1.000 18.12849  ? 233  GLU A CA    1 
ATOM   1818 C  C     . GLU A 1 233 ? -4.72100  13.07000  2.97800   1.000 16.40197  ? 233  GLU A C     1 
ATOM   1819 O  O     . GLU A 1 233 ? -3.72900  12.79200  3.66700   1.000 17.80740  ? 233  GLU A O     1 
ATOM   1820 C  CB    . GLU A 1 233 ? -5.00900  11.72200  0.95100   1.000 20.67616  ? 233  GLU A CB    1 
ATOM   1821 C  CG    . GLU A 1 233 ? -5.30800  10.39200  0.31600   1.000 25.27671  ? 233  GLU A CG    1 
ATOM   1822 C  CD    . GLU A 1 233 ? -4.57400  10.25200  -1.00900  1.000 25.61097  ? 233  GLU A CD    1 
ATOM   1823 O  OE1   . GLU A 1 233 ? -4.85100  11.05400  -1.93000  1.000 25.13986  ? 233  GLU A OE1   1 
ATOM   1824 O  OE2   . GLU A 1 233 ? -3.68300  9.37700   -1.11300  1.000 25.62939  ? 233  GLU A OE2   1 
ATOM   1825 N  N     . LEU A 1 234 ? -5.04800  14.32800  2.67100   1.000 17.30997  ? 234  LEU A N     1 
ATOM   1826 C  CA    . LEU A 1 234 ? -4.33700  15.44300  3.28400   1.000 17.71528  ? 234  LEU A CA    1 
ATOM   1827 C  C     . LEU A 1 234 ? -4.50100  15.40100  4.79600   1.000 15.83874  ? 234  LEU A C     1 
ATOM   1828 O  O     . LEU A 1 234 ? -3.52600  15.57500  5.54100   1.000 16.79149  ? 234  LEU A O     1 
ATOM   1829 C  CB    . LEU A 1 234 ? -4.84100  16.76900  2.70900   1.000 19.17335  ? 234  LEU A CB    1 
ATOM   1830 C  CG    . LEU A 1 234 ? -3.89100  17.96700  2.72400   1.000 19.19967  ? 234  LEU A CG    1 
ATOM   1831 C  CD1   . LEU A 1 234 ? -4.44900  19.07700  1.83900   1.000 19.78921  ? 234  LEU A CD1   1 
ATOM   1832 C  CD2   . LEU A 1 234 ? -3.64700  18.50500  4.11800   1.000 22.79747  ? 234  LEU A CD2   1 
ATOM   1833 N  N     . ILE A 1 235 ? -5.72500  15.14600  5.26400   1.000 15.56766  ? 235  ILE A N     1 
ATOM   1834 C  CA    . ILE A 1 235 ? -5.97000  14.99700  6.69800   1.000 16.68884  ? 235  ILE A CA    1 
ATOM   1835 C  C     . ILE A 1 235 ? -5.09500  13.89100  7.28300   1.000 16.73885  ? 235  ILE A C     1 
ATOM   1836 O  O     . ILE A 1 235 ? -4.42100  14.08500  8.30100   1.000 16.85465  ? 235  ILE A O     1 
ATOM   1837 C  CB    . ILE A 1 235 ? -7.46700  14.75000  6.96100   1.000 17.68370  ? 235  ILE A CB    1 
ATOM   1838 C  CG1   . ILE A 1 235 ? -8.26800  16.00800  6.62400   1.000 21.24992  ? 235  ILE A CG1   1 
ATOM   1839 C  CG2   . ILE A 1 235 ? -7.70600  14.29200  8.40400   1.000 19.71289  ? 235  ILE A CG2   1 
ATOM   1840 C  CD1   . ILE A 1 235 ? -9.77400  15.81500  6.71100   1.000 22.14476  ? 235  ILE A CD1   1 
ATOM   1841 N  N     . SER A 1 236 ? -5.08500  12.71900  6.63900   1.000 16.75990  ? 236  SER A N     1 
ATOM   1842 C  CA    . SER A 1 236 ? -4.30900  11.59400  7.15200   1.000 15.97034  ? 236  SER A CA    1 
ATOM   1843 C  C     . SER A 1 236 ? -2.82300  11.91400  7.17600   1.000 15.08865  ? 236  SER A C     1 
ATOM   1844 O  O     . SER A 1 236 ? -2.10800  11.52200  8.10900   1.000 16.86518  ? 236  SER A O     1 
ATOM   1845 C  CB    . SER A 1 236 ? -4.56300  10.36200  6.29000   1.000 18.59433  ? 236  SER A CB    1 
ATOM   1846 O  OG    . SER A 1 236 ? -5.91500  9.95000   6.39400   1.000 20.82618  ? 236  SER A OG    1 
ATOM   1847 N  N     . THR A 1 237 ? -2.33100  12.60400  6.14400   1.000 15.99665  ? 237  THR A N     1 
ATOM   1848 C  CA    . THR A 1 237 ? -0.91600  12.96500  6.09300   1.000 14.54911  ? 237  THR A CA    1 
ATOM   1849 C  C     . THR A 1 237 ? -0.56400  13.93900  7.21100   1.000 14.69387  ? 237  THR A C     1 
ATOM   1850 O  O     . THR A 1 237 ? 0.42600   13.74800  7.92800   1.000 16.44934  ? 237  THR A O     1 
ATOM   1851 C  CB    . THR A 1 237 ? -0.59300  13.58100  4.72900   1.000 17.42577  ? 237  THR A CB    1 
ATOM   1852 O  OG1   . THR A 1 237 ? -0.91700  12.64400  3.69600   1.000 20.95778  ? 237  THR A OG1   1 
ATOM   1853 C  CG2   . THR A 1 237 ? 0.88100   13.94100  4.63800   1.000 19.30231  ? 237  THR A CG2   1 
ATOM   1854 N  N     . ALA A 1 238 ? -1.36100  14.99500  7.36600   1.000 16.29143  ? 238  ALA A N     1 
ATOM   1855 C  CA    . ALA A 1 238 ? -1.12100  15.94900  8.44000   1.000 15.12023  ? 238  ALA A CA    1 
ATOM   1856 C  C     . ALA A 1 238 ? -1.19800  15.26800  9.79400   1.000 14.22802  ? 238  ALA A C     1 
ATOM   1857 O  O     . ALA A 1 238 ? -0.40100  15.56700  10.69400  1.000 16.58883  ? 238  ALA A O     1 
ATOM   1858 C  CB    . ALA A 1 238 ? -2.13900  17.08400  8.37500   1.000 16.77043  ? 238  ALA A CB    1 
ATOM   1859 N  N     . MET A 1 239 ? -2.14500  14.33600  9.95600   1.000 15.10971  ? 239  MET A N     1 
ATOM   1860 C  CA    . MET A 1 239 ? -2.30100  13.66400  11.24400  1.000 16.15720  ? 239  MET A CA    1 
ATOM   1861 C  C     . MET A 1 239 ? -1.08400  12.80400  11.56700  1.000 14.07011  ? 239  MET A C     1 
ATOM   1862 O  O     . MET A 1 239 ? -0.59400  12.79800  12.71000  1.000 15.79663  ? 239  MET A O     1 
ATOM   1863 C  CB    . MET A 1 239 ? -3.58000  12.82200  11.25600  1.000 16.75201  ? 239  MET A CB    1 
ATOM   1864 C  CG    . MET A 1 239 ? -3.95400  12.31600  12.64600  1.000 19.73395  ? 239  MET A CG    1 
ATOM   1865 S  SD    . MET A 1 239 ? -5.37100  11.22700  12.68100  1.000 21.14990  ? 239  MET A SD    1 
ATOM   1866 C  CE    . MET A 1 239 ? -6.51700  12.20300  11.73400  1.000 21.21307  ? 239  MET A CE    1 
ATOM   1867 N  N     . LEU A 1 240 ? -0.59000  12.05800  10.57600  1.000 14.34383  ? 240  LEU A N     1 
ATOM   1868 C  CA    . LEU A 1 240 ? 0.61500   11.25600  10.76700  1.000 15.15445  ? 240  LEU A CA    1 
ATOM   1869 C  C     . LEU A 1 240 ? 1.78400   12.12300  11.22400  1.000 13.58321  ? 240  LEU A C     1 
ATOM   1870 O  O     . LEU A 1 240 ? 2.48400   11.79100  12.18800  1.000 15.98350  ? 240  LEU A O     1 
ATOM   1871 C  CB    . LEU A 1 240 ? 0.96400   10.53200  9.46200   1.000 17.05204  ? 240  LEU A CB    1 
ATOM   1872 C  CG    . LEU A 1 240 ? 2.33000   9.82600   9.42200   1.000 18.73119  ? 240  LEU A CG    1 
ATOM   1873 C  CD1   . LEU A 1 240 ? 2.42300   8.73400   10.49200  1.000 18.58907  ? 240  LEU A CD1   1 
ATOM   1874 C  CD2   . LEU A 1 240 ? 2.59200   9.23000   8.05400   1.000 18.87068  ? 240  LEU A CD2   1 
ATOM   1875 N  N     . LEU A 1 241 ? 2.02600   13.23600  10.53200  1.000 14.77809  ? 241  LEU A N     1 
ATOM   1876 C  CA    . LEU A 1 241 ? 3.17900   14.06400  10.87300  1.000 13.71217  ? 241  LEU A CA    1 
ATOM   1877 C  C     . LEU A 1 241 ? 3.00200   14.72600  12.23900  1.000 14.56490  ? 241  LEU A C     1 
ATOM   1878 O  O     . LEU A 1 241 ? 3.96200   14.82700  13.01800  1.000 15.79400  ? 241  LEU A O     1 
ATOM   1879 C  CB    . LEU A 1 241 ? 3.42800   15.09800  9.77800   1.000 15.42290  ? 241  LEU A CB    1 
ATOM   1880 C  CG    . LEU A 1 241 ? 4.26400   14.59800  8.58600   1.000 20.20505  ? 241  LEU A CG    1 
ATOM   1881 C  CD1   . LEU A 1 241 ? 3.69400   13.37400  7.87500   1.000 23.78180  ? 241  LEU A CD1   1 
ATOM   1882 C  CD2   . LEU A 1 241 ? 4.41100   15.73000  7.60200   1.000 22.79484  ? 241  LEU A CD2   1 
ATOM   1883 N  N     . LEU A 1 242 ? 1.78000   15.16200  12.54800  1.000 14.60438  ? 242  LEU A N     1 
ATOM   1884 C  CA    . LEU A 1 242 ? 1.50000   15.76800  13.85000  1.000 15.36237  ? 242  LEU A CA    1 
ATOM   1885 C  C     . LEU A 1 242 ? 1.77200   14.78800  14.98500  1.000 17.07047  ? 242  LEU A C     1 
ATOM   1886 O  O     . LEU A 1 242 ? 2.46700   15.11400  15.95900  1.000 17.71791  ? 242  LEU A O     1 
ATOM   1887 C  CB    . LEU A 1 242 ? 0.04800   16.25000  13.89000  1.000 18.53117  ? 242  LEU A CB    1 
ATOM   1888 C  CG    . LEU A 1 242 ? -0.39500  16.97500  15.16200  1.000 20.80513  ? 242  LEU A CG    1 
ATOM   1889 C  CD1   . LEU A 1 242 ? 0.35700   18.28500  15.31300  1.000 27.60331  ? 242  LEU A CD1   1 
ATOM   1890 C  CD2   . LEU A 1 242 ? -1.88000  17.25300  15.14600  1.000 25.93732  ? 242  LEU A CD2   1 
ATOM   1891 N  N     . ILE A 1 243 ? 1.23200   13.57400  14.87200  1.000 17.20206  ? 243  ILE A N     1 
ATOM   1892 C  CA    . ILE A 1 243 ? 1.32600   12.61200  15.96400  1.000 16.73622  ? 243  ILE A CA    1 
ATOM   1893 C  C     . ILE A 1 243 ? 2.74100   12.07000  16.08000  1.000 15.45185  ? 243  ILE A C     1 
ATOM   1894 O  O     . ILE A 1 243 ? 3.30700   12.00600  17.17800  1.000 17.73897  ? 243  ILE A O     1 
ATOM   1895 C  CB    . ILE A 1 243 ? 0.30200   11.48300  15.78000  1.000 16.64147  ? 243  ILE A CB    1 
ATOM   1896 C  CG1   . ILE A 1 243 ? -1.12500  12.01800  15.93300  1.000 19.75237  ? 243  ILE A CG1   1 
ATOM   1897 C  CG2   . ILE A 1 243 ? 0.56900   10.38700  16.76700  1.000 19.95766  ? 243  ILE A CG2   1 
ATOM   1898 C  CD1   . ILE A 1 243 ? -2.18300  10.95900  15.77300  1.000 22.71588  ? 243  ILE A CD1   1 
ATOM   1899 N  N     . ALA A 1 244 ? 3.33400   11.65100  14.95900  1.000 14.73335  ? 244  ALA A N     1 
ATOM   1900 C  CA    . ALA A 1 244 ? 4.70800   11.16300  15.03300  1.000 15.28868  ? 244  ALA A CA    1 
ATOM   1901 C  C     . ALA A 1 244 ? 5.64500   12.25900  15.52200  1.000 15.43869  ? 244  ALA A C     1 
ATOM   1902 O  O     . ALA A 1 244 ? 6.56700   11.99800  16.30500  1.000 19.43654  ? 244  ALA A O     1 
ATOM   1903 C  CB    . ALA A 1 244 ? 5.16800   10.61100  13.68400  1.000 16.60989  ? 244  ALA A CB    1 
ATOM   1904 N  N     . GLY A 1 245 ? 5.41300   13.49700  15.08600  1.000 14.26750  ? 245  GLY A N     1 
ATOM   1905 C  CA    . GLY A 1 245 ? 6.30000   14.58000  15.45800  1.000 16.59673  ? 245  GLY A CA    1 
ATOM   1906 C  C     . GLY A 1 245 ? 6.29500   14.89600  16.94100  1.000 19.14703  ? 245  GLY A C     1 
ATOM   1907 O  O     . GLY A 1 245 ? 7.29400   15.38500  17.47700  1.000 24.03183  ? 245  GLY A O     1 
ATOM   1908 N  N     A HIS A 1 246 ? 5.22600   14.59600  17.65600  0.450 19.34442  ? 246  HIS A N     1 
ATOM   1909 N  N     B HIS A 1 246 ? 5.13400   14.68900  17.58600  0.550 19.86554  ? 246  HIS A N     1 
ATOM   1910 C  CA    A HIS A 1 246 ? 5.34100   14.87900  19.08000  0.450 18.99438  ? 246  HIS A CA    1 
ATOM   1911 C  CA    B HIS A 1 246 ? 4.90200   14.85300  19.02200  0.550 20.70248  ? 246  HIS A CA    1 
ATOM   1912 C  C     A HIS A 1 246 ? 5.33100   13.66500  19.99600  0.450 19.20493  ? 246  HIS A C     1 
ATOM   1913 C  C     B HIS A 1 246 ? 5.47100   13.67600  19.80000  0.550 16.53883  ? 246  HIS A C     1 
ATOM   1914 O  O     A HIS A 1 246 ? 5.72500   13.80000  21.15800  0.450 21.86578  ? 246  HIS A O     1 
ATOM   1915 O  O     B HIS A 1 246 ? 6.34400   13.83500  20.66400  0.550 14.99127  ? 246  HIS A O     1 
ATOM   1916 C  CB    A HIS A 1 246 ? 4.38300   15.98200  19.55400  0.450 16.38354  ? 246  HIS A CB    1 
ATOM   1917 C  CB    B HIS A 1 246 ? 3.38500   14.80400  19.28700  0.550 19.27600  ? 246  HIS A CB    1 
ATOM   1918 C  CG    A HIS A 1 246 ? 2.93800   15.64000  19.41800  0.450 19.74184  ? 246  HIS A CG    1 
ATOM   1919 C  CG    B HIS A 1 246 ? 2.66400   16.11300  19.17400  0.550 21.84736  ? 246  HIS A CG    1 
ATOM   1920 N  ND1   A HIS A 1 246 ? 1.95200   16.60200  19.40600  0.450 20.98146  ? 246  HIS A ND1   1 
ATOM   1921 N  ND1   B HIS A 1 246 ? 2.45900   16.75500  17.97100  0.550 21.15517  ? 246  HIS A ND1   1 
ATOM   1922 C  CD2   A HIS A 1 246 ? 2.30700   14.45100  19.30000  0.450 20.11820  ? 246  HIS A CD2   1 
ATOM   1923 C  CD2   B HIS A 1 246 ? 2.02600   16.85700  20.11000  0.550 20.82881  ? 246  HIS A CD2   1 
ATOM   1924 C  CE1   A HIS A 1 246 ? 0.77400   16.02000  19.27900  0.450 21.66312  ? 246  HIS A CE1   1 
ATOM   1925 C  CE1   B HIS A 1 246 ? 1.76900   17.86500  18.18100  0.550 19.76290  ? 246  HIS A CE1   1 
ATOM   1926 N  NE2   A HIS A 1 246 ? 0.96300   14.71500  19.20800  0.450 19.14440  ? 246  HIS A NE2   1 
ATOM   1927 N  NE2   B HIS A 1 246 ? 1.48800   17.94700  19.46800  0.550 20.13662  ? 246  HIS A NE2   1 
ATOM   1928 N  N     . GLU A 1 247 ? 4.94000   12.48200  19.52000  1.000 16.68621  ? 247  GLU A N     1 
ATOM   1929 C  CA    . GLU A 1 247 ? 4.99600   11.35800  20.45000  1.000 17.09942  ? 247  GLU A CA    1 
ATOM   1930 C  C     . GLU A 1 247 ? 6.37500   10.72300  20.50700  1.000 15.12550  ? 247  GLU A C     1 
ATOM   1931 O  O     . GLU A 1 247 ? 6.80700   10.27700  21.58100  1.000 17.85214  ? 247  GLU A O     1 
ATOM   1932 C  CB    . GLU A 1 247 ? 3.92000   10.32200  20.11300  1.000 19.13387  ? 247  GLU A CB    1 
ATOM   1933 C  CG    . GLU A 1 247 ? 2.48900   10.85600  20.14800  1.000 21.58680  ? 247  GLU A CG    1 
ATOM   1934 C  CD    . GLU A 1 247 ? 2.02500   11.32200  21.51900  1.000 24.82140  ? 247  GLU A CD    1 
ATOM   1935 O  OE1   . GLU A 1 247 ? 2.61000   10.90300  22.55000  1.000 26.07681  ? 247  GLU A OE1   1 
ATOM   1936 O  OE2   . GLU A 1 247 ? 1.04500   12.10500  21.56100  1.000 27.29538  ? 247  GLU A OE2   1 
ATOM   1937 N  N     . THR A 1 248 ? 7.07000   10.65700  19.37300  1.000 14.07537  ? 248  THR A N     1 
ATOM   1938 C  CA    . THR A 1 248 ? 8.35800   9.97800   19.32000  1.000 13.97273  ? 248  THR A CA    1 
ATOM   1939 C  C     . THR A 1 248 ? 9.41500   10.73500  20.11800  1.000 13.47004  ? 248  THR A C     1 
ATOM   1940 O  O     . THR A 1 248 ? 10.07800  10.16700  20.99900  1.000 16.80201  ? 248  THR A O     1 
ATOM   1941 C  CB    . THR A 1 248 ? 8.79600   9.84600   17.86400  1.000 15.50975  ? 248  THR A CB    1 
ATOM   1942 O  OG1   . THR A 1 248 ? 8.86800   11.16200  17.29300  1.000 15.97560  ? 248  THR A OG1   1 
ATOM   1943 C  CG2   . THR A 1 248 ? 7.79600   9.02400   17.07300  1.000 18.13112  ? 248  THR A CG2   1 
ATOM   1944 N  N     . THR A 1 249 ? 9.61700   12.01900  19.79500  1.000 13.93325  ? 249  THR A N     1 
ATOM   1945 C  CA    . THR A 1 249 ? 10.65300  12.77600  20.48800  1.000 15.54660  ? 249  THR A CA    1 
ATOM   1946 C  C     . THR A 1 249 ? 10.35000  12.88000  21.97000  1.000 15.36500  ? 249  THR A C     1 
ATOM   1947 O  O     . THR A 1 249 ? 11.26100  12.79600  22.80500  1.000 17.06257  ? 249  THR A O     1 
ATOM   1948 C  CB    . THR A 1 249 ? 10.78500  14.15500  19.85800  1.000 16.99151  ? 249  THR A CB    1 
ATOM   1949 O  OG1   . THR A 1 249 ? 11.13700  13.98000  18.48200  1.000 18.00742  ? 249  THR A OG1   1 
ATOM   1950 C  CG2   . THR A 1 249 ? 11.86800  14.99000  20.57000  1.000 17.98637  ? 249  THR A CG2   1 
ATOM   1951 N  N     . ALA A 1 250 ? 9.07700   13.04900  22.32200  1.000 15.90717  ? 250  ALA A N     1 
ATOM   1952 C  CA    . ALA A 1 250 ? 8.72400   13.12500  23.73900  1.000 17.57053  ? 250  ALA A CA    1 
ATOM   1953 C  C     . ALA A 1 250 ? 9.14400   11.85500  24.46900  1.000 16.32564  ? 250  ALA A C     1 
ATOM   1954 O  O     . ALA A 1 250 ? 9.72900   11.91600  25.55900  1.000 18.17850  ? 250  ALA A O     1 
ATOM   1955 C  CB    . ALA A 1 250 ? 7.22400   13.36300  23.90300  1.000 17.35734  ? 250  ALA A CB    1 
ATOM   1956 N  N     . SER A 1 251 ? 8.85600   10.69300  23.87300  1.000 17.36787  ? 251  SER A N     1 
ATOM   1957 C  CA    . SER A 1 251 ? 9.24100   9.42300   24.48100  1.000 15.93086  ? 251  SER A CA    1 
ATOM   1958 C  C     . SER A 1 251 ? 10.75500  9.29000   24.58100  1.000 16.89150  ? 251  SER A C     1 
ATOM   1959 O  O     . SER A 1 251 ? 11.27800  8.79400   25.58600  1.000 18.84173  ? 251  SER A O     1 
ATOM   1960 C  CB    . SER A 1 251 ? 8.65800   8.26600   23.67600  1.000 19.01281  ? 251  SER A CB    1 
ATOM   1961 O  OG    . SER A 1 251 ? 7.26200   8.21400   23.85900  1.000 24.06341  ? 251  SER A OG    1 
ATOM   1962 N  N     . MET A 1 252 ? 11.47700  9.69900   23.53800  1.000 15.43606  ? 252  MET A N     1 
ATOM   1963 C  CA    . MET A 1 252 ? 12.93000  9.60200   23.58500  1.000 17.06784  ? 252  MET A CA    1 
ATOM   1964 C  C     . MET A 1 252 ? 13.50300  10.48800  24.68000  1.000 16.73359  ? 252  MET A C     1 
ATOM   1965 O  O     . MET A 1 252 ? 14.46800  10.10900  25.34200  1.000 18.22587  ? 252  MET A O     1 
ATOM   1966 C  CB    . MET A 1 252 ? 13.54400  9.97000   22.23000  1.000 17.65212  ? 252  MET A CB    1 
ATOM   1967 C  CG    . MET A 1 252 ? 13.57500  8.83200   21.22200  1.000 17.71528  ? 252  MET A CG    1 
ATOM   1968 S  SD    . MET A 1 252 ? 14.46400  7.37400   21.82600  1.000 17.29944  ? 252  MET A SD    1 
ATOM   1969 C  CE    . MET A 1 252 ? 16.12100  8.00300   22.07900  1.000 18.45484  ? 252  MET A CE    1 
ATOM   1970 N  N     . THR A 1 253 ? 12.92900  11.67700  24.87700  1.000 16.72569  ? 253  THR A N     1 
ATOM   1971 C  CA    . THR A 1 253 ? 13.43600  12.57200  25.91500  1.000 17.47315  ? 253  THR A CA    1 
ATOM   1972 C  C     . THR A 1 253 ? 13.27800  11.95400  27.30000  1.000 17.67317  ? 253  THR A C     1 
ATOM   1973 O  O     . THR A 1 253 ? 14.24500  11.87200  28.07000  1.000 21.19991  ? 253  THR A O     1 
ATOM   1974 C  CB    . THR A 1 253 ? 12.71300  13.91700  25.83200  1.000 17.29681  ? 253  THR A CB    1 
ATOM   1975 O  OG1   . THR A 1 253 ? 13.05600  14.55900  24.59600  1.000 18.81805  ? 253  THR A OG1   1 
ATOM   1976 C  CG2   . THR A 1 253 ? 13.07800  14.82200  27.02700  1.000 18.46274  ? 253  THR A CG2   1 
ATOM   1977 N  N     . SER A 1 254 ? 12.06600  11.50400  27.63300  1.000 18.87858  ? 254  SER A N     1 
ATOM   1978 C  CA    A SER A 1 254 ? 11.82600  10.96800  28.97100  0.490 19.24968  ? 254  SER A CA    1 
ATOM   1979 C  CA    B SER A 1 254 ? 11.81400  10.96000  28.96700  0.510 19.55761  ? 254  SER A CA    1 
ATOM   1980 C  C     . SER A 1 254 ? 12.62500  9.69200   29.21000  1.000 19.10755  ? 254  SER A C     1 
ATOM   1981 O  O     . SER A 1 254 ? 13.22800  9.51900   30.27700  1.000 23.18436  ? 254  SER A O     1 
ATOM   1982 C  CB    A SER A 1 254 ? 10.33200  10.73000  29.19400  0.490 20.74986  ? 254  SER A CB    1 
ATOM   1983 C  CB    B SER A 1 254 ? 10.31700  10.68900  29.15200  0.510 21.23412  ? 254  SER A CB    1 
ATOM   1984 O  OG    A SER A 1 254 ? 9.60500   11.93800  29.08200  0.490 22.54218  ? 254  SER A OG    1 
ATOM   1985 O  OG    B SER A 1 254 ? 9.85800   9.67000   28.27100  0.510 21.09990  ? 254  SER A OG    1 
ATOM   1986 N  N     . LEU A 1 255 ? 12.63700  8.77800   28.23300  1.000 18.05480  ? 255  LEU A N     1 
ATOM   1987 C  CA    . LEU A 1 255 ? 13.38400  7.53900   28.41400  1.000 19.13650  ? 255  LEU A CA    1 
ATOM   1988 C  C     . LEU A 1 255 ? 14.88800  7.78600   28.43500  1.000 19.02860  ? 255  LEU A C     1 
ATOM   1989 O  O     . LEU A 1 255 ? 15.61800  7.08300   29.14800  1.000 20.98146  ? 255  LEU A O     1 
ATOM   1990 C  CB    . LEU A 1 255 ? 13.00200  6.52000   27.33400  1.000 19.70236  ? 255  LEU A CB    1 
ATOM   1991 C  CG    . LEU A 1 255 ? 11.58000  5.94300   27.40900  1.000 21.94474  ? 255  LEU A CG    1 
ATOM   1992 C  CD1   . LEU A 1 255 ? 11.33500  4.89200   26.32500  1.000 21.75261  ? 255  LEU A CD1   1 
ATOM   1993 C  CD2   . LEU A 1 255 ? 11.33100  5.35400   28.78600  1.000 28.44552  ? 255  LEU A CD2   1 
ATOM   1994 N  N     . SER A 1 256 ? 15.37400  8.76700   27.66800  1.000 18.77594  ? 256  SER A N     1 
ATOM   1995 C  CA    . SER A 1 256 ? 16.79900  9.09200   27.70900  1.000 19.22336  ? 256  SER A CA    1 
ATOM   1996 C  C     . SER A 1 256 ? 17.20000  9.64800   29.06900  1.000 20.40508  ? 256  SER A C     1 
ATOM   1997 O  O     . SER A 1 256 ? 18.29200  9.35200   29.56400  1.000 21.47100  ? 256  SER A O     1 
ATOM   1998 C  CB    . SER A 1 256 ? 17.17400  10.08300  26.60100  1.000 19.46286  ? 256  SER A CB    1 
ATOM   1999 O  OG    . SER A 1 256 ? 17.07200  9.50100   25.31100  1.000 19.37864  ? 256  SER A OG    1 
ATOM   2000 N  N     . VAL A 1 257 ? 16.34900  10.48200  29.66800  1.000 20.68143  ? 257  VAL A N     1 
ATOM   2001 C  CA    . VAL A 1 257 ? 16.65900  11.01200  30.99500  1.000 20.92356  ? 257  VAL A CA    1 
ATOM   2002 C  C     . VAL A 1 257 ? 16.75600  9.87800   32.00500  1.000 22.86853  ? 257  VAL A C     1 
ATOM   2003 O  O     . VAL A 1 257 ? 17.71800  9.79400   32.78000  1.000 26.20314  ? 257  VAL A O     1 
ATOM   2004 C  CB    . VAL A 1 257 ? 15.63700  12.08300  31.41600  1.000 22.03422  ? 257  VAL A CB    1 
ATOM   2005 C  CG1   . VAL A 1 257 ? 15.77300  12.38200  32.90500  1.000 23.32911  ? 257  VAL A CG1   1 
ATOM   2006 C  CG2   . VAL A 1 257 ? 15.85800  13.36100  30.62000  1.000 25.88731  ? 257  VAL A CG2   1 
ATOM   2007 N  N     . ILE A 1 258 ? 15.76700  8.97800   32.00200  1.000 22.63692  ? 258  ILE A N     1 
ATOM   2008 C  CA    . ILE A 1 258 ? 15.80500  7.83700   32.91500  1.000 23.44755  ? 258  ILE A CA    1 
ATOM   2009 C  C     . ILE A 1 258 ? 17.08200  7.03600   32.70900  1.000 22.99749  ? 258  ILE A C     1 
ATOM   2010 O  O     . ILE A 1 258 ? 17.77800  6.67000   33.66700  1.000 25.46621  ? 258  ILE A O     1 
ATOM   2011 C  CB    . ILE A 1 258 ? 14.55400  6.96000   32.73200  1.000 23.40807  ? 258  ILE A CB    1 
ATOM   2012 C  CG1   . ILE A 1 258 ? 13.29300  7.73500   33.11300  1.000 25.39778  ? 258  ILE A CG1   1 
ATOM   2013 C  CG2   . ILE A 1 258 ? 14.67700  5.68700   33.56000  1.000 24.90825  ? 258  ILE A CG2   1 
ATOM   2014 C  CD1   . ILE A 1 258 ? 12.02700  7.11700   32.56200  1.000 25.09511  ? 258  ILE A CD1   1 
ATOM   2015 N  N     . THR A 1 259 ? 17.40700  6.75400   31.44900  1.000 23.25805  ? 259  THR A N     1 
ATOM   2016 C  CA    . THR A 1 259 ? 18.54800  5.90700   31.13300  1.000 23.18436  ? 259  THR A CA    1 
ATOM   2017 C  C     . THR A 1 259 ? 19.85700  6.57300   31.53400  1.000 23.43965  ? 259  THR A C     1 
ATOM   2018 O  O     . THR A 1 259 ? 20.72100  5.93700   32.15200  1.000 25.56359  ? 259  THR A O     1 
ATOM   2019 C  CB    . THR A 1 259 ? 18.52200  5.57100   29.63700  1.000 21.80525  ? 259  THR A CB    1 
ATOM   2020 O  OG1   . THR A 1 259 ? 17.27200  4.93800   29.31700  1.000 21.44731  ? 259  THR A OG1   1 
ATOM   2021 C  CG2   . THR A 1 259 ? 19.67000  4.64300   29.25100  1.000 21.82893  ? 259  THR A CG2   1 
ATOM   2022 N  N     . LEU A 1 260 ? 20.02000  7.86000   31.20500  1.000 22.40269  ? 260  LEU A N     1 
ATOM   2023 C  CA    . LEU A 1 260 ? 21.26900  8.54700   31.53000  1.000 20.63932  ? 260  LEU A CA    1 
ATOM   2024 C  C     . LEU A 1 260 ? 21.47900  8.63300   33.03700  1.000 24.09499  ? 260  LEU A C     1 
ATOM   2025 O  O     . LEU A 1 260 ? 22.60500  8.46600   33.52300  1.000 26.16893  ? 260  LEU A O     1 
ATOM   2026 C  CB    . LEU A 1 260 ? 21.31400  9.93000   30.86700  1.000 22.11581  ? 260  LEU A CB    1 
ATOM   2027 C  CG    . LEU A 1 260 ? 21.49000  9.90100   29.33500  1.000 22.92643  ? 260  LEU A CG    1 
ATOM   2028 C  CD1   . LEU A 1 260 ? 21.17600  11.25200  28.72300  1.000 22.77115  ? 260  LEU A CD1   1 
ATOM   2029 C  CD2   . LEU A 1 260 ? 22.90600  9.47600   28.97000  1.000 24.89772  ? 260  LEU A CD2   1 
ATOM   2030 N  N     . LEU A 1 261 ? 20.40200  8.85700   33.79300  1.000 26.30842  ? 261  LEU A N     1 
ATOM   2031 C  CA    . LEU A 1 261 ? 20.53400  8.93000   35.24900  1.000 27.16642  ? 261  LEU A CA    1 
ATOM   2032 C  C     . LEU A 1 261 ? 20.91400  7.58400   35.86600  1.000 28.19812  ? 261  LEU A C     1 
ATOM   2033 O  O     . LEU A 1 261 ? 21.56800  7.55200   36.91800  1.000 29.81673  ? 261  LEU A O     1 
ATOM   2034 C  CB    . LEU A 1 261 ? 19.25800  9.49800   35.86300  1.000 28.29550  ? 261  LEU A CB    1 
ATOM   2035 C  CG    . LEU A 1 261 ? 18.98900  10.96500  35.53400  1.000 30.97740  ? 261  LEU A CG    1 
ATOM   2036 C  CD1   . LEU A 1 261 ? 17.64100  11.39600  36.07300  1.000 30.07729  ? 261  LEU A CD1   1 
ATOM   2037 C  CD2   . LEU A 1 261 ? 20.10600  11.86500  36.05100  1.000 29.76936  ? 261  LEU A CD2   1 
ATOM   2038 N  N     . ASP A 1 262 ? 20.52800  6.47000   35.23800  1.000 26.44001  ? 262  ASP A N     1 
ATOM   2039 C  CA    . ASP A 1 262 ? 20.97000  5.14600   35.66600  1.000 27.17431  ? 262  ASP A CA    1 
ATOM   2040 C  C     . ASP A 1 262 ? 22.38200  4.80200   35.20800  1.000 27.20589  ? 262  ASP A C     1 
ATOM   2041 O  O     . ASP A 1 262 ? 22.91000  3.76000   35.61700  1.000 30.54577  ? 262  ASP A O     1 
ATOM   2042 C  CB    . ASP A 1 262 ? 20.02300  4.05800   35.15600  1.000 29.85358  ? 262  ASP A CB    1 
ATOM   2043 C  CG    . ASP A 1 262 ? 18.91600  3.73700   36.13600  1.000 32.24860  ? 262  ASP A CG    1 
ATOM   2044 O  OD1   . ASP A 1 262 ? 18.71000  4.51600   37.09500  1.000 31.79065  ? 262  ASP A OD1   1 
ATOM   2045 O  OD2   . ASP A 1 262 ? 18.25500  2.69600   35.94800  1.000 33.60666  ? 262  ASP A OD2   1 
ATOM   2046 N  N     . HIS A 1 263 ? 23.00100  5.63800   34.37800  1.000 26.32947  ? 263  HIS A N     1 
ATOM   2047 C  CA    . HIS A 1 263 ? 24.37300  5.43700   33.91300  1.000 26.56898  ? 263  HIS A CA    1 
ATOM   2048 C  C     . HIS A 1 263 ? 25.16600  6.70900   34.18300  1.000 28.05336  ? 263  HIS A C     1 
ATOM   2049 O  O     . HIS A 1 263 ? 25.62800  7.38400   33.25600  1.000 26.70583  ? 263  HIS A O     1 
ATOM   2050 C  CB    . HIS A 1 263 ? 24.39800  5.06700   32.42900  1.000 25.95311  ? 263  HIS A CB    1 
ATOM   2051 C  CG    . HIS A 1 263 ? 23.70400  3.77800   32.11900  1.000 26.04523  ? 263  HIS A CG    1 
ATOM   2052 N  ND1   . HIS A 1 263 ? 22.33400  3.68100   32.00500  1.000 25.90574  ? 263  HIS A ND1   1 
ATOM   2053 C  CD2   . HIS A 1 263 ? 24.18900  2.52900   31.92000  1.000 26.85848  ? 263  HIS A CD2   1 
ATOM   2054 C  CE1   . HIS A 1 263 ? 22.00600  2.43000   31.72800  1.000 25.57412  ? 263  HIS A CE1   1 
ATOM   2055 N  NE2   . HIS A 1 263 ? 23.11400  1.71100   31.67200  1.000 27.37697  ? 263  HIS A NE2   1 
ATOM   2056 N  N     . PRO A 1 264 ? 25.35300  7.05700   35.46000  1.000 28.60343  ? 264  PRO A N     1 
ATOM   2057 C  CA    . PRO A 1 264 ? 25.92800  8.37300   35.78900  1.000 30.50366  ? 264  PRO A CA    1 
ATOM   2058 C  C     . PRO A 1 264 ? 27.32400  8.59400   35.24300  1.000 32.80393  ? 264  PRO A C     1 
ATOM   2059 O  O     . PRO A 1 264 ? 27.68200  9.73500   34.92600  1.000 35.44109  ? 264  PRO A O     1 
ATOM   2060 C  CB    . PRO A 1 264 ? 25.90100  8.39400   37.32500  1.000 31.40113  ? 264  PRO A CB    1 
ATOM   2061 C  CG    . PRO A 1 264 ? 25.85200  6.94500   37.72900  1.000 29.77989  ? 264  PRO A CG    1 
ATOM   2062 C  CD    . PRO A 1 264 ? 25.03500  6.27100   36.66400  1.000 28.55869  ? 264  PRO A CD    1 
ATOM   2063 N  N     . GLU A 1 265 ? 28.13000  7.53900   35.13200  1.000 33.80405  ? 265  GLU A N     1 
ATOM   2064 C  CA    . GLU A 1 265 ? 29.47000  7.69200   34.57900  1.000 36.22540  ? 265  GLU A CA    1 
ATOM   2065 C  C     . GLU A 1 265 ? 29.40900  8.19600   33.14300  1.000 35.41214  ? 265  GLU A C     1 
ATOM   2066 O  O     . GLU A 1 265 ? 30.14200  9.11700   32.76200  1.000 34.23568  ? 265  GLU A O     1 
ATOM   2067 C  CB    . GLU A 1 265 ? 30.20000  6.35400   34.65600  1.000 41.96293  ? 265  GLU A CB    1 
ATOM   2068 C  CG    . GLU A 1 265 ? 31.68800  6.42800   34.43100  1.000 50.54817  ? 265  GLU A CG    1 
ATOM   2069 C  CD    . GLU A 1 265 ? 32.42900  5.36000   35.21400  1.000 57.97537  ? 265  GLU A CD    1 
ATOM   2070 O  OE1   . GLU A 1 265 ? 31.87700  4.88500   36.23200  1.000 59.56504  ? 265  GLU A OE1   1 
ATOM   2071 O  OE2   . GLU A 1 265 ? 33.55400  4.99500   34.81200  1.000 61.40473  ? 265  GLU A OE2   1 
ATOM   2072 N  N     . GLN A 1 266 ? 28.51500  7.62500   32.33900  1.000 32.35125  ? 266  GLN A N     1 
ATOM   2073 C  CA    . GLN A 1 266 ? 28.41000  8.05300   30.95000  1.000 30.30100  ? 266  GLN A CA    1 
ATOM   2074 C  C     . GLN A 1 266 ? 27.76000  9.42200   30.83900  1.000 29.59302  ? 266  GLN A C     1 
ATOM   2075 O  O     . GLN A 1 266 ? 28.11200  10.21100  29.95200  1.000 31.16953  ? 266  GLN A O     1 
ATOM   2076 C  CB    . GLN A 1 266 ? 27.64700  7.01700   30.13500  1.000 30.12203  ? 266  GLN A CB    1 
ATOM   2077 C  CG    . GLN A 1 266 ? 28.29600  5.66200   30.20200  1.000 30.71158  ? 266  GLN A CG    1 
ATOM   2078 C  CD    . GLN A 1 266 ? 27.72500  4.69400   29.21300  1.000 28.05336  ? 266  GLN A CD    1 
ATOM   2079 O  OE1   . GLN A 1 266 ? 27.56200  5.01500   28.03300  1.000 30.43786  ? 266  GLN A OE1   1 
ATOM   2080 N  NE2   . GLN A 1 266 ? 27.40900  3.49500   29.68300  1.000 30.21415  ? 266  GLN A NE2   1 
ATOM   2081 N  N     . TYR A 1 267 ? 26.78900  9.71500   31.70400  1.000 29.16929  ? 267  TYR A N     1 
ATOM   2082 C  CA    . TYR A 1 267 ? 26.17600  11.03800  31.67200  1.000 29.51407  ? 267  TYR A CA    1 
ATOM   2083 C  C     . TYR A 1 267 ? 27.18400  12.11500  32.05300  1.000 30.81159  ? 267  TYR A C     1 
ATOM   2084 O  O     . TYR A 1 267 ? 27.19800  13.20000  31.45700  1.000 31.45377  ? 267  TYR A O     1 
ATOM   2085 C  CB    . TYR A 1 267 ? 24.94900  11.07600  32.58300  1.000 28.74292  ? 267  TYR A CB    1 
ATOM   2086 C  CG    . TYR A 1 267 ? 24.01800  12.23800  32.32300  1.000 29.38773  ? 267  TYR A CG    1 
ATOM   2087 C  CD1   . TYR A 1 267 ? 23.93900  12.83200  31.06600  1.000 28.47973  ? 267  TYR A CD1   1 
ATOM   2088 C  CD2   . TYR A 1 267 ? 23.22600  12.75500  33.34200  1.000 32.51969  ? 267  TYR A CD2   1 
ATOM   2089 C  CE1   . TYR A 1 267 ? 23.08000  13.89800  30.82900  1.000 30.48523  ? 267  TYR A CE1   1 
ATOM   2090 C  CE2   . TYR A 1 267 ? 22.37300  13.81800  33.11600  1.000 32.79867  ? 267  TYR A CE2   1 
ATOM   2091 C  CZ    . TYR A 1 267 ? 22.30100  14.38300  31.85700  1.000 31.49325  ? 267  TYR A CZ    1 
ATOM   2092 O  OH    . TYR A 1 267 ? 21.45700  15.44700  31.63500  1.000 33.74615  ? 267  TYR A OH    1 
ATOM   2093 N  N     . ALA A 1 268 ? 28.04000  11.83000  33.03900  1.000 30.76421  ? 268  ALA A N     1 
ATOM   2094 C  CA    . ALA A 1 268 ? 29.08400  12.78100  33.41000  1.000 33.37242  ? 268  ALA A CA    1 
ATOM   2095 C  C     . ALA A 1 268 ? 30.06600  12.99200  32.26600  1.000 35.06736  ? 268  ALA A C     1 
ATOM   2096 O  O     . ALA A 1 268 ? 30.50400  14.12000  32.01200  1.000 35.69375  ? 268  ALA A O     1 
ATOM   2097 C  CB    . ALA A 1 268 ? 29.81500  12.30300  34.66600  1.000 35.92799  ? 268  ALA A CB    1 
ATOM   2098 N  N     . ALA A 1 269 ? 30.42300  11.91600  31.56000  1.000 32.66707  ? 269  ALA A N     1 
ATOM   2099 C  CA    . ALA A 1 269 ? 31.32300  12.05700  30.42100  1.000 33.35926  ? 269  ALA A CA    1 
ATOM   2100 C  C     . ALA A 1 269 ? 30.67400  12.87900  29.31700  1.000 34.56730  ? 269  ALA A C     1 
ATOM   2101 O  O     . ALA A 1 269 ? 31.33600  13.69300  28.66100  1.000 35.08315  ? 269  ALA A O     1 
ATOM   2102 C  CB    . ALA A 1 269 ? 31.72500  10.67800  29.90000  1.000 31.41692  ? 269  ALA A CB    1 
ATOM   2103 N  N     . LEU A 1 270 ? 29.37500  12.67900  29.10100  1.000 32.36177  ? 270  LEU A N     1 
ATOM   2104 C  CA    . LEU A 1 270 ? 28.66500  13.46200  28.09900  1.000 31.55378  ? 270  LEU A CA    1 
ATOM   2105 C  C     . LEU A 1 270 ? 28.70300  14.94900  28.44100  1.000 33.49349  ? 270  LEU A C     1 
ATOM   2106 O  O     . LEU A 1 270 ? 28.93700  15.79100  27.56400  1.000 34.06198  ? 270  LEU A O     1 
ATOM   2107 C  CB    . LEU A 1 270 ? 27.22900  12.95000  27.98600  1.000 30.97740  ? 270  LEU A CB    1 
ATOM   2108 C  CG    . LEU A 1 270 ? 26.39700  13.43400  26.80800  1.000 31.04056  ? 270  LEU A CG    1 
ATOM   2109 C  CD1   . LEU A 1 270 ? 27.07800  13.05100  25.49700  1.000 32.07227  ? 270  LEU A CD1   1 
ATOM   2110 C  CD2   . LEU A 1 270 ? 25.01200  12.82300  26.90000  1.000 30.64841  ? 270  LEU A CD2   1 
ATOM   2111 N  N     . ARG A 1 271 ? 28.50100  15.29100  29.71700  1.000 32.03805  ? 271  ARG A N     1 
ATOM   2112 C  CA    A ARG A 1 271 ? 28.50700  16.69700  30.10800  0.510 34.00408  ? 271  ARG A CA    1 
ATOM   2113 C  CA    B ARG A 1 271 ? 28.50900  16.69600  30.11700  0.490 33.27504  ? 271  ARG A CA    1 
ATOM   2114 C  C     . ARG A 1 271 ? 29.88100  17.32400  29.89800  1.000 33.88827  ? 271  ARG A C     1 
ATOM   2115 O  O     . ARG A 1 271 ? 29.98500  18.48200  29.47800  1.000 33.92512  ? 271  ARG A O     1 
ATOM   2116 C  CB    A ARG A 1 271 ? 28.07100  16.83900  31.56600  0.510 35.33055  ? 271  ARG A CB    1 
ATOM   2117 C  CB    B ARG A 1 271 ? 28.07300  16.82300  31.58100  0.490 33.14608  ? 271  ARG A CB    1 
ATOM   2118 C  CG    A ARG A 1 271 ? 27.40400  18.16300  31.87700  0.510 38.38092  ? 271  ARG A CG    1 
ATOM   2119 C  CG    B ARG A 1 271 ? 27.96300  18.25500  32.10200  0.490 34.79628  ? 271  ARG A CG    1 
ATOM   2120 C  CD    A ARG A 1 271 ? 27.86300  18.72700  33.20700  0.510 41.32074  ? 271  ARG A CD    1 
ATOM   2121 C  CD    B ARG A 1 271 ? 26.92000  18.36800  33.21800  0.490 37.16761  ? 271  ARG A CD    1 
ATOM   2122 N  NE    A ARG A 1 271 ? 27.14700  19.94900  33.55200  0.510 43.30256  ? 271  ARG A NE    1 
ATOM   2123 N  NE    B ARG A 1 271 ? 27.37100  17.81200  34.49000  0.490 40.25483  ? 271  ARG A NE    1 
ATOM   2124 C  CZ    A ARG A 1 271 ? 27.39400  21.14100  33.02300  0.510 43.90526  ? 271  ARG A CZ    1 
ATOM   2125 C  CZ    B ARG A 1 271 ? 27.61000  18.53000  35.58100  0.490 41.46023  ? 271  ARG A CZ    1 
ATOM   2126 N  NH1   A ARG A 1 271 ? 28.32500  21.30800  32.09600  0.510 42.93673  ? 271  ARG A NH1   1 
ATOM   2127 N  NH1   B ARG A 1 271 ? 27.44600  19.84200  35.59500  0.490 42.46562  ? 271  ARG A NH1   1 
ATOM   2128 N  NH2   A ARG A 1 271 ? 26.68700  22.19100  33.43200  0.510 43.39731  ? 271  ARG A NH2   1 
ATOM   2129 N  NH2   B ARG A 1 271 ? 28.01600  17.91500  36.68900  0.490 40.36537  ? 271  ARG A NH2   1 
ATOM   2130 N  N     . ALA A 1 272 ? 30.94600  16.56700  30.16300  1.000 35.54900  ? 272  ALA A N     1 
ATOM   2131 C  CA    . ALA A 1 272 ? 32.30400  17.09000  30.06600  1.000 35.71744  ? 272  ALA A CA    1 
ATOM   2132 C  C     . ALA A 1 272 ? 32.79700  17.24600  28.63200  1.000 37.62293  ? 272  ALA A C     1 
ATOM   2133 O  O     . ALA A 1 272 ? 33.80000  17.93500  28.41200  1.000 40.24430  ? 272  ALA A O     1 
ATOM   2134 C  CB    . ALA A 1 272 ? 33.26600  16.19800  30.85300  1.000 35.46215  ? 272  ALA A CB    1 
ATOM   2135 N  N     . ASP A 1 273 ? 32.13400  16.62900  27.65400  1.000 36.54912  ? 273  ASP A N     1 
ATOM   2136 C  CA    . ASP A 1 273 ? 32.59000  16.72500  26.26500  1.000 35.87272  ? 273  ASP A CA    1 
ATOM   2137 C  C     . ASP A 1 273 ? 31.34700  16.68600  25.37500  1.000 31.93804  ? 273  ASP A C     1 
ATOM   2138 O  O     . ASP A 1 273 ? 30.89300  15.61500  24.96500  1.000 31.10373  ? 273  ASP A O     1 
ATOM   2139 C  CB    . ASP A 1 273 ? 33.57500  15.62000  25.91400  1.000 37.49923  ? 273  ASP A CB    1 
ATOM   2140 C  CG    . ASP A 1 273 ? 34.07400  15.71200  24.48000  1.000 41.29706  ? 273  ASP A CG    1 
ATOM   2141 O  OD1   . ASP A 1 273 ? 33.71100  16.68000  23.77300  1.000 40.06007  ? 273  ASP A OD1   1 
ATOM   2142 O  OD2   . ASP A 1 273 ? 34.82800  14.81100  24.05400  1.000 43.04463  ? 273  ASP A OD2   1 
ATOM   2143 N  N     . ARG A 1 274 ? 30.82000  17.87200  25.06600  1.000 31.31954  ? 274  ARG A N     1 
ATOM   2144 C  CA    . ARG A 1 274 ? 29.57200  17.96300  24.31900  1.000 28.81398  ? 274  ARG A CA    1 
ATOM   2145 C  C     . ARG A 1 274 ? 29.71300  17.50100  22.87800  1.000 27.89808  ? 274  ARG A C     1 
ATOM   2146 O  O     . ARG A 1 274 ? 28.69000  17.27000  22.22000  1.000 28.35340  ? 274  ARG A O     1 
ATOM   2147 C  CB    . ARG A 1 274 ? 29.02400  19.38900  24.34500  1.000 31.37481  ? 274  ARG A CB    1 
ATOM   2148 C  CG    . ARG A 1 274 ? 28.84100  19.95600  25.73100  1.000 31.45904  ? 274  ARG A CG    1 
ATOM   2149 C  CD    . ARG A 1 274 ? 28.00700  19.04800  26.63000  1.000 30.58788  ? 274  ARG A CD    1 
ATOM   2150 N  NE    . ARG A 1 274 ? 27.81600  19.67600  27.93000  1.000 31.86961  ? 274  ARG A NE    1 
ATOM   2151 C  CZ    . ARG A 1 274 ? 26.87400  20.57200  28.19000  1.000 30.54577  ? 274  ARG A CZ    1 
ATOM   2152 N  NH1   . ARG A 1 274 ? 25.95900  20.89500  27.28900  1.000 30.29837  ? 274  ARG A NH1   1 
ATOM   2153 N  NH2   . ARG A 1 274 ? 26.85300  21.16200  29.38200  1.000 32.44600  ? 274  ARG A NH2   1 
ATOM   2154 N  N     . SER A 1 275 ? 30.94200  17.35900  22.36700  1.000 28.55869  ? 275  SER A N     1 
ATOM   2155 C  CA    . SER A 1 275 ? 31.09800  16.79200  21.03000  1.000 28.69555  ? 275  SER A CA    1 
ATOM   2156 C  C     . SER A 1 275 ? 30.60200  15.35600  20.96700  1.000 27.00061  ? 275  SER A C     1 
ATOM   2157 O  O     . SER A 1 275 ? 30.38100  14.83300  19.86800  1.000 27.29801  ? 275  SER A O     1 
ATOM   2158 C  CB    . SER A 1 275 ? 32.55000  16.87600  20.55000  1.000 28.96926  ? 275  SER A CB    1 
ATOM   2159 O  OG    . SER A 1 275 ? 33.37400  15.92100  21.19900  1.000 32.47231  ? 275  SER A OG    1 
ATOM   2160 N  N     . LEU A 1 276 ? 30.40500  14.71900  22.12100  1.000 27.31906  ? 276  LEU A N     1 
ATOM   2161 C  CA    . LEU A 1 276 ? 29.87100  13.36500  22.19700  1.000 24.40029  ? 276  LEU A CA    1 
ATOM   2162 C  C     . LEU A 1 276 ? 28.35300  13.29500  22.05500  1.000 23.05540  ? 276  LEU A C     1 
ATOM   2163 O  O     . LEU A 1 276 ? 27.81900  12.19000  21.91000  1.000 23.00013  ? 276  LEU A O     1 
ATOM   2164 C  CB    . LEU A 1 276 ? 30.25700  12.74400  23.53700  1.000 27.69543  ? 276  LEU A CB    1 
ATOM   2165 C  CG    . LEU A 1 276 ? 31.75100  12.55100  23.75900  1.000 30.78001  ? 276  LEU A CG    1 
ATOM   2166 C  CD1   . LEU A 1 276 ? 32.01800  12.10800  25.18600  1.000 31.67748  ? 276  LEU A CD1   1 
ATOM   2167 C  CD2   . LEU A 1 276 ? 32.29700  11.54200  22.75900  1.000 30.28258  ? 276  LEU A CD2   1 
ATOM   2168 N  N     . VAL A 1 277 ? 27.64900  14.43000  22.10200  1.000 23.55019  ? 277  VAL A N     1 
ATOM   2169 C  CA    . VAL A 1 277 ? 26.18300  14.39100  22.10600  1.000 22.25004  ? 277  VAL A CA    1 
ATOM   2170 C  C     . VAL A 1 277 ? 25.58500  13.73400  20.86800  1.000 20.14715  ? 277  VAL A C     1 
ATOM   2171 O  O     . VAL A 1 277 ? 24.68900  12.88600  21.02000  1.000 20.52615  ? 277  VAL A O     1 
ATOM   2172 C  CB    . VAL A 1 277 ? 25.60700  15.79000  22.40500  1.000 22.17898  ? 277  VAL A CB    1 
ATOM   2173 C  CG1   . VAL A 1 277 ? 24.09300  15.77800  22.22200  1.000 23.38965  ? 277  VAL A CG1   1 
ATOM   2174 C  CG2   . VAL A 1 277 ? 25.98100  16.22000  23.80800  1.000 23.07645  ? 277  VAL A CG2   1 
ATOM   2175 N  N     . PRO A 1 278 ? 25.98400  14.07800  19.64000  1.000 22.03422  ? 278  PRO A N     1 
ATOM   2176 C  CA    . PRO A 1 278 ? 25.36600  13.40200  18.48300  1.000 19.66288  ? 278  PRO A CA    1 
ATOM   2177 C  C     . PRO A 1 278 ? 25.54600  11.89500  18.51300  1.000 20.19716  ? 278  PRO A C     1 
ATOM   2178 O  O     . PRO A 1 278 ? 24.58900  11.15300  18.25200  1.000 18.72593  ? 278  PRO A O     1 
ATOM   2179 C  CB    . PRO A 1 278 ? 26.05200  14.07000  17.28100  1.000 21.76577  ? 278  PRO A CB    1 
ATOM   2180 C  CG    . PRO A 1 278 ? 26.43600  15.42300  17.78100  1.000 24.34766  ? 278  PRO A CG    1 
ATOM   2181 C  CD    . PRO A 1 278 ? 26.86100  15.18500  19.21200  1.000 25.17407  ? 278  PRO A CD    1 
ATOM   2182 N  N     . GLY A 1 279 ? 26.74500  11.42200  18.86500  1.000 21.89473  ? 279  GLY A N     1 
ATOM   2183 C  CA    . GLY A 1 279 ? 26.95300  9.98800   18.99400  1.000 20.41034  ? 279  GLY A CA    1 
ATOM   2184 C  C     . GLY A 1 279 ? 26.13400  9.37600   20.11400  1.000 19.30231  ? 279  GLY A C     1 
ATOM   2185 O  O     . GLY A 1 279 ? 25.62100  8.25800   19.98200  1.000 20.36297  ? 279  GLY A O     1 
ATOM   2186 N  N     . ALA A 1 280 ? 25.99300  10.10000  21.22900  1.000 18.68645  ? 280  ALA A N     1 
ATOM   2187 C  CA    . ALA A 1 280 ? 25.18500  9.60300   22.34000  1.000 18.59170  ? 280  ALA A CA    1 
ATOM   2188 C  C     . ALA A 1 280 ? 23.71500  9.51300   21.95500  1.000 18.06006  ? 280  ALA A C     1 
ATOM   2189 O  O     . ALA A 1 280 ? 23.00900  8.59100   22.37900  1.000 18.25745  ? 280  ALA A O     1 
ATOM   2190 C  CB    . ALA A 1 280 ? 25.36300  10.50300  23.56000  1.000 20.35244  ? 280  ALA A CB    1 
ATOM   2191 N  N     . VAL A 1 281 ? 23.23800  10.45200  21.13900  1.000 17.96531  ? 281  VAL A N     1 
ATOM   2192 C  CA    . VAL A 1 281 ? 21.86200  10.38100  20.66000  1.000 17.42051  ? 281  VAL A CA    1 
ATOM   2193 C  C     . VAL A 1 281 ? 21.66100  9.13300   19.81100  1.000 17.28365  ? 281  VAL A C     1 
ATOM   2194 O  O     . VAL A 1 281 ? 20.64400  8.44200   19.93900  1.000 17.96268  ? 281  VAL A O     1 
ATOM   2195 C  CB    . VAL A 1 281 ? 21.48200  11.67500  19.91600  1.000 17.82319  ? 281  VAL A CB    1 
ATOM   2196 C  CG1   . VAL A 1 281 ? 20.16200  11.51000  19.18100  1.000 18.54696  ? 281  VAL A CG1   1 
ATOM   2197 C  CG2   . VAL A 1 281 ? 21.38300  12.82400  20.90600  1.000 17.92057  ? 281  VAL A CG2   1 
ATOM   2198 N  N     . GLU A 1 282 ? 22.62500  8.81800   18.93400  1.000 16.87571  ? 282  GLU A N     1 
ATOM   2199 C  CA    . GLU A 1 282 ? 22.49400  7.60900   18.12600  1.000 15.58345  ? 282  GLU A CA    1 
ATOM   2200 C  C     . GLU A 1 282 ? 22.46700  6.36800   19.00600  1.000 15.21761  ? 282  GLU A C     1 
ATOM   2201 O  O     . GLU A 1 282 ? 21.67500  5.44800   18.76500  1.000 15.72820  ? 282  GLU A O     1 
ATOM   2202 C  CB    . GLU A 1 282 ? 23.62400  7.51300   17.11100  1.000 16.05982  ? 282  GLU A CB    1 
ATOM   2203 C  CG    . GLU A 1 282 ? 23.56700  8.57600   16.04000  1.000 17.13363  ? 282  GLU A CG    1 
ATOM   2204 C  CD    . GLU A 1 282 ? 22.21300  8.66500   15.36200  1.000 17.08100  ? 282  GLU A CD    1 
ATOM   2205 O  OE1   . GLU A 1 282 ? 21.81700  7.69000   14.68000  1.000 18.97333  ? 282  GLU A OE1   1 
ATOM   2206 O  OE2   . GLU A 1 282 ? 21.54900  9.71300   15.51200  1.000 18.51275  ? 282  GLU A OE2   1 
ATOM   2207 N  N     . GLU A 1 283 ? 23.33100  6.32300   20.02700  1.000 16.61252  ? 283  GLU A N     1 
ATOM   2208 C  CA    . GLU A 1 283 ? 23.34400  5.16400   20.91600  1.000 16.68884  ? 283  GLU A CA    1 
ATOM   2209 C  C     . GLU A 1 283 ? 22.03300  5.04500   21.68300  1.000 18.22061  ? 283  GLU A C     1 
ATOM   2210 O  O     . GLU A 1 283 ? 21.48400  3.94400   21.81900  1.000 18.98649  ? 283  GLU A O     1 
ATOM   2211 C  CB    . GLU A 1 283 ? 24.55600  5.19600   21.85700  1.000 19.56814  ? 283  GLU A CB    1 
ATOM   2212 C  CG    . GLU A 1 283 ? 24.54500  4.14800   22.97100  1.000 19.17072  ? 283  GLU A CG    1 
ATOM   2213 C  CD    . GLU A 1 283 ? 24.78100  2.73000   22.47200  1.000 21.15517  ? 283  GLU A CD    1 
ATOM   2214 O  OE1   . GLU A 1 283 ? 24.63400  2.47400   21.25100  1.000 20.48667  ? 283  GLU A OE1   1 
ATOM   2215 O  OE2   . GLU A 1 283 ? 25.11500  1.86600   23.31000  1.000 22.23951  ? 283  GLU A OE2   1 
ATOM   2216 N  N     . LEU A 1 284 ? 21.50900  6.16500   22.18200  1.000 15.73610  ? 284  LEU A N     1 
ATOM   2217 C  CA    . LEU A 1 284 ? 20.22000  6.12900   22.86600  1.000 16.19668  ? 284  LEU A CA    1 
ATOM   2218 C  C     . LEU A 1 284 ? 19.10000  5.67700   21.93200  1.000 16.08877  ? 284  LEU A C     1 
ATOM   2219 O  O     . LEU A 1 284 ? 18.18900  4.95500   22.35200  1.000 16.08088  ? 284  LEU A O     1 
ATOM   2220 C  CB    . LEU A 1 284 ? 19.90500  7.49600   23.46300  1.000 17.02836  ? 284  LEU A CB    1 
ATOM   2221 C  CG    . LEU A 1 284 ? 20.74200  7.85700   24.70000  1.000 18.66540  ? 284  LEU A CG    1 
ATOM   2222 C  CD1   . LEU A 1 284 ? 20.72100  9.37200   24.96600  1.000 18.54170  ? 284  LEU A CD1   1 
ATOM   2223 C  CD2   . LEU A 1 284 ? 20.26200  7.08200   25.93000  1.000 21.07621  ? 284  LEU A CD2   1 
ATOM   2224 N  N     . LEU A 1 285 ? 19.12800  6.11400   20.67000  1.000 14.72282  ? 285  LEU A N     1 
ATOM   2225 C  CA    . LEU A 1 285 ? 18.12800  5.65600   19.71000  1.000 12.71468  ? 285  LEU A CA    1 
ATOM   2226 C  C     . LEU A 1 285 ? 18.21200  4.14500   19.52600  1.000 14.44384  ? 285  LEU A C     1 
ATOM   2227 O  O     . LEU A 1 285 ? 17.19200  3.44900   19.57100  1.000 15.08602  ? 285  LEU A O     1 
ATOM   2228 C  CB    . LEU A 1 285 ? 18.32700  6.37100   18.36400  1.000 14.72019  ? 285  LEU A CB    1 
ATOM   2229 C  CG    . LEU A 1 285 ? 17.87400  7.84200   18.35300  1.000 15.03075  ? 285  LEU A CG    1 
ATOM   2230 C  CD1   . LEU A 1 285 ? 18.52500  8.58500   17.22500  1.000 16.15194  ? 285  LEU A CD1   1 
ATOM   2231 C  CD2   . LEU A 1 285 ? 16.36200  7.96000   18.23700  1.000 15.93349  ? 285  LEU A CD2   1 
ATOM   2232 N  N     . ARG A 1 286 ? 19.42500  3.63300   19.29200  1.000 15.23867  ? 286  ARG A N     1 
ATOM   2233 C  CA    . ARG A 1 286 ? 19.63700  2.19200   19.15600  1.000 14.37541  ? 286  ARG A CA    1 
ATOM   2234 C  C     . ARG A 1 286 ? 19.11400  1.44900   20.37100  1.000 16.05192  ? 286  ARG A C     1 
ATOM   2235 O  O     . ARG A 1 286 ? 18.40300  0.44300   20.24500  1.000 16.20721  ? 286  ARG A O     1 
ATOM   2236 C  CB    . ARG A 1 286 ? 21.12500  1.88900   19.00900  1.000 14.89915  ? 286  ARG A CB    1 
ATOM   2237 C  CG    . ARG A 1 286 ? 21.42200  0.39300   18.91900  1.000 15.84927  ? 286  ARG A CG    1 
ATOM   2238 C  CD    . ARG A 1 286 ? 22.89900  0.06900   19.08000  1.000 16.40197  ? 286  ARG A CD    1 
ATOM   2239 N  NE    . ARG A 1 286 ? 23.35000  0.17900   20.46200  1.000 16.20194  ? 286  ARG A NE    1 
ATOM   2240 C  CZ    . ARG A 1 286 ? 23.36200  -0.82500  21.32900  1.000 18.14691  ? 286  ARG A CZ    1 
ATOM   2241 N  NH1   . ARG A 1 286 ? 22.91700  -2.02800  21.00100  1.000 18.96280  ? 286  ARG A NH1   1 
ATOM   2242 N  NH2   . ARG A 1 286 ? 23.84000  -0.61800  22.55500  1.000 20.31033  ? 286  ARG A NH2   1 
ATOM   2243 N  N     . TYR A 1 287 ? 19.49300  1.92400   21.56000  1.000 14.10959  ? 287  TYR A N     1 
ATOM   2244 C  CA    . TYR A 1 287 ? 19.31100  1.19000   22.80500  1.000 16.09667  ? 287  TYR A CA    1 
ATOM   2245 C  C     . TYR A 1 287 ? 17.86300  1.23000   23.27600  1.000 15.91770  ? 287  TYR A C     1 
ATOM   2246 O  O     . TYR A 1 287 ? 17.37300  0.25700   23.86900  1.000 18.01005  ? 287  TYR A O     1 
ATOM   2247 C  CB    . TYR A 1 287 ? 20.23000  1.81800   23.85700  1.000 16.33091  ? 287  TYR A CB    1 
ATOM   2248 C  CG    . TYR A 1 287 ? 20.58100  0.96000   25.05100  1.000 18.40484  ? 287  TYR A CG    1 
ATOM   2249 C  CD1   . TYR A 1 287 ? 21.27800  -0.23000  24.89900  1.000 22.11844  ? 287  TYR A CD1   1 
ATOM   2250 C  CD2   . TYR A 1 287 ? 20.27100  1.37000   26.33800  1.000 21.80525  ? 287  TYR A CD2   1 
ATOM   2251 C  CE1   . TYR A 1 287 ? 21.62700  -1.00600  26.00000  1.000 23.23173  ? 287  TYR A CE1   1 
ATOM   2252 C  CE2   . TYR A 1 287 ? 20.61600  0.61100   27.43400  1.000 22.93959  ? 287  TYR A CE2   1 
ATOM   2253 C  CZ    . TYR A 1 287 ? 21.29200  -0.57300  27.26500  1.000 24.42661  ? 287  TYR A CZ    1 
ATOM   2254 O  OH    . TYR A 1 287 ? 21.62900  -1.32200  28.39200  1.000 29.03506  ? 287  TYR A OH    1 
ATOM   2255 N  N     . LEU A 1 288 ? 17.16800  2.33900   23.03500  1.000 16.07035  ? 288  LEU A N     1 
ATOM   2256 C  CA    . LEU A 1 288 ? 15.80500  2.49700   23.51600  1.000 15.70978  ? 288  LEU A CA    1 
ATOM   2257 C  C     . LEU A 1 288 ? 14.76100  2.06200   22.50000  1.000 16.05456  ? 288  LEU A C     1 
ATOM   2258 O  O     . LEU A 1 288 ? 13.64100  1.73100   22.90700  1.000 16.97046  ? 288  LEU A O     1 
ATOM   2259 C  CB    . LEU A 1 288 ? 15.54500  3.94900   23.92400  1.000 17.08363  ? 288  LEU A CB    1 
ATOM   2260 C  CG    . LEU A 1 288 ? 16.39100  4.41200   25.11300  1.000 19.10229  ? 288  LEU A CG    1 
ATOM   2261 C  CD1   . LEU A 1 288 ? 16.22300  5.90500   25.38300  1.000 17.66264  ? 288  LEU A CD1   1 
ATOM   2262 C  CD2   . LEU A 1 288 ? 16.09000  3.61000   26.38900  1.000 23.46860  ? 288  LEU A CD2   1 
ATOM   2263 N  N     . ALA A 1 289 ? 15.09900  2.09400   21.19700  1.000 15.61766  ? 289  ALA A N     1 
ATOM   2264 C  CA    . ALA A 1 289 ? 14.28200  1.57900   20.09800  1.000 15.07286  ? 289  ALA A CA    1 
ATOM   2265 C  C     . ALA A 1 289 ? 12.78500  1.62100   20.39400  1.000 15.05180  ? 289  ALA A C     1 
ATOM   2266 O  O     . ALA A 1 289 ? 12.16000  0.58500   20.64600  1.000 18.63118  ? 289  ALA A O     1 
ATOM   2267 C  CB    . ALA A 1 289 ? 14.74800  0.17700   19.70300  1.000 17.92847  ? 289  ALA A CB    1 
ATOM   2268 N  N     . ILE A 1 290 ? 12.20400  2.82300   20.38000  1.000 15.51502  ? 290  ILE A N     1 
ATOM   2269 C  CA    . ILE A 1 290 ? 10.86600  3.00300   20.94100  1.000 16.83097  ? 290  ILE A CA    1 
ATOM   2270 C  C     . ILE A 1 290 ? 9.72100   2.60800   20.01600  1.000 18.22324  ? 290  ILE A C     1 
ATOM   2271 O  O     . ILE A 1 290 ? 8.56300   2.62400   20.45800  1.000 19.45496  ? 290  ILE A O     1 
ATOM   2272 C  CB    . ILE A 1 290 ? 10.67700  4.46900   21.36700  1.000 18.60486  ? 290  ILE A CB    1 
ATOM   2273 C  CG1   . ILE A 1 290 ? 10.85000  5.37700   20.14700  1.000 18.64697  ? 290  ILE A CG1   1 
ATOM   2274 C  CG2   . ILE A 1 290 ? 11.63900  4.82700   22.52200  1.000 19.82343  ? 290  ILE A CG2   1 
ATOM   2275 C  CD1   . ILE A 1 290 ? 10.32300  6.77000   20.33100  1.000 20.31296  ? 290  ILE A CD1   1 
ATOM   2276 N  N     . ALA A 1 291 ? 9.99400   2.25100   18.75800  1.000 18.85226  ? 291  ALA A N     1 
ATOM   2277 C  CA    . ALA A 1 291 ? 8.95900   2.17300   17.73300  1.000 16.39933  ? 291  ALA A CA    1 
ATOM   2278 C  C     . ALA A 1 291 ? 8.85200   0.80000   17.04900  1.000 17.71002  ? 291  ALA A C     1 
ATOM   2279 O  O     . ALA A 1 291 ? 8.62800   0.72200   15.84300  1.000 18.71277  ? 291  ALA A O     1 
ATOM   2280 C  CB    . ALA A 1 291 ? 9.12900   3.29900   16.71100  1.000 17.87056  ? 291  ALA A CB    1 
ATOM   2281 N  N     . ASP A 1 292 ? 8.93900   -0.31000  17.80400  1.000 20.58142  ? 292  ASP A N     1 
ATOM   2282 C  CA    . ASP A 1 292 ? 8.61300   -1.62300  17.22500  1.000 20.91567  ? 292  ASP A CA    1 
ATOM   2283 C  C     . ASP A 1 292 ? 7.19000   -1.67200  16.68300  1.000 19.47076  ? 292  ASP A C     1 
ATOM   2284 O  O     . ASP A 1 292 ? 6.88000   -2.50800  15.81900  1.000 20.07609  ? 292  ASP A O     1 
ATOM   2285 C  CB    . ASP A 1 292 ? 8.71600   -2.74000  18.26100  1.000 20.85513  ? 292  ASP A CB    1 
ATOM   2286 C  CG    . ASP A 1 292 ? 10.13800  -3.09200  18.63900  1.000 22.38689  ? 292  ASP A CG    1 
ATOM   2287 O  OD1   . ASP A 1 292 ? 11.04900  -2.97200  17.78900  1.000 21.66049  ? 292  ASP A OD1   1 
ATOM   2288 O  OD2   . ASP A 1 292 ? 10.34400  -3.53500  19.79300  1.000 22.99749  ? 292  ASP A OD2   1 
ATOM   2289 N  N     . ILE A 1 293 ? 6.29600   -0.83600  17.21700  1.000 20.85250  ? 293  ILE A N     1 
ATOM   2290 C  CA    . ILE A 1 293 ? 4.91100   -0.80100  16.76000  1.000 23.99235  ? 293  ILE A CA    1 
ATOM   2291 C  C     . ILE A 1 293 ? 4.81500   -0.48200  15.26300  1.000 25.13459  ? 293  ILE A C     1 
ATOM   2292 O  O     . ILE A 1 293 ? 3.78600   -0.75900  14.63000  1.000 28.04810  ? 293  ILE A O     1 
ATOM   2293 C  CB    . ILE A 1 293 ? 4.10500   0.17400   17.66500  1.000 26.25841  ? 293  ILE A CB    1 
ATOM   2294 C  CG1   . ILE A 1 293 ? 2.59700   0.04700   17.44200  1.000 33.13818  ? 293  ILE A CG1   1 
ATOM   2295 C  CG2   . ILE A 1 293 ? 4.56100   1.61000   17.46400  1.000 29.21666  ? 293  ILE A CG2   1 
ATOM   2296 C  CD1   . ILE A 1 293 ? 2.03400   -1.25100  17.94900  1.000 34.22252  ? 293  ILE A CD1   1 
ATOM   2297 N  N     . ALA A 1 294 ? 5.88200   0.06000   14.67300  1.000 21.22360  ? 294  ALA A N     1 
ATOM   2298 C  CA    . ALA A 1 294 ? 5.89900   0.47200   13.27800  1.000 24.47136  ? 294  ALA A CA    1 
ATOM   2299 C  C     . ALA A 1 294 ? 6.55900   -0.55500  12.36700  1.000 23.71337  ? 294  ALA A C     1 
ATOM   2300 O  O     . ALA A 1 294 ? 6.82400   -0.25500  11.19800  1.000 28.77713  ? 294  ALA A O     1 
ATOM   2301 C  CB    . ALA A 1 294 ? 6.57900   1.83700   13.14200  1.000 28.21654  ? 294  ALA A CB    1 
ATOM   2302 N  N     . GLY A 1 295 ? 6.81100   -1.76500  12.86000  1.000 18.74698  ? 295  GLY A N     1 
ATOM   2303 C  CA    . GLY A 1 295 ? 7.49400   -2.77500  12.07800  1.000 17.86530  ? 295  GLY A CA    1 
ATOM   2304 C  C     . GLY A 1 295 ? 6.62400   -3.75400  11.31400  1.000 18.26798  ? 295  GLY A C     1 
ATOM   2305 O  O     . GLY A 1 295 ? 7.15700   -4.67200  10.68000  1.000 18.69171  ? 295  GLY A O     1 
ATOM   2306 N  N     . GLY A 1 296 ? 5.30300   -3.59400  11.34600  1.000 18.24956  ? 296  GLY A N     1 
ATOM   2307 C  CA    . GLY A 1 296 ? 4.42000   -4.57400  10.71900  1.000 19.10492  ? 296  GLY A CA    1 
ATOM   2308 C  C     . GLY A 1 296 ? 4.43000   -4.49600  9.19800   1.000 19.58393  ? 296  GLY A C     1 
ATOM   2309 O  O     . GLY A 1 296 ? 4.48400   -3.41500  8.60400   1.000 19.47865  ? 296  GLY A O     1 
ATOM   2310 N  N     . ARG A 1 297 ? 4.35200   -5.67800  8.57600   1.000 18.95754  ? 297  ARG A N     1 
ATOM   2311 C  CA    . ARG A 1 297 ? 4.35900   -5.85800  7.12900   1.000 17.53368  ? 297  ARG A CA    1 
ATOM   2312 C  C     . ARG A 1 297 ? 3.51200   -7.07900  6.79800   1.000 19.64446  ? 297  ARG A C     1 
ATOM   2313 O  O     . ARG A 1 297 ? 3.26800   -7.93400  7.65200   1.000 21.62628  ? 297  ARG A O     1 
ATOM   2314 C  CB    . ARG A 1 297 ? 5.77300   -6.13900  6.60200   1.000 18.01532  ? 297  ARG A CB    1 
ATOM   2315 C  CG    . ARG A 1 297 ? 6.78500   -5.00500  6.78400   1.000 17.20733  ? 297  ARG A CG    1 
ATOM   2316 C  CD    . ARG A 1 297 ? 6.39200   -3.78000  5.97800   1.000 17.96268  ? 297  ARG A CD    1 
ATOM   2317 N  NE    . ARG A 1 297 ? 7.44100   -2.76900  5.96800   1.000 17.98374  ? 297  ARG A NE    1 
ATOM   2318 C  CZ    . ARG A 1 297 ? 7.50000   -1.73400  6.79800   1.000 16.45197  ? 297  ARG A CZ    1 
ATOM   2319 N  NH1   . ARG A 1 297 ? 6.65800   -1.61400  7.81500   1.000 17.55210  ? 297  ARG A NH1   1 
ATOM   2320 N  NH2   . ARG A 1 297 ? 8.40900   -0.78500  6.58800   1.000 17.44683  ? 297  ARG A NH2   1 
ATOM   2321 N  N     . VAL A 1 298 ? 3.08000   -7.18000  5.54300   1.000 19.63393  ? 298  VAL A N     1 
ATOM   2322 C  CA    . VAL A 1 298 ? 2.36200   -8.36400  5.07600   1.000 21.19991  ? 298  VAL A CA    1 
ATOM   2323 C  C     . VAL A 1 298 ? 2.97000   -8.80500  3.75300   1.000 21.15780  ? 298  VAL A C     1 
ATOM   2324 O  O     . VAL A 1 298 ? 3.19100   -7.98100  2.85800   1.000 22.67903  ? 298  VAL A O     1 
ATOM   2325 C  CB    . VAL A 1 298 ? 0.83700   -8.13500  4.95000   1.000 23.98445  ? 298  VAL A CB    1 
ATOM   2326 C  CG1   . VAL A 1 298 ? 0.51800   -7.01800  3.96400   1.000 24.77665  ? 298  VAL A CG1   1 
ATOM   2327 C  CG2   . VAL A 1 298 ? 0.12600   -9.43200  4.55100   1.000 26.51371  ? 298  VAL A CG2   1 
ATOM   2328 N  N     . ALA A 1 299 ? 3.25800   -10.09600 3.63200   1.000 22.90275  ? 299  ALA A N     1 
ATOM   2329 C  CA    . ALA A 1 299 ? 3.86700   -10.60900 2.41300   1.000 22.03422  ? 299  ALA A CA    1 
ATOM   2330 C  C     . ALA A 1 299 ? 2.82700   -10.71400 1.30000   1.000 24.29765  ? 299  ALA A C     1 
ATOM   2331 O  O     . ALA A 1 299 ? 1.72600   -11.23500 1.50900   1.000 25.42147  ? 299  ALA A O     1 
ATOM   2332 C  CB    . ALA A 1 299 ? 4.49100   -11.97900 2.67400   1.000 23.79496  ? 299  ALA A CB    1 
ATOM   2333 N  N     . THR A 1 300 ? 3.16900   -10.20200 0.12000   1.000 23.77390  ? 300  THR A N     1 
ATOM   2334 C  CA    . THR A 1 300 ? 2.32500   -10.35900 -1.06000  1.000 24.81350  ? 300  THR A CA    1 
ATOM   2335 C  C     . THR A 1 300 ? 2.80600   -11.47400 -1.98400  1.000 25.20829  ? 300  THR A C     1 
ATOM   2336 O  O     . THR A 1 300 ? 2.14900   -11.76000 -2.99300  1.000 29.15876  ? 300  THR A O     1 
ATOM   2337 C  CB    . THR A 1 300 ? 2.24100   -9.03900  -1.82900  1.000 25.49779  ? 300  THR A CB    1 
ATOM   2338 O  OG1   . THR A 1 300 ? 3.55800   -8.63600  -2.21900  1.000 25.06616  ? 300  THR A OG1   1 
ATOM   2339 C  CG2   . THR A 1 300 ? 1.62800   -7.95200  -0.95400  1.000 27.66648  ? 300  THR A CG2   1 
ATOM   2340 N  N     . ALA A 1 301 ? 3.93600   -12.09800 -1.65900  1.000 27.61647  ? 301  ALA A N     1 
ATOM   2341 C  CA    . ALA A 1 301 ? 4.50400   -13.20900 -2.40500  1.000 27.88492  ? 301  ALA A CA    1 
ATOM   2342 C  C     . ALA A 1 301 ? 5.41100   -13.96600 -1.44800  1.000 27.78754  ? 301  ALA A C     1 
ATOM   2343 O  O     . ALA A 1 301 ? 5.83800   -13.42500 -0.42400  1.000 27.64016  ? 301  ALA A O     1 
ATOM   2344 C  CB    . ALA A 1 301 ? 5.30900   -12.71800 -3.61200  1.000 29.81147  ? 301  ALA A CB    1 
ATOM   2345 N  N     . ASP A 1 302 ? 5.70100   -15.22300 -1.79200  1.000 28.50868  ? 302  ASP A N     1 
ATOM   2346 C  CA    . ASP A 1 302 ? 6.59900   -16.02400 -0.96900  1.000 28.28234  ? 302  ASP A CA    1 
ATOM   2347 C  C     . ASP A 1 302 ? 7.97700   -15.38000 -0.92300  1.000 28.87715  ? 302  ASP A C     1 
ATOM   2348 O  O     . ASP A 1 302 ? 8.46300   -14.84400 -1.92300  1.000 30.45628  ? 302  ASP A O     1 
ATOM   2349 C  CB    . ASP A 1 302 ? 6.74800   -17.42700 -1.55500  1.000 30.49839  ? 302  ASP A CB    1 
ATOM   2350 C  CG    . ASP A 1 302 ? 5.51200   -18.27700 -1.38400  1.000 34.59889  ? 302  ASP A CG    1 
ATOM   2351 O  OD1   . ASP A 1 302 ? 4.51000   -17.82300 -0.80300  1.000 36.88863  ? 302  ASP A OD1   1 
ATOM   2352 O  OD2   . ASP A 1 302 ? 5.55300   -19.42900 -1.85600  1.000 37.71242  ? 302  ASP A OD2   1 
ATOM   2353 N  N     . ILE A 1 303 ? 8.61300   -15.44800 0.24500   1.000 26.46896  ? 303  ILE A N     1 
ATOM   2354 C  CA    . ILE A 1 303 ? 9.96100   -14.92400 0.45600   1.000 27.51909  ? 303  ILE A CA    1 
ATOM   2355 C  C     . ILE A 1 303 ? 10.75200  -15.98300 1.21100   1.000 27.87439  ? 303  ILE A C     1 
ATOM   2356 O  O     . ILE A 1 303 ? 10.35600  -16.38200 2.31200   1.000 28.70871  ? 303  ILE A O     1 
ATOM   2357 C  CB    . ILE A 1 303 ? 9.94500   -13.61500 1.27000   1.000 26.64793  ? 303  ILE A CB    1 
ATOM   2358 C  CG1   . ILE A 1 303 ? 9.02900   -12.56300 0.63700   1.000 26.48212  ? 303  ILE A CG1   1 
ATOM   2359 C  CG2   . ILE A 1 303 ? 11.36600  -13.06900 1.44800   1.000 27.18484  ? 303  ILE A CG2   1 
ATOM   2360 C  CD1   . ILE A 1 303 ? 8.80000   -11.35900 1.54300   1.000 28.67975  ? 303  ILE A CD1   1 
ATOM   2361 N  N     . GLU A 1 304 ? 11.86700  -16.43000 0.63700   1.000 30.60104  ? 304  GLU A N     1 
ATOM   2362 C  CA    A GLU A 1 304 ? 12.77000  -17.34900 1.31900   0.480 32.38809  ? 304  GLU A CA    1 
ATOM   2363 C  CA    B GLU A 1 304 ? 12.76100  -17.34700 1.33000   0.520 32.15912  ? 304  GLU A CA    1 
ATOM   2364 C  C     . GLU A 1 304 ? 13.80300  -16.54400 2.09900   1.000 33.90407  ? 304  GLU A C     1 
ATOM   2365 O  O     . GLU A 1 304 ? 14.46500  -15.66500 1.53400   1.000 36.28330  ? 304  GLU A O     1 
ATOM   2366 C  CB    A GLU A 1 304 ? 13.48500  -18.25000 0.31100   0.480 34.68574  ? 304  GLU A CB    1 
ATOM   2367 C  CB    B GLU A 1 304 ? 13.44500  -18.29900 0.34800   0.520 34.24621  ? 304  GLU A CB    1 
ATOM   2368 C  CG    A GLU A 1 304 ? 12.57700  -18.89400 -0.71700  0.480 36.26487  ? 304  GLU A CG    1 
ATOM   2369 C  CG    B GLU A 1 304 ? 13.56800  -19.72500 0.86900   0.520 35.46741  ? 304  GLU A CG    1 
ATOM   2370 C  CD    A GLU A 1 304 ? 13.32300  -19.84700 -1.63300  0.480 39.76529  ? 304  GLU A CD    1 
ATOM   2371 C  CD    B GLU A 1 304 ? 15.00200  -20.16200 1.09000   0.520 38.02824  ? 304  GLU A CD    1 
ATOM   2372 O  OE1   A GLU A 1 304 ? 13.55900  -21.00400 -1.22600  0.480 38.94151  ? 304  GLU A OE1   1 
ATOM   2373 O  OE1   B GLU A 1 304 ? 15.68500  -19.56600 1.94800   0.520 40.09165  ? 304  GLU A OE1   1 
ATOM   2374 O  OE2   A GLU A 1 304 ? 13.68500  -19.43600 -2.75600  0.480 42.50246  ? 304  GLU A OE2   1 
ATOM   2375 O  OE2   B GLU A 1 304 ? 15.44700  -21.10500 0.40400   0.520 38.93888  ? 304  GLU A OE2   1 
ATOM   2376 N  N     . VAL A 1 305 ? 13.93800  -16.84500 3.39000   1.000 32.65392  ? 305  VAL A N     1 
ATOM   2377 C  CA    . VAL A 1 305 ? 14.87000  -16.15800 4.28300   1.000 31.88803  ? 305  VAL A CA    1 
ATOM   2378 C  C     . VAL A 1 305 ? 15.71200  -17.22500 4.97300   1.000 33.52770  ? 305  VAL A C     1 
ATOM   2379 O  O     . VAL A 1 305 ? 15.27900  -17.81400 5.96900   1.000 35.11210  ? 305  VAL A O     1 
ATOM   2380 C  CB    . VAL A 1 305 ? 14.15200  -15.28200 5.31700   1.000 34.04619  ? 305  VAL A CB    1 
ATOM   2381 C  CG1   . VAL A 1 305 ? 15.14100  -14.32700 5.96600   1.000 36.73598  ? 305  VAL A CG1   1 
ATOM   2382 C  CG2   . VAL A 1 305 ? 13.01000  -14.52200 4.67800   1.000 34.27779  ? 305  VAL A CG2   1 
ATOM   2383 N  N     . GLU A 1 306 ? 16.91500  -17.46700 4.45900   1.000 36.32014  ? 306  GLU A N     1 
ATOM   2384 C  CA    . GLU A 1 306 ? 17.88800  -18.35900 5.09800   1.000 37.02812  ? 306  GLU A CA    1 
ATOM   2385 C  C     . GLU A 1 306 ? 17.28500  -19.72200 5.44500   1.000 38.42829  ? 306  GLU A C     1 
ATOM   2386 O  O     . GLU A 1 306 ? 17.48400  -20.26000 6.53600   1.000 40.89701  ? 306  GLU A O     1 
ATOM   2387 C  CB    . GLU A 1 306 ? 18.52700  -17.69700 6.32300   1.000 36.34383  ? 306  GLU A CB    1 
ATOM   2388 C  CG    . GLU A 1 306 ? 19.09300  -16.31200 6.04400   1.000 36.56754  ? 306  GLU A CG    1 
ATOM   2389 C  CD    . GLU A 1 306 ? 19.79900  -15.70900 7.24200   1.000 38.72833  ? 306  GLU A CD    1 
ATOM   2390 O  OE1   . GLU A 1 306 ? 20.65000  -16.39800 7.84000   1.000 41.01281  ? 306  GLU A OE1   1 
ATOM   2391 O  OE2   . GLU A 1 306 ? 19.50200  -14.54400 7.58600   1.000 37.49134  ? 306  GLU A OE2   1 
ATOM   2392 N  N     . GLY A 1 307 ? 16.54000  -20.28900 4.50000   1.000 39.50474  ? 307  GLY A N     1 
ATOM   2393 C  CA    . GLY A 1 307 ? 15.90700  -21.57200 4.69700   1.000 41.72079  ? 307  GLY A CA    1 
ATOM   2394 C  C     . GLY A 1 307 ? 14.49800  -21.51800 5.25000   1.000 43.74998  ? 307  GLY A C     1 
ATOM   2395 O  O     . GLY A 1 307 ? 13.74900  -22.48600 5.08500   1.000 47.67677  ? 307  GLY A O     1 
ATOM   2396 N  N     . GLN A 1 308 ? 14.11700  -20.42600 5.90500   1.000 41.47339  ? 308  GLN A N     1 
ATOM   2397 C  CA    . GLN A 1 308 ? 12.75800  -20.25800 6.39200   1.000 40.92596  ? 308  GLN A CA    1 
ATOM   2398 C  C     . GLN A 1 308 ? 11.91400  -19.60200 5.30400   1.000 39.36788  ? 308  GLN A C     1 
ATOM   2399 O  O     . GLN A 1 308 ? 12.40100  -18.77400 4.52800   1.000 39.27313  ? 308  GLN A O     1 
ATOM   2400 C  CB    . GLN A 1 308 ? 12.75300  -19.41300 7.66800   1.000 43.51838  ? 308  GLN A CB    1 
ATOM   2401 C  CG    . GLN A 1 308 ? 13.65900  -19.97100 8.77000   1.000 45.83971  ? 308  GLN A CG    1 
ATOM   2402 C  CD    . GLN A 1 308 ? 13.60700  -19.16300 10.05900  1.000 47.76099  ? 308  GLN A CD    1 
ATOM   2403 O  OE1   . GLN A 1 308 ? 14.33600  -18.18300 10.22200  1.000 48.25842  ? 308  GLN A OE1   1 
ATOM   2404 N  NE2   . GLN A 1 308 ? 12.75100  -19.58000 10.98700  1.000 46.47399  ? 308  GLN A NE2   1 
ATOM   2405 N  N     . LEU A 1 309 ? 10.64200  -19.98300 5.24200   1.000 36.80968  ? 309  LEU A N     1 
ATOM   2406 C  CA    A LEU A 1 309 ? 9.75600   -19.55600 4.16600   0.660 34.20936  ? 309  LEU A CA    1 
ATOM   2407 C  CA    B LEU A 1 309 ? 9.74500   -19.57300 4.16800   0.340 33.45138  ? 309  LEU A CA    1 
ATOM   2408 C  C     . LEU A 1 309 ? 8.65400   -18.67100 4.72700   1.000 32.34072  ? 309  LEU A C     1 
ATOM   2409 O  O     . LEU A 1 309 ? 7.84200   -19.11500 5.54700   1.000 34.81207  ? 309  LEU A O     1 
ATOM   2410 C  CB    A LEU A 1 309 ? 9.15800   -20.75100 3.42300   0.660 35.12000  ? 309  LEU A CB    1 
ATOM   2411 C  CB    B LEU A 1 309 ? 9.10700   -20.80400 3.52700   0.340 31.92488  ? 309  LEU A CB    1 
ATOM   2412 C  CG    A LEU A 1 309 ? 8.16900   -20.41100 2.29900   0.660 34.77522  ? 309  LEU A CG    1 
ATOM   2413 C  CG    B LEU A 1 309 ? 10.06600  -21.84800 2.95700   0.340 29.50617  ? 309  LEU A CG    1 
ATOM   2414 C  CD1   A LEU A 1 309 ? 8.78100   -19.45600 1.27400   0.660 34.54098  ? 309  LEU A CD1   1 
ATOM   2415 C  CD1   B LEU A 1 309 ? 9.39100   -23.20700 2.87700   0.340 31.09583  ? 309  LEU A CD1   1 
ATOM   2416 C  CD2   A LEU A 1 309 ? 7.67000   -21.67700 1.62100   0.660 36.26487  ? 309  LEU A CD2   1 
ATOM   2417 C  CD2   B LEU A 1 309 ? 10.54500  -21.41500 1.58900   0.340 29.53249  ? 309  LEU A CD2   1 
ATOM   2418 N  N     . ILE A 1 310 ? 8.62900   -17.42100 4.28000   1.000 26.67162  ? 310  ILE A N     1 
ATOM   2419 C  CA    . ILE A 1 310 ? 7.49100   -16.54200 4.51000   1.000 25.52148  ? 310  ILE A CA    1 
ATOM   2420 C  C     . ILE A 1 310 ? 6.53900   -16.74100 3.34400   1.000 25.90574  ? 310  ILE A C     1 
ATOM   2421 O  O     . ILE A 1 310 ? 6.91800   -16.54700 2.18200   1.000 27.14273  ? 310  ILE A O     1 
ATOM   2422 C  CB    . ILE A 1 310 ? 7.92500   -15.07400 4.59500   1.000 24.27659  ? 310  ILE A CB    1 
ATOM   2423 C  CG1   . ILE A 1 310 ? 8.82700   -14.84400 5.80200   1.000 24.12131  ? 310  ILE A CG1   1 
ATOM   2424 C  CG2   . ILE A 1 310 ? 6.69700   -14.17800 4.64600   1.000 25.49779  ? 310  ILE A CG2   1 
ATOM   2425 C  CD1   . ILE A 1 310 ? 9.52900   -13.50100 5.76300   1.000 25.35567  ? 310  ILE A CD1   1 
ATOM   2426 N  N     . ARG A 1 311 ? 5.30800   -17.12500 3.64200   1.000 27.69543  ? 311  ARG A N     1 
ATOM   2427 C  CA    . ARG A 1 311 ? 4.34100   -17.39700 2.59300   1.000 30.25100  ? 311  ARG A CA    1 
ATOM   2428 C  C     . ARG A 1 311 ? 3.57800   -16.12400 2.25700   1.000 28.49289  ? 311  ARG A C     1 
ATOM   2429 O  O     . ARG A 1 311 ? 3.39000   -15.25300 3.10600   1.000 27.81912  ? 311  ARG A O     1 
ATOM   2430 C  CB    . ARG A 1 311 ? 3.36300   -18.47700 3.04800   1.000 33.38295  ? 311  ARG A CB    1 
ATOM   2431 C  CG    . ARG A 1 311 ? 4.02100   -19.79900 3.38500   1.000 36.18855  ? 311  ARG A CG    1 
ATOM   2432 C  CD    . ARG A 1 311 ? 3.02600   -20.73200 4.04500   1.000 38.43882  ? 311  ARG A CD    1 
ATOM   2433 N  NE    . ARG A 1 311 ? 1.83400   -20.90400 3.22400   1.000 42.41035  ? 311  ARG A NE    1 
ATOM   2434 C  CZ    . ARG A 1 311 ? 1.66200   -21.88700 2.34900   1.000 45.52388  ? 311  ARG A CZ    1 
ATOM   2435 N  NH1   . ARG A 1 311 ? 2.58300   -22.82200 2.16800   1.000 47.64255  ? 311  ARG A NH1   1 
ATOM   2436 N  NH2   . ARG A 1 311 ? 0.54200   -21.93100 1.63500   1.000 45.90287  ? 311  ARG A NH2   1 
ATOM   2437 N  N     . ALA A 1 312 ? 3.15000   -16.01900 1.00100   1.000 27.41908  ? 312  ALA A N     1 
ATOM   2438 C  CA    . ALA A 1 312 ? 2.28000   -14.92400 0.60300   1.000 28.73766  ? 312  ALA A CA    1 
ATOM   2439 C  C     . ALA A 1 312 ? 1.05700   -14.89100 1.50700   1.000 28.08495  ? 312  ALA A C     1 
ATOM   2440 O  O     . ALA A 1 312 ? 0.40900   -15.91400 1.73500   1.000 30.77737  ? 312  ALA A O     1 
ATOM   2441 C  CB    . ALA A 1 312 ? 1.84300   -15.10800 -0.85000  1.000 27.94546  ? 312  ALA A CB    1 
ATOM   2442 N  N     . GLY A 1 313 ? 0.76500   -13.71500 2.04500   1.000 27.89019  ? 313  GLY A N     1 
ATOM   2443 C  CA    . GLY A 1 313 ? -0.35700  -13.56100 2.94000   1.000 26.42159  ? 313  GLY A CA    1 
ATOM   2444 C  C     . GLY A 1 313 ? -0.03100  -13.68300 4.41000   1.000 28.21917  ? 313  GLY A C     1 
ATOM   2445 O  O     . GLY A 1 313 ? -0.93300  -13.52100 5.24000   1.000 32.05911  ? 313  GLY A O     1 
ATOM   2446 N  N     . GLU A 1 314 ? 1.22000   -13.95500 4.76600   1.000 26.95850  ? 314  GLU A N     1 
ATOM   2447 C  CA    . GLU A 1 314 ? 1.60800   -14.02300 6.16500   1.000 27.04798  ? 314  GLU A CA    1 
ATOM   2448 C  C     . GLU A 1 314 ? 2.04900   -12.66000 6.67200   1.000 26.99534  ? 314  GLU A C     1 
ATOM   2449 O  O     . GLU A 1 314 ? 2.66800   -11.87300 5.95000   1.000 25.91363  ? 314  GLU A O     1 
ATOM   2450 C  CB    . GLU A 1 314 ? 2.74900   -15.01300 6.37400   1.000 26.78742  ? 314  GLU A CB    1 
ATOM   2451 C  CG    . GLU A 1 314 ? 2.33700   -16.45200 6.26500   1.000 28.87715  ? 314  GLU A CG    1 
ATOM   2452 C  CD    . GLU A 1 314 ? 3.36400   -17.37400 6.87600   1.000 30.53261  ? 314  GLU A CD    1 
ATOM   2453 O  OE1   . GLU A 1 314 ? 4.48900   -17.45100 6.34100   1.000 30.54577  ? 314  GLU A OE1   1 
ATOM   2454 O  OE2   . GLU A 1 314 ? 3.05300   -17.99900 7.91000   1.000 33.59087  ? 314  GLU A OE2   1 
ATOM   2455 N  N     . GLY A 1 315 ? 1.74200   -12.40200 7.94100   1.000 25.21355  ? 315  GLY A N     1 
ATOM   2456 C  CA    . GLY A 1 315 ? 2.19700   -11.18000 8.58500   1.000 22.53165  ? 315  GLY A CA    1 
ATOM   2457 C  C     . GLY A 1 315 ? 3.62200   -11.32100 9.10400   1.000 23.84496  ? 315  GLY A C     1 
ATOM   2458 O  O     . GLY A 1 315 ? 4.04100   -12.38200 9.56600   1.000 23.53703  ? 315  GLY A O     1 
ATOM   2459 N  N     . VAL A 1 316 ? 4.37300   -10.22500 9.01400   1.000 20.56036  ? 316  VAL A N     1 
ATOM   2460 C  CA    . VAL A 1 316 ? 5.76700   -10.17700 9.44400   1.000 20.34981  ? 316  VAL A CA    1 
ATOM   2461 C  C     . VAL A 1 316 ? 5.97700   -8.87400  10.19800  1.000 20.28664  ? 316  VAL A C     1 
ATOM   2462 O  O     . VAL A 1 316 ? 5.63700   -7.80300  9.68500   1.000 22.23951  ? 316  VAL A O     1 
ATOM   2463 C  CB    . VAL A 1 316 ? 6.72900   -10.23800 8.23800   1.000 20.80249  ? 316  VAL A CB    1 
ATOM   2464 C  CG1   . VAL A 1 316 ? 8.16700   -10.19100 8.71200   1.000 20.09451  ? 316  VAL A CG1   1 
ATOM   2465 C  CG2   . VAL A 1 316 ? 6.46400   -11.48800 7.37400   1.000 21.98948  ? 316  VAL A CG2   1 
ATOM   2466 N  N     . ILE A 1 317 ? 6.53600   -8.94800  11.40600  1.000 18.12059  ? 317  ILE A N     1 
ATOM   2467 C  CA    . ILE A 1 317 ? 6.86900   -7.74900  12.17300  1.000 18.17850  ? 317  ILE A CA    1 
ATOM   2468 C  C     . ILE A 1 317 ? 8.38200   -7.66500  12.31700  1.000 18.26272  ? 317  ILE A C     1 
ATOM   2469 O  O     . ILE A 1 317 ? 9.01400   -8.56300  12.88900  1.000 18.84963  ? 317  ILE A O     1 
ATOM   2470 C  CB    . ILE A 1 317 ? 6.18200   -7.72200  13.54900  1.000 18.51801  ? 317  ILE A CB    1 
ATOM   2471 C  CG1   . ILE A 1 317 ? 4.66900   -7.87800  13.39800  1.000 20.35770  ? 317  ILE A CG1   1 
ATOM   2472 C  CG2   . ILE A 1 317 ? 6.50500   -6.42400  14.26000  1.000 20.36297  ? 317  ILE A CG2   1 
ATOM   2473 C  CD1   . ILE A 1 317 ? 3.93100   -8.03300  14.71500  1.000 22.26056  ? 317  ILE A CD1   1 
ATOM   2474 N  N     . VAL A 1 318 ? 8.96000   -6.58500  11.80400  1.000 17.55474  ? 318  VAL A N     1 
ATOM   2475 C  CA    . VAL A 1 318 ? 10.38900  -6.33900  11.93500  1.000 16.43618  ? 318  VAL A CA    1 
ATOM   2476 C  C     . VAL A 1 318 ? 10.60000  -5.64400  13.27500  1.000 17.25996  ? 318  VAL A C     1 
ATOM   2477 O  O     . VAL A 1 318 ? 10.25600  -4.46700  13.44500  1.000 18.46274  ? 318  VAL A O     1 
ATOM   2478 C  CB    . VAL A 1 318 ? 10.92900  -5.50000  10.77100  1.000 17.30997  ? 318  VAL A CB    1 
ATOM   2479 C  CG1   . VAL A 1 318 ? 12.43500  -5.37800  10.88400  1.000 19.43128  ? 318  VAL A CG1   1 
ATOM   2480 C  CG2   . VAL A 1 318 ? 10.53800  -6.13700  9.44000   1.000 20.38665  ? 318  VAL A CG2   1 
ATOM   2481 N  N     . VAL A 1 319 ? 11.15600  -6.37700  14.23500  1.000 17.94689  ? 319  VAL A N     1 
ATOM   2482 C  CA    . VAL A 1 319 ? 11.26500  -5.88700  15.61300  1.000 18.40221  ? 319  VAL A CA    1 
ATOM   2483 C  C     . VAL A 1 319 ? 12.62700  -5.21100  15.72800  1.000 18.17850  ? 319  VAL A C     1 
ATOM   2484 O  O     . VAL A 1 319 ? 13.63200  -5.83000  16.09700  1.000 18.43905  ? 319  VAL A O     1 
ATOM   2485 C  CB    . VAL A 1 319 ? 11.07100  -7.00400  16.63400  1.000 18.39168  ? 319  VAL A CB    1 
ATOM   2486 C  CG1   . VAL A 1 319 ? 10.94700  -6.40700  18.01400  1.000 19.78921  ? 319  VAL A CG1   1 
ATOM   2487 C  CG2   . VAL A 1 319 ? 9.83700   -7.84400  16.29000  1.000 20.53930  ? 319  VAL A CG2   1 
ATOM   2488 N  N     . ASN A 1 320 ? 12.65900  -3.90900  15.42700  1.000 15.91243  ? 320  ASN A N     1 
ATOM   2489 C  CA    . ASN A 1 320 ? 13.93000  -3.19900  15.38200  1.000 16.50198  ? 320  ASN A CA    1 
ATOM   2490 C  C     . ASN A 1 320 ? 14.61900  -3.11900  16.74600  1.000 16.96519  ? 320  ASN A C     1 
ATOM   2491 O  O     . ASN A 1 320 ? 15.84500  -2.98900  16.79400  1.000 17.74686  ? 320  ASN A O     1 
ATOM   2492 C  CB    . ASN A 1 320 ? 13.78500  -1.82200  14.72200  1.000 16.25984  ? 320  ASN A CB    1 
ATOM   2493 C  CG    . ASN A 1 320 ? 12.87700  -0.87700  15.49300  1.000 16.50724  ? 320  ASN A CG    1 
ATOM   2494 O  OD1   . ASN A 1 320 ? 13.24900  -0.35600  16.54900  1.000 18.24429  ? 320  ASN A OD1   1 
ATOM   2495 N  ND2   . ASN A 1 320 ? 11.69500  -0.61100  14.93800  1.000 18.85489  ? 320  ASN A ND2   1 
ATOM   2496 N  N     . SER A 1 321 ? 13.87400  -3.21200  17.85400  1.000 17.49947  ? 321  SER A N     1 
ATOM   2497 C  CA    . SER A 1 321 ? 14.53500  -3.19100  19.15300  1.000 18.58381  ? 321  SER A CA    1 
ATOM   2498 C  C     . SER A 1 321 ? 15.40200  -4.42400  19.35300  1.000 16.46776  ? 321  SER A C     1 
ATOM   2499 O  O     . SER A 1 321 ? 16.51900  -4.31800  19.87500  1.000 17.89688  ? 321  SER A O     1 
ATOM   2500 C  CB    . SER A 1 321 ? 13.52000  -3.04700  20.28500  1.000 18.42063  ? 321  SER A CB    1 
ATOM   2501 O  OG    . SER A 1 321 ? 12.70800  -4.20400  20.40600  1.000 19.25757  ? 321  SER A OG    1 
ATOM   2502 N  N     . ILE A 1 322 ? 14.90400  -5.59700  18.93600  1.000 18.30219  ? 322  ILE A N     1 
ATOM   2503 C  CA    . ILE A 1 322 ? 15.67700  -6.83300  19.03300  1.000 18.21008  ? 322  ILE A CA    1 
ATOM   2504 C  C     . ILE A 1 322 ? 16.82200  -6.82500  18.03200  1.000 17.27839  ? 322  ILE A C     1 
ATOM   2505 O  O     . ILE A 1 322 ? 17.95300  -7.21000  18.35500  1.000 19.20493  ? 322  ILE A O     1 
ATOM   2506 C  CB    . ILE A 1 322 ? 14.76200  -8.05300  18.83900  1.000 18.94438  ? 322  ILE A CB    1 
ATOM   2507 C  CG1   . ILE A 1 322 ? 13.70300  -8.12600  19.94700  1.000 19.53129  ? 322  ILE A CG1   1 
ATOM   2508 C  CG2   . ILE A 1 322 ? 15.58200  -9.33500  18.81200  1.000 22.86853  ? 322  ILE A CG2   1 
ATOM   2509 C  CD1   . ILE A 1 322 ? 12.64000  -9.19800  19.71900  1.000 19.90765  ? 322  ILE A CD1   1 
ATOM   2510 N  N     . ALA A 1 323 ? 16.54800  -6.38400  16.79800  1.000 17.55737  ? 323  ALA A N     1 
ATOM   2511 C  CA    . ALA A 1 323 ? 17.60500  -6.28700  15.79500  1.000 18.10480  ? 323  ALA A CA    1 
ATOM   2512 C  C     . ALA A 1 323 ? 18.72200  -5.34900  16.24700  1.000 17.75476  ? 323  ALA A C     1 
ATOM   2513 O  O     . ALA A 1 323 ? 19.89200  -5.56100  15.90500  1.000 17.33892  ? 323  ALA A O     1 
ATOM   2514 C  CB    . ALA A 1 323 ? 17.01900  -5.82700  14.45600  1.000 17.82845  ? 323  ALA A CB    1 
ATOM   2515 N  N     . ASN A 1 324 ? 18.38400  -4.30700  17.01100  1.000 16.65200  ? 324  ASN A N     1 
ATOM   2516 C  CA    . ASN A 1 324 ? 19.37600  -3.36600  17.51300  1.000 16.06245  ? 324  ASN A CA    1 
ATOM   2517 C  C     . ASN A 1 324 ? 20.21600  -3.93000  18.65000  1.000 16.73622  ? 324  ASN A C     1 
ATOM   2518 O  O     . ASN A 1 324 ? 21.16800  -3.27400  19.08100  1.000 18.01005  ? 324  ASN A O     1 
ATOM   2519 C  CB    . ASN A 1 324 ? 18.69100  -2.07400  17.95700  1.000 16.56251  ? 324  ASN A CB    1 
ATOM   2520 C  CG    . ASN A 1 324 ? 18.37300  -1.17100  16.78900  1.000 14.87810  ? 324  ASN A CG    1 
ATOM   2521 O  OD1   . ASN A 1 324 ? 18.85100  -1.41100  15.69400  1.000 17.84951  ? 324  ASN A OD1   1 
ATOM   2522 N  ND2   . ASN A 1 324 ? 17.58500  -0.13200  17.01500  1.000 17.86267  ? 324  ASN A ND2   1 
ATOM   2523 N  N     . ARG A 1 325 ? 19.88800  -5.13200  19.13600  1.000 17.56790  ? 325  ARG A N     1 
ATOM   2524 C  CA    . ARG A 1 325 ? 20.68100  -5.82800  20.13900  1.000 18.21534  ? 325  ARG A CA    1 
ATOM   2525 C  C     . ARG A 1 325 ? 21.39800  -7.03600  19.53200  1.000 19.36811  ? 325  ARG A C     1 
ATOM   2526 O  O     . ARG A 1 325 ? 21.70800  -8.00500  20.23200  1.000 20.71301  ? 325  ARG A O     1 
ATOM   2527 C  CB    . ARG A 1 325 ? 19.81900  -6.24700  21.33300  1.000 19.54971  ? 325  ARG A CB    1 
ATOM   2528 C  CG    . ARG A 1 325 ? 19.01300  -5.12600  21.98700  1.000 20.31296  ? 325  ARG A CG    1 
ATOM   2529 C  CD    . ARG A 1 325 ? 19.91200  -4.02100  22.51400  1.000 20.41034  ? 325  ARG A CD    1 
ATOM   2530 N  NE    . ARG A 1 325 ? 19.17200  -3.03700  23.30300  1.000 20.01293  ? 325  ARG A NE    1 
ATOM   2531 C  CZ    . ARG A 1 325 ? 19.03900  -3.08300  24.62000  1.000 20.78407  ? 325  ARG A CZ    1 
ATOM   2532 N  NH1   . ARG A 1 325 ? 19.59800  -4.04600  25.33500  1.000 22.71325  ? 325  ARG A NH1   1 
ATOM   2533 N  NH2   . ARG A 1 325 ? 18.33900  -2.13200  25.23700  1.000 19.92344  ? 325  ARG A NH2   1 
ATOM   2534 N  N     . ASP A 1 326 ? 21.65200  -6.99400  18.22400  1.000 18.61276  ? 326  ASP A N     1 
ATOM   2535 C  CA    . ASP A 1 326 ? 22.34100  -8.07000  17.52000  1.000 20.01556  ? 326  ASP A CA    1 
ATOM   2536 C  C     . ASP A 1 326 ? 23.83800  -7.92600  17.77200  1.000 19.97871  ? 326  ASP A C     1 
ATOM   2537 O  O     . ASP A 1 326 ? 24.46000  -6.95400  17.32500  1.000 21.28939  ? 326  ASP A O     1 
ATOM   2538 C  CB    . ASP A 1 326 ? 22.02800  -7.96100  16.03100  1.000 19.52076  ? 326  ASP A CB    1 
ATOM   2539 C  CG    . ASP A 1 326 ? 22.54300  -9.14500  15.22300  1.000 20.87092  ? 326  ASP A CG    1 
ATOM   2540 O  OD1   . ASP A 1 326 ? 23.56700  -9.75700  15.61300  1.000 22.24214  ? 326  ASP A OD1   1 
ATOM   2541 O  OD2   . ASP A 1 326 ? 21.92200  -9.44800  14.17100  1.000 20.71038  ? 326  ASP A OD2   1 
ATOM   2542 N  N     . GLY A 1 327 ? 24.41800  -8.88900  18.48600  1.000 21.38151  ? 327  GLY A N     1 
ATOM   2543 C  CA    . GLY A 1 327 ? 25.82400  -8.81800  18.85400  1.000 23.17909  ? 327  GLY A CA    1 
ATOM   2544 C  C     . GLY A 1 327 ? 26.79800  -8.98500  17.70400  1.000 24.44504  ? 327  GLY A C     1 
ATOM   2545 O  O     . GLY A 1 327 ? 27.99200  -8.71000  17.88500  1.000 25.42673  ? 327  GLY A O     1 
ATOM   2546 N  N     . THR A 1 328 ? 26.33200  -9.44800  16.54000  1.000 23.08961  ? 328  THR A N     1 
ATOM   2547 C  CA    . THR A 1 328 ? 27.20600  -9.48300  15.37200  1.000 23.52650  ? 328  THR A CA    1 
ATOM   2548 C  C     . THR A 1 328 ? 27.38700  -8.11200  14.74800  1.000 24.12395  ? 328  THR A C     1 
ATOM   2549 O  O     . THR A 1 328 ? 28.20800  -7.97000  13.83000  1.000 26.29263  ? 328  THR A O     1 
ATOM   2550 C  CB    . THR A 1 328 ? 26.67900  -10.46000 14.31300  1.000 24.86351  ? 328  THR A CB    1 
ATOM   2551 O  OG1   . THR A 1 328 ? 25.46300  -9.95500  13.73900  1.000 25.65308  ? 328  THR A OG1   1 
ATOM   2552 C  CG2   . THR A 1 328 ? 26.42300  -11.83000 14.92600  1.000 27.17957  ? 328  THR A CG2   1 
ATOM   2553 N  N     . VAL A 1 329 ? 26.63500  -7.11900  15.22100  1.000 21.22886  ? 329  VAL A N     1 
ATOM   2554 C  CA    . VAL A 1 329 ? 26.74600  -5.74700  14.75900  1.000 19.85501  ? 329  VAL A CA    1 
ATOM   2555 C  C     . VAL A 1 329 ? 27.22600  -4.82000  15.87000  1.000 19.51813  ? 329  VAL A C     1 
ATOM   2556 O  O     . VAL A 1 329 ? 28.09100  -3.97300  15.64000  1.000 22.63429  ? 329  VAL A O     1 
ATOM   2557 C  CB    . VAL A 1 329 ? 25.41900  -5.24900  14.14400  1.000 19.34442  ? 329  VAL A CB    1 
ATOM   2558 C  CG1   . VAL A 1 329 ? 25.55200  -3.80900  13.67900  1.000 18.81278  ? 329  VAL A CG1   1 
ATOM   2559 C  CG2   . VAL A 1 329 ? 24.98400  -6.16100  12.99600  1.000 22.74220  ? 329  VAL A CG2   1 
ATOM   2560 N  N     . TYR A 1 330 ? 26.69700  -4.98400  17.08600  1.000 19.97608  ? 330  TYR A N     1 
ATOM   2561 C  CA    . TYR A 1 330 ? 27.03100  -4.14200  18.24000  1.000 19.95502  ? 330  TYR A CA    1 
ATOM   2562 C  C     . TYR A 1 330 ? 27.63200  -5.04900  19.30200  1.000 22.12107  ? 330  TYR A C     1 
ATOM   2563 O  O     . TYR A 1 330 ? 26.90400  -5.79100  19.96600  1.000 23.79233  ? 330  TYR A O     1 
ATOM   2564 C  CB    . TYR A 1 330 ? 25.78600  -3.41800  18.75800  1.000 18.68382  ? 330  TYR A CB    1 
ATOM   2565 C  CG    . TYR A 1 330 ? 25.13700  -2.63700  17.64900  1.000 17.54684  ? 330  TYR A CG    1 
ATOM   2566 C  CD1   . TYR A 1 330 ? 25.75400  -1.50300  17.13000  1.000 17.23891  ? 330  TYR A CD1   1 
ATOM   2567 C  CD2   . TYR A 1 330 ? 23.94300  -3.06500  17.07300  1.000 17.59421  ? 330  TYR A CD2   1 
ATOM   2568 C  CE1   . TYR A 1 330 ? 25.19400  -0.80500  16.07400  1.000 18.97596  ? 330  TYR A CE1   1 
ATOM   2569 C  CE2   . TYR A 1 330 ? 23.37000  -2.37100  16.02300  1.000 17.14416  ? 330  TYR A CE2   1 
ATOM   2570 C  CZ    . TYR A 1 330 ? 24.00500  -1.24100  15.52500  1.000 17.81266  ? 330  TYR A CZ    1 
ATOM   2571 O  OH    . TYR A 1 330 ? 23.45600  -0.55500  14.47200  1.000 18.74172  ? 330  TYR A OH    1 
ATOM   2572 N  N     . GLU A 1 331 ? 28.95600  -4.99900  19.45200  1.000 24.50294  ? 331  GLU A N     1 
ATOM   2573 C  CA    . GLU A 1 331 ? 29.61600  -5.84200  20.44000  1.000 26.46370  ? 331  GLU A CA    1 
ATOM   2574 C  C     . GLU A 1 331 ? 29.11700  -5.47500  21.83200  1.000 25.71887  ? 331  GLU A C     1 
ATOM   2575 O  O     . GLU A 1 331 ? 28.98100  -4.29300  22.16300  1.000 25.36094  ? 331  GLU A O     1 
ATOM   2576 C  CB    . GLU A 1 331 ? 31.13200  -5.66200  20.36800  1.000 32.38809  ? 331  GLU A CB    1 
ATOM   2577 C  CG    . GLU A 1 331 ? 31.88200  -6.37900  21.48000  1.000 41.19178  ? 331  GLU A CG    1 
ATOM   2578 C  CD    . GLU A 1 331 ? 33.38400  -6.23300  21.35800  1.000 49.05588  ? 331  GLU A CD    1 
ATOM   2579 O  OE1   . GLU A 1 331 ? 33.92500  -6.54200  20.27400  1.000 50.30077  ? 331  GLU A OE1   1 
ATOM   2580 O  OE2   . GLU A 1 331 ? 34.02200  -5.80200  22.34400  1.000 54.16965  ? 331  GLU A OE2   1 
ATOM   2581 N  N     . ASP A 1 332 ? 28.82500  -6.49900  22.63700  1.000 26.90059  ? 332  ASP A N     1 
ATOM   2582 C  CA    A ASP A 1 332 ? 28.19500  -6.32300  23.94000  0.590 27.76386  ? 332  ASP A CA    1 
ATOM   2583 C  CA    B ASP A 1 332 ? 28.21200  -6.29200  23.94400  0.410 26.30315  ? 332  ASP A CA    1 
ATOM   2584 C  C     . ASP A 1 332 ? 26.92400  -5.49100  23.75700  1.000 26.00312  ? 332  ASP A C     1 
ATOM   2585 O  O     . ASP A 1 332 ? 26.81900  -4.37100  24.26800  1.000 25.65834  ? 332  ASP A O     1 
ATOM   2586 C  CB    A ASP A 1 332 ? 29.14700  -5.69100  24.94600  0.590 31.27480  ? 332  ASP A CB    1 
ATOM   2587 C  CB    B ASP A 1 332 ? 29.20800  -5.55200  24.84100  0.410 26.26631  ? 332  ASP A CB    1 
ATOM   2588 C  CG    A ASP A 1 332 ? 30.37900  -6.54900  25.17800  0.590 35.48320  ? 332  ASP A CG    1 
ATOM   2589 C  CG    B ASP A 1 332 ? 28.75700  -5.45100  26.27600  0.410 27.72174  ? 332  ASP A CG    1 
ATOM   2590 O  OD1   A ASP A 1 332 ? 30.27100  -7.57800  25.88000  0.590 39.43631  ? 332  ASP A OD1   1 
ATOM   2591 O  OD1   B ASP A 1 332 ? 27.82800  -6.18000  26.68200  0.410 28.85609  ? 332  ASP A OD1   1 
ATOM   2592 O  OD2   A ASP A 1 332 ? 31.44800  -6.22500  24.61900  0.590 35.47794  ? 332  ASP A OD2   1 
ATOM   2593 O  OD2   B ASP A 1 332 ? 29.35100  -4.62700  27.00200  0.410 28.74029  ? 332  ASP A OD2   1 
ATOM   2594 N  N     . PRO A 1 333 ? 25.94000  -6.02400  23.02500  1.000 24.32660  ? 333  PRO A N     1 
ATOM   2595 C  CA    . PRO A 1 333 ? 24.81000  -5.19600  22.56700  1.000 22.47112  ? 333  PRO A CA    1 
ATOM   2596 C  C     . PRO A 1 333 ? 23.90600  -4.67300  23.66600  1.000 23.87392  ? 333  PRO A C     1 
ATOM   2597 O  O     . PRO A 1 333 ? 23.21800  -3.66800  23.44100  1.000 24.08183  ? 333  PRO A O     1 
ATOM   2598 C  CB    . PRO A 1 333 ? 24.04400  -6.13700  21.62800  1.000 21.48415  ? 333  PRO A CB    1 
ATOM   2599 C  CG    . PRO A 1 333 ? 24.41300  -7.52600  22.11000  1.000 22.71062  ? 333  PRO A CG    1 
ATOM   2600 C  CD    . PRO A 1 333 ? 25.82700  -7.42700  22.58200  1.000 22.61850  ? 333  PRO A CD    1 
ATOM   2601 N  N     . ASP A 1 334 ? 23.85600  -5.32100  24.82600  1.000 24.70296  ? 334  ASP A N     1 
ATOM   2602 C  CA    . ASP A 1 334 ? 22.98500  -4.86300  25.90000  1.000 26.25578  ? 334  ASP A CA    1 
ATOM   2603 C  C     . ASP A 1 334 ? 23.64700  -3.84000  26.80700  1.000 25.75835  ? 334  ASP A C     1 
ATOM   2604 O  O     . ASP A 1 334 ? 23.04400  -3.43600  27.80600  1.000 29.34826  ? 334  ASP A O     1 
ATOM   2605 C  CB    . ASP A 1 334 ? 22.45700  -6.04800  26.71600  1.000 27.90071  ? 334  ASP A CB    1 
ATOM   2606 C  CG    . ASP A 1 334 ? 21.63100  -7.01000  25.87700  1.000 29.36668  ? 334  ASP A CG    1 
ATOM   2607 O  OD1   . ASP A 1 334 ? 21.06700  -6.57700  24.85000  1.000 24.73718  ? 334  ASP A OD1   1 
ATOM   2608 O  OD2   . ASP A 1 334 ? 21.54100  -8.19700  26.24200  1.000 34.83049  ? 334  ASP A OD2   1 
ATOM   2609 N  N     . ALA A 1 335 ? 24.85800  -3.40200  26.48500  1.000 26.34263  ? 335  ALA A N     1 
ATOM   2610 C  CA    . ALA A 1 335 ? 25.53600  -2.36500  27.24900  1.000 26.66636  ? 335  ALA A CA    1 
ATOM   2611 C  C     . ALA A 1 335 ? 25.30500  -1.01500  26.58600  1.000 25.80573  ? 335  ALA A C     1 
ATOM   2612 O  O     . ALA A 1 335 ? 25.49500  -0.87000  25.37000  1.000 25.57675  ? 335  ALA A O     1 
ATOM   2613 C  CB    . ALA A 1 335 ? 27.03800  -2.63600  27.31700  1.000 29.04822  ? 335  ALA A CB    1 
ATOM   2614 N  N     . LEU A 1 336 ? 24.89800  -0.03100  27.38400  1.000 25.24250  ? 336  LEU A N     1 
ATOM   2615 C  CA    . LEU A 1 336 ? 24.89600  1.34400   26.91200  1.000 23.32911  ? 336  LEU A CA    1 
ATOM   2616 C  C     . LEU A 1 336 ? 26.33500  1.83200   26.84900  1.000 24.24764  ? 336  LEU A C     1 
ATOM   2617 O  O     . LEU A 1 336 ? 27.08600  1.69900   27.82000  1.000 24.85298  ? 336  LEU A O     1 
ATOM   2618 C  CB    . LEU A 1 336 ? 24.08400  2.22900   27.85700  1.000 23.41597  ? 336  LEU A CB    1 
ATOM   2619 C  CG    . LEU A 1 336 ? 23.97700  3.70100   27.45000  1.000 24.81613  ? 336  LEU A CG    1 
ATOM   2620 C  CD1   . LEU A 1 336 ? 22.97800  3.87800   26.32500  1.000 25.76362  ? 336  LEU A CD1   1 
ATOM   2621 C  CD2   . LEU A 1 336 ? 23.56200  4.54900   28.63300  1.000 26.51371  ? 336  LEU A CD2   1 
ATOM   2622 N  N     . ASP A 1 337 ? 26.73600  2.35600   25.68900  1.000 20.53930  ? 337  ASP A N     1 
ATOM   2623 C  CA    . ASP A 1 337 ? 28.08900  2.88500   25.51000  1.000 21.15254  ? 337  ASP A CA    1 
ATOM   2624 C  C     . ASP A 1 337 ? 27.97200  4.08400   24.57900  1.000 21.87894  ? 337  ASP A C     1 
ATOM   2625 O  O     . ASP A 1 337 ? 27.93600  3.92100   23.35600  1.000 23.92655  ? 337  ASP A O     1 
ATOM   2626 C  CB    . ASP A 1 337 ? 29.02100  1.83300   24.92000  1.000 21.49731  ? 337  ASP A CB    1 
ATOM   2627 C  CG    . ASP A 1 337 ? 30.44800  2.34300   24.74800  1.000 25.97943  ? 337  ASP A CG    1 
ATOM   2628 O  OD1   . ASP A 1 337 ? 30.70800  3.52200   25.07000  1.000 27.74280  ? 337  ASP A OD1   1 
ATOM   2629 O  OD2   . ASP A 1 337 ? 31.31900  1.56500   24.30100  1.000 26.75584  ? 337  ASP A OD2   1 
ATOM   2630 N  N     . ILE A 1 338 ? 27.91800  5.28800   25.15300  1.000 23.18699  ? 338  ILE A N     1 
ATOM   2631 C  CA    . ILE A 1 338 ? 27.78700  6.47900   24.32300  1.000 23.77917  ? 338  ILE A CA    1 
ATOM   2632 C  C     . ILE A 1 338 ? 29.00000  6.71000   23.43800  1.000 24.96615  ? 338  ILE A C     1 
ATOM   2633 O  O     . ILE A 1 338 ? 28.94300  7.55100   22.53200  1.000 27.10325  ? 338  ILE A O     1 
ATOM   2634 C  CB    . ILE A 1 338 ? 27.46900  7.72400   25.17300  1.000 26.11629  ? 338  ILE A CB    1 
ATOM   2635 C  CG1   . ILE A 1 338 ? 28.60600  7.98400   26.16400  1.000 27.80333  ? 338  ILE A CG1   1 
ATOM   2636 C  CG2   . ILE A 1 338 ? 26.14300  7.54100   25.89300  1.000 25.77414  ? 338  ILE A CG2   1 
ATOM   2637 C  CD1   . ILE A 1 338 ? 28.60100  9.37000   26.77100  1.000 31.19321  ? 338  ILE A CD1   1 
ATOM   2638 N  N     . HIS A 1 339 ? 30.10200  5.99600   23.67900  1.000 24.38977  ? 339  HIS A N     1 
ATOM   2639 C  CA    . HIS A 1 339 ? 31.29200  6.10800   22.84800  1.000 26.85322  ? 339  HIS A CA    1 
ATOM   2640 C  C     . HIS A 1 339 ? 31.31900  5.11500   21.69700  1.000 26.75847  ? 339  HIS A C     1 
ATOM   2641 O  O     . HIS A 1 339 ? 32.18600  5.23900   20.82600  1.000 29.96938  ? 339  HIS A O     1 
ATOM   2642 C  CB    . HIS A 1 339 ? 32.55700  5.89900   23.68600  1.000 29.25088  ? 339  HIS A CB    1 
ATOM   2643 C  CG    . HIS A 1 339 ? 32.67700  6.83200   24.84600  1.000 32.34335  ? 339  HIS A CG    1 
ATOM   2644 N  ND1   . HIS A 1 339 ? 33.23000  8.08900   24.73400  1.000 34.04092  ? 339  HIS A ND1   1 
ATOM   2645 C  CD2   . HIS A 1 339 ? 32.32400  6.68800   26.14500  1.000 34.32517  ? 339  HIS A CD2   1 
ATOM   2646 C  CE1   . HIS A 1 339 ? 33.21200  8.67900   25.91600  1.000 34.92524  ? 339  HIS A CE1   1 
ATOM   2647 N  NE2   . HIS A 1 339 ? 32.66600  7.85100   26.78900  1.000 36.08327  ? 339  HIS A NE2   1 
ATOM   2648 N  N     . ARG A 1 340 ? 30.41100  4.13700   21.67100  1.000 24.26344  ? 340  ARG A N     1 
ATOM   2649 C  CA    . ARG A 1 340 ? 30.43600  3.14300   20.60600  1.000 24.17395  ? 340  ARG A CA    1 
ATOM   2650 C  C     . ARG A 1 340 ? 29.95900  3.75500   19.29000  1.000 25.92942  ? 340  ARG A C     1 
ATOM   2651 O  O     . ARG A 1 340 ? 29.35700  4.83100   19.24600  1.000 26.61635  ? 340  ARG A O     1 
ATOM   2652 C  CB    . ARG A 1 340 ? 29.53800  1.95100   20.94900  1.000 23.37122  ? 340  ARG A CB    1 
ATOM   2653 C  CG    . ARG A 1 340 ? 28.07300  2.16400   20.59900  1.000 22.85011  ? 340  ARG A CG    1 
ATOM   2654 C  CD    . ARG A 1 340 ? 27.27700  0.86000   20.52000  1.000 22.05001  ? 340  ARG A CD    1 
ATOM   2655 N  NE    . ARG A 1 340 ? 27.14500  0.18500   21.81100  1.000 22.00790  ? 340  ARG A NE    1 
ATOM   2656 C  CZ    . ARG A 1 340 ? 27.58400  -1.04400  22.05500  1.000 21.84736  ? 340  ARG A CZ    1 
ATOM   2657 N  NH1   . ARG A 1 340 ? 28.22300  -1.74000  21.12900  1.000 23.29490  ? 340  ARG A NH1   1 
ATOM   2658 N  NH2   . ARG A 1 340 ? 27.35900  -1.59200  23.25100  1.000 22.97907  ? 340  ARG A NH2   1 
ATOM   2659 N  N     . SER A 1 341 ? 30.23500  3.04800   18.19800  1.000 28.05863  ? 341  SER A N     1 
ATOM   2660 C  CA    . SER A 1 341 ? 29.59000  3.35100   16.92800  1.000 30.55366  ? 341  SER A CA    1 
ATOM   2661 C  C     . SER A 1 341 ? 28.22300  2.68800   16.93400  1.000 26.80058  ? 341  SER A C     1 
ATOM   2662 O  O     . SER A 1 341 ? 28.12400  1.45800   16.92300  1.000 28.24812  ? 341  SER A O     1 
ATOM   2663 C  CB    . SER A 1 341 ? 30.41500  2.82000   15.76400  1.000 33.38032  ? 341  SER A CB    1 
ATOM   2664 O  OG    . SER A 1 341 ? 29.67000  2.91500   14.56300  1.000 39.17049  ? 341  SER A OG    1 
ATOM   2665 N  N     . ALA A 1 342 ? 27.16800  3.49700   16.99600  1.000 23.35280  ? 342  ALA A N     1 
ATOM   2666 C  CA    . ALA A 1 342 ? 25.80600  3.00800   16.87200  1.000 20.33928  ? 342  ALA A CA    1 
ATOM   2667 C  C     . ALA A 1 342 ? 25.28500  3.16500   15.45100  1.000 18.37589  ? 342  ALA A C     1 
ATOM   2668 O  O     . ALA A 1 342 ? 24.07100  3.07200   15.21800  1.000 19.49707  ? 342  ALA A O     1 
ATOM   2669 C  CB    . ALA A 1 342 ? 24.89300  3.70100   17.88600  1.000 20.82092  ? 342  ALA A CB    1 
ATOM   2670 N  N     . ARG A 1 343 ? 26.18700  3.40000   14.49900  1.000 20.51825  ? 343  ARG A N     1 
ATOM   2671 C  CA    A ARG A 1 343 ? 25.84100  3.48700   13.08400  0.400 20.18926  ? 343  ARG A CA    1 
ATOM   2672 C  CA    B ARG A 1 343 ? 25.72500  3.54000   13.13600  0.600 22.31847  ? 343  ARG A CA    1 
ATOM   2673 C  C     . ARG A 1 343 ? 25.08600  2.24100   12.64500  1.000 17.43367  ? 343  ARG A C     1 
ATOM   2674 O  O     . ARG A 1 343 ? 25.28100  1.15000   13.19300  1.000 19.07334  ? 343  ARG A O     1 
ATOM   2675 C  CB    A ARG A 1 343 ? 27.11300  3.55500   12.23300  0.400 19.31547  ? 343  ARG A CB    1 
ATOM   2676 C  CB    B ARG A 1 343 ? 26.84100  4.07300   12.23900  0.600 25.04774  ? 343  ARG A CB    1 
ATOM   2677 C  CG    A ARG A 1 343 ? 28.05000  4.70800   12.52900  0.400 19.44707  ? 343  ARG A CG    1 
ATOM   2678 C  CG    B ARG A 1 343 ? 27.20200  5.51600   12.60500  0.600 25.20565  ? 343  ARG A CG    1 
ATOM   2679 C  CD    A ARG A 1 343 ? 29.18700  4.75300   11.51400  0.400 18.33641  ? 343  ARG A CD    1 
ATOM   2680 C  CD    B ARG A 1 343 ? 28.33700  6.08500   11.77700  0.600 26.37421  ? 343  ARG A CD    1 
ATOM   2681 N  NE    A ARG A 1 343 ? 28.68200  4.90100   10.15600  0.400 20.19716  ? 343  ARG A NE    1 
ATOM   2682 N  NE    B ARG A 1 343 ? 27.89600  6.45700   10.43900  0.600 25.96101  ? 343  ARG A NE    1 
ATOM   2683 C  CZ    A ARG A 1 343 ? 28.26300  6.04700   9.63700   0.400 18.85752  ? 343  ARG A CZ    1 
ATOM   2684 C  CZ    B ARG A 1 343 ? 28.07700  5.71100   9.35800   0.600 27.51119  ? 343  ARG A CZ    1 
ATOM   2685 N  NH1   A ARG A 1 343 ? 28.28500  7.17100   10.33600  0.400 19.16282  ? 343  ARG A NH1   1 
ATOM   2686 N  NH1   B ARG A 1 343 ? 28.72300  4.55700   9.41600   0.600 29.33773  ? 343  ARG A NH1   1 
ATOM   2687 N  NH2   A ARG A 1 343 ? 27.81200  6.06700   8.38700   0.400 21.13938  ? 343  ARG A NH2   1 
ATOM   2688 N  NH2   B ARG A 1 343 ? 27.60400  6.13600   8.19100   0.600 29.78252  ? 343  ARG A NH2   1 
ATOM   2689 N  N     . HIS A 1 344 ? 24.24100  2.39700   11.63200  1.000 16.21773  ? 344  HIS A N     1 
ATOM   2690 C  CA    . HIS A 1 344 ? 23.48200  1.31700   11.01200  1.000 15.74399  ? 344  HIS A CA    1 
ATOM   2691 C  C     . HIS A 1 344 ? 22.32900  0.82400   11.87800  1.000 15.75715  ? 344  HIS A C     1 
ATOM   2692 O  O     . HIS A 1 344 ? 21.70000  -0.17900  11.54100  1.000 15.88875  ? 344  HIS A O     1 
ATOM   2693 C  CB    . HIS A 1 344 ? 24.35900  0.14100   10.55900  1.000 18.12849  ? 344  HIS A CB    1 
ATOM   2694 C  CG    . HIS A 1 344 ? 25.69200  0.55800   10.01900  1.000 22.11055  ? 344  HIS A CG    1 
ATOM   2695 N  ND1   . HIS A 1 344 ? 25.82800  1.45300   8.98100   1.000 25.42673  ? 344  HIS A ND1   1 
ATOM   2696 C  CD2   . HIS A 1 344 ? 26.95000  0.23000   10.40100  1.000 25.93469  ? 344  HIS A CD2   1 
ATOM   2697 C  CE1   . HIS A 1 344 ? 27.11200  1.63400   8.72400   1.000 27.07167  ? 344  HIS A CE1   1 
ATOM   2698 N  NE2   . HIS A 1 344 ? 27.81500  0.91400   9.58100   1.000 27.04008  ? 344  HIS A NE2   1 
ATOM   2699 N  N     . HIS A 1 345 ? 22.01500  1.49900   12.97900  1.000 14.19907  ? 345  HIS A N     1 
ATOM   2700 C  CA    . HIS A 1 345 ? 20.90900  1.02000   13.79200  1.000 13.55426  ? 345  HIS A CA    1 
ATOM   2701 C  C     . HIS A 1 345 ? 19.58300  1.16800   13.04500  1.000 13.32791  ? 345  HIS A C     1 
ATOM   2702 O  O     . HIS A 1 345 ? 19.46700  1.90900   12.05100  1.000 14.49384  ? 345  HIS A O     1 
ATOM   2703 C  CB    . HIS A 1 345 ? 20.85400  1.72800   15.15100  1.000 14.48332  ? 345  HIS A CB    1 
ATOM   2704 C  CG    . HIS A 1 345 ? 20.42800  3.15900   15.06700  1.000 15.63082  ? 345  HIS A CG    1 
ATOM   2705 N  ND1   . HIS A 1 345 ? 19.11300  3.54200   14.89600  1.000 15.40711  ? 345  HIS A ND1   1 
ATOM   2706 C  CD2   . HIS A 1 345 ? 21.14900  4.30400   15.13600  1.000 17.07573  ? 345  HIS A CD2   1 
ATOM   2707 C  CE1   . HIS A 1 345 ? 19.04500  4.86100   14.84900  1.000 15.47817  ? 345  HIS A CE1   1 
ATOM   2708 N  NE2   . HIS A 1 345 ? 20.26600  5.34700   14.99500  1.000 15.59397  ? 345  HIS A NE2   1 
ATOM   2709 N  N     . LEU A 1 346 ? 18.58400  0.42300   13.53000  1.000 13.36476  ? 346  LEU A N     1 
ATOM   2710 C  CA    . LEU A 1 346 ? 17.27300  0.30700   12.90100  1.000 13.03577  ? 346  LEU A CA    1 
ATOM   2711 C  C     . LEU A 1 346 ? 16.17200  1.04000   13.65400  1.000 13.07262  ? 346  LEU A C     1 
ATOM   2712 O  O     . LEU A 1 346 ? 14.99000  0.81900   13.36200  1.000 14.67018  ? 346  LEU A O     1 
ATOM   2713 C  CB    . LEU A 1 346 ? 16.90500  -1.16900  12.72200  1.000 14.83599  ? 346  LEU A CB    1 
ATOM   2714 C  CG    . LEU A 1 346 ? 17.69400  -1.85500  11.60300  1.000 16.82570  ? 346  LEU A CG    1 
ATOM   2715 C  CD1   . LEU A 1 346 ? 17.68000  -3.35100  11.76900  1.000 18.72593  ? 346  LEU A CD1   1 
ATOM   2716 C  CD2   . LEU A 1 346 ? 17.08600  -1.44900  10.25500  1.000 18.06269  ? 346  LEU A CD2   1 
ATOM   2717 N  N     . ALA A 1 347 ? 16.51800  1.93500   14.59200  1.000 13.50688  ? 347  ALA A N     1 
ATOM   2718 C  CA    . ALA A 1 347 ? 15.47300  2.60600   15.36700  1.000 13.97010  ? 347  ALA A CA    1 
ATOM   2719 C  C     . ALA A 1 347 ? 14.54900  3.44500   14.49300  1.000 14.55964  ? 347  ALA A C     1 
ATOM   2720 O  O     . ALA A 1 347 ? 13.39100  3.68100   14.87300  1.000 14.74650  ? 347  ALA A O     1 
ATOM   2721 C  CB    . ALA A 1 347 ? 16.08300  3.48000   16.46300  1.000 15.60187  ? 347  ALA A CB    1 
ATOM   2722 N  N     . PHE A 1 348 ? 15.04300  3.91900   13.34000  1.000 14.37014  ? 348  PHE A N     1 
ATOM   2723 C  CA    . PHE A 1 348 ? 14.26300  4.69100   12.37800  1.000 13.12526  ? 348  PHE A CA    1 
ATOM   2724 C  C     . PHE A 1 348 ? 13.78200  3.85200   11.19900  1.000 13.79639  ? 348  PHE A C     1 
ATOM   2725 O  O     . PHE A 1 348 ? 13.26400  4.41200   10.21800  1.000 15.05444  ? 348  PHE A O     1 
ATOM   2726 C  CB    . PHE A 1 348 ? 15.08500  5.86100   11.81800  1.000 13.32528  ? 348  PHE A CB    1 
ATOM   2727 C  CG    . PHE A 1 348 ? 15.41100  6.95500   12.82400  1.000 14.18328  ? 348  PHE A CG    1 
ATOM   2728 C  CD1   . PHE A 1 348 ? 14.40700  7.68400   13.44900  1.000 15.70451  ? 348  PHE A CD1   1 
ATOM   2729 C  CD2   . PHE A 1 348 ? 16.73400  7.28300   13.09400  1.000 14.39120  ? 348  PHE A CD2   1 
ATOM   2730 C  CE1   . PHE A 1 348 ? 14.71400  8.71800   14.34300  1.000 15.25709  ? 348  PHE A CE1   1 
ATOM   2731 C  CE2   . PHE A 1 348 ? 17.06000  8.30600   13.98400  1.000 15.07549  ? 348  PHE A CE2   1 
ATOM   2732 C  CZ    . PHE A 1 348 ? 16.04400  9.03000   14.60900  1.000 15.33868  ? 348  PHE A CZ    1 
ATOM   2733 N  N     . GLY A 1 349 ? 13.94400  2.53100   11.25300  1.000 14.30435  ? 349  GLY A N     1 
ATOM   2734 C  CA    . GLY A 1 349 ? 13.65300  1.71200   10.08300  1.000 16.15457  ? 349  GLY A CA    1 
ATOM   2735 C  C     . GLY A 1 349 ? 14.77500  1.73700   9.05100   1.000 14.24644  ? 349  GLY A C     1 
ATOM   2736 O  O     . GLY A 1 349 ? 15.92000  2.09700   9.34300   1.000 15.98350  ? 349  GLY A O     1 
ATOM   2737 N  N     . PHE A 1 350 ? 14.42800  1.33800   7.82200   1.000 15.08339  ? 350  PHE A N     1 
ATOM   2738 C  CA    . PHE A 1 350 ? 15.39200  1.20600   6.73600   1.000 17.30207  ? 350  PHE A CA    1 
ATOM   2739 C  C     . PHE A 1 350 ? 14.60900  1.14300   5.43500   1.000 17.45472  ? 350  PHE A C     1 
ATOM   2740 O  O     . PHE A 1 350 ? 13.53500  0.54900   5.39500   1.000 19.19967  ? 350  PHE A O     1 
ATOM   2741 C  CB    . PHE A 1 350 ? 16.21000  -0.09500  6.86100   1.000 17.74950  ? 350  PHE A CB    1 
ATOM   2742 C  CG    . PHE A 1 350 ? 17.07400  -0.38700  5.65700   1.000 18.31009  ? 350  PHE A CG    1 
ATOM   2743 C  CD1   . PHE A 1 350 ? 18.34200  0.15900   5.54700   1.000 18.69435  ? 350  PHE A CD1   1 
ATOM   2744 C  CD2   . PHE A 1 350 ? 16.60900  -1.20200  4.62400   1.000 20.40771  ? 350  PHE A CD2   1 
ATOM   2745 C  CE1   . PHE A 1 350 ? 19.13500  -0.09800  4.43500   1.000 21.47363  ? 350  PHE A CE1   1 
ATOM   2746 C  CE2   . PHE A 1 350 ? 17.39900  -1.45700  3.50600   1.000 20.69722  ? 350  PHE A CE2   1 
ATOM   2747 C  CZ    . PHE A 1 350 ? 18.65900  -0.90200  3.41300   1.000 20.11294  ? 350  PHE A CZ    1 
ATOM   2748 N  N     . GLY A 1 351 ? 15.15100  1.74200   4.37500   1.000 18.59170  ? 351  GLY A N     1 
ATOM   2749 C  CA    . GLY A 1 351 ? 14.50700  1.61600   3.07900   1.000 19.27336  ? 351  GLY A CA    1 
ATOM   2750 C  C     . GLY A 1 351 ? 13.55200  2.74500   2.75400   1.000 19.30495  ? 351  GLY A C     1 
ATOM   2751 O  O     . GLY A 1 351 ? 13.72600  3.86700   3.24100   1.000 19.96818  ? 351  GLY A O     1 
ATOM   2752 N  N     . VAL A 1 352 ? 12.52000  2.46600   1.95400   1.000 20.48667  ? 352  VAL A N     1 
ATOM   2753 C  CA    . VAL A 1 352 ? 11.71000  3.56100   1.42300   1.000 20.74459  ? 352  VAL A CA    1 
ATOM   2754 C  C     . VAL A 1 352 ? 10.87700  4.23700   2.50700   1.000 19.71552  ? 352  VAL A C     1 
ATOM   2755 O  O     . VAL A 1 352 ? 10.52600  5.42000   2.37300   1.000 19.36811  ? 352  VAL A O     1 
ATOM   2756 C  CB    . VAL A 1 352 ? 10.86200  3.12200   0.21300   1.000 23.04224  ? 352  VAL A CB    1 
ATOM   2757 C  CG1   . VAL A 1 352 ? 11.74500  2.61300   -0.92500  1.000 23.75548  ? 352  VAL A CG1   1 
ATOM   2758 C  CG2   . VAL A 1 352 ? 9.83200   2.07800   0.62100   1.000 23.69231  ? 352  VAL A CG2   1 
ATOM   2759 N  N     . HIS A 1 353 ? 10.55000  3.52500   3.58800   1.000 16.85728  ? 353  HIS A N     1 
ATOM   2760 C  CA    . HIS A 1 353 ? 9.76500   4.09900   4.67500   1.000 17.29155  ? 353  HIS A CA    1 
ATOM   2761 C  C     . HIS A 1 353 ? 10.62000  4.60700   5.82100   1.000 16.69937  ? 353  HIS A C     1 
ATOM   2762 O  O     . HIS A 1 353 ? 10.06200  4.97200   6.86600   1.000 17.88636  ? 353  HIS A O     1 
ATOM   2763 C  CB    . HIS A 1 353 ? 8.75400   3.09100   5.23500   1.000 17.62053  ? 353  HIS A CB    1 
ATOM   2764 C  CG    . HIS A 1 353 ? 7.63500   2.75800   4.29900   1.000 17.77055  ? 353  HIS A CG    1 
ATOM   2765 N  ND1   . HIS A 1 353 ? 6.48000   3.50600   4.21400   1.000 19.17335  ? 353  HIS A ND1   1 
ATOM   2766 C  CD2   . HIS A 1 353 ? 7.48700   1.73900   3.41900   1.000 18.32851  ? 353  HIS A CD2   1 
ATOM   2767 C  CE1   . HIS A 1 353 ? 5.67100   2.96400   3.32000   1.000 19.18651  ? 353  HIS A CE1   1 
ATOM   2768 N  NE2   . HIS A 1 353 ? 6.26100   1.89400   2.82000   1.000 19.32074  ? 353  HIS A NE2   1 
ATOM   2769 N  N     . GLN A 1 354 ? 11.94400  4.64500   5.66600   1.000 16.46513  ? 354  GLN A N     1 
ATOM   2770 C  CA    A GLN A 1 354 ? 12.79700  5.11200   6.75400   0.560 14.75177  ? 354  GLN A CA    1 
ATOM   2771 C  CA    B GLN A 1 354 ? 12.78400  5.10500   6.76800   0.440 15.55713  ? 354  GLN A CA    1 
ATOM   2772 C  C     . GLN A 1 354 ? 12.33100  6.48000   7.24300   1.000 14.43857  ? 354  GLN A C     1 
ATOM   2773 O  O     . GLN A 1 354 ? 12.00000  7.36200   6.44300   1.000 16.83360  ? 354  GLN A O     1 
ATOM   2774 C  CB    A GLN A 1 354 ? 14.24700  5.18600   6.28300   0.560 14.08590  ? 354  GLN A CB    1 
ATOM   2775 C  CB    B GLN A 1 354 ? 14.27000  5.13100   6.39700   0.440 16.69674  ? 354  GLN A CB    1 
ATOM   2776 C  CG    A GLN A 1 354 ? 15.25700  5.45600   7.38900   0.560 13.64111  ? 354  GLN A CG    1 
ATOM   2777 C  CG    B GLN A 1 354 ? 15.15800  5.57800   7.57500   0.440 17.59685  ? 354  GLN A CG    1 
ATOM   2778 C  CD    A GLN A 1 354 ? 16.67200  5.28000   6.89400   0.560 12.85680  ? 354  GLN A CD    1 
ATOM   2779 C  CD    B GLN A 1 354 ? 16.62300  5.23800   7.38500   0.440 19.96292  ? 354  GLN A CD    1 
ATOM   2780 O  OE1   A GLN A 1 354 ? 17.14400  4.15500   6.71300   0.560 12.65152  ? 354  GLN A OE1   1 
ATOM   2781 O  OE1   B GLN A 1 354 ? 17.48400  5.69900   8.14400   0.440 21.37362  ? 354  GLN A OE1   1 
ATOM   2782 N  NE2   A GLN A 1 354 ? 17.35300  6.38600   6.64300   0.560 13.72270  ? 354  GLN A NE2   1 
ATOM   2783 N  NE2   B GLN A 1 354 ? 16.91600  4.41500   6.38400   0.440 20.67616  ? 354  GLN A NE2   1 
ATOM   2784 N  N     . CYS A 1 355 ? 12.31200  6.64700   8.56600   1.000 14.09643  ? 355  CYS A N     1 
ATOM   2785 C  CA    . CYS A 1 355 ? 11.72800  7.80500   9.23700   1.000 15.10444  ? 355  CYS A CA    1 
ATOM   2786 C  C     . CYS A 1 355 ? 11.95200  9.11900   8.49600   1.000 15.52028  ? 355  CYS A C     1 
ATOM   2787 O  O     . CYS A 1 355 ? 13.08600  9.57700   8.33400   1.000 15.19656  ? 355  CYS A O     1 
ATOM   2788 C  CB    . CYS A 1 355 ? 12.31300  7.91200   10.63900  1.000 16.69674  ? 355  CYS A CB    1 
ATOM   2789 S  SG    . CYS A 1 355 ? 11.68200  9.31600   11.54800  1.000 15.74926  ? 355  CYS A SG    1 
ATOM   2790 N  N     . LEU A 1 356 ? 10.84500  9.74800   8.10400   1.000 16.51514  ? 356  LEU A N     1 
ATOM   2791 C  CA    . LEU A 1 356 ? 10.89500  11.05100  7.45500   1.000 17.38893  ? 356  LEU A CA    1 
ATOM   2792 C  C     . LEU A 1 356 ? 11.50200  12.10700  8.36800   1.000 16.10193  ? 356  LEU A C     1 
ATOM   2793 O  O     . LEU A 1 356 ? 12.19000  13.02800  7.90300   1.000 16.62831  ? 356  LEU A O     1 
ATOM   2794 C  CB    . LEU A 1 356 ? 9.47600   11.47200  7.07600   1.000 20.67090  ? 356  LEU A CB    1 
ATOM   2795 C  CG    . LEU A 1 356 ? 9.35100   12.85500  6.44200   1.000 21.76050  ? 356  LEU A CG    1 
ATOM   2796 C  CD1   . LEU A 1 356 ? 9.99400   12.87700  5.05400   1.000 29.50091  ? 356  LEU A CD1   1 
ATOM   2797 C  CD2   . LEU A 1 356 ? 7.88800   13.27100  6.39800   1.000 23.67915  ? 356  LEU A CD2   1 
ATOM   2798 N  N     . GLY A 1 357 ? 11.21800  12.02600  9.66200   1.000 14.47279  ? 357  GLY A N     1 
ATOM   2799 C  CA    . GLY A 1 357 ? 11.60900  13.06800  10.58400  1.000 15.35447  ? 357  GLY A CA    1 
ATOM   2800 C  C     . GLY A 1 357 ? 12.91600  12.83900  11.30000  1.000 14.42015  ? 357  GLY A C     1 
ATOM   2801 O  O     . GLY A 1 357 ? 13.21000  13.57800  12.24500  1.000 16.08614  ? 357  GLY A O     1 
ATOM   2802 N  N     . GLN A 1 358 ? 13.72300  11.86000  10.87200  1.000 14.38594  ? 358  GLN A N     1 
ATOM   2803 C  CA    . GLN A 1 358 ? 14.84700  11.40900  11.69100  1.000 13.19369  ? 358  GLN A CA    1 
ATOM   2804 C  C     . GLN A 1 358 ? 15.82700  12.53600  11.98200  1.000 15.46238  ? 358  GLN A C     1 
ATOM   2805 O  O     . GLN A 1 358 ? 16.35700  12.62600  13.09800  1.000 18.04427  ? 358  GLN A O     1 
ATOM   2806 C  CB    . GLN A 1 358 ? 15.53300  10.19200  11.06200  1.000 15.39658  ? 358  GLN A CB    1 
ATOM   2807 C  CG    . GLN A 1 358 ? 16.05900  10.44600  9.65800   1.000 15.35974  ? 358  GLN A CG    1 
ATOM   2808 C  CD    . GLN A 1 358 ? 16.65700  9.20100   8.99700   1.000 17.14679  ? 358  GLN A CD    1 
ATOM   2809 O  OE1   . GLN A 1 358 ? 16.60500  9.06000   7.78200   1.000 22.01843  ? 358  GLN A OE1   1 
ATOM   2810 N  NE2   . GLN A 1 358 ? 17.23400  8.31300   9.79000   1.000 20.16558  ? 358  GLN A NE2   1 
ATOM   2811 N  N     . ASN A 1 359 ? 16.07800  13.41700  11.00700  1.000 15.63082  ? 359  ASN A N     1 
ATOM   2812 C  CA    . ASN A 1 359 ? 17.04300  14.47600  11.28700  1.000 17.48631  ? 359  ASN A CA    1 
ATOM   2813 C  C     . ASN A 1 359 ? 16.46300  15.61100  12.11800  1.000 16.00718  ? 359  ASN A C     1 
ATOM   2814 O  O     . ASN A 1 359 ? 17.20900  16.26400  12.85200  1.000 16.53356  ? 359  ASN A O     1 
ATOM   2815 C  CB    . ASN A 1 359 ? 17.75300  14.92000  10.02100  1.000 19.39180  ? 359  ASN A CB    1 
ATOM   2816 C  CG    . ASN A 1 359 ? 18.63300  13.82500  9.47900   1.000 17.73634  ? 359  ASN A CG    1 
ATOM   2817 O  OD1   . ASN A 1 359 ? 19.26100  13.07000  10.25500  1.000 21.88947  ? 359  ASN A OD1   1 
ATOM   2818 N  ND2   . ASN A 1 359 ? 18.64700  13.67700  8.16600   1.000 20.42087  ? 359  ASN A ND2   1 
ATOM   2819 N  N     . LEU A 1 360 ? 15.15200  15.84700  12.03700  1.000 15.36500  ? 360  LEU A N     1 
ATOM   2820 C  CA    . LEU A 1 360 ? 14.51200  16.73800  13.00000  1.000 14.72545  ? 360  LEU A CA    1 
ATOM   2821 C  C     . LEU A 1 360 ? 14.61400  16.16000  14.40600  1.000 14.93074  ? 360  LEU A C     1 
ATOM   2822 O  O     . LEU A 1 360 ? 14.94300  16.88000  15.35300  1.000 16.74674  ? 360  LEU A O     1 
ATOM   2823 C  CB    . LEU A 1 360 ? 13.05200  16.98700  12.62800  1.000 14.34119  ? 360  LEU A CB    1 
ATOM   2824 C  CG    . LEU A 1 360 ? 12.26300  17.80500  13.66200  1.000 17.28102  ? 360  LEU A CG    1 
ATOM   2825 C  CD1   . LEU A 1 360 ? 12.89500  19.18400  13.94300  1.000 19.91555  ? 360  LEU A CD1   1 
ATOM   2826 C  CD2   . LEU A 1 360 ? 10.81400  17.94500  13.20100  1.000 20.60247  ? 360  LEU A CD2   1 
ATOM   2827 N  N     . ALA A 1 361 ? 14.34100  14.85400  14.55800  1.000 15.34394  ? 361  ALA A N     1 
ATOM   2828 C  CA    . ALA A 1 361 ? 14.47400  14.19800  15.86500  1.000 14.70966  ? 361  ALA A CA    1 
ATOM   2829 C  C     . ALA A 1 361 ? 15.89100  14.31200  16.40600  1.000 14.61228  ? 361  ALA A C     1 
ATOM   2830 O  O     . ALA A 1 361 ? 16.09400  14.56400  17.60500  1.000 15.69136  ? 361  ALA A O     1 
ATOM   2831 C  CB    . ALA A 1 361 ? 14.06300  12.72300  15.77700  1.000 16.06772  ? 361  ALA A CB    1 
ATOM   2832 N  N     . ARG A 1 362 ? 16.88900  14.11500  15.54200  1.000 16.25721  ? 362  ARG A N     1 
ATOM   2833 C  CA    . ARG A 1 362 ? 18.27900  14.22000  15.97900  1.000 15.64924  ? 362  ARG A CA    1 
ATOM   2834 C  C     . ARG A 1 362 ? 18.61600  15.63100  16.43500  1.000 16.00192  ? 362  ARG A C     1 
ATOM   2835 O  O     . ARG A 1 362 ? 19.30800  15.81000  17.44600  1.000 18.35483  ? 362  ARG A O     1 
ATOM   2836 C  CB    . ARG A 1 362 ? 19.22200  13.77800  14.86300  1.000 16.20984  ? 362  ARG A CB    1 
ATOM   2837 C  CG    . ARG A 1 362 ? 19.22700  12.28200  14.65700  1.000 15.79400  ? 362  ARG A CG    1 
ATOM   2838 C  CD    . ARG A 1 362 ? 19.96800  11.89300  13.39300  1.000 15.42553  ? 362  ARG A CD    1 
ATOM   2839 N  NE    . ARG A 1 362 ? 20.14200  10.45200  13.29800  1.000 16.28880  ? 362  ARG A NE    1 
ATOM   2840 C  CZ    . ARG A 1 362 ? 20.08500  9.75400   12.17600  1.000 21.59469  ? 362  ARG A CZ    1 
ATOM   2841 N  NH1   . ARG A 1 362 ? 19.78100  10.32900  11.02100  1.000 27.19537  ? 362  ARG A NH1   1 
ATOM   2842 N  NH2   . ARG A 1 362 ? 20.32200  8.44300   12.21900  1.000 24.42661  ? 362  ARG A NH2   1 
ATOM   2843 N  N     . LEU A 1 363 ? 18.15000  16.64700  15.70400  1.000 16.54935  ? 363  LEU A N     1 
ATOM   2844 C  CA    . LEU A 1 363 ? 18.37100  18.02600  16.13200  1.000 18.17586  ? 363  LEU A CA    1 
ATOM   2845 C  C     . LEU A 1 363 ? 17.70000  18.28200  17.47400  1.000 17.47578  ? 363  LEU A C     1 
ATOM   2846 O  O     . LEU A 1 363 ? 18.31700  18.82800  18.40000  1.000 18.87332  ? 363  LEU A O     1 
ATOM   2847 C  CB    . LEU A 1 363 ? 17.84100  19.00800  15.08500  1.000 18.08375  ? 363  LEU A CB    1 
ATOM   2848 C  CG    . LEU A 1 363 ? 17.76400  20.47700  15.53900  1.000 19.25494  ? 363  LEU A CG    1 
ATOM   2849 C  CD1   . LEU A 1 363 ? 19.15900  21.04700  15.83100  1.000 20.49719  ? 363  LEU A CD1   1 
ATOM   2850 C  CD2   . LEU A 1 363 ? 17.00600  21.34700  14.53600  1.000 19.58656  ? 363  LEU A CD2   1 
ATOM   2851 N  N     . GLU A 1 364 ? 16.42800  17.88800  17.59700  1.000 16.79149  ? 364  GLU A N     1 
ATOM   2852 C  CA    . GLU A 1 364 ? 15.69400  18.11200  18.83900  1.000 15.47817  ? 364  GLU A CA    1 
ATOM   2853 C  C     . GLU A 1 364 ? 16.39900  17.46300  20.02000  1.000 16.61778  ? 364  GLU A C     1 
ATOM   2854 O  O     . GLU A 1 364 ? 16.59400  18.09300  21.06500  1.000 18.02848  ? 364  GLU A O     1 
ATOM   2855 C  CB    . GLU A 1 364 ? 14.26300  17.59100  18.70800  1.000 15.80453  ? 364  GLU A CB    1 
ATOM   2856 C  CG    . GLU A 1 364 ? 13.40100  18.43600  17.79100  1.000 17.84424  ? 364  GLU A CG    1 
ATOM   2857 C  CD    . GLU A 1 364 ? 12.04900  17.81100  17.49700  1.000 18.84173  ? 364  GLU A CD    1 
ATOM   2858 O  OE1   . GLU A 1 364 ? 11.93000  16.57300  17.57300  1.000 19.67341  ? 364  GLU A OE1   1 
ATOM   2859 O  OE2   . GLU A 1 364 ? 11.09900  18.56100  17.17700  1.000 19.45496  ? 364  GLU A OE2   1 
ATOM   2860 N  N     . LEU A 1 365 ? 16.80800  16.20300  19.87300  1.000 16.57830  ? 365  LEU A N     1 
ATOM   2861 C  CA    . LEU A 1 365 ? 17.39800  15.51200  21.01400  1.000 16.25458  ? 365  LEU A CA    1 
ATOM   2862 C  C     . LEU A 1 365 ? 18.76400  16.07400  21.38100  1.000 18.48643  ? 365  LEU A C     1 
ATOM   2863 O  O     . LEU A 1 365 ? 19.10800  16.10600  22.56600  1.000 18.89437  ? 365  LEU A O     1 
ATOM   2864 C  CB    . LEU A 1 365 ? 17.44300  14.00500  20.76100  1.000 16.65726  ? 365  LEU A CB    1 
ATOM   2865 C  CG    . LEU A 1 365 ? 16.05900  13.34900  20.71600  1.000 17.54158  ? 365  LEU A CG    1 
ATOM   2866 C  CD1   . LEU A 1 365 ? 16.12800  11.97000  20.07000  1.000 18.73119  ? 365  LEU A CD1   1 
ATOM   2867 C  CD2   . LEU A 1 365 ? 15.45400  13.23500  22.10700  1.000 20.08925  ? 365  LEU A CD2   1 
ATOM   2868 N  N     . GLU A 1 366 ? 19.54900  16.52400  20.39500  1.000 18.40747  ? 366  GLU A N     1 
ATOM   2869 C  CA    . GLU A 1 366 ? 20.81600  17.18400  20.69400  1.000 19.86817  ? 366  GLU A CA    1 
ATOM   2870 C  C     . GLU A 1 366 ? 20.58900  18.46600  21.48900  1.000 19.01544  ? 366  GLU A C     1 
ATOM   2871 O  O     . GLU A 1 366 ? 21.23400  18.69400  22.52100  1.000 20.85513  ? 366  GLU A O     1 
ATOM   2872 C  CB    . GLU A 1 366 ? 21.57200  17.47900  19.39500  1.000 20.87092  ? 366  GLU A CB    1 
ATOM   2873 C  CG    . GLU A 1 366 ? 22.81200  18.35400  19.56500  1.000 23.10803  ? 366  GLU A CG    1 
ATOM   2874 C  CD    . GLU A 1 366 ? 22.52400  19.85100  19.44100  1.000 26.34526  ? 366  GLU A CD    1 
ATOM   2875 O  OE1   . GLU A 1 366 ? 21.99100  20.27000  18.39300  1.000 25.81362  ? 366  GLU A OE1   1 
ATOM   2876 O  OE2   . GLU A 1 366 ? 22.82200  20.60200  20.39900  1.000 27.26643  ? 366  GLU A OE2   1 
ATOM   2877 N  N     . VAL A 1 367 ? 19.68800  19.32500  21.00700  1.000 19.49971  ? 367  VAL A N     1 
ATOM   2878 C  CA    . VAL A 1 367 ? 19.39900  20.57900  21.69900  1.000 20.39981  ? 367  VAL A CA    1 
ATOM   2879 C  C     . VAL A 1 367 ? 18.87300  20.29800  23.09800  1.000 20.60247  ? 367  VAL A C     1 
ATOM   2880 O  O     . VAL A 1 367 ? 19.24600  20.97100  24.07000  1.000 22.98433  ? 367  VAL A O     1 
ATOM   2881 C  CB    . VAL A 1 367 ? 18.41800  21.43400  20.87200  1.000 20.23664  ? 367  VAL A CB    1 
ATOM   2882 C  CG1   . VAL A 1 367 ? 17.94600  22.65000  21.67700  1.000 21.14201  ? 367  VAL A CG1   1 
ATOM   2883 C  CG2   . VAL A 1 367 ? 19.07000  21.86800  19.55700  1.000 21.67365  ? 367  VAL A CG2   1 
ATOM   2884 N  N     . ILE A 1 368 ? 18.01100  19.28600  23.22200  1.000 20.86566  ? 368  ILE A N     1 
ATOM   2885 C  CA    . ILE A 1 368 ? 17.40100  18.95300  24.50800  1.000 18.32062  ? 368  ILE A CA    1 
ATOM   2886 C  C     . ILE A 1 368 ? 18.45400  18.50500  25.51400  1.000 19.82606  ? 368  ILE A C     1 
ATOM   2887 O  O     . ILE A 1 368 ? 18.50100  19.00000  26.64500  1.000 21.75524  ? 368  ILE A O     1 
ATOM   2888 C  CB    . ILE A 1 368 ? 16.28700  17.90600  24.31900  1.000 20.12610  ? 368  ILE A CB    1 
ATOM   2889 C  CG1   . ILE A 1 368 ? 15.04000  18.57300  23.74100  1.000 20.50509  ? 368  ILE A CG1   1 
ATOM   2890 C  CG2   . ILE A 1 368 ? 15.98300  17.18000  25.62800  1.000 21.26044  ? 368  ILE A CG2   1 
ATOM   2891 C  CD1   . ILE A 1 368 ? 14.09300  17.60100  23.10900  1.000 20.66037  ? 368  ILE A CD1   1 
ATOM   2892 N  N     . LEU A 1 369 ? 19.31900  17.56600  25.12300  1.000 19.87870  ? 369  LEU A N     1 
ATOM   2893 C  CA    . LEU A 1 369 ? 20.31400  17.06100  26.06600  1.000 20.02082  ? 369  LEU A CA    1 
ATOM   2894 C  C     . LEU A 1 369 ? 21.29500  18.15200  26.46900  1.000 20.93672  ? 369  LEU A C     1 
ATOM   2895 O  O     . LEU A 1 369 ? 21.63600  18.28400  27.65400  1.000 24.07920  ? 369  LEU A O     1 
ATOM   2896 C  CB    . LEU A 1 369 ? 21.03900  15.84000  25.50300  1.000 20.39718  ? 369  LEU A CB    1 
ATOM   2897 C  CG    . LEU A 1 369 ? 20.17600  14.58600  25.31100  1.000 22.30267  ? 369  LEU A CG    1 
ATOM   2898 C  CD1   . LEU A 1 369 ? 20.99800  13.44100  24.76400  1.000 24.69243  ? 369  LEU A CD1   1 
ATOM   2899 C  CD2   . LEU A 1 369 ? 19.50800  14.18300  26.62100  1.000 25.36620  ? 369  LEU A CD2   1 
ATOM   2900 N  N     . ASN A 1 370 ? 21.74500  18.95600  25.50300  1.000 22.44216  ? 370  ASN A N     1 
ATOM   2901 C  CA    . ASN A 1 370 ? 22.63300  20.06000  25.83600  1.000 21.68681  ? 370  ASN A CA    1 
ATOM   2902 C  C     . ASN A 1 370 ? 21.94800  21.05000  26.76800  1.000 24.06341  ? 370  ASN A C     1 
ATOM   2903 O  O     . ASN A 1 370 ? 22.57500  21.56600  27.69900  1.000 27.30064  ? 370  ASN A O     1 
ATOM   2904 C  CB    . ASN A 1 370 ? 23.15500  20.73400  24.56500  1.000 25.30830  ? 370  ASN A CB    1 
ATOM   2905 C  CG    . ASN A 1 370 ? 24.38500  20.03000  24.00100  1.000 26.74005  ? 370  ASN A CG    1 
ATOM   2906 O  OD1   . ASN A 1 370 ? 25.31900  19.71100  24.74100  1.000 26.20577  ? 370  ASN A OD1   1 
ATOM   2907 N  ND2   . ASN A 1 370 ? 24.38500  19.77400  22.69500  1.000 26.01891  ? 370  ASN A ND2   1 
ATOM   2908 N  N     . ALA A 1 371 ? 20.65000  21.30100  26.56100  1.000 23.76864  ? 371  ALA A N     1 
ATOM   2909 C  CA    . ALA A 1 371 ? 19.95800  22.27500  27.40500  1.000 25.31619  ? 371  ALA A CA    1 
ATOM   2910 C  C     . ALA A 1 371 ? 19.78800  21.76200  28.83100  1.000 24.67138  ? 371  ALA A C     1 
ATOM   2911 O  O     . ALA A 1 371 ? 19.98500  22.51500  29.79800  1.000 27.68753  ? 371  ALA A O     1 
ATOM   2912 C  CB    . ALA A 1 371 ? 18.61000  22.65700  26.79300  1.000 25.88995  ? 371  ALA A CB    1 
ATOM   2913 N  N     . LEU A 1 372 ? 19.41900  20.48900  28.98600  1.000 24.08183  ? 372  LEU A N     1 
ATOM   2914 C  CA    . LEU A 1 372 ? 19.31600  19.90900  30.32100  1.000 25.58465  ? 372  LEU A CA    1 
ATOM   2915 C  C     . LEU A 1 372 ? 20.66200  19.93800  31.03700  1.000 26.73742  ? 372  LEU A C     1 
ATOM   2916 O  O     . LEU A 1 372 ? 20.73600  20.29400  32.22300  1.000 28.83767  ? 372  LEU A O     1 
ATOM   2917 C  CB    . LEU A 1 372 ? 18.77100  18.48300  30.23200  1.000 26.02154  ? 372  LEU A CB    1 
ATOM   2918 C  CG    . LEU A 1 372 ? 17.31200  18.33000  29.78800  1.000 23.41333  ? 372  LEU A CG    1 
ATOM   2919 C  CD1   . LEU A 1 372 ? 16.96000  16.85800  29.60700  1.000 24.91088  ? 372  LEU A CD1   1 
ATOM   2920 C  CD2   . LEU A 1 372 ? 16.38800  19.00200  30.79200  1.000 25.10564  ? 372  LEU A CD2   1 
ATOM   2921 N  N     . MET A 1 373 ? 21.74500  19.59500  30.33700  1.000 27.02692  ? 373  MET A N     1 
ATOM   2922 C  CA    . MET A 1 373 ? 23.05200  19.61600  30.99100  1.000 26.63214  ? 373  MET A CA    1 
ATOM   2923 C  C     . MET A 1 373 ? 23.48600  21.03800  31.33800  1.000 29.14560  ? 373  MET A C     1 
ATOM   2924 O  O     . MET A 1 373 ? 24.10600  21.25700  32.38300  1.000 31.48535  ? 373  MET A O     1 
ATOM   2925 C  CB    . MET A 1 373 ? 24.10500  18.89100  30.14700  1.000 26.02944  ? 373  MET A CB    1 
ATOM   2926 C  CG    . MET A 1 373 ? 23.84900  17.39900  30.02400  1.000 27.08746  ? 373  MET A CG    1 
ATOM   2927 S  SD    . MET A 1 373 ? 25.10800  16.50400  29.09200  1.000 27.94809  ? 373  MET A SD    1 
ATOM   2928 C  CE    . MET A 1 373 ? 24.83500  17.17400  27.45000  1.000 28.94294  ? 373  MET A CE    1 
ATOM   2929 N  N     . ASP A 1 374 ? 23.16000  22.01700  30.48700  1.000 29.26667  ? 374  ASP A N     1 
ATOM   2930 C  CA    . ASP A 1 374 ? 23.54900  23.40000  30.75500  1.000 31.23532  ? 374  ASP A CA    1 
ATOM   2931 C  C     . ASP A 1 374 ? 22.71100  23.99700  31.87600  1.000 32.40915  ? 374  ASP A C     1 
ATOM   2932 O  O     . ASP A 1 374 ? 23.24500  24.62300  32.80300  1.000 34.96472  ? 374  ASP A O     1 
ATOM   2933 C  CB    . ASP A 1 374 ? 23.36900  24.25700  29.49700  1.000 31.45904  ? 374  ASP A CB    1 
ATOM   2934 C  CG    . ASP A 1 374 ? 24.42300  23.99500  28.43700  1.000 35.02262  ? 374  ASP A CG    1 
ATOM   2935 O  OD1   . ASP A 1 374 ? 25.42000  23.30600  28.72900  1.000 36.65703  ? 374  ASP A OD1   1 
ATOM   2936 O  OD2   . ASP A 1 374 ? 24.25300  24.49700  27.30400  1.000 36.39647  ? 374  ASP A OD2   1 
ATOM   2937 N  N     . ARG A 1 375 ? 21.39200  23.84500  31.79300  1.000 32.79077  ? 375  ARG A N     1 
ATOM   2938 C  CA    . ARG A 1 375 ? 20.48200  24.62000  32.62600  1.000 32.86710  ? 375  ARG A CA    1 
ATOM   2939 C  C     . ARG A 1 375 ? 20.04400  23.89600  33.88800  1.000 33.53297  ? 375  ARG A C     1 
ATOM   2940 O  O     . ARG A 1 375 ? 19.73800  24.55900  34.88500  1.000 35.88851  ? 375  ARG A O     1 
ATOM   2941 C  CB    . ARG A 1 375 ? 19.24100  25.03300  31.82700  1.000 34.77522  ? 375  ARG A CB    1 
ATOM   2942 C  CG    . ARG A 1 375 ? 19.54500  25.69100  30.48000  1.000 39.59685  ? 375  ARG A CG    1 
ATOM   2943 C  CD    . ARG A 1 375 ? 19.58800  27.19600  30.60500  1.000 42.35245  ? 375  ARG A CD    1 
ATOM   2944 N  NE    . ARG A 1 375 ? 18.47800  27.67500  31.41700  1.000 46.39240  ? 375  ARG A NE    1 
ATOM   2945 C  CZ    . ARG A 1 375 ? 17.32100  28.11100  30.93700  1.000 49.25064  ? 375  ARG A CZ    1 
ATOM   2946 N  NH1   . ARG A 1 375 ? 17.17500  28.42400  29.65900  1.000 49.08746  ? 375  ARG A NH1   1 
ATOM   2947 N  NH2   . ARG A 1 375 ? 16.28400  28.24000  31.76100  1.000 50.12180  ? 375  ARG A NH2   1 
ATOM   2948 N  N     . VAL A 1 376 ? 20.00500  22.56600  33.88400  1.000 33.29610  ? 376  VAL A N     1 
ATOM   2949 C  CA    . VAL A 1 376 ? 19.61900  21.82700  35.08500  1.000 32.92763  ? 376  VAL A CA    1 
ATOM   2950 C  C     . VAL A 1 376 ? 20.55300  20.63900  35.31800  1.000 34.60152  ? 376  VAL A C     1 
ATOM   2951 O  O     . VAL A 1 376 ? 20.11200  19.47900  35.32500  1.000 36.20434  ? 376  VAL A O     1 
ATOM   2952 C  CB    . VAL A 1 376 ? 18.11300  21.49600  35.08400  1.000 35.16474  ? 376  VAL A CB    1 
ATOM   2953 C  CG1   . VAL A 1 376 ? 17.72700  20.62200  33.90100  1.000 37.50450  ? 376  VAL A CG1   1 
ATOM   2954 C  CG2   . VAL A 1 376 ? 17.67100  20.88700  36.39500  1.000 36.10696  ? 376  VAL A CG2   1 
ATOM   2955 N  N     . PRO A 1 377 ? 21.85100  20.88100  35.53000  1.000 35.66480  ? 377  PRO A N     1 
ATOM   2956 C  CA    . PRO A 1 377 ? 22.78000  19.76000  35.74900  1.000 38.41513  ? 377  PRO A CA    1 
ATOM   2957 C  C     . PRO A 1 377 ? 22.44600  18.91100  36.96400  1.000 41.58920  ? 377  PRO A C     1 
ATOM   2958 O  O     . PRO A 1 377 ? 22.86600  17.74800  37.01900  1.000 45.18436  ? 377  PRO A O     1 
ATOM   2959 C  CB    . PRO A 1 377 ? 24.14200  20.45400  35.90800  1.000 37.73347  ? 377  PRO A CB    1 
ATOM   2960 C  CG    . PRO A 1 377 ? 23.80300  21.86200  36.33700  1.000 35.96747  ? 377  PRO A CG    1 
ATOM   2961 C  CD    . PRO A 1 377 ? 22.54700  22.17900  35.56400  1.000 35.19369  ? 377  PRO A CD    1 
ATOM   2962 N  N     . THR A 1 378 ? 21.71600  19.44300  37.94100  1.000 40.97333  ? 378  THR A N     1 
ATOM   2963 C  CA    . THR A 1 378 ? 21.33800  18.67100  39.11600  1.000 38.20458  ? 378  THR A CA    1 
ATOM   2964 C  C     . THR A 1 378 ? 20.02000  17.93100  38.95000  1.000 35.72797  ? 378  THR A C     1 
ATOM   2965 O  O     . THR A 1 378 ? 19.51000  17.38300  39.92900  1.000 37.33606  ? 378  THR A O     1 
ATOM   2966 C  CB    . THR A 1 378 ? 21.30300  19.56000  40.35900  1.000 38.43619  ? 378  THR A CB    1 
ATOM   2967 O  OG1   . THR A 1 378 ? 20.25600  20.53300  40.23400  1.000 38.98099  ? 378  THR A OG1   1 
ATOM   2968 C  CG2   . THR A 1 378 ? 22.63200  20.25800  40.50400  1.000 38.80202  ? 378  THR A CG2   1 
ATOM   2969 N  N     . LEU A 1 379 ? 19.46400  17.88900  37.73400  1.000 33.42243  ? 379  LEU A N     1 
ATOM   2970 C  CA    . LEU A 1 379 ? 18.23600  17.14300  37.50100  1.000 31.77223  ? 379  LEU A CA    1 
ATOM   2971 C  C     . LEU A 1 379 ? 18.37700  15.71300  38.01000  1.000 34.75417  ? 379  LEU A C     1 
ATOM   2972 O  O     . LEU A 1 379 ? 19.40100  15.05700  37.79600  1.000 36.82810  ? 379  LEU A O     1 
ATOM   2973 C  CB    . LEU A 1 379 ? 17.93800  17.11100  35.99800  1.000 31.60116  ? 379  LEU A CB    1 
ATOM   2974 C  CG    . LEU A 1 379 ? 16.63100  16.44300  35.56400  1.000 30.55630  ? 379  LEU A CG    1 
ATOM   2975 C  CD1   . LEU A 1 379 ? 15.44500  17.28000  35.99800  1.000 30.93792  ? 379  LEU A CD1   1 
ATOM   2976 C  CD2   . LEU A 1 379 ? 16.60200  16.20200  34.04300  1.000 31.02477  ? 379  LEU A CD2   1 
ATOM   2977 N  N     . ARG A 1 380 ? 17.34400  15.23900  38.70300  1.000 37.58345  ? 380  ARG A N     1 
ATOM   2978 C  CA    . ARG A 1 380 ? 17.28400  13.85900  39.16000  1.000 36.73862  ? 380  ARG A CA    1 
ATOM   2979 C  C     . ARG A 1 380 ? 15.82100  13.45700  39.25900  1.000 36.14907  ? 380  ARG A C     1 
ATOM   2980 O  O     . ARG A 1 380 ? 14.92700  14.30600  39.28700  1.000 35.34371  ? 380  ARG A O     1 
ATOM   2981 C  CB    . ARG A 1 380 ? 17.97100  13.66700  40.52000  1.000 39.37841  ? 380  ARG A CB    1 
ATOM   2982 C  CG    . ARG A 1 380 ? 17.02200  13.78400  41.69200  1.000 45.99762  ? 380  ARG A CG    1 
ATOM   2983 C  CD    . ARG A 1 380 ? 17.72200  13.47700  43.00400  1.000 52.11414  ? 380  ARG A CD    1 
ATOM   2984 N  NE    . ARG A 1 380 ? 16.91700  13.89100  44.14500  1.000 56.69364  ? 380  ARG A NE    1 
ATOM   2985 C  CZ    . ARG A 1 380 ? 16.93100  15.11200  44.66300  1.000 58.63598  ? 380  ARG A CZ    1 
ATOM   2986 N  NH1   . ARG A 1 380 ? 17.69500  16.06800  44.15900  1.000 58.38858  ? 380  ARG A NH1   1 
ATOM   2987 N  NH2   . ARG A 1 380 ? 16.15400  15.38300  45.70900  1.000 59.39660  ? 380  ARG A NH2   1 
ATOM   2988 N  N     . LEU A 1 381 ? 15.58200  12.14800  39.30800  1.000 35.62006  ? 381  LEU A N     1 
ATOM   2989 C  CA    . LEU A 1 381 ? 14.22200  11.65100  39.44900  1.000 35.99642  ? 381  LEU A CA    1 
ATOM   2990 C  C     . LEU A 1 381 ? 13.71000  11.89100  40.86300  1.000 37.85980  ? 381  LEU A C     1 
ATOM   2991 O  O     . LEU A 1 381 ? 14.43000  11.69200  41.84900  1.000 40.53118  ? 381  LEU A O     1 
ATOM   2992 C  CB    . LEU A 1 381 ? 14.16400  10.16000  39.13700  1.000 36.14118  ? 381  LEU A CB    1 
ATOM   2993 C  CG    . LEU A 1 381 ? 14.52200  9.76100   37.70200  1.000 33.03028  ? 381  LEU A CG    1 
ATOM   2994 C  CD1   . LEU A 1 381 ? 14.10700  8.32400   37.41400  1.000 32.80130  ? 381  LEU A CD1   1 
ATOM   2995 C  CD2   . LEU A 1 381 ? 13.90400  10.72100  36.69800  1.000 30.31679  ? 381  LEU A CD2   1 
ATOM   2996 N  N     . ALA A 1 382 ? 12.45300  12.32000  40.96000  1.000 38.82571  ? 382  ALA A N     1 
ATOM   2997 C  CA    . ALA A 1 382 ? 11.82900  12.55600  42.26000  1.000 38.90993  ? 382  ALA A CA    1 
ATOM   2998 C  C     . ALA A 1 382 ? 11.26900  11.28400  42.88200  1.000 40.97860  ? 382  ALA A C     1 
ATOM   2999 O  O     . ALA A 1 382 ? 10.85200  11.30900  44.04700  1.000 42.64985  ? 382  ALA A O     1 
ATOM   3000 C  CB    . ALA A 1 382 ? 10.73000  13.61500  42.12800  1.000 37.95981  ? 382  ALA A CB    1 
ATOM   3001 N  N     . VAL A 1 383 ? 11.25200  10.18400  42.13600  1.000 42.92094  ? 383  VAL A N     1 
ATOM   3002 C  CA    . VAL A 1 383 ? 10.82000  8.87800   42.63000  1.000 43.04727  ? 383  VAL A CA    1 
ATOM   3003 C  C     . VAL A 1 383 ? 11.80800  7.83300   42.13700  1.000 44.09476  ? 383  VAL A C     1 
ATOM   3004 O  O     . VAL A 1 383 ? 12.54600  8.06300   41.16900  1.000 43.25519  ? 383  VAL A O     1 
ATOM   3005 C  CB    . VAL A 1 383 ? 9.39600   8.52200   42.14900  1.000 41.78922  ? 383  VAL A CB    1 
ATOM   3006 C  CG1   . VAL A 1 383 ? 8.39100   9.59000   42.56400  1.000 42.50773  ? 383  VAL A CG1   1 
ATOM   3007 C  CG2   . VAL A 1 383 ? 9.37500   8.32600   40.63800  1.000 42.43930  ? 383  VAL A CG2   1 
ATOM   3008 N  N     . PRO A 1 384 ? 11.86400  6.68000   42.80000  1.000 43.92895  ? 384  PRO A N     1 
ATOM   3009 C  CA    . PRO A 1 384 ? 12.71900  5.59900   42.30300  1.000 42.94199  ? 384  PRO A CA    1 
ATOM   3010 C  C     . PRO A 1 384 ? 12.21700  5.09100   40.96300  1.000 40.99702  ? 384  PRO A C     1 
ATOM   3011 O  O     . PRO A 1 384 ? 11.02700  5.17600   40.65000  1.000 41.19441  ? 384  PRO A O     1 
ATOM   3012 C  CB    . PRO A 1 384 ? 12.57700  4.51300   43.37400  1.000 43.59733  ? 384  PRO A CB    1 
ATOM   3013 C  CG    . PRO A 1 384 ? 12.12100  5.23300   44.59700  1.000 44.42901  ? 384  PRO A CG    1 
ATOM   3014 C  CD    . PRO A 1 384 ? 11.24500  6.33600   44.09100  1.000 43.75525  ? 384  PRO A CD    1 
ATOM   3015 N  N     . VAL A 1 385 ? 13.14600  4.54300   40.17100  1.000 39.46263  ? 385  VAL A N     1 
ATOM   3016 C  CA    . VAL A 1 385 ? 12.77700  3.96100   38.88100  1.000 39.03626  ? 385  VAL A CA    1 
ATOM   3017 C  C     . VAL A 1 385 ? 11.72700  2.86800   39.05100  1.000 42.02609  ? 385  VAL A C     1 
ATOM   3018 O  O     . VAL A 1 385 ? 10.88500  2.66500   38.16600  1.000 39.12838  ? 385  VAL A O     1 
ATOM   3019 C  CB    . VAL A 1 385 ? 14.03000  3.46500   38.12500  1.000 37.74400  ? 385  VAL A CB    1 
ATOM   3020 C  CG1   . VAL A 1 385 ? 13.64800  2.82500   36.79200  1.000 37.10708  ? 385  VAL A CG1   1 
ATOM   3021 C  CG2   . VAL A 1 385 ? 14.99100  4.61300   37.88500  1.000 38.54673  ? 385  VAL A CG2   1 
ATOM   3022 N  N     . GLU A 1 386 ? 11.73200  2.17900   40.20200  1.000 44.05265  ? 386  GLU A N     1 
ATOM   3023 C  CA    A GLU A 1 386 ? 10.78000  1.09700   40.43500  0.500 45.13962  ? 386  GLU A CA    1 
ATOM   3024 C  CA    B GLU A 1 386 ? 10.77700  1.09500   40.42300  0.500 46.05289  ? 386  GLU A CA    1 
ATOM   3025 C  C     . GLU A 1 386 ? 9.34000   1.59800   40.44800  1.000 46.08710  ? 386  GLU A C     1 
ATOM   3026 O  O     . GLU A 1 386 ? 8.41700   0.84200   40.12800  1.000 49.17695  ? 386  GLU A O     1 
ATOM   3027 C  CB    A GLU A 1 386 ? 11.10100  0.38200   41.75100  0.500 45.02645  ? 386  GLU A CB    1 
ATOM   3028 C  CB    B GLU A 1 386 ? 11.10100  0.34300   41.71800  0.500 47.88995  ? 386  GLU A CB    1 
ATOM   3029 C  CG    A GLU A 1 386 ? 12.41400  -0.40200  41.75900  0.500 45.09751  ? 386  GLU A CG    1 
ATOM   3030 C  CG    B GLU A 1 386 ? 10.43400  -1.03200  41.83900  0.500 50.13759  ? 386  GLU A CG    1 
ATOM   3031 C  CD    A GLU A 1 386 ? 13.62200  0.44800   42.12600  0.500 45.87919  ? 386  GLU A CD    1 
ATOM   3032 C  CD    B GLU A 1 386 ? 8.96900   -0.96300  42.25300  0.500 52.94845  ? 386  GLU A CD    1 
ATOM   3033 O  OE1   A GLU A 1 386 ? 13.49700  1.68900   42.16400  0.500 46.34766  ? 386  GLU A OE1   1 
ATOM   3034 O  OE1   B GLU A 1 386 ? 8.65100   -0.23800  43.22000  0.500 55.80406  ? 386  GLU A OE1   1 
ATOM   3035 O  OE2   A GLU A 1 386 ? 14.70000  -0.13000  42.38100  0.500 46.50294  ? 386  GLU A OE2   1 
ATOM   3036 O  OE2   B GLU A 1 386 ? 8.13200   -1.62000  41.59600  0.500 51.59303  ? 386  GLU A OE2   1 
ATOM   3037 N  N     . GLN A 1 387 ? 9.12400   2.86100   40.80900  1.000 44.30268  ? 387  GLN A N     1 
ATOM   3038 C  CA    . GLN A 1 387 ? 7.76800   3.38600   40.90900  1.000 41.15757  ? 387  GLN A CA    1 
ATOM   3039 C  C     . GLN A 1 387 ? 7.20900   3.92400   39.59500  1.000 36.91495  ? 387  GLN A C     1 
ATOM   3040 O  O     . GLN A 1 387 ? 6.02000   4.25600   39.54100  1.000 37.32026  ? 387  GLN A O     1 
ATOM   3041 C  CB    . GLN A 1 387 ? 7.68500   4.44400   42.01300  1.000 44.42901  ? 387  GLN A CB    1 
ATOM   3042 C  CG    . GLN A 1 387 ? 7.79200   3.83500   43.40800  1.000 49.73228  ? 387  GLN A CG    1 
ATOM   3043 C  CD    . GLN A 1 387 ? 7.96300   4.87000   44.49900  1.000 54.48548  ? 387  GLN A CD    1 
ATOM   3044 O  OE1   . GLN A 1 387 ? 7.71500   6.05600   44.28900  1.000 54.85395  ? 387  GLN A OE1   1 
ATOM   3045 N  NE2   . GLN A 1 387 ? 8.39300   4.42500   45.67700  1.000 57.76219  ? 387  GLN A NE2   1 
ATOM   3046 N  N     . LEU A 1 388 ? 8.01500   4.00300   38.54000  1.000 33.70930  ? 388  LEU A N     1 
ATOM   3047 C  CA    . LEU A 1 388 ? 7.51200   4.49600   37.26500  1.000 32.01700  ? 388  LEU A CA    1 
ATOM   3048 C  C     . LEU A 1 388 ? 6.61700   3.44600   36.60900  1.000 33.18556  ? 388  LEU A C     1 
ATOM   3049 O  O     . LEU A 1 388 ? 6.66400   2.25900   36.93600  1.000 34.83576  ? 388  LEU A O     1 
ATOM   3050 C  CB    . LEU A 1 388 ? 8.67600   4.85700   36.33500  1.000 30.75895  ? 388  LEU A CB    1 
ATOM   3051 C  CG    . LEU A 1 388 ? 9.65100   5.91200   36.87000  1.000 30.85633  ? 388  LEU A CG    1 
ATOM   3052 C  CD1   . LEU A 1 388 ? 10.85400  6.09800   35.94800  1.000 30.65368  ? 388  LEU A CD1   1 
ATOM   3053 C  CD2   . LEU A 1 388 ? 8.93000   7.22800   37.09100  1.000 31.38797  ? 388  LEU A CD2   1 
ATOM   3054 N  N     . VAL A 1 389 ? 5.79300   3.90000   35.66900  1.000 31.78276  ? 389  VAL A N     1 
ATOM   3055 C  CA    . VAL A 1 389 ? 4.86100   3.04500   34.93900  1.000 30.57472  ? 389  VAL A CA    1 
ATOM   3056 C  C     . VAL A 1 389 ? 5.21200   3.13800   33.46100  1.000 28.64554  ? 389  VAL A C     1 
ATOM   3057 O  O     . VAL A 1 389 ? 5.06300   4.20400   32.85400  1.000 29.29035  ? 389  VAL A O     1 
ATOM   3058 C  CB    . VAL A 1 389 ? 3.40500   3.46400   35.18200  1.000 32.26703  ? 389  VAL A CB    1 
ATOM   3059 C  CG1   . VAL A 1 389 ? 2.46200   2.64700   34.31500  1.000 33.18556  ? 389  VAL A CG1   1 
ATOM   3060 C  CG2   . VAL A 1 389 ? 3.05200   3.30600   36.65100  1.000 33.01448  ? 389  VAL A CG2   1 
ATOM   3061 N  N     . LEU A 1 390 ? 5.66000   2.02900   32.87500  1.000 28.17180  ? 390  LEU A N     1 
ATOM   3062 C  CA    . LEU A 1 390 ? 5.99700   1.99100   31.45600  1.000 27.64016  ? 390  LEU A CA    1 
ATOM   3063 C  C     . LEU A 1 390 ? 4.76900   1.62800   30.63200  1.000 27.31117  ? 390  LEU A C     1 
ATOM   3064 O  O     . LEU A 1 390 ? 3.94100   0.81700   31.05300  1.000 29.53512  ? 390  LEU A O     1 
ATOM   3065 C  CB    . LEU A 1 390 ? 7.09700   0.96000   31.19300  1.000 27.46119  ? 390  LEU A CB    1 
ATOM   3066 C  CG    . LEU A 1 390 ? 8.49800   1.32200   31.68200  1.000 27.21116  ? 390  LEU A CG    1 
ATOM   3067 C  CD1   . LEU A 1 390 ? 9.36900   0.08700   31.71600  1.000 28.40077  ? 390  LEU A CD1   1 
ATOM   3068 C  CD2   . LEU A 1 390 ? 9.10800   2.38100   30.76300  1.000 30.44049  ? 390  LEU A CD2   1 
ATOM   3069 N  N     . ARG A 1 391 ? 4.66900   2.21700   29.44100  1.000 25.85573  ? 391  ARG A N     1 
ATOM   3070 C  CA    . ARG A 1 391 ? 3.60100   1.85500   28.52700  1.000 25.37673  ? 391  ARG A CA    1 
ATOM   3071 C  C     . ARG A 1 391 ? 3.83000   0.43800   28.00400  1.000 24.85035  ? 391  ARG A C     1 
ATOM   3072 O  O     . ARG A 1 391 ? 4.96700   -0.03200  27.95200  1.000 25.31619  ? 391  ARG A O     1 
ATOM   3073 C  CB    . ARG A 1 391 ? 3.59100   2.80900   27.34500  1.000 25.95574  ? 391  ARG A CB    1 
ATOM   3074 C  CG    . ARG A 1 391 ? 3.45800   4.26200   27.72400  1.000 26.08207  ? 391  ARG A CG    1 
ATOM   3075 C  CD    . ARG A 1 391 ? 3.73200   5.09900   26.51000  1.000 26.51371  ? 391  ARG A CD    1 
ATOM   3076 N  NE    . ARG A 1 391 ? 3.66200   6.52600   26.78300  1.000 30.83528  ? 391  ARG A NE    1 
ATOM   3077 C  CZ    . ARG A 1 391 ? 4.18400   7.44400   25.98500  1.000 32.25913  ? 391  ARG A CZ    1 
ATOM   3078 N  NH1   . ARG A 1 391 ? 4.83300   7.10400   24.88400  1.000 31.49851  ? 391  ARG A NH1   1 
ATOM   3079 N  NH2   . ARG A 1 391 ? 4.05000   8.72900   26.29700  1.000 33.84090  ? 391  ARG A NH2   1 
ATOM   3080 N  N     . PRO A 1 392 ? 2.77000   -0.25400  27.59400  1.000 26.33474  ? 392  PRO A N     1 
ATOM   3081 C  CA    . PRO A 1 392 ? 2.92000   -1.62200  27.09000  1.000 25.29251  ? 392  PRO A CA    1 
ATOM   3082 C  C     . PRO A 1 392 ? 3.50600   -1.63300  25.68100  1.000 24.47925  ? 392  PRO A C     1 
ATOM   3083 O  O     . PRO A 1 392 ? 3.56000   -0.61900  24.98100  1.000 23.09224  ? 392  PRO A O     1 
ATOM   3084 C  CB    . PRO A 1 392 ? 1.47700   -2.13400  27.07300  1.000 25.58201  ? 392  PRO A CB    1 
ATOM   3085 C  CG    . PRO A 1 392 ? 0.67100   -0.90600  26.81100  1.000 28.17706  ? 392  PRO A CG    1 
ATOM   3086 C  CD    . PRO A 1 392 ? 1.35800   0.17300   27.60600  1.000 25.89521  ? 392  PRO A CD    1 
ATOM   3087 N  N     . GLY A 1 393 ? 3.94400   -2.82500  25.26700  1.000 24.34502  ? 393  GLY A N     1 
ATOM   3088 C  CA    . GLY A 1 393 ? 4.56900   -3.00300  23.96900  1.000 25.22671  ? 393  GLY A CA    1 
ATOM   3089 C  C     . GLY A 1 393 ? 3.64700   -2.82200  22.78700  1.000 24.58453  ? 393  GLY A C     1 
ATOM   3090 O  O     . GLY A 1 393 ? 4.10300   -2.87400  21.64000  1.000 25.20039  ? 393  GLY A O     1 
ATOM   3091 N  N     . THR A 1 394 ? 2.36200   -2.61600  23.03900  1.000 24.14763  ? 394  THR A N     1 
ATOM   3092 C  CA    . THR A 1 394 ? 1.38600   -2.37500  21.99100  1.000 22.99749  ? 394  THR A CA    1 
ATOM   3093 C  C     . THR A 1 394 ? 1.32700   -0.91500  21.55100  1.000 21.66049  ? 394  THR A C     1 
ATOM   3094 O  O     . THR A 1 394 ? 0.49400   -0.57900  20.70200  1.000 23.28174  ? 394  THR A O     1 
ATOM   3095 C  CB    . THR A 1 394 ? 0.01100   -2.83900  22.47600  1.000 25.24513  ? 394  THR A CB    1 
ATOM   3096 O  OG1   . THR A 1 394 ? -0.22700  -2.31300  23.78600  1.000 27.54804  ? 394  THR A OG1   1 
ATOM   3097 C  CG2   . THR A 1 394 ? -0.04500  -4.36300  22.52600  1.000 24.80297  ? 394  THR A CG2   1 
ATOM   3098 N  N     . THR A 1 395 ? 2.18000   -0.04400  22.09100  1.000 19.83922  ? 395  THR A N     1 
ATOM   3099 C  CA    . THR A 1 395 ? 2.21500   1.36100   21.69500  1.000 20.22085  ? 395  THR A CA    1 
ATOM   3100 C  C     . THR A 1 395 ? 3.67200   1.81500   21.61700  1.000 20.83408  ? 395  THR A C     1 
ATOM   3101 O  O     . THR A 1 395 ? 4.59800   1.01200   21.75900  1.000 20.84460  ? 395  THR A O     1 
ATOM   3102 C  CB    . THR A 1 395 ? 1.36300   2.23400   22.63100  1.000 21.22360  ? 395  THR A CB    1 
ATOM   3103 O  OG1   . THR A 1 395 ? 1.27700   3.56200   22.09700  1.000 22.35531  ? 395  THR A OG1   1 
ATOM   3104 C  CG2   . THR A 1 395 ? 1.96200   2.29600   24.02900  1.000 21.68681  ? 395  THR A CG2   1 
ATOM   3105 N  N     . ILE A 1 396 ? 3.87200   3.11000   21.35200  1.000 18.64171  ? 396  ILE A N     1 
ATOM   3106 C  CA    . ILE A 1 396 ? 5.20500   3.70000   21.41800  1.000 17.89162  ? 396  ILE A CA    1 
ATOM   3107 C  C     . ILE A 1 396 ? 5.70900   3.60800   22.84900  1.000 19.14177  ? 396  ILE A C     1 
ATOM   3108 O  O     . ILE A 1 396 ? 4.99400   3.96700   23.79500  1.000 21.20781  ? 396  ILE A O     1 
ATOM   3109 C  CB    . ILE A 1 396 ? 5.15400   5.16700   20.95200  1.000 18.34957  ? 396  ILE A CB    1 
ATOM   3110 C  CG1   . ILE A 1 396 ? 4.64600   5.27300   19.50500  1.000 21.56574  ? 396  ILE A CG1   1 
ATOM   3111 C  CG2   . ILE A 1 396 ? 6.53300   5.84900   21.08700  1.000 19.91555  ? 396  ILE A CG2   1 
ATOM   3112 C  CD1   . ILE A 1 396 ? 5.65300   4.83200   18.47300  1.000 27.35591  ? 396  ILE A CD1   1 
ATOM   3113 N  N     . GLN A 1 397 ? 6.94400   3.12600   23.02000  1.000 18.14954  ? 397  GLN A N     1 
ATOM   3114 C  CA    . GLN A 1 397 ? 7.49400   2.95300   24.36300  1.000 18.25219  ? 397  GLN A CA    1 
ATOM   3115 C  C     . GLN A 1 397 ? 7.62500   4.30500   25.05300  1.000 18.75488  ? 397  GLN A C     1 
ATOM   3116 O  O     . GLN A 1 397 ? 7.83100   5.34000   24.41100  1.000 21.03673  ? 397  GLN A O     1 
ATOM   3117 C  CB    . GLN A 1 397 ? 8.88600   2.31000   24.29600  1.000 19.52339  ? 397  GLN A CB    1 
ATOM   3118 C  CG    . GLN A 1 397 ? 8.98600   1.01700   23.48500  1.000 19.96029  ? 397  GLN A CG    1 
ATOM   3119 C  CD    . GLN A 1 397 ? 8.41900   -0.20100  24.20300  1.000 21.35782  ? 397  GLN A CD    1 
ATOM   3120 O  OE1   . GLN A 1 397 ? 8.24600   -0.20800  25.42700  1.000 22.79484  ? 397  GLN A OE1   1 
ATOM   3121 N  NE2   . GLN A 1 397 ? 8.15500   -1.25500  23.43800  1.000 24.51347  ? 397  GLN A NE2   1 
ATOM   3122 N  N     . GLY A 1 398 ? 7.51300   4.29800   26.37400  1.000 20.01819  ? 398  GLY A N     1 
ATOM   3123 C  CA    . GLY A 1 398 ? 7.72500   5.51300   27.13500  1.000 22.36847  ? 398  GLY A CA    1 
ATOM   3124 C  C     . GLY A 1 398 ? 7.04800   5.46200   28.49300  1.000 22.41321  ? 398  GLY A C     1 
ATOM   3125 O  O     . GLY A 1 398 ? 6.58600   4.41700   28.94600  1.000 23.61862  ? 398  GLY A O     1 
ATOM   3126 N  N     . VAL A 1 399 ? 7.00200   6.62800   29.12900  1.000 23.04487  ? 399  VAL A N     1 
ATOM   3127 C  CA    A VAL A 1 399 ? 6.34600   6.80500   30.42100  0.750 23.42386  ? 399  VAL A CA    1 
ATOM   3128 C  CA    B VAL A 1 399 ? 6.34500   6.79800   30.41500  0.250 23.50808  ? 399  VAL A CA    1 
ATOM   3129 C  C     . VAL A 1 399 ? 5.37800   7.97100   30.30100  1.000 24.56874  ? 399  VAL A C     1 
ATOM   3130 O  O     . VAL A 1 399 ? 5.68700   8.98100   29.66400  1.000 28.10337  ? 399  VAL A O     1 
ATOM   3131 C  CB    A VAL A 1 399 ? 7.35100   7.04600   31.57300  0.750 25.31883  ? 399  VAL A CB    1 
ATOM   3132 C  CB    B VAL A 1 399 ? 7.38400   6.99600   31.54300  0.250 24.00288  ? 399  VAL A CB    1 
ATOM   3133 C  CG1   A VAL A 1 399 ? 8.07300   5.75200   31.95100  0.750 25.39515  ? 399  VAL A CG1   1 
ATOM   3134 C  CG1   B VAL A 1 399 ? 8.03500   8.37800   31.47900  0.250 23.95550  ? 399  VAL A CG1   1 
ATOM   3135 C  CG2   A VAL A 1 399 ? 8.35200   8.14300   31.20600  0.750 24.30818  ? 399  VAL A CG2   1 
ATOM   3136 C  CG2   B VAL A 1 399 ? 6.76900   6.73600   32.89000  0.250 23.75022  ? 399  VAL A CG2   1 
ATOM   3137 N  N     . ASN A 1 400 ? 4.19200   7.82700   30.89400  1.000 28.58501  ? 400  ASN A N     1 
ATOM   3138 C  CA    . ASN A 1 400 ? 3.21800   8.91400   30.82300  1.000 31.42745  ? 400  ASN A CA    1 
ATOM   3139 C  C     . ASN A 1 400 ? 3.47800   10.02100  31.83900  1.000 30.94318  ? 400  ASN A C     1 
ATOM   3140 O  O     . ASN A 1 400 ? 3.02200   11.15200  31.62800  1.000 30.82738  ? 400  ASN A O     1 
ATOM   3141 C  CB    . ASN A 1 400 ? 1.78400   8.39000   30.93800  1.000 32.89605  ? 400  ASN A CB    1 
ATOM   3142 C  CG    . ASN A 1 400 ? 1.31600   7.69800   29.67400  1.000 35.40688  ? 400  ASN A CG    1 
ATOM   3143 O  OD1   . ASN A 1 400 ? 1.86600   7.91800   28.59100  1.000 37.11498  ? 400  ASN A OD1   1 
ATOM   3144 N  ND2   . ASN A 1 400 ? 0.28900   6.86600   29.80000  1.000 36.94127  ? 400  ASN A ND2   1 
ATOM   3145 N  N     . GLU A 1 401 ? 4.20100   9.72800   32.92400  1.000 31.31165  ? 401  GLU A N     1 
ATOM   3146 C  CA    . GLU A 1 401 ? 4.57900   10.72200  33.92100  1.000 33.44085  ? 401  GLU A CA    1 
ATOM   3147 C  C     . GLU A 1 401 ? 6.01500   10.46100  34.34300  1.000 30.77211  ? 401  GLU A C     1 
ATOM   3148 O  O     . GLU A 1 401 ? 6.43100   9.30500   34.44900  1.000 31.88277  ? 401  GLU A O     1 
ATOM   3149 C  CB    . GLU A 1 401 ? 3.69800   10.63800  35.17700  1.000 38.80202  ? 401  GLU A CB    1 
ATOM   3150 C  CG    . GLU A 1 401 ? 2.20300   10.60300  34.91600  1.000 48.81638  ? 401  GLU A CG    1 
ATOM   3151 C  CD    . GLU A 1 401 ? 1.39500   11.00700  36.13600  1.000 58.19645  ? 401  GLU A CD    1 
ATOM   3152 O  OE1   . GLU A 1 401 ? 1.08400   10.12800  36.96700  1.000 62.51013  ? 401  GLU A OE1   1 
ATOM   3153 O  OE2   . GLU A 1 401 ? 1.08300   12.21100  36.27000  1.000 60.92573  ? 401  GLU A OE2   1 
ATOM   3154 N  N     . LEU A 1 402 ? 6.77100   11.53000  34.59200  1.000 30.94318  ? 402  LEU A N     1 
ATOM   3155 C  CA    . LEU A 1 402 ? 8.16000   11.40300  35.03700  1.000 28.91136  ? 402  LEU A CA    1 
ATOM   3156 C  C     . LEU A 1 402 ? 8.47900   12.47000  36.07700  1.000 29.76936  ? 402  LEU A C     1 
ATOM   3157 O  O     . LEU A 1 402 ? 8.90800   13.58100  35.73900  1.000 29.34562  ? 402  LEU A O     1 
ATOM   3158 C  CB    . LEU A 1 402 ? 9.13200   11.46700  33.85700  1.000 27.22695  ? 402  LEU A CB    1 
ATOM   3159 C  CG    . LEU A 1 402 ? 10.58800  11.18900  34.23900  1.000 26.36895  ? 402  LEU A CG    1 
ATOM   3160 C  CD1   . LEU A 1 402 ? 10.69500  9.85700   34.95800  1.000 27.07167  ? 402  LEU A CD1   1 
ATOM   3161 C  CD2   . LEU A 1 402 ? 11.48900  11.20700  33.02400  1.000 26.51107  ? 402  LEU A CD2   1 
ATOM   3162 N  N     . PRO A 1 403 ? 8.28600   12.16300  37.36400  1.000 32.73550  ? 403  PRO A N     1 
ATOM   3163 C  CA    . PRO A 1 403 ? 8.57600   13.15400  38.41500  1.000 33.39348  ? 403  PRO A CA    1 
ATOM   3164 C  C     . PRO A 1 403 ? 10.07300  13.40500  38.54800  1.000 34.53835  ? 403  PRO A C     1 
ATOM   3165 O  O     . PRO A 1 403 ? 10.85900  12.47000  38.72200  1.000 35.71744  ? 403  PRO A O     1 
ATOM   3166 C  CB    . PRO A 1 403 ? 8.00600   12.50600  39.68500  1.000 34.58046  ? 403  PRO A CB    1 
ATOM   3167 C  CG    . PRO A 1 403 ? 7.01600   11.49900  39.20500  1.000 34.75943  ? 403  PRO A CG    1 
ATOM   3168 C  CD    . PRO A 1 403 ? 7.57100   10.98900  37.89000  1.000 32.43547  ? 403  PRO A CD    1 
ATOM   3169 N  N     . VAL A 1 404 ? 10.45800  14.68300  38.48900  1.000 34.23832  ? 404  VAL A N     1 
ATOM   3170 C  CA    . VAL A 1 404 ? 11.85200  15.10600  38.54300  1.000 31.96173  ? 404  VAL A CA    1 
ATOM   3171 C  C     . VAL A 1 404 ? 11.99700  16.26800  39.52200  1.000 33.46191  ? 404  VAL A C     1 
ATOM   3172 O  O     . VAL A 1 404 ? 11.03000  16.96000  39.84900  1.000 36.50174  ? 404  VAL A O     1 
ATOM   3173 C  CB    . VAL A 1 404 ? 12.39700  15.50300  37.14800  1.000 29.07717  ? 404  VAL A CB    1 
ATOM   3174 C  CG1   . VAL A 1 404 ? 12.44700  14.28800  36.20200  1.000 29.10349  ? 404  VAL A CG1   1 
ATOM   3175 C  CG2   . VAL A 1 404 ? 11.55100  16.62000  36.53400  1.000 29.75094  ? 404  VAL A CG2   1 
ATOM   3176 N  N     . THR A 1 405 ? 13.23200  16.48300  39.98400  1.000 34.81996  ? 405  THR A N     1 
ATOM   3177 C  CA    . THR A 1 405 ? 13.56500  17.61100  40.85500  1.000 35.91746  ? 405  THR A CA    1 
ATOM   3178 C  C     . THR A 1 405 ? 15.00700  18.02400  40.57700  1.000 34.30674  ? 405  THR A C     1 
ATOM   3179 O  O     . THR A 1 405 ? 15.67000  17.46400  39.70000  1.000 36.67282  ? 405  THR A O     1 
ATOM   3180 C  CB    . THR A 1 405 ? 13.29800  17.29400  42.32900  1.000 38.94677  ? 405  THR A CB    1 
ATOM   3181 O  OG1   . THR A 1 405 ? 13.47600  18.48500  43.10900  1.000 41.75237  ? 405  THR A OG1   1 
ATOM   3182 C  CG2   . THR A 1 405 ? 14.24200  16.21000  42.82200  1.000 37.60977  ? 405  THR A CG2   1 
ATOM   3183 N  N     . TRP A 1 406 ? 15.49200  19.01500  41.32300  1.000 35.05157  ? 406  TRP A N     1 
ATOM   3184 C  CA    . TRP A 1 406 ? 16.78500  19.62700  41.03500  1.000 37.05707  ? 406  TRP A CA    1 
ATOM   3185 C  C     . TRP A 1 406 ? 17.12900  20.60100  42.15700  1.000 41.89976  ? 406  TRP A C     1 
ATOM   3186 O  O     . TRP A 1 406 ? 16.27200  20.97400  42.96000  1.000 43.29466  ? 406  TRP A O     1 
ATOM   3187 C  CB    . TRP A 1 406 ? 16.75700  20.36700  39.69500  1.000 38.12299  ? 406  TRP A CB    1 
ATOM   3188 C  CG    . TRP A 1 406 ? 15.65400  21.38800  39.59300  1.000 36.31225  ? 406  TRP A CG    1 
ATOM   3189 C  CD1   . TRP A 1 406 ? 15.69000  22.68500  40.02600  1.000 38.37565  ? 406  TRP A CD1   1 
ATOM   3190 C  CD2   . TRP A 1 406 ? 14.35100  21.19400  39.02500  1.000 35.32792  ? 406  TRP A CD2   1 
ATOM   3191 N  NE1   . TRP A 1 406 ? 14.49500  23.30600  39.76300  1.000 37.10971  ? 406  TRP A NE1   1 
ATOM   3192 C  CE2   . TRP A 1 406 ? 13.65600  22.41400  39.14700  1.000 35.54110  ? 406  TRP A CE2   1 
ATOM   3193 C  CE3   . TRP A 1 406 ? 13.70900  20.11000  38.41900  1.000 36.25961  ? 406  TRP A CE3   1 
ATOM   3194 C  CZ2   . TRP A 1 406 ? 12.35100  22.57700  38.68700  1.000 35.32529  ? 406  TRP A CZ2   1 
ATOM   3195 C  CZ3   . TRP A 1 406 ? 12.41400  20.27200  37.96800  1.000 35.93852  ? 406  TRP A CZ3   1 
ATOM   3196 C  CH2   . TRP A 1 406 ? 11.74800  21.49600  38.10500  1.000 36.02274  ? 406  TRP A CH2   1 
ATOM   3197 N  N     . HIS A 1 407 ? 18.39800  21.01900  42.18300  1.000 49.60858  ? 407  HIS A N     1 
ATOM   3198 C  CA    . HIS A 1 407 ? 18.85000  22.08400  43.07500  1.000 56.59363  ? 407  HIS A CA    1 
ATOM   3199 C  C     . HIS A 1 407 ? 18.06800  23.35500  42.79500  1.000 65.34994  ? 407  HIS A C     1 
ATOM   3200 O  O     . HIS A 1 407 ? 18.09500  23.87400  41.67600  1.000 64.36298  ? 407  HIS A O     1 
ATOM   3201 C  CB    . HIS A 1 407 ? 20.34000  22.34700  42.83200  1.000 57.24371  ? 407  HIS A CB    1 
ATOM   3202 C  CG    . HIS A 1 407 ? 20.89500  23.52300  43.58500  1.000 57.90168  ? 407  HIS A CG    1 
ATOM   3203 N  ND1   . HIS A 1 407 ? 21.25000  24.70400  42.96600  1.000 56.46203  ? 407  HIS A ND1   1 
ATOM   3204 C  CD2   . HIS A 1 407 ? 21.18300  23.68900  44.89900  1.000 56.01461  ? 407  HIS A CD2   1 
ATOM   3205 C  CE1   . HIS A 1 407 ? 21.71800  25.55000  43.86600  1.000 56.03040  ? 407  HIS A CE1   1 
ATOM   3206 N  NE2   . HIS A 1 407 ? 21.68800  24.96000  45.04800  1.000 56.69627  ? 407  HIS A NE2   1 
ATOM   3207 N  N     . HIS A 1 408 ? 17.37700  23.85800  43.81000  1.000 74.18521  ? 408  HIS A N     1 
ATOM   3208 C  CA    . HIS A 1 408 ? 16.68000  25.12700  43.68200  1.000 81.42292  ? 408  HIS A CA    1 
ATOM   3209 C  C     . HIS A 1 408 ? 17.66900  26.25300  43.40200  1.000 71.72702  ? 408  HIS A C     1 
ATOM   3210 O  O     . HIS A 1 408 ? 17.55800  26.95200  42.39600  1.000 66.14477  ? 408  HIS A O     1 
ATOM   3211 C  CB    . HIS A 1 408 ? 15.88600  25.43800  44.94800  1.000 97.82752  ? 408  HIS A CB    1 
ATOM   3212 C  CG    . HIS A 1 408 ? 15.53300  26.88500  45.09100  1.000 100.64101 ? 408  HIS A CG    1 
ATOM   3213 N  ND1   . HIS A 1 408 ? 14.69800  27.53700  44.21000  1.000 100.53047 ? 408  HIS A ND1   1 
ATOM   3214 C  CD2   . HIS A 1 408 ? 15.91800  27.81000  46.00100  1.000 101.72799 ? 408  HIS A CD2   1 
ATOM   3215 C  CE1   . HIS A 1 408 ? 14.57500  28.80000  44.57700  1.000 100.97000 ? 408  HIS A CE1   1 
ATOM   3216 N  NE2   . HIS A 1 408 ? 15.30500  28.99200  45.66100  1.000 101.57007 ? 408  HIS A NE2   1 
HETATM 3217 C  CHA   . HEM B 2 .   ? 8.56400   6.46500   10.01900  1.000 15.15182  ? 501  HEM A CHA   1 
HETATM 3218 C  CHB   . HEM B 2 .   ? 10.75800  5.84800   14.29900  1.000 14.69124  ? 501  HEM A CHB   1 
HETATM 3219 C  CHC   . HEM B 2 .   ? 10.69800  10.65800  14.99900  1.000 16.16246  ? 501  HEM A CHC   1 
HETATM 3220 C  CHD   . HEM B 2 .   ? 7.77000   11.13200  11.13500  1.000 14.87284  ? 501  HEM A CHD   1 
HETATM 3221 C  C1A   . HEM B 2 .   ? 9.22600   5.88600   11.07900  1.000 14.43857  ? 501  HEM A C1A   1 
HETATM 3222 C  C2A   . HEM B 2 .   ? 9.61700   4.48300   11.18000  1.000 15.82032  ? 501  HEM A C2A   1 
HETATM 3223 C  C3A   . HEM B 2 .   ? 10.21700  4.32300   12.37100  1.000 14.70176  ? 501  HEM A C3A   1 
HETATM 3224 C  C4A   . HEM B 2 .   ? 10.22800  5.60600   13.05100  1.000 15.13603  ? 501  HEM A C4A   1 
HETATM 3225 C  CMA   . HEM B 2 .   ? 10.79100  3.01700   12.95900  1.000 15.43343  ? 501  HEM A CMA   1 
HETATM 3226 C  CAA   . HEM B 2 .   ? 9.41200   3.38200   10.10300  1.000 17.36524  ? 501  HEM A CAA   1 
HETATM 3227 C  CBA   . HEM B 2 .   ? 7.97300   2.92900   9.95000   1.000 19.44444  ? 501  HEM A CBA   1 
HETATM 3228 C  CGA   . HEM B 2 .   ? 7.84900   1.78300   8.97100   1.000 20.84460  ? 501  HEM A CGA   1 
HETATM 3229 O  O1A   . HEM B 2 .   ? 8.88100   1.25700   8.46100   1.000 20.07609  ? 501  HEM A O1A   1 
HETATM 3230 O  O2A   . HEM B 2 .   ? 6.68900   1.39300   8.69100   1.000 24.63453  ? 501  HEM A O2A   1 
HETATM 3231 C  C1B   . HEM B 2 .   ? 10.97300  7.09400   14.85500  1.000 15.20972  ? 501  HEM A C1B   1 
HETATM 3232 C  C2B   . HEM B 2 .   ? 11.72900  7.36400   16.06300  1.000 14.61754  ? 501  HEM A C2B   1 
HETATM 3233 C  C3B   . HEM B 2 .   ? 11.72100  8.68600   16.26900  1.000 15.40711  ? 501  HEM A C3B   1 
HETATM 3234 C  C4B   . HEM B 2 .   ? 10.94200  9.31000   15.19600  1.000 14.98074  ? 501  HEM A C4B   1 
HETATM 3235 C  CMB   . HEM B 2 .   ? 12.44500  6.30000   16.92700  1.000 17.07573  ? 501  HEM A CMB   1 
HETATM 3236 C  CAB   . HEM B 2 .   ? 12.44900  9.36600   17.45700  1.000 18.74962  ? 501  HEM A CAB   1 
HETATM 3237 C  CBB   . HEM B 2 .   ? 12.23700  10.62100  17.83800  1.000 22.86590  ? 501  HEM A CBB   1 
HETATM 3238 C  C1C   . HEM B 2 .   ? 9.88900   11.21700  14.02100  1.000 13.90167  ? 501  HEM A C1C   1 
HETATM 3239 C  C2C   . HEM B 2 .   ? 9.56000   12.62300  13.89000  1.000 14.78862  ? 501  HEM A C2C   1 
HETATM 3240 C  C3C   . HEM B 2 .   ? 8.73500   12.76200  12.84600  1.000 14.73335  ? 501  HEM A C3C   1 
HETATM 3241 C  C4C   . HEM B 2 .   ? 8.53600   11.45000  12.24100  1.000 14.70966  ? 501  HEM A C4C   1 
HETATM 3242 C  CMC   . HEM B 2 .   ? 10.05400  13.74300  14.84400  1.000 16.65463  ? 501  HEM A CMC   1 
HETATM 3243 C  CAC   . HEM B 2 .   ? 8.14900   14.11000  12.38700  1.000 16.48619  ? 501  HEM A CAC   1 
HETATM 3244 C  CBC   . HEM B 2 .   ? 6.98500   14.17200  11.75500  1.000 20.58668  ? 501  HEM A CBC   1 
HETATM 3245 C  C1D   . HEM B 2 .   ? 7.73100   9.90200   10.49800  1.000 15.00969  ? 501  HEM A C1D   1 
HETATM 3246 C  C2D   . HEM B 2 .   ? 7.00500   9.61300   9.27700   1.000 15.49396  ? 501  HEM A C2D   1 
HETATM 3247 C  C3D   . HEM B 2 .   ? 7.21600   8.32400   8.97000   1.000 17.13363  ? 501  HEM A C3D   1 
HETATM 3248 C  C4D   . HEM B 2 .   ? 8.09300   7.76300   9.98200   1.000 15.81769  ? 501  HEM A C4D   1 
HETATM 3249 C  CMD   . HEM B 2 .   ? 6.13900   10.63400  8.50600   1.000 17.83898  ? 501  HEM A CMD   1 
HETATM 3250 C  CAD   . HEM B 2 .   ? 6.66500   7.54200   7.75400   1.000 17.81529  ? 501  HEM A CAD   1 
HETATM 3251 C  CBD   . HEM B 2 .   ? 7.74300   7.47200   6.67600   1.000 16.37828  ? 501  HEM A CBD   1 
HETATM 3252 C  CGD   . HEM B 2 .   ? 7.27900   6.68100   5.47000   1.000 16.86781  ? 501  HEM A CGD   1 
HETATM 3253 O  O1D   . HEM B 2 .   ? 7.78200   6.93000   4.33800   1.000 19.98397  ? 501  HEM A O1D   1 
HETATM 3254 O  O2D   . HEM B 2 .   ? 6.38800   5.80300   5.59600   1.000 19.15230  ? 501  HEM A O2D   1 
HETATM 3255 N  NA    . HEM B 2 .   ? 9.62800   6.54100   12.22900  1.000 14.40173  ? 501  HEM A NA    1 
HETATM 3256 N  NB    . HEM B 2 .   ? 10.49600  8.29400   14.36400  1.000 13.95430  ? 501  HEM A NB    1 
HETATM 3257 N  NC    . HEM B 2 .   ? 9.26100   10.53300  12.98500  1.000 14.78598  ? 501  HEM A NC    1 
HETATM 3258 N  ND    . HEM B 2 .   ? 8.37300   8.74600   10.91300  1.000 15.00180  ? 501  HEM A ND    1 
HETATM 3259 FE FE    . HEM B 2 .   ? 9.64900   8.59200   12.50000  1.000 15.35184  ? 501  HEM A FE    1 
HETATM 3260 C  C     A TRS C 3 .   ? 26.14900  -2.88100  6.93600   0.470 25.73730  ? 502  TRS A C     1 
HETATM 3261 C  C     B TRS C 3 .   ? 26.08200  -3.04600  6.54300   0.530 31.45114  ? 502  TRS A C     1 
HETATM 3262 C  C1    A TRS C 3 .   ? 25.38100  -2.39900  8.17400   0.470 23.95550  ? 502  TRS A C1    1 
HETATM 3263 C  C1    B TRS C 3 .   ? 25.53000  -4.37600  6.01400   0.530 33.73826  ? 502  TRS A C1    1 
HETATM 3264 C  C2    A TRS C 3 .   ? 27.60700  -3.21600  7.24400   0.470 27.97177  ? 502  TRS A C2    1 
HETATM 3265 C  C2    B TRS C 3 .   ? 27.50100  -3.16600  7.09700   0.530 32.84604  ? 502  TRS A C2    1 
HETATM 3266 C  C3    A TRS C 3 .   ? 25.48200  -4.08400  6.27300   0.470 24.28186  ? 502  TRS A C3    1 
HETATM 3267 C  C3    B TRS C 3 .   ? 26.04000  -1.93600  5.49400   0.530 25.89784  ? 502  TRS A C3    1 
HETATM 3268 N  N     A TRS C 3 .   ? 26.14200  -1.74600  5.95000   0.470 27.20326  ? 502  TRS A N     1 
HETATM 3269 N  N     B TRS C 3 .   ? 25.17900  -2.61900  7.66600   0.530 34.28569  ? 502  TRS A N     1 
HETATM 3270 O  O1    A TRS C 3 .   ? 25.39200  -3.44800  9.10200   0.470 19.23389  ? 502  TRS A O1    1 
HETATM 3271 O  O1    B TRS C 3 .   ? 24.25100  -4.13400  5.49200   0.530 34.61204  ? 502  TRS A O1    1 
HETATM 3272 O  O2    A TRS C 3 .   ? 28.29000  -2.05500  7.64200   0.470 29.37721  ? 502  TRS A O2    1 
HETATM 3273 O  O2    B TRS C 3 .   ? 27.75000  -4.49700  7.48100   0.530 34.47519  ? 502  TRS A O2    1 
HETATM 3274 O  O3    A TRS C 3 .   ? 24.24900  -3.68700  5.72100   0.470 21.97895  ? 502  TRS A O3    1 
HETATM 3275 O  O3    B TRS C 3 .   ? 26.94200  -2.25100  4.46900   0.530 22.85537  ? 502  TRS A O3    1 
HETATM 3276 C  C1    . FLF D 4 .   ? -0.53400  6.62000   11.82000  0.750 30.62736  ? 503  FLF A C1    1 
HETATM 3277 O  O1    . FLF D 4 .   ? 0.72200   4.64400   11.51200  0.750 32.93816  ? 503  FLF A O1    1 
HETATM 3278 C  C2    . FLF D 4 .   ? -1.72400  7.27400   11.50200  0.750 31.33534  ? 503  FLF A C2    1 
HETATM 3279 C  C3    . FLF D 4 .   ? -2.07800  8.48900   12.06600  0.750 29.81936  ? 503  FLF A C3    1 
HETATM 3280 O  O2    . FLF D 4 .   ? -1.05200  4.94000   10.21500  0.750 34.54362  ? 503  FLF A O2    1 
HETATM 3281 C  C4    . FLF D 4 .   ? -1.21200  9.06800   12.98400  0.750 29.62987  ? 503  FLF A C4    1 
HETATM 3282 C  C5    . FLF D 4 .   ? -0.02200  8.44700   13.32200  0.750 28.90347  ? 503  FLF A C5    1 
HETATM 3283 C  C6    . FLF D 4 .   ? 0.34700   7.21500   12.76200  0.750 28.41130  ? 503  FLF A C6    1 
HETATM 3284 C  C7    . FLF D 4 .   ? -0.26000  5.29200   11.13200  0.750 31.90119  ? 503  FLF A C7    1 
HETATM 3285 N  N     . FLF D 4 .   ? 1.53400   6.57000   13.07700  0.750 25.65044  ? 503  FLF A N     1 
HETATM 3286 C  "C1'" . FLF D 4 .   ? 2.51300   6.83300   14.02100  0.750 24.17658  ? 503  FLF A "C1'" 1 
HETATM 3287 C  "C2'" . FLF D 4 .   ? 3.83400   6.49600   13.68700  0.750 22.92906  ? 503  FLF A "C2'" 1 
HETATM 3288 C  "C3'" . FLF D 4 .   ? 4.87000   6.71900   14.58600  0.750 23.01592  ? 503  FLF A "C3'" 1 
HETATM 3289 C  "C4'" . FLF D 4 .   ? 4.63800   7.27900   15.83400  0.750 23.08171  ? 503  FLF A "C4'" 1 
HETATM 3290 C  "C5'" . FLF D 4 .   ? 3.34500   7.61500   16.18700  0.750 18.68645  ? 503  FLF A "C5'" 1 
HETATM 3291 C  "C6'" . FLF D 4 .   ? 2.29700   7.39800   15.29600  0.750 23.59230  ? 503  FLF A "C6'" 1 
HETATM 3292 C  "C7'" . FLF D 4 .   ? 6.26300   6.34300   14.18200  0.750 28.33761  ? 503  FLF A "C7'" 1 
HETATM 3293 F  F1    . FLF D 4 .   ? 7.06700   7.39000   13.99100  0.750 30.18783  ? 503  FLF A F1    1 
HETATM 3294 F  F2    . FLF D 4 .   ? 6.85600   5.57800   15.10700  0.750 32.72234  ? 503  FLF A F2    1 
HETATM 3295 F  F3    . FLF D 4 .   ? 6.29300   5.62800   13.05200  0.750 28.49289  ? 503  FLF A F3    1 
HETATM 3296 C  C1    . EDO E 5 .   ? 0.20800   4.05100   16.99200  1.000 49.68227  ? 504  EDO A C1    1 
HETATM 3297 O  O1    . EDO E 5 .   ? -0.23300  5.00100   16.04700  1.000 52.79317  ? 504  EDO A O1    1 
HETATM 3298 C  C2    . EDO E 5 .   ? 0.25700   2.69900   16.32900  1.000 45.53177  ? 504  EDO A C2    1 
HETATM 3299 O  O2    . EDO E 5 .   ? 0.96100   2.82900   15.11400  1.000 47.73730  ? 504  EDO A O2    1 
HETATM 3300 C  C1    . EDO F 5 .   ? 22.25000  -17.22900 14.49500  1.000 58.72546  ? 505  EDO A C1    1 
HETATM 3301 O  O1    . EDO F 5 .   ? 21.20000  -17.08200 13.56400  1.000 55.08029  ? 505  EDO A O1    1 
HETATM 3302 C  C2    . EDO F 5 .   ? 22.14600  -16.16900 15.56600  1.000 60.68096  ? 505  EDO A C2    1 
HETATM 3303 O  O2    . EDO F 5 .   ? 22.25900  -16.74100 16.85200  1.000 62.37590  ? 505  EDO A O2    1 
HETATM 3304 C  C1    . EDO G 5 .   ? -1.40100  -10.42300 1.21500   1.000 55.73563  ? 506  EDO A C1    1 
HETATM 3305 O  O1    . EDO G 5 .   ? -0.79300  -11.04100 0.10500   1.000 57.79904  ? 506  EDO A O1    1 
HETATM 3306 C  C2    . EDO G 5 .   ? -2.81200  -10.93400 1.35000   1.000 53.42746  ? 506  EDO A C2    1 
HETATM 3307 O  O2    . EDO G 5 .   ? -3.22100  -10.86600 2.69600   1.000 51.06665  ? 506  EDO A O2    1 
HETATM 3308 C  C1    . EDO H 5 .   ? 29.04100  2.54300   32.80800  1.000 64.21559  ? 507  EDO A C1    1 
HETATM 3309 O  O1    . EDO H 5 .   ? 30.02100  3.36400   32.21100  1.000 65.93422  ? 507  EDO A O1    1 
HETATM 3310 C  C2    . EDO H 5 .   ? 27.69800  3.23400   32.86500  1.000 60.56252  ? 507  EDO A C2    1 
HETATM 3311 O  O2    . EDO H 5 .   ? 27.78000  4.47600   33.52900  1.000 57.18317  ? 507  EDO A O2    1 
HETATM 3312 C  C1    . EDO I 5 .   ? 23.16800  -0.98000  35.72400  1.000 81.07814  ? 508  EDO A C1    1 
HETATM 3313 O  O1    . EDO I 5 .   ? 21.84300  -1.13200  35.26900  1.000 81.78612  ? 508  EDO A O1    1 
HETATM 3314 C  C2    . EDO I 5 .   ? 23.45700  0.48100   35.95900  1.000 80.67809  ? 508  EDO A C2    1 
HETATM 3315 O  O2    . EDO I 5 .   ? 24.73200  0.80400   35.45100  1.000 80.61230  ? 508  EDO A O2    1 
HETATM 3316 O  O     . HOH J 6 .   ? 3.63100   -20.23000 7.86900   1.000 44.26320  ? 601  HOH A O     1 
HETATM 3317 O  O     . HOH J 6 .   ? -8.76800  2.86100   4.52600   1.000 55.14609  ? 602  HOH A O     1 
HETATM 3318 O  O     . HOH J 6 .   ? 2.17500   13.33800  32.07000  1.000 46.35293  ? 603  HOH A O     1 
HETATM 3319 O  O     . HOH J 6 .   ? 2.50100   -19.11800 -1.24800  1.000 47.62676  ? 604  HOH A O     1 
HETATM 3320 O  O     . HOH J 6 .   ? 28.76200  -5.44600  5.40500   1.000 48.52161  ? 605  HOH A O     1 
HETATM 3321 O  O     . HOH J 6 .   ? 25.64900  -7.28400  26.12500  1.000 34.32517  ? 606  HOH A O     1 
HETATM 3322 O  O     . HOH J 6 .   ? 17.39000  3.64800   4.04100   1.000 20.33139  ? 607  HOH A O     1 
HETATM 3323 O  O     . HOH J 6 .   ? 29.44600  9.78600   21.46500  1.000 47.91890  ? 608  HOH A O     1 
HETATM 3324 O  O     . HOH J 6 .   ? -5.16100  -7.75200  10.07900  1.000 43.93158  ? 609  HOH A O     1 
HETATM 3325 O  O     . HOH J 6 .   ? 5.92300   -20.70900 6.06400   1.000 31.73012  ? 610  HOH A O     1 
HETATM 3326 O  O     . HOH J 6 .   ? 1.60200   19.46100  28.64500  1.000 43.13412  ? 611  HOH A O     1 
HETATM 3327 O  O     . HOH J 6 .   ? 26.86200  0.32000   34.12500  1.000 48.13735  ? 612  HOH A O     1 
HETATM 3328 O  O     . HOH J 6 .   ? 14.13700  -10.88000 0.97400   1.000 39.92847  ? 613  HOH A O     1 
HETATM 3329 O  O     . HOH J 6 .   ? 25.21200  23.59400  25.10800  1.000 42.94989  ? 614  HOH A O     1 
HETATM 3330 O  O     . HOH J 6 .   ? 7.14200   -11.65600 23.07600  1.000 33.65404  ? 615  HOH A O     1 
HETATM 3331 O  O     . HOH J 6 .   ? 5.35200   1.20100   6.50700   1.000 25.98469  ? 616  HOH A O     1 
HETATM 3332 O  O     . HOH J 6 .   ? 13.90200  -6.97800  31.02600  1.000 42.28139  ? 617  HOH A O     1 
HETATM 3333 O  O     . HOH J 6 .   ? 3.27700   -25.33300 18.49400  1.000 29.77199  ? 618  HOH A O     1 
HETATM 3334 O  O     . HOH J 6 .   ? 3.08900   5.16800   31.51900  1.000 34.16989  ? 619  HOH A O     1 
HETATM 3335 O  O     . HOH J 6 .   ? 6.95700   24.66400  7.27900   1.000 28.81398  ? 620  HOH A O     1 
HETATM 3336 O  O     . HOH J 6 .   ? 6.09400   24.11100  33.53300  1.000 31.41166  ? 621  HOH A O     1 
HETATM 3337 O  O     . HOH J 6 .   ? -15.26200 20.05000  5.14900   1.000 55.21188  ? 622  HOH A O     1 
HETATM 3338 O  O     . HOH J 6 .   ? 21.69500  6.06800   39.03400  1.000 49.13484  ? 623  HOH A O     1 
HETATM 3339 O  O     . HOH J 6 .   ? -2.00100  5.65800   7.90500   1.000 52.84318  ? 624  HOH A O     1 
HETATM 3340 O  O     . HOH J 6 .   ? -13.20100 30.01200  5.50100   1.000 46.78719  ? 625  HOH A O     1 
HETATM 3341 O  O     . HOH J 6 .   ? 20.39400  -18.12100 9.77700   1.000 45.14225  ? 626  HOH A O     1 
HETATM 3342 O  O     . HOH J 6 .   ? 7.31200   9.99800   27.82400  1.000 38.81781  ? 627  HOH A O     1 
HETATM 3343 O  O     . HOH J 6 .   ? 23.98200  1.36200   7.12800   1.000 29.24298  ? 628  HOH A O     1 
HETATM 3344 O  O     . HOH J 6 .   ? 8.70100   17.66700  16.62900  1.000 19.96029  ? 629  HOH A O     1 
HETATM 3345 O  O     . HOH J 6 .   ? 4.71600   27.73300  9.63700   1.000 37.33342  ? 630  HOH A O     1 
HETATM 3346 O  O     . HOH J 6 .   ? -1.44400  0.00800   23.64400  1.000 31.53273  ? 631  HOH A O     1 
HETATM 3347 O  O     . HOH J 6 .   ? 12.36100  31.15300  17.14700  1.000 51.47722  ? 632  HOH A O     1 
HETATM 3348 O  O     . HOH J 6 .   ? 2.08500   26.74500  14.98800  1.000 27.54278  ? 633  HOH A O     1 
HETATM 3349 O  O     . HOH J 6 .   ? 0.28500   14.14900  23.03800  1.000 30.57472  ? 634  HOH A O     1 
HETATM 3350 O  O     . HOH J 6 .   ? -0.03000  3.47600   27.63100  1.000 39.05995  ? 635  HOH A O     1 
HETATM 3351 O  O     . HOH J 6 .   ? 29.21800  15.77700  35.70800  1.000 47.67940  ? 636  HOH A O     1 
HETATM 3352 O  O     . HOH J 6 .   ? 16.88500  15.18300  6.53400   1.000 36.67545  ? 637  HOH A O     1 
HETATM 3353 O  O     . HOH J 6 .   ? -3.06600  34.80600  2.68400   1.000 54.91974  ? 638  HOH A O     1 
HETATM 3354 O  O     . HOH J 6 .   ? 8.34200   18.17100  -0.82500  1.000 39.29682  ? 639  HOH A O     1 
HETATM 3355 O  O     . HOH J 6 .   ? -1.61000  -3.72100  25.56900  1.000 35.09105  ? 640  HOH A O     1 
HETATM 3356 O  O     . HOH J 6 .   ? 1.16800   11.12800  24.77500  1.000 49.43487  ? 641  HOH A O     1 
HETATM 3357 O  O     . HOH J 6 .   ? 19.36200  -9.51100  17.23800  1.000 21.39467  ? 642  HOH A O     1 
HETATM 3358 O  O     . HOH J 6 .   ? 20.86200  19.88600  9.08200   1.000 26.39527  ? 643  HOH A O     1 
HETATM 3359 O  O     . HOH J 6 .   ? 17.22100  6.62700   36.41400  1.000 32.41968  ? 644  HOH A O     1 
HETATM 3360 O  O     . HOH J 6 .   ? 15.74100  5.59000   2.90300   1.000 24.08447  ? 645  HOH A O     1 
HETATM 3361 O  O     . HOH J 6 .   ? -11.76300 20.48600  -0.43600  1.000 39.97585  ? 646  HOH A O     1 
HETATM 3362 O  O     . HOH J 6 .   ? -7.22500  6.03700   24.20300  1.000 56.14621  ? 647  HOH A O     1 
HETATM 3363 O  O     . HOH J 6 .   ? 21.35700  15.65400  36.06700  1.000 39.25734  ? 648  HOH A O     1 
HETATM 3364 O  O     . HOH J 6 .   ? 3.83800   -17.09600 10.64100  1.000 37.29658  ? 649  HOH A O     1 
HETATM 3365 O  O     . HOH J 6 .   ? 23.73400  -5.55400  9.13700   1.000 25.22145  ? 650  HOH A O     1 
HETATM 3366 O  O     . HOH J 6 .   ? 12.66300  -4.36400  23.08400  1.000 39.86004  ? 651  HOH A O     1 
HETATM 3367 O  O     . HOH J 6 .   ? 4.13300   -6.05500  -1.73200  1.000 32.86183  ? 652  HOH A O     1 
HETATM 3368 O  O     . HOH J 6 .   ? -0.02400  10.36700  2.58600   1.000 27.38749  ? 653  HOH A O     1 
HETATM 3369 O  O     . HOH J 6 .   ? 22.58800  11.98900  16.49500  1.000 20.44719  ? 654  HOH A O     1 
HETATM 3370 O  O     . HOH J 6 .   ? 2.17000   23.49400  26.26900  1.000 28.62448  ? 655  HOH A O     1 
HETATM 3371 O  O     . HOH J 6 .   ? 19.75700  -13.79300 10.16200  1.000 31.41166  ? 656  HOH A O     1 
HETATM 3372 O  O     . HOH J 6 .   ? -7.11000  23.71400  -2.06200  1.000 24.19237  ? 657  HOH A O     1 
HETATM 3373 O  O     . HOH J 6 .   ? 21.20000  13.78900  39.35600  1.000 42.43140  ? 658  HOH A O     1 
HETATM 3374 O  O     . HOH J 6 .   ? -8.71300  11.08000  6.80400   1.000 33.46454  ? 659  HOH A O     1 
HETATM 3375 O  O     . HOH J 6 .   ? 30.03700  2.90100   7.72900   1.000 53.32745  ? 660  HOH A O     1 
HETATM 3376 O  O     . HOH J 6 .   ? 8.77400   4.80700   -2.42600  1.000 27.51646  ? 661  HOH A O     1 
HETATM 3377 O  O     . HOH J 6 .   ? -12.97100 17.43400  16.21300  1.000 35.23317  ? 662  HOH A O     1 
HETATM 3378 O  O     . HOH J 6 .   ? 14.52100  -18.07800 15.37300  1.000 55.24610  ? 663  HOH A O     1 
HETATM 3379 O  O     . HOH J 6 .   ? -0.92700  -2.21600  18.89600  1.000 40.09165  ? 664  HOH A O     1 
HETATM 3380 O  O     . HOH J 6 .   ? 11.05100  16.26200  23.90000  1.000 23.93708  ? 665  HOH A O     1 
HETATM 3381 O  O     . HOH J 6 .   ? 16.73500  10.33000  42.27000  1.000 46.79508  ? 666  HOH A O     1 
HETATM 3382 O  O     . HOH J 6 .   ? 8.43900   -21.99300 16.36100  1.000 41.48129  ? 667  HOH A O     1 
HETATM 3383 O  O     . HOH J 6 .   ? -1.81600  1.85500   25.47500  1.000 39.66791  ? 668  HOH A O     1 
HETATM 3384 O  O     . HOH J 6 .   ? 18.44900  4.33200   39.79300  1.000 49.73228  ? 669  HOH A O     1 
HETATM 3385 O  O     . HOH J 6 .   ? 2.71600   10.96800  27.06600  1.000 69.95049  ? 670  HOH A O     1 
HETATM 3386 O  O     . HOH J 6 .   ? 12.42600  2.16600   17.13800  1.000 17.73897  ? 671  HOH A O     1 
HETATM 3387 O  O     . HOH J 6 .   ? 6.00700   -0.21000  0.99800   1.000 21.59733  ? 672  HOH A O     1 
HETATM 3388 O  O     . HOH J 6 .   ? 10.96300  0.74800   4.52200   1.000 22.87116  ? 673  HOH A O     1 
HETATM 3389 O  O     . HOH J 6 .   ? 4.92900   9.98300   23.64600  1.000 37.84138  ? 674  HOH A O     1 
HETATM 3390 O  O     . HOH J 6 .   ? 8.02400   -4.02500  23.96200  1.000 29.27193  ? 675  HOH A O     1 
HETATM 3391 O  O     . HOH J 6 .   ? 22.44200  9.64900   38.42600  1.000 35.27265  ? 676  HOH A O     1 
HETATM 3392 O  O     . HOH J 6 .   ? 6.66000   -1.94700  26.80400  1.000 27.89545  ? 677  HOH A O     1 
HETATM 3393 O  O     . HOH J 6 .   ? -8.71700  9.26300   -0.56300  1.000 29.15613  ? 678  HOH A O     1 
HETATM 3394 O  O     . HOH J 6 .   ? -0.57300  -8.88400  19.46900  1.000 27.01640  ? 679  HOH A O     1 
HETATM 3395 O  O     . HOH J 6 .   ? -1.74500  17.74300  -11.96200 1.000 32.31177  ? 680  HOH A O     1 
HETATM 3396 O  O     . HOH J 6 .   ? 1.72000   -6.19800  25.30200  1.000 44.56324  ? 681  HOH A O     1 
HETATM 3397 O  O     . HOH J 6 .   ? 7.39900   24.21300  31.01600  1.000 28.37972  ? 682  HOH A O     1 
HETATM 3398 O  O     . HOH J 6 .   ? 2.22100   -23.91300 20.79900  1.000 35.66480  ? 683  HOH A O     1 
HETATM 3399 O  O     . HOH J 6 .   ? 22.13100  18.81700  16.07900  1.000 30.29311  ? 684  HOH A O     1 
HETATM 3400 O  O     . HOH J 6 .   ? 7.96800   -4.39600  21.14300  1.000 33.60666  ? 685  HOH A O     1 
HETATM 3401 O  O     . HOH J 6 .   ? -14.07000 13.23000  22.02600  1.000 49.06378  ? 686  HOH A O     1 
HETATM 3402 O  O     . HOH J 6 .   ? -12.88900 15.46500  4.48800   1.000 56.41466  ? 687  HOH A O     1 
HETATM 3403 O  O     . HOH J 6 .   ? -12.62300 26.30300  9.23400   1.000 47.13460  ? 688  HOH A O     1 
HETATM 3404 O  O     . HOH J 6 .   ? 22.06500  -8.94400  28.82900  1.000 49.29802  ? 689  HOH A O     1 
HETATM 3405 O  O     . HOH J 6 .   ? 11.37700  -21.81300 10.18000  1.000 42.85514  ? 690  HOH A O     1 
HETATM 3406 O  O     . HOH J 6 .   ? -2.22000  27.94400  1.78900   1.000 23.77917  ? 691  HOH A O     1 
HETATM 3407 O  O     . HOH J 6 .   ? 3.93100   14.09300  -5.73100  1.000 32.43810  ? 692  HOH A O     1 
HETATM 3408 O  O     . HOH J 6 .   ? 34.07400  13.45300  28.68400  1.000 45.35281  ? 693  HOH A O     1 
HETATM 3409 O  O     . HOH J 6 .   ? 1.81800   -26.52300 25.56700  1.000 35.90694  ? 694  HOH A O     1 
HETATM 3410 O  O     . HOH J 6 .   ? 21.81600  24.75800  26.04900  1.000 35.69375  ? 695  HOH A O     1 
HETATM 3411 O  O     . HOH J 6 .   ? -2.96200  -6.43300  22.28400  1.000 42.36561  ? 696  HOH A O     1 
HETATM 3412 O  O     . HOH J 6 .   ? 21.12400  3.44900   10.47400  1.000 21.71576  ? 697  HOH A O     1 
HETATM 3413 O  O     . HOH J 6 .   ? 14.52900  -15.48800 16.46500  1.000 39.71266  ? 698  HOH A O     1 
HETATM 3414 O  O     . HOH J 6 .   ? 6.84100   -1.91700  2.86500   1.000 20.39192  ? 699  HOH A O     1 
HETATM 3415 O  O     . HOH J 6 .   ? 10.66600  -3.49200  23.90000  1.000 37.05181  ? 700  HOH A O     1 
HETATM 3416 O  O     . HOH J 6 .   ? 17.24400  3.43000   11.44200  1.000 14.23329  ? 701  HOH A O     1 
HETATM 3417 O  O     . HOH J 6 .   ? 2.46700   27.22200  3.10600   1.000 28.80872  ? 702  HOH A O     1 
HETATM 3418 O  O     . HOH J 6 .   ? 11.91300  6.87000   0.46600   1.000 26.84269  ? 703  HOH A O     1 
HETATM 3419 O  O     . HOH J 6 .   ? 22.49600  -9.78400  11.48200  1.000 23.95024  ? 704  HOH A O     1 
HETATM 3420 O  O     . HOH J 6 .   ? 27.63600  -3.29800  10.72400  1.000 60.77834  ? 705  HOH A O     1 
HETATM 3421 O  O     . HOH J 6 .   ? -1.58200  0.29200   0.84500   1.000 39.37841  ? 706  HOH A O     1 
HETATM 3422 O  O     . HOH J 6 .   ? 14.21200  9.41900   5.70900   1.000 25.20302  ? 707  HOH A O     1 
HETATM 3423 O  O     . HOH J 6 .   ? 19.91600  16.70400  12.39800  1.000 23.34227  ? 708  HOH A O     1 
HETATM 3424 O  O     . HOH J 6 .   ? -2.26000  7.48100   -3.24800  1.000 45.03172  ? 709  HOH A O     1 
HETATM 3425 O  O     . HOH J 6 .   ? 19.55500  26.50500  6.14800   1.000 44.69220  ? 710  HOH A O     1 
HETATM 3426 O  O     . HOH J 6 .   ? -7.18700  2.34600   27.71700  1.000 49.77439  ? 711  HOH A O     1 
HETATM 3427 O  O     . HOH J 6 .   ? 18.75600  -12.54600 5.79900   1.000 53.95910  ? 712  HOH A O     1 
HETATM 3428 O  O     . HOH J 6 .   ? -5.94400  13.14600  -5.60500  1.000 56.80944  ? 713  HOH A O     1 
HETATM 3429 O  O     . HOH J 6 .   ? 26.80300  19.02700  21.17200  1.000 27.56909  ? 714  HOH A O     1 
HETATM 3430 O  O     . HOH J 6 .   ? 14.17900  15.92700  2.73800   1.000 27.96914  ? 715  HOH A O     1 
HETATM 3431 O  O     . HOH J 6 .   ? 4.58800   -21.56100 10.20600  1.000 45.81339  ? 716  HOH A O     1 
HETATM 3432 O  O     . HOH J 6 .   ? 10.74700  22.84300  7.71000   1.000 40.46801  ? 717  HOH A O     1 
HETATM 3433 O  O     . HOH J 6 .   ? 20.95100  17.32900  33.63000  1.000 44.76326  ? 718  HOH A O     1 
HETATM 3434 O  O     . HOH J 6 .   ? 13.17100  22.50200  0.95100   1.000 39.99427  ? 719  HOH A O     1 
HETATM 3435 O  O     . HOH J 6 .   ? -2.00200  28.30800  10.85100  1.000 27.35591  ? 720  HOH A O     1 
HETATM 3436 O  O     . HOH J 6 .   ? 2.30100   -4.03500  -2.62100  1.000 40.37589  ? 721  HOH A O     1 
HETATM 3437 O  O     . HOH J 6 .   ? -4.38900  27.83100  0.05000   1.000 27.77701  ? 722  HOH A O     1 
HETATM 3438 O  O     . HOH J 6 .   ? 23.38500  -11.37000 19.26600  1.000 32.12227  ? 723  HOH A O     1 
HETATM 3439 O  O     . HOH J 6 .   ? 5.05600   20.64700  0.15900   1.000 50.33235  ? 724  HOH A O     1 
HETATM 3440 O  O     . HOH J 6 .   ? -10.70200 8.42800   22.58100  1.000 34.95156  ? 725  HOH A O     1 
HETATM 3441 O  O     . HOH J 6 .   ? 0.55700   -22.75400 25.48300  1.000 54.10386  ? 726  HOH A O     1 
HETATM 3442 O  O     . HOH J 6 .   ? -8.90600  16.17900  22.77800  1.000 32.43810  ? 727  HOH A O     1 
HETATM 3443 O  O     . HOH J 6 .   ? 14.34800  28.66100  13.15900  1.000 31.39587  ? 728  HOH A O     1 
HETATM 3444 O  O     . HOH J 6 .   ? 31.46200  20.60100  28.38300  1.000 49.35329  ? 729  HOH A O     1 
HETATM 3445 O  O     . HOH J 6 .   ? 6.12800   7.21100   -7.18000  1.000 34.02250  ? 730  HOH A O     1 
HETATM 3446 O  O     . HOH J 6 .   ? -10.97000 33.76900  0.13400   1.000 26.25052  ? 731  HOH A O     1 
HETATM 3447 O  O     . HOH J 6 .   ? 3.21500   -1.87200  12.09500  1.000 45.20542  ? 732  HOH A O     1 
HETATM 3448 O  O     . HOH J 6 .   ? -8.43700  16.73800  -4.50600  1.000 45.06856  ? 733  HOH A O     1 
HETATM 3449 O  O     . HOH J 6 .   ? 29.35700  12.48000  18.72500  1.000 29.31930  ? 734  HOH A O     1 
HETATM 3450 O  O     . HOH J 6 .   ? 6.57100   28.97000  35.64500  1.000 48.53740  ? 735  HOH A O     1 
HETATM 3451 O  O     . HOH J 6 .   ? 20.83700  22.58500  38.40200  1.000 33.43822  ? 736  HOH A O     1 
HETATM 3452 O  O     . HOH J 6 .   ? 1.39500   11.63100  29.21300  1.000 47.74783  ? 737  HOH A O     1 
HETATM 3453 O  O     . HOH J 6 .   ? 18.58800  2.06500   8.44500   1.000 14.94653  ? 738  HOH A O     1 
HETATM 3454 O  O     . HOH J 6 .   ? 7.30800   1.49500   27.46500  1.000 22.59218  ? 739  HOH A O     1 
HETATM 3455 O  O     . HOH J 6 .   ? 20.10300  -0.17700  9.21800   1.000 17.22575  ? 740  HOH A O     1 
HETATM 3456 O  O     . HOH J 6 .   ? 11.50000  1.39400   7.42200   1.000 19.60761  ? 741  HOH A O     1 
HETATM 3457 O  O     . HOH J 6 .   ? 4.25100   23.54800  -3.05500  1.000 53.00636  ? 742  HOH A O     1 
HETATM 3458 O  O     . HOH J 6 .   ? 19.94300  29.89000  18.60700  1.000 35.54374  ? 743  HOH A O     1 
HETATM 3459 O  O     . HOH J 6 .   ? 11.00800  9.22500   -3.73800  1.000 49.64016  ? 744  HOH A O     1 
HETATM 3460 O  O     . HOH J 6 .   ? 17.34300  30.60900  19.50400  1.000 34.20410  ? 745  HOH A O     1 
HETATM 3461 O  O     . HOH J 6 .   ? -0.17800  -13.79000 9.49100   1.000 43.60260  ? 746  HOH A O     1 
HETATM 3462 O  O     . HOH J 6 .   ? 6.13900   -2.76700  -2.04900  1.000 28.72186  ? 747  HOH A O     1 
HETATM 3463 O  O     . HOH J 6 .   ? 5.81800   -0.45600  34.22300  1.000 33.01712  ? 748  HOH A O     1 
HETATM 3464 O  O     . HOH J 6 .   ? 4.34800   1.20300   10.27300  1.000 34.71995  ? 749  HOH A O     1 
HETATM 3465 O  O     . HOH J 6 .   ? 21.81000  14.49000  17.61000  1.000 21.65523  ? 750  HOH A O     1 
HETATM 3466 O  O     . HOH J 6 .   ? 18.05400  -19.85500 9.28500   1.000 47.41358  ? 751  HOH A O     1 
HETATM 3467 O  O     . HOH J 6 .   ? 25.10800  -9.57400  10.94900  1.000 26.28473  ? 752  HOH A O     1 
HETATM 3468 O  O     . HOH J 6 .   ? 9.44300   -1.33600  3.79600   1.000 23.28174  ? 753  HOH A O     1 
HETATM 3469 O  O     . HOH J 6 .   ? 4.06300   -9.06400  -4.98000  1.000 48.90060  ? 754  HOH A O     1 
HETATM 3470 O  O     . HOH J 6 .   ? -8.44900  3.22100   25.16000  1.000 51.80621  ? 755  HOH A O     1 
HETATM 3471 O  O     . HOH J 6 .   ? 26.47800  11.96600  36.20800  1.000 41.82870  ? 756  HOH A O     1 
HETATM 3472 O  O     . HOH J 6 .   ? -0.51500  12.79600  -7.05900  1.000 32.36177  ? 757  HOH A O     1 
HETATM 3473 O  O     . HOH J 6 .   ? 27.94700  0.45900   13.90100  1.000 30.09045  ? 758  HOH A O     1 
HETATM 3474 O  O     . HOH J 6 .   ? -5.05100  24.73600  24.11300  1.000 33.68035  ? 759  HOH A O     1 
HETATM 3475 O  O     . HOH J 6 .   ? 14.44600  -13.62500 -0.44900  1.000 55.08029  ? 760  HOH A O     1 
HETATM 3476 O  O     . HOH J 6 .   ? 20.73700  23.38000  23.80400  1.000 28.38235  ? 761  HOH A O     1 
HETATM 3477 O  O     . HOH J 6 .   ? 9.63500   24.57100  9.23900   1.000 55.20662  ? 762  HOH A O     1 
HETATM 3478 O  O     . HOH J 6 .   ? -10.47800 23.29300  13.17700  1.000 41.16020  ? 763  HOH A O     1 
HETATM 3479 O  O     . HOH J 6 .   ? 21.14700  -4.37800  3.76000   1.000 23.75811  ? 764  HOH A O     1 
HETATM 3480 O  O     . HOH J 6 .   ? -4.24200  14.11700  27.77800  1.000 52.76159  ? 765  HOH A O     1 
HETATM 3481 O  O     . HOH J 6 .   ? -6.60600  -4.86100  8.32100   1.000 55.90934  ? 766  HOH A O     1 
HETATM 3482 O  O     . HOH J 6 .   ? 6.75900   0.41500   19.99300  1.000 20.79986  ? 767  HOH A O     1 
HETATM 3483 O  O     . HOH J 6 .   ? 3.03500   29.41000  11.13700  1.000 43.58417  ? 768  HOH A O     1 
HETATM 3484 O  O     . HOH J 6 .   ? 9.28400   24.39600  13.42800  1.000 39.00731  ? 769  HOH A O     1 
HETATM 3485 O  O     . HOH J 6 .   ? 3.71600   26.01100  17.21200  1.000 26.33737  ? 770  HOH A O     1 
HETATM 3486 O  O     . HOH J 6 .   ? -0.02000  1.63500   -2.22200  1.000 30.27731  ? 771  HOH A O     1 
HETATM 3487 O  O     . HOH J 6 .   ? 9.88200   -0.53300  10.45300  1.000 26.54792  ? 772  HOH A O     1 
HETATM 3488 O  O     . HOH J 6 .   ? 7.68000   22.78000  37.89900  1.000 35.49110  ? 773  HOH A O     1 
HETATM 3489 O  O     . HOH J 6 .   ? -0.48700  -1.03200  -1.24200  1.000 34.00671  ? 774  HOH A O     1 
HETATM 3490 O  O     . HOH J 6 .   ? 1.19500   21.10500  26.74000  1.000 29.21403  ? 775  HOH A O     1 
HETATM 3491 O  O     . HOH J 6 .   ? -1.18900  -11.30100 10.57900  1.000 61.39420  ? 776  HOH A O     1 
HETATM 3492 O  O     . HOH J 6 .   ? 20.33300  -12.84800 26.36900  1.000 45.03961  ? 777  HOH A O     1 
HETATM 3493 O  O     . HOH J 6 .   ? -2.85600  20.21200  -12.84800 1.000 28.57711  ? 778  HOH A O     1 
HETATM 3494 O  O     . HOH J 6 .   ? 28.86500  -9.30100  22.05400  1.000 33.99092  ? 779  HOH A O     1 
HETATM 3495 O  O     . HOH J 6 .   ? 9.68200   -0.84900  20.64700  1.000 21.19201  ? 780  HOH A O     1 
HETATM 3496 O  O     . HOH J 6 .   ? 29.81300  1.04800   28.40100  1.000 43.09464  ? 781  HOH A O     1 
HETATM 3497 O  O     . HOH J 6 .   ? 12.29300  -0.37600  1.30300   1.000 30.82212  ? 782  HOH A O     1 
HETATM 3498 O  O     . HOH J 6 .   ? -2.21000  9.21800   1.41500   1.000 28.61133  ? 783  HOH A O     1 
HETATM 3499 O  O     . HOH J 6 .   ? 30.53700  0.35600   10.27900  1.000 46.22133  ? 784  HOH A O     1 
HETATM 3500 O  O     . HOH J 6 .   ? 11.67600  18.57500  25.45200  1.000 35.13053  ? 785  HOH A O     1 
HETATM 3501 O  O     . HOH J 6 .   ? -1.16700  -17.10100 3.81400   1.000 51.58250  ? 786  HOH A O     1 
HETATM 3502 O  O     . HOH J 6 .   ? 31.04300  16.35800  33.72000  1.000 52.43260  ? 787  HOH A O     1 
HETATM 3503 O  O     . HOH J 6 .   ? 1.54100   23.29500  33.31600  1.000 47.35831  ? 788  HOH A O     1 
HETATM 3504 O  O     . HOH J 6 .   ? 17.24100  -1.99100  21.39200  1.000 17.19680  ? 789  HOH A O     1 
HETATM 3505 O  O     . HOH J 6 .   ? 3.32700   21.64700  -1.36700  1.000 43.51048  ? 790  HOH A O     1 
HETATM 3506 O  O     . HOH J 6 .   ? 13.60600  30.89200  24.92700  1.000 41.93134  ? 791  HOH A O     1 
HETATM 3507 O  O     . HOH J 6 .   ? 17.77100  29.81400  10.41300  1.000 53.89857  ? 792  HOH A O     1 
HETATM 3508 O  O     . HOH J 6 .   ? 11.19000  -1.94900  12.41400  1.000 19.81290  ? 793  HOH A O     1 
HETATM 3509 O  O     . HOH J 6 .   ? -0.90500  -5.02500  0.14600   1.000 38.50725  ? 794  HOH A O     1 
HETATM 3510 O  O     . HOH J 6 .   ? 6.62800   -21.13100 26.14600  1.000 39.27050  ? 795  HOH A O     1 
HETATM 3511 O  O     . HOH J 6 .   ? 0.39900   -18.41500 0.30500   1.000 49.07957  ? 796  HOH A O     1 
HETATM 3512 O  O     . HOH J 6 .   ? 9.28000   -4.22000  3.76700   1.000 27.14273  ? 797  HOH A O     1 
HETATM 3513 O  O     . HOH J 6 .   ? 4.77400   -8.87400  28.56400  1.000 46.81088  ? 798  HOH A O     1 
HETATM 3514 O  O     . HOH J 6 .   ? 6.88500   4.87800   -4.49800  1.000 29.64303  ? 799  HOH A O     1 
HETATM 3515 O  O     . HOH J 6 .   ? -4.71200  30.74600  7.31100   1.000 46.16606  ? 800  HOH A O     1 
HETATM 3516 O  O     . HOH J 6 .   ? -1.46600  17.75100  26.67300  1.000 39.94426  ? 801  HOH A O     1 
HETATM 3517 O  O     . HOH J 6 .   ? 12.40900  -4.72800  30.14300  1.000 25.72677  ? 802  HOH A O     1 
HETATM 3518 O  O     . HOH J 6 .   ? 9.91700   -20.07500 15.05600  1.000 30.19046  ? 803  HOH A O     1 
HETATM 3519 O  O     . HOH J 6 .   ? 9.93200   -21.86700 7.33300   1.000 35.91220  ? 804  HOH A O     1 
HETATM 3520 O  O     . HOH J 6 .   ? -6.65900  -4.02900  1.01700   1.000 53.60906  ? 805  HOH A O     1 
HETATM 3521 O  O     . HOH J 6 .   ? -10.77100 14.08800  26.31300  1.000 60.95731  ? 806  HOH A O     1 
HETATM 3522 O  O     . HOH J 6 .   ? 14.26300  12.26300  6.01100   1.000 35.37003  ? 807  HOH A O     1 
HETATM 3523 O  O     . HOH J 6 .   ? 21.54000  -9.17800  3.13500   1.000 53.08531  ? 808  HOH A O     1 
HETATM 3524 O  O     . HOH J 6 .   ? -11.77300 -3.00300  20.69200  1.000 48.46897  ? 809  HOH A O     1 
HETATM 3525 O  O     . HOH J 6 .   ? 22.13400  23.27600  21.36200  1.000 34.51203  ? 810  HOH A O     1 
HETATM 3526 O  O     . HOH J 6 .   ? 30.27600  16.59000  17.54700  1.000 50.84294  ? 811  HOH A O     1 
HETATM 3527 O  O     . HOH J 6 .   ? 3.28700   26.08500  33.50600  1.000 53.75645  ? 812  HOH A O     1 
HETATM 3528 O  O     . HOH J 6 .   ? 21.68600  -14.52400 12.25700  1.000 59.04129  ? 813  HOH A O     1 
HETATM 3529 O  O     . HOH J 6 .   ? 6.75700   13.89000  -7.02700  1.000 56.65679  ? 814  HOH A O     1 
HETATM 3530 O  O     . HOH J 6 .   ? 8.62600   -22.54600 28.12800  1.000 57.15685  ? 815  HOH A O     1 
HETATM 3531 O  O     . HOH J 6 .   ? 24.20600  -0.65200  30.35900  1.000 47.86363  ? 816  HOH A O     1 
HETATM 3532 O  O     . HOH J 6 .   ? 22.65700  -2.52200  2.49100   1.000 23.56862  ? 817  HOH A O     1 
HETATM 3533 O  O     . HOH J 6 .   ? 20.78000  -11.25700 9.82000   1.000 25.69782  ? 818  HOH A O     1 
HETATM 3534 O  O     . HOH J 6 .   ? 2.11100   25.43100  -2.00600  1.000 31.10636  ? 819  HOH A O     1 
HETATM 3535 O  O     . HOH J 6 .   ? 12.61000  -8.64600  -3.68600  1.000 42.69722  ? 820  HOH A O     1 
HETATM 3536 O  O     . HOH J 6 .   ? -10.60500 15.65900  -2.38400  1.000 52.48524  ? 821  HOH A O     1 
HETATM 3537 O  O     . HOH J 6 .   ? 5.39800   6.84000   35.64600  1.000 32.86183  ? 822  HOH A O     1 
HETATM 3538 O  O     . HOH J 6 .   ? 4.67800   -16.18900 -4.36100  1.000 48.05839  ? 823  HOH A O     1 
HETATM 3539 O  O     . HOH J 6 .   ? -8.77200  24.58200  21.12200  1.000 60.79150  ? 824  HOH A O     1 
HETATM 3540 O  O     . HOH J 6 .   ? 8.48300   -14.50600 -4.83600  1.000 51.02191  ? 825  HOH A O     1 
HETATM 3541 O  O     . HOH J 6 .   ? 27.10900  6.31800   17.80000  1.000 42.87356  ? 826  HOH A O     1 
HETATM 3542 O  O     . HOH J 6 .   ? 4.84600   -4.44000  16.69400  1.000 34.06461  ? 827  HOH A O     1 
HETATM 3543 O  O     . HOH J 6 .   ? 5.30600   -2.64100  32.39000  1.000 58.41490  ? 828  HOH A O     1 
HETATM 3544 O  O     . HOH J 6 .   ? 13.32800  -1.16000  -1.61500  1.000 53.84067  ? 829  HOH A O     1 
HETATM 3545 O  O     . HOH J 6 .   ? 8.87800   6.59500   -6.20100  1.000 49.26117  ? 830  HOH A O     1 
HETATM 3546 O  O     . HOH J 6 .   ? 14.21800  14.82600  9.05400   1.000 28.07705  ? 831  HOH A O     1 
HETATM 3547 O  O     . HOH J 6 .   ? 5.03000   -2.04900  30.09900  1.000 49.81913  ? 832  HOH A O     1 
HETATM 3548 O  O     . HOH J 6 .   ? 32.70000  10.10100  33.85200  1.000 51.17192  ? 833  HOH A O     1 
HETATM 3549 O  O     . HOH J 6 .   ? 7.11500   20.54200  -1.42600  1.000 46.24239  ? 834  HOH A O     1 
HETATM 3550 O  O     . HOH J 6 .   ? 15.31300  7.10900   40.79700  1.000 51.71410  ? 835  HOH A O     1 
HETATM 3551 O  O     . HOH J 6 .   ? 3.74200   -16.78000 25.38100  1.000 46.96616  ? 836  HOH A O     1 
HETATM 3552 O  O     . HOH J 6 .   ? 5.66100   20.00200  -3.56900  1.000 55.64615  ? 837  HOH A O     1 
HETATM 3553 O  O     . HOH J 6 .   ? 21.02700  -11.65800 17.97100  1.000 26.29526  ? 838  HOH A O     1 
HETATM 3554 O  O     . HOH J 6 .   ? 13.77700  9.48700   1.41800   1.000 43.73945  ? 839  HOH A O     1 
HETATM 3555 O  O     . HOH J 6 .   ? 10.26100  28.27900  8.35300   1.000 58.08591  ? 840  HOH A O     1 
HETATM 3556 O  O     . HOH J 6 .   ? 29.32100  -1.14700  18.43000  1.000 32.17754  ? 841  HOH A O     1 
HETATM 3557 O  O     . HOH J 6 .   ? 32.30200  20.32500  25.90600  1.000 47.07670  ? 842  HOH A O     1 
HETATM 3558 O  O     . HOH J 6 .   ? 14.49600  4.73000   19.72400  1.000 16.92308  ? 843  HOH A O     1 
HETATM 3559 O  O     . HOH J 6 .   ? 24.71900  -6.11300  2.99600   1.000 29.72988  ? 844  HOH A O     1 
HETATM 3560 O  O     . HOH J 6 .   ? 4.12500   16.77300  -5.25100  1.000 38.02035  ? 845  HOH A O     1 
HETATM 3561 O  O     . HOH J 6 .   ? 30.54100  -3.32200  17.53300  1.000 35.40688  ? 846  HOH A O     1 
HETATM 3562 O  O     . HOH J 6 .   ? 10.45800  -15.84000 23.48800  1.000 39.82846  ? 847  HOH A O     1 
HETATM 3563 O  O     . HOH J 6 .   ? 17.97300  10.34500  39.56100  1.000 37.24920  ? 848  HOH A O     1 
HETATM 3564 O  O     . HOH J 6 .   ? 0.47100   -17.43500 9.35000   1.000 50.41920  ? 849  HOH A O     1 
HETATM 3565 O  O     . HOH J 6 .   ? -7.33400  23.33200  23.10700  1.000 33.74352  ? 850  HOH A O     1 
HETATM 3566 O  O     . HOH J 6 .   ? -11.73500 10.83600  8.72100   1.000 49.20064  ? 851  HOH A O     1 
HETATM 3567 O  O     . HOH J 6 .   ? 11.93700  13.41900  45.90800  1.000 54.02753  ? 852  HOH A O     1 
HETATM 3568 O  O     . HOH J 6 .   ? 10.77500  -8.38500  31.38500  1.000 47.91890  ? 853  HOH A O     1 
HETATM 3569 O  O     . HOH J 6 .   ? 15.94100  4.27000   41.28700  1.000 59.03076  ? 854  HOH A O     1 
HETATM 3570 O  O     . HOH J 6 .   ? -1.87100  29.70100  17.84700  1.000 33.04870  ? 855  HOH A O     1 
HETATM 3571 O  O     . HOH J 6 .   ? -0.18300  8.14400   -6.84300  1.000 39.39420  ? 856  HOH A O     1 
HETATM 3572 O  O     . HOH J 6 .   ? 1.06500   32.67000  6.99800   1.000 35.36213  ? 857  HOH A O     1 
HETATM 3573 O  O     . HOH J 6 .   ? 5.26500   11.50200  26.00800  1.000 51.75094  ? 858  HOH A O     1 
HETATM 3574 O  O     . HOH J 6 .   ? -6.63800  -8.46900  1.93400   1.000 53.82751  ? 859  HOH A O     1 
HETATM 3575 O  O     . HOH J 6 .   ? -11.33300 13.17400  -3.79100  1.000 48.63478  ? 860  HOH A O     1 
HETATM 3576 O  O     . HOH J 6 .   ? 3.42300   6.64400   33.64700  1.000 42.18664  ? 861  HOH A O     1 
HETATM 3577 O  O     . HOH J 6 .   ? 22.94600  2.93400   38.55400  1.000 59.69400  ? 862  HOH A O     1 
HETATM 3578 O  O     . HOH J 6 .   ? -0.29400  29.48500  8.95200   1.000 43.64471  ? 863  HOH A O     1 
HETATM 3579 O  O     . HOH J 6 .   ? 25.15500  22.17400  19.20300  1.000 45.19489  ? 864  HOH A O     1 
HETATM 3580 O  O     . HOH J 6 .   ? 12.63400  -15.62500 -2.21400  1.000 38.21774  ? 865  HOH A O     1 
HETATM 3581 O  O     . HOH J 6 .   ? -16.40700 9.70200   16.70900  1.000 49.20064  ? 866  HOH A O     1 
HETATM 3582 O  O     . HOH J 6 .   ? -3.96300  18.37100  26.90700  1.000 47.12144  ? 867  HOH A O     1 
HETATM 3583 O  O     . HOH J 6 .   ? 15.18100  -1.82000  23.33300  1.000 42.21822  ? 868  HOH A O     1 
HETATM 3584 O  O     . HOH J 6 .   ? -3.17400  -17.69200 12.27600  1.000 57.38320  ? 869  HOH A O     1 
HETATM 3585 O  O     . HOH J 6 .   ? 5.51100   -2.08800  -4.56400  1.000 50.06916  ? 870  HOH A O     1 
HETATM 3586 O  O     . HOH J 6 .   ? -3.61900  -10.14600 14.09600  1.000 53.65907  ? 871  HOH A O     1 
HETATM 3587 O  O     . HOH J 6 .   ? -13.87700 -1.09300  21.18800  1.000 55.27505  ? 872  HOH A O     1 
HETATM 3588 O  O     . HOH J 6 .   ? 2.40100   -4.38100  14.10500  1.000 51.32984  ? 873  HOH A O     1 
HETATM 3589 O  O     . HOH J 6 .   ? -0.43400  -11.72100 21.89800  1.000 37.30447  ? 874  HOH A O     1 
HETATM 3590 O  O     . HOH J 6 .   ? 28.09700  -6.66100  11.02500  1.000 37.70715  ? 875  HOH A O     1 
HETATM 3591 O  O     . HOH J 6 .   ? 2.12800   -13.80900 -5.32800  1.000 57.84641  ? 876  HOH A O     1 
HETATM 3592 O  O     . HOH J 6 .   ? 5.34200   -22.90000 3.61400   1.000 45.62126  ? 877  HOH A O     1 
HETATM 3593 O  O     . HOH J 6 .   ? 9.75800   -2.56000  0.63700   1.000 54.51706  ? 878  HOH A O     1 
HETATM 3594 O  O     . HOH J 6 .   ? 32.31200  7.21300   29.81900  1.000 46.89246  ? 879  HOH A O     1 
HETATM 3595 O  O     . HOH J 6 .   ? 32.04500  0.51800   18.42300  1.000 42.34981  ? 880  HOH A O     1 
HETATM 3596 O  O     . HOH J 6 .   ? 22.84700  22.67500  12.60700  1.000 38.88887  ? 881  HOH A O     1 
HETATM 3597 O  O     . HOH J 6 .   ? 8.88000   -13.73100 23.56900  1.000 39.36788  ? 882  HOH A O     1 
HETATM 3598 O  O     . HOH J 6 .   ? 18.52100  -4.46700  2.22200   1.000 30.89844  ? 883  HOH A O     1 
HETATM 3599 O  O     . HOH J 6 .   ? 25.56000  15.39800  33.03200  1.000 44.61588  ? 884  HOH A O     1 
HETATM 3600 O  O     . HOH J 6 .   ? 19.27900  5.78100   10.84600  1.000 46.35556  ? 885  HOH A O     1 
HETATM 3601 O  O     . HOH J 6 .   ? 1.29400   32.37900  16.05800  1.000 36.12538  ? 886  HOH A O     1 
HETATM 3602 O  O     . HOH J 6 .   ? 15.77100  -21.29500 12.96300  1.000 52.60104  ? 887  HOH A O     1 
HETATM 3603 O  O     . HOH J 6 .   ? 11.47100  10.33000  -0.42800  1.000 33.80668  ? 888  HOH A O     1 
HETATM 3604 O  O     . HOH J 6 .   ? -14.54000 20.83000  10.32500  1.000 60.99416  ? 889  HOH A O     1 
HETATM 3605 O  O     . HOH J 6 .   ? -3.59900  -1.55300  22.82300  1.000 35.90957  ? 890  HOH A O     1 
HETATM 3606 O  O     . HOH J 6 .   ? -4.14100  13.83400  -10.09300 1.000 39.84688  ? 891  HOH A O     1 
HETATM 3607 O  O     . HOH J 6 .   ? -4.08100  26.13200  26.81500  1.000 55.55929  ? 892  HOH A O     1 
HETATM 3608 O  O     . HOH J 6 .   ? 1.71800   27.71100  12.57200  1.000 34.10935  ? 893  HOH A O     1 
HETATM 3609 O  O     . HOH J 6 .   ? -0.80000  28.11500  23.48600  1.000 48.68478  ? 894  HOH A O     1 
HETATM 3610 O  O     . HOH J 6 .   ? -4.90400  6.27500   -0.76900  1.000 53.99068  ? 895  HOH A O     1 
HETATM 3611 O  O     . HOH J 6 .   ? 24.14200  -10.01000 25.14400  1.000 49.21906  ? 896  HOH A O     1 
HETATM 3612 O  O     . HOH J 6 .   ? 16.79600  0.54200   38.09300  1.000 54.50127  ? 897  HOH A O     1 
HETATM 3613 O  O     . HOH J 6 .   ? 30.37700  -6.76700  16.50200  1.000 55.43296  ? 898  HOH A O     1 
HETATM 3614 O  O     . HOH J 6 .   ? -11.48200 6.05500   1.84800   1.000 61.66792  ? 899  HOH A O     1 
HETATM 3615 O  O     . HOH J 6 .   ? -4.10400  1.34800   0.00600   1.000 45.24490  ? 900  HOH A O     1 
HETATM 3616 O  O     . HOH J 6 .   ? -5.49400  3.38900   1.49100   1.000 40.56539  ? 901  HOH A O     1 
HETATM 3617 O  O     . HOH J 6 .   ? 21.76000  14.69000  12.06100  1.000 42.09715  ? 902  HOH A O     1 
HETATM 3618 O  O     . HOH J 6 .   ? 24.03200  16.98200  33.81900  1.000 52.30890  ? 903  HOH A O     1 
HETATM 3619 O  O     . HOH J 6 .   ? -2.09500  15.26200  26.37800  1.000 51.69567  ? 904  HOH A O     1 
HETATM 3620 O  O     . HOH J 6 .   ? 26.51300  14.51600  35.33400  1.000 42.61300  ? 905  HOH A O     1 
HETATM 3621 O  O     . HOH J 6 .   ? 15.01200  -12.53300 3.05300   1.000 58.55176  ? 906  HOH A O     1 
HETATM 3622 O  O     . HOH J 6 .   ? 1.04200   3.53400   30.68600  1.000 57.70955  ? 907  HOH A O     1 
HETATM 3623 O  O     . HOH J 6 .   ? 23.56400  14.23100  37.39800  1.000 52.75106  ? 908  HOH A O     1 
HETATM 3624 O  O     . HOH J 6 .   ? 21.93800  -11.85400 7.11100   1.000 42.86830  ? 909  HOH A O     1 
HETATM 3625 O  O     . HOH J 6 .   ? 21.04200  20.91700  11.75800  1.000 32.13543  ? 910  HOH A O     1 
HETATM 3626 O  O     . HOH J 6 .   ? 7.07500   -6.98100  -5.18900  1.000 43.29993  ? 911  HOH A O     1 
HETATM 3627 O  O     . HOH J 6 .   ? 20.84000  29.03500  16.17600  1.000 55.06713  ? 912  HOH A O     1 
HETATM 3628 O  O     . HOH J 6 .   ? 24.06300  -11.19600 22.28200  1.000 39.77056  ? 913  HOH A O     1 
HETATM 3629 O  O     . HOH J 6 .   ? 0.82100   7.17300   34.75000  1.000 50.26392  ? 914  HOH A O     1 
HETATM 3630 O  O     . HOH J 6 .   ? -12.76300 22.13100  14.24700  1.000 60.41251  ? 915  HOH A O     1 
HETATM 3631 O  O     . HOH J 6 .   ? 3.91400   17.15100  39.18900  1.000 61.88110  ? 916  HOH A O     1 
HETATM 3632 O  O     . HOH J 6 .   ? 32.15300  6.06600   9.17700   1.000 57.45952  ? 917  HOH A O     1 
HETATM 3633 O  O     . HOH J 6 .   ? 31.01300  5.96000   6.37400   1.000 47.16092  ? 918  HOH A O     1 
HETATM 3634 O  O     . HOH J 6 .   ? -9.26200  22.20900  24.71400  1.000 45.66600  ? 919  HOH A O     1 
HETATM 3635 O  O     . HOH J 6 .   ? 12.58400  -20.61400 15.11800  1.000 61.04153  ? 920  HOH A O     1 
HETATM 3636 O  O     . HOH J 6 .   ? 27.43600  21.78800  21.46700  1.000 41.50234  ? 921  HOH A O     1 
HETATM 3637 O  O     . HOH J 6 .   ? -0.27500  29.33100  0.26100   1.000 32.79604  ? 922  HOH A O     1 
HETATM 3638 O  O     . HOH J 6 .   ? 29.34200  -2.59600  30.33700  1.000 47.77678  ? 923  HOH A O     1 
HETATM 3639 O  O     . HOH J 6 .   ? 5.13500   1.45200   43.04800  1.000 54.25124  ? 924  HOH A O     1 
HETATM 3640 O  O     . HOH J 6 .   ? -13.58400 7.78500   23.58900  1.000 57.16212  ? 925  HOH A O     1 
HETATM 3641 O  O     . HOH J 6 .   ? 1.04300   -2.44100  30.83000  1.000 51.38774  ? 926  HOH A O     1 
HETATM 3642 O  O     . HOH J 6 .   ? 33.36900  15.01200  34.52200  1.000 47.56097  ? 927  HOH A O     1 
HETATM 3643 O  O     . HOH J 6 .   ? 34.79700  11.10800  27.18800  1.000 55.16977  ? 928  HOH A O     1 
HETATM 3644 O  O     . HOH J 6 .   ? 25.77900  -12.85300 18.40300  1.000 58.05696  ? 929  HOH A O     1 
HETATM 3645 O  O     . HOH J 6 .   ? 26.41200  11.12500  14.78100  1.000 53.62222  ? 930  HOH A O     1 
HETATM 3646 O  O     . HOH J 6 .   ? 17.26300  7.67600   38.93400  1.000 35.37529  ? 931  HOH A O     1 
HETATM 3647 O  O     . HOH J 6 .   ? -9.60900  7.27100   24.89400  1.000 62.02323  ? 932  HOH A O     1 
HETATM 3648 O  O     . HOH J 6 .   ? 21.32800  18.74800  13.52600  1.000 28.96400  ? 933  HOH A O     1 
HETATM 3649 O  O     . HOH J 6 .   ? 9.56800   25.78000  11.62100  1.000 57.42531  ? 934  HOH A O     1 
HETATM 3650 O  O     . HOH J 6 .   ? 26.63100  -7.23300  4.80900   1.000 41.71816  ? 935  HOH A O     1 
HETATM 3651 O  O     . HOH J 6 .   ? 25.77500  -7.38100  9.52700   1.000 29.09296  ? 936  HOH A O     1 
HETATM 3652 O  O     . HOH J 6 .   ? -0.36900  29.12800  12.92100  1.000 34.92524  ? 937  HOH A O     1 
HETATM 3653 O  O     . HOH J 6 .   ? 25.36200  22.02400  8.56800   1.000 43.17097  ? 938  HOH A O     1 
HETATM 3654 O  O     . HOH J 6 .   ? 25.15200  18.77000  16.40500  1.000 43.91579  ? 939  HOH A O     1 
HETATM 3655 O  O     . HOH J 6 .   ? 14.13500  -3.78100  35.98000  1.000 67.57126  ? 940  HOH A O     1 
HETATM 3656 O  O     . HOH J 6 .   ? 34.38100  12.52000  32.00800  1.000 60.01772  ? 941  HOH A O     1 
HETATM 3657 O  O     . HOH J 6 .   ? 5.45400   7.68200   -9.78100  1.000 41.19178  ? 942  HOH A O     1 
HETATM 3658 O  O     . HOH J 6 .   ? 11.89400  27.49000  12.25400  1.000 40.51275  ? 943  HOH A O     1 
HETATM 3659 O  O     . HOH J 6 .   ? 23.96500  12.72900  14.32400  1.000 35.32266  ? 944  HOH A O     1 
HETATM 3660 O  O     . HOH J 6 .   ? 23.12500  16.38100  16.23200  1.000 36.12802  ? 945  HOH A O     1 
HETATM 3661 O  O     . HOH J 6 .   ? 16.70400  -2.13600  36.19500  1.000 57.78324  ? 946  HOH A O     1 
HETATM 3662 O  O     . HOH J 6 .   ? 1.75400   15.09200  28.42900  1.000 48.30316  ? 947  HOH A O     1 
HETATM 3663 O  O     . HOH J 6 .   ? 8.32800   27.90800  10.21600  1.000 63.98925  ? 948  HOH A O     1 
HETATM 3664 O  O     . HOH J 6 .   ? -3.18200  5.96200   -7.52800  1.000 33.41453  ? 949  HOH A O     1 
HETATM 3665 O  O     . HOH J 6 .   ? 10.33400  18.60900  -2.79300  1.000 52.77475  ? 950  HOH A O     1 
HETATM 3666 O  O     . HOH J 6 .   ? -2.71000  2.45200   -2.29900  1.000 34.27253  ? 951  HOH A O     1 
HETATM 3667 O  O     . HOH J 6 .   ? -4.13700  4.33500   -5.59100  1.000 29.59829  ? 952  HOH A O     1 
HETATM 3668 O  O     . HOH J 6 .   ? 26.39900  -8.34500  7.15900   1.000 44.47639  ? 953  HOH A O     1 
HETATM 3669 O  O     . HOH J 6 .   ? -11.15000 36.28800  1.33800   1.000 56.61205  ? 954  HOH A O     1 
HETATM 3670 O  O     . HOH J 6 .   ? -3.74200  1.49000   -4.81700  1.000 40.71541  ? 955  HOH A O     1 
HETATM 3671 O  O     . HOH J 6 .   ? -4.09200  -3.99900  23.99000  1.000 49.75333  ? 956  HOH A O     1 
HETATM 3672 O  O     . HOH J 6 .   ? 1.69400   26.55300  -4.46800  1.000 36.84126  ? 957  HOH A O     1 
HETATM 3673 O  O     . HOH J 6 .   ? 1.95500   -7.94500  -6.01700  1.000 54.86710  ? 958  HOH A O     1 
HETATM 3674 O  O     . HOH J 6 .   ? 20.38400  17.22400  9.55500   1.000 27.87176  ? 959  HOH A O     1 
HETATM 3675 O  O     . HOH J 6 .   ? -3.26900  15.54600  -12.05600 1.000 37.01496  ? 960  HOH A O     1 
HETATM 3676 O  O     . HOH J 6 .   ? -8.76300  27.42600  23.82400  1.000 54.54601  ? 961  HOH A O     1 
HETATM 3677 O  O     . HOH J 6 .   ? -7.72100  6.65100   -1.27200  1.000 42.61564  ? 962  HOH A O     1 
HETATM 3678 O  O     . HOH J 6 .   ? 19.59200  -7.19600  1.39400   1.000 50.61923  ? 963  HOH A O     1 
HETATM 3679 O  O     . HOH J 6 .   ? 16.97800  31.78700  21.77400  1.000 55.70142  ? 964  HOH A O     1 
HETATM 3680 O  O     . HOH J 6 .   ? -7.81900  3.00000   1.85100   1.000 48.00049  ? 965  HOH A O     1 
HETATM 3681 O  O     . HOH J 6 .   ? -0.48500  -23.34400 15.41200  1.000 37.82296  ? 966  HOH A O     1 
HETATM 3682 O  O     . HOH J 6 .   ? 1.97700   27.87400  -0.21500  1.000 41.53656  ? 967  HOH A O     1 
HETATM 3683 O  O     . HOH J 6 .   ? 1.78400   14.07400  -7.33900  1.000 43.38678  ? 968  HOH A O     1 
HETATM 3684 O  O     . HOH J 6 .   ? 26.76400  -11.15000 21.39000  1.000 49.43751  ? 969  HOH A O     1 
HETATM 3685 O  O     . HOH J 6 .   ? 23.80700  8.59400   40.52000  1.000 54.20650  ? 970  HOH A O     1 
HETATM 3686 O  O     . HOH J 6 .   ? 10.83500  6.89100   -2.14300  1.000 47.49517  ? 971  HOH A O     1 
HETATM 3687 O  O     . HOH J 6 .   ? -9.88600  25.76500  13.60900  1.000 51.34037  ? 972  HOH A O     1 
HETATM 3688 O  O     . HOH J 6 .   ? 0.19500   17.30000  28.86000  1.000 37.73610  ? 973  HOH A O     1 
HETATM 3689 O  O     . HOH J 6 .   ? 15.14600  16.24100  0.09100   1.000 31.41692  ? 974  HOH A O     1 
HETATM 3690 O  O     . HOH J 6 .   ? -10.74000 18.62700  -3.80100  1.000 27.84018  ? 975  HOH A O     1 
HETATM 3691 O  O     . HOH J 6 .   ? -2.35100  31.72400  8.13100   1.000 46.37398  ? 976  HOH A O     1 
HETATM 3692 O  O     . HOH J 6 .   ? -9.18700  4.84600   0.44200   1.000 35.33582  ? 977  HOH A O     1 
HETATM 3693 O  O     . HOH J 6 .   ? 24.61600  -7.43400  0.79100   1.000 51.33510  ? 978  HOH A O     1 
HETATM 3694 O  O     . HOH J 6 .   ? -12.52100 8.97400   1.61000   1.000 48.89007  ? 979  HOH A O     1 
HETATM 3695 O  O     . HOH J 6 .   ? 20.73500  11.18900  39.83200  1.000 33.27504  ? 980  HOH A O     1 
HETATM 3696 O  O     . HOH J 6 .   ? 8.10200   -1.29000  -0.71800  1.000 28.34550  ? 981  HOH A O     1 
HETATM 3697 O  O     . HOH J 6 .   ? 1.29700   -25.19400 16.64600  1.000 30.92476  ? 982  HOH A O     1 
HETATM 3698 O  O     . HOH J 6 .   ? 23.84400  11.55600  36.68800  1.000 44.55008  ? 983  HOH A O     1 
HETATM 3699 O  O     . HOH J 6 .   ? 26.71000  19.00500  18.45400  1.000 42.85251  ? 984  HOH A O     1 
HETATM 3700 O  O     . HOH J 6 .   ? 31.28700  9.79200   19.15100  1.000 63.87345  ? 985  HOH A O     1 
HETATM 3701 O  O     . HOH J 6 .   ? -3.56400  5.00800   -2.82300  1.000 30.62209  ? 986  HOH A O     1 
HETATM 3702 O  O     . HOH J 6 .   ? 7.79300   -2.13000  -6.12200  1.000 42.35245  ? 987  HOH A O     1 
HETATM 3703 O  O     . HOH J 6 .   ? -2.51100  -2.36700  27.99500  1.000 51.74568  ? 988  HOH A O     1 
HETATM 3704 O  O     . HOH J 6 .   ? 28.73800  -9.16800  7.10300   1.000 44.58956  ? 989  HOH A O     1 
HETATM 3705 O  O     . HOH J 6 .   ? 12.22000  11.74100  -8.67100  1.000 54.68814  ? 990  HOH A O     1 
HETATM 3706 O  O     . HOH J 6 .   ? -4.51000  30.87200  17.14200  1.000 46.46873  ? 991  HOH A O     1 
HETATM 3707 O  O     . HOH J 6 .   ? -2.31400  0.44500   28.28200  1.000 55.33821  ? 992  HOH A O     1 
HETATM 3708 O  O     . HOH J 6 .   ? 10.38900  -0.53500  -2.76500  1.000 35.29371  ? 993  HOH A O     1 
HETATM 3709 O  O     . HOH J 6 .   ? 10.00100  2.87200   -3.91400  1.000 45.51862  ? 994  HOH A O     1 
HETATM 3710 O  O     . HOH J 6 .   ? 24.85900  -10.96200 6.98500   1.000 43.01305  ? 995  HOH A O     1 
HETATM 3711 O  O     . HOH J 6 .   ? -1.16400  30.27400  -2.46300  1.000 30.49050  ? 996  HOH A O     1 
HETATM 3712 O  O     . HOH J 6 .   ? 8.18700   -4.81200  -6.98900  1.000 53.74065  ? 997  HOH A O     1 
HETATM 3713 O  O     . HOH J 6 .   ? 6.89800   31.07200  7.93200   1.000 41.98924  ? 998  HOH A O     1 
HETATM 3714 O  O     . HOH J 6 .   ? 9.98300   -1.04400  -5.40700  1.000 33.28294  ? 999  HOH A O     1 
HETATM 3715 O  O     . HOH J 6 .   ? -11.50600 21.94000  18.62000  1.000 53.90120  ? 1000 HOH A O     1 
HETATM 3716 O  O     . HOH J 6 .   ? 9.76400   2.02100   -6.42300  1.000 46.95300  ? 1001 HOH A O     1 
HETATM 3717 O  O     . HOH J 6 .   ? 26.41100  8.32400   41.11400  1.000 64.65249  ? 1002 HOH A O     1 
HETATM 3718 O  O     . HOH J 6 .   ? 24.28600  15.45900  14.06800  1.000 47.64255  ? 1003 HOH A O     1 
HETATM 3719 O  O     . HOH J 6 .   ? -0.70800  1.45600   35.69700  1.000 55.82775  ? 1004 HOH A O     1 
HETATM 3720 O  O     . HOH J 6 .   ? -10.63400 3.95400   -1.59900  1.000 31.48535  ? 1005 HOH A O     1 
HETATM 3721 O  O     . HOH J 6 .   ? 11.77300  3.23200   -7.83700  1.000 55.31716  ? 1006 HOH A 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     . THR A 4   ? 0.81130 0.76340 0.40720 -0.13280 0.22880  -0.20090 4    THR A N     
2    C  CA    . THR A 4   ? 0.76450 0.78380 0.41710 -0.10940 0.23040  -0.21100 4    THR A CA    
3    C  C     . THR A 4   ? 0.72140 0.76370 0.43730 -0.12720 0.23280  -0.22050 4    THR A C     
4    O  O     . THR A 4   ? 0.71540 0.71950 0.46520 -0.17430 0.23790  -0.21830 4    THR A O     
5    C  CB    . THR A 4   ? 0.74700 0.80150 0.40980 -0.09790 0.21550  -0.21810 4    THR A CB    
6    O  OG1   . THR A 4   ? 0.74950 0.84050 0.41180 -0.13190 0.21080  -0.21550 4    THR A OG1   
7    C  CG2   . THR A 4   ? 0.66750 0.75400 0.40690 -0.07140 0.22480  -0.19870 4    THR A CG2   
8    N  N     . ALA A 5   ? 0.66160 0.73310 0.43100 -0.13830 0.20250  -0.22780 5    ALA A N     
9    C  CA    . ALA A 5   ? 0.59060 0.70980 0.42460 -0.07580 0.18880  -0.21240 5    ALA A CA    
10   C  C     . ALA A 5   ? 0.58480 0.68980 0.40390 -0.00650 0.14540  -0.21670 5    ALA A C     
11   O  O     . ALA A 5   ? 0.57930 0.64560 0.40720 0.01570  0.09730  -0.27190 5    ALA A O     
12   C  CB    . ALA A 5   ? 0.57120 0.67060 0.43150 -0.14190 0.20060  -0.19210 5    ALA A CB    
13   N  N     . THR A 6   ? 0.67020 0.67860 0.40390 0.01320  0.10910  -0.15130 6    THR A N     
14   C  CA    . THR A 6   ? 0.79730 0.65570 0.41200 0.02740  0.08550  -0.10670 6    THR A CA    
15   C  C     . THR A 6   ? 0.87240 0.66010 0.38800 0.09820  0.04180  -0.05370 6    THR A C     
16   O  O     . THR A 6   ? 0.96230 0.66730 0.39920 0.18030  0.00290  0.01150  6    THR A O     
17   C  CB    . THR A 6   ? 0.84820 0.65010 0.42840 -0.03000 0.09260  -0.12620 6    THR A CB    
18   O  OG1   . THR A 6   ? 0.87480 0.67040 0.42770 -0.04300 0.08220  -0.12090 6    THR A OG1   
19   C  CG2   . THR A 6   ? 0.85670 0.61920 0.43730 -0.07880 0.09540  -0.13190 6    THR A CG2   
20   N  N     . THR A 7   ? 0.79280 0.62110 0.34460 0.06640  0.05170  -0.06560 7    THR A N     
21   C  CA    . THR A 7   ? 0.70110 0.56560 0.32370 0.08000  0.06270  -0.06180 7    THR A CA    
22   C  C     . THR A 7   ? 0.62740 0.45070 0.32530 0.12220  0.07800  -0.05860 7    THR A C     
23   O  O     . THR A 7   ? 0.59880 0.42250 0.33640 0.13960  0.10560  0.00170  7    THR A O     
24   C  CB    . THR A 7   ? 0.74600 0.60020 0.33030 0.05230  0.05510  -0.07370 7    THR A CB    
25   O  OG1   . THR A 7   ? 0.73540 0.60810 0.31820 0.06120  0.08770  -0.08380 7    THR A OG1   
26   C  CG2   . THR A 7   ? 0.74190 0.60020 0.34540 0.04020  0.04510  -0.04960 7    THR A CG2   
27   N  N     . PRO A 8   ? 0.62100 0.34180 0.33370 0.13530  0.06440  -0.05900 8    PRO A N     
28   C  CA    . PRO A 8   ? 0.58190 0.27590 0.34540 0.11090  0.05400  -0.02770 8    PRO A CA    
29   C  C     . PRO A 8   ? 0.52840 0.28410 0.35670 0.12220  0.06550  -0.00270 8    PRO A C     
30   O  O     . PRO A 8   ? 0.53950 0.28080 0.36590 0.10590  0.07330  0.00840  8    PRO A O     
31   C  CB    . PRO A 8   ? 0.59230 0.31350 0.35970 0.13300  0.02790  -0.02870 8    PRO A CB    
32   C  CG    . PRO A 8   ? 0.62970 0.32450 0.35630 0.10020  0.03370  -0.03560 8    PRO A CG    
33   C  CD    . PRO A 8   ? 0.61950 0.31040 0.33720 0.12660  0.06350  -0.07440 8    PRO A CD    
34   N  N     . GLN A 9   ? 0.50590 0.26910 0.36420 0.12600  0.09220  -0.02480 9    GLN A N     
35   C  CA    . GLN A 9   ? 0.50380 0.25600 0.37680 0.11220  0.09100  -0.02190 9    GLN A CA    
36   C  C     . GLN A 9   ? 0.51590 0.21820 0.35550 0.08030  0.05350  -0.03160 9    GLN A C     
37   O  O     . GLN A 9   ? 0.57540 0.24130 0.36990 0.08830  0.04170  -0.01540 9    GLN A O     
38   C  CB    . GLN A 9   ? 0.52580 0.27550 0.42050 0.12700  0.09950  0.00620  9    GLN A CB    
39   C  CG    . GLN A 9   ? 0.62900 0.40760 0.45350 0.12350  0.12150  0.05130  9    GLN A CG    
40   C  CD    . GLN A 9   ? 0.67970 0.48570 0.50240 0.12630  0.16410  0.09780  9    GLN A CD    
41   O  OE1   . GLN A 9   ? 0.76370 0.51840 0.53080 0.21630  0.14530  0.08500  9    GLN A OE1   
42   N  NE2   . GLN A 9   ? 0.62170 0.49780 0.50980 0.05480  0.21200  0.14440  9    GLN A NE2   
43   N  N     . THR A 10  ? 0.47680 0.25450 0.33050 0.06050  0.05030  -0.05000 10   THR A N     
44   C  CA    . THR A 10  ? 0.45480 0.25980 0.31940 0.06400  0.01520  -0.03470 10   THR A CA    
45   C  C     . THR A 10  ? 0.44930 0.20720 0.31590 0.01880  0.00740  0.00200  10   THR A C     
46   O  O     . THR A 10  ? 0.44230 0.19210 0.30940 -0.01780 -0.00520 -0.01490 10   THR A O     
47   C  CB    . THR A 10  ? 0.43850 0.29690 0.32140 0.09650  -0.01190 -0.04530 10   THR A CB    
48   O  OG1   . THR A 10  ? 0.47670 0.34940 0.33620 0.04400  -0.00700 -0.05980 10   THR A OG1   
49   C  CG2   . THR A 10  ? 0.43310 0.29170 0.32890 0.08010  -0.01760 -0.04690 10   THR A CG2   
50   N  N     . THR A 11  ? 0.47060 0.16320 0.34260 -0.03510 -0.03530 -0.00590 11   THR A N     
51   C  CA    . THR A 11  ? 0.44140 0.19300 0.36180 0.02190  -0.00300 0.01100  11   THR A CA    
52   C  C     . THR A 11  ? 0.47410 0.17280 0.38180 -0.02260 0.00990  0.00130  11   THR A C     
53   O  O     . THR A 11  ? 0.49970 0.25540 0.38740 -0.01160 0.01530  -0.00690 11   THR A O     
54   C  CB    . THR A 11  ? 0.46840 0.20620 0.36720 0.01070  -0.01700 -0.00790 11   THR A CB    
55   O  OG1   . THR A 11  ? 0.45600 0.25950 0.35820 0.00970  0.00500  0.03010  11   THR A OG1   
56   C  CG2   . THR A 11  ? 0.49160 0.27890 0.38120 0.04380  -0.00940 -0.01400 11   THR A CG2   
57   N  N     . ASP A 12  ? 0.47940 0.13230 0.40000 -0.04560 0.02500  0.01720  12   ASP A N     
58   C  CA    . ASP A 12  ? 0.50580 0.16390 0.40800 -0.01180 0.01870  0.03160  12   ASP A CA    
59   C  C     . ASP A 12  ? 0.52940 0.16560 0.43780 -0.06020 0.01930  0.03900  12   ASP A C     
60   O  O     . ASP A 12  ? 0.53430 0.21040 0.45580 -0.05550 0.02460  0.05610  12   ASP A O     
61   C  CB    . ASP A 12  ? 0.49090 0.22930 0.39730 0.03800  0.03620  0.00330  12   ASP A CB    
62   C  CG    . ASP A 12  ? 0.46290 0.15550 0.38600 0.02050  0.05040  -0.01310 12   ASP A CG    
63   O  OD1   . ASP A 12  ? 0.52140 0.16990 0.39110 -0.01730 0.05250  -0.01370 12   ASP A OD1   
64   O  OD2   . ASP A 12  ? 0.48200 0.17730 0.38600 0.04820  0.07740  0.01850  12   ASP A OD2   
65   N  N     . ALA A 13  ? 0.50470 0.15360 0.43800 -0.03170 0.02800  0.05760  13   ALA A N     
66   C  CA    . ALA A 13  ? 0.51920 0.14170 0.45480 -0.02590 0.02530  0.04840  13   ALA A CA    
67   C  C     . ALA A 13  ? 0.52200 0.15470 0.47190 -0.00990 0.02800  0.07390  13   ALA A C     
68   O  O     . ALA A 13  ? 0.53368 0.16922 0.48670 -0.03000 0.02939  0.09939  13   ALA A O     
69   C  CB    . ALA A 13  ? 0.49970 0.15480 0.45110 -0.01010 0.00980  0.05200  13   ALA A CB    
70   N  N     . PRO A 14  ? 0.49070 0.17790 0.47110 -0.02800 0.03540  0.06570  14   PRO A N     
71   C  CA    . PRO A 14  ? 0.48310 0.19160 0.47410 -0.00350 0.03390  0.05010  14   PRO A CA    
72   C  C     . PRO A 14  ? 0.50110 0.18500 0.45580 0.00390  0.05380  0.09430  14   PRO A C     
73   O  O     . PRO A 14  ? 0.47808 0.17304 0.45978 -0.01260 0.05988  0.10608  14   PRO A O     
74   C  CB    . PRO A 14  ? 0.45790 0.22910 0.48210 -0.03410 0.02840  0.03930  14   PRO A CB    
75   C  CG    . PRO A 14  ? 0.48100 0.25090 0.48400 -0.06970 0.03430  0.02560  14   PRO A CG    
76   C  CD    . PRO A 14  ? 0.48860 0.19100 0.47180 -0.04290 0.04340  0.04400  14   PRO A CD    
77   N  N     . ALA A 15  ? 0.52930 0.18350 0.43430 -0.03040 0.04690  0.09550  15   ALA A N     
78   C  CA    . ALA A 15  ? 0.48460 0.17840 0.40760 -0.02510 0.06620  0.06840  15   ALA A CA    
79   C  C     . ALA A 15  ? 0.45230 0.14120 0.37810 -0.00860 0.07170  0.06090  15   ALA A C     
80   O  O     . ALA A 15  ? 0.51720 0.17570 0.37540 -0.00160 0.09070  0.05170  15   ALA A O     
81   C  CB    . ALA A 15  ? 0.51780 0.17790 0.40260 0.01000  0.09840  0.02410  15   ALA A CB    
82   N  N     . PHE A 16  ? 0.41790 0.16250 0.34450 -0.00580 0.06760  0.09750  16   PHE A N     
83   C  CA    . PHE A 16  ? 0.38729 0.15821 0.32560 -0.02160 0.06369  0.09439  16   PHE A CA    
84   C  C     . PHE A 16  ? 0.43180 0.14160 0.34940 -0.00780 0.08010  0.06360  16   PHE A C     
85   O  O     . PHE A 16  ? 0.42030 0.16320 0.37850 -0.00170 0.06660  0.03000  16   PHE A O     
86   C  CB    . PHE A 16  ? 0.41460 0.21870 0.31080 -0.02820 0.06940  0.03390  16   PHE A CB    
87   C  CG    . PHE A 16  ? 0.39460 0.19010 0.27640 -0.04620 0.06400  0.01610  16   PHE A CG    
88   C  CD1   . PHE A 16  ? 0.39290 0.17430 0.26760 -0.01830 0.07700  0.02410  16   PHE A CD1   
89   C  CD2   . PHE A 16  ? 0.40030 0.18660 0.26380 -0.03130 0.05230  0.01720  16   PHE A CD2   
90   C  CE1   . PHE A 16  ? 0.42910 0.18990 0.26230 -0.05370 0.08230  0.00960  16   PHE A CE1   
91   C  CE2   . PHE A 16  ? 0.41050 0.21190 0.26360 -0.07560 0.06320  0.01040  16   PHE A CE2   
92   C  CZ    . PHE A 16  ? 0.43930 0.22140 0.26340 -0.04710 0.07700  0.00340  16   PHE A CZ    
93   N  N     . PRO A 17  ? 0.46290 0.14880 0.33820 -0.00010 0.07900  0.05950  17   PRO A N     
94   C  CA    . PRO A 17  ? 0.42840 0.19860 0.33170 -0.01450 0.07030  0.06260  17   PRO A CA    
95   C  C     . PRO A 17  ? 0.45910 0.18020 0.32210 -0.04020 0.05460  0.07600  17   PRO A C     
96   O  O     . PRO A 17  ? 0.43480 0.29510 0.32540 -0.00870 0.07070  0.03510  17   PRO A O     
97   C  CB    . PRO A 17  ? 0.43700 0.19020 0.33700 -0.07440 0.03590  0.07170  17   PRO A CB    
98   C  CG    . PRO A 17  ? 0.47230 0.17070 0.35640 -0.03650 0.03290  0.04930  17   PRO A CG    
99   C  CD    . PRO A 17  ? 0.48690 0.18480 0.35790 -0.04940 0.06050  0.07510  17   PRO A CD    
100  N  N     . SER A 18  ? 0.50690 0.20510 0.31930 -0.02970 0.04360  0.04290  18   SER A N     
101  C  CA    . SER A 18  ? 0.52310 0.19260 0.30310 -0.02880 0.05640  0.04450  18   SER A CA    
102  C  C     . SER A 18  ? 0.52780 0.21880 0.29870 -0.04160 0.07420  0.04880  18   SER A C     
103  O  O     . SER A 18  ? 0.53450 0.22510 0.28120 -0.05160 0.08860  0.07980  18   SER A O     
104  C  CB    . SER A 18  ? 0.56870 0.18990 0.31170 -0.00920 0.03690  0.03030  18   SER A CB    
105  O  OG    . SER A 18  ? 0.67980 0.25560 0.31940 -0.00150 0.01520  0.06710  18   SER A OG    
106  N  N     . ASN A 19  ? 0.53870 0.22510 0.29710 0.00470  0.05690  0.07220  19   ASN A N     
107  C  CA    . ASN A 19  ? 0.49460 0.23060 0.29680 0.00380  0.07190  0.07840  19   ASN A CA    
108  C  C     . ASN A 19  ? 0.48310 0.24390 0.28750 0.00770  0.06880  0.08400  19   ASN A C     
109  O  O     . ASN A 19  ? 0.54240 0.22480 0.32300 -0.01780 0.03170  0.09930  19   ASN A O     
110  C  CB    . ASN A 19  ? 0.47950 0.28790 0.30030 -0.01030 0.10090  0.10360  19   ASN A CB    
111  C  CG    . ASN A 19  ? 0.50680 0.33410 0.31650 -0.05230 0.10600  0.13090  19   ASN A CG    
112  O  OD1   . ASN A 19  ? 0.50700 0.29700 0.32660 -0.01630 0.06270  0.14020  19   ASN A OD1   
113  N  ND2   . ASN A 19  ? 0.52510 0.43500 0.33310 -0.05860 0.12350  0.13420  19   ASN A ND2   
114  N  N     . ARG A 20  ? 0.46470 0.21880 0.26780 0.00700  0.10220  0.08930  20   ARG A N     
115  C  CA    . ARG A 20  ? 0.51090 0.26160 0.24280 0.01530  0.11940  0.09200  20   ARG A CA    
116  C  C     . ARG A 20  ? 0.57970 0.31230 0.25620 0.00860  0.10320  0.05730  20   ARG A C     
117  O  O     . ARG A 20  ? 0.60430 0.36450 0.27220 -0.02470 0.09450  0.05910  20   ARG A O     
118  C  CB    . ARG A 20  ? 0.51840 0.23800 0.22510 0.01500  0.12730  0.06620  20   ARG A CB    
119  C  CG    . ARG A 20  ? 0.47037 0.23761 0.21552 -0.02579 0.11188  0.06549  20   ARG A CG    
120  C  CD    . ARG A 20  ? 0.39989 0.25860 0.20830 -0.01500 0.09909  0.09100  20   ARG A CD    
121  N  NE    . ARG A 20  ? 0.40120 0.24090 0.18560 0.01050  0.06140  0.09660  20   ARG A NE    
122  C  CZ    . ARG A 20  ? 0.36478 0.17361 0.18251 0.01070  0.05749  0.07729  20   ARG A CZ    
123  N  NH1   . ARG A 20  ? 0.43150 0.14640 0.17590 0.01380  0.03450  0.04010  20   ARG A NH1   
124  N  NH2   . ARG A 20  ? 0.39360 0.20340 0.16600 0.05350  0.04190  0.06330  20   ARG A NH2   
125  N  N     . SER A 21  ? 0.56100 0.33020 0.25520 -0.03080 0.07550  0.05570  21   SER A N     
126  C  CA    . SER A 21  ? 0.58080 0.37740 0.26700 0.00780  0.06750  0.07980  21   SER A CA    
127  C  C     . SER A 21  ? 0.50870 0.38430 0.24990 0.03100  0.08250  0.04720  21   SER A C     
128  O  O     . SER A 21  ? 0.54220 0.50040 0.24500 -0.04710 0.07710  0.00220  21   SER A O     
129  C  CB    . SER A 21  ? 0.66330 0.34620 0.31410 0.01930  0.08440  0.09840  21   SER A CB    
130  O  OG    . SER A 21  ? 0.72020 0.35750 0.34990 0.02380  0.07900  0.09820  21   SER A OG    
131  N  N     . CYS A 22  ? 0.46120 0.31440 0.23160 0.02880  0.09250  0.06640  22   CYS A N     
132  C  CA    . CYS A 22  ? 0.48650 0.31930 0.22480 0.01790  0.06840  0.08260  22   CYS A CA    
133  C  C     . CYS A 22  ? 0.48140 0.29610 0.23070 0.06190  0.03230  0.06900  22   CYS A C     
134  O  O     . CYS A 22  ? 0.45750 0.31830 0.22900 0.03260  0.01650  0.05610  22   CYS A O     
135  C  CB    . CYS A 22  ? 0.52100 0.35700 0.23580 0.00720  0.02190  0.10380  22   CYS A CB    
136  S  SG    . CYS A 22  ? 0.52240 0.42500 0.23790 0.02950  -0.01500 0.08840  22   CYS A SG    
137  N  N     . PRO A 23  ? 0.49630 0.31160 0.23950 0.05710  0.00510  0.00540  23   PRO A N     
138  C  CA    . PRO A 23  ? 0.53210 0.30330 0.24870 0.04530  0.01700  0.02410  23   PRO A CA    
139  C  C     . PRO A 23  ? 0.48990 0.30330 0.22140 0.00780  -0.00780 0.06950  23   PRO A C     
140  O  O     . PRO A 23  ? 0.53980 0.30110 0.22130 0.01360  -0.05800 0.07400  23   PRO A O     
141  C  CB    . PRO A 23  ? 0.55140 0.31550 0.28620 0.07550  0.05020  -0.00750 23   PRO A CB    
142  C  CG    . PRO A 23  ? 0.60500 0.31980 0.30910 0.06010  0.02700  -0.03600 23   PRO A CG    
143  C  CD    . PRO A 23  ? 0.56600 0.33770 0.28170 0.02870  0.03330  -0.00810 23   PRO A CD    
144  N  N     . TYR A 24  ? 0.42300 0.29090 0.18520 0.02940  -0.00920 0.08070  24   TYR A N     
145  C  CA    . TYR A 24  ? 0.44910 0.28250 0.17830 0.02710  0.01560  0.05480  24   TYR A CA    
146  C  C     . TYR A 24  ? 0.43550 0.28070 0.19620 0.01010  0.03430  0.02720  24   TYR A C     
147  O  O     . TYR A 24  ? 0.49160 0.31500 0.20060 0.00160  0.06970  -0.01180 24   TYR A O     
148  C  CB    . TYR A 24  ? 0.45610 0.30210 0.15930 0.01380  0.02130  0.06340  24   TYR A CB    
149  C  CG    . TYR A 24  ? 0.47660 0.30610 0.15780 0.02660  0.01050  0.08300  24   TYR A CG    
150  C  CD1   . TYR A 24  ? 0.47840 0.32750 0.17970 0.06870  0.01210  0.08370  24   TYR A CD1   
151  C  CD2   . TYR A 24  ? 0.48280 0.33670 0.16480 0.06000  -0.02170 0.08280  24   TYR A CD2   
152  C  CE1   . TYR A 24  ? 0.51080 0.34930 0.18280 0.12810  -0.04130 0.03680  24   TYR A CE1   
153  C  CE2   . TYR A 24  ? 0.49110 0.36320 0.16300 0.07580  -0.02630 0.05760  24   TYR A CE2   
154  C  CZ    . TYR A 24  ? 0.51540 0.40330 0.17760 0.07770  -0.02300 0.03640  24   TYR A CZ    
155  O  OH    . TYR A 24  ? 0.60830 0.46600 0.20040 0.06650  -0.04140 0.02900  24   TYR A OH    
156  N  N     . GLN A 25  ? 0.45560 0.24820 0.20530 0.06850  0.03430  0.02210  25   GLN A N     
157  C  CA    A GLN A 25  ? 0.49510 0.25090 0.23450 0.03380  0.01790  0.02480  25   GLN A CA    
158  C  CA    B GLN A 25  ? 0.47560 0.25790 0.21770 0.04750  0.01410  0.02460  25   GLN A CA    
159  C  C     . GLN A 25  ? 0.48810 0.26010 0.23600 0.01970  0.01190  0.02350  25   GLN A C     
160  O  O     . GLN A 25  ? 0.48840 0.26940 0.23440 0.04570  -0.00540 0.04540  25   GLN A O     
161  C  CB    A GLN A 25  ? 0.51200 0.30480 0.25800 0.04690  0.01740  0.04990  25   GLN A CB    
162  C  CB    B GLN A 25  ? 0.48320 0.32640 0.22010 0.09260  -0.00870 0.03850  25   GLN A CB    
163  C  CG    A GLN A 25  ? 0.49370 0.28670 0.26190 0.05880  0.01100  0.09300  25   GLN A CG    
164  C  CG    B GLN A 25  ? 0.46000 0.33730 0.22300 0.14960  -0.03630 0.06430  25   GLN A CG    
165  C  CD    A GLN A 25  ? 0.45280 0.29450 0.27150 0.06280  0.05400  0.13910  25   GLN A CD    
166  C  CD    B GLN A 25  ? 0.50830 0.38830 0.24880 0.15930  -0.02990 0.05970  25   GLN A CD    
167  O  OE1   A GLN A 25  ? 0.52280 0.37160 0.28140 0.13170  0.08300  0.10020  25   GLN A OE1   
168  O  OE1   B GLN A 25  ? 0.54220 0.44460 0.25460 0.15490  -0.01660 0.09490  25   GLN A OE1   
169  N  NE2   A GLN A 25  ? 0.43359 0.39910 0.25501 0.13858  0.02530  0.14898  25   GLN A NE2   
170  N  NE2   B GLN A 25  ? 0.51570 0.37990 0.25450 0.19760  -0.03500 0.03310  25   GLN A NE2   
171  N  N     . LEU A 26  ? 0.50230 0.25310 0.23570 0.01580  0.05340  0.02280  26   LEU A N     
172  C  CA    . LEU A 26  ? 0.53790 0.32170 0.24440 -0.01770 0.09530  -0.00020 26   LEU A CA    
173  C  C     . LEU A 26  ? 0.62750 0.31490 0.25160 -0.04130 0.06000  0.04260  26   LEU A C     
174  O  O     . LEU A 26  ? 0.66430 0.32580 0.24380 -0.05180 0.05290  0.05430  26   LEU A O     
175  C  CB    . LEU A 26  ? 0.57440 0.33430 0.27220 0.00530  0.09650  0.00240  26   LEU A CB    
176  C  CG    . LEU A 26  ? 0.54870 0.32760 0.28620 -0.00120 0.10370  -0.01650 26   LEU A CG    
177  C  CD1   . LEU A 26  ? 0.58210 0.27710 0.29160 0.00150  0.12280  -0.04000 26   LEU A CD1   
178  C  CD2   . LEU A 26  ? 0.51010 0.39900 0.28480 -0.04220 0.04270  -0.02790 26   LEU A CD2   
179  N  N     . PRO A 27  ? 0.60500 0.27990 0.25970 -0.04590 0.04800  0.04900  27   PRO A N     
180  C  CA    . PRO A 27  ? 0.61820 0.32040 0.27740 -0.04950 0.04330  0.06810  27   PRO A CA    
181  C  C     . PRO A 27  ? 0.68090 0.36980 0.28160 -0.10450 0.03030  0.12240  27   PRO A C     
182  O  O     . PRO A 27  ? 0.68950 0.32520 0.26800 -0.06580 -0.02160 0.10410  27   PRO A O     
183  C  CB    . PRO A 27  ? 0.61960 0.32950 0.29450 -0.01700 0.05210  0.06740  27   PRO A CB    
184  C  CG    . PRO A 27  ? 0.59360 0.27420 0.30060 -0.00750 0.05280  0.03440  27   PRO A CG    
185  C  CD    . PRO A 27  ? 0.59640 0.26290 0.28060 -0.00750 0.03600  0.03590  27   PRO A CD    
186  N  N     . ASP A 28  ? 0.74510 0.46240 0.30420 -0.08600 0.02770  0.16150  28   ASP A N     
187  C  CA    . ASP A 28  ? 0.75917 0.54551 0.34883 -0.09418 0.05560  0.20898  28   ASP A CA    
188  C  C     . ASP A 28  ? 0.71258 0.48021 0.35541 -0.07949 0.05630  0.20799  28   ASP A C     
189  O  O     . ASP A 28  ? 0.70750 0.49930 0.35140 -0.06870 0.04390  0.17570  28   ASP A O     
190  C  CB    . ASP A 28  ? 0.85030 0.67240 0.38350 -0.09590 0.07090  0.24540  28   ASP A CB    
191  C  CG    . ASP A 28  ? 0.92780 0.81910 0.41770 -0.13140 0.09470  0.25010  28   ASP A CG    
192  O  OD1   . ASP A 28  ? 0.93760 0.86350 0.43200 -0.15060 0.09160  0.23880  28   ASP A OD1   
193  O  OD2   . ASP A 28  ? 0.96740 0.84740 0.45210 -0.14070 0.07960  0.27770  28   ASP A OD2   
194  N  N     . GLY A 29  ? 0.69987 0.42031 0.35752 -0.05839 0.05030  0.19729  29   GLY A N     
195  C  CA    . GLY A 29  ? 0.65380 0.36570 0.36140 -0.05900 0.05030  0.16950  29   GLY A CA    
196  C  C     . GLY A 29  ? 0.58350 0.34930 0.36940 -0.05470 0.04220  0.10720  29   GLY A C     
197  O  O     . GLY A 29  ? 0.53070 0.28490 0.37330 -0.00960 0.01970  0.05470  29   GLY A O     
198  N  N     . TYR A 30  ? 0.50890 0.26580 0.36520 -0.09520 0.02410  0.11770  30   TYR A N     
199  C  CA    . TYR A 30  ? 0.52410 0.24440 0.35900 -0.02010 0.00850  0.13830  30   TYR A CA    
200  C  C     . TYR A 30  ? 0.52230 0.31690 0.38280 -0.02430 -0.03820 0.16090  30   TYR A C     
201  O  O     . TYR A 30  ? 0.51270 0.29840 0.37410 -0.04980 -0.03780 0.13400  30   TYR A O     
202  C  CB    . TYR A 30  ? 0.54020 0.23130 0.33620 0.02550  0.01790  0.09210  30   TYR A CB    
203  C  CG    . TYR A 30  ? 0.51940 0.27400 0.30130 0.02250  0.06140  0.04560  30   TYR A CG    
204  C  CD1   . TYR A 30  ? 0.51270 0.27010 0.29330 0.02240  0.06460  0.04280  30   TYR A CD1   
205  C  CD2   . TYR A 30  ? 0.48510 0.24370 0.26810 0.00970  0.09380  0.05720  30   TYR A CD2   
206  C  CE1   . TYR A 30  ? 0.49720 0.27960 0.28380 -0.01250 0.06260  0.04390  30   TYR A CE1   
207  C  CE2   . TYR A 30  ? 0.46530 0.22020 0.25850 -0.00030 0.08890  0.04500  30   TYR A CE2   
208  C  CZ    . TYR A 30  ? 0.48180 0.23960 0.25870 -0.02170 0.06560  0.06380  30   TYR A CZ    
209  O  OH    . TYR A 30  ? 0.48380 0.23770 0.24860 -0.05410 0.03480  0.07340  30   TYR A OH    
210  N  N     . ALA A 31  ? 0.50410 0.34450 0.42230 -0.02130 -0.08600 0.17640  31   ALA A N     
211  C  CA    . ALA A 31  ? 0.51070 0.38610 0.45180 -0.00660 -0.09170 0.19450  31   ALA A CA    
212  C  C     . ALA A 31  ? 0.54240 0.32850 0.48520 -0.02660 -0.10200 0.18860  31   ALA A C     
213  O  O     . ALA A 31  ? 0.55590 0.29090 0.48050 -0.06020 -0.12050 0.18480  31   ALA A O     
214  C  CB    . ALA A 31  ? 0.50770 0.44560 0.44880 -0.00350 -0.10300 0.20490  31   ALA A CB    
215  N  N     . GLN A 32  ? 0.56780 0.35240 0.51490 -0.03850 -0.07710 0.22260  32   GLN A N     
216  C  CA    . GLN A 32  ? 0.61140 0.34300 0.55050 -0.05650 -0.02660 0.19340  32   GLN A CA    
217  C  C     . GLN A 32  ? 0.55670 0.25040 0.52770 0.02240  -0.02710 0.13760  32   GLN A C     
218  O  O     . GLN A 32  ? 0.57800 0.22830 0.54210 0.04820  -0.04400 0.14620  32   GLN A O     
219  C  CB    . GLN A 32  ? 0.74640 0.43780 0.60540 -0.12110 0.00380  0.21150  32   GLN A CB    
220  C  CG    . GLN A 32  ? 0.89480 0.54360 0.65390 -0.09310 0.03160  0.23390  32   GLN A CG    
221  C  CD    . GLN A 32  ? 1.02100 0.64270 0.69860 -0.07390 0.04420  0.21530  32   GLN A CD    
222  O  OE1   . GLN A 32  ? 1.07320 0.62220 0.71210 -0.09670 0.05090  0.22780  32   GLN A OE1   
223  N  NE2   . GLN A 32  ? 1.06330 0.72570 0.71450 -0.06840 0.05400  0.20430  32   GLN A NE2   
224  N  N     . LEU A 33  ? 0.50480 0.22040 0.48310 0.00080  -0.01750 0.12430  33   LEU A N     
225  C  CA    . LEU A 33  ? 0.43240 0.20330 0.44740 0.01250  -0.02960 0.06350  33   LEU A CA    
226  C  C     . LEU A 33  ? 0.41730 0.24720 0.44220 0.01490  -0.00230 0.04280  33   LEU A C     
227  O  O     . LEU A 33  ? 0.43620 0.22490 0.45580 0.03000  0.01170  0.03940  33   LEU A O     
228  C  CB    . LEU A 33  ? 0.41510 0.20220 0.41930 0.03480  -0.01620 -0.01020 33   LEU A CB    
229  C  CG    . LEU A 33  ? 0.42600 0.20500 0.40830 0.04750  0.02790  -0.05460 33   LEU A CG    
230  C  CD1   . LEU A 33  ? 0.47600 0.19440 0.39980 0.01250  0.03500  -0.04760 33   LEU A CD1   
231  C  CD2   . LEU A 33  ? 0.46570 0.18530 0.41860 0.03210  0.01250  -0.03870 33   LEU A CD2   
232  N  N     . ARG A 34  ? 0.41010 0.21030 0.43030 -0.00080 -0.01760 0.05050  34   ARG A N     
233  C  CA    . ARG A 34  ? 0.44190 0.19990 0.42340 0.02090  -0.02470 0.07480  34   ARG A CA    
234  C  C     . ARG A 34  ? 0.47320 0.20100 0.45300 0.02740  -0.03170 0.05450  34   ARG A C     
235  O  O     . ARG A 34  ? 0.52730 0.18870 0.46650 0.03290  -0.00300 0.08160  34   ARG A O     
236  C  CB    . ARG A 34  ? 0.43020 0.19820 0.39060 -0.02430 -0.01230 0.06150  34   ARG A CB    
237  C  CG    . ARG A 34  ? 0.42140 0.21140 0.36060 0.01130  0.00560  0.05280  34   ARG A CG    
238  C  CD    . ARG A 34  ? 0.42910 0.23970 0.34780 0.01370  0.00560  0.05810  34   ARG A CD    
239  N  NE    . ARG A 34  ? 0.46870 0.25260 0.34370 0.00380  -0.02910 0.09000  34   ARG A NE    
240  C  CZ    . ARG A 34  ? 0.48040 0.22630 0.33210 0.03860  -0.03810 0.11720  34   ARG A CZ    
241  N  NH1   . ARG A 34  ? 0.46359 0.20341 0.32840 0.03670  -0.02000 0.12940  34   ARG A NH1   
242  N  NH2   . ARG A 34  ? 0.51750 0.31540 0.32970 0.02070  -0.01070 0.14320  34   ARG A NH2   
243  N  N     . ASP A 35  ? 0.54840 0.17900 0.47120 0.05650  -0.06370 0.06410  35   ASP A N     
244  C  CA    . ASP A 35  ? 0.57340 0.22580 0.49240 0.11940  -0.08790 0.05950  35   ASP A CA    
245  C  C     . ASP A 35  ? 0.56860 0.26180 0.50750 0.03090  -0.07370 0.03830  35   ASP A C     
246  O  O     . ASP A 35  ? 0.60990 0.26480 0.53160 -0.03060 -0.08070 -0.01160 35   ASP A O     
247  C  CB    . ASP A 35  ? 0.67428 0.24172 0.50470 0.12269  -0.08099 0.07679  35   ASP A CB    
248  C  CG    . ASP A 35  ? 0.74280 0.26650 0.51170 0.08420  -0.09160 0.11330  35   ASP A CG    
249  O  OD1   . ASP A 35  ? 0.79040 0.24850 0.53160 0.06030  -0.08380 0.10100  35   ASP A OD1   
250  O  OD2   . ASP A 35  ? 0.74246 0.28133 0.49611 0.04899  -0.09288 0.14658  35   ASP A OD2   
251  N  N     . THR A 36  ? 0.49900 0.31070 0.48870 0.04600  -0.04560 0.06350  36   THR A N     
252  C  CA    . THR A 36  ? 0.49690 0.42070 0.46820 -0.02100 -0.04150 0.07890  36   THR A CA    
253  C  C     . THR A 36  ? 0.53460 0.37900 0.45690 0.03180  -0.04940 0.07610  36   THR A C     
254  O  O     . THR A 36  ? 0.59940 0.36770 0.44670 0.03370  -0.05180 0.07810  36   THR A O     
255  C  CB    . THR A 36  ? 0.48090 0.57740 0.46560 -0.07610 -0.03070 0.07640  36   THR A CB    
256  O  OG1   . THR A 36  ? 0.47180 0.63540 0.46450 -0.15220 0.00600  0.09440  36   THR A OG1   
257  C  CG2   . THR A 36  ? 0.45460 0.60240 0.46430 -0.07200 -0.04040 0.09790  36   THR A CG2   
258  N  N     . PRO A 37  ? 0.51250 0.28880 0.45750 0.06390  -0.04550 0.05170  37   PRO A N     
259  C  CA    . PRO A 37  ? 0.48180 0.27510 0.46690 0.08970  -0.03550 0.03120  37   PRO A CA    
260  C  C     . PRO A 37  ? 0.45400 0.28280 0.46340 0.08030  -0.00840 0.02650  37   PRO A C     
261  O  O     . PRO A 37  ? 0.40680 0.29530 0.46250 -0.00730 -0.01150 0.00930  37   PRO A O     
262  C  CB    . PRO A 37  ? 0.50810 0.26800 0.47150 0.09670  -0.02320 0.03330  37   PRO A CB    
263  C  CG    . PRO A 37  ? 0.52950 0.29100 0.47220 0.10180  -0.03830 0.06580  37   PRO A CG    
264  C  CD    . PRO A 37  ? 0.53760 0.28200 0.46660 0.10950  -0.03780 0.06820  37   PRO A CD    
265  N  N     . GLY A 38  ? 0.44620 0.23910 0.47440 0.02200  0.00530  0.00900  38   GLY A N     
266  C  CA    . GLY A 38  ? 0.46790 0.18690 0.46870 0.10270  0.03680  0.01990  38   GLY A CA    
267  C  C     . GLY A 38  ? 0.42170 0.18330 0.44940 0.08150  0.02350  -0.00730 38   GLY A C     
268  O  O     . GLY A 38  ? 0.43820 0.21880 0.44650 0.04490  0.01790  -0.05350 38   GLY A O     
269  N  N     . PRO A 39  ? 0.36050 0.17150 0.43140 -0.00320 0.04890  -0.05700 39   PRO A N     
270  C  CA    . PRO A 39  ? 0.34830 0.15660 0.40820 0.05030  0.04480  -0.05380 39   PRO A CA    
271  C  C     . PRO A 39  ? 0.35040 0.12290 0.37940 0.04010  0.04070  -0.05470 39   PRO A C     
272  O  O     . PRO A 39  ? 0.33320 0.12960 0.35760 0.02710  0.02050  -0.06280 39   PRO A O     
273  C  CB    . PRO A 39  ? 0.42320 0.16210 0.41930 0.03630  0.04980  -0.04480 39   PRO A CB    
274  C  CG    . PRO A 39  ? 0.43500 0.21160 0.42020 0.07320  0.07800  -0.05900 39   PRO A CG    
275  C  CD    . PRO A 39  ? 0.41390 0.20360 0.42570 -0.01950 0.04840  -0.05270 39   PRO A CD    
276  N  N     . LEU A 40  ? 0.34090 0.17220 0.39470 0.01130  0.02390  -0.00960 40   LEU A N     
277  C  CA    . LEU A 40  ? 0.32800 0.13690 0.39210 0.01240  0.01640  -0.03850 40   LEU A CA    
278  C  C     . LEU A 40  ? 0.35760 0.20330 0.40250 0.05540  0.00810  -0.03880 40   LEU A C     
279  O  O     . LEU A 40  ? 0.37880 0.19390 0.42340 0.02400  0.00640  -0.03330 40   LEU A O     
280  C  CB    . LEU A 40  ? 0.34540 0.16660 0.38570 0.02900  -0.00880 -0.05000 40   LEU A CB    
281  C  CG    . LEU A 40  ? 0.37920 0.18560 0.37600 -0.05180 0.02690  -0.05960 40   LEU A CG    
282  C  CD1   . LEU A 40  ? 0.41290 0.28190 0.37380 -0.02120 0.04980  -0.06810 40   LEU A CD1   
283  C  CD2   . LEU A 40  ? 0.41460 0.16980 0.38820 -0.03670 0.00780  -0.05500 40   LEU A CD2   
284  N  N     . HIS A 41  ? 0.35600 0.15870 0.38680 -0.00110 0.00240  -0.04500 41   HIS A N     
285  C  CA    . HIS A 41  ? 0.38610 0.18510 0.38090 -0.03120 0.01610  -0.02560 41   HIS A CA    
286  C  C     . HIS A 41  ? 0.38990 0.14420 0.37570 -0.05640 0.02790  -0.04790 41   HIS A C     
287  O  O     . HIS A 41  ? 0.39620 0.12230 0.36570 -0.01910 0.01950  -0.00730 41   HIS A O     
288  C  CB    . HIS A 41  ? 0.41020 0.11560 0.38330 -0.02330 0.01480  0.00800  41   HIS A CB    
289  C  CG    . HIS A 41  ? 0.39647 0.10795 0.39438 -0.03169 0.01358  0.02400  41   HIS A CG    
290  N  ND1   . HIS A 41  ? 0.42490 0.15570 0.40160 -0.01150 0.02290  0.03460  41   HIS A ND1   
291  C  CD2   . HIS A 41  ? 0.41540 0.14800 0.40940 0.04260  -0.00760 0.03930  41   HIS A CD2   
292  C  CE1   . HIS A 41  ? 0.42650 0.20450 0.40540 0.01700  0.00720  0.02940  41   HIS A CE1   
293  N  NE2   . HIS A 41  ? 0.41370 0.17730 0.40140 -0.00020 0.02000  0.04330  41   HIS A NE2   
294  N  N     . ARG A 42  ? 0.39310 0.14880 0.39840 -0.08980 0.03680  -0.03770 42   ARG A N     
295  C  CA    . ARG A 42  ? 0.37080 0.12430 0.42660 -0.04430 0.04760  -0.01840 42   ARG A CA    
296  C  C     . ARG A 42  ? 0.38600 0.13330 0.43300 -0.06280 0.03070  0.00660  42   ARG A C     
297  O  O     . ARG A 42  ? 0.41020 0.15320 0.42730 -0.02090 0.00260  -0.00080 42   ARG A O     
298  C  CB    . ARG A 42  ? 0.39849 0.13432 0.44359 -0.06149 0.04949  -0.01740 42   ARG A CB    
299  C  CG    . ARG A 42  ? 0.45789 0.13923 0.47549 -0.05409 0.03699  -0.03140 42   ARG A CG    
300  C  CD    . ARG A 42  ? 0.52249 0.20571 0.53269 -0.11619 0.09339  -0.06550 42   ARG A CD    
301  N  NE    . ARG A 42  ? 0.59310 0.26130 0.57240 -0.09370 0.10830  -0.10100 42   ARG A NE    
302  C  CZ    . ARG A 42  ? 0.70820 0.37740 0.59500 -0.09730 0.10190  -0.17150 42   ARG A CZ    
303  N  NH1   . ARG A 42  ? 0.75610 0.41990 0.60730 -0.10980 0.09720  -0.16420 42   ARG A NH1   
304  N  NH2   . ARG A 42  ? 0.73300 0.41050 0.60080 -0.05710 0.09170  -0.21870 42   ARG A NH2   
305  N  N     . VAL A 43  ? 0.37190 0.12830 0.44510 -0.02460 -0.00290 0.00430  43   VAL A N     
306  C  CA    . VAL A 43  ? 0.35990 0.11532 0.45198 -0.00680 0.02510  0.01180  43   VAL A CA    
307  C  C     . VAL A 43  ? 0.33140 0.15830 0.45980 -0.01770 0.02590  0.02540  43   VAL A C     
308  O  O     . VAL A 43  ? 0.33440 0.19910 0.45740 -0.02970 0.05640  0.02710  43   VAL A O     
309  C  CB    . VAL A 43  ? 0.41300 0.11751 0.43489 -0.04380 0.01100  0.01910  43   VAL A CB    
310  C  CG1   . VAL A 43  ? 0.37020 0.13750 0.45930 -0.04160 0.02030  0.00830  43   VAL A CG1   
311  C  CG2   . VAL A 43  ? 0.39720 0.12580 0.43970 -0.01410 0.04090  -0.01730 43   VAL A CG2   
312  N  N     . THR A 44  ? 0.36460 0.16160 0.45410 -0.05560 0.05250  0.03990  44   THR A N     
313  C  CA    . THR A 44  ? 0.38890 0.14010 0.47100 -0.05060 0.05060  0.03480  44   THR A CA    
314  C  C     . THR A 44  ? 0.39430 0.16450 0.48200 -0.01870 0.05460  0.03140  44   THR A C     
315  O  O     . THR A 44  ? 0.38620 0.20780 0.47820 -0.03770 0.07700  0.03260  44   THR A O     
316  C  CB    . THR A 44  ? 0.41600 0.17000 0.47930 -0.03040 0.03950  0.04930  44   THR A CB    
317  O  OG1   . THR A 44  ? 0.45420 0.19200 0.47800 -0.05660 0.06720  0.09130  44   THR A OG1   
318  C  CG2   . THR A 44  ? 0.43150 0.25440 0.48590 -0.00910 0.04540  0.05590  44   THR A CG2   
319  N  N     . LEU A 45  ? 0.38300 0.16630 0.49570 -0.04860 0.04900  0.01710  45   LEU A N     
320  C  CA    . LEU A 45  ? 0.39040 0.20360 0.48180 -0.00310 0.08080  0.04240  45   LEU A CA    
321  C  C     . LEU A 45  ? 0.40750 0.27080 0.48620 -0.00820 0.13030  0.04920  45   LEU A C     
322  O  O     . LEU A 45  ? 0.43610 0.25000 0.48900 -0.07210 0.14670  0.06320  45   LEU A O     
323  C  CB    . LEU A 45  ? 0.36130 0.21520 0.46000 -0.00170 0.05950  0.03090  45   LEU A CB    
324  C  CG    . LEU A 45  ? 0.35890 0.20120 0.44460 0.02010  0.04690  0.00790  45   LEU A CG    
325  C  CD1   . LEU A 45  ? 0.41780 0.20470 0.43770 -0.02690 0.02590  0.05030  45   LEU A CD1   
326  C  CD2   . LEU A 45  ? 0.38110 0.21940 0.43740 0.03070  0.07820  -0.04220 45   LEU A CD2   
327  N  N     . TYR A 46  ? 0.36740 0.32080 0.50500 -0.01200 0.15860  0.02860  46   TYR A N     
328  C  CA    . TYR A 46  ? 0.38210 0.32070 0.53120 -0.02250 0.12720  0.01530  46   TYR A CA    
329  C  C     . TYR A 46  ? 0.42430 0.38150 0.55290 -0.02990 0.12990  -0.00200 46   TYR A C     
330  O  O     . TYR A 46  ? 0.46220 0.42950 0.55160 -0.07320 0.13990  0.00520  46   TYR A O     
331  C  CB    . TYR A 46  ? 0.39170 0.25970 0.54150 0.02700  0.07920  0.02840  46   TYR A CB    
332  C  CG    . TYR A 46  ? 0.38100 0.27780 0.55970 0.03000  0.05340  0.01480  46   TYR A CG    
333  C  CD1   . TYR A 46  ? 0.42710 0.22630 0.56700 -0.00590 0.02160  0.02900  46   TYR A CD1   
334  C  CD2   . TYR A 46  ? 0.34770 0.31360 0.56500 0.08380  0.07040  0.00630  46   TYR A CD2   
335  C  CE1   . TYR A 46  ? 0.37810 0.20750 0.57640 0.01750  -0.00850 0.00680  46   TYR A CE1   
336  C  CE2   . TYR A 46  ? 0.35080 0.35450 0.57230 0.02090  0.03080  0.01360  46   TYR A CE2   
337  C  CZ    . TYR A 46  ? 0.37470 0.29930 0.58580 0.03010  -0.01150 -0.00090 46   TYR A CZ    
338  O  OH    . TYR A 46  ? 0.47100 0.36250 0.60960 0.04810  -0.02830 -0.02300 46   TYR A OH    
339  N  N     . ASP A 47  ? 0.40180 0.37900 0.57740 -0.04300 0.10590  -0.01500 47   ASP A N     
340  C  CA    . ASP A 47  ? 0.37560 0.38110 0.59940 -0.08180 0.08480  -0.03620 47   ASP A CA    
341  C  C     . ASP A 47  ? 0.32070 0.39690 0.61800 -0.14420 0.07290  -0.04570 47   ASP A C     
342  O  O     . ASP A 47  ? 0.40300 0.45040 0.63560 -0.11300 0.03030  -0.07890 47   ASP A O     
343  C  CB    . ASP A 47  ? 0.40320 0.42400 0.60720 -0.07180 0.07230  -0.02960 47   ASP A CB    
344  C  CG    . ASP A 47  ? 0.46690 0.42530 0.61890 -0.05090 0.01680  -0.02610 47   ASP A CG    
345  O  OD1   . ASP A 47  ? 0.45190 0.34390 0.62090 -0.06670 -0.01250 -0.01560 47   ASP A OD1   
346  O  OD2   . ASP A 47  ? 0.48310 0.47480 0.62020 0.00830  0.00080  -0.02330 47   ASP A OD2   
347  N  N     . GLY A 48  ? 0.38880 0.32420 0.61140 -0.08450 0.09210  -0.00540 48   GLY A N     
348  C  CA    . GLY A 48  ? 0.37180 0.30540 0.60350 -0.02880 0.10780  0.01420  48   GLY A CA    
349  C  C     . GLY A 48  ? 0.42740 0.34220 0.60360 -0.01310 0.04800  -0.00370 48   GLY A C     
350  O  O     . GLY A 48  ? 0.45740 0.35190 0.61540 -0.09100 0.03430  -0.01710 48   GLY A O     
351  N  N     . ARG A 49  ? 0.36980 0.33180 0.58830 -0.03530 0.04110  0.01560  49   ARG A N     
352  C  CA    . ARG A 49  ? 0.40110 0.34350 0.58060 -0.00170 0.03750  0.05670  49   ARG A CA    
353  C  C     . ARG A 49  ? 0.38090 0.25930 0.55610 -0.02440 0.03560  0.05920  49   ARG A C     
354  O  O     . ARG A 49  ? 0.38620 0.21460 0.55110 -0.02260 0.02360  0.03500  49   ARG A O     
355  C  CB    . ARG A 49  ? 0.51300 0.41900 0.59880 0.05460  0.03940  0.06760  49   ARG A CB    
356  C  CG    . ARG A 49  ? 0.68300 0.50320 0.61210 0.03640  0.05420  0.11340  49   ARG A CG    
357  C  CD    . ARG A 49  ? 0.83910 0.62380 0.62640 0.01280  0.06140  0.15950  49   ARG A CD    
358  N  NE    . ARG A 49  ? 0.98610 0.76710 0.64180 -0.01260 0.07850  0.18490  49   ARG A NE    
359  C  CZ    . ARG A 49  ? 1.10450 0.85840 0.65690 -0.03120 0.09090  0.19820  49   ARG A CZ    
360  N  NH1   . ARG A 49  ? 1.15650 0.90810 0.66160 -0.02690 0.08860  0.20460  49   ARG A NH1   
361  N  NH2   . ARG A 49  ? 1.12070 0.88720 0.66460 -0.03680 0.09580  0.18470  49   ARG A NH2   
362  N  N     . GLN A 50  ? 0.40630 0.26280 0.54520 -0.01590 0.03090  0.06620  50   GLN A N     
363  C  CA    . GLN A 50  ? 0.40620 0.24550 0.54000 0.03060  0.03330  0.06380  50   GLN A CA    
364  C  C     . GLN A 50  ? 0.41770 0.26720 0.51570 0.01060  0.01800  0.05980  50   GLN A C     
365  O  O     . GLN A 50  ? 0.40720 0.33570 0.52980 -0.04270 0.03860  0.09940  50   GLN A O     
366  C  CB    . GLN A 50  ? 0.52840 0.29190 0.56910 0.13740  0.04600  0.03170  50   GLN A CB    
367  C  CG    . GLN A 50  ? 0.71040 0.27530 0.59510 0.15730  0.05170  0.01630  50   GLN A CG    
368  C  CD    . GLN A 50  ? 0.83450 0.33150 0.61240 0.15850  0.05370  0.02360  50   GLN A CD    
369  O  OE1   . GLN A 50  ? 0.80137 0.27823 0.61410 0.18248  0.03819  0.05109  50   GLN A OE1   
370  N  NE2   . GLN A 50  ? 0.88320 0.33660 0.61860 0.09880  0.06670  0.01390  50   GLN A NE2   
371  N  N     . ALA A 51  ? 0.35470 0.19140 0.47230 -0.00370 0.05170  0.02890  51   ALA A N     
372  C  CA    . ALA A 51  ? 0.34790 0.13530 0.43470 -0.01750 0.06360  0.02860  51   ALA A CA    
373  C  C     . ALA A 51  ? 0.38110 0.16090 0.41780 -0.03010 0.03150  -0.00540 51   ALA A C     
374  O  O     . ALA A 51  ? 0.39330 0.18310 0.43420 0.00840  0.06410  0.00990  51   ALA A O     
375  C  CB    . ALA A 51  ? 0.38870 0.18670 0.43940 0.01030  0.06730  0.00810  51   ALA A CB    
376  N  N     . TRP A 52  ? 0.37760 0.12520 0.39620 -0.05180 0.02900  -0.03690 52   TRP A N     
377  C  CA    . TRP A 52  ? 0.30790 0.13990 0.37520 -0.06430 0.03890  -0.05350 52   TRP A CA    
378  C  C     . TRP A 52  ? 0.33270 0.12090 0.35120 -0.03560 0.02900  -0.03940 52   TRP A C     
379  O  O     . TRP A 52  ? 0.42260 0.13770 0.36170 0.00880  -0.00580 -0.02640 52   TRP A O     
380  C  CB    . TRP A 52  ? 0.35520 0.16110 0.35770 -0.01790 0.05460  -0.06110 52   TRP A CB    
381  C  CG    . TRP A 52  ? 0.35810 0.14020 0.35550 -0.02500 0.03630  -0.07640 52   TRP A CG    
382  C  CD1   . TRP A 52  ? 0.36130 0.15050 0.37050 -0.04680 -0.00160 -0.07310 52   TRP A CD1   
383  C  CD2   . TRP A 52  ? 0.34300 0.15200 0.35980 -0.00150 0.01640  -0.05160 52   TRP A CD2   
384  N  NE1   . TRP A 52  ? 0.38350 0.12610 0.38780 -0.03130 -0.03530 -0.04270 52   TRP A NE1   
385  C  CE2   . TRP A 52  ? 0.36220 0.15330 0.37730 0.02970  -0.04120 -0.04400 52   TRP A CE2   
386  C  CE3   . TRP A 52  ? 0.39310 0.13670 0.35110 0.00060  0.02430  -0.02000 52   TRP A CE3   
387  C  CZ2   . TRP A 52  ? 0.42670 0.16470 0.38550 0.03320  -0.04030 -0.03360 52   TRP A CZ2   
388  C  CZ3   . TRP A 52  ? 0.40600 0.14700 0.36240 -0.05710 -0.01180 -0.01690 52   TRP A CZ3   
389  C  CH2   . TRP A 52  ? 0.43400 0.17160 0.37750 -0.01870 -0.03500 -0.02240 52   TRP A CH2   
390  N  N     . VAL A 53  ? 0.33810 0.12870 0.32830 -0.03860 0.03780  -0.03370 53   VAL A N     
391  C  CA    . VAL A 53  ? 0.33070 0.12350 0.31350 -0.05280 0.03450  -0.03560 53   VAL A CA    
392  C  C     . VAL A 53  ? 0.34850 0.14180 0.30140 0.02310  0.01820  -0.03990 53   VAL A C     
393  O  O     . VAL A 53  ? 0.35400 0.13480 0.29420 0.01270  0.03890  -0.02010 53   VAL A O     
394  C  CB    . VAL A 53  ? 0.39590 0.13910 0.30820 0.00630  0.00670  -0.03840 53   VAL A CB    
395  C  CG1   . VAL A 53  ? 0.39770 0.16280 0.30310 -0.01750 0.05120  -0.03780 53   VAL A CG1   
396  C  CG2   . VAL A 53  ? 0.40410 0.16310 0.31570 -0.00320 -0.00170 -0.03330 53   VAL A CG2   
397  N  N     . VAL A 54  ? 0.35610 0.12690 0.29310 -0.01300 0.03540  -0.05070 54   VAL A N     
398  C  CA    . VAL A 54  ? 0.32190 0.14430 0.29920 -0.01210 0.00380  -0.03780 54   VAL A CA    
399  C  C     . VAL A 54  ? 0.32770 0.14490 0.29890 -0.00500 0.01150  -0.03900 54   VAL A C     
400  O  O     . VAL A 54  ? 0.35470 0.15060 0.31820 -0.03600 0.02760  -0.05850 54   VAL A O     
401  C  CB    . VAL A 54  ? 0.32730 0.14220 0.28260 0.01020  -0.00190 -0.00330 54   VAL A CB    
402  C  CG1   . VAL A 54  ? 0.33600 0.17120 0.29810 0.01550  0.02770  -0.02480 54   VAL A CG1   
403  C  CG2   . VAL A 54  ? 0.35390 0.14200 0.25090 -0.01430 -0.02070 -0.03920 54   VAL A CG2   
404  N  N     . THR A 55  ? 0.32010 0.14130 0.29790 0.02620  0.01430  -0.00380 55   THR A N     
405  C  CA    . THR A 55  ? 0.32610 0.20840 0.29820 -0.02160 0.03480  -0.01530 55   THR A CA    
406  C  C     . THR A 55  ? 0.32900 0.26130 0.30480 0.01430  0.00270  -0.04380 55   THR A C     
407  O  O     . THR A 55  ? 0.36210 0.41040 0.32780 -0.04050 -0.01560 -0.07700 55   THR A O     
408  C  CB    . THR A 55  ? 0.40460 0.22630 0.30940 -0.02710 0.05080  -0.00840 55   THR A CB    
409  O  OG1   . THR A 55  ? 0.47730 0.22320 0.31530 0.04470  0.00640  0.02750  55   THR A OG1   
410  C  CG2   . THR A 55  ? 0.40240 0.26170 0.31530 -0.08580 0.05120  -0.00340 55   THR A CG2   
411  N  N     . LYS A 56  ? 0.33180 0.19500 0.27090 0.06200  0.02010  -0.03970 56   LYS A N     
412  C  CA    . LYS A 56  ? 0.29470 0.14040 0.26430 0.03630  0.02710  -0.02230 56   LYS A CA    
413  C  C     . LYS A 56  ? 0.29570 0.14130 0.25630 0.03520  0.00310  -0.02120 56   LYS A C     
414  O  O     . LYS A 56  ? 0.32150 0.16970 0.24990 0.00280  -0.02850 0.00510  56   LYS A O     
415  C  CB    . LYS A 56  ? 0.36440 0.14800 0.29240 0.02340  0.04220  -0.01040 56   LYS A CB    
416  C  CG    . LYS A 56  ? 0.42050 0.16770 0.31430 0.02490  0.05480  -0.01010 56   LYS A CG    
417  C  CD    . LYS A 56  ? 0.46090 0.17600 0.36350 0.00840  0.02670  0.00810  56   LYS A CD    
418  C  CE    . LYS A 56  ? 0.42380 0.21240 0.40260 -0.02060 0.05150  0.02560  56   LYS A CE    
419  N  NZ    . LYS A 56  ? 0.52510 0.23690 0.42670 0.02820  0.06850  0.07580  56   LYS A NZ    
420  N  N     . HIS A 57  ? 0.28330 0.14510 0.23400 -0.00830 -0.00400 -0.03730 57   HIS A N     
421  C  CA    . HIS A 57  ? 0.31870 0.13840 0.20730 -0.01910 0.01530  -0.04930 57   HIS A CA    
422  C  C     . HIS A 57  ? 0.30559 0.13271 0.21820 0.06359  0.01800  -0.06169 57   HIS A C     
423  O  O     . HIS A 57  ? 0.33080 0.18970 0.21500 0.02030  -0.00950 -0.03110 57   HIS A O     
424  C  CB    . HIS A 57  ? 0.31330 0.16530 0.19530 -0.01860 -0.01430 -0.01240 57   HIS A CB    
425  C  CG    . HIS A 57  ? 0.30340 0.16010 0.15190 -0.02420 -0.01470 0.00360  57   HIS A CG    
426  N  ND1   . HIS A 57  ? 0.31050 0.21210 0.15990 -0.05590 -0.03410 0.01230  57   HIS A ND1   
427  C  CD2   . HIS A 57  ? 0.31600 0.15800 0.16280 0.02310  -0.02370 -0.00290 57   HIS A CD2   
428  C  CE1   . HIS A 57  ? 0.31520 0.19150 0.16520 0.02860  -0.00390 0.02350  57   HIS A CE1   
429  N  NE2   . HIS A 57  ? 0.33840 0.21700 0.14980 0.02620  0.02160  0.02470  57   HIS A NE2   
430  N  N     . GLU A 58  ? 0.32070 0.20880 0.23390 0.03440  0.00480  -0.12719 58   GLU A N     
431  C  CA    . GLU A 58  ? 0.28540 0.25860 0.24360 0.02030  0.00400  -0.11360 58   GLU A CA    
432  C  C     . GLU A 58  ? 0.29570 0.24220 0.25230 -0.01660 -0.00900 -0.09690 58   GLU A C     
433  O  O     . GLU A 58  ? 0.30940 0.21300 0.24980 -0.01070 0.00020  -0.08220 58   GLU A O     
434  C  CB    . GLU A 58  ? 0.33780 0.33380 0.25920 0.07230  -0.00030 -0.09530 58   GLU A CB    
435  C  CG    . GLU A 58  ? 0.35000 0.32740 0.28380 -0.00990 0.01900  -0.10310 58   GLU A CG    
436  C  CD    . GLU A 58  ? 0.39550 0.36410 0.27530 0.00420  0.02640  -0.10740 58   GLU A CD    
437  O  OE1   . GLU A 58  ? 0.38840 0.33150 0.28890 0.01050  0.02670  -0.07770 58   GLU A OE1   
438  O  OE2   . GLU A 58  ? 0.43760 0.37880 0.28410 -0.02610 0.01850  -0.10430 58   GLU A OE2   
439  N  N     . ALA A 59  ? 0.31020 0.17170 0.27010 0.01600  0.00400  -0.08720 59   ALA A N     
440  C  CA    . ALA A 59  ? 0.38240 0.15220 0.29420 0.01670  0.00510  -0.07850 59   ALA A CA    
441  C  C     . ALA A 59  ? 0.33800 0.13420 0.28770 0.00960  -0.02350 -0.09020 59   ALA A C     
442  O  O     . ALA A 59  ? 0.32170 0.20140 0.29400 0.04480  -0.03730 -0.09900 59   ALA A O     
443  C  CB    . ALA A 59  ? 0.39400 0.16570 0.30200 0.01290  0.01460  -0.05040 59   ALA A CB    
444  N  N     . ALA A 60  ? 0.31418 0.12452 0.25170 0.01519  0.00080  -0.08739 60   ALA A N     
445  C  CA    . ALA A 60  ? 0.32740 0.14180 0.22070 0.05080  0.01170  -0.06430 60   ALA A CA    
446  C  C     . ALA A 60  ? 0.33570 0.12280 0.22740 0.01930  0.02540  -0.04440 60   ALA A C     
447  O  O     . ALA A 60  ? 0.30570 0.15430 0.22870 0.00530  0.01640  -0.02640 60   ALA A O     
448  C  CB    . ALA A 60  ? 0.32110 0.16380 0.22590 0.03450  0.02310  -0.07080 60   ALA A CB    
449  N  N     . ARG A 61  ? 0.29070 0.16610 0.21120 0.00870  0.02960  -0.04310 61   ARG A N     
450  C  CA    . ARG A 61  ? 0.26820 0.21340 0.20890 -0.03610 0.00790  -0.03100 61   ARG A CA    
451  C  C     . ARG A 61  ? 0.29560 0.17410 0.23550 -0.03000 -0.01490 -0.05130 61   ARG A C     
452  O  O     . ARG A 61  ? 0.31530 0.19070 0.25060 -0.02820 -0.00670 -0.03210 61   ARG A O     
453  C  CB    . ARG A 61  ? 0.25620 0.17430 0.17970 -0.00550 0.00200  -0.01510 61   ARG A CB    
454  C  CG    . ARG A 61  ? 0.32600 0.19590 0.17530 -0.04350 -0.01040 0.00470  61   ARG A CG    
455  C  CD    . ARG A 61  ? 0.27500 0.22120 0.16890 -0.02830 0.01510  0.02210  61   ARG A CD    
456  N  NE    . ARG A 61  ? 0.32870 0.26120 0.17630 -0.00330 0.02280  0.03170  61   ARG A NE    
457  C  CZ    . ARG A 61  ? 0.34130 0.23070 0.16750 0.00440  0.05460  0.03010  61   ARG A CZ    
458  N  NH1   . ARG A 61  ? 0.32350 0.19990 0.14900 0.03300  0.01020  0.02160  61   ARG A NH1   
459  N  NH2   . ARG A 61  ? 0.31380 0.25420 0.15520 -0.01010 0.00740  0.01000  61   ARG A NH2   
460  N  N     . LYS A 62  ? 0.28620 0.17650 0.26190 -0.03690 0.03210  -0.08780 62   LYS A N     
461  C  CA    . LYS A 62  ? 0.29730 0.17350 0.26980 -0.02150 0.00890  -0.12190 62   LYS A CA    
462  C  C     . LYS A 62  ? 0.28470 0.20590 0.25210 -0.00610 0.02280  -0.11280 62   LYS A C     
463  O  O     . LYS A 62  ? 0.34120 0.28560 0.25300 -0.01460 0.01750  -0.06880 62   LYS A O     
464  C  CB    . LYS A 62  ? 0.39870 0.20460 0.30810 0.02540  0.02370  -0.14070 62   LYS A CB    
465  C  CG    . LYS A 62  ? 0.52820 0.27300 0.34470 0.02680  0.03100  -0.16760 62   LYS A CG    
466  C  CD    . LYS A 62  ? 0.70160 0.39310 0.36150 -0.02390 0.04120  -0.18790 62   LYS A CD    
467  C  CE    . LYS A 62  ? 0.76680 0.42620 0.39510 -0.04400 0.07010  -0.19160 62   LYS A CE    
468  N  NZ    . LYS A 62  ? 0.82140 0.49080 0.41960 -0.08300 0.05580  -0.17500 62   LYS A NZ    
469  N  N     . LEU A 63  ? 0.28480 0.14160 0.23130 -0.02390 0.02160  -0.05140 63   LEU A N     
470  C  CA    . LEU A 63  ? 0.29160 0.13030 0.22670 -0.03140 0.01490  -0.02820 63   LEU A CA    
471  C  C     . LEU A 63  ? 0.32570 0.14120 0.21640 -0.01730 0.01110  -0.05350 63   LEU A C     
472  O  O     . LEU A 63  ? 0.30770 0.18190 0.22370 -0.00850 0.02420  -0.03910 63   LEU A O     
473  C  CB    . LEU A 63  ? 0.35957 0.11493 0.22700 -0.01580 0.00430  -0.05719 63   LEU A CB    
474  C  CG    . LEU A 63  ? 0.36510 0.14690 0.23250 -0.01830 -0.01440 -0.07040 63   LEU A CG    
475  C  CD1   . LEU A 63  ? 0.36860 0.13960 0.23710 -0.02420 0.03050  -0.01920 63   LEU A CD1   
476  C  CD2   . LEU A 63  ? 0.39610 0.15460 0.25120 -0.01100 -0.03830 -0.05830 63   LEU A CD2   
477  N  N     . LEU A 64  ? 0.31740 0.11030 0.21390 -0.00260 0.00650  -0.04250 64   LEU A N     
478  C  CA    . LEU A 64  ? 0.31840 0.14750 0.19370 -0.02240 -0.00780 -0.05330 64   LEU A CA    
479  C  C     . LEU A 64  ? 0.32250 0.17720 0.20640 -0.01060 0.01960  -0.03960 64   LEU A C     
480  O  O     . LEU A 64  ? 0.30220 0.19260 0.23810 -0.01840 0.03310  -0.01560 64   LEU A O     
481  C  CB    . LEU A 64  ? 0.30940 0.15680 0.20100 -0.00840 -0.03320 -0.04570 64   LEU A CB    
482  C  CG    . LEU A 64  ? 0.26440 0.17950 0.22680 -0.01860 -0.02410 -0.01880 64   LEU A CG    
483  C  CD1   . LEU A 64  ? 0.36300 0.17260 0.23230 0.02610  -0.07870 -0.07250 64   LEU A CD1   
484  C  CD2   . LEU A 64  ? 0.27110 0.20820 0.23680 0.03930  -0.00550 -0.01040 64   LEU A CD2   
485  N  N     . GLY A 65  ? 0.31090 0.17050 0.19460 -0.02130 0.03520  -0.03520 65   GLY A N     
486  C  CA    . GLY A 65  ? 0.33920 0.22370 0.18180 -0.03400 0.02530  -0.05670 65   GLY A CA    
487  C  C     . GLY A 65  ? 0.31870 0.17210 0.20400 0.00420  0.03350  -0.02390 65   GLY A C     
488  O  O     . GLY A 65  ? 0.38860 0.23510 0.21620 -0.01880 0.05530  -0.05370 65   GLY A O     
489  N  N     . ASP A 66  ? 0.27820 0.20870 0.21070 -0.00960 0.01110  -0.03850 66   ASP A N     
490  C  CA    . ASP A 66  ? 0.29110 0.23190 0.21890 -0.03850 0.00740  -0.05510 66   ASP A CA    
491  C  C     . ASP A 66  ? 0.29000 0.22390 0.19970 -0.02920 0.00070  -0.04740 66   ASP A C     
492  O  O     . ASP A 66  ? 0.29890 0.26770 0.19580 -0.00680 -0.01370 -0.05150 66   ASP A O     
493  C  CB    . ASP A 66  ? 0.36260 0.19770 0.23380 0.02840  0.00380  -0.06570 66   ASP A CB    
494  C  CG    . ASP A 66  ? 0.37250 0.18550 0.23990 0.08450  -0.00260 -0.07470 66   ASP A CG    
495  O  OD1   . ASP A 66  ? 0.38140 0.23540 0.24230 0.00810  -0.01380 -0.07000 66   ASP A OD1   
496  O  OD2   . ASP A 66  ? 0.48300 0.26110 0.26410 0.09430  -0.00480 -0.09440 66   ASP A OD2   
497  N  N     . PRO A 67  ? 0.31120 0.25990 0.20880 -0.05780 0.03060  -0.03150 67   PRO A N     
498  C  CA    . PRO A 67  ? 0.33570 0.28450 0.21290 -0.05180 0.01790  -0.00760 67   PRO A CA    
499  C  C     . PRO A 67  ? 0.38020 0.24010 0.22280 -0.04150 0.01770  -0.04030 67   PRO A C     
500  O  O     . PRO A 67  ? 0.36160 0.21780 0.24030 -0.00770 -0.01990 -0.02440 67   PRO A O     
501  C  CB    . PRO A 67  ? 0.41440 0.35540 0.21170 -0.02800 0.00810  0.03170  67   PRO A CB    
502  C  CG    . PRO A 67  ? 0.44370 0.41020 0.20760 -0.01010 0.01380  0.03120  67   PRO A CG    
503  C  CD    . PRO A 67  ? 0.32710 0.37890 0.19150 -0.05490 -0.00850 -0.03480 67   PRO A CD    
504  N  N     . ARG A 68  ? 0.37630 0.16220 0.21900 -0.04390 0.01510  -0.08460 68   ARG A N     
505  C  CA    . ARG A 68  ? 0.37189 0.17091 0.22270 -0.02950 0.01530  -0.09689 68   ARG A CA    
506  C  C     . ARG A 68  ? 0.34210 0.17940 0.23510 -0.00870 0.00050  -0.06070 68   ARG A C     
507  O  O     . ARG A 68  ? 0.34450 0.20120 0.26430 -0.05230 -0.02410 -0.08030 68   ARG A O     
508  C  CB    . ARG A 68  ? 0.43450 0.22090 0.24630 0.00290  0.03530  -0.10130 68   ARG A CB    
509  C  CG    . ARG A 68  ? 0.40420 0.29120 0.25740 0.05170  0.01110  -0.14150 68   ARG A CG    
510  C  CD    . ARG A 68  ? 0.39620 0.28580 0.26410 0.04580  0.00710  -0.14740 68   ARG A CD    
511  N  NE    . ARG A 68  ? 0.41450 0.27980 0.29290 0.04580  0.00090  -0.13230 68   ARG A NE    
512  C  CZ    . ARG A 68  ? 0.44980 0.22940 0.31880 0.05100  0.01500  -0.14100 68   ARG A CZ    
513  N  NH1   . ARG A 68  ? 0.54308 0.23412 0.35471 0.02710  0.01650  -0.14339 68   ARG A NH1   
514  N  NH2   . ARG A 68  ? 0.42610 0.23000 0.32550 0.02430  0.01380  -0.09450 68   ARG A NH2   
515  N  N     . LEU A 69  ? 0.33160 0.18740 0.22130 0.00860  -0.00710 -0.03210 69   LEU A N     
516  C  CA    . LEU A 69  ? 0.31800 0.20760 0.23150 0.02440  -0.01070 -0.00770 69   LEU A CA    
517  C  C     . LEU A 69  ? 0.30630 0.18050 0.24260 0.00060  -0.01940 -0.05860 69   LEU A C     
518  O  O     . LEU A 69  ? 0.28900 0.19950 0.26410 -0.00840 -0.00640 -0.05110 69   LEU A O     
519  C  CB    . LEU A 69  ? 0.33950 0.22330 0.24440 -0.01200 -0.02570 -0.03210 69   LEU A CB    
520  C  CG    . LEU A 69  ? 0.32820 0.20490 0.28170 -0.00700 -0.05140 -0.01530 69   LEU A CG    
521  C  CD1   . LEU A 69  ? 0.35330 0.28820 0.29270 0.00130  -0.08630 0.03940  69   LEU A CD1   
522  C  CD2   . LEU A 69  ? 0.32600 0.20540 0.29530 -0.01990 -0.03730 -0.00390 69   LEU A CD2   
523  N  N     . SER A 70  ? 0.26990 0.23150 0.21910 0.03670  -0.06430 -0.09090 70   SER A N     
524  C  CA    . SER A 70  ? 0.28710 0.25200 0.25020 0.04580  -0.07530 -0.10490 70   SER A CA    
525  C  C     . SER A 70  ? 0.27740 0.22330 0.24760 0.05970  -0.06440 -0.09400 70   SER A C     
526  O  O     . SER A 70  ? 0.31850 0.18300 0.26510 0.01260  -0.05320 -0.07730 70   SER A O     
527  C  CB    . SER A 70  ? 0.34330 0.24560 0.27210 0.02130  -0.07850 -0.13210 70   SER A CB    
528  O  OG    . SER A 70  ? 0.35430 0.28220 0.28630 0.06020  -0.06050 -0.14340 70   SER A OG    
529  N  N     . SER A 71  ? 0.33130 0.19870 0.25000 0.06610  -0.06650 -0.10540 71   SER A N     
530  C  CA    . SER A 71  ? 0.32580 0.13350 0.27570 0.03830  -0.04320 -0.08300 71   SER A CA    
531  C  C     . SER A 71  ? 0.29770 0.19470 0.32310 0.02040  -0.07090 -0.08570 71   SER A C     
532  O  O     . SER A 71  ? 0.30930 0.20750 0.35240 -0.00150 -0.06000 -0.11780 71   SER A O     
533  C  CB    . SER A 71  ? 0.32819 0.15411 0.26620 0.06519  -0.06029 -0.08789 71   SER A CB    
534  O  OG    . SER A 71  ? 0.30790 0.16360 0.25730 0.06590  -0.06550 -0.06770 71   SER A OG    
535  N  N     . ASN A 72  ? 0.31450 0.22320 0.34640 -0.03320 -0.08400 -0.06450 72   ASN A N     
536  C  CA    . ASN A 72  ? 0.27230 0.24480 0.36590 -0.02070 -0.07730 -0.08440 72   ASN A CA    
537  C  C     . ASN A 72  ? 0.31430 0.32060 0.38450 -0.00550 -0.08010 -0.09440 72   ASN A C     
538  O  O     . ASN A 72  ? 0.36110 0.38040 0.37940 0.01170  -0.06750 -0.08550 72   ASN A O     
539  C  CB    . ASN A 72  ? 0.29960 0.25530 0.35840 0.02020  -0.12540 -0.08170 72   ASN A CB    
540  C  CG    . ASN A 72  ? 0.34970 0.26030 0.35850 0.00160  -0.08140 -0.07610 72   ASN A CG    
541  O  OD1   . ASN A 72  ? 0.38260 0.28580 0.37100 0.01290  -0.05400 -0.07580 72   ASN A OD1   
542  N  ND2   . ASN A 72  ? 0.44930 0.30360 0.34860 0.01270  -0.08020 -0.06930 72   ASN A ND2   
543  N  N     . ARG A 73  ? 0.30460 0.33320 0.42510 0.00180  -0.05310 -0.12840 73   ARG A N     
544  C  CA    A ARG A 73  ? 0.36320 0.37740 0.43810 -0.01550 -0.03590 -0.14020 73   ARG A CA    
545  C  CA    B ARG A 73  ? 0.34950 0.34270 0.43630 -0.02950 -0.05210 -0.15670 73   ARG A CA    
546  C  C     . ARG A 73  ? 0.36440 0.38480 0.46050 0.00560  -0.03660 -0.13490 73   ARG A C     
547  O  O     . ARG A 73  ? 0.38730 0.43340 0.47780 0.02070  -0.00090 -0.12010 73   ARG A O     
548  C  CB    A ARG A 73  ? 0.40190 0.41390 0.42900 -0.00790 -0.01590 -0.14870 73   ARG A CB    
549  C  CB    B ARG A 73  ? 0.34950 0.32870 0.42830 -0.02710 -0.06320 -0.18830 73   ARG A CB    
550  C  CG    A ARG A 73  ? 0.46030 0.46950 0.42790 -0.03800 0.00490  -0.13350 73   ARG A CG    
551  C  CG    B ARG A 73  ? 0.35950 0.35500 0.43860 -0.10190 -0.06480 -0.17130 73   ARG A CG    
552  C  CD    A ARG A 73  ? 0.49230 0.48730 0.41790 -0.08150 0.00850  -0.12200 73   ARG A CD    
553  C  CD    B ARG A 73  ? 0.40380 0.35550 0.42860 -0.11870 -0.09300 -0.16230 73   ARG A CD    
554  N  NE    A ARG A 73  ? 0.53550 0.47090 0.40850 -0.10850 0.00360  -0.11240 73   ARG A NE    
555  N  NE    B ARG A 73  ? 0.42220 0.39170 0.43020 -0.15680 -0.10150 -0.14290 73   ARG A NE    
556  C  CZ    A ARG A 73  ? 0.48480 0.41000 0.38490 -0.18170 0.00470  -0.09720 73   ARG A CZ    
557  C  CZ    B ARG A 73  ? 0.39460 0.35210 0.42260 -0.07440 -0.08980 -0.11700 73   ARG A CZ    
558  N  NH1   A ARG A 73  ? 0.53390 0.43040 0.39130 -0.16330 0.01110  -0.07830 73   ARG A NH1   
559  N  NH1   B ARG A 73  ? 0.45590 0.44760 0.43850 -0.07560 -0.06070 -0.08080 73   ARG A NH1   
560  N  NH2   A ARG A 73  ? 0.43610 0.33790 0.35290 -0.19390 0.01900  -0.11320 73   ARG A NH2   
561  N  NH2   B ARG A 73  ? 0.35020 0.30670 0.40560 -0.05940 -0.12120 -0.14340 73   ARG A NH2   
562  N  N     . THR A 74  ? 0.34110 0.43680 0.48400 -0.00660 -0.05610 -0.10010 74   THR A N     
563  C  CA    . THR A 74  ? 0.36050 0.48380 0.51460 0.00180  -0.06590 -0.06640 74   THR A CA    
564  C  C     . THR A 74  ? 0.34260 0.44480 0.51460 -0.08330 -0.06810 -0.08690 74   THR A C     
565  O  O     . THR A 74  ? 0.37260 0.50910 0.52040 -0.07560 -0.05210 -0.07250 74   THR A O     
566  C  CB    . THR A 74  ? 0.38730 0.50840 0.53850 -0.00110 -0.06290 -0.06150 74   THR A CB    
567  O  OG1   . THR A 74  ? 0.35720 0.52430 0.55220 0.03840  -0.06210 -0.03980 74   THR A OG1   
568  C  CG2   . THR A 74  ? 0.42710 0.54240 0.54370 0.02410  -0.05840 -0.08070 74   THR A CG2   
569  N  N     . ASP A 75  ? 0.37690 0.38960 0.51140 -0.01700 -0.04790 -0.09860 75   ASP A N     
570  C  CA    . ASP A 75  ? 0.39690 0.36230 0.52070 -0.03650 -0.04470 -0.10470 75   ASP A CA    
571  C  C     . ASP A 75  ? 0.39930 0.42180 0.54470 -0.05310 -0.02620 -0.08900 75   ASP A C     
572  O  O     . ASP A 75  ? 0.33090 0.43040 0.53820 -0.04400 -0.01200 -0.09130 75   ASP A O     
573  C  CB    . ASP A 75  ? 0.48390 0.31490 0.51170 -0.01770 -0.06060 -0.11620 75   ASP A CB    
574  C  CG    . ASP A 75  ? 0.63850 0.32500 0.51340 -0.09500 -0.07590 -0.10590 75   ASP A CG    
575  O  OD1   . ASP A 75  ? 0.74086 0.28453 0.50031 -0.11978 -0.08988 -0.11419 75   ASP A OD1   
576  O  OD2   . ASP A 75  ? 0.76810 0.34970 0.53620 -0.11360 -0.04690 -0.09920 75   ASP A OD2   
577  N  N     . ASP A 76  ? 0.39640 0.49270 0.57070 -0.09700 -0.02240 -0.08220 76   ASP A N     
578  C  CA    . ASP A 76  ? 0.45780 0.54960 0.59400 -0.14350 -0.01640 -0.09280 76   ASP A CA    
579  C  C     . ASP A 76  ? 0.44590 0.48530 0.56880 -0.10560 0.02360  -0.08740 76   ASP A C     
580  O  O     . ASP A 76  ? 0.46050 0.48350 0.58220 -0.07680 0.04940  -0.03290 76   ASP A O     
581  C  CB    . ASP A 76  ? 0.58080 0.68950 0.64000 -0.17970 -0.03060 -0.09750 76   ASP A CB    
582  C  CG    . ASP A 76  ? 0.68350 0.84060 0.67710 -0.22760 -0.03320 -0.10160 76   ASP A CG    
583  O  OD1   . ASP A 76  ? 0.72590 0.92720 0.69970 -0.20650 -0.01840 -0.09480 76   ASP A OD1   
584  O  OD2   . ASP A 76  ? 0.70500 0.87650 0.68620 -0.25350 -0.04350 -0.09990 76   ASP A OD2   
585  N  N     . ASN A 77  ? 0.41900 0.40970 0.53110 -0.13220 0.02860  -0.13520 77   ASN A N     
586  C  CA    . ASN A 77  ? 0.44330 0.36720 0.49990 -0.11950 0.01260  -0.14090 77   ASN A CA    
587  C  C     . ASN A 77  ? 0.36980 0.29940 0.47860 -0.12180 0.01070  -0.13880 77   ASN A C     
588  O  O     . ASN A 77  ? 0.42160 0.33900 0.48410 -0.13750 0.00270  -0.14140 77   ASN A O     
589  C  CB    . ASN A 77  ? 0.52630 0.43360 0.49620 -0.22330 0.03750  -0.12080 77   ASN A CB    
590  C  CG    . ASN A 77  ? 0.57420 0.53420 0.49570 -0.27030 0.07130  -0.12000 77   ASN A CG    
591  O  OD1   . ASN A 77  ? 0.63170 0.55280 0.50260 -0.32560 0.07200  -0.09540 77   ASN A OD1   
592  N  ND2   . ASN A 77  ? 0.59040 0.59590 0.49480 -0.23060 0.05850  -0.15050 77   ASN A ND2   
593  N  N     . PHE A 78  ? 0.36720 0.27340 0.45890 -0.06170 -0.00910 -0.14220 78   PHE A N     
594  C  CA    . PHE A 78  ? 0.31500 0.26430 0.44190 -0.06550 0.00390  -0.13430 78   PHE A CA    
595  C  C     . PHE A 78  ? 0.30480 0.30680 0.41750 -0.06250 0.01660  -0.07070 78   PHE A C     
596  O  O     . PHE A 78  ? 0.33810 0.37930 0.42120 -0.00690 0.02350  -0.09390 78   PHE A O     
597  C  CB    . PHE A 78  ? 0.34030 0.28470 0.46160 -0.05020 0.01510  -0.14200 78   PHE A CB    
598  C  CG    . PHE A 78  ? 0.30220 0.28840 0.46950 -0.01050 -0.03440 -0.13160 78   PHE A CG    
599  C  CD1   . PHE A 78  ? 0.34990 0.25850 0.46730 0.02830  -0.06340 -0.10160 78   PHE A CD1   
600  C  CD2   . PHE A 78  ? 0.28450 0.29410 0.47290 0.01910  -0.05010 -0.12270 78   PHE A CD2   
601  C  CE1   . PHE A 78  ? 0.35110 0.25730 0.46950 0.00430  -0.06670 -0.09870 78   PHE A CE1   
602  C  CE2   . PHE A 78  ? 0.35300 0.32450 0.47830 0.04060  -0.04440 -0.11720 78   PHE A CE2   
603  C  CZ    . PHE A 78  ? 0.36130 0.29670 0.47510 0.08100  -0.04450 -0.09980 78   PHE A CZ    
604  N  N     . PRO A 79  ? 0.29890 0.29630 0.37660 -0.05240 0.01290  -0.05950 79   PRO A N     
605  C  CA    . PRO A 79  ? 0.38250 0.28540 0.36400 -0.05370 0.05450  -0.07270 79   PRO A CA    
606  C  C     . PRO A 79  ? 0.41590 0.34550 0.37930 -0.03400 0.05780  -0.07800 79   PRO A C     
607  O  O     . PRO A 79  ? 0.43560 0.36320 0.41110 -0.07750 0.10540  -0.04880 79   PRO A O     
608  C  CB    . PRO A 79  ? 0.33540 0.27770 0.36220 -0.09510 0.03660  -0.06020 79   PRO A CB    
609  C  CG    . PRO A 79  ? 0.27940 0.25410 0.35430 -0.09510 0.01040  -0.05450 79   PRO A CG    
610  C  CD    . PRO A 79  ? 0.25650 0.27120 0.35500 -0.05640 0.01330  -0.05360 79   PRO A CD    
611  N  N     . ALA A 80  ? 0.37210 0.36730 0.35560 0.07710  0.03800  -0.07750 80   ALA A N     
612  C  CA    . ALA A 80  ? 0.40650 0.38710 0.32660 0.11320  0.01360  -0.07300 80   ALA A CA    
613  C  C     . ALA A 80  ? 0.43230 0.29590 0.32680 0.05570  0.04240  -0.04340 80   ALA A C     
614  O  O     . ALA A 80  ? 0.46500 0.29340 0.32350 0.00530  0.04420  -0.03620 80   ALA A O     
615  C  CB    . ALA A 80  ? 0.41990 0.46230 0.32470 0.16230  -0.03430 -0.04640 80   ALA A CB    
616  N  N     . THR A 81  ? 0.37530 0.28000 0.34420 0.01770  0.03590  -0.01080 81   THR A N     
617  C  CA    . THR A 81  ? 0.36500 0.22840 0.36860 -0.00340 0.01400  -0.02060 81   THR A CA    
618  C  C     . THR A 81  ? 0.43730 0.27090 0.38760 0.02960  0.00700  -0.04780 81   THR A C     
619  O  O     . THR A 81  ? 0.46290 0.29690 0.37520 0.01140  0.00650  -0.01270 81   THR A O     
620  C  CB    . THR A 81  ? 0.39510 0.22790 0.39190 -0.00400 0.01020  -0.00640 81   THR A CB    
621  O  OG1   . THR A 81  ? 0.47380 0.22440 0.41310 -0.05320 -0.03270 0.00250  81   THR A OG1   
622  C  CG2   . THR A 81  ? 0.37780 0.21870 0.40310 -0.02110 0.03070  0.00080  81   THR A CG2   
623  N  N     . SER A 82  ? 0.42750 0.34000 0.42310 0.03570  0.01770  -0.04140 82   SER A N     
624  C  CA    . SER A 82  ? 0.42410 0.39410 0.46680 -0.00200 0.00250  -0.03050 82   SER A CA    
625  C  C     . SER A 82  ? 0.41990 0.42380 0.50960 0.05040  -0.00570 -0.05460 82   SER A C     
626  O  O     . SER A 82  ? 0.36100 0.39880 0.50550 0.07010  -0.02300 -0.08590 82   SER A O     
627  C  CB    . SER A 82  ? 0.47320 0.42910 0.45230 -0.02440 -0.00910 -0.02370 82   SER A CB    
628  O  OG    . SER A 82  ? 0.52850 0.44400 0.44280 -0.02160 -0.02540 -0.00890 82   SER A OG    
629  N  N     . PRO A 83  ? 0.38820 0.49740 0.55480 0.07890  0.03120  -0.05930 83   PRO A N     
630  C  CA    . PRO A 83  ? 0.41330 0.56990 0.59690 0.12300  0.03150  -0.06340 83   PRO A CA    
631  C  C     . PRO A 83  ? 0.37710 0.63140 0.64550 0.18040  -0.00220 -0.07130 83   PRO A C     
632  O  O     . PRO A 83  ? 0.39760 0.68060 0.64370 0.16360  -0.01990 -0.09650 83   PRO A O     
633  C  CB    . PRO A 83  ? 0.43210 0.57560 0.59430 0.13480  0.03740  -0.06930 83   PRO A CB    
634  C  CG    . PRO A 83  ? 0.44350 0.55070 0.58100 0.11120  0.02920  -0.06800 83   PRO A CG    
635  C  CD    . PRO A 83  ? 0.45060 0.52490 0.56300 0.09650  0.03310  -0.07990 83   PRO A CD    
636  N  N     . ARG A 84  ? 0.44040 0.66180 0.69200 0.07470  -0.04440 -0.03230 84   ARG A N     
637  C  CA    . ARG A 84  ? 0.52770 0.65350 0.73320 0.02670  -0.05550 0.01120  84   ARG A CA    
638  C  C     . ARG A 84  ? 0.64520 0.73860 0.78000 -0.06530 -0.02570 0.04470  84   ARG A C     
639  O  O     . ARG A 84  ? 0.63510 0.71610 0.78830 -0.15150 -0.03240 0.05850  84   ARG A O     
640  C  CB    . ARG A 84  ? 0.58180 0.59170 0.72640 0.05320  -0.07940 0.02530  84   ARG A CB    
641  C  CG    . ARG A 84  ? 0.57460 0.56130 0.71320 0.06140  -0.09200 0.03310  84   ARG A CG    
642  C  CD    . ARG A 84  ? 0.55190 0.48180 0.69380 0.06570  -0.10370 0.03350  84   ARG A CD    
643  N  NE    . ARG A 84  ? 0.57800 0.40990 0.67540 0.05710  -0.09050 0.03680  84   ARG A NE    
644  C  CZ    . ARG A 84  ? 0.56000 0.38660 0.66610 0.09110  -0.07150 0.02550  84   ARG A CZ    
645  N  NH1   . ARG A 84  ? 0.61880 0.30220 0.65940 0.07510  -0.07320 0.05050  84   ARG A NH1   
646  N  NH2   . ARG A 84  ? 0.53810 0.42350 0.66440 0.10200  -0.05740 0.00210  84   ARG A NH2   
647  N  N     . PHE A 85  ? 0.76550 0.86370 0.81730 -0.03370 0.01960  0.05850  85   PHE A N     
648  C  CA    . PHE A 85  ? 0.91250 0.97110 0.85570 0.02440  0.06320  0.06070  85   PHE A CA    
649  C  C     . PHE A 85  ? 1.05840 1.08170 0.88780 -0.01290 0.06510  0.06140  85   PHE A C     
650  O  O     . PHE A 85  ? 1.15210 1.12810 0.89030 0.00590  0.07480  0.06360  85   PHE A O     
651  C  CB    . PHE A 85  ? 0.94260 0.93530 0.86170 0.14500  0.09740  0.06920  85   PHE A CB    
652  C  CG    . PHE A 85  ? 0.98800 0.92660 0.86290 0.23490  0.14480  0.07980  85   PHE A CG    
653  C  CD1   . PHE A 85  ? 1.00960 0.95780 0.86250 0.25310  0.16810  0.09190  85   PHE A CD1   
654  C  CD2   . PHE A 85  ? 0.98970 0.90000 0.85940 0.29080  0.16830  0.08590  85   PHE A CD2   
655  C  CE1   . PHE A 85  ? 1.00060 0.97680 0.86090 0.26840  0.17080  0.09540  85   PHE A CE1   
656  C  CE2   . PHE A 85  ? 1.01360 0.92200 0.85840 0.30620  0.18200  0.08910  85   PHE A CE2   
657  C  CZ    . PHE A 85  ? 1.01410 0.96400 0.86230 0.28860  0.17390  0.08920  85   PHE A CZ    
658  N  N     . GLU A 86  ? 1.07280 1.10590 0.91770 -0.05450 0.05900  0.06240  86   GLU A N     
659  C  CA    . GLU A 86  ? 1.07560 1.11660 0.94990 -0.04790 0.04900  0.06410  86   GLU A CA    
660  C  C     . GLU A 86  ? 1.11850 1.11370 0.96650 -0.01460 0.05170  0.08740  86   GLU A C     
661  O  O     . GLU A 86  ? 1.12200 1.08580 0.96800 -0.02390 0.05100  0.07630  86   GLU A O     
662  C  CB    . GLU A 86  ? 1.04460 1.13460 0.96570 -0.08100 0.03230  0.04490  86   GLU A CB    
663  C  CG    . GLU A 86  ? 1.04860 1.18650 0.98540 -0.09730 0.01140  0.02050  86   GLU A CG    
664  C  CD    . GLU A 86  ? 1.05770 1.24980 1.00400 -0.09360 -0.01230 -0.00250 86   GLU A CD    
665  O  OE1   . GLU A 86  ? 1.09040 1.29160 1.01190 -0.08000 -0.01470 -0.00860 86   GLU A OE1   
666  O  OE2   . GLU A 86  ? 1.03670 1.26160 1.00870 -0.08820 -0.02760 -0.00940 86   GLU A OE2   
667  N  N     . ALA A 87  ? 1.16270 1.15460 0.97960 -0.00090 0.04840  0.13180  87   ALA A N     
668  C  CA    . ALA A 87  ? 1.21590 1.20030 0.99250 -0.01210 0.04250  0.17190  87   ALA A CA    
669  C  C     . ALA A 87  ? 1.26320 1.29510 1.01110 -0.01140 0.03130  0.18740  87   ALA A C     
670  O  O     . ALA A 87  ? 1.27410 1.34090 1.01320 0.02020  0.02860  0.20150  87   ALA A O     
671  C  CB    . ALA A 87  ? 1.20290 1.15310 0.98620 -0.03140 0.04320  0.18100  87   ALA A CB    
672  N  N     . VAL A 88  ? 1.26810 1.31170 1.02440 -0.04620 0.01510  0.17890  88   VAL A N     
673  C  CA    . VAL A 88  ? 1.28140 1.29620 1.03710 -0.07030 -0.01930 0.16280  88   VAL A CA    
674  C  C     . VAL A 88  ? 1.32240 1.30170 1.04050 -0.06790 -0.02400 0.14690  88   VAL A C     
675  O  O     . VAL A 88  ? 1.33570 1.32070 1.03880 -0.07580 -0.03520 0.15680  88   VAL A O     
676  C  CB    . VAL A 88  ? 1.25750 1.26300 1.04530 -0.07110 -0.04970 0.15970  88   VAL A CB    
677  C  CG1   . VAL A 88  ? 1.25440 1.24030 1.04320 -0.06210 -0.06250 0.15940  88   VAL A CG1   
678  C  CG2   . VAL A 88  ? 1.22300 1.25070 1.05190 -0.06710 -0.05670 0.16140  88   VAL A CG2   
679  N  N     . ARG A 89  ? 1.33490 1.27160 1.04490 -0.03550 -0.00250 0.11430  89   ARG A N     
680  C  CA    . ARG A 89  ? 1.32890 1.23750 1.04950 0.01220  0.03100  0.07360  89   ARG A CA    
681  C  C     . ARG A 89  ? 1.30980 1.22720 1.04210 0.05780  0.02460  0.06200  89   ARG A C     
682  O  O     . ARG A 89  ? 1.32720 1.21910 1.04210 0.10390  0.02840  0.06130  89   ARG A O     
683  C  CB    . ARG A 89  ? 1.31980 1.22450 1.06300 0.01980  0.07550  0.04420  89   ARG A CB    
684  C  CG    . ARG A 89  ? 1.28980 1.23300 1.07750 0.01980  0.12470  0.02320  89   ARG A CG    
685  C  CD    . ARG A 89  ? 1.23640 1.25430 1.09010 0.01520  0.16980  0.00720  89   ARG A CD    
686  N  NE    . ARG A 89  ? 1.15920 1.28270 1.10030 -0.01550 0.21250  -0.00420 89   ARG A NE    
687  C  CZ    . ARG A 89  ? 1.07360 1.30980 1.10780 -0.07070 0.24370  -0.00740 89   ARG A CZ    
688  N  NH1   . ARG A 89  ? 1.03280 1.32650 1.10900 -0.08270 0.25840  -0.01190 89   ARG A NH1   
689  N  NH2   . ARG A 89  ? 1.04770 1.31360 1.11070 -0.09990 0.24700  -0.00380 89   ARG A NH2   
690  N  N     . GLU A 90  ? 1.26310 1.23590 1.03270 0.02000  0.00700  0.05110  90   GLU A N     
691  C  CA    . GLU A 90  ? 1.20230 1.23610 1.01860 -0.03880 -0.00830 0.02890  90   GLU A CA    
692  C  C     . GLU A 90  ? 1.12670 1.15570 0.98530 -0.12970 -0.02720 0.03490  90   GLU A C     
693  O  O     . GLU A 90  ? 1.12840 1.14990 0.98450 -0.15830 -0.05030 0.04240  90   GLU A O     
694  C  CB    . GLU A 90  ? 1.20970 1.27860 1.03300 -0.00250 -0.00350 -0.00200 90   GLU A CB    
695  C  CG    . GLU A 90  ? 1.24040 1.28600 1.04090 0.00610  -0.00750 -0.02900 90   GLU A CG    
696  C  CD    . GLU A 90  ? 1.28310 1.27660 1.04540 -0.00600 -0.01050 -0.05060 90   GLU A CD    
697  O  OE1   . GLU A 90  ? 1.30960 1.29430 1.04680 -0.01140 -0.00350 -0.05710 90   GLU A OE1   
698  O  OE2   . GLU A 90  ? 1.28840 1.24510 1.04600 -0.00770 -0.01750 -0.05920 90   GLU A OE2   
699  N  N     . SER A 91  ? 1.03000 1.06340 0.95070 -0.16890 -0.01940 0.02640  91   SER A N     
700  C  CA    . SER A 91  ? 0.90660 0.94840 0.91310 -0.19160 -0.01390 0.01160  91   SER A CA    
701  C  C     . SER A 91  ? 0.79420 0.83550 0.86350 -0.19130 -0.01220 0.01710  91   SER A C     
702  O  O     . SER A 91  ? 0.74310 0.83620 0.86220 -0.21540 -0.01010 0.03550  91   SER A O     
703  C  CB    . SER A 91  ? 0.91870 0.94200 0.92330 -0.19230 -0.02860 -0.00360 91   SER A CB    
704  O  OG    . SER A 91  ? 0.95780 0.94840 0.93080 -0.17550 -0.05020 -0.01010 91   SER A OG    
705  N  N     . PRO A 92  ? 0.74150 0.69470 0.81380 -0.13790 -0.01880 -0.00640 92   PRO A N     
706  C  CA    . PRO A 92  ? 0.60640 0.61740 0.75920 -0.07320 -0.06070 -0.03530 92   PRO A CA    
707  C  C     . PRO A 92  ? 0.44730 0.51250 0.67910 0.00750  -0.10260 -0.06160 92   PRO A C     
708  O  O     . PRO A 92  ? 0.40830 0.55740 0.67510 0.04000  -0.09630 -0.07380 92   PRO A O     
709  C  CB    . PRO A 92  ? 0.69540 0.65310 0.78240 -0.05010 -0.03630 -0.03860 92   PRO A CB    
710  C  CG    . PRO A 92  ? 0.78370 0.64220 0.80270 -0.04980 -0.02010 -0.02850 92   PRO A CG    
711  C  CD    . PRO A 92  ? 0.78850 0.66510 0.81230 -0.09070 -0.00130 -0.02070 92   PRO A CD    
712  N  N     . GLN A 93  ? 0.37790 0.38720 0.60330 -0.04450 -0.14760 -0.07060 93   GLN A N     
713  C  CA    A GLN A 93  ? 0.33930 0.29130 0.55680 0.03510  -0.16080 -0.09190 93   GLN A CA    
714  C  CA    B GLN A 93  ? 0.37190 0.30000 0.57650 0.01590  -0.14220 -0.07670 93   GLN A CA    
715  C  C     . GLN A 93  ? 0.36960 0.26080 0.53610 0.05210  -0.14970 -0.08670 93   GLN A C     
716  O  O     . GLN A 93  ? 0.42900 0.29150 0.56060 0.00620  -0.19990 -0.04580 93   GLN A O     
717  C  CB    A GLN A 93  ? 0.38880 0.28740 0.54300 0.05170  -0.16630 -0.11580 93   GLN A CB    
718  C  CB    B GLN A 93  ? 0.42290 0.27570 0.59370 0.02180  -0.13270 -0.07260 93   GLN A CB    
719  C  CG    A GLN A 93  ? 0.39240 0.32730 0.53550 0.03600  -0.15090 -0.09960 93   GLN A CG    
720  C  CG    B GLN A 93  ? 0.45920 0.27510 0.61180 0.00120  -0.11290 -0.05140 93   GLN A CG    
721  C  CD    A GLN A 93  ? 0.34950 0.29730 0.52100 0.05110  -0.16030 -0.09940 93   GLN A CD    
722  C  CD    B GLN A 93  ? 0.48040 0.26690 0.62740 -0.00150 -0.10530 -0.04450 93   GLN A CD    
723  O  OE1   A GLN A 93  ? 0.35170 0.29410 0.51410 0.07440  -0.13530 -0.06970 93   GLN A OE1   
724  O  OE1   B GLN A 93  ? 0.44450 0.31650 0.63500 0.01250  -0.11150 -0.03600 93   GLN A OE1   
725  N  NE2   A GLN A 93  ? 0.41920 0.35070 0.50860 0.07260  -0.19200 -0.07790 93   GLN A NE2   
726  N  NE2   B GLN A 93  ? 0.53080 0.23030 0.63400 -0.02340 -0.09890 -0.04780 93   GLN A NE2   
727  N  N     . ALA A 94  ? 0.31830 0.23700 0.45960 0.06790  -0.12370 -0.12620 94   ALA A N     
728  C  CA    . ALA A 94  ? 0.35270 0.25720 0.39540 0.08950  -0.13580 -0.13890 94   ALA A CA    
729  C  C     . ALA A 94  ? 0.35390 0.23480 0.34420 0.10200  -0.13440 -0.11190 94   ALA A C     
730  O  O     . ALA A 94  ? 0.42240 0.19300 0.33170 0.08210  -0.13950 -0.08150 94   ALA A O     
731  C  CB    . ALA A 94  ? 0.36380 0.27860 0.39230 0.03220  -0.13330 -0.15510 94   ALA A CB    
732  N  N     . PHE A 95  ? 0.33930 0.22120 0.31220 0.07790  -0.13450 -0.08350 95   PHE A N     
733  C  CA    . PHE A 95  ? 0.34320 0.20270 0.26260 0.06080  -0.10500 -0.06160 95   PHE A CA    
734  C  C     . PHE A 95  ? 0.37570 0.14630 0.24800 0.04360  -0.10250 -0.05480 95   PHE A C     
735  O  O     . PHE A 95  ? 0.36910 0.18330 0.25850 0.06840  -0.10120 -0.09610 95   PHE A O     
736  C  CB    . PHE A 95  ? 0.40960 0.24150 0.23160 0.00020  -0.10440 -0.07440 95   PHE A CB    
737  C  CG    . PHE A 95  ? 0.40340 0.19680 0.20100 0.08540  -0.09320 -0.03530 95   PHE A CG    
738  C  CD1   . PHE A 95  ? 0.42400 0.20820 0.17550 0.05550  -0.09530 -0.01310 95   PHE A CD1   
739  C  CD2   . PHE A 95  ? 0.46028 0.19042 0.21690 0.12899  -0.09929 -0.04889 95   PHE A CD2   
740  C  CE1   . PHE A 95  ? 0.43440 0.15330 0.19190 0.04680  -0.06890 0.00580  95   PHE A CE1   
741  C  CE2   . PHE A 95  ? 0.40280 0.23960 0.20920 0.06910  -0.07460 -0.02890 95   PHE A CE2   
742  C  CZ    . PHE A 95  ? 0.40810 0.23590 0.18770 0.11840  -0.08130 -0.01310 95   PHE A CZ    
743  N  N     . ILE A 96  ? 0.38300 0.17450 0.23910 0.07110  -0.07460 -0.03100 96   ILE A N     
744  C  CA    . ILE A 96  ? 0.34510 0.17570 0.21400 0.09130  -0.07770 -0.04340 96   ILE A CA    
745  C  C     . ILE A 96  ? 0.31500 0.17770 0.24510 0.06640  -0.05530 -0.03520 96   ILE A C     
746  O  O     . ILE A 96  ? 0.35700 0.17870 0.24240 0.06740  -0.06610 -0.06270 96   ILE A O     
747  C  CB    . ILE A 96  ? 0.35080 0.19260 0.19300 0.06670  -0.05600 -0.00450 96   ILE A CB    
748  C  CG1   . ILE A 96  ? 0.38270 0.17130 0.16360 0.05520  -0.06380 -0.02780 96   ILE A CG1   
749  C  CG2   . ILE A 96  ? 0.31370 0.19350 0.19860 0.00460  -0.03530 -0.03460 96   ILE A CG2   
750  C  CD1   . ILE A 96  ? 0.33980 0.25210 0.15920 0.00190  -0.05620 -0.02590 96   ILE A CD1   
751  N  N     . GLY A 97  ? 0.29640 0.18360 0.25510 0.04690  -0.06270 -0.07620 97   GLY A N     
752  C  CA    . GLY A 97  ? 0.32140 0.17860 0.25460 0.03260  -0.09250 -0.08290 97   GLY A CA    
753  C  C     . GLY A 97  ? 0.33180 0.19490 0.27380 0.02670  -0.12020 -0.06840 97   GLY A C     
754  O  O     . GLY A 97  ? 0.41530 0.24950 0.32040 -0.03560 -0.12570 -0.08330 97   GLY A O     
755  N  N     . LEU A 98  ? 0.36190 0.21990 0.24860 0.12740  -0.09510 -0.08060 98   LEU A N     
756  C  CA    . LEU A 98  ? 0.37840 0.19590 0.23320 0.06830  -0.09300 -0.07280 98   LEU A CA    
757  C  C     . LEU A 98  ? 0.37450 0.20490 0.23030 0.03830  -0.08210 -0.05260 98   LEU A C     
758  O  O     . LEU A 98  ? 0.36550 0.27250 0.22450 0.04480  -0.08690 -0.09210 98   LEU A O     
759  C  CB    . LEU A 98  ? 0.38350 0.24390 0.24640 0.05410  -0.07600 -0.05840 98   LEU A CB    
760  C  CG    . LEU A 98  ? 0.33280 0.24240 0.25120 0.04180  -0.09850 -0.07980 98   LEU A CG    
761  C  CD1   . LEU A 98  ? 0.37310 0.23900 0.25740 0.05860  -0.07640 -0.07150 98   LEU A CD1   
762  C  CD2   . LEU A 98  ? 0.32250 0.29890 0.28250 0.05650  -0.06170 -0.07770 98   LEU A CD2   
763  N  N     . ASP A 99  ? 0.44830 0.19860 0.23090 0.06510  -0.07170 -0.03980 99   ASP A N     
764  C  CA    . ASP A 99  ? 0.46150 0.18310 0.23510 0.06220  -0.07970 -0.06340 99   ASP A CA    
765  C  C     . ASP A 99  ? 0.50010 0.24860 0.23360 0.10870  -0.10230 -0.05290 99   ASP A C     
766  O  O     . ASP A 99  ? 0.47660 0.23090 0.22270 0.06330  -0.11690 -0.05290 99   ASP A O     
767  C  CB    . ASP A 99  ? 0.45490 0.19530 0.25640 0.04650  -0.08120 -0.06890 99   ASP A CB    
768  C  CG    . ASP A 99  ? 0.43550 0.19340 0.26950 0.05680  -0.07310 -0.08670 99   ASP A CG    
769  O  OD1   . ASP A 99  ? 0.40750 0.22530 0.29000 0.06020  -0.10830 -0.08360 99   ASP A OD1   
770  O  OD2   . ASP A 99  ? 0.46060 0.31160 0.28000 0.00800  -0.08330 -0.09380 99   ASP A OD2   
771  N  N     . PRO A 100 ? 0.52110 0.29940 0.22480 0.14770  -0.05750 -0.05920 100  PRO A N     
772  C  CA    . PRO A 100 ? 0.57120 0.31580 0.23080 0.11050  -0.03570 -0.10190 100  PRO A CA    
773  C  C     . PRO A 100 ? 0.63300 0.34960 0.22990 0.05890  -0.03080 -0.11170 100  PRO A C     
774  O  O     . PRO A 100 ? 0.75170 0.36240 0.25420 0.06770  0.00190  -0.10140 100  PRO A O     
775  C  CB    . PRO A 100 ? 0.57680 0.33200 0.23250 0.10170  -0.01190 -0.10500 100  PRO A CB    
776  C  CG    . PRO A 100 ? 0.56530 0.36620 0.25430 0.17140  0.00300  -0.05280 100  PRO A CG    
777  C  CD    . PRO A 100 ? 0.52920 0.36590 0.24590 0.18360  -0.01160 -0.06030 100  PRO A CD    
778  N  N     . PRO A 101 ? 0.57479 0.34970 0.19531 0.07250  -0.08270 -0.08000 101  PRO A N     
779  C  CA    . PRO A 101 ? 0.54440 0.38740 0.18820 0.02500  -0.06620 -0.08580 101  PRO A CA    
780  C  C     . PRO A 101 ? 0.46090 0.36450 0.21590 0.02110  -0.09870 -0.05390 101  PRO A C     
781  O  O     . PRO A 101 ? 0.43170 0.40030 0.22350 0.03470  -0.11300 -0.04620 101  PRO A O     
782  C  CB    . PRO A 101 ? 0.56520 0.46100 0.19140 0.02470  -0.08320 -0.07760 101  PRO A CB    
783  C  CG    . PRO A 101 ? 0.55140 0.44790 0.20500 -0.01420 -0.11130 -0.08810 101  PRO A CG    
784  C  CD    . PRO A 101 ? 0.60810 0.43600 0.20340 0.02070  -0.09950 -0.08010 101  PRO A CD    
785  N  N     . GLU A 102 ? 0.46700 0.39920 0.21860 0.00680  -0.11140 -0.05030 102  GLU A N     
786  C  CA    . GLU A 102 ? 0.41490 0.39490 0.23520 0.00630  -0.12670 -0.02040 102  GLU A CA    
787  C  C     . GLU A 102 ? 0.38330 0.34610 0.23070 0.09300  -0.10300 -0.03730 102  GLU A C     
788  O  O     . GLU A 102 ? 0.42910 0.34910 0.26800 0.10040  -0.09360 0.01280  102  GLU A O     
789  C  CB    . GLU A 102 ? 0.41160 0.45220 0.24430 -0.02950 -0.14150 0.02190  102  GLU A CB    
790  C  CG    . GLU A 102 ? 0.44700 0.52080 0.25010 -0.03840 -0.17530 0.03580  102  GLU A CG    
791  C  CD    . GLU A 102 ? 0.55600 0.63400 0.28750 -0.11000 -0.18460 -0.01480 102  GLU A CD    
792  O  OE1   . GLU A 102 ? 0.58159 0.67408 0.30182 -0.15198 -0.16768 -0.04310 102  GLU A OE1   
793  O  OE2   . GLU A 102 ? 0.63670 0.69250 0.29120 -0.11170 -0.17800 -0.02670 102  GLU A OE2   
794  N  N     . HIS A 103 ? 0.40710 0.27620 0.19190 0.10630  -0.11860 -0.05490 103  HIS A N     
795  C  CA    . HIS A 103 ? 0.37530 0.26850 0.19850 0.08700  -0.08420 -0.04400 103  HIS A CA    
796  C  C     . HIS A 103 ? 0.34170 0.21590 0.18410 0.07720  -0.08640 -0.04670 103  HIS A C     
797  O  O     . HIS A 103 ? 0.40310 0.19470 0.18640 0.06820  -0.05720 -0.03340 103  HIS A O     
798  C  CB    . HIS A 103 ? 0.38430 0.25870 0.20430 0.09550  -0.11720 -0.01820 103  HIS A CB    
799  C  CG    . HIS A 103 ? 0.36480 0.25200 0.19950 0.11770  -0.12220 -0.04690 103  HIS A CG    
800  N  ND1   . HIS A 103 ? 0.39499 0.24960 0.20751 0.15379  -0.13048 -0.07240 103  HIS A ND1   
801  C  CD2   . HIS A 103 ? 0.41870 0.22980 0.19310 0.08800  -0.13570 -0.04610 103  HIS A CD2   
802  C  CE1   . HIS A 103 ? 0.43360 0.26160 0.19750 0.12160  -0.11260 -0.08180 103  HIS A CE1   
803  N  NE2   . HIS A 103 ? 0.44330 0.19160 0.20930 0.08320  -0.14880 -0.04810 103  HIS A NE2   
804  N  N     . GLY A 104 ? 0.40170 0.25280 0.17290 0.09160  -0.06400 -0.06710 104  GLY A N     
805  C  CA    . GLY A 104 ? 0.40300 0.27020 0.17410 0.08100  -0.08260 -0.03610 104  GLY A CA    
806  C  C     . GLY A 104 ? 0.36850 0.25850 0.17730 0.05550  -0.08320 -0.04270 104  GLY A C     
807  O  O     . GLY A 104 ? 0.43030 0.28130 0.19650 0.03980  -0.06550 -0.05250 104  GLY A O     
808  N  N     . THR A 105 ? 0.36330 0.28050 0.17510 0.08890  -0.08110 -0.02730 105  THR A N     
809  C  CA    . THR A 105 ? 0.37440 0.32580 0.19300 0.08930  -0.06410 -0.03920 105  THR A CA    
810  C  C     . THR A 105 ? 0.40250 0.31260 0.21660 0.06810  -0.04310 -0.01720 105  THR A C     
811  O  O     . THR A 105 ? 0.45100 0.24480 0.24960 0.05280  -0.02980 -0.00250 105  THR A O     
812  C  CB    . THR A 105 ? 0.38040 0.43790 0.18880 0.11160  -0.04770 -0.07860 105  THR A CB    
813  O  OG1   . THR A 105 ? 0.41300 0.44610 0.18920 0.10790  -0.05070 -0.06310 105  THR A OG1   
814  C  CG2   . THR A 105 ? 0.37940 0.48560 0.19240 0.10560  -0.08040 -0.10470 105  THR A CG2   
815  N  N     . ARG A 106 ? 0.31720 0.29760 0.19880 0.05000  -0.02560 -0.02410 106  ARG A N     
816  C  CA    . ARG A 106 ? 0.27470 0.31470 0.21280 0.03410  -0.05970 -0.01580 106  ARG A CA    
817  C  C     . ARG A 106 ? 0.28300 0.26940 0.21740 0.03600  -0.04590 -0.00270 106  ARG A C     
818  O  O     . ARG A 106 ? 0.32750 0.25840 0.23930 0.05720  -0.04960 -0.02420 106  ARG A O     
819  C  CB    . ARG A 106 ? 0.26170 0.39930 0.24240 0.01550  -0.06310 -0.02000 106  ARG A CB    
820  C  CG    . ARG A 106 ? 0.34660 0.48070 0.25330 -0.00310 -0.05320 -0.03460 106  ARG A CG    
821  C  CD    . ARG A 106 ? 0.39360 0.52220 0.26420 0.05690  -0.05390 -0.02200 106  ARG A CD    
822  N  NE    . ARG A 106 ? 0.35700 0.46060 0.25470 0.01280  -0.09390 0.00260  106  ARG A NE    
823  C  CZ    . ARG A 106 ? 0.37080 0.32370 0.26910 0.04040  -0.03630 0.01200  106  ARG A CZ    
824  N  NH1   . ARG A 106 ? 0.35540 0.27730 0.28380 0.01170  0.00800  0.04110  106  ARG A NH1   
825  N  NH2   . ARG A 106 ? 0.37330 0.24720 0.27100 0.03910  -0.05410 0.04160  106  ARG A NH2   
826  N  N     . ARG A 107 ? 0.28460 0.23360 0.18450 0.02760  -0.07670 -0.01610 107  ARG A N     
827  C  CA    . ARG A 107 ? 0.28480 0.22560 0.18500 0.06760  -0.06100 0.00920  107  ARG A CA    
828  C  C     . ARG A 107 ? 0.31940 0.25070 0.19590 0.04450  -0.04130 -0.02080 107  ARG A C     
829  O  O     . ARG A 107 ? 0.33400 0.26260 0.21510 0.05460  -0.04560 -0.04540 107  ARG A O     
830  C  CB    . ARG A 107 ? 0.33220 0.25980 0.18450 0.10330  -0.08510 -0.04010 107  ARG A CB    
831  C  CG    . ARG A 107 ? 0.30920 0.28920 0.20080 0.07590  -0.08810 -0.05420 107  ARG A CG    
832  C  CD    . ARG A 107 ? 0.32710 0.30820 0.19580 0.10190  -0.06810 -0.02440 107  ARG A CD    
833  N  NE    . ARG A 107 ? 0.29440 0.36850 0.20740 0.08330  -0.07570 -0.02600 107  ARG A NE    
834  C  CZ    . ARG A 107 ? 0.33210 0.34190 0.24020 0.06260  -0.03270 -0.03300 107  ARG A CZ    
835  N  NH1   . ARG A 107 ? 0.35050 0.22320 0.21780 0.03230  -0.04880 -0.03120 107  ARG A NH1   
836  N  NH2   . ARG A 107 ? 0.40050 0.42470 0.27940 0.07350  -0.02980 -0.06140 107  ARG A NH2   
837  N  N     . ARG A 108 ? 0.36610 0.23480 0.17490 0.07770  -0.03650 -0.03130 108  ARG A N     
838  C  CA    . ARG A 108 ? 0.39290 0.28950 0.19430 0.09010  -0.02340 -0.03020 108  ARG A CA    
839  C  C     . ARG A 108 ? 0.33690 0.32410 0.21500 0.08230  0.00320  -0.02400 108  ARG A C     
840  O  O     . ARG A 108 ? 0.32870 0.36260 0.26970 0.05750  0.02560  -0.03070 108  ARG A O     
841  C  CB    . ARG A 108 ? 0.51730 0.34550 0.21310 0.08130  0.04290  -0.06720 108  ARG A CB    
842  C  CG    . ARG A 108 ? 0.66090 0.45150 0.24760 0.06420  0.03330  -0.07650 108  ARG A CG    
843  C  CD    . ARG A 108 ? 0.76120 0.53850 0.25510 0.05840  0.05340  -0.09290 108  ARG A CD    
844  N  NE    . ARG A 108 ? 0.78366 0.61430 0.26944 0.08898  0.10639  -0.11349 108  ARG A NE    
845  C  CZ    . ARG A 108 ? 0.77120 0.65970 0.29110 0.09150  0.09360  -0.13450 108  ARG A CZ    
846  N  NH1   . ARG A 108 ? 0.79500 0.68790 0.31060 0.13610  0.10460  -0.14010 108  ARG A NH1   
847  N  NH2   . ARG A 108 ? 0.69540 0.67860 0.30690 0.04420  0.08240  -0.12160 108  ARG A NH2   
848  N  N     . MET A 109 ? 0.30140 0.26140 0.17650 0.08220  -0.01010 -0.01630 109  MET A N     
849  C  CA    . MET A 109 ? 0.27870 0.21720 0.17860 0.03100  -0.03040 -0.01730 109  MET A CA    
850  C  C     . MET A 109 ? 0.31880 0.20900 0.18240 0.01320  -0.03060 -0.02270 109  MET A C     
851  O  O     . MET A 109 ? 0.37530 0.22940 0.20820 0.01500  -0.01180 -0.01720 109  MET A O     
852  C  CB    . MET A 109 ? 0.28790 0.30270 0.20580 0.02910  -0.05300 -0.00370 109  MET A CB    
853  C  CG    . MET A 109 ? 0.27380 0.29600 0.23600 0.01520  -0.09420 -0.00870 109  MET A CG    
854  S  SD    . MET A 109 ? 0.35010 0.26150 0.25320 0.04380  -0.08110 0.03990  109  MET A SD    
855  C  CE    . MET A 109 ? 0.33720 0.35050 0.24420 0.02900  -0.09420 -0.01130 109  MET A CE    
856  N  N     . THR A 110 ? 0.31220 0.23840 0.17320 0.05110  -0.04110 -0.00150 110  THR A N     
857  C  CA    . THR A 110 ? 0.31290 0.20210 0.16220 0.02960  -0.02060 -0.01070 110  THR A CA    
858  C  C     . THR A 110 ? 0.29630 0.23070 0.17530 0.04990  -0.02530 -0.02360 110  THR A C     
859  O  O     . THR A 110 ? 0.34680 0.19810 0.16390 -0.00340 -0.00500 -0.01140 110  THR A O     
860  C  CB    . THR A 110 ? 0.30990 0.17580 0.20440 0.06860  -0.01780 0.01050  110  THR A CB    
861  O  OG1   . THR A 110 ? 0.34320 0.22900 0.19670 0.00770  0.02090  0.00030  110  THR A OG1   
862  C  CG2   . THR A 110 ? 0.29480 0.19830 0.25020 0.04200  -0.02820 -0.00800 110  THR A CG2   
863  N  N     . ILE A 111 ? 0.31600 0.25690 0.19850 0.07340  -0.02620 -0.02320 111  ILE A N     
864  C  CA    . ILE A 111 ? 0.28980 0.26120 0.21600 0.03240  -0.02430 -0.07230 111  ILE A CA    
865  C  C     . ILE A 111 ? 0.32440 0.27540 0.21030 0.00250  -0.00090 -0.03700 111  ILE A C     
866  O  O     . ILE A 111 ? 0.29750 0.34250 0.22200 -0.03400 -0.01550 -0.01870 111  ILE A O     
867  C  CB    . ILE A 111 ? 0.40170 0.32980 0.22730 0.09270  -0.02100 -0.03790 111  ILE A CB    
868  C  CG1   . ILE A 111 ? 0.44520 0.39120 0.23710 0.11410  0.01230  -0.04130 111  ILE A CG1   
869  C  CG2   . ILE A 111 ? 0.49070 0.29460 0.23890 0.03590  -0.03080 0.00860  111  ILE A CG2   
870  C  CD1   . ILE A 111 ? 0.47850 0.43940 0.26650 0.10710  -0.00200 0.00730  111  ILE A CD1   
871  N  N     . SER A 112 ? 0.34940 0.29800 0.21840 0.01430  0.00840  0.00070  112  SER A N     
872  C  CA    . SER A 112 ? 0.39740 0.26730 0.22690 0.00220  0.00460  0.04730  112  SER A CA    
873  C  C     . SER A 112 ? 0.34190 0.29070 0.23240 -0.05210 0.01890  0.05760  112  SER A C     
874  O  O     . SER A 112 ? 0.39280 0.29610 0.25920 -0.02770 0.00610  0.07840  112  SER A O     
875  C  CB    . SER A 112 ? 0.53120 0.35660 0.26000 0.02140  -0.00820 0.08060  112  SER A CB    
876  O  OG    . SER A 112 ? 0.55810 0.42690 0.27370 0.04960  -0.03100 0.06070  112  SER A OG    
877  N  N     . GLU A 113 ? 0.31420 0.24370 0.21830 -0.04420 0.01820  0.03850  113  GLU A N     
878  C  CA    A GLU A 113 ? 0.31770 0.20330 0.21380 0.00050  0.01820  0.04650  113  GLU A CA    
879  C  CA    B GLU A 113 ? 0.34040 0.21600 0.22260 0.01750  0.00130  0.03230  113  GLU A CA    
880  C  C     . GLU A 113 ? 0.32550 0.18810 0.22670 -0.02950 0.00070  0.02090  113  GLU A C     
881  O  O     . GLU A 113 ? 0.36370 0.20210 0.24400 -0.00120 -0.02790 0.00280  113  GLU A O     
882  C  CB    A GLU A 113 ? 0.30280 0.24440 0.22090 0.02300  0.00720  0.03580  113  GLU A CB    
883  C  CB    B GLU A 113 ? 0.38240 0.26080 0.24310 0.07280  -0.03540 0.00870  113  GLU A CB    
884  C  CG    A GLU A 113 ? 0.35670 0.25970 0.24120 0.03020  -0.01290 0.04170  113  GLU A CG    
885  C  CG    B GLU A 113 ? 0.47080 0.29180 0.27620 0.10310  -0.06160 -0.00780 113  GLU A CG    
886  C  CD    A GLU A 113 ? 0.42200 0.23830 0.24270 0.00910  -0.00640 0.07060  113  GLU A CD    
887  C  CD    B GLU A 113 ? 0.58220 0.34170 0.30170 0.09150  -0.07790 -0.03630 113  GLU A CD    
888  O  OE1   A GLU A 113 ? 0.44370 0.22900 0.24350 0.03700  0.01750  0.07590  113  GLU A OE1   
889  O  OE1   B GLU A 113 ? 0.64690 0.34100 0.32390 0.09680  -0.06320 -0.03590 113  GLU A OE1   
890  O  OE2   A GLU A 113 ? 0.44710 0.25580 0.25780 0.02790  -0.01510 0.07550  113  GLU A OE2   
891  O  OE2   B GLU A 113 ? 0.63570 0.37720 0.30740 0.07350  -0.09010 -0.03650 113  GLU A OE2   
892  N  N     . PHE A 114 ? 0.27910 0.17220 0.21780 0.01510  0.01330  -0.01160 114  PHE A N     
893  C  CA    . PHE A 114 ? 0.33100 0.14570 0.21030 -0.00750 -0.01720 -0.00090 114  PHE A CA    
894  C  C     . PHE A 114 ? 0.27970 0.17800 0.24990 0.04730  -0.04070 -0.01370 114  PHE A C     
895  O  O     . PHE A 114 ? 0.35540 0.19220 0.28710 0.01040  -0.06010 -0.00850 114  PHE A O     
896  C  CB    . PHE A 114 ? 0.35890 0.13680 0.19570 -0.00930 0.01350  0.00020  114  PHE A CB    
897  C  CG    . PHE A 114 ? 0.36230 0.15820 0.17330 -0.00820 -0.00650 -0.00960 114  PHE A CG    
898  C  CD1   . PHE A 114 ? 0.40840 0.17150 0.15890 -0.03320 0.00010  -0.01280 114  PHE A CD1   
899  C  CD2   . PHE A 114 ? 0.35810 0.13750 0.17580 -0.02690 0.01130  0.00770  114  PHE A CD2   
900  C  CE1   . PHE A 114 ? 0.40140 0.15770 0.15410 -0.05720 0.01490  0.00400  114  PHE A CE1   
901  C  CE2   . PHE A 114 ? 0.36490 0.17610 0.17700 -0.03600 0.01570  0.02810  114  PHE A CE2   
902  C  CZ    . PHE A 114 ? 0.35470 0.16260 0.17810 -0.02840 -0.00670 0.02950  114  PHE A CZ    
903  N  N     . THR A 115 ? 0.30450 0.18460 0.23480 -0.01130 0.01190  -0.00040 115  THR A N     
904  C  CA    . THR A 115 ? 0.30250 0.25480 0.23400 -0.01660 -0.00120 0.00270  115  THR A CA    
905  C  C     . THR A 115 ? 0.29970 0.23970 0.24140 0.00410  -0.00970 -0.01860 115  THR A C     
906  O  O     . THR A 115 ? 0.33060 0.23410 0.22550 -0.02740 0.03430  -0.02180 115  THR A O     
907  C  CB    . THR A 115 ? 0.36640 0.26660 0.23570 -0.04790 0.01030  -0.05330 115  THR A CB    
908  O  OG1   . THR A 115 ? 0.37100 0.31710 0.24870 -0.11930 0.04110  -0.07100 115  THR A OG1   
909  C  CG2   . THR A 115 ? 0.33950 0.26850 0.22280 0.01130  -0.01050 -0.07070 115  THR A CG2   
910  N  N     . VAL A 116 ? 0.30970 0.22710 0.25210 0.02000  -0.01810 -0.03940 116  VAL A N     
911  C  CA    . VAL A 116 ? 0.36750 0.23270 0.25210 0.00350  0.00280  -0.08810 116  VAL A CA    
912  C  C     . VAL A 116 ? 0.38310 0.30580 0.26570 -0.03510 0.01280  -0.02530 116  VAL A C     
913  O  O     . VAL A 116 ? 0.37410 0.27320 0.25390 -0.09120 0.01570  -0.01820 116  VAL A O     
914  C  CB    . VAL A 116 ? 0.42740 0.30450 0.27580 0.06550  -0.00800 -0.07400 116  VAL A CB    
915  C  CG1   . VAL A 116 ? 0.45490 0.30080 0.28460 0.06450  -0.00920 -0.05150 116  VAL A CG1   
916  C  CG2   . VAL A 116 ? 0.42690 0.36030 0.26770 0.02340  -0.05230 -0.10860 116  VAL A CG2   
917  N  N     . LYS A 117 ? 0.40690 0.30060 0.27880 -0.03680 0.05880  0.00370  117  LYS A N     
918  C  CA    . LYS A 117 ? 0.36060 0.30830 0.27730 -0.03170 0.06070  0.01230  117  LYS A CA    
919  C  C     . LYS A 117 ? 0.34930 0.26380 0.24900 -0.07910 0.04580  -0.00760 117  LYS A C     
920  O  O     . LYS A 117 ? 0.45610 0.23220 0.22210 -0.10750 0.02150  -0.01650 117  LYS A O     
921  C  CB    . LYS A 117 ? 0.47320 0.38370 0.31440 -0.06150 0.06920  0.06100  117  LYS A CB    
922  C  CG    . LYS A 117 ? 0.61160 0.50390 0.35680 -0.09280 0.09080  0.09060  117  LYS A CG    
923  C  CD    . LYS A 117 ? 0.70280 0.59120 0.38260 -0.05430 0.13940  0.09960  117  LYS A CD    
924  C  CE    . LYS A 117 ? 0.81290 0.64470 0.40120 0.03570  0.16990  0.11570  117  LYS A CE    
925  N  NZ    . LYS A 117 ? 0.83910 0.67380 0.41060 0.08080  0.21200  0.11970  117  LYS A NZ    
926  N  N     . ARG A 118 ? 0.33320 0.25490 0.23810 -0.09390 0.06050  -0.01270 118  ARG A N     
927  C  CA    A ARG A 118 ? 0.38310 0.22090 0.23860 -0.02430 0.04570  -0.00210 118  ARG A CA    
928  C  CA    B ARG A 118 ? 0.36350 0.20940 0.24430 -0.04440 0.02330  0.00560  118  ARG A CA    
929  C  C     . ARG A 118 ? 0.39500 0.20090 0.23660 -0.05940 0.02130  0.02330  118  ARG A C     
930  O  O     . ARG A 118 ? 0.41210 0.24370 0.23820 -0.08070 0.03180  -0.01610 118  ARG A O     
931  C  CB    A ARG A 118 ? 0.43560 0.31820 0.25920 -0.05350 0.05350  0.01850  118  ARG A CB    
932  C  CB    B ARG A 118 ? 0.37960 0.24850 0.26910 -0.06840 -0.01120 0.02350  118  ARG A CB    
933  C  CG    A ARG A 118 ? 0.55060 0.44830 0.29610 -0.05140 0.04260  0.00840  118  ARG A CG    
934  C  CG    B ARG A 118 ? 0.46440 0.31590 0.30000 -0.04680 -0.04960 0.01260  118  ARG A CG    
935  C  CD    A ARG A 118 ? 0.62240 0.47290 0.31420 -0.02830 0.04540  0.02480  118  ARG A CD    
936  C  CD    B ARG A 118 ? 0.51380 0.31560 0.32530 -0.01160 -0.09420 0.04070  118  ARG A CD    
937  N  NE    A ARG A 118 ? 0.64010 0.52440 0.32740 -0.01900 0.07110  0.03950  118  ARG A NE    
938  N  NE    B ARG A 118 ? 0.55800 0.42000 0.35080 0.03560  -0.08280 0.02460  118  ARG A NE    
939  C  CZ    A ARG A 118 ? 0.64510 0.50210 0.32990 -0.02700 0.07970  0.03410  118  ARG A CZ    
940  C  CZ    B ARG A 118 ? 0.57250 0.45240 0.36660 0.04780  -0.07510 0.01930  118  ARG A CZ    
941  N  NH1   A ARG A 118 ? 0.57980 0.37390 0.32260 -0.04790 0.07000  0.02980  118  ARG A NH1   
942  N  NH1   B ARG A 118 ? 0.60860 0.44460 0.37590 0.04050  -0.06120 0.00840  118  ARG A NH1   
943  N  NH2   A ARG A 118 ? 0.65790 0.50340 0.32980 -0.03010 0.09030  0.05250  118  ARG A NH2   
944  N  NH2   B ARG A 118 ? 0.56110 0.47080 0.36850 0.05370  -0.08080 0.04590  118  ARG A NH2   
945  N  N     . ILE A 119 ? 0.34900 0.21900 0.24080 -0.05560 0.01080  0.02130  119  ILE A N     
946  C  CA    . ILE A 119 ? 0.34760 0.19930 0.22610 -0.06110 -0.01660 0.03280  119  ILE A CA    
947  C  C     . ILE A 119 ? 0.38300 0.25870 0.25400 -0.05850 0.00720  0.01530  119  ILE A C     
948  O  O     . ILE A 119 ? 0.42630 0.23920 0.22800 -0.08610 0.02270  0.00380  119  ILE A O     
949  C  CB    . ILE A 119 ? 0.40140 0.21430 0.23440 -0.01820 -0.00440 0.02230  119  ILE A CB    
950  C  CG1   . ILE A 119 ? 0.42770 0.30160 0.24450 -0.02660 0.03480  0.04680  119  ILE A CG1   
951  C  CG2   . ILE A 119 ? 0.42280 0.17850 0.21880 0.03030  -0.02130 0.01460  119  ILE A CG2   
952  C  CD1   . ILE A 119 ? 0.44250 0.25630 0.25560 -0.05140 0.10870  -0.00060 119  ILE A CD1   
953  N  N     . LYS A 120 ? 0.34950 0.21660 0.29810 -0.04250 0.03990  0.00160  120  LYS A N     
954  C  CA    . LYS A 120 ? 0.35680 0.22230 0.33480 -0.06850 0.04260  -0.03860 120  LYS A CA    
955  C  C     . LYS A 120 ? 0.39780 0.20110 0.33630 -0.08630 0.02900  -0.03390 120  LYS A C     
956  O  O     . LYS A 120 ? 0.44440 0.23040 0.34140 -0.04610 0.00660  -0.04550 120  LYS A O     
957  C  CB    . LYS A 120 ? 0.34120 0.24660 0.34970 -0.09180 0.06960  -0.04760 120  LYS A CB    
958  C  CG    . LYS A 120 ? 0.33320 0.23970 0.37060 -0.07030 0.05460  -0.06040 120  LYS A CG    
959  C  CD    . LYS A 120 ? 0.36950 0.28210 0.38310 -0.04680 0.05960  -0.09930 120  LYS A CD    
960  C  CE    . LYS A 120 ? 0.45120 0.39700 0.40100 -0.03530 0.10510  -0.12390 120  LYS A CE    
961  N  NZ    . LYS A 120 ? 0.46320 0.47000 0.40920 -0.06700 0.11770  -0.11270 120  LYS A NZ    
962  N  N     . GLY A 121 ? 0.41550 0.20880 0.33260 -0.04630 0.05240  -0.03710 121  GLY A N     
963  C  CA    . GLY A 121 ? 0.42670 0.23130 0.31930 0.02690  0.04820  -0.04900 121  GLY A CA    
964  C  C     . GLY A 121 ? 0.44920 0.19150 0.28940 -0.00230 0.05350  -0.04630 121  GLY A C     
965  O  O     . GLY A 121 ? 0.50410 0.19140 0.30490 -0.03390 0.03040  -0.02650 121  GLY A O     
966  N  N     . MET A 122 ? 0.41150 0.21380 0.25490 -0.04640 0.06240  -0.03840 122  MET A N     
967  C  CA    . MET A 122 ? 0.42050 0.19370 0.26930 -0.08210 0.00630  -0.02790 122  MET A CA    
968  C  C     . MET A 122 ? 0.43500 0.20890 0.27110 -0.03160 -0.00980 -0.04780 122  MET A C     
969  O  O     . MET A 122 ? 0.46510 0.20520 0.22630 0.00260  -0.01630 -0.01870 122  MET A O     
970  C  CB    . MET A 122 ? 0.46480 0.17090 0.27180 -0.10440 -0.02560 -0.02900 122  MET A CB    
971  C  CG    . MET A 122 ? 0.47120 0.23070 0.25300 -0.14150 -0.04720 -0.02750 122  MET A CG    
972  S  SD    . MET A 122 ? 0.51950 0.27550 0.25860 -0.04880 -0.01520 -0.01080 122  MET A SD    
973  C  CE    . MET A 122 ? 0.51910 0.28340 0.25970 -0.01630 0.04960  -0.02530 122  MET A CE    
974  N  N     . ARG A 123 ? 0.43080 0.21680 0.28820 -0.07580 -0.04090 -0.05660 123  ARG A N     
975  C  CA    . ARG A 123 ? 0.43130 0.23950 0.30390 -0.08140 -0.05100 -0.04330 123  ARG A CA    
976  C  C     . ARG A 123 ? 0.47210 0.21620 0.31900 -0.11470 -0.04710 -0.03010 123  ARG A C     
977  O  O     . ARG A 123 ? 0.43850 0.22930 0.30280 -0.05210 -0.04320 0.00060  123  ARG A O     
978  C  CB    . ARG A 123 ? 0.37400 0.29530 0.31990 -0.08950 -0.05370 -0.02220 123  ARG A CB    
979  C  CG    . ARG A 123 ? 0.37390 0.30550 0.34090 -0.06950 -0.05300 -0.03960 123  ARG A CG    
980  C  CD    . ARG A 123 ? 0.35780 0.32500 0.36030 -0.06390 -0.01780 -0.01290 123  ARG A CD    
981  N  NE    . ARG A 123 ? 0.42010 0.28990 0.35800 -0.04060 -0.05470 -0.00700 123  ARG A NE    
982  C  CZ    . ARG A 123 ? 0.41030 0.29660 0.33590 -0.04200 -0.07630 -0.00720 123  ARG A CZ    
983  N  NH1   . ARG A 123 ? 0.43930 0.30820 0.32060 -0.03220 -0.09840 -0.02670 123  ARG A NH1   
984  N  NH2   . ARG A 123 ? 0.41200 0.27130 0.33140 -0.07130 -0.06940 -0.03760 123  ARG A NH2   
985  N  N     . PRO A 124 ? 0.53640 0.18710 0.33370 -0.09100 -0.03810 -0.01900 124  PRO A N     
986  C  CA    . PRO A 124 ? 0.56020 0.22640 0.33440 -0.06130 -0.02390 -0.01520 124  PRO A CA    
987  C  C     . PRO A 124 ? 0.56480 0.15480 0.31760 -0.04630 -0.03030 0.01300  124  PRO A C     
988  O  O     . PRO A 124 ? 0.62820 0.18590 0.32710 -0.00850 -0.06080 -0.02160 124  PRO A O     
989  C  CB    . PRO A 124 ? 0.55960 0.22240 0.34700 -0.07240 -0.01360 -0.00900 124  PRO A CB    
990  C  CG    . PRO A 124 ? 0.48800 0.23850 0.34520 -0.09230 -0.00170 -0.01740 124  PRO A CG    
991  C  CD    . PRO A 124 ? 0.51120 0.22180 0.33940 -0.14090 -0.04000 -0.01510 124  PRO A CD    
992  N  N     . GLU A 125 ? 0.54140 0.16350 0.29600 -0.05820 -0.04870 0.00860  125  GLU A N     
993  C  CA    . GLU A 125 ? 0.50920 0.16610 0.28750 0.00920  -0.06090 -0.00750 125  GLU A CA    
994  C  C     . GLU A 125 ? 0.48690 0.15230 0.27070 0.01410  -0.05580 -0.00370 125  GLU A C     
995  O  O     . GLU A 125 ? 0.50010 0.18790 0.24940 0.02820  -0.06460 -0.02160 125  GLU A O     
996  C  CB    . GLU A 125 ? 0.45310 0.22740 0.29900 -0.00940 -0.07680 -0.00870 125  GLU A CB    
997  C  CG    . GLU A 125 ? 0.52730 0.29340 0.32770 0.08400  -0.02870 -0.03160 125  GLU A CG    
998  C  CD    . GLU A 125 ? 0.59430 0.37910 0.35570 -0.02550 -0.04840 0.03600  125  GLU A CD    
999  O  OE1   . GLU A 125 ? 0.69330 0.41090 0.37420 -0.01780 -0.02890 0.02730  125  GLU A OE1   
1000 O  OE2   . GLU A 125 ? 0.50670 0.43730 0.35500 -0.00700 -0.06820 0.07540  125  GLU A OE2   
1001 N  N     . VAL A 126 ? 0.45340 0.13400 0.26340 0.02910  -0.07450 -0.03680 126  VAL A N     
1002 C  CA    . VAL A 126 ? 0.43388 0.12362 0.24290 0.00740  -0.06099 -0.03629 126  VAL A CA    
1003 C  C     . VAL A 126 ? 0.42330 0.12680 0.26350 -0.00360 -0.06660 -0.03850 126  VAL A C     
1004 O  O     . VAL A 126 ? 0.44920 0.15470 0.28020 0.04320  -0.01630 -0.01620 126  VAL A O     
1005 C  CB    . VAL A 126 ? 0.42110 0.11420 0.21940 0.00140  -0.04690 -0.02140 126  VAL A CB    
1006 C  CG1   . VAL A 126 ? 0.40400 0.13730 0.22890 0.00390  -0.03380 -0.02190 126  VAL A CG1   
1007 C  CG2   . VAL A 126 ? 0.37430 0.19460 0.20800 -0.06760 -0.01370 -0.04040 126  VAL A CG2   
1008 N  N     . GLU A 127 ? 0.45070 0.14440 0.27180 -0.02640 -0.07290 -0.05030 127  GLU A N     
1009 C  CA    . GLU A 127 ? 0.40600 0.14690 0.30590 0.00910  -0.10820 -0.05660 127  GLU A CA    
1010 C  C     . GLU A 127 ? 0.46400 0.15250 0.29670 0.03840  -0.09840 -0.06130 127  GLU A C     
1011 O  O     . GLU A 127 ? 0.51390 0.16960 0.29400 0.04940  -0.13250 -0.05680 127  GLU A O     
1012 C  CB    . GLU A 127 ? 0.39400 0.15500 0.34670 0.01620  -0.11870 -0.07640 127  GLU A CB    
1013 C  CG    . GLU A 127 ? 0.46930 0.17130 0.39600 0.02640  -0.10080 -0.08120 127  GLU A CG    
1014 C  CD    . GLU A 127 ? 0.60970 0.30060 0.43230 -0.05490 -0.13340 -0.08170 127  GLU A CD    
1015 O  OE1   . GLU A 127 ? 0.65520 0.26020 0.45630 -0.06570 -0.12180 -0.07390 127  GLU A OE1   
1016 O  OE2   . GLU A 127 ? 0.66270 0.36170 0.44080 -0.11450 -0.15190 -0.06460 127  GLU A OE2   
1017 N  N     . GLU A 128 ? 0.47619 0.15401 0.29710 0.06660  -0.08380 -0.05300 128  GLU A N     
1018 C  CA    . GLU A 128 ? 0.48877 0.15963 0.31450 0.08879  -0.06659 -0.04029 128  GLU A CA    
1019 C  C     . GLU A 128 ? 0.51640 0.19520 0.29660 0.08100  -0.07740 -0.06040 128  GLU A C     
1020 O  O     . GLU A 128 ? 0.50930 0.20630 0.27190 0.06520  -0.10130 -0.09050 128  GLU A O     
1021 C  CB    . GLU A 128 ? 0.54140 0.21630 0.34610 0.11700  -0.08540 -0.01940 128  GLU A CB    
1022 C  CG    . GLU A 128 ? 0.68290 0.30760 0.37820 0.12690  -0.07730 0.03970  128  GLU A CG    
1023 C  CD    . GLU A 128 ? 0.79390 0.45090 0.41500 0.19080  -0.06110 0.11750  128  GLU A CD    
1024 O  OE1   . GLU A 128 ? 0.70240 0.40280 0.41350 0.14590  -0.04060 0.18120  128  GLU A OE1   
1025 O  OE2   . GLU A 128 ? 0.92880 0.59110 0.44470 0.20330  -0.05400 0.12140  128  GLU A OE2   
1026 N  N     . VAL A 129 ? 0.48469 0.14121 0.28860 0.04500  -0.06660 -0.04100 129  VAL A N     
1027 C  CA    . VAL A 129 ? 0.48568 0.15452 0.26040 0.06689  -0.11759 -0.04059 129  VAL A CA    
1028 C  C     . VAL A 129 ? 0.47680 0.18850 0.23990 0.06540  -0.09810 -0.03670 129  VAL A C     
1029 O  O     . VAL A 129 ? 0.46800 0.24960 0.22220 0.09010  -0.06880 -0.06940 129  VAL A O     
1030 C  CB    . VAL A 129 ? 0.46080 0.16860 0.24580 0.05260  -0.12290 -0.03310 129  VAL A CB    
1031 C  CG1   . VAL A 129 ? 0.48150 0.20580 0.23740 0.10560  -0.08220 -0.02650 129  VAL A CG1   
1032 C  CG2   . VAL A 129 ? 0.47320 0.22520 0.26340 0.03550  -0.14740 -0.00130 129  VAL A CG2   
1033 N  N     . VAL A 130 ? 0.48180 0.17200 0.24060 0.05450  -0.10280 -0.03950 130  VAL A N     
1034 C  CA    . VAL A 130 ? 0.44030 0.18110 0.22690 0.07890  -0.07200 -0.02180 130  VAL A CA    
1035 C  C     . VAL A 130 ? 0.46010 0.24350 0.24240 0.09920  -0.07470 -0.06480 130  VAL A C     
1036 O  O     . VAL A 130 ? 0.49930 0.26620 0.24360 0.09810  -0.06660 -0.08460 130  VAL A O     
1037 C  CB    . VAL A 130 ? 0.44550 0.20770 0.21780 0.08400  -0.07680 -0.02050 130  VAL A CB    
1038 C  CG1   . VAL A 130 ? 0.47910 0.25590 0.22960 0.09610  -0.07620 0.01840  130  VAL A CG1   
1039 C  CG2   . VAL A 130 ? 0.50020 0.16130 0.23360 -0.00760 -0.09080 -0.02530 130  VAL A CG2   
1040 N  N     . HIS A 131 ? 0.48280 0.21900 0.24260 0.08280  -0.10060 -0.07760 131  HIS A N     
1041 C  CA    . HIS A 131 ? 0.53150 0.27930 0.28660 0.08930  -0.09530 -0.11810 131  HIS A CA    
1042 C  C     . HIS A 131 ? 0.55488 0.30971 0.29111 0.09169  -0.08979 -0.14048 131  HIS A C     
1043 O  O     . HIS A 131 ? 0.59060 0.37290 0.29370 0.12200  -0.07180 -0.15020 131  HIS A O     
1044 C  CB    . HIS A 131 ? 0.54430 0.28880 0.32310 0.07980  -0.08670 -0.10640 131  HIS A CB    
1045 C  CG    . HIS A 131 ? 0.59090 0.40550 0.35620 0.10290  -0.06570 -0.07020 131  HIS A CG    
1046 N  ND1   . HIS A 131 ? 0.57810 0.46220 0.37600 0.14190  -0.05860 -0.04450 131  HIS A ND1   
1047 C  CD2   . HIS A 131 ? 0.61420 0.49220 0.36810 0.08520  -0.06130 -0.02230 131  HIS A CD2   
1048 C  CE1   . HIS A 131 ? 0.62890 0.49870 0.38640 0.06390  -0.04790 -0.00280 131  HIS A CE1   
1049 N  NE2   . HIS A 131 ? 0.61990 0.50790 0.37750 0.08500  -0.03390 -0.02040 131  HIS A NE2   
1050 N  N     . GLY A 132 ? 0.51890 0.30510 0.29200 0.08760  -0.09450 -0.14440 132  GLY A N     
1051 C  CA    . GLY A 132 ? 0.50127 0.27431 0.29231 0.08709  -0.07749 -0.13667 132  GLY A CA    
1052 C  C     . GLY A 132 ? 0.51549 0.31180 0.27951 0.09419  -0.10329 -0.13889 132  GLY A C     
1053 O  O     . GLY A 132 ? 0.54009 0.35770 0.29731 0.09459  -0.08049 -0.16389 132  GLY A O     
1054 N  N     . PHE A 133 ? 0.50280 0.23100 0.26420 0.10250  -0.09100 -0.09920 133  PHE A N     
1055 C  CA    . PHE A 133 ? 0.47329 0.23761 0.24270 0.12779  -0.09900 -0.09279 133  PHE A CA    
1056 C  C     . PHE A 133 ? 0.51720 0.32420 0.24740 0.16000  -0.10830 -0.09340 133  PHE A C     
1057 O  O     . PHE A 133 ? 0.56510 0.33690 0.23850 0.21100  -0.08100 -0.08630 133  PHE A O     
1058 C  CB    . PHE A 133 ? 0.47420 0.23730 0.21350 0.10620  -0.05650 -0.08740 133  PHE A CB    
1059 C  CG    . PHE A 133 ? 0.49289 0.21330 0.18461 0.09770  -0.03240 -0.06029 133  PHE A CG    
1060 C  CD1   . PHE A 133 ? 0.51760 0.23940 0.18970 0.07560  -0.02830 0.00220  133  PHE A CD1   
1061 C  CD2   . PHE A 133 ? 0.53940 0.21270 0.18110 0.07280  -0.03700 -0.00720 133  PHE A CD2   
1062 C  CE1   . PHE A 133 ? 0.52480 0.22790 0.18110 0.08790  -0.01070 -0.02500 133  PHE A CE1   
1063 C  CE2   . PHE A 133 ? 0.52590 0.18170 0.17830 0.00900  0.01070  -0.02550 133  PHE A CE2   
1064 C  CZ    . PHE A 133 ? 0.53140 0.14750 0.17320 0.02870  0.01250  -0.02080 133  PHE A CZ    
1065 N  N     . LEU A 134 ? 0.49860 0.39000 0.26790 0.16360  -0.06840 -0.08990 134  LEU A N     
1066 C  CA    . LEU A 134 ? 0.52030 0.54770 0.30480 0.17200  -0.03250 -0.08920 134  LEU A CA    
1067 C  C     . LEU A 134 ? 0.57120 0.67950 0.31380 0.18290  -0.07540 -0.10230 134  LEU A C     
1068 O  O     . LEU A 134 ? 0.60780 0.81850 0.30070 0.18560  -0.10560 -0.07760 134  LEU A O     
1069 C  CB    . LEU A 134 ? 0.56090 0.54840 0.34450 0.17210  0.00650  -0.07130 134  LEU A CB    
1070 C  CG    . LEU A 134 ? 0.57160 0.49240 0.36390 0.10560  0.08230  -0.13860 134  LEU A CG    
1071 C  CD1   . LEU A 134 ? 0.54520 0.52120 0.38100 0.10940  0.09630  -0.12100 134  LEU A CD1   
1072 C  CD2   . LEU A 134 ? 0.54740 0.50200 0.35670 0.13400  0.09450  -0.14460 134  LEU A CD2   
1073 N  N     . ASP A 135 ? 0.63150 0.64860 0.31980 0.13530  -0.07570 -0.14770 135  ASP A N     
1074 C  CA    . ASP A 135 ? 0.69930 0.60300 0.33700 0.03980  -0.10180 -0.19910 135  ASP A CA    
1075 C  C     . ASP A 135 ? 0.67430 0.53150 0.31160 0.06850  -0.10280 -0.19230 135  ASP A C     
1076 O  O     . ASP A 135 ? 0.68370 0.56110 0.32150 0.07650  -0.11200 -0.16970 135  ASP A O     
1077 C  CB    . ASP A 135 ? 0.81240 0.65660 0.38760 -0.04020 -0.07250 -0.24910 135  ASP A CB    
1078 C  CG    . ASP A 135 ? 0.88020 0.72240 0.41750 -0.07080 -0.06730 -0.28260 135  ASP A CG    
1079 O  OD1   . ASP A 135 ? 0.88430 0.79868 0.42652 -0.06209 -0.07440 -0.30277 135  ASP A OD1   
1080 O  OD2   . ASP A 135 ? 0.91760 0.70070 0.44620 -0.08990 -0.04520 -0.27030 135  ASP A OD2   
1081 N  N     . GLU A 136 ? 0.63090 0.48010 0.28950 0.07790  -0.11180 -0.15670 136  GLU A N     
1082 C  CA    . GLU A 136 ? 0.60800 0.42970 0.28220 0.14150  -0.08540 -0.14430 136  GLU A CA    
1083 C  C     . GLU A 136 ? 0.63170 0.42010 0.29850 0.19050  -0.07850 -0.14530 136  GLU A C     
1084 O  O     . GLU A 136 ? 0.66987 0.44360 0.30252 0.22838  -0.08370 -0.13547 136  GLU A O     
1085 C  CB    . GLU A 136 ? 0.58180 0.38720 0.27490 0.10450  -0.06300 -0.14990 136  GLU A CB    
1086 C  CG    . GLU A 136 ? 0.54880 0.34870 0.26730 0.11700  -0.04080 -0.14040 136  GLU A CG    
1087 C  CD    . GLU A 136 ? 0.61760 0.36300 0.25250 0.12490  -0.01280 -0.10620 136  GLU A CD    
1088 O  OE1   . GLU A 136 ? 0.58790 0.34180 0.24130 0.09720  -0.01870 -0.09780 136  GLU A OE1   
1089 O  OE2   . GLU A 136 ? 0.62080 0.39440 0.26370 0.12990  0.01250  -0.07900 136  GLU A OE2   
1090 N  N     . MET A 137 ? 0.63990 0.43530 0.30630 0.23580  -0.09310 -0.12960 137  MET A N     
1091 C  CA    . MET A 137 ? 0.61209 0.42430 0.30631 0.24828  -0.10510 -0.13148 137  MET A CA    
1092 C  C     . MET A 137 ? 0.63459 0.48760 0.33111 0.23789  -0.11700 -0.16839 137  MET A C     
1093 O  O     . MET A 137 ? 0.68377 0.50821 0.35372 0.27847  -0.11410 -0.16347 137  MET A O     
1094 C  CB    . MET A 137 ? 0.62520 0.40820 0.28750 0.24080  -0.08480 -0.11520 137  MET A CB    
1095 C  CG    . MET A 137 ? 0.63650 0.42300 0.28350 0.19970  -0.05640 -0.13030 137  MET A CG    
1096 S  SD    . MET A 137 ? 0.69400 0.52090 0.25980 0.27470  -0.05370 -0.09020 137  MET A SD    
1097 C  CE    . MET A 137 ? 0.69399 0.49630 0.25681 0.24809  -0.03370 -0.09109 137  MET A CE    
1098 N  N     . LEU A 138 ? 0.62229 0.55650 0.32731 0.24420  -0.14150 -0.17779 138  LEU A N     
1099 C  CA    . LEU A 138 ? 0.67970 0.61910 0.34600 0.22310  -0.17290 -0.18250 138  LEU A CA    
1100 C  C     . LEU A 138 ? 0.72050 0.62110 0.35390 0.19590  -0.17970 -0.18490 138  LEU A C     
1101 O  O     . LEU A 138 ? 0.77718 0.69329 0.35432 0.17189  -0.18498 -0.17838 138  LEU A O     
1102 C  CB    . LEU A 138 ? 0.68469 0.68819 0.35251 0.25669  -0.18239 -0.17469 138  LEU A CB    
1103 C  CG    . LEU A 138 ? 0.74700 0.75300 0.36610 0.29780  -0.19310 -0.12140 138  LEU A CG    
1104 C  CD1   . LEU A 138 ? 0.78190 0.76090 0.36600 0.28660  -0.19030 -0.11540 138  LEU A CD1   
1105 C  CD2   . LEU A 138 ? 0.79790 0.77760 0.38520 0.29290  -0.17830 -0.09440 138  LEU A CD2   
1106 N  N     . ALA A 139 ? 0.70810 0.52890 0.38330 0.16790  -0.13210 -0.21640 139  ALA A N     
1107 C  CA    . ALA A 139 ? 0.70009 0.47880 0.39521 0.11739  -0.10649 -0.22269 139  ALA A CA    
1108 C  C     . ALA A 139 ? 0.76630 0.46700 0.39310 0.09540  -0.08200 -0.21530 139  ALA A C     
1109 O  O     . ALA A 139 ? 0.82690 0.52940 0.39490 0.08530  -0.06900 -0.21650 139  ALA A O     
1110 C  CB    . ALA A 139 ? 0.71300 0.48360 0.39930 0.11430  -0.10370 -0.22550 139  ALA A CB    
1111 N  N     . ALA A 140 ? 0.82330 0.47440 0.36900 0.12500  -0.05830 -0.17230 140  ALA A N     
1112 C  CA    . ALA A 140 ? 0.86860 0.51590 0.36070 0.17940  -0.01050 -0.16890 140  ALA A CA    
1113 C  C     . ALA A 140 ? 0.89710 0.62660 0.35710 0.18370  0.02620  -0.16700 140  ALA A C     
1114 O  O     . ALA A 140 ? 0.95310 0.70880 0.35060 0.13240  0.04300  -0.13150 140  ALA A O     
1115 C  CB    . ALA A 140 ? 0.85800 0.49780 0.36070 0.18750  -0.01230 -0.14480 140  ALA A CB    
1116 N  N     . GLY A 141 ? 0.84858 0.65740 0.34963 0.21328  0.00930  -0.17828 141  GLY A N     
1117 C  CA    . GLY A 141 ? 0.81280 0.72640 0.32410 0.21740  -0.00300 -0.15350 141  GLY A CA    
1118 C  C     . GLY A 141 ? 0.78720 0.77050 0.32140 0.18420  0.00320  -0.14560 141  GLY A C     
1119 O  O     . GLY A 141 ? 0.83500 0.79460 0.31940 0.15370  0.01080  -0.12060 141  GLY A O     
1120 N  N     . PRO A 142 ? 0.75410 0.79230 0.33030 0.11720  -0.02850 -0.13340 142  PRO A N     
1121 C  CA    . PRO A 142 ? 0.71380 0.73830 0.32150 0.11920  -0.04280 -0.14520 142  PRO A CA    
1122 C  C     . PRO A 142 ? 0.67370 0.72870 0.30350 0.15290  -0.03690 -0.18100 142  PRO A C     
1123 O  O     . PRO A 142 ? 0.67860 0.77560 0.29010 0.15670  -0.02130 -0.17410 142  PRO A O     
1124 C  CB    . PRO A 142 ? 0.71990 0.76500 0.33190 0.07490  -0.03620 -0.10500 142  PRO A CB    
1125 C  CG    . PRO A 142 ? 0.74580 0.79630 0.33650 0.07270  -0.03460 -0.09170 142  PRO A CG    
1126 C  CD    . PRO A 142 ? 0.73930 0.81670 0.33410 0.10260  -0.02000 -0.10780 142  PRO A CD    
1127 N  N     . THR A 143 ? 0.60160 0.68490 0.28590 0.13520  -0.06560 -0.18600 143  THR A N     
1128 C  CA    . THR A 143 ? 0.54060 0.68750 0.26171 0.13960  -0.06950 -0.16060 143  THR A CA    
1129 C  C     . THR A 143 ? 0.57299 0.65959 0.25172 0.12669  -0.05080 -0.15569 143  THR A C     
1130 O  O     . THR A 143 ? 0.58490 0.70690 0.28251 0.17670  -0.05790 -0.17280 143  THR A O     
1131 C  CB    . THR A 143 ? 0.53590 0.77910 0.30230 0.08570  -0.05040 -0.10930 143  THR A CB    
1132 O  OG1   . THR A 143 ? 0.56520 0.84830 0.34080 0.08230  -0.06530 -0.06750 143  THR A OG1   
1133 C  CG2   . THR A 143 ? 0.54520 0.79920 0.28320 0.02860  -0.05090 -0.10450 143  THR A CG2   
1134 N  N     . ALA A 144 ? 0.55600 0.51030 0.22990 0.08930  -0.03920 -0.14860 144  ALA A N     
1135 C  CA    . ALA A 144 ? 0.55660 0.49840 0.19890 0.08240  -0.07510 -0.10090 144  ALA A CA    
1136 C  C     . ALA A 144 ? 0.56189 0.42700 0.19432 0.12549  -0.02700 -0.09139 144  ALA A C     
1137 O  O     . ALA A 144 ? 0.62980 0.41910 0.20960 0.14280  -0.05290 -0.08540 144  ALA A O     
1138 C  CB    . ALA A 144 ? 0.61550 0.52810 0.20550 0.07600  -0.06170 -0.08760 144  ALA A CB    
1139 N  N     . ASP A 145 ? 0.50018 0.37110 0.18123 0.11298  0.00110  -0.08589 145  ASP A N     
1140 C  CA    . ASP A 145 ? 0.51070 0.35200 0.15890 0.10250  0.02400  -0.04930 145  ASP A CA    
1141 C  C     . ASP A 145 ? 0.52800 0.35260 0.16120 0.15000  -0.00070 -0.03260 145  ASP A C     
1142 O  O     . ASP A 145 ? 0.51840 0.37250 0.18800 0.18990  -0.03640 -0.06340 145  ASP A O     
1143 C  CB    . ASP A 145 ? 0.57350 0.36340 0.16510 0.14020  0.00400  -0.02390 145  ASP A CB    
1144 C  CG    . ASP A 145 ? 0.62530 0.41350 0.19220 0.20040  -0.04390 -0.02170 145  ASP A CG    
1145 O  OD1   . ASP A 145 ? 0.64680 0.37010 0.18930 0.18730  -0.03070 0.00070  145  ASP A OD1   
1146 O  OD2   . ASP A 145 ? 0.66230 0.50080 0.23520 0.20390  -0.05480 -0.03760 145  ASP A OD2   
1147 N  N     . LEU A 146 ? 0.52457 0.34059 0.15564 0.15298  -0.01150 -0.02159 146  LEU A N     
1148 C  CA    . LEU A 146 ? 0.46690 0.30650 0.14720 0.16760  -0.02280 -0.02370 146  LEU A CA    
1149 C  C     . LEU A 146 ? 0.45989 0.27110 0.14561 0.12860  -0.05530 -0.03570 146  LEU A C     
1150 O  O     . LEU A 146 ? 0.54190 0.27370 0.15610 0.14030  -0.03920 -0.02040 146  LEU A O     
1151 C  CB    . LEU A 146 ? 0.45788 0.37089 0.16023 0.16548  -0.00910 -0.04659 146  LEU A CB    
1152 C  CG    . LEU A 146 ? 0.49170 0.36930 0.16040 0.13010  -0.01400 -0.05690 146  LEU A CG    
1153 C  CD1   . LEU A 146 ? 0.49280 0.37050 0.14970 0.10020  -0.03830 -0.04660 146  LEU A CD1   
1154 C  CD2   . LEU A 146 ? 0.46120 0.36440 0.17250 0.17990  -0.00270 -0.04360 146  LEU A CD2   
1155 N  N     . VAL A 147 ? 0.50750 0.31220 0.14790 0.13160  -0.02400 -0.00920 147  VAL A N     
1156 C  CA    . VAL A 147 ? 0.45850 0.31730 0.13710 0.10920  -0.00090 -0.00560 147  VAL A CA    
1157 C  C     . VAL A 147 ? 0.51180 0.28140 0.14400 0.12480  0.01930  -0.00440 147  VAL A C     
1158 O  O     . VAL A 147 ? 0.52900 0.27700 0.15950 0.14590  0.03390  -0.00740 147  VAL A O     
1159 C  CB    . VAL A 147 ? 0.44420 0.34110 0.15340 0.15750  0.00820  0.00220  147  VAL A CB    
1160 C  CG1   . VAL A 147 ? 0.47540 0.32210 0.17130 0.09300  0.01630  -0.01870 147  VAL A CG1   
1161 C  CG2   . VAL A 147 ? 0.49070 0.34880 0.15060 0.15890  0.01100  -0.00980 147  VAL A CG2   
1162 N  N     . SER A 148 ? 0.52570 0.29580 0.16300 0.15010  -0.00010 -0.03330 148  SER A N     
1163 C  CA    . SER A 148 ? 0.47000 0.33590 0.15600 0.12960  0.01300  -0.04680 148  SER A CA    
1164 C  C     . SER A 148 ? 0.48390 0.31270 0.16090 0.10020  -0.01670 -0.05350 148  SER A C     
1165 O  O     . SER A 148 ? 0.56110 0.33770 0.17000 0.11700  -0.01210 -0.03340 148  SER A O     
1166 C  CB    . SER A 148 ? 0.51640 0.39580 0.15530 0.12100  0.01760  -0.03140 148  SER A CB    
1167 O  OG    . SER A 148 ? 0.53240 0.42540 0.16310 0.14880  0.01170  -0.02200 148  SER A OG    
1168 N  N     . GLN A 149 ? 0.48450 0.31940 0.17750 0.14700  -0.03240 -0.06550 149  GLN A N     
1169 C  CA    A GLN A 149 ? 0.46130 0.34600 0.17710 0.12000  -0.03300 -0.05810 149  GLN A CA    
1170 C  CA    B GLN A 149 ? 0.47300 0.37570 0.18130 0.10430  -0.04160 -0.06100 149  GLN A CA    
1171 C  C     . GLN A 149 ? 0.44239 0.32110 0.18881 0.14000  -0.02610 -0.08890 149  GLN A C     
1172 O  O     . GLN A 149 ? 0.48900 0.28780 0.21150 0.11770  -0.01840 -0.09530 149  GLN A O     
1173 C  CB    A GLN A 149 ? 0.45690 0.34200 0.18300 0.13700  -0.04420 -0.05310 149  GLN A CB    
1174 C  CB    B GLN A 149 ? 0.48830 0.41990 0.20180 0.09160  -0.06940 -0.07310 149  GLN A CB    
1175 C  CG    A GLN A 149 ? 0.44650 0.32570 0.17900 0.18450  -0.02240 -0.05840 149  GLN A CG    
1176 C  CG    B GLN A 149 ? 0.49880 0.44190 0.20870 0.12180  -0.07660 -0.10780 149  GLN A CG    
1177 C  CD    A GLN A 149 ? 0.47510 0.32390 0.18180 0.16650  -0.02190 -0.05190 149  GLN A CD    
1178 C  CD    B GLN A 149 ? 0.51140 0.45510 0.22980 0.15620  -0.07500 -0.12230 149  GLN A CD    
1179 O  OE1   A GLN A 149 ? 0.53670 0.30870 0.19770 0.19240  -0.00880 -0.02300 149  GLN A OE1   
1180 O  OE1   B GLN A 149 ? 0.52879 0.41640 0.26341 0.18619  -0.08540 -0.13859 149  GLN A OE1   
1181 N  NE2   A GLN A 149 ? 0.43628 0.28160 0.19871 0.13959  -0.00930 -0.08019 149  GLN A NE2   
1182 N  NE2   B GLN A 149 ? 0.48030 0.47790 0.24080 0.17820  -0.05850 -0.10650 149  GLN A NE2   
1183 N  N     . PHE A 150 ? 0.43100 0.30210 0.18580 0.10590  -0.00790 -0.09490 150  PHE A N     
1184 C  CA    . PHE A 150 ? 0.42628 0.22901 0.18011 0.09339  -0.01850 -0.07689 150  PHE A CA    
1185 C  C     . PHE A 150 ? 0.42080 0.22370 0.15850 0.10660  -0.05580 -0.05610 150  PHE A C     
1186 O  O     . PHE A 150 ? 0.45490 0.18300 0.16210 0.07090  -0.04910 -0.03650 150  PHE A O     
1187 C  CB    . PHE A 150 ? 0.40710 0.27210 0.17510 0.13320  -0.02180 -0.05540 150  PHE A CB    
1188 C  CG    . PHE A 150 ? 0.41680 0.23470 0.16420 0.10360  -0.01150 -0.06570 150  PHE A CG    
1189 C  CD1   . PHE A 150 ? 0.41499 0.20520 0.16031 0.01120  -0.04420 -0.07019 150  PHE A CD1   
1190 C  CD2   . PHE A 150 ? 0.40410 0.27780 0.17050 0.07870  0.01380  -0.08860 150  PHE A CD2   
1191 C  CE1   . PHE A 150 ? 0.41750 0.22930 0.18110 0.01990  -0.05030 -0.07550 150  PHE A CE1   
1192 C  CE2   . PHE A 150 ? 0.40430 0.21960 0.17890 0.06080  -0.01600 -0.07430 150  PHE A CE2   
1193 C  CZ    . PHE A 150 ? 0.45810 0.27950 0.19110 0.06280  -0.04000 -0.06190 150  PHE A CZ    
1194 N  N     . ALA A 151 ? 0.40910 0.25050 0.15710 0.12820  -0.03050 -0.05160 151  ALA A N     
1195 C  CA    . ALA A 151 ? 0.41370 0.18460 0.14310 0.07250  -0.02470 -0.04650 151  ALA A CA    
1196 C  C     . ALA A 151 ? 0.38500 0.23140 0.14920 0.08550  -0.04170 -0.03550 151  ALA A C     
1197 O  O     . ALA A 151 ? 0.42790 0.18870 0.15330 0.05140  -0.04540 -0.05580 151  ALA A O     
1198 C  CB    . ALA A 151 ? 0.44080 0.18990 0.14080 0.10050  0.00810  -0.00960 151  ALA A CB    
1199 N  N     . LEU A 152 ? 0.38870 0.21570 0.14350 0.09700  -0.02920 -0.01180 152  LEU A N     
1200 C  CA    . LEU A 152 ? 0.34910 0.19830 0.15910 0.07260  -0.03130 0.00110  152  LEU A CA    
1201 C  C     . LEU A 152 ? 0.41830 0.18790 0.15150 0.09920  -0.00860 -0.03120 152  LEU A C     
1202 O  O     . LEU A 152 ? 0.40170 0.21040 0.16260 0.06420  -0.02970 -0.04490 152  LEU A O     
1203 C  CB    . LEU A 152 ? 0.34540 0.34430 0.18770 0.02610  -0.01510 -0.01970 152  LEU A CB    
1204 C  CG    . LEU A 152 ? 0.42470 0.46940 0.22640 -0.02930 0.01660  -0.07460 152  LEU A CG    
1205 C  CD1   . LEU A 152 ? 0.46030 0.47850 0.24420 0.02120  -0.00040 -0.05870 152  LEU A CD1   
1206 C  CD2   . LEU A 152 ? 0.57060 0.53530 0.27810 -0.00930 -0.00870 -0.08550 152  LEU A CD2   
1207 N  N     . PRO A 153 ? 0.46170 0.19400 0.15330 0.08600  0.00010  -0.03980 153  PRO A N     
1208 C  CA    . PRO A 153 ? 0.48310 0.19230 0.16910 0.12490  0.00950  -0.01630 153  PRO A CA    
1209 C  C     . PRO A 153 ? 0.43600 0.17710 0.16220 0.11750  -0.03800 -0.03400 153  PRO A C     
1210 O  O     . PRO A 153 ? 0.49210 0.20110 0.14530 0.11100  -0.04650 -0.02400 153  PRO A O     
1211 C  CB    . PRO A 153 ? 0.53280 0.21620 0.18730 0.13170  -0.00720 -0.03550 153  PRO A CB    
1212 C  CG    . PRO A 153 ? 0.54196 0.24192 0.19073 0.14587  -0.03130 -0.04787 153  PRO A CG    
1213 C  CD    . PRO A 153 ? 0.50430 0.23060 0.16880 0.12470  0.01250  -0.03460 153  PRO A CD    
1214 N  N     . VAL A 154 ? 0.41970 0.19100 0.17110 0.09030  -0.03240 -0.05190 154  VAL A N     
1215 C  CA    . VAL A 154 ? 0.39100 0.19420 0.13090 0.01610  -0.03150 -0.05230 154  VAL A CA    
1216 C  C     . VAL A 154 ? 0.40150 0.13040 0.14410 0.04820  -0.03190 -0.02860 154  VAL A C     
1217 O  O     . VAL A 154 ? 0.40800 0.11760 0.17330 0.02140  -0.05240 -0.00990 154  VAL A O     
1218 C  CB    . VAL A 154 ? 0.42440 0.21330 0.15390 0.03390  -0.05450 -0.03930 154  VAL A CB    
1219 C  CG1   . VAL A 154 ? 0.42260 0.17840 0.18610 0.01520  -0.05830 -0.03340 154  VAL A CG1   
1220 C  CG2   . VAL A 154 ? 0.47840 0.18580 0.16830 -0.00510 -0.06490 -0.04500 154  VAL A CG2   
1221 N  N     . PRO A 155 ? 0.39350 0.12180 0.15570 0.04750  -0.03970 -0.01120 155  PRO A N     
1222 C  CA    . PRO A 155 ? 0.35690 0.13330 0.15000 0.06690  -0.04970 -0.03530 155  PRO A CA    
1223 C  C     . PRO A 155 ? 0.35580 0.15690 0.15320 0.05410  -0.02640 -0.05920 155  PRO A C     
1224 O  O     . PRO A 155 ? 0.37490 0.14780 0.13310 0.02600  -0.04070 -0.03680 155  PRO A O     
1225 C  CB    . PRO A 155 ? 0.36670 0.13550 0.13680 0.05200  -0.04790 -0.03860 155  PRO A CB    
1226 C  CG    . PRO A 155 ? 0.34620 0.18470 0.14500 0.01160  -0.06050 -0.06250 155  PRO A CG    
1227 C  CD    . PRO A 155 ? 0.41170 0.14520 0.15800 0.02920  -0.04630 -0.03010 155  PRO A CD    
1228 N  N     . SER A 156 ? 0.31750 0.14080 0.16510 0.06340  -0.02580 -0.02040 156  SER A N     
1229 C  CA    . SER A 156 ? 0.31680 0.15530 0.16490 0.06970  -0.00720 0.01300  156  SER A CA    
1230 C  C     . SER A 156 ? 0.35000 0.12830 0.15810 0.05350  -0.00980 -0.03540 156  SER A C     
1231 O  O     . SER A 156 ? 0.38100 0.17820 0.16220 0.03960  -0.00790 -0.03500 156  SER A O     
1232 C  CB    . SER A 156 ? 0.28730 0.25750 0.18180 0.05800  0.02630  0.02430  156  SER A CB    
1233 O  OG    . SER A 156 ? 0.35940 0.35280 0.21110 0.05770  0.02000  0.05460  156  SER A OG    
1234 N  N     . MET A 157 ? 0.35530 0.11620 0.16600 0.03030  0.00110  -0.04170 157  MET A N     
1235 C  CA    . MET A 157 ? 0.36759 0.10181 0.18740 0.00410  -0.02430 -0.02920 157  MET A CA    
1236 C  C     . MET A 157 ? 0.34600 0.09840 0.16820 0.04550  -0.01530 0.00840  157  MET A C     
1237 O  O     . MET A 157 ? 0.38760 0.15120 0.17890 0.05980  -0.01100 0.01460  157  MET A O     
1238 C  CB    . MET A 157 ? 0.40280 0.11240 0.20410 0.04840  -0.01890 -0.01470 157  MET A CB    
1239 C  CG    . MET A 157 ? 0.45519 0.12921 0.21000 0.05310  -0.03200 -0.02340 157  MET A CG    
1240 S  SD    . MET A 157 ? 0.50499 0.15911 0.20640 0.04440  -0.01430 -0.04659 157  MET A SD    
1241 C  CE    . MET A 157 ? 0.48330 0.23810 0.19250 0.07610  0.05970  -0.03450 157  MET A CE    
1242 N  N     . VAL A 158 ? 0.36270 0.13750 0.16020 0.07290  -0.04450 -0.03960 158  VAL A N     
1243 C  CA    . VAL A 158 ? 0.29260 0.15290 0.15100 0.04630  -0.01280 -0.02610 158  VAL A CA    
1244 C  C     . VAL A 158 ? 0.25930 0.12920 0.15880 -0.01050 -0.00840 -0.02220 158  VAL A C     
1245 O  O     . VAL A 158 ? 0.36430 0.13470 0.14620 0.00330  -0.03550 0.00230  158  VAL A O     
1246 C  CB    . VAL A 158 ? 0.33540 0.16330 0.14990 0.03030  -0.02450 -0.04220 158  VAL A CB    
1247 C  CG1   . VAL A 158 ? 0.33130 0.19190 0.15240 -0.00310 0.01530  -0.03450 158  VAL A CG1   
1248 C  CG2   . VAL A 158 ? 0.37810 0.17770 0.15450 -0.00580 -0.08140 -0.04140 158  VAL A CG2   
1249 N  N     . ILE A 159 ? 0.25880 0.11840 0.17800 -0.00570 -0.02010 -0.03560 159  ILE A N     
1250 C  CA    . ILE A 159 ? 0.26580 0.13390 0.16730 -0.00520 -0.03340 -0.00670 159  ILE A CA    
1251 C  C     . ILE A 159 ? 0.29880 0.18750 0.17570 0.04710  -0.01060 -0.01370 159  ILE A C     
1252 O  O     . ILE A 159 ? 0.31120 0.15050 0.17620 0.01780  -0.02300 -0.00350 159  ILE A O     
1253 C  CB    . ILE A 159 ? 0.31290 0.10800 0.15290 -0.01190 -0.00020 -0.02770 159  ILE A CB    
1254 C  CG1   . ILE A 159 ? 0.33270 0.15220 0.14940 0.04640  -0.01540 -0.02660 159  ILE A CG1   
1255 C  CG2   . ILE A 159 ? 0.30450 0.15870 0.18900 -0.01190 -0.01970 0.00330  159  ILE A CG2   
1256 C  CD1   . ILE A 159 ? 0.39620 0.14510 0.17940 0.02400  0.00270  -0.00670 159  ILE A CD1   
1257 N  N     . CYS A 160 ? 0.26310 0.17170 0.19000 0.06360  0.00860  -0.02130 160  CYS A N     
1258 C  CA    . CYS A 160 ? 0.29810 0.15890 0.20550 0.07240  0.01110  -0.01310 160  CYS A CA    
1259 C  C     . CYS A 160 ? 0.33120 0.12510 0.21620 0.04760  -0.02330 -0.00030 160  CYS A C     
1260 O  O     . CYS A 160 ? 0.33520 0.15660 0.20140 0.05500  -0.04220 0.01300  160  CYS A O     
1261 C  CB    . CYS A 160 ? 0.34230 0.15890 0.22650 0.06630  0.00290  -0.00830 160  CYS A CB    
1262 S  SG    . CYS A 160 ? 0.36090 0.26410 0.22630 0.04130  0.01000  0.01460  160  CYS A SG    
1263 N  N     . ARG A 161 ? 0.37450 0.14450 0.24280 -0.01120 -0.01130 -0.00060 161  ARG A N     
1264 C  CA    . ARG A 161 ? 0.34280 0.16120 0.24010 0.00130  -0.04010 0.00930  161  ARG A CA    
1265 C  C     . ARG A 161 ? 0.35630 0.13680 0.20780 0.03460  -0.03090 0.01050  161  ARG A C     
1266 O  O     . ARG A 161 ? 0.39910 0.16010 0.21970 -0.01180 -0.06860 0.04200  161  ARG A O     
1267 C  CB    . ARG A 161 ? 0.38710 0.27140 0.29310 -0.02840 -0.07410 0.01640  161  ARG A CB    
1268 C  CG    . ARG A 161 ? 0.42850 0.32380 0.35700 0.01840  -0.06190 0.01320  161  ARG A CG    
1269 C  CD    . ARG A 161 ? 0.44550 0.27050 0.40280 0.07380  -0.01850 0.01830  161  ARG A CD    
1270 N  NE    . ARG A 161 ? 0.42980 0.29080 0.42970 -0.00050 -0.01220 0.02610  161  ARG A NE    
1271 C  CZ    . ARG A 161 ? 0.45300 0.29630 0.43410 -0.05200 0.00530  0.02830  161  ARG A CZ    
1272 N  NH1   . ARG A 161 ? 0.44430 0.23350 0.43670 -0.04040 -0.01050 0.02920  161  ARG A NH1   
1273 N  NH2   . ARG A 161 ? 0.44530 0.28280 0.42980 -0.05570 0.02010  0.04040  161  ARG A NH2   
1274 N  N     . LEU A 162 ? 0.31900 0.12400 0.17370 0.02730  -0.03150 -0.02740 162  LEU A N     
1275 C  CA    . LEU A 162 ? 0.29220 0.16170 0.17300 0.06180  -0.03470 -0.00490 162  LEU A CA    
1276 C  C     . LEU A 162 ? 0.28940 0.19880 0.16860 0.03000  -0.03630 0.00690  162  LEU A C     
1277 O  O     . LEU A 162 ? 0.32770 0.17220 0.18030 0.00320  -0.04240 0.02300  162  LEU A O     
1278 C  CB    . LEU A 162 ? 0.30070 0.14280 0.16790 0.07080  -0.01620 -0.00830 162  LEU A CB    
1279 C  CG    . LEU A 162 ? 0.28580 0.14950 0.17540 0.04790  -0.01070 -0.02590 162  LEU A CG    
1280 C  CD1   . LEU A 162 ? 0.28760 0.18590 0.21900 0.04500  -0.01220 0.01620  162  LEU A CD1   
1281 C  CD2   . LEU A 162 ? 0.34510 0.23260 0.14500 0.01370  -0.04350 -0.02970 162  LEU A CD2   
1282 N  N     . LEU A 163 ? 0.29160 0.12970 0.16670 0.01200  -0.02070 -0.00910 163  LEU A N     
1283 C  CA    . LEU A 163 ? 0.33820 0.09110 0.16650 0.01320  -0.03920 0.01430  163  LEU A CA    
1284 C  C     . LEU A 163 ? 0.31460 0.10410 0.16550 -0.00330 -0.05810 -0.00090 163  LEU A C     
1285 O  O     . LEU A 163 ? 0.31170 0.15310 0.16490 0.03030  -0.03660 0.00250  163  LEU A O     
1286 C  CB    . LEU A 163 ? 0.33680 0.11580 0.18420 -0.01230 -0.04850 0.04180  163  LEU A CB    
1287 C  CG    . LEU A 163 ? 0.32050 0.10020 0.16890 0.03060  -0.03240 0.01990  163  LEU A CG    
1288 C  CD1   . LEU A 163 ? 0.31480 0.14450 0.14610 -0.01390 -0.00770 0.05090  163  LEU A CD1   
1289 C  CD2   . LEU A 163 ? 0.40480 0.15340 0.16320 0.03760  -0.02440 -0.03500 163  LEU A CD2   
1290 N  N     . GLY A 164 ? 0.32840 0.10000 0.17240 0.02760  -0.03040 -0.00580 164  GLY A N     
1291 C  CA    . GLY A 164 ? 0.32870 0.12430 0.20330 0.04480  -0.02180 0.01250  164  GLY A CA    
1292 C  C     . GLY A 164 ? 0.32580 0.15170 0.21890 0.07650  -0.01650 0.02400  164  GLY A C     
1293 O  O     . GLY A 164 ? 0.37950 0.16380 0.25870 0.09900  -0.02740 0.01210  164  GLY A O     
1294 N  N     . VAL A 165 ? 0.33420 0.13760 0.20500 0.02180  -0.05130 0.00570  165  VAL A N     
1295 C  CA    . VAL A 165 ? 0.31470 0.18490 0.20660 0.05970  -0.01830 -0.01620 165  VAL A CA    
1296 C  C     . VAL A 165 ? 0.27770 0.17850 0.22150 0.06190  -0.02570 -0.00650 165  VAL A C     
1297 O  O     . VAL A 165 ? 0.35160 0.16150 0.22720 0.04880  -0.02990 -0.00100 165  VAL A O     
1298 C  CB    . VAL A 165 ? 0.34210 0.17350 0.20140 0.02150  0.00010  -0.00430 165  VAL A CB    
1299 C  CG1   . VAL A 165 ? 0.33800 0.22900 0.18120 0.02760  -0.00890 -0.02030 165  VAL A CG1   
1300 C  CG2   . VAL A 165 ? 0.30390 0.18530 0.23120 0.02790  -0.02680 -0.04250 165  VAL A CG2   
1301 N  N     . PRO A 166 ? 0.33690 0.16410 0.22530 0.07430  -0.02170 -0.01440 166  PRO A N     
1302 C  CA    . PRO A 166 ? 0.36710 0.15410 0.22620 0.10020  -0.00460 -0.02490 166  PRO A CA    
1303 C  C     . PRO A 166 ? 0.41210 0.16720 0.22840 0.01080  -0.00700 -0.04120 166  PRO A C     
1304 O  O     . PRO A 166 ? 0.44770 0.17070 0.23910 0.04380  0.01380  -0.04560 166  PRO A O     
1305 C  CB    . PRO A 166 ? 0.40470 0.18230 0.26340 0.05220  0.00880  -0.06310 166  PRO A CB    
1306 C  CG    . PRO A 166 ? 0.38150 0.20940 0.27130 0.08480  -0.04570 -0.05770 166  PRO A CG    
1307 C  CD    . PRO A 166 ? 0.35160 0.16600 0.24530 0.09990  -0.04070 -0.05830 166  PRO A CD    
1308 N  N     . TYR A 167 ? 0.43420 0.17020 0.20340 0.02440  -0.02880 -0.07440 167  TYR A N     
1309 C  CA    . TYR A 167 ? 0.46290 0.25580 0.21840 0.03060  -0.06660 -0.04460 167  TYR A CA    
1310 C  C     . TYR A 167 ? 0.48310 0.25100 0.23460 0.09740  -0.00960 -0.05920 167  TYR A C     
1311 O  O     . TYR A 167 ? 0.53020 0.26910 0.22130 0.01810  -0.00860 -0.06300 167  TYR A O     
1312 C  CB    . TYR A 167 ? 0.44320 0.25580 0.22740 0.08450  -0.04880 -0.02660 167  TYR A CB    
1313 C  CG    . TYR A 167 ? 0.46730 0.25530 0.19310 0.02640  0.01200  -0.01070 167  TYR A CG    
1314 C  CD1   . TYR A 167 ? 0.41980 0.26140 0.19890 0.07140  0.02480  -0.01110 167  TYR A CD1   
1315 C  CD2   . TYR A 167 ? 0.49320 0.26790 0.19940 -0.00560 0.00450  0.01040  167  TYR A CD2   
1316 C  CE1   . TYR A 167 ? 0.45000 0.33950 0.18890 0.04270  0.03800  0.01950  167  TYR A CE1   
1317 C  CE2   . TYR A 167 ? 0.50720 0.27390 0.19910 0.02930  0.00970  0.00370  167  TYR A CE2   
1318 C  CZ    . TYR A 167 ? 0.44830 0.31370 0.20270 0.04710  0.01380  0.00850  167  TYR A CZ    
1319 O  OH    . TYR A 167 ? 0.44970 0.32720 0.22360 0.05100  -0.00800 0.01920  167  TYR A OH    
1320 N  N     . ALA A 168 ? 0.52220 0.20910 0.28410 0.07610  0.05750  -0.06940 168  ALA A N     
1321 C  CA    . ALA A 168 ? 0.56400 0.21870 0.32100 0.10370  0.09040  -0.04840 168  ALA A CA    
1322 C  C     . ALA A 168 ? 0.56040 0.25850 0.32780 0.10510  0.06390  -0.09280 168  ALA A C     
1323 O  O     . ALA A 168 ? 0.58560 0.34260 0.34310 0.10040  0.08000  -0.09200 168  ALA A O     
1324 C  CB    . ALA A 168 ? 0.59980 0.29670 0.33840 0.09840  0.11050  -0.06300 168  ALA A CB    
1325 N  N     . ASP A 169 ? 0.50890 0.21760 0.31090 0.09200  0.04260  -0.07980 169  ASP A N     
1326 C  CA    . ASP A 169 ? 0.53400 0.22620 0.30470 0.09720  0.00630  -0.05790 169  ASP A CA    
1327 C  C     . ASP A 169 ? 0.48140 0.28380 0.25250 0.11850  0.02720  -0.06730 169  ASP A C     
1328 O  O     . ASP A 169 ? 0.44130 0.32500 0.24930 0.07220  0.02440  -0.05370 169  ASP A O     
1329 C  CB    . ASP A 169 ? 0.52380 0.22010 0.33060 0.11280  -0.02480 -0.05270 169  ASP A CB    
1330 C  CG    . ASP A 169 ? 0.55860 0.26070 0.36490 0.13300  -0.00230 -0.06050 169  ASP A CG    
1331 O  OD1   . ASP A 169 ? 0.58780 0.39460 0.40490 0.18530  0.00180  -0.03430 169  ASP A OD1   
1332 O  OD2   . ASP A 169 ? 0.51710 0.27590 0.36100 0.09300  -0.04110 -0.05160 169  ASP A OD2   
1333 N  N     . HIS A 170 ? 0.43870 0.28490 0.22950 0.07020  0.04730  -0.06280 170  HIS A N     
1334 C  CA    . HIS A 170 ? 0.45930 0.26460 0.21660 0.02960  0.05230  -0.08100 170  HIS A CA    
1335 C  C     . HIS A 170 ? 0.40120 0.27810 0.20000 0.05990  0.06030  -0.10100 170  HIS A C     
1336 O  O     . HIS A 170 ? 0.47259 0.24210 0.18991 0.02260  0.06850  -0.07590 170  HIS A O     
1337 C  CB    . HIS A 170 ? 0.47980 0.24170 0.20880 -0.01850 0.05840  -0.07360 170  HIS A CB    
1338 C  CG    . HIS A 170 ? 0.53780 0.27210 0.21220 0.10100  0.02350  -0.07770 170  HIS A CG    
1339 N  ND1   . HIS A 170 ? 0.54220 0.29600 0.21590 0.08030  0.02310  -0.06860 170  HIS A ND1   
1340 C  CD2   . HIS A 170 ? 0.55880 0.31890 0.23250 0.06260  0.00670  -0.05500 170  HIS A CD2   
1341 C  CE1   . HIS A 170 ? 0.60180 0.32670 0.22510 0.09360  -0.02280 -0.07590 170  HIS A CE1   
1342 N  NE2   . HIS A 170 ? 0.58360 0.31150 0.21990 0.08800  -0.02980 -0.06980 170  HIS A NE2   
1343 N  N     . GLU A 171 ? 0.45080 0.32820 0.21700 0.05720  0.05750  -0.07660 171  GLU A N     
1344 C  CA    . GLU A 171 ? 0.47530 0.40530 0.24060 0.03210  0.08380  -0.08910 171  GLU A CA    
1345 C  C     . GLU A 171 ? 0.46300 0.39110 0.24600 0.03130  0.07260  -0.05220 171  GLU A C     
1346 O  O     . GLU A 171 ? 0.46420 0.38900 0.25790 0.01580  0.05900  -0.04560 171  GLU A O     
1347 C  CB    . GLU A 171 ? 0.53060 0.47120 0.25040 0.05180  0.06540  -0.12930 171  GLU A CB    
1348 C  CG    . GLU A 171 ? 0.65600 0.56600 0.27040 0.09450  0.06120  -0.16210 171  GLU A CG    
1349 C  CD    . GLU A 171 ? 0.77050 0.68720 0.30220 0.13330  0.08500  -0.15580 171  GLU A CD    
1350 O  OE1   . GLU A 171 ? 0.82550 0.71680 0.33440 0.15210  0.11460  -0.15800 171  GLU A OE1   
1351 O  OE2   . GLU A 171 ? 0.81320 0.74170 0.30670 0.14320  0.05550  -0.12350 171  GLU A OE2   
1352 N  N     . PHE A 172 ? 0.40640 0.36060 0.24720 0.04860  0.05910  -0.07550 172  PHE A N     
1353 C  CA    . PHE A 172 ? 0.37130 0.33280 0.23720 0.05260  0.04550  -0.06670 172  PHE A CA    
1354 C  C     . PHE A 172 ? 0.38180 0.30690 0.21570 0.06160  0.05410  -0.04240 172  PHE A C     
1355 O  O     . PHE A 172 ? 0.38880 0.30140 0.22680 0.03160  0.02890  -0.03000 172  PHE A O     
1356 C  CB    . PHE A 172 ? 0.39330 0.34270 0.24610 0.11360  0.01680  -0.04030 172  PHE A CB    
1357 C  CG    . PHE A 172 ? 0.40850 0.38670 0.26770 0.10800  -0.00870 -0.06710 172  PHE A CG    
1358 C  CD1   . PHE A 172 ? 0.52430 0.43210 0.28700 0.05720  -0.03230 -0.06400 172  PHE A CD1   
1359 C  CD2   . PHE A 172 ? 0.47610 0.39770 0.26040 0.16340  -0.04130 -0.10700 172  PHE A CD2   
1360 C  CE1   . PHE A 172 ? 0.53950 0.45090 0.28830 0.07020  -0.07100 -0.06130 172  PHE A CE1   
1361 C  CE2   . PHE A 172 ? 0.52750 0.44220 0.28520 0.13840  -0.03130 -0.07680 172  PHE A CE2   
1362 C  CZ    . PHE A 172 ? 0.52280 0.46220 0.30270 0.06060  -0.03720 -0.05790 172  PHE A CZ    
1363 N  N     . PHE A 173 ? 0.38860 0.26860 0.20530 0.00840  0.02800  -0.03080 173  PHE A N     
1364 C  CA    . PHE A 173 ? 0.35560 0.23850 0.17750 0.03950  0.06320  -0.04170 173  PHE A CA    
1365 C  C     . PHE A 173 ? 0.35880 0.22890 0.17000 0.07260  0.05030  -0.03340 173  PHE A C     
1366 O  O     . PHE A 173 ? 0.37130 0.22490 0.18900 0.05360  0.05260  -0.01130 173  PHE A O     
1367 C  CB    . PHE A 173 ? 0.37160 0.24240 0.18290 -0.02480 0.05580  -0.04540 173  PHE A CB    
1368 C  CG    . PHE A 173 ? 0.40080 0.20460 0.20090 0.03240  0.05270  -0.02810 173  PHE A CG    
1369 C  CD1   . PHE A 173 ? 0.42070 0.24170 0.19220 0.00610  0.06550  -0.04420 173  PHE A CD1   
1370 C  CD2   . PHE A 173 ? 0.42950 0.23780 0.21870 0.05160  0.05570  -0.02520 173  PHE A CD2   
1371 C  CE1   . PHE A 173 ? 0.44010 0.24020 0.18140 -0.03560 0.06950  -0.04630 173  PHE A CE1   
1372 C  CE2   . PHE A 173 ? 0.41120 0.24540 0.22540 0.06320  0.05690  -0.01820 173  PHE A CE2   
1373 C  CZ    . PHE A 173 ? 0.43900 0.29010 0.20510 0.01850  0.07530  -0.01380 173  PHE A CZ    
1374 N  N     . GLN A 174 ? 0.35550 0.27600 0.16490 0.04190  0.02610  -0.00230 174  GLN A N     
1375 C  CA    . GLN A 174 ? 0.35490 0.28680 0.17220 0.04060  0.01290  -0.00770 174  GLN A CA    
1376 C  C     . GLN A 174 ? 0.36570 0.28150 0.19270 0.05970  0.05540  -0.01730 174  GLN A C     
1377 O  O     . GLN A 174 ? 0.46070 0.25270 0.19310 0.04040  0.03290  -0.02700 174  GLN A O     
1378 C  CB    . GLN A 174 ? 0.37670 0.30320 0.17700 -0.01330 0.00590  -0.03660 174  GLN A CB    
1379 C  CG    . GLN A 174 ? 0.34990 0.27290 0.17600 -0.00080 0.04360  -0.04050 174  GLN A CG    
1380 C  CD    . GLN A 174 ? 0.39720 0.36440 0.19910 0.02440  0.01670  -0.00850 174  GLN A CD    
1381 O  OE1   . GLN A 174 ? 0.41960 0.35650 0.20500 -0.02040 0.03110  -0.06790 174  GLN A OE1   
1382 N  NE2   . GLN A 174 ? 0.39380 0.28960 0.23050 0.11270  0.01510  0.01530  174  GLN A NE2   
1383 N  N     . ASP A 175 ? 0.34160 0.32270 0.18430 -0.00290 0.05350  -0.02550 175  ASP A N     
1384 C  CA    . ASP A 175 ? 0.39430 0.37740 0.19780 0.04690  0.05170  0.00250  175  ASP A CA    
1385 C  C     . ASP A 175 ? 0.41640 0.33300 0.20240 -0.00480 0.03180  0.02490  175  ASP A C     
1386 O  O     . ASP A 175 ? 0.44510 0.34140 0.21610 0.02250  0.04600  0.02190  175  ASP A O     
1387 C  CB    . ASP A 175 ? 0.41060 0.41320 0.21350 0.06010  0.07920  -0.01900 175  ASP A CB    
1388 C  CG    . ASP A 175 ? 0.48750 0.47350 0.23210 0.02360  0.11300  -0.01870 175  ASP A CG    
1389 O  OD1   . ASP A 175 ? 0.60550 0.51860 0.25460 -0.05320 0.12050  -0.01460 175  ASP A OD1   
1390 O  OD2   . ASP A 175 ? 0.50380 0.49300 0.25640 0.01690  0.08940  -0.03750 175  ASP A OD2   
1391 N  N     . ALA A 176 ? 0.36450 0.29080 0.20120 0.03760  0.03570  0.00770  176  ALA A N     
1392 C  CA    . ALA A 176 ? 0.34120 0.28900 0.23130 0.06530  0.02060  0.00230  176  ALA A CA    
1393 C  C     . ALA A 176 ? 0.35230 0.25550 0.23310 0.04000  0.04710  -0.00100 176  ALA A C     
1394 O  O     . ALA A 176 ? 0.39610 0.22000 0.25660 0.02750  0.05710  0.02720  176  ALA A O     
1395 C  CB    . ALA A 176 ? 0.34530 0.24550 0.24900 0.04430  0.01790  0.00930  176  ALA A CB    
1396 N  N     . SER A 177 ? 0.36140 0.22530 0.23520 0.07650  0.04780  0.01100  177  SER A N     
1397 C  CA    . SER A 177 ? 0.39570 0.21570 0.24500 0.07680  0.04630  0.01850  177  SER A CA    
1398 C  C     . SER A 177 ? 0.43750 0.25630 0.24650 -0.00370 0.05400  0.04210  177  SER A C     
1399 O  O     . SER A 177 ? 0.43980 0.24560 0.24740 0.01720  0.05390  0.03850  177  SER A O     
1400 C  CB    . SER A 177 ? 0.40960 0.18670 0.25140 0.05830  0.06190  -0.00970 177  SER A CB    
1401 O  OG    . SER A 177 ? 0.44690 0.20220 0.24020 0.04100  0.03820  -0.02410 177  SER A OG    
1402 N  N     . LYS A 178 ? 0.42780 0.27070 0.22560 0.03190  0.02650  0.07310  178  LYS A N     
1403 C  CA    . LYS A 178 ? 0.46630 0.31630 0.22750 0.00040  0.02180  0.11090  178  LYS A CA    
1404 C  C     . LYS A 178 ? 0.42740 0.30630 0.26960 0.03550  0.00670  0.11250  178  LYS A C     
1405 O  O     . LYS A 178 ? 0.47540 0.31090 0.27010 0.02550  -0.00410 0.10680  178  LYS A O     
1406 C  CB    . LYS A 178 ? 0.48460 0.41700 0.19610 0.02040  0.00600  0.07880  178  LYS A CB    
1407 C  CG    . LYS A 178 ? 0.52630 0.51050 0.21490 0.00380  -0.00100 0.04690  178  LYS A CG    
1408 C  CD    . LYS A 178 ? 0.59790 0.62050 0.22130 -0.02740 0.00290  0.00610  178  LYS A CD    
1409 C  CE    . LYS A 178 ? 0.67060 0.76800 0.25040 0.01530  0.02290  0.03390  178  LYS A CE    
1410 N  NZ    . LYS A 178 ? 0.68980 0.84710 0.25830 0.03350  0.01370  0.03650  178  LYS A NZ    
1411 N  N     . ARG A 179 ? 0.33230 0.33830 0.28550 0.02650  0.02580  0.08440  179  ARG A N     
1412 C  CA    . ARG A 179 ? 0.37060 0.29940 0.31520 0.03260  0.06290  0.05930  179  ARG A CA    
1413 C  C     . ARG A 179 ? 0.43510 0.30580 0.35330 0.05380  0.08410  0.09640  179  ARG A C     
1414 O  O     . ARG A 179 ? 0.50550 0.30510 0.38650 0.07300  0.09060  0.11160  179  ARG A O     
1415 C  CB    . ARG A 179 ? 0.39790 0.34860 0.31880 0.08840  0.08240  0.00920  179  ARG A CB    
1416 C  CG    . ARG A 179 ? 0.44310 0.36620 0.32880 0.09440  0.09430  0.01100  179  ARG A CG    
1417 C  CD    . ARG A 179 ? 0.43120 0.36890 0.32980 0.10540  0.10680  0.01960  179  ARG A CD    
1418 N  NE    . ARG A 179 ? 0.51200 0.45390 0.33970 0.11360  0.12890  0.00790  179  ARG A NE    
1419 C  CZ    . ARG A 179 ? 0.49790 0.45520 0.33080 0.11720  0.16970  0.08340  179  ARG A CZ    
1420 N  NH1   . ARG A 179 ? 0.51620 0.49690 0.32550 0.10100  0.17740  0.10220  179  ARG A NH1   
1421 N  NH2   . ARG A 179 ? 0.47120 0.45270 0.35380 0.15410  0.14970  0.07520  179  ARG A NH2   
1422 N  N     . LEU A 180 ? 0.40570 0.27690 0.34380 0.05320  0.06940  0.09070  180  LEU A N     
1423 C  CA    . LEU A 180 ? 0.43030 0.24130 0.35260 0.04630  0.05390  0.08530  180  LEU A CA    
1424 C  C     . LEU A 180 ? 0.39870 0.23050 0.37250 0.00210  0.03930  0.05090  180  LEU A C     
1425 O  O     . LEU A 180 ? 0.40930 0.25440 0.37650 0.02700  0.05060  0.02350  180  LEU A O     
1426 C  CB    . LEU A 180 ? 0.41020 0.19690 0.34820 0.03710  0.07700  0.06150  180  LEU A CB    
1427 C  CG    . LEU A 180 ? 0.51130 0.21230 0.37180 -0.01590 0.05680  0.04600  180  LEU A CG    
1428 C  CD1   . LEU A 180 ? 0.55480 0.29230 0.39850 -0.04340 0.06170  0.05640  180  LEU A CD1   
1429 C  CD2   . LEU A 180 ? 0.60570 0.23480 0.36040 -0.03260 0.06940  0.04910  180  LEU A CD2   
1430 N  N     . VAL A 181 ? 0.35130 0.23540 0.37210 -0.00790 -0.00150 0.08260  181  VAL A N     
1431 C  CA    . VAL A 181 ? 0.36540 0.18130 0.35330 0.04020  0.01160  0.05940  181  VAL A CA    
1432 C  C     . VAL A 181 ? 0.43930 0.32130 0.33390 0.03610  0.00370  0.09400  181  VAL A C     
1433 O  O     . VAL A 181 ? 0.44980 0.37260 0.32510 0.09390  0.00620  0.09880  181  VAL A O     
1434 C  CB    . VAL A 181 ? 0.48400 0.26420 0.35610 -0.06810 0.02420  0.06250  181  VAL A CB    
1435 C  CG1   . VAL A 181 ? 0.49970 0.30570 0.35420 -0.08770 0.02310  0.10170  181  VAL A CG1   
1436 C  CG2   . VAL A 181 ? 0.55020 0.35030 0.37880 -0.07160 -0.01530 0.05300  181  VAL A CG2   
1437 N  N     . GLN A 182 ? 0.46530 0.24860 0.33410 0.05150  0.06780  0.05920  182  GLN A N     
1438 C  CA    . GLN A 182 ? 0.52390 0.29230 0.33790 -0.00240 0.03150  0.07090  182  GLN A CA    
1439 C  C     . GLN A 182 ? 0.52870 0.31890 0.37300 -0.02220 0.02280  0.11490  182  GLN A C     
1440 O  O     . GLN A 182 ? 0.54440 0.35090 0.37850 -0.01620 0.01690  0.12680  182  GLN A O     
1441 C  CB    . GLN A 182 ? 0.53740 0.32920 0.30640 -0.00140 0.03140  0.04440  182  GLN A CB    
1442 C  CG    . GLN A 182 ? 0.52430 0.35640 0.27700 0.01170  0.03130  0.03250  182  GLN A CG    
1443 C  CD    . GLN A 182 ? 0.57570 0.48690 0.26690 -0.00340 0.01190  0.05940  182  GLN A CD    
1444 O  OE1   . GLN A 182 ? 0.62290 0.50970 0.24030 0.01020  0.05610  0.07000  182  GLN A OE1   
1445 N  NE2   . GLN A 182 ? 0.56720 0.56000 0.27440 -0.02430 -0.01280 0.06890  182  GLN A NE2   
1446 N  N     . SER A 183 ? 0.45130 0.31920 0.40170 -0.02020 -0.00510 0.13280  183  SER A N     
1447 C  CA    . SER A 183 ? 0.43250 0.34970 0.43060 -0.04450 0.03350  0.17520  183  SER A CA    
1448 C  C     . SER A 183 ? 0.44350 0.33540 0.45900 -0.04440 0.06100  0.16820  183  SER A C     
1449 O  O     . SER A 183 ? 0.45820 0.27480 0.48250 -0.02610 0.08340  0.15560  183  SER A O     
1450 C  CB    . SER A 183 ? 0.44270 0.42970 0.43000 -0.03820 0.02010  0.17240  183  SER A CB    
1451 O  OG    . SER A 183 ? 0.49850 0.43470 0.44550 -0.04500 -0.00810 0.17690  183  SER A OG    
1452 N  N     . THR A 184 ? 0.49220 0.41800 0.45480 -0.05370 0.07620  0.16750  184  THR A N     
1453 C  CA    . THR A 184 ? 0.50590 0.41480 0.45450 -0.07250 0.06040  0.21140  184  THR A CA    
1454 C  C     . THR A 184 ? 0.50060 0.44590 0.47090 -0.02520 0.05660  0.22740  184  THR A C     
1455 O  O     . THR A 184 ? 0.52140 0.46470 0.45820 -0.02330 0.04650  0.19670  184  THR A O     
1456 C  CB    . THR A 184 ? 0.52390 0.50580 0.45850 -0.10700 0.03050  0.16940  184  THR A CB    
1457 O  OG1   . THR A 184 ? 0.53810 0.53520 0.46010 -0.06770 0.03860  0.14580  184  THR A OG1   
1458 C  CG2   . THR A 184 ? 0.54810 0.51120 0.46170 -0.09880 0.00240  0.15720  184  THR A CG2   
1459 N  N     . ASP A 185 ? 0.46060 0.42690 0.49990 0.02430  0.03430  0.23570  185  ASP A N     
1460 C  CA    . ASP A 185 ? 0.44310 0.42470 0.52160 0.04050  0.04180  0.22930  185  ASP A CA    
1461 C  C     . ASP A 185 ? 0.45600 0.40600 0.52890 -0.01630 0.03490  0.20710  185  ASP A C     
1462 O  O     . ASP A 185 ? 0.47760 0.38790 0.52360 -0.01510 0.04040  0.21920  185  ASP A O     
1463 C  CB    . ASP A 185 ? 0.48920 0.48850 0.53100 0.06090  0.05340  0.21740  185  ASP A CB    
1464 C  CG    . ASP A 185 ? 0.55640 0.56740 0.54120 0.10210  0.05880  0.19480  185  ASP A CG    
1465 O  OD1   . ASP A 185 ? 0.59890 0.64370 0.54990 0.07750  0.05990  0.16710  185  ASP A OD1   
1466 O  OD2   . ASP A 185 ? 0.58770 0.52250 0.53760 0.15850  0.07380  0.23550  185  ASP A OD2   
1467 N  N     . ALA A 186 ? 0.44550 0.34570 0.52590 0.01340  0.01850  0.17910  186  ALA A N     
1468 C  CA    . ALA A 186 ? 0.41770 0.33390 0.52810 0.00850  0.04770  0.13590  186  ALA A CA    
1469 C  C     . ALA A 186 ? 0.39200 0.36070 0.51800 0.04730  0.07360  0.15190  186  ALA A C     
1470 O  O     . ALA A 186 ? 0.40340 0.35710 0.51670 0.01970  0.06830  0.16370  186  ALA A O     
1471 C  CB    . ALA A 186 ? 0.42840 0.33450 0.53720 -0.00350 0.03720  0.10130  186  ALA A CB    
1472 N  N     . GLN A 187 ? 0.39680 0.39430 0.50240 0.04060  0.10160  0.16860  187  GLN A N     
1473 C  CA    . GLN A 187 ? 0.42160 0.41950 0.50750 0.01360  0.09030  0.18360  187  GLN A CA    
1474 C  C     . GLN A 187 ? 0.39670 0.39840 0.47190 -0.00490 0.07520  0.17960  187  GLN A C     
1475 O  O     . GLN A 187 ? 0.43900 0.38020 0.47550 0.00720  0.07730  0.14870  187  GLN A O     
1476 C  CB    . GLN A 187 ? 0.47680 0.52120 0.55680 0.04530  0.08600  0.18440  187  GLN A CB    
1477 C  CG    . GLN A 187 ? 0.64940 0.64290 0.60480 0.06630  0.03560  0.18750  187  GLN A CG    
1478 C  CD    . GLN A 187 ? 0.75170 0.75070 0.64670 0.07760  0.01180  0.17070  187  GLN A CD    
1479 O  OE1   . GLN A 187 ? 0.82040 0.79380 0.66400 -0.00170 0.00630  0.16770  187  GLN A OE1   
1480 N  NE2   . GLN A 187 ? 0.73160 0.73920 0.65730 0.17750  -0.00140 0.16980  187  GLN A NE2   
1481 N  N     . SER A 188 ? 0.38600 0.41870 0.43740 0.00280  0.06020  0.17900  188  SER A N     
1482 C  CA    A SER A 188 ? 0.37890 0.40620 0.42660 0.00630  0.06310  0.17250  188  SER A CA    
1483 C  CA    B SER A 188 ? 0.39500 0.43290 0.42200 -0.03390 0.04710  0.19250  188  SER A CA    
1484 C  C     . SER A 188 ? 0.38310 0.38020 0.41600 0.00470  0.08100  0.15810  188  SER A C     
1485 O  O     . SER A 188 ? 0.39620 0.32740 0.41420 0.01980  0.10990  0.13690  188  SER A O     
1486 C  CB    A SER A 188 ? 0.37740 0.40150 0.42410 0.05480  0.05840  0.18060  188  SER A CB    
1487 C  CB    B SER A 188 ? 0.42070 0.45280 0.41090 -0.02270 0.01690  0.24630  188  SER A CB    
1488 O  OG    A SER A 188 ? 0.40950 0.40990 0.42660 0.07090  0.05510  0.16510  188  SER A OG    
1489 O  OG    B SER A 188 ? 0.46270 0.48180 0.41370 -0.07460 0.00270  0.24840  188  SER A OG    
1490 N  N     . ALA A 189 ? 0.35240 0.31990 0.40120 0.00840  0.08670  0.12940  189  ALA A N     
1491 C  CA    . ALA A 189 ? 0.34870 0.35600 0.38870 0.06670  0.07630  0.11520  189  ALA A CA    
1492 C  C     . ALA A 189 ? 0.37070 0.31180 0.36360 0.03670  0.06270  0.08540  189  ALA A C     
1493 O  O     . ALA A 189 ? 0.40110 0.30750 0.35090 0.04170  0.06850  0.05350  189  ALA A O     
1494 C  CB    . ALA A 189 ? 0.40850 0.37000 0.40790 0.12240  0.05240  0.09970  189  ALA A CB    
1495 N  N     . LEU A 190 ? 0.35190 0.28930 0.35940 0.02100  0.05380  0.07850  190  LEU A N     
1496 C  CA    . LEU A 190 ? 0.36850 0.29500 0.36370 0.03350  0.00950  0.07280  190  LEU A CA    
1497 C  C     . LEU A 190 ? 0.36880 0.26210 0.35570 0.03490  0.05430  0.05800  190  LEU A C     
1498 O  O     . LEU A 190 ? 0.39690 0.28140 0.36500 -0.01060 0.05400  0.06180  190  LEU A O     
1499 C  CB    . LEU A 190 ? 0.45430 0.31090 0.36610 -0.05100 -0.04580 0.10520  190  LEU A CB    
1500 C  CG    . LEU A 190 ? 0.62590 0.35830 0.38720 -0.15760 -0.05300 0.08010  190  LEU A CG    
1501 C  CD1   . LEU A 190 ? 0.68980 0.40330 0.39230 -0.20230 -0.04300 0.04620  190  LEU A CD1   
1502 C  CD2   . LEU A 190 ? 0.68750 0.45540 0.40430 -0.15140 -0.07410 0.05300  190  LEU A CD2   
1503 N  N     . THR A 191 ? 0.39840 0.29540 0.34770 0.04800  0.08760  0.03080  191  THR A N     
1504 C  CA    . THR A 191 ? 0.37980 0.27600 0.35490 0.02790  0.09500  0.05110  191  THR A CA    
1505 C  C     . THR A 191 ? 0.40020 0.30380 0.33320 0.03570  0.06030  0.04430  191  THR A C     
1506 O  O     . THR A 191 ? 0.36370 0.32570 0.34970 0.04290  0.07010  0.03820  191  THR A O     
1507 C  CB    . THR A 191 ? 0.40440 0.34290 0.38700 -0.03520 0.13760  0.04610  191  THR A CB    
1508 O  OG1   . THR A 191 ? 0.39070 0.43650 0.42580 -0.02840 0.10880  0.02970  191  THR A OG1   
1509 C  CG2   . THR A 191 ? 0.44230 0.36000 0.38370 -0.01840 0.13200  0.00970  191  THR A CG2   
1510 N  N     . ALA A 192 ? 0.36420 0.32220 0.30450 0.01310  0.05990  0.05140  192  ALA A N     
1511 C  CA    . ALA A 192 ? 0.35580 0.29290 0.28700 -0.01980 0.04790  0.04300  192  ALA A CA    
1512 C  C     . ALA A 192 ? 0.32720 0.25970 0.29080 0.03090  0.05470  0.03750  192  ALA A C     
1513 O  O     . ALA A 192 ? 0.37110 0.24550 0.29630 0.01740  0.06570  0.02210  192  ALA A O     
1514 C  CB    . ALA A 192 ? 0.39490 0.28470 0.28130 0.00610  0.03930  0.02770  192  ALA A CB    
1515 N  N     . ARG A 193 ? 0.34540 0.26820 0.29150 0.02070  0.06140  0.02090  193  ARG A N     
1516 C  CA    . ARG A 193 ? 0.38410 0.24690 0.27370 0.02010  0.04720  0.00940  193  ARG A CA    
1517 C  C     . ARG A 193 ? 0.33060 0.27310 0.27980 0.00400  0.00980  0.02270  193  ARG A C     
1518 O  O     . ARG A 193 ? 0.33990 0.34710 0.26340 0.02920  0.03080  0.02200  193  ARG A O     
1519 C  CB    . ARG A 193 ? 0.39290 0.31180 0.25650 0.01580  0.04910  -0.01260 193  ARG A CB    
1520 C  CG    . ARG A 193 ? 0.45240 0.36350 0.24590 -0.00020 0.08410  -0.01430 193  ARG A CG    
1521 C  CD    . ARG A 193 ? 0.56030 0.46470 0.26280 -0.03060 0.04290  0.06490  193  ARG A CD    
1522 N  NE    . ARG A 193 ? 0.67310 0.51360 0.28480 -0.12960 0.02780  0.10250  193  ARG A NE    
1523 C  CZ    . ARG A 193 ? 0.82900 0.54790 0.29600 -0.19300 -0.04300 0.02690  193  ARG A CZ    
1524 N  NH1   . ARG A 193 ? 0.90750 0.50090 0.30810 -0.18630 -0.08460 -0.01800 193  ARG A NH1   
1525 N  NH2   . ARG A 193 ? 0.85330 0.54420 0.29730 -0.29590 -0.03840 0.01130  193  ARG A NH2   
1526 N  N     . ASN A 194 ? 0.37300 0.22390 0.31010 0.02540  0.04310  0.02280  194  ASN A N     
1527 C  CA    . ASN A 194 ? 0.33500 0.27020 0.35180 0.02080  0.03010  0.03330  194  ASN A CA    
1528 C  C     . ASN A 194 ? 0.33480 0.31780 0.34300 0.02690  0.04330  0.01690  194  ASN A C     
1529 O  O     . ASN A 194 ? 0.32540 0.34390 0.36060 0.07670  0.03300  0.02480  194  ASN A O     
1530 C  CB    . ASN A 194 ? 0.39500 0.33360 0.39320 -0.00350 -0.01310 0.03330  194  ASN A CB    
1531 C  CG    . ASN A 194 ? 0.52390 0.39180 0.42310 -0.07560 -0.04280 0.06350  194  ASN A CG    
1532 O  OD1   . ASN A 194 ? 0.64370 0.43570 0.42830 -0.11220 -0.06760 0.07290  194  ASN A OD1   
1533 N  ND2   . ASN A 194 ? 0.59450 0.39640 0.43690 -0.05910 -0.07150 0.06880  194  ASN A ND2   
1534 N  N     . ASP A 195 ? 0.34030 0.32200 0.31530 0.00510  0.05100  -0.00450 195  ASP A N     
1535 C  CA    . ASP A 195 ? 0.38050 0.28060 0.30270 -0.00950 0.02470  -0.00290 195  ASP A CA    
1536 C  C     . ASP A 195 ? 0.34710 0.26970 0.29020 0.01740  0.01560  -0.01060 195  ASP A C     
1537 O  O     . ASP A 195 ? 0.40940 0.27150 0.28970 0.06400  0.04280  -0.00160 195  ASP A O     
1538 C  CB    . ASP A 195 ? 0.42520 0.31800 0.31120 0.03470  0.07850  -0.01570 195  ASP A CB    
1539 C  CG    . ASP A 195 ? 0.49810 0.37240 0.32030 0.07450  0.07440  0.01630  195  ASP A CG    
1540 O  OD1   . ASP A 195 ? 0.49250 0.40860 0.33770 0.06670  0.08180  0.04790  195  ASP A OD1   
1541 O  OD2   . ASP A 195 ? 0.52040 0.39430 0.32250 0.05940  0.07600  0.01970  195  ASP A OD2   
1542 N  N     . LEU A 196 ? 0.31910 0.26290 0.28950 0.04390  0.00800  -0.01650 196  LEU A N     
1543 C  CA    . LEU A 196 ? 0.33440 0.27350 0.30510 0.03200  -0.00670 0.01300  196  LEU A CA    
1544 C  C     . LEU A 196 ? 0.30900 0.21150 0.27160 0.02780  0.01600  0.00710  196  LEU A C     
1545 O  O     . LEU A 196 ? 0.35690 0.22320 0.26380 0.02680  0.05540  -0.00600 196  LEU A O     
1546 C  CB    . LEU A 196 ? 0.35110 0.28010 0.32660 0.05920  0.01200  -0.00150 196  LEU A CB    
1547 C  CG    . LEU A 196 ? 0.44110 0.29970 0.32990 0.07670  0.00380  -0.04200 196  LEU A CG    
1548 C  CD1   . LEU A 196 ? 0.43220 0.33030 0.33510 0.15560  -0.00550 -0.04240 196  LEU A CD1   
1549 C  CD2   . LEU A 196 ? 0.45460 0.34450 0.31320 0.05390  0.00460  -0.08910 196  LEU A CD2   
1550 N  N     . ALA A 197 ? 0.29590 0.22070 0.26450 0.04670  0.03780  -0.00990 197  ALA A N     
1551 C  CA    . ALA A 197 ? 0.30710 0.20090 0.27880 0.03490  0.03220  0.01090  197  ALA A CA    
1552 C  C     . ALA A 197 ? 0.31340 0.20210 0.30970 0.02350  0.04750  -0.00670 197  ALA A C     
1553 O  O     . ALA A 197 ? 0.37430 0.20350 0.32370 0.02810  0.02820  0.00850  197  ALA A O     
1554 C  CB    . ALA A 197 ? 0.36340 0.17060 0.26090 -0.03670 -0.00060 -0.00180 197  ALA A CB    
1555 N  N     . GLY A 198 ? 0.31480 0.25510 0.33440 0.04410  0.04230  -0.00980 198  GLY A N     
1556 C  CA    . GLY A 198 ? 0.32490 0.23320 0.36870 0.02460  0.05090  -0.03270 198  GLY A CA    
1557 C  C     . GLY A 198 ? 0.29550 0.23000 0.37220 0.04970  0.02730  -0.03330 198  GLY A C     
1558 O  O     . GLY A 198 ? 0.33870 0.24010 0.40380 0.05600  0.03590  -0.02380 198  GLY A O     
1559 N  N     . TYR A 199 ? 0.31780 0.26400 0.36510 0.04260  0.04600  -0.02430 199  TYR A N     
1560 C  CA    . TYR A 199 ? 0.29690 0.25160 0.34890 0.01980  0.01560  -0.04420 199  TYR A CA    
1561 C  C     . TYR A 199 ? 0.29080 0.17770 0.35830 0.01830  0.02710  -0.02550 199  TYR A C     
1562 O  O     . TYR A 199 ? 0.36570 0.19820 0.36970 0.04040  0.03240  -0.03750 199  TYR A O     
1563 C  CB    . TYR A 199 ? 0.30920 0.29890 0.34780 0.03230  0.02470  -0.03950 199  TYR A CB    
1564 C  CG    . TYR A 199 ? 0.30590 0.22820 0.33290 0.02040  0.06500  -0.07190 199  TYR A CG    
1565 C  CD1   . TYR A 199 ? 0.34720 0.28650 0.34160 0.03050  0.05110  -0.06170 199  TYR A CD1   
1566 C  CD2   . TYR A 199 ? 0.31460 0.24650 0.32510 0.01300  0.05660  -0.05590 199  TYR A CD2   
1567 C  CE1   . TYR A 199 ? 0.36420 0.30100 0.33560 -0.02040 0.03890  -0.03900 199  TYR A CE1   
1568 C  CE2   . TYR A 199 ? 0.36640 0.26270 0.32600 -0.02300 0.03720  -0.06310 199  TYR A CE2   
1569 C  CZ    . TYR A 199 ? 0.37680 0.27650 0.32880 0.00370  0.04310  -0.04130 199  TYR A CZ    
1570 O  OH    . TYR A 199 ? 0.41560 0.29390 0.32970 -0.04460 0.01810  0.00470  199  TYR A OH    
1571 N  N     . LEU A 200 ? 0.30620 0.21000 0.34700 0.01880  0.04090  -0.03300 200  LEU A N     
1572 C  CA    . LEU A 200 ? 0.27400 0.20820 0.33760 0.09340  0.01250  -0.03030 200  LEU A CA    
1573 C  C     . LEU A 200 ? 0.31460 0.20390 0.35460 0.07700  -0.00210 -0.03990 200  LEU A C     
1574 O  O     . LEU A 200 ? 0.28530 0.22030 0.35070 0.03780  -0.00750 0.00390  200  LEU A O     
1575 C  CB    . LEU A 200 ? 0.27310 0.18290 0.32370 0.06440  -0.02400 -0.00280 200  LEU A CB    
1576 C  CG    . LEU A 200 ? 0.31280 0.21180 0.32320 0.00860  -0.01920 -0.00360 200  LEU A CG    
1577 C  CD1   . LEU A 200 ? 0.31260 0.15610 0.30600 0.04040  0.00140  0.00240  200  LEU A CD1   
1578 C  CD2   . LEU A 200 ? 0.30220 0.19850 0.33810 -0.02390 -0.01520 -0.00570 200  LEU A CD2   
1579 N  N     . ASP A 201 ? 0.30030 0.24740 0.37990 0.05470  -0.02600 -0.03870 201  ASP A N     
1580 C  CA    . ASP A 201 ? 0.29420 0.23640 0.41630 0.03290  -0.05640 -0.00180 201  ASP A CA    
1581 C  C     . ASP A 201 ? 0.30870 0.20090 0.44670 0.02730  -0.04830 -0.00140 201  ASP A C     
1582 O  O     . ASP A 201 ? 0.34850 0.23000 0.45470 0.03790  -0.05190 -0.00650 201  ASP A O     
1583 C  CB    . ASP A 201 ? 0.33200 0.29080 0.40980 0.05270  -0.07410 0.06330  201  ASP A CB    
1584 C  CG    . ASP A 201 ? 0.46740 0.41400 0.41720 -0.02060 -0.07140 0.04160  201  ASP A CG    
1585 O  OD1   . ASP A 201 ? 0.54660 0.41390 0.41060 0.00010  -0.06310 -0.00300 201  ASP A OD1   
1586 O  OD2   . ASP A 201 ? 0.49940 0.52680 0.43020 -0.00330 -0.05900 0.04250  201  ASP A OD2   
1587 N  N     . GLY A 202 ? 0.32220 0.24520 0.47240 0.07590  -0.01690 -0.02210 202  GLY A N     
1588 C  CA    . GLY A 202 ? 0.35590 0.20740 0.49480 0.08230  -0.01310 -0.05380 202  GLY A CA    
1589 C  C     . GLY A 202 ? 0.33760 0.18730 0.51060 0.05340  -0.05130 -0.06580 202  GLY A C     
1590 O  O     . GLY A 202 ? 0.36210 0.18760 0.53270 0.03840  -0.00050 -0.06190 202  GLY A O     
1591 N  N     . LEU A 203 ? 0.31330 0.25080 0.49880 0.06450  -0.06460 -0.09280 203  LEU A N     
1592 C  CA    . LEU A 203 ? 0.28170 0.20650 0.49210 0.05770  -0.06460 -0.08840 203  LEU A CA    
1593 C  C     . LEU A 203 ? 0.30010 0.20330 0.49110 -0.02570 -0.06580 -0.06860 203  LEU A C     
1594 O  O     . LEU A 203 ? 0.32960 0.18070 0.48910 0.02400  -0.05400 -0.08650 203  LEU A O     
1595 C  CB    . LEU A 203 ? 0.32130 0.26150 0.50070 0.06090  -0.05480 -0.08250 203  LEU A CB    
1596 C  CG    . LEU A 203 ? 0.37310 0.28970 0.50300 0.07590  -0.07190 -0.07090 203  LEU A CG    
1597 C  CD1   . LEU A 203 ? 0.45190 0.25400 0.50400 0.03510  -0.08540 -0.06480 203  LEU A CD1   
1598 C  CD2   . LEU A 203 ? 0.33340 0.31600 0.50900 0.08490  -0.10430 -0.07360 203  LEU A CD2   
1599 N  N     . ILE A 204 ? 0.31350 0.18470 0.48040 0.03180  -0.06990 -0.05340 204  ILE A N     
1600 C  CA    . ILE A 204 ? 0.32990 0.15380 0.48350 0.06560  -0.08490 -0.01250 204  ILE A CA    
1601 C  C     . ILE A 204 ? 0.29200 0.17170 0.55580 0.02840  -0.07820 0.01730  204  ILE A C     
1602 O  O     . ILE A 204 ? 0.29130 0.20270 0.55370 -0.00760 -0.06930 0.01200  204  ILE A O     
1603 C  CB    . ILE A 204 ? 0.35460 0.12010 0.43590 0.03220  -0.04870 0.01160  204  ILE A CB    
1604 C  CG1   . ILE A 204 ? 0.34050 0.12240 0.40250 0.03540  -0.01980 0.05900  204  ILE A CG1   
1605 C  CG2   . ILE A 204 ? 0.38010 0.20280 0.45010 -0.01230 -0.03080 0.00440  204  ILE A CG2   
1606 C  CD1   . ILE A 204 ? 0.34450 0.12840 0.40670 0.00230  -0.00790 0.03800  204  ILE A CD1   
1607 N  N     . THR A 205 ? 0.27261 0.18893 0.59126 0.06438  -0.07789 -0.01990 205  THR A N     
1608 C  CA    . THR A 205 ? 0.25550 0.19710 0.65350 0.04180  -0.07650 -0.00960 205  THR A CA    
1609 C  C     . THR A 205 ? 0.29550 0.20580 0.60800 0.04400  -0.05220 0.00720  205  THR A C     
1610 O  O     . THR A 205 ? 0.38270 0.19750 0.60950 0.05560  -0.04480 0.02270  205  THR A O     
1611 C  CB    . THR A 205 ? 0.30430 0.21630 0.71900 -0.01440 -0.11650 0.01670  205  THR A CB    
1612 O  OG1   . THR A 205 ? 0.34100 0.26290 0.76540 0.02070  -0.16320 0.03560  205  THR A OG1   
1613 C  CG2   . THR A 205 ? 0.34020 0.21830 0.72870 -0.01640 -0.09960 0.05140  205  THR A CG2   
1614 N  N     . GLN A 206 ? 0.32360 0.17380 0.55260 0.01330  -0.02510 -0.06460 206  GLN A N     
1615 C  CA    . GLN A 206 ? 0.38810 0.18250 0.51260 0.03230  -0.01380 -0.03540 206  GLN A CA    
1616 C  C     . GLN A 206 ? 0.33380 0.24050 0.47230 -0.00040 -0.06150 -0.05070 206  GLN A C     
1617 O  O     . GLN A 206 ? 0.35170 0.21640 0.43960 -0.00550 -0.00050 -0.04380 206  GLN A O     
1618 C  CB    . GLN A 206 ? 0.42790 0.18430 0.49970 0.01840  -0.03980 -0.07870 206  GLN A CB    
1619 C  CG    . GLN A 206 ? 0.60980 0.41640 0.52070 -0.00730 -0.02850 -0.06370 206  GLN A CG    
1620 C  CD    . GLN A 206 ? 0.77670 0.62680 0.55930 -0.01030 -0.03420 -0.01880 206  GLN A CD    
1621 O  OE1   . GLN A 206 ? 0.85520 0.69860 0.58130 -0.00710 -0.01360 -0.01320 206  GLN A OE1   
1622 N  NE2   . GLN A 206 ? 0.81840 0.71590 0.56910 -0.00190 -0.04690 -0.00590 206  GLN A NE2   
1623 N  N     . PHE A 207 ? 0.34400 0.21120 0.45400 0.04010  -0.08110 -0.04450 207  PHE A N     
1624 C  CA    . PHE A 207 ? 0.33850 0.21290 0.41690 -0.01610 -0.10160 -0.00480 207  PHE A CA    
1625 C  C     . PHE A 207 ? 0.32550 0.21050 0.40590 0.00780  -0.10090 0.03250  207  PHE A C     
1626 O  O     . PHE A 207 ? 0.42460 0.18050 0.39140 -0.00290 -0.10490 0.04510  207  PHE A O     
1627 C  CB    . PHE A 207 ? 0.35020 0.16370 0.40380 0.03170  -0.10950 0.00400  207  PHE A CB    
1628 C  CG    . PHE A 207 ? 0.38660 0.16580 0.39840 0.00610  -0.10710 0.00840  207  PHE A CG    
1629 C  CD1   . PHE A 207 ? 0.41970 0.23200 0.39200 -0.01390 -0.11410 0.00520  207  PHE A CD1   
1630 C  CD2   . PHE A 207 ? 0.36930 0.25090 0.38950 0.02080  -0.13390 0.00170  207  PHE A CD2   
1631 C  CE1   . PHE A 207 ? 0.43220 0.19010 0.39380 -0.00340 -0.09460 0.02340  207  PHE A CE1   
1632 C  CE2   . PHE A 207 ? 0.39020 0.19010 0.38390 0.01030  -0.11350 0.01060  207  PHE A CE2   
1633 C  CZ    . PHE A 207 ? 0.39030 0.17000 0.38860 -0.00790 -0.09600 0.00440  207  PHE A CZ    
1634 N  N     . GLN A 208 ? 0.35110 0.20270 0.39030 0.07420  -0.10130 -0.02800 208  GLN A N     
1635 C  CA    . GLN A 208 ? 0.32610 0.15530 0.37100 0.06280  -0.10810 0.00050  208  GLN A CA    
1636 C  C     . GLN A 208 ? 0.37040 0.20000 0.33150 0.06850  -0.11800 0.00520  208  GLN A C     
1637 O  O     . GLN A 208 ? 0.46400 0.23800 0.34630 0.03310  -0.13350 0.02590  208  GLN A O     
1638 C  CB    . GLN A 208 ? 0.40520 0.16050 0.37670 0.02230  -0.09300 -0.00330 208  GLN A CB    
1639 C  CG    . GLN A 208 ? 0.39860 0.13070 0.38410 0.04780  -0.06850 -0.00380 208  GLN A CG    
1640 C  CD    . GLN A 208 ? 0.37560 0.17310 0.36250 0.04270  -0.07200 0.00500  208  GLN A CD    
1641 O  OE1   . GLN A 208 ? 0.35290 0.26750 0.36030 -0.04190 0.01050  -0.00580 208  GLN A OE1   
1642 N  NE2   . GLN A 208 ? 0.44420 0.20450 0.34110 0.02420  -0.07590 0.01170  208  GLN A NE2   
1643 N  N     . THR A 209 ? 0.29480 0.16070 0.29980 0.07180  -0.06090 -0.07570 209  THR A N     
1644 C  CA    . THR A 209 ? 0.35230 0.18710 0.29530 0.00400  -0.03050 -0.01110 209  THR A CA    
1645 C  C     . THR A 209 ? 0.43540 0.18790 0.35160 0.05080  -0.09910 -0.02780 209  THR A C     
1646 O  O     . THR A 209 ? 0.48160 0.21450 0.35950 0.04620  -0.07570 -0.00060 209  THR A O     
1647 C  CB    . THR A 209 ? 0.40920 0.23810 0.25980 0.04470  0.06030  -0.02450 209  THR A CB    
1648 O  OG1   . THR A 209 ? 0.46620 0.36010 0.28570 0.03000  0.01110  0.00570  209  THR A OG1   
1649 C  CG2   . THR A 209 ? 0.46420 0.23550 0.23950 0.10550  -0.00780 -0.04700 209  THR A CG2   
1650 N  N     . GLU A 210 ? 0.40310 0.21530 0.40030 0.08820  -0.14720 -0.05840 210  GLU A N     
1651 C  CA    . GLU A 210 ? 0.45800 0.23400 0.45800 0.10880  -0.13280 -0.03430 210  GLU A CA    
1652 C  C     . GLU A 210 ? 0.42200 0.15650 0.43920 0.01770  -0.15810 -0.02020 210  GLU A C     
1653 O  O     . GLU A 210 ? 0.48180 0.15530 0.46870 -0.00780 -0.11380 -0.01700 210  GLU A O     
1654 C  CB    . GLU A 210 ? 0.62060 0.39650 0.51220 0.14220  -0.09770 -0.05070 210  GLU A CB    
1655 C  CG    . GLU A 210 ? 0.82740 0.61920 0.57270 0.12630  -0.07590 -0.04680 210  GLU A CG    
1656 C  CD    . GLU A 210 ? 1.00290 0.80840 0.62570 0.10660  -0.04890 -0.05350 210  GLU A CD    
1657 O  OE1   . GLU A 210 ? 1.06570 0.86820 0.64890 0.11190  -0.03950 -0.05050 210  GLU A OE1   
1658 O  OE2   . GLU A 210 ? 1.05360 0.87120 0.63930 0.08640  -0.03460 -0.05220 210  GLU A OE2   
1659 N  N     . PRO A 211 ? 0.43450 0.21270 0.40910 -0.00840 -0.17800 0.03370  211  PRO A N     
1660 C  CA    . PRO A 211 ? 0.40200 0.24780 0.38480 0.01050  -0.18100 0.01850  211  PRO A CA    
1661 C  C     . PRO A 211 ? 0.41110 0.19120 0.37810 0.04260  -0.19730 0.02220  211  PRO A C     
1662 O  O     . PRO A 211 ? 0.50190 0.18060 0.39890 -0.01210 -0.17270 -0.03060 211  PRO A O     
1663 C  CB    . PRO A 211 ? 0.44910 0.32360 0.39120 0.03160  -0.15160 0.02250  211  PRO A CB    
1664 C  CG    . PRO A 211 ? 0.49380 0.34730 0.39990 0.06270  -0.14430 0.01130  211  PRO A CG    
1665 C  CD    . PRO A 211 ? 0.44990 0.29450 0.39620 0.07030  -0.16640 0.03700  211  PRO A CD    
1666 N  N     . GLY A 212 ? 0.44450 0.21880 0.36130 0.05700  -0.18210 0.04340  212  GLY A N     
1667 C  CA    . GLY A 212 ? 0.40750 0.25370 0.35200 0.06080  -0.19700 0.02870  212  GLY A CA    
1668 C  C     . GLY A 212 ? 0.38390 0.22630 0.34590 0.03500  -0.16040 0.04550  212  GLY A C     
1669 O  O     . GLY A 212 ? 0.34940 0.20000 0.33810 -0.00310 -0.11210 0.07430  212  GLY A O     
1670 N  N     . ALA A 213 ? 0.38820 0.27770 0.34190 0.04570  -0.14080 0.05100  213  ALA A N     
1671 C  CA    . ALA A 213 ? 0.37030 0.19510 0.31610 -0.05480 -0.09870 0.06820  213  ALA A CA    
1672 C  C     . ALA A 213 ? 0.32520 0.17870 0.30500 -0.08560 -0.07860 0.06530  213  ALA A C     
1673 O  O     . ALA A 213 ? 0.35410 0.26680 0.33680 -0.01410 -0.10370 0.10510  213  ALA A O     
1674 C  CB    . ALA A 213 ? 0.40560 0.28520 0.31430 -0.04710 -0.09180 0.06560  213  ALA A CB    
1675 N  N     . GLY A 214 ? 0.35020 0.16920 0.26860 0.00740  -0.06300 0.04600  214  GLY A N     
1676 C  CA    . GLY A 214 ? 0.34180 0.11770 0.23120 -0.03610 -0.07540 0.01220  214  GLY A CA    
1677 C  C     . GLY A 214 ? 0.34770 0.10160 0.21410 0.01280  -0.07700 0.01610  214  GLY A C     
1678 O  O     . GLY A 214 ? 0.40950 0.20940 0.20140 0.02920  -0.08630 0.06180  214  GLY A O     
1679 N  N     . LEU A 215 ? 0.31210 0.08670 0.20030 -0.00100 -0.04230 0.02380  215  LEU A N     
1680 C  CA    . LEU A 215 ? 0.29630 0.09490 0.19650 0.03150  -0.02950 -0.02310 215  LEU A CA    
1681 C  C     . LEU A 215 ? 0.31540 0.16110 0.16520 0.02900  -0.02780 0.00270  215  LEU A C     
1682 O  O     . LEU A 215 ? 0.34020 0.19800 0.16690 0.03600  -0.04370 0.00740  215  LEU A O     
1683 C  CB    . LEU A 215 ? 0.34768 0.09882 0.20300 0.04629  -0.02300 -0.01180 215  LEU A CB    
1684 C  CG    . LEU A 215 ? 0.34960 0.14470 0.17550 0.05800  -0.00290 0.00920  215  LEU A CG    
1685 C  CD1   . LEU A 215 ? 0.38440 0.21120 0.14470 0.00210  -0.02700 0.00240  215  LEU A CD1   
1686 C  CD2   . LEU A 215 ? 0.42750 0.18850 0.20040 0.11030  -0.01070 0.03210  215  LEU A CD2   
1687 N  N     . VAL A 216 ? 0.30520 0.19460 0.16760 0.02780  -0.02880 0.00380  216  VAL A N     
1688 C  CA    . VAL A 216 ? 0.28510 0.17220 0.18080 -0.00120 -0.04550 0.04020  216  VAL A CA    
1689 C  C     . VAL A 216 ? 0.34380 0.14420 0.19730 0.06520  -0.02820 0.03180  216  VAL A C     
1690 O  O     . VAL A 216 ? 0.34820 0.19700 0.20950 0.03040  -0.05700 0.02230  216  VAL A O     
1691 C  CB    . VAL A 216 ? 0.28720 0.17450 0.18870 0.04010  -0.03760 0.04200  216  VAL A CB    
1692 C  CG1   . VAL A 216 ? 0.32360 0.19710 0.18790 0.04140  -0.04490 0.02430  216  VAL A CG1   
1693 C  CG2   . VAL A 216 ? 0.33430 0.18600 0.21390 0.04280  -0.02090 0.01010  216  VAL A CG2   
1694 N  N     . GLY A 217 ? 0.36357 0.09673 0.19040 0.01730  -0.03009 0.01569  217  GLY A N     
1695 C  CA    . GLY A 217 ? 0.40010 0.11550 0.18270 0.03360  -0.04930 0.01870  217  GLY A CA    
1696 C  C     . GLY A 217 ? 0.35940 0.20040 0.17830 0.00540  -0.04510 0.02710  217  GLY A C     
1697 O  O     . GLY A 217 ? 0.36980 0.17370 0.18770 0.02600  -0.04610 0.00130  217  GLY A O     
1698 N  N     . ALA A 218 ? 0.32960 0.16360 0.18510 0.02800  -0.05510 0.01260  218  ALA A N     
1699 C  CA    . ALA A 218 ? 0.29370 0.23220 0.17820 -0.00280 -0.03890 0.00880  218  ALA A CA    
1700 C  C     . ALA A 218 ? 0.30120 0.19310 0.15640 -0.03990 -0.01780 0.01720  218  ALA A C     
1701 O  O     . ALA A 218 ? 0.35430 0.24790 0.13050 0.01340  -0.06020 0.00810  218  ALA A O     
1702 C  CB    . ALA A 218 ? 0.28910 0.20000 0.18970 0.01200  -0.04150 0.02450  218  ALA A CB    
1703 N  N     . LEU A 219 ? 0.30080 0.15240 0.17140 -0.00520 -0.03370 0.01530  219  LEU A N     
1704 C  CA    . LEU A 219 ? 0.32210 0.16650 0.18440 0.00030  -0.05090 0.01230  219  LEU A CA    
1705 C  C     . LEU A 219 ? 0.29060 0.15310 0.19910 0.00170  -0.05380 0.03970  219  LEU A C     
1706 O  O     . LEU A 219 ? 0.33710 0.22310 0.19720 -0.02100 -0.08440 0.01380  219  LEU A O     
1707 C  CB    . LEU A 219 ? 0.33320 0.17090 0.19720 0.00470  -0.09380 0.01810  219  LEU A CB    
1708 C  CG    . LEU A 219 ? 0.36450 0.17680 0.20150 0.06930  -0.05840 -0.01090 219  LEU A CG    
1709 C  CD1   . LEU A 219 ? 0.41200 0.17000 0.19530 0.05720  -0.05440 0.02740  219  LEU A CD1   
1710 C  CD2   . LEU A 219 ? 0.36810 0.26800 0.20760 0.11020  -0.04860 -0.05020 219  LEU A CD2   
1711 N  N     . VAL A 220 ? 0.28450 0.13280 0.20640 0.03830  -0.03070 0.02590  220  VAL A N     
1712 C  CA    . VAL A 220 ? 0.32980 0.14240 0.20460 0.03810  -0.02770 0.01730  220  VAL A CA    
1713 C  C     . VAL A 220 ? 0.34900 0.17110 0.17580 -0.01820 -0.05030 0.04760  220  VAL A C     
1714 O  O     . VAL A 220 ? 0.39960 0.19390 0.16450 -0.01950 -0.10650 0.02660  220  VAL A O     
1715 C  CB    . VAL A 220 ? 0.29340 0.18350 0.20140 0.06260  -0.02590 0.02760  220  VAL A CB    
1716 C  CG1   . VAL A 220 ? 0.29890 0.17570 0.23060 0.03840  -0.04930 0.03210  220  VAL A CG1   
1717 C  CG2   . VAL A 220 ? 0.32570 0.15990 0.16440 0.03100  -0.02870 0.03130  220  VAL A CG2   
1718 N  N     . ALA A 221 ? 0.38450 0.14170 0.18630 0.00540  -0.06320 0.03860  221  ALA A N     
1719 C  CA    . ALA A 221 ? 0.37210 0.15340 0.19740 -0.02810 -0.08750 0.03420  221  ALA A CA    
1720 C  C     . ALA A 221 ? 0.36490 0.20320 0.19930 -0.04560 -0.05350 0.03530  221  ALA A C     
1721 O  O     . ALA A 221 ? 0.35660 0.25000 0.18450 -0.01980 -0.02880 0.08840  221  ALA A O     
1722 C  CB    . ALA A 221 ? 0.40160 0.18530 0.24240 -0.08990 -0.07100 0.03480  221  ALA A CB    
1723 N  N     . ASP A 222 ? 0.35420 0.22040 0.21310 -0.02970 -0.02930 0.04790  222  ASP A N     
1724 C  CA    . ASP A 222 ? 0.27790 0.22730 0.21130 0.00990  -0.00190 0.05860  222  ASP A CA    
1725 C  C     . ASP A 222 ? 0.30440 0.20070 0.19420 0.00720  -0.03390 0.06760  222  ASP A C     
1726 O  O     . ASP A 222 ? 0.33020 0.20060 0.19350 -0.00060 -0.08700 0.05250  222  ASP A O     
1727 C  CB    . ASP A 222 ? 0.31510 0.28360 0.24260 0.03920  -0.00120 0.05020  222  ASP A CB    
1728 C  CG    . ASP A 222 ? 0.32750 0.35370 0.28800 0.03210  0.00300  0.04030  222  ASP A CG    
1729 O  OD1   . ASP A 222 ? 0.37070 0.30590 0.29430 0.04890  -0.01630 0.05220  222  ASP A OD1   
1730 O  OD2   . ASP A 222 ? 0.35450 0.48410 0.32260 0.02420  0.02400  0.02640  222  ASP A OD2   
1731 N  N     . GLN A 223 ? 0.30570 0.21650 0.18980 -0.00520 -0.05510 0.04640  223  GLN A N     
1732 C  CA    . GLN A 223 ? 0.32240 0.19560 0.21450 -0.00520 -0.08430 0.04980  223  GLN A CA    
1733 C  C     . GLN A 223 ? 0.31130 0.18660 0.19360 -0.03820 -0.07250 0.02580  223  GLN A C     
1734 O  O     . GLN A 223 ? 0.34050 0.20360 0.18990 -0.01380 -0.07290 0.00960  223  GLN A O     
1735 C  CB    . GLN A 223 ? 0.31500 0.20050 0.23920 0.04270  -0.12180 0.05460  223  GLN A CB    
1736 C  CG    . GLN A 223 ? 0.35500 0.19350 0.24880 0.01280  -0.10570 0.03280  223  GLN A CG    
1737 C  CD    . GLN A 223 ? 0.37550 0.21640 0.25730 0.02690  -0.07890 0.02690  223  GLN A CD    
1738 O  OE1   . GLN A 223 ? 0.35120 0.22760 0.24260 0.01970  -0.09470 0.03870  223  GLN A OE1   
1739 N  NE2   . GLN A 223 ? 0.38760 0.25600 0.27210 -0.02360 -0.05900 0.01620  223  GLN A NE2   
1740 N  N     . LEU A 224 ? 0.30050 0.18830 0.19710 0.03300  -0.04410 0.03510  224  LEU A N     
1741 C  CA    . LEU A 224 ? 0.31100 0.19840 0.16950 0.02570  0.00020  0.05650  224  LEU A CA    
1742 C  C     . LEU A 224 ? 0.29510 0.17660 0.16750 0.03500  -0.06080 0.06500  224  LEU A C     
1743 O  O     . LEU A 224 ? 0.30740 0.22810 0.16940 -0.03760 -0.06550 0.05140  224  LEU A O     
1744 C  CB    . LEU A 224 ? 0.32270 0.20930 0.17430 -0.02500 -0.00940 0.02970  224  LEU A CB    
1745 C  CG    . LEU A 224 ? 0.33940 0.18080 0.19320 0.01180  -0.04640 0.02510  224  LEU A CG    
1746 C  CD1   . LEU A 224 ? 0.35650 0.21610 0.23010 -0.03250 -0.06100 0.04400  224  LEU A CD1   
1747 C  CD2   . LEU A 224 ? 0.40680 0.24400 0.19210 -0.01840 -0.04300 0.00100  224  LEU A CD2   
1748 N  N     . ALA A 225 ? 0.34819 0.13161 0.17520 0.00090  -0.03160 0.05959  225  ALA A N     
1749 C  CA    . ALA A 225 ? 0.36049 0.10261 0.17400 0.03360  -0.01960 0.02110  225  ALA A CA    
1750 C  C     . ALA A 225 ? 0.31290 0.12670 0.16430 0.00260  -0.01730 0.04730  225  ALA A C     
1751 O  O     . ALA A 225 ? 0.31590 0.15920 0.18390 -0.01140 -0.04620 0.04390  225  ALA A O     
1752 C  CB    . ALA A 225 ? 0.38150 0.15140 0.17980 0.04630  -0.03100 0.02790  225  ALA A CB    
1753 N  N     . ASN A 226 ? 0.31190 0.15440 0.15030 -0.01420 -0.02250 0.01890  226  ASN A N     
1754 C  CA    . ASN A 226 ? 0.35550 0.17300 0.15580 -0.00720 -0.04770 0.02420  226  ASN A CA    
1755 C  C     . ASN A 226 ? 0.39290 0.17800 0.16360 -0.02070 -0.06850 0.04670  226  ASN A C     
1756 O  O     . ASN A 226 ? 0.44300 0.20710 0.16510 -0.02550 -0.07300 0.03600  226  ASN A O     
1757 C  CB    . ASN A 226 ? 0.29640 0.18530 0.17550 0.01460  -0.04150 0.02540  226  ASN A CB    
1758 C  CG    . ASN A 226 ? 0.31800 0.19740 0.17170 -0.00630 -0.06810 0.05760  226  ASN A CG    
1759 O  OD1   . ASN A 226 ? 0.43420 0.18910 0.17670 -0.02120 -0.05730 0.05930  226  ASN A OD1   
1760 N  ND2   . ASN A 226 ? 0.33050 0.28100 0.15540 -0.00130 -0.04410 0.03370  226  ASN A ND2   
1761 N  N     . GLY A 227 ? 0.34210 0.14210 0.16770 -0.01250 -0.06690 0.04960  227  GLY A N     
1762 C  CA    . GLY A 227 ? 0.35420 0.13170 0.22770 0.00110  -0.06800 0.05250  227  GLY A CA    
1763 C  C     . GLY A 227 ? 0.35290 0.16040 0.24250 -0.01030 -0.09180 0.01690  227  GLY A C     
1764 O  O     . GLY A 227 ? 0.41750 0.23240 0.29820 -0.02480 -0.10470 -0.01200 227  GLY A O     
1765 N  N     . GLU A 228 ? 0.34890 0.18330 0.19110 -0.01690 -0.07130 0.05360  228  GLU A N     
1766 C  CA    . GLU A 228 ? 0.31990 0.22900 0.17980 0.02130  -0.04760 0.07350  228  GLU A CA    
1767 C  C     . GLU A 228 ? 0.33510 0.23970 0.18500 0.08580  -0.06680 0.04770  228  GLU A C     
1768 O  O     . GLU A 228 ? 0.38860 0.26520 0.20780 0.09540  -0.04670 0.06420  228  GLU A O     
1769 C  CB    . GLU A 228 ? 0.35740 0.26130 0.19320 0.04290  -0.01120 0.04540  228  GLU A CB    
1770 C  CG    . GLU A 228 ? 0.39990 0.29920 0.20250 0.00450  -0.04310 0.07530  228  GLU A CG    
1771 C  CD    . GLU A 228 ? 0.45780 0.39590 0.23230 -0.03070 -0.02830 0.08910  228  GLU A CD    
1772 O  OE1   . GLU A 228 ? 0.43430 0.47060 0.23030 -0.03310 -0.02280 0.09540  228  GLU A OE1   
1773 O  OE2   . GLU A 228 ? 0.49740 0.42150 0.26630 -0.09130 0.00030  0.04150  228  GLU A OE2   
1774 N  N     . ILE A 229 ? 0.36360 0.22930 0.17510 -0.00930 -0.04240 0.03770  229  ILE A N     
1775 C  CA    . ILE A 229 ? 0.33880 0.22550 0.18140 -0.01900 -0.06610 0.06060  229  ILE A CA    
1776 C  C     . ILE A 229 ? 0.30330 0.30270 0.19050 -0.02270 -0.06640 0.05980  229  ILE A C     
1777 O  O     . ILE A 229 ? 0.33720 0.26470 0.21700 0.02280  -0.07040 0.02920  229  ILE A O     
1778 C  CB    . ILE A 229 ? 0.36890 0.17920 0.19220 -0.01540 -0.09480 0.06500  229  ILE A CB    
1779 C  CG1   . ILE A 229 ? 0.39730 0.17630 0.19010 -0.03930 -0.09320 0.04320  229  ILE A CG1   
1780 C  CG2   . ILE A 229 ? 0.37950 0.16030 0.22030 -0.03070 -0.08000 0.02610  229  ILE A CG2   
1781 C  CD1   . ILE A 229 ? 0.36470 0.25790 0.20150 -0.03970 -0.06120 0.02620  229  ILE A CD1   
1782 N  N     . ASP A 230 ? 0.33950 0.29750 0.20430 -0.07650 -0.02870 0.04360  230  ASP A N     
1783 C  CA    . ASP A 230 ? 0.32170 0.36050 0.22280 -0.11120 -0.04630 0.01970  230  ASP A CA    
1784 C  C     . ASP A 230 ? 0.31790 0.31630 0.23530 -0.06550 -0.02380 0.03190  230  ASP A C     
1785 O  O     . ASP A 230 ? 0.28780 0.22700 0.23590 -0.00940 -0.04050 0.02780  230  ASP A O     
1786 C  CB    . ASP A 230 ? 0.36480 0.37700 0.22790 -0.12080 -0.05540 0.01610  230  ASP A CB    
1787 C  CG    . ASP A 230 ? 0.44840 0.42870 0.25600 -0.12360 -0.00080 0.00840  230  ASP A CG    
1788 O  OD1   . ASP A 230 ? 0.57970 0.50110 0.26670 -0.17460 -0.01850 0.00530  230  ASP A OD1   
1789 O  OD2   . ASP A 230 ? 0.34120 0.34020 0.25850 -0.06700 0.03510  -0.03350 230  ASP A OD2   
1790 N  N     . ARG A 231 ? 0.31500 0.28310 0.23400 0.02680  -0.04520 0.03720  231  ARG A N     
1791 C  CA    . ARG A 231 ? 0.36000 0.25360 0.24280 0.02760  -0.02800 0.01970  231  ARG A CA    
1792 C  C     . ARG A 231 ? 0.35410 0.17870 0.22900 -0.01920 -0.07420 0.00870  231  ARG A C     
1793 O  O     . ARG A 231 ? 0.33710 0.23310 0.22420 -0.00310 -0.03920 0.02530  231  ARG A O     
1794 C  CB    . ARG A 231 ? 0.38480 0.25530 0.25490 0.04880  -0.04300 0.00660  231  ARG A CB    
1795 C  CG    . ARG A 231 ? 0.33550 0.30100 0.26330 0.05640  -0.08800 -0.03550 231  ARG A CG    
1796 C  CD    . ARG A 231 ? 0.28950 0.40890 0.30280 -0.02390 -0.05840 -0.07770 231  ARG A CD    
1797 N  NE    . ARG A 231 ? 0.34650 0.40870 0.35690 -0.04020 -0.04790 -0.04930 231  ARG A NE    
1798 C  CZ    . ARG A 231 ? 0.33830 0.42820 0.37230 -0.03480 -0.03460 -0.00710 231  ARG A CZ    
1799 N  NH1   . ARG A 231 ? 0.28150 0.42270 0.39420 -0.06130 -0.04500 0.05500  231  ARG A NH1   
1800 N  NH2   . ARG A 231 ? 0.36080 0.42490 0.35740 -0.07620 -0.02200 0.00890  231  ARG A NH2   
1801 N  N     . GLU A 232 ? 0.31370 0.23130 0.22580 0.01140  -0.08520 -0.00220 232  GLU A N     
1802 C  CA    A GLU A 232 ? 0.29550 0.23890 0.22950 0.00340  -0.06780 0.00330  232  GLU A CA    
1803 C  CA    B GLU A 232 ? 0.27810 0.24480 0.22940 0.01000  -0.08050 0.00790  232  GLU A CA    
1804 C  C     . GLU A 232 ? 0.28440 0.20390 0.20390 -0.01340 -0.06920 0.02750  232  GLU A C     
1805 O  O     . GLU A 232 ? 0.28390 0.18780 0.19350 -0.00280 -0.03660 0.02740  232  GLU A O     
1806 C  CB    A GLU A 232 ? 0.31740 0.26340 0.26550 -0.04230 -0.05520 -0.00090 232  GLU A CB    
1807 C  CB    B GLU A 232 ? 0.27060 0.27960 0.26570 -0.01090 -0.07920 0.00150  232  GLU A CB    
1808 C  CG    A GLU A 232 ? 0.38590 0.36840 0.27800 -0.01360 -0.05150 0.00930  232  GLU A CG    
1809 C  CG    B GLU A 232 ? 0.28380 0.38850 0.29540 0.03780  -0.08910 0.03360  232  GLU A CG    
1810 C  CD    A GLU A 232 ? 0.35800 0.31530 0.26630 0.03790  -0.04110 0.02160  232  GLU A CD    
1811 C  CD    B GLU A 232 ? 0.31350 0.42470 0.32500 0.07590  -0.05650 0.06130  232  GLU A CD    
1812 O  OE1   A GLU A 232 ? 0.24070 0.19000 0.18780 -0.05330 -0.05030 0.03110  232  GLU A OE1   
1813 O  OE1   B GLU A 232 ? 0.34340 0.42260 0.32950 0.06300  -0.04660 0.10240  232  GLU A OE1   
1814 O  OE2   A GLU A 232 ? 0.50020 0.28120 0.29330 0.06500  -0.08390 0.04350  232  GLU A OE2   
1815 O  OE2   B GLU A 232 ? 0.41640 0.45850 0.33970 0.07920  -0.03400 0.06810  232  GLU A OE2   
1816 N  N     . GLU A 233 ? 0.32180 0.18640 0.21090 -0.00520 -0.04630 0.02850  233  GLU A N     
1817 C  CA    . GLU A 233 ? 0.31090 0.18570 0.19220 0.01900  -0.04930 0.01380  233  GLU A CA    
1818 C  C     . GLU A 233 ? 0.26260 0.17940 0.18120 0.00930  -0.01740 0.04730  233  GLU A C     
1819 O  O     . GLU A 233 ? 0.29710 0.20840 0.17110 0.05470  -0.01010 0.03560  233  GLU A O     
1820 C  CB    . GLU A 233 ? 0.36150 0.21930 0.20480 0.00970  -0.05590 -0.01990 233  GLU A CB    
1821 C  CG    . GLU A 233 ? 0.45830 0.26430 0.23780 0.00530  0.00510  -0.02230 233  GLU A CG    
1822 C  CD    . GLU A 233 ? 0.45350 0.25920 0.26040 -0.00810 -0.00000 -0.02570 233  GLU A CD    
1823 O  OE1   . GLU A 233 ? 0.42630 0.25780 0.27110 -0.00150 -0.00310 -0.05630 233  GLU A OE1   
1824 O  OE2   . GLU A 233 ? 0.43880 0.24000 0.29500 0.03800  -0.05550 -0.03090 233  GLU A OE2   
1825 N  N     . LEU A 234 ? 0.32350 0.15470 0.17950 0.02820  -0.00850 0.01620  234  LEU A N     
1826 C  CA    . LEU A 234 ? 0.34410 0.15930 0.16970 0.02810  -0.02300 0.02160  234  LEU A CA    
1827 C  C     . LEU A 234 ? 0.27930 0.16860 0.15390 0.00850  -0.04020 0.02120  234  LEU A C     
1828 O  O     . LEU A 234 ? 0.30360 0.17650 0.15790 0.01520  -0.03270 0.02950  234  LEU A O     
1829 C  CB    . LEU A 234 ? 0.38850 0.16410 0.17590 0.00830  -0.02700 0.03200  234  LEU A CB    
1830 C  CG    . LEU A 234 ? 0.40030 0.14190 0.18730 -0.01100 -0.05590 0.03660  234  LEU A CG    
1831 C  CD1   . LEU A 234 ? 0.40400 0.14430 0.20360 0.02990  -0.02850 0.03800  234  LEU A CD1   
1832 C  CD2   . LEU A 234 ? 0.43810 0.23710 0.19100 -0.02740 -0.10090 0.04860  234  LEU A CD2   
1833 N  N     . ILE A 235 ? 0.26270 0.15900 0.16980 -0.00400 -0.00640 0.05110  235  ILE A N     
1834 C  CA    . ILE A 235 ? 0.27100 0.17160 0.19150 0.01480  -0.00990 0.04710  235  ILE A CA    
1835 C  C     . ILE A 235 ? 0.28590 0.17030 0.17980 0.02630  0.00180  0.02430  235  ILE A C     
1836 O  O     . ILE A 235 ? 0.28550 0.17000 0.18490 0.00220  -0.01720 0.00920  235  ILE A O     
1837 C  CB    . ILE A 235 ? 0.28970 0.16000 0.22220 0.05270  -0.00610 0.02210  235  ILE A CB    
1838 C  CG1   . ILE A 235 ? 0.31580 0.20820 0.28340 0.09420  0.02400  -0.03520 235  ILE A CG1   
1839 C  CG2   . ILE A 235 ? 0.33760 0.19300 0.21840 0.01900  0.03430  0.03920  235  ILE A CG2   
1840 C  CD1   . ILE A 235 ? 0.27890 0.24240 0.32010 0.05990  0.02030  -0.06600 235  ILE A CD1   
1841 N  N     . SER A 236 ? 0.28770 0.17130 0.17780 0.02910  -0.01080 0.03140  236  SER A N     
1842 C  CA    . SER A 236 ? 0.28620 0.14580 0.17480 0.02590  -0.03260 0.01380  236  SER A CA    
1843 C  C     . SER A 236 ? 0.27540 0.14630 0.15160 0.04430  -0.02210 0.01530  236  SER A C     
1844 O  O     . SER A 236 ? 0.31290 0.19670 0.13120 0.03110  -0.00740 0.02880  236  SER A O     
1845 C  CB    . SER A 236 ? 0.30110 0.17360 0.23180 -0.01730 -0.02440 -0.00640 236  SER A CB    
1846 O  OG    . SER A 236 ? 0.30650 0.23140 0.25340 0.00360  -0.00530 -0.01220 236  SER A OG    
1847 N  N     . THR A 237 ? 0.28600 0.16220 0.15960 0.01980  0.00260  0.01950  237  THR A N     
1848 C  CA    . THR A 237 ? 0.25810 0.14300 0.15170 -0.02750 0.00490  0.01560  237  THR A CA    
1849 C  C     . THR A 237 ? 0.29340 0.12260 0.14230 0.01510  -0.02600 0.03560  237  THR A C     
1850 O  O     . THR A 237 ? 0.30680 0.15910 0.15910 0.05380  -0.01520 0.03060  237  THR A O     
1851 C  CB    . THR A 237 ? 0.30870 0.19000 0.16340 0.03190  0.01880  0.01980  237  THR A CB    
1852 O  OG1   . THR A 237 ? 0.39160 0.22590 0.17880 0.02000  0.00560  -0.00830 237  THR A OG1   
1853 C  CG2   . THR A 237 ? 0.29620 0.25920 0.17800 -0.00460 0.00820  0.04260  237  THR A CG2   
1854 N  N     . ALA A 238 ? 0.33840 0.13250 0.14810 0.03750  -0.01500 0.02680  238  ALA A N     
1855 C  CA    . ALA A 238 ? 0.30150 0.13790 0.13510 0.02720  -0.03260 0.02150  238  ALA A CA    
1856 C  C     . ALA A 238 ? 0.27400 0.12180 0.14480 -0.01120 -0.00740 0.01170  238  ALA A C     
1857 O  O     . ALA A 238 ? 0.27380 0.17240 0.18410 0.01570  -0.03490 0.00230  238  ALA A O     
1858 C  CB    . ALA A 238 ? 0.31890 0.15590 0.16240 0.03680  -0.01990 0.00710  238  ALA A CB    
1859 N  N     . MET A 239 ? 0.29450 0.13230 0.14730 0.03210  0.00280  0.00470  239  MET A N     
1860 C  CA    . MET A 239 ? 0.32150 0.15130 0.14110 0.00690  0.00330  0.03080  239  MET A CA    
1861 C  C     . MET A 239 ? 0.29320 0.11200 0.12940 0.02350  -0.00500 0.00230  239  MET A C     
1862 O  O     . MET A 239 ? 0.31010 0.16400 0.12610 0.00450  -0.01650 0.00380  239  MET A O     
1863 C  CB    . MET A 239 ? 0.32490 0.14970 0.16190 0.00620  0.02130  0.02090  239  MET A CB    
1864 C  CG    . MET A 239 ? 0.33630 0.22760 0.18590 -0.02380 0.02000  0.06790  239  MET A CG    
1865 S  SD    . MET A 239 ? 0.34500 0.25760 0.20100 0.00630  0.00590  0.05480  239  MET A SD    
1866 C  CE    . MET A 239 ? 0.34080 0.24590 0.21930 0.01050  0.02610  0.03830  239  MET A CE    
1867 N  N     . LEU A 240 ? 0.29870 0.11390 0.13240 0.03590  0.01310  -0.00360 240  LEU A N     
1868 C  CA    . LEU A 240 ? 0.29770 0.13990 0.13820 0.02850  -0.00370 -0.01220 240  LEU A CA    
1869 C  C     . LEU A 240 ? 0.24100 0.14600 0.12910 0.03010  0.00100  0.01990  240  LEU A C     
1870 O  O     . LEU A 240 ? 0.30690 0.16440 0.13600 0.03000  -0.02550 0.01580  240  LEU A O     
1871 C  CB    . LEU A 240 ? 0.30460 0.20270 0.14060 0.04120  -0.03880 -0.00870 240  LEU A CB    
1872 C  CG    . LEU A 240 ? 0.35080 0.20190 0.15900 0.07720  -0.03450 -0.00280 240  LEU A CG    
1873 C  CD1   . LEU A 240 ? 0.36710 0.18290 0.15630 0.06460  -0.05820 0.00300  240  LEU A CD1   
1874 C  CD2   . LEU A 240 ? 0.34040 0.21950 0.15710 0.04250  -0.02460 -0.05090 240  LEU A CD2   
1875 N  N     . LEU A 241 ? 0.27330 0.15760 0.13060 0.01470  0.01140  0.01930  241  LEU A N     
1876 C  CA    . LEU A 241 ? 0.29760 0.10540 0.11800 0.01550  -0.00500 0.01690  241  LEU A CA    
1877 C  C     . LEU A 241 ? 0.30350 0.12540 0.12450 0.05280  0.01960  -0.01680 241  LEU A C     
1878 O  O     . LEU A 241 ? 0.29910 0.15650 0.14450 0.02570  -0.01370 0.00120  241  LEU A O     
1879 C  CB    . LEU A 241 ? 0.32570 0.12500 0.13530 0.01180  0.02420  0.00580  241  LEU A CB    
1880 C  CG    . LEU A 241 ? 0.47260 0.13290 0.16220 -0.05990 0.04410  -0.01110 241  LEU A CG    
1881 C  CD1   . LEU A 241 ? 0.45650 0.25910 0.18800 0.02550  0.03240  0.04350  241  LEU A CD1   
1882 C  CD2   . LEU A 241 ? 0.54310 0.14060 0.18240 0.02080  0.07160  0.00480  241  LEU A CD2   
1883 N  N     . LEU A 242 ? 0.29760 0.11440 0.14290 0.04060  0.02520  -0.01770 242  LEU A N     
1884 C  CA    . LEU A 242 ? 0.28950 0.14270 0.15150 0.06250  0.02890  -0.00720 242  LEU A CA    
1885 C  C     . LEU A 242 ? 0.34120 0.17580 0.13160 0.02930  0.00490  -0.01890 242  LEU A C     
1886 O  O     . LEU A 242 ? 0.32480 0.20780 0.14060 0.00150  0.00810  -0.01280 242  LEU A O     
1887 C  CB    . LEU A 242 ? 0.30430 0.21130 0.18850 0.05300  0.03300  -0.04590 242  LEU A CB    
1888 C  CG    . LEU A 242 ? 0.29450 0.28310 0.21290 0.01500  -0.00550 -0.13030 242  LEU A CG    
1889 C  CD1   . LEU A 242 ? 0.39940 0.39050 0.25890 0.02140  0.02810  -0.12270 242  LEU A CD1   
1890 C  CD2   . LEU A 242 ? 0.35240 0.40100 0.23210 0.02840  0.04250  -0.11170 242  LEU A CD2   
1891 N  N     . ILE A 243 ? 0.32570 0.17810 0.14980 0.09010  -0.00590 0.00140  243  ILE A N     
1892 C  CA    . ILE A 243 ? 0.31320 0.16100 0.16170 0.02140  -0.02150 0.01300  243  ILE A CA    
1893 C  C     . ILE A 243 ? 0.28130 0.15120 0.15460 0.00130  -0.00960 -0.00060 243  ILE A C     
1894 O  O     . ILE A 243 ? 0.32320 0.20050 0.15030 0.05490  -0.02360 0.00120  243  ILE A O     
1895 C  CB    . ILE A 243 ? 0.26780 0.17150 0.19300 -0.00840 0.00280  0.04120  243  ILE A CB    
1896 C  CG1   . ILE A 243 ? 0.31130 0.21300 0.22620 -0.05060 0.00290  0.00740  243  ILE A CG1   
1897 C  CG2   . ILE A 243 ? 0.34310 0.20770 0.20750 -0.02910 0.01150  0.04810  243  ILE A CG2   
1898 C  CD1   . ILE A 243 ? 0.38650 0.22780 0.24880 -0.01790 0.01020  0.06760  243  ILE A CD1   
1899 N  N     . ALA A 244 ? 0.27580 0.13450 0.14950 0.02090  -0.01830 -0.00270 244  ALA A N     
1900 C  CA    . ALA A 244 ? 0.30580 0.12320 0.15190 0.01490  -0.00280 0.00270  244  ALA A CA    
1901 C  C     . ALA A 244 ? 0.31640 0.12340 0.14680 -0.00430 -0.01100 -0.00960 244  ALA A C     
1902 O  O     . ALA A 244 ? 0.39850 0.16070 0.17930 0.03120  -0.04580 -0.01720 244  ALA A O     
1903 C  CB    . ALA A 244 ? 0.32430 0.15990 0.14690 0.04120  -0.00220 -0.02360 244  ALA A CB    
1904 N  N     . GLY A 245 ? 0.29430 0.10670 0.14110 -0.01800 0.00280  -0.00410 245  GLY A N     
1905 C  CA    . GLY A 245 ? 0.35150 0.11620 0.16290 -0.02030 -0.03850 -0.02560 245  GLY A CA    
1906 C  C     . GLY A 245 ? 0.42310 0.13040 0.17400 0.01620  -0.06860 -0.01860 245  GLY A C     
1907 O  O     . GLY A 245 ? 0.46830 0.23000 0.21480 0.01370  -0.11680 -0.05880 245  GLY A O     
1908 N  N     A HIS A 246 ? 0.42720 0.15540 0.15240 0.06460  -0.02970 -0.02510 246  HIS A N     
1909 N  N     B HIS A 246 ? 0.42610 0.18150 0.14720 0.05690  -0.03590 -0.01300 246  HIS A N     
1910 C  CA    A HIS A 246 ? 0.38800 0.18840 0.14530 0.09790  -0.03230 -0.02610 246  HIS A CA    
1911 C  CA    B HIS A 246 ? 0.41370 0.22500 0.14790 0.07890  -0.01040 -0.01050 246  HIS A CA    
1912 C  C     A HIS A 246 ? 0.41790 0.16890 0.14290 0.03860  -0.00360 -0.01670 246  HIS A C     
1913 C  C     B HIS A 246 ? 0.33390 0.14360 0.15090 0.03370  0.01950  0.00010  246  HIS A C     
1914 O  O     A HIS A 246 ? 0.48300 0.22190 0.12590 0.00490  0.02850  -0.01470 246  HIS A O     
1915 O  O     B HIS A 246 ? 0.25890 0.16230 0.14840 0.03030  0.06880  -0.02130 246  HIS A O     
1916 C  CB    A HIS A 246 ? 0.31310 0.13950 0.16990 0.09250  -0.00660 -0.03450 246  HIS A CB    
1917 C  CB    B HIS A 246 ? 0.40130 0.18350 0.14760 0.05630  0.00110  -0.03570 246  HIS A CB    
1918 C  CG    A HIS A 246 ? 0.39480 0.17280 0.18250 0.10720  0.00330  -0.02590 246  HIS A CG    
1919 C  CG    B HIS A 246 ? 0.44170 0.22570 0.16270 0.07150  0.01150  -0.03200 246  HIS A CG    
1920 N  ND1   A HIS A 246 ? 0.43160 0.17480 0.19080 0.10740  -0.01980 0.00830  246  HIS A ND1   
1921 N  ND1   B HIS A 246 ? 0.45420 0.17580 0.17380 0.01820  0.00430  -0.02420 246  HIS A ND1   
1922 C  CD2   A HIS A 246 ? 0.39510 0.18250 0.18680 0.07520  0.02150  -0.02730 246  HIS A CD2   
1923 C  CD2   B HIS A 246 ? 0.46660 0.15050 0.17430 0.07550  -0.01660 -0.01410 246  HIS A CD2   
1924 C  CE1   A HIS A 246 ? 0.42630 0.20950 0.18730 0.02870  0.00890  0.01680  246  HIS A CE1   
1925 C  CE1   B HIS A 246 ? 0.43970 0.14650 0.16470 0.04750  0.01400  -0.03240 246  HIS A CE1   
1926 N  NE2   A HIS A 246 ? 0.37509 0.16081 0.19150 0.10289  0.03130  -0.02589 246  HIS A NE2   
1927 N  NE2   B HIS A 246 ? 0.40930 0.17780 0.17800 0.09180  -0.00170 -0.01740 246  HIS A NE2   
1928 N  N     . GLU A 247 ? 0.32450 0.15540 0.15410 0.05240  0.00180  -0.00810 247  GLU A N     
1929 C  CA    . GLU A 247 ? 0.35320 0.14810 0.14840 0.05130  -0.00390 0.02670  247  GLU A CA    
1930 C  C     . GLU A 247 ? 0.30610 0.17170 0.09690 0.05360  -0.00310 0.01800  247  GLU A C     
1931 O  O     . GLU A 247 ? 0.35107 0.22450 0.10273 0.05699  -0.01930 0.02649  247  GLU A O     
1932 C  CB    . GLU A 247 ? 0.33640 0.19200 0.19860 0.03060  0.02310  -0.00640 247  GLU A CB    
1933 C  CG    . GLU A 247 ? 0.34170 0.28280 0.19570 0.04480  0.07040  0.01330  247  GLU A CG    
1934 C  CD    . GLU A 247 ? 0.41470 0.33470 0.19370 0.13940  0.04740  0.05890  247  GLU A CD    
1935 O  OE1   . GLU A 247 ? 0.42280 0.37180 0.19620 0.10410  0.05060  0.07190  247  GLU A OE1   
1936 O  OE2   . GLU A 247 ? 0.44960 0.39040 0.19710 0.13800  0.06050  0.04190  247  GLU A OE2   
1937 N  N     . THR A 248 ? 0.29020 0.13260 0.11200 0.05190  0.01890  -0.01180 248  THR A N     
1938 C  CA    . THR A 248 ? 0.31150 0.11400 0.10540 0.01720  0.02370  -0.01010 248  THR A CA    
1939 C  C     . THR A 248 ? 0.31960 0.08720 0.10500 0.01010  0.01960  0.01090  248  THR A C     
1940 O  O     . THR A 248 ? 0.39240 0.13750 0.10850 0.03550  -0.02200 0.00610  248  THR A O     
1941 C  CB    . THR A 248 ? 0.33980 0.13880 0.11070 -0.01730 0.01060  -0.01810 248  THR A CB    
1942 O  OG1   . THR A 248 ? 0.33530 0.15440 0.11730 0.00150  0.01870  -0.00870 248  THR A OG1   
1943 C  CG2   . THR A 248 ? 0.36540 0.16560 0.15790 -0.03390 0.00760  -0.03530 248  THR A CG2   
1944 N  N     . THR A 249 ? 0.32610 0.09710 0.10620 -0.00190 -0.00720 0.00280  249  THR A N     
1945 C  CA    . THR A 249 ? 0.34520 0.12240 0.12310 0.00650  -0.03160 0.01460  249  THR A CA    
1946 C  C     . THR A 249 ? 0.33300 0.13230 0.11850 -0.01100 0.00240  -0.01360 249  THR A C     
1947 O  O     . THR A 249 ? 0.33820 0.16650 0.14360 0.02200  -0.01980 -0.03560 249  THR A O     
1948 C  CB    . THR A 249 ? 0.35310 0.14280 0.14970 0.00520  -0.01090 -0.00520 249  THR A CB    
1949 O  OG1   . THR A 249 ? 0.41030 0.13520 0.13870 0.02270  0.01620  -0.00440 249  THR A OG1   
1950 C  CG2   . THR A 249 ? 0.35110 0.17640 0.15590 0.00350  -0.00250 -0.04270 249  THR A CG2   
1951 N  N     . ALA A 250 ? 0.31780 0.17030 0.11630 0.03680  0.02840  -0.00760 250  ALA A N     
1952 C  CA    . ALA A 250 ? 0.33980 0.20400 0.12380 0.09690  0.03660  -0.02220 250  ALA A CA    
1953 C  C     . ALA A 250 ? 0.33760 0.15290 0.12980 0.06670  -0.00320 -0.00910 250  ALA A C     
1954 O  O     . ALA A 250 ? 0.40090 0.16170 0.12810 0.05430  -0.02570 -0.03500 250  ALA A O     
1955 C  CB    . ALA A 250 ? 0.34890 0.18590 0.12470 0.07140  0.03420  -0.03330 250  ALA A CB    
1956 N  N     . SER A 251 ? 0.37930 0.13690 0.14370 0.05530  -0.01370 -0.02000 251  SER A N     
1957 C  CA    . SER A 251 ? 0.31240 0.11640 0.17650 0.00910  -0.00380 0.00970  251  SER A CA    
1958 C  C     . SER A 251 ? 0.35320 0.14490 0.14370 0.00350  -0.01210 0.02520  251  SER A C     
1959 O  O     . SER A 251 ? 0.38780 0.20100 0.12710 0.02410  -0.02680 0.01530  251  SER A O     
1960 C  CB    . SER A 251 ? 0.33620 0.16070 0.22550 -0.01260 0.02320  -0.01140 251  SER A CB    
1961 O  OG    . SER A 251 ? 0.40270 0.24470 0.26690 -0.00600 0.02770  -0.02690 251  SER A OG    
1962 N  N     . MET A 252 ? 0.31280 0.13760 0.13610 0.00730  0.00450  0.02510  252  MET A N     
1963 C  CA    . MET A 252 ? 0.31660 0.19670 0.13520 0.02530  -0.01640 0.00390  252  MET A CA    
1964 C  C     . MET A 252 ? 0.32050 0.18580 0.12950 0.03010  -0.01000 -0.00910 252  MET A C     
1965 O  O     . MET A 252 ? 0.35000 0.20550 0.13700 0.03920  -0.02920 -0.00150 252  MET A O     
1966 C  CB    . MET A 252 ? 0.38140 0.16540 0.12390 0.01360  0.01320  0.00250  252  MET A CB    
1967 C  CG    . MET A 252 ? 0.39020 0.14460 0.13830 0.03890  -0.02420 -0.00120 252  MET A CG    
1968 S  SD    . MET A 252 ? 0.35550 0.15870 0.14310 0.03810  0.00160  0.01020  252  MET A SD    
1969 C  CE    . MET A 252 ? 0.36840 0.18920 0.14360 0.07390  -0.03680 -0.02910 252  MET A CE    
1970 N  N     . THR A 253 ? 0.34610 0.16870 0.12070 0.06240  -0.00700 -0.02800 253  THR A N     
1971 C  CA    . THR A 253 ? 0.40446 0.13452 0.12492 0.05089  -0.02460 -0.02438 253  THR A CA    
1972 C  C     . THR A 253 ? 0.37770 0.17240 0.12140 0.08250  -0.01220 -0.00860 253  THR A C     
1973 O  O     . THR A 253 ? 0.43310 0.22250 0.14990 0.07400  -0.03520 -0.01210 253  THR A O     
1974 C  CB    . THR A 253 ? 0.39160 0.13260 0.13300 0.04500  -0.01800 -0.02860 253  THR A CB    
1975 O  OG1   . THR A 253 ? 0.40710 0.18380 0.12410 0.02170  -0.04060 -0.00280 253  THR A OG1   
1976 C  CG2   . THR A 253 ? 0.40580 0.15460 0.14110 0.04160  -0.01590 -0.03690 253  THR A CG2   
1977 N  N     . SER A 254 ? 0.39890 0.19520 0.12320 0.07610  -0.01240 0.00710  254  SER A N     
1978 C  CA    A SER A 254 ? 0.41330 0.19810 0.12000 0.04290  -0.00550 -0.00530 254  SER A CA    
1979 C  CA    B SER A 254 ? 0.40670 0.21170 0.12470 0.06720  -0.00100 -0.00580 254  SER A CA    
1980 C  C     . SER A 254 ? 0.40340 0.20750 0.11510 0.04900  -0.04120 -0.01970 254  SER A C     
1981 O  O     . SER A 254 ? 0.47110 0.27240 0.13740 0.05740  -0.04700 -0.01610 254  SER A O     
1982 C  CB    A SER A 254 ? 0.44280 0.20390 0.14170 0.00420  -0.00780 -0.01070 254  SER A CB    
1983 C  CB    B SER A 254 ? 0.42480 0.22730 0.15470 0.05730  0.00980  -0.00530 254  SER A CB    
1984 O  OG    A SER A 254 ? 0.46700 0.23810 0.15140 0.05220  -0.01080 0.02280  254  SER A OG    
1985 O  OG    B SER A 254 ? 0.42210 0.20810 0.17150 0.06110  0.01960  -0.00170 254  SER A OG    
1986 N  N     . LEU A 255 ? 0.38620 0.17870 0.12110 0.06030  0.00570  -0.01350 255  LEU A N     
1987 C  CA    . LEU A 255 ? 0.39430 0.19360 0.13920 0.07220  0.00040  -0.01840 255  LEU A CA    
1988 C  C     . LEU A 255 ? 0.40250 0.18850 0.13200 0.07810  -0.03250 -0.00690 255  LEU A C     
1989 O  O     . LEU A 255 ? 0.44330 0.22320 0.13070 0.09970  -0.02910 0.00600  255  LEU A O     
1990 C  CB    . LEU A 255 ? 0.44890 0.16850 0.13120 0.03330  -0.00740 -0.01320 255  LEU A CB    
1991 C  CG    . LEU A 255 ? 0.49600 0.20270 0.13510 -0.01530 0.00280  -0.00060 255  LEU A CG    
1992 C  CD1   . LEU A 255 ? 0.45430 0.21920 0.15300 -0.00270 0.01500  -0.02720 255  LEU A CD1   
1993 C  CD2   . LEU A 255 ? 0.59730 0.31850 0.16500 -0.06390 -0.02530 0.04330  255  LEU A CD2   
1994 N  N     . SER A 256 ? 0.39160 0.21080 0.11100 0.06130  -0.04300 -0.01430 256  SER A N     
1995 C  CA    . SER A 256 ? 0.38030 0.23280 0.11730 0.04740  -0.06190 0.00540  256  SER A CA    
1996 C  C     . SER A 256 ? 0.41810 0.23090 0.12630 0.08650  -0.05620 -0.00900 256  SER A C     
1997 O  O     . SER A 256 ? 0.42430 0.25350 0.13800 0.08420  -0.07370 -0.02980 256  SER A O     
1998 C  CB    . SER A 256 ? 0.40720 0.21170 0.12060 0.01770  -0.02670 0.01550  256  SER A CB    
1999 O  OG    . SER A 256 ? 0.38770 0.23000 0.11860 0.04780  -0.02550 -0.00680 256  SER A OG    
2000 N  N     . VAL A 257 ? 0.39990 0.24870 0.13720 0.06540  -0.04540 -0.06080 257  VAL A N     
2001 C  CA    . VAL A 257 ? 0.42260 0.22590 0.14650 0.07370  -0.03430 -0.06020 257  VAL A CA    
2002 C  C     . VAL A 257 ? 0.46940 0.24320 0.15630 0.10260  -0.05330 -0.05380 257  VAL A C     
2003 O  O     . VAL A 257 ? 0.49230 0.33710 0.16620 0.10000  -0.07160 -0.05950 257  VAL A O     
2004 C  CB    . VAL A 257 ? 0.42868 0.26500 0.14352 0.10219  -0.04210 -0.05509 257  VAL A CB    
2005 C  CG1   . VAL A 257 ? 0.41680 0.31930 0.15030 0.07650  -0.03110 -0.06700 257  VAL A CG1   
2006 C  CG2   . VAL A 257 ? 0.48107 0.36190 0.14063 0.04979  -0.06689 -0.01400 257  VAL A CG2   
2007 N  N     . ILE A 258 ? 0.46850 0.24410 0.14750 0.09710  -0.02760 -0.03270 258  ILE A N     
2008 C  CA    . ILE A 258 ? 0.48120 0.25390 0.15580 0.13820  -0.02850 0.01100  258  ILE A CA    
2009 C  C     . ILE A 258 ? 0.47600 0.25150 0.14630 0.11460  -0.05030 0.00640  258  ILE A C     
2010 O  O     . ILE A 258 ? 0.50708 0.30430 0.15622 0.12819  -0.05939 -0.00440 258  ILE A O     
2011 C  CB    . ILE A 258 ? 0.44600 0.29000 0.15340 0.11230  -0.02100 0.02310  258  ILE A CB    
2012 C  CG1   . ILE A 258 ? 0.45420 0.36770 0.14310 0.07670  -0.03320 0.00440  258  ILE A CG1   
2013 C  CG2   . ILE A 258 ? 0.47160 0.32680 0.14800 0.09130  -0.01190 0.03760  258  ILE A CG2   
2014 C  CD1   . ILE A 258 ? 0.46500 0.35290 0.13560 0.03200  -0.03560 -0.03060 258  ILE A CD1   
2015 N  N     . THR A 259 ? 0.46589 0.28770 0.13011 0.09410  -0.02120 -0.02090 259  THR A N     
2016 C  CA    . THR A 259 ? 0.46510 0.28360 0.13220 0.09590  -0.02660 -0.02610 259  THR A CA    
2017 C  C     . THR A 259 ? 0.47200 0.27440 0.14420 0.08110  -0.06310 -0.01860 259  THR A C     
2018 O  O     . THR A 259 ? 0.51250 0.29970 0.15910 0.13120  -0.05840 0.00090  259  THR A O     
2019 C  CB    . THR A 259 ? 0.46320 0.23580 0.12950 0.06720  -0.02430 -0.03080 259  THR A CB    
2020 O  OG1   . THR A 259 ? 0.47230 0.21230 0.13030 0.06570  -0.03220 0.01310  259  THR A OG1   
2021 C  CG2   . THR A 259 ? 0.47979 0.21770 0.13191 0.07590  -0.02660 -0.02350 259  THR A CG2   
2022 N  N     . LEU A 260 ? 0.43210 0.25520 0.16390 0.07710  -0.06030 -0.05230 260  LEU A N     
2023 C  CA    . LEU A 260 ? 0.43640 0.18970 0.15810 0.06980  -0.07390 -0.05070 260  LEU A CA    
2024 C  C     . LEU A 260 ? 0.45760 0.30080 0.15710 0.09310  -0.07680 -0.05440 260  LEU A C     
2025 O  O     . LEU A 260 ? 0.48660 0.29880 0.20890 0.08120  -0.09980 -0.05250 260  LEU A O     
2026 C  CB    . LEU A 260 ? 0.48128 0.19361 0.16541 0.12459  -0.06490 -0.03859 260  LEU A CB    
2027 C  CG    . LEU A 260 ? 0.46810 0.22130 0.18170 0.13640  -0.01650 -0.02890 260  LEU A CG    
2028 C  CD1   . LEU A 260 ? 0.46540 0.21850 0.18130 0.08020  -0.06670 0.01880  260  LEU A CD1   
2029 C  CD2   . LEU A 260 ? 0.53210 0.23410 0.17980 0.05900  -0.01370 -0.01540 260  LEU A CD2   
2030 N  N     . LEU A 261 ? 0.51650 0.31360 0.16950 0.13840  -0.06740 -0.05200 261  LEU A N     
2031 C  CA    . LEU A 261 ? 0.52340 0.34300 0.16580 0.14200  -0.06510 -0.03580 261  LEU A CA    
2032 C  C     . LEU A 261 ? 0.54230 0.34870 0.18040 0.15770  -0.07870 -0.04800 261  LEU A C     
2033 O  O     . LEU A 261 ? 0.55320 0.37990 0.19980 0.19260  -0.09390 -0.05790 261  LEU A O     
2034 C  CB    . LEU A 261 ? 0.56637 0.34919 0.15954 0.11359  -0.03569 -0.02649 261  LEU A CB    
2035 C  CG    . LEU A 261 ? 0.61470 0.37580 0.18650 0.09280  -0.02750 -0.07070 261  LEU A CG    
2036 C  CD1   . LEU A 261 ? 0.57297 0.38690 0.18293 0.12978  -0.00410 -0.06569 261  LEU A CD1   
2037 C  CD2   . LEU A 261 ? 0.62706 0.30141 0.20263 0.13508  -0.02930 -0.06148 261  LEU A CD2   
2038 N  N     . ASP A 262 ? 0.49730 0.33340 0.17390 0.14160  -0.08810 -0.04690 262  ASP A N     
2039 C  CA    . ASP A 262 ? 0.50570 0.33870 0.18810 0.14200  -0.09360 0.00350  262  ASP A CA    
2040 C  C     . ASP A 262 ? 0.50228 0.33590 0.19553 0.14888  -0.08778 0.01639  262  ASP A C     
2041 O  O     . ASP A 262 ? 0.58190 0.36650 0.21220 0.14850  -0.09220 0.02680  262  ASP A O     
2042 C  CB    . ASP A 262 ? 0.59057 0.36370 0.18003 0.12209  -0.07949 -0.00870 262  ASP A CB    
2043 C  CG    . ASP A 262 ? 0.65070 0.38620 0.18840 0.07730  -0.05690 -0.01810 262  ASP A CG    
2044 O  OD1   . ASP A 262 ? 0.62060 0.40300 0.18430 0.12750  -0.02770 -0.00610 262  ASP A OD1   
2045 O  OD2   . ASP A 262 ? 0.68129 0.40510 0.19051 0.07820  -0.05530 -0.04710 262  ASP A OD2   
2046 N  N     . HIS A 263 ? 0.49057 0.33840 0.17143 0.06829  -0.10838 -0.03169 263  HIS A N     
2047 C  CA    . HIS A 263 ? 0.49438 0.33130 0.18382 0.09429  -0.11428 -0.04989 263  HIS A CA    
2048 C  C     . HIS A 263 ? 0.52296 0.34499 0.19795 0.09098  -0.12407 -0.05868 263  HIS A C     
2049 O  O     . HIS A 263 ? 0.49890 0.30990 0.20590 0.10190  -0.11580 -0.05370 263  HIS A O     
2050 C  CB    . HIS A 263 ? 0.49479 0.31240 0.17891 0.06110  -0.11409 -0.04530 263  HIS A CB    
2051 C  CG    . HIS A 263 ? 0.50550 0.30830 0.17580 0.10070  -0.08850 -0.06180 263  HIS A CG    
2052 N  ND1   . HIS A 263 ? 0.53629 0.28340 0.16461 0.10450  -0.08060 -0.02640 263  HIS A ND1   
2053 C  CD2   . HIS A 263 ? 0.54738 0.29370 0.17942 0.13599  -0.09289 -0.02460 263  HIS A CD2   
2054 C  CE1   . HIS A 263 ? 0.53090 0.27340 0.16740 0.13390  -0.06450 -0.03400 263  HIS A CE1   
2055 N  NE2   . HIS A 263 ? 0.55200 0.30740 0.18080 0.13120  -0.05790 -0.02290 263  HIS A NE2   
2056 N  N     . PRO A 264 ? 0.51040 0.36780 0.20860 0.09880  -0.13470 -0.06390 264  PRO A N     
2057 C  CA    . PRO A 264 ? 0.55340 0.38700 0.21860 0.04960  -0.14260 -0.06670 264  PRO A CA    
2058 C  C     . PRO A 264 ? 0.57900 0.41580 0.25160 0.09950  -0.17340 -0.06260 264  PRO A C     
2059 O  O     . PRO A 264 ? 0.61638 0.46999 0.26023 0.12668  -0.17537 -0.04919 264  PRO A O     
2060 C  CB    . PRO A 264 ? 0.58640 0.39210 0.21460 0.06090  -0.13970 -0.04170 264  PRO A CB    
2061 C  CG    . PRO A 264 ? 0.52020 0.38820 0.22310 0.06910  -0.15710 -0.04670 264  PRO A CG    
2062 C  CD    . PRO A 264 ? 0.51068 0.37819 0.19622 0.11059  -0.12448 -0.03300 264  PRO A CD    
2063 N  N     . GLU A 265 ? 0.59230 0.42540 0.26670 0.13100  -0.18160 -0.03240 265  GLU A N     
2064 C  CA    . GLU A 265 ? 0.59530 0.47350 0.30760 0.13420  -0.17930 -0.02640 265  GLU A CA    
2065 C  C     . GLU A 265 ? 0.55190 0.47120 0.32240 0.13290  -0.16060 -0.03890 265  GLU A C     
2066 O  O     . GLU A 265 ? 0.53570 0.41950 0.34560 0.05290  -0.16220 -0.04420 265  GLU A O     
2067 C  CB    . GLU A 265 ? 0.69600 0.55410 0.34430 0.13870  -0.15760 0.01610  265  GLU A CB    
2068 C  CG    . GLU A 265 ? 0.87990 0.64970 0.39100 0.11710  -0.09890 0.04220  265  GLU A CG    
2069 C  CD    . GLU A 265 ? 1.03750 0.72970 0.43560 0.07720  -0.03490 0.07710  265  GLU A CD    
2070 O  OE1   . GLU A 265 ? 1.06580 0.75290 0.44450 0.03370  -0.01210 0.07470  265  GLU A OE1   
2071 O  OE2   . GLU A 265 ? 1.12710 0.74490 0.46110 0.08920  -0.02590 0.08690  265  GLU A OE2   
2072 N  N     . GLN A 266 ? 0.52100 0.42270 0.28550 0.18750  -0.17360 -0.05380 266  GLN A N     
2073 C  CA    . GLN A 266 ? 0.50100 0.37900 0.27130 0.15820  -0.17629 -0.05920 266  GLN A CA    
2074 C  C     . GLN A 266 ? 0.48840 0.37370 0.26230 0.13070  -0.17440 -0.08490 266  GLN A C     
2075 O  O     . GLN A 266 ? 0.51330 0.39690 0.27410 0.09970  -0.15040 -0.09750 266  GLN A O     
2076 C  CB    . GLN A 266 ? 0.56940 0.30490 0.27020 0.12660  -0.16540 -0.03570 266  GLN A CB    
2077 C  CG    . GLN A 266 ? 0.61610 0.27590 0.27490 0.12340  -0.14230 -0.03430 266  GLN A CG    
2078 C  CD    . GLN A 266 ? 0.57140 0.23140 0.26310 0.09110  -0.15130 -0.02490 266  GLN A CD    
2079 O  OE1   . GLN A 266 ? 0.60960 0.30300 0.24390 0.10920  -0.11150 -0.02200 266  GLN A OE1   
2080 N  NE2   . GLN A 266 ? 0.58990 0.27720 0.28090 0.05510  -0.12940 0.01070  266  GLN A NE2   
2081 N  N     . TYR A 267 ? 0.50210 0.33740 0.26880 0.14260  -0.18160 -0.07720 267  TYR A N     
2082 C  CA    . TYR A 267 ? 0.48379 0.35460 0.28301 0.12200  -0.17479 -0.11819 267  TYR A CA    
2083 C  C     . TYR A 267 ? 0.50570 0.37880 0.28620 0.04330  -0.17840 -0.10830 267  TYR A C     
2084 O  O     . TYR A 267 ? 0.50830 0.40300 0.28380 0.05650  -0.17800 -0.09810 267  TYR A O     
2085 C  CB    . TYR A 267 ? 0.47740 0.32970 0.28500 0.11690  -0.15060 -0.13500 267  TYR A CB    
2086 C  CG    . TYR A 267 ? 0.48889 0.33380 0.29390 0.11040  -0.14330 -0.14339 267  TYR A CG    
2087 C  CD1   . TYR A 267 ? 0.50597 0.26492 0.31121 0.12578  -0.13108 -0.12337 267  TYR A CD1   
2088 C  CD2   . TYR A 267 ? 0.55939 0.38000 0.29621 0.12100  -0.12430 -0.15439 267  TYR A CD2   
2089 C  CE1   . TYR A 267 ? 0.55110 0.29670 0.31050 0.09640  -0.12130 -0.13350 267  TYR A CE1   
2090 C  CE2   . TYR A 267 ? 0.55160 0.39090 0.30370 0.13930  -0.11860 -0.13170 267  TYR A CE2   
2091 C  CZ    . TYR A 267 ? 0.49850 0.38340 0.31470 0.19870  -0.11230 -0.12460 267  TYR A CZ    
2092 O  OH    . TYR A 267 ? 0.52490 0.44230 0.31500 0.17700  -0.09600 -0.13500 267  TYR A OH    
2093 N  N     . ALA A 268 ? 0.50610 0.37520 0.28760 0.04230  -0.19080 -0.09050 268  ALA A N     
2094 C  CA    . ALA A 268 ? 0.53780 0.43290 0.29730 0.06460  -0.21100 -0.06350 268  ALA A CA    
2095 C  C     . ALA A 268 ? 0.56940 0.43320 0.32980 0.11310  -0.21130 -0.06590 268  ALA A C     
2096 O  O     . ALA A 268 ? 0.55820 0.45770 0.34030 0.11040  -0.23390 -0.07370 268  ALA A O     
2097 C  CB    . ALA A 268 ? 0.57128 0.49140 0.30242 -0.00920 -0.22087 -0.03720 268  ALA A CB    
2098 N  N     . ALA A 269 ? 0.54100 0.36100 0.33920 0.10580  -0.19210 -0.08940 269  ALA A N     
2099 C  CA    . ALA A 269 ? 0.51170 0.39640 0.35940 0.08500  -0.20170 -0.07290 269  ALA A CA    
2100 C  C     . ALA A 269 ? 0.47190 0.46330 0.37820 0.02610  -0.19170 -0.04530 269  ALA A C     
2101 O  O     . ALA A 269 ? 0.45500 0.48760 0.39040 0.00480  -0.20220 -0.04090 269  ALA A O     
2102 C  CB    . ALA A 269 ? 0.49470 0.33680 0.36220 0.09870  -0.19690 -0.07570 269  ALA A CB    
2103 N  N     . LEU A 270 ? 0.44710 0.41000 0.37250 0.04290  -0.22790 -0.05820 270  LEU A N     
2104 C  CA    . LEU A 270 ? 0.44730 0.38410 0.36750 0.03280  -0.22070 -0.08680 270  LEU A CA    
2105 C  C     . LEU A 270 ? 0.49740 0.38900 0.38620 0.04570  -0.21580 -0.10590 270  LEU A C     
2106 O  O     . LEU A 270 ? 0.48780 0.41840 0.38800 -0.00240 -0.22110 -0.09970 270  LEU A O     
2107 C  CB    . LEU A 270 ? 0.44610 0.38800 0.34290 0.06410  -0.21410 -0.05010 270  LEU A CB    
2108 C  CG    . LEU A 270 ? 0.47960 0.36620 0.33360 0.02080  -0.19330 -0.03800 270  LEU A CG    
2109 C  CD1   . LEU A 270 ? 0.53710 0.35820 0.32330 0.01580  -0.12850 -0.05790 270  LEU A CD1   
2110 C  CD2   . LEU A 270 ? 0.42010 0.39970 0.34470 -0.08280 -0.17290 -0.02280 270  LEU A CD2   
2111 N  N     . ARG A 271 ? 0.49160 0.33870 0.38700 0.05210  -0.22339 -0.12569 271  ARG A N     
2112 C  CA    A ARG A 271 ? 0.52750 0.36290 0.40160 0.06690  -0.22370 -0.12340 271  ARG A CA    
2113 C  CA    B ARG A 271 ? 0.51928 0.34441 0.40061 0.03740  -0.22696 -0.12797 271  ARG A CA    
2114 C  C     . ARG A 271 ? 0.51470 0.35380 0.41910 0.04780  -0.22020 -0.11320 271  ARG A C     
2115 O  O     . ARG A 271 ? 0.53190 0.33530 0.42180 0.03590  -0.21740 -0.11770 271  ARG A O     
2116 C  CB    A ARG A 271 ? 0.55450 0.38540 0.40250 0.11730  -0.21550 -0.13500 271  ARG A CB    
2117 C  CB    B ARG A 271 ? 0.51920 0.33700 0.40320 0.02840  -0.21490 -0.13570 271  ARG A CB    
2118 C  CG    A ARG A 271 ? 0.57740 0.46490 0.41600 0.15340  -0.20720 -0.11580 271  ARG A CG    
2119 C  CG    B ARG A 271 ? 0.53109 0.37470 0.41630 0.02150  -0.23258 -0.13289 271  ARG A CG    
2120 C  CD    A ARG A 271 ? 0.61420 0.52730 0.42850 0.18790  -0.17650 -0.10240 271  ARG A CD    
2121 C  CD    B ARG A 271 ? 0.56990 0.41760 0.42470 -0.00520 -0.23000 -0.14430 271  ARG A CD    
2122 N  NE    A ARG A 271 ? 0.64770 0.55540 0.44220 0.22770  -0.15600 -0.08810 271  ARG A NE    
2123 N  NE    B ARG A 271 ? 0.63220 0.44690 0.45040 0.02450  -0.18790 -0.12000 271  ARG A NE    
2124 C  CZ    A ARG A 271 ? 0.63850 0.59120 0.43850 0.22500  -0.18320 -0.08460 271  ARG A CZ    
2125 C  CZ    B ARG A 271 ? 0.65220 0.45630 0.46680 0.04440  -0.15610 -0.11120 271  ARG A CZ    
2126 N  NH1   A ARG A 271 ? 0.60580 0.59580 0.42980 0.22860  -0.23280 -0.08760 271  ARG A NH1   
2127 N  NH1   B ARG A 271 ? 0.68220 0.44590 0.48540 0.04960  -0.11780 -0.11070 271  ARG A NH1   
2128 N  NH2   A ARG A 271 ? 0.63250 0.57850 0.43790 0.21550  -0.17530 -0.09640 271  ARG A NH2   
2129 N  NH2   B ARG A 271 ? 0.62290 0.45650 0.45430 0.02900  -0.16400 -0.12470 271  ARG A NH2   
2130 N  N     . ALA A 272 ? 0.51470 0.38570 0.45030 0.02740  -0.23190 -0.07680 272  ALA A N     
2131 C  CA    . ALA A 272 ? 0.52880 0.35450 0.47380 -0.03910 -0.25410 -0.06130 272  ALA A CA    
2132 C  C     . ALA A 272 ? 0.57150 0.37420 0.48380 -0.03200 -0.27830 -0.05630 272  ALA A C     
2133 O  O     . ALA A 272 ? 0.62160 0.40680 0.50070 -0.03200 -0.29130 -0.05640 272  ALA A O     
2134 C  CB    . ALA A 272 ? 0.49900 0.36590 0.48250 0.02660  -0.24700 -0.05160 272  ALA A CB    
2135 N  N     . ASP A 273 ? 0.54360 0.37140 0.47370 -0.00320 -0.27530 -0.03840 273  ASP A N     
2136 C  CA    . ASP A 273 ? 0.47210 0.41830 0.47260 0.01190  -0.23760 -0.04370 273  ASP A CA    
2137 C  C     . ASP A 273 ? 0.43160 0.33050 0.45140 -0.01190 -0.21100 -0.05550 273  ASP A C     
2138 O  O     . ASP A 273 ? 0.40700 0.31730 0.45750 0.01340  -0.17990 -0.04920 273  ASP A O     
2139 C  CB    . ASP A 273 ? 0.44960 0.47940 0.49580 0.01410  -0.21020 -0.02660 273  ASP A CB    
2140 C  CG    . ASP A 273 ? 0.47140 0.55950 0.53820 0.00490  -0.13500 -0.02410 273  ASP A CG    
2141 O  OD1   . ASP A 273 ? 0.44590 0.53680 0.53940 -0.05790 -0.11130 -0.01100 273  ASP A OD1   
2142 O  OD2   . ASP A 273 ? 0.46240 0.61620 0.55690 0.08280  -0.08360 -0.04110 273  ASP A OD2   
2143 N  N     . ARG A 274 ? 0.46850 0.28180 0.43970 0.02290  -0.20000 -0.05090 274  ARG A N     
2144 C  CA    . ARG A 274 ? 0.44030 0.24060 0.41390 0.00400  -0.21180 -0.04800 274  ARG A CA    
2145 C  C     . ARG A 274 ? 0.41220 0.23430 0.41350 0.00540  -0.17580 -0.06590 274  ARG A C     
2146 O  O     . ARG A 274 ? 0.38920 0.26580 0.42230 -0.03260 -0.16810 -0.06370 274  ARG A O     
2147 C  CB    . ARG A 274 ? 0.48580 0.29030 0.41600 -0.00500 -0.15680 -0.07120 274  ARG A CB    
2148 C  CG    . ARG A 274 ? 0.46520 0.32560 0.40450 0.01510  -0.14050 -0.08840 274  ARG A CG    
2149 C  CD    . ARG A 274 ? 0.43640 0.33090 0.39490 0.00370  -0.13660 -0.14150 274  ARG A CD    
2150 N  NE    . ARG A 274 ? 0.44270 0.37760 0.39060 0.00020  -0.16610 -0.16120 274  ARG A NE    
2151 C  CZ    . ARG A 274 ? 0.44410 0.33330 0.38320 0.02670  -0.16140 -0.14390 274  ARG A CZ    
2152 N  NH1   . ARG A 274 ? 0.48810 0.28330 0.37980 0.00510  -0.17160 -0.12620 274  ARG A NH1   
2153 N  NH2   . ARG A 274 ? 0.50870 0.35510 0.36900 0.07340  -0.12870 -0.13290 274  ARG A NH2   
2154 N  N     . SER A 275 ? 0.42270 0.25590 0.40650 -0.01260 -0.14810 -0.08390 275  SER A N     
2155 C  CA    . SER A 275 ? 0.38030 0.28920 0.42080 -0.03990 -0.09450 -0.07710 275  SER A CA    
2156 C  C     . SER A 275 ? 0.37620 0.24990 0.39980 -0.04450 -0.08470 -0.06200 275  SER A C     
2157 O  O     . SER A 275 ? 0.39700 0.27270 0.36750 -0.08410 -0.08960 -0.05130 275  SER A O     
2158 C  CB    . SER A 275 ? 0.34440 0.31250 0.44380 -0.03400 -0.08840 -0.06470 275  SER A CB    
2159 O  OG    . SER A 275 ? 0.34580 0.42220 0.46580 -0.02770 -0.08800 -0.06010 275  SER A OG    
2160 N  N     . LEU A 276 ? 0.36440 0.26540 0.40820 -0.01540 -0.10790 -0.04590 276  LEU A N     
2161 C  CA    . LEU A 276 ? 0.33360 0.19980 0.39370 -0.01600 -0.11840 -0.04740 276  LEU A CA    
2162 C  C     . LEU A 276 ? 0.33970 0.20220 0.33410 0.01080  -0.10380 -0.03600 276  LEU A C     
2163 O  O     . LEU A 276 ? 0.37480 0.19250 0.30660 -0.00580 -0.09160 -0.02880 276  LEU A O     
2164 C  CB    . LEU A 276 ? 0.37070 0.25810 0.42350 -0.01660 -0.15790 -0.03790 276  LEU A CB    
2165 C  CG    . LEU A 276 ? 0.39640 0.32330 0.44980 -0.00150 -0.13450 -0.02860 276  LEU A CG    
2166 C  CD1   . LEU A 276 ? 0.43280 0.32130 0.44950 -0.01880 -0.14010 0.01690  276  LEU A CD1   
2167 C  CD2   . LEU A 276 ? 0.37310 0.31320 0.46430 0.07100  -0.09030 -0.03300 276  LEU A CD2   
2168 N  N     . VAL A 277 ? 0.38000 0.21650 0.29830 0.03250  -0.09170 -0.03120 277  VAL A N     
2169 C  CA    . VAL A 277 ? 0.32070 0.24660 0.27810 0.04480  -0.09090 -0.03570 277  VAL A CA    
2170 C  C     . VAL A 277 ? 0.31300 0.19590 0.25660 0.01890  -0.10050 -0.04100 277  VAL A C     
2171 O  O     . VAL A 277 ? 0.31300 0.21880 0.24810 0.03190  -0.06540 -0.03680 277  VAL A O     
2172 C  CB    . VAL A 277 ? 0.32760 0.22370 0.29140 0.05730  -0.13020 -0.04290 277  VAL A CB    
2173 C  CG1   . VAL A 277 ? 0.33560 0.25250 0.30060 0.05250  -0.11870 -0.02840 277  VAL A CG1   
2174 C  CG2   . VAL A 277 ? 0.37760 0.21150 0.28770 -0.00180 -0.14220 -0.06260 277  VAL A CG2   
2175 N  N     . PRO A 278 ? 0.35560 0.22270 0.25890 -0.01290 -0.09260 -0.02860 278  PRO A N     
2176 C  CA    . PRO A 278 ? 0.35780 0.15900 0.23030 -0.05470 -0.05410 -0.01570 278  PRO A CA    
2177 C  C     . PRO A 278 ? 0.35230 0.19350 0.22160 -0.02000 -0.07270 -0.02870 278  PRO A C     
2178 O  O     . PRO A 278 ? 0.31990 0.17720 0.21440 -0.01740 -0.05550 -0.02580 278  PRO A O     
2179 C  CB    . PRO A 278 ? 0.43710 0.14840 0.24150 -0.06670 -0.05200 0.00200  278  PRO A CB    
2180 C  CG    . PRO A 278 ? 0.46070 0.20580 0.25860 -0.06980 -0.07470 -0.01130 278  PRO A CG    
2181 C  CD    . PRO A 278 ? 0.45280 0.23550 0.26820 -0.08410 -0.09020 -0.02970 278  PRO A CD    
2182 N  N     . GLY A 279 ? 0.37010 0.22750 0.23430 -0.02670 -0.06840 -0.01630 279  GLY A N     
2183 C  CA    . GLY A 279 ? 0.35490 0.19320 0.22740 -0.02160 -0.04950 -0.00280 279  GLY A CA    
2184 C  C     . GLY A 279 ? 0.34070 0.18610 0.20660 -0.04360 -0.02470 -0.01930 279  GLY A C     
2185 O  O     . GLY A 279 ? 0.32510 0.24250 0.20610 -0.02180 -0.04860 -0.03940 279  GLY A O     
2186 N  N     . ALA A 280 ? 0.31070 0.20120 0.19810 0.01300  -0.06190 -0.00600 280  ALA A N     
2187 C  CA    . ALA A 280 ? 0.32720 0.18730 0.19190 0.02380  -0.06220 -0.01170 280  ALA A CA    
2188 C  C     . ALA A 280 ? 0.31420 0.20060 0.17140 -0.00460 -0.05260 -0.00880 280  ALA A C     
2189 O  O     . ALA A 280 ? 0.34940 0.19180 0.15250 0.02000  -0.05420 -0.02850 280  ALA A O     
2190 C  CB    . ALA A 280 ? 0.37490 0.19920 0.19920 0.00730  -0.07520 -0.04700 280  ALA A CB    
2191 N  N     . VAL A 281 ? 0.29610 0.21240 0.17410 0.03130  -0.05670 -0.01760 281  VAL A N     
2192 C  CA    . VAL A 281 ? 0.32660 0.17590 0.15940 0.01800  -0.05950 -0.01960 281  VAL A CA    
2193 C  C     . VAL A 281 ? 0.33280 0.18640 0.13750 0.03570  -0.04590 -0.01160 281  VAL A C     
2194 O  O     . VAL A 281 ? 0.33720 0.18670 0.15860 0.00780  -0.04650 -0.01460 281  VAL A O     
2195 C  CB    . VAL A 281 ? 0.35520 0.15260 0.16940 -0.00260 -0.09030 -0.02990 281  VAL A CB    
2196 C  CG1   . VAL A 281 ? 0.36490 0.17390 0.16590 0.01450  -0.08350 -0.04920 281  VAL A CG1   
2197 C  CG2   . VAL A 281 ? 0.34060 0.15090 0.18940 -0.01320 -0.06530 -0.03810 281  VAL A CG2   
2198 N  N     . GLU A 282 ? 0.33400 0.18300 0.12420 0.02240  -0.02800 0.00970  282  GLU A N     
2199 C  CA    . GLU A 282 ? 0.34080 0.12000 0.13130 0.02010  -0.02550 0.00300  282  GLU A CA    
2200 C  C     . GLU A 282 ? 0.30240 0.13270 0.14310 0.01290  -0.05860 -0.01060 282  GLU A C     
2201 O  O     . GLU A 282 ? 0.29220 0.15410 0.15130 0.00180  -0.03410 -0.00600 282  GLU A O     
2202 C  CB    . GLU A 282 ? 0.30110 0.15060 0.15850 0.00280  -0.01200 0.00450  282  GLU A CB    
2203 C  CG    . GLU A 282 ? 0.33100 0.15100 0.16900 0.00380  -0.05590 0.03030  282  GLU A CG    
2204 C  CD    . GLU A 282 ? 0.33400 0.15370 0.16130 0.02810  -0.05460 0.01180  282  GLU A CD    
2205 O  OE1   . GLU A 282 ? 0.39610 0.15160 0.17320 -0.03340 -0.03470 0.02190  282  GLU A OE1   
2206 O  OE2   . GLU A 282 ? 0.35230 0.18040 0.17070 0.01060  -0.04540 0.02070  282  GLU A OE2   
2207 N  N     . GLU A 283 ? 0.32500 0.18520 0.12100 0.02320  -0.05830 0.02550  283  GLU A N     
2208 C  CA    . GLU A 283 ? 0.32150 0.19360 0.11900 -0.01520 -0.05920 0.04550  283  GLU A CA    
2209 C  C     . GLU A 283 ? 0.36010 0.19250 0.13970 -0.01200 -0.03320 0.02740  283  GLU A C     
2210 O  O     . GLU A 283 ? 0.36570 0.19000 0.16570 0.00630  0.00410  0.02400  283  GLU A O     
2211 C  CB    . GLU A 283 ? 0.36680 0.24500 0.13170 0.04250  -0.04890 0.05400  283  GLU A CB    
2212 C  CG    . GLU A 283 ? 0.39850 0.18000 0.14990 0.04400  -0.09600 -0.00120 283  GLU A CG    
2213 C  CD    . GLU A 283 ? 0.42490 0.20930 0.16960 0.05530  -0.07340 -0.01170 283  GLU A CD    
2214 O  OE1   . GLU A 283 ? 0.41160 0.20510 0.16170 0.06390  -0.06080 0.00870  283  GLU A OE1   
2215 O  OE2   . GLU A 283 ? 0.45300 0.19280 0.19920 0.03550  -0.07010 -0.00660 283  GLU A OE2   
2216 N  N     . LEU A 284 ? 0.31970 0.15830 0.11990 -0.01890 -0.04040 0.01430  284  LEU A N     
2217 C  CA    . LEU A 284 ? 0.30920 0.18320 0.12300 0.02450  -0.03780 -0.01580 284  LEU A CA    
2218 C  C     . LEU A 284 ? 0.34250 0.15670 0.11210 0.00500  -0.03930 -0.02360 284  LEU A C     
2219 O  O     . LEU A 284 ? 0.35420 0.14210 0.11470 0.01860  -0.02520 0.01760  284  LEU A O     
2220 C  CB    . LEU A 284 ? 0.32560 0.19070 0.13070 0.02460  -0.03140 -0.02950 284  LEU A CB    
2221 C  CG    . LEU A 284 ? 0.39860 0.18940 0.12120 -0.02230 -0.03130 0.02120  284  LEU A CG    
2222 C  CD1   . LEU A 284 ? 0.40160 0.16690 0.13600 -0.00080 -0.01690 -0.00250 284  LEU A CD1   
2223 C  CD2   . LEU A 284 ? 0.42750 0.26270 0.11060 0.01010  -0.02800 0.00800  284  LEU A CD2   
2224 N  N     . LEU A 285 ? 0.31480 0.13890 0.10570 0.02420  -0.04670 -0.01750 285  LEU A N     
2225 C  CA    . LEU A 285 ? 0.30040 0.09620 0.08650 -0.00490 -0.03790 0.00880  285  LEU A CA    
2226 C  C     . LEU A 285 ? 0.31970 0.12820 0.10090 -0.00740 -0.00520 0.02960  285  LEU A C     
2227 O  O     . LEU A 285 ? 0.33830 0.12860 0.10630 0.00450  0.02030  0.00740  285  LEU A O     
2228 C  CB    . LEU A 285 ? 0.34199 0.10961 0.10771 0.02950  -0.03050 0.01429  285  LEU A CB    
2229 C  CG    . LEU A 285 ? 0.31300 0.11850 0.13960 0.01460  -0.02510 0.01240  285  LEU A CG    
2230 C  CD1   . LEU A 285 ? 0.33458 0.10682 0.17230 0.00920  0.00930  0.04489  285  LEU A CD1   
2231 C  CD2   . LEU A 285 ? 0.31570 0.15950 0.13020 0.00380  -0.03070 0.01900  285  LEU A CD2   
2232 N  N     . ARG A 286 ? 0.28620 0.17980 0.11300 0.01180  -0.02580 -0.01310 286  ARG A N     
2233 C  CA    . ARG A 286 ? 0.30080 0.12380 0.12160 0.05820  -0.01970 -0.01070 286  ARG A CA    
2234 C  C     . ARG A 286 ? 0.31360 0.16930 0.12700 -0.01040 -0.00200 0.01500  286  ARG A C     
2235 O  O     . ARG A 286 ? 0.32460 0.16040 0.13080 -0.00390 -0.01130 0.02540  286  ARG A O     
2236 C  CB    . ARG A 286 ? 0.30940 0.12620 0.13050 0.05170  -0.00820 0.00530  286  ARG A CB    
2237 C  CG    . ARG A 286 ? 0.32890 0.13310 0.14020 0.05950  -0.03240 0.00460  286  ARG A CG    
2238 C  CD    . ARG A 286 ? 0.32270 0.16610 0.13440 0.03060  -0.07020 0.01970  286  ARG A CD    
2239 N  NE    . ARG A 286 ? 0.31830 0.16970 0.12760 0.01120  -0.05550 0.02350  286  ARG A NE    
2240 C  CZ    . ARG A 286 ? 0.36670 0.17810 0.14470 0.04860  -0.06210 0.00110  286  ARG A CZ    
2241 N  NH1   . ARG A 286 ? 0.38940 0.17720 0.15390 0.01180  -0.04510 0.01840  286  ARG A NH1   
2242 N  NH2   . ARG A 286 ? 0.38340 0.25030 0.13800 0.04750  -0.06000 -0.01510 286  ARG A NH2   
2243 N  N     . TYR A 287 ? 0.30480 0.12760 0.10370 0.03230  -0.02050 0.01990  287  TYR A N     
2244 C  CA    . TYR A 287 ? 0.32110 0.19550 0.09500 0.02480  -0.00970 0.01580  287  TYR A CA    
2245 C  C     . TYR A 287 ? 0.33870 0.14980 0.11630 0.05030  0.01190  0.02970  287  TYR A C     
2246 O  O     . TYR A 287 ? 0.40090 0.14770 0.13570 0.04270  0.00170  0.03670  287  TYR A O     
2247 C  CB    . TYR A 287 ? 0.33100 0.17630 0.11320 0.03300  -0.04090 0.02800  287  TYR A CB    
2248 C  CG    . TYR A 287 ? 0.37509 0.20870 0.11551 0.03750  -0.03740 0.03350  287  TYR A CG    
2249 C  CD1   . TYR A 287 ? 0.44058 0.25570 0.14411 0.02720  -0.06549 0.04319  287  TYR A CD1   
2250 C  CD2   . TYR A 287 ? 0.43130 0.27810 0.11910 0.04620  -0.01610 0.01940  287  TYR A CD2   
2251 C  CE1   . TYR A 287 ? 0.45807 0.27460 0.15002 0.01980  -0.04259 0.06459  287  TYR A CE1   
2252 C  CE2   . TYR A 287 ? 0.43950 0.30340 0.12870 0.05310  -0.02520 0.04280  287  TYR A CE2   
2253 C  CZ    . TYR A 287 ? 0.45800 0.32090 0.14920 0.06280  -0.02240 0.06730  287  TYR A CZ    
2254 O  OH    . TYR A 287 ? 0.53920 0.39200 0.17200 0.03530  -0.02170 0.09070  287  TYR A OH    
2255 N  N     . LEU A 288 ? 0.33780 0.13910 0.13370 0.05340  -0.00310 -0.01130 288  LEU A N     
2256 C  CA    . LEU A 288 ? 0.33410 0.13240 0.13040 0.01940  -0.01640 -0.00130 288  LEU A CA    
2257 C  C     . LEU A 288 ? 0.34630 0.14250 0.12120 -0.03470 -0.01090 0.03240  288  LEU A C     
2258 O  O     . LEU A 288 ? 0.33890 0.16100 0.14490 0.00210  0.01010  0.02660  288  LEU A O     
2259 C  CB    . LEU A 288 ? 0.37540 0.15110 0.12260 0.02110  -0.01820 -0.01720 288  LEU A CB    
2260 C  CG    . LEU A 288 ? 0.44497 0.16930 0.11153 0.00280  0.00870  -0.00010 288  LEU A CG    
2261 C  CD1   . LEU A 288 ? 0.38966 0.16051 0.12093 0.02879  -0.01580 -0.03708 288  LEU A CD1   
2262 C  CD2   . LEU A 288 ? 0.52640 0.23090 0.13440 0.01900  0.00680  0.01530  288  LEU A CD2   
2263 N  N     . ALA A 289 ? 0.35660 0.13530 0.10150 0.00100  0.01480  0.00890  289  ALA A N     
2264 C  CA    . ALA A 289 ? 0.30790 0.13630 0.12850 -0.02720 0.03040  -0.02910 289  ALA A CA    
2265 C  C     . ALA A 289 ? 0.25110 0.17200 0.14880 0.02920  0.05110  0.00990  289  ALA A C     
2266 O  O     . ALA A 289 ? 0.31580 0.24760 0.14450 -0.03620 0.02730  0.03320  289  ALA A O     
2267 C  CB    . ALA A 289 ? 0.36520 0.15360 0.16240 -0.04030 0.01260  -0.06230 289  ALA A CB    
2268 N  N     . ILE A 290 ? 0.28740 0.16680 0.13530 0.08140  0.03300  0.01940  290  ILE A N     
2269 C  CA    . ILE A 290 ? 0.31030 0.18470 0.14450 0.06920  0.01630  0.01830  290  ILE A CA    
2270 C  C     . ILE A 290 ? 0.31790 0.23220 0.14230 0.07130  0.00240  0.02280  290  ILE A C     
2271 O  O     . ILE A 290 ? 0.31730 0.26680 0.15510 0.03510  0.00960  0.04750  290  ILE A O     
2272 C  CB    . ILE A 290 ? 0.35430 0.18030 0.17230 0.03160  0.02260  0.04840  290  ILE A CB    
2273 C  CG1   . ILE A 290 ? 0.37490 0.13200 0.20160 0.02050  0.04650  0.03780  290  ILE A CG1   
2274 C  CG2   . ILE A 290 ? 0.36280 0.21410 0.17630 -0.00340 0.02360  0.02560  290  ILE A CG2   
2275 C  CD1   . ILE A 290 ? 0.39880 0.13230 0.24070 0.01570  0.04930  -0.03190 290  ILE A CD1   
2276 N  N     . ALA A 291 ? 0.33120 0.25310 0.13200 0.01950  -0.01750 0.01220  291  ALA A N     
2277 C  CA    . ALA A 291 ? 0.32710 0.14840 0.14760 0.00500  -0.00640 0.02550  291  ALA A CA    
2278 C  C     . ALA A 291 ? 0.35910 0.14260 0.17120 0.02190  0.02380  0.02950  291  ALA A C     
2279 O  O     . ALA A 291 ? 0.36340 0.17870 0.16890 0.02610  0.04200  0.02350  291  ALA A O     
2280 C  CB    . ALA A 291 ? 0.37150 0.15640 0.15110 0.02210  -0.03090 0.03580  291  ALA A CB    
2281 N  N     . ASP A 292 ? 0.39100 0.17010 0.22090 -0.01600 0.06110  0.03490  292  ASP A N     
2282 C  CA    . ASP A 292 ? 0.38150 0.16190 0.25130 0.02250  0.01600  0.02370  292  ASP A CA    
2283 C  C     . ASP A 292 ? 0.36380 0.12630 0.24970 -0.01920 0.02020  0.01190  292  ASP A C     
2284 O  O     . ASP A 292 ? 0.34940 0.15030 0.26310 -0.00930 -0.02220 -0.02750 292  ASP A O     
2285 C  CB    . ASP A 292 ? 0.37540 0.14850 0.26850 0.03440  0.01240  0.02920  292  ASP A CB    
2286 C  CG    . ASP A 292 ? 0.39690 0.19790 0.25580 0.02710  0.01650  0.00370  292  ASP A CG    
2287 O  OD1   . ASP A 292 ? 0.36990 0.18950 0.26360 0.06160  0.03840  0.00520  292  ASP A OD1   
2288 O  OD2   . ASP A 292 ? 0.38880 0.24390 0.24110 0.02870  0.01680  0.00460  292  ASP A OD2   
2289 N  N     . ILE A 293 ? 0.30050 0.22640 0.26540 -0.00040 0.04490  -0.00880 293  ILE A N     
2290 C  CA    . ILE A 293 ? 0.36260 0.25330 0.29570 -0.00840 0.03190  -0.08240 293  ILE A CA    
2291 C  C     . ILE A 293 ? 0.39300 0.27110 0.29090 0.00080  -0.00430 -0.07640 293  ILE A C     
2292 O  O     . ILE A 293 ? 0.44090 0.29890 0.32590 0.01550  -0.02660 -0.05620 293  ILE A O     
2293 C  CB    . ILE A 293 ? 0.33230 0.31200 0.35340 -0.04630 0.08410  -0.10070 293  ILE A CB    
2294 C  CG1   . ILE A 293 ? 0.45300 0.40460 0.40150 -0.15060 0.15430  -0.08700 293  ILE A CG1   
2295 C  CG2   . ILE A 293 ? 0.43780 0.32440 0.34790 -0.04420 0.01890  -0.11740 293  ILE A CG2   
2296 C  CD1   . ILE A 293 ? 0.44750 0.42470 0.42810 -0.19420 0.15570  -0.08160 293  ILE A CD1   
2297 N  N     . ALA A 294 ? 0.35490 0.18670 0.26480 -0.00140 0.01070  -0.04250 294  ALA A N     
2298 C  CA    . ALA A 294 ? 0.43550 0.19350 0.30080 -0.07800 0.03330  -0.02210 294  ALA A CA    
2299 C  C     . ALA A 294 ? 0.39010 0.23300 0.27790 -0.02180 0.05860  -0.01920 294  ALA A C     
2300 O  O     . ALA A 294 ? 0.47420 0.32720 0.29200 0.04550  0.08400  -0.02020 294  ALA A O     
2301 C  CB    . ALA A 294 ? 0.50760 0.24530 0.31920 -0.11720 0.00480  -0.03150 294  ALA A CB    
2302 N  N     . GLY A 295 ? 0.32120 0.13600 0.25510 -0.00110 -0.02130 -0.04580 295  GLY A N     
2303 C  CA    . GLY A 295 ? 0.28920 0.16090 0.22870 0.00810  -0.02120 -0.07370 295  GLY A CA    
2304 C  C     . GLY A 295 ? 0.31170 0.16640 0.21600 -0.02700 -0.02090 -0.06000 295  GLY A C     
2305 O  O     . GLY A 295 ? 0.30830 0.18430 0.21760 -0.02420 0.01180  -0.06840 295  GLY A O     
2306 N  N     . GLY A 296 ? 0.28410 0.20030 0.20900 -0.02920 -0.03190 -0.05030 296  GLY A N     
2307 C  CA    . GLY A 296 ? 0.33110 0.19720 0.19760 -0.06070 -0.04360 -0.04480 296  GLY A CA    
2308 C  C     . GLY A 296 ? 0.35510 0.17390 0.21510 0.00260  -0.00850 -0.00610 296  GLY A C     
2309 O  O     . GLY A 296 ? 0.31370 0.21220 0.21420 -0.00440 -0.00500 -0.02930 296  GLY A O     
2310 N  N     . ARG A 297 ? 0.31350 0.18020 0.22660 -0.01640 0.00870  -0.06010 297  ARG A N     
2311 C  CA    . ARG A 297 ? 0.28320 0.14810 0.23490 -0.00680 0.01610  -0.06290 297  ARG A CA    
2312 C  C     . ARG A 297 ? 0.26370 0.23800 0.24470 0.00090  -0.01660 -0.07870 297  ARG A C     
2313 O  O     . ARG A 297 ? 0.32080 0.23760 0.26330 -0.05640 -0.01530 -0.08040 297  ARG A O     
2314 C  CB    . ARG A 297 ? 0.28840 0.13160 0.26450 0.00750  0.02570  -0.03890 297  ARG A CB    
2315 C  CG    . ARG A 297 ? 0.29490 0.10450 0.25440 -0.04030 -0.03300 -0.00600 297  ARG A CG    
2316 C  CD    . ARG A 297 ? 0.32040 0.11210 0.25000 -0.02720 -0.02510 -0.02290 297  ARG A CD    
2317 N  NE    . ARG A 297 ? 0.33620 0.11620 0.23090 -0.02650 -0.05010 -0.03360 297  ARG A NE    
2318 C  CZ    . ARG A 297 ? 0.25900 0.14380 0.22230 -0.03070 -0.03290 -0.04840 297  ARG A CZ    
2319 N  NH1   . ARG A 297 ? 0.26320 0.19030 0.21340 0.03480  -0.00260 -0.02880 297  ARG A NH1   
2320 N  NH2   . ARG A 297 ? 0.29210 0.13850 0.23230 -0.02810 -0.03240 -0.02040 297  ARG A NH2   
2321 N  N     . VAL A 298 ? 0.29120 0.21540 0.23940 -0.02960 -0.02120 -0.07660 298  VAL A N     
2322 C  CA    . VAL A 298 ? 0.30220 0.25010 0.25320 -0.09900 -0.01070 -0.10780 298  VAL A CA    
2323 C  C     . VAL A 298 ? 0.34140 0.21070 0.25180 -0.08770 0.00940  -0.10930 298  VAL A C     
2324 O  O     . VAL A 298 ? 0.33900 0.25860 0.26410 -0.09110 0.00710  -0.08350 298  VAL A O     
2325 C  CB    . VAL A 298 ? 0.36110 0.26820 0.28200 -0.13810 -0.01210 -0.08640 298  VAL A CB    
2326 C  CG1   . VAL A 298 ? 0.35290 0.28980 0.29870 -0.08300 -0.03250 -0.07080 298  VAL A CG1   
2327 C  CG2   . VAL A 298 ? 0.37670 0.32940 0.30130 -0.16530 -0.00420 -0.08760 298  VAL A CG2   
2328 N  N     . ALA A 299 ? 0.38850 0.22590 0.25580 -0.06090 -0.00790 -0.12510 299  ALA A N     
2329 C  CA    . ALA A 299 ? 0.36670 0.20910 0.26140 -0.02210 -0.00600 -0.10190 299  ALA A CA    
2330 C  C     . ALA A 299 ? 0.38670 0.24660 0.28990 -0.04870 -0.00510 -0.10240 299  ALA A C     
2331 O  O     . ALA A 299 ? 0.37040 0.27700 0.31850 -0.06110 -0.00360 -0.11360 299  ALA A O     
2332 C  CB    . ALA A 299 ? 0.43680 0.19380 0.27350 0.02180  0.00290  -0.07950 299  ALA A CB    
2333 N  N     . THR A 300 ? 0.37270 0.23020 0.30040 -0.03350 -0.01030 -0.10580 300  THR A N     
2334 C  CA    . THR A 300 ? 0.40770 0.24560 0.28950 -0.02160 -0.04660 -0.12390 300  THR A CA    
2335 C  C     . THR A 300 ? 0.40698 0.24281 0.30800 -0.06290 -0.06838 -0.13249 300  THR A C     
2336 O  O     . THR A 300 ? 0.50450 0.28180 0.32160 -0.03740 -0.08240 -0.12450 300  THR A O     
2337 C  CB    . THR A 300 ? 0.39520 0.27190 0.30170 -0.03740 -0.03920 -0.07930 300  THR A CB    
2338 O  OG1   . THR A 300 ? 0.37720 0.28060 0.29460 -0.02100 -0.04140 -0.05860 300  THR A OG1   
2339 C  CG2   . THR A 300 ? 0.40900 0.32210 0.32010 -0.02430 -0.02420 -0.08320 300  THR A CG2   
2340 N  N     . ALA A 301 ? 0.44370 0.29180 0.31380 -0.03120 -0.05030 -0.13140 301  ALA A N     
2341 C  CA    . ALA A 301 ? 0.45480 0.29830 0.30640 0.00940  -0.02720 -0.14520 301  ALA A CA    
2342 C  C     . ALA A 301 ? 0.46280 0.27830 0.31470 -0.00940 -0.01710 -0.15440 301  ALA A C     
2343 O  O     . ALA A 301 ? 0.47460 0.27910 0.29650 -0.03260 -0.02870 -0.15870 301  ALA A O     
2344 C  CB    . ALA A 301 ? 0.49610 0.33410 0.30250 0.03950  -0.03770 -0.15880 301  ALA A CB    
2345 N  N     . ASP A 302 ? 0.46330 0.28700 0.33290 0.00800  -0.02720 -0.15300 302  ASP A N     
2346 C  CA    . ASP A 302 ? 0.48040 0.24800 0.34620 0.01370  -0.02960 -0.14030 302  ASP A CA    
2347 C  C     . ASP A 302 ? 0.49210 0.26530 0.33980 -0.01050 -0.04540 -0.11990 302  ASP A C     
2348 O  O     . ASP A 302 ? 0.49580 0.33020 0.33120 0.02220  -0.05230 -0.12700 302  ASP A O     
2349 C  CB    . ASP A 302 ? 0.53856 0.25463 0.36561 0.00150  -0.01599 -0.16538 302  ASP A CB    
2350 C  CG    . ASP A 302 ? 0.61610 0.30230 0.39620 -0.01810 -0.01660 -0.18780 302  ASP A CG    
2351 O  OD1   . ASP A 302 ? 0.67330 0.35180 0.37650 -0.04780 -0.02780 -0.16020 302  ASP A OD1   
2352 O  OD2   . ASP A 302 ? 0.70356 0.29713 0.43221 -0.02490 0.00860  -0.17488 302  ASP A OD2   
2353 N  N     . ILE A 303 ? 0.47880 0.19970 0.32720 0.05790  -0.02560 -0.09910 303  ILE A N     
2354 C  CA    . ILE A 303 ? 0.49330 0.21370 0.33860 0.08220  -0.02800 -0.07610 303  ILE A CA    
2355 C  C     . ILE A 303 ? 0.45680 0.23630 0.36600 0.10540  -0.01600 -0.06260 303  ILE A C     
2356 O  O     . ILE A 303 ? 0.48670 0.22970 0.37440 0.04440  0.00290  -0.03560 303  ILE A O     
2357 C  CB    . ILE A 303 ? 0.49720 0.17680 0.33850 0.04110  -0.03050 -0.06250 303  ILE A CB    
2358 C  CG1   . ILE A 303 ? 0.50240 0.19380 0.31000 0.04450  -0.00570 -0.09020 303  ILE A CG1   
2359 C  CG2   . ILE A 303 ? 0.48380 0.20500 0.34410 0.03310  -0.04790 -0.04670 303  ILE A CG2   
2360 C  CD1   . ILE A 303 ? 0.51270 0.28260 0.29440 0.02100  -0.00860 -0.11770 303  ILE A CD1   
2361 N  N     . GLU A 304 ? 0.47330 0.30340 0.38600 0.09120  -0.02020 -0.08950 304  GLU A N     
2362 C  CA    A GLU A 304 ? 0.49550 0.33690 0.39820 0.15530  -0.01420 -0.10370 304  GLU A CA    
2363 C  CA    B GLU A 304 ? 0.49380 0.33260 0.39550 0.13920  -0.00190 -0.11770 304  GLU A CA    
2364 C  C     . GLU A 304 ? 0.49090 0.38700 0.41030 0.11910  -0.01710 -0.09720 304  GLU A C     
2365 O  O     . GLU A 304 ? 0.49530 0.44360 0.43970 0.13030  -0.03730 -0.06430 304  GLU A O     
2366 C  CB    A GLU A 304 ? 0.56460 0.35200 0.40130 0.18650  -0.02160 -0.12050 304  GLU A CB    
2367 C  CB    B GLU A 304 ? 0.56450 0.34180 0.39490 0.13090  0.01070  -0.15610 304  GLU A CB    
2368 C  CG    A GLU A 304 ? 0.60100 0.37560 0.40130 0.19650  -0.02970 -0.12390 304  GLU A CG    
2369 C  CG    B GLU A 304 ? 0.59380 0.36580 0.38800 0.10400  0.02220  -0.17390 304  GLU A CG    
2370 C  CD    A GLU A 304 ? 0.66940 0.43480 0.40670 0.18260  -0.04620 -0.11260 304  GLU A CD    
2371 C  CD    B GLU A 304 ? 0.65290 0.41300 0.37900 0.01190  0.00890  -0.19280 304  GLU A CD    
2372 O  OE1   A GLU A 304 ? 0.68240 0.38700 0.41020 0.18160  -0.04590 -0.11680 304  GLU A OE1   
2373 O  OE1   B GLU A 304 ? 0.70800 0.44270 0.37260 0.00530  -0.00320 -0.22780 304  GLU A OE1   
2374 O  OE2   A GLU A 304 ? 0.70100 0.50390 0.41000 0.16790  -0.06520 -0.09390 304  GLU A OE2   
2375 O  OE2   B GLU A 304 ? 0.66450 0.44070 0.37430 -0.01160 0.02110  -0.17720 304  GLU A OE2   
2376 N  N     . VAL A 305 ? 0.45650 0.38340 0.40080 0.11350  -0.03300 -0.12160 305  VAL A N     
2377 C  CA    . VAL A 305 ? 0.40250 0.39900 0.41010 0.16740  -0.02200 -0.12990 305  VAL A CA    
2378 C  C     . VAL A 305 ? 0.42560 0.42980 0.41850 0.18970  -0.02270 -0.13460 305  VAL A C     
2379 O  O     . VAL A 305 ? 0.46820 0.45010 0.41580 0.17060  -0.03810 -0.13480 305  VAL A O     
2380 C  CB    . VAL A 305 ? 0.48790 0.39430 0.41140 0.10500  -0.06030 -0.13850 305  VAL A CB    
2381 C  CG1   . VAL A 305 ? 0.52760 0.45370 0.41450 0.10300  -0.07530 -0.16140 305  VAL A CG1   
2382 C  CG2   . VAL A 305 ? 0.46560 0.43350 0.40330 0.10010  -0.07410 -0.11210 305  VAL A CG2   
2383 N  N     . GLU A 306 ? 0.46270 0.48010 0.43720 0.15680  -0.00040 -0.11630 306  GLU A N     
2384 C  CA    . GLU A 306 ? 0.47050 0.47140 0.46500 0.14230  -0.01560 -0.09160 306  GLU A CA    
2385 C  C     . GLU A 306 ? 0.51870 0.45010 0.49130 0.12240  -0.03050 -0.10150 306  GLU A C     
2386 O  O     . GLU A 306 ? 0.59820 0.45850 0.49720 0.15450  -0.04090 -0.08290 306  GLU A O     
2387 C  CB    . GLU A 306 ? 0.45690 0.45420 0.46980 0.09270  0.00650  -0.08620 306  GLU A CB    
2388 C  CG    . GLU A 306 ? 0.44680 0.46420 0.47840 0.07820  0.00240  -0.09920 306  GLU A CG    
2389 C  CD    . GLU A 306 ? 0.45030 0.52600 0.49520 0.05310  0.00250  -0.07960 306  GLU A CD    
2390 O  OE1   . GLU A 306 ? 0.50710 0.54490 0.50630 0.02350  -0.00920 -0.08140 306  GLU A OE1   
2391 O  OE2   . GLU A 306 ? 0.40920 0.51710 0.49820 0.06990  0.02760  -0.07070 306  GLU A OE2   
2392 N  N     . GLY A 307 ? 0.54070 0.43900 0.52130 0.12450  -0.00260 -0.09210 307  GLY A N     
2393 C  CA    . GLY A 307 ? 0.59670 0.44630 0.54220 0.11270  -0.00540 -0.08670 307  GLY A CA    
2394 C  C     . GLY A 307 ? 0.67190 0.44160 0.54880 0.06990  -0.02520 -0.08610 307  GLY A C     
2395 O  O     . GLY A 307 ? 0.72220 0.51990 0.56940 0.03650  -0.05580 -0.09200 307  GLY A O     
2396 N  N     . GLN A 308 ? 0.62230 0.42760 0.52590 0.14260  -0.03270 -0.08130 308  GLN A N     
2397 C  CA    . GLN A 308 ? 0.61890 0.42730 0.50880 0.10990  -0.01770 -0.08030 308  GLN A CA    
2398 C  C     . GLN A 308 ? 0.62470 0.38700 0.48410 0.02480  -0.03730 -0.07620 308  GLN A C     
2399 O  O     . GLN A 308 ? 0.64830 0.35870 0.48520 0.03720  -0.03940 -0.07500 308  GLN A O     
2400 C  CB    . GLN A 308 ? 0.63920 0.49320 0.52110 0.11950  0.02290  -0.08250 308  GLN A CB    
2401 C  CG    . GLN A 308 ? 0.65110 0.55020 0.54040 0.10480  0.06310  -0.08180 308  GLN A CG    
2402 C  CD    . GLN A 308 ? 0.65450 0.60250 0.55770 0.07610  0.11140  -0.05310 308  GLN A CD    
2403 O  OE1   . GLN A 308 ? 0.65450 0.62050 0.55860 0.06310  0.15570  -0.06700 308  GLN A OE1   
2404 N  NE2   . GLN A 308 ? 0.62160 0.58290 0.56130 0.11280  0.13320  -0.03450 308  GLN A NE2   
2405 N  N     . LEU A 309 ? 0.60500 0.34200 0.45160 0.02810  -0.05990 -0.06250 309  LEU A N     
2406 C  CA    A LEU A 309 ? 0.57670 0.29470 0.42840 -0.02150 -0.05460 -0.09330 309  LEU A CA    
2407 C  CA    B LEU A 309 ? 0.56730 0.27540 0.42830 0.00180  -0.05510 -0.09680 309  LEU A CA    
2408 C  C     . LEU A 309 ? 0.59160 0.23150 0.40570 -0.03150 -0.04830 -0.09890 309  LEU A C     
2409 O  O     . LEU A 309 ? 0.69780 0.22330 0.40160 -0.00330 -0.04140 -0.10230 309  LEU A O     
2410 C  CB    A LEU A 309 ? 0.58190 0.31870 0.43380 -0.08490 -0.03540 -0.10740 309  LEU A CB    
2411 C  CB    B LEU A 309 ? 0.53230 0.25100 0.42970 -0.00470 -0.05070 -0.11740 309  LEU A CB    
2412 C  CG    A LEU A 309 ? 0.58910 0.30520 0.42700 -0.09150 -0.00260 -0.13220 309  LEU A CG    
2413 C  CG    B LEU A 309 ? 0.49500 0.20231 0.42380 0.03410  -0.03980 -0.13769 309  LEU A CG    
2414 C  CD1   A LEU A 309 ? 0.61709 0.27461 0.42070 -0.07869 -0.00420 -0.16149 309  LEU A CD1   
2415 C  CD1   B LEU A 309 ? 0.50940 0.24550 0.42660 0.00000  -0.04660 -0.12720 309  LEU A CD1   
2416 C  CD2   A LEU A 309 ? 0.63680 0.31380 0.42730 -0.07790 0.01960  -0.13780 309  LEU A CD2   
2417 C  CD2   B LEU A 309 ? 0.51020 0.18010 0.43180 0.02570  -0.03790 -0.11480 309  LEU A CD2   
2418 N  N     . ILE A 310 ? 0.48210 0.15910 0.37220 0.00070  -0.03090 -0.09420 310  ILE A N     
2419 C  CA    . ILE A 310 ? 0.42730 0.18630 0.35610 -0.04370 -0.04610 -0.11980 310  ILE A CA    
2420 C  C     . ILE A 310 ? 0.42870 0.19050 0.36510 -0.04430 -0.05940 -0.11790 310  ILE A C     
2421 O  O     . ILE A 310 ? 0.39140 0.26590 0.37400 -0.00550 -0.03480 -0.07270 310  ILE A O     
2422 C  CB    . ILE A 310 ? 0.41936 0.15784 0.34520 -0.03759 -0.02609 -0.10148 310  ILE A CB    
2423 C  CG1   . ILE A 310 ? 0.40420 0.18990 0.32240 -0.08610 -0.00200 -0.10500 310  ILE A CG1   
2424 C  CG2   . ILE A 310 ? 0.38590 0.22920 0.35370 -0.01900 -0.05000 -0.10330 310  ILE A CG2   
2425 C  CD1   . ILE A 310 ? 0.43720 0.20040 0.32580 -0.06730 0.01050  -0.11580 310  ILE A CD1   
2426 N  N     . ARG A 311 ? 0.45390 0.22450 0.37390 -0.12320 -0.04550 -0.08660 311  ARG A N     
2427 C  CA    . ARG A 311 ? 0.49800 0.26880 0.38260 -0.11490 -0.06710 -0.05030 311  ARG A CA    
2428 C  C     . ARG A 311 ? 0.46190 0.26170 0.35900 -0.11040 -0.05780 -0.06820 311  ARG A C     
2429 O  O     . ARG A 311 ? 0.47190 0.24730 0.33780 -0.11540 -0.03940 -0.09280 311  ARG A O     
2430 C  CB    . ARG A 311 ? 0.52630 0.32780 0.41430 -0.16170 -0.10790 -0.04980 311  ARG A CB    
2431 C  CG    . ARG A 311 ? 0.59140 0.34490 0.43870 -0.20050 -0.11060 -0.03430 311  ARG A CG    
2432 C  CD    . ARG A 311 ? 0.62000 0.38430 0.45620 -0.25590 -0.09160 -0.02860 311  ARG A CD    
2433 N  NE    . ARG A 311 ? 0.75420 0.39590 0.46130 -0.26160 -0.10550 -0.04020 311  ARG A NE    
2434 C  CZ    . ARG A 311 ? 0.83350 0.42410 0.47210 -0.29160 -0.10480 -0.00880 311  ARG A CZ    
2435 N  NH1   . ARG A 311 ? 0.90610 0.42580 0.47830 -0.28730 -0.08150 0.00020  311  ARG A NH1   
2436 N  NH2   . ARG A 311 ? 0.83140 0.44200 0.47070 -0.26490 -0.14870 0.01640  311  ARG A NH2   
2437 N  N     . ALA A 312 ? 0.42630 0.26500 0.35050 -0.06540 -0.04820 -0.08530 312  ALA A N     
2438 C  CA    . ALA A 312 ? 0.44300 0.28770 0.36120 -0.05410 -0.04300 -0.11860 312  ALA A CA    
2439 C  C     . ALA A 312 ? 0.40700 0.28370 0.37640 -0.09080 -0.02750 -0.09970 312  ALA A C     
2440 O  O     . ALA A 312 ? 0.45650 0.32480 0.38810 -0.13030 -0.01220 -0.08380 312  ALA A O     
2441 C  CB    . ALA A 312 ? 0.45470 0.24700 0.36010 -0.03480 -0.08570 -0.13310 312  ALA A CB    
2442 N  N     . GLY A 313 ? 0.39810 0.28140 0.38020 -0.08300 -0.01740 -0.11210 313  GLY A N     
2443 C  CA    . GLY A 313 ? 0.33060 0.28760 0.38570 -0.11300 -0.01250 -0.10190 313  GLY A CA    
2444 C  C     . GLY A 313 ? 0.37890 0.29840 0.39490 -0.16540 0.00700  -0.08840 313  GLY A C     
2445 O  O     . GLY A 313 ? 0.45970 0.34550 0.41290 -0.13760 0.04580  -0.07570 313  GLY A O     
2446 N  N     . GLU A 314 ? 0.38030 0.26400 0.38000 -0.13410 -0.03210 -0.10860 314  GLU A N     
2447 C  CA    . GLU A 314 ? 0.41130 0.25630 0.36010 -0.10270 0.00850  -0.07930 314  GLU A CA    
2448 C  C     . GLU A 314 ? 0.42200 0.26770 0.33600 -0.13020 0.00610  -0.08720 314  GLU A C     
2449 O  O     . GLU A 314 ? 0.40330 0.24640 0.33490 -0.10710 0.03680  -0.11420 314  GLU A O     
2450 C  CB    . GLU A 314 ? 0.44257 0.19273 0.38250 -0.11797 -0.03199 -0.07129 314  GLU A CB    
2451 C  CG    . GLU A 314 ? 0.44490 0.26520 0.38710 -0.12210 -0.04600 -0.07740 314  GLU A CG    
2452 C  CD    . GLU A 314 ? 0.48690 0.28350 0.38970 -0.11930 -0.03530 -0.02030 314  GLU A CD    
2453 O  OE1   . GLU A 314 ? 0.51260 0.27860 0.36940 -0.16040 0.01390  -0.06250 314  GLU A OE1   
2454 O  OE2   . GLU A 314 ? 0.52960 0.34640 0.40030 -0.09320 -0.01870 0.04210  314  GLU A OE2   
2455 N  N     . GLY A 315 ? 0.38590 0.26230 0.30980 -0.09440 0.00490  -0.08630 315  GLY A N     
2456 C  CA    . GLY A 315 ? 0.36070 0.19890 0.29650 -0.05170 -0.00380 -0.07810 315  GLY A CA    
2457 C  C     . GLY A 315 ? 0.39810 0.21410 0.29380 -0.06730 0.01040  -0.07200 315  GLY A C     
2458 O  O     . GLY A 315 ? 0.40050 0.20330 0.29050 -0.06680 0.01660  -0.07060 315  GLY A O     
2459 N  N     . VAL A 316 ? 0.33250 0.16600 0.28270 -0.06630 -0.01490 -0.05950 316  VAL A N     
2460 C  CA    . VAL A 316 ? 0.30280 0.19350 0.27690 -0.09950 0.01500  -0.03560 316  VAL A CA    
2461 C  C     . VAL A 316 ? 0.34930 0.16770 0.25380 -0.08910 -0.02690 -0.04450 316  VAL A C     
2462 O  O     . VAL A 316 ? 0.37780 0.19550 0.27170 -0.03340 -0.02890 -0.01990 316  VAL A O     
2463 C  CB    . VAL A 316 ? 0.33940 0.17320 0.27780 -0.05970 -0.01430 -0.01920 316  VAL A CB    
2464 C  CG1   . VAL A 316 ? 0.29750 0.17360 0.29240 -0.03710 0.00730  -0.01270 316  VAL A CG1   
2465 C  CG2   . VAL A 316 ? 0.39610 0.16200 0.27740 -0.07020 -0.02850 -0.01000 316  VAL A CG2   
2466 N  N     . ILE A 317 ? 0.29000 0.15490 0.24360 -0.06280 -0.01400 -0.07130 317  ILE A N     
2467 C  CA    . ILE A 317 ? 0.27710 0.18830 0.22530 -0.05320 0.01390  -0.04590 317  ILE A CA    
2468 C  C     . ILE A 317 ? 0.31740 0.15250 0.22400 -0.02980 0.03310  -0.03620 317  ILE A C     
2469 O  O     . ILE A 317 ? 0.35100 0.12680 0.23840 -0.02230 0.03890  -0.01920 317  ILE A O     
2470 C  CB    . ILE A 317 ? 0.28640 0.17140 0.24580 -0.00450 0.02840  -0.03640 317  ILE A CB    
2471 C  CG1   . ILE A 317 ? 0.25870 0.25740 0.25740 0.00820  0.02900  -0.02330 317  ILE A CG1   
2472 C  CG2   . ILE A 317 ? 0.35750 0.16840 0.24780 -0.03640 0.03800  -0.02410 317  ILE A CG2   
2473 C  CD1   . ILE A 317 ? 0.31690 0.25900 0.26990 -0.03000 0.02810  -0.04410 317  ILE A CD1   
2474 N  N     . VAL A 318 ? 0.29140 0.15640 0.21920 -0.04830 0.00980  -0.04330 318  VAL A N     
2475 C  CA    . VAL A 318 ? 0.29290 0.11530 0.21630 -0.03240 0.02270  -0.02580 318  VAL A CA    
2476 C  C     . VAL A 318 ? 0.32920 0.11200 0.21460 -0.01210 -0.00450 -0.00310 318  VAL A C     
2477 O  O     . VAL A 318 ? 0.33380 0.13700 0.23070 0.01180  -0.00210 0.00530  318  VAL A O     
2478 C  CB    . VAL A 318 ? 0.26980 0.17400 0.21390 0.00550  0.02920  -0.03360 318  VAL A CB    
2479 C  CG1   . VAL A 318 ? 0.28250 0.20720 0.24860 0.02430  0.01930  -0.02620 318  VAL A CG1   
2480 C  CG2   . VAL A 318 ? 0.33990 0.22350 0.21120 0.00410  0.00720  -0.02870 318  VAL A CG2   
2481 N  N     . VAL A 319 ? 0.35830 0.12620 0.19740 -0.04630 0.01120  0.02260  319  VAL A N     
2482 C  CA    . VAL A 319 ? 0.34450 0.16620 0.18850 -0.01080 -0.01910 0.02600  319  VAL A CA    
2483 C  C     . VAL A 319 ? 0.37860 0.10550 0.20660 0.00480  -0.00220 -0.00250 319  VAL A C     
2484 O  O     . VAL A 319 ? 0.35280 0.12420 0.22360 -0.00250 0.00940  0.01340  319  VAL A O     
2485 C  CB    . VAL A 319 ? 0.32540 0.14670 0.22670 -0.00300 -0.00820 0.02780  319  VAL A CB    
2486 C  CG1   . VAL A 319 ? 0.36720 0.15440 0.23030 0.01540  0.01920  -0.00100 319  VAL A CG1   
2487 C  CG2   . VAL A 319 ? 0.35060 0.19190 0.23790 -0.05900 -0.00680 0.03540  319  VAL A CG2   
2488 N  N     . ASN A 320 ? 0.31700 0.10580 0.18180 -0.01600 -0.01370 -0.00500 320  ASN A N     
2489 C  CA    . ASN A 320 ? 0.33370 0.11930 0.17400 -0.05600 0.00850  0.01820  320  ASN A CA    
2490 C  C     . ASN A 320 ? 0.35200 0.10840 0.18420 -0.02670 0.01030  0.00630  320  ASN A C     
2491 O  O     . ASN A 320 ? 0.33570 0.13340 0.20520 0.00920  -0.02170 0.02310  320  ASN A O     
2492 C  CB    . ASN A 320 ? 0.32730 0.10460 0.18590 0.02670  0.02670  0.01420  320  ASN A CB    
2493 C  CG    . ASN A 320 ? 0.31560 0.13640 0.17520 -0.01400 -0.00000 0.02300  320  ASN A CG    
2494 O  OD1   . ASN A 320 ? 0.36310 0.15730 0.17280 -0.02050 -0.03220 0.01810  320  ASN A OD1   
2495 N  ND2   . ASN A 320 ? 0.36390 0.15120 0.20130 0.00820  0.00260  0.02760  320  ASN A ND2   
2496 N  N     . SER A 321 ? 0.35850 0.10570 0.20070 -0.00020 0.00660  0.03650  321  SER A N     
2497 C  CA    . SER A 321 ? 0.31790 0.16530 0.22290 0.03550  -0.00700 0.02480  321  SER A CA    
2498 C  C     . SER A 321 ? 0.31500 0.09620 0.21450 0.03430  0.01830  0.02640  321  SER A C     
2499 O  O     . SER A 321 ? 0.31920 0.15020 0.21060 0.03560  -0.04470 0.01120  321  SER A O     
2500 C  CB    . SER A 321 ? 0.31000 0.16010 0.22980 -0.01110 0.02380  0.02630  321  SER A CB    
2501 O  OG    . SER A 321 ? 0.35980 0.14250 0.22940 -0.00910 0.01610  0.03490  321  SER A OG    
2502 N  N     . ILE A 322 ? 0.36870 0.09390 0.23280 -0.00270 0.01420  0.01330  322  ILE A N     
2503 C  CA    . ILE A 322 ? 0.34510 0.10510 0.24170 -0.00010 0.01310  0.01870  322  ILE A CA    
2504 C  C     . ILE A 322 ? 0.32290 0.12960 0.20400 -0.01220 0.00500  0.00760  322  ILE A C     
2505 O  O     . ILE A 322 ? 0.37610 0.15170 0.20190 0.00750  -0.01970 0.01320  322  ILE A O     
2506 C  CB    . ILE A 322 ? 0.34908 0.09663 0.27410 -0.01020 0.03669  0.02900  322  ILE A CB    
2507 C  CG1   . ILE A 322 ? 0.36460 0.10660 0.27090 -0.03840 0.04630  0.01200  322  ILE A CG1   
2508 C  CG2   . ILE A 322 ? 0.43430 0.12550 0.30910 0.04050  0.04600  0.03950  322  ILE A CG2   
2509 C  CD1   . ILE A 322 ? 0.37400 0.11350 0.26890 0.00310  0.06060  -0.01520 322  ILE A CD1   
2510 N  N     . ALA A 323 ? 0.34580 0.13450 0.18680 0.04190  0.02730  -0.01660 323  ALA A N     
2511 C  CA    . ALA A 323 ? 0.34080 0.15700 0.19010 0.06320  0.00180  -0.00450 323  ALA A CA    
2512 C  C     . ALA A 323 ? 0.32680 0.14780 0.20000 0.03250  -0.00110 -0.00200 323  ALA A C     
2513 O  O     . ALA A 323 ? 0.30320 0.16800 0.18760 0.03260  -0.01590 0.01860  323  ALA A O     
2514 C  CB    . ALA A 323 ? 0.35390 0.14600 0.17750 0.04450  -0.01080 0.01000  323  ALA A CB    
2515 N  N     . ASN A 324 ? 0.35070 0.10120 0.18080 0.00470  0.00550  0.00040  324  ASN A N     
2516 C  CA    . ASN A 324 ? 0.33597 0.09643 0.17790 0.00810  -0.01990 0.03189  324  ASN A CA    
2517 C  C     . ASN A 324 ? 0.34400 0.11040 0.18150 0.01980  -0.02040 0.03620  324  ASN A C     
2518 O  O     . ASN A 324 ? 0.32670 0.17220 0.18540 -0.01300 -0.02030 0.02290  324  ASN A O     
2519 C  CB    . ASN A 324 ? 0.33389 0.11471 0.18070 0.06340  -0.00970 0.02890  324  ASN A CB    
2520 C  CG    . ASN A 324 ? 0.31920 0.09330 0.15280 0.04970  -0.01090 -0.00630 324  ASN A CG    
2521 O  OD1   . ASN A 324 ? 0.32840 0.21070 0.13910 0.04430  -0.00650 0.03650  324  ASN A OD1   
2522 N  ND2   . ASN A 324 ? 0.38170 0.12650 0.17050 0.05840  0.03980  0.01780  324  ASN A ND2   
2523 N  N     . ARG A 325 ? 0.36499 0.11411 0.18840 0.03240  -0.01170 0.04000  325  ARG A N     
2524 C  CA    . ARG A 325 ? 0.35640 0.14720 0.18850 0.04440  -0.00850 0.03950  325  ARG A CA    
2525 C  C     . ARG A 325 ? 0.36160 0.16680 0.20750 0.05710  -0.02180 0.01610  325  ARG A C     
2526 O  O     . ARG A 325 ? 0.37730 0.19260 0.21710 0.07660  -0.02240 0.01520  325  ARG A O     
2527 C  CB    . ARG A 325 ? 0.37180 0.17210 0.19890 0.05450  0.00470  0.02210  325  ARG A CB    
2528 C  CG    . ARG A 325 ? 0.39840 0.18690 0.18650 0.02180  0.00300  0.00400  325  ARG A CG    
2529 C  CD    . ARG A 325 ? 0.39930 0.19270 0.18350 0.05220  0.00650  -0.01020 325  ARG A CD    
2530 N  NE    . ARG A 325 ? 0.41320 0.20780 0.13940 0.04220  -0.02440 0.01440  325  ARG A NE    
2531 C  CZ    . ARG A 325 ? 0.40750 0.22630 0.15590 0.06240  -0.00230 0.06020  325  ARG A CZ    
2532 N  NH1   . ARG A 325 ? 0.39730 0.24740 0.21830 0.05830  0.00410  0.05490  325  ARG A NH1   
2533 N  NH2   . ARG A 325 ? 0.41849 0.18920 0.14931 0.05480  0.00960  0.05569  325  ARG A NH2   
2534 N  N     . ASP A 326 ? 0.35260 0.14130 0.21330 0.04380  -0.02110 0.00330  326  ASP A N     
2535 C  CA    . ASP A 326 ? 0.34980 0.19550 0.21520 0.05980  -0.02670 -0.00180 326  ASP A CA    
2536 C  C     . ASP A 326 ? 0.34180 0.18430 0.23300 0.08910  -0.03290 0.00390  326  ASP A C     
2537 O  O     . ASP A 326 ? 0.35850 0.21020 0.24020 0.04300  -0.04960 0.00860  326  ASP A O     
2538 C  CB    . ASP A 326 ? 0.35850 0.17750 0.20570 0.06350  -0.02890 -0.02730 326  ASP A CB    
2539 C  CG    . ASP A 326 ? 0.38050 0.16530 0.24720 0.04500  -0.03050 -0.00750 326  ASP A CG    
2540 O  OD1   . ASP A 326 ? 0.35200 0.20930 0.28380 0.09390  -0.03580 -0.04380 326  ASP A OD1   
2541 O  OD2   . ASP A 326 ? 0.35410 0.19760 0.23520 0.04900  -0.01540 -0.01000 326  ASP A OD2   
2542 N  N     . GLY A 327 ? 0.35160 0.20870 0.25210 0.09510  -0.04110 0.01660  327  GLY A N     
2543 C  CA    . GLY A 327 ? 0.36810 0.23930 0.27330 0.10140  -0.08620 0.01980  327  GLY A CA    
2544 C  C     . GLY A 327 ? 0.34100 0.26490 0.32290 0.03990  -0.06110 0.00860  327  GLY A C     
2545 O  O     . GLY A 327 ? 0.35100 0.24110 0.37400 0.06630  -0.04510 -0.02240 327  GLY A O     
2546 N  N     . THR A 328 ? 0.35580 0.22250 0.29900 0.07070  -0.04480 -0.01900 328  THR A N     
2547 C  CA    . THR A 328 ? 0.36450 0.22070 0.30870 0.07380  -0.01780 -0.04710 328  THR A CA    
2548 C  C     . THR A 328 ? 0.41600 0.20460 0.29600 0.06340  0.00820  -0.05820 328  THR A C     
2549 O  O     . THR A 328 ? 0.43590 0.23800 0.32510 0.05960  0.02730  -0.06530 328  THR A O     
2550 C  CB    . THR A 328 ? 0.37700 0.22850 0.33920 0.07240  -0.03250 -0.06840 328  THR A CB    
2551 O  OG1   . THR A 328 ? 0.37510 0.22400 0.37560 0.06860  -0.05280 -0.05670 328  THR A OG1   
2552 C  CG2   . THR A 328 ? 0.44170 0.24520 0.34580 0.03530  -0.03900 -0.04130 328  THR A CG2   
2553 N  N     . VAL A 329 ? 0.35580 0.17950 0.27130 0.05060  -0.06610 -0.06530 329  VAL A N     
2554 C  CA    . VAL A 329 ? 0.29950 0.22040 0.23450 0.07480  -0.04130 -0.05070 329  VAL A CA    
2555 C  C     . VAL A 329 ? 0.28810 0.23790 0.21560 0.05280  -0.05500 -0.04940 329  VAL A C     
2556 O  O     . VAL A 329 ? 0.31220 0.32720 0.22060 0.00480  -0.01880 -0.04900 329  VAL A O     
2557 C  CB    . VAL A 329 ? 0.32790 0.20080 0.20630 -0.00110 -0.05370 -0.05240 329  VAL A CB    
2558 C  CG1   . VAL A 329 ? 0.32590 0.17230 0.21660 0.01760  -0.04710 -0.03800 329  VAL A CG1   
2559 C  CG2   . VAL A 329 ? 0.38480 0.27290 0.20640 0.01580  -0.05060 -0.07180 329  VAL A CG2   
2560 N  N     . TYR A 330 ? 0.31980 0.23910 0.20010 0.06600  -0.05680 -0.04050 330  TYR A N     
2561 C  CA    . TYR A 330 ? 0.36570 0.20360 0.18890 0.08020  -0.08810 0.00190  330  TYR A CA    
2562 C  C     . TYR A 330 ? 0.38530 0.23720 0.21800 0.04450  -0.10460 0.01660  330  TYR A C     
2563 O  O     . TYR A 330 ? 0.41480 0.25770 0.23150 0.00760  -0.08790 0.04300  330  TYR A O     
2564 C  CB    . TYR A 330 ? 0.33740 0.20990 0.16260 0.07010  -0.04500 0.00750  330  TYR A CB    
2565 C  CG    . TYR A 330 ? 0.34980 0.19000 0.12690 0.05220  -0.05400 0.01160  330  TYR A CG    
2566 C  CD1   . TYR A 330 ? 0.34360 0.17880 0.13260 0.06730  -0.02810 -0.00360 330  TYR A CD1   
2567 C  CD2   . TYR A 330 ? 0.34620 0.17190 0.15040 0.02550  -0.04290 0.02480  330  TYR A CD2   
2568 C  CE1   . TYR A 330 ? 0.35250 0.22830 0.14020 0.06830  -0.00800 0.01530  330  TYR A CE1   
2569 C  CE2   . TYR A 330 ? 0.32930 0.17430 0.14780 0.05400  -0.03540 0.01830  330  TYR A CE2   
2570 C  CZ    . TYR A 330 ? 0.33870 0.19910 0.13900 0.06420  -0.00330 0.01280  330  TYR A CZ    
2571 O  OH    . TYR A 330 ? 0.33630 0.23300 0.14280 0.04010  -0.01060 0.03140  330  TYR A OH    
2572 N  N     . GLU A 331 ? 0.40140 0.29110 0.23850 0.08410  -0.11240 0.03460  331  GLU A N     
2573 C  CA    . GLU A 331 ? 0.44070 0.31200 0.25280 0.08540  -0.10120 0.07090  331  GLU A CA    
2574 C  C     . GLU A 331 ? 0.46200 0.26330 0.25190 0.03740  -0.09620 0.02510  331  GLU A C     
2575 O  O     . GLU A 331 ? 0.45860 0.24780 0.25720 0.04370  -0.10570 -0.01530 331  GLU A O     
2576 C  CB    . GLU A 331 ? 0.41870 0.51750 0.29440 0.12190  -0.08380 0.11970  331  GLU A CB    
2577 C  CG    . GLU A 331 ? 0.46400 0.74780 0.35330 0.08970  -0.06490 0.11660  331  GLU A CG    
2578 C  CD    . GLU A 331 ? 0.48210 0.98470 0.39710 0.08010  -0.04370 0.09240  331  GLU A CD    
2579 O  OE1   . GLU A 331 ? 0.45460 1.04490 0.41170 0.07810  -0.02070 0.07520  331  GLU A OE1   
2580 O  OE2   . GLU A 331 ? 0.53280 1.10420 0.42120 0.04070  -0.04630 0.05440  331  GLU A OE2   
2581 N  N     . ASP A 332 ? 0.48120 0.29030 0.25060 0.06230  -0.10190 0.03160  332  ASP A N     
2582 C  CA    A ASP A 332 ? 0.48840 0.32710 0.23940 0.03620  -0.14800 0.02840  332  ASP A CA    
2583 C  CA    B ASP A 332 ? 0.46570 0.28520 0.24850 0.07730  -0.11750 0.02590  332  ASP A CA    
2584 C  C     . ASP A 332 ? 0.50210 0.26050 0.22540 0.04270  -0.11200 0.02590  332  ASP A C     
2585 O  O     . ASP A 332 ? 0.49059 0.27230 0.21201 0.05880  -0.13069 0.03590  332  ASP A O     
2586 C  CB    A ASP A 332 ? 0.54270 0.39230 0.25330 0.01700  -0.16400 0.03420  332  ASP A CB    
2587 C  CB    B ASP A 332 ? 0.44410 0.27940 0.27450 0.14410  -0.09640 0.01980  332  ASP A CB    
2588 C  CG    A ASP A 332 ? 0.64820 0.42830 0.27170 -0.03570 -0.14850 0.07190  332  ASP A CG    
2589 C  CG    B ASP A 332 ? 0.49220 0.26500 0.29610 0.16140  -0.05490 0.04850  332  ASP A CG    
2590 O  OD1   A ASP A 332 ? 0.72340 0.47960 0.29540 -0.04940 -0.15080 0.03920  332  ASP A OD1   
2591 O  OD1   B ASP A 332 ? 0.50500 0.28570 0.30570 0.15690  -0.04560 0.07730  332  ASP A OD1   
2592 O  OD2   A ASP A 332 ? 0.65430 0.41410 0.27960 -0.06590 -0.16130 0.07130  332  ASP A OD2   
2593 O  OD2   B ASP A 332 ? 0.51519 0.27910 0.29770 0.16799  -0.06010 0.05510  332  ASP A OD2   
2594 N  N     . PRO A 333 ? 0.46300 0.22680 0.23450 0.06270  -0.11340 0.03960  333  PRO A N     
2595 C  CA    . PRO A 333 ? 0.39910 0.24380 0.21090 0.05460  -0.10870 0.04810  333  PRO A CA    
2596 C  C     . PRO A 333 ? 0.48240 0.22430 0.20040 0.04030  -0.05930 0.06870  333  PRO A C     
2597 O  O     . PRO A 333 ? 0.48320 0.23160 0.20020 0.03730  -0.06980 0.05930  333  PRO A O     
2598 C  CB    . PRO A 333 ? 0.40440 0.18800 0.22390 0.02700  -0.11920 0.03570  333  PRO A CB    
2599 C  CG    . PRO A 333 ? 0.39260 0.22820 0.24210 0.07300  -0.10170 0.03050  333  PRO A CG    
2600 C  CD    . PRO A 333 ? 0.43640 0.17840 0.24460 0.05190  -0.11260 0.04320  333  PRO A CD    
2601 N  N     . ASP A 334 ? 0.47740 0.27020 0.19100 0.01510  -0.04700 0.06530  334  ASP A N     
2602 C  CA    . ASP A 334 ? 0.54960 0.25590 0.19210 -0.00460 -0.05530 0.06930  334  ASP A CA    
2603 C  C     . ASP A 334 ? 0.53757 0.24161 0.19952 0.03809  -0.07149 0.06239  334  ASP A C     
2604 O  O     . ASP A 334 ? 0.64578 0.27490 0.19442 0.04970  -0.04160 0.04929  334  ASP A O     
2605 C  CB    . ASP A 334 ? 0.55330 0.29310 0.21370 0.01710  -0.09120 0.08170  334  ASP A CB    
2606 C  CG    . ASP A 334 ? 0.55929 0.32040 0.23611 0.01560  -0.07580 0.11429  334  ASP A CG    
2607 O  OD1   . ASP A 334 ? 0.48890 0.22380 0.22720 0.04480  -0.04100 0.09060  334  ASP A OD1   
2608 O  OD2   . ASP A 334 ? 0.67339 0.38780 0.26221 -0.01370 -0.05520 0.13709  334  ASP A OD2   
2609 N  N     . ALA A 335 ? 0.54020 0.26220 0.19850 0.01920  -0.11090 0.04810  335  ALA A N     
2610 C  CA    . ALA A 335 ? 0.54520 0.24770 0.22030 0.05040  -0.12770 0.03740  335  ALA A CA    
2611 C  C     . ALA A 335 ? 0.53840 0.23030 0.21180 0.04090  -0.09490 0.03250  335  ALA A C     
2612 O  O     . ALA A 335 ? 0.53550 0.21730 0.21900 0.04030  -0.08100 0.01080  335  ALA A O     
2613 C  CB    . ALA A 335 ? 0.57210 0.29670 0.23490 0.05640  -0.13410 0.05100  335  ALA A CB    
2614 N  N     . LEU A 336 ? 0.51810 0.23520 0.20580 0.01150  -0.09850 0.02340  336  LEU A N     
2615 C  CA    . LEU A 336 ? 0.45250 0.23680 0.19710 0.07500  -0.05280 -0.01200 336  LEU A CA    
2616 C  C     . LEU A 336 ? 0.46320 0.26270 0.19540 0.10060  -0.04130 0.01050  336  LEU A C     
2617 O  O     . LEU A 336 ? 0.42780 0.31200 0.20450 0.08930  -0.08180 0.02690  336  LEU A O     
2618 C  CB    . LEU A 336 ? 0.45760 0.25440 0.17770 0.11090  -0.06580 -0.02380 336  LEU A CB    
2619 C  CG    . LEU A 336 ? 0.43110 0.32980 0.18200 0.04990  -0.08240 -0.01360 336  LEU A CG    
2620 C  CD1   . LEU A 336 ? 0.45750 0.35470 0.16670 0.03850  -0.10370 -0.01300 336  LEU A CD1   
2621 C  CD2   . LEU A 336 ? 0.48330 0.34100 0.18310 0.10760  -0.06320 -0.02610 336  LEU A CD2   
2622 N  N     . ASP A 337 ? 0.38740 0.23060 0.16240 0.07100  -0.05790 0.01910  337  ASP A N     
2623 C  CA    . ASP A 337 ? 0.36970 0.24710 0.18690 0.02990  -0.02790 0.01690  337  ASP A CA    
2624 C  C     . ASP A 337 ? 0.41040 0.21890 0.20200 0.04730  -0.06190 -0.00170 337  ASP A C     
2625 O  O     . ASP A 337 ? 0.41350 0.30670 0.18890 0.04910  -0.07230 -0.01540 337  ASP A O     
2626 C  CB    . ASP A 337 ? 0.35540 0.24700 0.21440 0.07940  -0.03920 0.01530  337  ASP A CB    
2627 C  CG    . ASP A 337 ? 0.39880 0.34030 0.24800 0.08910  -0.05480 0.04580  337  ASP A CG    
2628 O  OD1   . ASP A 337 ? 0.35890 0.42220 0.27300 0.05700  -0.09680 0.04070  337  ASP A OD1   
2629 O  OD2   . ASP A 337 ? 0.40040 0.35930 0.25690 0.10130  -0.02910 0.05650  337  ASP A OD2   
2630 N  N     . ILE A 338 ? 0.37520 0.28730 0.21850 0.03130  -0.06660 -0.00530 338  ILE A N     
2631 C  CA    . ILE A 338 ? 0.37710 0.27140 0.25500 0.07950  -0.07260 0.01390  338  ILE A CA    
2632 C  C     . ILE A 338 ? 0.38470 0.29420 0.26970 0.02170  -0.09940 0.02680  338  ILE A C     
2633 O  O     . ILE A 338 ? 0.40720 0.32540 0.29720 -0.01000 -0.08520 0.06100  338  ILE A O     
2634 C  CB    . ILE A 338 ? 0.44650 0.28780 0.25800 0.11490  -0.06310 -0.02010 338  ILE A CB    
2635 C  CG1   . ILE A 338 ? 0.48350 0.31070 0.26220 0.07140  -0.08330 -0.06090 338  ILE A CG1   
2636 C  CG2   . ILE A 338 ? 0.45420 0.26150 0.26360 0.10850  -0.04130 -0.00070 338  ILE A CG2   
2637 C  CD1   . ILE A 338 ? 0.53560 0.37870 0.27090 0.04680  -0.08620 -0.07680 338  ILE A CD1   
2638 N  N     . HIS A 339 ? 0.34410 0.30410 0.27850 0.03390  -0.12160 0.00520  339  HIS A N     
2639 C  CA    . HIS A 339 ? 0.37660 0.35860 0.28510 0.01820  -0.12700 -0.01730 339  HIS A CA    
2640 C  C     . HIS A 339 ? 0.37050 0.38850 0.25770 -0.01040 -0.08020 -0.02660 339  HIS A C     
2641 O  O     . HIS A 339 ? 0.42140 0.45640 0.26090 -0.04930 -0.04730 -0.04310 339  HIS A O     
2642 C  CB    . HIS A 339 ? 0.40260 0.39600 0.31280 0.02870  -0.14760 -0.05540 339  HIS A CB    
2643 C  CG    . HIS A 339 ? 0.47810 0.39930 0.35150 0.05790  -0.16520 -0.05980 339  HIS A CG    
2644 N  ND1   . HIS A 339 ? 0.51770 0.40960 0.36610 0.10400  -0.14430 -0.05220 339  HIS A ND1   
2645 C  CD2   . HIS A 339 ? 0.55840 0.39110 0.35470 0.08480  -0.16020 -0.05630 339  HIS A CD2   
2646 C  CE1   . HIS A 339 ? 0.57670 0.38420 0.36610 0.09270  -0.15020 -0.06080 339  HIS A CE1   
2647 N  NE2   . HIS A 339 ? 0.62190 0.38440 0.36470 0.09480  -0.16410 -0.04100 339  HIS A NE2   
2648 N  N     . ARG A 340 ? 0.37200 0.31150 0.23840 0.00090  -0.10000 -0.00120 340  ARG A N     
2649 C  CA    . ARG A 340 ? 0.37780 0.32060 0.22010 0.01970  -0.07100 0.00690  340  ARG A CA    
2650 C  C     . ARG A 340 ? 0.36070 0.39930 0.22520 -0.01790 -0.05750 -0.00050 340  ARG A C     
2651 O  O     . ARG A 340 ? 0.37670 0.39300 0.24160 -0.02070 -0.07870 0.05040  340  ARG A O     
2652 C  CB    . ARG A 340 ? 0.35650 0.31610 0.21540 0.05910  -0.02380 0.04300  340  ARG A CB    
2653 C  CG    . ARG A 340 ? 0.35560 0.29610 0.21650 0.01660  0.00380  0.04410  340  ARG A CG    
2654 C  CD    . ARG A 340 ? 0.37300 0.26220 0.20260 0.00700  -0.02120 0.06320  340  ARG A CD    
2655 N  NE    . ARG A 340 ? 0.42450 0.24300 0.16870 0.05300  -0.04230 0.02610  340  ARG A NE    
2656 C  CZ    . ARG A 340 ? 0.41820 0.25410 0.15780 0.00150  -0.07450 0.00830  340  ARG A CZ    
2657 N  NH1   . ARG A 340 ? 0.40020 0.27490 0.21000 -0.00810 -0.08020 -0.03960 340  ARG A NH1   
2658 N  NH2   . ARG A 340 ? 0.46300 0.25850 0.15160 0.01190  -0.05220 0.01940  340  ARG A NH2   
2659 N  N     . SER A 341 ? 0.35600 0.51530 0.19480 -0.04350 -0.04400 0.01980  341  SER A N     
2660 C  CA    . SER A 341 ? 0.35900 0.60510 0.19680 -0.04030 -0.02920 0.00010  341  SER A CA    
2661 C  C     . SER A 341 ? 0.31940 0.50540 0.19350 -0.01350 -0.02920 -0.05280 341  SER A C     
2662 O  O     . SER A 341 ? 0.30830 0.53370 0.23130 0.01620  -0.03320 -0.10190 341  SER A O     
2663 C  CB    . SER A 341 ? 0.38090 0.69830 0.18910 0.00340  -0.02260 -0.01490 341  SER A CB    
2664 O  OG    . SER A 341 ? 0.46320 0.79940 0.22570 -0.05220 -0.02050 -0.00740 341  SER A OG    
2665 N  N     . ALA A 342 ? 0.33310 0.37550 0.17870 -0.00730 -0.02070 -0.00920 342  ALA A N     
2666 C  CA    . ALA A 342 ? 0.34100 0.27010 0.16170 0.00300  -0.02280 -0.00570 342  ALA A CA    
2667 C  C     . ALA A 342 ? 0.29830 0.25120 0.14870 0.06530  0.00020  0.01820  342  ALA A C     
2668 O  O     . ALA A 342 ? 0.32130 0.25230 0.16720 0.05730  -0.00910 0.03860  342  ALA A O     
2669 C  CB    . ALA A 342 ? 0.39330 0.23480 0.16300 -0.00200 -0.00720 -0.01460 342  ALA A CB    
2670 N  N     . ARG A 343 ? 0.33560 0.31730 0.12670 -0.02010 0.00140  0.05570  343  ARG A N     
2671 C  CA    A ARG A 343 ? 0.34070 0.29430 0.13210 -0.05440 -0.00250 0.03640  343  ARG A CA    
2672 C  CA    B ARG A 343 ? 0.36510 0.34310 0.13980 -0.07320 -0.01220 0.04130  343  ARG A CA    
2673 C  C     . ARG A 343 ? 0.30380 0.23000 0.12860 -0.00310 0.00440  0.03860  343  ARG A C     
2674 O  O     . ARG A 343 ? 0.34330 0.25500 0.12640 0.04070  -0.01070 0.05960  343  ARG A O     
2675 C  CB    A ARG A 343 ? 0.34140 0.24770 0.14480 -0.10010 0.00480  0.02320  343  ARG A CB    
2676 C  CB    B ARG A 343 ? 0.39430 0.38130 0.17610 -0.13290 -0.03600 0.05830  343  ARG A CB    
2677 C  CG    A ARG A 343 ? 0.32720 0.26550 0.14620 -0.07320 0.00480  0.01120  343  ARG A CG    
2678 C  CG    B ARG A 343 ? 0.36380 0.39160 0.20230 -0.11570 -0.02820 0.05170  343  ARG A CG    
2679 C  CD    A ARG A 343 ? 0.32700 0.22960 0.14010 -0.00640 -0.01230 0.00070  343  ARG A CD    
2680 C  CD    B ARG A 343 ? 0.38790 0.39250 0.22170 -0.08260 0.01990  0.07040  343  ARG A CD    
2681 N  NE    A ARG A 343 ? 0.34660 0.27650 0.14430 -0.01970 -0.00610 0.00320  343  ARG A NE    
2682 N  NE    B ARG A 343 ? 0.39250 0.36340 0.23050 -0.09200 0.05980  0.08690  343  ARG A NE    
2683 C  CZ    A ARG A 343 ? 0.32180 0.24570 0.14900 -0.00700 0.01550  0.03780  343  ARG A CZ    
2684 C  CZ    B ARG A 343 ? 0.42250 0.37900 0.24380 -0.06600 0.09740  0.08620  343  ARG A CZ    
2685 N  NH1   A ARG A 343 ? 0.35600 0.22220 0.14990 0.03020  0.02290  0.03140  343  ARG A NH1   
2686 N  NH1   B ARG A 343 ? 0.48450 0.37220 0.25800 -0.00770 0.09990  0.03620  343  ARG A NH1   
2687 N  NH2   A ARG A 343 ? 0.32580 0.32170 0.15570 0.01220  -0.02020 0.05360  343  ARG A NH2   
2688 N  NH2   B ARG A 343 ? 0.44330 0.43360 0.25470 -0.05490 0.06090  0.08950  343  ARG A NH2   
2689 N  N     . HIS A 344 ? 0.26930 0.21530 0.13160 0.01270  -0.02380 0.01810  344  HIS A N     
2690 C  CA    . HIS A 344 ? 0.23300 0.22070 0.14450 0.01810  -0.01470 -0.00160 344  HIS A CA    
2691 C  C     . HIS A 344 ? 0.28630 0.19450 0.11790 0.03050  -0.00670 0.00700  344  HIS A C     
2692 O  O     . HIS A 344 ? 0.30630 0.18130 0.11610 0.02030  -0.02790 -0.00660 344  HIS A O     
2693 C  CB    . HIS A 344 ? 0.26620 0.25030 0.17230 0.07410  0.02940  0.02740  344  HIS A CB    
2694 C  CG    . HIS A 344 ? 0.37760 0.25110 0.21140 0.09120  0.02010  0.06870  344  HIS A CG    
2695 N  ND1   . HIS A 344 ? 0.43740 0.29130 0.23740 0.15150  0.06890  0.03740  344  HIS A ND1   
2696 C  CD2   . HIS A 344 ? 0.42580 0.32500 0.23460 0.08970  0.06990  0.04870  344  HIS A CD2   
2697 C  CE1   . HIS A 344 ? 0.41890 0.36370 0.24600 0.10150  0.08230  0.07950  344  HIS A CE1   
2698 N  NE2   . HIS A 344 ? 0.43390 0.34900 0.24450 0.09360  0.07370  0.06020  344  HIS A NE2   
2699 N  N     . HIS A 345 ? 0.27940 0.14950 0.11060 0.00350  0.00880  0.01370  345  HIS A N     
2700 C  CA    . HIS A 345 ? 0.26560 0.14650 0.10290 -0.00980 -0.01110 0.01090  345  HIS A CA    
2701 C  C     . HIS A 345 ? 0.27490 0.11010 0.12140 0.03920  -0.02060 -0.00420 345  HIS A C     
2702 O  O     . HIS A 345 ? 0.29290 0.13220 0.12560 0.00400  -0.01530 0.00310  345  HIS A O     
2703 C  CB    . HIS A 345 ? 0.28900 0.15510 0.10620 0.05260  -0.01510 -0.01350 345  HIS A CB    
2704 C  CG    . HIS A 345 ? 0.31120 0.16030 0.12240 0.04750  -0.01710 0.00520  345  HIS A CG    
2705 N  ND1   . HIS A 345 ? 0.28850 0.17120 0.12570 0.05730  -0.04770 -0.02490 345  HIS A ND1   
2706 C  CD2   . HIS A 345 ? 0.36180 0.16250 0.12450 -0.01370 0.00430  0.01600  345  HIS A CD2   
2707 C  CE1   . HIS A 345 ? 0.31050 0.15150 0.12610 0.05400  -0.05440 -0.03160 345  HIS A CE1   
2708 N  NE2   . HIS A 345 ? 0.30480 0.16830 0.11940 0.00300  -0.02730 -0.00150 345  HIS A NE2   
2709 N  N     . LEU A 346 ? 0.24680 0.13720 0.12380 0.01440  0.00500  0.01170  346  LEU A N     
2710 C  CA    . LEU A 346 ? 0.25320 0.11820 0.12390 0.00790  -0.01180 0.00920  346  LEU A CA    
2711 C  C     . LEU A 346 ? 0.26610 0.11520 0.11540 -0.02410 -0.01200 0.00680  346  LEU A C     
2712 O  O     . LEU A 346 ? 0.29420 0.12750 0.13570 0.00990  -0.01740 -0.00340 346  LEU A O     
2713 C  CB    . LEU A 346 ? 0.30550 0.10890 0.14930 0.00220  -0.00120 0.00790  346  LEU A CB    
2714 C  CG    . LEU A 346 ? 0.33830 0.12720 0.17380 0.03180  0.00010  -0.01720 346  LEU A CG    
2715 C  CD1   . LEU A 346 ? 0.36880 0.12550 0.21720 0.01380  0.02860  -0.00280 346  LEU A CD1   
2716 C  CD2   . LEU A 346 ? 0.34360 0.17920 0.16350 0.03530  0.00510  -0.02130 346  LEU A CD2   
2717 N  N     . ALA A 347 ? 0.26780 0.15470 0.09070 0.01590  -0.00350 0.00650  347  ALA A N     
2718 C  CA    . ALA A 347 ? 0.24350 0.15260 0.13470 0.01850  -0.00850 -0.00260 347  ALA A CA    
2719 C  C     . ALA A 347 ? 0.24540 0.15880 0.14900 -0.01580 -0.05040 0.00170  347  ALA A C     
2720 O  O     . ALA A 347 ? 0.26110 0.13870 0.16050 -0.01320 -0.03100 0.01000  347  ALA A O     
2721 C  CB    . ALA A 347 ? 0.26100 0.18210 0.14970 0.04410  -0.04350 -0.05060 347  ALA A CB    
2722 N  N     . PHE A 348 ? 0.29220 0.12920 0.12460 -0.00300 -0.03440 0.02340  348  PHE A N     
2723 C  CA    . PHE A 348 ? 0.28050 0.08940 0.12880 -0.01920 -0.01760 -0.00310 348  PHE A CA    
2724 C  C     . PHE A 348 ? 0.29170 0.09640 0.13610 -0.00250 -0.00930 -0.02300 348  PHE A C     
2725 O  O     . PHE A 348 ? 0.26750 0.13800 0.16650 -0.01520 -0.03160 -0.00140 348  PHE A O     
2726 C  CB    . PHE A 348 ? 0.28199 0.10951 0.11481 -0.04479 -0.01620 -0.02919 348  PHE A CB    
2727 C  CG    . PHE A 348 ? 0.30850 0.12420 0.10620 -0.02740 -0.03170 -0.00880 348  PHE A CG    
2728 C  CD1   . PHE A 348 ? 0.32120 0.15830 0.11720 -0.04030 0.01050  0.00570  348  PHE A CD1   
2729 C  CD2   . PHE A 348 ? 0.31660 0.12860 0.10160 -0.03870 -0.04370 0.01120  348  PHE A CD2   
2730 C  CE1   . PHE A 348 ? 0.29750 0.16040 0.12180 -0.00290 0.00660  -0.00850 348  PHE A CE1   
2731 C  CE2   . PHE A 348 ? 0.32335 0.16560 0.08385 -0.01769 -0.02099 0.00580  348  PHE A CE2   
2732 C  CZ    . PHE A 348 ? 0.36520 0.11270 0.10490 -0.03260 -0.01440 0.00990  348  PHE A CZ    
2733 N  N     . GLY A 349 ? 0.29050 0.11790 0.13510 0.00910  -0.01580 -0.03180 349  GLY A N     
2734 C  CA    . GLY A 349 ? 0.30460 0.16490 0.14430 0.01620  -0.03350 -0.06420 349  GLY A CA    
2735 C  C     . GLY A 349 ? 0.28120 0.10160 0.15850 -0.01080 -0.04170 -0.03170 349  GLY A C     
2736 O  O     . GLY A 349 ? 0.27110 0.15510 0.18110 -0.00710 -0.04920 -0.03720 349  GLY A O     
2737 N  N     . PHE A 350 ? 0.29720 0.11830 0.15760 -0.01090 -0.02310 -0.01590 350  PHE A N     
2738 C  CA    . PHE A 350 ? 0.31590 0.17920 0.16230 0.03260  -0.04500 0.00110  350  PHE A CA    
2739 C  C     . PHE A 350 ? 0.31270 0.19550 0.15500 0.04870  -0.05220 -0.03010 350  PHE A C     
2740 O  O     . PHE A 350 ? 0.37630 0.15380 0.19940 0.02780  -0.07510 -0.04620 350  PHE A O     
2741 C  CB    . PHE A 350 ? 0.36168 0.10892 0.20380 0.05509  -0.05449 -0.00990 350  PHE A CB    
2742 C  CG    . PHE A 350 ? 0.32670 0.12880 0.24020 0.03340  -0.05080 -0.06420 350  PHE A CG    
2743 C  CD1   . PHE A 350 ? 0.27050 0.18210 0.25770 0.02570  -0.04630 -0.05730 350  PHE A CD1   
2744 C  CD2   . PHE A 350 ? 0.33680 0.20680 0.23180 0.00030  -0.01160 -0.10260 350  PHE A CD2   
2745 C  CE1   . PHE A 350 ? 0.31900 0.22160 0.27530 0.01750  -0.04040 -0.07890 350  PHE A CE1   
2746 C  CE2   . PHE A 350 ? 0.32900 0.19820 0.25920 0.02280  -0.01130 -0.10070 350  PHE A CE2   
2747 C  CZ    . PHE A 350 ? 0.29580 0.19660 0.27180 -0.03680 -0.02830 -0.06800 350  PHE A CZ    
2748 N  N     . GLY A 351 ? 0.33530 0.20420 0.16690 0.06180  -0.04530 -0.03760 351  GLY A N     
2749 C  CA    . GLY A 351 ? 0.34870 0.21660 0.16700 0.12260  -0.08210 -0.02230 351  GLY A CA    
2750 C  C     . GLY A 351 ? 0.31610 0.25410 0.16330 0.06230  -0.09910 -0.02650 351  GLY A C     
2751 O  O     . GLY A 351 ? 0.36130 0.23680 0.16060 0.01180  -0.05460 -0.03910 351  GLY A O     
2752 N  N     . VAL A 352 ? 0.34349 0.27559 0.15932 0.12659  -0.09358 -0.05939 352  VAL A N     
2753 C  CA    . VAL A 352 ? 0.33280 0.28020 0.17520 0.11110  -0.09790 -0.06350 352  VAL A CA    
2754 C  C     . VAL A 352 ? 0.34150 0.23720 0.17040 0.06650  -0.07040 -0.04650 352  VAL A C     
2755 O  O     . VAL A 352 ? 0.32860 0.23840 0.16890 0.05890  -0.05850 -0.03050 352  VAL A O     
2756 C  CB    . VAL A 352 ? 0.34970 0.32890 0.19690 0.04910  -0.09720 -0.08560 352  VAL A CB    
2757 C  CG1   . VAL A 352 ? 0.36560 0.32060 0.21640 0.04030  -0.08230 -0.10740 352  VAL A CG1   
2758 C  CG2   . VAL A 352 ? 0.36460 0.29950 0.23610 -0.00050 -0.07320 -0.07130 352  VAL A CG2   
2759 N  N     . HIS A 353 ? 0.29360 0.18010 0.16680 0.03440  -0.02910 -0.06610 353  HIS A N     
2760 C  CA    . HIS A 353 ? 0.29550 0.17840 0.18310 -0.00320 -0.06240 -0.03800 353  HIS A CA    
2761 C  C     . HIS A 353 ? 0.28820 0.17200 0.17430 -0.01540 -0.04790 -0.03850 353  HIS A C     
2762 O  O     . HIS A 353 ? 0.32050 0.18750 0.17160 0.01450  -0.05280 -0.04280 353  HIS A O     
2763 C  CB    . HIS A 353 ? 0.30290 0.16050 0.20610 0.04000  -0.09330 0.00830  353  HIS A CB    
2764 C  CG    . HIS A 353 ? 0.29430 0.16950 0.21140 0.08650  -0.08690 -0.04020 353  HIS A CG    
2765 N  ND1   . HIS A 353 ? 0.35400 0.17020 0.20430 0.04670  -0.10590 -0.05530 353  HIS A ND1   
2766 C  CD2   . HIS A 353 ? 0.30830 0.15710 0.23100 0.03960  -0.07670 -0.04160 353  HIS A CD2   
2767 C  CE1   . HIS A 353 ? 0.34190 0.17000 0.21710 0.04020  -0.08220 -0.06420 353  HIS A CE1   
2768 N  NE2   . HIS A 353 ? 0.31130 0.19410 0.22870 0.07610  -0.07400 -0.05440 353  HIS A NE2   
2769 N  N     . GLN A 354 ? 0.30620 0.16170 0.15770 0.02030  -0.04850 -0.03770 354  GLN A N     
2770 C  CA    A GLN A 354 ? 0.25480 0.15500 0.15070 -0.01210 -0.06090 -0.02140 354  GLN A CA    
2771 C  CA    B GLN A 354 ? 0.24880 0.19580 0.14650 -0.00750 -0.06300 -0.01600 354  GLN A CA    
2772 C  C     . GLN A 354 ? 0.28740 0.11790 0.14330 0.01410  -0.04680 -0.02060 354  GLN A C     
2773 O  O     . GLN A 354 ? 0.33900 0.12640 0.17420 0.03070  -0.05330 -0.01980 354  GLN A O     
2774 C  CB    A GLN A 354 ? 0.25140 0.14670 0.13710 0.01790  -0.03830 0.00350  354  GLN A CB    
2775 C  CB    B GLN A 354 ? 0.22590 0.27700 0.13150 -0.01560 -0.05410 0.02770  354  GLN A CB    
2776 C  CG    A GLN A 354 ? 0.25070 0.12000 0.14760 -0.00960 -0.02190 -0.00360 354  GLN A CG    
2777 C  CG    B GLN A 354 ? 0.21160 0.33250 0.12450 0.00470  -0.05160 0.02780  354  GLN A CG    
2778 C  CD    A GLN A 354 ? 0.25440 0.09060 0.14350 -0.01540 0.00960  0.00540  354  GLN A CD    
2779 C  CD    B GLN A 354 ? 0.27240 0.34580 0.14030 0.04440  -0.07550 0.04560  354  GLN A CD    
2780 O  OE1   A GLN A 354 ? 0.26628 0.07212 0.14230 0.02670  0.01790  0.00760  354  GLN A OE1   
2781 O  OE1   B GLN A 354 ? 0.30420 0.35970 0.14820 0.04110  -0.05780 0.08090  354  GLN A OE1   
2782 N  NE2   A GLN A 354 ? 0.28989 0.08451 0.14700 -0.03340 0.00170  0.01990  354  GLN A NE2   
2783 N  NE2   B GLN A 354 ? 0.28600 0.35870 0.14090 0.07790  -0.07000 0.02140  354  GLN A NE2   
2784 N  N     . CYS A 355 ? 0.28570 0.11870 0.13120 0.02500  -0.03190 -0.02950 355  CYS A N     
2785 C  CA    . CYS A 355 ? 0.30740 0.14180 0.12470 0.03390  -0.02100 -0.00280 355  CYS A CA    
2786 C  C     . CYS A 355 ? 0.28980 0.16130 0.13860 0.02490  -0.01960 -0.00680 355  CYS A C     
2787 O  O     . CYS A 355 ? 0.26090 0.17130 0.14520 0.01200  0.00410  -0.00180 355  CYS A O     
2788 C  CB    . CYS A 355 ? 0.34780 0.16300 0.12360 -0.00580 -0.05990 -0.03200 355  CYS A CB    
2789 S  SG    . CYS A 355 ? 0.34080 0.12940 0.12820 0.00990  -0.00000 -0.01760 355  CYS A SG    
2790 N  N     . LEU A 356 ? 0.33730 0.13590 0.15430 0.05750  -0.07320 -0.02470 356  LEU A N     
2791 C  CA    . LEU A 356 ? 0.36510 0.13270 0.16290 0.02860  -0.08740 -0.00460 356  LEU A CA    
2792 C  C     . LEU A 356 ? 0.32190 0.14920 0.14070 -0.00830 -0.04220 0.01450  356  LEU A C     
2793 O  O     . LEU A 356 ? 0.30990 0.16640 0.15550 0.02470  -0.00630 0.01540  356  LEU A O     
2794 C  CB    . LEU A 356 ? 0.41869 0.15981 0.20690 0.06349  -0.11969 0.00589  356  LEU A CB    
2795 C  CG    . LEU A 356 ? 0.42527 0.20101 0.20052 0.06528  -0.11387 0.02549  356  LEU A CG    
2796 C  CD1   . LEU A 356 ? 0.62859 0.27510 0.21721 0.02910  -0.07190 0.06740  356  LEU A CD1   
2797 C  CD2   . LEU A 356 ? 0.39060 0.25380 0.25530 0.03450  -0.13640 0.04290  356  LEU A CD2   
2798 N  N     . GLY A 357 ? 0.30100 0.14050 0.10840 0.01620  -0.03660 -0.04160 357  GLY A N     
2799 C  CA    . GLY A 357 ? 0.32719 0.13201 0.12421 0.04460  -0.02080 -0.04169 357  GLY A CA    
2800 C  C     . GLY A 357 ? 0.24830 0.15760 0.14200 0.02440  -0.00090 -0.00510 357  GLY A C     
2801 O  O     . GLY A 357 ? 0.30510 0.14690 0.15920 0.02860  0.00580  -0.03590 357  GLY A O     
2802 N  N     . GLN A 358 ? 0.23680 0.15360 0.15620 0.04840  -0.00070 0.00420  358  GLN A N     
2803 C  CA    . GLN A 358 ? 0.24910 0.09510 0.15710 0.00760  -0.02010 -0.02090 358  GLN A CA    
2804 C  C     . GLN A 358 ? 0.28770 0.13670 0.16310 -0.00520 0.00450  0.02310  358  GLN A C     
2805 O  O     . GLN A 358 ? 0.32520 0.19620 0.16420 0.02050  -0.02190 -0.01650 358  GLN A O     
2806 C  CB    . GLN A 358 ? 0.29450 0.13010 0.16040 0.04050  0.00310  -0.00140 358  GLN A CB    
2807 C  CG    . GLN A 358 ? 0.31920 0.11850 0.14590 0.00990  0.04390  -0.01230 358  GLN A CG    
2808 C  CD    . GLN A 358 ? 0.31120 0.16260 0.17770 -0.04190 0.02290  -0.02120 358  GLN A CD    
2809 O  OE1   . GLN A 358 ? 0.42070 0.22680 0.18910 -0.00320 0.05100  -0.01420 358  GLN A OE1   
2810 N  NE2   . GLN A 358 ? 0.33300 0.23810 0.19510 0.04740  -0.00550 -0.03180 358  GLN A NE2   
2811 N  N     . ASN A 359 ? 0.28980 0.11640 0.18770 -0.03480 0.03200  -0.01520 359  ASN A N     
2812 C  CA    . ASN A 359 ? 0.31210 0.17280 0.17950 -0.00580 0.03500  -0.01700 359  ASN A CA    
2813 C  C     . ASN A 359 ? 0.29500 0.13030 0.18290 0.00320  0.01760  -0.03070 359  ASN A C     
2814 O  O     . ASN A 359 ? 0.29770 0.13320 0.19730 -0.02430 -0.00180 -0.01340 359  ASN A O     
2815 C  CB    . ASN A 359 ? 0.36740 0.20330 0.16610 -0.02580 0.05480  -0.01530 359  ASN A CB    
2816 C  CG    . ASN A 359 ? 0.33870 0.17340 0.16180 0.01140  0.05160  0.03630  359  ASN A CG    
2817 O  OD1   . ASN A 359 ? 0.36400 0.29940 0.16830 0.07460  0.01690  0.09630  359  ASN A OD1   
2818 N  ND2   . ASN A 359 ? 0.40600 0.23230 0.13760 -0.00120 0.03560  0.03800  359  ASN A ND2   
2819 N  N     . LEU A 360 ? 0.29110 0.12010 0.17260 0.02840  0.00910  -0.00870 360  LEU A N     
2820 C  CA    . LEU A 360 ? 0.28120 0.12040 0.15790 0.03930  -0.01050 0.01810  360  LEU A CA    
2821 C  C     . LEU A 360 ? 0.31680 0.10860 0.14190 0.02890  0.00180  0.03280  360  LEU A C     
2822 O  O     . LEU A 360 ? 0.31910 0.15250 0.16470 -0.00200 -0.02980 -0.01710 360  LEU A O     
2823 C  CB    . LEU A 360 ? 0.28280 0.08970 0.17240 0.02840  -0.01730 -0.02560 360  LEU A CB    
2824 C  CG    . LEU A 360 ? 0.34880 0.11200 0.19580 0.01340  -0.04610 -0.03950 360  LEU A CG    
2825 C  CD1   . LEU A 360 ? 0.43790 0.14160 0.17720 0.03490  -0.01200 -0.03020 360  LEU A CD1   
2826 C  CD2   . LEU A 360 ? 0.31580 0.25140 0.21560 0.01820  -0.06080 -0.03800 360  LEU A CD2   
2827 N  N     . ALA A 361 ? 0.30920 0.10430 0.16950 -0.01040 -0.00120 0.02580  361  ALA A N     
2828 C  CA    . ALA A 361 ? 0.29070 0.09780 0.17040 -0.03330 -0.01640 0.01970  361  ALA A CA    
2829 C  C     . ALA A 361 ? 0.27500 0.12280 0.15740 0.00560  -0.01320 0.00970  361  ALA A C     
2830 O  O     . ALA A 361 ? 0.30350 0.15040 0.14230 0.00890  -0.02870 -0.01850 361  ALA A O     
2831 C  CB    . ALA A 361 ? 0.33960 0.09540 0.17550 -0.02270 -0.00670 0.00600  361  ALA A CB    
2832 N  N     . ARG A 362 ? 0.25790 0.18330 0.17650 -0.02300 -0.02560 0.00130  362  ARG A N     
2833 C  CA    . ARG A 362 ? 0.25920 0.16110 0.17430 -0.01780 -0.02750 -0.02090 362  ARG A CA    
2834 C  C     . ARG A 362 ? 0.27660 0.14580 0.18560 -0.04640 -0.04020 -0.02430 362  ARG A C     
2835 O  O     . ARG A 362 ? 0.31040 0.17600 0.21100 -0.02180 -0.03110 -0.02410 362  ARG A O     
2836 C  CB    . ARG A 362 ? 0.29890 0.14770 0.16930 -0.00670 -0.00280 0.00150  362  ARG A CB    
2837 C  CG    . ARG A 362 ? 0.30200 0.14120 0.15690 -0.02390 -0.00190 -0.01250 362  ARG A CG    
2838 C  CD    . ARG A 362 ? 0.30660 0.12430 0.15520 0.00250  0.00420  -0.03920 362  ARG A CD    
2839 N  NE    . ARG A 362 ? 0.34590 0.12490 0.14810 0.02640  -0.02330 -0.03380 362  ARG A NE    
2840 C  CZ    . ARG A 362 ? 0.45270 0.19270 0.17510 0.03610  -0.06370 -0.03030 362  ARG A CZ    
2841 N  NH1   . ARG A 362 ? 0.57790 0.26030 0.19510 0.08290  -0.12210 -0.03280 362  ARG A NH1   
2842 N  NH2   . ARG A 362 ? 0.47030 0.25260 0.20520 0.03520  -0.07620 -0.03670 362  ARG A NH2   
2843 N  N     . LEU A 363 ? 0.32120 0.12980 0.17780 -0.03040 -0.02570 0.01170  363  LEU A N     
2844 C  CA    . LEU A 363 ? 0.33620 0.14620 0.20820 -0.00420 -0.01710 0.00710  363  LEU A CA    
2845 C  C     . LEU A 363 ? 0.33840 0.12680 0.19880 0.00920  -0.02310 -0.01400 363  LEU A C     
2846 O  O     . LEU A 363 ? 0.37050 0.13970 0.20690 -0.01370 -0.04230 -0.00840 363  LEU A O     
2847 C  CB    . LEU A 363 ? 0.34600 0.11600 0.22510 0.02230  -0.03930 -0.00870 363  LEU A CB    
2848 C  CG    . LEU A 363 ? 0.35190 0.12960 0.25010 0.01420  -0.05000 -0.01410 363  LEU A CG    
2849 C  CD1   . LEU A 363 ? 0.33000 0.16340 0.28540 -0.01020 -0.06690 -0.05220 363  LEU A CD1   
2850 C  CD2   . LEU A 363 ? 0.38960 0.12590 0.22870 0.02020  -0.01950 -0.00430 363  LEU A CD2   
2851 N  N     . GLU A 364 ? 0.32190 0.11590 0.20020 -0.01470 -0.01320 -0.01800 364  GLU A N     
2852 C  CA    . GLU A 364 ? 0.28090 0.12240 0.18480 -0.00560 -0.01420 -0.00490 364  GLU A CA    
2853 C  C     . GLU A 364 ? 0.33680 0.10410 0.19050 0.03620  -0.05300 -0.01210 364  GLU A C     
2854 O  O     . GLU A 364 ? 0.35560 0.13110 0.19830 0.02910  -0.04480 -0.02420 364  GLU A O     
2855 C  CB    . GLU A 364 ? 0.27190 0.15670 0.17190 -0.01300 0.00820  0.00500  364  GLU A CB    
2856 C  CG    . GLU A 364 ? 0.31840 0.19580 0.16380 0.05850  -0.02970 0.01000  364  GLU A CG    
2857 C  CD    . GLU A 364 ? 0.36910 0.17920 0.16760 0.08030  -0.02830 0.01380  364  GLU A CD    
2858 O  OE1   . GLU A 364 ? 0.38770 0.18440 0.17540 0.02210  -0.04370 0.01610  364  GLU A OE1   
2859 O  OE2   . GLU A 364 ? 0.38960 0.17140 0.17820 0.07250  -0.02060 -0.02540 364  GLU A OE2   
2860 N  N     . LEU A 365 ? 0.31490 0.12390 0.19110 0.02990  -0.05060 0.00740  365  LEU A N     
2861 C  CA    . LEU A 365 ? 0.32740 0.09180 0.19840 -0.01170 -0.05850 -0.01600 365  LEU A CA    
2862 C  C     . LEU A 365 ? 0.36940 0.13600 0.19700 0.04920  -0.05310 -0.01580 365  LEU A C     
2863 O  O     . LEU A 365 ? 0.36410 0.15990 0.19390 0.04350  -0.06860 -0.01740 365  LEU A O     
2864 C  CB    . LEU A 365 ? 0.35190 0.09650 0.18450 -0.02690 -0.03170 0.00300  365  LEU A CB    
2865 C  CG    . LEU A 365 ? 0.34900 0.12810 0.18940 -0.02100 0.00730  -0.02900 365  LEU A CG    
2866 C  CD1   . LEU A 365 ? 0.38980 0.12050 0.20140 0.00890  0.01820  -0.02120 365  LEU A CD1   
2867 C  CD2   . LEU A 365 ? 0.37880 0.18600 0.19850 0.00160  0.01380  -0.05780 365  LEU A CD2   
2868 N  N     . GLU A 366 ? 0.34490 0.14550 0.20900 0.01430  -0.04790 -0.03910 366  GLU A N     
2869 C  CA    . GLU A 366 ? 0.36610 0.16780 0.22100 0.01520  -0.06250 -0.06400 366  GLU A CA    
2870 C  C     . GLU A 366 ? 0.34850 0.14920 0.22480 0.02140  -0.07680 -0.05660 366  GLU A C     
2871 O  O     . GLU A 366 ? 0.39820 0.17690 0.21730 0.00110  -0.09050 -0.04960 366  GLU A O     
2872 C  CB    . GLU A 366 ? 0.33340 0.21820 0.24140 -0.06950 -0.05100 -0.07170 366  GLU A CB    
2873 C  CG    . GLU A 366 ? 0.39100 0.21770 0.26930 -0.01240 -0.08330 -0.07170 366  GLU A CG    
2874 C  CD    . GLU A 366 ? 0.43620 0.27110 0.29370 -0.00010 -0.09800 -0.04360 366  GLU A CD    
2875 O  OE1   . GLU A 366 ? 0.43750 0.22840 0.31490 -0.00300 -0.09830 -0.02190 366  GLU A OE1   
2876 O  OE2   . GLU A 366 ? 0.44240 0.29120 0.30240 -0.03440 -0.09760 0.00480  366  GLU A OE2   
2877 N  N     . VAL A 367 ? 0.39309 0.11521 0.23260 0.02190  -0.07210 -0.03400 367  VAL A N     
2878 C  CA    . VAL A 367 ? 0.41840 0.14160 0.21510 0.03610  -0.08550 -0.05190 367  VAL A CA    
2879 C  C     . VAL A 367 ? 0.42657 0.13612 0.22010 0.05309  -0.06339 -0.04529 367  VAL A C     
2880 O  O     . VAL A 367 ? 0.47718 0.16282 0.23330 0.00890  -0.08829 -0.05699 367  VAL A O     
2881 C  CB    . VAL A 367 ? 0.39410 0.16930 0.20550 0.02290  -0.05650 -0.05640 367  VAL A CB    
2882 C  CG1   . VAL A 367 ? 0.41196 0.17482 0.21651 0.01150  -0.03359 -0.08758 367  VAL A CG1   
2883 C  CG2   . VAL A 367 ? 0.41710 0.19140 0.21500 -0.02000 -0.03170 -0.03050 367  VAL A CG2   
2884 N  N     . ILE A 368 ? 0.42700 0.14690 0.21890 0.05360  -0.05280 -0.02120 368  ILE A N     
2885 C  CA    . ILE A 368 ? 0.33140 0.17350 0.19120 0.00950  -0.06830 -0.03830 368  ILE A CA    
2886 C  C     . ILE A 368 ? 0.41120 0.14310 0.19900 0.03040  -0.07850 -0.01190 368  ILE A C     
2887 O  O     . ILE A 368 ? 0.45080 0.19260 0.18320 0.06950  -0.09840 -0.03620 368  ILE A O     
2888 C  CB    . ILE A 368 ? 0.37920 0.19770 0.18780 -0.01020 -0.07180 -0.04180 368  ILE A CB    
2889 C  CG1   . ILE A 368 ? 0.36080 0.20060 0.21770 -0.00240 -0.09690 -0.06230 368  ILE A CG1   
2890 C  CG2   . ILE A 368 ? 0.41370 0.21180 0.18230 0.05430  -0.05980 -0.04940 368  ILE A CG2   
2891 C  CD1   . ILE A 368 ? 0.35510 0.17140 0.25850 0.02270  -0.08900 -0.00020 368  ILE A CD1   
2892 N  N     . LEU A 369 ? 0.39370 0.16090 0.20070 0.05080  -0.08580 -0.01100 369  LEU A N     
2893 C  CA    . LEU A 369 ? 0.39420 0.17020 0.19630 0.05140  -0.11450 -0.04290 369  LEU A CA    
2894 C  C     . LEU A 369 ? 0.44060 0.15030 0.20460 0.02660  -0.07410 -0.01630 369  LEU A C     
2895 O  O     . LEU A 369 ? 0.47710 0.23170 0.20610 0.06110  -0.06700 -0.07380 369  LEU A O     
2896 C  CB    . LEU A 369 ? 0.41360 0.16360 0.19780 0.06020  -0.09380 -0.04780 369  LEU A CB    
2897 C  CG    . LEU A 369 ? 0.42650 0.22380 0.19710 0.02630  -0.08480 -0.03760 369  LEU A CG    
2898 C  CD1   . LEU A 369 ? 0.47310 0.24920 0.21590 0.04450  -0.08400 -0.03650 369  LEU A CD1   
2899 C  CD2   . LEU A 369 ? 0.50180 0.28070 0.18130 0.03450  -0.10260 -0.03360 369  LEU A CD2   
2900 N  N     . ASN A 370 ? 0.45940 0.15820 0.23510 0.00370  -0.09370 -0.03640 370  ASN A N     
2901 C  CA    . ASN A 370 ? 0.38860 0.18980 0.24560 0.03650  -0.12380 -0.06640 370  ASN A CA    
2902 C  C     . ASN A 370 ? 0.41000 0.25190 0.25240 0.10630  -0.13370 -0.08930 370  ASN A C     
2903 O  O     . ASN A 370 ? 0.47490 0.28640 0.27600 0.04980  -0.16690 -0.06620 370  ASN A O     
2904 C  CB    . ASN A 370 ? 0.44350 0.23210 0.28600 0.03520  -0.10370 -0.05040 370  ASN A CB    
2905 C  CG    . ASN A 370 ? 0.45270 0.25910 0.30420 0.03090  -0.11900 -0.05510 370  ASN A CG    
2906 O  OD1   . ASN A 370 ? 0.43540 0.25870 0.30160 0.00350  -0.16300 -0.06660 370  ASN A OD1   
2907 N  ND2   . ASN A 370 ? 0.46370 0.21120 0.31370 0.00700  -0.08980 -0.07590 370  ASN A ND2   
2908 N  N     . ALA A 371 ? 0.43690 0.21560 0.25060 0.09320  -0.11660 -0.09520 371  ALA A N     
2909 C  CA    . ALA A 371 ? 0.44699 0.25551 0.25941 0.06090  -0.11749 -0.11519 371  ALA A CA    
2910 C  C     . ALA A 371 ? 0.45378 0.21182 0.27181 0.03470  -0.09179 -0.10708 371  ALA A C     
2911 O  O     . ALA A 371 ? 0.49740 0.24980 0.30480 0.06350  -0.12020 -0.12360 371  ALA A O     
2912 C  CB    . ALA A 371 ? 0.45490 0.26170 0.26710 0.04330  -0.09430 -0.12800 371  ALA A CB    
2913 N  N     . LEU A 372 ? 0.46960 0.19160 0.25380 0.05830  -0.12540 -0.07750 372  LEU A N     
2914 C  CA    . LEU A 372 ? 0.46830 0.26480 0.23900 0.01490  -0.13940 -0.08210 372  LEU A CA    
2915 C  C     . LEU A 372 ? 0.48680 0.27450 0.25460 0.02210  -0.13370 -0.09960 372  LEU A C     
2916 O  O     . LEU A 372 ? 0.53370 0.29870 0.26330 0.04640  -0.14530 -0.10300 372  LEU A O     
2917 C  CB    . LEU A 372 ? 0.46510 0.29490 0.22870 0.00140  -0.12480 -0.09150 372  LEU A CB    
2918 C  CG    . LEU A 372 ? 0.40738 0.25101 0.23121 0.03299  -0.07848 -0.11918 372  LEU A CG    
2919 C  CD1   . LEU A 372 ? 0.44660 0.26730 0.23260 0.07550  -0.06820 -0.10430 372  LEU A CD1   
2920 C  CD2   . LEU A 372 ? 0.42020 0.29880 0.23490 0.09550  -0.06900 -0.09130 372  LEU A CD2   
2921 N  N     . MET A 373 ? 0.46728 0.28931 0.27031 0.01890  -0.14198 -0.10918 373  MET A N     
2922 C  CA    . MET A 373 ? 0.44099 0.28540 0.28550 0.02170  -0.14279 -0.11849 373  MET A CA    
2923 C  C     . MET A 373 ? 0.49170 0.30640 0.30930 0.02530  -0.16920 -0.11590 373  MET A C     
2924 O  O     . MET A 373 ? 0.54050 0.33480 0.32100 0.04840  -0.15720 -0.14130 373  MET A O     
2925 C  CB    . MET A 373 ? 0.47690 0.23860 0.27350 0.07740  -0.16990 -0.08550 373  MET A CB    
2926 C  CG    . MET A 373 ? 0.48700 0.25500 0.28720 0.05380  -0.12630 -0.06790 373  MET A CG    
2927 S  SD    . MET A 373 ? 0.51250 0.27050 0.27890 0.05680  -0.14370 -0.09220 373  MET A SD    
2928 C  CE    . MET A 373 ? 0.50980 0.31140 0.27850 0.01480  -0.16850 -0.07410 373  MET A CE    
2929 N  N     . ASP A 374 ? 0.54300 0.26510 0.30390 0.04440  -0.16850 -0.10040 374  ASP A N     
2930 C  CA    . ASP A 374 ? 0.56467 0.28742 0.33471 0.00600  -0.16257 -0.11538 374  ASP A CA    
2931 C  C     . ASP A 374 ? 0.58060 0.28800 0.36280 0.02440  -0.15380 -0.13480 374  ASP A C     
2932 O  O     . ASP A 374 ? 0.60270 0.31940 0.40640 0.00190  -0.14720 -0.16210 374  ASP A O     
2933 C  CB    . ASP A 374 ? 0.59100 0.25740 0.34690 0.00440  -0.16980 -0.09370 374  ASP A CB    
2934 C  CG    . ASP A 374 ? 0.66700 0.29900 0.36470 -0.05610 -0.16820 -0.08440 374  ASP A CG    
2935 O  OD1   . ASP A 374 ? 0.70750 0.29160 0.39370 -0.03740 -0.14360 -0.11450 374  ASP A OD1   
2936 O  OD2   . ASP A 374 ? 0.66350 0.34790 0.37150 -0.08550 -0.16070 -0.06220 374  ASP A OD2   
2937 N  N     . ARG A 375 ? 0.61459 0.28361 0.34770 0.03870  -0.12779 -0.13429 375  ARG A N     
2938 C  CA    . ARG A 375 ? 0.61540 0.27380 0.35960 0.06830  -0.13520 -0.13180 375  ARG A CA    
2939 C  C     . ARG A 375 ? 0.60269 0.32990 0.34150 0.04910  -0.14309 -0.14979 375  ARG A C     
2940 O  O     . ARG A 375 ? 0.65316 0.35042 0.36002 0.06209  -0.14687 -0.15876 375  ARG A O     
2941 C  CB    . ARG A 375 ? 0.65200 0.27850 0.39080 0.08990  -0.16290 -0.09970 375  ARG A CB    
2942 C  CG    . ARG A 375 ? 0.72670 0.34600 0.43180 0.13170  -0.14140 -0.07530 375  ARG A CG    
2943 C  CD    . ARG A 375 ? 0.78570 0.36680 0.45670 0.18060  -0.13480 -0.06440 375  ARG A CD    
2944 N  NE    . ARG A 375 ? 0.88020 0.40920 0.47330 0.20490  -0.13480 -0.06710 375  ARG A NE    
2945 C  CZ    . ARG A 375 ? 0.94380 0.44710 0.48040 0.26410  -0.15860 -0.05080 375  ARG A CZ    
2946 N  NH1   . ARG A 375 ? 0.95350 0.44010 0.47150 0.26100  -0.19180 -0.04080 375  ARG A NH1   
2947 N  NH2   . ARG A 375 ? 0.97200 0.44470 0.48770 0.31200  -0.14280 -0.05190 375  ARG A NH2   
2948 N  N     . VAL A 376 ? 0.58899 0.36040 0.31571 0.08500  -0.16109 -0.14229 376  VAL A N     
2949 C  CA    . VAL A 376 ? 0.58290 0.37560 0.29260 0.11710  -0.17350 -0.12340 376  VAL A CA    
2950 C  C     . VAL A 376 ? 0.62320 0.41730 0.27420 0.12430  -0.15120 -0.12230 376  VAL A C     
2951 O  O     . VAL A 376 ? 0.67590 0.43410 0.26560 0.16700  -0.13830 -0.10900 376  VAL A O     
2952 C  CB    . VAL A 376 ? 0.61090 0.41230 0.31290 0.02820  -0.18870 -0.09880 376  VAL A CB    
2953 C  CG1   . VAL A 376 ? 0.62740 0.49390 0.30370 -0.04020 -0.18830 -0.08760 376  VAL A CG1   
2954 C  CG2   . VAL A 376 ? 0.63540 0.41260 0.32390 0.02600  -0.16420 -0.09610 376  VAL A CG2   
2955 N  N     . PRO A 377 ? 0.61549 0.47330 0.26632 0.17099  -0.14619 -0.11739 377  PRO A N     
2956 C  CA    . PRO A 377 ? 0.64738 0.55329 0.25893 0.18849  -0.13849 -0.09379 377  PRO A CA    
2957 C  C     . PRO A 377 ? 0.70658 0.60119 0.27243 0.22129  -0.13609 -0.09119 377  PRO A C     
2958 O  O     . PRO A 377 ? 0.77400 0.65170 0.29110 0.25510  -0.13550 -0.09340 377  PRO A O     
2959 C  CB    . PRO A 377 ? 0.64390 0.53750 0.25230 0.16430  -0.13430 -0.09750 377  PRO A CB    
2960 C  CG    . PRO A 377 ? 0.59330 0.50710 0.26620 0.11980  -0.16070 -0.10960 377  PRO A CG    
2961 C  CD    . PRO A 377 ? 0.57068 0.50409 0.26243 0.11439  -0.15318 -0.11708 377  PRO A CD    
2962 N  N     . THR A 378 ? 0.67550 0.61170 0.26960 0.18280  -0.13810 -0.10600 378  THR A N     
2963 C  CA    . THR A 378 ? 0.62170 0.56040 0.26950 0.15380  -0.14180 -0.12560 378  THR A CA    
2964 C  C     . THR A 378 ? 0.58999 0.52300 0.24451 0.13939  -0.12879 -0.10869 378  THR A C     
2965 O  O     . THR A 378 ? 0.61108 0.56399 0.24353 0.15019  -0.10829 -0.11609 378  THR A O     
2966 C  CB    . THR A 378 ? 0.58330 0.60260 0.27451 0.17090  -0.12590 -0.14569 378  THR A CB    
2967 O  OG1   . THR A 378 ? 0.55040 0.60940 0.32130 0.16640  -0.14750 -0.18850 378  THR A OG1   
2968 C  CG2   . THR A 378 ? 0.58650 0.62430 0.26350 0.17610  -0.09470 -0.14600 378  THR A CG2   
2969 N  N     . LEU A 379 ? 0.59260 0.45450 0.22280 0.15130  -0.12100 -0.07600 379  LEU A N     
2970 C  CA    . LEU A 379 ? 0.59008 0.39530 0.22182 0.11949  -0.11689 -0.08889 379  LEU A CA    
2971 C  C     . LEU A 379 ? 0.63588 0.45739 0.22723 0.16369  -0.10969 -0.08169 379  LEU A C     
2972 O  O     . LEU A 379 ? 0.68680 0.46020 0.25230 0.23780  -0.09360 -0.09400 379  LEU A O     
2973 C  CB    . LEU A 379 ? 0.59980 0.38400 0.21690 0.13070  -0.10600 -0.08460 379  LEU A CB    
2974 C  CG    . LEU A 379 ? 0.60449 0.34680 0.20971 0.11370  -0.10410 -0.07380 379  LEU A CG    
2975 C  CD1   . LEU A 379 ? 0.61310 0.34130 0.22110 0.09790  -0.10030 -0.08800 379  LEU A CD1   
2976 C  CD2   . LEU A 379 ? 0.60430 0.36960 0.20490 0.08560  -0.12070 -0.05170 379  LEU A CD2   
2977 N  N     . ARG A 380 ? 0.64458 0.54029 0.24312 0.15809  -0.09739 -0.11449 380  ARG A N     
2978 C  CA    . ARG A 380 ? 0.61799 0.54259 0.23532 0.19349  -0.11559 -0.06989 380  ARG A CA    
2979 C  C     . ARG A 380 ? 0.59038 0.56299 0.22013 0.21658  -0.08049 -0.05909 380  ARG A C     
2980 O  O     . ARG A 380 ? 0.61250 0.50660 0.22380 0.25230  -0.07740 -0.05860 380  ARG A O     
2981 C  CB    . ARG A 380 ? 0.63010 0.60530 0.26080 0.22610  -0.13070 -0.06640 380  ARG A CB    
2982 C  CG    . ARG A 380 ? 0.68219 0.75458 0.31094 0.18758  -0.17967 -0.05179 380  ARG A CG    
2983 C  CD    . ARG A 380 ? 0.76590 0.87440 0.33980 0.20310  -0.18970 -0.04670 380  ARG A CD    
2984 N  NE    . ARG A 380 ? 0.83390 0.95190 0.36830 0.21910  -0.20530 -0.06590 380  ARG A NE    
2985 C  CZ    . ARG A 380 ? 0.85610 0.98200 0.38980 0.22970  -0.20970 -0.07510 380  ARG A CZ    
2986 N  NH1   . ARG A 380 ? 0.84500 0.96570 0.40780 0.23720  -0.23090 -0.06360 380  ARG A NH1   
2987 N  NH2   . ARG A 380 ? 0.87340 0.98920 0.39420 0.22920  -0.22200 -0.07370 380  ARG A NH2   
2988 N  N     . LEU A 381 ? 0.56468 0.58098 0.20773 0.21218  -0.05339 -0.04989 381  LEU A N     
2989 C  CA    . LEU A 381 ? 0.55160 0.60890 0.20720 0.20610  -0.03080 -0.05850 381  LEU A CA    
2990 C  C     . LEU A 381 ? 0.56740 0.64090 0.23020 0.24360  -0.01850 -0.07440 381  LEU A C     
2991 O  O     . LEU A 381 ? 0.63360 0.66210 0.24430 0.29420  -0.04690 -0.05170 381  LEU A O     
2992 C  CB    . LEU A 381 ? 0.58460 0.59090 0.19770 0.16790  -0.03820 -0.04280 381  LEU A CB    
2993 C  CG    . LEU A 381 ? 0.52870 0.51710 0.20920 0.14220  -0.05630 -0.00570 381  LEU A CG    
2994 C  CD1   . LEU A 381 ? 0.53610 0.49190 0.21830 0.11040  -0.05170 0.00230  381  LEU A CD1   
2995 C  CD2   . LEU A 381 ? 0.45470 0.47770 0.21950 0.13650  -0.05990 0.05070  381  LEU A CD2   
2996 N  N     . ALA A 382 ? 0.57020 0.67020 0.23480 0.21450  -0.00520 -0.08900 382  ALA A N     
2997 C  CA    . ALA A 382 ? 0.57759 0.66348 0.23733 0.18478  0.02180  -0.09729 382  ALA A CA    
2998 C  C     . ALA A 382 ? 0.64170 0.69770 0.21760 0.18220  0.00550  -0.03680 382  ALA A C     
2999 O  O     . ALA A 382 ? 0.66280 0.73090 0.22680 0.20540  0.00590  -0.01020 382  ALA A O     
3000 C  CB    . ALA A 382 ? 0.55350 0.64750 0.24130 0.17710  0.01940  -0.11260 382  ALA A CB    
3001 N  N     . VAL A 383 ? 0.68310 0.73050 0.21721 0.15640  -0.01390 -0.01750 383  VAL A N     
3002 C  CA    . VAL A 383 ? 0.67610 0.73740 0.22210 0.17630  0.00290  -0.01490 383  VAL A CA    
3003 C  C     . VAL A 383 ? 0.71190 0.73270 0.23080 0.19040  -0.01300 0.02530  383  VAL A C     
3004 O  O     . VAL A 383 ? 0.67400 0.73240 0.23710 0.20060  -0.02050 0.05330  383  VAL A O     
3005 C  CB    . VAL A 383 ? 0.61219 0.75498 0.22062 0.16979  0.02490  -0.02060 383  VAL A CB    
3006 C  CG1   . VAL A 383 ? 0.61760 0.77100 0.22650 0.16460  0.04730  -0.01000 383  VAL A CG1   
3007 C  CG2   . VAL A 383 ? 0.59790 0.79289 0.22171 0.15950  -0.01870 -0.01260 383  VAL A CG2   
3008 N  N     . PRO A 384 ? 0.76118 0.67109 0.23683 0.18828  -0.00630 0.05599  384  PRO A N     
3009 C  CA    . PRO A 384 ? 0.73490 0.64240 0.25430 0.21940  -0.02990 0.05380  384  PRO A CA    
3010 C  C     . PRO A 384 ? 0.70260 0.59200 0.26310 0.18810  -0.06040 0.09460  384  PRO A C     
3011 O  O     . PRO A 384 ? 0.70240 0.60520 0.25760 0.13950  -0.04560 0.12490  384  PRO A O     
3012 C  CB    . PRO A 384 ? 0.75279 0.65159 0.25212 0.22719  -0.04200 0.05070  384  PRO A CB    
3013 C  CG    . PRO A 384 ? 0.76310 0.66270 0.26230 0.22000  -0.00010 0.05020  384  PRO A CG    
3014 C  CD    . PRO A 384 ? 0.75860 0.65510 0.24880 0.22840  0.00220  0.06380  384  PRO A CD    
3015 N  N     . VAL A 385 ? 0.65640 0.57540 0.26760 0.12330  -0.06800 0.09570  385  VAL A N     
3016 C  CA    . VAL A 385 ? 0.65360 0.54290 0.28670 0.06250  -0.06840 0.09900  385  VAL A CA    
3017 C  C     . VAL A 385 ? 0.67270 0.60460 0.31950 0.02780  -0.08370 0.10660  385  VAL A C     
3018 O  O     . VAL A 385 ? 0.66640 0.52220 0.29810 -0.00030 -0.05530 0.12950  385  VAL A O     
3019 C  CB    . VAL A 385 ? 0.64650 0.50420 0.28340 0.06830  -0.07760 0.03850  385  VAL A CB    
3020 C  CG1   . VAL A 385 ? 0.65170 0.49330 0.26490 0.09950  -0.05640 0.05290  385  VAL A CG1   
3021 C  CG2   . VAL A 385 ? 0.65500 0.51080 0.29880 0.04420  -0.04260 0.02270  385  VAL A CG2   
3022 N  N     . GLU A 386 ? 0.65960 0.65850 0.35570 0.05640  -0.12830 0.14380  386  GLU A N     
3023 C  CA    A GLU A 386 ? 0.65840 0.68230 0.37440 0.02950  -0.13090 0.14870  386  GLU A CA    
3024 C  CA    B GLU A 386 ? 0.68080 0.70460 0.36440 0.02610  -0.11480 0.14060  386  GLU A CA    
3025 C  C     . GLU A 386 ? 0.67180 0.71020 0.36910 0.00940  -0.11750 0.13610  386  GLU A C     
3026 O  O     . GLU A 386 ? 0.71770 0.73660 0.41420 -0.04570 -0.10450 0.10580  386  GLU A O     
3027 C  CB    A GLU A 386 ? 0.63920 0.67850 0.39310 0.02210  -0.15170 0.16020  386  GLU A CB    
3028 C  CB    B GLU A 386 ? 0.71330 0.74320 0.36310 0.01460  -0.10270 0.14050  386  GLU A CB    
3029 C  CG    A GLU A 386 ? 0.62920 0.67790 0.40640 0.00970  -0.18570 0.16400  386  GLU A CG    
3030 C  CG    B GLU A 386 ? 0.76840 0.77950 0.35710 0.00200  -0.10160 0.12900  386  GLU A CG    
3031 C  CD    A GLU A 386 ? 0.64270 0.67820 0.42230 0.01460  -0.20150 0.15110  386  GLU A CD    
3032 C  CD    B GLU A 386 ? 0.85320 0.80370 0.35490 -0.00180 -0.10620 0.12110  386  GLU A CD    
3033 O  OE1   A GLU A 386 ? 0.66710 0.66450 0.42940 0.02380  -0.20680 0.15700  386  GLU A OE1   
3034 O  OE1   B GLU A 386 ? 0.91990 0.83400 0.36640 0.02890  -0.09340 0.10010  386  GLU A OE1   
3035 O  OE2   A GLU A 386 ? 0.63810 0.70030 0.42850 -0.01490 -0.19750 0.13100  386  GLU A OE2   
3036 O  OE2   B GLU A 386 ? 0.83950 0.78190 0.33890 -0.03070 -0.11730 0.14150  386  GLU A OE2   
3037 N  N     . GLN A 387 ? 0.67070 0.69540 0.31720 0.03370  -0.07200 0.15870  387  GLN A N     
3038 C  CA    . GLN A 387 ? 0.66520 0.63180 0.26680 0.04940  -0.02600 0.17590  387  GLN A CA    
3039 C  C     . GLN A 387 ? 0.61270 0.55260 0.23730 0.03900  0.02790  0.16520  387  GLN A C     
3040 O  O     . GLN A 387 ? 0.61030 0.57870 0.22900 0.04790  0.02990  0.15450  387  GLN A O     
3041 C  CB    . GLN A 387 ? 0.73700 0.68540 0.26570 -0.00520 -0.01940 0.19120  387  GLN A CB    
3042 C  CG    . GLN A 387 ? 0.84260 0.77730 0.26970 -0.02260 -0.03060 0.17050  387  GLN A CG    
3043 C  CD    . GLN A 387 ? 0.93229 0.85640 0.28152 -0.04479 -0.02970 0.15479  387  GLN A CD    
3044 O  OE1   . GLN A 387 ? 0.94800 0.85650 0.27970 -0.01330 -0.04660 0.15150  387  GLN A OE1   
3045 N  NE2   . GLN A 387 ? 0.97170 0.92210 0.30090 -0.04420 -0.04080 0.13400  387  GLN A NE2   
3046 N  N     . LEU A 388 ? 0.58300 0.46670 0.23110 0.04940  0.03810  0.15140  388  LEU A N     
3047 C  CA    . LEU A 388 ? 0.56650 0.43300 0.21700 0.07270  0.05500  0.12790  388  LEU A CA    
3048 C  C     . LEU A 388 ? 0.57190 0.47530 0.21370 0.06530  0.07670  0.11690  388  LEU A C     
3049 O  O     . LEU A 388 ? 0.63460 0.44910 0.23990 0.04260  0.07550  0.10490  388  LEU A O     
3050 C  CB    . LEU A 388 ? 0.54500 0.42250 0.20120 0.06110  0.04830  0.08560  388  LEU A CB    
3051 C  CG    . LEU A 388 ? 0.53350 0.43860 0.20030 0.10860  0.03990  0.09560  388  LEU A CG    
3052 C  CD1   . LEU A 388 ? 0.51200 0.45070 0.20200 0.13310  0.03530  0.07150  388  LEU A CD1   
3053 C  CD2   . LEU A 388 ? 0.54910 0.43230 0.21120 0.08350  0.01050  0.06730  388  LEU A CD2   
3054 N  N     . VAL A 389 ? 0.51630 0.49260 0.19870 0.09480  0.08700  0.09320  389  VAL A N     
3055 C  CA    . VAL A 389 ? 0.48789 0.47609 0.19772 0.04289  0.11299  0.08629  389  VAL A CA    
3056 C  C     . VAL A 389 ? 0.48510 0.42210 0.18120 0.05050  0.10710  0.06600  389  VAL A C     
3057 O  O     . VAL A 389 ? 0.55790 0.37370 0.18130 0.07780  0.08170  0.06620  389  VAL A O     
3058 C  CB    . VAL A 389 ? 0.51350 0.52150 0.19100 0.07620  0.09870  0.07050  389  VAL A CB    
3059 C  CG1   . VAL A 389 ? 0.59040 0.48090 0.18960 0.06580  0.07260  0.08220  389  VAL A CG1   
3060 C  CG2   . VAL A 389 ? 0.50990 0.54360 0.20090 0.08280  0.11910  0.04220  389  VAL A CG2   
3061 N  N     . LEU A 390 ? 0.50050 0.38860 0.18130 0.02240  0.07870  0.05710  390  LEU A N     
3062 C  CA    . LEU A 390 ? 0.48050 0.35940 0.21030 0.04770  0.08790  0.05510  390  LEU A CA    
3063 C  C     . LEU A 390 ? 0.48950 0.33170 0.21650 0.01310  0.11850  0.06320  390  LEU A C     
3064 O  O     . LEU A 390 ? 0.53050 0.35270 0.23900 -0.03260 0.14010  0.07950  390  LEU A O     
3065 C  CB    . LEU A 390 ? 0.45570 0.34080 0.24690 0.03580  0.08700  0.05430  390  LEU A CB    
3066 C  CG    . LEU A 390 ? 0.45990 0.28950 0.28450 0.04010  0.06530  0.08970  390  LEU A CG    
3067 C  CD1   . LEU A 390 ? 0.50440 0.28060 0.29410 0.08620  0.02480  0.02650  390  LEU A CD1   
3068 C  CD2   . LEU A 390 ? 0.49490 0.34020 0.32150 -0.03280 0.05100  0.11520  390  LEU A CD2   
3069 N  N     . ARG A 391 ? 0.47170 0.29360 0.21710 0.01400  0.11170  0.04430  391  ARG A N     
3070 C  CA    . ARG A 391 ? 0.49430 0.25020 0.21970 0.05740  0.08250  0.06330  391  ARG A CA    
3071 C  C     . ARG A 391 ? 0.46470 0.25070 0.22880 0.03530  0.05990  0.06380  391  ARG A C     
3072 O  O     . ARG A 391 ? 0.46420 0.28440 0.21330 0.03360  0.03060  0.04360  391  ARG A O     
3073 C  CB    . ARG A 391 ? 0.52170 0.23590 0.22860 0.05210  0.04420  0.04550  391  ARG A CB    
3074 C  CG    . ARG A 391 ? 0.51770 0.22890 0.24440 0.02310  0.03740  0.03000  391  ARG A CG    
3075 C  CD    . ARG A 391 ? 0.57560 0.18470 0.24710 0.07870  0.03040  0.02680  391  ARG A CD    
3076 N  NE    . ARG A 391 ? 0.63360 0.28780 0.25020 0.07750  0.02420  0.03990  391  ARG A NE    
3077 C  CZ    . ARG A 391 ? 0.63790 0.31730 0.27050 0.08550  0.04000  0.02680  391  ARG A CZ    
3078 N  NH1   . ARG A 391 ? 0.65820 0.28070 0.25790 0.10140  0.04760  -0.01060 391  ARG A NH1   
3079 N  NH2   . ARG A 391 ? 0.64980 0.34310 0.29290 0.12970  0.01660  0.02950  391  ARG A NH2   
3080 N  N     . PRO A 392 ? 0.44660 0.31410 0.23990 0.02470  0.05090  0.05460  392  PRO A N     
3081 C  CA    . PRO A 392 ? 0.40380 0.29480 0.26240 0.03370  0.07150  0.06380  392  PRO A CA    
3082 C  C     . PRO A 392 ? 0.41640 0.24670 0.26700 0.06480  0.04420  0.06660  392  PRO A C     
3083 O  O     . PRO A 392 ? 0.40830 0.20240 0.26670 0.01480  0.03170  0.04310  392  PRO A O     
3084 C  CB    . PRO A 392 ? 0.38500 0.30770 0.27930 0.05340  0.07270  0.05640  392  PRO A CB    
3085 C  CG    . PRO A 392 ? 0.43370 0.36410 0.27280 0.05380  0.04770  0.03610  392  PRO A CG    
3086 C  CD    . PRO A 392 ? 0.42180 0.31540 0.24670 0.02460  0.00320  0.05140  392  PRO A CD    
3087 N  N     . GLY A 393 ? 0.42430 0.22260 0.27810 0.03480  0.06040  0.05270  393  GLY A N     
3088 C  CA    . GLY A 393 ? 0.46220 0.20860 0.28770 -0.00080 0.06440  0.06090  393  GLY A CA    
3089 C  C     . GLY A 393 ? 0.44060 0.18080 0.31270 -0.00400 0.06310  0.04050  393  GLY A C     
3090 O  O     . GLY A 393 ? 0.46450 0.17680 0.31620 0.03170  0.05220  0.02990  393  GLY A O     
3091 N  N     . THR A 394 ? 0.39350 0.20660 0.31740 -0.00680 0.05170  0.03960  394  THR A N     
3092 C  CA    . THR A 394 ? 0.37740 0.19610 0.30030 -0.00550 0.05590  0.05500  394  THR A CA    
3093 C  C     . THR A 394 ? 0.38950 0.16300 0.27050 0.01370  0.06150  0.04340  394  THR A C     
3094 O  O     . THR A 394 ? 0.41980 0.19390 0.27090 0.01600  0.04570  0.05720  394  THR A O     
3095 C  CB    . THR A 394 ? 0.42200 0.22740 0.30980 -0.01680 0.06500  0.03290  394  THR A CB    
3096 O  OG1   . THR A 394 ? 0.46450 0.27130 0.31090 -0.02630 0.07240  0.01670  394  THR A OG1   
3097 C  CG2   . THR A 394 ? 0.43420 0.19830 0.30990 -0.05380 0.08690  0.05660  394  THR A CG2   
3098 N  N     . THR A 395 ? 0.36060 0.14380 0.24940 0.02400  0.06430  0.00570  395  THR A N     
3099 C  CA    . THR A 395 ? 0.33860 0.18950 0.24020 0.06510  0.04530  0.01390  395  THR A CA    
3100 C  C     . THR A 395 ? 0.35530 0.21070 0.22560 0.06150  0.05030  0.03760  395  THR A C     
3101 O  O     . THR A 395 ? 0.36680 0.18070 0.24450 0.02640  0.07870  0.04050  395  THR A O     
3102 C  CB    . THR A 395 ? 0.36410 0.20080 0.24150 0.01930  0.03170  0.03440  395  THR A CB    
3103 O  OG1   . THR A 395 ? 0.36650 0.21880 0.26410 0.02770  0.05140  0.06420  395  THR A OG1   
3104 C  CG2   . THR A 395 ? 0.38710 0.21870 0.21820 0.01930  0.05440  -0.00360 395  THR A CG2   
3105 N  N     . ILE A 396 ? 0.35020 0.17030 0.18780 0.00460  0.04230  -0.00370 396  ILE A N     
3106 C  CA    . ILE A 396 ? 0.34580 0.16600 0.16800 0.02500  0.03080  0.00890  396  ILE A CA    
3107 C  C     . ILE A 396 ? 0.37840 0.18490 0.16400 0.02230  0.02940  0.02420  396  ILE A C     
3108 O  O     . ILE A 396 ? 0.38690 0.26690 0.15200 0.03810  0.02720  0.00980  396  ILE A O     
3109 C  CB    . ILE A 396 ? 0.36930 0.15540 0.17250 0.00140  0.01100  0.01260  396  ILE A CB    
3110 C  CG1   . ILE A 396 ? 0.38930 0.25620 0.17390 0.02720  0.03030  0.02610  396  ILE A CG1   
3111 C  CG2   . ILE A 396 ? 0.41470 0.16440 0.17760 -0.01280 0.03570  0.03700  396  ILE A CG2   
3112 C  CD1   . ILE A 396 ? 0.45790 0.36610 0.21540 -0.00010 0.00940  0.05490  396  ILE A CD1   
3113 N  N     . GLN A 397 ? 0.34830 0.16980 0.17150 0.02740  0.01390  0.01240  397  GLN A N     
3114 C  CA    . GLN A 397 ? 0.38370 0.16850 0.14130 0.03640  -0.00590 -0.00130 397  GLN A CA    
3115 C  C     . GLN A 397 ? 0.38400 0.19000 0.13860 -0.00710 0.03620  0.00790  397  GLN A C     
3116 O  O     . GLN A 397 ? 0.47260 0.17320 0.15350 0.01190  0.01530  0.00080  397  GLN A O     
3117 C  CB    . GLN A 397 ? 0.39010 0.19930 0.15240 0.04810  -0.00870 -0.01580 397  GLN A CB    
3118 C  CG    . GLN A 397 ? 0.40160 0.18670 0.17010 0.05450  0.04370  0.01480  397  GLN A CG    
3119 C  CD    . GLN A 397 ? 0.42450 0.21720 0.16980 0.00530  0.00970  0.01720  397  GLN A CD    
3120 O  OE1   . GLN A 397 ? 0.44040 0.25200 0.17370 0.03500  0.03310  0.03260  397  GLN A OE1   
3121 N  NE2   . GLN A 397 ? 0.45810 0.27850 0.19480 0.04610  0.02070  0.01670  397  GLN A NE2   
3122 N  N     . GLY A 398 ? 0.42000 0.21470 0.12590 -0.01840 0.05420  -0.01560 398  GLY A N     
3123 C  CA    . GLY A 398 ? 0.45098 0.25540 0.14352 -0.00930 0.05549  -0.05269 398  GLY A CA    
3124 C  C     . GLY A 398 ? 0.46250 0.24550 0.14360 0.06950  0.05980  -0.00700 398  GLY A C     
3125 O  O     . GLY A 398 ? 0.45810 0.26980 0.16950 0.05620  0.05070  0.02490  398  GLY A O     
3126 N  N     . VAL A 399 ? 0.46700 0.26400 0.14460 0.07560  0.06470  0.00610  399  VAL A N     
3127 C  CA    A VAL A 399 ? 0.48300 0.25250 0.15450 0.06140  0.02800  -0.01100 399  VAL A CA    
3128 C  CA    B VAL A 399 ? 0.45940 0.27160 0.16220 0.06400  0.04280  -0.00880 399  VAL A CA    
3129 C  C     . VAL A 399 ? 0.46860 0.28290 0.18200 0.05940  0.03360  -0.01360 399  VAL A C     
3130 O  O     . VAL A 399 ? 0.49380 0.33580 0.23820 0.12260  -0.01880 0.00990  399  VAL A O     
3131 C  CB    A VAL A 399 ? 0.52510 0.28180 0.15510 0.05340  0.01410  0.05450  399  VAL A CB    
3132 C  CB    B VAL A 399 ? 0.44770 0.30180 0.16250 0.05730  0.04090  -0.00410 399  VAL A CB    
3133 C  CG1   A VAL A 399 ? 0.54238 0.26620 0.15632 0.05080  0.02030  0.04789  399  VAL A CG1   
3134 C  CG1   B VAL A 399 ? 0.44170 0.30670 0.16180 0.06980  0.04010  -0.02900 399  VAL A CG1   
3135 C  CG2   A VAL A 399 ? 0.50370 0.26990 0.15000 0.07310  -0.02080 0.01950  399  VAL A CG2   
3136 C  CG2   B VAL A 399 ? 0.43610 0.30990 0.15640 0.03570  0.03670  -0.00580 399  VAL A CG2   
3137 N  N     . ASN A 400 ? 0.49920 0.36070 0.22620 0.13400  0.01970  -0.02230 400  ASN A N     
3138 C  CA    . ASN A 400 ? 0.53860 0.41580 0.23970 0.10860  0.03630  -0.01430 400  ASN A CA    
3139 C  C     . ASN A 400 ? 0.53380 0.41310 0.22880 0.13350  0.06330  -0.02000 400  ASN A C     
3140 O  O     . ASN A 400 ? 0.54100 0.40820 0.22210 0.15640  0.05090  -0.00610 400  ASN A O     
3141 C  CB    . ASN A 400 ? 0.53980 0.46380 0.24630 0.07650  0.00190  -0.01670 400  ASN A CB    
3142 C  CG    . ASN A 400 ? 0.57330 0.51850 0.25350 0.17830  -0.00480 0.01100  400  ASN A CG    
3143 O  OD1   . ASN A 400 ? 0.56320 0.56590 0.28110 0.22210  0.00340  -0.02570 400  ASN A OD1   
3144 N  ND2   . ASN A 400 ? 0.60140 0.54740 0.25480 0.17360  -0.03670 0.02920  400  ASN A ND2   
3145 N  N     . GLU A 401 ? 0.52940 0.43330 0.22700 0.13010  0.12140  0.02940  401  GLU A N     
3146 C  CA    . GLU A 401 ? 0.55000 0.48160 0.23900 0.13220  0.12710  0.06150  401  GLU A CA    
3147 C  C     . GLU A 401 ? 0.55229 0.41830 0.19861 0.14110  0.09420  0.07360  401  GLU A C     
3148 O  O     . GLU A 401 ? 0.58300 0.42950 0.19890 0.17060  0.06770  0.06840  401  GLU A O     
3149 C  CB    . GLU A 401 ? 0.56150 0.62030 0.29250 0.15810  0.16370  0.07570  401  GLU A CB    
3150 C  CG    . GLU A 401 ? 0.69460 0.80990 0.35030 0.19060  0.19300  0.08110  401  GLU A CG    
3151 C  CD    . GLU A 401 ? 0.82290 0.98030 0.40800 0.18760  0.19140  0.10550  401  GLU A CD    
3152 O  OE1   . GLU A 401 ? 0.86530 1.06900 0.44080 0.20980  0.19060  0.07750  401  GLU A OE1   
3153 O  OE2   . GLU A 401 ? 0.88710 1.01430 0.41350 0.17850  0.19840  0.11370  401  GLU A OE2   
3154 N  N     . LEU A 402 ? 0.57070 0.42290 0.18210 0.16290  0.06500  0.02590  402  LEU A N     
3155 C  CA    . LEU A 402 ? 0.55970 0.37290 0.16590 0.12860  0.05030  -0.00370 402  LEU A CA    
3156 C  C     . LEU A 402 ? 0.57609 0.38760 0.16741 0.15739  0.01750  0.00080  402  LEU A C     
3157 O  O     . LEU A 402 ? 0.58820 0.35490 0.17190 0.17750  -0.01030 -0.01190 402  LEU A O     
3158 C  CB    . LEU A 402 ? 0.53610 0.33360 0.16480 0.12020  0.03980  0.01560  402  LEU A CB    
3159 C  CG    . LEU A 402 ? 0.52070 0.32060 0.16060 0.07610  0.01290  0.00370  402  LEU A CG    
3160 C  CD1   . LEU A 402 ? 0.55170 0.31730 0.15960 0.09850  0.02900  0.03480  402  LEU A CD1   
3161 C  CD2   . LEU A 402 ? 0.54110 0.31930 0.14690 0.09360  0.02450  -0.00460 402  LEU A CD2   
3162 N  N     . PRO A 403 ? 0.59900 0.46140 0.18340 0.15460  0.04540  -0.01040 403  PRO A N     
3163 C  CA    . PRO A 403 ? 0.59240 0.48530 0.19110 0.14910  0.04630  -0.03780 403  PRO A CA    
3164 C  C     . PRO A 403 ? 0.62060 0.48980 0.20190 0.18230  0.02750  -0.04250 403  PRO A C     
3165 O  O     . PRO A 403 ? 0.61770 0.51870 0.22070 0.27780  0.00100  -0.02960 403  PRO A O     
3166 C  CB    . PRO A 403 ? 0.61940 0.50790 0.18660 0.12200  0.05760  -0.01850 403  PRO A CB    
3167 C  CG    . PRO A 403 ? 0.63480 0.49600 0.18990 0.11640  0.06180  -0.02420 403  PRO A CG    
3168 C  CD    . PRO A 403 ? 0.58630 0.45800 0.18810 0.12640  0.08090  -0.00830 403  PRO A CD    
3169 N  N     . VAL A 404 ? 0.64930 0.44910 0.20250 0.16380  0.01500  -0.05320 404  VAL A N     
3170 C  CA    . VAL A 404 ? 0.59970 0.41200 0.20270 0.16670  -0.01630 -0.07360 404  VAL A CA    
3171 C  C     . VAL A 404 ? 0.58877 0.46459 0.21804 0.17528  -0.05559 -0.09868 404  VAL A C     
3172 O  O     . VAL A 404 ? 0.63849 0.51680 0.23161 0.19349  -0.07340 -0.09719 404  VAL A O     
3173 C  CB    . VAL A 404 ? 0.57410 0.32700 0.20370 0.16760  -0.00790 -0.06270 404  VAL A CB    
3174 C  CG1   . VAL A 404 ? 0.56160 0.33680 0.20740 0.15910  -0.03500 -0.08070 404  VAL A CG1   
3175 C  CG2   . VAL A 404 ? 0.59110 0.33500 0.20430 0.15640  -0.04040 -0.07350 404  VAL A CG2   
3176 N  N     . THR A 405 ? 0.63019 0.45040 0.24241 0.18900  -0.09530 -0.10740 405  THR A N     
3177 C  CA    . THR A 405 ? 0.62288 0.49179 0.25004 0.21898  -0.10179 -0.11068 405  THR A CA    
3178 C  C     . THR A 405 ? 0.56837 0.47039 0.26474 0.19758  -0.13198 -0.12957 405  THR A C     
3179 O  O     . THR A 405 ? 0.59979 0.52400 0.26961 0.24749  -0.09660 -0.13109 405  THR A O     
3180 C  CB    . THR A 405 ? 0.68828 0.51969 0.27182 0.22679  -0.09899 -0.12319 405  THR A CB    
3181 O  OG1   . THR A 405 ? 0.71839 0.56850 0.29952 0.26309  -0.09570 -0.13989 405  THR A OG1   
3182 C  CG2   . THR A 405 ? 0.64620 0.52460 0.25820 0.22060  -0.11880 -0.10790 405  THR A CG2   
3183 N  N     . TRP A 406 ? 0.53560 0.49930 0.29690 0.16560  -0.15230 -0.15960 406  TRP A N     
3184 C  CA    . TRP A 406 ? 0.54720 0.51300 0.34780 0.14410  -0.17340 -0.19090 406  TRP A CA    
3185 C  C     . TRP A 406 ? 0.57330 0.60030 0.41840 0.08530  -0.14930 -0.25980 406  TRP A C     
3186 O  O     . TRP A 406 ? 0.58860 0.66000 0.39640 0.13310  -0.17900 -0.23510 406  TRP A O     
3187 C  CB    . TRP A 406 ? 0.59570 0.51850 0.33430 0.13180  -0.15000 -0.19180 406  TRP A CB    
3188 C  CG    . TRP A 406 ? 0.56209 0.48710 0.33051 0.16739  -0.14509 -0.18769 406  TRP A CG    
3189 C  CD1   . TRP A 406 ? 0.62450 0.49750 0.33610 0.12010  -0.16090 -0.17240 406  TRP A CD1   
3190 C  CD2   . TRP A 406 ? 0.54900 0.45170 0.34161 0.15090  -0.15350 -0.18799 406  TRP A CD2   
3191 N  NE1   . TRP A 406 ? 0.59510 0.47120 0.34370 0.12370  -0.14350 -0.17450 406  TRP A NE1   
3192 C  CE2   . TRP A 406 ? 0.57270 0.43770 0.34000 0.12000  -0.14500 -0.18619 406  TRP A CE2   
3193 C  CE3   . TRP A 406 ? 0.53600 0.49130 0.35040 0.10410  -0.17570 -0.16850 406  TRP A CE3   
3194 C  CZ2   . TRP A 406 ? 0.57390 0.42430 0.34400 0.13040  -0.13520 -0.17180 406  TRP A CZ2   
3195 C  CZ3   . TRP A 406 ? 0.53320 0.47120 0.36110 0.16440  -0.14670 -0.14840 406  TRP A CZ3   
3196 C  CH2   . TRP A 406 ? 0.56200 0.45600 0.35070 0.16150  -0.14190 -0.14240 406  TRP A CH2   
3197 N  N     . HIS A 407 ? 0.67560 0.68240 0.52690 0.08560  -0.14860 -0.33039 407  HIS A N     
3198 C  CA    . HIS A 407 ? 0.73440 0.73510 0.68080 0.00290  -0.10920 -0.33400 407  HIS A CA    
3199 C  C     . HIS A 407 ? 0.79020 0.87050 0.82230 0.00070  -0.08010 -0.23840 407  HIS A C     
3200 O  O     . HIS A 407 ? 0.73940 0.88920 0.81690 -0.02850 -0.10500 -0.23570 407  HIS A O     
3201 C  CB    . HIS A 407 ? 0.76640 0.71420 0.69440 -0.05010 -0.11220 -0.36130 407  HIS A CB    
3202 C  CG    . HIS A 407 ? 0.76950 0.70880 0.72170 -0.09280 -0.08170 -0.32360 407  HIS A CG    
3203 N  ND1   . HIS A 407 ? 0.73980 0.67380 0.73170 -0.16760 -0.06460 -0.31070 407  HIS A ND1   
3204 C  CD2   . HIS A 407 ? 0.74390 0.65440 0.73000 -0.14570 -0.09750 -0.34860 407  HIS A CD2   
3205 C  CE1   . HIS A 407 ? 0.72850 0.66090 0.73950 -0.15900 -0.05360 -0.30230 407  HIS A CE1   
3206 N  NE2   . HIS A 407 ? 0.72960 0.68440 0.74020 -0.12380 -0.07050 -0.32010 407  HIS A NE2   
3207 N  N     . HIS A 408 ? 0.89760 0.95910 0.96200 0.05240  -0.00080 -0.17150 408  HIS A N     
3208 C  CA    . HIS A 408 ? 0.98740 1.01250 1.09380 0.05080  0.07680  -0.12250 408  HIS A CA    
3209 C  C     . HIS A 408 ? 0.79180 0.83540 1.09810 0.01890  0.17950  -0.14280 408  HIS A C     
3210 O  O     . HIS A 408 ? 0.67570 0.73230 1.10520 0.02430  0.22240  -0.16640 408  HIS A O     
3211 C  CB    . HIS A 408 ? 1.23900 1.23900 1.23900 0.04810  0.04870  -0.08410 408  HIS A CB    
3212 C  CG    . HIS A 408 ? 1.26080 1.27010 1.29300 0.04610  0.03180  -0.05810 408  HIS A CG    
3213 N  ND1   . HIS A 408 ? 1.23880 1.26250 1.31840 0.05610  0.02350  -0.04780 408  HIS A ND1   
3214 C  CD2   . HIS A 408 ? 1.26490 1.27840 1.32190 0.02630  0.02320  -0.04940 408  HIS A CD2   
3215 C  CE1   . HIS A 408 ? 1.23140 1.26680 1.33820 0.03070  0.01540  -0.04330 408  HIS A CE1   
3216 N  NE2   . HIS A 408 ? 1.24790 1.27350 1.33780 0.01170  0.01490  -0.04550 408  HIS A NE2   
3217 C  CHA   . HEM B .   ? 0.29930 0.12080 0.15560 0.02770  -0.02800 0.02210  501  HEM A CHA   
3218 C  CHB   . HEM B .   ? 0.29230 0.15510 0.11080 -0.05230 0.01190  -0.00630 501  HEM A CHB   
3219 C  CHC   . HEM B .   ? 0.33680 0.16100 0.11630 0.01600  0.00990  0.02140  501  HEM A CHC   
3220 C  CHD   . HEM B .   ? 0.26690 0.15020 0.14800 0.02760  0.01550  -0.01190 501  HEM A CHD   
3221 C  C1A   . HEM B .   ? 0.30550 0.11030 0.13280 -0.01970 -0.02660 -0.00780 501  HEM A C1A   
3222 C  C2A   . HEM B .   ? 0.32260 0.12510 0.15340 -0.01840 -0.03710 -0.01810 501  HEM A C2A   
3223 C  C3A   . HEM B .   ? 0.28240 0.12440 0.15180 -0.00870 -0.01720 -0.00870 501  HEM A C3A   
3224 C  C4A   . HEM B .   ? 0.33940 0.10510 0.13060 -0.00140 -0.00130 0.01020  501  HEM A C4A   
3225 C  CMA   . HEM B .   ? 0.30790 0.11820 0.16030 0.04180  0.00620  0.02250  501  HEM A CMA   
3226 C  CAA   . HEM B .   ? 0.32110 0.13750 0.20120 0.00800  -0.06860 -0.05070 501  HEM A CAA   
3227 C  CBA   . HEM B .   ? 0.32540 0.19320 0.22020 -0.04490 -0.06920 -0.05040 501  HEM A CBA   
3228 C  CGA   . HEM B .   ? 0.34090 0.20500 0.24610 0.02970  -0.04940 -0.06710 501  HEM A CGA   
3229 O  O1A   . HEM B .   ? 0.39450 0.14610 0.22220 0.00110  -0.06650 -0.03220 501  HEM A O1A   
3230 O  O2A   . HEM B .   ? 0.34550 0.29590 0.29460 0.03700  -0.06130 -0.03850 501  HEM A O2A   
3231 C  C1B   . HEM B .   ? 0.31420 0.14950 0.11420 -0.03030 0.00240  0.00060  501  HEM A C1B   
3232 C  C2B   . HEM B .   ? 0.31210 0.11190 0.13140 0.00020  0.03290  -0.01510 501  HEM A C2B   
3233 C  C3B   . HEM B .   ? 0.33300 0.11940 0.13300 -0.01550 0.05450  -0.01850 501  HEM A C3B   
3234 C  C4B   . HEM B .   ? 0.33300 0.11270 0.12350 -0.00710 0.01680  0.01400  501  HEM A C4B   
3235 C  CMB   . HEM B .   ? 0.36400 0.13610 0.14870 0.06640  0.03030  0.03160  501  HEM A CMB   
3236 C  CAB   . HEM B .   ? 0.38960 0.17000 0.15280 -0.03610 0.04130  0.01570  501  HEM A CAB   
3237 C  CBB   . HEM B .   ? 0.47950 0.19490 0.19440 -0.03810 0.04680  0.05770  501  HEM A CBB   
3238 C  C1C   . HEM B .   ? 0.30450 0.10290 0.12080 0.02740  -0.00520 0.00380  501  HEM A C1C   
3239 C  C2C   . HEM B .   ? 0.29940 0.14390 0.11860 0.03160  -0.01260 0.00170  501  HEM A C2C   
3240 C  C3C   . HEM B .   ? 0.30650 0.13620 0.11710 -0.02860 -0.01180 0.00090  501  HEM A C3C   
3241 C  C4C   . HEM B .   ? 0.28090 0.15770 0.12030 -0.02120 -0.00000 -0.00930 501  HEM A C4C   
3242 C  CMC   . HEM B .   ? 0.34336 0.14302 0.14642 0.02069  -0.01470 -0.05768 501  HEM A CMC   
3243 C  CAC   . HEM B .   ? 0.34760 0.15190 0.12690 0.00450  -0.02480 0.00780  501  HEM A CAC   
3244 C  CBC   . HEM B .   ? 0.42580 0.19980 0.15660 -0.00900 -0.04110 -0.01600 501  HEM A CBC   
3245 C  C1D   . HEM B .   ? 0.29080 0.13840 0.14110 0.01350  0.00710  -0.04620 501  HEM A C1D   
3246 C  C2D   . HEM B .   ? 0.30470 0.12090 0.16310 0.01410  -0.02740 -0.02430 501  HEM A C2D   
3247 C  C3D   . HEM B .   ? 0.31890 0.16700 0.16510 0.01030  -0.02550 -0.01870 501  HEM A C3D   
3248 C  C4D   . HEM B .   ? 0.29520 0.14660 0.15920 -0.00170 -0.02720 0.01050  501  HEM A C4D   
3249 C  CMD   . HEM B .   ? 0.34360 0.14990 0.18430 0.08820  -0.03590 -0.00620 501  HEM A CMD   
3250 C  CAD   . HEM B .   ? 0.33420 0.21550 0.12720 0.03190  -0.05510 -0.02440 501  HEM A CAD   
3251 C  CBD   . HEM B .   ? 0.30700 0.18260 0.13270 0.04150  -0.04520 -0.05250 501  HEM A CBD   
3252 C  CGD   . HEM B .   ? 0.31180 0.17090 0.15820 0.02230  -0.05770 -0.00670 501  HEM A CGD   
3253 O  O1D   . HEM B .   ? 0.41830 0.19500 0.14600 0.06870  -0.07810 -0.04350 501  HEM A O1D   
3254 O  O2D   . HEM B .   ? 0.32390 0.20850 0.19530 0.05310  -0.06600 -0.03000 501  HEM A O2D   
3255 N  NA    . HEM B .   ? 0.29670 0.11370 0.13680 -0.02540 -0.00330 0.00840  501  HEM A NA    
3256 N  NB    . HEM B .   ? 0.28810 0.12520 0.11690 0.00710  -0.01300 0.01930  501  HEM A NB    
3257 N  NC    . HEM B .   ? 0.31520 0.13610 0.11050 0.00600  -0.01340 0.02410  501  HEM A NC    
3258 N  ND    . HEM B .   ? 0.28690 0.14010 0.14300 -0.01270 -0.00830 -0.00890 501  HEM A ND    
3259 FE FE    . HEM B .   ? 0.32000 0.13210 0.13120 0.00790  -0.00520 -0.00430 501  HEM A FE    
3260 C  C     A TRS C .   ? 0.43520 0.26390 0.27880 -0.04610 -0.01270 -0.05480 502  TRS A C     
3261 C  C     B TRS C .   ? 0.62080 0.32730 0.24690 -0.07110 -0.06430 0.01070  502  TRS A C     
3262 C  C1    A TRS C .   ? 0.41490 0.23550 0.25980 -0.02070 0.01300  -0.07160 502  TRS A C1    
3263 C  C1    B TRS C .   ? 0.65260 0.38090 0.24840 -0.07380 -0.09070 -0.01350 502  TRS A C1    
3264 C  C2    A TRS C .   ? 0.51770 0.24970 0.29540 -0.05420 -0.03230 -0.02700 502  TRS A C2    
3265 C  C2    B TRS C .   ? 0.61380 0.36330 0.27090 -0.01520 -0.06070 0.02920  502  TRS A C2    
3266 C  C3    A TRS C .   ? 0.36620 0.28590 0.27050 -0.00850 0.00540  -0.08260 502  TRS A C3    
3267 C  C3    B TRS C .   ? 0.54060 0.22000 0.22340 -0.08580 -0.03300 0.02510  502  TRS A C3    
3268 N  N     A TRS C .   ? 0.43640 0.30280 0.29440 -0.03460 -0.04820 -0.03580 502  TRS A N     
3269 N  N     B TRS C .   ? 0.67530 0.36760 0.25980 -0.05190 -0.06860 -0.01000 502  TRS A N     
3270 O  O1    A TRS C .   ? 0.34910 0.14960 0.23210 -0.02190 0.00830  -0.03250 502  TRS A O1    
3271 O  O1    B TRS C .   ? 0.68500 0.38910 0.24100 -0.07080 -0.07330 -0.01430 502  TRS A O1    
3272 O  O2    A TRS C .   ? 0.59530 0.22220 0.29870 -0.08810 -0.03750 -0.03240 502  TRS A O2    
3273 O  O2    B TRS C .   ? 0.62410 0.39750 0.28830 -0.00000 -0.03990 0.02580  502  TRS A O2    
3274 O  O3    A TRS C .   ? 0.31160 0.26280 0.26070 -0.00860 0.03740  -0.08550 502  TRS A O3    
3275 O  O3    B TRS C .   ? 0.44730 0.22970 0.19140 -0.07580 0.01060  0.02180  502  TRS A O3    
3276 C  C1    . FLF D .   ? 0.43920 0.32670 0.39780 -0.02630 -0.02720 -0.02530 503  FLF A C1    
3277 O  O1    . FLF D .   ? 0.43770 0.37730 0.43650 0.00550  -0.07790 -0.08420 503  FLF A O1    
3278 C  C2    . FLF D .   ? 0.47170 0.32690 0.39200 -0.02790 -0.02180 -0.03750 503  FLF A C2    
3279 C  C3    . FLF D .   ? 0.44000 0.31720 0.37580 -0.04990 -0.01790 -0.05910 503  FLF A C3    
3280 O  O2    . FLF D .   ? 0.42980 0.43450 0.44820 0.00100  -0.09300 -0.03260 503  FLF A O2    
3281 C  C4    . FLF D .   ? 0.43410 0.32780 0.36390 -0.01120 0.00830  -0.01750 503  FLF A C4    
3282 C  C5    . FLF D .   ? 0.41950 0.31980 0.35890 0.04090  0.01270  -0.00010 503  FLF A C5    
3283 C  C6    . FLF D .   ? 0.41260 0.30500 0.36190 0.00910  -0.01240 0.01760  503  FLF A C6    
3284 C  C7    . FLF D .   ? 0.43290 0.35110 0.42810 -0.01090 -0.06890 -0.05430 503  FLF A C7    
3285 N  N     . FLF D .   ? 0.37440 0.26030 0.33990 0.02160  0.00310  0.06630  503  FLF A N     
3286 C  "C1'" . FLF D .   ? 0.34440 0.24490 0.32930 0.01800  -0.00560 0.06310  503  FLF A "C1'" 
3287 C  "C2'" . FLF D .   ? 0.35260 0.19000 0.32860 0.05230  -0.01130 0.05400  503  FLF A "C2'" 
3288 C  "C3'" . FLF D .   ? 0.36350 0.18310 0.32790 0.04250  -0.03450 0.01140  503  FLF A "C3'" 
3289 C  "C4'" . FLF D .   ? 0.38940 0.15940 0.32820 0.01910  -0.04850 0.05100  503  FLF A "C4'" 
3290 C  "C5'" . FLF D .   ? 0.26900 0.11440 0.32660 0.01620  0.00910  0.02130  503  FLF A "C5'" 
3291 C  "C6'" . FLF D .   ? 0.34680 0.21400 0.33560 0.03200  0.01090  0.01100  503  FLF A "C6'" 
3292 C  "C7'" . FLF D .   ? 0.41370 0.32150 0.34150 0.08790  -0.03330 -0.02010 503  FLF A "C7'" 
3293 F  F1    . FLF D .   ? 0.43780 0.35870 0.35050 0.10020  -0.01220 -0.06170 503  FLF A F1    
3294 F  F2    . FLF D .   ? 0.45230 0.43490 0.35610 0.18990  -0.03850 0.00440  503  FLF A F2    
3295 F  F3    . FLF D .   ? 0.39570 0.35560 0.33130 0.05250  -0.02630 -0.07360 503  FLF A F3    
3296 C  C1    . EDO E .   ? 0.62380 0.63920 0.62470 0.11410  0.15250  -0.07440 504  EDO A C1    
3297 O  O1    . EDO E .   ? 0.69750 0.67760 0.63080 0.05780  0.13050  -0.06580 504  EDO A O1    
3298 C  C2    . EDO E .   ? 0.50980 0.60450 0.61570 0.21880  0.17510  -0.09240 504  EDO A C2    
3299 O  O2    . EDO E .   ? 0.56770 0.61780 0.62830 0.17940  0.15370  -0.08070 504  EDO A O2    
3300 C  C1    . EDO F .   ? 0.57740 0.76800 0.88590 -0.13580 -0.06850 -0.03720 505  EDO A C1    
3301 O  O1    . EDO F .   ? 0.47530 0.73890 0.87860 -0.11020 -0.05420 -0.03180 505  EDO A O1    
3302 C  C2    . EDO F .   ? 0.63780 0.77510 0.89270 -0.11560 -0.07860 -0.05120 505  EDO A C2    
3303 O  O2    . EDO F .   ? 0.68300 0.78890 0.89810 -0.12340 -0.08040 -0.06900 505  EDO A O2    
3304 C  C1    . EDO G .   ? 0.70250 0.72170 0.69350 -0.14680 0.07690  0.03770  506  EDO A C1    
3305 O  O1    . EDO G .   ? 0.71240 0.78350 0.70020 -0.15210 0.09970  0.08220  506  EDO A O1    
3306 C  C2    . EDO G .   ? 0.69230 0.64760 0.69010 -0.16200 0.06370  0.00470  506  EDO A C2    
3307 O  O2    . EDO G .   ? 0.68760 0.57140 0.68130 -0.16310 0.02250  -0.04560 506  EDO A O2    
3308 C  C1    . EDO H .   ? 0.76970 0.97030 0.69990 0.06660  -0.15310 0.30840  507  EDO A C1    
3309 O  O1    . EDO H .   ? 0.82370 0.98280 0.69870 0.09360  -0.13270 0.30290  507  EDO A O1    
3310 C  C2    . EDO H .   ? 0.66410 0.94350 0.69350 0.07310  -0.19870 0.33270  507  EDO A C2    
3311 O  O2    . EDO H .   ? 0.56800 0.90880 0.69590 0.08170  -0.21220 0.32330  507  EDO A O2    
3312 C  C1    . EDO I .   ? 0.99680 1.05950 1.02430 -0.02460 -0.03990 -0.02140 508  EDO A C1    
3313 O  O1    . EDO I .   ? 1.02490 1.06230 1.02030 -0.04800 -0.03290 -0.03050 508  EDO A O1    
3314 C  C2    . EDO I .   ? 0.99030 1.05220 1.02290 0.00930  -0.05310 -0.01580 508  EDO A C2    
3315 O  O2    . EDO I .   ? 0.99340 1.05310 1.01640 0.04130  -0.06200 -0.01170 508  EDO A O2    
3316 O  O     . HOH J .   ? 0.57100 0.48530 0.62550 -0.15260 -0.02880 -0.27670 601  HOH A O     
3317 O  O     . HOH J .   ? 0.86980 0.71180 0.51370 -0.02900 -0.07460 0.09820  602  HOH A O     
3318 O  O     . HOH J .   ? 0.62080 0.71890 0.42150 0.29190  -0.05760 -0.01810 603  HOH A O     
3319 O  O     . HOH J .   ? 0.61890 0.50660 0.68410 -0.21850 0.15640  -0.29180 604  HOH A O     
3320 O  O     . HOH J .   ? 0.55170 0.46340 0.82850 0.06530  0.21260  0.08630  605  HOH A O     
3321 O  O     . HOH J .   ? 0.64698 0.34611 0.31111 0.06699  -0.05449 0.14669  606  HOH A O     
3322 O  O     . HOH J .   ? 0.33840 0.25430 0.17980 0.02290  0.01270  0.00400  607  HOH A O     
3323 O  O     . HOH J .   ? 0.41560 0.41190 0.99320 0.03080  -0.25440 -0.13870 608  HOH A O     
3324 O  O     . HOH J .   ? 0.44890 0.67120 0.54910 -0.05850 0.11460  -0.21310 609  HOH A O     
3325 O  O     . HOH J .   ? 0.41700 0.29510 0.49350 0.02300  -0.03900 -0.00100 610  HOH A O     
3326 O  O     . HOH J .   ? 0.67130 0.40480 0.56280 -0.14140 -0.16120 0.21520  611  HOH A O     
3327 O  O     . HOH J .   ? 0.78860 0.53770 0.50270 0.10430  0.03520  0.14040  612  HOH A O     
3328 O  O     . HOH J .   ? 0.58520 0.41020 0.52170 -0.01740 0.09760  0.06040  613  HOH A O     
3329 O  O     . HOH J .   ? 0.70590 0.37880 0.54720 -0.12580 -0.19480 -0.05840 614  HOH A O     
3330 O  O     . HOH J .   ? 0.55700 0.28220 0.43950 -0.11850 0.01690  0.11140  615  HOH A O     
3331 O  O     . HOH J .   ? 0.38240 0.23181 0.37310 0.08440  -0.14090 -0.13829 616  HOH A O     
3332 O  O     . HOH J .   ? 0.83800 0.49730 0.27120 0.13090  -0.01500 0.10830  617  HOH A O     
3333 O  O     . HOH J .   ? 0.50590 0.25800 0.36730 -0.02900 -0.01000 0.04730  618  HOH A O     
3334 O  O     . HOH J .   ? 0.50900 0.38360 0.40570 0.03260  0.07810  0.07180  619  HOH A O     
3335 O  O     . HOH J .   ? 0.40170 0.33270 0.36040 -0.00900 0.05910  0.09350  620  HOH A O     
3336 O  O     . HOH J .   ? 0.61420 0.38000 0.19930 0.15750  0.00210  -0.02440 621  HOH A O     
3337 O  O     . HOH J .   ? 0.46050 0.78060 0.85670 0.08349  0.06950  0.48566  622  HOH A O     
3338 O  O     . HOH J .   ? 0.81210 0.79360 0.26120 -0.00350 -0.06870 0.01130  623  HOH A O     
3339 O  O     . HOH J .   ? 0.53870 1.00330 0.46580 0.21660  -0.11930 0.00000  624  HOH A O     
3340 O  O     . HOH J .   ? 0.78910 0.34230 0.64630 0.21100  -0.22870 -0.07380 625  HOH A O     
3341 O  O     . HOH J .   ? 0.60950 0.60990 0.49580 0.21340  0.10260  -0.01520 626  HOH A O     
3342 O  O     . HOH J .   ? 0.40310 0.82990 0.24190 0.10050  0.03190  -0.09050 627  HOH A O     
3343 O  O     . HOH J .   ? 0.51390 0.29010 0.30710 -0.11090 0.12310  0.01240  628  HOH A O     
3344 O  O     . HOH J .   ? 0.35950 0.21930 0.17960 0.07250  -0.08110 -0.03060 629  HOH A O     
3345 O  O     . HOH J .   ? 0.84666 0.23653 0.33530 -0.05959 -0.03790 0.04849  630  HOH A O     
3346 O  O     . HOH J .   ? 0.46760 0.40150 0.32900 0.02780  0.01910  0.02040  631  HOH A O     
3347 O  O     . HOH J .   ? 0.96990 0.31220 0.67380 0.14070  0.13520  0.11130  632  HOH A O     
3348 O  O     . HOH J .   ? 0.38330 0.21970 0.44350 0.06040  0.00770  -0.02850 633  HOH A O     
3349 O  O     . HOH J .   ? 0.47510 0.37760 0.30900 -0.00670 -0.01280 0.03230  634  HOH A O     
3350 O  O     . HOH J .   ? 0.47100 0.37120 0.64190 -0.02500 -0.02710 0.18950  635  HOH A O     
3351 O  O     . HOH J .   ? 0.92908 0.32712 0.55540 0.06150  -0.25619 -0.12289 636  HOH A O     
3352 O  O     . HOH J .   ? 0.65680 0.47640 0.26030 0.25630  -0.04580 0.04800  637  HOH A O     
3353 O  O     . HOH J .   ? 0.84118 0.32094 0.92458 -0.22768 0.01988  0.02461  638  HOH A O     
3354 O  O     . HOH J .   ? 0.55480 0.37710 0.56120 -0.08410 -0.29260 0.11220  639  HOH A O     
3355 O  O     . HOH J .   ? 0.51980 0.45660 0.35690 -0.09100 0.05520  0.13850  640  HOH A O     
3356 O  O     . HOH J .   ? 0.50120 1.04100 0.33610 0.25960  0.09590  0.09970  641  HOH A O     
3357 O  O     . HOH J .   ? 0.38740 0.14890 0.27660 0.04770  0.00470  0.02530  642  HOH A O     
3358 O  O     . HOH J .   ? 0.45190 0.19930 0.35170 0.01790  -0.00600 -0.00850 643  HOH A O     
3359 O  O     . HOH J .   ? 0.55700 0.49800 0.17680 0.17650  0.00370  -0.00430 644  HOH A O     
3360 O  O     . HOH J .   ? 0.39540 0.24260 0.27710 0.02470  -0.00020 0.05280  645  HOH A O     
3361 O  O     . HOH J .   ? 0.46520 0.74440 0.30930 -0.30380 -0.10680 0.12920  646  HOH A O     
3362 O  O     . HOH J .   ? 0.87930 0.53400 0.72000 -0.01460 0.18430  0.32020  647  HOH A O     
3363 O  O     . HOH J .   ? 0.75750 0.50360 0.23050 0.16700  -0.01750 -0.02690 648  HOH A O     
3364 O  O     . HOH J .   ? 0.47830 0.48890 0.44990 -0.01020 0.07760  -0.10730 649  HOH A O     
3365 O  O     . HOH J .   ? 0.43170 0.25380 0.27280 0.01540  0.01110  -0.02290 650  HOH A O     
3366 O  O     . HOH J .   ? 0.93738 0.28221 0.29491 -0.09870 -0.03700 0.04529  651  HOH A O     
3367 O  O     . HOH J .   ? 0.40690 0.25260 0.58910 -0.05750 0.02380  -0.05730 652  HOH A O     
3368 O  O     . HOH J .   ? 0.44290 0.21680 0.38090 0.07250  -0.12070 -0.06120 653  HOH A O     
3369 O  O     . HOH J .   ? 0.38330 0.18250 0.21110 0.00750  -0.07170 -0.00390 654  HOH A O     
3370 O  O     . HOH J .   ? 0.50090 0.33290 0.25380 0.02950  -0.03040 -0.00560 655  HOH A O     
3371 O  O     . HOH J .   ? 0.41520 0.25290 0.52540 0.01520  0.02290  -0.06940 656  HOH A O     
3372 O  O     . HOH J .   ? 0.33510 0.34290 0.24120 0.01520  -0.03810 -0.01460 657  HOH A O     
3373 O  O     . HOH J .   ? 0.81077 0.44420 0.35723 0.10259  -0.26067 -0.04090 658  HOH A O     
3374 O  O     . HOH J .   ? 0.42370 0.49860 0.34920 -0.02800 0.06620  0.09530  659  HOH A O     
3375 O  O     . HOH J .   ? 0.46200 1.04320 0.52100 0.24030  0.08970  0.29980  660  HOH A O     
3376 O  O     . HOH J .   ? 0.46590 0.35990 0.21970 0.15180  -0.02700 -0.03560 661  HOH A O     
3377 O  O     . HOH J .   ? 0.37140 0.53560 0.43170 0.10040  0.06410  -0.06840 662  HOH A O     
3378 O  O     . HOH J .   ? 0.80920 0.61260 0.67730 -0.07760 -0.36010 0.22040  663  HOH A O     
3379 O  O     . HOH J .   ? 0.66330 0.31380 0.54620 -0.16030 0.01660  0.00300  664  HOH A O     
3380 O  O     . HOH J .   ? 0.42790 0.25390 0.22770 0.10290  -0.01630 -0.01430 665  HOH A O     
3381 O  O     . HOH J .   ? 0.70880 0.79470 0.27450 0.25010  -0.05810 -0.09950 666  HOH A O     
3382 O  O     . HOH J .   ? 0.41020 0.25310 0.91280 0.00020  0.10390  0.10000  667  HOH A O     
3383 O  O     . HOH J .   ? 0.56450 0.25230 0.69040 0.12460  0.08050  0.03720  668  HOH A O     
3384 O  O     . HOH J .   ? 0.68390 0.83598 0.36972 0.17879  -0.05940 0.21688  669  HOH A O     
3385 O  O     . HOH J .   ? 0.88700 0.98610 0.78470 -0.06370 0.07770  -0.06960 670  HOH A O     
3386 O  O     . HOH J .   ? 0.31700 0.20200 0.15500 0.02810  0.01950  0.02970  671  HOH A O     
3387 O  O     . HOH J .   ? 0.39920 0.19940 0.22200 0.03390  -0.07330 -0.03370 672  HOH A O     
3388 O  O     . HOH J .   ? 0.43380 0.21710 0.21810 0.12810  -0.11200 -0.07920 673  HOH A O     
3389 O  O     . HOH J .   ? 0.45790 0.65368 0.32622 0.10239  0.08669  0.22857  674  HOH A O     
3390 O  O     . HOH J .   ? 0.39800 0.25150 0.46270 -0.01300 0.03580  0.09460  675  HOH A O     
3391 O  O     . HOH J .   ? 0.62590 0.42420 0.29010 0.20770  -0.10350 -0.13800 676  HOH A O     
3392 O  O     . HOH J .   ? 0.48540 0.26700 0.30750 0.04370  0.11830  0.08880  677  HOH A O     
3393 O  O     . HOH J .   ? 0.40580 0.42580 0.27620 -0.07500 -0.06410 0.04860  678  HOH A O     
3394 O  O     . HOH J .   ? 0.39070 0.26490 0.37090 0.00320  0.05640  0.08490  679  HOH A O     
3395 O  O     . HOH J .   ? 0.55020 0.43540 0.24210 -0.09860 -0.00700 0.04080  680  HOH A O     
3396 O  O     . HOH J .   ? 0.87250 0.35490 0.46580 -0.22730 -0.23260 0.10550  681  HOH A O     
3397 O  O     . HOH J .   ? 0.57940 0.26510 0.23380 0.16280  -0.04960 -0.06690 682  HOH A O     
3398 O  O     . HOH J .   ? 0.80080 0.22950 0.32480 0.05990  0.00960  0.02470  683  HOH A O     
3399 O  O     . HOH J .   ? 0.44740 0.26570 0.43790 -0.00630 0.04110  0.00410  684  HOH A O     
3400 O  O     . HOH J .   ? 0.48380 0.31110 0.48200 0.01520  0.04580  0.21870  685  HOH A O     
3401 O  O     . HOH J .   ? 0.75010 0.40810 0.70600 -0.02190 0.40170  -0.02900 686  HOH A O     
3402 O  O     . HOH J .   ? 0.75130 0.65980 0.73240 -0.27900 -0.04230 0.11370  687  HOH A O     
3403 O  O     . HOH J .   ? 0.41381 0.33651 1.04058 0.10259  0.09110  0.01920  688  HOH A O     
3404 O  O     . HOH J .   ? 0.86620 0.42820 0.57870 -0.02820 -0.12930 0.25010  689  HOH A O     
3405 O  O     . HOH J .   ? 0.50520 0.28220 0.84090 0.07830  0.05660  0.09840  690  HOH A O     
3406 O  O     . HOH J .   ? 0.43430 0.17410 0.29510 0.02220  -0.13370 0.03930  691  HOH A O     
3407 O  O     . HOH J .   ? 0.69100 0.26430 0.27720 0.03510  0.03070  0.06200  692  HOH A O     
3408 O  O     . HOH J .   ? 0.47330 0.42720 0.82270 -0.00270 -0.28590 -0.03950 693  HOH A O     
3409 O  O     . HOH J .   ? 0.63710 0.47470 0.25250 -0.16670 0.08700  -0.12650 694  HOH A O     
3410 O  O     . HOH J .   ? 0.56870 0.26600 0.52150 0.03570  -0.12200 -0.08510 695  HOH A O     
3411 O  O     . HOH J .   ? 0.69310 0.57590 0.34070 -0.19720 0.09840  -0.04110 696  HOH A O     
3412 O  O     . HOH J .   ? 0.33040 0.23830 0.25640 0.04200  0.01200  0.09700  697  HOH A O     
3413 O  O     . HOH J .   ? 0.47570 0.30390 0.72930 -0.04090 0.01370  0.03520  698  HOH A O     
3414 O  O     . HOH J .   ? 0.30510 0.20840 0.26130 0.00720  -0.05170 -0.05250 699  HOH A O     
3415 O  O     . HOH J .   ? 0.58920 0.19510 0.62350 0.04850  0.00560  -0.03430 700  HOH A O     
3416 O  O     . HOH J .   ? 0.27810 0.13480 0.12790 0.03780  -0.00280 -0.03060 701  HOH A O     
3417 O  O     . HOH J .   ? 0.52660 0.21900 0.34900 -0.04740 -0.00160 0.02760  702  HOH A O     
3418 O  O     . HOH J .   ? 0.43660 0.30160 0.28170 0.06630  0.06900  0.01340  703  HOH A O     
3419 O  O     . HOH J .   ? 0.38690 0.24210 0.28100 0.07140  0.00770  -0.06610 704  HOH A O     
3420 O  O     . HOH J .   ? 1.00009 0.66420 0.64501 -0.05990 0.44269  0.06040  705  HOH A O     
3421 O  O     . HOH J .   ? 0.52590 0.59820 0.37210 -0.05440 -0.09670 -0.21400 706  HOH A O     
3422 O  O     . HOH J .   ? 0.35870 0.37080 0.22810 -0.03490 0.01230  0.00430  707  HOH A O     
3423 O  O     . HOH J .   ? 0.34750 0.28950 0.24990 -0.02330 -0.00130 -0.01620 708  HOH A O     
3424 O  O     . HOH J .   ? 0.70820 0.35340 0.64940 -0.02070 -0.33050 -0.10850 709  HOH A O     
3425 O  O     . HOH J .   ? 0.69980 0.41540 0.58290 -0.25460 0.04630  0.11300  710  HOH A O     
3426 O  O     . HOH J .   ? 0.83630 0.50060 0.55430 0.17840  0.01210  0.01450  711  HOH A O     
3427 O  O     . HOH J .   ? 0.85028 0.69960 0.50032 0.33716  0.00369  -0.20997 712  HOH A O     
3428 O  O     . HOH J .   ? 0.94930 0.71610 0.49310 -0.40210 -0.24140 0.06260  713  HOH A O     
3429 O  O     . HOH J .   ? 0.45070 0.24240 0.35440 0.02700  -0.11010 0.00870  714  HOH A O     
3430 O  O     . HOH J .   ? 0.40830 0.34690 0.30750 0.06750  -0.02400 -0.07190 715  HOH A O     
3431 O  O     . HOH J .   ? 0.64800 0.58610 0.50660 -0.07990 -0.07700 -0.10240 716  HOH A O     
3432 O  O     . HOH J .   ? 0.45310 0.24833 0.83617 0.02259  0.15169  -0.08989 717  HOH A O     
3433 O  O     . HOH J .   ? 0.89500 0.52530 0.28050 0.09230  -0.02880 -0.12120 718  HOH A O     
3434 O  O     . HOH J .   ? 0.58839 0.58359 0.34763 -0.16428 -0.06899 0.22387  719  HOH A O     
3435 O  O     . HOH J .   ? 0.43450 0.20850 0.39640 0.03660  -0.03800 0.02400  720  HOH A O     
3436 O  O     . HOH J .   ? 0.60710 0.33720 0.58980 0.02640  -0.17390 -0.17850 721  HOH A O     
3437 O  O     . HOH J .   ? 0.48360 0.21870 0.35310 0.01360  -0.13590 -0.01620 722  HOH A O     
3438 O  O     . HOH J .   ? 0.48960 0.22090 0.51000 0.04600  -0.04380 0.08110  723  HOH A O     
3439 O  O     . HOH J .   ? 0.70490 0.58370 0.62380 0.17080  0.12990  0.33389  724  HOH A O     
3440 O  O     . HOH J .   ? 0.57830 0.32200 0.42770 0.04430  0.10160  0.09990  725  HOH A O     
3441 O  O     . HOH J .   ? 0.53680 0.39750 1.12140 -0.04270 -0.09130 -0.11590 726  HOH A O     
3442 O  O     . HOH J .   ? 0.45220 0.35910 0.42120 0.05620  0.05060  -0.06160 727  HOH A O     
3443 O  O     . HOH J .   ? 0.59240 0.27480 0.32570 -0.00550 0.02520  -0.01120 728  HOH A O     
3444 O  O     . HOH J .   ? 0.54980 0.55350 0.77190 -0.03240 -0.26490 0.02990  729  HOH A O     
3445 O  O     . HOH J .   ? 0.54200 0.41110 0.33960 0.12700  0.04970  0.06610  730  HOH A O     
3446 O  O     . HOH J .   ? 0.41230 0.25690 0.32820 0.02090  -0.07030 -0.02560 731  HOH A O     
3447 O  O     . HOH J .   ? 0.33360 0.42800 0.95600 0.07730  -0.16640 -0.30950 732  HOH A O     
3448 O  O     . HOH J .   ? 0.46690 0.89129 0.35421 0.08170  -0.11540 0.15680  733  HOH A O     
3449 O  O     . HOH J .   ? 0.43500 0.28510 0.39390 -0.09540 -0.03630 -0.10200 734  HOH A O     
3450 O  O     . HOH J .   ? 0.95567 0.52781 0.36073 0.28538  -0.08420 -0.12958 735  HOH A O     
3451 O  O     . HOH J .   ? 0.53459 0.51089 0.22502 0.02659  -0.09419 -0.13629 736  HOH A O     
3452 O  O     . HOH J .   ? 0.55460 0.76649 0.49311 0.14719  -0.00120 0.32429  737  HOH A O     
3453 O  O     . HOH J .   ? 0.28410 0.13430 0.14950 -0.00550 -0.01550 -0.00100 738  HOH A O     
3454 O  O     . HOH J .   ? 0.46940 0.21050 0.17850 0.02850  0.04540  0.03850  739  HOH A O     
3455 O  O     . HOH J .   ? 0.33480 0.16270 0.15700 0.01230  -0.04470 -0.02190 740  HOH A O     
3456 O  O     . HOH J .   ? 0.33230 0.17670 0.23600 0.02180  -0.05670 -0.05740 741  HOH A O     
3457 O  O     . HOH J .   ? 0.36090 0.89150 0.76160 -0.00500 0.00860  0.48290  742  HOH A O     
3458 O  O     . HOH J .   ? 0.63760 0.23680 0.47610 0.03020  -0.05830 0.01840  743  HOH A O     
3459 O  O     . HOH J .   ? 0.63120 0.56210 0.69280 0.03550  -0.23440 0.07770  744  HOH A O     
3460 O  O     . HOH J .   ? 0.58390 0.21280 0.50290 -0.00460 -0.11410 -0.08240 745  HOH A O     
3461 O  O     . HOH J .   ? 0.61820 0.50580 0.53270 -0.29999 0.19180  -0.07820 746  HOH A O     
3462 O  O     . HOH J .   ? 0.41920 0.24000 0.43210 0.00180  -0.11130 -0.03700 747  HOH A O     
3463 O  O     . HOH J .   ? 0.58250 0.38580 0.28620 0.10410  0.09170  0.11460  748  HOH A O     
3464 O  O     . HOH J .   ? 0.52550 0.50600 0.28770 0.20580  0.00110  -0.04400 749  HOH A O     
3465 O  O     . HOH J .   ? 0.39890 0.18560 0.23830 0.01200  -0.07410 -0.04850 750  HOH A O     
3466 O  O     . HOH J .   ? 0.89478 0.31442 0.59230 0.03860  0.15919  -0.13979 751  HOH A O     
3467 O  O     . HOH J .   ? 0.36270 0.32570 0.31030 0.04550  -0.02720 -0.04690 752  HOH A O     
3468 O  O     . HOH J .   ? 0.29030 0.33340 0.26090 0.05080  -0.01020 -0.11890 753  HOH A O     
3469 O  O     . HOH J .   ? 0.97070 0.51700 0.37030 0.00860  0.19680  -0.02470 754  HOH A O     
3470 O  O     . HOH J .   ? 0.75550 0.87410 0.33880 -0.19050 -0.01540 0.00610  755  HOH A O     
3471 O  O     . HOH J .   ? 0.66100 0.61500 0.31330 0.12150  -0.11810 -0.19260 756  HOH A O     
3472 O  O     . HOH J .   ? 0.47280 0.40220 0.35460 0.14320  -0.00720 0.03280  757  HOH A O     
3473 O  O     . HOH J .   ? 0.35250 0.47970 0.31110 0.04810  -0.04980 0.05250  758  HOH A O     
3474 O  O     . HOH J .   ? 0.67700 0.30630 0.29640 0.10310  0.06450  -0.09570 759  HOH A O     
3475 O  O     . HOH J .   ? 0.61930 0.39330 1.08020 0.03650  -0.14280 -0.19580 760  HOH A O     
3476 O  O     . HOH J .   ? 0.49230 0.22820 0.35790 -0.01040 -0.14710 -0.04120 761  HOH A O     
3477 O  O     . HOH J .   ? 0.55440 0.64780 0.89540 -0.13730 0.15780  -0.24700 762  HOH A O     
3478 O  O     . HOH J .   ? 0.58300 0.45900 0.52190 0.21990  0.02240  -0.06530 763  HOH A O     
3479 O  O     . HOH J .   ? 0.40630 0.30020 0.19620 -0.00070 0.07290  -0.05250 764  HOH A O     
3480 O  O     . HOH J .   ? 0.60220 1.04920 0.35330 0.05130  0.02990  -0.06430 765  HOH A O     
3481 O  O     . HOH J .   ? 0.61920 0.93680 0.56830 -0.20240 -0.06860 0.04180  766  HOH A O     
3482 O  O     . HOH J .   ? 0.33670 0.21580 0.23780 0.02100  0.04670  -0.01510 767  HOH A O     
3483 O  O     . HOH J .   ? 0.62170 0.39290 0.64140 -0.07860 -0.17530 -0.01360 768  HOH A O     
3484 O  O     . HOH J .   ? 0.39610 0.33350 0.75250 -0.07460 -0.10490 0.19360  769  HOH A O     
3485 O  O     . HOH J .   ? 0.47450 0.26910 0.25710 0.13990  0.03200  -0.00430 770  HOH A O     
3486 O  O     . HOH J .   ? 0.41710 0.38150 0.35180 0.08150  -0.15839 -0.17899 771  HOH A O     
3487 O  O     . HOH J .   ? 0.54760 0.23310 0.22800 0.09250  -0.04070 -0.02430 772  HOH A O     
3488 O  O     . HOH J .   ? 0.54190 0.36460 0.44200 0.11870  -0.07000 -0.05830 773  HOH A O     
3489 O  O     . HOH J .   ? 0.53070 0.35290 0.40850 0.09860  -0.13210 -0.10670 774  HOH A O     
3490 O  O     . HOH J .   ? 0.51180 0.36400 0.23420 -0.00450 -0.00260 -0.00500 775  HOH A O     
3491 O  O     . HOH J .   ? 1.04800 0.36460 0.92010 -0.17580 -0.25130 0.00600  776  HOH A O     
3492 O  O     . HOH J .   ? 0.76099 0.40940 0.54090 0.05710  -0.06010 0.26080  777  HOH A O     
3493 O  O     . HOH J .   ? 0.57050 0.28480 0.23050 -0.11300 0.05480  -0.03040 778  HOH A O     
3494 O  O     . HOH J .   ? 0.55950 0.30130 0.43070 0.08520  -0.00860 -0.07220 779  HOH A O     
3495 O  O     . HOH J .   ? 0.38300 0.24760 0.17460 0.04160  0.02170  0.01290  780  HOH A O     
3496 O  O     . HOH J .   ? 0.65840 0.65670 0.32230 0.31470  -0.15250 -0.07330 781  HOH A O     
3497 O  O     . HOH J .   ? 0.60028 0.27142 0.29940 0.17548  -0.16359 -0.08958 782  HOH A O     
3498 O  O     . HOH J .   ? 0.35970 0.40320 0.32420 0.01950  -0.06680 -0.00850 783  HOH A O     
3499 O  O     . HOH J .   ? 0.58710 0.74820 0.42090 0.11280  -0.04410 0.14360  784  HOH A O     
3500 O  O     . HOH J .   ? 0.74619 0.28441 0.30421 -0.05660 0.15659  -0.08239 785  HOH A O     
3501 O  O     . HOH J .   ? 0.85080 0.53610 0.57300 -0.17190 -0.05550 -0.03940 786  HOH A O     
3502 O  O     . HOH J .   ? 0.61750 0.86920 0.50550 -0.08750 -0.28000 -0.12510 787  HOH A O     
3503 O  O     . HOH J .   ? 0.64630 0.77250 0.38060 -0.03700 0.00890  -0.15670 788  HOH A O     
3504 O  O     . HOH J .   ? 0.35600 0.14290 0.15450 0.00690  -0.00020 0.02360  789  HOH A O     
3505 O  O     . HOH J .   ? 0.49280 0.65340 0.50700 0.13790  -0.15580 -0.31710 790  HOH A O     
3506 O  O     . HOH J .   ? 0.84876 0.32613 0.41831 0.11559  -0.15609 -0.12997 791  HOH A O     
3507 O  O     . HOH J .   ? 1.07439 0.39021 0.58330 -0.21220 0.35420  -0.09730 792  HOH A O     
3508 O  O     . HOH J .   ? 0.36710 0.17470 0.21100 0.02710  0.00030  -0.03110 793  HOH A O     
3509 O  O     . HOH J .   ? 0.38960 0.54910 0.52440 0.03560  -0.10950 -0.30240 794  HOH A O     
3510 O  O     . HOH J .   ? 0.67600 0.29810 0.51800 -0.11600 -0.05750 -0.07420 795  HOH A O     
3511 O  O     . HOH J .   ? 0.80310 0.46760 0.59410 -0.26920 -0.23990 -0.00680 796  HOH A O     
3512 O  O     . HOH J .   ? 0.39330 0.20540 0.43260 -0.04360 -0.10050 -0.07030 797  HOH A O     
3513 O  O     . HOH J .   ? 0.74630 0.34581 0.68649 -0.07520 0.03280  0.24658  798  HOH A O     
3514 O  O     . HOH J .   ? 0.50630 0.32170 0.29830 0.13660  -0.07580 -0.12640 799  HOH A O     
3515 O  O     . HOH J .   ? 0.69730 0.31360 0.74320 0.05750  -0.20980 0.03950  800  HOH A O     
3516 O  O     . HOH J .   ? 0.54390 0.75550 0.21830 -0.16810 0.03380  0.01850  801  HOH A O     
3517 O  O     . HOH J .   ? 0.44350 0.28290 0.25110 0.04890  0.01910  0.07080  802  HOH A O     
3518 O  O     . HOH J .   ? 0.45750 0.13843 0.55117 -0.01230 -0.00420 -0.00620 803  HOH A O     
3519 O  O     . HOH J .   ? 0.47900 0.43790 0.44760 0.03890  0.01010  0.12560  804  HOH A O     
3520 O  O     . HOH J .   ? 0.63040 0.90370 0.50280 0.09010  -0.10220 0.12860  805  HOH A O     
3521 O  O     . HOH J .   ? 0.80850 1.00410 0.50350 0.38170  0.04150  -0.16840 806  HOH A O     
3522 O  O     . HOH J .   ? 0.55910 0.54960 0.23520 -0.10840 0.10170  -0.03870 807  HOH A O     
3523 O  O     . HOH J .   ? 0.68780 0.90790 0.42130 -0.01660 0.01130  -0.31000 808  HOH A O     
3524 O  O     . HOH J .   ? 0.40500 0.28950 1.14710 0.00720  0.05730  -0.02490 809  HOH A O     
3525 O  O     . HOH J .   ? 0.48850 0.32790 0.49490 -0.07280 -0.09060 -0.07050 810  HOH A O     
3526 O  O     . HOH J .   ? 0.61860 0.79080 0.52240 -0.31930 -0.07580 0.07250  811  HOH A O     
3527 O  O     . HOH J .   ? 1.14650 0.53730 0.35870 0.06520  0.09130  -0.04650 812  HOH A O     
3528 O  O     . HOH J .   ? 0.90080 0.57490 0.76760 0.29220  0.43170  0.22910  813  HOH A O     
3529 O  O     . HOH J .   ? 0.71009 1.09288 0.34972 0.38999  0.07069  0.06400  814  HOH A O     
3530 O  O     . HOH J .   ? 0.92400 0.38150 0.86620 -0.03220 0.31730  -0.18230 815  HOH A O     
3531 O  O     . HOH J .   ? 1.09159 0.34500 0.38201 -0.07950 -0.24140 0.04950  816  HOH A O     
3532 O  O     . HOH J .   ? 0.42160 0.31850 0.15540 0.01030  0.02000  -0.03020 817  HOH A O     
3533 O  O     . HOH J .   ? 0.44820 0.22280 0.30540 0.07330  -0.01040 -0.06030 818  HOH A O     
3534 O  O     . HOH J .   ? 0.55080 0.36610 0.26500 -0.09370 -0.06130 0.07910  819  HOH A O     
3535 O  O     . HOH J .   ? 0.60400 0.35000 0.66830 -0.12960 0.33080  -0.14990 820  HOH A O     
3536 O  O     . HOH J .   ? 0.50120 0.75370 0.73930 0.05300  -0.34339 0.05270  821  HOH A O     
3537 O  O     . HOH J .   ? 0.54990 0.40050 0.29820 0.04660  0.03260  -0.01900 822  HOH A O     
3538 O  O     . HOH J .   ? 0.78000 0.47610 0.56990 -0.12170 -0.17160 -0.22510 823  HOH A O     
3539 O  O     . HOH J .   ? 0.78460 0.71500 0.81020 0.34440  0.01530  0.29730  824  HOH A O     
3540 O  O     . HOH J .   ? 0.77830 0.65010 0.51020 0.30070  -0.15780 -0.26990 825  HOH A O     
3541 O  O     . HOH J .   ? 0.39320 0.32980 0.90600 -0.02770 -0.13140 0.09590  826  HOH A O     
3542 O  O     . HOH J .   ? 0.64380 0.20530 0.44520 0.01890  0.20440  -0.00810 827  HOH A O     
3543 O  O     . HOH J .   ? 0.86630 0.65630 0.69690 0.00090  0.18070  0.00320  828  HOH A O     
3544 O  O     . HOH J .   ? 0.67300 0.37990 0.99280 0.08600  0.14210  0.01930  829  HOH A O     
3545 O  O     . HOH J .   ? 0.69960 0.75610 0.41600 -0.04340 -0.08470 0.07370  830  HOH A O     
3546 O  O     . HOH J .   ? 0.38910 0.48750 0.19020 -0.09340 -0.04670 0.09870  831  HOH A O     
3547 O  O     . HOH J .   ? 1.18970 0.31690 0.38630 -0.05790 -0.06070 0.01280  832  HOH A O     
3548 O  O     . HOH J .   ? 0.58850 0.81090 0.54490 0.05460  -0.33320 0.03620  833  HOH A O     
3549 O  O     . HOH J .   ? 0.61500 0.35800 0.78400 0.13760  -0.10610 -0.14170 834  HOH A O     
3550 O  O     . HOH J .   ? 0.87380 0.86260 0.22850 0.02580  -0.00360 0.05290  835  HOH A O     
3551 O  O     . HOH J .   ? 0.98260 0.34630 0.45560 0.11990  0.19350  0.11960  836  HOH A O     
3552 O  O     . HOH J .   ? 0.48530 0.46260 1.16640 -0.05120 -0.18530 0.11670  837  HOH A O     
3553 O  O     . HOH J .   ? 0.43300 0.18380 0.38230 0.05520  -0.04510 0.02320  838  HOH A O     
3554 O  O     . HOH J .   ? 0.57010 0.52010 0.57170 0.04050  0.17510  0.21990  839  HOH A O     
3555 O  O     . HOH J .   ? 0.58480 0.86570 0.75650 0.12430  -0.20810 -0.17280 840  HOH A O     
3556 O  O     . HOH J .   ? 0.42650 0.43500 0.36110 -0.01530 0.01720  -0.09950 841  HOH A O     
3557 O  O     . HOH J .   ? 0.57780 0.45651 0.75439 -0.12720 -0.14539 -0.24119 842  HOH A O     
3558 O  O     . HOH J .   ? 0.33710 0.15370 0.15220 0.02250  -0.00850 0.02910  843  HOH A O     
3559 O  O     . HOH J .   ? 0.44270 0.30080 0.38610 -0.04400 0.06570  -0.03240 844  HOH A O     
3560 O  O     . HOH J .   ? 0.79820 0.26490 0.38150 0.05810  0.20360  0.02980  845  HOH A O     
3561 O  O     . HOH J .   ? 0.48710 0.39120 0.46700 0.05610  0.00670  0.01210  846  HOH A O     
3562 O  O     . HOH J .   ? 0.62390 0.31440 0.57500 0.01470  -0.03820 0.06210  847  HOH A O     
3563 O  O     . HOH J .   ? 0.70990 0.46760 0.23780 0.26770  -0.07890 -0.03060 848  HOH A O     
3564 O  O     . HOH J .   ? 0.75450 0.62560 0.53560 -0.12770 0.15740  0.01710  849  HOH A O     
3565 O  O     . HOH J .   ? 0.51520 0.34000 0.42690 0.06450  0.03150  -0.12370 850  HOH A O     
3566 O  O     . HOH J .   ? 0.81010 0.35710 0.70220 0.03120  -0.24370 0.01090  851  HOH A O     
3567 O  O     . HOH J .   ? 0.99840 0.68780 0.36660 -0.10420 0.01570  -0.15540 852  HOH A O     
3568 O  O     . HOH J .   ? 0.63700 0.74230 0.44140 -0.15310 0.13070  0.08200  853  HOH A O     
3569 O  O     . HOH J .   ? 0.71810 1.05510 0.46970 0.33870  -0.07260 -0.08760 854  HOH A O     
3570 O  O     . HOH J .   ? 0.50360 0.23340 0.51870 0.00560  0.06100  -0.11090 855  HOH A O     
3571 O  O     . HOH J .   ? 0.80750 0.42350 0.26580 0.07760  -0.09710 0.04290  856  HOH A O     
3572 O  O     . HOH J .   ? 0.50280 0.33480 0.50600 -0.07070 -0.08540 -0.12750 857  HOH A O     
3573 O  O     . HOH J .   ? 0.82890 0.69570 0.44170 -0.18170 0.24230  0.11220  858  HOH A O     
3574 O  O     . HOH J .   ? 0.64410 0.77110 0.63000 -0.30990 -0.24850 -0.01270 859  HOH A O     
3575 O  O     . HOH J .   ? 0.39990 0.75540 0.69260 -0.11700 -0.05360 0.41520  860  HOH A O     
3576 O  O     . HOH J .   ? 0.68930 0.35140 0.56220 0.00800  -0.00770 0.24170  861  HOH A O     
3577 O  O     . HOH J .   ? 0.63000 1.07450 0.56360 -0.02080 -0.00240 0.14730  862  HOH A O     
3578 O  O     . HOH J .   ? 0.87670 0.50790 0.27370 -0.26340 -0.08630 0.05370  863  HOH A O     
3579 O  O     . HOH J .   ? 0.55560 0.51060 0.65100 -0.05530 -0.13550 -0.03360 864  HOH A O     
3580 O  O     . HOH J .   ? 0.57970 0.56750 0.30490 0.09440  0.03890  -0.03450 865  HOH A O     
3581 O  O     . HOH J .   ? 0.48990 0.73130 0.64820 -0.05800 0.06630  -0.28390 866  HOH A O     
3582 O  O     . HOH J .   ? 0.73760 0.76920 0.28360 0.13470  0.02630  0.13940  867  HOH A O     
3583 O  O     . HOH J .   ? 0.37780 0.97590 0.25040 -0.00400 -0.00830 0.05890  868  HOH A O     
3584 O  O     . HOH J .   ? 0.81990 0.54270 0.81770 0.12630  0.15980  -0.20890 869  HOH A O     
3585 O  O     . HOH J .   ? 1.01750 0.57690 0.30800 0.00600  -0.17950 -0.00350 870  HOH A O     
3586 O  O     . HOH J .   ? 0.40980 0.42500 1.20400 -0.06030 -0.07440 0.24070  871  HOH A O     
3587 O  O     . HOH J .   ? 0.42690 0.62320 1.05010 -0.13260 -0.05170 -0.11890 872  HOH A O     
3588 O  O     . HOH J .   ? 0.60750 0.51500 0.82780 -0.00080 0.09710  0.32200  873  HOH A O     
3589 O  O     . HOH J .   ? 0.47870 0.52500 0.41370 -0.04140 0.09230  -0.01790 874  HOH A O     
3590 O  O     . HOH J .   ? 0.50250 0.54020 0.39000 0.08450  0.00520  -0.10910 875  HOH A O     
3591 O  O     . HOH J .   ? 0.73540 0.74540 0.71710 0.01520  -0.30940 0.02290  876  HOH A O     
3592 O  O     . HOH J .   ? 0.54690 0.78100 0.40550 -0.00560 0.08280  0.11960  877  HOH A O     
3593 O  O     . HOH J .   ? 0.74790 0.60520 0.71830 0.29620  -0.37350 -0.31500 878  HOH A O     
3594 O  O     . HOH J .   ? 0.72060 0.53320 0.52790 -0.13660 0.05110  -0.20360 879  HOH A O     
3595 O  O     . HOH J .   ? 0.53230 0.53810 0.53870 0.11550  -0.13290 -0.20990 880  HOH A O     
3596 O  O     . HOH J .   ? 0.69470 0.47870 0.30420 -0.20640 -0.01880 -0.01460 881  HOH A O     
3597 O  O     . HOH J .   ? 0.72950 0.28570 0.48060 -0.00900 -0.18110 0.04860  882  HOH A O     
3598 O  O     . HOH J .   ? 0.68408 0.27150 0.21842 -0.00630 0.09219  0.04909  883  HOH A O     
3599 O  O     . HOH J .   ? 0.70180 0.55910 0.43430 0.16570  -0.22510 -0.01060 884  HOH A O     
3600 O  O     . HOH J .   ? 0.78810 0.35010 0.62310 0.13800  0.39680  0.13050  885  HOH A O     
3601 O  O     . HOH J .   ? 0.49690 0.33850 0.53720 0.03320  0.02740  -0.05020 886  HOH A O     
3602 O  O     . HOH J .   ? 0.82160 0.57980 0.59720 0.18680  -0.09210 -0.13660 887  HOH A O     
3603 O  O     . HOH J .   ? 0.43560 0.53920 0.30970 -0.13130 0.10320  -0.09470 888  HOH A O     
3604 O  O     . HOH J .   ? 0.32252 0.85980 1.13518 -0.07280 0.13629  -0.05940 889  HOH A O     
3605 O  O     . HOH J .   ? 0.47800 0.42330 0.46310 0.00080  0.00040  0.00740  890  HOH A O     
3606 O  O     . HOH J .   ? 0.49760 0.73390 0.28250 -0.18630 0.03180  -0.00890 891  HOH A O     
3607 O  O     . HOH J .   ? 1.11350 0.46150 0.53600 0.12040  0.33890  -0.04210 892  HOH A O     
3608 O  O     . HOH J .   ? 0.50200 0.32160 0.47240 -0.02390 0.02860  -0.19660 893  HOH A O     
3609 O  O     . HOH J .   ? 0.76330 0.59890 0.48760 0.13120  -0.07010 -0.19360 894  HOH A O     
3610 O  O     . HOH J .   ? 0.49530 0.78540 0.77070 0.26700  -0.00780 0.06880  895  HOH A O     
3611 O  O     . HOH J .   ? 0.85840 0.29250 0.71920 0.00560  -0.01840 0.11630  896  HOH A O     
3612 O  O     . HOH J .   ? 0.65910 0.79940 0.61230 0.13280  -0.06860 0.13040  897  HOH A O     
3613 O  O     . HOH J .   ? 0.62730 0.94470 0.53420 0.21030  -0.07600 -0.09240 898  HOH A O     
3614 O  O     . HOH J .   ? 1.19700 0.41580 0.73030 -0.08820 0.41440  0.02140  899  HOH A O     
3615 O  O     . HOH J .   ? 0.74810 0.45180 0.51920 -0.13190 -0.32690 0.11260  900  HOH A O     
3616 O  O     . HOH J .   ? 0.44450 0.82980 0.26700 -0.05260 -0.07110 -0.11960 901  HOH A O     
3617 O  O     . HOH J .   ? 0.63010 0.44000 0.52940 0.10090  0.12610  0.13200  902  HOH A O     
3618 O  O     . HOH J .   ? 0.95298 0.60061 0.43392 0.34467  -0.07670 -0.16378 903  HOH A O     
3619 O  O     . HOH J .   ? 0.91000 0.62840 0.42580 -0.22200 -0.11010 0.22920  904  HOH A O     
3620 O  O     . HOH J .   ? 0.75810 0.42060 0.44040 0.13150  -0.14620 -0.20450 905  HOH A O     
3621 O  O     . HOH J .   ? 0.52320 1.06060 0.64090 0.20630  -0.15890 -0.18680 906  HOH A O     
3622 O  O     . HOH J .   ? 0.74000 0.78880 0.66390 -0.02460 0.29440  0.03100  907  HOH A O     
3623 O  O     . HOH J .   ? 0.77300 0.32500 0.90630 0.12680  0.08920  -0.01900 908  HOH A O     
3624 O  O     . HOH J .   ? 0.74590 0.38670 0.49620 -0.06110 0.24580  -0.17420 909  HOH A O     
3625 O  O     . HOH J .   ? 0.57160 0.28600 0.36340 0.02330  -0.12770 -0.03850 910  HOH A O     
3626 O  O     . HOH J .   ? 0.91180 0.35820 0.37520 -0.12110 -0.27070 0.04780  911  HOH A O     
3627 O  O     . HOH J .   ? 0.87870 0.27900 0.93460 -0.14570 0.00820  0.02630  912  HOH A O     
3628 O  O     . HOH J .   ? 0.53600 0.29320 0.68190 0.01350  0.00760  0.11340  913  HOH A O     
3629 O  O     . HOH J .   ? 0.63510 0.83590 0.43880 -0.03450 -0.08700 0.18260  914  HOH A O     
3630 O  O     . HOH J .   ? 0.56290 0.55930 1.17320 0.01030  0.34790  -0.22470 915  HOH A O     
3631 O  O     . HOH J .   ? 1.11480 0.73040 0.50600 0.43950  0.11910  -0.05680 916  HOH A O     
3632 O  O     . HOH J .   ? 0.57100 0.97830 0.63390 -0.32210 -0.09690 0.17250  917  HOH A O     
3633 O  O     . HOH J .   ? 0.57290 0.57040 0.64860 -0.24380 -0.22190 0.25800  918  HOH A O     
3634 O  O     . HOH J .   ? 0.66580 0.64130 0.42800 -0.00930 0.21040  -0.09780 919  HOH A O     
3635 O  O     . HOH J .   ? 1.16720 0.42270 0.72940 -0.06170 0.21620  -0.20280 920  HOH A O     
3636 O  O     . HOH J .   ? 0.63900 0.37080 0.56710 -0.09440 -0.00410 -0.05970 921  HOH A O     
3637 O  O     . HOH J .   ? 0.55400 0.25830 0.43380 -0.09950 -0.22510 0.08040  922  HOH A O     
3638 O  O     . HOH J .   ? 0.42010 1.00750 0.38770 -0.10780 -0.00480 0.17420  923  HOH A O     
3639 O  O     . HOH J .   ? 1.17108 0.54830 0.34192 -0.00990 0.06120  0.10479  924  HOH A O     
3640 O  O     . HOH J .   ? 0.80640 0.88490 0.48060 0.09340  0.10390  0.21630  925  HOH A O     
3641 O  O     . HOH J .   ? 0.77090 0.75540 0.42620 0.12740  0.04700  0.12280  926  HOH A O     
3642 O  O     . HOH J .   ? 0.73830 0.52150 0.54730 -0.05070 -0.26810 -0.11800 927  HOH A O     
3643 O  O     . HOH J .   ? 0.58910 0.59890 0.90819 0.09640  -0.35288 -0.30309 928  HOH A O     
3644 O  O     . HOH J .   ? 1.10860 0.58610 0.51120 0.33830  0.25340  0.05680  929  HOH A O     
3645 O  O     . HOH J .   ? 0.61730 0.78460 0.63550 0.11670  0.17610  -0.07150 930  HOH A O     
3646 O  O     . HOH J .   ? 0.62880 0.50930 0.20600 0.22160  -0.04540 -0.01140 931  HOH A O     
3647 O  O     . HOH J .   ? 0.71010 0.77820 0.86830 -0.19770 0.13540  0.36910  932  HOH A O     
3648 O  O     . HOH J .   ? 0.44340 0.23940 0.41770 -0.05590 0.01410  -0.06280 933  HOH A O     
3649 O  O     . HOH J .   ? 0.59690 0.48410 1.10089 -0.03630 0.27410  0.24899  934  HOH A O     
3650 O  O     . HOH J .   ? 0.60600 0.50450 0.47460 0.07730  0.02900  0.05550  935  HOH A O     
3651 O  O     . HOH J .   ? 0.40330 0.44560 0.25650 0.09700  -0.00630 0.00630  936  HOH A O     
3652 O  O     . HOH J .   ? 0.52980 0.38300 0.41420 0.00710  -0.10750 0.06460  937  HOH A O     
3653 O  O     . HOH J .   ? 0.87900 0.42800 0.33330 -0.00290 0.15050  -0.05290 938  HOH A O     
3654 O  O     . HOH J .   ? 0.53880 0.52700 0.60280 0.03520  -0.12790 0.00270  939  HOH A O     
3655 O  O     . HOH J .   ? 1.21167 0.76891 0.58682 0.14859  -0.10559 0.31698  940  HOH A O     
3656 O  O     . HOH J .   ? 0.65050 0.49590 1.13400 0.04660  -0.45400 -0.08780 941  HOH A O     
3657 O  O     . HOH J .   ? 0.54140 0.65300 0.37070 0.13770  -0.00970 -0.06180 942  HOH A O     
3658 O  O     . HOH J .   ? 0.76630 0.32540 0.44760 -0.05710 0.03460  -0.14060 943  HOH A O     
3659 O  O     . HOH J .   ? 0.51840 0.53410 0.28960 -0.24410 0.04520  -0.06440 944  HOH A O     
3660 O  O     . HOH J .   ? 0.55160 0.25350 0.56760 0.08470  0.08940  0.04410  945  HOH A O     
3661 O  O     . HOH J .   ? 0.79120 0.91990 0.48440 -0.07170 0.15290  -0.10330 946  HOH A O     
3662 O  O     . HOH J .   ? 0.61940 0.53480 0.68110 0.02350  -0.04910 -0.19920 947  HOH A O     
3663 O  O     . HOH J .   ? 0.99400 0.60610 0.83120 0.03890  -0.04820 0.36810  948  HOH A O     
3664 O  O     . HOH J .   ? 0.54700 0.32400 0.39860 0.08110  -0.02850 -0.00270 949  HOH A O     
3665 O  O     . HOH J .   ? 0.67770 0.91640 0.41110 0.15460  0.16860  0.15890  950  HOH A O     
3666 O  O     . HOH J .   ? 0.54570 0.32440 0.43210 0.11600  -0.25740 -0.13960 951  HOH A O     
3667 O  O     . HOH J .   ? 0.44530 0.33210 0.34720 0.01290  -0.10320 -0.07080 952  HOH A O     
3668 O  O     . HOH J .   ? 0.73100 0.67930 0.27960 0.26540  0.12010  0.06060  953  HOH A O     
3669 O  O     . HOH J .   ? 0.68950 0.56120 0.90030 0.26630  0.06570  0.22170  954  HOH A O     
3670 O  O     . HOH J .   ? 0.70480 0.48490 0.35730 -0.02820 -0.17740 -0.10040 955  HOH A O     
3671 O  O     . HOH J .   ? 1.01589 0.56170 0.31281 -0.01620 0.01030  0.13390  956  HOH A O     
3672 O  O     . HOH J .   ? 0.59760 0.41520 0.38700 0.02160  -0.12720 0.05590  957  HOH A O     
3673 O  O     . HOH J .   ? 0.72580 0.80990 0.54900 0.13860  -0.19830 -0.03120 958  HOH A O     
3674 O  O     . HOH J .   ? 0.44550 0.31970 0.29380 -0.07210 0.07550  -0.05820 959  HOH A O     
3675 O  O     . HOH J .   ? 0.47300 0.47190 0.46150 -0.07700 0.01330  0.15290  960  HOH A O     
3676 O  O     . HOH J .   ? 0.78690 0.85730 0.42830 0.02320  -0.09090 -0.25080 961  HOH A O     
3677 O  O     . HOH J .   ? 0.52440 0.38700 0.70780 0.06760  -0.31650 0.02810  962  HOH A O     
3678 O  O     . HOH J .   ? 0.75040 0.54090 0.63200 0.12230  0.31500  0.25880  963  HOH A O     
3679 O  O     . HOH J .   ? 0.64580 0.94840 0.52220 -0.29840 0.04180  -0.30540 964  HOH A O     
3680 O  O     . HOH J .   ? 0.60910 0.71130 0.50340 0.16610  -0.01500 0.08310  965  HOH A O     
3681 O  O     . HOH J .   ? 0.59150 0.26120 0.58440 -0.07940 0.08880  -0.09150 966  HOH A O     
3682 O  O     . HOH J .   ? 0.46660 0.35890 0.75270 -0.10600 -0.08710 0.08050  967  HOH A O     
3683 O  O     . HOH J .   ? 0.59690 0.61060 0.44100 0.02080  -0.04060 0.20040  968  HOH A O     
3684 O  O     . HOH J .   ? 0.56020 0.46050 0.85770 0.12630  0.03260  0.22320  969  HOH A O     
3685 O  O     . HOH J .   ? 0.88470 0.82130 0.35360 0.46160  -0.08080 -0.03290 970  HOH A O     
3686 O  O     . HOH J .   ? 0.63380 0.76100 0.40980 -0.09670 -0.18560 0.18990  971  HOH A O     
3687 O  O     . HOH J .   ? 0.74510 0.59080 0.61480 0.38980  -0.02290 -0.05420 972  HOH A O     
3688 O  O     . HOH J .   ? 0.64610 0.38840 0.39930 0.07600  -0.08400 -0.01980 973  HOH A O     
3689 O  O     . HOH J .   ? 0.51090 0.39130 0.29150 0.03190  0.01950  -0.05640 974  HOH A O     
3690 O  O     . HOH J .   ? 0.37610 0.36480 0.31690 -0.00140 -0.01310 0.01590  975  HOH A O     
3691 O  O     . HOH J .   ? 0.70070 0.66960 0.39170 -0.00990 -0.17110 0.03950  976  HOH A O     
3692 O  O     . HOH J .   ? 0.54960 0.36880 0.42420 -0.01280 -0.01380 -0.01880 977  HOH A O     
3693 O  O     . HOH J .   ? 0.95520 0.65020 0.34510 0.32700  0.16960  0.08020  978  HOH A O     
3694 O  O     . HOH J .   ? 0.82770 0.33420 0.69570 -0.01570 0.31240  -0.00520 979  HOH A O     
3695 O  O     . HOH J .   ? 0.63140 0.40180 0.23110 0.12320  -0.05980 -0.04240 980  HOH A O     
3696 O  O     . HOH J .   ? 0.47670 0.28360 0.31670 0.00030  -0.07050 -0.08790 981  HOH A O     
3697 O  O     . HOH J .   ? 0.54050 0.34620 0.28830 -0.08310 -0.05840 -0.01480 982  HOH A O     
3698 O  O     . HOH J .   ? 0.75448 0.61509 0.32312 0.19978  -0.19998 -0.02630 983  HOH A O     
3699 O  O     . HOH J .   ? 0.67480 0.40600 0.54740 -0.14740 -0.05350 0.02370  984  HOH A O     
3700 O  O     . HOH J .   ? 0.71590 1.10230 0.60870 0.30440  0.13160  0.08800  985  HOH A O     
3701 O  O     . HOH J .   ? 0.52810 0.32590 0.30950 0.09020  -0.10940 -0.02040 986  HOH A O     
3702 O  O     . HOH J .   ? 0.69110 0.53850 0.37960 0.03570  -0.03690 -0.20460 987  HOH A O     
3703 O  O     . HOH J .   ? 0.77539 0.79139 0.39931 -0.30549 0.08569  0.14079  988  HOH A O     
3704 O  O     . HOH J .   ? 0.58490 0.59500 0.51430 0.09780  0.02420  -0.07090 989  HOH A O     
3705 O  O     . HOH J .   ? 0.77740 0.67000 0.63050 0.02450  0.05910  0.15830  990  HOH A O     
3706 O  O     . HOH J .   ? 0.79770 0.34780 0.62010 0.17480  -0.07520 -0.04450 991  HOH A O     
3707 O  O     . HOH J .   ? 0.92140 0.84000 0.34120 0.00970  -0.11560 -0.06650 992  HOH A O     
3708 O  O     . HOH J .   ? 0.51660 0.40120 0.42320 -0.04540 -0.07960 -0.18160 993  HOH A O     
3709 O  O     . HOH J .   ? 0.57460 0.77949 0.37541 0.33140  -0.15660 -0.21569 994  HOH A O     
3710 O  O     . HOH J .   ? 0.78200 0.35620 0.49610 0.21290  0.07640  -0.06600 995  HOH A O     
3711 O  O     . HOH J .   ? 0.49750 0.30360 0.35740 -0.01920 -0.18460 0.04380  996  HOH A O     
3712 O  O     . HOH J .   ? 0.59590 1.09610 0.34990 -0.08780 -0.06620 -0.07310 997  HOH A O     
3713 O  O     . HOH J .   ? 0.75650 0.30860 0.53030 0.02560  -0.19750 -0.00050 998  HOH A O     
3714 O  O     . HOH J .   ? 0.49520 0.51850 0.25090 -0.15280 0.05260  -0.04620 999  HOH A O     
3715 O  O     . HOH J .   ? 0.57620 0.83680 0.63500 0.06340  0.05660  0.08500  1000 HOH A O     
3716 O  O     . HOH J .   ? 0.49380 0.92229 0.36790 0.10610  0.10960  0.23460  1001 HOH A O     
3717 O  O     . HOH J .   ? 1.05419 0.96450 0.43781 0.06700  -0.31919 -0.00640 1002 HOH A O     
3718 O  O     . HOH J .   ? 0.85970 0.54830 0.40220 0.36680  0.22730  0.15810  1003 HOH A O     
3719 O  O     . HOH J .   ? 0.53490 1.22530 0.36100 -0.17060 0.03990  0.12560  1004 HOH A O     
3720 O  O     . HOH J .   ? 0.47940 0.40880 0.30810 0.09230  -0.01140 0.09420  1005 HOH A O     
3721 O  O     . HOH J .   ? 0.40690 0.98130 0.71360 0.06050  0.09320  0.45970  1006 HOH A O     
# 
