data_9JI6
# 
_entry.id   9JI6 
# 
_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   9JI6         pdb_00009ji6 10.2210/pdb9ji6/pdb 
WWPDB D_1300051408 ?            ?                   
# 
_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                        9JI6 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB '9JHW is the wild type complexed with diclofenac (DIF)'      9JHW unspecified 
PDB '9JHW is the wild type complexed with flufenamic Acid (FLF)' 9JI1 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'                       44991.742 1   1.14.15.- R84A ? ? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                616.487   1   ?         ?    ? ? 
3 non-polymer syn '2-[2,6-DICHLOROPHENYL)AMINO]BENZENEACETIC ACID' 296.149   1   ?         ?    ? ? 
4 non-polymer syn 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL         122.143   1   ?         ?    ? ? 
5 non-polymer syn 1,2-ETHANEDIOL                                   62.068    2   ?         ?    ? ? 
6 water       nat water                                            18.015    376 ?         ?    ? ? 
# 
_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
TSPAFEAVRESPQAFIGLDPPEHGTRRRMTISEFTVKRIKGMRPEVEEVVHGFLDEMLAAGPTADLVSQFALPVPSMVIC
RLLGVPYADHEFFQDASKRLVQSTDAQSALTARNDLAGYLDGLITQFQTEPGAGLVGALVADQLANGEIDREELISTAML
LLIAGHETTASMTSLSVITLLDHPEQYAALRADRSLVPGAVEELLRYLAIADIAGGRVATADIEVEGQLIRAGEGVIVVN
SIANRDGTVYEDPDALDIHRSARHHLAFGFGVHQCLGQNLARLELEVILNALMDRVPTLRLAVPVEQLVLRPGTTIQGVN
ELPVTWHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTDTATTPQTTDAPAFPSNRSCPYQLPDGYAQLRDTPGPLHRVTLYDGRQAWVVTKHEAARKLLGDPRLSSNRTDDNFPA
TSPAFEAVRESPQAFIGLDPPEHGTRRRMTISEFTVKRIKGMRPEVEEVVHGFLDEMLAAGPTADLVSQFALPVPSMVIC
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-[2,6-DICHLOROPHENYL)AMINO]BENZENEACETIC ACID' DIF 
4 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL         TRS 
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  ALA 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 
DIF non-polymer         . '2-[2,6-DICHLOROPHENYL)AMINO]BENZENEACETIC ACID' DICLOFENAC        'C14 H11 Cl2 N O2' 296.149 
EDO non-polymer         . 1,2-ETHANEDIOL                                   'ETHYLENE GLYCOL' 'C2 H6 O2'         62.068  
GLN 'L-peptide linking' y GLUTAMINE                                        ?                 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                  ?                 'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                                          ?                 'C2 H5 N O2'       75.067  
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   2   THR THR A . n 
A 1 3   ASP 3   3   3   ASP ASP 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  ALA 84  84  84  ALA ALA 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 409 409 409 HIS HIS 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 
# 
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 DIF 1   502 501 DIF DIF A . 
D 4 TRS 1   503 3   TRS TRS A . 
E 5 EDO 1   504 7   EDO EDO A . 
F 5 EDO 1   505 10  EDO EDO A . 
G 6 HOH 1   601 268 HOH HOH A . 
G 6 HOH 2   602 23  HOH HOH A . 
G 6 HOH 3   603 269 HOH HOH A . 
G 6 HOH 4   604 183 HOH HOH A . 
G 6 HOH 5   605 16  HOH HOH A . 
G 6 HOH 6   606 345 HOH HOH A . 
G 6 HOH 7   607 118 HOH HOH A . 
G 6 HOH 8   608 380 HOH HOH A . 
G 6 HOH 9   609 138 HOH HOH A . 
G 6 HOH 10  610 190 HOH HOH A . 
G 6 HOH 11  611 295 HOH HOH A . 
G 6 HOH 12  612 298 HOH HOH A . 
G 6 HOH 13  613 372 HOH HOH A . 
G 6 HOH 14  614 209 HOH HOH A . 
G 6 HOH 15  615 103 HOH HOH A . 
G 6 HOH 16  616 265 HOH HOH A . 
G 6 HOH 17  617 129 HOH HOH A . 
G 6 HOH 18  618 122 HOH HOH A . 
G 6 HOH 19  619 136 HOH HOH A . 
G 6 HOH 20  620 318 HOH HOH A . 
G 6 HOH 21  621 381 HOH HOH A . 
G 6 HOH 22  622 335 HOH HOH A . 
G 6 HOH 23  623 343 HOH HOH A . 
G 6 HOH 24  624 7   HOH HOH A . 
G 6 HOH 25  625 15  HOH HOH A . 
G 6 HOH 26  626 262 HOH HOH A . 
G 6 HOH 27  627 4   HOH HOH A . 
G 6 HOH 28  628 336 HOH HOH A . 
G 6 HOH 29  629 293 HOH HOH A . 
G 6 HOH 30  630 139 HOH HOH A . 
G 6 HOH 31  631 131 HOH HOH A . 
G 6 HOH 32  632 373 HOH HOH A . 
G 6 HOH 33  633 217 HOH HOH A . 
G 6 HOH 34  634 206 HOH HOH A . 
G 6 HOH 35  635 189 HOH HOH A . 
G 6 HOH 36  636 241 HOH HOH A . 
G 6 HOH 37  637 289 HOH HOH A . 
G 6 HOH 38  638 140 HOH HOH A . 
G 6 HOH 39  639 89  HOH HOH A . 
G 6 HOH 40  640 248 HOH HOH A . 
G 6 HOH 41  641 195 HOH HOH A . 
G 6 HOH 42  642 409 HOH HOH A . 
G 6 HOH 43  643 18  HOH HOH A . 
G 6 HOH 44  644 85  HOH HOH A . 
G 6 HOH 45  645 234 HOH HOH A . 
G 6 HOH 46  646 39  HOH HOH A . 
G 6 HOH 47  647 222 HOH HOH A . 
G 6 HOH 48  648 384 HOH HOH A . 
G 6 HOH 49  649 20  HOH HOH A . 
G 6 HOH 50  650 387 HOH HOH A . 
G 6 HOH 51  651 369 HOH HOH A . 
G 6 HOH 52  652 170 HOH HOH A . 
G 6 HOH 53  653 342 HOH HOH A . 
G 6 HOH 54  654 197 HOH HOH A . 
G 6 HOH 55  655 401 HOH HOH A . 
G 6 HOH 56  656 10  HOH HOH A . 
G 6 HOH 57  657 40  HOH HOH A . 
G 6 HOH 58  658 54  HOH HOH A . 
G 6 HOH 59  659 187 HOH HOH A . 
G 6 HOH 60  660 30  HOH HOH A . 
G 6 HOH 61  661 242 HOH HOH A . 
G 6 HOH 62  662 337 HOH HOH A . 
G 6 HOH 63  663 194 HOH HOH A . 
G 6 HOH 64  664 414 HOH HOH A . 
G 6 HOH 65  665 303 HOH HOH A . 
G 6 HOH 66  666 232 HOH HOH A . 
G 6 HOH 67  667 148 HOH HOH A . 
G 6 HOH 68  668 80  HOH HOH A . 
G 6 HOH 69  669 256 HOH HOH A . 
G 6 HOH 70  670 79  HOH HOH A . 
G 6 HOH 71  671 83  HOH HOH A . 
G 6 HOH 72  672 333 HOH HOH A . 
G 6 HOH 73  673 71  HOH HOH A . 
G 6 HOH 74  674 226 HOH HOH A . 
G 6 HOH 75  675 21  HOH HOH A . 
G 6 HOH 76  676 163 HOH HOH A . 
G 6 HOH 77  677 11  HOH HOH A . 
G 6 HOH 78  678 200 HOH HOH A . 
G 6 HOH 79  679 130 HOH HOH A . 
G 6 HOH 80  680 219 HOH HOH A . 
G 6 HOH 81  681 235 HOH HOH A . 
G 6 HOH 82  682 142 HOH HOH A . 
G 6 HOH 83  683 116 HOH HOH A . 
G 6 HOH 84  684 91  HOH HOH A . 
G 6 HOH 85  685 119 HOH HOH A . 
G 6 HOH 86  686 162 HOH HOH A . 
G 6 HOH 87  687 114 HOH HOH A . 
G 6 HOH 88  688 159 HOH HOH A . 
G 6 HOH 89  689 302 HOH HOH A . 
G 6 HOH 90  690 198 HOH HOH A . 
G 6 HOH 91  691 9   HOH HOH A . 
G 6 HOH 92  692 26  HOH HOH A . 
G 6 HOH 93  693 141 HOH HOH A . 
G 6 HOH 94  694 25  HOH HOH A . 
G 6 HOH 95  695 310 HOH HOH A . 
G 6 HOH 96  696 161 HOH HOH A . 
G 6 HOH 97  697 29  HOH HOH A . 
G 6 HOH 98  698 367 HOH HOH A . 
G 6 HOH 99  699 236 HOH HOH A . 
G 6 HOH 100 700 98  HOH HOH A . 
G 6 HOH 101 701 254 HOH HOH A . 
G 6 HOH 102 702 132 HOH HOH A . 
G 6 HOH 103 703 329 HOH HOH A . 
G 6 HOH 104 704 112 HOH HOH A . 
G 6 HOH 105 705 28  HOH HOH A . 
G 6 HOH 106 706 319 HOH HOH A . 
G 6 HOH 107 707 123 HOH HOH A . 
G 6 HOH 108 708 224 HOH HOH A . 
G 6 HOH 109 709 41  HOH HOH A . 
G 6 HOH 110 710 291 HOH HOH A . 
G 6 HOH 111 711 227 HOH HOH A . 
G 6 HOH 112 712 215 HOH HOH A . 
G 6 HOH 113 713 339 HOH HOH A . 
G 6 HOH 114 714 2   HOH HOH A . 
G 6 HOH 115 715 168 HOH HOH A . 
G 6 HOH 116 716 5   HOH HOH A . 
G 6 HOH 117 717 386 HOH HOH A . 
G 6 HOH 118 718 19  HOH HOH A . 
G 6 HOH 119 719 167 HOH HOH A . 
G 6 HOH 120 720 22  HOH HOH A . 
G 6 HOH 121 721 17  HOH HOH A . 
G 6 HOH 122 722 92  HOH HOH A . 
G 6 HOH 123 723 211 HOH HOH A . 
G 6 HOH 124 724 375 HOH HOH A . 
G 6 HOH 125 725 1   HOH HOH A . 
G 6 HOH 126 726 12  HOH HOH A . 
G 6 HOH 127 727 184 HOH HOH A . 
G 6 HOH 128 728 292 HOH HOH A . 
G 6 HOH 129 729 150 HOH HOH A . 
G 6 HOH 130 730 106 HOH HOH A . 
G 6 HOH 131 731 301 HOH HOH A . 
G 6 HOH 132 732 286 HOH HOH A . 
G 6 HOH 133 733 27  HOH HOH A . 
G 6 HOH 134 734 307 HOH HOH A . 
G 6 HOH 135 735 216 HOH HOH A . 
G 6 HOH 136 736 73  HOH HOH A . 
G 6 HOH 137 737 252 HOH HOH A . 
G 6 HOH 138 738 38  HOH HOH A . 
G 6 HOH 139 739 204 HOH HOH A . 
G 6 HOH 140 740 374 HOH HOH A . 
G 6 HOH 141 741 81  HOH HOH A . 
G 6 HOH 142 742 82  HOH HOH A . 
G 6 HOH 143 743 178 HOH HOH A . 
G 6 HOH 144 744 406 HOH HOH A . 
G 6 HOH 145 745 109 HOH HOH A . 
G 6 HOH 146 746 259 HOH HOH A . 
G 6 HOH 147 747 55  HOH HOH A . 
G 6 HOH 148 748 246 HOH HOH A . 
G 6 HOH 149 749 382 HOH HOH A . 
G 6 HOH 150 750 220 HOH HOH A . 
G 6 HOH 151 751 14  HOH HOH A . 
G 6 HOH 152 752 156 HOH HOH A . 
G 6 HOH 153 753 152 HOH HOH A . 
G 6 HOH 154 754 233 HOH HOH A . 
G 6 HOH 155 755 285 HOH HOH A . 
G 6 HOH 156 756 177 HOH HOH A . 
G 6 HOH 157 757 378 HOH HOH A . 
G 6 HOH 158 758 74  HOH HOH A . 
G 6 HOH 159 759 317 HOH HOH A . 
G 6 HOH 160 760 237 HOH HOH A . 
G 6 HOH 161 761 53  HOH HOH A . 
G 6 HOH 162 762 223 HOH HOH A . 
G 6 HOH 163 763 205 HOH HOH A . 
G 6 HOH 164 764 70  HOH HOH A . 
G 6 HOH 165 765 124 HOH HOH A . 
G 6 HOH 166 766 102 HOH HOH A . 
G 6 HOH 167 767 37  HOH HOH A . 
G 6 HOH 168 768 69  HOH HOH A . 
G 6 HOH 169 769 36  HOH HOH A . 
G 6 HOH 170 770 8   HOH HOH A . 
G 6 HOH 171 771 287 HOH HOH A . 
G 6 HOH 172 772 33  HOH HOH A . 
G 6 HOH 173 773 210 HOH HOH A . 
G 6 HOH 174 774 87  HOH HOH A . 
G 6 HOH 175 775 44  HOH HOH A . 
G 6 HOH 176 776 390 HOH HOH A . 
G 6 HOH 177 777 34  HOH HOH A . 
G 6 HOH 178 778 104 HOH HOH A . 
G 6 HOH 179 779 31  HOH HOH A . 
G 6 HOH 180 780 72  HOH HOH A . 
G 6 HOH 181 781 169 HOH HOH A . 
G 6 HOH 182 782 127 HOH HOH A . 
G 6 HOH 183 783 86  HOH HOH A . 
G 6 HOH 184 784 278 HOH HOH A . 
G 6 HOH 185 785 3   HOH HOH A . 
G 6 HOH 186 786 294 HOH HOH A . 
G 6 HOH 187 787 245 HOH HOH A . 
G 6 HOH 188 788 370 HOH HOH A . 
G 6 HOH 189 789 90  HOH HOH A . 
G 6 HOH 190 790 43  HOH HOH A . 
G 6 HOH 191 791 257 HOH HOH A . 
G 6 HOH 192 792 208 HOH HOH A . 
G 6 HOH 193 793 230 HOH HOH A . 
G 6 HOH 194 794 357 HOH HOH A . 
G 6 HOH 195 795 415 HOH HOH A . 
G 6 HOH 196 796 121 HOH HOH A . 
G 6 HOH 197 797 338 HOH HOH A . 
G 6 HOH 198 798 67  HOH HOH A . 
G 6 HOH 199 799 166 HOH HOH A . 
G 6 HOH 200 800 13  HOH HOH A . 
G 6 HOH 201 801 244 HOH HOH A . 
G 6 HOH 202 802 99  HOH HOH A . 
G 6 HOH 203 803 377 HOH HOH A . 
G 6 HOH 204 804 270 HOH HOH A . 
G 6 HOH 205 805 207 HOH HOH A . 
G 6 HOH 206 806 133 HOH HOH A . 
G 6 HOH 207 807 393 HOH HOH A . 
G 6 HOH 208 808 105 HOH HOH A . 
G 6 HOH 209 809 45  HOH HOH A . 
G 6 HOH 210 810 315 HOH HOH A . 
G 6 HOH 211 811 296 HOH HOH A . 
G 6 HOH 212 812 407 HOH HOH A . 
G 6 HOH 213 813 158 HOH HOH A . 
G 6 HOH 214 814 403 HOH HOH A . 
G 6 HOH 215 815 273 HOH HOH A . 
G 6 HOH 216 816 264 HOH HOH A . 
G 6 HOH 217 817 143 HOH HOH A . 
G 6 HOH 218 818 398 HOH HOH A . 
G 6 HOH 219 819 221 HOH HOH A . 
G 6 HOH 220 820 260 HOH HOH A . 
G 6 HOH 221 821 368 HOH HOH A . 
G 6 HOH 222 822 88  HOH HOH A . 
G 6 HOH 223 823 266 HOH HOH A . 
G 6 HOH 224 824 153 HOH HOH A . 
G 6 HOH 225 825 164 HOH HOH A . 
G 6 HOH 226 826 392 HOH HOH A . 
G 6 HOH 227 827 413 HOH HOH A . 
G 6 HOH 228 828 145 HOH HOH A . 
G 6 HOH 229 829 305 HOH HOH A . 
G 6 HOH 230 830 243 HOH HOH A . 
G 6 HOH 231 831 165 HOH HOH A . 
G 6 HOH 232 832 229 HOH HOH A . 
G 6 HOH 233 833 258 HOH HOH A . 
G 6 HOH 234 834 225 HOH HOH A . 
G 6 HOH 235 835 348 HOH HOH A . 
G 6 HOH 236 836 388 HOH HOH A . 
G 6 HOH 237 837 394 HOH HOH A . 
G 6 HOH 238 838 364 HOH HOH A . 
G 6 HOH 239 839 283 HOH HOH A . 
G 6 HOH 240 840 115 HOH HOH A . 
G 6 HOH 241 841 297 HOH HOH A . 
G 6 HOH 242 842 344 HOH HOH A . 
G 6 HOH 243 843 179 HOH HOH A . 
G 6 HOH 244 844 361 HOH HOH A . 
G 6 HOH 245 845 400 HOH HOH A . 
G 6 HOH 246 846 321 HOH HOH A . 
G 6 HOH 247 847 240 HOH HOH A . 
G 6 HOH 248 848 231 HOH HOH A . 
G 6 HOH 249 849 322 HOH HOH A . 
G 6 HOH 250 850 325 HOH HOH A . 
G 6 HOH 251 851 383 HOH HOH A . 
G 6 HOH 252 852 288 HOH HOH A . 
G 6 HOH 253 853 261 HOH HOH A . 
G 6 HOH 254 854 255 HOH HOH A . 
G 6 HOH 255 855 371 HOH HOH A . 
G 6 HOH 256 856 341 HOH HOH A . 
G 6 HOH 257 857 186 HOH HOH A . 
G 6 HOH 258 858 199 HOH HOH A . 
G 6 HOH 259 859 351 HOH HOH A . 
G 6 HOH 260 860 408 HOH HOH A . 
G 6 HOH 261 861 107 HOH HOH A . 
G 6 HOH 262 862 78  HOH HOH A . 
G 6 HOH 263 863 144 HOH HOH A . 
G 6 HOH 264 864 75  HOH HOH A . 
G 6 HOH 265 865 412 HOH HOH A . 
G 6 HOH 266 866 376 HOH HOH A . 
G 6 HOH 267 867 330 HOH HOH A . 
G 6 HOH 268 868 201 HOH HOH A . 
G 6 HOH 269 869 316 HOH HOH A . 
G 6 HOH 270 870 276 HOH HOH A . 
G 6 HOH 271 871 32  HOH HOH A . 
G 6 HOH 272 872 397 HOH HOH A . 
G 6 HOH 273 873 379 HOH HOH A . 
G 6 HOH 274 874 308 HOH HOH A . 
G 6 HOH 275 875 385 HOH HOH A . 
G 6 HOH 276 876 362 HOH HOH A . 
G 6 HOH 277 877 277 HOH HOH A . 
G 6 HOH 278 878 391 HOH HOH A . 
G 6 HOH 279 879 180 HOH HOH A . 
G 6 HOH 280 880 249 HOH HOH A . 
G 6 HOH 281 881 354 HOH HOH A . 
G 6 HOH 282 882 399 HOH HOH A . 
G 6 HOH 283 883 6   HOH HOH A . 
G 6 HOH 284 884 356 HOH HOH A . 
G 6 HOH 285 885 389 HOH HOH A . 
G 6 HOH 286 886 328 HOH HOH A . 
G 6 HOH 287 887 402 HOH HOH A . 
G 6 HOH 288 888 311 HOH HOH A . 
G 6 HOH 289 889 331 HOH HOH A . 
G 6 HOH 290 890 366 HOH HOH A . 
G 6 HOH 291 891 101 HOH HOH A . 
G 6 HOH 292 892 212 HOH HOH A . 
G 6 HOH 293 893 160 HOH HOH A . 
G 6 HOH 294 894 313 HOH HOH A . 
G 6 HOH 295 895 76  HOH HOH A . 
G 6 HOH 296 896 275 HOH HOH A . 
G 6 HOH 297 897 355 HOH HOH A . 
G 6 HOH 298 898 213 HOH HOH A . 
G 6 HOH 299 899 100 HOH HOH A . 
G 6 HOH 300 900 96  HOH HOH A . 
G 6 HOH 301 901 52  HOH HOH A . 
G 6 HOH 302 902 410 HOH HOH A . 
G 6 HOH 303 903 306 HOH HOH A . 
G 6 HOH 304 904 93  HOH HOH A . 
G 6 HOH 305 905 290 HOH HOH A . 
G 6 HOH 306 906 340 HOH HOH A . 
G 6 HOH 307 907 110 HOH HOH A . 
G 6 HOH 308 908 77  HOH HOH A . 
G 6 HOH 309 909 323 HOH HOH A . 
G 6 HOH 310 910 251 HOH HOH A . 
G 6 HOH 311 911 284 HOH HOH A . 
G 6 HOH 312 912 352 HOH HOH A . 
G 6 HOH 313 913 111 HOH HOH A . 
G 6 HOH 314 914 324 HOH HOH A . 
G 6 HOH 315 915 134 HOH HOH A . 
G 6 HOH 316 916 42  HOH HOH A . 
G 6 HOH 317 917 272 HOH HOH A . 
G 6 HOH 318 918 404 HOH HOH A . 
G 6 HOH 319 919 49  HOH HOH A . 
G 6 HOH 320 920 176 HOH HOH A . 
G 6 HOH 321 921 250 HOH HOH A . 
G 6 HOH 322 922 360 HOH HOH A . 
G 6 HOH 323 923 411 HOH HOH A . 
G 6 HOH 324 924 395 HOH HOH A . 
G 6 HOH 325 925 155 HOH HOH A . 
G 6 HOH 326 926 126 HOH HOH A . 
G 6 HOH 327 927 228 HOH HOH A . 
G 6 HOH 328 928 267 HOH HOH A . 
G 6 HOH 329 929 314 HOH HOH A . 
G 6 HOH 330 930 218 HOH HOH A . 
G 6 HOH 331 931 281 HOH HOH A . 
G 6 HOH 332 932 50  HOH HOH A . 
G 6 HOH 333 933 304 HOH HOH A . 
G 6 HOH 334 934 280 HOH HOH A . 
G 6 HOH 335 935 214 HOH HOH A . 
G 6 HOH 336 936 191 HOH HOH A . 
G 6 HOH 337 937 358 HOH HOH A . 
G 6 HOH 338 938 57  HOH HOH A . 
G 6 HOH 339 939 125 HOH HOH A . 
G 6 HOH 340 940 365 HOH HOH A . 
G 6 HOH 341 941 149 HOH HOH A . 
G 6 HOH 342 942 171 HOH HOH A . 
G 6 HOH 343 943 238 HOH HOH A . 
G 6 HOH 344 944 188 HOH HOH A . 
G 6 HOH 345 945 97  HOH HOH A . 
G 6 HOH 346 946 181 HOH HOH A . 
G 6 HOH 347 947 203 HOH HOH A . 
G 6 HOH 348 948 353 HOH HOH A . 
G 6 HOH 349 949 274 HOH HOH A . 
G 6 HOH 350 950 94  HOH HOH A . 
G 6 HOH 351 951 146 HOH HOH A . 
G 6 HOH 352 952 405 HOH HOH A . 
G 6 HOH 353 953 282 HOH HOH A . 
G 6 HOH 354 954 279 HOH HOH A . 
G 6 HOH 355 955 347 HOH HOH A . 
G 6 HOH 356 956 253 HOH HOH A . 
G 6 HOH 357 957 299 HOH HOH A . 
G 6 HOH 358 958 113 HOH HOH A . 
G 6 HOH 359 959 202 HOH HOH A . 
G 6 HOH 360 960 56  HOH HOH A . 
G 6 HOH 361 961 271 HOH HOH A . 
G 6 HOH 362 962 309 HOH HOH A . 
G 6 HOH 363 963 135 HOH HOH A . 
G 6 HOH 364 964 396 HOH HOH A . 
G 6 HOH 365 965 108 HOH HOH A . 
G 6 HOH 366 966 157 HOH HOH A . 
G 6 HOH 367 967 359 HOH HOH A . 
G 6 HOH 368 968 147 HOH HOH A . 
G 6 HOH 369 969 58  HOH HOH A . 
G 6 HOH 370 970 65  HOH HOH A . 
G 6 HOH 371 971 66  HOH HOH A . 
G 6 HOH 372 972 59  HOH HOH A . 
G 6 HOH 373 973 60  HOH HOH A . 
G 6 HOH 374 974 61  HOH HOH A . 
G 6 HOH 375 975 62  HOH HOH A . 
G 6 HOH 376 976 63  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                     9JI6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     52.452 
_cell.length_a_esd                 ? 
_cell.length_b                     53.319 
_cell.length_b_esd                 ? 
_cell.length_c                     138.800 
_cell.length_c_esd                 ? 
_cell.volume                       388180.328 
_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                         9JI6 
_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                   9JI6 
_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             2.19 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.98 
_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              ? 
_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)

Diclofenac (DIF) was introduced by three times soaking of the crystal to the mother liqure containing 11 mM DIF.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            297 
# 
_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         2022-05-20 
_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                          21.55 
_reflns.entry_id                                       9JI6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.55 
_reflns.d_resolution_low                               50.0 
_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                                     57734 
_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                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.54 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.07 
_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                                0.067 
_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                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.061 
_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                                    1.55 
_reflns_shell.d_res_low                                     1.64 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.65 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             9135 
_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                               5.60 
_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                               0.699 
_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                                  0.832 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.1 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.634 
_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                               31.50 
_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                                 9JI6 
_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                            1.55 
_refine.ls_d_res_low                             36.10 
_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                     57729 
_refine.ls_number_reflns_R_free                  2887 
_refine.ls_number_reflns_R_work                  54842 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.77 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1450 
_refine.ls_R_factor_R_free                       0.2058 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1418 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       '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                 20.8489 
_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                            0.1784 
_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                       1.55 
_refine_hist.d_res_low                        36.10 
_refine_hist.number_atoms_solvent             376 
_refine_hist.number_atoms_total               3579 
_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        3125 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         78 
_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' ? 0.0052  ? 3352 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.7996  ? 4599 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0490  ? 520  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0076  ? 610  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 15.1167 ? 1248 ? 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' 1.55 1.57  . . 130 2481 97.17  . . . . 0.2215 . . . . . . . . . . . 0.3005 
'X-RAY DIFFRACTION' 1.57 1.60  . . 136 2585 99.96  . . . . 0.1892 . . . . . . . . . . . 0.2670 
'X-RAY DIFFRACTION' 1.60 1.63  . . 137 2598 100.00 . . . . 0.1726 . . . . . . . . . . . 0.2519 
'X-RAY DIFFRACTION' 1.63 1.66  . . 134 2555 99.89  . . . . 0.1665 . . . . . . . . . . . 0.2539 
'X-RAY DIFFRACTION' 1.66 1.69  . . 137 2600 99.89  . . . . 0.1619 . . . . . . . . . . . 0.2418 
'X-RAY DIFFRACTION' 1.69 1.73  . . 135 2551 99.93  . . . . 0.1631 . . . . . . . . . . . 0.2426 
'X-RAY DIFFRACTION' 1.73 1.77  . . 136 2599 99.93  . . . . 0.1603 . . . . . . . . . . . 0.2555 
'X-RAY DIFFRACTION' 1.77 1.81  . . 137 2591 99.96  . . . . 0.1604 . . . . . . . . . . . 0.2358 
'X-RAY DIFFRACTION' 1.81 1.86  . . 136 2588 99.96  . . . . 0.1505 . . . . . . . . . . . 0.2336 
'X-RAY DIFFRACTION' 1.86 1.92  . . 137 2603 99.96  . . . . 0.1400 . . . . . . . . . . . 0.2127 
'X-RAY DIFFRACTION' 1.92 1.98  . . 137 2607 100.00 . . . . 0.1352 . . . . . . . . . . . 0.2281 
'X-RAY DIFFRACTION' 1.98 2.05  . . 136 2583 99.93  . . . . 0.1385 . . . . . . . . . . . 0.1909 
'X-RAY DIFFRACTION' 2.05 2.13  . . 137 2597 99.49  . . . . 0.1346 . . . . . . . . . . . 0.2128 
'X-RAY DIFFRACTION' 2.13 2.23  . . 137 2609 99.93  . . . . 0.1379 . . . . . . . . . . . 0.2148 
'X-RAY DIFFRACTION' 2.23 2.35  . . 138 2609 99.96  . . . . 0.1324 . . . . . . . . . . . 0.2203 
'X-RAY DIFFRACTION' 2.35 2.49  . . 139 2637 99.89  . . . . 0.1356 . . . . . . . . . . . 0.2122 
'X-RAY DIFFRACTION' 2.49 2.69  . . 138 2621 99.93  . . . . 0.1461 . . . . . . . . . . . 0.2072 
'X-RAY DIFFRACTION' 2.69 2.96  . . 140 2660 100.00 . . . . 0.1485 . . . . . . . . . . . 0.2303 
'X-RAY DIFFRACTION' 2.96 3.38  . . 140 2659 99.96  . . . . 0.1428 . . . . . . . . . . . 0.1937 
'X-RAY DIFFRACTION' 3.38 4.26  . . 141 2683 99.82  . . . . 0.1248 . . . . . . . . . . . 0.1564 
'X-RAY DIFFRACTION' 4.26 36.10 . . 149 2826 99.70  . . . . 0.1406 . . . . . . . . . . . 0.2007 
# 
_struct.entry_id                     9JI6 
_struct.title                        'CYP105A1 R84A complexed with diclofenac (DIF)' 
_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        9JI6 
_struct_keywords.text            
'P450, CYP105A1, nonsteroidal anti-inflammatory drugs, diclofenac, flufenamic acid, R84A, 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 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              9JI6 
_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 9JI6 ALA A 84  ? UNP P18326 ARG 84  'engineered mutation' 84  1 
1 9JI6 GLN A 308 ? UNP P18326 HIS 308 variant               308 2 
1 9JI6 HIS A 407 ? UNP P18326 ?   ?   'expression tag'      407 3 
1 9JI6 HIS A 408 ? UNP P18326 ?   ?   'expression tag'      408 4 
1 9JI6 HIS A 409 ? UNP P18326 ?   ?   'expression tag'      409 5 
1 9JI6 HIS A 410 ? UNP P18326 ?   ?   'expression tag'      410 6 
1 9JI6 HIS A 411 ? UNP P18326 ?   ?   'expression tag'      411 7 
1 9JI6 HIS A 412 ? UNP P18326 ?   ?   'expression tag'      412 8 
# 
_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 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1190  ? 
1 MORE         -24   ? 
1 'SSA (A^2)'  17650 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                '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]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 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 SER A 82  ? ALA A 84  ? SER A 82  ALA A 84  5 ? 3  
HELX_P HELX_P4  AA4 PHE A 85  ? SER A 91  ? PHE A 85  SER A 91  1 ? 7  
HELX_P HELX_P5  AA5 ALA A 94  ? LEU A 98  ? ALA A 94  LEU A 98  5 ? 5  
HELX_P HELX_P6  AA6 PRO A 101 ? ARG A 108 ? PRO A 101 ARG A 108 1 ? 8  
HELX_P HELX_P7  AA7 MET A 109 ? PHE A 114 ? MET A 109 PHE A 114 5 ? 6  
HELX_P HELX_P8  AA8 THR A 115 ? MET A 122 ? THR A 115 MET A 122 1 ? 8  
HELX_P HELX_P9  AA9 MET A 122 ? GLY A 141 ? MET A 122 GLY A 141 1 ? 20 
HELX_P HELX_P10 AB1 LEU A 146 ? PHE A 150 ? LEU A 146 PHE A 150 1 ? 5  
HELX_P HELX_P11 AB2 LEU A 152 ? GLY A 164 ? LEU A 152 GLY A 164 1 ? 13 
HELX_P HELX_P12 AB3 PRO A 166 ? ALA A 168 ? PRO A 166 ALA A 168 5 ? 3  
HELX_P HELX_P13 AB4 ASP A 169 ? SER A 183 ? ASP A 169 SER A 183 1 ? 15 
HELX_P HELX_P14 AB5 ASP A 185 ? GLU A 210 ? ASP A 185 GLU A 210 1 ? 26 
HELX_P HELX_P15 AB6 ALA A 213 ? ASP A 222 ? ALA A 213 ASP A 222 1 ? 10 
HELX_P HELX_P16 AB7 ASP A 230 ? ASP A 262 ? ASP A 230 ASP A 262 1 ? 33 
HELX_P HELX_P17 AB8 HIS A 263 ? ASP A 273 ? HIS A 263 ASP A 273 1 ? 11 
HELX_P HELX_P18 AB9 LEU A 276 ? ALA A 289 ? LEU A 276 ALA A 289 1 ? 14 
HELX_P HELX_P19 AC1 ALA A 291 ? ALA A 294 ? ALA A 291 ALA A 294 5 ? 4  
HELX_P HELX_P20 AC2 VAL A 319 ? ASN A 324 ? VAL A 319 ASN A 324 1 ? 6  
HELX_P HELX_P21 AC3 GLY A 357 ? VAL A 376 ? GLY A 357 VAL A 376 1 ? 20 
HELX_P HELX_P22 AC4 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               2.315 
_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_555 104.1 ? 
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 91.7  ? 
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 89.6  ? 
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 86.9  ? 
5  NA ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 NC ? B HEM . ? A HEM 501 ? 1_555 169.1 ? 
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 99.7  ? 
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 88.5  ? 
9  NB ? B HEM .   ? A HEM 501 ? 1_555 FE ? B HEM . ? A HEM 501 ? 1_555 ND ? B HEM . ? A HEM 501 ? 1_555 168.6 ? 
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 -2.07 
2 PRO 100 A . ? PRO 100 A PRO 101 A ? PRO 101 A 1 4.03  
# 
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 HIS A 41  ? N HIS A 41  O VAL A 53  ? O VAL A 53  
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                   9JI6 
_pdbx_entry_details.has_ligand_of_interest     N 
_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 ? ? -149.28 -54.38 
2 1 ASP A 222 ? ? -109.50 -80.58 
3 1 ALA A 289 ? ? 24.83   73.12  
4 1 ALA A 291 ? ? -117.80 52.04  
5 1 CYS A 355 ? ? -39.47  119.31 
# 
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 966 ? 5.94  . 
2  1 O ? A HOH 967 ? 5.97  . 
3  1 O ? A HOH 968 ? 6.30  . 
4  1 O ? A HOH 969 ? 6.37  . 
5  1 O ? A HOH 970 ? 8.73  . 
6  1 O ? A HOH 971 ? 10.24 . 
7  1 O ? A HOH 972 ? 12.65 . 
8  1 O ? A HOH 973 ? 13.39 . 
9  1 O ? A HOH 974 ? 17.07 . 
10 1 O ? A HOH 975 ? 18.59 . 
11 1 O ? A HOH 976 ? 18.62 . 
# 
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 HIS 410 ? A HIS 410 
3 1 Y 1 A HIS 411 ? A HIS 411 
4 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  
DIF C1   C  Y N 88  
DIF C2   C  Y N 89  
DIF CL2  CL N N 90  
DIF C3   C  Y N 91  
DIF C4   C  Y N 92  
DIF CL4  CL N N 93  
DIF C5   C  Y N 94  
DIF C6   C  Y N 95  
DIF N1   N  N N 96  
DIF C7   C  Y N 97  
DIF C8   C  Y N 98  
DIF C9   C  Y N 99  
DIF C10  C  Y N 100 
DIF C11  C  Y N 101 
DIF C12  C  Y N 102 
DIF C13  C  N N 103 
DIF C14  C  N N 104 
DIF O1   O  N N 105 
DIF O2   O  N N 106 
DIF H1   H  N N 107 
DIF H5   H  N N 108 
DIF H6   H  N N 109 
DIF HN1  H  N N 110 
DIF H9   H  N N 111 
DIF H10  H  N N 112 
DIF H11  H  N N 113 
DIF H12  H  N N 114 
DIF H131 H  N N 115 
DIF H132 H  N N 116 
DIF HO1  H  N N 117 
EDO C1   C  N N 118 
EDO O1   O  N N 119 
EDO C2   C  N N 120 
EDO O2   O  N N 121 
EDO H11  H  N N 122 
EDO H12  H  N N 123 
EDO HO1  H  N N 124 
EDO H21  H  N N 125 
EDO H22  H  N N 126 
EDO HO2  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  
DIF C1  C2   doub Y N 83  
DIF C1  C6   sing Y N 84  
DIF C1  H1   sing N N 85  
DIF C2  CL2  sing N N 86  
DIF C2  C3   sing Y N 87  
DIF C3  C4   doub Y N 88  
DIF C3  N1   sing N N 89  
DIF C4  CL4  sing N N 90  
DIF C4  C5   sing Y N 91  
DIF C5  C6   doub Y N 92  
DIF C5  H5   sing N N 93  
DIF C6  H6   sing N N 94  
DIF N1  C8   sing N N 95  
DIF N1  HN1  sing N N 96  
DIF C7  C8   doub Y N 97  
DIF C7  C12  sing Y N 98  
DIF C7  C13  sing N N 99  
DIF C8  C9   sing Y N 100 
DIF C9  C10  doub Y N 101 
DIF C9  H9   sing N N 102 
DIF C10 C11  sing Y N 103 
DIF C10 H10  sing N N 104 
DIF C11 C12  doub Y N 105 
DIF C11 H11  sing N N 106 
DIF C12 H12  sing N N 107 
DIF C13 C14  sing N N 108 
DIF C13 H131 sing N N 109 
DIF C13 H132 sing N N 110 
DIF C14 O1   sing N N 111 
DIF C14 O2   doub N N 112 
DIF O1  HO1  sing N N 113 
EDO C1  O1   sing N N 114 
EDO C1  C2   sing N N 115 
EDO C1  H11  sing N N 116 
EDO C1  H12  sing N N 117 
EDO O1  HO1  sing N N 118 
EDO C2  O2   sing N N 119 
EDO C2  H21  sing N N 120 
EDO C2  H22  sing N N 121 
EDO O2  HO2  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                    9JI6 
_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]   0.019065 
_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]   0.018755 
_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]   0.007205 
_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.
;
? 
CL ? ? 9.50761  7.44341 ? ? 1.04373  23.83732 ? ? 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 2   ? -16.67144 -28.00748 33.49681  1.000 75.58818 ? 2   THR A N   1 
ATOM   2    C  CA  . THR A 1 2   ? -15.84189 -27.91750 32.30008  1.000 76.61105 ? 2   THR A CA  1 
ATOM   3    C  C   . THR A 1 2   ? -14.36806 -28.15960 32.63374  1.000 80.88698 ? 2   THR A C   1 
ATOM   4    O  O   . THR A 1 2   ? -13.81796 -27.54097 33.54512  1.000 83.59034 ? 2   THR A O   1 
ATOM   5    C  CB  . THR A 1 2   ? -15.98900 -26.54236 31.61024  1.000 72.22367 ? 2   THR A CB  1 
ATOM   6    O  OG1 . THR A 1 2   ? -17.37695 -26.24744 31.41012  1.000 70.95040 ? 2   THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 2   ? -15.28397 -26.54370 30.26315  1.000 70.54961 ? 2   THR A CG2 1 
ATOM   8    N  N   . ASP A 1 3   ? -13.73962 -29.06558 31.88817  1.000 80.64592 ? 3   ASP A N   1 
ATOM   9    C  CA  . ASP A 1 3   ? -12.33764 -29.39581 32.09840  1.000 79.33903 ? 3   ASP A CA  1 
ATOM   10   C  C   . ASP A 1 3   ? -11.45069 -28.19956 31.75376  1.000 73.86330 ? 3   ASP A C   1 
ATOM   11   O  O   . ASP A 1 3   ? -11.83239 -27.31784 30.98105  1.000 75.73865 ? 3   ASP A O   1 
ATOM   12   C  CB  . ASP A 1 3   ? -11.95652 -30.61084 31.24986  1.000 83.48418 ? 3   ASP A CB  1 
ATOM   13   C  CG  . ASP A 1 3   ? -10.99126 -31.53979 31.95640  1.000 87.21707 ? 3   ASP A CG  1 
ATOM   14   O  OD1 . ASP A 1 3   ? -9.82339  -31.14747 32.15637  1.000 89.47182 ? 3   ASP A OD1 1 
ATOM   15   O  OD2 . ASP A 1 3   ? -11.40676 -32.66058 32.32273  1.000 87.80412 ? 3   ASP A OD2 1 
ATOM   16   N  N   . THR A 1 4   ? -10.25756 -28.16942 32.34712  1.000 66.06832 ? 4   THR A N   1 
ATOM   17   C  CA  . THR A 1 4   ? -9.28358  -27.09971 32.13130  1.000 57.21833 ? 4   THR A CA  1 
ATOM   18   C  C   . THR A 1 4   ? -7.97075  -27.68143 31.60904  1.000 51.75406 ? 4   THR A C   1 
ATOM   19   O  O   . THR A 1 4   ? -7.84494  -28.88476 31.37580  1.000 50.82243 ? 4   THR A O   1 
ATOM   20   C  CB  . THR A 1 4   ? -9.03384  -26.29884 33.41513  1.000 53.04179 ? 4   THR A CB  1 
ATOM   21   O  OG1 . THR A 1 4   ? -8.48033  -27.15750 34.42067  1.000 50.90484 ? 4   THR A OG1 1 
ATOM   22   C  CG2 . THR A 1 4   ? -10.32677 -25.66900 33.92456  1.000 48.33342 ? 4   THR A CG2 1 
ATOM   23   N  N   . ALA A 1 5   ? -6.98316  -26.80346 31.43563  1.000 46.53146 ? 5   ALA A N   1 
ATOM   24   C  CA  . ALA A 1 5   ? -5.69401  -27.18691 30.86907  1.000 46.26986 ? 5   ALA A CA  1 
ATOM   25   C  C   . ALA A 1 5   ? -4.86074  -27.92039 31.91390  1.000 46.14636 ? 5   ALA A C   1 
ATOM   26   O  O   . ALA A 1 5   ? -4.50971  -27.34793 32.95153  1.000 45.62830 ? 5   ALA A O   1 
ATOM   27   C  CB  . ALA A 1 5   ? -4.95115  -25.95585 30.35525  1.000 44.34886 ? 5   ALA A CB  1 
ATOM   28   N  N   . THR A 1 6   ? -4.52918  -29.17872 31.63093  1.000 46.70840 ? 6   THR A N   1 
ATOM   29   C  CA  . THR A 1 6   ? -3.81742  -30.03411 32.56897  1.000 50.60894 ? 6   THR A CA  1 
ATOM   30   C  C   . THR A 1 6   ? -2.42140  -30.42039 32.09617  1.000 50.03210 ? 6   THR A C   1 
ATOM   31   O  O   . THR A 1 6   ? -1.75268  -31.21280 32.76756  1.000 52.53915 ? 6   THR A O   1 
ATOM   32   C  CB  . THR A 1 6   ? -4.64130  -31.30023 32.84379  1.000 54.58330 ? 6   THR A CB  1 
ATOM   33   O  OG1 . THR A 1 6   ? -3.84883  -32.24776 33.56950  1.000 61.39730 ? 6   THR A OG1 1 
ATOM   34   C  CG2 . THR A 1 6   ? -5.11390  -31.92676 31.53770  1.000 51.12351 ? 6   THR A CG2 1 
ATOM   35   N  N   . THR A 1 7   ? -1.96157  -29.87728 30.98082  1.000 44.80307 ? 7   THR A N   1 
ATOM   36   C  CA  . THR A 1 7   ? -0.69243  -30.20351 30.35475  1.000 40.82843 ? 7   THR A CA  1 
ATOM   37   C  C   . THR A 1 7   ? 0.25935   -29.01117 30.42607  1.000 37.68408 ? 7   THR A C   1 
ATOM   38   O  O   . THR A 1 7   ? -0.15717  -27.89024 30.73769  1.000 40.80138 ? 7   THR A O   1 
ATOM   39   C  CB  . THR A 1 7   ? -0.93504  -30.60921 28.89568  1.000 42.59981 ? 7   THR A CB  1 
ATOM   40   O  OG1 . THR A 1 7   ? -1.62071  -29.55099 28.21962  1.000 43.85034 ? 7   THR A OG1 1 
ATOM   41   C  CG2 . THR A 1 7   ? -1.77966  -31.88279 28.82523  1.000 46.81266 ? 7   THR A CG2 1 
ATOM   42   N  N   . PRO A 1 8   ? 1.55854   -29.22124 30.17099  1.000 32.77178 ? 8   PRO A N   1 
ATOM   43   C  CA  . PRO A 1 8   ? 2.50320   -28.09297 30.17901  1.000 30.49614 ? 8   PRO A CA  1 
ATOM   44   C  C   . PRO A 1 8   ? 2.09680   -27.01837 29.18142  1.000 28.99151 ? 8   PRO A C   1 
ATOM   45   O  O   . PRO A 1 8   ? 1.49640   -27.30432 28.14428  1.000 32.38620 ? 8   PRO A O   1 
ATOM   46   C  CB  . PRO A 1 8   ? 3.83816   -28.73754 29.78575  1.000 32.74677 ? 8   PRO A CB  1 
ATOM   47   C  CG  . PRO A 1 8   ? 3.69461   -30.17566 30.14051  1.000 34.19456 ? 8   PRO A CG  1 
ATOM   48   C  CD  . PRO A 1 8   ? 2.24360   -30.51612 29.97760  1.000 30.94955 ? 8   PRO A CD  1 
ATOM   49   N  N   . GLN A 1 9   ? 2.45942   -25.77071 29.49347  1.000 29.39541 ? 9   GLN A N   1 
ATOM   50   C  CA  . GLN A 1 9   ? 1.96659   -24.60297 28.76620  1.000 29.44944 ? 9   GLN A CA  1 
ATOM   51   C  C   . GLN A 1 9   ? 2.99680   -23.95703 27.84952  1.000 26.31801 ? 9   GLN A C   1 
ATOM   52   O  O   . GLN A 1 9   ? 2.68067   -22.94643 27.20614  1.000 28.63233 ? 9   GLN A O   1 
ATOM   53   C  CB  . GLN A 1 9   ? 1.43813   -23.56184 29.75715  1.000 32.32890 ? 9   GLN A CB  1 
ATOM   54   C  CG  . GLN A 1 9   ? 0.21351   -24.04388 30.53134  1.000 36.98107 ? 9   GLN A CG  1 
ATOM   55   C  CD  . GLN A 1 9   ? -0.95451  -24.35886 29.61411  1.000 39.46538 ? 9   GLN A CD  1 
ATOM   56   O  OE1 . GLN A 1 9   ? -1.59359  -23.45600 29.07439  1.000 43.15693 ? 9   GLN A OE1 1 
ATOM   57   N  NE2 . GLN A 1 9   ? -1.22747  -25.64304 29.41802  1.000 39.24357 ? 9   GLN A NE2 1 
ATOM   58   N  N   . THR A 1 10  ? 4.21480   -24.49443 27.78688  1.000 26.48569 ? 10  THR A N   1 
ATOM   59   C  CA  . THR A 1 10  ? 5.23365   -24.01485 26.85562  1.000 26.20473 ? 10  THR A CA  1 
ATOM   60   C  C   . THR A 1 10  ? 4.67079   -23.93790 25.44475  1.000 24.61369 ? 10  THR A C   1 
ATOM   61   O  O   . THR A 1 10  ? 3.95962   -24.83772 24.99814  1.000 24.58303 ? 10  THR A O   1 
ATOM   62   C  CB  . THR A 1 10  ? 6.44464   -24.96096 26.88477  1.000 26.79200 ? 10  THR A CB  1 
ATOM   63   O  OG1 . THR A 1 10  ? 7.07584   -24.90448 28.17354  1.000 33.10543 ? 10  THR A OG1 1 
ATOM   64   C  CG2 . THR A 1 10  ? 7.46812   -24.61397 25.80392  1.000 28.22177 ? 10  THR A CG2 1 
ATOM   65   N  N   . THR A 1 11  ? 4.96564   -22.83883 24.75173  1.000 26.82180 ? 11  THR A N   1 
ATOM   66   C  CA  . THR A 1 11  ? 4.56817   -22.68163 23.35943  1.000 28.60434 ? 11  THR A CA  1 
ATOM   67   C  C   . THR A 1 11  ? 5.78348   -22.30822 22.52384  1.000 31.03931 ? 11  THR A C   1 
ATOM   68   O  O   . THR A 1 11  ? 6.74890   -21.73695 23.03213  1.000 33.49901 ? 11  THR A O   1 
ATOM   69   C  CB  . THR A 1 11  ? 3.47869   -21.60482 23.19375  1.000 31.29883 ? 11  THR A CB  1 
ATOM   70   O  OG1 . THR A 1 11  ? 3.16943   -21.45152 21.80399  1.000 34.08179 ? 11  THR A OG1 1 
ATOM   71   C  CG2 . THR A 1 11  ? 3.95448   -20.26313 23.75333  1.000 33.38839 ? 11  THR A CG2 1 
ATOM   72   N  N   . ASP A 1 12  ? 5.74161   -22.63791 21.23596  1.000 31.73288 ? 12  ASP A N   1 
ATOM   73   C  CA  . ASP A 1 12  ? 6.74741   -22.12207 20.31731  1.000 34.36002 ? 12  ASP A CA  1 
ATOM   74   C  C   . ASP A 1 12  ? 6.25279   -20.90806 19.53952  1.000 34.40533 ? 12  ASP A C   1 
ATOM   75   O  O   . ASP A 1 12  ? 6.90024   -20.50237 18.56978  1.000 36.71772 ? 12  ASP A O   1 
ATOM   76   C  CB  . ASP A 1 12  ? 7.22576   -23.21723 19.35957  1.000 36.83387 ? 12  ASP A CB  1 
ATOM   77   C  CG  . ASP A 1 12  ? 6.12183   -23.75575 18.48658  1.000 36.15118 ? 12  ASP A CG  1 
ATOM   78   O  OD1 . ASP A 1 12  ? 4.94924   -23.39621 18.71963  1.000 32.34174 ? 12  ASP A OD1 1 
ATOM   79   O  OD2 . ASP A 1 12  ? 6.43490   -24.54127 17.56302  1.000 37.39014 ? 12  ASP A OD2 1 
ATOM   80   N  N   . ALA A 1 13  ? 5.12247   -20.32496 19.94139  1.000 31.65401 ? 13  ALA A N   1 
ATOM   81   C  CA  . ALA A 1 13  ? 4.61594   -19.08184 19.35452  1.000 31.05268 ? 13  ALA A CA  1 
ATOM   82   C  C   . ALA A 1 13  ? 4.14517   -18.17485 20.48078  1.000 30.58907 ? 13  ALA A C   1 
ATOM   83   O  O   . ALA A 1 13  ? 2.94106   -18.03634 20.73436  1.000 32.50966 ? 13  ALA A O   1 
ATOM   84   C  CB  . ALA A 1 13  ? 3.48793   -19.35596 18.35983  1.000 30.41938 ? 13  ALA A CB  1 
ATOM   85   N  N   . PRO A 1 14  ? 5.07484   -17.54454 21.19156  1.000 30.12521 ? 14  PRO A N   1 
ATOM   86   C  CA  . PRO A 1 14  ? 4.69679   -16.77529 22.38080  1.000 30.11825 ? 14  PRO A CA  1 
ATOM   87   C  C   . PRO A 1 14  ? 3.85124   -15.56201 22.02692  1.000 30.48453 ? 14  PRO A C   1 
ATOM   88   O  O   . PRO A 1 14  ? 3.89949   -15.02921 20.91523  1.000 29.73756 ? 14  PRO A O   1 
ATOM   89   C  CB  . PRO A 1 14  ? 6.04359   -16.35651 22.97819  1.000 32.75513 ? 14  PRO A CB  1 
ATOM   90   C  CG  . PRO A 1 14  ? 7.00139   -16.43564 21.84324  1.000 35.05841 ? 14  PRO A CG  1 
ATOM   91   C  CD  . PRO A 1 14  ? 6.53026   -17.57244 20.99309  1.000 31.57982 ? 14  PRO A CD  1 
ATOM   92   N  N   . ALA A 1 15  ? 3.06443   -15.13087 23.01053  1.000 28.29099 ? 15  ALA A N   1 
ATOM   93   C  CA  . ALA A 1 15  ? 2.24954   -13.94263 22.83744  1.000 28.48441 ? 15  ALA A CA  1 
ATOM   94   C  C   . ALA A 1 15  ? 3.14706   -12.75518 22.52949  1.000 28.46150 ? 15  ALA A C   1 
ATOM   95   O  O   . ALA A 1 15  ? 4.21248   -12.58790 23.13429  1.000 30.84477 ? 15  ALA A O   1 
ATOM   96   C  CB  . ALA A 1 15  ? 1.41577   -13.67678 24.08931  1.000 30.15528 ? 15  ALA A CB  1 
ATOM   97   N  N   . PHE A 1 16  ? 2.71333   -11.94008 21.56467  1.000 27.42254 ? 16  PHE A N   1 
ATOM   98   C  CA  . PHE A 1 16  ? 3.42852   -10.76109 21.11580  1.000 26.28510 ? 16  PHE A CA  1 
ATOM   99   C  C   . PHE A 1 16  ? 2.42194   -9.63740  20.90129  1.000 25.94360 ? 16  PHE A C   1 
ATOM   100  O  O   . PHE A 1 16  ? 1.32253   -9.88932  20.39114  1.000 29.24206 ? 16  PHE A O   1 
ATOM   101  C  CB  . PHE A 1 16  ? 4.18926   -11.03263 19.80835  1.000 24.45597 ? 16  PHE A CB  1 
ATOM   102  C  CG  . PHE A 1 16  ? 5.00885   -9.87577  19.33683  1.000 23.36750 ? 16  PHE A CG  1 
ATOM   103  C  CD1 . PHE A 1 16  ? 4.45014   -8.89884  18.52618  1.000 23.30713 ? 16  PHE A CD1 1 
ATOM   104  C  CD2 . PHE A 1 16  ? 6.33931   -9.76083  19.70379  1.000 25.30981 ? 16  PHE A CD2 1 
ATOM   105  C  CE1 . PHE A 1 16  ? 5.19448   -7.82173  18.10350  1.000 26.28272 ? 16  PHE A CE1 1 
ATOM   106  C  CE2 . PHE A 1 16  ? 7.10013   -8.68274  19.27622  1.000 24.21685 ? 16  PHE A CE2 1 
ATOM   107  C  CZ  . PHE A 1 16  ? 6.52479   -7.71413  18.46866  1.000 27.11099 ? 16  PHE A CZ  1 
ATOM   108  N  N   . PRO A 1 17  ? 2.76213   -8.38533  21.26384  1.000 27.12129 ? 17  PRO A N   1 
ATOM   109  C  CA  . PRO A 1 17  ? 4.00056   -7.91879  21.90193  1.000 24.09619 ? 17  PRO A CA  1 
ATOM   110  C  C   . PRO A 1 17  ? 4.06094   -8.20756  23.39323  1.000 25.15799 ? 17  PRO A C   1 
ATOM   111  O  O   . PRO A 1 17  ? 3.09704   -8.63733  24.01567  1.000 29.16863 ? 17  PRO A O   1 
ATOM   112  C  CB  . PRO A 1 17  ? 3.96417   -6.40084  21.65971  1.000 23.81647 ? 17  PRO A CB  1 
ATOM   113  C  CG  . PRO A 1 17  ? 2.51283   -6.08002  21.66287  1.000 26.61428 ? 17  PRO A CG  1 
ATOM   114  C  CD  . PRO A 1 17  ? 1.86876   -7.25598  20.94685  1.000 26.08551 ? 17  PRO A CD  1 
ATOM   115  N  N   . SER A 1 18  ? 5.22679   -7.95547  23.96862  1.000 28.43324 ? 18  SER A N   1 
ATOM   116  C  CA  . SER A 1 18  ? 5.45388   -8.01730  25.40040  1.000 28.17066 ? 18  SER A CA  1 
ATOM   117  C  C   . SER A 1 18  ? 5.65888   -6.61325  25.93850  1.000 29.01258 ? 18  SER A C   1 
ATOM   118  O  O   . SER A 1 18  ? 5.99482   -5.68489  25.19909  1.000 28.79022 ? 18  SER A O   1 
ATOM   119  C  CB  . SER A 1 18  ? 6.66976   -8.88623  25.72970  1.000 34.13071 ? 18  SER A CB  1 
ATOM   120  O  OG  . SER A 1 18  ? 6.46260   -10.21395 25.29413  1.000 38.79337 ? 18  SER A OG  1 
ATOM   121  N  N   . ASN A 1 19  ? 5.46148   -6.46698  27.24283  1.000 29.37558 ? 19  ASN A N   1 
ATOM   122  C  CA  . ASN A 1 19  ? 5.61564   -5.17816  27.89493  1.000 28.13674 ? 19  ASN A CA  1 
ATOM   123  C  C   . ASN A 1 19  ? 6.99705   -5.07632  28.52104  1.000 27.44095 ? 19  ASN A C   1 
ATOM   124  O  O   . ASN A 1 19  ? 7.50092   -6.04159  29.09953  1.000 27.44849 ? 19  ASN A O   1 
ATOM   125  C  CB  . ASN A 1 19  ? 4.53739   -4.97286  28.95988  1.000 29.63006 ? 19  ASN A CB  1 
ATOM   126  C  CG  . ASN A 1 19  ? 3.13799   -4.98047  28.38058  1.000 32.01145 ? 19  ASN A CG  1 
ATOM   127  O  OD1 . ASN A 1 19  ? 2.94020   -4.74688  27.18693  1.000 32.93184 ? 19  ASN A OD1 1 
ATOM   128  N  ND2 . ASN A 1 19  ? 2.15480   -5.24501  29.22819  1.000 38.86238 ? 19  ASN A ND2 1 
ATOM   129  N  N   . ARG A 1 20  ? 7.60290   -3.90024  28.40550  1.000 25.84560 ? 20  ARG A N   1 
ATOM   130  C  CA  . ARG A 1 20  ? 8.83452   -3.62586  29.12943  1.000 26.53304 ? 20  ARG A CA  1 
ATOM   131  C  C   . ARG A 1 20  ? 8.57290   -3.52979  30.62170  1.000 28.82284 ? 20  ARG A C   1 
ATOM   132  O  O   . ARG A 1 20  ? 7.55372   -2.98771  31.06173  1.000 32.29360 ? 20  ARG A O   1 
ATOM   133  C  CB  . ARG A 1 20  ? 9.46427   -2.32195  28.65152  1.000 25.03927 ? 20  ARG A CB  1 
ATOM   134  C  CG  . ARG A 1 20  ? 10.13475  -2.46367  27.33371  1.000 25.56806 ? 20  ARG A CG  1 
ATOM   135  C  CD  . ARG A 1 20  ? 10.89992  -1.22514  26.93119  1.000 23.12937 ? 20  ARG A CD  1 
ATOM   136  N  NE  . ARG A 1 20  ? 11.19886  -1.34959  25.51566  1.000 22.23371 ? 20  ARG A NE  1 
ATOM   137  C  CZ  . ARG A 1 20  ? 11.83437  -0.44445  24.79395  1.000 23.24491 ? 20  ARG A CZ  1 
ATOM   138  N  NH1 . ARG A 1 20  ? 12.31126  0.66375   25.34094  1.000 22.86603 ? 20  ARG A NH1 1 
ATOM   139  N  NH2 . ARG A 1 20  ? 11.97069  -0.64607  23.48762  1.000 21.89635 ? 20  ARG A NH2 1 
ATOM   140  N  N   . SER A 1 21  ? 9.50848   -4.06604  31.39800  1.000 29.16458 ? 21  SER A N   1 
ATOM   141  C  CA  . SER A 1 21  ? 9.54073   -3.86580  32.83587  1.000 30.94141 ? 21  SER A CA  1 
ATOM   142  C  C   . SER A 1 21  ? 10.63046  -2.89287  33.25241  1.000 29.58973 ? 21  SER A C   1 
ATOM   143  O  O   . SER A 1 21  ? 10.51565  -2.27055  34.31198  1.000 33.84313 ? 21  SER A O   1 
ATOM   144  C  CB  . SER A 1 21  ? 9.75234   -5.20723  33.54654  1.000 34.47036 ? 21  SER A CB  1 
ATOM   145  O  OG  . SER A 1 21  ? 10.87902  -5.86898  33.00549  1.000 37.79642 ? 21  SER A OG  1 
ATOM   146  N  N   . CYS A 1 22  ? 11.67199  -2.74736  32.43644  1.000 27.52348 ? 22  CYS A N   1 
ATOM   147  C  CA  . CYS A 1 22  ? 12.72101  -1.76950  32.61562  1.000 29.70644 ? 22  CYS A CA  1 
ATOM   148  C  C   . CYS A 1 22  ? 12.77739  -0.91122  31.36172  1.000 26.72452 ? 22  CYS A C   1 
ATOM   149  O  O   . CYS A 1 22  ? 12.76295  -1.45987  30.25431  1.000 26.69990 ? 22  CYS A O   1 
ATOM   150  C  CB  . CYS A 1 22  ? 14.07596  -2.45238  32.84595  1.000 31.69038 ? 22  CYS A CB  1 
ATOM   151  S  SG  . CYS A 1 22  ? 15.51348  -1.35999  32.70895  1.000 31.03005 ? 22  CYS A SG  1 
ATOM   152  N  N   . PRO A 1 23  ? 12.83274  0.41756   31.48252  1.000 26.99279 ? 23  PRO A N   1 
ATOM   153  C  CA  . PRO A 1 23  ? 12.68822  1.26529   30.28740  1.000 25.76631 ? 23  PRO A CA  1 
ATOM   154  C  C   . PRO A 1 23  ? 13.72785  1.01333   29.20757  1.000 25.51913 ? 23  PRO A C   1 
ATOM   155  O  O   . PRO A 1 23  ? 13.44188  1.25901   28.02976  1.000 27.12504 ? 23  PRO A O   1 
ATOM   156  C  CB  . PRO A 1 23  ? 12.79244  2.69424   30.85079  1.000 30.19904 ? 23  PRO A CB  1 
ATOM   157  C  CG  . PRO A 1 23  ? 13.26571  2.55038   32.25591  1.000 32.36335 ? 23  PRO A CG  1 
ATOM   158  C  CD  . PRO A 1 23  ? 12.82998  1.20454   32.72808  1.000 29.69553 ? 23  PRO A CD  1 
ATOM   159  N  N   . TYR A 1 24  ? 14.91495  0.50924   29.55243  1.000 22.97584 ? 24  TYR A N   1 
ATOM   160  C  CA  . TYR A 1 24  ? 15.99748  0.37699   28.58194  1.000 22.28814 ? 24  TYR A CA  1 
ATOM   161  C  C   . TYR A 1 24  ? 16.49031  -1.06269  28.44832  1.000 24.10791 ? 24  TYR A C   1 
ATOM   162  O  O   . TYR A 1 24  ? 17.62116  -1.29378  28.00342  1.000 25.50995 ? 24  TYR A O   1 
ATOM   163  C  CB  . TYR A 1 24  ? 17.15269  1.31895   28.94230  1.000 23.47487 ? 24  TYR A CB  1 
ATOM   164  C  CG  . TYR A 1 24  ? 17.62387  1.18137   30.37829  1.000 22.99993 ? 24  TYR A CG  1 
ATOM   165  C  CD1 . TYR A 1 24  ? 18.51049  0.17620   30.73879  1.000 24.72235 ? 24  TYR A CD1 1 
ATOM   166  C  CD2 . TYR A 1 24  ? 17.18538  2.06148   31.36678  1.000 23.68889 ? 24  TYR A CD2 1 
ATOM   167  C  CE1 . TYR A 1 24  ? 18.94242  0.03434   32.04654  1.000 25.64103 ? 24  TYR A CE1 1 
ATOM   168  C  CE2 . TYR A 1 24  ? 17.61415  1.93126   32.68286  1.000 24.68830 ? 24  TYR A CE2 1 
ATOM   169  C  CZ  . TYR A 1 24  ? 18.49329  0.91461   33.01492  1.000 26.36040 ? 24  TYR A CZ  1 
ATOM   170  O  OH  . TYR A 1 24  ? 18.93014  0.76428   34.31402  1.000 30.93252 ? 24  TYR A OH  1 
ATOM   171  N  N   . GLN A 1 25  ? 15.67889  -2.04336  28.81814  1.000 22.81576 ? 25  GLN A N   1 
ATOM   172  C  CA  A GLN A 1 25  ? 16.03717  -3.42488  28.54981  0.558 25.62429 ? 25  GLN A CA  1 
ATOM   173  C  CA  B GLN A 1 25  ? 16.00846  -3.45136  28.63139  0.442 26.36755 ? 25  GLN A CA  1 
ATOM   174  C  C   . GLN A 1 25  ? 14.90231  -4.13811  27.83728  1.000 25.90929 ? 25  GLN A C   1 
ATOM   175  O  O   . GLN A 1 25  ? 13.73416  -3.76162  27.93494  1.000 26.07828 ? 25  GLN A O   1 
ATOM   176  C  CB  A GLN A 1 25  ? 16.41723  -4.19359  29.81854  0.558 27.47034 ? 25  GLN A CB  1 
ATOM   177  C  CB  B GLN A 1 25  ? 16.20708  -4.16616  29.98694  0.442 29.54391 ? 25  GLN A CB  1 
ATOM   178  C  CG  A GLN A 1 25  ? 17.80751  -3.85674  30.36064  0.558 28.95541 ? 25  GLN A CG  1 
ATOM   179  C  CG  B GLN A 1 25  ? 17.39197  -3.64267  30.80474  0.442 32.80030 ? 25  GLN A CG  1 
ATOM   180  C  CD  A GLN A 1 25  ? 18.94757  -4.10481  29.36808  0.558 27.18233 ? 25  GLN A CD  1 
ATOM   181  C  CD  B GLN A 1 25  ? 17.42676  -4.16483  32.23536  0.442 34.64142 ? 25  GLN A CD  1 
ATOM   182  O  OE1 A GLN A 1 25  ? 18.75445  -4.63636  28.26511  0.558 28.57187 ? 25  GLN A OE1 1 
ATOM   183  O  OE1 B GLN A 1 25  ? 16.47556  -4.78984  32.71263  0.442 34.15558 ? 25  GLN A OE1 1 
ATOM   184  N  NE2 A GLN A 1 25  ? 20.15253  -3.71886  29.76978  0.558 28.08586 ? 25  GLN A NE2 1 
ATOM   185  N  NE2 B GLN A 1 25  ? 18.53098  -3.90022  32.93104  0.442 34.84516 ? 25  GLN A NE2 1 
ATOM   186  N  N   . LEU A 1 26  ? 15.27639  -5.15814  27.07478  1.000 27.52959 ? 26  LEU A N   1 
ATOM   187  C  CA  . LEU A 1 26  ? 14.27973  -5.95838  26.38405  1.000 29.01218 ? 26  LEU A CA  1 
ATOM   188  C  C   . LEU A 1 26  ? 13.36312  -6.63847  27.39685  1.000 30.41935 ? 26  LEU A C   1 
ATOM   189  O  O   . LEU A 1 26  ? 13.82976  -7.10023  28.44720  1.000 32.64886 ? 26  LEU A O   1 
ATOM   190  C  CB  . LEU A 1 26  ? 14.94120  -7.02865  25.51351  1.000 30.83952 ? 26  LEU A CB  1 
ATOM   191  C  CG  . LEU A 1 26  ? 15.83212  -6.60687  24.35095  1.000 31.43058 ? 26  LEU A CG  1 
ATOM   192  C  CD1 . LEU A 1 26  ? 16.32894  -7.86012  23.64586  1.000 32.92701 ? 26  LEU A CD1 1 
ATOM   193  C  CD2 . LEU A 1 26  ? 15.06223  -5.72215  23.38997  1.000 35.00512 ? 26  LEU A CD2 1 
ATOM   194  N  N   . PRO A 1 27  ? 12.06440  -6.71606  27.11918  1.000 29.43776 ? 27  PRO A N   1 
ATOM   195  C  CA  . PRO A 1 27  ? 11.21096  -7.64847  27.85783  1.000 31.53000 ? 27  PRO A CA  1 
ATOM   196  C  C   . PRO A 1 27  ? 11.83303  -9.03829  27.84039  1.000 32.83698 ? 27  PRO A C   1 
ATOM   197  O  O   . PRO A 1 27  ? 12.52830  -9.41077  26.89299  1.000 35.49063 ? 27  PRO A O   1 
ATOM   198  C  CB  . PRO A 1 27  ? 9.88960   -7.61181  27.08307  1.000 31.90397 ? 27  PRO A CB  1 
ATOM   199  C  CG  . PRO A 1 27  ? 9.90776   -6.31143  26.33963  1.000 31.49171 ? 27  PRO A CG  1 
ATOM   200  C  CD  . PRO A 1 27  ? 11.34120  -6.00823  26.04772  1.000 29.01462 ? 27  PRO A CD  1 
ATOM   201  N  N   . ASP A 1 28  ? 11.59268  -9.80461  28.90917  1.000 36.62854 ? 28  ASP A N   1 
ATOM   202  C  CA  . ASP A 1 28  ? 12.20278  -11.12692 29.00992  1.000 42.70345 ? 28  ASP A CA  1 
ATOM   203  C  C   . ASP A 1 28  ? 11.93783  -11.96753 27.76749  1.000 42.11130 ? 28  ASP A C   1 
ATOM   204  O  O   . ASP A 1 28  ? 12.84877  -12.61678 27.24150  1.000 42.13604 ? 28  ASP A O   1 
ATOM   205  C  CB  . ASP A 1 28  ? 11.69252  -11.84670 30.25796  1.000 47.57158 ? 28  ASP A CB  1 
ATOM   206  C  CG  . ASP A 1 28  ? 12.09611  -11.14258 31.52687  1.000 58.07043 ? 28  ASP A CG  1 
ATOM   207  O  OD1 . ASP A 1 28  ? 11.30898  -11.15214 32.50236  1.000 61.68605 ? 28  ASP A OD1 1 
ATOM   208  O  OD2 . ASP A 1 28  ? 13.20129  -10.55940 31.53473  1.000 60.60041 ? 28  ASP A OD2 1 
ATOM   209  N  N   . GLY A 1 29  ? 10.69954  -11.95333 27.27431  1.000 39.31847 ? 29  GLY A N   1 
ATOM   210  C  CA  . GLY A 1 29  ? 10.37864  -12.73208 26.09270  1.000 35.79250 ? 29  GLY A CA  1 
ATOM   211  C  C   . GLY A 1 29  ? 11.14062  -12.29240 24.85772  1.000 34.53934 ? 29  GLY A C   1 
ATOM   212  O  O   . GLY A 1 29  ? 11.43523  -13.11316 23.98318  1.000 36.83990 ? 29  GLY A O   1 
ATOM   213  N  N   . TYR A 1 30  ? 11.46971  -10.99929 24.76020  1.000 31.71468 ? 30  TYR A N   1 
ATOM   214  C  CA  . TYR A 1 30  ? 12.19834  -10.52405 23.58661  1.000 31.97870 ? 30  TYR A CA  1 
ATOM   215  C  C   . TYR A 1 30  ? 13.65501  -10.95180 23.63899  1.000 32.40657 ? 30  TYR A C   1 
ATOM   216  O  O   . TYR A 1 30  ? 14.27319  -11.19855 22.59726  1.000 32.29337 ? 30  TYR A O   1 
ATOM   217  C  CB  . TYR A 1 30  ? 12.12761  -9.00084  23.47091  1.000 30.69860 ? 30  TYR A CB  1 
ATOM   218  C  CG  . TYR A 1 30  ? 10.80114  -8.43694  23.03838  1.000 30.30365 ? 30  TYR A CG  1 
ATOM   219  C  CD1 . TYR A 1 30  ? 9.64390   -9.21648  23.02204  1.000 29.14794 ? 30  TYR A CD1 1 
ATOM   220  C  CD2 . TYR A 1 30  ? 10.70522  -7.10769  22.64114  1.000 29.89097 ? 30  TYR A CD2 1 
ATOM   221  C  CE1 . TYR A 1 30  ? 8.42987   -8.67091  22.62364  1.000 28.64594 ? 30  TYR A CE1 1 
ATOM   222  C  CE2 . TYR A 1 30  ? 9.51149   -6.56602  22.24602  1.000 27.64408 ? 30  TYR A CE2 1 
ATOM   223  C  CZ  . TYR A 1 30  ? 8.38067   -7.34057  22.23546  1.000 29.09087 ? 30  TYR A CZ  1 
ATOM   224  O  OH  . TYR A 1 30  ? 7.20438   -6.75985  21.83500  1.000 30.52318 ? 30  TYR A OH  1 
ATOM   225  N  N   . ALA A 1 31  ? 14.23629  -10.98771 24.83966  1.000 34.52047 ? 31  ALA A N   1 
ATOM   226  C  CA  . ALA A 1 31  ? 15.58539  -11.51794 24.97869  1.000 35.57359 ? 31  ALA A CA  1 
ATOM   227  C  C   . ALA A 1 31  ? 15.63553  -12.96190 24.50509  1.000 36.24386 ? 31  ALA A C   1 
ATOM   228  O  O   . ALA A 1 31  ? 16.60484  -13.38164 23.86199  1.000 34.31108 ? 31  ALA A O   1 
ATOM   229  C  CB  . ALA A 1 31  ? 16.05283  -11.39939 26.43186  1.000 36.55649 ? 31  ALA A CB  1 
ATOM   230  N  N   . GLN A 1 32  ? 14.58238  -13.72984 24.79968  1.000 36.26489 ? 32  GLN A N   1 
ATOM   231  C  CA  A GLN A 1 32  ? 14.52672  -15.10839 24.33027  0.511 37.21001 ? 32  GLN A CA  1 
ATOM   232  C  CA  B GLN A 1 32  ? 14.50235  -15.10959 24.32971  0.489 37.47135 ? 32  GLN A CA  1 
ATOM   233  C  C   . GLN A 1 32  ? 14.46714  -15.16703 22.80906  1.000 36.68269 ? 32  GLN A C   1 
ATOM   234  O  O   . GLN A 1 32  ? 15.18232  -15.95961 22.18759  1.000 37.41552 ? 32  GLN A O   1 
ATOM   235  C  CB  A GLN A 1 32  ? 13.33199  -15.82656 24.95777  0.511 37.85493 ? 32  GLN A CB  1 
ATOM   236  C  CB  B GLN A 1 32  ? 13.26767  -15.79110 24.91903  0.489 38.34183 ? 32  GLN A CB  1 
ATOM   237  C  CG  A GLN A 1 32  ? 13.43539  -15.97288 26.47320  0.511 38.38394 ? 32  GLN A CG  1 
ATOM   238  C  CG  B GLN A 1 32  ? 12.96741  -17.15498 24.31722  0.489 39.02373 ? 32  GLN A CG  1 
ATOM   239  C  CD  A GLN A 1 32  ? 12.30304  -16.79069 27.06569  0.511 40.94379 ? 32  GLN A CD  1 
ATOM   240  C  CD  B GLN A 1 32  ? 14.03648  -18.18210 24.63284  0.489 40.45919 ? 32  GLN A CD  1 
ATOM   241  O  OE1 A GLN A 1 32  ? 11.16175  -16.33476 27.13788  0.511 42.60858 ? 32  GLN A OE1 1 
ATOM   242  O  OE1 B GLN A 1 32  ? 14.93329  -18.43184 23.82617  0.489 40.72722 ? 32  GLN A OE1 1 
ATOM   243  N  NE2 A GLN A 1 32  ? 12.61502  -18.00738 27.49147  0.511 41.44922 ? 32  GLN A NE2 1 
ATOM   244  N  NE2 B GLN A 1 32  ? 13.94639  -18.78427 25.81279  0.489 40.61769 ? 32  GLN A NE2 1 
ATOM   245  N  N   . LEU A 1 33  ? 13.63389  -14.32703 22.19016  1.000 32.70559 ? 33  LEU A N   1 
ATOM   246  C  CA  . LEU A 1 33  ? 13.58862  -14.28300 20.73165  1.000 30.14186 ? 33  LEU A CA  1 
ATOM   247  C  C   . LEU A 1 33  ? 14.93038  -13.84866 20.15524  1.000 30.80269 ? 33  LEU A C   1 
ATOM   248  O  O   . LEU A 1 33  ? 15.38359  -14.38953 19.13851  1.000 31.44805 ? 33  LEU A O   1 
ATOM   249  C  CB  . LEU A 1 33  ? 12.47540  -13.34142 20.27308  1.000 30.42889 ? 33  LEU A CB  1 
ATOM   250  C  CG  . LEU A 1 33  ? 11.04817  -13.77419 20.60467  1.000 30.26724 ? 33  LEU A CG  1 
ATOM   251  C  CD1 . LEU A 1 33  ? 10.06525  -12.67384 20.26459  1.000 28.66127 ? 33  LEU A CD1 1 
ATOM   252  C  CD2 . LEU A 1 33  ? 10.69801  -15.06686 19.86574  1.000 31.56836 ? 33  LEU A CD2 1 
ATOM   253  N  N   . ARG A 1 34  ? 15.57733  -12.86697 20.79318  1.000 30.68774 ? 34  ARG A N   1 
ATOM   254  C  CA  . ARG A 1 34  ? 16.88572  -12.40527 20.33782  1.000 31.07166 ? 34  ARG A CA  1 
ATOM   255  C  C   . ARG A 1 34  ? 17.89237  -13.55033 20.29254  1.000 34.07436 ? 34  ARG A C   1 
ATOM   256  O  O   . ARG A 1 34  ? 18.71918  -13.62928 19.37340  1.000 32.37062 ? 34  ARG A O   1 
ATOM   257  C  CB  . ARG A 1 34  ? 17.37590  -11.28257 21.25990  1.000 27.20818 ? 34  ARG A CB  1 
ATOM   258  C  CG  . ARG A 1 34  ? 18.59818  -10.51671 20.77152  1.000 26.49720 ? 34  ARG A CG  1 
ATOM   259  C  CD  . ARG A 1 34  ? 19.88773  -11.11417 21.32779  1.000 27.43248 ? 34  ARG A CD  1 
ATOM   260  N  NE  . ARG A 1 34  ? 19.84939  -11.19420 22.78325  1.000 30.19681 ? 34  ARG A NE  1 
ATOM   261  C  CZ  . ARG A 1 34  ? 20.10955  -10.17187 23.58599  1.000 30.13540 ? 34  ARG A CZ  1 
ATOM   262  N  NH1 . ARG A 1 34  ? 20.45181  -8.98734  23.10519  1.000 31.32733 ? 34  ARG A NH1 1 
ATOM   263  N  NH2 . ARG A 1 34  ? 20.02371  -10.34022 24.90435  1.000 32.18960 ? 34  ARG A NH2 1 
ATOM   264  N  N   . ASP A 1 35  ? 17.82816  -14.45303 21.27183  1.000 35.88766 ? 35  ASP A N   1 
ATOM   265  C  CA  . ASP A 1 35  ? 18.80607  -15.52519 21.41545  1.000 37.72537 ? 35  ASP A CA  1 
ATOM   266  C  C   . ASP A 1 35  ? 18.52268  -16.74930 20.55285  1.000 39.98431 ? 35  ASP A C   1 
ATOM   267  O  O   . ASP A 1 35  ? 19.43418  -17.55952 20.34848  1.000 42.71096 ? 35  ASP A O   1 
ATOM   268  C  CB  . ASP A 1 35  ? 18.88843  -15.96060 22.88272  1.000 40.27693 ? 35  ASP A CB  1 
ATOM   269  C  CG  . ASP A 1 35  ? 19.56325  -14.92484 23.76134  1.000 42.84183 ? 35  ASP A CG  1 
ATOM   270  O  OD1 . ASP A 1 35  ? 20.08755  -13.92853 23.21965  1.000 43.71626 ? 35  ASP A OD1 1 
ATOM   271  O  OD2 . ASP A 1 35  ? 19.57541  -15.10748 24.99488  1.000 42.36038 ? 35  ASP A OD2 1 
ATOM   272  N  N   . THR A 1 36  ? 17.30049  -16.91984 20.06061  1.000 38.16425 ? 36  THR A N   1 
ATOM   273  C  CA  . THR A 1 36  ? 16.99233  -18.08842 19.24189  1.000 40.44487 ? 36  THR A CA  1 
ATOM   274  C  C   . THR A 1 36  ? 17.60356  -17.92630 17.85302  1.000 39.58583 ? 36  THR A C   1 
ATOM   275  O  O   . THR A 1 36  ? 17.43368  -16.87648 17.22674  1.000 41.33801 ? 36  THR A O   1 
ATOM   276  C  CB  . THR A 1 36  ? 15.48071  -18.29446 19.12793  1.000 44.75724 ? 36  THR A CB  1 
ATOM   277  O  OG1 . THR A 1 36  ? 14.88138  -17.15150 18.50257  1.000 50.83227 ? 36  THR A OG1 1 
ATOM   278  C  CG2 . THR A 1 36  ? 14.86396  -18.49509 20.49567  1.000 43.42678 ? 36  THR A CG2 1 
ATOM   279  N  N   . PRO A 1 37  ? 18.32178  -18.92661 17.34559  1.000 35.79101 ? 37  PRO A N   1 
ATOM   280  C  CA  . PRO A 1 37  ? 18.91559  -18.81015 16.00935  1.000 36.03684 ? 37  PRO A CA  1 
ATOM   281  C  C   . PRO A 1 37  ? 17.85807  -18.64450 14.92614  1.000 37.51745 ? 37  PRO A C   1 
ATOM   282  O  O   . PRO A 1 37  ? 16.69658  -19.03134 15.07564  1.000 37.58461 ? 37  PRO A O   1 
ATOM   283  C  CB  . PRO A 1 37  ? 19.67852  -20.13166 15.84744  1.000 37.33853 ? 37  PRO A CB  1 
ATOM   284  C  CG  . PRO A 1 37  ? 20.02868  -20.51479 17.25300  1.000 37.09884 ? 37  PRO A CG  1 
ATOM   285  C  CD  . PRO A 1 37  ? 18.84624  -20.08738 18.08433  1.000 34.64446 ? 37  PRO A CD  1 
ATOM   286  N  N   . GLY A 1 38  ? 18.27891  -18.05218 13.81571  1.000 35.80196 ? 38  GLY A N   1 
ATOM   287  C  CA  . GLY A 1 38  ? 17.40253  -17.88184 12.68576  1.000 33.15532 ? 38  GLY A CA  1 
ATOM   288  C  C   . GLY A 1 38  ? 16.78226  -16.50469 12.65131  1.000 30.36293 ? 38  GLY A C   1 
ATOM   289  O  O   . GLY A 1 38  ? 16.58816  -15.85387 13.67981  1.000 30.10671 ? 38  GLY A O   1 
ATOM   290  N  N   . PRO A 1 39  ? 16.46396  -16.03966 11.44340  1.000 28.73858 ? 39  PRO A N   1 
ATOM   291  C  CA  . PRO A 1 39  ? 15.96847  -14.66594 11.28992  1.000 26.10897 ? 39  PRO A CA  1 
ATOM   292  C  C   . PRO A 1 39  ? 14.54063  -14.46688 11.75240  1.000 23.12182 ? 39  PRO A C   1 
ATOM   293  O  O   . PRO A 1 39  ? 14.17534  -13.33365 12.08754  1.000 23.63990 ? 39  PRO A O   1 
ATOM   294  C  CB  . PRO A 1 39  ? 16.09668  -14.42177 9.78028   1.000 29.05048 ? 39  PRO A CB  1 
ATOM   295  C  CG  . PRO A 1 39  ? 16.04453  -15.79389 9.16925   1.000 32.67234 ? 39  PRO A CG  1 
ATOM   296  C  CD  . PRO A 1 39  ? 16.73266  -16.69251 10.15111  1.000 30.61888 ? 39  PRO A CD  1 
ATOM   297  N  N   . LEU A 1 40  ? 13.71926  -15.51621 11.77398  1.000 25.19682 ? 40  LEU A N   1 
ATOM   298  C  CA  . LEU A 1 40  ? 12.28867  -15.39468 12.01858  1.000 23.67608 ? 40  LEU A CA  1 
ATOM   299  C  C   . LEU A 1 40  ? 11.87546  -16.22859 13.22226  1.000 27.14946 ? 40  LEU A C   1 
ATOM   300  O  O   . LEU A 1 40  ? 12.51282  -17.23574 13.54723  1.000 30.78215 ? 40  LEU A O   1 
ATOM   301  C  CB  . LEU A 1 40  ? 11.47379  -15.85720 10.80380  1.000 23.85620 ? 40  LEU A CB  1 
ATOM   302  C  CG  . LEU A 1 40  ? 11.76198  -15.21749 9.44648   1.000 25.72107 ? 40  LEU A CG  1 
ATOM   303  C  CD1 . LEU A 1 40  ? 10.89072  -15.87354 8.37454   1.000 29.22027 ? 40  LEU A CD1 1 
ATOM   304  C  CD2 . LEU A 1 40  ? 11.52782  -13.71624 9.51104   1.000 27.21511 ? 40  LEU A CD2 1 
ATOM   305  N  N   . HIS A 1 41  ? 10.78158  -15.81943 13.86626  1.000 24.17571 ? 41  HIS A N   1 
ATOM   306  C  CA  . HIS A 1 41  ? 10.17855  -16.63362 14.90956  1.000 25.13071 ? 41  HIS A CA  1 
ATOM   307  C  C   . HIS A 1 41  ? 8.66955   -16.44858 14.87718  1.000 24.83863 ? 41  HIS A C   1 
ATOM   308  O  O   . HIS A 1 41  ? 8.17521   -15.34326 14.64233  1.000 24.76504 ? 41  HIS A O   1 
ATOM   309  C  CB  . HIS A 1 41  ? 10.72371  -16.27978 16.29818  1.000 26.48460 ? 41  HIS A CB  1 
ATOM   310  C  CG  . HIS A 1 41  ? 10.59666  -17.39229 17.29365  1.000 27.18604 ? 41  HIS A CG  1 
ATOM   311  N  ND1 . HIS A 1 41  ? 9.40698   -17.70443 17.91744  1.000 27.82637 ? 41  HIS A ND1 1 
ATOM   312  C  CD2 . HIS A 1 41  ? 11.50625  -18.28567 17.75143  1.000 29.64677 ? 41  HIS A CD2 1 
ATOM   313  C  CE1 . HIS A 1 41  ? 9.59226   -18.73362 18.72602  1.000 30.38783 ? 41  HIS A CE1 1 
ATOM   314  N  NE2 . HIS A 1 41  ? 10.85870  -19.10278 18.64709  1.000 30.35509 ? 41  HIS A NE2 1 
ATOM   315  N  N   . ARG A 1 42  ? 7.94345   -17.52887 15.13347  1.000 26.27835 ? 42  ARG A N   1 
ATOM   316  C  CA  . ARG A 1 42  ? 6.49678   -17.44337 15.22133  1.000 26.30161 ? 42  ARG A CA  1 
ATOM   317  C  C   . ARG A 1 42  ? 6.07944   -16.78399 16.53092  1.000 26.32727 ? 42  ARG A C   1 
ATOM   318  O  O   . ARG A 1 42  ? 6.74217   -16.92479 17.56338  1.000 27.46013 ? 42  ARG A O   1 
ATOM   319  C  CB  . ARG A 1 42  ? 5.87727   -18.83671 15.11198  1.000 28.18754 ? 42  ARG A CB  1 
ATOM   320  C  CG  . ARG A 1 42  ? 6.29240   -19.56855 13.84304  1.000 31.57452 ? 42  ARG A CG  1 
ATOM   321  C  CD  . ARG A 1 42  ? 5.70840   -20.96421 13.80109  1.000 39.65344 ? 42  ARG A CD  1 
ATOM   322  N  NE  . ARG A 1 42  ? 6.11438   -21.73778 12.63023  1.000 44.21183 ? 42  ARG A NE  1 
ATOM   323  C  CZ  . ARG A 1 42  ? 7.17096   -22.53818 12.59050  1.000 47.15402 ? 42  ARG A CZ  1 
ATOM   324  N  NH1 . ARG A 1 42  ? 7.96731   -22.68268 13.63810  1.000 48.35725 ? 42  ARG A NH1 1 
ATOM   325  N  NH2 . ARG A 1 42  ? 7.43698   -23.20846 11.47142  1.000 50.48609 ? 42  ARG A NH2 1 
ATOM   326  N  N   . VAL A 1 43  ? 4.98286   -16.02798 16.46762  1.000 25.92401 ? 43  VAL A N   1 
ATOM   327  C  CA  . VAL A 1 43  ? 4.36916   -15.41027 17.63601  1.000 26.21671 ? 43  VAL A CA  1 
ATOM   328  C  C   . VAL A 1 43  ? 2.85892   -15.52476 17.49288  1.000 26.81518 ? 43  VAL A C   1 
ATOM   329  O  O   . VAL A 1 43  ? 2.33327   -15.81163 16.41689  1.000 27.48144 ? 43  VAL A O   1 
ATOM   330  C  CB  . VAL A 1 43  ? 4.75991   -13.92206 17.82316  1.000 24.88054 ? 43  VAL A CB  1 
ATOM   331  C  CG1 . VAL A 1 43  ? 6.24586   -13.76611 18.10259  1.000 24.50972 ? 43  VAL A CG1 1 
ATOM   332  C  CG2 . VAL A 1 43  ? 4.34491   -13.10007 16.61170  1.000 25.54974 ? 43  VAL A CG2 1 
ATOM   333  N  N   . THR A 1 44  ? 2.16051   -15.28612 18.59820  1.000 28.20651 ? 44  THR A N   1 
ATOM   334  C  CA  . THR A 1 44  ? 0.70265   -15.27166 18.62734  1.000 27.80528 ? 44  THR A CA  1 
ATOM   335  C  C   . THR A 1 44  ? 0.23217   -13.86041 18.96951  1.000 29.09264 ? 44  THR A C   1 
ATOM   336  O  O   . THR A 1 44  ? 0.62239   -13.30526 20.00437  1.000 28.92861 ? 44  THR A O   1 
ATOM   337  C  CB  . THR A 1 44  ? 0.16602   -16.28427 19.63890  1.000 29.24619 ? 44  THR A CB  1 
ATOM   338  O  OG1 . THR A 1 44  ? 0.67486   -17.59117 19.32725  1.000 32.75308 ? 44  THR A OG1 1 
ATOM   339  C  CG2 . THR A 1 44  ? -1.35627  -16.32163 19.59329  1.000 32.01822 ? 44  THR A CG2 1 
ATOM   340  N  N   . LEU A 1 45  ? -0.60497  -13.28327 18.10511  1.000 28.42866 ? 45  LEU A N   1 
ATOM   341  C  CA  . LEU A 1 45  ? -1.10621  -11.93483 18.32283  1.000 28.23408 ? 45  LEU A CA  1 
ATOM   342  C  C   . LEU A 1 45  ? -2.34417  -11.97024 19.21747  1.000 31.14529 ? 45  LEU A C   1 
ATOM   343  O  O   . LEU A 1 45  ? -2.85297  -13.03782 19.57288  1.000 34.64957 ? 45  LEU A O   1 
ATOM   344  C  CB  . LEU A 1 45  ? -1.39440  -11.25097 16.98490  1.000 26.57967 ? 45  LEU A CB  1 
ATOM   345  C  CG  . LEU A 1 45  ? -0.18642  -11.15137 16.05440  1.000 28.70268 ? 45  LEU A CG  1 
ATOM   346  C  CD1 . LEU A 1 45  ? -0.54974  -10.37433 14.79710  1.000 28.03721 ? 45  LEU A CD1 1 
ATOM   347  C  CD2 . LEU A 1 45  ? 1.00485   -10.51002 16.76217  1.000 26.68854 ? 45  LEU A CD2 1 
ATOM   348  N  N   . TYR A 1 46  ? -2.84446  -10.78098 19.57443  1.000 32.88833 ? 46  TYR A N   1 
ATOM   349  C  CA  . TYR A 1 46  ? -3.84619  -10.66712 20.63328  1.000 32.32103 ? 46  TYR A CA  1 
ATOM   350  C  C   . TYR A 1 46  ? -5.09674  -11.48720 20.34366  1.000 36.95911 ? 46  TYR A C   1 
ATOM   351  O  O   . TYR A 1 46  ? -5.74925  -11.96694 21.27706  1.000 40.82456 ? 46  TYR A O   1 
ATOM   352  C  CB  . TYR A 1 46  ? -4.22739  -9.19822  20.84477  1.000 34.15660 ? 46  TYR A CB  1 
ATOM   353  C  CG  . TYR A 1 46  ? -5.17310  -8.65398  19.79586  1.000 37.23636 ? 46  TYR A CG  1 
ATOM   354  C  CD1 . TYR A 1 46  ? -4.69887  -8.19920  18.57297  1.000 37.81959 ? 46  TYR A CD1 1 
ATOM   355  C  CD2 . TYR A 1 46  ? -6.54298  -8.60046  20.02781  1.000 37.46416 ? 46  TYR A CD2 1 
ATOM   356  C  CE1 . TYR A 1 46  ? -5.56215  -7.70711  17.61161  1.000 39.13559 ? 46  TYR A CE1 1 
ATOM   357  C  CE2 . TYR A 1 46  ? -7.40961  -8.11673  19.07368  1.000 38.66346 ? 46  TYR A CE2 1 
ATOM   358  C  CZ  . TYR A 1 46  ? -6.91720  -7.66924  17.86892  1.000 41.56637 ? 46  TYR A CZ  1 
ATOM   359  O  OH  . TYR A 1 46  ? -7.78564  -7.18089  16.91792  1.000 43.58255 ? 46  TYR A OH  1 
ATOM   360  N  N   . ASP A 1 47  ? -5.45696  -11.64823 19.07397  1.000 40.29611 ? 47  ASP A N   1 
ATOM   361  C  CA  . ASP A 1 47  ? -6.67458  -12.35723 18.70523  1.000 39.73860 ? 47  ASP A CA  1 
ATOM   362  C  C   . ASP A 1 47  ? -6.44062  -13.83822 18.43360  1.000 42.90191 ? 47  ASP A C   1 
ATOM   363  O  O   . ASP A 1 47  ? -7.36015  -14.52215 17.97216  1.000 45.63202 ? 47  ASP A O   1 
ATOM   364  C  CB  . ASP A 1 47  ? -7.32509  -11.69439 17.48540  1.000 41.78777 ? 47  ASP A CB  1 
ATOM   365  C  CG  . ASP A 1 47  ? -6.40761  -11.64769 16.28207  1.000 43.81327 ? 47  ASP A CG  1 
ATOM   366  O  OD1 . ASP A 1 47  ? -5.21631  -12.00646 16.41392  1.000 40.26934 ? 47  ASP A OD1 1 
ATOM   367  O  OD2 . ASP A 1 47  ? -6.88410  -11.25433 15.19490  1.000 46.37723 ? 47  ASP A OD2 1 
ATOM   368  N  N   . GLY A 1 48  ? -5.24241  -14.34954 18.71632  1.000 41.37517 ? 48  GLY A N   1 
ATOM   369  C  CA  . GLY A 1 48  ? -4.93150  -15.74757 18.50893  1.000 40.11962 ? 48  GLY A CA  1 
ATOM   370  C  C   . GLY A 1 48  ? -4.32814  -16.08071 17.16186  1.000 39.68364 ? 48  GLY A C   1 
ATOM   371  O  O   . GLY A 1 48  ? -3.93711  -17.23406 16.94359  1.000 39.80098 ? 48  GLY A O   1 
ATOM   372  N  N   . ARG A 1 49  ? -4.23459  -15.11261 16.25803  1.000 39.35772 ? 49  ARG A N   1 
ATOM   373  C  CA  . ARG A 1 49  ? -3.66400  -15.34215 14.94071  1.000 39.80202 ? 49  ARG A CA  1 
ATOM   374  C  C   . ARG A 1 49  ? -2.14096  -15.36635 15.02466  1.000 35.75379 ? 49  ARG A C   1 
ATOM   375  O  O   . ARG A 1 49  ? -1.53231  -14.60687 15.78626  1.000 35.44468 ? 49  ARG A O   1 
ATOM   376  C  CB  . ARG A 1 49  ? -4.15272  -14.25443 13.98161  1.000 47.79888 ? 49  ARG A CB  1 
ATOM   377  C  CG  . ARG A 1 49  ? -3.32871  -14.02649 12.73241  1.000 57.38823 ? 49  ARG A CG  1 
ATOM   378  C  CD  . ARG A 1 49  ? -3.61433  -12.62768 12.19445  1.000 67.33375 ? 49  ARG A CD  1 
ATOM   379  N  NE  . ARG A 1 49  ? -3.83604  -11.69254 13.29294  1.000 74.24179 ? 49  ARG A NE  1 
ATOM   380  C  CZ  . ARG A 1 49  ? -3.80199  -10.37121 13.18445  1.000 78.12478 ? 49  ARG A CZ  1 
ATOM   381  N  NH1 . ARG A 1 49  ? -3.54584  -9.77845  12.02988  1.000 77.18418 ? 49  ARG A NH1 1 
ATOM   382  N  NH2 . ARG A 1 49  ? -4.02534  -9.62614  14.26474  1.000 79.41879 ? 49  ARG A NH2 1 
ATOM   383  N  N   . GLN A 1 50  ? -1.52661  -16.26228 14.25811  1.000 34.54128 ? 50  GLN A N   1 
ATOM   384  C  CA  . GLN A 1 50  ? -0.07857  -16.39299 14.25137  1.000 32.76092 ? 50  GLN A CA  1 
ATOM   385  C  C   . GLN A 1 50  ? 0.53971   -15.44763 13.22876  1.000 30.52867 ? 50  GLN A C   1 
ATOM   386  O  O   . GLN A 1 50  ? -0.04738  -15.15555 12.18236  1.000 34.81605 ? 50  GLN A O   1 
ATOM   387  C  CB  . GLN A 1 50  ? 0.33851   -17.83900 13.95611  1.000 36.15757 ? 50  GLN A CB  1 
ATOM   388  C  CG  . GLN A 1 50  ? 0.09388   -18.80649 15.11277  1.000 45.81336 ? 50  GLN A CG  1 
ATOM   389  C  CD  . GLN A 1 50  ? 0.97317   -20.05059 15.04307  1.000 50.86262 ? 50  GLN A CD  1 
ATOM   390  O  OE1 . GLN A 1 50  ? 1.59019   -20.33640 14.01048  1.000 50.95315 ? 50  GLN A OE1 1 
ATOM   391  N  NE2 . GLN A 1 50  ? 1.03767   -20.79506 16.14978  1.000 48.53046 ? 50  GLN A NE2 1 
ATOM   392  N  N   . ALA A 1 51  ? 1.73355   -14.95721 13.55361  1.000 26.91920 ? 51  ALA A N   1 
ATOM   393  C  CA  . ALA A 1 51  ? 2.49090   -14.08078 12.67532  1.000 24.26458 ? 51  ALA A CA  1 
ATOM   394  C  C   . ALA A 1 51  ? 3.96889   -14.39702 12.85135  1.000 24.87917 ? 51  ALA A C   1 
ATOM   395  O  O   . ALA A 1 51  ? 4.35886   -15.15445 13.74494  1.000 25.33665 ? 51  ALA A O   1 
ATOM   396  C  CB  . ALA A 1 51  ? 2.19444   -12.59939 12.96688  1.000 24.73275 ? 51  ALA A CB  1 
ATOM   397  N  N   . TRP A 1 52  ? 4.79075   -13.84761 11.96063  1.000 22.43473 ? 52  TRP A N   1 
ATOM   398  C  CA  . TRP A 1 52  ? 6.23975   -13.93217 12.07385  1.000 20.22632 ? 52  TRP A CA  1 
ATOM   399  C  C   . TRP A 1 52  ? 6.76916   -12.63929 12.66285  1.000 22.08185 ? 52  TRP A C   1 
ATOM   400  O  O   . TRP A 1 52  ? 6.25529   -11.55768 12.35698  1.000 24.55412 ? 52  TRP A O   1 
ATOM   401  C  CB  . TRP A 1 52  ? 6.91454   -14.14105 10.71658  1.000 23.08490 ? 52  TRP A CB  1 
ATOM   402  C  CG  . TRP A 1 52  ? 6.65304   -15.44588 10.04858  1.000 23.49953 ? 52  TRP A CG  1 
ATOM   403  C  CD1 . TRP A 1 52  ? 5.80655   -15.67324 9.00001   1.000 24.88501 ? 52  TRP A CD1 1 
ATOM   404  C  CD2 . TRP A 1 52  ? 7.24651   -16.71164 10.37015  1.000 24.32384 ? 52  TRP A CD2 1 
ATOM   405  N  NE1 . TRP A 1 52  ? 5.84498   -17.00009 8.64288   1.000 27.47683 ? 52  TRP A NE1 1 
ATOM   406  C  CE2 . TRP A 1 52  ? 6.71872   -17.66041 9.46941   1.000 27.46105 ? 52  TRP A CE2 1 
ATOM   407  C  CE3 . TRP A 1 52  ? 8.18217   -17.13122 11.32318  1.000 24.59571 ? 52  TRP A CE3 1 
ATOM   408  C  CZ2 . TRP A 1 52  ? 7.08651   -19.00949 9.50050   1.000 30.78547 ? 52  TRP A CZ2 1 
ATOM   409  C  CZ3 . TRP A 1 52  ? 8.54660   -18.47098 11.35786  1.000 27.10312 ? 52  TRP A CZ3 1 
ATOM   410  C  CH2 . TRP A 1 52  ? 7.99834   -19.39730 10.44868  1.000 27.84222 ? 52  TRP A CH2 1 
ATOM   411  N  N   . VAL A 1 53  ? 7.81626   -12.74779 13.47803  1.000 21.58528 ? 53  VAL A N   1 
ATOM   412  C  CA  . VAL A 1 53  ? 8.63770   -11.59663 13.84147  1.000 19.03003 ? 53  VAL A CA  1 
ATOM   413  C  C   . VAL A 1 53  ? 10.03994  -11.80867 13.28950  1.000 20.22489 ? 53  VAL A C   1 
ATOM   414  O  O   . VAL A 1 53  ? 10.52753  -12.94385 13.19663  1.000 21.65221 ? 53  VAL A O   1 
ATOM   415  C  CB  . VAL A 1 53  ? 8.68013   -11.34091 15.36434  1.000 20.51628 ? 53  VAL A CB  1 
ATOM   416  C  CG1 . VAL A 1 53  ? 7.32254   -10.90561 15.86126  1.000 23.07783 ? 53  VAL A CG1 1 
ATOM   417  C  CG2 . VAL A 1 53  ? 9.18786   -12.56663 16.12700  1.000 22.75641 ? 53  VAL A CG2 1 
ATOM   418  N  N   . VAL A 1 54  ? 10.66689  -10.71489 12.87765  1.000 19.41128 ? 54  VAL A N   1 
ATOM   419  C  CA  . VAL A 1 54  ? 12.05007  -10.70678 12.42644  1.000 20.74549 ? 54  VAL A CA  1 
ATOM   420  C  C   . VAL A 1 54  ? 12.89917  -10.24669 13.59683  1.000 21.69871 ? 54  VAL A C   1 
ATOM   421  O  O   . VAL A 1 54  ? 12.61749  -9.20829  14.20042  1.000 22.05073 ? 54  VAL A O   1 
ATOM   422  C  CB  . VAL A 1 54  ? 12.23276  -9.78382  11.21091  1.000 22.56949 ? 54  VAL A CB  1 
ATOM   423  C  CG1 . VAL A 1 54  ? 13.62838  -9.92395  10.63252  1.000 23.46155 ? 54  VAL A CG1 1 
ATOM   424  C  CG2 . VAL A 1 54  ? 11.16110  -10.06725 10.15612  1.000 21.69961 ? 54  VAL A CG2 1 
ATOM   425  N  N   . THR A 1 55  ? 13.92508  -11.02711 13.93536  1.000 22.04815 ? 55  THR A N   1 
ATOM   426  C  CA  . THR A 1 55  ? 14.64635  -10.83417 15.18383  1.000 22.17289 ? 55  THR A CA  1 
ATOM   427  C  C   . THR A 1 55  ? 16.13481  -10.58242 15.01411  1.000 25.35437 ? 55  THR A C   1 
ATOM   428  O  O   . THR A 1 55  ? 16.84726  -10.50147 16.02409  1.000 32.04694 ? 55  THR A O   1 
ATOM   429  C  CB  . THR A 1 55  ? 14.46653  -12.06181 16.08022  1.000 23.89346 ? 55  THR A CB  1 
ATOM   430  O  OG1 . THR A 1 55  ? 15.01417  -13.20812 15.41708  1.000 25.71856 ? 55  THR A OG1 1 
ATOM   431  C  CG2 . THR A 1 55  ? 12.98908  -12.30257 16.37430  1.000 24.53045 ? 55  THR A CG2 1 
ATOM   432  N  N   . LYS A 1 56  ? 16.62964  -10.48503 13.78249  1.000 22.04322 ? 56  LYS A N   1 
ATOM   433  C  CA  . LYS A 1 56  ? 18.04913  -10.32404 13.51138  1.000 20.79581 ? 56  LYS A CA  1 
ATOM   434  C  C   . LYS A 1 56  ? 18.25259  -9.12775  12.59491  1.000 19.44787 ? 56  LYS A C   1 
ATOM   435  O  O   . LYS A 1 56  ? 17.40321  -8.81929  11.75401  1.000 21.65764 ? 56  LYS A O   1 
ATOM   436  C  CB  . LYS A 1 56  ? 18.64829  -11.58308 12.86891  1.000 22.66966 ? 56  LYS A CB  1 
ATOM   437  C  CG  . LYS A 1 56  ? 18.38555  -12.87421 13.64084  1.000 25.24166 ? 56  LYS A CG  1 
ATOM   438  C  CD  . LYS A 1 56  ? 19.06785  -12.88136 15.00590  1.000 26.07838 ? 56  LYS A CD  1 
ATOM   439  C  CE  . LYS A 1 56  ? 18.91773  -14.22655 15.71957  1.000 26.32840 ? 56  LYS A CE  1 
ATOM   440  N  NZ  . LYS A 1 56  ? 17.53559  -14.46440 16.22697  1.000 27.22516 ? 56  LYS A NZ  1 
ATOM   441  N  N   . HIS A 1 57  ? 19.41586  -8.48845  12.73740  1.000 20.87536 ? 57  HIS A N   1 
ATOM   442  C  CA  . HIS A 1 57  ? 19.64584  -7.17656  12.13783  1.000 20.51901 ? 57  HIS A CA  1 
ATOM   443  C  C   . HIS A 1 57  ? 19.69067  -7.23492  10.61180  1.000 21.62434 ? 57  HIS A C   1 
ATOM   444  O  O   . HIS A 1 57  ? 18.99419  -6.46928  9.93645   1.000 22.54917 ? 57  HIS A O   1 
ATOM   445  C  CB  . HIS A 1 57  ? 20.94040  -6.58837  12.69315  1.000 19.21400 ? 57  HIS A CB  1 
ATOM   446  C  CG  . HIS A 1 57  ? 21.19212  -5.17514  12.27616  1.000 21.87913 ? 57  HIS A CG  1 
ATOM   447  N  ND1 . HIS A 1 57  ? 21.83686  -4.84519  11.10080  1.000 23.77297 ? 57  HIS A ND1 1 
ATOM   448  C  CD2 . HIS A 1 57  ? 20.89207  -4.00225  12.88529  1.000 23.01406 ? 57  HIS A CD2 1 
ATOM   449  C  CE1 . HIS A 1 57  ? 21.91264  -3.52918  11.00075  1.000 24.50285 ? 57  HIS A CE1 1 
ATOM   450  N  NE2 . HIS A 1 57  ? 21.35285  -2.99440  12.07319  1.000 23.78652 ? 57  HIS A NE2 1 
ATOM   451  N  N   . GLU A 1 58  ? 20.50845  -8.12051  10.03780  1.000 22.32261 ? 58  GLU A N   1 
ATOM   452  C  CA  . GLU A 1 58  ? 20.62159  -8.10134  8.57871   1.000 24.26737 ? 58  GLU A CA  1 
ATOM   453  C  C   . GLU A 1 58  ? 19.33623  -8.59123  7.91520   1.000 22.80792 ? 58  GLU A C   1 
ATOM   454  O  O   . GLU A 1 58  ? 18.90354  -8.02824  6.90291   1.000 22.24561 ? 58  GLU A O   1 
ATOM   455  C  CB  . GLU A 1 58  ? 21.83390  -8.90744  8.11328   1.000 30.79083 ? 58  GLU A CB  1 
ATOM   456  C  CG  . GLU A 1 58  ? 22.13200  -8.76767  6.60634   1.000 37.71433 ? 58  GLU A CG  1 
ATOM   457  C  CD  . GLU A 1 58  ? 22.19672  -7.31238  6.09664   1.000 42.15423 ? 58  GLU A CD  1 
ATOM   458  O  OE1 . GLU A 1 58  ? 22.66837  -6.41396  6.83087   1.000 39.80409 ? 58  GLU A OE1 1 
ATOM   459  O  OE2 . GLU A 1 58  ? 21.78383  -7.07162  4.93357   1.000 43.53244 ? 58  GLU A OE2 1 
ATOM   460  N  N   . ALA A 1 59  ? 18.69817  -9.61920  8.47865   1.000 21.05338 ? 59  ALA A N   1 
ATOM   461  C  CA  . ALA A 1 59  ? 17.41032  -10.06044 7.94813   1.000 20.95203 ? 59  ALA A CA  1 
ATOM   462  C  C   . ALA A 1 59  ? 16.36347  -8.96122  8.03416   1.000 21.16978 ? 59  ALA A C   1 
ATOM   463  O  O   . ALA A 1 59  ? 15.49287  -8.86040  7.16044   1.000 21.34336 ? 59  ALA A O   1 
ATOM   464  C  CB  . ALA A 1 59  ? 16.91538  -11.29142 8.69336   1.000 24.54460 ? 59  ALA A CB  1 
ATOM   465  N  N   . ALA A 1 60  ? 16.42836  -8.12849  9.07800   1.000 20.00280 ? 60  ALA A N   1 
ATOM   466  C  CA  . ALA A 1 60  ? 15.48255  -7.02479  9.18031   1.000 20.00120 ? 60  ALA A CA  1 
ATOM   467  C  C   . ALA A 1 60  ? 15.67625  -6.03273  8.03947   1.000 20.12938 ? 60  ALA A C   1 
ATOM   468  O  O   . ALA A 1 60  ? 14.69899  -5.59054  7.42924   1.000 19.87214 ? 60  ALA A O   1 
ATOM   469  C  CB  . ALA A 1 60  ? 15.62668  -6.33642  10.53727  1.000 19.23250 ? 60  ALA A CB  1 
ATOM   470  N  N   . ARG A 1 61  ? 16.93004  -5.67453  7.73153   1.000 20.34428 ? 61  ARG A N   1 
ATOM   471  C  CA  . ARG A 1 61  ? 17.18805  -4.80042  6.58710   1.000 21.51038 ? 61  ARG A CA  1 
ATOM   472  C  C   . ARG A 1 61  ? 16.71132  -5.43552  5.28999   1.000 20.14613 ? 61  ARG A C   1 
ATOM   473  O  O   . ARG A 1 61  ? 16.10710  -4.76571  4.44423   1.000 21.96506 ? 61  ARG A O   1 
ATOM   474  C  CB  . ARG A 1 61  ? 18.68017  -4.46491  6.47306   1.000 20.19458 ? 61  ARG A CB  1 
ATOM   475  C  CG  . ARG A 1 61  ? 19.18305  -3.49463  7.51641   1.000 21.87551 ? 61  ARG A CG  1 
ATOM   476  C  CD  . ARG A 1 61  ? 20.69145  -3.35527  7.44594   1.000 23.26818 ? 61  ARG A CD  1 
ATOM   477  N  NE  . ARG A 1 61  ? 21.18319  -2.76303  6.20226   1.000 24.39297 ? 61  ARG A NE  1 
ATOM   478  C  CZ  . ARG A 1 61  ? 21.76711  -1.57323  6.11733   1.000 21.26824 ? 61  ARG A CZ  1 
ATOM   479  N  NH1 . ARG A 1 61  ? 21.84087  -0.76235  7.16605   1.000 19.52925 ? 61  ARG A NH1 1 
ATOM   480  N  NH2 . ARG A 1 61  ? 22.32085  -1.20052  4.96078   1.000 21.62231 ? 61  ARG A NH2 1 
ATOM   481  N  N   . LYS A 1 62  ? 16.98947  -6.72330  5.10643   1.000 20.35605 ? 62  LYS A N   1 
ATOM   482  C  CA  . LYS A 1 62  ? 16.59190  -7.37536  3.86585   1.000 20.07009 ? 62  LYS A CA  1 
ATOM   483  C  C   . LYS A 1 62  ? 15.07922  -7.36334  3.70844   1.000 21.52651 ? 62  LYS A C   1 
ATOM   484  O  O   . LYS A 1 62  ? 14.55650  -7.05015  2.62943   1.000 23.48776 ? 62  LYS A O   1 
ATOM   485  C  CB  . LYS A 1 62  ? 17.13110  -8.80377  3.83741   1.000 24.96816 ? 62  LYS A CB  1 
ATOM   486  C  CG  . LYS A 1 62  ? 16.74753  -9.56273  2.58105   1.000 32.76479 ? 62  LYS A CG  1 
ATOM   487  C  CD  . LYS A 1 62  ? 17.60828  -10.80384 2.38004   1.000 39.59468 ? 62  LYS A CD  1 
ATOM   488  C  CE  . LYS A 1 62  ? 17.28867  -11.47813 1.04881   1.000 44.72773 ? 62  LYS A CE  1 
ATOM   489  N  NZ  . LYS A 1 62  ? 15.91814  -11.15383 0.55140   1.000 49.18951 ? 62  LYS A NZ  1 
ATOM   490  N  N   . LEU A 1 63  ? 14.35373  -7.67200  4.78182   1.000 20.15928 ? 63  LEU A N   1 
ATOM   491  C  CA  . LEU A 1 63  ? 12.90537  -7.76378  4.65149   1.000 19.05051 ? 63  LEU A CA  1 
ATOM   492  C  C   . LEU A 1 63  ? 12.23839  -6.39087  4.58506   1.000 19.76441 ? 63  LEU A C   1 
ATOM   493  O  O   . LEU A 1 63  ? 11.23377  -6.23783  3.88000   1.000 20.26493 ? 63  LEU A O   1 
ATOM   494  C  CB  . LEU A 1 63  ? 12.34351  -8.61193  5.79105   1.000 19.30225 ? 63  LEU A CB  1 
ATOM   495  C  CG  . LEU A 1 63  ? 12.64166  -10.10287 5.59150   1.000 18.71683 ? 63  LEU A CG  1 
ATOM   496  C  CD1 . LEU A 1 63  ? 12.31688  -10.89322 6.85632   1.000 19.45413 ? 63  LEU A CD1 1 
ATOM   497  C  CD2 . LEU A 1 63  ? 11.88501  -10.68066 4.37700   1.000 21.15105 ? 63  LEU A CD2 1 
ATOM   498  N  N   . LEU A 1 64  ? 12.77365  -5.37967  5.28123   1.000 17.92020 ? 64  LEU A N   1 
ATOM   499  C  CA  . LEU A 1 64  ? 12.24677  -4.02977  5.10864   1.000 17.03581 ? 64  LEU A CA  1 
ATOM   500  C  C   . LEU A 1 64  ? 12.48147  -3.50913  3.69406   1.000 19.75636 ? 64  LEU A C   1 
ATOM   501  O  O   . LEU A 1 64  ? 11.72896  -2.65563  3.20977   1.000 20.46032 ? 64  LEU A O   1 
ATOM   502  C  CB  . LEU A 1 64  ? 12.87810  -3.08167  6.13378   1.000 17.98203 ? 64  LEU A CB  1 
ATOM   503  C  CG  . LEU A 1 64  ? 12.33319  -3.26214  7.55105   1.000 16.81730 ? 64  LEU A CG  1 
ATOM   504  C  CD1 . LEU A 1 64  ? 13.19147  -2.52525  8.55742   1.000 19.58909 ? 64  LEU A CD1 1 
ATOM   505  C  CD2 . LEU A 1 64  ? 10.88542  -2.77748  7.62392   1.000 18.61734 ? 64  LEU A CD2 1 
ATOM   506  N  N   . GLY A 1 65  ? 13.50441  -4.01193  3.01202   1.000 19.04259 ? 65  GLY A N   1 
ATOM   507  C  CA  . GLY A 1 65  ? 13.73441  -3.61591  1.63722   1.000 20.81309 ? 65  GLY A CA  1 
ATOM   508  C  C   . GLY A 1 65  ? 13.01402  -4.44197  0.59477   1.000 19.62959 ? 65  GLY A C   1 
ATOM   509  O  O   . GLY A 1 65  ? 13.08117  -4.12075  -0.60006  1.000 23.09090 ? 65  GLY A O   1 
ATOM   510  N  N   . ASP A 1 66  ? 12.31498  -5.49526  1.01239   1.000 19.90211 ? 66  ASP A N   1 
ATOM   511  C  CA  . ASP A 1 66  ? 11.70977  -6.44016  0.07504   1.000 20.62833 ? 66  ASP A CA  1 
ATOM   512  C  C   . ASP A 1 66  ? 10.32286  -5.94492  -0.31152  1.000 22.02106 ? 66  ASP A C   1 
ATOM   513  O  O   . ASP A 1 66  ? 9.44403   -5.88625  0.55236   1.000 24.40020 ? 66  ASP A O   1 
ATOM   514  C  CB  . ASP A 1 66  ? 11.62000  -7.82255  0.71532   1.000 21.62929 ? 66  ASP A CB  1 
ATOM   515  C  CG  . ASP A 1 66  ? 11.25284  -8.92171  -0.27355  1.000 25.15838 ? 66  ASP A CG  1 
ATOM   516  O  OD1 . ASP A 1 66  ? 10.53408  -8.65282  -1.25489  1.000 25.61537 ? 66  ASP A OD1 1 
ATOM   517  O  OD2 . ASP A 1 66  ? 11.67207  -10.07610 -0.04732  1.000 30.43215 ? 66  ASP A OD2 1 
ATOM   518  N  N   . PRO A 1 67  ? 10.07149  -5.59213  -1.57966  1.000 23.63499 ? 67  PRO A N   1 
ATOM   519  C  CA  . PRO A 1 67  ? 8.74595   -5.05943  -1.94041  1.000 23.08623 ? 67  PRO A CA  1 
ATOM   520  C  C   . PRO A 1 67  ? 7.61998   -6.07279  -1.81938  1.000 24.10026 ? 67  PRO A C   1 
ATOM   521  O  O   . PRO A 1 67  ? 6.44710   -5.67934  -1.89611  1.000 23.81788 ? 67  PRO A O   1 
ATOM   522  C  CB  . PRO A 1 67  ? 8.92972   -4.60339  -3.39494  1.000 26.89567 ? 67  PRO A CB  1 
ATOM   523  C  CG  . PRO A 1 67  ? 10.06935  -5.41832  -3.90989  1.000 27.80044 ? 67  PRO A CG  1 
ATOM   524  C  CD  . PRO A 1 67  ? 10.98471  -5.64095  -2.73560  1.000 26.36720 ? 67  PRO A CD  1 
ATOM   525  N  N   . ARG A 1 68  ? 7.93290   -7.35462  -1.63928  1.000 23.47235 ? 68  ARG A N   1 
ATOM   526  C  CA  . ARG A 1 68  ? 6.90038   -8.35445  -1.39783  1.000 22.17657 ? 68  ARG A CA  1 
ATOM   527  C  C   . ARG A 1 68  ? 6.32890   -8.28145  0.00978   1.000 23.23021 ? 68  ARG A C   1 
ATOM   528  O  O   . ARG A 1 68  ? 5.32306   -8.94491  0.28033   1.000 24.29724 ? 68  ARG A O   1 
ATOM   529  C  CB  . ARG A 1 68  ? 7.45083   -9.75419  -1.65669  1.000 24.24213 ? 68  ARG A CB  1 
ATOM   530  C  CG  . ARG A 1 68  ? 7.83148   -10.00228 -3.10397  1.000 27.31959 ? 68  ARG A CG  1 
ATOM   531  C  CD  . ARG A 1 68  ? 8.58333   -11.31364 -3.25622  1.000 28.25060 ? 68  ARG A CD  1 
ATOM   532  N  NE  . ARG A 1 68  ? 9.85624   -11.30586 -2.54402  1.000 28.34176 ? 68  ARG A NE  1 
ATOM   533  C  CZ  . ARG A 1 68  ? 10.72536  -12.30673 -2.55961  1.000 29.87815 ? 68  ARG A CZ  1 
ATOM   534  N  NH1 . ARG A 1 68  ? 10.49018  -13.41442 -3.24553  1.000 33.35507 ? 68  ARG A NH1 1 
ATOM   535  N  NH2 . ARG A 1 68  ? 11.86302  -12.19037 -1.87934  1.000 30.18079 ? 68  ARG A NH2 1 
ATOM   536  N  N   . LEU A 1 69  ? 6.94353   -7.51128  0.91049   1.000 21.08938 ? 69  LEU A N   1 
ATOM   537  C  CA  . LEU A 1 69  ? 6.37009   -7.22775  2.22702   1.000 19.78240 ? 69  LEU A CA  1 
ATOM   538  C  C   . LEU A 1 69  ? 5.69895   -5.86073  2.15125   1.000 18.37268 ? 69  LEU A C   1 
ATOM   539  O  O   . LEU A 1 69  ? 6.36628   -4.82416  2.21136   1.000 21.44216 ? 69  LEU A O   1 
ATOM   540  C  CB  . LEU A 1 69  ? 7.43050   -7.26655  3.32300   1.000 20.06703 ? 69  LEU A CB  1 
ATOM   541  C  CG  . LEU A 1 69  ? 7.82379   -8.62525  3.89548   1.000 24.23389 ? 69  LEU A CG  1 
ATOM   542  C  CD1 . LEU A 1 69  ? 8.70632   -8.42727  5.12244   1.000 26.31992 ? 69  LEU A CD1 1 
ATOM   543  C  CD2 . LEU A 1 69  ? 6.58733   -9.46157  4.23887   1.000 23.43365 ? 69  LEU A CD2 1 
ATOM   544  N  N   . SER A 1 70  ? 4.37416   -5.86905  2.02831   1.000 19.86825 ? 70  SER A N   1 
ATOM   545  C  CA  . SER A 1 70  ? 3.58354   -4.66045  1.83270   1.000 21.25748 ? 70  SER A CA  1 
ATOM   546  C  C   . SER A 1 70  ? 3.28878   -3.96147  3.16021   1.000 18.76281 ? 70  SER A C   1 
ATOM   547  O  O   . SER A 1 70  ? 3.17138   -4.59584  4.21365   1.000 20.26198 ? 70  SER A O   1 
ATOM   548  C  CB  . SER A 1 70  ? 2.27412   -5.01830  1.12318   1.000 21.83139 ? 70  SER A CB  1 
ATOM   549  O  OG  . SER A 1 70  ? 1.30983   -3.98781  1.22611   1.000 22.61422 ? 70  SER A OG  1 
ATOM   550  N  N   . SER A 1 71  ? 3.15074   -2.63607  3.09399   1.000 20.45940 ? 71  SER A N   1 
ATOM   551  C  CA  . SER A 1 71  ? 2.81418   -1.80819  4.24679   1.000 18.39618 ? 71  SER A CA  1 
ATOM   552  C  C   . SER A 1 71  ? 1.32777   -1.47629  4.31721   1.000 20.57853 ? 71  SER A C   1 
ATOM   553  O  O   . SER A 1 71  ? 0.93086   -0.61398  5.10360   1.000 21.89582 ? 71  SER A O   1 
ATOM   554  C  CB  . SER A 1 71  ? 3.63015   -0.51600  4.21127   1.000 18.92143 ? 71  SER A CB  1 
ATOM   555  O  OG  . SER A 1 71  ? 4.97990   -0.77556  4.53227   1.000 19.09588 ? 71  SER A OG  1 
ATOM   556  N  N   . ASN A 1 72  ? 0.50122   -2.13974  3.51862   1.000 23.09583 ? 72  ASN A N   1 
ATOM   557  C  CA  . ASN A 1 72  ? -0.92120  -1.81097  3.39640   1.000 24.44898 ? 72  ASN A CA  1 
ATOM   558  C  C   . ASN A 1 72  ? -1.68176  -2.23626  4.65310   1.000 24.33138 ? 72  ASN A C   1 
ATOM   559  O  O   . ASN A 1 72  ? -2.03065  -3.40574  4.81554   1.000 24.94140 ? 72  ASN A O   1 
ATOM   560  C  CB  . ASN A 1 72  ? -1.47869  -2.49269  2.15127   1.000 25.18341 ? 72  ASN A CB  1 
ATOM   561  C  CG  . ASN A 1 72  ? -2.95488  -2.21923  1.93255   1.000 26.32224 ? 72  ASN A CG  1 
ATOM   562  O  OD1 . ASN A 1 72  ? -3.54622  -1.35475  2.57597   1.000 26.00048 ? 72  ASN A OD1 1 
ATOM   563  N  ND2 . ASN A 1 72  ? -3.55332  -2.95204  1.00149   1.000 30.28155 ? 72  ASN A ND2 1 
ATOM   564  N  N   . ARG A 1 73  ? -1.98754  -1.27822  5.53447   1.000 23.33045 ? 73  ARG A N   1 
ATOM   565  C  CA  . ARG A 1 73  ? -2.69876  -1.60549  6.76883   1.000 25.16298 ? 73  ARG A CA  1 
ATOM   566  C  C   . ARG A 1 73  ? -4.14555  -2.02518  6.53742   1.000 28.29396 ? 73  ARG A C   1 
ATOM   567  O  O   . ARG A 1 73  ? -4.74434  -2.62963  7.43381   1.000 29.58369 ? 73  ARG A O   1 
ATOM   568  C  CB  . ARG A 1 73  ? -2.68895  -0.41905  7.73824   1.000 28.74449 ? 73  ARG A CB  1 
ATOM   569  C  CG  . ARG A 1 73  ? -1.40803  -0.24121  8.51896   1.000 31.55753 ? 73  ARG A CG  1 
ATOM   570  C  CD  . ARG A 1 73  ? -0.43162  0.65047   7.79695   1.000 31.23278 ? 73  ARG A CD  1 
ATOM   571  N  NE  . ARG A 1 73  ? 0.62867   1.08555   8.69675   1.000 32.16123 ? 73  ARG A NE  1 
ATOM   572  C  CZ  . ARG A 1 73  ? 0.54390   2.13710   9.50031   1.000 32.77501 ? 73  ARG A CZ  1 
ATOM   573  N  NH1 . ARG A 1 73  ? -0.53478  2.90602   9.52502   1.000 33.55134 ? 73  ARG A NH1 1 
ATOM   574  N  NH2 . ARG A 1 73  ? 1.56659   2.42544   10.29862  1.000 30.34439 ? 73  ARG A NH2 1 
ATOM   575  N  N   . THR A 1 74  ? -4.73649  -1.69369  5.38621   1.000 29.08905 ? 74  THR A N   1 
ATOM   576  C  CA  . THR A 1 74  ? -6.11398  -2.10013  5.12289   1.000 31.83338 ? 74  THR A CA  1 
ATOM   577  C  C   . THR A 1 74  ? -6.22806  -3.54999  4.66802   1.000 30.32477 ? 74  THR A C   1 
ATOM   578  O  O   . THR A 1 74  ? -7.34829  -4.04608  4.52072   1.000 33.35513 ? 74  THR A O   1 
ATOM   579  C  CB  . THR A 1 74  ? -6.76325  -1.19750  4.06922   1.000 33.79545 ? 74  THR A CB  1 
ATOM   580  O  OG1 . THR A 1 74  ? -6.19420  -1.47049  2.78326   1.000 35.02971 ? 74  THR A OG1 1 
ATOM   581  C  CG2 . THR A 1 74  ? -6.56121  0.27672   4.41696   1.000 31.97504 ? 74  THR A CG2 1 
ATOM   582  N  N   . ASP A 1 75  ? -5.11007  -4.23325  4.43655   1.000 31.00941 ? 75  ASP A N   1 
ATOM   583  C  CA  . ASP A 1 75  ? -5.15615  -5.63706  4.06289   1.000 31.83688 ? 75  ASP A CA  1 
ATOM   584  C  C   . ASP A 1 75  ? -5.68859  -6.46891  5.22585   1.000 32.17278 ? 75  ASP A C   1 
ATOM   585  O  O   . ASP A 1 75  ? -5.31784  -6.25433  6.38354   1.000 28.82291 ? 75  ASP A O   1 
ATOM   586  C  CB  . ASP A 1 75  ? -3.76084  -6.11023  3.64737   1.000 32.31885 ? 75  ASP A CB  1 
ATOM   587  C  CG  . ASP A 1 75  ? -3.76460  -7.50865  3.06848   1.000 36.91116 ? 75  ASP A CG  1 
ATOM   588  O  OD1 . ASP A 1 75  ? -3.96470  -8.46934  3.83464   1.000 34.06349 ? 75  ASP A OD1 1 
ATOM   589  O  OD2 . ASP A 1 75  ? -3.57069  -7.64443  1.84404   1.000 43.48808 ? 75  ASP A OD2 1 
ATOM   590  N  N   . ASP A 1 76  ? -6.58157  -7.41277  4.91365   1.000 35.52178 ? 76  ASP A N   1 
ATOM   591  C  CA  . ASP A 1 76  ? -7.20809  -8.22404  5.95603   1.000 39.60766 ? 76  ASP A CA  1 
ATOM   592  C  C   . ASP A 1 76  ? -6.20134  -9.03073  6.76273   1.000 37.10454 ? 76  ASP A C   1 
ATOM   593  O  O   . ASP A 1 76  ? -6.50718  -9.43009  7.89401   1.000 39.56315 ? 76  ASP A O   1 
ATOM   594  C  CB  . ASP A 1 76  ? -8.23880  -9.17965  5.35147   1.000 44.24974 ? 76  ASP A CB  1 
ATOM   595  C  CG  . ASP A 1 76  ? -9.48805  -8.47015  4.88927   1.000 54.38512 ? 76  ASP A CG  1 
ATOM   596  O  OD1 . ASP A 1 76  ? -9.84390  -8.60933  3.70242   1.000 58.85236 ? 76  ASP A OD1 1 
ATOM   597  O  OD2 . ASP A 1 76  ? -10.10547 -7.76026  5.71241   1.000 57.76321 ? 76  ASP A OD2 1 
ATOM   598  N  N   . ASN A 1 77  ? -5.01477  -9.28148  6.21480   1.000 34.48361 ? 77  ASN A N   1 
ATOM   599  C  CA  . ASN A 1 77  ? -4.00223  -10.08696 6.87901   1.000 32.82889 ? 77  ASN A CA  1 
ATOM   600  C  C   . ASN A 1 77  ? -2.89015  -9.25755  7.50607   1.000 29.84693 ? 77  ASN A C   1 
ATOM   601  O  O   . ASN A 1 77  ? -1.91095  -9.83052  7.99451   1.000 29.13568 ? 77  ASN A O   1 
ATOM   602  C  CB  . ASN A 1 77  ? -3.40863  -11.09084 5.89286   1.000 34.54223 ? 77  ASN A CB  1 
ATOM   603  C  CG  . ASN A 1 77  ? -4.40635  -12.13891 5.47327   1.000 38.69028 ? 77  ASN A CG  1 
ATOM   604  O  OD1 . ASN A 1 77  ? -5.08764  -12.72345 6.31123   1.000 39.13340 ? 77  ASN A OD1 1 
ATOM   605  N  ND2 . ASN A 1 77  ? -4.51618  -12.36993 4.17013   1.000 38.93816 ? 77  ASN A ND2 1 
ATOM   606  N  N   . PHE A 1 78  ? -3.01462  -7.93358  7.51219   1.000 27.85536 ? 78  PHE A N   1 
ATOM   607  C  CA  . PHE A 1 78  ? -2.00557  -7.11676  8.16458   1.000 25.57604 ? 78  PHE A CA  1 
ATOM   608  C  C   . PHE A 1 78  ? -1.97099  -7.44767  9.65714   1.000 25.76261 ? 78  PHE A C   1 
ATOM   609  O  O   . PHE A 1 78  ? -3.02582  -7.63782  10.27583  1.000 29.02776 ? 78  PHE A O   1 
ATOM   610  C  CB  . PHE A 1 78  ? -2.29005  -5.63113  7.95131   1.000 26.45521 ? 78  PHE A CB  1 
ATOM   611  C  CG  . PHE A 1 78  ? -1.15550  -4.74699  8.35850   1.000 24.62516 ? 78  PHE A CG  1 
ATOM   612  C  CD1 . PHE A 1 78  ? -1.03994  -4.31482  9.66421   1.000 25.45316 ? 78  PHE A CD1 1 
ATOM   613  C  CD2 . PHE A 1 78  ? -0.19034  -4.36996  7.44375   1.000 27.57090 ? 78  PHE A CD2 1 
ATOM   614  C  CE1 . PHE A 1 78  ? 0.00460   -3.50980  10.04592  1.000 28.35005 ? 78  PHE A CE1 1 
ATOM   615  C  CE2 . PHE A 1 78  ? 0.86110   -3.56452  7.82918   1.000 26.49640 ? 78  PHE A CE2 1 
ATOM   616  C  CZ  . PHE A 1 78  ? 0.95200   -3.13767  9.12876   1.000 28.69034 ? 78  PHE A CZ  1 
ATOM   617  N  N   . PRO A 1 79  ? -0.78294  -7.55270  10.26215  1.000 24.44977 ? 79  PRO A N   1 
ATOM   618  C  CA  . PRO A 1 79  ? -0.70583  -8.03324  11.64914  1.000 25.65506 ? 79  PRO A CA  1 
ATOM   619  C  C   . PRO A 1 79  ? -1.11331  -6.98486  12.67600  1.000 30.91421 ? 79  PRO A C   1 
ATOM   620  O  O   . PRO A 1 79  ? -0.28803  -6.17948  13.10917  1.000 36.15091 ? 79  PRO A O   1 
ATOM   621  C  CB  . PRO A 1 79  ? 0.76976   -8.42218  11.79521  1.000 24.73192 ? 79  PRO A CB  1 
ATOM   622  C  CG  . PRO A 1 79  ? 1.48422   -7.51275  10.82671  1.000 23.64516 ? 79  PRO A CG  1 
ATOM   623  C  CD  . PRO A 1 79  ? 0.55034   -7.39301  9.65512   1.000 24.93248 ? 79  PRO A CD  1 
ATOM   624  N  N   . ALA A 1 80  ? -2.37913  -7.00583  13.08758  1.000 34.55052 ? 80  ALA A N   1 
ATOM   625  C  CA  . ALA A 1 80  ? -2.85076  -6.13521  14.15856  1.000 36.03136 ? 80  ALA A CA  1 
ATOM   626  C  C   . ALA A 1 80  ? -2.34234  -6.63032  15.50400  1.000 33.35027 ? 80  ALA A C   1 
ATOM   627  O  O   . ALA A 1 80  ? -2.45495  -7.81795  15.81297  1.000 35.61599 ? 80  ALA A O   1 
ATOM   628  C  CB  . ALA A 1 80  ? -4.37588  -6.10167  14.17009  1.000 36.95059 ? 80  ALA A CB  1 
ATOM   629  N  N   . THR A 1 81  ? -1.80325  -5.72180  16.32519  1.000 33.54671 ? 81  THR A N   1 
ATOM   630  C  CA  . THR A 1 81  ? -1.29502  -6.12514  17.62960  1.000 31.30526 ? 81  THR A CA  1 
ATOM   631  C  C   . THR A 1 81  ? -2.19875  -5.73274  18.78930  1.000 31.71748 ? 81  THR A C   1 
ATOM   632  O  O   . THR A 1 81  ? -1.93761  -6.15329  19.92115  1.000 31.33291 ? 81  THR A O   1 
ATOM   633  C  CB  . THR A 1 81  ? 0.11377   -5.56242  17.86813  1.000 28.51597 ? 81  THR A CB  1 
ATOM   634  O  OG1 . THR A 1 81  ? 0.10613   -4.14131  17.69631  1.000 32.70250 ? 81  THR A OG1 1 
ATOM   635  C  CG2 . THR A 1 81  ? 1.09855   -6.19717  16.89550  1.000 28.15788 ? 81  THR A CG2 1 
ATOM   636  N  N   . SER A 1 82  ? -3.24634  -4.95469  18.54711  1.000 30.42657 ? 82  SER A N   1 
ATOM   637  C  CA  . SER A 1 82  ? -4.25057  -4.68470  19.56321  1.000 34.02418 ? 82  SER A CA  1 
ATOM   638  C  C   . SER A 1 82  ? -5.57944  -4.45797  18.86309  1.000 37.71921 ? 82  SER A C   1 
ATOM   639  O  O   . SER A 1 82  ? -5.60974  -4.20862  17.65122  1.000 37.64341 ? 82  SER A O   1 
ATOM   640  C  CB  . SER A 1 82  ? -3.87194  -3.46968  20.42061  1.000 34.97257 ? 82  SER A CB  1 
ATOM   641  O  OG  . SER A 1 82  ? -4.05662  -2.26901  19.69910  1.000 40.98772 ? 82  SER A OG  1 
ATOM   642  N  N   . PRO A 1 83  ? -6.69956  -4.55529  19.58973  1.000 41.61068 ? 83  PRO A N   1 
ATOM   643  C  CA  . PRO A 1 83  ? -7.99619  -4.24784  18.96381  1.000 42.38864 ? 83  PRO A CA  1 
ATOM   644  C  C   . PRO A 1 83  ? -8.05711  -2.84706  18.38759  1.000 41.55598 ? 83  PRO A C   1 
ATOM   645  O  O   . PRO A 1 83  ? -8.80694  -2.60823  17.43301  1.000 43.58838 ? 83  PRO A O   1 
ATOM   646  C  CB  . PRO A 1 83  ? -8.99698  -4.42845  20.11572  1.000 41.84819 ? 83  PRO A CB  1 
ATOM   647  C  CG  . PRO A 1 83  ? -8.32306  -5.35236  21.06608  1.000 42.30424 ? 83  PRO A CG  1 
ATOM   648  C  CD  . PRO A 1 83  ? -6.85370  -5.07013  20.96352  1.000 41.91106 ? 83  PRO A CD  1 
ATOM   649  N  N   . ALA A 1 84  ? -7.27162  -1.91323  18.92698  1.000 42.02781 ? 84  ALA A N   1 
ATOM   650  C  CA  . ALA A 1 84  ? -7.30427  -0.54112  18.44066  1.000 42.64277 ? 84  ALA A CA  1 
ATOM   651  C  C   . ALA A 1 84  ? -6.78683  -0.41197  17.01585  1.000 45.98717 ? 84  ALA A C   1 
ATOM   652  O  O   . ALA A 1 84  ? -7.09535  0.58407   16.35337  1.000 45.03361 ? 84  ALA A O   1 
ATOM   653  C  CB  . ALA A 1 84  ? -6.49812  0.36634   19.36866  1.000 41.28104 ? 84  ALA A CB  1 
ATOM   654  N  N   . PHE A 1 85  ? -6.01274  -1.38861  16.52916  1.000 48.11170 ? 85  PHE A N   1 
ATOM   655  C  CA  . PHE A 1 85  ? -5.53136  -1.31932  15.15340  1.000 52.15597 ? 85  PHE A CA  1 
ATOM   656  C  C   . PHE A 1 85  ? -6.67575  -1.32269  14.15188  1.000 55.18021 ? 85  PHE A C   1 
ATOM   657  O  O   . PHE A 1 85  ? -6.55779  -0.71698  13.08028  1.000 52.76967 ? 85  PHE A O   1 
ATOM   658  C  CB  . PHE A 1 85  ? -4.58887  -2.47727  14.83523  1.000 56.23819 ? 85  PHE A CB  1 
ATOM   659  C  CG  . PHE A 1 85  ? -4.20315  -2.53937  13.38092  1.000 59.56147 ? 85  PHE A CG  1 
ATOM   660  C  CD1 . PHE A 1 85  ? -3.14293  -1.78934  12.90406  1.000 59.45400 ? 85  PHE A CD1 1 
ATOM   661  C  CD2 . PHE A 1 85  ? -4.92932  -3.31265  12.48242  1.000 60.66362 ? 85  PHE A CD2 1 
ATOM   662  C  CE1 . PHE A 1 85  ? -2.80157  -1.82833  11.57201  1.000 58.69853 ? 85  PHE A CE1 1 
ATOM   663  C  CE2 . PHE A 1 85  ? -4.58993  -3.35547  11.14937  1.000 59.77551 ? 85  PHE A CE2 1 
ATOM   664  C  CZ  . PHE A 1 85  ? -3.53111  -2.60961  10.69406  1.000 59.32860 ? 85  PHE A CZ  1 
ATOM   665  N  N   . GLU A 1 86  ? -7.77764  -2.01230  14.46592  1.000 58.31556 ? 86  GLU A N   1 
ATOM   666  C  CA  . GLU A 1 86  ? -8.90108  -2.07872  13.53665  1.000 61.01821 ? 86  GLU A CA  1 
ATOM   667  C  C   . GLU A 1 86  ? -9.42023  -0.69671  13.16583  1.000 61.14615 ? 86  GLU A C   1 
ATOM   668  O  O   . GLU A 1 86  ? -10.11726 -0.55831  12.15479  1.000 62.33886 ? 86  GLU A O   1 
ATOM   669  C  CB  . GLU A 1 86  ? -10.02956 -2.92459  14.13026  1.000 64.05426 ? 86  GLU A CB  1 
ATOM   670  C  CG  . GLU A 1 86  ? -9.59752  -4.32263  14.55277  1.000 68.40956 ? 86  GLU A CG  1 
ATOM   671  C  CD  . GLU A 1 86  ? -8.99409  -5.12554  13.41386  1.000 72.16003 ? 86  GLU A CD  1 
ATOM   672  O  OE1 . GLU A 1 86  ? -9.44627  -4.96716  12.25771  1.000 74.10788 ? 86  GLU A OE1 1 
ATOM   673  O  OE2 . GLU A 1 86  ? -8.06062  -5.91524  13.67477  1.000 71.90817 ? 86  GLU A OE2 1 
ATOM   674  N  N   . ALA A 1 87  ? -9.09051  0.32564   13.95884  1.000 60.17901 ? 87  ALA A N   1 
ATOM   675  C  CA  . ALA A 1 87  ? -9.40763  1.69698   13.58152  1.000 58.02830 ? 87  ALA A CA  1 
ATOM   676  C  C   . ALA A 1 87  ? -8.60580  2.13676   12.36357  1.000 61.83286 ? 87  ALA A C   1 
ATOM   677  O  O   . ALA A 1 87  ? -9.12124  2.86236   11.50517  1.000 64.13156 ? 87  ALA A O   1 
ATOM   678  C  CB  . ALA A 1 87  ? -9.14967  2.63470   14.75952  1.000 58.75853 ? 87  ALA A CB  1 
ATOM   679  N  N   . VAL A 1 88  ? -7.34278  1.71208   12.27291  1.000 63.04121 ? 88  VAL A N   1 
ATOM   680  C  CA  . VAL A 1 88  ? -6.50906  2.08586   11.13426  1.000 65.90903 ? 88  VAL A CA  1 
ATOM   681  C  C   . VAL A 1 88  ? -6.85953  1.25709   9.90138   1.000 65.40224 ? 88  VAL A C   1 
ATOM   682  O  O   . VAL A 1 88  ? -6.78386  1.75742   8.77363   1.000 64.19994 ? 88  VAL A O   1 
ATOM   683  C  CB  . VAL A 1 88  ? -5.01804  1.95073   11.49487  1.000 69.57975 ? 88  VAL A CB  1 
ATOM   684  C  CG1 . VAL A 1 88  ? -4.14091  2.54947   10.39998  1.000 69.38123 ? 88  VAL A CG1 1 
ATOM   685  C  CG2 . VAL A 1 88  ? -4.72993  2.61144   12.83747  1.000 70.73393 ? 88  VAL A CG2 1 
ATOM   686  N  N   . ARG A 1 89  ? -7.24361  -0.01018  10.08563  1.000 67.53989 ? 89  ARG A N   1 
ATOM   687  C  CA  . ARG A 1 89  ? -7.66382  -0.82822  8.95163   1.000 69.83391 ? 89  ARG A CA  1 
ATOM   688  C  C   . ARG A 1 89  ? -8.91087  -0.25762  8.28435   1.000 72.30563 ? 89  ARG A C   1 
ATOM   689  O  O   . ARG A 1 89  ? -9.11294  -0.44386  7.07874   1.000 72.35297 ? 89  ARG A O   1 
ATOM   690  C  CB  . ARG A 1 89  ? -7.90595  -2.27341  9.40533   1.000 68.99582 ? 89  ARG A CB  1 
ATOM   691  C  CG  . ARG A 1 89  ? -8.29980  -3.22476  8.27943   1.000 68.95223 ? 89  ARG A CG  1 
ATOM   692  C  CD  . ARG A 1 89  ? -8.52053  -4.65465  8.76003   1.000 70.45153 ? 89  ARG A CD  1 
ATOM   693  N  NE  . ARG A 1 89  ? -7.30056  -5.45470  8.72446   1.000 72.63055 ? 89  ARG A NE  1 
ATOM   694  C  CZ  . ARG A 1 89  ? -6.70556  -5.97101  9.79246   1.000 72.80527 ? 89  ARG A CZ  1 
ATOM   695  N  NH1 . ARG A 1 89  ? -7.19424  -5.79648  11.00949  1.000 73.77132 ? 89  ARG A NH1 1 
ATOM   696  N  NH2 . ARG A 1 89  ? -5.59725  -6.68957  9.63425   1.000 69.21247 ? 89  ARG A NH2 1 
ATOM   697  N  N   . GLU A 1 90  ? -9.74297  0.45558   9.04201   1.000 74.63230 ? 90  GLU A N   1 
ATOM   698  C  CA  . GLU A 1 90  ? -10.98097 1.01808   8.51902   1.000 77.41887 ? 90  GLU A CA  1 
ATOM   699  C  C   . GLU A 1 90  ? -10.82044 2.41985   7.94848   1.000 73.18047 ? 90  GLU A C   1 
ATOM   700  O  O   . GLU A 1 90  ? -11.70052 2.87468   7.20884   1.000 73.25411 ? 90  GLU A O   1 
ATOM   701  C  CB  . GLU A 1 90  ? -12.04547 1.05236   9.62071   1.000 83.47568 ? 90  GLU A CB  1 
ATOM   702  C  CG  . GLU A 1 90  ? -12.84260 -0.22645  9.74238   1.000 89.55977 ? 90  GLU A CG  1 
ATOM   703  C  CD  . GLU A 1 90  ? -13.76660 -0.43304  8.56162   1.000 95.22614 ? 90  GLU A CD  1 
ATOM   704  O  OE1 . GLU A 1 90  ? -14.65996 0.41537   8.35055   1.000 96.65425 ? 90  GLU A OE1 1 
ATOM   705  O  OE2 . GLU A 1 90  ? -13.59000 -1.43360  7.83560   1.000 97.29707 ? 90  GLU A OE2 1 
ATOM   706  N  N   . SER A 1 91  ? -9.72937  3.10306   8.25987   1.000 68.98014 ? 91  SER A N   1 
ATOM   707  C  CA  . SER A 1 91  ? -9.57276  4.52217   7.98720   1.000 64.25408 ? 91  SER A CA  1 
ATOM   708  C  C   . SER A 1 91  ? -8.73813  4.75983   6.73443   1.000 58.67177 ? 91  SER A C   1 
ATOM   709  O  O   . SER A 1 91  ? -8.00100  3.87672   6.28574   1.000 56.09341 ? 91  SER A O   1 
ATOM   710  C  CB  . SER A 1 91  ? -8.91539  5.20843   9.19009   1.000 65.14985 ? 91  SER A CB  1 
ATOM   711  O  OG  . SER A 1 91  ? -9.66229  4.97606   10.37334  1.000 64.32964 ? 91  SER A OG  1 
ATOM   712  N  N   . PRO A 1 92  ? -8.83955  5.94771   6.13279   1.000 52.20554 ? 92  PRO A N   1 
ATOM   713  C  CA  . PRO A 1 92  ? -7.94701  6.28822   5.01826   1.000 49.15786 ? 92  PRO A CA  1 
ATOM   714  C  C   . PRO A 1 92  ? -6.49203  6.27422   5.46429   1.000 45.61050 ? 92  PRO A C   1 
ATOM   715  O  O   . PRO A 1 92  ? -6.17921  6.35022   6.65612   1.000 49.91124 ? 92  PRO A O   1 
ATOM   716  C  CB  . PRO A 1 92  ? -8.39681  7.69780   4.61816   1.000 49.40625 ? 92  PRO A CB  1 
ATOM   717  C  CG  . PRO A 1 92  ? -9.80137  7.80106   5.11594   1.000 49.95516 ? 92  PRO A CG  1 
ATOM   718  C  CD  . PRO A 1 92  ? -9.83850  7.00231   6.38037   1.000 50.21776 ? 92  PRO A CD  1 
ATOM   719  N  N   . GLN A 1 93  ? -5.58852  6.16825   4.49162   1.000 35.37392 ? 93  GLN A N   1 
ATOM   720  C  CA  . GLN A 1 93  ? -4.18639  5.90545   4.79355   1.000 28.96892 ? 93  GLN A CA  1 
ATOM   721  C  C   . GLN A 1 93  ? -3.28157  7.03158   4.32568   1.000 28.63327 ? 93  GLN A C   1 
ATOM   722  O  O   . GLN A 1 93  ? -3.41499  7.52909   3.20317   1.000 34.08539 ? 93  GLN A O   1 
ATOM   723  C  CB  . GLN A 1 93  ? -3.70061  4.60989   4.15393   1.000 31.14418 ? 93  GLN A CB  1 
ATOM   724  C  CG  . GLN A 1 93  ? -4.32621  3.37031   4.72179   1.000 32.67932 ? 93  GLN A CG  1 
ATOM   725  C  CD  . GLN A 1 93  ? -3.45847  2.16512   4.47401   1.000 38.63284 ? 93  GLN A CD  1 
ATOM   726  O  OE1 . GLN A 1 93  ? -2.79644  1.66941   5.38549   1.000 40.77668 ? 93  GLN A OE1 1 
ATOM   727  N  NE2 . GLN A 1 93  ? -3.42813  1.70092   3.22446   1.000 39.42153 ? 93  GLN A NE2 1 
ATOM   728  N  N   . ALA A 1 94  ? -2.33880  7.39869   5.18798   1.000 24.68176 ? 94  ALA A N   1 
ATOM   729  C  CA  . ALA A 1 94  ? -1.21793  8.23645   4.80549   1.000 23.82962 ? 94  ALA A CA  1 
ATOM   730  C  C   . ALA A 1 94  ? -0.14998  7.36805   4.14515   1.000 22.02331 ? 94  ALA A C   1 
ATOM   731  O  O   . ALA A 1 94  ? -0.27827  6.14248   4.06519   1.000 22.78686 ? 94  ALA A O   1 
ATOM   732  C  CB  . ALA A 1 94  ? -0.67135  8.97904   6.02502   1.000 22.36876 ? 94  ALA A CB  1 
ATOM   733  N  N   . PHE A 1 95  ? 0.93264   7.99613   3.67118   1.000 23.69424 ? 95  PHE A N   1 
ATOM   734  C  CA  . PHE A 1 95  ? 1.87476   7.23925   2.84992   1.000 21.16940 ? 95  PHE A CA  1 
ATOM   735  C  C   . PHE A 1 95  ? 2.64455   6.17695   3.62917   1.000 20.69523 ? 95  PHE A C   1 
ATOM   736  O  O   . PHE A 1 95  ? 3.23580   5.29117   3.00028   1.000 20.93516 ? 95  PHE A O   1 
ATOM   737  C  CB  . PHE A 1 95  ? 2.83816   8.17752   2.09260   1.000 21.07976 ? 95  PHE A CB  1 
ATOM   738  C  CG  . PHE A 1 95  ? 3.64984   9.11458   2.95867   1.000 20.75626 ? 95  PHE A CG  1 
ATOM   739  C  CD1 . PHE A 1 95  ? 4.81421   8.68850   3.57157   1.000 19.94421 ? 95  PHE A CD1 1 
ATOM   740  C  CD2 . PHE A 1 95  ? 3.28709   10.45070  3.07272   1.000 21.23936 ? 95  PHE A CD2 1 
ATOM   741  C  CE1 . PHE A 1 95  ? 5.57525   9.56792   4.33768   1.000 19.04127 ? 95  PHE A CE1 1 
ATOM   742  C  CE2 . PHE A 1 95  ? 4.03445   11.33486  3.82942   1.000 19.37842 ? 95  PHE A CE2 1 
ATOM   743  C  CZ  . PHE A 1 95  ? 5.18747   10.89971  4.46522   1.000 19.93986 ? 95  PHE A CZ  1 
ATOM   744  N  N   . ILE A 1 96  ? 2.61075   6.20327   4.96411   1.000 18.94618 ? 96  ILE A N   1 
ATOM   745  C  CA  . ILE A 1 96  ? 3.21447   5.12827   5.74322   1.000 18.94461 ? 96  ILE A CA  1 
ATOM   746  C  C   . ILE A 1 96  ? 2.52487   3.79883   5.45706   1.000 20.33821 ? 96  ILE A C   1 
ATOM   747  O  O   . ILE A 1 96  ? 3.12453   2.73350   5.64162   1.000 21.48945 ? 96  ILE A O   1 
ATOM   748  C  CB  . ILE A 1 96  ? 3.18093   5.47713   7.24969   1.000 21.13619 ? 96  ILE A CB  1 
ATOM   749  C  CG1 . ILE A 1 96  ? 4.11146   4.54865   8.05140   1.000 20.76184 ? 96  ILE A CG1 1 
ATOM   750  C  CG2 . ILE A 1 96  ? 1.75367   5.44657   7.80664   1.000 21.50962 ? 96  ILE A CG2 1 
ATOM   751  C  CD1 . ILE A 1 96  ? 4.29183   4.99662   9.49901   1.000 20.54230 ? 96  ILE A CD1 1 
ATOM   752  N  N   . GLY A 1 97  ? 1.27786   3.83301   4.99288   1.000 21.48829 ? 97  GLY A N   1 
ATOM   753  C  CA  . GLY A 1 97  ? 0.53534   2.63871   4.65393   1.000 20.95509 ? 97  GLY A CA  1 
ATOM   754  C  C   . GLY A 1 97  ? 0.45337   2.36209   3.17255   1.000 21.17295 ? 97  GLY A C   1 
ATOM   755  O  O   . GLY A 1 97  ? -0.33897  1.50649   2.75806   1.000 26.05206 ? 97  GLY A O   1 
ATOM   756  N  N   . LEU A 1 98  ? 1.23380   3.06338   2.35826   1.000 20.97627 ? 98  LEU A N   1 
ATOM   757  C  CA  . LEU A 1 98  ? 1.23270   2.85574   0.92078   1.000 21.32688 ? 98  LEU A CA  1 
ATOM   758  C  C   . LEU A 1 98  ? 2.49037   2.11620   0.48644   1.000 18.73941 ? 98  LEU A C   1 
ATOM   759  O  O   . LEU A 1 98  ? 3.52143   2.14401   1.16115   1.000 22.15985 ? 98  LEU A O   1 
ATOM   760  C  CB  . LEU A 1 98  ? 1.13604   4.19176   0.17703   1.000 22.26671 ? 98  LEU A CB  1 
ATOM   761  C  CG  . LEU A 1 98  ? -0.10037  5.03724   0.49506   1.000 20.70643 ? 98  LEU A CG  1 
ATOM   762  C  CD1 . LEU A 1 98  ? -0.05691  6.38650   -0.23012  1.000 21.84993 ? 98  LEU A CD1 1 
ATOM   763  C  CD2 . LEU A 1 98  ? -1.36643  4.26652   0.12568   1.000 22.79277 ? 98  LEU A CD2 1 
ATOM   764  N  N   . ASP A 1 99  ? 2.39531   1.45448   -0.65980  1.000 21.60929 ? 99  ASP A N   1 
ATOM   765  C  CA  . ASP A 1 99  ? 3.54378   0.85103   -1.30847  1.000 22.79249 ? 99  ASP A CA  1 
ATOM   766  C  C   . ASP A 1 99  ? 3.91543   1.63996   -2.55821  1.000 25.31218 ? 99  ASP A C   1 
ATOM   767  O  O   . ASP A 1 99  ? 3.09224   2.39116   -3.09078  1.000 24.52370 ? 99  ASP A O   1 
ATOM   768  C  CB  . ASP A 1 99  ? 3.24020   -0.60362  -1.69655  1.000 23.99747 ? 99  ASP A CB  1 
ATOM   769  C  CG  . ASP A 1 99  ? 2.88004   -1.46454  -0.50973  1.000 23.57509 ? 99  ASP A CG  1 
ATOM   770  O  OD1 . ASP A 1 99  ? 3.52332   -1.32400  0.55796   1.000 22.88786 ? 99  ASP A OD1 1 
ATOM   771  O  OD2 . ASP A 1 99  ? 1.95580   -2.29731  -0.65182  1.000 25.43380 ? 99  ASP A OD2 1 
ATOM   772  N  N   . PRO A 1 100 ? 5.14801   1.50715   -3.04816  1.000 25.60538 ? 100 PRO A N   1 
ATOM   773  C  CA  . PRO A 1 100 ? 5.50472   2.11202   -4.34434  1.000 24.61391 ? 100 PRO A CA  1 
ATOM   774  C  C   . PRO A 1 100 ? 4.57311   1.61279   -5.43125  1.000 32.10562 ? 100 PRO A C   1 
ATOM   775  O  O   . PRO A 1 100 ? 4.17854   0.43586   -5.41539  1.000 36.38125 ? 100 PRO A O   1 
ATOM   776  C  CB  . PRO A 1 100 ? 6.94181   1.62283   -4.57927  1.000 28.26259 ? 100 PRO A CB  1 
ATOM   777  C  CG  . PRO A 1 100 ? 7.47760   1.37363   -3.19074  1.000 29.33663 ? 100 PRO A CG  1 
ATOM   778  C  CD  . PRO A 1 100 ? 6.30047   0.83508   -2.41601  1.000 27.68847 ? 100 PRO A CD  1 
ATOM   779  N  N   . PRO A 1 101 ? 4.21497   2.46560   -6.40898  1.000 31.28378 ? 101 PRO A N   1 
ATOM   780  C  CA  . PRO A 1 101 ? 4.67543   3.84128   -6.62616  1.000 30.24222 ? 101 PRO A CA  1 
ATOM   781  C  C   . PRO A 1 101 ? 3.89090   4.90166   -5.86783  1.000 27.96476 ? 101 PRO A C   1 
ATOM   782  O  O   . PRO A 1 101 ? 4.32484   6.05036   -5.79902  1.000 27.93880 ? 101 PRO A O   1 
ATOM   783  C  CB  . PRO A 1 101 ? 4.48161   4.01712   -8.13741  1.000 33.26871 ? 101 PRO A CB  1 
ATOM   784  C  CG  . PRO A 1 101 ? 3.23759   3.22580   -8.41179  1.000 34.05874 ? 101 PRO A CG  1 
ATOM   785  C  CD  . PRO A 1 101 ? 3.33539   2.01622   -7.50442  1.000 33.96947 ? 101 PRO A CD  1 
ATOM   786  N  N   . GLU A 1 102 ? 2.72487   4.55475   -5.31829  1.000 26.46995 ? 102 GLU A N   1 
ATOM   787  C  CA  . GLU A 1 102 ? 1.88319   5.55277   -4.67178  1.000 27.74318 ? 102 GLU A CA  1 
ATOM   788  C  C   . GLU A 1 102 ? 2.57279   6.15414   -3.45510  1.000 24.63644 ? 102 GLU A C   1 
ATOM   789  O  O   . GLU A 1 102 ? 2.42887   7.35267   -3.18726  1.000 26.86203 ? 102 GLU A O   1 
ATOM   790  C  CB  . GLU A 1 102 ? 0.54252   4.93382   -4.26726  1.000 31.62637 ? 102 GLU A CB  1 
ATOM   791  C  CG  . GLU A 1 102 ? -0.32977  4.45454   -5.42112  1.000 38.68899 ? 102 GLU A CG  1 
ATOM   792  C  CD  . GLU A 1 102 ? 0.12189   3.12130   -5.98585  1.000 44.87698 ? 102 GLU A CD  1 
ATOM   793  O  OE1 . GLU A 1 102 ? 0.71243   2.32022   -5.22926  1.000 46.16280 ? 102 GLU A OE1 1 
ATOM   794  O  OE2 . GLU A 1 102 ? -0.10721  2.87946   -7.19065  1.000 48.77256 ? 102 GLU A OE2 1 
ATOM   795  N  N   . HIS A 1 103 ? 3.33997   5.34277   -2.72325  1.000 22.07309 ? 103 HIS A N   1 
ATOM   796  C  CA  . HIS A 1 103 ? 4.04863   5.83155   -1.54374  1.000 20.50450 ? 103 HIS A CA  1 
ATOM   797  C  C   . HIS A 1 103 ? 4.92859   7.03067   -1.87992  1.000 20.75293 ? 103 HIS A C   1 
ATOM   798  O  O   . HIS A 1 103 ? 4.90335   8.05234   -1.18144  1.000 21.58545 ? 103 HIS A O   1 
ATOM   799  C  CB  . HIS A 1 103 ? 4.89500   4.70509   -0.94218  1.000 21.02631 ? 103 HIS A CB  1 
ATOM   800  C  CG  . HIS A 1 103 ? 5.91443   5.18772   0.04139   1.000 21.20181 ? 103 HIS A CG  1 
ATOM   801  N  ND1 . HIS A 1 103 ? 7.24921   5.32745   -0.27511  1.000 22.89422 ? 103 HIS A ND1 1 
ATOM   802  C  CD2 . HIS A 1 103 ? 5.78920   5.58431   1.33053   1.000 22.10991 ? 103 HIS A CD2 1 
ATOM   803  C  CE1 . HIS A 1 103 ? 7.90466   5.77741   0.78142   1.000 23.18466 ? 103 HIS A CE1 1 
ATOM   804  N  NE2 . HIS A 1 103 ? 7.04163   5.94430   1.76787   1.000 23.78898 ? 103 HIS A NE2 1 
ATOM   805  N  N   . GLY A 1 104 ? 5.72144   6.91779   -2.94570  1.000 20.86077 ? 104 GLY A N   1 
ATOM   806  C  CA  . GLY A 1 104 ? 6.66101   7.97549   -3.27202  1.000 22.79446 ? 104 GLY A CA  1 
ATOM   807  C  C   . GLY A 1 104 ? 5.98495   9.25690   -3.71667  1.000 25.21101 ? 104 GLY A C   1 
ATOM   808  O  O   . GLY A 1 104 ? 6.45538   10.35514  -3.40063  1.000 25.67973 ? 104 GLY A O   1 
ATOM   809  N  N   . THR A 1 105 ? 4.88307   9.14483   -4.46707  1.000 22.76039 ? 105 THR A N   1 
ATOM   810  C  CA  . THR A 1 105 ? 4.22001   10.36648  -4.92318  1.000 22.75655 ? 105 THR A CA  1 
ATOM   811  C  C   . THR A 1 105 ? 3.66221   11.16158  -3.75099  1.000 24.70320 ? 105 THR A C   1 
ATOM   812  O  O   . THR A 1 105 ? 3.64638   12.39342  -3.79443  1.000 27.38963 ? 105 THR A O   1 
ATOM   813  C  CB  . THR A 1 105 ? 3.11067   10.05804  -5.93297  1.000 26.86356 ? 105 THR A CB  1 
ATOM   814  O  OG1 . THR A 1 105 ? 1.97905   9.47738   -5.27170  1.000 28.44035 ? 105 THR A OG1 1 
ATOM   815  C  CG2 . THR A 1 105 ? 3.62517   9.11768   -7.00657  1.000 27.42393 ? 105 THR A CG2 1 
ATOM   816  N  N   . ARG A 1 106 ? 3.22119   10.48740  -2.68798  1.000 22.55348 ? 106 ARG A N   1 
ATOM   817  C  CA  . ARG A 1 106 ? 2.74097   11.22905  -1.52578  1.000 20.53124 ? 106 ARG A CA  1 
ATOM   818  C  C   . ARG A 1 106 ? 3.89129   11.68770  -0.63384  1.000 20.18801 ? 106 ARG A C   1 
ATOM   819  O  O   . ARG A 1 106 ? 3.90258   12.84025  -0.18340  1.000 21.58215 ? 106 ARG A O   1 
ATOM   820  C  CB  . ARG A 1 106 ? 1.73938   10.38940  -0.72493  1.000 22.03517 ? 106 ARG A CB  1 
ATOM   821  C  CG  . ARG A 1 106 ? 0.28214   10.54287  -1.17399  1.000 27.16554 ? 106 ARG A CG  1 
ATOM   822  C  CD  . ARG A 1 106 ? -0.10202  9.62868   -2.32651  1.000 27.79103 ? 106 ARG A CD  1 
ATOM   823  N  NE  . ARG A 1 106 ? -1.41947  9.99607   -2.83885  1.000 27.22250 ? 106 ARG A NE  1 
ATOM   824  C  CZ  . ARG A 1 106 ? -1.62096  10.75507  -3.90836  1.000 26.29599 ? 106 ARG A CZ  1 
ATOM   825  N  NH1 . ARG A 1 106 ? -0.61396  11.15856  -4.66817  1.000 26.51657 ? 106 ARG A NH1 1 
ATOM   826  N  NH2 . ARG A 1 106 ? -2.86291  11.11627  -4.22409  1.000 25.46356 ? 106 ARG A NH2 1 
ATOM   827  N  N   . ARG A 1 107 ? 4.87713   10.81751  -0.37811  1.000 18.25861 ? 107 ARG A N   1 
ATOM   828  C  CA  . ARG A 1 107 ? 5.98816   11.21458  0.48817   1.000 16.70686 ? 107 ARG A CA  1 
ATOM   829  C  C   . ARG A 1 107 ? 6.71234   12.42986  -0.07587  1.000 18.44880 ? 107 ARG A C   1 
ATOM   830  O  O   . ARG A 1 107 ? 7.04306   13.36342  0.66327   1.000 20.04701 ? 107 ARG A O   1 
ATOM   831  C  CB  . ARG A 1 107 ? 6.95976   10.05001  0.67744   1.000 17.80065 ? 107 ARG A CB  1 
ATOM   832  C  CG  . ARG A 1 107 ? 8.22516   10.43992  1.43781   1.000 19.15091 ? 107 ARG A CG  1 
ATOM   833  C  CD  . ARG A 1 107 ? 9.03070   9.21835   1.87270   1.000 19.73248 ? 107 ARG A CD  1 
ATOM   834  N  NE  . ARG A 1 107 ? 10.34466  9.57702   2.39187   1.000 21.56044 ? 107 ARG A NE  1 
ATOM   835  C  CZ  . ARG A 1 107 ? 10.86181  9.13596   3.53478   1.000 24.54144 ? 107 ARG A CZ  1 
ATOM   836  N  NH1 . ARG A 1 107 ? 10.19218  8.31993   4.33618   1.000 22.75928 ? 107 ARG A NH1 1 
ATOM   837  N  NH2 . ARG A 1 107 ? 12.08626  9.52070   3.88191   1.000 27.73658 ? 107 ARG A NH2 1 
ATOM   838  N  N   . ARG A 1 108 ? 6.91507   12.46322  -1.39489  1.000 19.86645 ? 108 ARG A N   1 
ATOM   839  C  CA  . ARG A 1 108 ? 7.61685   13.58459  -2.00597  1.000 19.48882 ? 108 ARG A CA  1 
ATOM   840  C  C   . ARG A 1 108 ? 6.86962   14.90226  -1.83378  1.000 19.38272 ? 108 ARG A C   1 
ATOM   841  O  O   . ARG A 1 108 ? 7.47615   15.96479  -2.00199  1.000 23.98982 ? 108 ARG A O   1 
ATOM   842  C  CB  . ARG A 1 108 ? 7.86226   13.30911  -3.49321  1.000 22.18776 ? 108 ARG A CB  1 
ATOM   843  C  CG  . ARG A 1 108 ? 9.02149   12.35719  -3.75844  1.000 28.61965 ? 108 ARG A CG  1 
ATOM   844  C  CD  . ARG A 1 108 ? 9.39588   12.28012  -5.24354  1.000 33.64408 ? 108 ARG A CD  1 
ATOM   845  N  NE  . ARG A 1 108 ? 8.32003   11.74294  -6.07018  1.000 35.93660 ? 108 ARG A NE  1 
ATOM   846  C  CZ  . ARG A 1 108 ? 8.12075   10.44932  -6.29339  1.000 39.47131 ? 108 ARG A CZ  1 
ATOM   847  N  NH1 . ARG A 1 108 ? 8.89177   9.52612   -5.74238  1.000 40.01739 ? 108 ARG A NH1 1 
ATOM   848  N  NH2 . ARG A 1 108 ? 7.12262   10.07268  -7.08974  1.000 38.51080 ? 108 ARG A NH2 1 
ATOM   849  N  N   . MET A 1 109 ? 5.57682   14.86695  -1.49806  1.000 18.66112 ? 109 MET A N   1 
ATOM   850  C  CA  . MET A 1 109 ? 4.85904   16.10898  -1.22120  1.000 19.20057 ? 109 MET A CA  1 
ATOM   851  C  C   . MET A 1 109 ? 5.27767   16.73609  0.09994   1.000 20.77232 ? 109 MET A C   1 
ATOM   852  O  O   . MET A 1 109 ? 4.98641   17.91761  0.33448   1.000 21.39861 ? 109 MET A O   1 
ATOM   853  C  CB  . MET A 1 109 ? 3.35317   15.86065  -1.21062  1.000 19.42739 ? 109 MET A CB  1 
ATOM   854  C  CG  . MET A 1 109 ? 2.81507   15.39231  -2.54920  1.000 21.16914 ? 109 MET A CG  1 
ATOM   855  S  SD  . MET A 1 109 ? 1.08099   15.00796  -2.37966  1.000 23.39703 ? 109 MET A SD  1 
ATOM   856  C  CE  . MET A 1 109 ? 0.71280   14.50996  -4.06751  1.000 24.94855 ? 109 MET A CE  1 
ATOM   857  N  N   . THR A 1 110 ? 5.95783   15.98471  0.96156   1.000 20.46196 ? 110 THR A N   1 
ATOM   858  C  CA  . THR A 1 110 ? 6.29922   16.47735  2.29084   1.000 20.34331 ? 110 THR A CA  1 
ATOM   859  C  C   . THR A 1 110 ? 7.79451   16.60863  2.54321   1.000 19.71557 ? 110 THR A C   1 
ATOM   860  O  O   . THR A 1 110 ? 8.17128   17.21156  3.55203   1.000 20.58912 ? 110 THR A O   1 
ATOM   861  C  CB  . THR A 1 110 ? 5.71540   15.56353  3.38706   1.000 19.13083 ? 110 THR A CB  1 
ATOM   862  O  OG1 . THR A 1 110 ? 6.39465   14.30185  3.36812   1.000 21.89682 ? 110 THR A OG1 1 
ATOM   863  C  CG2 . THR A 1 110 ? 4.23346   15.32965  3.18338   1.000 21.74412 ? 110 THR A CG2 1 
ATOM   864  N  N   . ILE A 1 111 ? 8.65521   16.08901  1.66117   1.000 22.29583 ? 111 ILE A N   1 
ATOM   865  C  CA  . ILE A 1 111 ? 10.07118  15.95690  2.00778   1.000 21.30923 ? 111 ILE A CA  1 
ATOM   866  C  C   . ILE A 1 111 ? 10.75887  17.30676  2.14912   1.000 21.97519 ? 111 ILE A C   1 
ATOM   867  O  O   . ILE A 1 111 ? 11.74322  17.42583  2.89338   1.000 24.34519 ? 111 ILE A O   1 
ATOM   868  C  CB  . ILE A 1 111 ? 10.81464  15.09438  0.97454   1.000 23.07899 ? 111 ILE A CB  1 
ATOM   869  C  CG1 . ILE A 1 111 ? 10.59332  15.66283  -0.43275  1.000 25.11973 ? 111 ILE A CG1 1 
ATOM   870  C  CG2 . ILE A 1 111 ? 10.38788  13.65084  1.09827   1.000 23.22538 ? 111 ILE A CG2 1 
ATOM   871  C  CD1 . ILE A 1 111 ? 11.39363  14.98124  -1.50311  1.000 29.31348 ? 111 ILE A CD1 1 
ATOM   872  N  N   . SER A 1 112 ? 10.28163  18.33203  1.43677   1.000 23.95133 ? 112 SER A N   1 
ATOM   873  C  CA  . SER A 1 112 ? 10.95545  19.62450  1.44730   1.000 26.85168 ? 112 SER A CA  1 
ATOM   874  C  C   . SER A 1 112 ? 11.05038  20.21868  2.84820   1.000 24.68303 ? 112 SER A C   1 
ATOM   875  O  O   . SER A 1 112 ? 11.94419  21.02972  3.10899   1.000 26.48277 ? 112 SER A O   1 
ATOM   876  C  CB  . SER A 1 112 ? 10.23090  20.59446  0.51227   1.000 31.67754 ? 112 SER A CB  1 
ATOM   877  O  OG  . SER A 1 112 ? 8.90110   20.83505  0.94907   1.000 36.68137 ? 112 SER A OG  1 
ATOM   878  N  N   . GLU A 1 113 ? 10.17820  19.81078  3.76542   1.000 23.94330 ? 113 GLU A N   1 
ATOM   879  C  CA  . GLU A 1 113 ? 10.21004  20.34922  5.11619   1.000 23.75054 ? 113 GLU A CA  1 
ATOM   880  C  C   . GLU A 1 113 ? 11.21232  19.64454  6.01586   1.000 22.37425 ? 113 GLU A C   1 
ATOM   881  O  O   . GLU A 1 113 ? 11.42849  20.09562  7.14286   1.000 23.64865 ? 113 GLU A O   1 
ATOM   882  C  CB  . GLU A 1 113 ? 8.82616   20.24846  5.74861   1.000 25.90274 ? 113 GLU A CB  1 
ATOM   883  C  CG  . GLU A 1 113 ? 7.73123   20.90864  4.93627   1.000 30.70894 ? 113 GLU A CG  1 
ATOM   884  C  CD  . GLU A 1 113 ? 7.73925   22.41699  5.06609   1.000 40.99419 ? 113 GLU A CD  1 
ATOM   885  O  OE1 . GLU A 1 113 ? 8.43342   22.93476  5.96982   1.000 40.29438 ? 113 GLU A OE1 1 
ATOM   886  O  OE2 . GLU A 1 113 ? 7.04164   23.08022  4.27318   1.000 46.66005 ? 113 GLU A OE2 1 
ATOM   887  N  N   . PHE A 1 114 ? 11.81329  18.54960  5.55739   1.000 20.62075 ? 114 PHE A N   1 
ATOM   888  C  CA  . PHE A 1 114 ? 12.63774  17.70245  6.40570   1.000 19.48709 ? 114 PHE A CA  1 
ATOM   889  C  C   . PHE A 1 114 ? 14.05708  17.54035  5.87867   1.000 23.24180 ? 114 PHE A C   1 
ATOM   890  O  O   . PHE A 1 114 ? 14.81543  16.72779  6.42458   1.000 25.29846 ? 114 PHE A O   1 
ATOM   891  C  CB  . PHE A 1 114 ? 11.96337  16.33809  6.57223   1.000 19.50761 ? 114 PHE A CB  1 
ATOM   892  C  CG  . PHE A 1 114 ? 10.65721  16.39995  7.31938   1.000 20.34125 ? 114 PHE A CG  1 
ATOM   893  C  CD1 . PHE A 1 114 ? 10.63205  16.31498  8.70444   1.000 21.68331 ? 114 PHE A CD1 1 
ATOM   894  C  CD2 . PHE A 1 114 ? 9.46106   16.56579  6.64164   1.000 19.94919 ? 114 PHE A CD2 1 
ATOM   895  C  CE1 . PHE A 1 114 ? 9.43189   16.38802  9.40410   1.000 22.17941 ? 114 PHE A CE1 1 
ATOM   896  C  CE2 . PHE A 1 114 ? 8.25719   16.63197  7.32791   1.000 22.39775 ? 114 PHE A CE2 1 
ATOM   897  C  CZ  . PHE A 1 114 ? 8.24305   16.53981  8.71287   1.000 20.76759 ? 114 PHE A CZ  1 
ATOM   898  N  N   . THR A 1 115 ? 14.43664  18.30189  4.84770   1.000 23.53897 ? 115 THR A N   1 
ATOM   899  C  CA  . THR A 1 115 ? 15.78558  18.25168  4.29912   1.000 24.62460 ? 115 THR A CA  1 
ATOM   900  C  C   . THR A 1 115 ? 16.80519  18.66046  5.34990   1.000 25.93083 ? 115 THR A C   1 
ATOM   901  O  O   . THR A 1 115 ? 16.48545  19.33661  6.32971   1.000 26.01084 ? 115 THR A O   1 
ATOM   902  C  CB  . THR A 1 115 ? 15.93533  19.19426  3.10638   1.000 29.86217 ? 115 THR A CB  1 
ATOM   903  O  OG1 . THR A 1 115 ? 15.85116  20.54985  3.56769   1.000 31.68023 ? 115 THR A OG1 1 
ATOM   904  C  CG2 . THR A 1 115 ? 14.86072  18.93660  2.06632   1.000 29.39421 ? 115 THR A CG2 1 
ATOM   905  N  N   . VAL A 1 116 ? 18.06076  18.27755  5.11134   1.000 30.14628 ? 116 VAL A N   1 
ATOM   906  C  CA  . VAL A 1 116 ? 19.13208  18.66407  6.03009   1.000 30.64872 ? 116 VAL A CA  1 
ATOM   907  C  C   . VAL A 1 116 ? 19.23234  20.18044  6.13631   1.000 32.59819 ? 116 VAL A C   1 
ATOM   908  O  O   . VAL A 1 116 ? 19.42829  20.72662  7.22765   1.000 31.18462 ? 116 VAL A O   1 
ATOM   909  C  CB  . VAL A 1 116 ? 20.47572  18.04768  5.59877   1.000 38.24450 ? 116 VAL A CB  1 
ATOM   910  C  CG1 . VAL A 1 116 ? 20.49849  16.57216  5.90429   1.000 41.81588 ? 116 VAL A CG1 1 
ATOM   911  C  CG2 . VAL A 1 116 ? 20.73418  18.29022  4.12543   1.000 38.00122 ? 116 VAL A CG2 1 
ATOM   912  N  N   . LYS A 1 117 ? 19.10620  20.88495  5.01192   1.000 33.46280 ? 117 LYS A N   1 
ATOM   913  C  CA  . LYS A 1 117 ? 19.18845  22.34014  5.05139   1.000 36.03648 ? 117 LYS A CA  1 
ATOM   914  C  C   . LYS A 1 117 ? 18.05803  22.92830  5.88411   1.000 33.32161 ? 117 LYS A C   1 
ATOM   915  O  O   . LYS A 1 117 ? 18.27353  23.86499  6.66222   1.000 34.99045 ? 117 LYS A O   1 
ATOM   916  C  CB  . LYS A 1 117 ? 19.17928  22.91586  3.62788   1.000 40.42614 ? 117 LYS A CB  1 
ATOM   917  C  CG  . LYS A 1 117 ? 19.18417  24.44002  3.58907   1.000 46.04369 ? 117 LYS A CG  1 
ATOM   918  C  CD  . LYS A 1 117 ? 19.54994  25.00353  2.21910   1.000 49.92415 ? 117 LYS A CD  1 
ATOM   919  C  CE  . LYS A 1 117 ? 20.11201  26.41680  2.36542   1.000 51.07928 ? 117 LYS A CE  1 
ATOM   920  N  NZ  . LYS A 1 117 ? 20.53702  27.02338  1.06933   1.000 51.49338 ? 117 LYS A NZ  1 
ATOM   921  N  N   . ARG A 1 118 ? 16.84630  22.38390  5.74780   1.000 29.91724 ? 118 ARG A N   1 
ATOM   922  C  CA  . ARG A 1 118 ? 15.72921  22.90516  6.52538   1.000 32.72997 ? 118 ARG A CA  1 
ATOM   923  C  C   . ARG A 1 118 ? 15.91125  22.60715  8.00582   1.000 30.85050 ? 118 ARG A C   1 
ATOM   924  O  O   . ARG A 1 118 ? 15.65978  23.47285  8.85525   1.000 32.91151 ? 118 ARG A O   1 
ATOM   925  C  CB  . ARG A 1 118 ? 14.41081  22.32389  6.02215   1.000 37.36193 ? 118 ARG A CB  1 
ATOM   926  C  CG  . ARG A 1 118 ? 13.23628  23.27000  6.18510   1.000 47.34458 ? 118 ARG A CG  1 
ATOM   927  C  CD  . ARG A 1 118 ? 13.31025  24.41148  5.18034   1.000 52.62628 ? 118 ARG A CD  1 
ATOM   928  N  NE  . ARG A 1 118 ? 12.47076  24.15768  4.01549   1.000 63.60224 ? 118 ARG A NE  1 
ATOM   929  C  CZ  . ARG A 1 118 ? 12.41339  24.93783  2.94388   1.000 71.76822 ? 118 ARG A CZ  1 
ATOM   930  N  NH1 . ARG A 1 118 ? 13.15558  26.02900  2.84170   1.000 73.96653 ? 118 ARG A NH1 1 
ATOM   931  N  NH2 . ARG A 1 118 ? 11.59079  24.61472  1.94887   1.000 75.76237 ? 118 ARG A NH2 1 
ATOM   932  N  N   . ILE A 1 119 ? 16.35396  21.39082  8.33265   1.000 30.17209 ? 119 ILE A N   1 
ATOM   933  C  CA  . ILE A 1 119 ? 16.56889  21.03693  9.73579   1.000 28.37539 ? 119 ILE A CA  1 
ATOM   934  C  C   . ILE A 1 119 ? 17.60522  21.96479  10.36327  1.000 34.50560 ? 119 ILE A C   1 
ATOM   935  O  O   . ILE A 1 119 ? 17.45271  22.41221  11.50778  1.000 33.19956 ? 119 ILE A O   1 
ATOM   936  C  CB  . ILE A 1 119 ? 16.97858  19.55524  9.85908   1.000 28.27244 ? 119 ILE A CB  1 
ATOM   937  C  CG1 . ILE A 1 119 ? 15.88383  18.64549  9.30260   1.000 30.38485 ? 119 ILE A CG1 1 
ATOM   938  C  CG2 . ILE A 1 119 ? 17.27086  19.18285  11.30876  1.000 25.35164 ? 119 ILE A CG2 1 
ATOM   939  C  CD1 . ILE A 1 119 ? 14.49429  18.96889  9.81271   1.000 30.32682 ? 119 ILE A CD1 1 
ATOM   940  N  N   . LYS A 1 120 ? 18.66791  22.28027  9.62155   1.000 36.41663 ? 120 LYS A N   1 
ATOM   941  C  CA  . LYS A 1 120 ? 19.68452  23.19801  10.13243  1.000 36.33164 ? 120 LYS A CA  1 
ATOM   942  C  C   . LYS A 1 120 ? 19.09141  24.56780  10.43635  1.000 39.39224 ? 120 LYS A C   1 
ATOM   943  O  O   . LYS A 1 120 ? 19.37064  25.16459  11.48517  1.000 40.45321 ? 120 LYS A O   1 
ATOM   944  C  CB  . LYS A 1 120 ? 20.82535  23.33070  9.12893   1.000 39.18948 ? 120 LYS A CB  1 
ATOM   945  C  CG  . LYS A 1 120 ? 21.81712  24.41322  9.51245   1.000 43.97063 ? 120 LYS A CG  1 
ATOM   946  C  CD  . LYS A 1 120 ? 22.94502  24.54839  8.50615   1.000 45.87826 ? 120 LYS A CD  1 
ATOM   947  C  CE  . LYS A 1 120 ? 23.98299  25.53322  9.02252   1.000 50.33306 ? 120 LYS A CE  1 
ATOM   948  N  NZ  . LYS A 1 120 ? 25.20101  25.59294  8.16628   1.000 53.21864 ? 120 LYS A NZ  1 
ATOM   949  N  N   . GLY A 1 121 ? 18.27539  25.08869  9.51981   1.000 40.23321 ? 121 GLY A N   1 
ATOM   950  C  CA  . GLY A 1 121 ? 17.62462  26.36493  9.74511   1.000 41.01510 ? 121 GLY A CA  1 
ATOM   951  C  C   . GLY A 1 121 ? 16.62211  26.35251  10.88039  1.000 36.63252 ? 121 GLY A C   1 
ATOM   952  O  O   . GLY A 1 121 ? 16.20058  27.42294  11.33270  1.000 41.89361 ? 121 GLY A O   1 
ATOM   953  N  N   . MET A 1 122 ? 16.22105  25.16941  11.34990  1.000 36.89843 ? 122 MET A N   1 
ATOM   954  C  CA  . MET A 1 122 ? 15.28387  25.10001  12.45786  1.000 34.82691 ? 122 MET A CA  1 
ATOM   955  C  C   . MET A 1 122 ? 15.95555  25.16854  13.81770  1.000 35.37499 ? 122 MET A C   1 
ATOM   956  O  O   . MET A 1 122 ? 15.25018  25.31721  14.81870  1.000 36.03977 ? 122 MET A O   1 
ATOM   957  C  CB  . MET A 1 122 ? 14.45721  23.81551  12.38293  1.000 36.36196 ? 122 MET A CB  1 
ATOM   958  C  CG  . MET A 1 122 ? 13.59232  23.74230  11.15118  1.000 37.51352 ? 122 MET A CG  1 
ATOM   959  S  SD  . MET A 1 122 ? 12.70372  22.19067  11.13576  1.000 37.25615 ? 122 MET A SD  1 
ATOM   960  C  CE  . MET A 1 122 ? 11.51359  22.49978  12.43694  1.000 38.32049 ? 122 MET A CE  1 
ATOM   961  N  N   . ARG A 1 123 ? 17.28189  25.07298  13.88120  1.000 35.60147 ? 123 ARG A N   1 
ATOM   962  C  CA  . ARG A 1 123 ? 17.95143  25.06046  15.17942  1.000 38.95239 ? 123 ARG A CA  1 
ATOM   963  C  C   . ARG A 1 123 ? 17.59694  26.23999  16.08132  1.000 39.53869 ? 123 ARG A C   1 
ATOM   964  O  O   . ARG A 1 123 ? 17.35466  26.00605  17.27685  1.000 39.44525 ? 123 ARG A O   1 
ATOM   965  C  CB  . ARG A 1 123 ? 19.47132  24.99039  15.00304  1.000 40.14976 ? 123 ARG A CB  1 
ATOM   966  C  CG  . ARG A 1 123 ? 20.20683  25.24970  16.30707  1.000 41.79139 ? 123 ARG A CG  1 
ATOM   967  C  CD  . ARG A 1 123 ? 21.69639  25.12637  16.13028  1.000 40.47646 ? 123 ARG A CD  1 
ATOM   968  N  NE  . ARG A 1 123 ? 22.04234  23.83081  15.56747  1.000 39.20073 ? 123 ARG A NE  1 
ATOM   969  C  CZ  . ARG A 1 123 ? 22.24243  22.73734  16.28716  1.000 37.86471 ? 123 ARG A CZ  1 
ATOM   970  N  NH1 . ARG A 1 123 ? 22.14604  22.75144  17.60815  1.000 38.75360 ? 123 ARG A NH1 1 
ATOM   971  N  NH2 . ARG A 1 123 ? 22.54332  21.60118  15.66721  1.000 36.94823 ? 123 ARG A NH2 1 
ATOM   972  N  N   . PRO A 1 124 ? 17.55039  27.49515  15.61471  1.000 40.10837 ? 124 PRO A N   1 
ATOM   973  C  CA  . PRO A 1 124 ? 17.20729  28.58100  16.55000  1.000 40.05334 ? 124 PRO A CA  1 
ATOM   974  C  C   . PRO A 1 124 ? 15.81212  28.46021  17.12979  1.000 37.93925 ? 124 PRO A C   1 
ATOM   975  O  O   . PRO A 1 124 ? 15.62510  28.73898  18.32087  1.000 39.01074 ? 124 PRO A O   1 
ATOM   976  C  CB  . PRO A 1 124 ? 17.35881  29.84437  15.68907  1.000 42.13694 ? 124 PRO A CB  1 
ATOM   977  C  CG  . PRO A 1 124 ? 18.28379  29.44828  14.59428  1.000 41.58383 ? 124 PRO A CG  1 
ATOM   978  C  CD  . PRO A 1 124 ? 17.92267  28.02714  14.29114  1.000 40.94670 ? 124 PRO A CD  1 
ATOM   979  N  N   . GLU A 1 125 ? 14.82389  28.05785  16.32103  1.000 36.14160 ? 125 GLU A N   1 
ATOM   980  C  CA  . GLU A 1 125 ? 13.47669  27.85209  16.84583  1.000 32.82908 ? 125 GLU A CA  1 
ATOM   981  C  C   . GLU A 1 125 ? 13.46520  26.72657  17.86300  1.000 30.17603 ? 125 GLU A C   1 
ATOM   982  O  O   . GLU A 1 125 ? 12.84421  26.84941  18.92270  1.000 33.52294 ? 125 GLU A O   1 
ATOM   983  C  CB  . GLU A 1 125 ? 12.48597  27.55430  15.71177  1.000 37.56100 ? 125 GLU A CB  1 
ATOM   984  C  CG  . GLU A 1 125 ? 11.20562  26.78756  16.13657  1.000 43.34692 ? 125 GLU A CG  1 
ATOM   985  C  CD  . GLU A 1 125 ? 10.03903  27.68451  16.58670  1.000 47.80969 ? 125 GLU A CD  1 
ATOM   986  O  OE1 . GLU A 1 125 ? 10.18554  28.92394  16.58740  1.000 49.59154 ? 125 GLU A OE1 1 
ATOM   987  O  OE2 . GLU A 1 125 ? 8.96276   27.14132  16.94108  1.000 46.78539 ? 125 GLU A OE2 1 
ATOM   988  N  N   . VAL A 1 126 ? 14.14539  25.61753  17.55530  1.000 29.00431 ? 126 VAL A N   1 
ATOM   989  C  CA  . VAL A 1 126 ? 14.18989  24.49165  18.48427  1.000 26.02183 ? 126 VAL A CA  1 
ATOM   990  C  C   . VAL A 1 126 ? 14.86316  24.90748  19.78946  1.000 24.56485 ? 126 VAL A C   1 
ATOM   991  O  O   . VAL A 1 126 ? 14.36989  24.61231  20.88589  1.000 25.51107 ? 126 VAL A O   1 
ATOM   992  C  CB  . VAL A 1 126 ? 14.89716  23.28594  17.83417  1.000 23.33243 ? 126 VAL A CB  1 
ATOM   993  C  CG1 . VAL A 1 126 ? 15.03353  22.13398  18.82989  1.000 21.32724 ? 126 VAL A CG1 1 
ATOM   994  C  CG2 . VAL A 1 126 ? 14.13177  22.82494  16.59458  1.000 24.04310 ? 126 VAL A CG2 1 
ATOM   995  N  N   . GLU A 1 127 ? 16.00358  25.59535  19.69740  1.000 24.93974 ? 127 GLU A N   1 
ATOM   996  C  CA  . GLU A 1 127 ? 16.68533  26.01282  20.92144  1.000 27.40594 ? 127 GLU A CA  1 
ATOM   997  C  C   . GLU A 1 127 ? 15.84406  27.01690  21.69873  1.000 26.13107 ? 127 GLU A C   1 
ATOM   998  O  O   . GLU A 1 127 ? 15.76943  26.95475  22.93322  1.000 26.07216 ? 127 GLU A O   1 
ATOM   999  C  CB  . GLU A 1 127 ? 18.06388  26.58972  20.59374  1.000 27.95994 ? 127 GLU A CB  1 
ATOM   1000 C  CG  . GLU A 1 127 ? 18.98502  25.57179  19.93811  1.000 37.35708 ? 127 GLU A CG  1 
ATOM   1001 C  CD  . GLU A 1 127 ? 20.40509  26.06688  19.76288  1.000 44.12104 ? 127 GLU A CD  1 
ATOM   1002 O  OE1 . GLU A 1 127 ? 20.62147  27.29210  19.83861  1.000 46.13376 ? 127 GLU A OE1 1 
ATOM   1003 O  OE2 . GLU A 1 127 ? 21.30671  25.22394  19.55072  1.000 44.85647 ? 127 GLU A OE2 1 
ATOM   1004 N  N   . GLU A 1 128 ? 15.19605  27.94537  20.99358  1.000 26.40413 ? 128 GLU A N   1 
ATOM   1005 C  CA  . GLU A 1 128 ? 14.32631  28.90166  21.67141  1.000 27.72827 ? 128 GLU A CA  1 
ATOM   1006 C  C   . GLU A 1 128 ? 13.15936  28.19537  22.34911  1.000 31.14591 ? 128 GLU A C   1 
ATOM   1007 O  O   . GLU A 1 128 ? 12.81254  28.51122  23.49628  1.000 29.99003 ? 128 GLU A O   1 
ATOM   1008 C  CB  . GLU A 1 128 ? 13.81743  29.95981  20.68470  1.000 32.15871 ? 128 GLU A CB  1 
ATOM   1009 C  CG  . GLU A 1 128 ? 12.97988  31.03200  21.35374  1.000 39.77463 ? 128 GLU A CG  1 
ATOM   1010 C  CD  . GLU A 1 128 ? 12.19997  31.87734  20.37338  1.000 45.79018 ? 128 GLU A CD  1 
ATOM   1011 O  OE1 . GLU A 1 128 ? 12.55701  31.88566  19.18085  1.000 49.30197 ? 128 GLU A OE1 1 
ATOM   1012 O  OE2 . GLU A 1 128 ? 11.21868  32.51735  20.80027  1.000 46.91364 ? 128 GLU A OE2 1 
ATOM   1013 N  N   . VAL A 1 129 ? 12.54891  27.22587  21.65949  1.000 29.09340 ? 129 VAL A N   1 
ATOM   1014 C  CA  . VAL A 1 129 ? 11.42614  26.49281  22.23816  1.000 27.04257 ? 129 VAL A CA  1 
ATOM   1015 C  C   . VAL A 1 129 ? 11.88303  25.69288  23.45446  1.000 26.39856 ? 129 VAL A C   1 
ATOM   1016 O  O   . VAL A 1 129 ? 11.23512  25.71360  24.50842  1.000 29.83318 ? 129 VAL A O   1 
ATOM   1017 C  CB  . VAL A 1 129 ? 10.76502  25.59377  21.17474  1.000 26.74139 ? 129 VAL A CB  1 
ATOM   1018 C  CG1 . VAL A 1 129 ? 9.80912   24.61121  21.82872  1.000 27.25418 ? 129 VAL A CG1 1 
ATOM   1019 C  CG2 . VAL A 1 129 ? 10.02069  26.44552  20.13873  1.000 27.99866 ? 129 VAL A CG2 1 
ATOM   1020 N  N   . VAL A 1 130 ? 13.00612  24.97605  23.32551  1.000 25.87093 ? 130 VAL A N   1 
ATOM   1021 C  CA  . VAL A 1 130 ? 13.51654  24.15985  24.42880  1.000 24.31861 ? 130 VAL A CA  1 
ATOM   1022 C  C   . VAL A 1 130 ? 13.80161  25.02465  25.64785  1.000 26.24437 ? 130 VAL A C   1 
ATOM   1023 O  O   . VAL A 1 130 ? 13.39639  24.70261  26.77334  1.000 27.52976 ? 130 VAL A O   1 
ATOM   1024 C  CB  . VAL A 1 130 ? 14.77466  23.38820  23.98654  1.000 22.48239 ? 130 VAL A CB  1 
ATOM   1025 C  CG1 . VAL A 1 130 ? 15.50763  22.81688  25.18618  1.000 24.47127 ? 130 VAL A CG1 1 
ATOM   1026 C  CG2 . VAL A 1 130 ? 14.40532  22.27999  23.01539  1.000 23.70988 ? 130 VAL A CG2 1 
ATOM   1027 N  N   . HIS A 1 131 ? 14.51500  26.12965  25.44574  1.000 26.55987 ? 131 HIS A N   1 
ATOM   1028 C  CA  . HIS A 1 131 ? 14.90482  26.95401  26.58352  1.000 30.66233 ? 131 HIS A CA  1 
ATOM   1029 C  C   . HIS A 1 131 ? 13.71297  27.70714  27.15900  1.000 31.22094 ? 131 HIS A C   1 
ATOM   1030 O  O   . HIS A 1 131 ? 13.67540  27.97866  28.36522  1.000 31.92312 ? 131 HIS A O   1 
ATOM   1031 C  CB  . HIS A 1 131 ? 16.02949  27.90607  26.17393  1.000 29.87784 ? 131 HIS A CB  1 
ATOM   1032 C  CG  . HIS A 1 131 ? 17.36894  27.23788  26.07650  1.000 32.29601 ? 131 HIS A CG  1 
ATOM   1033 N  ND1 . HIS A 1 131 ? 18.21161  27.10062  27.15910  1.000 35.49954 ? 131 HIS A ND1 1 
ATOM   1034 C  CD2 . HIS A 1 131 ? 17.99479  26.63780  25.03616  1.000 32.47589 ? 131 HIS A CD2 1 
ATOM   1035 C  CE1 . HIS A 1 131 ? 19.30634  26.46285  26.78517  1.000 34.69238 ? 131 HIS A CE1 1 
ATOM   1036 N  NE2 . HIS A 1 131 ? 19.20071  26.17116  25.50201  1.000 32.64904 ? 131 HIS A NE2 1 
ATOM   1037 N  N   . GLY A 1 132 ? 12.71652  28.00925  26.32740  1.000 31.26494 ? 132 GLY A N   1 
ATOM   1038 C  CA  . GLY A 1 132 ? 11.51601  28.65607  26.83123  1.000 30.84902 ? 132 GLY A CA  1 
ATOM   1039 C  C   . GLY A 1 132 ? 10.73068  27.77220  27.78001  1.000 31.74034 ? 132 GLY A C   1 
ATOM   1040 O  O   . GLY A 1 132 ? 10.32579  28.20721  28.85977  1.000 33.86011 ? 132 GLY A O   1 
ATOM   1041 N  N   . PHE A 1 133 ? 10.48911  26.51614  27.38593  1.000 27.55343 ? 133 PHE A N   1 
ATOM   1042 C  CA  . PHE A 1 133 ? 9.78509   25.61152  28.29027  1.000 29.08636 ? 133 PHE A CA  1 
ATOM   1043 C  C   . PHE A 1 133 ? 10.62523  25.28625  29.52104  1.000 29.68202 ? 133 PHE A C   1 
ATOM   1044 O  O   . PHE A 1 133 ? 10.06991  25.07419  30.60942  1.000 31.48030 ? 133 PHE A O   1 
ATOM   1045 C  CB  . PHE A 1 133 ? 9.35303   24.34192  27.54783  1.000 27.08042 ? 133 PHE A CB  1 
ATOM   1046 C  CG  . PHE A 1 133 ? 8.13055   24.54589  26.69323  1.000 26.58911 ? 133 PHE A CG  1 
ATOM   1047 C  CD1 . PHE A 1 133 ? 6.87842   24.68186  27.27312  1.000 28.88467 ? 133 PHE A CD1 1 
ATOM   1048 C  CD2 . PHE A 1 133 ? 8.23255   24.62448  25.31076  1.000 26.27581 ? 133 PHE A CD2 1 
ATOM   1049 C  CE1 . PHE A 1 133 ? 5.74697   24.88638  26.48884  1.000 28.90453 ? 133 PHE A CE1 1 
ATOM   1050 C  CE2 . PHE A 1 133 ? 7.10774   24.82636  24.52362  1.000 26.13382 ? 133 PHE A CE2 1 
ATOM   1051 C  CZ  . PHE A 1 133 ? 5.86588   24.96046  25.10992  1.000 27.24679 ? 133 PHE A CZ  1 
ATOM   1052 N  N   . LEU A 1 134 ? 11.95413  25.27932  29.38777  1.000 29.70338 ? 134 LEU A N   1 
ATOM   1053 C  CA  . LEU A 1 134 ? 12.80069  25.10439  30.56677  1.000 32.20161 ? 134 LEU A CA  1 
ATOM   1054 C  C   . LEU A 1 134 ? 12.67141  26.28675  31.51686  1.000 37.14398 ? 134 LEU A C   1 
ATOM   1055 O  O   . LEU A 1 134 ? 12.54361  26.10213  32.73461  1.000 40.34216 ? 134 LEU A O   1 
ATOM   1056 C  CB  . LEU A 1 134 ? 14.25733  24.90709  30.15492  1.000 31.56195 ? 134 LEU A CB  1 
ATOM   1057 C  CG  . LEU A 1 134 ? 14.65810  23.47683  29.80533  1.000 30.89493 ? 134 LEU A CG  1 
ATOM   1058 C  CD1 . LEU A 1 134 ? 16.14483  23.41992  29.48452  1.000 30.52187 ? 134 LEU A CD1 1 
ATOM   1059 C  CD2 . LEU A 1 134 ? 14.31694  22.51956  30.94857  1.000 31.61982 ? 134 LEU A CD2 1 
ATOM   1060 N  N   . ASP A 1 135 ? 12.72389  27.51085  30.98089  1.000 39.34358 ? 135 ASP A N   1 
ATOM   1061 C  CA  . ASP A 1 135 ? 12.47358  28.70199  31.79217  1.000 40.56346 ? 135 ASP A CA  1 
ATOM   1062 C  C   . ASP A 1 135 ? 11.21268  28.54126  32.63040  1.000 39.16749 ? 135 ASP A C   1 
ATOM   1063 O  O   . ASP A 1 135 ? 11.21911  28.77513  33.84720  1.000 40.35078 ? 135 ASP A O   1 
ATOM   1064 C  CB  . ASP A 1 135 ? 12.33349  29.93713  30.89582  1.000 43.83491 ? 135 ASP A CB  1 
ATOM   1065 C  CG  . ASP A 1 135 ? 13.63759  30.36156  30.25675  1.000 47.49531 ? 135 ASP A CG  1 
ATOM   1066 O  OD1 . ASP A 1 135 ? 14.70516  29.85882  30.66202  1.000 49.81670 ? 135 ASP A OD1 1 
ATOM   1067 O  OD2 . ASP A 1 135 ? 13.58548  31.20167  29.33258  1.000 48.89575 ? 135 ASP A OD2 1 
ATOM   1068 N  N   . GLU A 1 136 ? 10.11489  28.14132  31.98495  1.000 37.96462 ? 136 GLU A N   1 
ATOM   1069 C  CA  . GLU A 1 136 ? 8.83251   28.04838  32.67096  1.000 36.21297 ? 136 GLU A CA  1 
ATOM   1070 C  C   . GLU A 1 136 ? 8.85614   26.96092  33.73775  1.000 36.25856 ? 136 GLU A C   1 
ATOM   1071 O  O   . GLU A 1 136 ? 8.41404   27.18084  34.86964  1.000 37.55261 ? 136 GLU A O   1 
ATOM   1072 C  CB  . GLU A 1 136 ? 7.71295   27.79844  31.65493  1.000 36.45822 ? 136 GLU A CB  1 
ATOM   1073 C  CG  . GLU A 1 136 ? 6.32952   27.74400  32.27455  1.000 35.32898 ? 136 GLU A CG  1 
ATOM   1074 C  CD  . GLU A 1 136 ? 5.21307   27.80288  31.25163  1.000 39.48669 ? 136 GLU A CD  1 
ATOM   1075 O  OE1 . GLU A 1 136 ? 5.47919   27.60833  30.03998  1.000 37.72877 ? 136 GLU A OE1 1 
ATOM   1076 O  OE2 . GLU A 1 136 ? 4.05990   28.05021  31.66535  1.000 42.01471 ? 136 GLU A OE2 1 
ATOM   1077 N  N   . MET A 1 137 ? 9.38727   25.78341  33.40047  1.000 34.83300 ? 137 MET A N   1 
ATOM   1078 C  CA  . MET A 1 137 ? 9.38906   24.67471  34.34876  1.000 34.94144 ? 137 MET A CA  1 
ATOM   1079 C  C   . MET A 1 137 ? 10.23847  24.99427  35.57178  1.000 40.04009 ? 137 MET A C   1 
ATOM   1080 O  O   . MET A 1 137 ? 9.80869   24.78257  36.71441  1.000 42.25488 ? 137 MET A O   1 
ATOM   1081 C  CB  . MET A 1 137 ? 9.89276   23.40697  33.66162  1.000 34.22090 ? 137 MET A CB  1 
ATOM   1082 C  CG  . MET A 1 137 ? 9.80001   22.16725  34.52732  1.000 35.39537 ? 137 MET A CG  1 
ATOM   1083 S  SD  . MET A 1 137 ? 10.58490  20.76111  33.74200  1.000 34.29789 ? 137 MET A SD  1 
ATOM   1084 C  CE  . MET A 1 137 ? 12.32077  21.15160  33.96787  1.000 36.92482 ? 137 MET A CE  1 
ATOM   1085 N  N   . LEU A 1 138 ? 11.45261  25.50977  35.35130  1.000 42.46701 ? 138 LEU A N   1 
ATOM   1086 C  CA  . LEU A 1 138 ? 12.34258  25.80787  36.47019  1.000 45.90269 ? 138 LEU A CA  1 
ATOM   1087 C  C   . LEU A 1 138 ? 11.76239  26.88124  37.37798  1.000 47.90737 ? 138 LEU A C   1 
ATOM   1088 O  O   . LEU A 1 138 ? 12.02687  26.88362  38.58574  1.000 52.26903 ? 138 LEU A O   1 
ATOM   1089 C  CB  . LEU A 1 138 ? 13.71660  26.23772  35.95293  1.000 46.69846 ? 138 LEU A CB  1 
ATOM   1090 C  CG  . LEU A 1 138 ? 14.45961  25.17272  35.14131  1.000 48.10215 ? 138 LEU A CG  1 
ATOM   1091 C  CD1 . LEU A 1 138 ? 15.74717  25.72667  34.54423  1.000 48.08847 ? 138 LEU A CD1 1 
ATOM   1092 C  CD2 . LEU A 1 138 ? 14.74187  23.95145  36.00831  1.000 51.55128 ? 138 LEU A CD2 1 
ATOM   1093 N  N   . ALA A 1 139 ? 10.96172  27.79045  36.82595  1.000 44.96801 ? 139 ALA A N   1 
ATOM   1094 C  CA  . ALA A 1 139 ? 10.38538  28.85250  37.63818  1.000 44.02183 ? 139 ALA A CA  1 
ATOM   1095 C  C   . ALA A 1 139 ? 9.10838   28.43046  38.35284  1.000 48.20211 ? 139 ALA A C   1 
ATOM   1096 O  O   . ALA A 1 139 ? 8.73652   29.06133  39.34911  1.000 53.44826 ? 139 ALA A O   1 
ATOM   1097 C  CB  . ALA A 1 139 ? 10.10924  30.07797  36.76728  1.000 43.17186 ? 139 ALA A CB  1 
ATOM   1098 N  N   . ALA A 1 140 ? 8.44327   27.37566  37.88646  1.000 50.62720 ? 140 ALA A N   1 
ATOM   1099 C  CA  . ALA A 1 140 ? 7.09965   27.03860  38.33995  1.000 52.71527 ? 140 ALA A CA  1 
ATOM   1100 C  C   . ALA A 1 140 ? 7.06631   26.20952  39.61766  1.000 55.19013 ? 140 ALA A C   1 
ATOM   1101 O  O   . ALA A 1 140 ? 5.99005   26.06148  40.20703  1.000 58.57437 ? 140 ALA A O   1 
ATOM   1102 C  CB  . ALA A 1 140 ? 6.34698   26.28967  37.23279  1.000 53.02676 ? 140 ALA A CB  1 
ATOM   1103 N  N   . GLY A 1 141 ? 8.19443   25.66584  40.06480  1.000 53.87621 ? 141 GLY A N   1 
ATOM   1104 C  CA  . GLY A 1 141 ? 8.20408   24.88437  41.27830  1.000 53.36505 ? 141 GLY A CA  1 
ATOM   1105 C  C   . GLY A 1 141 ? 9.48276   24.09629  41.46832  1.000 52.42900 ? 141 GLY A C   1 
ATOM   1106 O  O   . GLY A 1 141 ? 10.31149  23.98952  40.56333  1.000 51.24490 ? 141 GLY A O   1 
ATOM   1107 N  N   . PRO A 1 142 ? 9.67340   23.54021  42.67001  1.000 52.78070 ? 142 PRO A N   1 
ATOM   1108 C  CA  . PRO A 1 142 ? 10.86673  22.71624  42.91539  1.000 50.24610 ? 142 PRO A CA  1 
ATOM   1109 C  C   . PRO A 1 142 ? 10.79858  21.34544  42.27138  1.000 45.70842 ? 142 PRO A C   1 
ATOM   1110 O  O   . PRO A 1 142 ? 11.85068  20.74752  42.01061  1.000 44.01882 ? 142 PRO A O   1 
ATOM   1111 C  CB  . PRO A 1 142 ? 10.91320  22.61251  44.44494  1.000 52.60996 ? 142 PRO A CB  1 
ATOM   1112 C  CG  . PRO A 1 142 ? 9.49072   22.76188  44.86905  1.000 54.29604 ? 142 PRO A CG  1 
ATOM   1113 C  CD  . PRO A 1 142 ? 8.85867   23.71644  43.88276  1.000 54.91415 ? 142 PRO A CD  1 
ATOM   1114 N  N   . THR A 1 143 ? 9.60712   20.82068  42.02138  1.000 40.22586 ? 143 THR A N   1 
ATOM   1115 C  CA  . THR A 1 143 ? 9.44560   19.57420  41.29113  1.000 38.84462 ? 143 THR A CA  1 
ATOM   1116 C  C   . THR A 1 143 ? 8.62656   19.82999  40.03659  1.000 35.01769 ? 143 THR A C   1 
ATOM   1117 O  O   . THR A 1 143 ? 7.99725   20.88047  39.87761  1.000 36.51012 ? 143 THR A O   1 
ATOM   1118 C  CB  . THR A 1 143 ? 8.76106   18.50628  42.14764  1.000 40.88202 ? 143 THR A CB  1 
ATOM   1119 O  OG1 . THR A 1 143 ? 7.44391   18.95180  42.48488  1.000 40.83752 ? 143 THR A OG1 1 
ATOM   1120 C  CG2 . THR A 1 143 ? 9.55474   18.26113  43.42368  1.000 42.84629 ? 143 THR A CG2 1 
ATOM   1121 N  N   . ALA A 1 144 ? 8.63571   18.84501  39.14294  1.000 29.07581 ? 144 ALA A N   1 
ATOM   1122 C  CA  . ALA A 1 144 ? 7.85688   18.93888  37.91834  1.000 28.99148 ? 144 ALA A CA  1 
ATOM   1123 C  C   . ALA A 1 144 ? 7.60358   17.53975  37.38265  1.000 29.45575 ? 144 ALA A C   1 
ATOM   1124 O  O   . ALA A 1 144 ? 8.32809   16.59443  37.69707  1.000 31.00810 ? 144 ALA A O   1 
ATOM   1125 C  CB  . ALA A 1 144 ? 8.57638   19.78279  36.85870  1.000 31.10316 ? 144 ALA A CB  1 
ATOM   1126 N  N   . ASP A 1 145 ? 6.55791   17.42170  36.56771  1.000 25.89864 ? 145 ASP A N   1 
ATOM   1127 C  CA  . ASP A 1 145 ? 6.40742   16.28637  35.66200  1.000 25.26269 ? 145 ASP A CA  1 
ATOM   1128 C  C   . ASP A 1 145 ? 7.12191   16.63781  34.36158  1.000 24.00868 ? 145 ASP A C   1 
ATOM   1129 O  O   . ASP A 1 145 ? 6.66126   17.50607  33.61663  1.000 25.99736 ? 145 ASP A O   1 
ATOM   1130 C  CB  . ASP A 1 145 ? 4.93432   15.97609  35.40814  1.000 26.98704 ? 145 ASP A CB  1 
ATOM   1131 C  CG  . ASP A 1 145 ? 4.73091   15.02346  34.23125  1.000 29.23724 ? 145 ASP A CG  1 
ATOM   1132 O  OD1 . ASP A 1 145 ? 5.62468   14.18889  33.97297  1.000 28.95143 ? 145 ASP A OD1 1 
ATOM   1133 O  OD2 . ASP A 1 145 ? 3.68492   15.12593  33.54912  1.000 32.32939 ? 145 ASP A OD2 1 
ATOM   1134 N  N   . LEU A 1 146 ? 8.25079   15.97251  34.09395  1.000 23.51909 ? 146 LEU A N   1 
ATOM   1135 C  CA  . LEU A 1 146 ? 9.03394   16.30153  32.90701  1.000 23.14585 ? 146 LEU A CA  1 
ATOM   1136 C  C   . LEU A 1 146 ? 8.24548   16.07011  31.62443  1.000 24.01807 ? 146 LEU A C   1 
ATOM   1137 O  O   . LEU A 1 146 ? 8.51889   16.71899  30.61062  1.000 21.99976 ? 146 LEU A O   1 
ATOM   1138 C  CB  . LEU A 1 146 ? 10.32404  15.48201  32.86811  1.000 23.08443 ? 146 LEU A CB  1 
ATOM   1139 C  CG  . LEU A 1 146 ? 11.37252  15.98642  31.87004  1.000 25.46341 ? 146 LEU A CG  1 
ATOM   1140 C  CD1 . LEU A 1 146 ? 12.06338  17.23883  32.39562  1.000 25.52407 ? 146 LEU A CD1 1 
ATOM   1141 C  CD2 . LEU A 1 146 ? 12.38677  14.90278  31.54134  1.000 28.59668 ? 146 LEU A CD2 1 
ATOM   1142 N  N   . VAL A 1 147 ? 7.27873   15.15281  31.64102  1.000 24.20795 ? 147 VAL A N   1 
ATOM   1143 C  CA  . VAL A 1 147 ? 6.54603   14.82863  30.41567  1.000 23.46563 ? 147 VAL A CA  1 
ATOM   1144 C  C   . VAL A 1 147 ? 5.63161   15.98271  30.01913  1.000 25.38211 ? 147 VAL A C   1 
ATOM   1145 O  O   . VAL A 1 147 ? 5.77246   16.57311  28.93870  1.000 23.84311 ? 147 VAL A O   1 
ATOM   1146 C  CB  . VAL A 1 147 ? 5.75796   13.51506  30.58208  1.000 24.03388 ? 147 VAL A CB  1 
ATOM   1147 C  CG1 . VAL A 1 147 ? 4.95073   13.20606  29.31686  1.000 23.14527 ? 147 VAL A CG1 1 
ATOM   1148 C  CG2 . VAL A 1 147 ? 6.69554   12.36794  30.89425  1.000 25.35121 ? 147 VAL A CG2 1 
ATOM   1149 N  N   . SER A 1 148 ? 4.68186   16.32499  30.88875  1.000 23.79995 ? 148 SER A N   1 
ATOM   1150 C  CA  . SER A 1 148 ? 3.71277   17.35585  30.53525  1.000 24.77223 ? 148 SER A CA  1 
ATOM   1151 C  C   . SER A 1 148 ? 4.33082   18.75069  30.49548  1.000 27.48201 ? 148 SER A C   1 
ATOM   1152 O  O   . SER A 1 148 ? 3.81535   19.62770  29.79397  1.000 27.75429 ? 148 SER A O   1 
ATOM   1153 C  CB  . SER A 1 148 ? 2.54098   17.33380  31.51555  1.000 25.61206 ? 148 SER A CB  1 
ATOM   1154 O  OG  . SER A 1 148 ? 2.97956   17.61652  32.83241  1.000 26.42399 ? 148 SER A OG  1 
ATOM   1155 N  N   . GLN A 1 149 ? 5.42140   18.99280  31.22767  1.000 24.97272 ? 149 GLN A N   1 
ATOM   1156 C  CA  A GLN A 1 149 ? 6.00081   20.32807  31.31139  0.378 25.44875 ? 149 GLN A CA  1 
ATOM   1157 C  CA  B GLN A 1 149 ? 5.97985   20.33670  31.28999  0.622 25.99941 ? 149 GLN A CA  1 
ATOM   1158 C  C   . GLN A 1 149 ? 7.14237   20.55873  30.32903  1.000 24.35145 ? 149 GLN A C   1 
ATOM   1159 O  O   . GLN A 1 149 ? 7.54284   21.70853  30.12815  1.000 26.39741 ? 149 GLN A O   1 
ATOM   1160 C  CB  A GLN A 1 149 ? 6.50142   20.60477  32.73725  0.378 26.39614 ? 149 GLN A CB  1 
ATOM   1161 C  CB  B GLN A 1 149 ? 6.41576   20.66427  32.72854  0.622 27.98279 ? 149 GLN A CB  1 
ATOM   1162 C  CG  A GLN A 1 149 ? 5.45448   20.38555  33.81616  0.378 27.24590 ? 149 GLN A CG  1 
ATOM   1163 C  CG  B GLN A 1 149 ? 5.23542   20.78330  33.69060  0.622 30.00312 ? 149 GLN A CG  1 
ATOM   1164 C  CD  A GLN A 1 149 ? 4.16974   21.13492  33.53865  0.378 29.21410 ? 149 GLN A CD  1 
ATOM   1165 C  CD  B GLN A 1 149 ? 5.64710   21.01204  35.13279  0.622 32.62594 ? 149 GLN A CD  1 
ATOM   1166 O  OE1 A GLN A 1 149 ? 3.10515   20.53257  33.39722  0.378 32.06197 ? 149 GLN A OE1 1 
ATOM   1167 O  OE1 B GLN A 1 149 ? 5.38718   20.17689  36.00474  0.622 33.36113 ? 149 GLN A OE1 1 
ATOM   1168 N  NE2 A GLN A 1 149 ? 4.26149   22.45616  33.45705  0.378 28.70292 ? 149 GLN A NE2 1 
ATOM   1169 N  NE2 B GLN A 1 149 ? 6.27909   22.15234  35.39518  0.622 32.91684 ? 149 GLN A NE2 1 
ATOM   1170 N  N   . PHE A 1 150 ? 7.67369   19.50908  29.70374  1.000 22.68716 ? 150 PHE A N   1 
ATOM   1171 C  CA  . PHE A 1 150 ? 8.84507   19.71959  28.85897  1.000 20.62599 ? 150 PHE A CA  1 
ATOM   1172 C  C   . PHE A 1 150 ? 8.91329   18.74601  27.68741  1.000 21.90483 ? 150 PHE A C   1 
ATOM   1173 O  O   . PHE A 1 150 ? 9.02192   19.17002  26.53103  1.000 21.14193 ? 150 PHE A O   1 
ATOM   1174 C  CB  . PHE A 1 150 ? 10.11531  19.62023  29.71514  1.000 21.00323 ? 150 PHE A CB  1 
ATOM   1175 C  CG  . PHE A 1 150 ? 11.39005  19.79709  28.93926  1.000 21.50235 ? 150 PHE A CG  1 
ATOM   1176 C  CD1 . PHE A 1 150 ? 11.72932  21.03046  28.40765  1.000 22.50971 ? 150 PHE A CD1 1 
ATOM   1177 C  CD2 . PHE A 1 150 ? 12.25772  18.72297  28.75362  1.000 22.19836 ? 150 PHE A CD2 1 
ATOM   1178 C  CE1 . PHE A 1 150 ? 12.90341  21.19637  27.68884  1.000 20.94454 ? 150 PHE A CE1 1 
ATOM   1179 C  CE2 . PHE A 1 150 ? 13.43355  18.87680  28.03830  1.000 23.17297 ? 150 PHE A CE2 1 
ATOM   1180 C  CZ  . PHE A 1 150 ? 13.75827  20.12485  27.50060  1.000 23.09943 ? 150 PHE A CZ  1 
ATOM   1181 N  N   . ALA A 1 151 ? 8.85431   17.44420  27.97549  1.000 22.00245 ? 151 ALA A N   1 
ATOM   1182 C  CA  . ALA A 1 151 ? 9.11115   16.44695  26.93677  1.000 20.68795 ? 151 ALA A CA  1 
ATOM   1183 C  C   . ALA A 1 151 ? 8.07717   16.50773  25.81803  1.000 19.00439 ? 151 ALA A C   1 
ATOM   1184 O  O   . ALA A 1 151 ? 8.41765   16.31582  24.64131  1.000 20.62028 ? 151 ALA A O   1 
ATOM   1185 C  CB  . ALA A 1 151 ? 9.14987   15.04341  27.54379  1.000 20.78986 ? 151 ALA A CB  1 
ATOM   1186 N  N   . LEU A 1 152 ? 6.80915   16.73343  26.15621  1.000 18.17759 ? 152 LEU A N   1 
ATOM   1187 C  CA  . LEU A 1 152 ? 5.77765   16.78701  25.12266  1.000 20.18667 ? 152 LEU A CA  1 
ATOM   1188 C  C   . LEU A 1 152 ? 5.60953   18.17560  24.49386  1.000 23.04602 ? 152 LEU A C   1 
ATOM   1189 O  O   . LEU A 1 152 ? 5.51183   18.26702  23.26080  1.000 23.09445 ? 152 LEU A O   1 
ATOM   1190 C  CB  . LEU A 1 152 ? 4.43357   16.30458  25.67611  1.000 24.81081 ? 152 LEU A CB  1 
ATOM   1191 C  CG  . LEU A 1 152 ? 3.33385   16.33479  24.60787  1.000 29.71451 ? 152 LEU A CG  1 
ATOM   1192 C  CD1 . LEU A 1 152 ? 3.55527   15.22497  23.56468  1.000 30.40779 ? 152 LEU A CD1 1 
ATOM   1193 C  CD2 . LEU A 1 152 ? 1.94997   16.26554  25.21628  1.000 40.41558 ? 152 LEU A CD2 1 
ATOM   1194 N  N   . PRO A 1 153 ? 5.53355   19.27396  25.26921  1.000 22.21353 ? 153 PRO A N   1 
ATOM   1195 C  CA  . PRO A 1 153 ? 5.26491   20.57415  24.62469  1.000 23.73420 ? 153 PRO A CA  1 
ATOM   1196 C  C   . PRO A 1 153 ? 6.32710   20.98841  23.62167  1.000 22.93249 ? 153 PRO A C   1 
ATOM   1197 O  O   . PRO A 1 153 ? 5.99483   21.60492  22.60118  1.000 24.97762 ? 153 PRO A O   1 
ATOM   1198 C  CB  . PRO A 1 153 ? 5.19718   21.55564  25.80807  1.000 26.42785 ? 153 PRO A CB  1 
ATOM   1199 C  CG  . PRO A 1 153 ? 4.96554   20.72826  26.99390  1.000 29.40498 ? 153 PRO A CG  1 
ATOM   1200 C  CD  . PRO A 1 153 ? 5.58006   19.40426  26.74031  1.000 24.80413 ? 153 PRO A CD  1 
ATOM   1201 N  N   . VAL A 1 154 ? 7.59241   20.65538  23.86557  1.000 22.26777 ? 154 VAL A N   1 
ATOM   1202 C  CA  . VAL A 1 154 ? 8.66916   21.09468  22.97768  1.000 22.82954 ? 154 VAL A CA  1 
ATOM   1203 C  C   . VAL A 1 154 ? 8.47762   20.53401  21.56764  1.000 21.45295 ? 154 VAL A C   1 
ATOM   1204 O  O   . VAL A 1 154 ? 8.32698   21.32915  20.63147  1.000 19.76888 ? 154 VAL A O   1 
ATOM   1205 C  CB  . VAL A 1 154 ? 10.05066  20.74820  23.56169  1.000 20.31467 ? 154 VAL A CB  1 
ATOM   1206 C  CG1 . VAL A 1 154 ? 11.12856  20.83160  22.47833  1.000 20.46239 ? 154 VAL A CG1 1 
ATOM   1207 C  CG2 . VAL A 1 154 ? 10.35817  21.67003  24.75942  1.000 23.27847 ? 154 VAL A CG2 1 
ATOM   1208 N  N   . PRO A 1 155 ? 8.43968   19.21242  21.34131  1.000 21.19289 ? 155 PRO A N   1 
ATOM   1209 C  CA  . PRO A 1 155 ? 8.24414   18.74643  19.95538  1.000 19.58104 ? 155 PRO A CA  1 
ATOM   1210 C  C   . PRO A 1 155 ? 6.87310   19.08929  19.40001  1.000 18.20425 ? 155 PRO A C   1 
ATOM   1211 O  O   . PRO A 1 155 ? 6.73088   19.21705  18.17633  1.000 19.86388 ? 155 PRO A O   1 
ATOM   1212 C  CB  . PRO A 1 155 ? 8.45505   17.22548  20.05021  1.000 19.28463 ? 155 PRO A CB  1 
ATOM   1213 C  CG  . PRO A 1 155 ? 8.15056   16.89468  21.47393  1.000 17.09762 ? 155 PRO A CG  1 
ATOM   1214 C  CD  . PRO A 1 155 ? 8.60495   18.08248  22.27598  1.000 20.35800 ? 155 PRO A CD  1 
ATOM   1215 N  N   . SER A 1 156 ? 5.86408   19.22950  20.26222  1.000 19.64629 ? 156 SER A N   1 
ATOM   1216 C  CA  . SER A 1 156 ? 4.54611   19.66859  19.81373  1.000 19.04637 ? 156 SER A CA  1 
ATOM   1217 C  C   . SER A 1 156 ? 4.61813   21.04360  19.15960  1.000 20.24032 ? 156 SER A C   1 
ATOM   1218 O  O   . SER A 1 156 ? 4.13163   21.24495  18.04071  1.000 22.73482 ? 156 SER A O   1 
ATOM   1219 C  CB  . SER A 1 156 ? 3.57997   19.69201  21.00341  1.000 21.04304 ? 156 SER A CB  1 
ATOM   1220 O  OG  . SER A 1 156 ? 2.26971   20.05938  20.58295  1.000 26.45404 ? 156 SER A OG  1 
ATOM   1221 N  N   . MET A 1 157 ? 5.23454   22.00467  19.84327  1.000 20.82719 ? 157 MET A N   1 
ATOM   1222 C  CA  . MET A 1 157 ? 5.31974   23.35417  19.29771  1.000 20.73922 ? 157 MET A CA  1 
ATOM   1223 C  C   . MET A 1 157 ? 6.13910   23.37463  18.01164  1.000 17.80481 ? 157 MET A C   1 
ATOM   1224 O  O   . MET A 1 157 ? 5.78122   24.06224  17.04429  1.000 19.92687 ? 157 MET A O   1 
ATOM   1225 C  CB  . MET A 1 157 ? 5.90933   24.29224  20.35114  1.000 21.58635 ? 157 MET A CB  1 
ATOM   1226 C  CG  . MET A 1 157 ? 6.15126   25.70817  19.84575  1.000 23.75284 ? 157 MET A CG  1 
ATOM   1227 S  SD  . MET A 1 157 ? 6.44813   26.87990  21.19523  1.000 28.27815 ? 157 MET A SD  1 
ATOM   1228 C  CE  . MET A 1 157 ? 4.82396   26.99988  21.94645  1.000 30.46239 ? 157 MET A CE  1 
ATOM   1229 N  N   . VAL A 1 158 ? 7.21577   22.58749  17.96285  1.000 17.76136 ? 158 VAL A N   1 
ATOM   1230 C  CA  . VAL A 1 158 ? 8.06417   22.55558  16.77490  1.000 19.06191 ? 158 VAL A CA  1 
ATOM   1231 C  C   . VAL A 1 158 ? 7.30899   21.96504  15.58527  1.000 15.60743 ? 158 VAL A C   1 
ATOM   1232 O  O   . VAL A 1 158 ? 7.31752   22.53609  14.48558  1.000 18.80910 ? 158 VAL A O   1 
ATOM   1233 C  CB  . VAL A 1 158 ? 9.36288   21.77693  17.06474  1.000 18.48324 ? 158 VAL A CB  1 
ATOM   1234 C  CG1 . VAL A 1 158 ? 10.18404  21.58021  15.77376  1.000 19.43594 ? 158 VAL A CG1 1 
ATOM   1235 C  CG2 . VAL A 1 158 ? 10.18886  22.49996  18.13573  1.000 19.50942 ? 158 VAL A CG2 1 
ATOM   1236 N  N   . ILE A 1 159 ? 6.64669   20.81499  15.77180  1.000 17.39170 ? 159 ILE A N   1 
ATOM   1237 C  CA  . ILE A 1 159 ? 5.98589   20.20832  14.61291  1.000 18.49840 ? 159 ILE A CA  1 
ATOM   1238 C  C   . ILE A 1 159 ? 4.78200   21.04557  14.18160  1.000 21.52281 ? 159 ILE A C   1 
ATOM   1239 O  O   . ILE A 1 159 ? 4.46264   21.11455  12.98731  1.000 19.13557 ? 159 ILE A O   1 
ATOM   1240 C  CB  . ILE A 1 159 ? 5.60276   18.73410  14.87800  1.000 18.70898 ? 159 ILE A CB  1 
ATOM   1241 C  CG1 . ILE A 1 159 ? 5.29410   18.00970  13.56155  1.000 19.49557 ? 159 ILE A CG1 1 
ATOM   1242 C  CG2 . ILE A 1 159 ? 4.39051   18.61812  15.79882  1.000 19.64892 ? 159 ILE A CG2 1 
ATOM   1243 C  CD1 . ILE A 1 159 ? 6.49465   17.79959  12.65745  1.000 21.94878 ? 159 ILE A CD1 1 
ATOM   1244 N  N   . CYS A 1 160 ? 4.12779   21.73994  15.11697  1.000 20.11846 ? 160 CYS A N   1 
ATOM   1245 C  CA  . CYS A 1 160 ? 2.99734   22.57401  14.72102  1.000 19.35116 ? 160 CYS A CA  1 
ATOM   1246 C  C   . CYS A 1 160 ? 3.45102   23.74380  13.85532  1.000 20.03592 ? 160 CYS A C   1 
ATOM   1247 O  O   . CYS A 1 160 ? 2.75853   24.11476  12.90009  1.000 21.87608 ? 160 CYS A O   1 
ATOM   1248 C  CB  . CYS A 1 160 ? 2.24005   23.07040  15.95646  1.000 22.29010 ? 160 CYS A CB  1 
ATOM   1249 S  SG  . CYS A 1 160 ? 1.22268   21.77891  16.71686  1.000 27.04577 ? 160 CYS A SG  1 
ATOM   1250 N  N   . ARG A 1 161 ? 4.61324   24.33264  14.16216  1.000 22.21795 ? 161 ARG A N   1 
ATOM   1251 C  CA  . ARG A 1 161 ? 5.15580   25.38466  13.30047  1.000 22.28005 ? 161 ARG A CA  1 
ATOM   1252 C  C   . ARG A 1 161 ? 5.48213   24.84638  11.91475  1.000 21.35597 ? 161 ARG A C   1 
ATOM   1253 O  O   . ARG A 1 161 ? 5.22285   25.50874  10.89927  1.000 22.06073 ? 161 ARG A O   1 
ATOM   1254 C  CB  . ARG A 1 161 ? 6.40790   25.99721  13.92887  1.000 25.65218 ? 161 ARG A CB  1 
ATOM   1255 C  CG  . ARG A 1 161 ? 6.10634   27.02906  14.98106  1.000 30.84696 ? 161 ARG A CG  1 
ATOM   1256 C  CD  . ARG A 1 161 ? 5.25602   28.15544  14.41195  1.000 37.21312 ? 161 ARG A CD  1 
ATOM   1257 N  NE  . ARG A 1 161 ? 4.90654   29.13112  15.43662  1.000 38.97841 ? 161 ARG A NE  1 
ATOM   1258 C  CZ  . ARG A 1 161 ? 3.98540   30.07225  15.28368  1.000 40.95794 ? 161 ARG A CZ  1 
ATOM   1259 N  NH1 . ARG A 1 161 ? 3.30247   30.19397  14.15357  1.000 38.90854 ? 161 ARG A NH1 1 
ATOM   1260 N  NH2 . ARG A 1 161 ? 3.75093   30.91950  16.28252  1.000 41.39634 ? 161 ARG A NH2 1 
ATOM   1261 N  N   . LEU A 1 162 ? 6.06276   23.65165  11.85242  1.000 19.90583 ? 162 LEU A N   1 
ATOM   1262 C  CA  . LEU A 1 162 ? 6.38105   23.05485  10.55668  1.000 18.79041 ? 162 LEU A CA  1 
ATOM   1263 C  C   . LEU A 1 162 ? 5.11884   22.81990  9.73346   1.000 19.73643 ? 162 LEU A C   1 
ATOM   1264 O  O   . LEU A 1 162 ? 5.10352   23.05272  8.51354   1.000 20.35853 ? 162 LEU A O   1 
ATOM   1265 C  CB  . LEU A 1 162 ? 7.13599   21.73649  10.76582  1.000 19.61331 ? 162 LEU A CB  1 
ATOM   1266 C  CG  . LEU A 1 162 ? 7.61228   20.96395  9.52749   1.000 20.61415 ? 162 LEU A CG  1 
ATOM   1267 C  CD1 . LEU A 1 162 ? 8.88667   20.20657  9.85438   1.000 21.22097 ? 162 LEU A CD1 1 
ATOM   1268 C  CD2 . LEU A 1 162 ? 6.55035   19.98972  8.97090   1.000 21.41514 ? 162 LEU A CD2 1 
ATOM   1269 N  N   . LEU A 1 163 ? 4.05212   22.35280  10.38365  1.000 17.82991 ? 163 LEU A N   1 
ATOM   1270 C  CA  . LEU A 1 163 ? 2.81927   21.99610  9.69301   1.000 17.82843 ? 163 LEU A CA  1 
ATOM   1271 C  C   . LEU A 1 163 ? 1.91071   23.18574  9.40676   1.000 18.75371 ? 163 LEU A C   1 
ATOM   1272 O  O   . LEU A 1 163 ? 1.07401   23.09697  8.49958   1.000 18.79517 ? 163 LEU A O   1 
ATOM   1273 C  CB  . LEU A 1 163 ? 2.03750   20.96791  10.51447  1.000 19.12565 ? 163 LEU A CB  1 
ATOM   1274 C  CG  . LEU A 1 163 ? 2.65266   19.57606  10.64017  1.000 19.54030 ? 163 LEU A CG  1 
ATOM   1275 C  CD1 . LEU A 1 163 ? 1.88044   18.77297  11.68539  1.000 20.08194 ? 163 LEU A CD1 1 
ATOM   1276 C  CD2 . LEU A 1 163 ? 2.64332   18.88781  9.26757   1.000 20.72892 ? 163 LEU A CD2 1 
ATOM   1277 N  N   . GLY A 1 164 ? 2.02911   24.27730  10.16082  1.000 18.92035 ? 164 GLY A N   1 
ATOM   1278 C  CA  . GLY A 1 164 ? 1.04253   25.33595  10.06818  1.000 19.76418 ? 164 GLY A CA  1 
ATOM   1279 C  C   . GLY A 1 164 ? -0.17654  25.11962  10.93523  1.000 19.18927 ? 164 GLY A C   1 
ATOM   1280 O  O   . GLY A 1 164 ? -1.23145  25.70956  10.67025  1.000 22.11228 ? 164 GLY A O   1 
ATOM   1281 N  N   . VAL A 1 165 ? -0.06084  24.28521  11.96334  1.000 20.45920 ? 165 VAL A N   1 
ATOM   1282 C  CA  . VAL A 1 165 ? -1.14857  24.02188  12.89913  1.000 21.55849 ? 165 VAL A CA  1 
ATOM   1283 C  C   . VAL A 1 165 ? -1.02311  25.01517  14.05364  1.000 21.50346 ? 165 VAL A C   1 
ATOM   1284 O  O   . VAL A 1 165 ? 0.04908   25.09168  14.66654  1.000 23.65666 ? 165 VAL A O   1 
ATOM   1285 C  CB  . VAL A 1 165 ? -1.08803  22.57872  13.41395  1.000 21.79209 ? 165 VAL A CB  1 
ATOM   1286 C  CG1 . VAL A 1 165 ? -2.06367  22.37848  14.56959  1.000 23.82658 ? 165 VAL A CG1 1 
ATOM   1287 C  CG2 . VAL A 1 165 ? -1.36277  21.59109  12.27133  1.000 20.73009 ? 165 VAL A CG2 1 
ATOM   1288 N  N   . PRO A 1 166 ? -2.06162  25.78957  14.37116  1.000 20.56832 ? 166 PRO A N   1 
ATOM   1289 C  CA  . PRO A 1 166 ? -1.90999  26.83665  15.39732  1.000 21.71867 ? 166 PRO A CA  1 
ATOM   1290 C  C   . PRO A 1 166 ? -1.79295  26.24647  16.79927  1.000 26.06550 ? 166 PRO A C   1 
ATOM   1291 O  O   . PRO A 1 166 ? -2.63775  25.46024  17.23556  1.000 25.68034 ? 166 PRO A O   1 
ATOM   1292 C  CB  . PRO A 1 166 ? -3.18196  27.67761  15.24045  1.000 24.79914 ? 166 PRO A CB  1 
ATOM   1293 C  CG  . PRO A 1 166 ? -4.16482  26.77478  14.60988  1.000 25.36494 ? 166 PRO A CG  1 
ATOM   1294 C  CD  . PRO A 1 166 ? -3.37938  25.84042  13.71507  1.000 22.09520 ? 166 PRO A CD  1 
ATOM   1295 N  N   . TYR A 1 167 ? -0.74138  26.64533  17.51652  1.000 25.49690 ? 167 TYR A N   1 
ATOM   1296 C  CA  . TYR A 1 167 ? -0.52564  26.05826  18.83399  1.000 27.75951 ? 167 TYR A CA  1 
ATOM   1297 C  C   . TYR A 1 167 ? -1.57579  26.48179  19.85230  1.000 31.00750 ? 167 TYR A C   1 
ATOM   1298 O  O   . TYR A 1 167 ? -1.68788  25.82743  20.89324  1.000 34.82501 ? 167 TYR A O   1 
ATOM   1299 C  CB  . TYR A 1 167 ? 0.87029   26.39734  19.35950  1.000 26.96769 ? 167 TYR A CB  1 
ATOM   1300 C  CG  . TYR A 1 167 ? 1.31315   25.51494  20.52094  1.000 28.86804 ? 167 TYR A CG  1 
ATOM   1301 C  CD1 . TYR A 1 167 ? 1.77089   24.22513  20.29451  1.000 27.16940 ? 167 TYR A CD1 1 
ATOM   1302 C  CD2 . TYR A 1 167 ? 1.26106   25.96830  21.84041  1.000 31.33413 ? 167 TYR A CD2 1 
ATOM   1303 C  CE1 . TYR A 1 167 ? 2.17483   23.40888  21.33849  1.000 30.27565 ? 167 TYR A CE1 1 
ATOM   1304 C  CE2 . TYR A 1 167 ? 1.67017   25.15453  22.89659  1.000 31.73790 ? 167 TYR A CE2 1 
ATOM   1305 C  CZ  . TYR A 1 167 ? 2.12033   23.87474  22.63564  1.000 29.77671 ? 167 TYR A CZ  1 
ATOM   1306 O  OH  . TYR A 1 167 ? 2.52409   23.04452  23.66324  1.000 28.15172 ? 167 TYR A OH  1 
ATOM   1307 N  N   . ALA A 1 168 ? -2.36326  27.52822  19.57557  1.000 31.48437 ? 168 ALA A N   1 
ATOM   1308 C  CA  . ALA A 1 168 ? -3.44494  27.90103  20.48715  1.000 32.28619 ? 168 ALA A CA  1 
ATOM   1309 C  C   . ALA A 1 168 ? -4.39040  26.73767  20.77040  1.000 33.69039 ? 168 ALA A C   1 
ATOM   1310 O  O   . ALA A 1 168 ? -5.04806  26.72388  21.81705  1.000 36.48007 ? 168 ALA A O   1 
ATOM   1311 C  CB  . ALA A 1 168 ? -4.24306  29.08095  19.92312  1.000 32.70977 ? 168 ALA A CB  1 
ATOM   1312 N  N   . ASP A 1 169 ? -4.46235  25.75613  19.87140  1.000 30.87113 ? 169 ASP A N   1 
ATOM   1313 C  CA  . ASP A 1 169 ? -5.35493  24.61768  20.01879  1.000 31.18982 ? 169 ASP A CA  1 
ATOM   1314 C  C   . ASP A 1 169 ? -4.65809  23.40252  20.63085  1.000 28.46265 ? 169 ASP A C   1 
ATOM   1315 O  O   . ASP A 1 169 ? -5.18035  22.28858  20.54134  1.000 29.25008 ? 169 ASP A O   1 
ATOM   1316 C  CB  . ASP A 1 169 ? -5.96051  24.26390  18.65642  1.000 31.50541 ? 169 ASP A CB  1 
ATOM   1317 C  CG  . ASP A 1 169 ? -6.81880  25.39023  18.08618  1.000 33.14849 ? 169 ASP A CG  1 
ATOM   1318 O  OD1 . ASP A 1 169 ? -7.56827  26.00987  18.86665  1.000 36.80161 ? 169 ASP A OD1 1 
ATOM   1319 O  OD2 . ASP A 1 169 ? -6.74778  25.66187  16.86596  1.000 32.61983 ? 169 ASP A OD2 1 
ATOM   1320 N  N   . HIS A 1 170 ? -3.50884  23.59859  21.28427  1.000 29.40870 ? 170 HIS A N   1 
ATOM   1321 C  CA  . HIS A 1 170 ? -2.65728  22.46194  21.62784  1.000 29.25978 ? 170 HIS A CA  1 
ATOM   1322 C  C   . HIS A 1 170 ? -3.29141  21.55195  22.67694  1.000 29.60193 ? 170 HIS A C   1 
ATOM   1323 O  O   . HIS A 1 170 ? -3.09599  20.33184  22.63447  1.000 28.86890 ? 170 HIS A O   1 
ATOM   1324 C  CB  . HIS A 1 170 ? -1.28326  22.94457  22.08748  1.000 29.69564 ? 170 HIS A CB  1 
ATOM   1325 C  CG  . HIS A 1 170 ? -1.29095  23.61872  23.42089  1.000 30.66867 ? 170 HIS A CG  1 
ATOM   1326 N  ND1 . HIS A 1 170 ? -1.49936  24.97401  23.57067  1.000 33.59640 ? 170 HIS A ND1 1 
ATOM   1327 C  CD2 . HIS A 1 170 ? -1.11605  23.12335  24.66842  1.000 32.32766 ? 170 HIS A CD2 1 
ATOM   1328 C  CE1 . HIS A 1 170 ? -1.45034  25.28429  24.85368  1.000 36.33621 ? 170 HIS A CE1 1 
ATOM   1329 N  NE2 . HIS A 1 170 ? -1.21732  24.17951  25.54098  1.000 35.36189 ? 170 HIS A NE2 1 
ATOM   1330 N  N   . GLU A 1 171 ? -4.04408  22.10383  23.63263  1.000 30.83247 ? 171 GLU A N   1 
ATOM   1331 C  CA  . GLU A 1 171 ? -4.69356  21.22226  24.60063  1.000 34.09649 ? 171 GLU A CA  1 
ATOM   1332 C  C   . GLU A 1 171 ? -5.60520  20.22256  23.89354  1.000 32.59495 ? 171 GLU A C   1 
ATOM   1333 O  O   . GLU A 1 171 ? -5.59730  19.02807  24.21676  1.000 33.38372 ? 171 GLU A O   1 
ATOM   1334 C  CB  . GLU A 1 171 ? -5.45425  22.03780  25.65123  1.000 37.30014 ? 171 GLU A CB  1 
ATOM   1335 C  CG  . GLU A 1 171 ? -4.51582  22.84681  26.54382  1.000 40.98515 ? 171 GLU A CG  1 
ATOM   1336 C  CD  . GLU A 1 171 ? -5.07481  23.15644  27.93121  1.000 45.12205 ? 171 GLU A CD  1 
ATOM   1337 O  OE1 . GLU A 1 171 ? -6.26247  22.86964  28.19759  1.000 46.62564 ? 171 GLU A OE1 1 
ATOM   1338 O  OE2 . GLU A 1 171 ? -4.30782  23.68778  28.76185  1.000 47.72555 ? 171 GLU A OE2 1 
ATOM   1339 N  N   . PHE A 1 172 ? -6.34147  20.67654  22.87679  1.000 32.60103 ? 172 PHE A N   1 
ATOM   1340 C  CA  . PHE A 1 172 ? -7.21590  19.77389  22.13299  1.000 30.37641 ? 172 PHE A CA  1 
ATOM   1341 C  C   . PHE A 1 172 ? -6.42507  18.70858  21.37046  1.000 29.21811 ? 172 PHE A C   1 
ATOM   1342 O  O   . PHE A 1 172 ? -6.67867  17.50789  21.52972  1.000 29.72649 ? 172 PHE A O   1 
ATOM   1343 C  CB  . PHE A 1 172 ? -8.10688  20.55836  21.16682  1.000 30.69715 ? 172 PHE A CB  1 
ATOM   1344 C  CG  . PHE A 1 172 ? -8.76533  19.68818  20.13465  1.000 32.25346 ? 172 PHE A CG  1 
ATOM   1345 C  CD1 . PHE A 1 172 ? -9.90300  18.96071  20.44825  1.000 35.29901 ? 172 PHE A CD1 1 
ATOM   1346 C  CD2 . PHE A 1 172 ? -8.22036  19.55953  18.86318  1.000 31.56272 ? 172 PHE A CD2 1 
ATOM   1347 C  CE1 . PHE A 1 172 ? -10.49170 18.13371  19.50869  1.000 37.66371 ? 172 PHE A CE1 1 
ATOM   1348 C  CE2 . PHE A 1 172 ? -8.81103  18.73747  17.91742  1.000 33.95357 ? 172 PHE A CE2 1 
ATOM   1349 C  CZ  . PHE A 1 172 ? -9.94837  18.02867  18.23979  1.000 36.55447 ? 172 PHE A CZ  1 
ATOM   1350 N  N   . PHE A 1 173 ? -5.48673  19.11216  20.50645  1.000 28.31180 ? 173 PHE A N   1 
ATOM   1351 C  CA  . PHE A 1 173 ? -4.88854  18.08383  19.65659  1.000 24.91100 ? 173 PHE A CA  1 
ATOM   1352 C  C   . PHE A 1 173 ? -3.79269  17.28947  20.36208  1.000 22.72561 ? 173 PHE A C   1 
ATOM   1353 O  O   . PHE A 1 173 ? -3.50632  16.16146  19.93806  1.000 24.85741 ? 173 PHE A O   1 
ATOM   1354 C  CB  . PHE A 1 173 ? -4.38315  18.65651  18.31543  1.000 27.41108 ? 173 PHE A CB  1 
ATOM   1355 C  CG  . PHE A 1 173 ? -3.39456  19.79162  18.42567  1.000 25.34794 ? 173 PHE A CG  1 
ATOM   1356 C  CD1 . PHE A 1 173 ? -2.10043  19.57275  18.85927  1.000 25.92909 ? 173 PHE A CD1 1 
ATOM   1357 C  CD2 . PHE A 1 173 ? -3.74631  21.06886  18.00746  1.000 27.41135 ? 173 PHE A CD2 1 
ATOM   1358 C  CE1 . PHE A 1 173 ? -1.18906  20.61395  18.92803  1.000 28.82455 ? 173 PHE A CE1 1 
ATOM   1359 C  CE2 . PHE A 1 173 ? -2.83948  22.11263  18.06923  1.000 26.49436 ? 173 PHE A CE2 1 
ATOM   1360 C  CZ  . PHE A 1 173 ? -1.56040  21.88768  18.53012  1.000 28.42561 ? 173 PHE A CZ  1 
ATOM   1361 N  N   . GLN A 1 174 ? -3.19034  17.81870  21.43654  1.000 25.28708 ? 174 GLN A N   1 
ATOM   1362 C  CA  . GLN A 1 174 ? -2.28723  16.97769  22.22074  1.000 24.26639 ? 174 GLN A CA  1 
ATOM   1363 C  C   . GLN A 1 174 ? -3.06327  15.87010  22.91383  1.000 25.38170 ? 174 GLN A C   1 
ATOM   1364 O  O   . GLN A 1 174 ? -2.62011  14.71274  22.94593  1.000 25.89057 ? 174 GLN A O   1 
ATOM   1365 C  CB  . GLN A 1 174 ? -1.51614  17.81120  23.25299  1.000 25.32298 ? 174 GLN A CB  1 
ATOM   1366 C  CG  . GLN A 1 174 ? -0.46675  18.73538  22.63990  1.000 25.18926 ? 174 GLN A CG  1 
ATOM   1367 C  CD  . GLN A 1 174 ? 0.08927   19.73782  23.63386  1.000 27.81355 ? 174 GLN A CD  1 
ATOM   1368 O  OE1 . GLN A 1 174 ? -0.35416  19.80756  24.79336  1.000 30.40037 ? 174 GLN A OE1 1 
ATOM   1369 N  NE2 . GLN A 1 174 ? 1.07128   20.52022  23.19077  1.000 28.18903 ? 174 GLN A NE2 1 
ATOM   1370 N  N   . ASP A 1 175 ? -4.22583  16.21006  23.48148  1.000 23.24250 ? 175 ASP A N   1 
ATOM   1371 C  CA  . ASP A 1 175 ? -5.05959  15.19028  24.10354  1.000 25.45635 ? 175 ASP A CA  1 
ATOM   1372 C  C   . ASP A 1 175 ? -5.54448  14.17212  23.08206  1.000 24.53678 ? 175 ASP A C   1 
ATOM   1373 O  O   . ASP A 1 175 ? -5.52964  12.96461  23.34648  1.000 25.23748 ? 175 ASP A O   1 
ATOM   1374 C  CB  . ASP A 1 175 ? -6.24537  15.83710  24.81309  1.000 29.64000 ? 175 ASP A CB  1 
ATOM   1375 C  CG  . ASP A 1 175 ? -7.20240  14.81545  25.37774  1.000 34.65376 ? 175 ASP A CG  1 
ATOM   1376 O  OD1 . ASP A 1 175 ? -6.85782  14.18637  26.40101  1.000 38.49957 ? 175 ASP A OD1 1 
ATOM   1377 O  OD2 . ASP A 1 175 ? -8.28937  14.63231  24.79366  1.000 35.81768 ? 175 ASP A OD2 1 
ATOM   1378 N  N   . ALA A 1 176 ? -5.97530  14.63778  21.90368  1.000 25.76194 ? 176 ALA A N   1 
ATOM   1379 C  CA  . ALA A 1 176 ? -6.45727  13.70354  20.89009  1.000 25.26728 ? 176 ALA A CA  1 
ATOM   1380 C  C   . ALA A 1 176 ? -5.32971  12.81971  20.36893  1.000 22.44868 ? 176 ALA A C   1 
ATOM   1381 O  O   . ALA A 1 176 ? -5.53780  11.62736  20.12640  1.000 25.65848 ? 176 ALA A O   1 
ATOM   1382 C  CB  . ALA A 1 176 ? -7.13476  14.46116  19.74941  1.000 25.89809 ? 176 ALA A CB  1 
ATOM   1383 N  N   . SER A 1 177 ? -4.12968  13.38139  20.19292  1.000 21.76656 ? 177 SER A N   1 
ATOM   1384 C  CA  . SER A 1 177 ? -2.98853  12.57837  19.76753  1.000 23.77249 ? 177 SER A CA  1 
ATOM   1385 C  C   . SER A 1 177 ? -2.67745  11.48435  20.78171  1.000 26.08327 ? 177 SER A C   1 
ATOM   1386 O  O   . SER A 1 177 ? -2.42401  10.33119  20.41037  1.000 28.74618 ? 177 SER A O   1 
ATOM   1387 C  CB  . SER A 1 177 ? -1.77023  13.48123  19.56158  1.000 23.75488 ? 177 SER A CB  1 
ATOM   1388 O  OG  . SER A 1 177 ? -0.58946  12.74481  19.26998  1.000 27.54902 ? 177 SER A OG  1 
ATOM   1389 N  N   . LYS A 1 178 ? -2.69301  11.82623  22.07171  1.000 26.70685 ? 178 LYS A N   1 
ATOM   1390 C  CA  . LYS A 1 178 ? -2.40753  10.82335  23.08953  1.000 26.80585 ? 178 LYS A CA  1 
ATOM   1391 C  C   . LYS A 1 178 ? -3.47142  9.73195   23.10010  1.000 27.45074 ? 178 LYS A C   1 
ATOM   1392 O  O   . LYS A 1 178 ? -3.14898  8.54086   23.17846  1.000 28.24661 ? 178 LYS A O   1 
ATOM   1393 C  CB  . LYS A 1 178 ? -2.30190  11.49157  24.45514  1.000 28.63505 ? 178 LYS A CB  1 
ATOM   1394 C  CG  . LYS A 1 178 ? -1.98810  10.53633  25.58486  1.000 31.09083 ? 178 LYS A CG  1 
ATOM   1395 C  CD  . LYS A 1 178 ? -1.96738  11.26761  26.90403  1.000 33.91985 ? 178 LYS A CD  1 
ATOM   1396 C  CE  . LYS A 1 178 ? -1.59912  10.32862  28.04519  1.000 38.97793 ? 178 LYS A CE  1 
ATOM   1397 N  NZ  . LYS A 1 178 ? -1.52161  11.04604  29.35394  1.000 42.48294 ? 178 LYS A NZ  1 
ATOM   1398 N  N   . ARG A 1 179 ? -4.74620  10.11825  23.00303  1.000 26.12072 ? 179 ARG A N   1 
ATOM   1399 C  CA  . ARG A 1 179 ? -5.82076  9.13060   23.00989  1.000 29.06989 ? 179 ARG A CA  1 
ATOM   1400 C  C   . ARG A 1 179 ? -5.69541  8.16927   21.83662  1.000 31.21083 ? 179 ARG A C   1 
ATOM   1401 O  O   . ARG A 1 179 ? -5.92385  6.96412   21.98629  1.000 33.72216 ? 179 ARG A O   1 
ATOM   1402 C  CB  . ARG A 1 179 ? -7.18168  9.82721   22.98132  1.000 32.22749 ? 179 ARG A CB  1 
ATOM   1403 C  CG  . ARG A 1 179 ? -7.57170  10.49949  24.29178  1.000 33.32772 ? 179 ARG A CG  1 
ATOM   1404 C  CD  . ARG A 1 179 ? -9.01348  11.01347  24.27889  1.000 35.27528 ? 179 ARG A CD  1 
ATOM   1405 N  NE  . ARG A 1 179 ? -9.15866  12.26069  23.53338  1.000 38.22885 ? 179 ARG A NE  1 
ATOM   1406 C  CZ  . ARG A 1 179 ? -9.88684  12.40857  22.43431  1.000 39.34899 ? 179 ARG A CZ  1 
ATOM   1407 N  NH1 . ARG A 1 179 ? -10.55334 11.39658  21.90298  1.000 39.13337 ? 179 ARG A NH1 1 
ATOM   1408 N  NH2 . ARG A 1 179 ? -9.95180  13.60535  21.85585  1.000 38.08465 ? 179 ARG A NH2 1 
ATOM   1409 N  N   . LEU A 1 180 ? -5.32914  8.68109   20.66143  1.000 28.10866 ? 180 LEU A N   1 
ATOM   1410 C  CA  . LEU A 1 180 ? -5.21524  7.82190   19.48792  1.000 30.14782 ? 180 LEU A CA  1 
ATOM   1411 C  C   . LEU A 1 180 ? -4.04631  6.84976   19.62738  1.000 30.29611 ? 180 LEU A C   1 
ATOM   1412 O  O   . LEU A 1 180 ? -4.20102  5.63606   19.42392  1.000 31.52657 ? 180 LEU A O   1 
ATOM   1413 C  CB  . LEU A 1 180 ? -5.07413  8.68472   18.22922  1.000 27.99071 ? 180 LEU A CB  1 
ATOM   1414 C  CG  . LEU A 1 180 ? -4.92771  7.94896   16.88932  1.000 31.09519 ? 180 LEU A CG  1 
ATOM   1415 C  CD1 . LEU A 1 180 ? -5.96368  6.85676   16.74642  1.000 32.35561 ? 180 LEU A CD1 1 
ATOM   1416 C  CD2 . LEU A 1 180 ? -5.06866  8.93440   15.74447  1.000 33.23328 ? 180 LEU A CD2 1 
ATOM   1417 N  N   . VAL A 1 181 ? -2.86936  7.36030   19.99475  1.000 27.88248 ? 181 VAL A N   1 
ATOM   1418 C  CA  . VAL A 1 181 ? -1.67725  6.51557   20.02772  1.000 28.66623 ? 181 VAL A CA  1 
ATOM   1419 C  C   . VAL A 1 181 ? -1.77273  5.48123   21.13925  1.000 32.59625 ? 181 VAL A C   1 
ATOM   1420 O  O   . VAL A 1 181 ? -1.33524  4.33351   20.97653  1.000 32.09206 ? 181 VAL A O   1 
ATOM   1421 C  CB  . VAL A 1 181 ? -0.42289  7.39073   20.17622  1.000 31.50250 ? 181 VAL A CB  1 
ATOM   1422 C  CG1 . VAL A 1 181 ? 0.79994   6.54912   20.48673  1.000 33.23962 ? 181 VAL A CG1 1 
ATOM   1423 C  CG2 . VAL A 1 181 ? -0.21718  8.15572   18.91862  1.000 30.94037 ? 181 VAL A CG2 1 
ATOM   1424 N  N   . GLN A 1 182 ? -2.34706  5.85776   22.27894  1.000 32.55500 ? 182 GLN A N   1 
ATOM   1425 C  CA  . GLN A 1 182 ? -2.38357  4.97979   23.43990  1.000 33.84500 ? 182 GLN A CA  1 
ATOM   1426 C  C   . GLN A 1 182 ? -3.71978  4.27175   23.61827  1.000 38.50328 ? 182 GLN A C   1 
ATOM   1427 O  O   . GLN A 1 182 ? -3.91427  3.59526   24.63330  1.000 39.70526 ? 182 GLN A O   1 
ATOM   1428 C  CB  . GLN A 1 182 ? -2.04255  5.76431   24.70499  1.000 35.57224 ? 182 GLN A CB  1 
ATOM   1429 C  CG  . GLN A 1 182 ? -0.71332  6.49075   24.62413  1.000 37.96746 ? 182 GLN A CG  1 
ATOM   1430 C  CD  . GLN A 1 182 ? -0.22350  6.95176   25.97612  1.000 41.54376 ? 182 GLN A CD  1 
ATOM   1431 O  OE1 . GLN A 1 182 ? -0.54434  6.34904   27.00187  1.000 42.30178 ? 182 GLN A OE1 1 
ATOM   1432 N  NE2 . GLN A 1 182 ? 0.56244   8.02297   25.98721  1.000 41.60802 ? 182 GLN A NE2 1 
ATOM   1433 N  N   . SER A 1 183 ? -4.63983  4.40565   22.66631  1.000 39.76719 ? 183 SER A N   1 
ATOM   1434 C  CA  . SER A 1 183 ? -5.90689  3.69105   22.76093  1.000 42.90969 ? 183 SER A CA  1 
ATOM   1435 C  C   . SER A 1 183 ? -5.67714  2.18552   22.78806  1.000 44.27212 ? 183 SER A C   1 
ATOM   1436 O  O   . SER A 1 183 ? -4.83696  1.65255   22.05751  1.000 40.67915 ? 183 SER A O   1 
ATOM   1437 C  CB  . SER A 1 183 ? -6.81065  4.04751   21.58454  1.000 48.61965 ? 183 SER A CB  1 
ATOM   1438 O  OG  . SER A 1 183 ? -6.16897  3.74044   20.35771  1.000 52.35143 ? 183 SER A OG  1 
ATOM   1439 N  N   . THR A 1 184 ? -6.43714  1.50036   23.64033  1.000 46.31349 ? 184 THR A N   1 
ATOM   1440 C  CA  . THR A 1 184 ? -6.40743  0.04884   23.72351  1.000 49.14371 ? 184 THR A CA  1 
ATOM   1441 C  C   . THR A 1 184 ? -7.59685  -0.61269  23.04278  1.000 46.76398 ? 184 THR A C   1 
ATOM   1442 O  O   . THR A 1 184 ? -7.57097  -1.83068  22.83722  1.000 46.05011 ? 184 THR A O   1 
ATOM   1443 C  CB  . THR A 1 184 ? -6.36297  -0.39664  25.18824  1.000 54.74333 ? 184 THR A CB  1 
ATOM   1444 O  OG1 . THR A 1 184 ? -7.23283  0.44043   25.96080  1.000 56.69512 ? 184 THR A OG1 1 
ATOM   1445 C  CG2 . THR A 1 184 ? -4.94201  -0.31433  25.73587  1.000 56.36733 ? 184 THR A CG2 1 
ATOM   1446 N  N   . ASP A 1 185 ? -8.63428  0.14647   22.69976  1.000 44.48575 ? 185 ASP A N   1 
ATOM   1447 C  CA  . ASP A 1 185 ? -9.80634  -0.39338  22.02832  1.000 46.03150 ? 185 ASP A CA  1 
ATOM   1448 C  C   . ASP A 1 185 ? -10.07824 0.41276   20.76672  1.000 42.10959 ? 185 ASP A C   1 
ATOM   1449 O  O   . ASP A 1 185 ? -9.56868  1.52230   20.59068  1.000 40.80877 ? 185 ASP A O   1 
ATOM   1450 C  CB  . ASP A 1 185 ? -11.04463 -0.37628  22.93508  1.000 49.31201 ? 185 ASP A CB  1 
ATOM   1451 C  CG  . ASP A 1 185 ? -11.43785 1.02392   23.34817  1.000 54.66442 ? 185 ASP A CG  1 
ATOM   1452 O  OD1 . ASP A 1 185 ? -10.65856 1.66739   24.08300  1.000 56.51508 ? 185 ASP A OD1 1 
ATOM   1453 O  OD2 . ASP A 1 185 ? -12.51133 1.49557   22.91807  1.000 55.61125 ? 185 ASP A OD2 1 
ATOM   1454 N  N   . ALA A 1 186 ? -10.89801 -0.16167  19.88424  1.000 38.27343 ? 186 ALA A N   1 
ATOM   1455 C  CA  . ALA A 1 186 ? -11.13242 0.46113   18.58699  1.000 38.74403 ? 186 ALA A CA  1 
ATOM   1456 C  C   . ALA A 1 186 ? -11.99203 1.71297   18.70287  1.000 40.63581 ? 186 ALA A C   1 
ATOM   1457 O  O   . ALA A 1 186 ? -11.78821 2.67458   17.94885  1.000 40.59552 ? 186 ALA A O   1 
ATOM   1458 C  CB  . ALA A 1 186 ? -11.78036 -0.53732  17.63083  1.000 38.35437 ? 186 ALA A CB  1 
ATOM   1459 N  N   . GLN A 1 187 ? -12.94556 1.72995   19.63630  1.000 38.35614 ? 187 GLN A N   1 
ATOM   1460 C  CA  . GLN A 1 187 ? -13.88686 2.84385   19.68782  1.000 44.35223 ? 187 GLN A CA  1 
ATOM   1461 C  C   . GLN A 1 187 ? -13.20789 4.12734   20.15274  1.000 39.94117 ? 187 GLN A C   1 
ATOM   1462 O  O   . GLN A 1 187 ? -13.43793 5.19768   19.57764  1.000 39.28827 ? 187 GLN A O   1 
ATOM   1463 C  CB  . GLN A 1 187 ? -15.07461 2.49893   20.58382  1.000 52.43475 ? 187 GLN A CB  1 
ATOM   1464 C  CG  . GLN A 1 187 ? -16.26350 3.43202   20.38186  1.000 61.10402 ? 187 GLN A CG  1 
ATOM   1465 C  CD  . GLN A 1 187 ? -16.38815 3.90766   18.94087  1.000 67.66780 ? 187 GLN A CD  1 
ATOM   1466 O  OE1 . GLN A 1 187 ? -16.84654 3.16977   18.06630  1.000 70.07341 ? 187 GLN A OE1 1 
ATOM   1467 N  NE2 . GLN A 1 187 ? -15.96840 5.14567   18.68695  1.000 68.55243 ? 187 GLN A NE2 1 
ATOM   1468 N  N   . SER A 1 188 ? -12.34968 4.04651   21.17142  1.000 40.12435 ? 188 SER A N   1 
ATOM   1469 C  CA  . SER A 1 188 ? -11.64583 5.25018   21.60518  1.000 42.19308 ? 188 SER A CA  1 
ATOM   1470 C  C   . SER A 1 188 ? -10.59043 5.68630   20.59158  1.000 38.57842 ? 188 SER A C   1 
ATOM   1471 O  O   . SER A 1 188 ? -10.29506 6.88257   20.48671  1.000 36.57697 ? 188 SER A O   1 
ATOM   1472 C  CB  . SER A 1 188 ? -11.01795 5.03510   22.98089  1.000 48.77521 ? 188 SER A CB  1 
ATOM   1473 O  OG  . SER A 1 188 ? -10.47989 3.73787   23.08640  1.000 55.04014 ? 188 SER A OG  1 
ATOM   1474 N  N   . ALA A 1 189 ? -10.01571 4.74554   19.83841  1.000 35.10478 ? 189 ALA A N   1 
ATOM   1475 C  CA  . ALA A 1 189 ? -9.09838  5.12653   18.76752  1.000 34.15510 ? 189 ALA A CA  1 
ATOM   1476 C  C   . ALA A 1 189 ? -9.84279  5.84466   17.65023  1.000 32.37647 ? 189 ALA A C   1 
ATOM   1477 O  O   . ALA A 1 189 ? -9.37863  6.86981   17.13339  1.000 30.19628 ? 189 ALA A O   1 
ATOM   1478 C  CB  . ALA A 1 189 ? -8.37439  3.89462   18.22000  1.000 35.30469 ? 189 ALA A CB  1 
ATOM   1479 N  N   . LEU A 1 190 ? -11.00520 5.31405   17.26664  1.000 30.53895 ? 190 LEU A N   1 
ATOM   1480 C  CA  . LEU A 1 190 ? -11.78827 5.92289   16.19737  1.000 28.82733 ? 190 LEU A CA  1 
ATOM   1481 C  C   . LEU A 1 190 ? -12.26336 7.31519   16.58673  1.000 27.54196 ? 190 LEU A C   1 
ATOM   1482 O  O   . LEU A 1 190 ? -12.24668 8.23583   15.76230  1.000 30.00581 ? 190 LEU A O   1 
ATOM   1483 C  CB  . LEU A 1 190 ? -12.98129 5.03431   15.84855  1.000 32.77840 ? 190 LEU A CB  1 
ATOM   1484 C  CG  . LEU A 1 190 ? -12.71056 3.79129   14.99945  1.000 38.56840 ? 190 LEU A CG  1 
ATOM   1485 C  CD1 . LEU A 1 190 ? -13.95012 2.91664   14.94131  1.000 40.57142 ? 190 LEU A CD1 1 
ATOM   1486 C  CD2 . LEU A 1 190 ? -12.27342 4.18740   13.59619  1.000 42.35770 ? 190 LEU A CD2 1 
ATOM   1487 N  N   . THR A 1 191 ? -12.69614 7.49096   17.83873  1.000 30.67525 ? 191 THR A N   1 
ATOM   1488 C  CA  . THR A 1 191 ? -13.14477 8.80905   18.27334  1.000 31.12047 ? 191 THR A CA  1 
ATOM   1489 C  C   . THR A 1 191 ? -12.00340 9.81381   18.23343  1.000 29.02027 ? 191 THR A C   1 
ATOM   1490 O  O   . THR A 1 191 ? -12.17328 10.93785  17.74724  1.000 28.73738 ? 191 THR A O   1 
ATOM   1491 C  CB  . THR A 1 191 ? -13.73956 8.73876   19.67890  1.000 32.77434 ? 191 THR A CB  1 
ATOM   1492 O  OG1 . THR A 1 191 ? -14.88232 7.87728   19.66922  1.000 35.62367 ? 191 THR A OG1 1 
ATOM   1493 C  CG2 . THR A 1 191 ? -14.16565 10.12844  20.13731  1.000 35.50857 ? 191 THR A CG2 1 
ATOM   1494 N  N   . ALA A 1 192 ? -10.82824 9.42226   18.73040  1.000 28.24477 ? 192 ALA A N   1 
ATOM   1495 C  CA  . ALA A 1 192 ? -9.67954  10.31972  18.70059  1.000 27.75769 ? 192 ALA A CA  1 
ATOM   1496 C  C   . ALA A 1 192 ? -9.29422  10.66829  17.27119  1.000 27.95069 ? 192 ALA A C   1 
ATOM   1497 O  O   . ALA A 1 192 ? -8.99493  11.82999  16.96617  1.000 25.95824 ? 192 ALA A O   1 
ATOM   1498 C  CB  . ALA A 1 192 ? -8.49854  9.68882   19.43600  1.000 28.75363 ? 192 ALA A CB  1 
ATOM   1499 N  N   . ARG A 1 193 ? -9.30377  9.67805   16.37679  1.000 25.76799 ? 193 ARG A N   1 
ATOM   1500 C  CA  . ARG A 1 193 ? -8.98859  9.95783   14.97976  1.000 26.64549 ? 193 ARG A CA  1 
ATOM   1501 C  C   . ARG A 1 193 ? -9.99389  10.92487  14.37637  1.000 25.27927 ? 193 ARG A C   1 
ATOM   1502 O  O   . ARG A 1 193 ? -9.61503  11.85420  13.65051  1.000 26.33414 ? 193 ARG A O   1 
ATOM   1503 C  CB  . ARG A 1 193 ? -8.95366  8.66745   14.16403  1.000 28.08499 ? 193 ARG A CB  1 
ATOM   1504 C  CG  . ARG A 1 193 ? -8.27697  8.87597   12.81836  1.000 31.59557 ? 193 ARG A CG  1 
ATOM   1505 C  CD  . ARG A 1 193 ? -8.91822  8.08127   11.70203  1.000 39.78340 ? 193 ARG A CD  1 
ATOM   1506 N  NE  . ARG A 1 193 ? -8.12715  8.17618   10.47999  1.000 46.02627 ? 193 ARG A NE  1 
ATOM   1507 C  CZ  . ARG A 1 193 ? -8.26536  9.12629   9.56313   1.000 48.83917 ? 193 ARG A CZ  1 
ATOM   1508 N  NH1 . ARG A 1 193 ? -9.17095  10.08202  9.68804   1.000 48.21449 ? 193 ARG A NH1 1 
ATOM   1509 N  NH2 . ARG A 1 193 ? -7.47475  9.11593   8.49390   1.000 51.43667 ? 193 ARG A NH2 1 
ATOM   1510 N  N   . ASN A 1 194 ? -11.28195 10.71932  14.66286  1.000 25.61632 ? 194 ASN A N   1 
ATOM   1511 C  CA  . ASN A 1 194 ? -12.31135 11.59121  14.10677  1.000 27.71444 ? 194 ASN A CA  1 
ATOM   1512 C  C   . ASN A 1 194 ? -12.20062 13.00507  14.66467  1.000 26.78903 ? 194 ASN A C   1 
ATOM   1513 O  O   . ASN A 1 194 ? -12.46827 13.98337  13.95009  1.000 29.11673 ? 194 ASN A O   1 
ATOM   1514 C  CB  . ASN A 1 194 ? -13.69786 11.01193  14.38869  1.000 32.75574 ? 194 ASN A CB  1 
ATOM   1515 C  CG  . ASN A 1 194 ? -13.95638 9.71677   13.63949  1.000 43.06732 ? 194 ASN A CG  1 
ATOM   1516 O  OD1 . ASN A 1 194 ? -13.32096 9.43086   12.62112  1.000 48.45102 ? 194 ASN A OD1 1 
ATOM   1517 N  ND2 . ASN A 1 194 ? -14.90396 8.93001   14.13686  1.000 43.31099 ? 194 ASN A ND2 1 
ATOM   1518 N  N   . ASP A 1 195 ? -11.82320 13.13004  15.94345  1.000 26.75127 ? 195 ASP A N   1 
ATOM   1519 C  CA  . ASP A 1 195 ? -11.59510 14.44667  16.53725  1.000 26.87288 ? 195 ASP A CA  1 
ATOM   1520 C  C   . ASP A 1 195 ? -10.51406 15.20860  15.77598  1.000 22.62637 ? 195 ASP A C   1 
ATOM   1521 O  O   . ASP A 1 195 ? -10.70443 16.37167  15.39286  1.000 25.29576 ? 195 ASP A O   1 
ATOM   1522 C  CB  . ASP A 1 195 ? -11.20205 14.30013  18.01364  1.000 28.73699 ? 195 ASP A CB  1 
ATOM   1523 C  CG  . ASP A 1 195 ? -12.36264 13.85902  18.91035  1.000 31.66335 ? 195 ASP A CG  1 
ATOM   1524 O  OD1 . ASP A 1 195 ? -13.54210 14.02435  18.53149  1.000 32.76013 ? 195 ASP A OD1 1 
ATOM   1525 O  OD2 . ASP A 1 195 ? -12.08141 13.35801  20.02129  1.000 34.85173 ? 195 ASP A OD2 1 
ATOM   1526 N  N   . LEU A 1 196 ? -9.35899  14.56874  15.56413  1.000 24.31642 ? 196 LEU A N   1 
ATOM   1527 C  CA  . LEU A 1 196 ? -8.28076  15.20553  14.81271  1.000 23.72498 ? 196 LEU A CA  1 
ATOM   1528 C  C   . LEU A 1 196 ? -8.68351  15.46861  13.36878  1.000 22.65955 ? 196 LEU A C   1 
ATOM   1529 O  O   . LEU A 1 196 ? -8.31460  16.49844  12.79542  1.000 25.86451 ? 196 LEU A O   1 
ATOM   1530 C  CB  . LEU A 1 196 ? -7.02255  14.33667  14.84984  1.000 23.35243 ? 196 LEU A CB  1 
ATOM   1531 C  CG  . LEU A 1 196 ? -6.26634  14.25125  16.18047  1.000 27.19603 ? 196 LEU A CG  1 
ATOM   1532 C  CD1 . LEU A 1 196 ? -5.16490  13.20458  16.10620  1.000 28.13148 ? 196 LEU A CD1 1 
ATOM   1533 C  CD2 . LEU A 1 196 ? -5.67453  15.60399  16.53467  1.000 28.39921 ? 196 LEU A CD2 1 
ATOM   1534 N  N   . ALA A 1 197 ? -9.41197  14.53378  12.75213  1.000 22.18693 ? 197 ALA A N   1 
ATOM   1535 C  CA  . ALA A 1 197 ? -9.78981  14.69853  11.35186  1.000 23.76832 ? 197 ALA A CA  1 
ATOM   1536 C  C   . ALA A 1 197 ? -10.69988 15.90675  11.16793  1.000 24.81524 ? 197 ALA A C   1 
ATOM   1537 O  O   . ALA A 1 197 ? -10.51716 16.69689  10.23311  1.000 25.56884 ? 197 ALA A O   1 
ATOM   1538 C  CB  . ALA A 1 197 ? -10.46479 13.42636  10.84009  1.000 23.71100 ? 197 ALA A CB  1 
ATOM   1539 N  N   . GLY A 1 198 ? -11.68159 16.07423  12.05682  1.000 25.82614 ? 198 GLY A N   1 
ATOM   1540 C  CA  . GLY A 1 198 ? -12.56470 17.22469  11.95051  1.000 26.51795 ? 198 GLY A CA  1 
ATOM   1541 C  C   . GLY A 1 198 ? -11.82558 18.53077  12.15420  1.000 26.17267 ? 198 GLY A C   1 
ATOM   1542 O  O   . GLY A 1 198 ? -12.09467 19.52156  11.47033  1.000 27.93443 ? 198 GLY A O   1 
ATOM   1543 N  N   . TYR A 1 199 ? -10.86232 18.54114  13.07814  1.000 25.38924 ? 199 TYR A N   1 
ATOM   1544 C  CA  . TYR A 1 199 ? -10.04512 19.73219  13.28847  1.000 22.85048 ? 199 TYR A CA  1 
ATOM   1545 C  C   . TYR A 1 199 ? -9.23948  20.07257  12.04230  1.000 24.66764 ? 199 TYR A C   1 
ATOM   1546 O  O   . TYR A 1 199 ? -9.21558  21.22563  11.59408  1.000 26.29084 ? 199 TYR A O   1 
ATOM   1547 C  CB  . TYR A 1 199 ? -9.11894  19.51836  14.48426  1.000 26.45725 ? 199 TYR A CB  1 
ATOM   1548 C  CG  . TYR A 1 199 ? -8.15492  20.65242  14.71292  1.000 26.12132 ? 199 TYR A CG  1 
ATOM   1549 C  CD1 . TYR A 1 199 ? -8.59325  21.87631  15.21306  1.000 27.24763 ? 199 TYR A CD1 1 
ATOM   1550 C  CD2 . TYR A 1 199 ? -6.80345  20.49854  14.44825  1.000 27.07408 ? 199 TYR A CD2 1 
ATOM   1551 C  CE1 . TYR A 1 199 ? -7.71378  22.91449  15.41961  1.000 29.06424 ? 199 TYR A CE1 1 
ATOM   1552 C  CE2 . TYR A 1 199 ? -5.91947  21.52805  14.65532  1.000 28.78166 ? 199 TYR A CE2 1 
ATOM   1553 C  CZ  . TYR A 1 199 ? -6.37755  22.73471  15.14113  1.000 29.51233 ? 199 TYR A CZ  1 
ATOM   1554 O  OH  . TYR A 1 199 ? -5.48753  23.75837  15.33825  1.000 31.58341 ? 199 TYR A OH  1 
ATOM   1555 N  N   . LEU A 1 200 ? -8.56054  19.07920  11.47433  1.000 23.06955 ? 200 LEU A N   1 
ATOM   1556 C  CA  . LEU A 1 200 ? -7.71233  19.34035  10.31718  1.000 21.32976 ? 200 LEU A CA  1 
ATOM   1557 C  C   . LEU A 1 200 ? -8.54744  19.71334  9.10067   1.000 23.75633 ? 200 LEU A C   1 
ATOM   1558 O  O   . LEU A 1 200 ? -8.10694  20.50889  8.26047   1.000 25.80437 ? 200 LEU A O   1 
ATOM   1559 C  CB  . LEU A 1 200 ? -6.84145  18.11694  10.02507  1.000 21.76176 ? 200 LEU A CB  1 
ATOM   1560 C  CG  . LEU A 1 200 ? -5.80995  17.78168  11.10539  1.000 24.12629 ? 200 LEU A CG  1 
ATOM   1561 C  CD1 . LEU A 1 200 ? -5.23684  16.35489  10.95691  1.000 23.57698 ? 200 LEU A CD1 1 
ATOM   1562 C  CD2 . LEU A 1 200 ? -4.71358  18.84816  11.11195  1.000 23.69125 ? 200 LEU A CD2 1 
ATOM   1563 N  N   . ASP A 1 201 ? -9.75223  19.15248  8.99647   1.000 25.27170 ? 201 ASP A N   1 
ATOM   1564 C  CA  . ASP A 1 201 ? -10.64000 19.50664  7.89676   1.000 26.19692 ? 201 ASP A CA  1 
ATOM   1565 C  C   . ASP A 1 201 ? -11.00510 20.98533  7.93959   1.000 27.84838 ? 201 ASP A C   1 
ATOM   1566 O  O   . ASP A 1 201 ? -11.04078 21.65457  6.90046   1.000 27.90912 ? 201 ASP A O   1 
ATOM   1567 C  CB  . ASP A 1 201 ? -11.89801 18.64347  7.94048   1.000 29.94323 ? 201 ASP A CB  1 
ATOM   1568 C  CG  . ASP A 1 201 ? -12.85495 18.97349  6.82298   1.000 37.54072 ? 201 ASP A CG  1 
ATOM   1569 O  OD1 . ASP A 1 201 ? -12.63221 18.49293  5.69492   1.000 38.36691 ? 201 ASP A OD1 1 
ATOM   1570 O  OD2 . ASP A 1 201 ? -13.81476 19.73421  7.07016   1.000 42.15747 ? 201 ASP A OD2 1 
ATOM   1571 N  N   . GLY A 1 202 ? -11.27740 21.51237  9.13468   1.000 25.37500 ? 202 GLY A N   1 
ATOM   1572 C  CA  . GLY A 1 202 ? -11.56479 22.93225  9.25574   1.000 27.73159 ? 202 GLY A CA  1 
ATOM   1573 C  C   . GLY A 1 202 ? -10.36694 23.79374  8.90755   1.000 26.55283 ? 202 GLY A C   1 
ATOM   1574 O  O   . GLY A 1 202 ? -10.51411 24.88042  8.33193   1.000 27.52199 ? 202 GLY A O   1 
ATOM   1575 N  N   . LEU A 1 203 ? -9.16447  23.32510  9.25312   1.000 25.47519 ? 203 LEU A N   1 
ATOM   1576 C  CA  . LEU A 1 203 ? -7.95882  24.07560  8.92713   1.000 26.19272 ? 203 LEU A CA  1 
ATOM   1577 C  C   . LEU A 1 203 ? -7.75569  24.15074  7.41882   1.000 25.86040 ? 203 LEU A C   1 
ATOM   1578 O  O   . LEU A 1 203 ? -7.29976  25.17549  6.89497   1.000 25.29137 ? 203 LEU A O   1 
ATOM   1579 C  CB  . LEU A 1 203 ? -6.74767  23.43786  9.60839   1.000 28.81481 ? 203 LEU A CB  1 
ATOM   1580 C  CG  . LEU A 1 203 ? -5.45357  24.25419  9.61395   1.000 30.37631 ? 203 LEU A CG  1 
ATOM   1581 C  CD1 . LEU A 1 203 ? -5.64299  25.55147  10.40182  1.000 35.97013 ? 203 LEU A CD1 1 
ATOM   1582 C  CD2 . LEU A 1 203 ? -4.30238  23.42800  10.17796  1.000 32.41103 ? 203 LEU A CD2 1 
ATOM   1583 N  N   . ILE A 1 204 ? -8.09060  23.07453  6.70378   1.000 23.06647 ? 204 ILE A N   1 
ATOM   1584 C  CA  . ILE A 1 204 ? -7.93737  23.06299  5.24994   1.000 21.33797 ? 204 ILE A CA  1 
ATOM   1585 C  C   . ILE A 1 204 ? -8.84279  24.10905  4.60735   1.000 22.68831 ? 204 ILE A C   1 
ATOM   1586 O  O   . ILE A 1 204 ? -8.41005  24.89430  3.75377   1.000 25.16911 ? 204 ILE A O   1 
ATOM   1587 C  CB  . ILE A 1 204 ? -8.22554  21.65527  4.70255   1.000 21.53377 ? 204 ILE A CB  1 
ATOM   1588 C  CG1 . ILE A 1 204 ? -7.09859  20.69832  5.09430   1.000 22.80367 ? 204 ILE A CG1 1 
ATOM   1589 C  CG2 . ILE A 1 204 ? -8.45523  21.69887  3.17923   1.000 24.31839 ? 204 ILE A CG2 1 
ATOM   1590 C  CD1 . ILE A 1 204 ? -7.43482  19.23567  4.84731   1.000 25.28946 ? 204 ILE A CD1 1 
ATOM   1591 N  N   . THR A 1 205 ? -10.11444 24.13397  5.00701   1.000 23.76515 ? 205 THR A N   1 
ATOM   1592 C  CA  . THR A 1 205 ? -11.04552 25.10758  4.44731   1.000 23.30455 ? 205 THR A CA  1 
ATOM   1593 C  C   . THR A 1 205 ? -10.59501 26.52837  4.74833   1.000 25.99994 ? 205 THR A C   1 
ATOM   1594 O  O   . THR A 1 205 ? -10.69678 27.42055  3.89415   1.000 26.34276 ? 205 THR A O   1 
ATOM   1595 C  CB  . THR A 1 205 ? -12.44657 24.85362  4.99535   1.000 23.77557 ? 205 THR A CB  1 
ATOM   1596 O  OG1 . THR A 1 205 ? -12.89529 23.57235  4.54074   1.000 29.77832 ? 205 THR A OG1 1 
ATOM   1597 C  CG2 . THR A 1 205 ? -13.42043 25.93312  4.51822   1.000 27.19341 ? 205 THR A CG2 1 
ATOM   1598 N  N   . GLN A 1 206 ? -10.07174 26.75098  5.95292   1.000 24.84995 ? 206 GLN A N   1 
ATOM   1599 C  CA  . GLN A 1 206 ? -9.55682  28.06643  6.30047   1.000 24.72985 ? 206 GLN A CA  1 
ATOM   1600 C  C   . GLN A 1 206 ? -8.42451  28.48181  5.36739   1.000 25.50366 ? 206 GLN A C   1 
ATOM   1601 O  O   . GLN A 1 206 ? -8.35284  29.64334  4.94897   1.000 26.30667 ? 206 GLN A O   1 
ATOM   1602 C  CB  . GLN A 1 206 ? -9.08573  28.05645  7.75426   1.000 28.20931 ? 206 GLN A CB  1 
ATOM   1603 C  CG  . GLN A 1 206 ? -8.71083  29.41310  8.29807   1.000 35.51120 ? 206 GLN A CG  1 
ATOM   1604 C  CD  . GLN A 1 206 ? -8.10371  29.31936  9.66972   1.000 43.06810 ? 206 GLN A CD  1 
ATOM   1605 O  OE1 . GLN A 1 206 ? -6.91497  29.57603  9.85057   1.000 47.93545 ? 206 GLN A OE1 1 
ATOM   1606 N  NE2 . GLN A 1 206 ? -8.91396  28.94466  10.65101  1.000 44.01118 ? 206 GLN A NE2 1 
ATOM   1607 N  N   . PHE A 1 207 ? -7.52367  27.54669  5.03808   1.000 22.92429 ? 207 PHE A N   1 
ATOM   1608 C  CA  . PHE A 1 207 ? -6.41628  27.86168  4.13807   1.000 23.22501 ? 207 PHE A CA  1 
ATOM   1609 C  C   . PHE A 1 207 ? -6.88509  28.07493  2.69946   1.000 23.44008 ? 207 PHE A C   1 
ATOM   1610 O  O   . PHE A 1 207 ? -6.21795  28.77847  1.93423   1.000 23.48997 ? 207 PHE A O   1 
ATOM   1611 C  CB  . PHE A 1 207 ? -5.36539  26.75022  4.18539   1.000 22.32834 ? 207 PHE A CB  1 
ATOM   1612 C  CG  . PHE A 1 207 ? -4.53888  26.72998  5.45675   1.000 27.11551 ? 207 PHE A CG  1 
ATOM   1613 C  CD1 . PHE A 1 207 ? -4.55825  27.79640  6.34682   1.000 32.55793 ? 207 PHE A CD1 1 
ATOM   1614 C  CD2 . PHE A 1 207 ? -3.74656  25.63433  5.75760   1.000 30.07187 ? 207 PHE A CD2 1 
ATOM   1615 C  CE1 . PHE A 1 207 ? -3.79528  27.76173  7.51530   1.000 33.48013 ? 207 PHE A CE1 1 
ATOM   1616 C  CE2 . PHE A 1 207 ? -2.97412  25.59539  6.91704   1.000 30.43826 ? 207 PHE A CE2 1 
ATOM   1617 C  CZ  . PHE A 1 207 ? -2.99826  26.65888  7.79090   1.000 30.31003 ? 207 PHE A CZ  1 
ATOM   1618 N  N   . GLN A 1 208 ? -8.00659  27.46617  2.30145   1.000 21.44418 ? 208 GLN A N   1 
ATOM   1619 C  CA  . GLN A 1 208 ? -8.55081  27.75626  0.97517   1.000 22.58012 ? 208 GLN A CA  1 
ATOM   1620 C  C   . GLN A 1 208 ? -9.12162  29.17218  0.91151   1.000 25.22380 ? 208 GLN A C   1 
ATOM   1621 O  O   . GLN A 1 208 ? -9.11276  29.80198  -0.15701  1.000 26.47996 ? 208 GLN A O   1 
ATOM   1622 C  CB  . GLN A 1 208 ? -9.60385  26.70561  0.60187   1.000 23.42984 ? 208 GLN A CB  1 
ATOM   1623 C  CG  . GLN A 1 208 ? -8.98425  25.32094  0.45286   1.000 22.62737 ? 208 GLN A CG  1 
ATOM   1624 C  CD  . GLN A 1 208 ? -9.98671  24.20484  0.21027   1.000 22.57700 ? 208 GLN A CD  1 
ATOM   1625 O  OE1 . GLN A 1 208 ? -11.08831 24.20757  0.75799   1.000 25.47193 ? 208 GLN A OE1 1 
ATOM   1626 N  NE2 . GLN A 1 208 ? -9.58726  23.22035  -0.59135  1.000 23.95964 ? 208 GLN A NE2 1 
ATOM   1627 N  N   . THR A 1 209 ? -9.60514  29.69050  2.04247   1.000 22.44398 ? 209 THR A N   1 
ATOM   1628 C  CA  . THR A 1 209 ? -10.05834 31.07580  2.11393   1.000 22.79975 ? 209 THR A CA  1 
ATOM   1629 C  C   . THR A 1 209 ? -8.87994  32.02781  2.19266   1.000 26.08974 ? 209 THR A C   1 
ATOM   1630 O  O   . THR A 1 209 ? -8.81912  33.03174  1.47026   1.000 28.81267 ? 209 THR A O   1 
ATOM   1631 C  CB  . THR A 1 209 ? -10.94477 31.28605  3.34680   1.000 25.57817 ? 209 THR A CB  1 
ATOM   1632 O  OG1 . THR A 1 209 ? -12.06714 30.39881  3.29760   1.000 28.40148 ? 209 THR A OG1 1 
ATOM   1633 C  CG2 . THR A 1 209 ? -11.42421 32.75484  3.43017   1.000 25.46879 ? 209 THR A CG2 1 
ATOM   1634 N  N   . GLU A 1 210 ? -7.95409  31.73756  3.09950   1.000 23.95066 ? 210 GLU A N   1 
ATOM   1635 C  CA  A GLU A 1 210 ? -6.80473  32.59907  3.35729   0.498 26.14555 ? 210 GLU A CA  1 
ATOM   1636 C  CA  B GLU A 1 210 ? -6.80811  32.59763  3.37269   0.502 27.05190 ? 210 GLU A CA  1 
ATOM   1637 C  C   . GLU A 1 210 ? -5.57046  31.71359  3.38940   1.000 25.67496 ? 210 GLU A C   1 
ATOM   1638 O  O   . GLU A 1 210 ? -5.30871  31.04966  4.40703   1.000 26.01305 ? 210 GLU A O   1 
ATOM   1639 C  CB  A GLU A 1 210 ? -6.96338  33.37205  4.66072   0.498 30.53008 ? 210 GLU A CB  1 
ATOM   1640 C  CB  B GLU A 1 210 ? -7.00443  33.32213  4.69912   0.502 33.20206 ? 210 GLU A CB  1 
ATOM   1641 C  CG  A GLU A 1 210 ? -5.97276  34.51715  4.80659   0.498 36.51439 ? 210 GLU A CG  1 
ATOM   1642 C  CG  B GLU A 1 210 ? -5.85547  34.19764  5.15456   0.502 40.73599 ? 210 GLU A CG  1 
ATOM   1643 C  CD  A GLU A 1 210 ? -6.14179  35.57197  3.72677   0.498 38.90106 ? 210 GLU A CD  1 
ATOM   1644 C  CD  B GLU A 1 210 ? -6.23858  35.05026  6.35029   0.502 46.17951 ? 210 GLU A CD  1 
ATOM   1645 O  OE1 A GLU A 1 210 ? -7.27636  36.06470  3.54939   0.498 41.08216 ? 210 GLU A OE1 1 
ATOM   1646 O  OE1 B GLU A 1 210 ? -7.39460  35.52291  6.39366   0.502 48.39231 ? 210 GLU A OE1 1 
ATOM   1647 O  OE2 A GLU A 1 210 ? -5.14601  35.89867  3.04576   0.498 38.03349 ? 210 GLU A OE2 1 
ATOM   1648 O  OE2 B GLU A 1 210 ? -5.39378  35.23886  7.24938   0.502 49.04628 ? 210 GLU A OE2 1 
ATOM   1649 N  N   . PRO A 1 211 ? -4.80797  31.66473  2.29272   1.000 26.31220 ? 211 PRO A N   1 
ATOM   1650 C  CA  . PRO A 1 211 ? -3.64144  30.77956  2.22991   1.000 24.33293 ? 211 PRO A CA  1 
ATOM   1651 C  C   . PRO A 1 211 ? -2.76512  30.91437  3.46392   1.000 26.97122 ? 211 PRO A C   1 
ATOM   1652 O  O   . PRO A 1 211 ? -2.57074  32.01069  4.00795   1.000 27.68933 ? 211 PRO A O   1 
ATOM   1653 C  CB  . PRO A 1 211 ? -2.92392  31.23714  0.95640   1.000 28.02052 ? 211 PRO A CB  1 
ATOM   1654 C  CG  . PRO A 1 211 ? -4.04078  31.70153  0.08318   1.000 31.28199 ? 211 PRO A CG  1 
ATOM   1655 C  CD  . PRO A 1 211 ? -5.03116  32.36690  1.01659   1.000 27.88300 ? 211 PRO A CD  1 
ATOM   1656 N  N   . GLY A 1 212 ? -2.26725  29.76555  3.92827   1.000 28.84415 ? 212 GLY A N   1 
ATOM   1657 C  CA  . GLY A 1 212 ? -1.66439  29.65636  5.23435   1.000 32.40326 ? 212 GLY A CA  1 
ATOM   1658 C  C   . GLY A 1 212 ? -0.21393  29.20347  5.17851   1.000 29.32669 ? 212 GLY A C   1 
ATOM   1659 O  O   . GLY A 1 212 ? 0.31718   28.81558  4.12843   1.000 24.35709 ? 212 GLY A O   1 
ATOM   1660 N  N   . ALA A 1 213 ? 0.41920   29.26260  6.34421   1.000 31.18301 ? 213 ALA A N   1 
ATOM   1661 C  CA  . ALA A 1 213 ? 1.81553   28.91122  6.50450   1.000 28.83263 ? 213 ALA A CA  1 
ATOM   1662 C  C   . ALA A 1 213 ? 1.96851   27.40645  6.63087   1.000 24.37079 ? 213 ALA A C   1 
ATOM   1663 O  O   . ALA A 1 213 ? 0.99956   26.66116  6.79834   1.000 29.94479 ? 213 ALA A O   1 
ATOM   1664 C  CB  . ALA A 1 213 ? 2.40369   29.58751  7.74220   1.000 32.33088 ? 213 ALA A CB  1 
ATOM   1665 N  N   . GLY A 1 214 ? 3.20858   26.96242  6.55393   1.000 21.82771 ? 214 GLY A N   1 
ATOM   1666 C  CA  . GLY A 1 214 ? 3.53218   25.60229  6.92237   1.000 22.32407 ? 214 GLY A CA  1 
ATOM   1667 C  C   . GLY A 1 214 ? 3.14734   24.60450  5.85430   1.000 21.60089 ? 214 GLY A C   1 
ATOM   1668 O  O   . GLY A 1 214 ? 2.60048   24.93139  4.80077   1.000 23.73762 ? 214 GLY A O   1 
ATOM   1669 N  N   . LEU A 1 215 ? 3.41799   23.33916  6.16921   1.000 19.40218 ? 215 LEU A N   1 
ATOM   1670 C  CA  . LEU A 1 215 ? 3.24311   22.26887  5.19543   1.000 17.39395 ? 215 LEU A CA  1 
ATOM   1671 C  C   . LEU A 1 215 ? 1.77655   22.06692  4.84403   1.000 17.91693 ? 215 LEU A C   1 
ATOM   1672 O  O   . LEU A 1 215 ? 1.44601   21.82905  3.67634   1.000 21.70652 ? 215 LEU A O   1 
ATOM   1673 C  CB  . LEU A 1 215 ? 3.85651   20.97552  5.73523   1.000 19.44358 ? 215 LEU A CB  1 
ATOM   1674 C  CG  . LEU A 1 215 ? 3.66992   19.72766  4.85799   1.000 20.69752 ? 215 LEU A CG  1 
ATOM   1675 C  CD1 . LEU A 1 215 ? 4.21823   19.94662  3.45045   1.000 22.80982 ? 215 LEU A CD1 1 
ATOM   1676 C  CD2 . LEU A 1 215 ? 4.36752   18.54607  5.49602   1.000 22.43919 ? 215 LEU A CD2 1 
ATOM   1677 N  N   . VAL A 1 216 ? 0.87389   22.16831  5.82808   1.000 20.12664 ? 216 VAL A N   1 
ATOM   1678 C  CA  . VAL A 1 216 ? -0.54301  22.02210  5.49942   1.000 20.22060 ? 216 VAL A CA  1 
ATOM   1679 C  C   . VAL A 1 216 ? -0.97170  23.14010  4.55748   1.000 18.94983 ? 216 VAL A C   1 
ATOM   1680 O  O   . VAL A 1 216 ? -1.69134  22.90880  3.57887   1.000 22.99811 ? 216 VAL A O   1 
ATOM   1681 C  CB  . VAL A 1 216 ? -1.40682  21.97546  6.77461   1.000 20.33467 ? 216 VAL A CB  1 
ATOM   1682 C  CG1 . VAL A 1 216 ? -2.88370  21.91550  6.41361   1.000 20.44171 ? 216 VAL A CG1 1 
ATOM   1683 C  CG2 . VAL A 1 216 ? -1.02779  20.77347  7.62037   1.000 23.80019 ? 216 VAL A CG2 1 
ATOM   1684 N  N   . GLY A 1 217 ? -0.51481  24.36504  4.81781   1.000 18.50177 ? 217 GLY A N   1 
ATOM   1685 C  CA  . GLY A 1 217 ? -0.82970  25.46105  3.90714   1.000 18.95820 ? 217 GLY A CA  1 
ATOM   1686 C  C   . GLY A 1 217 ? -0.32111  25.21683  2.49866   1.000 20.69163 ? 217 GLY A C   1 
ATOM   1687 O  O   . GLY A 1 217 ? -0.99645  25.54396  1.51415   1.000 21.70111 ? 217 GLY A O   1 
ATOM   1688 N  N   . ALA A 1 218 ? 0.87603   24.64005  2.38070   1.000 21.19468 ? 218 ALA A N   1 
ATOM   1689 C  CA  . ALA A 1 218 ? 1.45082   24.39434  1.06074   1.000 19.56936 ? 218 ALA A CA  1 
ATOM   1690 C  C   . ALA A 1 218 ? 0.69794   23.29307  0.32630   1.000 21.07540 ? 218 ALA A C   1 
ATOM   1691 O  O   . ALA A 1 218 ? 0.45788   23.39935  -0.88338  1.000 23.36387 ? 218 ALA A O   1 
ATOM   1692 C  CB  . ALA A 1 218 ? 2.93072   24.03731  1.19194   1.000 21.95017 ? 218 ALA A CB  1 
ATOM   1693 N  N   . LEU A 1 219 ? 0.32370   22.22382  1.03725   1.000 20.34325 ? 219 LEU A N   1 
ATOM   1694 C  CA  . LEU A 1 219 ? -0.41731  21.13287  0.40391   1.000 20.83037 ? 219 LEU A CA  1 
ATOM   1695 C  C   . LEU A 1 219 ? -1.79012  21.59614  -0.05991  1.000 18.95883 ? 219 LEU A C   1 
ATOM   1696 O  O   . LEU A 1 219 ? -2.27024  21.17684  -1.11930  1.000 22.71607 ? 219 LEU A O   1 
ATOM   1697 C  CB  . LEU A 1 219 ? -0.55277  19.94734  1.36454   1.000 20.12703 ? 219 LEU A CB  1 
ATOM   1698 C  CG  . LEU A 1 219 ? 0.74441   19.19628  1.68444   1.000 20.09191 ? 219 LEU A CG  1 
ATOM   1699 C  CD1 . LEU A 1 219 ? 0.57015   18.20097  2.84553   1.000 21.46037 ? 219 LEU A CD1 1 
ATOM   1700 C  CD2 . LEU A 1 219 ? 1.25898   18.47760  0.44368   1.000 24.18638 ? 219 LEU A CD2 1 
ATOM   1701 N  N   . VAL A 1 220 ? -2.44172  22.45742  0.71964   1.000 19.48078 ? 220 VAL A N   1 
ATOM   1702 C  CA  . VAL A 1 220 ? -3.73507  22.99987  0.30598   1.000 19.87323 ? 220 VAL A CA  1 
ATOM   1703 C  C   . VAL A 1 220 ? -3.58725  23.86396  -0.94274  1.000 19.41929 ? 220 VAL A C   1 
ATOM   1704 O  O   . VAL A 1 220 ? -4.36743  23.74895  -1.90116  1.000 20.99390 ? 220 VAL A O   1 
ATOM   1705 C  CB  . VAL A 1 220 ? -4.37122  23.79743  1.45780   1.000 17.30495 ? 220 VAL A CB  1 
ATOM   1706 C  CG1 . VAL A 1 220 ? -5.62986  24.51501  0.95986   1.000 19.87660 ? 220 VAL A CG1 1 
ATOM   1707 C  CG2 . VAL A 1 220 ? -4.71106  22.85977  2.61304   1.000 20.14775 ? 220 VAL A CG2 1 
ATOM   1708 N  N   . ALA A 1 221 ? -2.58342  24.74130  -0.95470  1.000 20.00921 ? 221 ALA A N   1 
ATOM   1709 C  CA  . ALA A 1 221 ? -2.46352  25.70491  -2.04704  1.000 21.37323 ? 221 ALA A CA  1 
ATOM   1710 C  C   . ALA A 1 221 ? -1.97531  25.05960  -3.33817  1.000 22.19404 ? 221 ALA A C   1 
ATOM   1711 O  O   . ALA A 1 221 ? -2.27753  25.55797  -4.43059  1.000 24.73205 ? 221 ALA A O   1 
ATOM   1712 C  CB  . ALA A 1 221 ? -1.52541  26.84334  -1.64211  1.000 23.41552 ? 221 ALA A CB  1 
ATOM   1713 N  N   . ASP A 1 222 ? -1.21237  23.97579  -3.24176  1.000 20.91645 ? 222 ASP A N   1 
ATOM   1714 C  CA  . ASP A 1 222 ? -0.60495  23.37847  -4.42471  1.000 21.14572 ? 222 ASP A CA  1 
ATOM   1715 C  C   . ASP A 1 222 ? -1.25096  22.03841  -4.77450  1.000 21.56052 ? 222 ASP A C   1 
ATOM   1716 O  O   . ASP A 1 222 ? -2.12112  21.97904  -5.64891  1.000 22.28254 ? 222 ASP A O   1 
ATOM   1717 C  CB  . ASP A 1 222 ? 0.89626   23.23944  -4.19172  1.000 23.20761 ? 222 ASP A CB  1 
ATOM   1718 C  CG  . ASP A 1 222 ? 1.65589   22.85002  -5.44017  1.000 27.92863 ? 222 ASP A CG  1 
ATOM   1719 O  OD1 . ASP A 1 222 ? 1.02413   22.65016  -6.49856  1.000 29.79026 ? 222 ASP A OD1 1 
ATOM   1720 O  OD2 . ASP A 1 222 ? 2.89666   22.75502  -5.35992  1.000 34.63174 ? 222 ASP A OD2 1 
ATOM   1721 N  N   . GLN A 1 223 ? -0.85773  20.96163  -4.08955  1.000 21.68615 ? 223 GLN A N   1 
ATOM   1722 C  CA  . GLN A 1 223 ? -1.28815  19.62486  -4.50014  1.000 19.59839 ? 223 GLN A CA  1 
ATOM   1723 C  C   . GLN A 1 223 ? -2.80923  19.46885  -4.44687  1.000 19.54620 ? 223 GLN A C   1 
ATOM   1724 O  O   . GLN A 1 223 ? -3.41228  18.89193  -5.36026  1.000 20.57183 ? 223 GLN A O   1 
ATOM   1725 C  CB  . GLN A 1 223 ? -0.59931  18.56551  -3.63221  1.000 21.15553 ? 223 GLN A CB  1 
ATOM   1726 C  CG  . GLN A 1 223 ? 0.85785   18.30078  -3.99186  1.000 21.64117 ? 223 GLN A CG  1 
ATOM   1727 C  CD  . GLN A 1 223 ? 1.82916   19.25389  -3.31189  1.000 22.59637 ? 223 GLN A CD  1 
ATOM   1728 O  OE1 . GLN A 1 223 ? 1.41925   20.20476  -2.63741  1.000 23.86451 ? 223 GLN A OE1 1 
ATOM   1729 N  NE2 . GLN A 1 223 ? 3.12774   19.00663  -3.49189  1.000 27.18296 ? 223 GLN A NE2 1 
ATOM   1730 N  N   . LEU A 1 224 ? -3.45240  19.96620  -3.38846  1.000 19.78477 ? 224 LEU A N   1 
ATOM   1731 C  CA  . LEU A 1 224 ? -4.90313  19.82653  -3.29648  1.000 19.30854 ? 224 LEU A CA  1 
ATOM   1732 C  C   . LEU A 1 224 ? -5.59763  20.62388  -4.39451  1.000 19.88176 ? 224 LEU A C   1 
ATOM   1733 O  O   . LEU A 1 224 ? -6.52982  20.12610  -5.04265  1.000 22.16388 ? 224 LEU A O   1 
ATOM   1734 C  CB  . LEU A 1 224 ? -5.39472  20.26498  -1.91320  1.000 18.80470 ? 224 LEU A CB  1 
ATOM   1735 C  CG  . LEU A 1 224 ? -6.89412  20.09849  -1.65754  1.000 19.00302 ? 224 LEU A CG  1 
ATOM   1736 C  CD1 . LEU A 1 224 ? -7.30630  18.61418  -1.65697  1.000 20.57104 ? 224 LEU A CD1 1 
ATOM   1737 C  CD2 . LEU A 1 224 ? -7.25869  20.74397  -0.33403  1.000 20.75345 ? 224 LEU A CD2 1 
ATOM   1738 N  N   . ALA A 1 225 ? -5.13781  21.85041  -4.64255  1.000 20.57895 ? 225 ALA A N   1 
ATOM   1739 C  CA  . ALA A 1 225 ? -5.76262  22.66450  -5.68212  1.000 19.34871 ? 225 ALA A CA  1 
ATOM   1740 C  C   . ALA A 1 225 ? -5.54914  22.08509  -7.07578  1.000 17.99492 ? 225 ALA A C   1 
ATOM   1741 O  O   . ALA A 1 225 ? -6.26594  22.46613  -8.00590  1.000 19.35618 ? 225 ALA A O   1 
ATOM   1742 C  CB  . ALA A 1 225 ? -5.24094  24.10376  -5.62649  1.000 21.90997 ? 225 ALA A CB  1 
ATOM   1743 N  N   . ASN A 1 226 ? -4.57375  21.19267  -7.24355  1.000 17.97176 ? 226 ASN A N   1 
ATOM   1744 C  CA  . ASN A 1 226 ? -4.33935  20.49677  -8.50148  1.000 20.45143 ? 226 ASN A CA  1 
ATOM   1745 C  C   . ASN A 1 226 ? -4.95321  19.10209  -8.53330  1.000 23.84069 ? 226 ASN A C   1 
ATOM   1746 O  O   . ASN A 1 226 ? -4.75425  18.37406  -9.51375  1.000 24.16540 ? 226 ASN A O   1 
ATOM   1747 C  CB  . ASN A 1 226 ? -2.83616  20.40343  -8.77494  1.000 21.31490 ? 226 ASN A CB  1 
ATOM   1748 C  CG  . ASN A 1 226 ? -2.26670  21.69004  -9.33027  1.000 22.17554 ? 226 ASN A CG  1 
ATOM   1749 O  OD1 . ASN A 1 226 ? -2.20826  21.86823  -10.54417 1.000 24.98155 ? 226 ASN A OD1 1 
ATOM   1750 N  ND2 . ASN A 1 226 ? -1.83733  22.59291  -8.44623  1.000 23.55651 ? 226 ASN A ND2 1 
ATOM   1751 N  N   . GLY A 1 227 ? -5.68783  18.71351  -7.49103  1.000 20.13784 ? 227 GLY A N   1 
ATOM   1752 C  CA  . GLY A 1 227 ? -6.25669  17.38234  -7.41353  1.000 19.76629 ? 227 GLY A CA  1 
ATOM   1753 C  C   . GLY A 1 227 ? -5.24756  16.26785  -7.26684  1.000 21.48344 ? 227 GLY A C   1 
ATOM   1754 O  O   . GLY A 1 227 ? -5.59862  15.10151  -7.48276  1.000 25.18459 ? 227 GLY A O   1 
ATOM   1755 N  N   . GLU A 1 228 ? -4.00403  16.58957  -6.90836  1.000 21.07436 ? 228 GLU A N   1 
ATOM   1756 C  CA  . GLU A 1 228 ? -2.95005  15.58992  -6.83454  1.000 21.11300 ? 228 GLU A CA  1 
ATOM   1757 C  C   . GLU A 1 228 ? -2.96942  14.82960  -5.51975  1.000 22.77058 ? 228 GLU A C   1 
ATOM   1758 O  O   . GLU A 1 228 ? -2.35109  13.76826  -5.42610  1.000 24.13052 ? 228 GLU A O   1 
ATOM   1759 C  CB  . GLU A 1 228 ? -1.58429  16.24958  -7.05130  1.000 22.56684 ? 228 GLU A CB  1 
ATOM   1760 C  CG  . GLU A 1 228 ? -1.40857  16.76294  -8.48429  1.000 25.85349 ? 228 GLU A CG  1 
ATOM   1761 C  CD  . GLU A 1 228 ? -0.21499  17.66859  -8.64869  1.000 30.24174 ? 228 GLU A CD  1 
ATOM   1762 O  OE1 . GLU A 1 228 ? 0.28657   18.19383  -7.63196  1.000 31.38961 ? 228 GLU A OE1 1 
ATOM   1763 O  OE2 . GLU A 1 228 ? 0.21983   17.85772  -9.80535  1.000 33.15631 ? 228 GLU A OE2 1 
ATOM   1764 N  N   . ILE A 1 229 ? -3.68341  15.34014  -4.52278  1.000 21.78460 ? 229 ILE A N   1 
ATOM   1765 C  CA  . ILE A 1 229 ? -3.92344  14.64220  -3.26970  1.000 21.79121 ? 229 ILE A CA  1 
ATOM   1766 C  C   . ILE A 1 229 ? -5.39658  14.82085  -2.95329  1.000 21.34091 ? 229 ILE A C   1 
ATOM   1767 O  O   . ILE A 1 229 ? -5.97515  15.87179  -3.25270  1.000 22.21155 ? 229 ILE A O   1 
ATOM   1768 C  CB  . ILE A 1 229 ? -3.02645  15.17183  -2.12729  1.000 21.27481 ? 229 ILE A CB  1 
ATOM   1769 C  CG1 . ILE A 1 229 ? -3.09044  14.24911  -0.91336  1.000 22.95597 ? 229 ILE A CG1 1 
ATOM   1770 C  CG2 . ILE A 1 229 ? -3.40095  16.60747  -1.73745  1.000 21.86213 ? 229 ILE A CG2 1 
ATOM   1771 C  CD1 . ILE A 1 229 ? -2.08798  14.60254  0.14806   1.000 26.95555 ? 229 ILE A CD1 1 
ATOM   1772 N  N   . ASP A 1 230 ? -6.02129  13.77532  -2.41657  1.000 23.20043 ? 230 ASP A N   1 
ATOM   1773 C  CA  . ASP A 1 230 ? -7.39807  13.89619  -1.97625  1.000 25.39419 ? 230 ASP A CA  1 
ATOM   1774 C  C   . ASP A 1 230 ? -7.42739  14.65775  -0.65542  1.000 25.15666 ? 230 ASP A C   1 
ATOM   1775 O  O   . ASP A 1 230 ? -6.47232  14.61686  0.12509   1.000 23.19795 ? 230 ASP A O   1 
ATOM   1776 C  CB  . ASP A 1 230 ? -8.04760  12.51819  -1.80840  1.000 27.24367 ? 230 ASP A CB  1 
ATOM   1777 C  CG  . ASP A 1 230 ? -8.11880  11.72757  -3.10830  1.000 30.66876 ? 230 ASP A CG  1 
ATOM   1778 O  OD1 . ASP A 1 230 ? -8.21294  12.33403  -4.20005  1.000 33.77503 ? 230 ASP A OD1 1 
ATOM   1779 O  OD2 . ASP A 1 230 ? -8.10446  10.47983  -3.03380  1.000 30.69398 ? 230 ASP A OD2 1 
ATOM   1780 N  N   . ARG A 1 231 ? -8.52526  15.37998  -0.42583  1.000 24.41698 ? 231 ARG A N   1 
ATOM   1781 C  CA  . ARG A 1 231 ? -8.70267  16.09128  0.83892   1.000 23.90419 ? 231 ARG A CA  1 
ATOM   1782 C  C   . ARG A 1 231 ? -8.53050  15.15686  2.03190   1.000 21.63638 ? 231 ARG A C   1 
ATOM   1783 O  O   . ARG A 1 231 ? -7.86974  15.49357  3.02158   1.000 22.35893 ? 231 ARG A O   1 
ATOM   1784 C  CB  . ARG A 1 231 ? -10.08389 16.72970  0.86643   1.000 28.07089 ? 231 ARG A CB  1 
ATOM   1785 C  CG  . ARG A 1 231 ? -10.34554 17.60950  2.05336   1.000 29.62396 ? 231 ARG A CG  1 
ATOM   1786 C  CD  . ARG A 1 231 ? -11.70844 18.25786  1.91833   1.000 35.71071 ? 231 ARG A CD  1 
ATOM   1787 N  NE  . ARG A 1 231 ? -11.95249 19.16725  3.02423   1.000 37.08404 ? 231 ARG A NE  1 
ATOM   1788 C  CZ  . ARG A 1 231 ? -11.92744 20.48798  2.92778   1.000 37.04700 ? 231 ARG A CZ  1 
ATOM   1789 N  NH1 . ARG A 1 231 ? -11.77789 21.09303  1.75836   1.000 36.15395 ? 231 ARG A NH1 1 
ATOM   1790 N  NH2 . ARG A 1 231 ? -12.06327 21.21898  4.03103   1.000 35.30142 ? 231 ARG A NH2 1 
ATOM   1791 N  N   . GLU A 1 232 ? -9.13095  13.97900  1.95346   1.000 22.68631 ? 232 GLU A N   1 
ATOM   1792 C  CA  A GLU A 1 232 ? -9.05835  13.00571  3.03343   0.567 22.49619 ? 232 GLU A CA  1 
ATOM   1793 C  CA  B GLU A 1 232 ? -9.03810  13.05010  3.07610   0.433 23.80208 ? 232 GLU A CA  1 
ATOM   1794 C  C   . GLU A 1 232 ? -7.62747  12.50334  3.23034   1.000 22.69252 ? 232 GLU A C   1 
ATOM   1795 O  O   . GLU A 1 232 ? -7.20196  12.22541  4.36148   1.000 21.63299 ? 232 GLU A O   1 
ATOM   1796 C  CB  A GLU A 1 232 ? -10.02588 11.86636  2.70679   0.567 26.54335 ? 232 GLU A CB  1 
ATOM   1797 C  CB  B GLU A 1 232 ? -10.04209 11.90556  2.92250   0.433 29.36170 ? 232 GLU A CB  1 
ATOM   1798 C  CG  A GLU A 1 232 ? -11.52066 12.29129  2.58281   0.567 32.25812 ? 232 GLU A CG  1 
ATOM   1799 C  CG  B GLU A 1 232 ? -11.48335 12.27250  3.28028   0.433 34.86935 ? 232 GLU A CG  1 
ATOM   1800 C  CD  A GLU A 1 232 ? -11.84566 13.34933  1.49361   0.567 32.22826 ? 232 GLU A CD  1 
ATOM   1801 C  CD  B GLU A 1 232 ? -11.74680 12.34388  4.77986   0.433 38.58988 ? 232 GLU A CD  1 
ATOM   1802 O  OE1 A GLU A 1 232 ? -11.36849 13.24911  0.32955   0.567 22.84807 ? 232 GLU A OE1 1 
ATOM   1803 O  OE1 B GLU A 1 232 ? -10.88287 11.91295  5.57777   0.433 38.65702 ? 232 GLU A OE1 1 
ATOM   1804 O  OE2 A GLU A 1 232 ? -12.60225 14.29832  1.81801   0.567 34.36308 ? 232 GLU A OE2 1 
ATOM   1805 O  OE2 B GLU A 1 232 ? -12.83470 12.82729  5.16278   0.433 39.70051 ? 232 GLU A OE2 1 
ATOM   1806 N  N   . GLU A 1 233 ? -6.88152  12.36237  2.12645   1.000 23.67318 ? 233 GLU A N   1 
ATOM   1807 C  CA  . GLU A 1 233 ? -5.47168  11.98742  2.21221   1.000 21.09579 ? 233 GLU A CA  1 
ATOM   1808 C  C   . GLU A 1 233 ? -4.65138  13.08060  2.87307   1.000 18.95798 ? 233 GLU A C   1 
ATOM   1809 O  O   . GLU A 1 233 ? -3.69594  12.78760  3.60282   1.000 22.08360 ? 233 GLU A O   1 
ATOM   1810 C  CB  . GLU A 1 233 ? -4.87993  11.73165  0.83224   1.000 22.53549 ? 233 GLU A CB  1 
ATOM   1811 C  CG  . GLU A 1 233 ? -5.23758  10.46420  0.13614   1.000 26.70695 ? 233 GLU A CG  1 
ATOM   1812 C  CD  . GLU A 1 233 ? -4.46003  10.34615  -1.15802  1.000 30.00063 ? 233 GLU A CD  1 
ATOM   1813 O  OE1 . GLU A 1 233 ? -4.70310  11.16820  -2.07772  1.000 27.61028 ? 233 GLU A OE1 1 
ATOM   1814 O  OE2 . GLU A 1 233 ? -3.57240  9.46708   -1.23752  1.000 30.68552 ? 233 GLU A OE2 1 
ATOM   1815 N  N   . LEU A 1 234 ? -4.94662  14.34551  2.54962   1.000 20.16668 ? 234 LEU A N   1 
ATOM   1816 C  CA  . LEU A 1 234 ? -4.23886  15.44923  3.18811   1.000 18.60512 ? 234 LEU A CA  1 
ATOM   1817 C  C   . LEU A 1 234 ? -4.44380  15.40766  4.69772   1.000 19.80725 ? 234 LEU A C   1 
ATOM   1818 O  O   . LEU A 1 234 ? -3.48713  15.54992  5.47044   1.000 19.28001 ? 234 LEU A O   1 
ATOM   1819 C  CB  . LEU A 1 234 ? -4.70773  16.78939  2.59650   1.000 19.88179 ? 234 LEU A CB  1 
ATOM   1820 C  CG  . LEU A 1 234 ? -3.78028  18.00867  2.61395   1.000 20.58285 ? 234 LEU A CG  1 
ATOM   1821 C  CD1 . LEU A 1 234 ? -4.34474  19.13795  1.75830   1.000 22.66562 ? 234 LEU A CD1 1 
ATOM   1822 C  CD2 . LEU A 1 234 ? -3.53013  18.52300  4.01571   1.000 24.38149 ? 234 LEU A CD2 1 
ATOM   1823 N  N   . ILE A 1 235 ? -5.68431  15.18271  5.12848   1.000 18.36764 ? 235 ILE A N   1 
ATOM   1824 C  CA  . ILE A 1 235 ? -5.98455  15.03840  6.55279   1.000 19.12177 ? 235 ILE A CA  1 
ATOM   1825 C  C   . ILE A 1 235 ? -5.14922  13.91763  7.17174   1.000 20.08035 ? 235 ILE A C   1 
ATOM   1826 O  O   . ILE A 1 235 ? -4.53077  14.09887  8.22893   1.000 19.67025 ? 235 ILE A O   1 
ATOM   1827 C  CB  . ILE A 1 235 ? -7.49540  14.80923  6.75222   1.000 19.37348 ? 235 ILE A CB  1 
ATOM   1828 C  CG1 . ILE A 1 235 ? -8.27448  16.07591  6.38686   1.000 19.80908 ? 235 ILE A CG1 1 
ATOM   1829 C  CG2 . ILE A 1 235 ? -7.80438  14.40074  8.18579   1.000 22.87273 ? 235 ILE A CG2 1 
ATOM   1830 C  CD1 . ILE A 1 235 ? -9.77440  15.87057  6.39910   1.000 22.24922 ? 235 ILE A CD1 1 
ATOM   1831 N  N   . SER A 1 236 ? -5.13028  12.74007  6.53232   1.000 20.66672 ? 236 SER A N   1 
ATOM   1832 C  CA  . SER A 1 236 ? -4.37917  11.60598  7.07898   1.000 17.13708 ? 236 SER A CA  1 
ATOM   1833 C  C   . SER A 1 236 ? -2.88871  11.90378  7.13349   1.000 18.34415 ? 236 SER A C   1 
ATOM   1834 O  O   . SER A 1 236 ? -2.20179  11.51782  8.09128   1.000 20.74595 ? 236 SER A O   1 
ATOM   1835 C  CB  . SER A 1 236 ? -4.62092  10.34654  6.24390   1.000 20.83870 ? 236 SER A CB  1 
ATOM   1836 O  OG  . SER A 1 236 ? -5.97110  9.95000   6.30840   1.000 23.93944 ? 236 SER A OG  1 
ATOM   1837 N  N   . THR A 1 237 ? -2.36911  12.57101  6.10156   1.000 18.86327 ? 237 THR A N   1 
ATOM   1838 C  CA  . THR A 1 237 ? -0.95150  12.91693  6.06005   1.000 16.84177 ? 237 THR A CA  1 
ATOM   1839 C  C   . THR A 1 237 ? -0.59886  13.90082  7.16565   1.000 16.25843 ? 237 THR A C   1 
ATOM   1840 O  O   . THR A 1 237 ? 0.38561   13.71536  7.89167   1.000 16.23738 ? 237 THR A O   1 
ATOM   1841 C  CB  . THR A 1 237 ? -0.60911  13.52012  4.69395   1.000 17.03235 ? 237 THR A CB  1 
ATOM   1842 O  OG1 . THR A 1 237 ? -1.03541  12.62531  3.65422   1.000 22.74201 ? 237 THR A OG1 1 
ATOM   1843 C  CG2 . THR A 1 237 ? 0.88808   13.75852  4.56906   1.000 17.72506 ? 237 THR A CG2 1 
ATOM   1844 N  N   . ALA A 1 238 ? -1.39204  14.96073  7.30312   1.000 17.67097 ? 238 ALA A N   1 
ATOM   1845 C  CA  . ALA A 1 238 ? -1.12543  15.92254  8.36448   1.000 17.07270 ? 238 ALA A CA  1 
ATOM   1846 C  C   . ALA A 1 238 ? -1.25504  15.26400  9.72716   1.000 16.82797 ? 238 ALA A C   1 
ATOM   1847 O  O   . ALA A 1 238 ? -0.47768  15.55128  10.64207  1.000 18.48877 ? 238 ALA A O   1 
ATOM   1848 C  CB  . ALA A 1 238 ? -2.07776  17.10985  8.26000   1.000 18.87771 ? 238 ALA A CB  1 
ATOM   1849 N  N   . MET A 1 239 ? -2.22661  14.36798  9.87614   1.000 16.36092 ? 239 MET A N   1 
ATOM   1850 C  CA  . MET A 1 239 ? -2.40387  13.69506  11.15889  1.000 18.68197 ? 239 MET A CA  1 
ATOM   1851 C  C   . MET A 1 239 ? -1.20141  12.82141  11.49556  1.000 17.90484 ? 239 MET A C   1 
ATOM   1852 O  O   . MET A 1 239 ? -0.72500  12.81535  12.63656  1.000 17.03086 ? 239 MET A O   1 
ATOM   1853 C  CB  . MET A 1 239 ? -3.68599  12.86302  11.13933  1.000 19.27170 ? 239 MET A CB  1 
ATOM   1854 C  CG  . MET A 1 239 ? -4.10733  12.36688  12.52888  1.000 22.27307 ? 239 MET A CG  1 
ATOM   1855 S  SD  . MET A 1 239 ? -5.52790  11.28069  12.48587  1.000 23.62853 ? 239 MET A SD  1 
ATOM   1856 C  CE  . MET A 1 239 ? -6.66763  12.33038  11.59956  1.000 22.79347 ? 239 MET A CE  1 
ATOM   1857 N  N   . LEU A 1 240 ? -0.69621  12.07202  10.51844  1.000 16.63860 ? 240 LEU A N   1 
ATOM   1858 C  CA  . LEU A 1 240 ? 0.48579   11.25144  10.75879  1.000 18.25977 ? 240 LEU A CA  1 
ATOM   1859 C  C   . LEU A 1 240 ? 1.66543   12.10923  11.19786  1.000 18.51573 ? 240 LEU A C   1 
ATOM   1860 O  O   . LEU A 1 240 ? 2.35676   11.78852  12.16650  1.000 18.24883 ? 240 LEU A O   1 
ATOM   1861 C  CB  . LEU A 1 240 ? 0.83710   10.46032  9.49715   1.000 19.62819 ? 240 LEU A CB  1 
ATOM   1862 C  CG  . LEU A 1 240 ? 2.18161   9.72731   9.53454   1.000 23.71573 ? 240 LEU A CG  1 
ATOM   1863 C  CD1 . LEU A 1 240 ? 2.16868   8.65009   10.60021  1.000 25.23995 ? 240 LEU A CD1 1 
ATOM   1864 C  CD2 . LEU A 1 240 ? 2.49601   9.12977   8.17296   1.000 22.42960 ? 240 LEU A CD2 1 
ATOM   1865 N  N   . LEU A 1 241 ? 1.91142   13.21275  10.49855  1.000 17.87103 ? 241 LEU A N   1 
ATOM   1866 C  CA  A LEU A 1 241 ? 3.06363   14.02931  10.85077  0.432 16.69907 ? 241 LEU A CA  1 
ATOM   1867 C  CA  B LEU A 1 241 ? 3.05343   14.05213  10.84244  0.568 17.22801 ? 241 LEU A CA  1 
ATOM   1868 C  C   . LEU A 1 241 ? 2.87213   14.69031  12.21261  1.000 15.89374 ? 241 LEU A C   1 
ATOM   1869 O  O   . LEU A 1 241 ? 3.82947   14.81317  12.98348  1.000 18.41975 ? 241 LEU A O   1 
ATOM   1870 C  CB  A LEU A 1 241 ? 3.32880   15.06098  9.75308   0.432 16.16316 ? 241 LEU A CB  1 
ATOM   1871 C  CB  B LEU A 1 241 ? 3.25031   15.12347  9.77279   0.568 17.16141 ? 241 LEU A CB  1 
ATOM   1872 C  CG  A LEU A 1 241 ? 4.25057   14.54081  8.63717   0.432 16.86054 ? 241 LEU A CG  1 
ATOM   1873 C  CG  B LEU A 1 241 ? 3.68495   14.56333  8.42089   0.568 20.50874 ? 241 LEU A CG  1 
ATOM   1874 C  CD1 A LEU A 1 241 ? 3.67303   13.33797  7.87771   0.432 16.70095 ? 241 LEU A CD1 1 
ATOM   1875 C  CD1 B LEU A 1 241 ? 3.53405   15.61905  7.33453   0.568 22.00196 ? 241 LEU A CD1 1 
ATOM   1876 C  CD2 A LEU A 1 241 ? 4.60694   15.65600  7.67156   0.432 18.32098 ? 241 LEU A CD2 1 
ATOM   1877 C  CD2 B LEU A 1 241 ? 5.11842   14.04560  8.49896   0.568 21.33758 ? 241 LEU A CD2 1 
ATOM   1878 N  N   . LEU A 1 242 ? 1.64597   15.09714  12.53113  1.000 16.39430 ? 242 LEU A N   1 
ATOM   1879 C  CA  . LEU A 1 242 ? 1.36401   15.70873  13.83090  1.000 17.91480 ? 242 LEU A CA  1 
ATOM   1880 C  C   . LEU A 1 242 ? 1.61488   14.72890  14.97187  1.000 22.16413 ? 242 LEU A C   1 
ATOM   1881 O  O   . LEU A 1 242 ? 2.26677   15.06085  15.97106  1.000 21.90765 ? 242 LEU A O   1 
ATOM   1882 C  CB  . LEU A 1 242 ? -0.08285  16.20720  13.85659  1.000 20.95828 ? 242 LEU A CB  1 
ATOM   1883 C  CG  . LEU A 1 242 ? -0.53876  16.99946  15.08297  1.000 21.83185 ? 242 LEU A CG  1 
ATOM   1884 C  CD1 . LEU A 1 242 ? 0.17600   18.34326  15.14348  1.000 30.56215 ? 242 LEU A CD1 1 
ATOM   1885 C  CD2 . LEU A 1 242 ? -2.04195  17.20590  15.04904  1.000 25.18571 ? 242 LEU A CD2 1 
ATOM   1886 N  N   . ILE A 1 243 ? 1.10499   13.50992  14.83787  1.000 19.53941 ? 243 ILE A N   1 
ATOM   1887 C  CA  . ILE A 1 243 ? 1.20326   12.54690  15.92750  1.000 18.83026 ? 243 ILE A CA  1 
ATOM   1888 C  C   . ILE A 1 243 ? 2.63361   12.04956  16.07688  1.000 18.90095 ? 243 ILE A C   1 
ATOM   1889 O  O   . ILE A 1 243 ? 3.17349   11.98174  17.18850  1.000 21.90010 ? 243 ILE A O   1 
ATOM   1890 C  CB  . ILE A 1 243 ? 0.22132   11.39316  15.68754  1.000 22.98568 ? 243 ILE A CB  1 
ATOM   1891 C  CG1 . ILE A 1 243 ? -1.21086  11.88298  15.91548  1.000 26.46286 ? 243 ILE A CG1 1 
ATOM   1892 C  CG2 . ILE A 1 243 ? 0.58259   10.21921  16.54001  1.000 29.57290 ? 243 ILE A CG2 1 
ATOM   1893 C  CD1 . ILE A 1 243 ? -2.24728  10.89226  15.49180  1.000 31.93975 ? 243 ILE A CD1 1 
ATOM   1894 N  N   . ALA A 1 244 ? 3.26991   11.67338  14.96513  1.000 17.78406 ? 244 ALA A N   1 
ATOM   1895 C  CA  . ALA A 1 244 ? 4.65843   11.23923  15.05366  1.000 17.37620 ? 244 ALA A CA  1 
ATOM   1896 C  C   . ALA A 1 244 ? 5.54821   12.36393  15.57237  1.000 19.45333 ? 244 ALA A C   1 
ATOM   1897 O  O   . ALA A 1 244 ? 6.42659   12.13303  16.41153  1.000 21.62421 ? 244 ALA A O   1 
ATOM   1898 C  CB  . ALA A 1 244 ? 5.14668   10.74898  13.68792  1.000 19.25817 ? 244 ALA A CB  1 
ATOM   1899 N  N   . GLY A 1 245 ? 5.32670   13.59124  15.09678  1.000 18.94986 ? 245 GLY A N   1 
ATOM   1900 C  CA  . GLY A 1 245 ? 6.14292   14.70102  15.55481  1.000 22.73943 ? 245 GLY A CA  1 
ATOM   1901 C  C   . GLY A 1 245 ? 5.99804   14.98875  17.03840  1.000 23.77305 ? 245 GLY A C   1 
ATOM   1902 O  O   . GLY A 1 245 ? 6.93676   15.48728  17.66999  1.000 30.10631 ? 245 GLY A O   1 
ATOM   1903 N  N   . HIS A 1 246 ? 4.81828   14.71314  17.60389  1.000 23.77396 ? 246 HIS A N   1 
ATOM   1904 C  CA  . HIS A 1 246 ? 4.56495   14.85773  19.03848  1.000 28.37182 ? 246 HIS A CA  1 
ATOM   1905 C  C   . HIS A 1 246 ? 5.17505   13.70880  19.82842  1.000 23.97403 ? 246 HIS A C   1 
ATOM   1906 O  O   . HIS A 1 246 ? 5.98067   13.91054  20.74820  1.000 26.40723 ? 246 HIS A O   1 
ATOM   1907 C  CB  . HIS A 1 246 ? 3.04909   14.86400  19.31946  1.000 28.68699 ? 246 HIS A CB  1 
ATOM   1908 C  CG  . HIS A 1 246 ? 2.37760   16.19232  19.18075  1.000 31.68770 ? 246 HIS A CG  1 
ATOM   1909 N  ND1 . HIS A 1 246 ? 2.21339   16.83095  17.96957  1.000 35.77438 ? 246 HIS A ND1 1 
ATOM   1910 C  CD2 . HIS A 1 246 ? 1.77517   16.97813  20.10497  1.000 35.89280 ? 246 HIS A CD2 1 
ATOM   1911 C  CE1 . HIS A 1 246 ? 1.56081   17.96498  18.15917  1.000 36.01304 ? 246 HIS A CE1 1 
ATOM   1912 N  NE2 . HIS A 1 246 ? 1.28520   18.07864  19.44605  1.000 36.17508 ? 246 HIS A NE2 1 
ATOM   1913 N  N   . GLU A 1 247 ? 4.75597   12.49029  19.51060  1.000 20.58982 ? 247 GLU A N   1 
ATOM   1914 C  CA  . GLU A 1 247 ? 4.82765   11.43145  20.50703  1.000 18.00289 ? 247 GLU A CA  1 
ATOM   1915 C  C   . GLU A 1 247 ? 6.18914   10.76227  20.54962  1.000 21.27231 ? 247 GLU A C   1 
ATOM   1916 O  O   . GLU A 1 247 ? 6.60516   10.29109  21.61309  1.000 22.42160 ? 247 GLU A O   1 
ATOM   1917 C  CB  . GLU A 1 247 ? 3.73782   10.39199  20.23594  1.000 20.66506 ? 247 GLU A CB  1 
ATOM   1918 C  CG  . GLU A 1 247 ? 2.32095   10.94211  20.21211  1.000 26.40865 ? 247 GLU A CG  1 
ATOM   1919 C  CD  . GLU A 1 247 ? 1.86849   11.51436  21.55153  1.000 32.20810 ? 247 GLU A CD  1 
ATOM   1920 O  OE1 . GLU A 1 247 ? 2.42681   11.12708  22.60431  1.000 34.55777 ? 247 GLU A OE1 1 
ATOM   1921 O  OE2 . GLU A 1 247 ? 0.94650   12.36058  21.54618  1.000 35.11077 ? 247 GLU A OE2 1 
ATOM   1922 N  N   . THR A 1 248 ? 6.88252   10.70112  19.41576  1.000 19.10788 ? 248 THR A N   1 
ATOM   1923 C  CA  . THR A 1 248 ? 8.14923   9.98505   19.34781  1.000 19.15074 ? 248 THR A CA  1 
ATOM   1924 C  C   . THR A 1 248 ? 9.24905   10.71952  20.10552  1.000 17.56214 ? 248 THR A C   1 
ATOM   1925 O  O   . THR A 1 248 ? 9.92357   10.13532  20.96447  1.000 18.44765 ? 248 THR A O   1 
ATOM   1926 C  CB  . THR A 1 248 ? 8.55209   9.79379   17.89057  1.000 20.18712 ? 248 THR A CB  1 
ATOM   1927 O  OG1 . THR A 1 248 ? 8.70187   11.08594  17.28052  1.000 23.38592 ? 248 THR A OG1 1 
ATOM   1928 C  CG2 . THR A 1 248 ? 7.49009   9.00658   17.13781  1.000 22.98549 ? 248 THR A CG2 1 
ATOM   1929 N  N   . THR A 1 249 ? 9.47418   11.99322  19.77221  1.000 16.98897 ? 249 THR A N   1 
ATOM   1930 C  CA  . THR A 1 249 ? 10.53968  12.73447  20.42961  1.000 17.08332 ? 249 THR A CA  1 
ATOM   1931 C  C   . THR A 1 249 ? 10.26643  12.86883  21.91418  1.000 18.22652 ? 249 THR A C   1 
ATOM   1932 O  O   . THR A 1 249 ? 11.18269  12.75117  22.73587  1.000 21.67646 ? 249 THR A O   1 
ATOM   1933 C  CB  . THR A 1 249 ? 10.69505  14.11242  19.80016  1.000 21.28307 ? 249 THR A CB  1 
ATOM   1934 O  OG1 . THR A 1 249 ? 11.09578  13.94607  18.43810  1.000 22.64989 ? 249 THR A OG1 1 
ATOM   1935 C  CG2 . THR A 1 249 ? 11.76125  14.92283  20.56703  1.000 21.59102 ? 249 THR A CG2 1 
ATOM   1936 N  N   . ALA A 1 250 ? 9.00817   13.10774  22.28020  1.000 17.72109 ? 250 ALA A N   1 
ATOM   1937 C  CA  . ALA A 1 250 ? 8.67415   13.21477  23.70002  1.000 16.38014 ? 250 ALA A CA  1 
ATOM   1938 C  C   . ALA A 1 250 ? 9.04843   11.94182  24.44967  1.000 18.83192 ? 250 ALA A C   1 
ATOM   1939 O  O   . ALA A 1 250 ? 9.56396   12.00362  25.57040  1.000 19.67114 ? 250 ALA A O   1 
ATOM   1940 C  CB  . ALA A 1 250 ? 7.18612   13.52117  23.86588  1.000 18.79757 ? 250 ALA A CB  1 
ATOM   1941 N  N   . SER A 1 251 ? 8.80852   10.78157  23.83929  1.000 18.67416 ? 251 SER A N   1 
ATOM   1942 C  CA  . SER A 1 251 ? 9.15911   9.51072   24.46871  1.000 18.46921 ? 251 SER A CA  1 
ATOM   1943 C  C   . SER A 1 251 ? 10.66470  9.33285   24.56702  1.000 19.06197 ? 251 SER A C   1 
ATOM   1944 O  O   . SER A 1 251 ? 11.17488  8.84087   25.58040  1.000 20.05640 ? 251 SER A O   1 
ATOM   1945 C  CB  . SER A 1 251 ? 8.54426   8.35511   23.68561  1.000 20.79958 ? 251 SER A CB  1 
ATOM   1946 O  OG  . SER A 1 251 ? 7.14330   8.33516   23.87536  1.000 27.83508 ? 251 SER A OG  1 
ATOM   1947 N  N   . MET A 1 252 ? 11.38909  9.69147   23.51076  1.000 17.84125 ? 252 MET A N   1 
ATOM   1948 C  CA  . MET A 1 252 ? 12.84120  9.59963   23.55562  1.000 18.05068 ? 252 MET A CA  1 
ATOM   1949 C  C   . MET A 1 252 ? 13.41078  10.48886  24.64640  1.000 18.64970 ? 252 MET A C   1 
ATOM   1950 O  O   . MET A 1 252 ? 14.36205  10.10594  25.32728  1.000 19.30530 ? 252 MET A O   1 
ATOM   1951 C  CB  . MET A 1 252 ? 13.43749  9.97864   22.20330  1.000 18.96824 ? 252 MET A CB  1 
ATOM   1952 C  CG  . MET A 1 252 ? 13.48506  8.84483   21.20678  1.000 19.16277 ? 252 MET A CG  1 
ATOM   1953 S  SD  . MET A 1 252 ? 14.34137  7.38530   21.82335  1.000 19.26427 ? 252 MET A SD  1 
ATOM   1954 C  CE  . MET A 1 252 ? 16.02180  7.98121   21.97415  1.000 20.22005 ? 252 MET A CE  1 
ATOM   1955 N  N   . THR A 1 253 ? 12.82848  11.67034  24.84416  1.000 18.94633 ? 253 THR A N   1 
ATOM   1956 C  CA  . THR A 1 253 ? 13.33790  12.57494  25.87309  1.000 18.19848 ? 253 THR A CA  1 
ATOM   1957 C  C   . THR A 1 253 ? 13.17852  11.97185  27.26391  1.000 18.12280 ? 253 THR A C   1 
ATOM   1958 O  O   . THR A 1 253 ? 14.14340  11.89303  28.03292  1.000 19.78472 ? 253 THR A O   1 
ATOM   1959 C  CB  . THR A 1 253 ? 12.62614  13.92683  25.79743  1.000 19.22341 ? 253 THR A CB  1 
ATOM   1960 O  OG1 . THR A 1 253 ? 12.96565  14.56671  24.55973  1.000 19.98334 ? 253 THR A OG1 1 
ATOM   1961 C  CG2 . THR A 1 253 ? 13.03148  14.83121  26.98123  1.000 19.15009 ? 253 THR A CG2 1 
ATOM   1962 N  N   . SER A 1 254 ? 11.96962  11.52437  27.60115  1.000 18.33551 ? 254 SER A N   1 
ATOM   1963 C  CA  A SER A 1 254 ? 11.74996  10.99479  28.94295  0.635 18.64994 ? 254 SER A CA  1 
ATOM   1964 C  CA  B SER A 1 254 ? 11.73459  10.98602  28.93793  0.365 19.94889 ? 254 SER A CA  1 
ATOM   1965 C  C   . SER A 1 254 ? 12.54161  9.71604   29.17034  1.000 18.75169 ? 254 SER A C   1 
ATOM   1966 O  O   . SER A 1 254 ? 13.15883  9.54687   30.22979  1.000 21.54476 ? 254 SER A O   1 
ATOM   1967 C  CB  A SER A 1 254 ? 10.26156  10.75759  29.18498  0.635 20.33914 ? 254 SER A CB  1 
ATOM   1968 C  CB  B SER A 1 254 ? 10.24179  10.72301  29.14510  0.365 23.41699 ? 254 SER A CB  1 
ATOM   1969 O  OG  A SER A 1 254 ? 9.53530   11.95399  29.02221  0.635 21.51921 ? 254 SER A OG  1 
ATOM   1970 O  OG  B SER A 1 254 ? 9.77600   9.69573   28.28446  0.365 25.73320 ? 254 SER A OG  1 
ATOM   1971 N  N   . LEU A 1 255 ? 12.56872  8.81517   28.18599  1.000 18.10409 ? 255 LEU A N   1 
ATOM   1972 C  CA  . LEU A 1 255 ? 13.29628  7.56947   28.40565  1.000 18.31769 ? 255 LEU A CA  1 
ATOM   1973 C  C   . LEU A 1 255 ? 14.80446  7.79388   28.41310  1.000 20.35733 ? 255 LEU A C   1 
ATOM   1974 O  O   . LEU A 1 255 ? 15.52601  7.09236   29.13412  1.000 19.28613 ? 255 LEU A O   1 
ATOM   1975 C  CB  . LEU A 1 255 ? 12.90336  6.52247   27.35987  1.000 17.86395 ? 255 LEU A CB  1 
ATOM   1976 C  CG  . LEU A 1 255 ? 11.47781  5.96409   27.45694  1.000 19.70097 ? 255 LEU A CG  1 
ATOM   1977 C  CD1 . LEU A 1 255 ? 11.22451  4.95428   26.32202  1.000 22.61518 ? 255 LEU A CD1 1 
ATOM   1978 C  CD2 . LEU A 1 255 ? 11.22307  5.31299   28.79741  1.000 27.32468 ? 255 LEU A CD2 1 
ATOM   1979 N  N   . SER A 1 256 ? 15.29688  8.77364   27.64636  1.000 18.33262 ? 256 SER A N   1 
ATOM   1980 C  CA  . SER A 1 256 ? 16.72382  9.08263   27.67970  1.000 17.41647 ? 256 SER A CA  1 
ATOM   1981 C  C   . SER A 1 256 ? 17.13029  9.63129   29.03959  1.000 19.27041 ? 256 SER A C   1 
ATOM   1982 O  O   . SER A 1 256 ? 18.22599  9.33540   29.53068  1.000 19.94167 ? 256 SER A O   1 
ATOM   1983 C  CB  . SER A 1 256 ? 17.08861  10.08455  26.58350  1.000 20.71919 ? 256 SER A CB  1 
ATOM   1984 O  OG  . SER A 1 256 ? 17.00533  9.49098   25.29591  1.000 19.90862 ? 256 SER A OG  1 
ATOM   1985 N  N   . VAL A 1 257 ? 16.27867  10.46013  29.64621  1.000 19.24349 ? 257 VAL A N   1 
ATOM   1986 C  CA  . VAL A 1 257 ? 16.60201  10.99422  30.96685  1.000 20.59381 ? 257 VAL A CA  1 
ATOM   1987 C  C   . VAL A 1 257 ? 16.69434  9.86258   31.98260  1.000 22.53571 ? 257 VAL A C   1 
ATOM   1988 O  O   . VAL A 1 257 ? 17.66090  9.77292   32.75202  1.000 22.54131 ? 257 VAL A O   1 
ATOM   1989 C  CB  . VAL A 1 257 ? 15.57374  12.06135  31.38878  1.000 20.91782 ? 257 VAL A CB  1 
ATOM   1990 C  CG1 . VAL A 1 257 ? 15.75641  12.42223  32.86134  1.000 21.44896 ? 257 VAL A CG1 1 
ATOM   1991 C  CG2 . VAL A 1 257 ? 15.73075  13.31298  30.53565  1.000 23.07166 ? 257 VAL A CG2 1 
ATOM   1992 N  N   . ILE A 1 258 ? 15.68930  8.98131   32.00429  1.000 22.46693 ? 258 ILE A N   1 
ATOM   1993 C  CA  . ILE A 1 258 ? 15.72351  7.84172   32.92527  1.000 22.23670 ? 258 ILE A CA  1 
ATOM   1994 C  C   . ILE A 1 258 ? 16.98170  7.01700   32.69832  1.000 22.93354 ? 258 ILE A C   1 
ATOM   1995 O  O   . ILE A 1 258 ? 17.66115  6.59356   33.64609  1.000 23.02264 ? 258 ILE A O   1 
ATOM   1996 C  CB  . ILE A 1 258 ? 14.46171  6.97611   32.75826  1.000 22.62881 ? 258 ILE A CB  1 
ATOM   1997 C  CG1 . ILE A 1 258 ? 13.21042  7.76012   33.14715  1.000 22.83421 ? 258 ILE A CG1 1 
ATOM   1998 C  CG2 . ILE A 1 258 ? 14.58451  5.68603   33.57436  1.000 25.47995 ? 258 ILE A CG2 1 
ATOM   1999 C  CD1 . ILE A 1 258 ? 11.92286  7.16269   32.59362  1.000 22.61637 ? 258 ILE A CD1 1 
ATOM   2000 N  N   . THR A 1 259 ? 17.29634  6.75602   31.43436  1.000 21.68077 ? 259 THR A N   1 
ATOM   2001 C  CA  . THR A 1 259 ? 18.42317  5.89284   31.11982  1.000 21.37778 ? 259 THR A CA  1 
ATOM   2002 C  C   . THR A 1 259 ? 19.74157  6.53907   31.51176  1.000 21.38162 ? 259 THR A C   1 
ATOM   2003 O  O   . THR A 1 259 ? 20.60778  5.88030   32.09791  1.000 22.58418 ? 259 THR A O   1 
ATOM   2004 C  CB  . THR A 1 259 ? 18.39996  5.55476   29.63014  1.000 20.33375 ? 259 THR A CB  1 
ATOM   2005 O  OG1 . THR A 1 259 ? 17.14470  4.94221   29.32209  1.000 19.21981 ? 259 THR A OG1 1 
ATOM   2006 C  CG2 . THR A 1 259 ? 19.53307  4.60771   29.26603  1.000 20.95979 ? 259 THR A CG2 1 
ATOM   2007 N  N   . LEU A 1 260 ? 19.91289  7.82917   31.20343  1.000 20.16844 ? 260 LEU A N   1 
ATOM   2008 C  CA  . LEU A 1 260 ? 21.17756  8.48735   31.51243  1.000 22.11857 ? 260 LEU A CA  1 
ATOM   2009 C  C   . LEU A 1 260 ? 21.39500  8.58963   33.01586  1.000 22.40715 ? 260 LEU A C   1 
ATOM   2010 O  O   . LEU A 1 260 ? 22.52229  8.42326   33.49993  1.000 23.62993 ? 260 LEU A O   1 
ATOM   2011 C  CB  . LEU A 1 260 ? 21.22550  9.86925   30.86495  1.000 21.81381 ? 260 LEU A CB  1 
ATOM   2012 C  CG  . LEU A 1 260 ? 21.40980  9.78730   29.34754  1.000 21.16477 ? 260 LEU A CG  1 
ATOM   2013 C  CD1 . LEU A 1 260 ? 21.08494  11.12926  28.68415  1.000 22.86658 ? 260 LEU A CD1 1 
ATOM   2014 C  CD2 . LEU A 1 260 ? 22.83787  9.35311   29.01872  1.000 24.09347 ? 260 LEU A CD2 1 
ATOM   2015 N  N   . LEU A 1 261 ? 20.32961  8.84755   33.77304  1.000 23.05421 ? 261 LEU A N   1 
ATOM   2016 C  CA  . LEU A 1 261 ? 20.48794  8.93108   35.22355  1.000 22.47693 ? 261 LEU A CA  1 
ATOM   2017 C  C   . LEU A 1 261 ? 20.82040  7.57837   35.84653  1.000 24.15311 ? 261 LEU A C   1 
ATOM   2018 O  O   . LEU A 1 261 ? 21.42776  7.54056   36.92616  1.000 25.99873 ? 261 LEU A O   1 
ATOM   2019 C  CB  . LEU A 1 261 ? 19.23098  9.52465   35.86032  1.000 24.44030 ? 261 LEU A CB  1 
ATOM   2020 C  CG  . LEU A 1 261 ? 18.96367  10.97925  35.47758  1.000 27.77004 ? 261 LEU A CG  1 
ATOM   2021 C  CD1 . LEU A 1 261 ? 17.61385  11.45367  36.00714  1.000 29.93537 ? 261 LEU A CD1 1 
ATOM   2022 C  CD2 . LEU A 1 261 ? 20.09699  11.87100  35.98745  1.000 26.71895 ? 261 LEU A CD2 1 
ATOM   2023 N  N   . ASP A 1 262 ? 20.45613  6.47240   35.18866  1.000 24.26232 ? 262 ASP A N   1 
ATOM   2024 C  CA  . ASP A 1 262 ? 20.86474  5.14285   35.62919  1.000 23.66832 ? 262 ASP A CA  1 
ATOM   2025 C  C   . ASP A 1 262 ? 22.26692  4.76836   35.16885  1.000 23.49960 ? 262 ASP A C   1 
ATOM   2026 O  O   . ASP A 1 262 ? 22.77439  3.71754   35.57489  1.000 27.97342 ? 262 ASP A O   1 
ATOM   2027 C  CB  . ASP A 1 262 ? 19.88590  4.08194   35.11984  1.000 26.10274 ? 262 ASP A CB  1 
ATOM   2028 C  CG  . ASP A 1 262 ? 18.82452  3.71082   36.14612  1.000 30.19921 ? 262 ASP A CG  1 
ATOM   2029 O  OD1 . ASP A 1 262 ? 18.62428  4.45224   37.14315  1.000 27.32760 ? 262 ASP A OD1 1 
ATOM   2030 O  OD2 . ASP A 1 262 ? 18.18621  2.65770   35.94590  1.000 31.20814 ? 262 ASP A OD2 1 
ATOM   2031 N  N   . HIS A 1 263 ? 22.90129  5.58843   34.33713  1.000 23.87779 ? 263 HIS A N   1 
ATOM   2032 C  CA  . HIS A 1 263 ? 24.27348  5.36078   33.88392  1.000 24.76660 ? 263 HIS A CA  1 
ATOM   2033 C  C   . HIS A 1 263 ? 25.07952  6.62705   34.14198  1.000 25.66922 ? 263 HIS A C   1 
ATOM   2034 O  O   . HIS A 1 263 ? 25.52975  7.29768   33.20720  1.000 26.02160 ? 263 HIS A O   1 
ATOM   2035 C  CB  . HIS A 1 263 ? 24.30000  4.97030   32.40525  1.000 23.64501 ? 263 HIS A CB  1 
ATOM   2036 C  CG  . HIS A 1 263 ? 23.56273  3.70004   32.10282  1.000 24.45042 ? 263 HIS A CG  1 
ATOM   2037 N  ND1 . HIS A 1 263 ? 22.18928  3.64331   31.99773  1.000 24.08569 ? 263 HIS A ND1 1 
ATOM   2038 C  CD2 . HIS A 1 263 ? 24.00909  2.43921   31.88037  1.000 25.52391 ? 263 HIS A CD2 1 
ATOM   2039 C  CE1 . HIS A 1 263 ? 21.82177  2.40380   31.71906  1.000 25.71680 ? 263 HIS A CE1 1 
ATOM   2040 N  NE2 . HIS A 1 263 ? 22.90644  1.65339   31.64664  1.000 26.39143 ? 263 HIS A NE2 1 
ATOM   2041 N  N   . PRO A 1 264 ? 25.29040  6.97830   35.41548  1.000 26.78214 ? 264 PRO A N   1 
ATOM   2042 C  CA  . PRO A 1 264 ? 25.85204  8.30441   35.72155  1.000 27.78266 ? 264 PRO A CA  1 
ATOM   2043 C  C   . PRO A 1 264 ? 27.26375  8.52907   35.20085  1.000 29.29003 ? 264 PRO A C   1 
ATOM   2044 O  O   . PRO A 1 264 ? 27.60606  9.67197   34.87242  1.000 30.87657 ? 264 PRO A O   1 
ATOM   2045 C  CB  . PRO A 1 264 ? 25.79785  8.36321   37.25717  1.000 30.04339 ? 264 PRO A CB  1 
ATOM   2046 C  CG  . PRO A 1 264 ? 25.69894  6.93793   37.70818  1.000 29.75761 ? 264 PRO A CG  1 
ATOM   2047 C  CD  . PRO A 1 264 ? 24.94664  6.21755   36.62679  1.000 26.44222 ? 264 PRO A CD  1 
ATOM   2048 N  N   . GLU A 1 265 ? 28.09954  7.49180   35.11759  1.000 31.52975 ? 265 GLU A N   1 
ATOM   2049 C  CA  . GLU A 1 265 ? 29.43563  7.67768   34.55763  1.000 33.99230 ? 265 GLU A CA  1 
ATOM   2050 C  C   . GLU A 1 265 ? 29.35935  8.19099   33.12495  1.000 32.37269 ? 265 GLU A C   1 
ATOM   2051 O  O   . GLU A 1 265 ? 30.06147  9.13850   32.74921  1.000 32.13149 ? 265 GLU A O   1 
ATOM   2052 C  CB  . GLU A 1 265 ? 30.22205  6.36843   34.60361  1.000 38.71336 ? 265 GLU A CB  1 
ATOM   2053 C  CG  . GLU A 1 265 ? 30.73565  5.97423   35.96095  1.000 49.53065 ? 265 GLU A CG  1 
ATOM   2054 C  CD  . GLU A 1 265 ? 31.85847  4.96454   35.85002  1.000 58.12036 ? 265 GLU A CD  1 
ATOM   2055 O  OE1 . GLU A 1 265 ? 32.71663  5.13705   34.95429  1.000 59.87455 ? 265 GLU A OE1 1 
ATOM   2056 O  OE2 . GLU A 1 265 ? 31.87249  3.99411   36.63753  1.000 62.14929 ? 265 GLU A OE2 1 
ATOM   2057 N  N   . GLN A 1 266 ? 28.50272  7.57502   32.30859  1.000 29.52797 ? 266 GLN A N   1 
ATOM   2058 C  CA  . GLN A 1 266 ? 28.37553  8.00266   30.92005  1.000 27.96004 ? 266 GLN A CA  1 
ATOM   2059 C  C   . GLN A 1 266 ? 27.70852  9.36546   30.80825  1.000 26.47917 ? 266 GLN A C   1 
ATOM   2060 O  O   . GLN A 1 266 ? 28.08074  10.17149  29.94693  1.000 26.88149 ? 266 GLN A O   1 
ATOM   2061 C  CB  . GLN A 1 266 ? 27.59971  6.96122   30.12448  1.000 27.53734 ? 266 GLN A CB  1 
ATOM   2062 C  CG  . GLN A 1 266 ? 28.31962  5.63487   30.06817  1.000 28.59128 ? 266 GLN A CG  1 
ATOM   2063 C  CD  . GLN A 1 266 ? 27.64041  4.65097   29.16245  1.000 28.52145 ? 266 GLN A CD  1 
ATOM   2064 O  OE1 . GLN A 1 266 ? 27.42234  4.92336   27.97764  1.000 28.61940 ? 266 GLN A OE1 1 
ATOM   2065 N  NE2 . GLN A 1 266 ? 27.29092  3.49546   29.70931  1.000 27.18545 ? 266 GLN A NE2 1 
ATOM   2066 N  N   . TYR A 1 267 ? 26.70725  9.63833   31.64734  1.000 26.06298 ? 267 TYR A N   1 
ATOM   2067 C  CA  . TYR A 1 267 ? 26.10398  10.97036  31.63592  1.000 25.74879 ? 267 TYR A CA  1 
ATOM   2068 C  C   . TYR A 1 267 ? 27.13430  12.03576  31.99022  1.000 28.54397 ? 267 TYR A C   1 
ATOM   2069 O  O   . TYR A 1 267 ? 27.17827  13.10245  31.36210  1.000 28.58611 ? 267 TYR A O   1 
ATOM   2070 C  CB  . TYR A 1 267 ? 24.91802  11.03212  32.60127  1.000 25.79682 ? 267 TYR A CB  1 
ATOM   2071 C  CG  . TYR A 1 267 ? 23.96128  12.17650  32.32650  1.000 24.87098 ? 267 TYR A CG  1 
ATOM   2072 C  CD1 . TYR A 1 267 ? 23.86875  12.74710  31.05883  1.000 28.26212 ? 267 TYR A CD1 1 
ATOM   2073 C  CD2 . TYR A 1 267 ? 23.14374  12.68061  33.32984  1.000 29.94857 ? 267 TYR A CD2 1 
ATOM   2074 C  CE1 . TYR A 1 267 ? 22.98949  13.79334  30.80386  1.000 29.31904 ? 267 TYR A CE1 1 
ATOM   2075 C  CE2 . TYR A 1 267 ? 22.26380  13.73724  33.08309  1.000 30.63835 ? 267 TYR A CE2 1 
ATOM   2076 C  CZ  . TYR A 1 267 ? 22.19398  14.28369  31.81842  1.000 29.04380 ? 267 TYR A CZ  1 
ATOM   2077 O  OH  . TYR A 1 267 ? 21.33090  15.32201  31.55172  1.000 32.75796 ? 267 TYR A OH  1 
ATOM   2078 N  N   . ALA A 1 268 ? 27.97674  11.75985  32.99206  1.000 29.08729 ? 268 ALA A N   1 
ATOM   2079 C  CA  . ALA A 1 268 ? 29.01224  12.71405  33.37808  1.000 30.36219 ? 268 ALA A CA  1 
ATOM   2080 C  C   . ALA A 1 268 ? 30.02895  12.90741  32.26103  1.000 30.92479 ? 268 ALA A C   1 
ATOM   2081 O  O   . ALA A 1 268 ? 30.49877  14.02797  32.02516  1.000 32.10027 ? 268 ALA A O   1 
ATOM   2082 C  CB  . ALA A 1 268 ? 29.70454  12.25061  34.66300  1.000 31.45596 ? 268 ALA A CB  1 
ATOM   2083 N  N   . ALA A 1 269 ? 30.38408  11.82609  31.56020  1.000 28.45181 ? 269 ALA A N   1 
ATOM   2084 C  CA  . ALA A 1 269 ? 31.29169  11.96050  30.42726  1.000 30.19618 ? 269 ALA A CA  1 
ATOM   2085 C  C   . ALA A 1 269 ? 30.65283  12.79339  29.32734  1.000 30.79268 ? 269 ALA A C   1 
ATOM   2086 O  O   . ALA A 1 269 ? 31.32154  13.60670  28.67793  1.000 32.33154 ? 269 ALA A O   1 
ATOM   2087 C  CB  . ALA A 1 269 ? 31.68340  10.58255  29.89411  1.000 29.28291 ? 269 ALA A CB  1 
ATOM   2088 N  N   . LEU A 1 270 ? 29.35256  12.60199  29.10883  1.000 29.16966 ? 270 LEU A N   1 
ATOM   2089 C  CA  . LEU A 1 270 ? 28.64424  13.37865  28.09916  1.000 28.69673 ? 270 LEU A CA  1 
ATOM   2090 C  C   . LEU A 1 270 ? 28.66646  14.86600  28.43987  1.000 31.99142 ? 270 LEU A C   1 
ATOM   2091 O  O   . LEU A 1 270 ? 28.87858  15.71103  27.56225  1.000 35.35529 ? 270 LEU A O   1 
ATOM   2092 C  CB  . LEU A 1 270 ? 27.20889  12.86208  27.97479  1.000 29.25940 ? 270 LEU A CB  1 
ATOM   2093 C  CG  . LEU A 1 270 ? 26.33353  13.33962  26.81537  1.000 26.93508 ? 270 LEU A CG  1 
ATOM   2094 C  CD1 . LEU A 1 270 ? 26.98060  13.01654  25.47404  1.000 27.74333 ? 270 LEU A CD1 1 
ATOM   2095 C  CD2 . LEU A 1 270 ? 24.94069  12.72091  26.91204  1.000 27.85485 ? 270 LEU A CD2 1 
ATOM   2096 N  N   . ARG A 1 271 ? 28.46521  15.20723  29.71306  1.000 29.11608 ? 271 ARG A N   1 
ATOM   2097 C  CA  A ARG A 1 271 ? 28.46193  16.61701  30.08519  0.480 31.32892 ? 271 ARG A CA  1 
ATOM   2098 C  CA  B ARG A 1 271 ? 28.46736  16.61210  30.10654  0.520 30.96483 ? 271 ARG A CA  1 
ATOM   2099 C  C   . ARG A 1 271 ? 29.83592  17.24911  29.90613  1.000 31.41857 ? 271 ARG A C   1 
ATOM   2100 O  O   . ARG A 1 271 ? 29.92800  18.42076  29.52118  1.000 33.06515 ? 271 ARG A O   1 
ATOM   2101 C  CB  A ARG A 1 271 ? 27.98741  16.79656  31.52498  0.480 33.84229 ? 271 ARG A CB  1 
ATOM   2102 C  CB  B ARG A 1 271 ? 28.01700  16.74748  31.56204  0.520 32.97653 ? 271 ARG A CB  1 
ATOM   2103 C  CG  A ARG A 1 271 ? 27.52386  18.21579  31.79655  0.480 37.76218 ? 271 ARG A CG  1 
ATOM   2104 C  CG  B ARG A 1 271 ? 27.88774  18.18533  32.03962  0.520 36.57675 ? 271 ARG A CG  1 
ATOM   2105 C  CD  A ARG A 1 271 ? 27.52150  18.55911  33.27122  0.480 39.24117 ? 271 ARG A CD  1 
ATOM   2106 C  CD  B ARG A 1 271 ? 26.80796  18.31293  33.10346  0.520 38.26718 ? 271 ARG A CD  1 
ATOM   2107 N  NE  A ARG A 1 271 ? 26.81022  19.80683  33.52857  0.480 38.38814 ? 271 ARG A NE  1 
ATOM   2108 N  NE  B ARG A 1 271 ? 27.27334  17.91987  34.42974  0.520 40.37457 ? 271 ARG A NE  1 
ATOM   2109 C  CZ  A ARG A 1 271 ? 27.25974  21.01282  33.20497  0.480 38.15205 ? 271 ARG A CZ  1 
ATOM   2110 C  CZ  B ARG A 1 271 ? 27.61998  18.77361  35.38432  0.520 40.21163 ? 271 ARG A CZ  1 
ATOM   2111 N  NH1 A ARG A 1 271 ? 28.41771  21.17830  32.58484  0.480 38.85985 ? 271 ARG A NH1 1 
ATOM   2112 N  NH1 B ARG A 1 271 ? 27.57865  20.08136  35.19007  0.520 41.69287 ? 271 ARG A NH1 1 
ATOM   2113 N  NH2 A ARG A 1 271 ? 26.52426  22.08010  33.50192  0.480 35.43851 ? 271 ARG A NH2 1 
ATOM   2114 N  NH2 B ARG A 1 271 ? 28.00897  18.30431  36.56601  0.520 38.48415 ? 271 ARG A NH2 1 
ATOM   2115 N  N   . ALA A 1 272 ? 30.90293  16.49696  30.15959  1.000 31.38779 ? 272 ALA A N   1 
ATOM   2116 C  CA  . ALA A 1 272 ? 32.26106  17.01425  30.06214  1.000 31.84530 ? 272 ALA A CA  1 
ATOM   2117 C  C   . ALA A 1 272 ? 32.75917  17.14813  28.62784  1.000 33.77207 ? 272 ALA A C   1 
ATOM   2118 O  O   . ALA A 1 272 ? 33.80990  17.76028  28.41235  1.000 36.39068 ? 272 ALA A O   1 
ATOM   2119 C  CB  . ALA A 1 272 ? 33.20867  16.11231  30.85138  1.000 32.18316 ? 272 ALA A CB  1 
ATOM   2120 N  N   . ASP A 1 273 ? 32.04981  16.59227  27.64394  1.000 31.59078 ? 273 ASP A N   1 
ATOM   2121 C  CA  . ASP A 1 273 ? 32.51751  16.65237  26.25489  1.000 33.86965 ? 273 ASP A CA  1 
ATOM   2122 C  C   . ASP A 1 273 ? 31.28222  16.59776  25.35502  1.000 30.54755 ? 273 ASP A C   1 
ATOM   2123 O  O   . ASP A 1 273 ? 30.82707  15.51906  24.97052  1.000 29.46854 ? 273 ASP A O   1 
ATOM   2124 C  CB  . ASP A 1 273 ? 33.49389  15.52441  25.94896  1.000 35.34280 ? 273 ASP A CB  1 
ATOM   2125 C  CG  . ASP A 1 273 ? 34.02658  15.56837  24.52127  1.000 40.02150 ? 273 ASP A CG  1 
ATOM   2126 O  OD1 . ASP A 1 273 ? 33.66115  16.48362  23.74882  1.000 39.25170 ? 273 ASP A OD1 1 
ATOM   2127 O  OD2 . ASP A 1 273 ? 34.82533  14.67417  24.17117  1.000 43.54097 ? 273 ASP A OD2 1 
ATOM   2128 N  N   . ARG A 1 274 ? 30.76403  17.77611  25.00694  1.000 29.84130 ? 274 ARG A N   1 
ATOM   2129 C  CA  . ARG A 1 274 ? 29.52519  17.83218  24.23996  1.000 25.55305 ? 274 ARG A CA  1 
ATOM   2130 C  C   . ARG A 1 274 ? 29.69473  17.34634  22.80934  1.000 25.78334 ? 274 ARG A C   1 
ATOM   2131 O  O   . ARG A 1 274 ? 28.68840  17.10504  22.13554  1.000 27.65422 ? 274 ARG A O   1 
ATOM   2132 C  CB  . ARG A 1 274 ? 28.96800  19.25544  24.24700  1.000 25.64230 ? 274 ARG A CB  1 
ATOM   2133 C  CG  . ARG A 1 274 ? 28.83150  19.83577  25.64807  1.000 29.33526 ? 274 ARG A CG  1 
ATOM   2134 C  CD  . ARG A 1 274 ? 28.01014  18.92548  26.56304  1.000 27.92535 ? 274 ARG A CD  1 
ATOM   2135 N  NE  . ARG A 1 274 ? 27.82980  19.53122  27.87499  1.000 29.89405 ? 274 ARG A NE  1 
ATOM   2136 C  CZ  . ARG A 1 274 ? 26.85888  20.38210  28.17398  1.000 28.75360 ? 274 ARG A CZ  1 
ATOM   2137 N  NH1 . ARG A 1 274 ? 25.92335  20.70161  27.29199  1.000 29.52600 ? 274 ARG A NH1 1 
ATOM   2138 N  NH2 . ARG A 1 274 ? 26.83494  20.94106  29.38034  1.000 30.48710 ? 274 ARG A NH2 1 
ATOM   2139 N  N   . SER A 1 275 ? 30.92905  17.18743  22.32673  1.000 25.58795 ? 275 SER A N   1 
ATOM   2140 C  CA  . SER A 1 275 ? 31.09421  16.59432  21.00517  1.000 26.56420 ? 275 SER A CA  1 
ATOM   2141 C  C   . SER A 1 275 ? 30.61448  15.14910  20.98326  1.000 27.60095 ? 275 SER A C   1 
ATOM   2142 O  O   . SER A 1 275 ? 30.40395  14.58820  19.90272  1.000 29.44458 ? 275 SER A O   1 
ATOM   2143 C  CB  . SER A 1 275 ? 32.55678  16.68406  20.55359  1.000 28.01225 ? 275 SER A CB  1 
ATOM   2144 O  OG  . SER A 1 275 ? 33.36799  15.76155  21.25375  1.000 32.45878 ? 275 SER A OG  1 
ATOM   2145 N  N   . LEU A 1 276 ? 30.41649  14.54593  22.15451  1.000 27.01039 ? 276 LEU A N   1 
ATOM   2146 C  CA  . LEU A 1 276 ? 29.86200  13.20229  22.27038  1.000 24.25927 ? 276 LEU A CA  1 
ATOM   2147 C  C   . LEU A 1 276 ? 28.34806  13.14738  22.08869  1.000 22.50499 ? 276 LEU A C   1 
ATOM   2148 O  O   . LEU A 1 276 ? 27.80098  12.04306  21.96931  1.000 24.00586 ? 276 LEU A O   1 
ATOM   2149 C  CB  . LEU A 1 276 ? 30.21328  12.61329  23.63735  1.000 26.53158 ? 276 LEU A CB  1 
ATOM   2150 C  CG  . LEU A 1 276 ? 31.69646  12.47472  23.95842  1.000 30.15744 ? 276 LEU A CG  1 
ATOM   2151 C  CD1 . LEU A 1 276 ? 31.88800  11.93774  25.37187  1.000 31.71013 ? 276 LEU A CD1 1 
ATOM   2152 C  CD2 . LEU A 1 276 ? 32.38126  11.57451  22.95039  1.000 33.72980 ? 276 LEU A CD2 1 
ATOM   2153 N  N   . VAL A 1 277 ? 27.65277  14.28990  22.08804  1.000 21.23449 ? 277 VAL A N   1 
ATOM   2154 C  CA  . VAL A 1 277 ? 26.18677  14.25534  22.11481  1.000 20.14194 ? 277 VAL A CA  1 
ATOM   2155 C  C   . VAL A 1 277 ? 25.59304  13.61370  20.86719  1.000 19.98694 ? 277 VAL A C   1 
ATOM   2156 O  O   . VAL A 1 277 ? 24.68624  12.77788  21.00671  1.000 20.08200 ? 277 VAL A O   1 
ATOM   2157 C  CB  . VAL A 1 277 ? 25.61904  15.66099  22.38605  1.000 21.19100 ? 277 VAL A CB  1 
ATOM   2158 C  CG1 . VAL A 1 277 ? 24.11104  15.63878  22.17542  1.000 23.87065 ? 277 VAL A CG1 1 
ATOM   2159 C  CG2 . VAL A 1 277 ? 25.93562  16.09404  23.80181  1.000 23.49418 ? 277 VAL A CG2 1 
ATOM   2160 N  N   . PRO A 1 278 ? 26.02166  13.94366  19.63840  1.000 21.63716 ? 278 PRO A N   1 
ATOM   2161 C  CA  . PRO A 1 278 ? 25.41033  13.25678  18.48387  1.000 20.96018 ? 278 PRO A CA  1 
ATOM   2162 C  C   . PRO A 1 278 ? 25.55775  11.74565  18.54746  1.000 23.14332 ? 278 PRO A C   1 
ATOM   2163 O  O   . PRO A 1 278 ? 24.60169  11.01790  18.24991  1.000 21.47977 ? 278 PRO A O   1 
ATOM   2164 C  CB  . PRO A 1 278 ? 26.15367  13.86100  17.27748  1.000 24.41554 ? 278 PRO A CB  1 
ATOM   2165 C  CG  . PRO A 1 278 ? 26.55584  15.22475  17.74315  1.000 25.85639 ? 278 PRO A CG  1 
ATOM   2166 C  CD  . PRO A 1 278 ? 26.93287  15.02342  19.20121  1.000 25.14429 ? 278 PRO A CD  1 
ATOM   2167 N  N   . GLY A 1 279 ? 26.72814  11.25122  18.95810  1.000 21.72202 ? 279 GLY A N   1 
ATOM   2168 C  CA  . GLY A 1 279 ? 26.91432  9.81188   19.05433  1.000 22.52312 ? 279 GLY A CA  1 
ATOM   2169 C  C   . GLY A 1 279 ? 26.09270  9.20326   20.17354  1.000 21.34240 ? 279 GLY A C   1 
ATOM   2170 O  O   . GLY A 1 279 ? 25.60337  8.07473   20.05555  1.000 21.35463 ? 279 GLY A O   1 
ATOM   2171 N  N   . ALA A 1 280 ? 25.92825  9.94041   21.27480  1.000 21.01730 ? 280 ALA A N   1 
ATOM   2172 C  CA  . ALA A 1 280 ? 25.09800  9.45427   22.37049  1.000 19.43228 ? 280 ALA A CA  1 
ATOM   2173 C  C   . ALA A 1 280 ? 23.63734  9.38028   21.95562  1.000 19.74210 ? 280 ALA A C   1 
ATOM   2174 O  O   . ALA A 1 280 ? 22.91220  8.46849   22.36557  1.000 18.94179 ? 280 ALA A O   1 
ATOM   2175 C  CB  . ALA A 1 280 ? 25.26649  10.35236  23.59628  1.000 21.23162 ? 280 ALA A CB  1 
ATOM   2176 N  N   . VAL A 1 281 ? 23.18143  10.33433  21.14880  1.000 18.25130 ? 281 VAL A N   1 
ATOM   2177 C  CA  . VAL A 1 281 ? 21.80598  10.27912  20.66265  1.000 17.89499 ? 281 VAL A CA  1 
ATOM   2178 C  C   . VAL A 1 281 ? 21.59527  9.03514   19.80473  1.000 17.55752 ? 281 VAL A C   1 
ATOM   2179 O  O   . VAL A 1 281 ? 20.57046  8.35096   19.92228  1.000 16.90985 ? 281 VAL A O   1 
ATOM   2180 C  CB  . VAL A 1 281 ? 21.45895  11.57171  19.89909  1.000 18.32497 ? 281 VAL A CB  1 
ATOM   2181 C  CG1 . VAL A 1 281 ? 20.18185  11.38989  19.07950  1.000 21.04169 ? 281 VAL A CG1 1 
ATOM   2182 C  CG2 . VAL A 1 281 ? 21.28721  12.72710  20.87316  1.000 19.30917 ? 281 VAL A CG2 1 
ATOM   2183 N  N   . GLU A 1 282 ? 22.56087  8.71180   18.93787  1.000 18.30860 ? 282 GLU A N   1 
ATOM   2184 C  CA  . GLU A 1 282 ? 22.41957  7.50184   18.12597  1.000 17.97709 ? 282 GLU A CA  1 
ATOM   2185 C  C   . GLU A 1 282 ? 22.38347  6.25541   18.99842  1.000 17.66129 ? 282 GLU A C   1 
ATOM   2186 O  O   . GLU A 1 282 ? 21.59879  5.33695   18.74879  1.000 17.38342 ? 282 GLU A O   1 
ATOM   2187 C  CB  . GLU A 1 282 ? 23.55616  7.38309   17.11664  1.000 18.32300 ? 282 GLU A CB  1 
ATOM   2188 C  CG  . GLU A 1 282 ? 23.52437  8.42084   16.02165  1.000 20.91518 ? 282 GLU A CG  1 
ATOM   2189 C  CD  . GLU A 1 282 ? 22.17585  8.49574   15.33587  1.000 22.00246 ? 282 GLU A CD  1 
ATOM   2190 O  OE1 . GLU A 1 282 ? 21.75203  7.49747   14.70711  1.000 22.69191 ? 282 GLU A OE1 1 
ATOM   2191 O  OE2 . GLU A 1 282 ? 21.53013  9.55377   15.44221  1.000 22.35543 ? 282 GLU A OE2 1 
ATOM   2192 N  N   . GLU A 1 283 ? 23.22557  6.20818   20.02674  1.000 17.48357 ? 283 GLU A N   1 
ATOM   2193 C  CA  . GLU A 1 283 ? 23.19664  5.05079   20.91051  1.000 17.68442 ? 283 GLU A CA  1 
ATOM   2194 C  C   . GLU A 1 283 ? 21.87357  4.96847   21.66694  1.000 17.78924 ? 283 GLU A C   1 
ATOM   2195 O  O   . GLU A 1 283 ? 21.31988  3.87336   21.82652  1.000 20.94281 ? 283 GLU A O   1 
ATOM   2196 C  CB  . GLU A 1 283 ? 24.39468  5.07688   21.86297  1.000 19.78574 ? 283 GLU A CB  1 
ATOM   2197 C  CG  . GLU A 1 283 ? 24.37431  4.00051   22.96539  1.000 19.33590 ? 283 GLU A CG  1 
ATOM   2198 C  CD  . GLU A 1 283 ? 24.52165  2.57422   22.45860  1.000 21.97042 ? 283 GLU A CD  1 
ATOM   2199 O  OE1 . GLU A 1 283 ? 24.31924  2.30621   21.24851  1.000 25.64599 ? 283 GLU A OE1 1 
ATOM   2200 O  OE2 . GLU A 1 283 ? 24.87332  1.70342   23.28341  1.000 21.48143 ? 283 GLU A OE2 1 
ATOM   2201 N  N   . LEU A 1 284 ? 21.33886  6.10970   22.12323  1.000 17.17780 ? 284 LEU A N   1 
ATOM   2202 C  CA  . LEU A 1 284 ? 20.05571  6.07788   22.81976  1.000 15.96536 ? 284 LEU A CA  1 
ATOM   2203 C  C   . LEU A 1 284 ? 18.93277  5.62592   21.89050  1.000 18.19092 ? 284 LEU A C   1 
ATOM   2204 O  O   . LEU A 1 284 ? 18.03588  4.88499   22.31537  1.000 17.67049 ? 284 LEU A O   1 
ATOM   2205 C  CB  . LEU A 1 284 ? 19.74099  7.44338   23.43076  1.000 17.27510 ? 284 LEU A CB  1 
ATOM   2206 C  CG  . LEU A 1 284 ? 20.57959  7.74966   24.67783  1.000 18.72150 ? 284 LEU A CG  1 
ATOM   2207 C  CD1 . LEU A 1 284 ? 20.59699  9.25841   24.96150  1.000 19.58334 ? 284 LEU A CD1 1 
ATOM   2208 C  CD2 . LEU A 1 284 ? 20.08870  6.96449   25.91793  1.000 20.60758 ? 284 LEU A CD2 1 
ATOM   2209 N  N   . LEU A 1 285 ? 18.95718  6.07620   20.62859  1.000 16.88780 ? 285 LEU A N   1 
ATOM   2210 C  CA  . LEU A 1 285 ? 17.97933  5.61183   19.64791  1.000 14.08897 ? 285 LEU A CA  1 
ATOM   2211 C  C   . LEU A 1 285 ? 18.05261  4.09456   19.47003  1.000 14.39340 ? 285 LEU A C   1 
ATOM   2212 O  O   . LEU A 1 285 ? 17.02595  3.40443   19.48527  1.000 16.73837 ? 285 LEU A O   1 
ATOM   2213 C  CB  . LEU A 1 285 ? 18.21341  6.32134   18.30785  1.000 14.93901 ? 285 LEU A CB  1 
ATOM   2214 C  CG  . LEU A 1 285 ? 17.77215  7.79493   18.29199  1.000 14.69826 ? 285 LEU A CG  1 
ATOM   2215 C  CD1 . LEU A 1 285 ? 18.41784  8.59604   17.15504  1.000 17.14791 ? 285 LEU A CD1 1 
ATOM   2216 C  CD2 . LEU A 1 285 ? 16.24721  7.95089   18.24087  1.000 16.88987 ? 285 LEU A CD2 1 
ATOM   2217 N  N   . ARG A 1 286 ? 19.26029  3.56354   19.25873  1.000 16.28640 ? 286 ARG A N   1 
ATOM   2218 C  CA  . ARG A 1 286 ? 19.43176  2.12055   19.11041  1.000 14.23727 ? 286 ARG A CA  1 
ATOM   2219 C  C   . ARG A 1 286 ? 18.91173  1.37574   20.32999  1.000 18.37430 ? 286 ARG A C   1 
ATOM   2220 O  O   . ARG A 1 286 ? 18.17931  0.38181   20.20489  1.000 17.79273 ? 286 ARG A O   1 
ATOM   2221 C  CB  . ARG A 1 286 ? 20.90844  1.78222   18.91408  1.000 16.52691 ? 286 ARG A CB  1 
ATOM   2222 C  CG  . ARG A 1 286 ? 21.18027  0.26270   18.86149  1.000 17.40662 ? 286 ARG A CG  1 
ATOM   2223 C  CD  . ARG A 1 286 ? 22.65741  -0.09339  19.05869  1.000 17.48802 ? 286 ARG A CD  1 
ATOM   2224 N  NE  . ARG A 1 286 ? 23.08857  0.01101   20.45397  1.000 18.91075 ? 286 ARG A NE  1 
ATOM   2225 C  CZ  . ARG A 1 286 ? 23.09494  -1.00911  21.30667  1.000 20.02770 ? 286 ARG A CZ  1 
ATOM   2226 N  NH1 . ARG A 1 286 ? 22.64556  -2.20481  20.95692  1.000 21.43488 ? 286 ARG A NH1 1 
ATOM   2227 N  NH2 . ARG A 1 286 ? 23.56015  -0.82676  22.54154  1.000 21.29952 ? 286 ARG A NH2 1 
ATOM   2228 N  N   . TYR A 1 287 ? 19.30048  1.85339   21.51994  1.000 17.53360 ? 287 TYR A N   1 
ATOM   2229 C  CA  . TYR A 1 287 ? 19.10551  1.13617   22.77773  1.000 16.27733 ? 287 TYR A CA  1 
ATOM   2230 C  C   . TYR A 1 287 ? 17.65158  1.19179   23.23355  1.000 14.41549 ? 287 TYR A C   1 
ATOM   2231 O  O   . TYR A 1 287 ? 17.11972  0.21479   23.78094  1.000 18.11035 ? 287 TYR A O   1 
ATOM   2232 C  CB  . TYR A 1 287 ? 20.02710  1.75504   23.82738  1.000 16.98579 ? 287 TYR A CB  1 
ATOM   2233 C  CG  . TYR A 1 287 ? 20.33495  0.91006   25.04556  1.000 17.11149 ? 287 TYR A CG  1 
ATOM   2234 C  CD1 . TYR A 1 287 ? 20.93365  -0.33229  24.91723  1.000 20.81694 ? 287 TYR A CD1 1 
ATOM   2235 C  CD2 . TYR A 1 287 ? 20.08692  1.39405   26.33019  1.000 20.11808 ? 287 TYR A CD2 1 
ATOM   2236 C  CE1 . TYR A 1 287 ? 21.25123  -1.08740  26.03329  1.000 23.58366 ? 287 TYR A CE1 1 
ATOM   2237 C  CE2 . TYR A 1 287 ? 20.40160  0.64968   27.45081  1.000 23.27274 ? 287 TYR A CE2 1 
ATOM   2238 C  CZ  . TYR A 1 287 ? 20.97779  -0.59404  27.29990  1.000 24.96773 ? 287 TYR A CZ  1 
ATOM   2239 O  OH  . TYR A 1 287 ? 21.29567  -1.33988  28.41604  1.000 28.18051 ? 287 TYR A OH  1 
ATOM   2240 N  N   . LEU A 1 288 ? 16.99752  2.33431   23.03407  1.000 15.28076 ? 288 LEU A N   1 
ATOM   2241 C  CA  . LEU A 1 288 ? 15.63281  2.51240   23.51172  1.000 15.77197 ? 288 LEU A CA  1 
ATOM   2242 C  C   . LEU A 1 288 ? 14.58386  2.07940   22.50021  1.000 18.41113 ? 288 LEU A C   1 
ATOM   2243 O  O   . LEU A 1 288 ? 13.45892  1.76860   22.90919  1.000 19.23465 ? 288 LEU A O   1 
ATOM   2244 C  CB  . LEU A 1 288 ? 15.40950  3.97416   23.90425  1.000 19.53880 ? 288 LEU A CB  1 
ATOM   2245 C  CG  . LEU A 1 288 ? 16.21632  4.39730   25.13503  1.000 19.42684 ? 288 LEU A CG  1 
ATOM   2246 C  CD1 . LEU A 1 288 ? 16.04774  5.89158   25.39370  1.000 19.40966 ? 288 LEU A CD1 1 
ATOM   2247 C  CD2 . LEU A 1 288 ? 15.79464  3.57686   26.35452  1.000 22.23015 ? 288 LEU A CD2 1 
ATOM   2248 N  N   . ALA A 1 289 ? 14.93016  2.07251   21.20396  1.000 18.18473 ? 289 ALA A N   1 
ATOM   2249 C  CA  . ALA A 1 289 ? 14.08905  1.61570   20.09541  1.000 16.67947 ? 289 ALA A CA  1 
ATOM   2250 C  C   . ALA A 1 289 ? 12.59300  1.68972   20.38877  1.000 19.22392 ? 289 ALA A C   1 
ATOM   2251 O  O   . ALA A 1 289 ? 11.92913  0.66441   20.58968  1.000 20.85055 ? 289 ALA A O   1 
ATOM   2252 C  CB  . ALA A 1 289 ? 14.49697  0.19267   19.70528  1.000 18.34551 ? 289 ALA A CB  1 
ATOM   2253 N  N   . ILE A 1 290 ? 12.04544  2.90801   20.40340  1.000 17.50007 ? 290 ILE A N   1 
ATOM   2254 C  CA  . ILE A 1 290 ? 10.71417  3.10158   20.98072  1.000 19.21617 ? 290 ILE A CA  1 
ATOM   2255 C  C   . ILE A 1 290 ? 9.57282   2.75182   20.03800  1.000 20.73329 ? 290 ILE A C   1 
ATOM   2256 O  O   . ILE A 1 290 ? 8.41177   2.71797   20.47772  1.000 21.82091 ? 290 ILE A O   1 
ATOM   2257 C  CB  . ILE A 1 290 ? 10.54635  4.55439   21.45223  1.000 18.42621 ? 290 ILE A CB  1 
ATOM   2258 C  CG1 . ILE A 1 290 ? 10.71815  5.48804   20.25608  1.000 21.23117 ? 290 ILE A CG1 1 
ATOM   2259 C  CG2 . ILE A 1 290 ? 11.54187  4.86163   22.58309  1.000 20.66501 ? 290 ILE A CG2 1 
ATOM   2260 C  CD1 . ILE A 1 290 ? 10.15524  6.86084   20.46813  1.000 23.62127 ? 290 ILE A CD1 1 
ATOM   2261 N  N   . ALA A 1 291 ? 9.85461   2.47667   18.76037  1.000 20.34859 ? 291 ALA A N   1 
ATOM   2262 C  CA  . ALA A 1 291 ? 8.77986   2.28441   17.78612  1.000 18.67050 ? 291 ALA A CA  1 
ATOM   2263 C  C   . ALA A 1 291 ? 8.71684   0.89497   17.13814  1.000 22.83531 ? 291 ALA A C   1 
ATOM   2264 O  O   . ALA A 1 291 ? 8.64415   0.80566   15.91429  1.000 24.70729 ? 291 ALA A O   1 
ATOM   2265 C  CB  . ALA A 1 291 ? 8.89965   3.35053   16.68883  1.000 18.53594 ? 291 ALA A CB  1 
ATOM   2266 N  N   . ASP A 1 292 ? 8.70202   -0.19474  17.92346  1.000 28.45084 ? 292 ASP A N   1 
ATOM   2267 C  CA  . ASP A 1 292 ? 8.44977   -1.52048  17.33330  1.000 26.54862 ? 292 ASP A CA  1 
ATOM   2268 C  C   . ASP A 1 292 ? 7.07307   -1.61116  16.68910  1.000 27.41038 ? 292 ASP A C   1 
ATOM   2269 O  O   . ASP A 1 292 ? 6.85792   -2.42852  15.78738  1.000 29.15127 ? 292 ASP A O   1 
ATOM   2270 C  CB  . ASP A 1 292 ? 8.54209   -2.62723  18.37711  1.000 31.87234 ? 292 ASP A CB  1 
ATOM   2271 C  CG  . ASP A 1 292 ? 9.96297   -2.97798  18.74949  1.000 35.71345 ? 292 ASP A CG  1 
ATOM   2272 O  OD1 . ASP A 1 292 ? 10.85294  -2.93397  17.86985  1.000 32.63548 ? 292 ASP A OD1 1 
ATOM   2273 O  OD2 . ASP A 1 292 ? 10.17482  -3.31860  19.93464  1.000 38.07481 ? 292 ASP A OD2 1 
ATOM   2274 N  N   . ILE A 1 293 ? 6.11218   -0.80873  17.14676  1.000 29.17580 ? 293 ILE A N   1 
ATOM   2275 C  CA  . ILE A 1 293 ? 4.77786   -0.89092  16.56860  1.000 36.82270 ? 293 ILE A CA  1 
ATOM   2276 C  C   . ILE A 1 293 ? 4.76623   -0.46456  15.11205  1.000 35.94439 ? 293 ILE A C   1 
ATOM   2277 O  O   . ILE A 1 293 ? 3.74020   -0.60611  14.43488  1.000 36.50249 ? 293 ILE A O   1 
ATOM   2278 C  CB  . ILE A 1 293 ? 3.78151   -0.04728  17.38221  1.000 44.34984 ? 293 ILE A CB  1 
ATOM   2279 C  CG1 . ILE A 1 293 ? 4.22159   1.41015   17.39488  1.000 46.31948 ? 293 ILE A CG1 1 
ATOM   2280 C  CG2 . ILE A 1 293 ? 3.68563   -0.57044  18.79740  1.000 48.23962 ? 293 ILE A CG2 1 
ATOM   2281 C  CD1 . ILE A 1 293 ? 3.12212   2.32468   17.05302  1.000 49.71519 ? 293 ILE A CD1 1 
ATOM   2282 N  N   . ALA A 1 294 ? 5.90041   0.01883   14.61089  1.000 30.79872 ? 294 ALA A N   1 
ATOM   2283 C  CA  . ALA A 1 294 ? 6.03273   0.52401   13.25882  1.000 32.20545 ? 294 ALA A CA  1 
ATOM   2284 C  C   . ALA A 1 294 ? 6.63583   -0.49464  12.30564  1.000 31.36897 ? 294 ALA A C   1 
ATOM   2285 O  O   . ALA A 1 294 ? 7.04607   -0.12308  11.20326  1.000 39.20169 ? 294 ALA A O   1 
ATOM   2286 C  CB  . ALA A 1 294 ? 6.88750   1.79157   13.26775  1.000 34.66580 ? 294 ALA A CB  1 
ATOM   2287 N  N   . GLY A 1 295 ? 6.70266   -1.76733  12.69516  1.000 22.64783 ? 295 GLY A N   1 
ATOM   2288 C  CA  . GLY A 1 295 ? 7.33746   -2.77962  11.87322  1.000 22.31294 ? 295 GLY A CA  1 
ATOM   2289 C  C   . GLY A 1 295 ? 6.40935   -3.74368  11.17448  1.000 21.08266 ? 295 GLY A C   1 
ATOM   2290 O  O   . GLY A 1 295 ? 6.89463   -4.72432  10.58603  1.000 20.94767 ? 295 GLY A O   1 
ATOM   2291 N  N   . GLY A 1 296 ? 5.09732   -3.51586  11.20502  1.000 20.39092 ? 296 GLY A N   1 
ATOM   2292 C  CA  . GLY A 1 296 ? 4.15217   -4.47227  10.63774  1.000 21.31357 ? 296 GLY A CA  1 
ATOM   2293 C  C   . GLY A 1 296 ? 4.15936   -4.45878  9.11794   1.000 20.38913 ? 296 GLY A C   1 
ATOM   2294 O  O   . GLY A 1 296 ? 4.27993   -3.40917  8.48226   1.000 20.69437 ? 296 GLY A O   1 
ATOM   2295 N  N   . ARG A 1 297 ? 4.02042   -5.65831  8.54346   1.000 18.89699 ? 297 ARG A N   1 
ATOM   2296 C  CA  . ARG A 1 297 ? 4.02342   -5.88522  7.10171   1.000 18.12403 ? 297 ARG A CA  1 
ATOM   2297 C  C   . ARG A 1 297 ? 3.14417   -7.08933  6.79839   1.000 21.31336 ? 297 ARG A C   1 
ATOM   2298 O  O   . ARG A 1 297 ? 2.86990   -7.91480  7.67340   1.000 21.37267 ? 297 ARG A O   1 
ATOM   2299 C  CB  . ARG A 1 297 ? 5.43737   -6.15525  6.55922   1.000 18.13201 ? 297 ARG A CB  1 
ATOM   2300 C  CG  . ARG A 1 297 ? 6.49078   -5.05720  6.75540   1.000 18.53972 ? 297 ARG A CG  1 
ATOM   2301 C  CD  . ARG A 1 297 ? 6.19106   -3.83808  5.89731   1.000 18.28891 ? 297 ARG A CD  1 
ATOM   2302 N  NE  . ARG A 1 297 ? 7.26296   -2.84800  5.89703   1.000 19.10518 ? 297 ARG A NE  1 
ATOM   2303 C  CZ  . ARG A 1 297 ? 7.31654   -1.80474  6.71651   1.000 16.83921 ? 297 ARG A CZ  1 
ATOM   2304 N  NH1 . ARG A 1 297 ? 6.46743   -1.68039  7.72736   1.000 19.21585 ? 297 ARG A NH1 1 
ATOM   2305 N  NH2 . ARG A 1 297 ? 8.22606   -0.85241  6.50029   1.000 16.73262 ? 297 ARG A NH2 1 
ATOM   2306 N  N   . VAL A 1 298 ? 2.71748   -7.20602  5.54416   1.000 21.58361 ? 298 VAL A N   1 
ATOM   2307 C  CA  . VAL A 1 298 ? 1.97753   -8.38110  5.09379   1.000 21.34775 ? 298 VAL A CA  1 
ATOM   2308 C  C   . VAL A 1 298 ? 2.59391   -8.86156  3.78288   1.000 20.48788 ? 298 VAL A C   1 
ATOM   2309 O  O   . VAL A 1 298 ? 2.87634   -8.05628  2.89149   1.000 23.59445 ? 298 VAL A O   1 
ATOM   2310 C  CB  . VAL A 1 298 ? 0.46676   -8.08870  4.94178   1.000 23.00777 ? 298 VAL A CB  1 
ATOM   2311 C  CG1 . VAL A 1 298 ? 0.22135   -6.89644  4.00657   1.000 26.45770 ? 298 VAL A CG1 1 
ATOM   2312 C  CG2 . VAL A 1 298 ? -0.29856  -9.33979  4.47766   1.000 27.77760 ? 298 VAL A CG2 1 
ATOM   2313 N  N   . ALA A 1 299 ? 2.85350   -10.16224 3.68633   1.000 21.97127 ? 299 ALA A N   1 
ATOM   2314 C  CA  . ALA A 1 299 ? 3.45017   -10.71427 2.47886   1.000 22.59143 ? 299 ALA A CA  1 
ATOM   2315 C  C   . ALA A 1 299 ? 2.40484   -10.80731 1.37854   1.000 25.29008 ? 299 ALA A C   1 
ATOM   2316 O  O   . ALA A 1 299 ? 1.30492   -11.32859 1.59784   1.000 27.05315 ? 299 ALA A O   1 
ATOM   2317 C  CB  . ALA A 1 299 ? 4.04371   -12.09701 2.75181   1.000 26.00688 ? 299 ALA A CB  1 
ATOM   2318 N  N   . THR A 1 300 ? 2.74417   -10.29666 0.19419   1.000 24.32405 ? 300 THR A N   1 
ATOM   2319 C  CA  . THR A 1 300 ? 1.88874   -10.45199 -0.97655  1.000 24.20180 ? 300 THR A CA  1 
ATOM   2320 C  C   . THR A 1 300 ? 2.34298   -11.59036 -1.87272  1.000 26.93091 ? 300 THR A C   1 
ATOM   2321 O  O   . THR A 1 300 ? 1.65764   -11.90953 -2.84931  1.000 29.83054 ? 300 THR A O   1 
ATOM   2322 C  CB  . THR A 1 300 ? 1.83087   -9.14306  -1.77633  1.000 26.01331 ? 300 THR A CB  1 
ATOM   2323 O  OG1 . THR A 1 300 ? 3.14946   -8.77813  -2.21537  1.000 26.25457 ? 300 THR A OG1 1 
ATOM   2324 C  CG2 . THR A 1 300 ? 1.24924   -8.03358  -0.90767  1.000 28.08559 ? 300 THR A CG2 1 
ATOM   2325 N  N   . ALA A 1 301 ? 3.47585   -12.20793 -1.55174  1.000 27.39639 ? 301 ALA A N   1 
ATOM   2326 C  CA  . ALA A 1 301 ? 3.99921   -13.36101 -2.26673  1.000 28.86938 ? 301 ALA A CA  1 
ATOM   2327 C  C   . ALA A 1 301 ? 4.85056   -14.15498 -1.29066  1.000 29.47644 ? 301 ALA A C   1 
ATOM   2328 O  O   . ALA A 1 301 ? 5.26240   -13.64037 -0.24431  1.000 29.93162 ? 301 ALA A O   1 
ATOM   2329 C  CB  . ALA A 1 301 ? 4.81928   -12.94445 -3.49286  1.000 33.84949 ? 301 ALA A CB  1 
ATOM   2330 N  N   . ASP A 1 302 ? 5.10814   -15.41861 -1.63502  1.000 31.63577 ? 302 ASP A N   1 
ATOM   2331 C  CA  . ASP A 1 302 ? 5.99442   -16.23900 -0.81583  1.000 32.87152 ? 302 ASP A CA  1 
ATOM   2332 C  C   . ASP A 1 302 ? 7.39868   -15.63956 -0.79514  1.000 32.30929 ? 302 ASP A C   1 
ATOM   2333 O  O   . ASP A 1 302 ? 7.89928   -15.15344 -1.81507  1.000 32.79215 ? 302 ASP A O   1 
ATOM   2334 C  CB  . ASP A 1 302 ? 6.05044   -17.67501 -1.35109  1.000 34.15862 ? 302 ASP A CB  1 
ATOM   2335 C  CG  . ASP A 1 302 ? 4.77489   -18.46904 -1.08485  1.000 36.76085 ? 302 ASP A CG  1 
ATOM   2336 O  OD1 . ASP A 1 302 ? 3.76863   -17.88848 -0.64733  1.000 37.74343 ? 302 ASP A OD1 1 
ATOM   2337 O  OD2 . ASP A 1 302 ? 4.78407   -19.70272 -1.33946  1.000 43.20639 ? 302 ASP A OD2 1 
ATOM   2338 N  N   . ILE A 1 303 ? 8.03871   -15.67325 0.37553   1.000 28.65583 ? 303 ILE A N   1 
ATOM   2339 C  CA  . ILE A 1 303 ? 9.39227   -15.15343 0.55697   1.000 29.05784 ? 303 ILE A CA  1 
ATOM   2340 C  C   . ILE A 1 303 ? 10.21484  -16.20488 1.29181   1.000 30.80503 ? 303 ILE A C   1 
ATOM   2341 O  O   . ILE A 1 303 ? 9.86029   -16.59601 2.40868   1.000 31.82170 ? 303 ILE A O   1 
ATOM   2342 C  CB  . ILE A 1 303 ? 9.40342   -13.83294 1.34941   1.000 27.10654 ? 303 ILE A CB  1 
ATOM   2343 C  CG1 . ILE A 1 303 ? 8.43734   -12.82296 0.74033   1.000 27.59440 ? 303 ILE A CG1 1 
ATOM   2344 C  CG2 . ILE A 1 303 ? 10.81034  -13.26278 1.39764   1.000 29.15088 ? 303 ILE A CG2 1 
ATOM   2345 C  CD1 . ILE A 1 303 ? 8.19936   -11.62099 1.63242   1.000 28.40782 ? 303 ILE A CD1 1 
ATOM   2346 N  N   . GLU A 1 304 ? 11.31845  -16.64331 0.68276   1.000 34.29721 ? 304 GLU A N   1 
ATOM   2347 C  CA  . GLU A 1 304 ? 12.25148  -17.56258 1.32989   1.000 37.72679 ? 304 GLU A CA  1 
ATOM   2348 C  C   . GLU A 1 304 ? 13.25749  -16.77275 2.15593   1.000 40.38296 ? 304 GLU A C   1 
ATOM   2349 O  O   . GLU A 1 304 ? 13.89271  -15.84291 1.64576   1.000 40.40133 ? 304 GLU A O   1 
ATOM   2350 C  CB  . GLU A 1 304 ? 13.00270  -18.41458 0.30475   1.000 42.31453 ? 304 GLU A CB  1 
ATOM   2351 C  CG  . GLU A 1 304 ? 12.16874  -18.92589 -0.84373  1.000 53.24990 ? 304 GLU A CG  1 
ATOM   2352 C  CD  . GLU A 1 304 ? 12.97583  -19.79646 -1.79376  1.000 64.73335 ? 304 GLU A CD  1 
ATOM   2353 O  OE1 . GLU A 1 304 ? 12.66514  -21.00043 -1.90554  1.000 68.57059 ? 304 GLU A OE1 1 
ATOM   2354 O  OE2 . GLU A 1 304 ? 13.92770  -19.27993 -2.42002  1.000 69.86340 ? 304 GLU A OE2 1 
ATOM   2355 N  N   . VAL A 1 305 ? 13.41295  -17.15193 3.42344   1.000 40.05891 ? 305 VAL A N   1 
ATOM   2356 C  CA  . VAL A 1 305 ? 14.29599  -16.45678 4.35712   1.000 42.04400 ? 305 VAL A CA  1 
ATOM   2357 C  C   . VAL A 1 305 ? 15.14031  -17.50723 5.07186   1.000 43.05858 ? 305 VAL A C   1 
ATOM   2358 O  O   . VAL A 1 305 ? 14.68859  -18.11170 6.05029   1.000 45.91354 ? 305 VAL A O   1 
ATOM   2359 C  CB  . VAL A 1 305 ? 13.52325  -15.59945 5.36748   1.000 41.05744 ? 305 VAL A CB  1 
ATOM   2360 C  CG1 . VAL A 1 305 ? 14.48688  -14.72666 6.15728   1.000 42.32666 ? 305 VAL A CG1 1 
ATOM   2361 C  CG2 . VAL A 1 305 ? 12.47315  -14.74850 4.67366   1.000 38.92834 ? 305 VAL A CG2 1 
ATOM   2362 N  N   . GLU A 1 306 ? 16.36544  -17.71910 4.59045   1.000 43.78655 ? 306 GLU A N   1 
ATOM   2363 C  CA  . GLU A 1 306 ? 17.36519  -18.57605 5.23851   1.000 45.09719 ? 306 GLU A CA  1 
ATOM   2364 C  C   . GLU A 1 306 ? 16.77641  -19.91128 5.69646   1.000 48.74442 ? 306 GLU A C   1 
ATOM   2365 O  O   . GLU A 1 306 ? 16.97855  -20.35080 6.82937   1.000 52.75466 ? 306 GLU A O   1 
ATOM   2366 C  CB  . GLU A 1 306 ? 18.02715  -17.84805 6.41284   1.000 48.31630 ? 306 GLU A CB  1 
ATOM   2367 C  CG  . GLU A 1 306 ? 18.54036  -16.45265 6.08176   1.000 51.89831 ? 306 GLU A CG  1 
ATOM   2368 C  CD  . GLU A 1 306 ? 19.30824  -15.81763 7.22924   1.000 55.74126 ? 306 GLU A CD  1 
ATOM   2369 O  OE1 . GLU A 1 306 ? 19.96568  -16.55991 7.99163   1.000 57.19535 ? 306 GLU A OE1 1 
ATOM   2370 O  OE2 . GLU A 1 306 ? 19.25234  -14.57569 7.37030   1.000 54.90725 ? 306 GLU A OE2 1 
ATOM   2371 N  N   . GLY A 1 307 ? 16.03847  -20.56709 4.80100   1.000 47.57395 ? 307 GLY A N   1 
ATOM   2372 C  CA  . GLY A 1 307 ? 15.46223  -21.86273 5.09044   1.000 48.92649 ? 307 GLY A CA  1 
ATOM   2373 C  C   . GLY A 1 307 ? 14.03582  -21.83900 5.60179   1.000 49.50387 ? 307 GLY A C   1 
ATOM   2374 O  O   . GLY A 1 307 ? 13.37835  -22.88759 5.60788   1.000 49.63803 ? 307 GLY A O   1 
ATOM   2375 N  N   . GLN A 1 308 ? 13.54618  -20.68682 6.05196   1.000 47.42188 ? 308 GLN A N   1 
ATOM   2376 C  CA  A GLN A 1 308 ? 12.16079  -20.55095 6.46725   0.521 49.42334 ? 308 GLN A CA  1 
ATOM   2377 C  CA  B GLN A 1 308 ? 12.16720  -20.51750 6.48442   0.479 48.71026 ? 308 GLN A CA  1 
ATOM   2378 C  C   . GLN A 1 308 ? 11.36394  -19.85081 5.37411   1.000 48.00374 ? 308 GLN A C   1 
ATOM   2379 O  O   . GLN A 1 308 ? 11.90400  -19.08104 4.57638   1.000 49.11193 ? 308 GLN A O   1 
ATOM   2380 C  CB  A GLN A 1 308 ? 12.05216  -19.78077 7.78615   0.521 52.99670 ? 308 GLN A CB  1 
ATOM   2381 C  CB  B GLN A 1 308 ? 12.09637  -19.67210 7.76023   0.479 50.70423 ? 308 GLN A CB  1 
ATOM   2382 C  CG  A GLN A 1 308 ? 12.86605  -20.39841 8.92243   0.521 56.14232 ? 308 GLN A CG  1 
ATOM   2383 C  CG  B GLN A 1 308 ? 12.97457  -20.18081 8.90126   0.479 52.84559 ? 308 GLN A CG  1 
ATOM   2384 C  CD  A GLN A 1 308 ? 12.18280  -20.27543 10.27190  0.521 58.39532 ? 308 GLN A CD  1 
ATOM   2385 C  CD  B GLN A 1 308 ? 13.14440  -19.15862 10.01436  0.479 53.34137 ? 308 GLN A CD  1 
ATOM   2386 O  OE1 A GLN A 1 308 ? 12.57501  -19.46163 11.11067  0.521 58.84981 ? 308 GLN A OE1 1 
ATOM   2387 O  OE1 B GLN A 1 308 ? 13.77799  -18.11970 9.82725   0.479 51.90530 ? 308 GLN A OE1 1 
ATOM   2388 N  NE2 A GLN A 1 308 ? 11.15830  -21.09321 10.49115  0.521 58.33729 ? 308 GLN A NE2 1 
ATOM   2389 N  NE2 B GLN A 1 308 ? 12.57734  -19.45074 11.17991  0.479 54.15721 ? 308 GLN A NE2 1 
ATOM   2390 N  N   . LEU A 1 309 ? 10.06670  -20.13986 5.33243   1.000 44.41137 ? 309 LEU A N   1 
ATOM   2391 C  CA  . LEU A 1 309 ? 9.19678   -19.61839 4.28631   1.000 38.37509 ? 309 LEU A CA  1 
ATOM   2392 C  C   . LEU A 1 309 ? 8.12263   -18.73509 4.89856   1.000 35.39175 ? 309 LEU A C   1 
ATOM   2393 O  O   . LEU A 1 309 ? 7.33858   -19.19202 5.73849   1.000 35.77109 ? 309 LEU A O   1 
ATOM   2394 C  CB  . LEU A 1 309 ? 8.55190   -20.75096 3.48929   1.000 38.89537 ? 309 LEU A CB  1 
ATOM   2395 C  CG  . LEU A 1 309 ? 7.65962   -20.32104 2.31917   1.000 40.80700 ? 309 LEU A CG  1 
ATOM   2396 C  CD1 . LEU A 1 309 ? 8.46685   -19.63607 1.22865   1.000 42.25841 ? 309 LEU A CD1 1 
ATOM   2397 C  CD2 . LEU A 1 309 ? 6.90272   -21.51584 1.76040   1.000 43.81530 ? 309 LEU A CD2 1 
ATOM   2398 N  N   . ILE A 1 310 ? 8.09329   -17.47720 4.47948   1.000 30.42454 ? 310 ILE A N   1 
ATOM   2399 C  CA  . ILE A 1 310 ? 6.95050   -16.60669 4.71172   1.000 29.33736 ? 310 ILE A CA  1 
ATOM   2400 C  C   . ILE A 1 310 ? 5.98466   -16.82928 3.56163   1.000 31.18788 ? 310 ILE A C   1 
ATOM   2401 O  O   . ILE A 1 310 ? 6.34123   -16.62164 2.39722   1.000 32.33847 ? 310 ILE A O   1 
ATOM   2402 C  CB  . ILE A 1 310 ? 7.36962   -15.13344 4.79016   1.000 28.06519 ? 310 ILE A CB  1 
ATOM   2403 C  CG1 . ILE A 1 310 ? 8.36345   -14.91850 5.93024   1.000 26.60952 ? 310 ILE A CG1 1 
ATOM   2404 C  CG2 . ILE A 1 310 ? 6.13697   -14.25498 4.93816   1.000 29.02441 ? 310 ILE A CG2 1 
ATOM   2405 C  CD1 . ILE A 1 310 ? 8.99194   -13.53476 5.92771   1.000 26.96881 ? 310 ILE A CD1 1 
ATOM   2406 N  N   . ARG A 1 311 ? 4.77000   -17.25040 3.87639   1.000 31.55235 ? 311 ARG A N   1 
ATOM   2407 C  CA  . ARG A 1 311 ? 3.79248   -17.53026 2.83751   1.000 31.60115 ? 311 ARG A CA  1 
ATOM   2408 C  C   . ARG A 1 311 ? 2.98375   -16.27711 2.53044   1.000 30.63901 ? 311 ARG A C   1 
ATOM   2409 O  O   . ARG A 1 311 ? 2.80611   -15.40647 3.38594   1.000 29.88450 ? 311 ARG A O   1 
ATOM   2410 C  CB  . ARG A 1 311 ? 2.87706   -18.67848 3.26249   1.000 35.61042 ? 311 ARG A CB  1 
ATOM   2411 C  CG  . ARG A 1 311 ? 3.64339   -19.98096 3.48060   1.000 37.27570 ? 311 ARG A CG  1 
ATOM   2412 C  CD  . ARG A 1 311 ? 2.77791   -21.12734 3.98836   1.000 44.92886 ? 311 ARG A CD  1 
ATOM   2413 N  NE  . ARG A 1 311 ? 2.33410   -20.93805 5.36473   1.000 48.59771 ? 311 ARG A NE  1 
ATOM   2414 C  CZ  . ARG A 1 311 ? 1.07031   -20.76158 5.72523   1.000 49.79957 ? 311 ARG A CZ  1 
ATOM   2415 N  NH1 . ARG A 1 311 ? 0.09134   -20.76093 4.83388   1.000 55.57769 ? 311 ARG A NH1 1 
ATOM   2416 N  NH2 . ARG A 1 311 ? 0.78075   -20.58769 7.01125   1.000 42.39709 ? 311 ARG A NH2 1 
ATOM   2417 N  N   . ALA A 1 312 ? 2.51359   -16.18450 1.28619   1.000 32.18735 ? 312 ALA A N   1 
ATOM   2418 C  CA  . ALA A 1 312 ? 1.64968   -15.08148 0.89478   1.000 32.15291 ? 312 ALA A CA  1 
ATOM   2419 C  C   . ALA A 1 312 ? 0.45933   -14.98823 1.84007   1.000 30.12778 ? 312 ALA A C   1 
ATOM   2420 O  O   . ALA A 1 312 ? -0.17792  -15.99491 2.16232   1.000 31.79782 ? 312 ALA A O   1 
ATOM   2421 C  CB  . ALA A 1 312 ? 1.17416   -15.26498 -0.54907  1.000 33.14290 ? 312 ALA A CB  1 
ATOM   2422 N  N   . GLY A 1 313 ? 0.18502   -13.77589 2.31226   1.000 29.06498 ? 313 GLY A N   1 
ATOM   2423 C  CA  . GLY A 1 313 ? -0.90962  -13.55885 3.22592   1.000 27.69849 ? 313 GLY A CA  1 
ATOM   2424 C  C   . GLY A 1 313 ? -0.54621  -13.64563 4.68993   1.000 29.21887 ? 313 GLY A C   1 
ATOM   2425 O  O   . GLY A 1 313 ? -1.41142  -13.40333 5.53698   1.000 31.60476 ? 313 GLY A O   1 
ATOM   2426 N  N   . GLU A 1 314 ? 0.69486   -13.98862 5.02047   1.000 27.49179 ? 314 GLU A N   1 
ATOM   2427 C  CA  . GLU A 1 314 ? 1.12311   -14.01103 6.40976   1.000 24.31723 ? 314 GLU A CA  1 
ATOM   2428 C  C   . GLU A 1 314 ? 1.59208   -12.63818 6.86059   1.000 23.08046 ? 314 GLU A C   1 
ATOM   2429 O  O   . GLU A 1 314 ? 2.17721   -11.86699 6.08994   1.000 24.84774 ? 314 GLU A O   1 
ATOM   2430 C  CB  . GLU A 1 314 ? 2.24968   -15.01229 6.63376   1.000 26.40473 ? 314 GLU A CB  1 
ATOM   2431 C  CG  . GLU A 1 314 ? 1.78024   -16.43168 6.65716   1.000 30.90851 ? 314 GLU A CG  1 
ATOM   2432 C  CD  . GLU A 1 314 ? 2.83368   -17.34651 7.20727   1.000 34.25418 ? 314 GLU A CD  1 
ATOM   2433 O  OE1 . GLU A 1 314 ? 3.92143   -17.42565 6.59335   1.000 34.74396 ? 314 GLU A OE1 1 
ATOM   2434 O  OE2 . GLU A 1 314 ? 2.58105   -17.96271 8.26737   1.000 39.52386 ? 314 GLU A OE2 1 
ATOM   2435 N  N   . GLY A 1 315 ? 1.34284   -12.35124 8.13467   1.000 23.70023 ? 315 GLY A N   1 
ATOM   2436 C  CA  . GLY A 1 315 ? 1.79570   -11.11264 8.74138   1.000 23.96166 ? 315 GLY A CA  1 
ATOM   2437 C  C   . GLY A 1 315 ? 3.22219   -11.26165 9.24393   1.000 22.78435 ? 315 GLY A C   1 
ATOM   2438 O  O   . GLY A 1 315 ? 3.62554   -12.32788 9.70761   1.000 23.43991 ? 315 GLY A O   1 
ATOM   2439 N  N   . VAL A 1 316 ? 3.98386   -10.17691 9.12734   1.000 21.77619 ? 316 VAL A N   1 
ATOM   2440 C  CA  . VAL A 1 316 ? 5.37951   -10.13151 9.54136   1.000 20.91877 ? 316 VAL A CA  1 
ATOM   2441 C  C   . VAL A 1 316 ? 5.59043   -8.83056  10.29876  1.000 20.55420 ? 316 VAL A C   1 
ATOM   2442 O  O   . VAL A 1 316 ? 5.19089   -7.76366  9.82293   1.000 24.45245 ? 316 VAL A O   1 
ATOM   2443 C  CB  . VAL A 1 316 ? 6.34393   -10.21217 8.34210   1.000 20.14284 ? 316 VAL A CB  1 
ATOM   2444 C  CG1 . VAL A 1 316 ? 7.79099   -10.12257 8.81820   1.000 20.50495 ? 316 VAL A CG1 1 
ATOM   2445 C  CG2 . VAL A 1 316 ? 6.11210   -11.48052 7.53560   1.000 24.04041 ? 316 VAL A CG2 1 
ATOM   2446 N  N   . ILE A 1 317 ? 6.21024   -8.90354  11.47033  1.000 18.24485 ? 317 ILE A N   1 
ATOM   2447 C  CA  . ILE A 1 317 ? 6.55293   -7.69498  12.21420  1.000 17.28018 ? 317 ILE A CA  1 
ATOM   2448 C  C   . ILE A 1 317 ? 8.06458   -7.64253  12.33246  1.000 18.41597 ? 317 ILE A C   1 
ATOM   2449 O  O   . ILE A 1 317 ? 8.67578   -8.55025  12.90784  1.000 19.92903 ? 317 ILE A O   1 
ATOM   2450 C  CB  . ILE A 1 317 ? 5.89496   -7.64897  13.60409  1.000 20.44135 ? 317 ILE A CB  1 
ATOM   2451 C  CG1 . ILE A 1 317 ? 4.36724   -7.74852  13.48124  1.000 21.05497 ? 317 ILE A CG1 1 
ATOM   2452 C  CG2 . ILE A 1 317 ? 6.29168   -6.36253  14.32664  1.000 26.22204 ? 317 ILE A CG2 1 
ATOM   2453 C  CD1 . ILE A 1 317 ? 3.64150   -7.85819  14.82073  1.000 25.32222 ? 317 ILE A CD1 1 
ATOM   2454 N  N   . VAL A 1 318 ? 8.66594   -6.58620  11.79335  1.000 17.86632 ? 318 VAL A N   1 
ATOM   2455 C  CA  . VAL A 1 318 ? 10.10162  -6.37003  11.90570  1.000 17.59756 ? 318 VAL A CA  1 
ATOM   2456 C  C   . VAL A 1 318 ? 10.32714  -5.64867  13.22993  1.000 19.09229 ? 318 VAL A C   1 
ATOM   2457 O  O   . VAL A 1 318 ? 10.01205  -4.46535  13.36486  1.000 21.35146 ? 318 VAL A O   1 
ATOM   2458 C  CB  . VAL A 1 318 ? 10.65333  -5.57230  10.71475  1.000 16.30162 ? 318 VAL A CB  1 
ATOM   2459 C  CG1 . VAL A 1 318 ? 12.16540  -5.44138  10.81027  1.000 18.25624 ? 318 VAL A CG1 1 
ATOM   2460 C  CG2 . VAL A 1 318 ? 10.26818  -6.25088  9.38906   1.000 20.15235 ? 318 VAL A CG2 1 
ATOM   2461 N  N   . VAL A 1 319 ? 10.83873  -6.36900  14.22568  1.000 21.73072 ? 319 VAL A N   1 
ATOM   2462 C  CA  . VAL A 1 319 ? 10.93070  -5.83913  15.59369  1.000 19.26412 ? 319 VAL A CA  1 
ATOM   2463 C  C   . VAL A 1 319 ? 12.30408  -5.18949  15.72316  1.000 19.94168 ? 319 VAL A C   1 
ATOM   2464 O  O   . VAL A 1 319 ? 13.30040  -5.84405  16.03130  1.000 19.29966 ? 319 VAL A O   1 
ATOM   2465 C  CB  . VAL A 1 319 ? 10.70409  -6.92040  16.64594  1.000 20.32555 ? 319 VAL A CB  1 
ATOM   2466 C  CG1 . VAL A 1 319 ? 10.62626  -6.28665  18.03088  1.000 20.53715 ? 319 VAL A CG1 1 
ATOM   2467 C  CG2 . VAL A 1 319 ? 9.44111   -7.72174  16.34025  1.000 20.55039 ? 319 VAL A CG2 1 
ATOM   2468 N  N   . ASN A 1 320 ? 12.35542  -3.87265  15.50799  1.000 19.14008 ? 320 ASN A N   1 
ATOM   2469 C  CA  . ASN A 1 320 ? 13.65515  -3.22056  15.45304  1.000 17.83854 ? 320 ASN A CA  1 
ATOM   2470 C  C   . ASN A 1 320 ? 14.33477  -3.14634  16.81665  1.000 17.89494 ? 320 ASN A C   1 
ATOM   2471 O  O   . ASN A 1 320 ? 15.56146  -3.04916  16.85743  1.000 18.70696 ? 320 ASN A O   1 
ATOM   2472 C  CB  . ASN A 1 320 ? 13.54725  -1.82716  14.79799  1.000 17.93907 ? 320 ASN A CB  1 
ATOM   2473 C  CG  . ASN A 1 320 ? 12.59935  -0.88624  15.51883  1.000 17.55711 ? 320 ASN A CG  1 
ATOM   2474 O  OD1 . ASN A 1 320 ? 12.91202  -0.37879  16.59740  1.000 20.83521 ? 320 ASN A OD1 1 
ATOM   2475 N  ND2 . ASN A 1 320 ? 11.45162  -0.61408  14.90504  1.000 18.96308 ? 320 ASN A ND2 1 
ATOM   2476 N  N   . SER A 1 321 ? 13.59242  -3.21290  17.93299  1.000 19.50995 ? 321 SER A N   1 
ATOM   2477 C  CA  . SER A 1 321 ? 14.27388  -3.20976  19.22447  1.000 20.69100 ? 321 SER A CA  1 
ATOM   2478 C  C   . SER A 1 321 ? 15.12225  -4.46130  19.39488  1.000 18.70804 ? 321 SER A C   1 
ATOM   2479 O  O   . SER A 1 321 ? 16.26276  -4.38065  19.87322  1.000 19.71554 ? 321 SER A O   1 
ATOM   2480 C  CB  . SER A 1 321 ? 13.27778  -3.06271  20.37870  1.000 20.79773 ? 321 SER A CB  1 
ATOM   2481 O  OG  . SER A 1 321 ? 12.35329  -4.13070  20.42525  1.000 20.99063 ? 321 SER A OG  1 
ATOM   2482 N  N   . ILE A 1 322 ? 14.59844  -5.61769  18.97376  1.000 20.14455 ? 322 ILE A N   1 
ATOM   2483 C  CA  . ILE A 1 322 ? 15.34975  -6.86934  19.06129  1.000 20.71660 ? 322 ILE A CA  1 
ATOM   2484 C  C   . ILE A 1 322 ? 16.48830  -6.87978  18.05363  1.000 20.26802 ? 322 ILE A C   1 
ATOM   2485 O  O   . ILE A 1 322 ? 17.61381  -7.28517  18.36946  1.000 19.49705 ? 322 ILE A O   1 
ATOM   2486 C  CB  . ILE A 1 322 ? 14.40502  -8.06775  18.84880  1.000 21.28637 ? 322 ILE A CB  1 
ATOM   2487 C  CG1 . ILE A 1 322 ? 13.33706  -8.10873  19.94469  1.000 19.86693 ? 322 ILE A CG1 1 
ATOM   2488 C  CG2 . ILE A 1 322 ? 15.18440  -9.39824  18.77155  1.000 23.30590 ? 322 ILE A CG2 1 
ATOM   2489 C  CD1 . ILE A 1 322 ? 12.25851  -9.15508  19.69473  1.000 21.33262 ? 322 ILE A CD1 1 
ATOM   2490 N  N   . ALA A 1 323 ? 16.21678  -6.42996  16.82425  1.000 19.73061 ? 323 ALA A N   1 
ATOM   2491 C  CA  . ALA A 1 323 ? 17.26744  -6.37068  15.81362  1.000 17.85837 ? 323 ALA A CA  1 
ATOM   2492 C  C   . ALA A 1 323 ? 18.39090  -5.44194  16.24610  1.000 18.79364 ? 323 ALA A C   1 
ATOM   2493 O  O   . ALA A 1 323 ? 19.56052  -5.67429  15.90261  1.000 18.69417 ? 323 ALA A O   1 
ATOM   2494 C  CB  . ALA A 1 323 ? 16.67967  -5.91710  14.47325  1.000 19.53064 ? 323 ALA A CB  1 
ATOM   2495 N  N   . ASN A 1 324 ? 18.05820  -4.39565  17.01307  1.000 18.97932 ? 324 ASN A N   1 
ATOM   2496 C  CA  . ASN A 1 324 ? 19.06665  -3.47928  17.52070  1.000 19.36921 ? 324 ASN A CA  1 
ATOM   2497 C  C   . ASN A 1 324 ? 19.88841  -4.06827  18.65872  1.000 18.63885 ? 324 ASN A C   1 
ATOM   2498 O  O   . ASN A 1 324 ? 20.88755  -3.45853  19.04639  1.000 19.76180 ? 324 ASN A O   1 
ATOM   2499 C  CB  . ASN A 1 324 ? 18.41164  -2.15885  17.95787  1.000 16.01418 ? 324 ASN A CB  1 
ATOM   2500 C  CG  . ASN A 1 324 ? 18.13256  -1.23843  16.77653  1.000 16.44999 ? 324 ASN A CG  1 
ATOM   2501 O  OD1 . ASN A 1 324 ? 18.59581  -1.48895  15.66901  1.000 21.28958 ? 324 ASN A OD1 1 
ATOM   2502 N  ND2 . ASN A 1 324 ? 17.36798  -0.18723  17.00361  1.000 19.22104 ? 324 ASN A ND2 1 
ATOM   2503 N  N   . ARG A 1 325 ? 19.52072  -5.24439  19.17849  1.000 18.81169 ? 325 ARG A N   1 
ATOM   2504 C  CA  . ARG A 1 325 ? 20.31629  -5.94001  20.17974  1.000 21.94246 ? 325 ARG A CA  1 
ATOM   2505 C  C   . ARG A 1 325 ? 21.01326  -7.16510  19.58108  1.000 22.60812 ? 325 ARG A C   1 
ATOM   2506 O  O   . ARG A 1 325 ? 21.28918  -8.14133  20.28415  1.000 23.24297 ? 325 ARG A O   1 
ATOM   2507 C  CB  . ARG A 1 325 ? 19.45072  -6.34467  21.37621  1.000 23.10018 ? 325 ARG A CB  1 
ATOM   2508 C  CG  . ARG A 1 325 ? 18.65402  -5.20058  22.04259  1.000 23.39892 ? 325 ARG A CG  1 
ATOM   2509 C  CD  . ARG A 1 325 ? 19.55487  -4.09562  22.59008  1.000 24.06297 ? 325 ARG A CD  1 
ATOM   2510 N  NE  . ARG A 1 325 ? 18.82655  -3.08519  23.35866  1.000 22.66278 ? 325 ARG A NE  1 
ATOM   2511 C  CZ  . ARG A 1 325 ? 18.70757  -3.09414  24.67891  1.000 21.98101 ? 325 ARG A CZ  1 
ATOM   2512 N  NH1 . ARG A 1 325 ? 19.23174  -4.06722  25.41427  1.000 22.98406 ? 325 ARG A NH1 1 
ATOM   2513 N  NH2 . ARG A 1 325 ? 18.05072  -2.10352  25.27915  1.000 19.94573 ? 325 ARG A NH2 1 
ATOM   2514 N  N   . ASP A 1 326 ? 21.30186  -7.11904  18.27897  1.000 22.24659 ? 326 ASP A N   1 
ATOM   2515 C  CA  . ASP A 1 326 ? 21.98928  -8.19651  17.57323  1.000 22.39780 ? 326 ASP A CA  1 
ATOM   2516 C  C   . ASP A 1 326 ? 23.48442  -8.07738  17.84737  1.000 24.50488 ? 326 ASP A C   1 
ATOM   2517 O  O   . ASP A 1 326 ? 24.13488  -7.13525  17.38062  1.000 24.89179 ? 326 ASP A O   1 
ATOM   2518 C  CB  . ASP A 1 326 ? 21.67864  -8.10252  16.08034  1.000 21.81287 ? 326 ASP A CB  1 
ATOM   2519 C  CG  . ASP A 1 326 ? 22.16108  -9.31653  15.28269  1.000 23.46806 ? 326 ASP A CG  1 
ATOM   2520 O  OD1 . ASP A 1 326 ? 23.14661  -9.98480  15.68796  1.000 24.44745 ? 326 ASP A OD1 1 
ATOM   2521 O  OD2 . ASP A 1 326 ? 21.55205  -9.59034  14.22157  1.000 23.49386 ? 326 ASP A OD2 1 
ATOM   2522 N  N   . GLY A 1 327 ? 24.02869  -9.02283  18.61327  1.000 24.26147 ? 327 GLY A N   1 
ATOM   2523 C  CA  . GLY A 1 327 ? 25.43342  -8.98933  18.99855  1.000 26.69949 ? 327 GLY A CA  1 
ATOM   2524 C  C   . GLY A 1 327 ? 26.41759  -9.25050  17.87193  1.000 29.63979 ? 327 GLY A C   1 
ATOM   2525 O  O   . GLY A 1 327 ? 27.62384  -9.06624  18.07987  1.000 31.06579 ? 327 GLY A O   1 
ATOM   2526 N  N   . THR A 1 328 ? 25.94951  -9.69773  16.70328  1.000 28.83462 ? 328 THR A N   1 
ATOM   2527 C  CA  . THR A 1 328 ? 26.83463  -9.76452  15.54525  1.000 31.93317 ? 328 THR A CA  1 
ATOM   2528 C  C   . THR A 1 328 ? 27.03599  -8.40370  14.89829  1.000 29.01399 ? 328 THR A C   1 
ATOM   2529 O  O   . THR A 1 328 ? 27.86206  -8.28675  13.98293  1.000 31.75419 ? 328 THR A O   1 
ATOM   2530 C  CB  . THR A 1 328 ? 26.30323  -10.74032 14.48749  1.000 31.00145 ? 328 THR A CB  1 
ATOM   2531 O  OG1 . THR A 1 328 ? 25.12561  -10.19675 13.87470  1.000 30.98780 ? 328 THR A OG1 1 
ATOM   2532 C  CG2 . THR A 1 328 ? 25.98312  -12.08734 15.10511  1.000 31.23996 ? 328 THR A CG2 1 
ATOM   2533 N  N   . VAL A 1 329 ? 26.28948  -7.39194  15.33911  1.000 25.93226 ? 329 VAL A N   1 
ATOM   2534 C  CA  . VAL A 1 329 ? 26.43708  -6.02824  14.85739  1.000 23.58380 ? 329 VAL A CA  1 
ATOM   2535 C  C   . VAL A 1 329 ? 26.92424  -5.09469  15.95958  1.000 22.91509 ? 329 VAL A C   1 
ATOM   2536 O  O   . VAL A 1 329 ? 27.78774  -4.24669  15.71797  1.000 25.86753 ? 329 VAL A O   1 
ATOM   2537 C  CB  . VAL A 1 329 ? 25.11092  -5.51964  14.25013  1.000 24.45961 ? 329 VAL A CB  1 
ATOM   2538 C  CG1 . VAL A 1 329 ? 25.26509  -4.09463  13.73568  1.000 23.83010 ? 329 VAL A CG1 1 
ATOM   2539 C  CG2 . VAL A 1 329 ? 24.64616  -6.45119  13.13393  1.000 28.34950 ? 329 VAL A CG2 1 
ATOM   2540 N  N   . TYR A 1 330 ? 26.39367  -5.24764  17.17499  1.000 21.74330 ? 330 TYR A N   1 
ATOM   2541 C  CA  . TYR A 1 330 ? 26.71924  -4.39269  18.32339  1.000 22.53012 ? 330 TYR A CA  1 
ATOM   2542 C  C   . TYR A 1 330 ? 27.29619  -5.27497  19.41973  1.000 25.39044 ? 330 TYR A C   1 
ATOM   2543 O  O   . TYR A 1 330 ? 26.55032  -5.99024  20.09600  1.000 29.30106 ? 330 TYR A O   1 
ATOM   2544 C  CB  . TYR A 1 330 ? 25.48540  -3.63545  18.81678  1.000 20.80540 ? 330 TYR A CB  1 
ATOM   2545 C  CG  . TYR A 1 330 ? 24.85008  -2.87080  17.68929  1.000 19.11636 ? 330 TYR A CG  1 
ATOM   2546 C  CD1 . TYR A 1 330 ? 25.49205  -1.76734  17.13858  1.000 20.10204 ? 330 TYR A CD1 1 
ATOM   2547 C  CD2 . TYR A 1 330 ? 23.62574  -3.26310  17.16065  1.000 17.70000 ? 330 TYR A CD2 1 
ATOM   2548 C  CE1 . TYR A 1 330 ? 24.94420  -1.07966  16.07289  1.000 20.48054 ? 330 TYR A CE1 1 
ATOM   2549 C  CE2 . TYR A 1 330 ? 23.06699  -2.58439  16.08655  1.000 19.12316 ? 330 TYR A CE2 1 
ATOM   2550 C  CZ  . TYR A 1 330 ? 23.73264  -1.48398  15.56172  1.000 19.21905 ? 330 TYR A CZ  1 
ATOM   2551 O  OH  . TYR A 1 330 ? 23.20447  -0.79787  14.49617  1.000 21.48298 ? 330 TYR A OH  1 
ATOM   2552 N  N   . GLU A 1 331 ? 28.61731  -5.21658  19.59392  1.000 28.19457 ? 331 GLU A N   1 
ATOM   2553 C  CA  . GLU A 1 331 ? 29.27434  -6.04420  20.59467  1.000 27.23995 ? 331 GLU A CA  1 
ATOM   2554 C  C   . GLU A 1 331 ? 28.72960  -5.69868  21.97107  1.000 28.23533 ? 331 GLU A C   1 
ATOM   2555 O  O   . GLU A 1 331 ? 28.62358  -4.51769  22.32208  1.000 28.40562 ? 331 GLU A O   1 
ATOM   2556 C  CB  . GLU A 1 331 ? 30.78572  -5.83627  20.55364  1.000 33.82504 ? 331 GLU A CB  1 
ATOM   2557 C  CG  . GLU A 1 331 ? 31.53871  -6.73355  21.52671  1.000 43.71808 ? 331 GLU A CG  1 
ATOM   2558 C  CD  . GLU A 1 331 ? 33.03078  -6.47615  21.52411  1.000 51.53229 ? 331 GLU A CD  1 
ATOM   2559 O  OE1 . GLU A 1 331 ? 33.58037  -6.12218  22.59252  1.000 54.31375 ? 331 GLU A OE1 1 
ATOM   2560 O  OE2 . GLU A 1 331 ? 33.64995  -6.62627  20.45041  1.000 53.88447 ? 331 GLU A OE2 1 
ATOM   2561 N  N   . ASP A 1 332 ? 28.38109  -6.73949  22.74831  1.000 29.32097 ? 332 ASP A N   1 
ATOM   2562 C  CA  A ASP A 1 332 ? 27.72283  -6.55527  24.03808  0.715 29.06654 ? 332 ASP A CA  1 
ATOM   2563 C  CA  B ASP A 1 332 ? 27.74534  -6.52743  24.03685  0.285 28.48122 ? 332 ASP A CA  1 
ATOM   2564 C  C   . ASP A 1 332 ? 26.49803  -5.67054  23.82696  1.000 27.22213 ? 332 ASP A C   1 
ATOM   2565 O  O   . ASP A 1 332 ? 26.42745  -4.53949  24.32912  1.000 27.37012 ? 332 ASP A O   1 
ATOM   2566 C  CB  A ASP A 1 332 ? 28.69458  -5.96812  25.06204  0.715 32.73537 ? 332 ASP A CB  1 
ATOM   2567 C  CB  B ASP A 1 332 ? 28.75088  -5.87555  24.98363  0.285 29.65385 ? 332 ASP A CB  1 
ATOM   2568 C  CG  A ASP A 1 332 ? 29.90883  -6.86128  25.27993  0.715 37.26645 ? 332 ASP A CG  1 
ATOM   2569 C  CG  B ASP A 1 332 ? 28.19677  -5.62370  26.34648  0.285 32.36529 ? 332 ASP A CG  1 
ATOM   2570 O  OD1 A ASP A 1 332 ? 29.73661  -8.02924  25.70202  0.715 37.05442 ? 332 ASP A OD1 1 
ATOM   2571 O  OD1 B ASP A 1 332 ? 27.23111  -6.30194  26.75699  0.285 33.64539 ? 332 ASP A OD1 1 
ATOM   2572 O  OD2 A ASP A 1 332 ? 31.03574  -6.41011  24.99576  0.715 39.76925 ? 332 ASP A OD2 1 
ATOM   2573 O  OD2 B ASP A 1 332 ? 28.74587  -4.72201  27.00525  0.285 34.22136 ? 332 ASP A OD2 1 
ATOM   2574 N  N   . PRO A 1 333 ? 25.50337  -6.16970  23.08676  1.000 25.47802 ? 333 PRO A N   1 
ATOM   2575 C  CA  . PRO A 1 333 ? 24.40464  -5.30545  22.62688  1.000 24.99916 ? 333 PRO A CA  1 
ATOM   2576 C  C   . PRO A 1 333 ? 23.51022  -4.77887  23.72427  1.000 25.20049 ? 333 PRO A C   1 
ATOM   2577 O  O   . PRO A 1 333 ? 22.80934  -3.78972  23.49362  1.000 26.19569 ? 333 PRO A O   1 
ATOM   2578 C  CB  . PRO A 1 333 ? 23.61680  -6.22248  21.68546  1.000 24.36549 ? 333 PRO A CB  1 
ATOM   2579 C  CG  . PRO A 1 333 ? 23.90996  -7.60972  22.19210  1.000 26.68019 ? 333 PRO A CG  1 
ATOM   2580 C  CD  . PRO A 1 333 ? 25.34138  -7.56250  22.62911  1.000 25.98728 ? 333 PRO A CD  1 
ATOM   2581 N  N   . ASP A 1 334 ? 23.47676  -5.41100  24.89071  1.000 26.60617 ? 334 ASP A N   1 
ATOM   2582 C  CA  . ASP A 1 334 ? 22.58664  -4.96096  25.94964  1.000 28.84846 ? 334 ASP A CA  1 
ATOM   2583 C  C   . ASP A 1 334 ? 23.25065  -3.95730  26.87558  1.000 29.09131 ? 334 ASP A C   1 
ATOM   2584 O  O   . ASP A 1 334 ? 22.64307  -3.54869  27.87520  1.000 30.68668 ? 334 ASP A O   1 
ATOM   2585 C  CB  . ASP A 1 334 ? 22.06391  -6.15504  26.74720  1.000 30.88276 ? 334 ASP A CB  1 
ATOM   2586 C  CG  . ASP A 1 334 ? 21.19263  -7.08184  25.91267  1.000 32.39060 ? 334 ASP A CG  1 
ATOM   2587 O  OD1 . ASP A 1 334 ? 20.57072  -6.62607  24.92014  1.000 32.18657 ? 334 ASP A OD1 1 
ATOM   2588 O  OD2 . ASP A 1 334 ? 21.12180  -8.27560  26.26131  1.000 38.09761 ? 334 ASP A OD2 1 
ATOM   2589 N  N   . ALA A 1 335 ? 24.47345  -3.54574  26.56354  1.000 27.93943 ? 335 ALA A N   1 
ATOM   2590 C  CA  . ALA A 1 335 ? 25.15062  -2.50489  27.31896  1.000 29.06642 ? 335 ALA A CA  1 
ATOM   2591 C  C   . ALA A 1 335 ? 24.93049  -1.15813  26.65695  1.000 26.26897 ? 335 ALA A C   1 
ATOM   2592 O  O   . ALA A 1 335 ? 25.11013  -1.01826  25.44243  1.000 26.37947 ? 335 ALA A O   1 
ATOM   2593 C  CB  . ALA A 1 335 ? 26.64532  -2.76826  27.40103  1.000 30.66724 ? 335 ALA A CB  1 
ATOM   2594 N  N   . LEU A 1 336 ? 24.57716  -0.15915  27.45962  1.000 24.60240 ? 336 LEU A N   1 
ATOM   2595 C  CA  . LEU A 1 336 ? 24.61859  1.20787   26.96541  1.000 21.99312 ? 336 LEU A CA  1 
ATOM   2596 C  C   . LEU A 1 336 ? 26.07344  1.64642   26.83541  1.000 22.22701 ? 336 LEU A C   1 
ATOM   2597 O  O   . LEU A 1 336 ? 26.85199  1.52501   27.78399  1.000 24.72549 ? 336 LEU A O   1 
ATOM   2598 C  CB  . LEU A 1 336 ? 23.86191  2.13648   27.90997  1.000 21.55711 ? 336 LEU A CB  1 
ATOM   2599 C  CG  . LEU A 1 336 ? 23.79880  3.57812   27.42537  1.000 21.04119 ? 336 LEU A CG  1 
ATOM   2600 C  CD1 . LEU A 1 336 ? 22.80269  3.70427   26.28152  1.000 22.68060 ? 336 LEU A CD1 1 
ATOM   2601 C  CD2 . LEU A 1 336 ? 23.43276  4.50291   28.57458  1.000 23.79391 ? 336 LEU A CD2 1 
ATOM   2602 N  N   . ASP A 1 337 ? 26.45590  2.13907   25.65847  1.000 22.17213 ? 337 ASP A N   1 
ATOM   2603 C  CA  . ASP A 1 337 ? 27.81854  2.64022   25.45883  1.000 23.53524 ? 337 ASP A CA  1 
ATOM   2604 C  C   . ASP A 1 337 ? 27.74618  3.83996   24.52360  1.000 23.27337 ? 337 ASP A C   1 
ATOM   2605 O  O   . ASP A 1 337 ? 27.73107  3.67678   23.29956  1.000 24.52846 ? 337 ASP A O   1 
ATOM   2606 C  CB  . ASP A 1 337 ? 28.74585  1.57103   24.89808  1.000 25.68817 ? 337 ASP A CB  1 
ATOM   2607 C  CG  . ASP A 1 337 ? 30.17363  2.07317   24.72015  1.000 26.87995 ? 337 ASP A CG  1 
ATOM   2608 O  OD1 . ASP A 1 337 ? 30.46427  3.22232   25.11266  1.000 27.28589 ? 337 ASP A OD1 1 
ATOM   2609 O  OD2 . ASP A 1 337 ? 31.01197  1.32240   24.17948  1.000 27.98344 ? 337 ASP A OD2 1 
ATOM   2610 N  N   . ILE A 1 338 ? 27.73323  5.04447   25.09774  1.000 20.60514 ? 338 ILE A N   1 
ATOM   2611 C  CA  . ILE A 1 338 ? 27.62269  6.23929   24.26762  1.000 22.16254 ? 338 ILE A CA  1 
ATOM   2612 C  C   . ILE A 1 338 ? 28.83610  6.44311   23.37777  1.000 25.17619 ? 338 ILE A C   1 
ATOM   2613 O  O   . ILE A 1 338 ? 28.76707  7.23678   22.43046  1.000 26.71187 ? 338 ILE A O   1 
ATOM   2614 C  CB  . ILE A 1 338 ? 27.37904  7.49835   25.12266  1.000 26.32367 ? 338 ILE A CB  1 
ATOM   2615 C  CG1 . ILE A 1 338 ? 28.52635  7.72132   26.11983  1.000 28.69201 ? 338 ILE A CG1 1 
ATOM   2616 C  CG2 . ILE A 1 338 ? 26.02234  7.40657   25.81536  1.000 26.39192 ? 338 ILE A CG2 1 
ATOM   2617 C  CD1 . ILE A 1 338 ? 28.48151  9.06991   26.81209  1.000 31.94141 ? 338 ILE A CD1 1 
ATOM   2618 N  N   . HIS A 1 339 ? 29.93160  5.72760   23.63757  1.000 27.25993 ? 339 HIS A N   1 
ATOM   2619 C  CA  . HIS A 1 339 ? 31.12355  5.77563   22.80099  1.000 27.11278 ? 339 HIS A CA  1 
ATOM   2620 C  C   . HIS A 1 339 ? 31.12233  4.74090   21.68361  1.000 28.27954 ? 339 HIS A C   1 
ATOM   2621 O  O   . HIS A 1 339 ? 32.02995  4.76534   20.84525  1.000 31.79249 ? 339 HIS A O   1 
ATOM   2622 C  CB  . HIS A 1 339 ? 32.38072  5.56205   23.64835  1.000 29.18699 ? 339 HIS A CB  1 
ATOM   2623 C  CG  . HIS A 1 339 ? 32.50041  6.50564   24.80372  1.000 33.00362 ? 339 HIS A CG  1 
ATOM   2624 N  ND1 . HIS A 1 339 ? 33.07182  7.75324   24.68776  1.000 34.15611 ? 339 HIS A ND1 1 
ATOM   2625 C  CD2 . HIS A 1 339 ? 32.12817  6.38085   26.10000  1.000 35.95051 ? 339 HIS A CD2 1 
ATOM   2626 C  CE1 . HIS A 1 339 ? 33.04673  8.35727   25.86268  1.000 35.92482 ? 339 HIS A CE1 1 
ATOM   2627 N  NE2 . HIS A 1 339 ? 32.47724  7.54618   26.73597  1.000 37.41110 ? 339 HIS A NE2 1 
ATOM   2628 N  N   . ARG A 1 340 ? 30.15339  3.82880   21.64744  1.000 25.80815 ? 340 ARG A N   1 
ATOM   2629 C  CA  . ARG A 1 340 ? 30.17341  2.81611   20.59901  1.000 26.30647 ? 340 ARG A CA  1 
ATOM   2630 C  C   . ARG A 1 340 ? 29.74787  3.41724   19.26737  1.000 28.39253 ? 340 ARG A C   1 
ATOM   2631 O  O   . ARG A 1 340 ? 29.17185  4.50438   19.19923  1.000 27.62703 ? 340 ARG A O   1 
ATOM   2632 C  CB  . ARG A 1 340 ? 29.24288  1.64880   20.92519  1.000 22.84751 ? 340 ARG A CB  1 
ATOM   2633 C  CG  . ARG A 1 340 ? 27.77791  1.92882   20.62289  1.000 23.60259 ? 340 ARG A CG  1 
ATOM   2634 C  CD  . ARG A 1 340 ? 26.95786  0.64505   20.53348  1.000 23.40346 ? 340 ARG A CD  1 
ATOM   2635 N  NE  . ARG A 1 340 ? 26.81620  -0.01735  21.82960  1.000 23.55378 ? 340 ARG A NE  1 
ATOM   2636 C  CZ  . ARG A 1 340 ? 27.26864  -1.23692  22.10304  1.000 25.68542 ? 340 ARG A CZ  1 
ATOM   2637 N  NH1 . ARG A 1 340 ? 27.91294  -1.95768  21.19657  1.000 26.21727 ? 340 ARG A NH1 1 
ATOM   2638 N  NH2 . ARG A 1 340 ? 27.04994  -1.75695  23.30845  1.000 26.33927 ? 340 ARG A NH2 1 
ATOM   2639 N  N   . SER A 1 341 ? 30.02355  2.68225   18.19493  1.000 29.77459 ? 341 SER A N   1 
ATOM   2640 C  CA  . SER A 1 341 ? 29.39278  2.98117   16.91740  1.000 29.41290 ? 341 SER A CA  1 
ATOM   2641 C  C   . SER A 1 341 ? 28.00674  2.36037   16.93047  1.000 29.97984 ? 341 SER A C   1 
ATOM   2642 O  O   . SER A 1 341 ? 27.86504  1.13169   16.91901  1.000 31.35397 ? 341 SER A O   1 
ATOM   2643 C  CB  . SER A 1 341 ? 30.20687  2.44932   15.74481  1.000 34.04355 ? 341 SER A CB  1 
ATOM   2644 O  OG  . SER A 1 341 ? 29.43217  2.52890   14.56043  1.000 39.68111 ? 341 SER A OG  1 
ATOM   2645 N  N   . ALA A 1 342 ? 26.98651  3.20277   17.00279  1.000 23.53221 ? 342 ALA A N   1 
ATOM   2646 C  CA  . ALA A 1 342 ? 25.61827  2.74406   16.86441  1.000 22.72967 ? 342 ALA A CA  1 
ATOM   2647 C  C   . ALA A 1 342 ? 25.13244  2.86820   15.43340  1.000 23.37090 ? 342 ALA A C   1 
ATOM   2648 O  O   . ALA A 1 342 ? 23.92018  2.82833   15.19249  1.000 22.94256 ? 342 ALA A O   1 
ATOM   2649 C  CB  . ALA A 1 342 ? 24.70179  3.51079   17.82028  1.000 22.27122 ? 342 ALA A CB  1 
ATOM   2650 N  N   . ARG A 1 343 ? 26.05531  3.05008   14.48799  1.000 24.70580 ? 343 ARG A N   1 
ATOM   2651 C  CA  . ARG A 1 343 ? 25.68199  3.14713   13.08581  1.000 23.17519 ? 343 ARG A CA  1 
ATOM   2652 C  C   . ARG A 1 343 ? 24.87685  1.92952   12.66013  1.000 21.18136 ? 343 ARG A C   1 
ATOM   2653 O  O   . ARG A 1 343 ? 25.03908  0.82542   13.19351  1.000 23.80756 ? 343 ARG A O   1 
ATOM   2654 C  CB  . ARG A 1 343 ? 26.92108  3.25766   12.19043  1.000 28.68095 ? 343 ARG A CB  1 
ATOM   2655 C  CG  . ARG A 1 343 ? 27.82289  4.43817   12.44859  1.000 34.84626 ? 343 ARG A CG  1 
ATOM   2656 C  CD  . ARG A 1 343 ? 29.00342  4.45340   11.45405  1.000 35.58499 ? 343 ARG A CD  1 
ATOM   2657 N  NE  . ARG A 1 343 ? 28.55882  4.60936   10.07225  1.000 33.04748 ? 343 ARG A NE  1 
ATOM   2658 C  CZ  . ARG A 1 343 ? 28.02508  5.72505   9.59396   1.000 31.60671 ? 343 ARG A CZ  1 
ATOM   2659 N  NH1 . ARG A 1 343 ? 27.88470  6.80181   10.35197  1.000 32.12748 ? 343 ARG A NH1 1 
ATOM   2660 N  NH2 . ARG A 1 343 ? 27.61024  5.75981   8.32837   1.000 31.06682 ? 343 ARG A NH2 1 
ATOM   2661 N  N   . HIS A 1 344 ? 24.02238  2.14330   11.66340  1.000 21.01306 ? 344 HIS A N   1 
ATOM   2662 C  CA  . HIS A 1 344 ? 23.23421  1.11843   10.99416  1.000 20.20489 ? 344 HIS A CA  1 
ATOM   2663 C  C   . HIS A 1 344 ? 22.08548  0.61251   11.85573  1.000 20.77299 ? 344 HIS A C   1 
ATOM   2664 O  O   . HIS A 1 344 ? 21.45581  -0.39265  11.50287  1.000 20.54242 ? 344 HIS A O   1 
ATOM   2665 C  CB  . HIS A 1 344 ? 24.10501  -0.06277  10.53373  1.000 24.00725 ? 344 HIS A CB  1 
ATOM   2666 C  CG  . HIS A 1 344 ? 25.43271  0.34472   9.96567   1.000 27.00642 ? 344 HIS A CG  1 
ATOM   2667 N  ND1 . HIS A 1 344 ? 25.55567  1.22296   8.90884   1.000 30.95970 ? 344 HIS A ND1 1 
ATOM   2668 C  CD2 . HIS A 1 344 ? 26.69583  -0.00078  10.31349  1.000 29.22105 ? 344 HIS A CD2 1 
ATOM   2669 C  CE1 . HIS A 1 344 ? 26.83545  1.39542   8.62775   1.000 32.13710 ? 344 HIS A CE1 1 
ATOM   2670 N  NE2 . HIS A 1 344 ? 27.54906  0.66631   9.46737   1.000 32.31279 ? 344 HIS A NE2 1 
ATOM   2671 N  N   . HIS A 1 345 ? 21.76316  1.29400   12.95482  1.000 18.25049 ? 345 HIS A N   1 
ATOM   2672 C  CA  . HIS A 1 345 ? 20.66982  0.82528   13.78692  1.000 17.61797 ? 345 HIS A CA  1 
ATOM   2673 C  C   . HIS A 1 345 ? 19.34367  1.01210   13.05304  1.000 16.21878 ? 345 HIS A C   1 
ATOM   2674 O  O   . HIS A 1 345 ? 19.24220  1.73307   12.04233  1.000 17.67025 ? 345 HIS A O   1 
ATOM   2675 C  CB  . HIS A 1 345 ? 20.65653  1.54073   15.14692  1.000 16.87095 ? 345 HIS A CB  1 
ATOM   2676 C  CG  . HIS A 1 345 ? 20.26889  2.98455   15.06791  1.000 16.53194 ? 345 HIS A CG  1 
ATOM   2677 N  ND1 . HIS A 1 345 ? 18.96555  3.39111   14.87776  1.000 16.86986 ? 345 HIS A ND1 1 
ATOM   2678 C  CD2 . HIS A 1 345 ? 21.01035  4.11602   15.14796  1.000 18.44627 ? 345 HIS A CD2 1 
ATOM   2679 C  CE1 . HIS A 1 345 ? 18.91953  4.71181   14.83732  1.000 17.94734 ? 345 HIS A CE1 1 
ATOM   2680 N  NE2 . HIS A 1 345 ? 20.14713  5.17529   15.00285  1.000 19.94716 ? 345 HIS A NE2 1 
ATOM   2681 N  N   . LEU A 1 346 ? 18.32881  0.30883   13.54669  1.000 16.56789 ? 346 LEU A N   1 
ATOM   2682 C  CA  . LEU A 1 346 ? 17.03719  0.22564   12.88569  1.000 15.13612 ? 346 LEU A CA  1 
ATOM   2683 C  C   . LEU A 1 346 ? 15.94812  0.97962   13.63001  1.000 16.45451 ? 346 LEU A C   1 
ATOM   2684 O  O   . LEU A 1 346 ? 14.76461  0.76195   13.35834  1.000 17.49595 ? 346 LEU A O   1 
ATOM   2685 C  CB  . LEU A 1 346 ? 16.64578  -1.24370  12.71032  1.000 15.40469 ? 346 LEU A CB  1 
ATOM   2686 C  CG  . LEU A 1 346 ? 17.47011  -1.92270  11.61211  1.000 17.35620 ? 346 LEU A CG  1 
ATOM   2687 C  CD1 . LEU A 1 346 ? 17.46461  -3.42418  11.79432  1.000 20.18724 ? 346 LEU A CD1 1 
ATOM   2688 C  CD2 . LEU A 1 346 ? 16.91683  -1.54315  10.22328  1.000 20.97121 ? 346 LEU A CD2 1 
ATOM   2689 N  N   . ALA A 1 347 ? 16.31038  1.86134   14.56799  1.000 16.47464 ? 347 ALA A N   1 
ATOM   2690 C  CA  . ALA A 1 347 ? 15.26013  2.53270   15.32845  1.000 16.93657 ? 347 ALA A CA  1 
ATOM   2691 C  C   . ALA A 1 347 ? 14.34877  3.37118   14.44347  1.000 16.41789 ? 347 ALA A C   1 
ATOM   2692 O  O   . ALA A 1 347 ? 13.21004  3.63430   14.83562  1.000 17.03359 ? 347 ALA A O   1 
ATOM   2693 C  CB  . ALA A 1 347 ? 15.85126  3.42096   16.43217  1.000 18.85511 ? 347 ALA A CB  1 
ATOM   2694 N  N   . PHE A 1 348 ? 14.83698  3.81574   13.28174  1.000 17.00095 ? 348 PHE A N   1 
ATOM   2695 C  CA  . PHE A 1 348 ? 14.06002  4.57982   12.31081  1.000 15.16883 ? 348 PHE A CA  1 
ATOM   2696 C  C   . PHE A 1 348 ? 13.60644  3.73316   11.12704  1.000 16.62831 ? 348 PHE A C   1 
ATOM   2697 O  O   . PHE A 1 348 ? 13.12164  4.28601   10.12816  1.000 17.47415 ? 348 PHE A O   1 
ATOM   2698 C  CB  . PHE A 1 348 ? 14.88232  5.76386   11.78462  1.000 15.16981 ? 348 PHE A CB  1 
ATOM   2699 C  CG  . PHE A 1 348 ? 15.18246  6.83854   12.81437  1.000 16.66048 ? 348 PHE A CG  1 
ATOM   2700 C  CD1 . PHE A 1 348 ? 14.15748  7.54938   13.42858  1.000 16.07153 ? 348 PHE A CD1 1 
ATOM   2701 C  CD2 . PHE A 1 348 ? 16.49764  7.19238   13.09406  1.000 18.24451 ? 348 PHE A CD2 1 
ATOM   2702 C  CE1 . PHE A 1 348 ? 14.44618  8.56864   14.34900  1.000 17.13907 ? 348 PHE A CE1 1 
ATOM   2703 C  CE2 . PHE A 1 348 ? 16.80035  8.20661   14.00537  1.000 18.93561 ? 348 PHE A CE2 1 
ATOM   2704 C  CZ  . PHE A 1 348 ? 15.77305  8.90069   14.63239  1.000 17.14484 ? 348 PHE A CZ  1 
ATOM   2705 N  N   . GLY A 1 349 ? 13.76508  2.41707   11.19655  1.000 17.82391 ? 349 GLY A N   1 
ATOM   2706 C  CA  . GLY A 1 349 ? 13.48530  1.59709   10.02637  1.000 19.02172 ? 349 GLY A CA  1 
ATOM   2707 C  C   . GLY A 1 349 ? 14.62402  1.60783   9.01750   1.000 18.48879 ? 349 GLY A C   1 
ATOM   2708 O  O   . GLY A 1 349 ? 15.76525  1.98583   9.30909   1.000 18.25254 ? 349 GLY A O   1 
ATOM   2709 N  N   . PHE A 1 350 ? 14.28689  1.18680   7.79557   1.000 16.42389 ? 350 PHE A N   1 
ATOM   2710 C  CA  . PHE A 1 350 ? 15.23657  1.04314   6.69505   1.000 18.64626 ? 350 PHE A CA  1 
ATOM   2711 C  C   . PHE A 1 350 ? 14.45648  1.00477   5.38860   1.000 17.36338 ? 350 PHE A C   1 
ATOM   2712 O  O   . PHE A 1 350 ? 13.38189  0.41221   5.33298   1.000 19.63024 ? 350 PHE A O   1 
ATOM   2713 C  CB  . PHE A 1 350 ? 16.07237  -0.24032  6.82500   1.000 21.85237 ? 350 PHE A CB  1 
ATOM   2714 C  CG  . PHE A 1 350 ? 16.90367  -0.54208  5.60869   1.000 20.02371 ? 350 PHE A CG  1 
ATOM   2715 C  CD1 . PHE A 1 350 ? 18.16784  0.00677   5.46198   1.000 19.86483 ? 350 PHE A CD1 1 
ATOM   2716 C  CD2 . PHE A 1 350 ? 16.41251  -1.36578  4.60411   1.000 19.25712 ? 350 PHE A CD2 1 
ATOM   2717 C  CE1 . PHE A 1 350 ? 18.92709  -0.24520  4.33111   1.000 21.15260 ? 350 PHE A CE1 1 
ATOM   2718 C  CE2 . PHE A 1 350 ? 17.16190  -1.62068  3.46861   1.000 20.33242 ? 350 PHE A CE2 1 
ATOM   2719 C  CZ  . PHE A 1 350 ? 18.42658  -1.06032  3.33269   1.000 21.34293 ? 350 PHE A CZ  1 
ATOM   2720 N  N   . GLY A 1 351 ? 15.00532  1.62063   4.34035   1.000 18.25124 ? 351 GLY A N   1 
ATOM   2721 C  CA  . GLY A 1 351 ? 14.39680  1.49481   3.02682   1.000 18.55100 ? 351 GLY A CA  1 
ATOM   2722 C  C   . GLY A 1 351 ? 13.43606  2.61445   2.69314   1.000 20.35090 ? 351 GLY A C   1 
ATOM   2723 O  O   . GLY A 1 351 ? 13.61374  3.73527   3.17284   1.000 20.81399 ? 351 GLY A O   1 
ATOM   2724 N  N   . VAL A 1 352 ? 12.41007  2.33659   1.88162   1.000 21.11406 ? 352 VAL A N   1 
ATOM   2725 C  CA  . VAL A 1 352 ? 11.60770  3.44225   1.35996   1.000 22.05074 ? 352 VAL A CA  1 
ATOM   2726 C  C   . VAL A 1 352 ? 10.80099  4.13209   2.45597   1.000 22.01232 ? 352 VAL A C   1 
ATOM   2727 O  O   . VAL A 1 352 ? 10.49201  5.32689   2.33157   1.000 22.02131 ? 352 VAL A O   1 
ATOM   2728 C  CB  . VAL A 1 352 ? 10.69129  2.98306   0.20635   1.000 24.37465 ? 352 VAL A CB  1 
ATOM   2729 C  CG1 . VAL A 1 352 ? 11.52037  2.47664   -0.97759  1.000 25.18103 ? 352 VAL A CG1 1 
ATOM   2730 C  CG2 . VAL A 1 352 ? 9.68296   1.94042   0.66563   1.000 25.25903 ? 352 VAL A CG2 1 
ATOM   2731 N  N   . HIS A 1 353 ? 10.43509  3.41652   3.52800   1.000 19.51150 ? 353 HIS A N   1 
ATOM   2732 C  CA  . HIS A 1 353 ? 9.65678   3.99637   4.62117   1.000 19.07643 ? 353 HIS A CA  1 
ATOM   2733 C  C   . HIS A 1 353 ? 10.50865  4.47429   5.78585   1.000 19.32563 ? 353 HIS A C   1 
ATOM   2734 O  O   . HIS A 1 353 ? 9.94614   4.78966   6.84574   1.000 19.08518 ? 353 HIS A O   1 
ATOM   2735 C  CB  . HIS A 1 353 ? 8.62809   3.00141   5.16784   1.000 17.08024 ? 353 HIS A CB  1 
ATOM   2736 C  CG  . HIS A 1 353 ? 7.53938   2.64353   4.20411   1.000 17.58533 ? 353 HIS A CG  1 
ATOM   2737 N  ND1 . HIS A 1 353 ? 6.39856   3.40530   4.04721   1.000 19.62569 ? 353 HIS A ND1 1 
ATOM   2738 C  CD2 . HIS A 1 353 ? 7.40752   1.58816   3.36249   1.000 18.62499 ? 353 HIS A CD2 1 
ATOM   2739 C  CE1 . HIS A 1 353 ? 5.61685   2.83720   3.14303   1.000 19.33414 ? 353 HIS A CE1 1 
ATOM   2740 N  NE2 . HIS A 1 353 ? 6.20987   1.74016   2.70633   1.000 18.51597 ? 353 HIS A NE2 1 
ATOM   2741 N  N   . GLN A 1 354 ? 11.83788  4.51347   5.64052   1.000 16.51861 ? 354 GLN A N   1 
ATOM   2742 C  CA  A GLN A 1 354 ? 12.67145  4.98779   6.73698   0.679 16.93791 ? 354 GLN A CA  1 
ATOM   2743 C  CA  B GLN A 1 354 ? 12.68790  4.99878   6.71967   0.321 16.60805 ? 354 GLN A CA  1 
ATOM   2744 C  C   . GLN A 1 354 ? 12.19490  6.35936   7.19684   1.000 16.19356 ? 354 GLN A C   1 
ATOM   2745 O  O   . GLN A 1 354 ? 11.87867  7.23443   6.38590   1.000 17.17706 ? 354 GLN A O   1 
ATOM   2746 C  CB  A GLN A 1 354 ? 14.14592  5.04746   6.33661   0.679 18.45832 ? 354 GLN A CB  1 
ATOM   2747 C  CB  B GLN A 1 354 ? 14.13919  5.08930   6.24573   0.321 17.27261 ? 354 GLN A CB  1 
ATOM   2748 C  CG  A GLN A 1 354 ? 15.03252  5.44489   7.51897   0.679 17.89696 ? 354 GLN A CG  1 
ATOM   2749 C  CG  B GLN A 1 354 ? 15.14581  5.30883   7.36298   0.321 16.77603 ? 354 GLN A CG  1 
ATOM   2750 C  CD  A GLN A 1 354 ? 16.48270  5.00961   7.38879   0.679 19.80014 ? 354 GLN A CD  1 
ATOM   2751 C  CD  B GLN A 1 354 ? 16.58295  5.24424   6.87694   0.321 18.51296 ? 354 GLN A CD  1 
ATOM   2752 O  OE1 A GLN A 1 354 ? 16.81607  4.12768   6.59261   0.679 19.80056 ? 354 GLN A OE1 1 
ATOM   2753 O  OE1 B GLN A 1 354 ? 17.23352  6.27234   6.68367   0.321 19.94412 ? 354 GLN A OE1 1 
ATOM   2754 N  NE2 A GLN A 1 354 ? 17.35232  5.62148   8.18771   0.679 19.94461 ? 354 GLN A NE2 1 
ATOM   2755 N  NE2 B GLN A 1 354 ? 17.08548  4.02977   6.67710   0.321 18.44121 ? 354 GLN A NE2 1 
ATOM   2756 N  N   . CYS A 1 355 ? 12.14169  6.53174   8.51906   1.000 14.16239 ? 355 CYS A N   1 
ATOM   2757 C  CA  . CYS A 1 355 ? 11.53823  7.68450   9.17921   1.000 15.64862 ? 355 CYS A CA  1 
ATOM   2758 C  C   . CYS A 1 355 ? 11.81546  9.00477   8.46516   1.000 15.51339 ? 355 CYS A C   1 
ATOM   2759 O  O   . CYS A 1 355 ? 12.96329  9.42659   8.34278   1.000 17.40504 ? 355 CYS A O   1 
ATOM   2760 C  CB  . CYS A 1 355 ? 12.05713  7.76189   10.61223  1.000 17.12994 ? 355 CYS A CB  1 
ATOM   2761 S  SG  . CYS A 1 355 ? 11.38631  9.17489   11.51664  1.000 17.83364 ? 355 CYS A SG  1 
ATOM   2762 N  N   . LEU A 1 356 ? 10.74468  9.67277   8.02688   1.000 17.06246 ? 356 LEU A N   1 
ATOM   2763 C  CA  . LEU A 1 356 ? 10.86242  10.99507  7.42028   1.000 20.36935 ? 356 LEU A CA  1 
ATOM   2764 C  C   . LEU A 1 356 ? 11.39645  12.03287  8.39469   1.000 16.19286 ? 356 LEU A C   1 
ATOM   2765 O  O   . LEU A 1 356 ? 12.09430  12.97439  7.98648   1.000 17.47636 ? 356 LEU A O   1 
ATOM   2766 C  CB  . LEU A 1 356 ? 9.49797   11.43925  6.90431   1.000 21.32553 ? 356 LEU A CB  1 
ATOM   2767 C  CG  . LEU A 1 356 ? 9.39758   12.82058  6.26693   1.000 26.13091 ? 356 LEU A CG  1 
ATOM   2768 C  CD1 . LEU A 1 356 ? 10.17809  12.88084  4.95329   1.000 30.50772 ? 356 LEU A CD1 1 
ATOM   2769 C  CD2 . LEU A 1 356 ? 7.93020   13.16312  6.05808   1.000 28.45927 ? 356 LEU A CD2 1 
ATOM   2770 N  N   . GLY A 1 357 ? 11.04996  11.90784  9.66712   1.000 15.14123 ? 357 GLY A N   1 
ATOM   2771 C  CA  . GLY A 1 357 ? 11.41595  12.89559  10.65490  1.000 16.59851 ? 357 GLY A CA  1 
ATOM   2772 C  C   . GLY A 1 357 ? 12.72651  12.64087  11.36236  1.000 15.95655 ? 357 GLY A C   1 
ATOM   2773 O  O   . GLY A 1 357 ? 13.02939  13.34159  12.33063  1.000 17.52047 ? 357 GLY A O   1 
ATOM   2774 N  N   . GLN A 1 358 ? 13.53649  11.68868  10.88766  1.000 16.71782 ? 358 GLN A N   1 
ATOM   2775 C  CA  . GLN A 1 358 ? 14.65043  11.19482  11.69722  1.000 17.13953 ? 358 GLN A CA  1 
ATOM   2776 C  C   . GLN A 1 358 ? 15.66249  12.28784  12.01749  1.000 19.85687 ? 358 GLN A C   1 
ATOM   2777 O  O   . GLN A 1 358 ? 16.22762  12.30848  13.11373  1.000 20.61536 ? 358 GLN A O   1 
ATOM   2778 C  CB  . GLN A 1 358 ? 15.34345  10.01989  11.00305  1.000 18.81121 ? 358 GLN A CB  1 
ATOM   2779 C  CG  . GLN A 1 358 ? 15.91492  10.32796  9.61423   1.000 16.64092 ? 358 GLN A CG  1 
ATOM   2780 C  CD  . GLN A 1 358 ? 16.54182  9.10329   8.97184   1.000 20.52369 ? 358 GLN A CD  1 
ATOM   2781 O  OE1 . GLN A 1 358 ? 17.16949  8.29069   9.64417   1.000 23.72177 ? 358 GLN A OE1 1 
ATOM   2782 N  NE2 . GLN A 1 358 ? 16.36126  8.96207   7.66214   1.000 23.57816 ? 358 GLN A NE2 1 
ATOM   2783 N  N   . ASN A 1 359 ? 15.91857  13.20577  11.08583  1.000 19.23872 ? 359 ASN A N   1 
ATOM   2784 C  CA  . ASN A 1 359 ? 16.91951  14.21460  11.40624  1.000 20.01493 ? 359 ASN A CA  1 
ATOM   2785 C  C   . ASN A 1 359 ? 16.34564  15.37751  12.20335  1.000 18.29788 ? 359 ASN A C   1 
ATOM   2786 O  O   . ASN A 1 359 ? 17.09479  16.02419  12.93606  1.000 19.11195 ? 359 ASN A O   1 
ATOM   2787 C  CB  . ASN A 1 359 ? 17.61216  14.68405  10.13761  1.000 22.39176 ? 359 ASN A CB  1 
ATOM   2788 C  CG  . ASN A 1 359 ? 18.46001  13.58441  9.53965   1.000 19.04741 ? 359 ASN A CG  1 
ATOM   2789 O  OD1 . ASN A 1 359 ? 19.06651  12.77481  10.27752  1.000 21.78844 ? 359 ASN A OD1 1 
ATOM   2790 N  ND2 . ASN A 1 359 ? 18.48548  13.50668  8.21636   1.000 23.24706 ? 359 ASN A ND2 1 
ATOM   2791 N  N   . LEU A 1 360 ? 15.03981  15.62819  12.11295  1.000 17.02783 ? 360 LEU A N   1 
ATOM   2792 C  CA  . LEU A 1 360 ? 14.41326  16.53981  13.06136  1.000 17.31618 ? 360 LEU A CA  1 
ATOM   2793 C  C   . LEU A 1 360 ? 14.49190  15.96346  14.46756  1.000 17.42167 ? 360 LEU A C   1 
ATOM   2794 O  O   . LEU A 1 360 ? 14.77668  16.68352  15.42848  1.000 18.54476 ? 360 LEU A O   1 
ATOM   2795 C  CB  . LEU A 1 360 ? 12.95748  16.80613  12.66774  1.000 17.46585 ? 360 LEU A CB  1 
ATOM   2796 C  CG  . LEU A 1 360 ? 12.16998  17.64127  13.70134  1.000 16.71586 ? 360 LEU A CG  1 
ATOM   2797 C  CD1 . LEU A 1 360 ? 12.79206  19.02398  13.92153  1.000 17.94396 ? 360 LEU A CD1 1 
ATOM   2798 C  CD2 . LEU A 1 360 ? 10.69097  17.76120  13.32240  1.000 21.66439 ? 360 LEU A CD2 1 
ATOM   2799 N  N   . ALA A 1 361 ? 14.26712  14.65090  14.59958  1.000 16.63384 ? 361 ALA A N   1 
ATOM   2800 C  CA  . ALA A 1 361 ? 14.34895  14.01821  15.91434  1.000 17.23921 ? 361 ALA A CA  1 
ATOM   2801 C  C   . ALA A 1 361 ? 15.77007  14.07727  16.46507  1.000 19.25649 ? 361 ALA A C   1 
ATOM   2802 O  O   . ALA A 1 361 ? 15.97102  14.33705  17.66092  1.000 17.70439 ? 361 ALA A O   1 
ATOM   2803 C  CB  . ALA A 1 361 ? 13.84943  12.57179  15.83247  1.000 18.46480 ? 361 ALA A CB  1 
ATOM   2804 N  N   . ARG A 1 362 ? 16.76765  13.85277  15.60947  1.000 19.45673 ? 362 ARG A N   1 
ATOM   2805 C  CA  . ARG A 1 362 ? 18.15962  13.94331  16.04460  1.000 17.86119 ? 362 ARG A CA  1 
ATOM   2806 C  C   . ARG A 1 362 ? 18.51570  15.35888  16.49039  1.000 18.12904 ? 362 ARG A C   1 
ATOM   2807 O  O   . ARG A 1 362 ? 19.22338  15.54773  17.48792  1.000 19.79668 ? 362 ARG A O   1 
ATOM   2808 C  CB  . ARG A 1 362 ? 19.08579  13.49625  14.91716  1.000 17.58820 ? 362 ARG A CB  1 
ATOM   2809 C  CG  . ARG A 1 362 ? 19.09251  12.01413  14.67736  1.000 16.40707 ? 362 ARG A CG  1 
ATOM   2810 C  CD  . ARG A 1 362 ? 19.93024  11.69399  13.45176  1.000 18.75998 ? 362 ARG A CD  1 
ATOM   2811 N  NE  . ARG A 1 362 ? 20.19171  10.26509  13.35863  1.000 21.26002 ? 362 ARG A NE  1 
ATOM   2812 C  CZ  . ARG A 1 362 ? 19.74086  9.47036   12.39922  1.000 19.40418 ? 362 ARG A CZ  1 
ATOM   2813 N  NH1 . ARG A 1 362 ? 19.01442  9.93869   11.39385  1.000 24.53397 ? 362 ARG A NH1 1 
ATOM   2814 N  NH2 . ARG A 1 362 ? 20.02242  8.16917   12.45437  1.000 21.39824 ? 362 ARG A NH2 1 
ATOM   2815 N  N   . LEU A 1 363 ? 18.05147  16.36521  15.75382  1.000 19.24619 ? 363 LEU A N   1 
ATOM   2816 C  CA  . LEU A 1 363 ? 18.29844  17.74811  16.15181  1.000 19.55513 ? 363 LEU A CA  1 
ATOM   2817 C  C   . LEU A 1 363 ? 17.64959  18.04415  17.49371  1.000 18.11967 ? 363 LEU A C   1 
ATOM   2818 O  O   . LEU A 1 363 ? 18.28046  18.61978  18.38828  1.000 19.34731 ? 363 LEU A O   1 
ATOM   2819 C  CB  . LEU A 1 363 ? 17.76925  18.71370  15.08785  1.000 19.17572 ? 363 LEU A CB  1 
ATOM   2820 C  CG  . LEU A 1 363 ? 17.71382  20.18421  15.52902  1.000 23.02791 ? 363 LEU A CG  1 
ATOM   2821 C  CD1 . LEU A 1 363 ? 19.11432  20.73689  15.78717  1.000 26.16382 ? 363 LEU A CD1 1 
ATOM   2822 C  CD2 . LEU A 1 363 ? 16.95347  21.04586  14.51316  1.000 21.91592 ? 363 LEU A CD2 1 
ATOM   2823 N  N   . GLU A 1 364 ? 16.37876  17.65927  17.64368  1.000 17.08173 ? 364 GLU A N   1 
ATOM   2824 C  CA  . GLU A 1 364 ? 15.65619  17.94003  18.87988  1.000 16.92742 ? 364 GLU A CA  1 
ATOM   2825 C  C   . GLU A 1 364 ? 16.34598  17.29765  20.07462  1.000 18.53273 ? 364 GLU A C   1 
ATOM   2826 O  O   . GLU A 1 364 ? 16.54203  17.94507  21.11022  1.000 17.88620 ? 364 GLU A O   1 
ATOM   2827 C  CB  . GLU A 1 364 ? 14.19894  17.47105  18.76446  1.000 16.65408 ? 364 GLU A CB  1 
ATOM   2828 C  CG  . GLU A 1 364 ? 13.35430  18.35201  17.82508  1.000 17.95426 ? 364 GLU A CG  1 
ATOM   2829 C  CD  . GLU A 1 364 ? 11.97628  17.77265  17.51957  1.000 22.06366 ? 364 GLU A CD  1 
ATOM   2830 O  OE1 . GLU A 1 364 ? 11.80081  16.54397  17.58561  1.000 26.47243 ? 364 GLU A OE1 1 
ATOM   2831 O  OE2 . GLU A 1 364 ? 11.06178  18.54591  17.17592  1.000 24.24416 ? 364 GLU A OE2 1 
ATOM   2832 N  N   . LEU A 1 365 ? 16.74225  16.03076  19.95183  1.000 15.49533 ? 365 LEU A N   1 
ATOM   2833 C  CA  . LEU A 1 365 ? 17.32784  15.35939  21.11204  1.000 15.46486 ? 365 LEU A CA  1 
ATOM   2834 C  C   . LEU A 1 365 ? 18.70560  15.91283  21.45481  1.000 17.65231 ? 365 LEU A C   1 
ATOM   2835 O  O   . LEU A 1 365 ? 19.05526  15.99597  22.63670  1.000 20.05909 ? 365 LEU A O   1 
ATOM   2836 C  CB  . LEU A 1 365 ? 17.38903  13.85685  20.87530  1.000 17.57534 ? 365 LEU A CB  1 
ATOM   2837 C  CG  . LEU A 1 365 ? 16.00584  13.21750  20.79648  1.000 21.82303 ? 365 LEU A CG  1 
ATOM   2838 C  CD1 . LEU A 1 365 ? 16.10166  11.82723  20.18536  1.000 25.88793 ? 365 LEU A CD1 1 
ATOM   2839 C  CD2 . LEU A 1 365 ? 15.35972  13.15185  22.18898  1.000 25.27936 ? 365 LEU A CD2 1 
ATOM   2840 N  N   . GLU A 1 366 ? 19.48593  16.33065  20.45339  1.000 18.78156 ? 366 GLU A N   1 
ATOM   2841 C  CA  . GLU A 1 366 ? 20.76147  16.97492  20.74480  1.000 19.90677 ? 366 GLU A CA  1 
ATOM   2842 C  C   . GLU A 1 366 ? 20.54796  18.28379  21.49254  1.000 19.86743 ? 366 GLU A C   1 
ATOM   2843 O  O   . GLU A 1 366 ? 21.21623  18.54922  22.49737  1.000 21.16370 ? 366 GLU A O   1 
ATOM   2844 C  CB  . GLU A 1 366 ? 21.54618  17.22134  19.45597  1.000 20.97261 ? 366 GLU A CB  1 
ATOM   2845 C  CG  . GLU A 1 366 ? 22.78829  18.09845  19.64354  1.000 26.35931 ? 366 GLU A CG  1 
ATOM   2846 C  CD  . GLU A 1 366 ? 22.50681  19.59557  19.46811  1.000 32.84481 ? 366 GLU A CD  1 
ATOM   2847 O  OE1 . GLU A 1 366 ? 21.94904  19.98305  18.41825  1.000 35.36810 ? 366 GLU A OE1 1 
ATOM   2848 O  OE2 . GLU A 1 366 ? 22.83714  20.38313  20.38624  1.000 35.42916 ? 366 GLU A OE2 1 
ATOM   2849 N  N   . VAL A 1 367 ? 19.63990  19.13310  20.99742  1.000 20.12336 ? 367 VAL A N   1 
ATOM   2850 C  CA  . VAL A 1 367 ? 19.38756  20.41065  21.67068  1.000 19.32806 ? 367 VAL A CA  1 
ATOM   2851 C  C   . VAL A 1 367 ? 18.86641  20.16123  23.07687  1.000 19.87473 ? 367 VAL A C   1 
ATOM   2852 O  O   . VAL A 1 367 ? 19.27357  20.82867  24.04159  1.000 21.80265 ? 367 VAL A O   1 
ATOM   2853 C  CB  . VAL A 1 367 ? 18.40876  21.27664  20.84641  1.000 19.83757 ? 367 VAL A CB  1 
ATOM   2854 C  CG1 . VAL A 1 367 ? 17.94469  22.51319  21.63713  1.000 20.66750 ? 367 VAL A CG1 1 
ATOM   2855 C  CG2 . VAL A 1 367 ? 19.05326  21.69773  19.53051  1.000 21.39464 ? 367 VAL A CG2 1 
ATOM   2856 N  N   . ILE A 1 368 ? 17.97631  19.17812  23.21968  1.000 18.92672 ? 368 ILE A N   1 
ATOM   2857 C  CA  . ILE A 1 368 ? 17.36475  18.90066  24.51963  1.000 19.30806 ? 368 ILE A CA  1 
ATOM   2858 C  C   . ILE A 1 368 ? 18.41404  18.42738  25.52225  1.000 20.56891 ? 368 ILE A C   1 
ATOM   2859 O  O   . ILE A 1 368 ? 18.46588  18.90440  26.66180  1.000 21.76630 ? 368 ILE A O   1 
ATOM   2860 C  CB  . ILE A 1 368 ? 16.22287  17.87791  24.36159  1.000 18.85733 ? 368 ILE A CB  1 
ATOM   2861 C  CG1 . ILE A 1 368 ? 14.99418  18.55868  23.75135  1.000 19.91051 ? 368 ILE A CG1 1 
ATOM   2862 C  CG2 . ILE A 1 368 ? 15.87339  17.21559  25.71966  1.000 19.16958 ? 368 ILE A CG2 1 
ATOM   2863 C  CD1 . ILE A 1 368 ? 13.95267  17.57592  23.22230  1.000 21.57149 ? 368 ILE A CD1 1 
ATOM   2864 N  N   . LEU A 1 369 ? 19.26482  17.47856  25.12258  1.000 19.67187 ? 369 LEU A N   1 
ATOM   2865 C  CA  . LEU A 1 369 ? 20.25249  16.97950  26.07550  1.000 19.15046 ? 369 LEU A CA  1 
ATOM   2866 C  C   . LEU A 1 369 ? 21.25072  18.06741  26.44717  1.000 20.73667 ? 369 LEU A C   1 
ATOM   2867 O  O   . LEU A 1 369 ? 21.60532  18.21306  27.62514  1.000 22.26280 ? 369 LEU A O   1 
ATOM   2868 C  CB  . LEU A 1 369 ? 20.96787  15.74323  25.53019  1.000 19.35406 ? 369 LEU A CB  1 
ATOM   2869 C  CG  . LEU A 1 369 ? 20.12359  14.46756  25.38035  1.000 21.03742 ? 369 LEU A CG  1 
ATOM   2870 C  CD1 . LEU A 1 369 ? 20.96963  13.37886  24.74798  1.000 23.51357 ? 369 LEU A CD1 1 
ATOM   2871 C  CD2 . LEU A 1 369 ? 19.56045  13.98988  26.71587  1.000 23.41782 ? 369 LEU A CD2 1 
ATOM   2872 N  N   . ASN A 1 370 ? 21.70757  18.85281  25.46617  1.000 21.43514 ? 370 ASN A N   1 
ATOM   2873 C  CA  . ASN A 1 370 ? 22.62922  19.93560  25.79462  1.000 20.65296 ? 370 ASN A CA  1 
ATOM   2874 C  C   . ASN A 1 370 ? 21.96855  20.94127  26.72342  1.000 22.58103 ? 370 ASN A C   1 
ATOM   2875 O  O   . ASN A 1 370 ? 22.61173  21.45803  27.64078  1.000 24.29220 ? 370 ASN A O   1 
ATOM   2876 C  CB  . ASN A 1 370 ? 23.14466  20.61732  24.52272  1.000 22.31914 ? 370 ASN A CB  1 
ATOM   2877 C  CG  . ASN A 1 370 ? 24.37013  19.92459  23.95558  1.000 22.65549 ? 370 ASN A CG  1 
ATOM   2878 O  OD1 . ASN A 1 370 ? 25.31807  19.63834  24.68595  1.000 25.25509 ? 370 ASN A OD1 1 
ATOM   2879 N  ND2 . ASN A 1 370 ? 24.34834  19.62605  22.65621  1.000 23.57366 ? 370 ASN A ND2 1 
ATOM   2880 N  N   . ALA A 1 371 ? 20.67121  21.19512  26.53018  1.000 23.17637 ? 371 ALA A N   1 
ATOM   2881 C  CA  . ALA A 1 371 ? 19.98853  22.18898  27.35656  1.000 23.52443 ? 371 ALA A CA  1 
ATOM   2882 C  C   . ALA A 1 371 ? 19.78471  21.68679  28.77891  1.000 22.69745 ? 371 ALA A C   1 
ATOM   2883 O  O   . ALA A 1 371 ? 19.92195  22.45452  29.73959  1.000 23.43273 ? 371 ALA A O   1 
ATOM   2884 C  CB  . ALA A 1 371 ? 18.65050  22.57397  26.72688  1.000 25.85382 ? 371 ALA A CB  1 
ATOM   2885 N  N   . LEU A 1 372 ? 19.44926  20.40847  28.94049  1.000 22.82269 ? 372 LEU A N   1 
ATOM   2886 C  CA  . LEU A 1 372 ? 19.32686  19.85531  30.28449  1.000 22.95315 ? 372 LEU A CA  1 
ATOM   2887 C  C   . LEU A 1 372 ? 20.66739  19.87642  31.01089  1.000 25.20257 ? 372 LEU A C   1 
ATOM   2888 O  O   . LEU A 1 372 ? 20.73882  20.24520  32.18752  1.000 24.24429 ? 372 LEU A O   1 
ATOM   2889 C  CB  . LEU A 1 372 ? 18.76541  18.43376  30.21064  1.000 23.06151 ? 372 LEU A CB  1 
ATOM   2890 C  CG  . LEU A 1 372 ? 17.30087  18.32166  29.78850  1.000 23.32242 ? 372 LEU A CG  1 
ATOM   2891 C  CD1 . LEU A 1 372 ? 16.91019  16.85526  29.62047  1.000 24.09586 ? 372 LEU A CD1 1 
ATOM   2892 C  CD2 . LEU A 1 372 ? 16.40249  19.00092  30.81580  1.000 25.29596 ? 372 LEU A CD2 1 
ATOM   2893 N  N   . MET A 1 373 ? 21.74828  19.50178  30.32506  1.000 25.02652 ? 373 MET A N   1 
ATOM   2894 C  CA  . MET A 1 373 ? 23.05487  19.53236  30.97577  1.000 25.30286 ? 373 MET A CA  1 
ATOM   2895 C  C   . MET A 1 373 ? 23.50482  20.95828  31.28418  1.000 27.39370 ? 373 MET A C   1 
ATOM   2896 O  O   . MET A 1 373 ? 24.20653  21.17828  32.28052  1.000 29.89700 ? 373 MET A O   1 
ATOM   2897 C  CB  . MET A 1 373 ? 24.08718  18.81312  30.11202  1.000 24.12787 ? 373 MET A CB  1 
ATOM   2898 C  CG  . MET A 1 373 ? 23.79680  17.32203  29.96268  1.000 25.70798 ? 373 MET A CG  1 
ATOM   2899 S  SD  . MET A 1 373 ? 25.06032  16.39900  29.06138  1.000 25.56387 ? 373 MET A SD  1 
ATOM   2900 C  CE  . MET A 1 373 ? 24.81784  17.01203  27.40064  1.000 24.72682 ? 373 MET A CE  1 
ATOM   2901 N  N   . ASP A 1 374 ? 23.11627  21.93574  30.45574  1.000 28.52163 ? 374 ASP A N   1 
ATOM   2902 C  CA  . ASP A 1 374 ? 23.50662  23.32427  30.69756  1.000 29.48370 ? 374 ASP A CA  1 
ATOM   2903 C  C   . ASP A 1 374 ? 22.68418  23.95150  31.81650  1.000 29.54244 ? 374 ASP A C   1 
ATOM   2904 O  O   . ASP A 1 374 ? 23.23685  24.58590  32.72287  1.000 34.15946 ? 374 ASP A O   1 
ATOM   2905 C  CB  . ASP A 1 374 ? 23.34425  24.16495  29.42406  1.000 28.11967 ? 374 ASP A CB  1 
ATOM   2906 C  CG  . ASP A 1 374 ? 24.44416  23.92284  28.39286  1.000 33.12102 ? 374 ASP A CG  1 
ATOM   2907 O  OD1 . ASP A 1 374 ? 25.44710  23.25258  28.70855  1.000 35.02306 ? 374 ASP A OD1 1 
ATOM   2908 O  OD2 . ASP A 1 374 ? 24.29621  24.41181  27.25033  1.000 35.17779 ? 374 ASP A OD2 1 
ATOM   2909 N  N   . ARG A 1 375 ? 21.36111  23.80294  31.75341  1.000 29.02441 ? 375 ARG A N   1 
ATOM   2910 C  CA  . ARG A 1 375 ? 20.45597  24.55282  32.61604  1.000 30.70722 ? 375 ARG A CA  1 
ATOM   2911 C  C   . ARG A 1 375 ? 20.08792  23.81129  33.88926  1.000 28.48019 ? 375 ARG A C   1 
ATOM   2912 O  O   . ARG A 1 375 ? 19.83418  24.45867  34.91306  1.000 32.74457 ? 375 ARG A O   1 
ATOM   2913 C  CB  . ARG A 1 375 ? 19.15889  24.89880  31.87715  1.000 32.09800 ? 375 ARG A CB  1 
ATOM   2914 C  CG  . ARG A 1 375 ? 19.32435  25.60842  30.53152  1.000 38.58956 ? 375 ARG A CG  1 
ATOM   2915 C  CD  . ARG A 1 375 ? 19.37574  27.11232  30.69890  1.000 39.27713 ? 375 ARG A CD  1 
ATOM   2916 N  NE  . ARG A 1 375 ? 18.26340  27.61562  31.49758  1.000 39.34606 ? 375 ARG A NE  1 
ATOM   2917 C  CZ  . ARG A 1 375 ? 17.09438  27.99972  31.00194  1.000 42.20729 ? 375 ARG A CZ  1 
ATOM   2918 N  NH1 . ARG A 1 375 ? 16.84112  27.94297  29.70314  1.000 41.24741 ? 375 ARG A NH1 1 
ATOM   2919 N  NH2 . ARG A 1 375 ? 16.15468  28.45067  31.83004  1.000 42.29202 ? 375 ARG A NH2 1 
ATOM   2920 N  N   . VAL A 1 376 ? 20.02538  22.48152  33.85418  1.000 28.34639 ? 376 VAL A N   1 
ATOM   2921 C  CA  . VAL A 1 376 ? 19.63425  21.73290  35.04718  1.000 28.56730 ? 376 VAL A CA  1 
ATOM   2922 C  C   . VAL A 1 376 ? 20.59377  20.56119  35.25549  1.000 30.21712 ? 376 VAL A C   1 
ATOM   2923 O  O   . VAL A 1 376 ? 20.17833  19.39231  35.26884  1.000 31.03364 ? 376 VAL A O   1 
ATOM   2924 C  CB  . VAL A 1 376 ? 18.15076  21.32034  34.96595  1.000 32.37758 ? 376 VAL A CB  1 
ATOM   2925 C  CG1 . VAL A 1 376 ? 17.85706  20.39293  33.78432  1.000 36.43417 ? 376 VAL A CG1 1 
ATOM   2926 C  CG2 . VAL A 1 376 ? 17.66378  20.75121  36.27180  1.000 33.85788 ? 376 VAL A CG2 1 
ATOM   2927 N  N   . PRO A 1 377 ? 21.88708  20.82772  35.45735  1.000 31.63103 ? 377 PRO A N   1 
ATOM   2928 C  CA  . PRO A 1 377 ? 22.83785  19.72193  35.64447  1.000 34.90648 ? 377 PRO A CA  1 
ATOM   2929 C  C   . PRO A 1 377 ? 22.54701  18.87348  36.87131  1.000 36.02201 ? 377 PRO A C   1 
ATOM   2930 O  O   . PRO A 1 377 ? 23.03076  17.73735  36.94289  1.000 38.88787 ? 377 PRO A O   1 
ATOM   2931 C  CB  . PRO A 1 377 ? 24.18740  20.44211  35.76585  1.000 34.83530 ? 377 PRO A CB  1 
ATOM   2932 C  CG  . PRO A 1 377 ? 23.82541  21.79134  36.33279  1.000 34.11370 ? 377 PRO A CG  1 
ATOM   2933 C  CD  . PRO A 1 377 ? 22.53317  22.13931  35.63947  1.000 35.81716 ? 377 PRO A CD  1 
ATOM   2934 N  N   . THR A 1 378 ? 21.76203  19.37363  37.82529  1.000 35.47304 ? 378 THR A N   1 
ATOM   2935 C  CA  . THR A 1 378 ? 21.39590  18.61361  39.01468  1.000 34.93323 ? 378 THR A CA  1 
ATOM   2936 C  C   . THR A 1 378 ? 20.06512  17.89007  38.87822  1.000 33.70066 ? 378 THR A C   1 
ATOM   2937 O  O   . THR A 1 378 ? 19.57742  17.34001  39.86691  1.000 34.82646 ? 378 THR A O   1 
ATOM   2938 C  CB  . THR A 1 378 ? 21.35678  19.52805  40.24480  1.000 38.81855 ? 378 THR A CB  1 
ATOM   2939 O  OG1 . THR A 1 378 ? 20.23811  20.43319  40.16661  1.000 37.06464 ? 378 THR A OG1 1 
ATOM   2940 C  CG2 . THR A 1 378 ? 22.62715  20.30922  40.29850  1.000 40.79684 ? 378 THR A CG2 1 
ATOM   2941 N  N   . LEU A 1 379 ? 19.47671  17.86790  37.68215  1.000 32.35098 ? 379 LEU A N   1 
ATOM   2942 C  CA  . LEU A 1 379 ? 18.22581  17.15064  37.46639  1.000 30.56856 ? 379 LEU A CA  1 
ATOM   2943 C  C   . LEU A 1 379 ? 18.32980  15.72640  37.99490  1.000 28.77456 ? 379 LEU A C   1 
ATOM   2944 O  O   . LEU A 1 379 ? 19.32996  15.04401  37.77240  1.000 29.68261 ? 379 LEU A O   1 
ATOM   2945 C  CB  . LEU A 1 379 ? 17.88944  17.12802  35.97312  1.000 34.22077 ? 379 LEU A CB  1 
ATOM   2946 C  CG  . LEU A 1 379 ? 16.60047  16.43507  35.51729  1.000 33.93884 ? 379 LEU A CG  1 
ATOM   2947 C  CD1 . LEU A 1 379 ? 15.37803  17.24153  35.92012  1.000 34.69364 ? 379 LEU A CD1 1 
ATOM   2948 C  CD2 . LEU A 1 379 ? 16.61754  16.20497  34.00115  1.000 35.92227 ? 379 LEU A CD2 1 
ATOM   2949 N  N   . ARG A 1 380 ? 17.29586  15.28760  38.70773  1.000 30.93218 ? 380 ARG A N   1 
ATOM   2950 C  CA  . ARG A 1 380 ? 17.22973  13.91570  39.18995  1.000 31.33272 ? 380 ARG A CA  1 
ATOM   2951 C  C   . ARG A 1 380 ? 15.77172  13.48999  39.24981  1.000 29.84676 ? 380 ARG A C   1 
ATOM   2952 O  O   . ARG A 1 380 ? 14.86103  14.32163  39.26590  1.000 30.66117 ? 380 ARG A O   1 
ATOM   2953 C  CB  . ARG A 1 380 ? 17.89772  13.75962  40.56304  1.000 37.04696 ? 380 ARG A CB  1 
ATOM   2954 C  CG  . ARG A 1 380 ? 17.34910  14.69846  41.62060  1.000 45.55339 ? 380 ARG A CG  1 
ATOM   2955 C  CD  . ARG A 1 380 ? 18.26006  14.77454  42.83988  1.000 54.11726 ? 380 ARG A CD  1 
ATOM   2956 N  NE  . ARG A 1 380 ? 17.72297  15.66978  43.85770  1.000 60.21105 ? 380 ARG A NE  1 
ATOM   2957 C  CZ  . ARG A 1 380 ? 16.77721  15.32890  44.72271  1.000 64.81448 ? 380 ARG A CZ  1 
ATOM   2958 N  NH1 . ARG A 1 380 ? 16.22288  14.12631  44.70125  1.000 67.77262 ? 380 ARG A NH1 1 
ATOM   2959 N  NH2 . ARG A 1 380 ? 16.37139  16.21788  45.62713  1.000 63.80549 ? 380 ARG A NH2 1 
ATOM   2960 N  N   . LEU A 1 381 ? 15.55685  12.17814  39.25434  1.000 28.91597 ? 381 LEU A N   1 
ATOM   2961 C  CA  . LEU A 1 381 ? 14.20685  11.66186  39.41765  1.000 28.96052 ? 381 LEU A CA  1 
ATOM   2962 C  C   . LEU A 1 381 ? 13.72436  11.93350  40.83403  1.000 31.03245 ? 381 LEU A C   1 
ATOM   2963 O  O   . LEU A 1 381 ? 14.48590  11.82273  41.80266  1.000 31.24117 ? 381 LEU A O   1 
ATOM   2964 C  CB  . LEU A 1 381 ? 14.15317  10.16591  39.12368  1.000 30.34904 ? 381 LEU A CB  1 
ATOM   2965 C  CG  . LEU A 1 381 ? 14.54502  9.73401   37.70541  1.000 31.68123 ? 381 LEU A CG  1 
ATOM   2966 C  CD1 . LEU A 1 381 ? 14.06853  8.30967   37.43165  1.000 30.33286 ? 381 LEU A CD1 1 
ATOM   2967 C  CD2 . LEU A 1 381 ? 14.01027  10.69296  36.64685  1.000 30.07626 ? 381 LEU A CD2 1 
ATOM   2968 N  N   . ALA A 1 382 ? 12.45510  12.31997  40.94556  1.000 32.38701 ? 382 ALA A N   1 
ATOM   2969 C  CA  . ALA A 1 382 ? 11.84549  12.59872  42.23716  1.000 35.56251 ? 382 ALA A CA  1 
ATOM   2970 C  C   . ALA A 1 382 ? 11.20661  11.36473  42.85790  1.000 38.98006 ? 382 ALA A C   1 
ATOM   2971 O  O   . ALA A 1 382 ? 10.78613  11.41814  44.02053  1.000 41.35476 ? 382 ALA A O   1 
ATOM   2972 C  CB  . ALA A 1 382 ? 10.80329  13.71757  42.09483  1.000 35.21419 ? 382 ALA A CB  1 
ATOM   2973 N  N   . VAL A 1 383 ? 11.12324  10.26874  42.11048  1.000 39.20116 ? 383 VAL A N   1 
ATOM   2974 C  CA  . VAL A 1 383 ? 10.65174  8.98033   42.61441  1.000 39.74740 ? 383 VAL A CA  1 
ATOM   2975 C  C   . VAL A 1 383 ? 11.62826  7.91255   42.14078  1.000 38.12516 ? 383 VAL A C   1 
ATOM   2976 O  O   . VAL A 1 383 ? 12.35317  8.11144   41.15199  1.000 38.21583 ? 383 VAL A O   1 
ATOM   2977 C  CB  . VAL A 1 383 ? 9.21295   8.66778   42.13538  1.000 39.98609 ? 383 VAL A CB  1 
ATOM   2978 C  CG1 . VAL A 1 383 ? 8.22992   9.72861   42.61382  1.000 40.35019 ? 383 VAL A CG1 1 
ATOM   2979 C  CG2 . VAL A 1 383 ? 9.17060   8.54466   40.61406  1.000 40.64781 ? 383 VAL A CG2 1 
ATOM   2980 N  N   . PRO A 1 384 ? 11.69502  6.77790   42.83727  1.000 40.05053 ? 384 PRO A N   1 
ATOM   2981 C  CA  . PRO A 1 384 ? 12.53182  5.67390   42.35323  1.000 41.05849 ? 384 PRO A CA  1 
ATOM   2982 C  C   . PRO A 1 384 ? 12.03637  5.17805   41.00273  1.000 40.51043 ? 384 PRO A C   1 
ATOM   2983 O  O   . PRO A 1 384 ? 10.84844  5.26909   40.68484  1.000 40.74851 ? 384 PRO A O   1 
ATOM   2984 C  CB  . PRO A 1 384 ? 12.37308  4.59920   43.43808  1.000 43.20211 ? 384 PRO A CB  1 
ATOM   2985 C  CG  . PRO A 1 384 ? 11.91248  5.33366   44.65111  1.000 43.35814 ? 384 PRO A CG  1 
ATOM   2986 C  CD  . PRO A 1 384 ? 11.08036  6.47610   44.13995  1.000 39.95032 ? 384 PRO A CD  1 
ATOM   2987 N  N   . VAL A 1 385 ? 12.96942  4.65069   40.20153  1.000 38.94290 ? 385 VAL A N   1 
ATOM   2988 C  CA  . VAL A 1 385 ? 12.60329  4.08866   38.90204  1.000 38.02813 ? 385 VAL A CA  1 
ATOM   2989 C  C   . VAL A 1 385 ? 11.52069  3.02985   39.06472  1.000 40.83414 ? 385 VAL A C   1 
ATOM   2990 O  O   . VAL A 1 385 ? 10.65780  2.87361   38.19171  1.000 39.84316 ? 385 VAL A O   1 
ATOM   2991 C  CB  . VAL A 1 385 ? 13.84957  3.52402   38.18448  1.000 37.31541 ? 385 VAL A CB  1 
ATOM   2992 C  CG1 . VAL A 1 385 ? 13.44979  2.71661   36.94869  1.000 37.43334 ? 385 VAL A CG1 1 
ATOM   2993 C  CG2 . VAL A 1 385 ? 14.78980  4.64639   37.77595  1.000 34.40911 ? 385 VAL A CG2 1 
ATOM   2994 N  N   . GLU A 1 386 ? 11.51605  2.32437   40.20210  1.000 44.92570 ? 386 GLU A N   1 
ATOM   2995 C  CA  . GLU A 1 386 ? 10.55040  1.25563   40.44287  1.000 47.22840 ? 386 GLU A CA  1 
ATOM   2996 C  C   . GLU A 1 386 ? 9.11818   1.75793   40.56697  1.000 44.26795 ? 386 GLU A C   1 
ATOM   2997 O  O   . GLU A 1 386 ? 8.18856   0.95006   40.47521  1.000 45.07550 ? 386 GLU A O   1 
ATOM   2998 C  CB  . GLU A 1 386 ? 10.92222  0.47567   41.70750  1.000 51.98075 ? 386 GLU A CB  1 
ATOM   2999 C  CG  . GLU A 1 386 ? 12.23655  -0.28557  41.62751  1.000 59.02434 ? 386 GLU A CG  1 
ATOM   3000 C  CD  . GLU A 1 386 ? 13.42491  0.53202   42.10419  1.000 64.35840 ? 386 GLU A CD  1 
ATOM   3001 O  OE1 . GLU A 1 386 ? 13.37482  1.77602   42.00645  1.000 66.72457 ? 386 GLU A OE1 1 
ATOM   3002 O  OE2 . GLU A 1 386 ? 14.40812  -0.07249  42.58662  1.000 64.79837 ? 386 GLU A OE2 1 
ATOM   3003 N  N   . GLN A 1 387 ? 8.91400   3.05607   40.78130  1.000 40.77393 ? 387 GLN A N   1 
ATOM   3004 C  CA  . GLN A 1 387 ? 7.57293   3.61292   40.89869  1.000 37.54652 ? 387 GLN A CA  1 
ATOM   3005 C  C   . GLN A 1 387 ? 7.04586   4.15869   39.57509  1.000 33.79054 ? 387 GLN A C   1 
ATOM   3006 O  O   . GLN A 1 387 ? 5.87941   4.56072   39.50171  1.000 32.80746 ? 387 GLN A O   1 
ATOM   3007 C  CB  . GLN A 1 387 ? 7.55338   4.70922   41.97166  1.000 39.77665 ? 387 GLN A CB  1 
ATOM   3008 C  CG  . GLN A 1 387 ? 7.75715   4.16449   43.38539  1.000 43.86100 ? 387 GLN A CG  1 
ATOM   3009 C  CD  . GLN A 1 387 ? 7.74062   5.23517   44.46495  1.000 48.00605 ? 387 GLN A CD  1 
ATOM   3010 O  OE1 . GLN A 1 387 ? 7.37436   6.38289   44.22253  1.000 51.35147 ? 387 GLN A OE1 1 
ATOM   3011 N  NE2 . GLN A 1 387 ? 8.14101   4.85490   45.67007  1.000 49.91159 ? 387 GLN A NE2 1 
ATOM   3012 N  N   . LEU A 1 388 ? 7.86437   4.16573   38.52927  1.000 32.75716 ? 388 LEU A N   1 
ATOM   3013 C  CA  . LEU A 1 388 ? 7.41802   4.65475   37.23351  1.000 30.24241 ? 388 LEU A CA  1 
ATOM   3014 C  C   . LEU A 1 388 ? 6.53615   3.61278   36.55497  1.000 29.44256 ? 388 LEU A C   1 
ATOM   3015 O  O   . LEU A 1 388 ? 6.62086   2.41534   36.84039  1.000 30.42998 ? 388 LEU A O   1 
ATOM   3016 C  CB  . LEU A 1 388 ? 8.61957   4.99856   36.34854  1.000 27.34801 ? 388 LEU A CB  1 
ATOM   3017 C  CG  . LEU A 1 388 ? 9.54614   6.07182   36.92416  1.000 27.86368 ? 388 LEU A CG  1 
ATOM   3018 C  CD1 . LEU A 1 388 ? 10.79945  6.23465   36.07902  1.000 29.84040 ? 388 LEU A CD1 1 
ATOM   3019 C  CD2 . LEU A 1 388 ? 8.80850   7.39566   37.05003  1.000 28.33529 ? 388 LEU A CD2 1 
ATOM   3020 N  N   . VAL A 1 389 ? 5.67238   4.08317   35.65877  1.000 27.51940 ? 389 VAL A N   1 
ATOM   3021 C  CA  . VAL A 1 389 ? 4.74236   3.22936   34.93006  1.000 27.45079 ? 389 VAL A CA  1 
ATOM   3022 C  C   . VAL A 1 389 ? 5.07769   3.33013   33.44926  1.000 27.09960 ? 389 VAL A C   1 
ATOM   3023 O  O   . VAL A 1 389 ? 4.93920   4.40524   32.85056  1.000 27.55642 ? 389 VAL A O   1 
ATOM   3024 C  CB  . VAL A 1 389 ? 3.28131   3.62638   35.19044  1.000 29.32667 ? 389 VAL A CB  1 
ATOM   3025 C  CG1 . VAL A 1 389 ? 2.34802   2.78947   34.33716  1.000 30.25523 ? 389 VAL A CG1 1 
ATOM   3026 C  CG2 . VAL A 1 389 ? 2.94768   3.47897   36.67320  1.000 32.16224 ? 389 VAL A CG2 1 
ATOM   3027 N  N   . LEU A 1 390 ? 5.51640   2.21793   32.85991  1.000 26.09694 ? 390 LEU A N   1 
ATOM   3028 C  CA  . LEU A 1 390 ? 5.83862   2.17490   31.43851  1.000 26.13628 ? 390 LEU A CA  1 
ATOM   3029 C  C   . LEU A 1 390 ? 4.60152   1.83198   30.61931  1.000 26.43778 ? 390 LEU A C   1 
ATOM   3030 O  O   . LEU A 1 390 ? 3.74189   1.06566   31.05247  1.000 30.25066 ? 390 LEU A O   1 
ATOM   3031 C  CB  . LEU A 1 390 ? 6.93284   1.14539   31.15972  1.000 24.54312 ? 390 LEU A CB  1 
ATOM   3032 C  CG  . LEU A 1 390 ? 8.30146   1.40507   31.79062  1.000 26.54415 ? 390 LEU A CG  1 
ATOM   3033 C  CD1 . LEU A 1 390 ? 9.19987   0.21174   31.57545  1.000 29.12017 ? 390 LEU A CD1 1 
ATOM   3034 C  CD2 . LEU A 1 390 ? 8.94500   2.64377   31.19648  1.000 31.22632 ? 390 LEU A CD2 1 
ATOM   3035 N  N   . ARG A 1 391 ? 4.52099   2.41096   29.42371  1.000 25.04589 ? 391 ARG A N   1 
ATOM   3036 C  CA  . ARG A 1 391 ? 3.44598   2.07443   28.50773  1.000 24.82041 ? 391 ARG A CA  1 
ATOM   3037 C  C   . ARG A 1 391 ? 3.60148   0.64270   28.00147  1.000 24.48932 ? 391 ARG A C   1 
ATOM   3038 O  O   . ARG A 1 391 ? 4.71178   0.11331   27.95667  1.000 25.17224 ? 391 ARG A O   1 
ATOM   3039 C  CB  . ARG A 1 391 ? 3.45090   3.01570   27.31773  1.000 25.25193 ? 391 ARG A CB  1 
ATOM   3040 C  CG  . ARG A 1 391 ? 3.29943   4.46552   27.67591  1.000 26.24416 ? 391 ARG A CG  1 
ATOM   3041 C  CD  . ARG A 1 391 ? 3.48708   5.27323   26.43146  1.000 29.65081 ? 391 ARG A CD  1 
ATOM   3042 N  NE  . ARG A 1 391 ? 3.57823   6.69303   26.72345  1.000 33.05744 ? 391 ARG A NE  1 
ATOM   3043 C  CZ  . ARG A 1 391 ? 4.22488   7.55572   25.95726  1.000 37.86791 ? 391 ARG A CZ  1 
ATOM   3044 N  NH1 . ARG A 1 391 ? 4.86773   7.16072   24.87158  1.000 36.18887 ? 391 ARG A NH1 1 
ATOM   3045 N  NH2 . ARG A 1 391 ? 4.23011   8.84320   26.29171  1.000 39.46436 ? 391 ARG A NH2 1 
ATOM   3046 N  N   . PRO A 1 392 ? 2.51113   0.00566   27.58684  1.000 27.07698 ? 392 PRO A N   1 
ATOM   3047 C  CA  . PRO A 1 392 ? 2.59603   -1.37688  27.10682  1.000 25.99814 ? 392 PRO A CA  1 
ATOM   3048 C  C   . PRO A 1 392 ? 3.18621   -1.45167  25.70385  1.000 26.42124 ? 392 PRO A C   1 
ATOM   3049 O  O   . PRO A 1 392 ? 3.31712   -0.45319  24.98835  1.000 24.74519 ? 392 PRO A O   1 
ATOM   3050 C  CB  . PRO A 1 392 ? 1.13725   -1.84132  27.11663  1.000 26.37209 ? 392 PRO A CB  1 
ATOM   3051 C  CG  . PRO A 1 392 ? 0.35984   -0.59464  26.89900  1.000 29.03387 ? 392 PRO A CG  1 
ATOM   3052 C  CD  . PRO A 1 392 ? 1.11484   0.47487   27.65370  1.000 30.32592 ? 392 PRO A CD  1 
ATOM   3053 N  N   . GLY A 1 393 ? 3.55066   -2.67610  25.32099  1.000 26.06308 ? 393 GLY A N   1 
ATOM   3054 C  CA  . GLY A 1 393 ? 4.22765   -2.89903  24.06276  1.000 25.57484 ? 393 GLY A CA  1 
ATOM   3055 C  C   . GLY A 1 393 ? 3.36765   -2.73007  22.83468  1.000 23.13097 ? 393 GLY A C   1 
ATOM   3056 O  O   . GLY A 1 393 ? 3.88252   -2.84382  21.71937  1.000 25.16983 ? 393 GLY A O   1 
ATOM   3057 N  N   . THR A 1 394 ? 2.08021   -2.45153  23.00713  1.000 23.98015 ? 394 THR A N   1 
ATOM   3058 C  CA  . THR A 1 394 ? 1.17184   -2.19582  21.90226  1.000 24.69700 ? 394 THR A CA  1 
ATOM   3059 C  C   . THR A 1 394 ? 1.18650   -0.74431  21.43123  1.000 22.08615 ? 394 THR A C   1 
ATOM   3060 O  O   . THR A 1 394 ? 0.45017   -0.40896  20.49828  1.000 25.56410 ? 394 THR A O   1 
ATOM   3061 C  CB  . THR A 1 394 ? -0.25445  -2.58861  22.30579  1.000 26.01987 ? 394 THR A CB  1 
ATOM   3062 O  OG1 . THR A 1 394 ? -0.57041  -1.98803  23.56958  1.000 28.25363 ? 394 THR A OG1 1 
ATOM   3063 C  CG2 . THR A 1 394 ? -0.37419  -4.09772  22.42021  1.000 28.80333 ? 394 THR A CG2 1 
ATOM   3064 N  N   . THR A 1 395 ? 1.99602   0.12083   22.03821  1.000 21.47474 ? 395 THR A N   1 
ATOM   3065 C  CA  . THR A 1 395 ? 2.06594   1.51624   21.62145  1.000 22.43084 ? 395 THR A CA  1 
ATOM   3066 C  C   . THR A 1 395 ? 3.53110   1.93862   21.55619  1.000 20.90962 ? 395 THR A C   1 
ATOM   3067 O  O   . THR A 1 395 ? 4.43718   1.11884   21.70428  1.000 22.25512 ? 395 THR A O   1 
ATOM   3068 C  CB  . THR A 1 395 ? 1.24404   2.42050   22.55342  1.000 24.29942 ? 395 THR A CB  1 
ATOM   3069 O  OG1 . THR A 1 395 ? 1.21804   3.75410   22.02463  1.000 26.38568 ? 395 THR A OG1 1 
ATOM   3070 C  CG2 . THR A 1 395 ? 1.81951   2.44741   23.96452  1.000 23.39958 ? 395 THR A CG2 1 
ATOM   3071 N  N   . ILE A 1 396 ? 3.76276   3.22605   21.28348  1.000 20.73099 ? 396 ILE A N   1 
ATOM   3072 C  CA  . ILE A 1 396 ? 5.10774   3.78596   21.37800  1.000 19.28969 ? 396 ILE A CA  1 
ATOM   3073 C  C   . ILE A 1 396 ? 5.59621   3.67686   22.81568  1.000 21.43615 ? 396 ILE A C   1 
ATOM   3074 O  O   . ILE A 1 396 ? 4.87763   4.03955   23.75533  1.000 22.13194 ? 396 ILE A O   1 
ATOM   3075 C  CB  . ILE A 1 396 ? 5.11088   5.25366   20.92025  1.000 20.89580 ? 396 ILE A CB  1 
ATOM   3076 C  CG1 . ILE A 1 396 ? 4.58995   5.38082   19.48963  1.000 25.23600 ? 396 ILE A CG1 1 
ATOM   3077 C  CG2 . ILE A 1 396 ? 6.51546   5.86427   21.05322  1.000 22.48527 ? 396 ILE A CG2 1 
ATOM   3078 C  CD1 . ILE A 1 396 ? 5.49556   4.75808   18.46249  1.000 34.89290 ? 396 ILE A CD1 1 
ATOM   3079 N  N   . GLN A 1 397 ? 6.82927   3.19650   22.99990  1.000 19.56526 ? 397 GLN A N   1 
ATOM   3080 C  CA  . GLN A 1 397 ? 7.35345   3.02702   24.35468  1.000 18.90041 ? 397 GLN A CA  1 
ATOM   3081 C  C   . GLN A 1 397 ? 7.51214   4.37948   25.03747  1.000 20.43385 ? 397 GLN A C   1 
ATOM   3082 O  O   . GLN A 1 397 ? 7.77219   5.39556   24.38828  1.000 22.86484 ? 397 GLN A O   1 
ATOM   3083 C  CB  . GLN A 1 397 ? 8.70874   2.32170   24.33935  1.000 19.72139 ? 397 GLN A CB  1 
ATOM   3084 C  CG  . GLN A 1 397 ? 8.75556   1.03177   23.52720  1.000 20.36338 ? 397 GLN A CG  1 
ATOM   3085 C  CD  . GLN A 1 397 ? 8.12380   -0.16472  24.22499  1.000 26.19193 ? 397 GLN A CD  1 
ATOM   3086 O  OE1 . GLN A 1 397 ? 7.89551   -0.16581  25.44323  1.000 23.93121 ? 397 GLN A OE1 1 
ATOM   3087 N  NE2 . GLN A 1 397 ? 7.86988   -1.20596  23.45506  1.000 32.76995 ? 397 GLN A NE2 1 
ATOM   3088 N  N   . GLY A 1 398 ? 7.36651   4.38600   26.35667  1.000 20.97538 ? 398 GLY A N   1 
ATOM   3089 C  CA  . GLY A 1 398 ? 7.58975   5.59966   27.11518  1.000 22.71833 ? 398 GLY A CA  1 
ATOM   3090 C  C   . GLY A 1 398 ? 6.93173   5.54423   28.48115  1.000 22.92945 ? 398 GLY A C   1 
ATOM   3091 O  O   . GLY A 1 398 ? 6.43803   4.50407   28.91896  1.000 23.71685 ? 398 GLY A O   1 
ATOM   3092 N  N   . VAL A 1 399 ? 6.95411   6.69772   29.14626  1.000 24.01592 ? 399 VAL A N   1 
ATOM   3093 C  CA  . VAL A 1 399 ? 6.27708   6.91014   30.42364  1.000 23.48871 ? 399 VAL A CA  1 
ATOM   3094 C  C   . VAL A 1 399 ? 5.33211   8.09082   30.26476  1.000 25.32390 ? 399 VAL A C   1 
ATOM   3095 O  O   . VAL A 1 399 ? 5.67985   9.08916   29.62825  1.000 28.63468 ? 399 VAL A O   1 
ATOM   3096 C  CB  . VAL A 1 399 ? 7.26431   7.17778   31.58289  1.000 24.82566 ? 399 VAL A CB  1 
ATOM   3097 C  CG1 . VAL A 1 399 ? 8.04616   5.91872   31.93323  1.000 28.45519 ? 399 VAL A CG1 1 
ATOM   3098 C  CG2 . VAL A 1 399 ? 8.21192   8.33297   31.24933  1.000 25.82944 ? 399 VAL A CG2 1 
ATOM   3099 N  N   . ASN A 1 400 ? 4.14113   7.98955   30.85225  1.000 27.93426 ? 400 ASN A N   1 
ATOM   3100 C  CA  . ASN A 1 400 ? 3.20739   9.10486   30.74621  1.000 29.37948 ? 400 ASN A CA  1 
ATOM   3101 C  C   . ASN A 1 400 ? 3.45781   10.19290  31.78304  1.000 29.37059 ? 400 ASN A C   1 
ATOM   3102 O  O   . ASN A 1 400 ? 3.02058   11.33043  31.57494  1.000 30.01296 ? 400 ASN A O   1 
ATOM   3103 C  CB  . ASN A 1 400 ? 1.76734   8.60688   30.83955  1.000 30.65410 ? 400 ASN A CB  1 
ATOM   3104 C  CG  . ASN A 1 400 ? 1.31266   7.93242   29.56901  1.000 33.49177 ? 400 ASN A CG  1 
ATOM   3105 O  OD1 . ASN A 1 400 ? 1.86054   8.18238   28.49301  1.000 33.15997 ? 400 ASN A OD1 1 
ATOM   3106 N  ND2 . ASN A 1 400 ? 0.30867   7.07066   29.67950  1.000 35.26495 ? 400 ASN A ND2 1 
ATOM   3107 N  N   . GLU A 1 401 ? 4.13758   9.88104   32.88934  1.000 25.12298 ? 401 GLU A N   1 
ATOM   3108 C  CA  A GLU A 1 401 ? 4.53109   10.87928  33.87452  0.606 26.12427 ? 401 GLU A CA  1 
ATOM   3109 C  CA  B GLU A 1 401 ? 4.55758   10.91015  33.82619  0.394 26.65263 ? 401 GLU A CA  1 
ATOM   3110 C  C   . GLU A 1 401 ? 5.94825   10.57428  34.33958  1.000 25.00319 ? 401 GLU A C   1 
ATOM   3111 O  O   . GLU A 1 401 ? 6.31718   9.40611   34.47573  1.000 29.44387 ? 401 GLU A O   1 
ATOM   3112 C  CB  A GLU A 1 401 ? 3.56157   10.89960  35.06770  0.606 32.55361 ? 401 GLU A CB  1 
ATOM   3113 C  CB  B GLU A 1 401 ? 3.56706   11.07795  34.98871  0.394 31.91300 ? 401 GLU A CB  1 
ATOM   3114 C  CG  A GLU A 1 401 ? 3.72316   12.11204  35.97996  0.606 38.76362 ? 401 GLU A CG  1 
ATOM   3115 C  CG  B GLU A 1 401 ? 3.18129   9.80431   35.70404  0.394 36.13954 ? 401 GLU A CG  1 
ATOM   3116 C  CD  A GLU A 1 401 ? 2.64797   12.20007  37.05529  0.606 44.16516 ? 401 GLU A CD  1 
ATOM   3117 C  CD  B GLU A 1 401 ? 2.25776   10.06753  36.88472  0.394 40.73362 ? 401 GLU A CD  1 
ATOM   3118 O  OE1 A GLU A 1 401 ? 1.60504   11.52180  36.92776  0.606 45.23789 ? 401 GLU A OE1 1 
ATOM   3119 O  OE1 B GLU A 1 401 ? 2.68712   10.74078  37.84751  0.394 43.04048 ? 401 GLU A OE1 1 
ATOM   3120 O  OE2 A GLU A 1 401 ? 2.84722   12.95249  38.03164  0.606 45.17270 ? 401 GLU A OE2 1 
ATOM   3121 O  OE2 B GLU A 1 401 ? 1.09589   9.61472   36.84040  0.394 42.00328 ? 401 GLU A OE2 1 
ATOM   3122 N  N   . LEU A 1 402 ? 6.73971   11.61841  34.58498  1.000 23.66087 ? 402 LEU A N   1 
ATOM   3123 C  CA  . LEU A 1 402 ? 8.12216   11.44910  35.03792  1.000 23.68203 ? 402 LEU A CA  1 
ATOM   3124 C  C   . LEU A 1 402 ? 8.43768   12.51846  36.07434  1.000 27.76609 ? 402 LEU A C   1 
ATOM   3125 O  O   . LEU A 1 402 ? 8.88644   13.62127  35.73797  1.000 26.49141 ? 402 LEU A O   1 
ATOM   3126 C  CB  . LEU A 1 402 ? 9.10536   11.51136  33.86440  1.000 23.01051 ? 402 LEU A CB  1 
ATOM   3127 C  CG  . LEU A 1 402 ? 10.57836  11.27974  34.22556  1.000 22.68991 ? 402 LEU A CG  1 
ATOM   3128 C  CD1 . LEU A 1 402 ? 10.78390  9.94780   34.95895  1.000 24.22256 ? 402 LEU A CD1 1 
ATOM   3129 C  CD2 . LEU A 1 402 ? 11.48091  11.36456  32.99282  1.000 25.50722 ? 402 LEU A CD2 1 
ATOM   3130 N  N   . PRO A 1 403 ? 8.21115   12.22602  37.35421  1.000 30.31838 ? 403 PRO A N   1 
ATOM   3131 C  CA  . PRO A 1 403 ? 8.49208   13.22594  38.39657  1.000 29.10372 ? 403 PRO A CA  1 
ATOM   3132 C  C   . PRO A 1 403 ? 9.98869   13.47490  38.52600  1.000 30.59171 ? 403 PRO A C   1 
ATOM   3133 O  O   . PRO A 1 403 ? 10.78156  12.53714  38.65127  1.000 28.87759 ? 403 PRO A O   1 
ATOM   3134 C  CB  . PRO A 1 403 ? 7.91083   12.59132  39.66844  1.000 30.83369 ? 403 PRO A CB  1 
ATOM   3135 C  CG  . PRO A 1 403 ? 6.90821   11.57678  39.16333  1.000 31.40242 ? 403 PRO A CG  1 
ATOM   3136 C  CD  . PRO A 1 403 ? 7.50974   11.04710  37.88882  1.000 30.21831 ? 403 PRO A CD  1 
ATOM   3137 N  N   . VAL A 1 404 ? 10.37300  14.75457  38.50415  1.000 28.26281 ? 404 VAL A N   1 
ATOM   3138 C  CA  . VAL A 1 404 ? 11.77570  15.14692  38.55635  1.000 27.23735 ? 404 VAL A CA  1 
ATOM   3139 C  C   . VAL A 1 404 ? 11.94174  16.31621  39.52019  1.000 28.55466 ? 404 VAL A C   1 
ATOM   3140 O  O   . VAL A 1 404 ? 10.99431  17.04156  39.83319  1.000 31.48108 ? 404 VAL A O   1 
ATOM   3141 C  CB  . VAL A 1 404 ? 12.33463  15.52537  37.16342  1.000 24.59962 ? 404 VAL A CB  1 
ATOM   3142 C  CG1 . VAL A 1 404 ? 12.32084  14.31040  36.22297  1.000 26.26283 ? 404 VAL A CG1 1 
ATOM   3143 C  CG2 . VAL A 1 404 ? 11.53663  16.67693  36.56638  1.000 26.55038 ? 404 VAL A CG2 1 
ATOM   3144 N  N   . THR A 1 405 ? 13.17031  16.48772  40.00199  1.000 27.96063 ? 405 THR A N   1 
ATOM   3145 C  CA  . THR A 1 405 ? 13.49860  17.61812  40.85845  1.000 28.96668 ? 405 THR A CA  1 
ATOM   3146 C  C   . THR A 1 405 ? 14.93352  18.02403  40.55168  1.000 27.80067 ? 405 THR A C   1 
ATOM   3147 O  O   . THR A 1 405 ? 15.59025  17.43862  39.68297  1.000 29.72848 ? 405 THR A O   1 
ATOM   3148 C  CB  . THR A 1 405 ? 13.26667  17.27404  42.33754  1.000 33.17581 ? 405 THR A CB  1 
ATOM   3149 O  OG1 . THR A 1 405 ? 13.48785  18.43427  43.15216  1.000 36.17680 ? 405 THR A OG1 1 
ATOM   3150 C  CG2 . THR A 1 405 ? 14.17702  16.15082  42.77620  1.000 35.38578 ? 405 THR A CG2 1 
ATOM   3151 N  N   . TRP A 1 406 ? 15.41150  19.04786  41.24754  1.000 29.35252 ? 406 TRP A N   1 
ATOM   3152 C  CA  . TRP A 1 406 ? 16.69616  19.66428  40.93488  1.000 34.18164 ? 406 TRP A CA  1 
ATOM   3153 C  C   . TRP A 1 406 ? 17.01570  20.66556  42.03928  1.000 37.86897 ? 406 TRP A C   1 
ATOM   3154 O  O   . TRP A 1 406 ? 16.19892  20.91659  42.92959  1.000 40.71275 ? 406 TRP A O   1 
ATOM   3155 C  CB  . TRP A 1 406 ? 16.66380  20.34461  39.56210  1.000 34.24018 ? 406 TRP A CB  1 
ATOM   3156 C  CG  . TRP A 1 406 ? 15.58558  21.38855  39.45764  1.000 34.28532 ? 406 TRP A CG  1 
ATOM   3157 C  CD1 . TRP A 1 406 ? 15.64459  22.67934  39.90441  1.000 35.71324 ? 406 TRP A CD1 1 
ATOM   3158 C  CD2 . TRP A 1 406 ? 14.27925  21.21966  38.89801  1.000 32.02189 ? 406 TRP A CD2 1 
ATOM   3159 N  NE1 . TRP A 1 406 ? 14.46038  23.32509  39.64778  1.000 37.14170 ? 406 TRP A NE1 1 
ATOM   3160 C  CE2 . TRP A 1 406 ? 13.60506  22.45053  39.03006  1.000 34.09440 ? 406 TRP A CE2 1 
ATOM   3161 C  CE3 . TRP A 1 406 ? 13.61657  20.14646  38.29050  1.000 31.22913 ? 406 TRP A CE3 1 
ATOM   3162 C  CZ2 . TRP A 1 406 ? 12.30171  22.63901  38.57726  1.000 35.16021 ? 406 TRP A CZ2 1 
ATOM   3163 C  CZ3 . TRP A 1 406 ? 12.32364  20.33417  37.84521  1.000 33.05308 ? 406 TRP A CZ3 1 
ATOM   3164 C  CH2 . TRP A 1 406 ? 11.67820  21.57364  37.99069  1.000 34.83442 ? 406 TRP A CH2 1 
ATOM   3165 N  N   . HIS A 1 407 ? 18.21358  21.24381  41.95944  1.000 42.08424 ? 407 HIS A N   1 
ATOM   3166 C  CA  . HIS A 1 407 ? 18.62929  22.31802  42.85427  1.000 45.00367 ? 407 HIS A CA  1 
ATOM   3167 C  C   . HIS A 1 407 ? 17.90489  23.61329  42.50298  1.000 54.32035 ? 407 HIS A C   1 
ATOM   3168 O  O   . HIS A 1 407 ? 17.82765  23.99727  41.33431  1.000 57.49103 ? 407 HIS A O   1 
ATOM   3169 C  CB  . HIS A 1 407 ? 20.14054  22.51848  42.73783  1.000 41.47248 ? 407 HIS A CB  1 
ATOM   3170 C  CG  . HIS A 1 407 ? 20.73211  23.39352  43.79919  1.000 41.02385 ? 407 HIS A CG  1 
ATOM   3171 N  ND1 . HIS A 1 407 ? 21.01673  24.72695  43.59376  1.000 43.29358 ? 407 HIS A ND1 1 
ATOM   3172 C  CD2 . HIS A 1 407 ? 21.12549  23.11608  45.06492  1.000 42.04081 ? 407 HIS A CD2 1 
ATOM   3173 C  CE1 . HIS A 1 407 ? 21.54506  25.23560  44.69308  1.000 42.26537 ? 407 HIS A CE1 1 
ATOM   3174 N  NE2 . HIS A 1 407 ? 21.61853  24.28074  45.60220  1.000 46.10477 ? 407 HIS A NE2 1 
ATOM   3175 N  N   . HIS A 1 408 ? 17.40369  24.30741  43.52359  1.000 62.53777 ? 408 HIS A N   1 
ATOM   3176 C  CA  . HIS A 1 408 ? 16.59039  25.49823  43.30783  1.000 69.81327 ? 408 HIS A CA  1 
ATOM   3177 C  C   . HIS A 1 408 ? 17.40735  26.61793  42.65870  1.000 69.44511 ? 408 HIS A C   1 
ATOM   3178 O  O   . HIS A 1 408 ? 18.62722  26.53092  42.49392  1.000 70.47217 ? 408 HIS A O   1 
ATOM   3179 C  CB  . HIS A 1 408 ? 15.99153  25.98860  44.62844  1.000 77.47499 ? 408 HIS A CB  1 
ATOM   3180 C  CG  . HIS A 1 408 ? 16.92840  26.82126  45.45111  1.000 84.22977 ? 408 HIS A CG  1 
ATOM   3181 N  ND1 . HIS A 1 408 ? 16.95734  28.19849  45.38283  1.000 86.86509 ? 408 HIS A ND1 1 
ATOM   3182 C  CD2 . HIS A 1 408 ? 17.86665  26.47125  46.36310  1.000 86.05512 ? 408 HIS A CD2 1 
ATOM   3183 C  CE1 . HIS A 1 408 ? 17.87357  28.66006  46.21582  1.000 87.52784 ? 408 HIS A CE1 1 
ATOM   3184 N  NE2 . HIS A 1 408 ? 18.43980  27.63264  46.82287  1.000 87.36278 ? 408 HIS A NE2 1 
ATOM   3185 N  N   . HIS A 1 409 ? 16.70617  27.68706  42.29070  1.000 70.99725 ? 409 HIS A N   1 
ATOM   3186 C  CA  . HIS A 1 409 ? 17.32847  28.88536  41.72842  1.000 69.69064 ? 409 HIS A CA  1 
ATOM   3187 C  C   . HIS A 1 409 ? 18.06001  29.70459  42.79418  1.000 64.54836 ? 409 HIS A C   1 
ATOM   3188 O  O   . HIS A 1 409 ? 19.04472  29.25696  43.38556  1.000 60.43256 ? 409 HIS A O   1 
ATOM   3189 C  CB  . HIS A 1 409 ? 16.26867  29.75075  41.03601  1.000 70.78312 ? 409 HIS A CB  1 
ATOM   3190 C  CG  . HIS A 1 409 ? 16.32253  31.19995  41.41264  1.000 72.61267 ? 409 HIS A CG  1 
ATOM   3191 N  ND1 . HIS A 1 409 ? 15.82341  31.67961  42.60534  1.000 73.00304 ? 409 HIS A ND1 1 
ATOM   3192 C  CD2 . HIS A 1 409 ? 16.80007  32.27731  40.74535  1.000 73.50869 ? 409 HIS A CD2 1 
ATOM   3193 C  CE1 . HIS A 1 409 ? 16.00441  32.98694  42.66276  1.000 73.57143 ? 409 HIS A CE1 1 
ATOM   3194 N  NE2 . HIS A 1 409 ? 16.59219  33.37522  41.54520  1.000 74.03371 ? 409 HIS A NE2 1 
HETATM 3195 C  CHA . HEM B 2 .   ? 8.39583   6.34099   9.88528   1.000 17.69580 ? 501 HEM A CHA 1 
HETATM 3196 C  CHB . HEM B 2 .   ? 10.51229  5.73671   14.22215  1.000 16.43627 ? 501 HEM A CHB 1 
HETATM 3197 C  CHC . HEM B 2 .   ? 10.41893  10.55298  14.90249  1.000 18.07873 ? 501 HEM A CHC 1 
HETATM 3198 C  CHD . HEM B 2 .   ? 7.56482   11.03008  10.98625  1.000 17.83333 ? 501 HEM A CHD 1 
HETATM 3199 C  C1A . HEM B 2 .   ? 9.04243   5.75469   10.95334  1.000 17.98651 ? 501 HEM A C1A 1 
HETATM 3200 C  C2A . HEM B 2 .   ? 9.47184   4.36756   11.07868  1.000 16.77347 ? 501 HEM A C2A 1 
HETATM 3201 C  C3A . HEM B 2 .   ? 10.04662  4.22804   12.27774  1.000 17.33433 ? 501 HEM A C3A 1 
HETATM 3202 C  C4A . HEM B 2 .   ? 10.00758  5.49566   12.96419  1.000 17.53930 ? 501 HEM A C4A 1 
HETATM 3203 C  CMA . HEM B 2 .   ? 10.65685  2.94728   12.87637  1.000 17.81442 ? 501 HEM A CMA 1 
HETATM 3204 C  CAA . HEM B 2 .   ? 9.33195   3.24125   10.01438  1.000 16.47882 ? 501 HEM A CAA 1 
HETATM 3205 C  CBA . HEM B 2 .   ? 7.87708   2.84168   9.84585   1.000 18.67258 ? 501 HEM A CBA 1 
HETATM 3206 C  CGA . HEM B 2 .   ? 7.72585   1.70452   8.86301   1.000 19.85934 ? 501 HEM A CGA 1 
HETATM 3207 O  O1A . HEM B 2 .   ? 8.73877   1.16563   8.33726   1.000 20.54752 ? 501 HEM A O1A 1 
HETATM 3208 O  O2A . HEM B 2 .   ? 6.55913   1.33032   8.61487   1.000 24.82703 ? 501 HEM A O2A 1 
HETATM 3209 C  C1B . HEM B 2 .   ? 10.71370  6.98663   14.76415  1.000 16.60162 ? 501 HEM A C1B 1 
HETATM 3210 C  C2B . HEM B 2 .   ? 11.48239  7.27590   15.94730  1.000 17.38294 ? 501 HEM A C2B 1 
HETATM 3211 C  C3B . HEM B 2 .   ? 11.46123  8.60106   16.16395  1.000 17.06623 ? 501 HEM A C3B 1 
HETATM 3212 C  C4B . HEM B 2 .   ? 10.68589  9.21249   15.09559  1.000 18.14299 ? 501 HEM A C4B 1 
HETATM 3213 C  CMB . HEM B 2 .   ? 12.20503  6.21344   16.80485  1.000 17.66593 ? 501 HEM A CMB 1 
HETATM 3214 C  CAB . HEM B 2 .   ? 12.20452  9.28806   17.34027  1.000 19.19866 ? 501 HEM A CAB 1 
HETATM 3215 C  CBB . HEM B 2 .   ? 11.93031  10.50842  17.77555  1.000 26.12244 ? 501 HEM A CBB 1 
HETATM 3216 C  C1C . HEM B 2 .   ? 9.62764   11.09939  13.91516  1.000 18.24573 ? 501 HEM A C1C 1 
HETATM 3217 C  C2C . HEM B 2 .   ? 9.31677   12.50247  13.78511  1.000 18.96104 ? 501 HEM A C2C 1 
HETATM 3218 C  C3C . HEM B 2 .   ? 8.51458   12.65260  12.72543  1.000 18.77346 ? 501 HEM A C3C 1 
HETATM 3219 C  C4C . HEM B 2 .   ? 8.30849   11.34689  12.11189  1.000 17.67770 ? 501 HEM A C4C 1 
HETATM 3220 C  CMC . HEM B 2 .   ? 9.80399   13.61831  14.74265  1.000 20.93638 ? 501 HEM A CMC 1 
HETATM 3221 C  CAC . HEM B 2 .   ? 7.96490   14.02370  12.27315  1.000 23.73536 ? 501 HEM A CAC 1 
HETATM 3222 C  CBC . HEM B 2 .   ? 6.92221   14.11323  11.46315  1.000 28.86252 ? 501 HEM A CBC 1 
HETATM 3223 C  C1D . HEM B 2 .   ? 7.55807   9.80034   10.34192  1.000 19.30611 ? 501 HEM A C1D 1 
HETATM 3224 C  C2D . HEM B 2 .   ? 6.88985   9.49886   9.08833   1.000 19.66175 ? 501 HEM A C2D 1 
HETATM 3225 C  C3D . HEM B 2 .   ? 7.12325   8.21005   8.79137   1.000 19.30726 ? 501 HEM A C3D 1 
HETATM 3226 C  C4D . HEM B 2 .   ? 7.94359   7.64306   9.83810   1.000 17.48947 ? 501 HEM A C4D 1 
HETATM 3227 C  CMD . HEM B 2 .   ? 6.05342   10.49470  8.25175   1.000 21.33280 ? 501 HEM A CMD 1 
HETATM 3228 C  CAD . HEM B 2 .   ? 6.62166   7.41764   7.56247   1.000 19.90385 ? 501 HEM A CAD 1 
HETATM 3229 C  CBD . HEM B 2 .   ? 7.72092   7.38275   6.49812   1.000 19.97736 ? 501 HEM A CBD 1 
HETATM 3230 C  CGD . HEM B 2 .   ? 7.23982   6.64321   5.27036   1.000 21.76743 ? 501 HEM A CGD 1 
HETATM 3231 O  O1D . HEM B 2 .   ? 7.79651   6.89223   4.17664   1.000 21.82998 ? 501 HEM A O1D 1 
HETATM 3232 O  O2D . HEM B 2 .   ? 6.29849   5.81879   5.37179   1.000 21.84746 ? 501 HEM A O2D 1 
HETATM 3233 N  NA  . HEM B 2 .   ? 9.39429   6.41131   12.12179  1.000 17.01672 ? 501 HEM A NA  1 
HETATM 3234 N  NB  . HEM B 2 .   ? 10.23759  8.18702   14.27432  1.000 17.40672 ? 501 HEM A NB  1 
HETATM 3235 N  NC  . HEM B 2 .   ? 9.01182   10.42787  12.87375  1.000 17.48185 ? 501 HEM A NC  1 
HETATM 3236 N  ND  . HEM B 2 .   ? 8.18504   8.63340   10.77434  1.000 17.77883 ? 501 HEM A ND  1 
HETATM 3237 FE FE  . HEM B 2 .   ? 9.37704   8.46041   12.41692  1.000 17.85843 ? 501 HEM A FE  1 
HETATM 3238 C  C1  . DIF C 3 .   ? 5.57003   7.09250   15.07432  0.779 39.05759 ? 502 DIF A C1  1 
HETATM 3239 C  C2  . DIF C 3 .   ? 4.22088   6.87784   14.87541  0.779 41.37294 ? 502 DIF A C2  1 
HETATM 3240 CL CL2 . DIF C 3 .   ? 3.10975   7.99490   15.57739  0.779 44.40438 ? 502 DIF A CL2 1 
HETATM 3241 C  C3  . DIF C 3 .   ? 3.72253   5.78931   14.14578  0.779 42.22443 ? 502 DIF A C3  1 
HETATM 3242 C  C4  . DIF C 3 .   ? 4.69768   4.93543   13.60579  0.779 40.62770 ? 502 DIF A C4  1 
HETATM 3243 CL CL4 . DIF C 3 .   ? 4.20101   3.55806   12.67925  0.779 41.01116 ? 502 DIF A CL4 1 
HETATM 3244 C  C5  . DIF C 3 .   ? 6.05681   5.13489   13.79575  0.779 37.50892 ? 502 DIF A C5  1 
HETATM 3245 C  C6  . DIF C 3 .   ? 6.49728   6.22104   14.53338  0.779 34.43083 ? 502 DIF A C6  1 
HETATM 3246 N  N1  . DIF C 3 .   ? 2.36765   5.61056   13.94342  0.779 43.82848 ? 502 DIF A N1  1 
HETATM 3247 C  C7  . DIF C 3 .   ? 0.02731   5.71941   14.49355  0.779 44.68682 ? 502 DIF A C7  1 
HETATM 3248 C  C8  . DIF C 3 .   ? 1.35323   5.44989   14.88965  0.779 46.00434 ? 502 DIF A C8  1 
HETATM 3249 C  C9  . DIF C 3 .   ? 1.59961   5.02528   16.18973  0.779 47.70473 ? 502 DIF A C9  1 
HETATM 3250 C  C10 . DIF C 3 .   ? 0.56780   4.85538   17.10150  0.779 49.09566 ? 502 DIF A C10 1 
HETATM 3251 C  C11 . DIF C 3 .   ? -0.73961  5.12469   16.72427  0.779 49.12781 ? 502 DIF A C11 1 
HETATM 3252 C  C12 . DIF C 3 .   ? -0.98894  5.55464   15.42780  0.779 48.03530 ? 502 DIF A C12 1 
HETATM 3253 C  C13 . DIF C 3 .   ? -0.31268  6.20404   13.10721  0.779 43.73393 ? 502 DIF A C13 1 
HETATM 3254 C  C14 . DIF C 3 .   ? 0.14293   5.29578   11.94713  0.779 43.69123 ? 502 DIF A C14 1 
HETATM 3255 O  O1  . DIF C 3 .   ? 1.27496   4.76481   12.07672  0.779 46.15022 ? 502 DIF A O1  1 
HETATM 3256 O  O2  . DIF C 3 .   ? -0.61898  5.15992   10.98005  0.779 43.67510 ? 502 DIF A O2  1 
HETATM 3257 C  C   . TRS D 4 .   ? 25.96749  -3.17969  6.83500   1.000 48.53400 ? 503 TRS A C   1 
HETATM 3258 C  C1  . TRS D 4 .   ? 26.04756  -2.06877  5.77557   1.000 49.49068 ? 503 TRS A C1  1 
HETATM 3259 C  C2  . TRS D 4 .   ? 25.38009  -4.47846  6.29533   1.000 47.54436 ? 503 TRS A C2  1 
HETATM 3260 C  C3  . TRS D 4 .   ? 25.16978  -2.75197  8.06514   1.000 48.64170 ? 503 TRS A C3  1 
HETATM 3261 N  N   . TRS D 4 .   ? 27.38198  -3.46084  7.25401   1.000 49.36899 ? 503 TRS A N   1 
HETATM 3262 O  O1  . TRS D 4 .   ? 26.91326  -2.48549  4.75256   1.000 48.73207 ? 503 TRS A O1  1 
HETATM 3263 O  O2  . TRS D 4 .   ? 24.09554  -4.21065  5.79359   1.000 45.47361 ? 503 TRS A O2  1 
HETATM 3264 O  O3  . TRS D 4 .   ? 25.28163  -3.72515  9.07754   1.000 46.78286 ? 503 TRS A O3  1 
HETATM 3265 C  C1  . EDO E 5 .   ? 0.82503   17.40453  -13.98235 1.000 69.25874 ? 504 EDO A C1  1 
HETATM 3266 O  O1  . EDO E 5 .   ? 0.80261   18.78491  -14.27451 1.000 73.17757 ? 504 EDO A O1  1 
HETATM 3267 C  C2  . EDO E 5 .   ? 0.44745   16.61315  -15.20736 1.000 64.84574 ? 504 EDO A C2  1 
HETATM 3268 O  O2  . EDO E 5 .   ? 0.11472   15.29814  -14.82921 1.000 61.84308 ? 504 EDO A O2  1 
HETATM 3269 C  C1  . EDO F 5 .   ? -3.77670  7.87964   11.18937  1.000 60.72818 ? 505 EDO A C1  1 
HETATM 3270 O  O1  . EDO F 5 .   ? -4.85285  7.17916   11.77075  1.000 61.46304 ? 505 EDO A O1  1 
HETATM 3271 C  C2  . EDO F 5 .   ? -3.10924  7.00202   10.16505  1.000 59.75992 ? 505 EDO A C2  1 
HETATM 3272 O  O2  . EDO F 5 .   ? -1.86889  7.55719   9.79005   1.000 59.85023 ? 505 EDO A O2  1 
HETATM 3273 O  O   . HOH G 6 .   ? 13.70135  -11.27599 1.07223   1.000 41.71735 ? 601 HOH A O   1 
HETATM 3274 O  O   . HOH G 6 .   ? 25.31989  -7.44863  26.23355  1.000 35.28916 ? 602 HOH A O   1 
HETATM 3275 O  O   . HOH G 6 .   ? 14.83343  -9.61910  -0.85899  1.000 47.24532 ? 603 HOH A O   1 
HETATM 3276 O  O   . HOH G 6 .   ? 3.17117   5.33773   31.49856  1.000 35.22897 ? 604 HOH A O   1 
HETATM 3277 O  O   . HOH G 6 .   ? 23.82166  1.29725   7.23138   1.000 34.52677 ? 605 HOH A O   1 
HETATM 3278 O  O   . HOH G 6 .   ? 5.43995   -20.55084 6.36794   1.000 51.43025 ? 606 HOH A O   1 
HETATM 3279 O  O   . HOH G 6 .   ? 17.69562  -6.52649  27.19080  1.000 48.94552 ? 607 HOH A O   1 
HETATM 3280 O  O   . HOH G 6 .   ? 19.34948  27.07331  49.02110  1.000 58.98116 ? 608 HOH A O   1 
HETATM 3281 O  O   . HOH G 6 .   ? 1.75459   19.45744  28.47751  1.000 42.00324 ? 609 HOH A O   1 
HETATM 3282 O  O   . HOH G 6 .   ? -15.14130 22.83030  5.24205   1.000 57.57714 ? 610 HOH A O   1 
HETATM 3283 O  O   . HOH G 6 .   ? 2.12638   13.52897  32.41817  1.000 40.95443 ? 611 HOH A O   1 
HETATM 3284 O  O   . HOH G 6 .   ? -2.31582  2.01674   20.85156  1.000 53.76500 ? 612 HOH A O   1 
HETATM 3285 O  O   . HOH G 6 .   ? -3.08862  34.35477  3.23335   1.000 56.74811 ? 613 HOH A O   1 
HETATM 3286 O  O   . HOH G 6 .   ? -8.77150  11.15669  6.73603   1.000 34.95735 ? 614 HOH A O   1 
HETATM 3287 O  O   . HOH G 6 .   ? -9.12913  2.84990   4.26881   1.000 46.25340 ? 615 HOH A O   1 
HETATM 3288 O  O   . HOH G 6 .   ? 3.42850   -20.35059 8.33330   1.000 42.61687 ? 616 HOH A O   1 
HETATM 3289 O  O   . HOH G 6 .   ? 6.05488   24.25325  33.47513  1.000 35.82554 ? 617 HOH A O   1 
HETATM 3290 O  O   . HOH G 6 .   ? -0.16329  -13.91852 9.95741   1.000 42.21145 ? 618 HOH A O   1 
HETATM 3291 O  O   . HOH G 6 .   ? -14.36162 20.56484  10.90692  1.000 65.98982 ? 619 HOH A O   1 
HETATM 3292 O  O   . HOH G 6 .   ? 29.60092  -9.83223  19.51479  1.000 59.73970 ? 620 HOH A O   1 
HETATM 3293 O  O   . HOH G 6 .   ? -15.13899 19.88220  4.88100   1.000 61.13917 ? 621 HOH A O   1 
HETATM 3294 O  O   . HOH G 6 .   ? 16.67774  14.96995  6.64768   1.000 44.54411 ? 622 HOH A O   1 
HETATM 3295 O  O   . HOH G 6 .   ? 16.08495  -8.21748  28.97237  1.000 57.65522 ? 623 HOH A O   1 
HETATM 3296 O  O   . HOH G 6 .   ? 5.20451   1.19078   6.42515   1.000 27.77964 ? 624 HOH A O   1 
HETATM 3297 O  O   . HOH G 6 .   ? 8.65741   17.73317  16.68621  1.000 22.26703 ? 625 HOH A O   1 
HETATM 3298 O  O   . HOH G 6 .   ? 3.22295   -19.14685 12.39235  1.000 56.58762 ? 626 HOH A O   1 
HETATM 3299 O  O   . HOH G 6 .   ? 18.98967  -9.62069  17.19373  1.000 23.96501 ? 627 HOH A O   1 
HETATM 3300 O  O   . HOH G 6 .   ? 14.34721  -17.99546 15.46755  1.000 46.29058 ? 628 HOH A O   1 
HETATM 3301 O  O   . HOH G 6 .   ? 1.36074   11.80908  24.87541  1.000 54.67418 ? 629 HOH A O   1 
HETATM 3302 O  O   . HOH G 6 .   ? 0.22354   14.35018  23.06514  1.000 32.91847 ? 630 HOH A O   1 
HETATM 3303 O  O   . HOH G 6 .   ? 6.87762   24.60955  7.22428   1.000 35.08896 ? 631 HOH A O   1 
HETATM 3304 O  O   . HOH G 6 .   ? -2.63880  3.25513   7.45273   1.000 52.99663 ? 632 HOH A O   1 
HETATM 3305 O  O   . HOH G 6 .   ? 22.15013  18.65493  16.17810  1.000 57.49113 ? 633 HOH A O   1 
HETATM 3306 O  O   . HOH G 6 .   ? 29.44617  9.64036   21.66537  1.000 42.76335 ? 634 HOH A O   1 
HETATM 3307 O  O   . HOH G 6 .   ? -11.52041 20.23170  -0.69483  1.000 49.45304 ? 635 HOH A O   1 
HETATM 3308 O  O   . HOH G 6 .   ? 14.20538  -15.49789 16.41060  1.000 41.07679 ? 636 HOH A O   1 
HETATM 3309 O  O   . HOH G 6 .   ? 2.06206   26.77479  14.76812  1.000 34.47250 ? 637 HOH A O   1 
HETATM 3310 O  O   . HOH G 6 .   ? -10.77521 8.60340   22.42234  1.000 36.85813 ? 638 HOH A O   1 
HETATM 3311 O  O   . HOH G 6 .   ? 10.95218  16.26507  23.92263  1.000 24.32948 ? 639 HOH A O   1 
HETATM 3312 O  O   . HOH G 6 .   ? -13.11837 -31.82637 34.14423  1.000 59.29427 ? 640 HOH A O   1 
HETATM 3313 O  O   . HOH G 6 .   ? -13.27420 30.02575  5.61601   1.000 43.88853 ? 641 HOH A O   1 
HETATM 3314 O  O   . HOH G 6 .   ? 28.85110  -5.42638  6.25946   1.000 58.15488 ? 642 HOH A O   1 
HETATM 3315 O  O   . HOH G 6 .   ? 10.91436  0.65386   4.40310   1.000 20.76994 ? 643 HOH A O   1 
HETATM 3316 O  O   . HOH G 6 .   ? 10.75102  9.26239   -3.87433  1.000 49.28524 ? 644 HOH A O   1 
HETATM 3317 O  O   . HOH G 6 .   ? -1.46158  0.50710   23.63805  1.000 44.18104 ? 645 HOH A O   1 
HETATM 3318 O  O   . HOH G 6 .   ? 3.85095   -6.21641  -1.90257  1.000 34.56822 ? 646 HOH A O   1 
HETATM 3319 O  O   . HOH G 6 .   ? 20.92588  19.88924  9.25438   1.000 39.49566 ? 647 HOH A O   1 
HETATM 3320 O  O   . HOH G 6 .   ? -7.55994  -7.60354  2.45212   1.000 52.30606 ? 648 HOH A O   1 
HETATM 3321 O  O   . HOH G 6 .   ? 22.57819  11.80150  16.41700  1.000 24.07872 ? 649 HOH A O   1 
HETATM 3322 O  O   . HOH G 6 .   ? 4.99814   20.58164  0.19399   1.000 60.07815 ? 650 HOH A O   1 
HETATM 3323 O  O   . HOH G 6 .   ? -5.44451  31.01745  7.07220   1.000 45.43952 ? 651 HOH A O   1 
HETATM 3324 O  O   . HOH G 6 .   ? -1.62699  0.41166   0.69135   1.000 30.83159 ? 652 HOH A O   1 
HETATM 3325 O  O   . HOH G 6 .   ? 8.55108   -8.06889  30.48818  1.000 55.73568 ? 653 HOH A O   1 
HETATM 3326 O  O   . HOH G 6 .   ? 19.81258  -12.86911 26.43662  1.000 44.89097 ? 654 HOH A O   1 
HETATM 3327 O  O   . HOH G 6 .   ? 17.86602  3.61800   39.56731  1.000 50.85534 ? 655 HOH A O   1 
HETATM 3328 O  O   . HOH G 6 .   ? 5.98847   -0.33953  0.90461   1.000 20.73046 ? 656 HOH A O   1 
HETATM 3329 O  O   . HOH G 6 .   ? 3.65313   -9.41624  -4.76814  1.000 50.70233 ? 657 HOH A O   1 
HETATM 3330 O  O   . HOH G 6 .   ? -2.46226  27.77464  1.75621   1.000 28.69455 ? 658 HOH A O   1 
HETATM 3331 O  O   . HOH G 6 .   ? 1.74463   -26.37794 25.63990  1.000 45.91958 ? 659 HOH A O   1 
HETATM 3332 O  O   . HOH G 6 .   ? 7.35197   24.23386  31.01477  1.000 32.97787 ? 660 HOH A O   1 
HETATM 3333 O  O   . HOH G 6 .   ? 6.72821   -11.59152 23.00633  1.000 41.53427 ? 661 HOH A O   1 
HETATM 3334 O  O   . HOH G 6 .   ? 18.08568  23.42544  45.96592  1.000 62.90268 ? 662 HOH A O   1 
HETATM 3335 O  O   . HOH G 6 .   ? -12.69814 26.43048  8.52455   1.000 42.36372 ? 663 HOH A O   1 
HETATM 3336 O  O   . HOH G 6 .   ? 23.00196  -0.78911  30.52782  1.000 42.84346 ? 664 HOH A O   1 
HETATM 3337 O  O   . HOH G 6 .   ? 2.94848   17.94560  -7.34623  1.000 44.01651 ? 665 HOH A O   1 
HETATM 3338 O  O   . HOH G 6 .   ? 1.19473   -5.83444  25.45293  1.000 51.62354 ? 666 HOH A O   1 
HETATM 3339 O  O   . HOH G 6 .   ? 7.21785   10.29018  27.69715  1.000 44.47609 ? 667 HOH A O   1 
HETATM 3340 O  O   . HOH G 6 .   ? -0.44232  12.78784  -7.05286  1.000 33.85772 ? 668 HOH A O   1 
HETATM 3341 O  O   . HOH G 6 .   ? 7.24881   -4.11012  21.35270  1.000 43.36942 ? 669 HOH A O   1 
HETATM 3342 O  O   . HOH G 6 .   ? -5.68141  13.12246  -5.65545  1.000 53.95283 ? 670 HOH A O   1 
HETATM 3343 O  O   . HOH G 6 .   ? 12.00423  6.81434   0.66848   1.000 39.88554 ? 671 HOH A O   1 
HETATM 3344 O  O   . HOH G 6 .   ? 9.48327   -0.80136  20.61677  1.000 31.94185 ? 672 HOH A O   1 
HETATM 3345 O  O   . HOH G 6 .   ? 4.33456   1.31770   10.14347  1.000 36.25977 ? 673 HOH A O   1 
HETATM 3346 O  O   . HOH G 6 .   ? 30.88588  15.89758  33.93352  1.000 43.81564 ? 674 HOH A O   1 
HETATM 3347 O  O   . HOH G 6 .   ? -0.96464  -8.76330  19.50309  1.000 27.04825 ? 675 HOH A O   1 
HETATM 3348 O  O   . HOH G 6 .   ? 21.37945  15.45191  36.05818  1.000 43.96296 ? 676 HOH A O   1 
HETATM 3349 O  O   . HOH G 6 .   ? 12.21158  2.17929   17.13576  1.000 18.09649 ? 677 HOH A O   1 
HETATM 3350 O  O   . HOH G 6 .   ? -4.33377  6.87828   -1.45186  1.000 38.12516 ? 678 HOH A O   1 
HETATM 3351 O  O   . HOH G 6 .   ? 3.99507   27.85959  10.35182  1.000 46.58676 ? 679 HOH A O   1 
HETATM 3352 O  O   . HOH G 6 .   ? 30.46645  15.88354  17.52259  1.000 48.69322 ? 680 HOH A O   1 
HETATM 3353 O  O   . HOH G 6 .   ? -1.98620  1.91761   25.53821  1.000 55.52354 ? 681 HOH A O   1 
HETATM 3354 O  O   . HOH G 6 .   ? -12.94277 17.78647  15.99599  1.000 37.08780 ? 682 HOH A O   1 
HETATM 3355 O  O   . HOH G 6 .   ? 4.74213   10.26076  23.73059  1.000 35.37924 ? 683 HOH A O   1 
HETATM 3356 O  O   . HOH G 6 .   ? 7.77504   -3.90127  24.18351  1.000 31.03550 ? 684 HOH A O   1 
HETATM 3357 O  O   . HOH G 6 .   ? 21.90154  -9.02280  28.76074  1.000 47.01877 ? 685 HOH A O   1 
HETATM 3358 O  O   . HOH G 6 .   ? 20.84080  16.98528  33.65321  1.000 47.35754 ? 686 HOH A O   1 
HETATM 3359 O  O   . HOH G 6 .   ? -0.27422  3.71890   27.66867  1.000 38.63240 ? 687 HOH A O   1 
HETATM 3360 O  O   . HOH G 6 .   ? 25.30928  23.36255  24.94386  1.000 54.83759 ? 688 HOH A O   1 
HETATM 3361 O  O   . HOH G 6 .   ? 4.47695   20.81948  -6.45866  1.000 53.96864 ? 689 HOH A O   1 
HETATM 3362 O  O   . HOH G 6 .   ? -3.36574  -10.66003 2.31828   1.000 47.86151 ? 690 HOH A O   1 
HETATM 3363 O  O   . HOH G 6 .   ? 6.68556   -2.05394  2.81930   1.000 20.32241 ? 691 HOH A O   1 
HETATM 3364 O  O   . HOH G 6 .   ? 5.96794   -2.98856  -2.06148  1.000 30.22105 ? 692 HOH A O   1 
HETATM 3365 O  O   . HOH G 6 .   ? -13.78688 13.59927  22.15217  1.000 48.55139 ? 693 HOH A O   1 
HETATM 3366 O  O   . HOH G 6 .   ? 11.31434  1.24695   7.39841   1.000 21.46566 ? 694 HOH A O   1 
HETATM 3367 O  O   . HOH G 6 .   ? -8.19470  16.64346  -4.67437  1.000 50.36887 ? 695 HOH A O   1 
HETATM 3368 O  O   . HOH G 6 .   ? 26.84115  18.91833  21.21233  1.000 28.61393 ? 696 HOH A O   1 
HETATM 3369 O  O   . HOH G 6 .   ? 9.32338   -1.43677  3.74737   1.000 21.91536 ? 697 HOH A O   1 
HETATM 3370 O  O   . HOH G 6 .   ? 29.54605  7.19358   19.79357  1.000 42.31658 ? 698 HOH A O   1 
HETATM 3371 O  O   . HOH G 6 .   ? -7.60234  6.14683   24.00606  1.000 56.50272 ? 699 HOH A O   1 
HETATM 3372 O  O   . HOH G 6 .   ? 22.39043  9.67580   38.37061  1.000 31.62279 ? 700 HOH A O   1 
HETATM 3373 O  O   . HOH G 6 .   ? 1.89794   -23.72189 20.90706  1.000 46.79284 ? 701 HOH A O   1 
HETATM 3374 O  O   . HOH G 6 .   ? 10.69295  22.58375  8.06168   1.000 42.65738 ? 702 HOH A O   1 
HETATM 3375 O  O   . HOH G 6 .   ? 21.29160  13.77226  39.22556  1.000 40.97531 ? 703 HOH A O   1 
HETATM 3376 O  O   . HOH G 6 .   ? -1.79749  -3.40258  25.58828  1.000 40.35066 ? 704 HOH A O   1 
HETATM 3377 O  O   . HOH G 6 .   ? -7.10851  23.82534  -2.15949  1.000 26.13903 ? 705 HOH A O   1 
HETATM 3378 O  O   . HOH G 6 .   ? 28.44817  -9.43638  22.18944  1.000 44.01755 ? 706 HOH A O   1 
HETATM 3379 O  O   . HOH G 6 .   ? -1.41237  -11.17005 10.35193  1.000 48.31375 ? 707 HOH A O   1 
HETATM 3380 O  O   A HOH G 6 .   ? 27.41284  5.86381   16.41012  0.505 26.57292 ? 708 HOH A O   1 
HETATM 3381 O  O   B HOH G 6 .   ? 27.04556  6.15422   18.44813  0.495 28.85668 ? 708 HOH A O   1 
HETATM 3382 O  O   . HOH G 6 .   ? 2.06380   -4.11428  -2.72757  1.000 43.00048 ? 709 HOH A O   1 
HETATM 3383 O  O   . HOH G 6 .   ? -2.12655  28.31197  10.89252  1.000 27.63607 ? 710 HOH A O   1 
HETATM 3384 O  O   . HOH G 6 .   ? 32.47601  9.89678   33.85592  1.000 44.61987 ? 711 HOH A O   1 
HETATM 3385 O  O   . HOH G 6 .   ? 21.88541  24.71851  25.93619  1.000 42.24268 ? 712 HOH A O   1 
HETATM 3386 O  O   . HOH G 6 .   ? -10.55888 14.04259  26.25584  1.000 62.20835 ? 713 HOH A O   1 
HETATM 3387 O  O   . HOH G 6 .   ? 19.96316  -0.37018  9.17616   1.000 20.08417 ? 714 HOH A O   1 
HETATM 3388 O  O   . HOH G 6 .   ? -0.36441  -1.11663  -1.58256  1.000 34.05776 ? 715 HOH A O   1 
HETATM 3389 O  O   . HOH G 6 .   ? 6.26335   -1.91711  26.83132  1.000 24.32710 ? 716 HOH A O   1 
HETATM 3390 O  O   . HOH G 6 .   ? -1.67406  7.60246   -4.20671  1.000 59.95324 ? 717 HOH A O   1 
HETATM 3391 O  O   . HOH G 6 .   ? 6.55718   0.39862   20.06919  1.000 24.24320 ? 718 HOH A O   1 
HETATM 3392 O  O   . HOH G 6 .   ? 20.64545  22.49311  38.35538  1.000 32.82283 ? 719 HOH A O   1 
HETATM 3393 O  O   . HOH G 6 .   ? 15.12162  -7.15822  -0.08337  1.000 29.29972 ? 720 HOH A O   1 
HETATM 3394 O  O   . HOH G 6 .   ? 7.11927   1.59929   27.44317  1.000 22.59796 ? 721 HOH A O   1 
HETATM 3395 O  O   . HOH G 6 .   ? 17.13521  6.67770   36.40072  1.000 34.08082 ? 722 HOH A O   1 
HETATM 3396 O  O   . HOH G 6 .   ? 6.76862   13.77817  -7.15559  1.000 51.05331 ? 723 HOH A O   1 
HETATM 3397 O  O   . HOH G 6 .   ? 17.46981  30.37828  19.60097  1.000 39.21026 ? 724 HOH A O   1 
HETATM 3398 O  O   . HOH G 6 .   ? 17.05623  3.33039   11.40888  1.000 15.86660 ? 725 HOH A O   1 
HETATM 3399 O  O   . HOH G 6 .   ? -7.78904  24.75278  -8.43587  1.000 17.84603 ? 726 HOH A O   1 
HETATM 3400 O  O   . HOH G 6 .   ? -4.57968  29.36419  11.34564  1.000 54.15285 ? 727 HOH A O   1 
HETATM 3401 O  O   . HOH G 6 .   ? -5.09645  24.91178  23.92792  1.000 34.97945 ? 728 HOH A O   1 
HETATM 3402 O  O   . HOH G 6 .   ? 29.33766  12.31311  18.70306  1.000 28.35923 ? 729 HOH A O   1 
HETATM 3403 O  O   . HOH G 6 .   ? 8.26537   -21.90241 16.58727  1.000 37.17699 ? 730 HOH A O   1 
HETATM 3404 O  O   . HOH G 6 .   ? 3.37049   21.75523  -1.39196  1.000 43.85298 ? 731 HOH A O   1 
HETATM 3405 O  O   . HOH G 6 .   ? 13.42328  22.34486  1.14467   1.000 41.92021 ? 732 HOH A O   1 
HETATM 3406 O  O   . HOH G 6 .   ? 0.05531   10.40765  2.35637   1.000 24.14650 ? 733 HOH A O   1 
HETATM 3407 O  O   . HOH G 6 .   ? -4.47851  15.70342  -10.28385 1.000 47.50374 ? 734 HOH A O   1 
HETATM 3408 O  O   . HOH G 6 .   ? 22.11861  22.89428  21.37584  1.000 44.98736 ? 735 HOH A O   1 
HETATM 3409 O  O   . HOH G 6 .   ? -1.95162  5.85718   7.48958   1.000 33.84874 ? 736 HOH A O   1 
HETATM 3410 O  O   . HOH G 6 .   ? -4.16166  -22.75844 28.20009  1.000 51.47404 ? 737 HOH A O   1 
HETATM 3411 O  O   . HOH G 6 .   ? 2.51600   27.33846  3.21620   1.000 30.98199 ? 738 HOH A O   1 
HETATM 3412 O  O   . HOH G 6 .   ? 26.45400  11.87553  36.16438  1.000 37.73759 ? 739 HOH A O   1 
HETATM 3413 O  O   . HOH G 6 .   ? 19.68154  29.79531  18.99899  1.000 50.49552 ? 740 HOH A O   1 
HETATM 3414 O  O   . HOH G 6 .   ? 4.10044   14.16603  -5.92081  1.000 29.26905 ? 741 HOH A O   1 
HETATM 3415 O  O   . HOH G 6 .   ? 6.36671   7.22521   -7.32411  1.000 42.23271 ? 742 HOH A O   1 
HETATM 3416 O  O   . HOH G 6 .   ? -8.98679  16.34288  22.67899  1.000 33.99029 ? 743 HOH A O   1 
HETATM 3417 O  O   . HOH G 6 .   ? 7.10927   4.95564   -4.40281  1.000 42.49299 ? 744 HOH A O   1 
HETATM 3418 O  O   . HOH G 6 .   ? 8.26335   18.38715  -0.81114  1.000 39.28734 ? 745 HOH A O   1 
HETATM 3419 O  O   . HOH G 6 .   ? 4.76903   -8.75536  28.72406  1.000 49.78061 ? 746 HOH A O   1 
HETATM 3420 O  O   . HOH G 6 .   ? -8.02103  31.39047  -2.20664  1.000 36.27657 ? 747 HOH A O   1 
HETATM 3421 O  O   . HOH G 6 .   ? 0.31794   -22.33474 25.80200  1.000 57.43977 ? 748 HOH A O   1 
HETATM 3422 O  O   . HOH G 6 .   ? 31.50042  20.55919  28.57873  1.000 49.82766 ? 749 HOH A O   1 
HETATM 3423 O  O   . HOH G 6 .   ? 34.10141  13.16365  28.52154  1.000 41.65396 ? 750 HOH A O   1 
HETATM 3424 O  O   . HOH G 6 .   ? 14.05813  14.65008  9.12261   1.000 26.10355 ? 751 HOH A O   1 
HETATM 3425 O  O   . HOH G 6 .   ? 21.77636  14.34559  17.52513  1.000 25.13207 ? 752 HOH A O   1 
HETATM 3426 O  O   . HOH G 6 .   ? 7.82520   -14.82296 -4.62085  1.000 54.66563 ? 753 HOH A O   1 
HETATM 3427 O  O   . HOH G 6 .   ? -3.17871  -6.49349  22.43804  1.000 43.91401 ? 754 HOH A O   1 
HETATM 3428 O  O   . HOH G 6 .   ? 13.96280  15.67419  2.97501   1.000 40.61445 ? 755 HOH A O   1 
HETATM 3429 O  O   . HOH G 6 .   ? 11.58355  18.58170  25.46540  1.000 37.56580 ? 756 HOH A O   1 
HETATM 3430 O  O   . HOH G 6 .   ? 32.43179  -8.69612  26.28457  1.000 63.31420 ? 757 HOH A O   1 
HETATM 3431 O  O   . HOH G 6 .   ? -2.17368  9.13917   1.21136   1.000 27.80986 ? 758 HOH A O   1 
HETATM 3432 O  O   . HOH G 6 .   ? -0.64730  -18.42064 0.76176   1.000 48.87470 ? 759 HOH A O   1 
HETATM 3433 O  O   . HOH G 6 .   ? 14.43268  28.48035  13.28888  1.000 48.43378 ? 760 HOH A O   1 
HETATM 3434 O  O   . HOH G 6 .   ? -4.49048  27.93348  -0.15738  1.000 25.54041 ? 761 HOH A O   1 
HETATM 3435 O  O   . HOH G 6 .   ? 10.59483  -3.50240  23.75832  1.000 39.71571 ? 762 HOH A O   1 
HETATM 3436 O  O   . HOH G 6 .   ? 7.65233   22.81279  37.81725  1.000 37.97794 ? 763 HOH A O   1 
HETATM 3437 O  O   . HOH G 6 .   ? 3.14307   -1.42997  11.77536  1.000 44.98874 ? 764 HOH A O   1 
HETATM 3438 O  O   . HOH G 6 .   ? 3.53537   -17.34946 10.87948  1.000 40.72353 ? 765 HOH A O   1 
HETATM 3439 O  O   . HOH G 6 .   ? 5.34160   6.96039   35.57501  1.000 32.75477 ? 766 HOH A O   1 
HETATM 3440 O  O   . HOH G 6 .   ? 9.78390   -0.54517  10.36935  1.000 27.58703 ? 767 HOH A O   1 
HETATM 3441 O  O   . HOH G 6 .   ? 9.13281   24.40157  13.31236  1.000 45.18830 ? 768 HOH A O   1 
HETATM 3442 O  O   . HOH G 6 .   ? 11.02126  -1.97583  12.39492  1.000 23.34941 ? 769 HOH A O   1 
HETATM 3443 O  O   . HOH G 6 .   ? 17.07205  -2.00011  21.37994  1.000 20.19596 ? 770 HOH A O   1 
HETATM 3444 O  O   . HOH G 6 .   ? 15.83027  22.63110  1.60760   1.000 48.37841 ? 771 HOH A O   1 
HETATM 3445 O  O   . HOH G 6 .   ? -2.51265  20.21714  -12.85879 1.000 32.34023 ? 772 HOH A O   1 
HETATM 3446 O  O   . HOH G 6 .   ? 22.44287  -12.71065 16.22625  1.000 34.60128 ? 773 HOH A O   1 
HETATM 3447 O  O   . HOH G 6 .   ? 27.71954  -0.00286  13.82450  1.000 42.97930 ? 774 HOH A O   1 
HETATM 3448 O  O   . HOH G 6 .   ? -1.38424  -10.59792 0.88337   1.000 47.30993 ? 775 HOH A O   1 
HETATM 3449 O  O   . HOH G 6 .   ? -1.61685  17.94703  26.59057  1.000 37.19644 ? 776 HOH A O   1 
HETATM 3450 O  O   . HOH G 6 .   ? -1.59042  17.71657  -12.04366 1.000 37.74381 ? 777 HOH A O   1 
HETATM 3451 O  O   . HOH G 6 .   ? 5.73853   -0.29960  34.24864  1.000 30.87391 ? 778 HOH A O   1 
HETATM 3452 O  O   . HOH G 6 .   ? 12.07825  -4.69601  30.10370  1.000 23.77025 ? 779 HOH A O   1 
HETATM 3453 O  O   . HOH G 6 .   ? 2.96864   -0.46713  8.02538   1.000 42.86595 ? 780 HOH A O   1 
HETATM 3454 O  O   . HOH G 6 .   ? 0.03993   1.51556   -2.33346  1.000 31.40421 ? 781 HOH A O   1 
HETATM 3455 O  O   . HOH G 6 .   ? 13.82060  30.90182  24.77034  1.000 43.02689 ? 782 HOH A O   1 
HETATM 3456 O  O   . HOH G 6 .   ? 29.14471  -1.72107  18.59046  1.000 39.50709 ? 783 HOH A O   1 
HETATM 3457 O  O   . HOH G 6 .   ? -4.63584  6.23871   0.92055   1.000 48.31178 ? 784 HOH A O   1 
HETATM 3458 O  O   . HOH G 6 .   ? -5.33586  23.20553  -10.64306 1.000 25.18421 ? 785 HOH A O   1 
HETATM 3459 O  O   . HOH G 6 .   ? 1.25443   11.86441  29.28410  1.000 47.30149 ? 786 HOH A O   1 
HETATM 3460 O  O   . HOH G 6 .   ? 8.51822   -22.39543 28.31282  1.000 63.87290 ? 787 HOH A O   1 
HETATM 3461 O  O   . HOH G 6 .   ? 6.81287   21.93064  42.31071  1.000 55.39849 ? 788 HOH A O   1 
HETATM 3462 O  O   . HOH G 6 .   ? 20.72665  23.32447  23.73873  1.000 28.14479 ? 789 HOH A O   1 
HETATM 3463 O  O   . HOH G 6 .   ? -1.13739  -5.05405  0.05469   1.000 39.32437 ? 790 HOH A O   1 
HETATM 3464 O  O   . HOH G 6 .   ? 14.88746  -1.60562  23.32768  1.000 50.34583 ? 791 HOH A O   1 
HETATM 3465 O  O   . HOH G 6 .   ? -12.09117 -2.65796  20.82047  1.000 49.30355 ? 792 HOH A O   1 
HETATM 3466 O  O   . HOH G 6 .   ? -0.59919  -11.63253 22.06423  1.000 39.88680 ? 793 HOH A O   1 
HETATM 3467 O  O   . HOH G 6 .   ? 21.31291  5.85205   39.30795  1.000 55.52487 ? 794 HOH A O   1 
HETATM 3468 O  O   . HOH G 6 .   ? 25.20745  -0.75462  30.25013  1.000 47.56984 ? 795 HOH A O   1 
HETATM 3469 O  O   . HOH G 6 .   ? 20.29869  -11.60701 9.90382   1.000 34.52985 ? 796 HOH A O   1 
HETATM 3470 O  O   . HOH G 6 .   ? -4.19103  18.58223  26.74336  1.000 49.95872 ? 797 HOH A O   1 
HETATM 3471 O  O   . HOH G 6 .   ? 8.96516   -4.39093  3.79770   1.000 25.46225 ? 798 HOH A O   1 
HETATM 3472 O  O   . HOH G 6 .   ? 16.89394  10.21969  42.26640  1.000 43.27796 ? 799 HOH A O   1 
HETATM 3473 O  O   . HOH G 6 .   ? 12.25553  -0.50266  1.15056   1.000 30.74967 ? 800 HOH A O   1 
HETATM 3474 O  O   . HOH G 6 .   ? 3.18267   -16.60964 25.54556  1.000 49.97598 ? 801 HOH A O   1 
HETATM 3475 O  O   . HOH G 6 .   ? 28.77761  15.54600  35.89408  1.000 43.97906 ? 802 HOH A O   1 
HETATM 3476 O  O   . HOH G 6 .   ? 5.02297   -2.30997  32.40461  1.000 49.66314 ? 803 HOH A O   1 
HETATM 3477 O  O   . HOH G 6 .   ? 9.74867   -2.96603  0.82895   1.000 41.70154 ? 804 HOH A O   1 
HETATM 3478 O  O   . HOH G 6 .   ? -14.32960 -0.52531  21.76759  1.000 48.33257 ? 805 HOH A O   1 
HETATM 3479 O  O   . HOH G 6 .   ? 14.33583  26.06458  8.35942   1.000 57.51477 ? 806 HOH A O   1 
HETATM 3480 O  O   . HOH G 6 .   ? -8.40768  3.25541   25.16400  1.000 61.20556 ? 807 HOH A O   1 
HETATM 3481 O  O   . HOH G 6 .   ? 9.50161   -20.04578 15.08884  1.000 39.04919 ? 808 HOH A O   1 
HETATM 3482 O  O   . HOH G 6 .   ? -1.51658  -17.05880 4.58097   1.000 54.10485 ? 809 HOH A O   1 
HETATM 3483 O  O   . HOH G 6 .   ? 4.79249   -4.23603  16.90359  1.000 53.64266 ? 810 HOH A O   1 
HETATM 3484 O  O   . HOH G 6 .   ? 3.59209   6.90579   33.71274  1.000 42.42406 ? 811 HOH A O   1 
HETATM 3485 O  O   . HOH G 6 .   ? 8.81256   4.87801   -2.76513  1.000 34.36913 ? 812 HOH A O   1 
HETATM 3486 O  O   . HOH G 6 .   ? 19.98160  16.59507  12.49635  1.000 38.11963 ? 813 HOH A O   1 
HETATM 3487 O  O   . HOH G 6 .   ? -0.98986  29.87930  8.89287   1.000 48.51129 ? 814 HOH A O   1 
HETATM 3488 O  O   . HOH G 6 .   ? 5.45421   -2.13857  -4.63579  1.000 42.47320 ? 815 HOH A O   1 
HETATM 3489 O  O   . HOH G 6 .   ? -3.36535  -18.09353 12.79523  1.000 58.85422 ? 816 HOH A O   1 
HETATM 3490 O  O   . HOH G 6 .   ? 4.09700   23.99436  -2.93005  1.000 58.50055 ? 817 HOH A O   1 
HETATM 3491 O  O   . HOH G 6 .   ? 18.79131  -12.22514 5.59531   1.000 55.57674 ? 818 HOH A O   1 
HETATM 3492 O  O   . HOH G 6 .   ? 32.34024  20.16204  25.85137  1.000 43.17331 ? 819 HOH A O   1 
HETATM 3493 O  O   . HOH G 6 .   ? 20.96704  -16.76147 13.73442  1.000 43.91415 ? 820 HOH A O   1 
HETATM 3494 O  O   . HOH G 6 .   ? 3.40620   -3.81327  18.93633  1.000 61.26740 ? 821 HOH A O   1 
HETATM 3495 O  O   . HOH G 6 .   ? 14.36072  4.72796   19.74093  1.000 19.03372 ? 822 HOH A O   1 
HETATM 3496 O  O   . HOH G 6 .   ? 3.93501   -21.87312 10.58496  1.000 51.63967 ? 823 HOH A O   1 
HETATM 3497 O  O   . HOH G 6 .   ? 12.03976  -15.91164 -2.13864  1.000 41.09952 ? 824 HOH A O   1 
HETATM 3498 O  O   . HOH G 6 .   ? 17.86800  10.28758  39.59753  1.000 32.21055 ? 825 HOH A O   1 
HETATM 3499 O  O   . HOH G 6 .   ? -4.25017  14.48599  27.87284  1.000 52.43917 ? 826 HOH A O   1 
HETATM 3500 O  O   . HOH G 6 .   ? 27.36504  4.57342   35.03645  1.000 58.10501 ? 827 HOH A O   1 
HETATM 3501 O  O   . HOH G 6 .   ? -10.41314 15.86690  -2.74278  1.000 45.74497 ? 828 HOH A O   1 
HETATM 3502 O  O   . HOH G 6 .   ? -2.54845  13.96281  -14.28226 1.000 40.77969 ? 829 HOH A O   1 
HETATM 3503 O  O   . HOH G 6 .   ? 8.49217   -13.81328 23.81035  1.000 48.46656 ? 830 HOH A O   1 
HETATM 3504 O  O   . HOH G 6 .   ? 15.21414  7.17170   40.78817  1.000 48.79887 ? 831 HOH A O   1 
HETATM 3505 O  O   . HOH G 6 .   ? 31.95274  7.04887   29.68305  1.000 44.22725 ? 832 HOH A O   1 
HETATM 3506 O  O   . HOH G 6 .   ? 4.70164   -1.90822  30.22200  1.000 47.60910 ? 833 HOH A O   1 
HETATM 3507 O  O   . HOH G 6 .   ? 29.27160  7.30471   13.01386  1.000 66.15570 ? 834 HOH A O   1 
HETATM 3508 O  O   . HOH G 6 .   ? -0.72813  -23.08241 15.16606  1.000 44.02949 ? 835 HOH A O   1 
HETATM 3509 O  O   . HOH G 6 .   ? 16.09731  25.21793  2.94844   1.000 64.77043 ? 836 HOH A O   1 
HETATM 3510 O  O   . HOH G 6 .   ? -16.40523 9.77205   16.66405  1.000 49.63603 ? 837 HOH A O   1 
HETATM 3511 O  O   . HOH G 6 .   ? 23.54355  -9.99699  25.52837  1.000 49.85110 ? 838 HOH A O   1 
HETATM 3512 O  O   . HOH G 6 .   ? 7.03413   20.50929  -1.45651  1.000 53.84971 ? 839 HOH A O   1 
HETATM 3513 O  O   . HOH G 6 .   ? 5.36965   11.69305  26.21505  1.000 37.88225 ? 840 HOH A O   1 
HETATM 3514 O  O   . HOH G 6 .   ? 4.67706   7.16447   38.40285  1.000 56.99817 ? 841 HOH A O   1 
HETATM 3515 O  O   . HOH G 6 .   ? 9.26752   -21.81205 7.78975   1.000 49.59191 ? 842 HOH A O   1 
HETATM 3516 O  O   . HOH G 6 .   ? 4.39157   16.85013  -5.29755  1.000 32.85716 ? 843 HOH A O   1 
HETATM 3517 O  O   . HOH G 6 .   ? 4.20499   -16.39276 -4.41930  1.000 49.18850 ? 844 HOH A O   1 
HETATM 3518 O  O   . HOH G 6 .   ? 15.86801  4.27168   41.19147  1.000 55.52410 ? 845 HOH A O   1 
HETATM 3519 O  O   . HOH G 6 .   ? 30.20827  -3.49170  17.58827  1.000 47.51273 ? 846 HOH A O   1 
HETATM 3520 O  O   . HOH G 6 .   ? 2.58858   11.31724  27.15394  1.000 54.21872 ? 847 HOH A O   1 
HETATM 3521 O  O   . HOH G 6 .   ? 0.19632   -9.64019  23.61254  1.000 66.06824 ? 848 HOH A O   1 
HETATM 3522 O  O   . HOH G 6 .   ? 31.80514  0.14308   18.26169  1.000 44.99159 ? 849 HOH A O   1 
HETATM 3523 O  O   . HOH G 6 .   ? 18.64416  24.31396  37.78155  1.000 55.00493 ? 850 HOH A O   1 
HETATM 3524 O  O   . HOH G 6 .   ? 0.92441   -17.90526 23.09939  1.000 51.08242 ? 851 HOH A O   1 
HETATM 3525 O  O   . HOH G 6 .   ? 22.87890  22.67984  12.76725  1.000 42.12333 ? 852 HOH A O   1 
HETATM 3526 O  O   . HOH G 6 .   ? 19.40620  -13.96677 10.42575  1.000 41.62895 ? 853 HOH A O   1 
HETATM 3527 O  O   . HOH G 6 .   ? 6.88913   -21.04838 26.44106  1.000 47.86865 ? 854 HOH A O   1 
HETATM 3528 O  O   . HOH G 6 .   ? -7.48502  23.59851  22.90081  1.000 36.84440 ? 855 HOH A O   1 
HETATM 3529 O  O   . HOH G 6 .   ? -3.27549  -27.07312 27.20938  1.000 60.30682 ? 856 HOH A O   1 
HETATM 3530 O  O   . HOH G 6 .   ? 2.21275   -29.72942 26.26125  1.000 33.60275 ? 857 HOH A O   1 
HETATM 3531 O  O   . HOH G 6 .   ? 1.86360   27.88770  12.51672  1.000 46.83180 ? 858 HOH A O   1 
HETATM 3532 O  O   . HOH G 6 .   ? 8.55364   6.46892   -6.55348  1.000 52.36107 ? 859 HOH A O   1 
HETATM 3533 O  O   . HOH G 6 .   ? 11.63041  10.43265  -0.39537  1.000 44.37452 ? 860 HOH A O   1 
HETATM 3534 O  O   . HOH G 6 .   ? -13.34324 28.15414  1.41011   1.000 38.46994 ? 861 HOH A O   1 
HETATM 3535 O  O   . HOH G 6 .   ? -0.25840  8.03234   -7.07406  1.000 49.85125 ? 862 HOH A O   1 
HETATM 3536 O  O   . HOH G 6 .   ? -10.51569 21.09208  -2.84987  1.000 27.70668 ? 863 HOH A O   1 
HETATM 3537 O  O   . HOH G 6 .   ? -5.39173  3.38296   1.25832   1.000 37.85458 ? 864 HOH A O   1 
HETATM 3538 O  O   . HOH G 6 .   ? 27.85564  3.57671   32.90861  1.000 42.53009 ? 865 HOH A O   1 
HETATM 3539 O  O   . HOH G 6 .   ? 24.35374  -6.34596  3.06716   1.000 37.79705 ? 866 HOH A O   1 
HETATM 3540 O  O   . HOH G 6 .   ? 29.98478  -7.29947  16.68549  1.000 60.79580 ? 867 HOH A O   1 
HETATM 3541 O  O   . HOH G 6 .   ? 25.03543  -3.82222  2.43581   1.000 43.28344 ? 868 HOH A O   1 
HETATM 3542 O  O   . HOH G 6 .   ? 0.69847   -21.46257 1.69591   1.000 44.68751 ? 869 HOH A O   1 
HETATM 3543 O  O   . HOH G 6 .   ? -5.83795  -9.81494  0.71786   1.000 61.30851 ? 870 HOH A O   1 
HETATM 3544 O  O   . HOH G 6 .   ? -7.19889  21.04944  -10.87755 1.000 31.04281 ? 871 HOH A O   1 
HETATM 3545 O  O   . HOH G 6 .   ? 23.92871  16.85775  33.82828  1.000 52.84605 ? 872 HOH A O   1 
HETATM 3546 O  O   . HOH G 6 .   ? 16.97149  26.41383  49.60581  1.000 59.35102 ? 873 HOH A O   1 
HETATM 3547 O  O   . HOH G 6 .   ? -4.06354  13.14844  -9.78006  1.000 53.11279 ? 874 HOH A O   1 
HETATM 3548 O  O   . HOH G 6 .   ? -15.75749 0.41170   16.35172  1.000 62.14391 ? 875 HOH A O   1 
HETATM 3549 O  O   . HOH G 6 .   ? 13.63618  -13.23967 -4.68860  1.000 70.17524 ? 876 HOH A O   1 
HETATM 3550 O  O   . HOH G 6 .   ? -11.27432 4.59389   4.01037   1.000 59.50998 ? 877 HOH A O   1 
HETATM 3551 O  O   . HOH G 6 .   ? -2.04783  15.25724  26.36181  1.000 50.34555 ? 878 HOH A O   1 
HETATM 3552 O  O   . HOH G 6 .   ? 3.18625   28.26718  18.51814  1.000 46.19159 ? 879 HOH A O   1 
HETATM 3553 O  O   . HOH G 6 .   ? 1.46609   -30.05763 33.64107  1.000 58.29338 ? 880 HOH A O   1 
HETATM 3554 O  O   . HOH G 6 .   ? 20.92646  20.91574  11.98900  1.000 51.96268 ? 881 HOH A O   1 
HETATM 3555 O  O   . HOH G 6 .   ? 21.79619  -12.10049 7.22741   1.000 57.90360 ? 882 HOH A O   1 
HETATM 3556 O  O   . HOH G 6 .   ? -9.01330  23.13316  -4.10625  1.000 20.70147 ? 883 HOH A O   1 
HETATM 3557 O  O   . HOH G 6 .   ? 25.30478  1.21087   35.47074  1.000 60.36855 ? 884 HOH A O   1 
HETATM 3558 O  O   . HOH G 6 .   ? 20.88568  28.80612  16.61922  1.000 70.05748 ? 885 HOH A O   1 
HETATM 3559 O  O   . HOH G 6 .   ? 21.56700  14.81214  41.41579  1.000 60.82613 ? 886 HOH A O   1 
HETATM 3560 O  O   . HOH G 6 .   ? 19.17091  6.11028   40.26401  1.000 66.16231 ? 887 HOH A O   1 
HETATM 3561 O  O   . HOH G 6 .   ? 31.37285  18.43392  33.16296  1.000 51.93114 ? 888 HOH A O   1 
HETATM 3562 O  O   . HOH G 6 .   ? 0.79922   3.63324   30.70281  1.000 51.94902 ? 889 HOH A O   1 
HETATM 3563 O  O   . HOH G 6 .   ? 23.48806  -11.28747 22.54771  1.000 40.47314 ? 890 HOH A O   1 
HETATM 3564 O  O   . HOH G 6 .   ? 26.50526  14.44986  35.25117  1.000 40.36487 ? 891 HOH A O   1 
HETATM 3565 O  O   . HOH G 6 .   ? 1.51482   6.26570   -8.33226  1.000 43.83724 ? 892 HOH A O   1 
HETATM 3566 O  O   . HOH G 6 .   ? 27.26029  21.65514  21.63858  1.000 57.71499 ? 893 HOH A O   1 
HETATM 3567 O  O   . HOH G 6 .   ? 26.90011  25.46839  32.04198  1.000 56.18075 ? 894 HOH A O   1 
HETATM 3568 O  O   . HOH G 6 .   ? -3.86547  1.42539   -0.45733  1.000 43.91249 ? 895 HOH A O   1 
HETATM 3569 O  O   . HOH G 6 .   ? 6.78279   -7.32485  -5.25294  1.000 51.42409 ? 896 HOH A O   1 
HETATM 3570 O  O   . HOH G 6 .   ? 25.36967  21.93718  9.06025   1.000 58.25103 ? 897 HOH A O   1 
HETATM 3571 O  O   . HOH G 6 .   ? 10.58612  9.58254   -9.17422  1.000 56.50028 ? 898 HOH A O   1 
HETATM 3572 O  O   . HOH G 6 .   ? 33.35933  14.71677  34.49100  1.000 42.68905 ? 899 HOH A O   1 
HETATM 3573 O  O   . HOH G 6 .   ? 23.46880  13.92388  37.29101  1.000 48.86775 ? 900 HOH A O   1 
HETATM 3574 O  O   . HOH G 6 .   ? 3.66875   -27.23218 17.16433  1.000 35.15576 ? 901 HOH A O   1 
HETATM 3575 O  O   . HOH G 6 .   ? 22.58273  -12.23621 27.20800  1.000 59.19994 ? 902 HOH A O   1 
HETATM 3576 O  O   . HOH G 6 .   ? -2.72783  15.36673  -12.07314 1.000 40.11921 ? 903 HOH A O   1 
HETATM 3577 O  O   . HOH G 6 .   ? 17.35641  7.74900   38.94565  1.000 31.95272 ? 904 HOH A O   1 
HETATM 3578 O  O   . HOH G 6 .   ? -0.45946  29.10810  12.88077  1.000 39.74767 ? 905 HOH A O   1 
HETATM 3579 O  O   . HOH G 6 .   ? -18.40685 -29.84448 30.00255  1.000 67.97724 ? 906 HOH A O   1 
HETATM 3580 O  O   . HOH G 6 .   ? 1.08686   -32.10636 26.70121  1.000 36.44527 ? 907 HOH A O   1 
HETATM 3581 O  O   . HOH G 6 .   ? -2.43396  2.49263   -2.71183  1.000 43.10852 ? 908 HOH A O   1 
HETATM 3582 O  O   . HOH G 6 .   ? 21.16176  18.36435  13.68154  1.000 44.34409 ? 909 HOH A O   1 
HETATM 3583 O  O   . HOH G 6 .   ? 0.92696   -25.53550 33.84155  1.000 54.94585 ? 910 HOH A O   1 
HETATM 3584 O  O   . HOH G 6 .   ? 10.48133  18.80266  -2.58293  1.000 54.62227 ? 911 HOH A O   1 
HETATM 3585 O  O   . HOH G 6 .   ? 5.27630   7.58230   -9.75869  1.000 60.97970 ? 912 HOH A O   1 
HETATM 3586 O  O   . HOH G 6 .   ? -4.24339  -3.95473  23.96152  1.000 49.66730 ? 913 HOH A O   1 
HETATM 3587 O  O   . HOH G 6 .   ? 20.06370  17.11520  9.43446   1.000 43.56477 ? 914 HOH A O   1 
HETATM 3588 O  O   . HOH G 6 .   ? -9.71815  25.86106  13.28282  1.000 45.70521 ? 915 HOH A O   1 
HETATM 3589 O  O   . HOH G 6 .   ? -0.57063  -5.05979  -2.48111  1.000 47.62672 ? 916 HOH A O   1 
HETATM 3590 O  O   . HOH G 6 .   ? 4.86441   -6.17809  -5.74792  1.000 66.28953 ? 917 HOH A O   1 
HETATM 3591 O  O   . HOH G 6 .   ? -2.94436  31.83159  8.18329   1.000 43.71190 ? 918 HOH A O   1 
HETATM 3592 O  O   . HOH G 6 .   ? 1.20973   -24.95830 16.64997  1.000 39.14254 ? 919 HOH A O   1 
HETATM 3593 O  O   . HOH G 6 .   ? 10.70542  7.14032   -1.83144  1.000 44.76031 ? 920 HOH A O   1 
HETATM 3594 O  O   . HOH G 6 .   ? 2.91098   -27.23436 33.63631  1.000 55.67715 ? 921 HOH A O   1 
HETATM 3595 O  O   . HOH G 6 .   ? 27.93871  11.41582  38.73635  1.000 52.03222 ? 922 HOH A O   1 
HETATM 3596 O  O   . HOH G 6 .   ? -8.92340  18.90427  26.88119  1.000 64.94432 ? 923 HOH A O   1 
HETATM 3597 O  O   . HOH G 6 .   ? 28.81293  -2.48573  30.64005  1.000 51.71551 ? 924 HOH A O   1 
HETATM 3598 O  O   . HOH G 6 .   ? 23.33053  16.24932  16.54846  1.000 34.05123 ? 925 HOH A O   1 
HETATM 3599 O  O   . HOH G 6 .   ? 17.31902  21.92533  -0.23039  1.000 44.30053 ? 926 HOH A O   1 
HETATM 3600 O  O   . HOH G 6 .   ? 34.33338  7.55231   30.62817  1.000 58.36254 ? 927 HOH A O   1 
HETATM 3601 O  O   . HOH G 6 .   ? 19.10068  -7.23930  1.35295   1.000 49.82329 ? 928 HOH A O   1 
HETATM 3602 O  O   . HOH G 6 .   ? 31.08603  9.79705   19.80092  1.000 52.74554 ? 929 HOH A O   1 
HETATM 3603 O  O   . HOH G 6 .   ? 26.61833  18.57223  18.59042  1.000 56.53971 ? 930 HOH A O   1 
HETATM 3604 O  O   . HOH G 6 .   ? -3.08321  6.01618   -7.82877  1.000 54.59263 ? 931 HOH A O   1 
HETATM 3605 O  O   . HOH G 6 .   ? -1.89845  -23.58588 17.80265  1.000 34.97625 ? 932 HOH A O   1 
HETATM 3606 O  O   . HOH G 6 .   ? 1.72571   14.06352  -7.50741  1.000 46.65978 ? 933 HOH A O   1 
HETATM 3607 O  O   . HOH G 6 .   ? -3.52039  1.20606   -4.96142  1.000 49.11352 ? 934 HOH A O   1 
HETATM 3608 O  O   . HOH G 6 .   ? 11.31593  12.13028  -9.27033  1.000 66.57450 ? 935 HOH A O   1 
HETATM 3609 O  O   . HOH G 6 .   ? -16.40025 25.31394  6.65748   1.000 48.13374 ? 936 HOH A O   1 
HETATM 3610 O  O   . HOH G 6 .   ? 23.92177  8.59852   40.52801  1.000 57.43569 ? 937 HOH A O   1 
HETATM 3611 O  O   . HOH G 6 .   ? -3.69491  29.39617  -2.52134  1.000 29.35965 ? 938 HOH A O   1 
HETATM 3612 O  O   . HOH G 6 .   ? 15.07043  15.90111  0.23034   1.000 36.31363 ? 939 HOH A O   1 
HETATM 3613 O  O   . HOH G 6 .   ? 25.96877  -11.12873 22.12418  1.000 53.49497 ? 940 HOH A O   1 
HETATM 3614 O  O   . HOH G 6 .   ? 32.43575  10.11739  36.49485  1.000 55.45702 ? 941 HOH A O   1 
HETATM 3615 O  O   . HOH G 6 .   ? 8.03546   -1.57295  -0.71259  1.000 28.22437 ? 942 HOH A O   1 
HETATM 3616 O  O   . HOH G 6 .   ? 11.48576  26.83352  12.74036  1.000 62.00275 ? 943 HOH A O   1 
HETATM 3617 O  O   . HOH G 6 .   ? -10.62424 18.49466  -3.77275  1.000 42.65129 ? 944 HOH A O   1 
HETATM 3618 O  O   . HOH G 6 .   ? 23.79049  11.47041  36.77766  1.000 33.38195 ? 945 HOH A O   1 
HETATM 3619 O  O   . HOH G 6 .   ? 7.69040   -2.41277  -6.22521  1.000 42.04006 ? 946 HOH A O   1 
HETATM 3620 O  O   . HOH G 6 .   ? 28.46793  0.84579   1.98687   1.000 40.77513 ? 947 HOH A O   1 
HETATM 3621 O  O   . HOH G 6 .   ? 17.50844  17.26745  0.64187   1.000 46.55757 ? 948 HOH A O   1 
HETATM 3622 O  O   . HOH G 6 .   ? 10.20056  -1.08389  -2.57882  1.000 31.19044 ? 949 HOH A O   1 
HETATM 3623 O  O   . HOH G 6 .   ? 20.52851  11.02764  39.86453  1.000 33.74020 ? 950 HOH A O   1 
HETATM 3624 O  O   . HOH G 6 .   ? -12.09005 14.17610  -6.00385  1.000 47.22288 ? 951 HOH A O   1 
HETATM 3625 O  O   . HOH G 6 .   ? -7.80580  2.86222   1.60102   1.000 59.01666 ? 952 HOH A O   1 
HETATM 3626 O  O   . HOH G 6 .   ? 13.14479  11.21545  -4.29377  1.000 56.18716 ? 953 HOH A O   1 
HETATM 3627 O  O   . HOH G 6 .   ? -3.22076  5.08814   -3.18243  1.000 44.75930 ? 954 HOH A O   1 
HETATM 3628 O  O   . HOH G 6 .   ? -3.84722  -22.04346 17.01819  1.000 52.46641 ? 955 HOH A O   1 
HETATM 3629 O  O   . HOH G 6 .   ? -0.71190  -24.88745 23.59024  1.000 58.10284 ? 956 HOH A O   1 
HETATM 3630 O  O   . HOH G 6 .   ? -17.03012 -1.84018  18.23689  1.000 70.76965 ? 957 HOH A O   1 
HETATM 3631 O  O   . HOH G 6 .   ? -2.83897  -2.25371  28.05583  1.000 55.24006 ? 958 HOH A O   1 
HETATM 3632 O  O   . HOH G 6 .   ? 26.17748  -2.50609  -0.49714  1.000 51.29309 ? 959 HOH A O   1 
HETATM 3633 O  O   . HOH G 6 .   ? -5.44894  31.15762  -3.75212  1.000 33.42767 ? 960 HOH A O   1 
HETATM 3634 O  O   . HOH G 6 .   ? 8.23059   -5.20567  -7.02343  1.000 62.27388 ? 961 HOH A O   1 
HETATM 3635 O  O   . HOH G 6 .   ? -4.45059  11.69166  -11.67851 1.000 52.67739 ? 962 HOH A O   1 
HETATM 3636 O  O   . HOH G 6 .   ? -11.85865 22.48469  18.78533  1.000 67.95896 ? 963 HOH A O   1 
HETATM 3637 O  O   . HOH G 6 .   ? 29.57953  -0.35677  33.97229  1.000 62.89580 ? 964 HOH A O   1 
HETATM 3638 O  O   . HOH G 6 .   ? 9.95240   -1.28927  -5.27415  1.000 38.19927 ? 965 HOH A O   1 
HETATM 3639 O  O   . HOH G 6 .   ? 24.32818  15.30247  14.11428  1.000 46.07314 ? 966 HOH A O   1 
HETATM 3640 O  O   . HOH G 6 .   ? 20.59906  10.59963  42.54636  1.000 50.40558 ? 967 HOH A O   1 
HETATM 3641 O  O   . HOH G 6 .   ? -12.11214 17.28169  -5.66190  1.000 37.22266 ? 968 HOH A O   1 
HETATM 3642 O  O   . HOH G 6 .   ? -5.05403  36.22824  -3.31612  1.000 47.88660 ? 969 HOH A O   1 
HETATM 3643 O  O   . HOH G 6 .   ? -2.74596  32.82712  -9.24223  1.000 34.93100 ? 970 HOH A O   1 
HETATM 3644 O  O   . HOH G 6 .   ? -0.78134  34.26627  -9.60935  1.000 37.53658 ? 971 HOH A O   1 
HETATM 3645 O  O   . HOH G 6 .   ? -1.48528  36.33577  -11.01273 1.000 36.04613 ? 972 HOH A O   1 
HETATM 3646 O  O   . HOH G 6 .   ? -4.16783  36.69506  -11.61888 1.000 30.43525 ? 973 HOH A O   1 
HETATM 3647 O  O   . HOH G 6 .   ? -4.07650  40.75849  -13.28560 1.000 49.24477 ? 974 HOH A O   1 
HETATM 3648 O  O   . HOH G 6 .   ? -5.80352  38.49020  -18.04514 1.000 28.39941 ? 975 HOH A O   1 
HETATM 3649 O  O   . HOH G 6 .   ? -3.27973  38.17267  -19.47720 1.000 32.73397 ? 976 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 2   ? 0.76648 0.99261 1.11292 0.27184  -0.02410 0.13548  2   THR A N   
2    C  CA  . THR A 2   ? 0.80066 0.99682 1.11339 0.23331  -0.05062 0.13355  2   THR A CA  
3    C  C   . THR A 2   ? 0.90958 1.05521 1.10855 0.19172  -0.04899 0.08853  2   THR A C   
4    O  O   . THR A 2   ? 0.96283 1.10161 1.11161 0.18121  -0.05976 0.09302  2   THR A O   
5    C  CB  . THR A 2   ? 0.71842 0.91238 1.11336 0.21974  -0.05575 0.17159  2   THR A CB  
6    O  OG1 . THR A 2   ? 0.68452 0.89701 1.11426 0.21248  -0.04605 0.17716  2   THR A OG1 
7    C  CG2 . THR A 2   ? 0.69990 0.87294 1.10772 0.19157  -0.05834 0.18480  2   THR A CG2 
8    N  N   . ASP A 3   ? 0.92863 1.04138 1.09416 0.14512  -0.03254 0.04500  3   ASP A N   
9    C  CA  . ASP A 3   ? 0.94440 1.00256 1.06755 0.08101  -0.03508 0.01594  3   ASP A CA  
10   C  C   . ASP A 3   ? 0.86993 0.95331 0.98324 0.06950  -0.00409 -0.04062 3   ASP A C   
11   O  O   . ASP A 3   ? 0.89875 0.99191 0.98707 0.08316  -0.01022 -0.04824 3   ASP A O   
12   C  CB  . ASP A 3   ? 1.04167 1.01552 1.11482 0.01031  -0.07192 0.04101  3   ASP A CB  
13   C  CG  . ASP A 3   ? 1.13021 1.03375 1.14989 -0.05257 -0.10384 0.05926  3   ASP A CG  
14   O  OD1 . ASP A 3   ? 1.19688 1.04094 1.16170 -0.07621 -0.10627 0.07712  3   ASP A OD1 
15   O  OD2 . ASP A 3   ? 1.13296 1.04082 1.16237 -0.07854 -0.11769 0.05136  3   ASP A OD2 
16   N  N   . THR A 4   ? 0.75771 0.86405 0.88853 0.03150  0.03104  -0.09553 4   THR A N   
17   C  CA  . THR A 4   ? 0.60222 0.77879 0.79302 0.00425  0.07542  -0.15792 4   THR A CA  
18   C  C   . THR A 4   ? 0.52674 0.70327 0.73641 -0.02054 0.10315  -0.15939 4   THR A C   
19   O  O   . THR A 4   ? 0.53184 0.65487 0.74431 -0.05536 0.13704  -0.15295 4   THR A O   
20   C  CB  . THR A 4   ? 0.52243 0.73276 0.76016 0.01992  0.11180  -0.19957 4   THR A CB  
21   O  OG1 . THR A 4   ? 0.47238 0.72147 0.74030 -0.03285 0.11293  -0.23462 4   THR A OG1 
22   C  CG2 . THR A 4   ? 0.46440 0.63077 0.74127 0.14398  0.15266  -0.22392 4   THR A CG2 
23   N  N   . ALA A 5   ? 0.45849 0.63503 0.67446 -0.01683 0.10389  -0.17955 5   ALA A N   
24   C  CA  . ALA A 5   ? 0.51080 0.61534 0.63191 0.01733  0.08448  -0.16204 5   ALA A CA  
25   C  C   . ALA A 5   ? 0.57301 0.58531 0.59503 0.05847  0.08194  -0.12505 5   ALA A C   
26   O  O   . ALA A 5   ? 0.57547 0.56805 0.59015 0.13258  0.08558  -0.18777 5   ALA A O   
27   C  CB  . ALA A 5   ? 0.45495 0.60251 0.62760 -0.02599 0.10041  -0.13786 5   ALA A CB  
28   N  N   . THR A 6   ? 0.61667 0.58781 0.57023 0.02742  0.09577  -0.03661 6   THR A N   
29   C  CA  . THR A 6   ? 0.73834 0.61390 0.57067 -0.02104 0.08050  0.03236  6   THR A CA  
30   C  C   . THR A 6   ? 0.80337 0.57143 0.52619 0.00243  0.11397  0.06413  6   THR A C   
31   O  O   . THR A 6   ? 0.87941 0.59046 0.52638 0.02843  0.12885  0.13662  6   THR A O   
32   C  CB  . THR A 6   ? 0.77477 0.69578 0.60337 -0.06643 0.04929  0.09205  6   THR A CB  
33   O  OG1 . THR A 6   ? 0.84807 0.85101 0.63373 -0.08949 0.03514  0.06026  6   THR A OG1 
34   C  CG2 . THR A 6   ? 0.73978 0.60419 0.59849 -0.10001 0.04627  0.11175  6   THR A CG2 
35   N  N   . THR A 7   ? 0.71948 0.50459 0.47825 -0.03285 0.14255  0.01106  7   THR A N   
36   C  CA  . THR A 7   ? 0.66310 0.45322 0.43497 0.03195  0.13790  -0.03584 7   THR A CA  
37   C  C   . THR A 7   ? 0.61797 0.42507 0.38879 0.08179  0.13669  -0.01424 7   THR A C   
38   O  O   . THR A 7   ? 0.67243 0.50094 0.37690 0.07738  0.13066  0.02271  7   THR A O   
39   C  CB  . THR A 7   ? 0.71447 0.45929 0.44484 -0.00485 0.11216  -0.07576 7   THR A CB  
40   O  OG1 . THR A 7   ? 0.72566 0.49824 0.44222 0.02324  0.10844  -0.14493 7   THR A OG1 
41   C  CG2 . THR A 7   ? 0.74703 0.57758 0.45406 0.04267  0.10684  -0.04195 7   THR A CG2 
42   N  N   . PRO A 8   ? 0.50747 0.35401 0.38369 0.14469  0.10754  -0.00024 8   PRO A N   
43   C  CA  . PRO A 8   ? 0.44689 0.33523 0.37659 0.12895  0.08808  0.03309  8   PRO A CA  
44   C  C   . PRO A 8   ? 0.42657 0.27488 0.40009 0.09771  0.09951  0.06606  8   PRO A C   
45   O  O   . PRO A 8   ? 0.43619 0.36793 0.42641 0.06368  0.07107  0.10717  8   PRO A O   
46   C  CB  . PRO A 8   ? 0.45136 0.40678 0.38608 0.13759  0.04299  0.05577  8   PRO A CB  
47   C  CG  . PRO A 8   ? 0.45317 0.44302 0.40304 0.15904  0.04889  0.01099  8   PRO A CG  
48   C  CD  . PRO A 8   ? 0.43238 0.34752 0.39604 0.18983  0.10854  -0.02833 8   PRO A CD  
49   N  N   . GLN A 9   ? 0.41993 0.30120 0.39575 0.11921  0.11629  0.05081  9   GLN A N   
50   C  CA  . GLN A 9   ? 0.42763 0.28271 0.40860 0.10602  0.09528  0.03498  9   GLN A CA  
51   C  C   . GLN A 9   ? 0.44114 0.20670 0.35213 0.07592  0.01657  -0.01229 9   GLN A C   
52   O  O   . GLN A 9   ? 0.47946 0.26499 0.34345 0.05921  -0.01021 -0.02061 9   GLN A O   
53   C  CB  . GLN A 9   ? 0.42816 0.33604 0.46414 0.11137  0.16372  0.05403  9   GLN A CB  
54   C  CG  . GLN A 9   ? 0.44419 0.43499 0.52593 0.12909  0.16730  0.10523  9   GLN A CG  
55   C  CD  . GLN A 9   ? 0.46205 0.46303 0.57443 0.18141  0.17454  0.15900  9   GLN A CD  
56   O  OE1 . GLN A 9   ? 0.60017 0.43916 0.60044 0.21231  0.14830  0.14367  9   GLN A OE1 
57   N  NE2 . GLN A 9   ? 0.44375 0.46364 0.58368 0.12713  0.21460  0.20285  9   GLN A NE2 
58   N  N   . THR A 10  ? 0.41283 0.27399 0.31952 0.05430  0.02840  -0.01814 10  THR A N   
59   C  CA  . THR A 10  ? 0.39269 0.32226 0.28071 0.01486  0.00007  0.02830  10  THR A CA  
60   C  C   . THR A 10  ? 0.41012 0.23541 0.28967 0.04060  0.00678  0.05750  10  THR A C   
61   O  O   . THR A 10  ? 0.37835 0.26636 0.28933 0.01279  0.00201  -0.00126 10  THR A O   
62   C  CB  . THR A 10  ? 0.33039 0.41447 0.27312 0.02794  -0.02051 0.00071  10  THR A CB  
63   O  OG1 . THR A 10  ? 0.45062 0.51140 0.29583 0.02247  -0.01484 -0.05239 10  THR A OG1 
64   C  CG2 . THR A 10  ? 0.30826 0.48560 0.27844 0.05163  -0.01321 0.02377  10  THR A CG2 
65   N  N   . THR A 11  ? 0.46465 0.23745 0.31700 0.01530  -0.03522 0.08765  11  THR A N   
66   C  CA  . THR A 11  ? 0.49063 0.25043 0.34577 0.02949  -0.03720 0.06541  11  THR A CA  
67   C  C   . THR A 11  ? 0.56059 0.25927 0.35949 0.02246  0.01627  0.01537  11  THR A C   
68   O  O   . THR A 11  ? 0.50088 0.37733 0.39460 0.00887  0.04238  0.01335  11  THR A O   
69   C  CB  . THR A 11  ? 0.52942 0.27412 0.38568 0.01550  -0.06219 0.03492  11  THR A CB  
70   O  OG1 . THR A 11  ? 0.52284 0.37365 0.39846 -0.02624 -0.03075 0.07412  11  THR A OG1 
71   C  CG2 . THR A 11  ? 0.58960 0.26845 0.41056 0.09790  -0.06176 0.02991  11  THR A CG2 
72   N  N   . ASP A 12  ? 0.65659 0.18562 0.36349 -0.00186 0.05238  0.01527  12  ASP A N   
73   C  CA  . ASP A 12  ? 0.68321 0.27479 0.34752 0.01319  0.04751  0.01564  12  ASP A CA  
74   C  C   . ASP A 12  ? 0.70511 0.25331 0.34883 -0.01001 0.03171  0.00309  12  ASP A C   
75   O  O   . ASP A 12  ? 0.71213 0.35443 0.32854 -0.01393 0.03730  -0.00216 12  ASP A O   
76   C  CB  . ASP A 12  ? 0.65219 0.37141 0.37591 -0.01818 0.04445  -0.00284 12  ASP A CB  
77   C  CG  . ASP A 12  ? 0.62008 0.36329 0.39021 -0.06708 0.02897  -0.02399 12  ASP A CG  
78   O  OD1 . ASP A 12  ? 0.60164 0.23152 0.39567 -0.00005 0.05199  -0.01950 12  ASP A OD1 
79   O  OD2 . ASP A 12  ? 0.57061 0.43811 0.41193 -0.04216 0.04030  -0.01037 12  ASP A OD2 
80   N  N   . ALA A 13  ? 0.62674 0.22362 0.35235 -0.00544 0.01333  -0.02713 13  ALA A N   
81   C  CA  . ALA A 13  ? 0.59367 0.21892 0.36727 -0.06279 -0.01656 -0.00483 13  ALA A CA  
82   C  C   . ALA A 13  ? 0.56945 0.20287 0.38992 -0.10318 -0.03107 -0.00419 13  ALA A C   
83   O  O   . ALA A 13  ? 0.61794 0.19912 0.41816 -0.02237 -0.04690 0.01478  13  ALA A O   
84   C  CB  . ALA A 13  ? 0.57230 0.22497 0.35853 -0.12897 -0.05205 -0.00672 13  ALA A CB  
85   N  N   . PRO A 14  ? 0.57790 0.20033 0.36638 -0.09139 -0.00958 0.02558  14  PRO A N   
86   C  CA  . PRO A 14  ? 0.55268 0.20854 0.38314 -0.07202 -0.00990 0.01321  14  PRO A CA  
87   C  C   . PRO A 14  ? 0.51827 0.24832 0.39168 -0.04697 0.00964  0.02014  14  PRO A C   
88   O  O   . PRO A 14  ? 0.49267 0.24186 0.39536 -0.05931 -0.01150 0.00025  14  PRO A O   
89   C  CB  . PRO A 14  ? 0.51273 0.34850 0.38331 -0.11729 0.00090  0.04818  14  PRO A CB  
90   C  CG  . PRO A 14  ? 0.56249 0.38786 0.38171 -0.14447 -0.01904 0.02899  14  PRO A CG  
91   C  CD  . PRO A 14  ? 0.54202 0.29764 0.36023 -0.12615 -0.01629 0.02153  14  PRO A CD  
92   N  N   . ALA A 15  ? 0.46079 0.22354 0.39060 -0.02319 0.06768  0.05292  15  ALA A N   
93   C  CA  . ALA A 15  ? 0.46823 0.24395 0.37010 -0.08854 0.05783  0.05655  15  ALA A CA  
94   C  C   . ALA A 15  ? 0.52259 0.20335 0.35548 -0.08642 0.03354  0.05264  15  ALA A C   
95   O  O   . ALA A 15  ? 0.58366 0.26089 0.32741 -0.02200 0.07177  0.04242  15  ALA A O   
96   C  CB  . ALA A 15  ? 0.48475 0.29395 0.36707 -0.01964 0.04935  0.00999  15  ALA A CB  
97   N  N   . PHE A 16  ? 0.48516 0.20536 0.35141 -0.05701 0.02324  0.08975  16  PHE A N   
98   C  CA  . PHE A 16  ? 0.43430 0.22064 0.34377 -0.07343 0.05924  0.07463  16  PHE A CA  
99   C  C   . PHE A 16  ? 0.41991 0.21656 0.34926 0.00093  0.04100  0.05142  16  PHE A C   
100  O  O   . PHE A 16  ? 0.42688 0.31153 0.37266 -0.05829 0.01716  0.01819  16  PHE A O   
101  C  CB  . PHE A 16  ? 0.41934 0.19603 0.31384 -0.04991 0.05072  -0.00100 16  PHE A CB  
102  C  CG  . PHE A 16  ? 0.37699 0.20508 0.30579 -0.08265 0.03810  -0.00039 16  PHE A CG  
103  C  CD1 . PHE A 16  ? 0.35465 0.22754 0.30337 -0.02191 0.09059  0.06094  16  PHE A CD1 
104  C  CD2 . PHE A 16  ? 0.39812 0.25867 0.30487 -0.05037 0.03280  -0.00255 16  PHE A CD2 
105  C  CE1 . PHE A 16  ? 0.41461 0.26609 0.31793 -0.05738 0.02396  0.02245  16  PHE A CE1 
106  C  CE2 . PHE A 16  ? 0.40659 0.21436 0.29918 -0.00841 0.06603  -0.01447 16  PHE A CE2 
107  C  CZ  . PHE A 16  ? 0.42656 0.28948 0.31405 0.01588  0.01124  0.02096  16  PHE A CZ  
108  N  N   . PRO A 17  ? 0.46781 0.21599 0.34669 -0.00966 0.00604  0.03363  17  PRO A N   
109  C  CA  . PRO A 17  ? 0.40127 0.18749 0.32678 -0.04243 -0.03507 0.07256  17  PRO A CA  
110  C  C   . PRO A 17  ? 0.42280 0.21742 0.31566 -0.06169 -0.01665 0.07638  17  PRO A C   
111  O  O   . PRO A 17  ? 0.42791 0.34743 0.33294 -0.04949 -0.02109 0.04244  17  PRO A O   
112  C  CB  . PRO A 17  ? 0.38659 0.17584 0.34249 -0.00602 -0.04998 0.05450  17  PRO A CB  
113  C  CG  . PRO A 17  ? 0.47835 0.16565 0.36722 -0.03905 -0.00223 0.00120  17  PRO A CG  
114  C  CD  . PRO A 17  ? 0.46829 0.14952 0.37332 -0.03257 0.00645  0.03031  17  PRO A CD  
115  N  N   . SER A 18  ? 0.48448 0.27763 0.31823 -0.08167 -0.02610 0.03378  18  SER A N   
116  C  CA  . SER A 18  ? 0.54002 0.20999 0.32034 -0.06650 -0.05088 0.04680  18  SER A CA  
117  C  C   . SER A 18  ? 0.55406 0.23331 0.31498 -0.02723 -0.01701 0.03948  18  SER A C   
118  O  O   . SER A 18  ? 0.51668 0.24614 0.33107 -0.09424 0.02370  0.05331  18  SER A O   
119  C  CB  . SER A 18  ? 0.63870 0.29462 0.36349 0.02351  -0.05402 0.00798  18  SER A CB  
120  O  OG  . SER A 18  ? 0.71011 0.37856 0.38530 0.05741  -0.04791 0.04641  18  SER A OG  
121  N  N   . ASN A 19  ? 0.53586 0.27147 0.30881 -0.02057 -0.02342 0.06145  19  ASN A N   
122  C  CA  . ASN A 19  ? 0.49654 0.28546 0.28707 -0.00507 -0.01564 0.02589  19  ASN A CA  
123  C  C   . ASN A 19  ? 0.46945 0.28993 0.28326 0.00515  -0.00910 0.03353  19  ASN A C   
124  O  O   . ASN A 19  ? 0.47042 0.27969 0.29281 -0.00510 -0.01328 0.05520  19  ASN A O   
125  C  CB  . ASN A 19  ? 0.47793 0.34229 0.30558 -0.08415 0.00071  0.02230  19  ASN A CB  
126  C  CG  . ASN A 19  ? 0.48560 0.40737 0.32332 -0.12661 0.01741  0.07471  19  ASN A CG  
127  O  OD1 . ASN A 19  ? 0.53942 0.37695 0.33489 -0.04387 -0.00850 0.05710  19  ASN A OD1 
128  N  ND2 . ASN A 19  ? 0.55171 0.57847 0.34642 -0.10325 0.04213  0.12201  19  ASN A ND2 
129  N  N   . ARG A 20  ? 0.41813 0.29443 0.26945 0.00379  -0.00462 0.02161  20  ARG A N   
130  C  CA  . ARG A 20  ? 0.45072 0.29878 0.25864 -0.03352 0.03611  0.07980  20  ARG A CA  
131  C  C   . ARG A 20  ? 0.48248 0.32461 0.28804 -0.06791 -0.00319 0.03866  20  ARG A C   
132  O  O   . ARG A 20  ? 0.48038 0.44446 0.30218 -0.06027 0.02701  0.00204  20  ARG A O   
133  C  CB  . ARG A 20  ? 0.47203 0.25574 0.22360 -0.08851 0.08545  0.04686  20  ARG A CB  
134  C  CG  . ARG A 20  ? 0.49141 0.26183 0.21823 -0.02092 0.09250  0.08340  20  ARG A CG  
135  C  CD  . ARG A 20  ? 0.42894 0.24029 0.20958 -0.01500 0.10320  0.07808  20  ARG A CD  
136  N  NE  . ARG A 20  ? 0.36307 0.25211 0.22960 -0.01805 0.05128  0.05445  20  ARG A NE  
137  C  CZ  . ARG A 20  ? 0.34820 0.27574 0.25926 -0.03239 0.06911  0.06618  20  ARG A CZ  
138  N  NH1 . ARG A 20  ? 0.33923 0.25787 0.27171 -0.01629 0.03298  0.04935  20  ARG A NH1 
139  N  NH2 . ARG A 20  ? 0.30483 0.26708 0.26005 -0.00983 0.03626  0.03923  20  ARG A NH2 
140  N  N   . SER A 21  ? 0.44506 0.36958 0.29348 -0.06669 -0.03934 0.05566  21  SER A N   
141  C  CA  . SER A 21  ? 0.46389 0.41985 0.29189 -0.05003 -0.02232 0.08487  21  SER A CA  
142  C  C   . SER A 21  ? 0.42382 0.40900 0.29146 -0.03769 0.01419  0.07035  21  SER A C   
143  O  O   . SER A 21  ? 0.44112 0.54017 0.30459 -0.04289 0.00196  -0.00506 21  SER A O   
144  C  CB  . SER A 21  ? 0.52481 0.45644 0.32847 -0.08399 0.03143  0.10789  21  SER A CB  
145  O  OG  . SER A 21  ? 0.62099 0.45709 0.35801 -0.06568 0.03819  0.11768  21  SER A OG  
146  N  N   . CYS A 22  ? 0.39102 0.37103 0.28372 -0.06281 0.05005  0.07136  22  CYS A N   
147  C  CA  . CYS A 22  ? 0.44684 0.38294 0.29894 -0.08229 0.04452  0.07701  22  CYS A CA  
148  C  C   . CYS A 22  ? 0.44919 0.26143 0.30479 -0.01621 0.01996  0.03556  22  CYS A C   
149  O  O   . CYS A 22  ? 0.44132 0.28669 0.28646 -0.01380 0.00797  0.03907  22  CYS A O   
150  C  CB  . CYS A 22  ? 0.45363 0.42890 0.32155 -0.08836 -0.00686 0.07805  22  CYS A CB  
151  S  SG  . CYS A 22  ? 0.43461 0.42942 0.31498 -0.07135 -0.06141 0.10585  22  CYS A SG  
152  N  N   . PRO A 23  ? 0.40770 0.29391 0.32399 -0.00615 0.02410  -0.02957 23  PRO A N   
153  C  CA  . PRO A 23  ? 0.41507 0.22826 0.33567 0.01262  0.02925  0.00319  23  PRO A CA  
154  C  C   . PRO A 23  ? 0.40938 0.25375 0.30648 0.03473  -0.01151 0.02822  23  PRO A C   
155  O  O   . PRO A 23  ? 0.43575 0.28710 0.30778 -0.00309 -0.07283 0.05690  23  PRO A O   
156  C  CB  . PRO A 23  ? 0.48187 0.30235 0.36320 0.02794  0.04130  -0.04051 23  PRO A CB  
157  C  CG  . PRO A 23  ? 0.52033 0.32660 0.38274 0.02154  0.00441  -0.06551 23  PRO A CG  
158  C  CD  . PRO A 23  ? 0.44480 0.33042 0.35308 -0.06339 0.03330  -0.04583 23  PRO A CD  
159  N  N   . TYR A 24  ? 0.35740 0.22973 0.28584 0.01722  0.02034  0.01799  24  TYR A N   
160  C  CA  . TYR A 24  ? 0.34946 0.22464 0.27274 -0.02490 0.00210  -0.00698 24  TYR A CA  
161  C  C   . TYR A 24  ? 0.35416 0.27912 0.28272 0.00100  -0.02269 0.00358  24  TYR A C   
162  O  O   . TYR A 24  ? 0.36647 0.30534 0.29746 0.00258  0.00042  -0.02542 24  TYR A O   
163  C  CB  . TYR A 24  ? 0.38800 0.26210 0.24184 -0.07208 -0.01831 0.02187  24  TYR A CB  
164  C  CG  . TYR A 24  ? 0.37387 0.28585 0.21417 -0.00395 -0.00766 0.05316  24  TYR A CG  
165  C  CD1 . TYR A 24  ? 0.36802 0.34064 0.23068 -0.00117 -0.00447 0.06218  24  TYR A CD1 
166  C  CD2 . TYR A 24  ? 0.37827 0.32541 0.19639 -0.02767 -0.01300 0.04451  24  TYR A CD2 
167  C  CE1 . TYR A 24  ? 0.45793 0.29377 0.22254 0.09202  -0.03688 0.00711  24  TYR A CE1 
168  C  CE2 . TYR A 24  ? 0.42557 0.31152 0.20096 0.02190  -0.03916 0.06300  24  TYR A CE2 
169  C  CZ  . TYR A 24  ? 0.45079 0.33863 0.21215 0.08448  -0.07829 0.00761  24  TYR A CZ  
170  O  OH  . TYR A 24  ? 0.53546 0.40958 0.23026 0.07821  -0.08893 0.01033  24  TYR A OH  
171  N  N   . GLN A 25  ? 0.36583 0.22123 0.27983 -0.00154 -0.02058 -0.00198 25  GLN A N   
172  C  CA  A GLN A 25  ? 0.42832 0.23782 0.30746 -0.01252 -0.03303 0.01129  25  GLN A CA  
173  C  CA  B GLN A 25  ? 0.43086 0.25928 0.31170 0.02165  -0.02786 0.01440  25  GLN A CA  
174  C  C   . GLN A 25  ? 0.41940 0.25423 0.31080 0.01501  -0.01153 0.01910  25  GLN A C   
175  O  O   . GLN A 25  ? 0.35872 0.30854 0.32359 0.04740  -0.04565 0.03990  25  GLN A O   
176  C  CB  A GLN A 25  ? 0.45018 0.26803 0.32554 -0.01065 -0.07923 0.01998  25  GLN A CB  
177  C  CB  B GLN A 25  ? 0.47706 0.30814 0.33733 0.07179  -0.05982 0.03439  25  GLN A CB  
178  C  CG  A GLN A 25  ? 0.47651 0.27787 0.34579 -0.02369 -0.08083 0.00921  25  GLN A CG  
179  C  CG  B GLN A 25  ? 0.53161 0.35554 0.35911 0.10487  -0.06068 0.02924  25  GLN A CG  
180  C  CD  A GLN A 25  ? 0.41077 0.29184 0.33020 0.00649  -0.08358 -0.01033 25  GLN A CD  
181  C  CD  B GLN A 25  ? 0.53451 0.41277 0.36894 0.16569  -0.06272 0.01497  25  GLN A CD  
182  O  OE1 A GLN A 25  ? 0.39257 0.38577 0.30726 0.09370  -0.06208 0.05348  25  GLN A OE1 
183  O  OE1 B GLN A 25  ? 0.55316 0.37203 0.37257 0.19131  -0.04784 0.00625  25  GLN A OE1 
184  N  NE2 A GLN A 25  ? 0.44905 0.28265 0.33544 -0.10033 -0.10388 -0.05944 25  GLN A NE2 
185  N  NE2 B GLN A 25  ? 0.52384 0.44450 0.35562 0.23738  -0.08104 0.02990  25  GLN A NE2 
186  N  N   . LEU A 26  ? 0.45627 0.28543 0.30431 -0.01467 0.03109  -0.00272 26  LEU A N   
187  C  CA  . LEU A 26  ? 0.46834 0.32209 0.31190 -0.06558 0.08833  -0.00729 26  LEU A CA  
188  C  C   . LEU A 26  ? 0.52189 0.33872 0.29519 -0.04369 0.06090  0.01131  26  LEU A C   
189  O  O   . LEU A 26  ? 0.55003 0.38380 0.30667 -0.02299 0.06333  0.03027  26  LEU A O   
190  C  CB  . LEU A 26  ? 0.51656 0.31789 0.33731 -0.04791 0.12072  -0.00897 26  LEU A CB  
191  C  CG  . LEU A 26  ? 0.51656 0.31718 0.36047 -0.04349 0.13398  -0.01184 26  LEU A CG  
192  C  CD1 . LEU A 26  ? 0.57336 0.30547 0.37225 -0.03744 0.15932  -0.01540 26  LEU A CD1 
193  C  CD2 . LEU A 26  ? 0.55535 0.39499 0.37969 -0.07160 0.08442  -0.00044 26  LEU A CD2 
194  N  N   . PRO A 27  ? 0.50974 0.30033 0.30843 -0.06548 0.05830  0.02011  27  PRO A N   
195  C  CA  . PRO A 27  ? 0.54516 0.32370 0.32914 -0.11370 0.05243  0.04129  27  PRO A CA  
196  C  C   . PRO A 27  ? 0.61828 0.29701 0.33236 -0.16995 0.04187  0.07895  27  PRO A C   
197  O  O   . PRO A 27  ? 0.66588 0.35318 0.32942 -0.11123 0.00028  0.05982  27  PRO A O   
198  C  CB  . PRO A 27  ? 0.54251 0.33944 0.33026 -0.05618 0.01060  0.05889  27  PRO A CB  
199  C  CG  . PRO A 27  ? 0.51568 0.34450 0.33636 -0.09612 0.02580  0.04668  27  PRO A CG  
200  C  CD  . PRO A 27  ? 0.50377 0.28199 0.31666 -0.10208 0.04678  0.02460  27  PRO A CD  
201  N  N   . ASP A 28  ? 0.69502 0.36110 0.33560 -0.13355 0.02535  0.09953  28  ASP A N   
202  C  CA  . ASP A 28  ? 0.75219 0.50737 0.36298 -0.13739 0.01535  0.13454  28  ASP A CA  
203  C  C   . ASP A 28  ? 0.75468 0.48646 0.35890 -0.18513 -0.00214 0.12794  28  ASP A C   
204  O  O   . ASP A 28  ? 0.76263 0.46821 0.37013 -0.21260 0.01010  0.12801  28  ASP A O   
205  C  CB  . ASP A 28  ? 0.79681 0.62584 0.38485 -0.20108 0.06097  0.17323  28  ASP A CB  
206  C  CG  . ASP A 28  ? 0.89205 0.87378 0.44058 -0.21426 0.07011  0.17778  28  ASP A CG  
207  O  OD1 . ASP A 28  ? 0.93985 0.94633 0.45761 -0.22618 0.09997  0.19316  28  ASP A OD1 
208  O  OD2 . ASP A 28  ? 0.89480 0.95286 0.45488 -0.22730 0.05524  0.19277  28  ASP A OD2 
209  N  N   . GLY A 29  ? 0.72841 0.41996 0.34556 -0.19161 -0.04049 0.14487  29  GLY A N   
210  C  CA  . GLY A 29  ? 0.69238 0.31089 0.35668 -0.18708 -0.03216 0.09667  29  GLY A CA  
211  C  C   . GLY A 29  ? 0.64319 0.30122 0.36793 -0.16350 0.00743  0.10150  29  GLY A C   
212  O  O   . GLY A 29  ? 0.63311 0.38304 0.38360 -0.09564 0.08457  0.09740  29  GLY A O   
213  N  N   . TYR A 30  ? 0.57431 0.26215 0.36855 -0.13977 -0.02656 0.08512  30  TYR A N   
214  C  CA  . TYR A 30  ? 0.59953 0.27311 0.34241 -0.09791 -0.01973 0.06017  30  TYR A CA  
215  C  C   . TYR A 30  ? 0.61122 0.26444 0.35564 -0.05859 -0.04548 0.05113  30  TYR A C   
216  O  O   . TYR A 30  ? 0.59315 0.27432 0.35953 -0.09854 -0.05116 0.04547  30  TYR A O   
217  C  CB  . TYR A 30  ? 0.57513 0.27011 0.32116 -0.06965 -0.00849 0.04008  30  TYR A CB  
218  C  CG  . TYR A 30  ? 0.56935 0.28311 0.29894 -0.06992 0.00348  0.03455  30  TYR A CG  
219  C  CD1 . TYR A 30  ? 0.51388 0.30579 0.28782 -0.11907 0.02225  0.01091  30  TYR A CD1 
220  C  CD2 . TYR A 30  ? 0.58140 0.26694 0.28738 -0.03469 0.01642  0.03512  30  TYR A CD2 
221  C  CE1 . TYR A 30  ? 0.46555 0.32657 0.29630 -0.11225 0.01673  -0.00018 30  TYR A CE1 
222  C  CE2 . TYR A 30  ? 0.49139 0.27690 0.28206 -0.06133 0.02447  -0.01182 30  TYR A CE2 
223  C  CZ  . TYR A 30  ? 0.49452 0.31691 0.29389 -0.11205 0.01041  0.00588  30  TYR A CZ  
224  O  OH  . TYR A 30  ? 0.53523 0.30148 0.32303 -0.11744 0.01434  0.05975  30  TYR A OH  
225  N  N   . ALA A 31  ? 0.62809 0.29670 0.38683 -0.05081 -0.07683 0.07552  31  ALA A N   
226  C  CA  . ALA A 31  ? 0.64095 0.32607 0.38462 0.00346  -0.13097 0.11739  31  ALA A CA  
227  C  C   . ALA A 31  ? 0.64783 0.32507 0.40420 -0.03543 -0.09048 0.13035  31  ALA A C   
228  O  O   . ALA A 31  ? 0.61894 0.31780 0.36692 -0.02852 -0.11884 0.09441  31  ALA A O   
229  C  CB  . ALA A 31  ? 0.64162 0.37974 0.36762 -0.02177 -0.16482 0.08839  31  ALA A CB  
230  N  N   . GLN A 32  ? 0.61745 0.31912 0.44134 -0.10917 -0.03192 0.14289  32  GLN A N   
231  C  CA  A GLN A 32  ? 0.61380 0.35179 0.44822 -0.08750 -0.01157 0.12956  32  GLN A CA  
232  C  CA  B GLN A 32  ? 0.61459 0.34875 0.46040 -0.08007 -0.00523 0.12575  32  GLN A CA  
233  C  C   . GLN A 32  ? 0.61384 0.33202 0.44791 -0.02452 -0.02722 0.11511  32  GLN A C   
234  O  O   . GLN A 32  ? 0.66008 0.29775 0.46379 0.02776  -0.03856 0.09901  32  GLN A O   
235  C  CB  A GLN A 32  ? 0.61235 0.37671 0.44926 -0.10896 0.01942  0.12382  32  GLN A CB  
236  C  CB  B GLN A 32  ? 0.60883 0.36239 0.48560 -0.08988 0.02879  0.10795  32  GLN A CB  
237  C  CG  A GLN A 32  ? 0.62981 0.37902 0.44959 -0.11623 0.05226  0.13873  32  GLN A CG  
238  C  CG  B GLN A 32  ? 0.61911 0.35677 0.50684 -0.07259 0.05261  0.10631  32  GLN A CG  
239  C  CD  A GLN A 32  ? 0.66972 0.43353 0.45243 -0.04281 0.06426  0.14644  32  GLN A CD  
240  C  CD  B GLN A 32  ? 0.65977 0.35907 0.51842 -0.03698 0.07039  0.09653  32  GLN A CD  
241  O  OE1 A GLN A 32  ? 0.69933 0.45974 0.45986 -0.05247 0.06827  0.13336  32  GLN A OE1 
242  O  OE1 B GLN A 32  ? 0.68536 0.33841 0.52367 0.01355  0.04057  0.05951  32  GLN A OE1 
243  N  NE2 A GLN A 32  ? 0.67538 0.44541 0.45409 -0.01164 0.05296  0.13555  32  GLN A NE2 
244  N  NE2 B GLN A 32  ? 0.65862 0.36241 0.52225 -0.09158 0.11074  0.13513  32  GLN A NE2 
245  N  N   . LEU A 33  ? 0.54563 0.28499 0.41204 -0.03292 -0.05671 0.11909  33  LEU A N   
246  C  CA  . LEU A 33  ? 0.51644 0.22330 0.40552 0.01818  -0.03578 0.05605  33  LEU A CA  
247  C  C   . LEU A 33  ? 0.46489 0.26588 0.43959 0.02114  -0.06011 0.00731  33  LEU A C   
248  O  O   . LEU A 33  ? 0.47301 0.24220 0.47967 0.03501  -0.07510 -0.02047 33  LEU A O   
249  C  CB  . LEU A 33  ? 0.50639 0.27658 0.37319 0.04036  -0.00919 0.01910  33  LEU A CB  
250  C  CG  . LEU A 33  ? 0.51644 0.26304 0.37055 0.04439  0.04438  -0.02646 33  LEU A CG  
251  C  CD1 . LEU A 33  ? 0.49100 0.23836 0.35964 0.02760  0.08090  -0.01399 33  LEU A CD1 
252  C  CD2 . LEU A 33  ? 0.55242 0.24948 0.39755 -0.08829 0.05187  -0.05542 33  LEU A CD2 
253  N  N   . ARG A 34  ? 0.46006 0.26661 0.43932 0.00762  -0.07218 -0.00268 34  ARG A N   
254  C  CA  . ARG A 34  ? 0.48917 0.25543 0.43599 -0.00323 -0.10100 -0.01553 34  ARG A CA  
255  C  C   . ARG A 34  ? 0.55298 0.27100 0.47069 0.06226  -0.10504 -0.00486 34  ARG A C   
256  O  O   . ARG A 34  ? 0.52348 0.24875 0.45771 0.04323  -0.09427 0.01804  34  ARG A O   
257  C  CB  . ARG A 34  ? 0.42192 0.21120 0.40066 -0.05842 -0.06888 -0.04024 34  ARG A CB  
258  C  CG  . ARG A 34  ? 0.39458 0.23474 0.37745 0.02178  -0.06641 0.01543  34  ARG A CG  
259  C  CD  . ARG A 34  ? 0.44022 0.24986 0.35222 0.05788  -0.09978 0.04944  34  ARG A CD  
260  N  NE  . ARG A 34  ? 0.51384 0.27927 0.35423 0.01302  -0.11593 0.05036  34  ARG A NE  
261  C  CZ  . ARG A 34  ? 0.53374 0.27222 0.33905 0.04787  -0.09901 0.05958  34  ARG A CZ  
262  N  NH1 . ARG A 34  ? 0.58202 0.26940 0.33887 0.03806  -0.08811 0.06566  34  ARG A NH1 
263  N  NH2 . ARG A 34  ? 0.60224 0.28142 0.33940 -0.03552 -0.04570 0.12287  34  ARG A NH2 
264  N  N   . ASP A 35  ? 0.62388 0.23758 0.50211 0.10306  -0.12178 0.02846  35  ASP A N   
265  C  CA  . ASP A 35  ? 0.63772 0.27788 0.51780 0.16408  -0.12719 0.04780  35  ASP A CA  
266  C  C   . ASP A 35  ? 0.62685 0.34452 0.54785 0.12908  -0.10371 0.03490  35  ASP A C   
267  O  O   . ASP A 35  ? 0.67812 0.35962 0.58508 0.07960  -0.09702 -0.01394 35  ASP A O   
268  C  CB  . ASP A 35  ? 0.74367 0.29620 0.49047 0.14550  -0.13650 0.07433  35  ASP A CB  
269  C  CG  . ASP A 35  ? 0.84442 0.29900 0.48437 0.10438  -0.11895 0.09815  35  ASP A CG  
270  O  OD1 . ASP A 35  ? 0.90304 0.27014 0.48784 0.06929  -0.10570 0.07239  35  ASP A OD1 
271  O  OD2 . ASP A 35  ? 0.84430 0.31057 0.45462 0.07270  -0.12237 0.09524  35  ASP A OD2 
272  N  N   . THR A 36  ? 0.59470 0.31978 0.53560 0.01407  -0.09150 0.05613  36  THR A N   
273  C  CA  . THR A 36  ? 0.61260 0.38664 0.53748 0.04919  -0.08681 0.04495  36  THR A CA  
274  C  C   . THR A 36  ? 0.58897 0.37957 0.53554 0.08956  -0.06432 0.02646  36  THR A C   
275  O  O   . THR A 36  ? 0.64573 0.39164 0.53328 0.16118  -0.08591 0.03628  36  THR A O   
276  C  CB  . THR A 36  ? 0.64658 0.49216 0.56183 0.01952  -0.09173 0.02205  36  THR A CB  
277  O  OG1 . THR A 36  ? 0.72185 0.62723 0.58231 -0.01439 -0.08990 -0.04840 36  THR A OG1 
278  C  CG2 . THR A 36  ? 0.63183 0.45313 0.56506 -0.02763 -0.08292 0.00808  36  THR A CG2 
279  N  N   . PRO A 37  ? 0.54667 0.29452 0.51870 0.15672  -0.02952 0.00939  37  PRO A N   
280  C  CA  . PRO A 37  ? 0.54810 0.30749 0.51365 0.13083  -0.03286 0.03268  37  PRO A CA  
281  C  C   . PRO A 37  ? 0.57464 0.35212 0.49874 0.08665  -0.00123 0.02556  37  PRO A C   
282  O  O   . PRO A 37  ? 0.57491 0.33995 0.51318 0.04652  -0.02215 -0.00342 37  PRO A O   
283  C  CB  . PRO A 37  ? 0.55477 0.34376 0.52016 0.07773  -0.04634 0.05904  37  PRO A CB  
284  C  CG  . PRO A 37  ? 0.53831 0.34412 0.52715 0.12183  -0.04362 0.07980  37  PRO A CG  
285  C  CD  . PRO A 37  ? 0.49930 0.29996 0.51706 0.20486  -0.04475 0.05610  37  PRO A CD  
286  N  N   . GLY A 38  ? 0.55180 0.32628 0.48223 0.10882  -0.00689 -0.00712 38  GLY A N   
287  C  CA  . GLY A 38  ? 0.51835 0.28890 0.45250 0.12422  0.00901  -0.03408 38  GLY A CA  
288  C  C   . GLY A 38  ? 0.44744 0.27450 0.43172 0.13121  -0.00985 -0.02760 38  GLY A C   
289  O  O   . GLY A 38  ? 0.45601 0.25022 0.43769 0.05782  0.00390  -0.01690 38  GLY A O   
290  N  N   . PRO A 39  ? 0.39302 0.29006 0.40885 0.08620  -0.02286 -0.01577 39  PRO A N   
291  C  CA  . PRO A 39  ? 0.34095 0.26883 0.38224 0.06006  0.00403  0.01274  39  PRO A CA  
292  C  C   . PRO A 39  ? 0.31931 0.19700 0.36221 0.04901  0.01337  0.00303  39  PRO A C   
293  O  O   . PRO A 39  ? 0.35464 0.18515 0.35842 0.10167  -0.02306 0.00354  39  PRO A O   
294  C  CB  . PRO A 39  ? 0.38185 0.32605 0.39589 0.04865  -0.00363 0.05382  39  PRO A CB  
295  C  CG  . PRO A 39  ? 0.41155 0.42484 0.40501 0.09088  -0.01354 0.00618  39  PRO A CG  
296  C  CD  . PRO A 39  ? 0.40145 0.35910 0.40283 0.06502  0.00821  -0.00149 39  PRO A CD  
297  N  N   . LEU A 40  ? 0.38199 0.20059 0.37478 -0.01517 -0.01459 -0.00578 40  LEU A N   
298  C  CA  . LEU A 40  ? 0.31126 0.21897 0.36936 0.03794  -0.01148 0.01019  40  LEU A CA  
299  C  C   . LEU A 40  ? 0.37593 0.25439 0.40124 0.09187  -0.00995 0.00670  40  LEU A C   
300  O  O   . LEU A 40  ? 0.42955 0.30743 0.43260 0.10231  -0.03782 -0.00520 40  LEU A O   
301  C  CB  . LEU A 40  ? 0.32098 0.22709 0.35835 0.01896  -0.03800 0.01665  40  LEU A CB  
302  C  CG  . LEU A 40  ? 0.41058 0.22792 0.33878 -0.08609 -0.03761 0.00757  40  LEU A CG  
303  C  CD1 . LEU A 40  ? 0.47399 0.27847 0.35777 -0.08778 -0.02654 -0.01385 40  LEU A CD1 
304  C  CD2 . LEU A 40  ? 0.40884 0.28108 0.34413 -0.02951 -0.08337 0.00186  40  LEU A CD2 
305  N  N   . HIS A 41  ? 0.34906 0.18815 0.38135 0.03737  -0.03231 -0.01282 41  HIS A N   
306  C  CA  . HIS A 41  ? 0.39351 0.20738 0.35396 0.00465  -0.00439 -0.00486 41  HIS A CA  
307  C  C   . HIS A 41  ? 0.42851 0.15768 0.35757 -0.06928 -0.00691 -0.00928 41  HIS A C   
308  O  O   . HIS A 41  ? 0.40976 0.19200 0.33920 -0.06046 -0.03923 0.02811  41  HIS A O   
309  C  CB  . HIS A 41  ? 0.43530 0.22097 0.35003 0.03327  -0.02042 0.00207  41  HIS A CB  
310  C  CG  . HIS A 41  ? 0.49261 0.19634 0.34399 0.06308  -0.01240 0.00595  41  HIS A CG  
311  N  ND1 . HIS A 41  ? 0.49399 0.21808 0.34520 0.01765  -0.02578 0.03090  41  HIS A ND1 
312  C  CD2 . HIS A 41  ? 0.52894 0.23209 0.36541 0.15078  -0.02203 0.04975  41  HIS A CD2 
313  C  CE1 . HIS A 41  ? 0.53295 0.24914 0.37251 0.15652  -0.00890 0.05851  41  HIS A CE1 
314  N  NE2 . HIS A 41  ? 0.55031 0.23661 0.36643 0.12041  0.01318  0.07303  41  HIS A NE2 
315  N  N   . ARG A 42  ? 0.43938 0.18784 0.37124 -0.06898 0.00282  -0.03656 42  ARG A N   
316  C  CA  . ARG A 42  ? 0.46104 0.14969 0.38861 -0.02324 -0.01263 -0.04791 42  ARG A CA  
317  C  C   . ARG A 42  ? 0.46297 0.16290 0.37445 -0.05680 -0.02366 -0.00807 42  ARG A C   
318  O  O   . ARG A 42  ? 0.47346 0.21078 0.35912 -0.02737 -0.04879 0.01134  42  ARG A O   
319  C  CB  . ARG A 42  ? 0.47791 0.15509 0.43800 -0.06308 -0.03733 -0.06713 42  ARG A CB  
320  C  CG  . ARG A 42  ? 0.51728 0.19177 0.49063 -0.06718 -0.02908 -0.12099 42  ARG A CG  
321  C  CD  . ARG A 42  ? 0.61264 0.35908 0.53493 -0.09011 -0.02617 -0.12612 42  ARG A CD  
322  N  NE  . ARG A 42  ? 0.67485 0.44790 0.55710 -0.08317 -0.02307 -0.14954 42  ARG A NE  
323  C  CZ  . ARG A 42  ? 0.71916 0.49740 0.57508 -0.05842 -0.03135 -0.16566 42  ARG A CZ  
324  N  NH1 . ARG A 42  ? 0.73951 0.51310 0.58475 -0.07684 -0.03147 -0.17734 42  ARG A NH1 
325  N  NH2 . ARG A 42  ? 0.75808 0.56341 0.59674 -0.05506 -0.04662 -0.14890 42  ARG A NH2 
326  N  N   . VAL A 43  ? 0.41383 0.19440 0.37677 -0.04907 -0.02388 0.00966  43  VAL A N   
327  C  CA  . VAL A 43  ? 0.41985 0.19616 0.38010 -0.08163 -0.02673 0.01961  43  VAL A CA  
328  C  C   . VAL A 43  ? 0.40935 0.21802 0.39149 -0.07705 0.00020  0.00013  43  VAL A C   
329  O  O   . VAL A 43  ? 0.45417 0.22801 0.36200 -0.10330 0.00735  0.02495  43  VAL A O   
330  C  CB  . VAL A 43  ? 0.40697 0.17818 0.36019 -0.06797 -0.05354 0.03252  43  VAL A CB  
331  C  CG1 . VAL A 43  ? 0.35649 0.21385 0.36091 -0.07739 -0.03730 0.06648  43  VAL A CG1 
332  C  CG2 . VAL A 43  ? 0.45936 0.18193 0.32948 -0.03379 -0.05739 0.04924  43  VAL A CG2 
333  N  N   . THR A 44  ? 0.41111 0.26456 0.39605 -0.16991 0.04182  -0.00209 44  THR A N   
334  C  CA  . THR A 44  ? 0.41034 0.23021 0.41593 -0.12201 0.05245  -0.00869 44  THR A CA  
335  C  C   . THR A 44  ? 0.41375 0.27844 0.41320 -0.07935 0.03230  -0.01087 44  THR A C   
336  O  O   . THR A 44  ? 0.41545 0.26745 0.41625 -0.12245 0.02360  -0.03445 44  THR A O   
337  C  CB  . THR A 44  ? 0.46763 0.21407 0.42953 -0.10671 0.07497  0.00870  44  THR A CB  
338  O  OG1 . THR A 44  ? 0.54480 0.25611 0.44355 -0.11979 0.08410  0.04309  44  THR A OG1 
339  C  CG2 . THR A 44  ? 0.48344 0.30794 0.42516 -0.12769 0.06817  0.00484  44  THR A CG2 
340  N  N   . LEU A 45  ? 0.35870 0.30571 0.41575 -0.13426 0.03805  -0.00797 45  LEU A N   
341  C  CA  . LEU A 45  ? 0.37795 0.27350 0.42132 -0.12354 0.04767  0.00901  45  LEU A CA  
342  C  C   . LEU A 45  ? 0.40363 0.33724 0.44251 -0.14389 0.09205  0.00857  45  LEU A C   
343  O  O   . LEU A 45  ? 0.43150 0.42180 0.46323 -0.13944 0.07591  0.00507  45  LEU A O   
344  C  CB  . LEU A 45  ? 0.31796 0.28625 0.40569 -0.02473 0.03696  0.02811  45  LEU A CB  
345  C  CG  . LEU A 45  ? 0.34653 0.34027 0.40377 -0.08989 0.01234  0.01869  45  LEU A CG  
346  C  CD1 . LEU A 45  ? 0.40365 0.27523 0.38640 -0.07162 -0.03529 0.04606  45  LEU A CD1 
347  C  CD2 . LEU A 45  ? 0.34992 0.25251 0.41162 -0.07272 0.04576  0.00317  45  LEU A CD2 
348  N  N   . TYR A 46  ? 0.37658 0.41752 0.45552 -0.07165 0.13303  -0.01468 46  TYR A N   
349  C  CA  . TYR A 46  ? 0.32245 0.42410 0.48150 -0.18410 0.12700  -0.03579 46  TYR A CA  
350  C  C   . TYR A 46  ? 0.38717 0.51930 0.49780 -0.20322 0.15815  -0.06904 46  TYR A C   
351  O  O   . TYR A 46  ? 0.48342 0.57795 0.48978 -0.21963 0.16658  -0.07495 46  TYR A O   
352  C  CB  . TYR A 46  ? 0.34970 0.42789 0.52020 -0.08010 0.11657  -0.05125 46  TYR A CB  
353  C  CG  . TYR A 46  ? 0.38246 0.46828 0.56407 -0.02998 0.06195  -0.06030 46  TYR A CG  
354  C  CD1 . TYR A 46  ? 0.40530 0.44570 0.58596 -0.04482 0.01450  -0.04825 46  TYR A CD1 
355  C  CD2 . TYR A 46  ? 0.35682 0.48099 0.58566 0.04292  0.03607  -0.06693 46  TYR A CD2 
356  C  CE1 . TYR A 46  ? 0.39205 0.49059 0.60434 -0.00917 -0.00917 -0.06368 46  TYR A CE1 
357  C  CE2 . TYR A 46  ? 0.40045 0.46580 0.60279 0.01727  0.01773  -0.06024 46  TYR A CE2 
358  C  CZ  . TYR A 46  ? 0.42814 0.53472 0.61647 0.04439  -0.01646 -0.07055 46  TYR A CZ  
359  O  OH  . TYR A 46  ? 0.40552 0.61462 0.63580 0.05462  -0.07425 -0.05629 46  TYR A OH  
360  N  N   . ASP A 47  ? 0.42860 0.58139 0.52108 -0.24751 0.11288  -0.06851 47  ASP A N   
361  C  CA  . ASP A 47  ? 0.44400 0.52028 0.54560 -0.24961 0.05950  -0.05293 47  ASP A CA  
362  C  C   . ASP A 47  ? 0.51246 0.56028 0.55734 -0.20602 0.07467  -0.05983 47  ASP A C   
363  O  O   . ASP A 47  ? 0.53888 0.62591 0.56902 -0.23138 0.07062  -0.09663 47  ASP A O   
364  C  CB  . ASP A 47  ? 0.47976 0.54789 0.56009 -0.15651 0.02073  -0.04524 47  ASP A CB  
365  C  CG  . ASP A 47  ? 0.53904 0.54573 0.57994 -0.03561 -0.01815 -0.04787 47  ASP A CG  
366  O  OD1 . ASP A 47  ? 0.51022 0.43559 0.58425 0.00580  -0.05708 -0.05244 47  ASP A OD1 
367  O  OD2 . ASP A 47  ? 0.54278 0.62822 0.59112 0.03143  -0.01913 -0.05030 47  ASP A OD2 
368  N  N   . GLY A 48  ? 0.52667 0.48783 0.55757 -0.18548 0.07968  -0.03001 48  GLY A N   
369  C  CA  . GLY A 48  ? 0.52858 0.43280 0.56298 -0.22764 0.06243  0.02162  48  GLY A CA  
370  C  C   . GLY A 48  ? 0.52705 0.41294 0.56781 -0.22665 0.01537  0.01171  48  GLY A C   
371  O  O   . GLY A 48  ? 0.53030 0.42373 0.55823 -0.23552 -0.02737 -0.01131 48  GLY A O   
372  N  N   . ARG A 49  ? 0.52733 0.37648 0.59160 -0.17026 0.03622  0.04264  49  ARG A N   
373  C  CA  . ARG A 49  ? 0.56322 0.34091 0.60817 -0.19088 0.03701  0.05321  49  ARG A CA  
374  C  C   . ARG A 49  ? 0.49845 0.28716 0.57287 -0.19883 -0.00833 0.03952  49  ARG A C   
375  O  O   . ARG A 49  ? 0.44938 0.32350 0.57385 -0.17038 -0.05898 0.02979  49  ARG A O   
376  C  CB  . ARG A 49  ? 0.72316 0.42846 0.66452 -0.14694 0.07797  0.06364  49  ARG A CB  
377  C  CG  . ARG A 49  ? 0.90948 0.55223 0.71878 -0.10309 0.10593  0.07230  49  ARG A CG  
378  C  CD  . ARG A 49  ? 1.07034 0.72117 0.76686 -0.01914 0.12712  0.08325  49  ARG A CD  
379  N  NE  . ARG A 49  ? 1.16599 0.84438 0.81048 0.00050  0.14231  0.10598  49  ARG A NE  
380  C  CZ  . ARG A 49  ? 1.20231 0.93176 0.83432 0.02074  0.15089  0.11821  49  ARG A CZ  
381  N  NH1 . ARG A 49  ? 1.16535 0.93001 0.83729 -0.02935 0.18506  0.13342  49  ARG A NH1 
382  N  NH2 . ARG A 49  ? 1.22116 0.95849 0.83790 0.03970  0.14024  0.10869  49  ARG A NH2 
383  N  N   . GLN A 50  ? 0.43084 0.33652 0.54505 -0.11321 0.00599  0.05003  50  GLN A N   
384  C  CA  . GLN A 50  ? 0.44315 0.28618 0.51544 -0.09702 -0.00230 0.03003  50  GLN A CA  
385  C  C   . GLN A 50  ? 0.35155 0.33984 0.46855 -0.11333 -0.01197 0.00896  50  GLN A C   
386  O  O   . GLN A 50  ? 0.35858 0.47075 0.49353 -0.10476 -0.01353 0.03856  50  GLN A O   
387  C  CB  . GLN A 50  ? 0.57117 0.26174 0.54091 -0.16816 -0.02079 0.03704  50  GLN A CB  
388  C  CG  . GLN A 50  ? 0.72384 0.45179 0.56507 -0.10001 -0.02904 0.02342  50  GLN A CG  
389  C  CD  . GLN A 50  ? 0.81126 0.56035 0.56094 -0.11332 -0.03967 0.02784  50  GLN A CD  
390  O  OE1 . GLN A 50  ? 0.77438 0.59673 0.56487 -0.14222 -0.01628 0.01481  50  GLN A OE1 
391  N  NE2 . GLN A 50  ? 0.78911 0.51758 0.53725 -0.13054 -0.04015 0.04158  50  GLN A NE2 
392  N  N   . ALA A 51  ? 0.31644 0.28662 0.41975 -0.12163 -0.01775 0.03973  51  ALA A N   
393  C  CA  . ALA A 51  ? 0.31923 0.19503 0.40768 -0.04031 0.00200  0.01478  51  ALA A CA  
394  C  C   . ALA A 51  ? 0.31873 0.24578 0.38079 -0.00372 0.00065  0.00675  51  ALA A C   
395  O  O   . ALA A 51  ? 0.35567 0.21498 0.39203 -0.02899 -0.01157 0.02314  51  ALA A O   
396  C  CB  . ALA A 51  ? 0.31504 0.19571 0.42899 0.00501  0.02025  -0.01032 51  ALA A CB  
397  N  N   . TRP A 52  ? 0.24907 0.24805 0.35530 -0.02922 0.01347  -0.02377 52  TRP A N   
398  C  CA  . TRP A 52  ? 0.23559 0.19272 0.34020 0.00075  0.00096  -0.04460 52  TRP A CA  
399  C  C   . TRP A 52  ? 0.28217 0.22316 0.33368 -0.03461 -0.03471 -0.04279 52  TRP A C   
400  O  O   . TRP A 52  ? 0.33041 0.26992 0.33261 0.04841  -0.03050 -0.02704 52  TRP A O   
401  C  CB  . TRP A 52  ? 0.31258 0.21862 0.34592 -0.00779 0.00608  -0.07488 52  TRP A CB  
402  C  CG  . TRP A 52  ? 0.32931 0.20259 0.36097 -0.03237 -0.03171 -0.09218 52  TRP A CG  
403  C  CD1 . TRP A 52  ? 0.36761 0.20754 0.37036 -0.05126 -0.04589 -0.06158 52  TRP A CD1 
404  C  CD2 . TRP A 52  ? 0.37902 0.16701 0.37816 0.02790  -0.05378 -0.04302 52  TRP A CD2 
405  N  NE1 . TRP A 52  ? 0.41429 0.23102 0.39868 0.03682  -0.04695 -0.04983 52  TRP A NE1 
406  C  CE2 . TRP A 52  ? 0.40415 0.23305 0.40619 -0.04962 -0.04969 -0.02927 52  TRP A CE2 
407  C  CE3 . TRP A 52  ? 0.39092 0.16344 0.38017 0.01148  -0.04320 -0.05035 52  TRP A CE3 
408  C  CZ2 . TRP A 52  ? 0.46163 0.28250 0.42558 -0.01847 -0.06638 -0.03824 52  TRP A CZ2 
409  C  CZ3 . TRP A 52  ? 0.42324 0.19726 0.40930 -0.02514 -0.05138 -0.04414 52  TRP A CZ3 
410  C  CH2 . TRP A 52  ? 0.44104 0.20091 0.41593 -0.00726 -0.10913 -0.04025 52  TRP A CH2 
411  N  N   . VAL A 53  ? 0.32122 0.18214 0.31679 -0.04614 -0.01117 -0.01661 53  VAL A N   
412  C  CA  . VAL A 53  ? 0.26355 0.16400 0.29550 -0.04157 0.00435  -0.03305 53  VAL A CA  
413  C  C   . VAL A 53  ? 0.28744 0.16912 0.31189 0.02843  -0.00913 -0.02248 53  VAL A C   
414  O  O   . VAL A 53  ? 0.33731 0.17962 0.30575 0.04939  -0.00660 -0.01752 53  VAL A O   
415  C  CB  . VAL A 53  ? 0.29428 0.22018 0.26506 0.05553  -0.03345 -0.02718 53  VAL A CB  
416  C  CG1 . VAL A 53  ? 0.28750 0.34856 0.24079 0.01603  -0.00788 -0.04001 53  VAL A CG1 
417  C  CG2 . VAL A 53  ? 0.34996 0.22628 0.28840 0.01791  -0.01795 0.01643  53  VAL A CG2 
418  N  N   . VAL A 54  ? 0.23475 0.18100 0.32179 0.01272  -0.05429 -0.02542 54  VAL A N   
419  C  CA  . VAL A 54  ? 0.23858 0.23890 0.31075 0.03833  -0.06655 -0.00019 54  VAL A CA  
420  C  C   . VAL A 54  ? 0.29346 0.22657 0.30442 0.07048  -0.05869 -0.03418 54  VAL A C   
421  O  O   . VAL A 54  ? 0.30121 0.21875 0.31786 0.04033  -0.04393 -0.04011 54  VAL A O   
422  C  CB  . VAL A 54  ? 0.31729 0.24191 0.29833 0.05222  -0.06228 0.02254  54  VAL A CB  
423  C  CG1 . VAL A 54  ? 0.35825 0.21954 0.31363 0.00367  -0.02897 0.03524  54  VAL A CG1 
424  C  CG2 . VAL A 54  ? 0.30457 0.25144 0.26848 0.04493  -0.06099 0.01119  54  VAL A CG2 
425  N  N   . THR A 55  ? 0.25807 0.28526 0.29439 0.06350  -0.05854 0.00606  55  THR A N   
426  C  CA  . THR A 55  ? 0.28031 0.27639 0.28577 0.06241  -0.05263 0.00033  55  THR A CA  
427  C  C   . THR A 55  ? 0.32646 0.33999 0.29690 0.06083  -0.04345 -0.05451 55  THR A C   
428  O  O   . THR A 55  ? 0.37004 0.54403 0.30357 0.04825  -0.04539 -0.07075 55  THR A O   
429  C  CB  . THR A 55  ? 0.33584 0.26959 0.30241 0.04136  0.03635  -0.00324 55  THR A CB  
430  O  OG1 . THR A 55  ? 0.34034 0.32571 0.31114 0.08850  -0.00216 0.00706  55  THR A OG1 
431  C  CG2 . THR A 55  ? 0.26372 0.36199 0.30634 -0.04880 0.04132  -0.01152 55  THR A CG2 
432  N  N   . LYS A 56  ? 0.28901 0.24499 0.30354 0.08081  -0.00174 -0.03369 56  LYS A N   
433  C  CA  . LYS A 56  ? 0.26503 0.21255 0.31256 0.10030  -0.02845 0.00172  56  LYS A CA  
434  C  C   . LYS A 56  ? 0.22085 0.19786 0.32023 0.03453  -0.05032 -0.01680 56  LYS A C   
435  O  O   . LYS A 56  ? 0.25731 0.24465 0.32093 0.04854  -0.05955 -0.00010 56  LYS A O   
436  C  CB  . LYS A 56  ? 0.31613 0.21542 0.32979 0.12207  -0.02611 -0.01509 56  LYS A CB  
437  C  CG  . LYS A 56  ? 0.39528 0.21214 0.35165 0.04105  -0.04312 -0.00607 56  LYS A CG  
438  C  CD  . LYS A 56  ? 0.39845 0.22159 0.37082 0.03631  -0.04508 0.01216  56  LYS A CD  
439  C  CE  . LYS A 56  ? 0.31357 0.30290 0.38389 0.01808  -0.03707 0.03199  56  LYS A CE  
440  N  NZ  . LYS A 56  ? 0.36909 0.28781 0.37753 0.04801  0.00872  0.05840  56  LYS A NZ  
441  N  N   . HIS A 57  ? 0.20685 0.28772 0.29860 -0.02649 0.03288  -0.04066 57  HIS A N   
442  C  CA  . HIS A 57  ? 0.27546 0.24509 0.25907 -0.00776 -0.01072 -0.04046 57  HIS A CA  
443  C  C   . HIS A 57  ? 0.28336 0.26839 0.26987 0.06667  -0.02525 -0.06255 57  HIS A C   
444  O  O   . HIS A 57  ? 0.27239 0.31118 0.27319 0.04711  -0.03072 0.00357  57  HIS A O   
445  C  CB  . HIS A 57  ? 0.22427 0.24631 0.25946 -0.03383 -0.04425 -0.01584 57  HIS A CB  
446  C  CG  . HIS A 57  ? 0.31264 0.28005 0.23861 -0.00211 -0.01499 0.03037  57  HIS A CG  
447  N  ND1 . HIS A 57  ? 0.32726 0.32887 0.24713 0.02231  -0.04241 -0.01171 57  HIS A ND1 
448  C  CD2 . HIS A 57  ? 0.34265 0.27197 0.25982 0.06321  -0.02903 0.05026  57  HIS A CD2 
449  C  CE1 . HIS A 57  ? 0.27928 0.38118 0.27053 0.06797  -0.04196 0.03625  57  HIS A CE1 
450  N  NE2 . HIS A 57  ? 0.31909 0.31872 0.26597 0.04507  -0.00983 0.04250  57  HIS A NE2 
451  N  N   . GLU A 58  ? 0.26971 0.31719 0.26126 0.06922  -0.00917 -0.10342 58  GLU A N   
452  C  CA  . GLU A 58  ? 0.25573 0.40143 0.26489 0.10402  -0.01644 -0.12266 58  GLU A CA  
453  C  C   . GLU A 58  ? 0.30982 0.29220 0.26458 0.00152  -0.03178 -0.05144 58  GLU A C   
454  O  O   . GLU A 58  ? 0.29432 0.27567 0.27524 0.04954  -0.01434 -0.01856 58  GLU A O   
455  C  CB  . GLU A 58  ? 0.35038 0.52574 0.29379 0.13429  -0.01562 -0.12519 58  GLU A CB  
456  C  CG  . GLU A 58  ? 0.48153 0.61552 0.33593 0.13410  -0.01096 -0.10577 58  GLU A CG  
457  C  CD  . GLU A 58  ? 0.58077 0.66406 0.35684 0.15375  0.00104  -0.12570 58  GLU A CD  
458  O  OE1 . GLU A 58  ? 0.52759 0.61437 0.37041 0.12948  -0.00144 -0.14710 58  GLU A OE1 
459  O  OE2 . GLU A 58  ? 0.63641 0.63585 0.38177 0.15016  0.02496  -0.11836 58  GLU A OE2 
460  N  N   . ALA A 59  ? 0.27477 0.23266 0.29250 0.01992  0.02158  -0.03030 59  ALA A N   
461  C  CA  . ALA A 59  ? 0.27907 0.19966 0.31735 0.02793  -0.01600 -0.03862 59  ALA A CA  
462  C  C   . ALA A 59  ? 0.28958 0.21374 0.30103 0.04271  -0.03562 -0.04793 59  ALA A C   
463  O  O   . ALA A 59  ? 0.27501 0.24907 0.28686 0.00185  -0.01510 -0.03059 59  ALA A O   
464  C  CB  . ALA A 59  ? 0.35303 0.22829 0.35126 0.03922  0.00358  -0.01604 59  ALA A CB  
465  N  N   . ALA A 60  ? 0.28126 0.19453 0.28422 0.04262  0.00933  -0.07669 60  ALA A N   
466  C  CA  . ALA A 60  ? 0.29175 0.20316 0.26504 0.01621  -0.00108 -0.05487 60  ALA A CA  
467  C  C   . ALA A 60  ? 0.26554 0.23351 0.26577 0.09086  0.00201  -0.01929 60  ALA A C   
468  O  O   . ALA A 60  ? 0.24166 0.23525 0.27815 0.03395  -0.01573 -0.02042 60  ALA A O   
469  C  CB  . ALA A 60  ? 0.23622 0.22336 0.27116 0.04513  -0.03420 -0.05801 60  ALA A CB  
470  N  N   . ARG A 61  ? 0.27258 0.25075 0.24966 0.05450  0.02020  -0.03042 61  ARG A N   
471  C  CA  . ARG A 61  ? 0.25411 0.30807 0.25511 0.04773  0.01846  -0.05389 61  ARG A CA  
472  C  C   . ARG A 61  ? 0.26440 0.23690 0.26416 0.00630  0.01414  -0.04651 61  ARG A C   
473  O  O   . ARG A 61  ? 0.29691 0.26470 0.27297 -0.03446 -0.00856 -0.02306 61  ARG A O   
474  C  CB  . ARG A 61  ? 0.20344 0.32028 0.24358 0.00887  0.01486  -0.09260 61  ARG A CB  
475  C  CG  . ARG A 61  ? 0.29865 0.27126 0.26126 0.01860  0.02586  -0.06280 61  ARG A CG  
476  C  CD  . ARG A 61  ? 0.28499 0.34243 0.25667 0.05270  0.06641  0.00752  61  ARG A CD  
477  N  NE  . ARG A 61  ? 0.29478 0.37355 0.25848 0.03451  0.04838  0.02426  61  ARG A NE  
478  C  CZ  . ARG A 61  ? 0.28099 0.28767 0.23943 0.01411  0.05284  0.03767  61  ARG A CZ  
479  N  NH1 . ARG A 61  ? 0.28639 0.19694 0.25869 0.06373  0.03964  0.02862  61  ARG A NH1 
480  N  NH2 . ARG A 61  ? 0.25170 0.34537 0.22447 -0.01685 0.04040  0.03315  61  ARG A NH2 
481  N  N   . LYS A 62  ? 0.24816 0.25504 0.27023 0.01419  0.02778  -0.02439 62  LYS A N   
482  C  CA  . LYS A 62  ? 0.23046 0.25179 0.28031 0.01628  -0.01615 -0.04831 62  LYS A CA  
483  C  C   . LYS A 62  ? 0.28144 0.27006 0.26641 -0.01253 0.00220  -0.02085 62  LYS A C   
484  O  O   . LYS A 62  ? 0.27879 0.35932 0.25432 -0.00219 0.02664  -0.01759 62  LYS A O   
485  C  CB  . LYS A 62  ? 0.34474 0.31289 0.29105 0.01334  -0.02682 -0.07017 62  LYS A CB  
486  C  CG  . LYS A 62  ? 0.45835 0.48082 0.30575 0.00767  -0.02975 -0.06986 62  LYS A CG  
487  C  CD  . LYS A 62  ? 0.59667 0.57729 0.33046 -0.03963 -0.06247 -0.04245 62  LYS A CD  
488  C  CE  . LYS A 62  ? 0.67056 0.66274 0.36615 -0.10386 -0.07985 -0.01916 62  LYS A CE  
489  N  NZ  . LYS A 62  ? 0.78495 0.69404 0.38999 -0.15660 -0.06941 0.00164  62  LYS A NZ  
490  N  N   . LEU A 63  ? 0.27157 0.21731 0.27707 -0.03584 0.00215  0.00533  63  LEU A N   
491  C  CA  . LEU A 63  ? 0.23255 0.22145 0.26983 -0.01268 -0.01186 -0.00231 63  LEU A CA  
492  C  C   . LEU A 63  ? 0.28953 0.20845 0.25299 -0.01380 -0.00010 -0.04264 63  LEU A C   
493  O  O   . LEU A 63  ? 0.25186 0.27098 0.24714 0.01061  0.00640  -0.02032 63  LEU A O   
494  C  CB  . LEU A 63  ? 0.30399 0.18143 0.24797 0.01977  -0.00677 -0.02969 63  LEU A CB  
495  C  CG  . LEU A 63  ? 0.30907 0.16923 0.23286 -0.03161 -0.02633 -0.04903 63  LEU A CG  
496  C  CD1 . LEU A 63  ? 0.25712 0.22075 0.26129 0.00507  0.02526  0.05963  63  LEU A CD1 
497  C  CD2 . LEU A 63  ? 0.36772 0.19273 0.24320 0.02110  -0.02126 -0.05230 63  LEU A CD2 
498  N  N   . LEU A 64  ? 0.28083 0.14968 0.25037 0.01430  0.00348  -0.01830 64  LEU A N   
499  C  CA  . LEU A 64  ? 0.22936 0.19187 0.22605 -0.02551 -0.00405 -0.02446 64  LEU A CA  
500  C  C   . LEU A 64  ? 0.24559 0.25909 0.24598 0.02581  -0.01561 0.01405  64  LEU A C   
501  O  O   . LEU A 64  ? 0.29113 0.23917 0.24710 -0.00495 -0.01569 0.01889  64  LEU A O   
502  C  CB  . LEU A 64  ? 0.21261 0.24898 0.22165 0.00715  -0.03256 -0.04290 64  LEU A CB  
503  C  CG  . LEU A 64  ? 0.19900 0.22472 0.21527 -0.00618 -0.02744 -0.02204 64  LEU A CG  
504  C  CD1 . LEU A 64  ? 0.32468 0.18470 0.23491 -0.00411 -0.02075 -0.03558 64  LEU A CD1 
505  C  CD2 . LEU A 64  ? 0.20194 0.27821 0.22723 0.04744  -0.01291 0.01026  64  LEU A CD2 
506  N  N   . GLY A 65  ? 0.21704 0.26244 0.24406 0.02143  0.00198  0.00065  65  GLY A N   
507  C  CA  . GLY A 65  ? 0.29387 0.25771 0.23922 0.01975  0.02161  0.00737  65  GLY A CA  
508  C  C   . GLY A 65  ? 0.26437 0.22659 0.25487 0.02404  0.00909  -0.03459 65  GLY A C   
509  O  O   . GLY A 65  ? 0.29065 0.31887 0.26783 -0.00654 0.03937  -0.03221 65  GLY A O   
510  N  N   . ASP A 66  ? 0.25841 0.23420 0.26357 -0.00055 -0.00163 -0.02462 66  ASP A N   
511  C  CA  . ASP A 66  ? 0.26214 0.23851 0.28314 0.01223  -0.03111 -0.04638 66  ASP A CA  
512  C  C   . ASP A 66  ? 0.25908 0.31448 0.26314 0.03811  -0.04233 -0.03067 66  ASP A C   
513  O  O   . ASP A 66  ? 0.31018 0.36811 0.24881 -0.02421 0.00601  -0.06663 66  ASP A O   
514  C  CB  . ASP A 66  ? 0.33040 0.19901 0.29241 -0.00837 -0.01270 -0.03616 66  ASP A CB  
515  C  CG  . ASP A 66  ? 0.40456 0.24941 0.30194 0.05804  -0.02716 -0.04551 66  ASP A CG  
516  O  OD1 . ASP A 66  ? 0.37050 0.30632 0.29645 0.04158  -0.00385 -0.09450 66  ASP A OD1 
517  O  OD2 . ASP A 66  ? 0.48314 0.34836 0.32479 0.04697  -0.05824 -0.07502 66  ASP A OD2 
518  N  N   . PRO A 67  ? 0.28483 0.33919 0.27401 0.02038  -0.03084 -0.02647 67  PRO A N   
519  C  CA  . PRO A 67  ? 0.27763 0.31900 0.28054 -0.00924 -0.03870 -0.00399 67  PRO A CA  
520  C  C   . PRO A 67  ? 0.32841 0.30739 0.27990 -0.03348 -0.01977 -0.00188 67  PRO A C   
521  O  O   . PRO A 67  ? 0.30308 0.31789 0.28400 0.00629  -0.03852 -0.01510 67  PRO A O   
522  C  CB  . PRO A 67  ? 0.36212 0.37124 0.28855 0.04513  -0.05173 0.00355  67  PRO A CB  
523  C  CG  . PRO A 67  ? 0.31201 0.45759 0.28668 0.07953  -0.03421 -0.00062 67  PRO A CG  
524  C  CD  . PRO A 67  ? 0.30442 0.42800 0.26942 0.01750  -0.04054 -0.03742 67  PRO A CD  
525  N  N   . ARG A 68  ? 0.31761 0.30720 0.26704 -0.07812 -0.03527 -0.04715 68  ARG A N   
526  C  CA  . ARG A 68  ? 0.31033 0.25310 0.27917 -0.01541 0.01229  -0.08779 68  ARG A CA  
527  C  C   . ARG A 68  ? 0.32201 0.27387 0.28676 -0.00940 0.00468  -0.02715 68  ARG A C   
528  O  O   . ARG A 68  ? 0.31258 0.29030 0.32030 -0.02023 -0.00131 -0.07808 68  ARG A O   
529  C  CB  . ARG A 68  ? 0.34838 0.28437 0.28834 0.00699  0.02359  -0.08428 68  ARG A CB  
530  C  CG  . ARG A 68  ? 0.36462 0.37075 0.30264 0.05810  -0.00030 -0.09525 68  ARG A CG  
531  C  CD  . ARG A 68  ? 0.37667 0.37032 0.32641 0.04252  -0.02147 -0.11054 68  ARG A CD  
532  N  NE  . ARG A 68  ? 0.38980 0.34518 0.34188 0.01753  -0.00542 -0.11408 68  ARG A NE  
533  C  CZ  . ARG A 68  ? 0.42180 0.36454 0.34889 0.01301  0.01077  -0.13318 68  ARG A CZ  
534  N  NH1 . ARG A 68  ? 0.50035 0.39015 0.37685 0.01516  0.01806  -0.16391 68  ARG A NH1 
535  N  NH2 . ARG A 68  ? 0.44190 0.37662 0.32820 0.06381  0.02465  -0.08488 68  ARG A NH2 
536  N  N   . LEU A 69  ? 0.29062 0.24338 0.26730 -0.00867 -0.01059 -0.03653 69  LEU A N   
537  C  CA  . LEU A 69  ? 0.23261 0.23810 0.28093 0.04108  -0.02770 -0.00349 69  LEU A CA  
538  C  C   . LEU A 69  ? 0.22548 0.17952 0.29307 -0.03780 -0.00633 -0.00237 69  LEU A C   
539  O  O   . LEU A 69  ? 0.29258 0.20938 0.31275 -0.05884 -0.00393 -0.01814 69  LEU A O   
540  C  CB  . LEU A 69  ? 0.20582 0.26175 0.29489 0.03348  -0.06175 0.03268  69  LEU A CB  
541  C  CG  . LEU A 69  ? 0.27823 0.31611 0.32644 -0.03229 -0.06863 0.03908  69  LEU A CG  
542  C  CD1 . LEU A 69  ? 0.26217 0.41192 0.32594 -0.04326 -0.09572 0.05907  69  LEU A CD1 
543  C  CD2 . LEU A 69  ? 0.24745 0.30140 0.34152 -0.02171 -0.07608 0.04262  69  LEU A CD2 
544  N  N   . SER A 70  ? 0.23012 0.25842 0.26637 -0.00730 -0.02670 -0.02479 70  SER A N   
545  C  CA  . SER A 70  ? 0.26961 0.27506 0.26302 0.03764  -0.06477 -0.03399 70  SER A CA  
546  C  C   . SER A 70  ? 0.24759 0.21428 0.25103 0.01883  -0.05534 -0.02680 70  SER A C   
547  O  O   . SER A 70  ? 0.27631 0.24696 0.24659 0.00243  -0.05638 -0.02028 70  SER A O   
548  C  CB  . SER A 70  ? 0.25094 0.29425 0.28430 -0.00953 -0.01935 -0.03245 70  SER A CB  
549  O  OG  . SER A 70  ? 0.31591 0.25895 0.28438 0.01158  -0.01647 -0.05634 70  SER A OG  
550  N  N   . SER A 71  ? 0.29362 0.23341 0.25034 0.05839  -0.05014 -0.03837 71  SER A N   
551  C  CA  . SER A 71  ? 0.22264 0.18899 0.28733 0.00494  -0.04229 -0.01593 71  SER A CA  
552  C  C   . SER A 71  ? 0.21040 0.23972 0.33176 0.04245  -0.06081 -0.01307 71  SER A C   
553  O  O   . SER A 71  ? 0.21504 0.25364 0.36326 0.02488  -0.00716 -0.06495 71  SER A O   
554  C  CB  . SER A 71  ? 0.19039 0.25571 0.27283 -0.00078 -0.05091 -0.04543 71  SER A CB  
555  O  OG  . SER A 71  ? 0.21983 0.23731 0.26842 0.03802  -0.04113 -0.00144 71  SER A OG  
556  N  N   . ASN A 72  ? 0.27920 0.25424 0.34410 -0.00690 -0.09231 0.01763  72  ASN A N   
557  C  CA  . ASN A 72  ? 0.25877 0.30943 0.36076 0.02714  -0.06281 0.00738  72  ASN A CA  
558  C  C   . ASN A 72  ? 0.29184 0.28306 0.34958 0.06797  -0.05200 -0.01015 72  ASN A C   
559  O  O   . ASN A 72  ? 0.29958 0.30830 0.33979 0.04379  -0.07525 0.00489  72  ASN A O   
560  C  CB  . ASN A 72  ? 0.23356 0.35842 0.36487 0.01098  -0.08140 -0.01355 72  ASN A CB  
561  C  CG  . ASN A 72  ? 0.27561 0.35185 0.37267 -0.01289 -0.07016 -0.00035 72  ASN A CG  
562  O  OD1 . ASN A 72  ? 0.30578 0.32063 0.36148 -0.03214 -0.04585 -0.00753 72  ASN A OD1 
563  N  ND2 . ASN A 72  ? 0.34358 0.42783 0.37915 -0.00280 -0.07596 -0.02181 72  ASN A ND2 
564  N  N   . ARG A 73  ? 0.24791 0.28005 0.35849 0.05769  -0.02813 -0.01437 73  ARG A N   
565  C  CA  . ARG A 73  ? 0.30873 0.27233 0.37502 0.04628  -0.02486 -0.03003 73  ARG A CA  
566  C  C   . ARG A 73  ? 0.33351 0.33527 0.40627 0.00824  -0.03605 -0.00765 73  ARG A C   
567  O  O   . ARG A 73  ? 0.30724 0.40424 0.41257 -0.02631 -0.00870 0.02930  73  ARG A O   
568  C  CB  . ARG A 73  ? 0.34698 0.37614 0.36904 0.10283  -0.03362 -0.06511 73  ARG A CB  
569  C  CG  . ARG A 73  ? 0.39365 0.41967 0.38572 0.04198  -0.02074 -0.01968 73  ARG A CG  
570  C  CD  . ARG A 73  ? 0.31928 0.47516 0.39226 0.01392  -0.02779 0.01987  73  ARG A CD  
571  N  NE  . ARG A 73  ? 0.44298 0.38527 0.39373 -0.04584 -0.03550 0.08221  73  ARG A NE  
572  C  CZ  . ARG A 73  ? 0.41609 0.43043 0.39878 0.05456  0.00209  0.08533  73  ARG A CZ  
573  N  NH1 . ARG A 73  ? 0.35340 0.50507 0.41633 0.12670  0.02763  0.11932  73  ARG A NH1 
574  N  NH2 . ARG A 73  ? 0.42161 0.34322 0.38813 -0.00732 -0.02027 0.07021  73  ARG A NH2 
575  N  N   . THR A 74  ? 0.35471 0.33023 0.42032 0.02881  -0.06723 -0.04060 74  THR A N   
576  C  CA  . THR A 74  ? 0.37073 0.37465 0.46415 -0.01745 -0.06053 0.00815  74  THR A CA  
577  C  C   . THR A 74  ? 0.30972 0.36406 0.47842 -0.03227 -0.06985 0.00505  74  THR A C   
578  O  O   . THR A 74  ? 0.37359 0.38554 0.50822 -0.05751 -0.07489 0.02923  74  THR A O   
579  C  CB  . THR A 74  ? 0.36023 0.43542 0.48843 0.00683  -0.08330 -0.01389 74  THR A CB  
580  O  OG1 . THR A 74  ? 0.33336 0.49873 0.49888 0.05661  -0.10478 -0.01100 74  THR A OG1 
581  C  CG2 . THR A 74  ? 0.37165 0.35042 0.49284 0.02442  -0.09163 -0.01998 74  THR A CG2 
582  N  N   . ASP A 75  ? 0.32232 0.36852 0.48738 0.02408  -0.06384 0.01768  75  ASP A N   
583  C  CA  . ASP A 75  ? 0.32800 0.39342 0.48824 0.04120  -0.05358 0.00419  75  ASP A CA  
584  C  C   . ASP A 75  ? 0.36480 0.36310 0.49451 -0.01089 -0.05274 0.00990  75  ASP A C   
585  O  O   . ASP A 75  ? 0.34765 0.28080 0.46669 0.00037  -0.04529 -0.01802 75  ASP A O   
586  C  CB  . ASP A 75  ? 0.40414 0.33123 0.49260 0.02852  -0.04170 -0.04451 75  ASP A CB  
587  C  CG  . ASP A 75  ? 0.51817 0.38627 0.49802 0.00217  -0.05532 -0.10636 75  ASP A CG  
588  O  OD1 . ASP A 75  ? 0.45480 0.33676 0.50269 -0.02943 -0.05463 -0.06514 75  ASP A OD1 
589  O  OD2 . ASP A 75  ? 0.68861 0.45573 0.50801 -0.07069 -0.07503 -0.15201 75  ASP A OD2 
590  N  N   . ASP A 76  ? 0.39857 0.41941 0.53168 -0.05540 -0.06516 -0.01124 76  ASP A N   
591  C  CA  . ASP A 76  ? 0.44017 0.50041 0.56433 -0.06910 -0.09303 0.01454  76  ASP A CA  
592  C  C   . ASP A 76  ? 0.46473 0.39306 0.55202 -0.12856 -0.07133 0.01207  76  ASP A C   
593  O  O   . ASP A 76  ? 0.56025 0.37150 0.57148 -0.05181 -0.04814 0.04909  76  ASP A O   
594  C  CB  . ASP A 76  ? 0.42727 0.64798 0.60604 -0.08386 -0.10164 0.02640  76  ASP A CB  
595  C  CG  . ASP A 76  ? 0.53906 0.90005 0.62728 -0.10516 -0.09910 0.04145  76  ASP A CG  
596  O  OD1 . ASP A 76  ? 0.58899 1.01928 0.62786 -0.08391 -0.10133 0.02482  76  ASP A OD1 
597  O  OD2 . ASP A 76  ? 0.57238 0.97581 0.64655 -0.09735 -0.09633 0.05503  76  ASP A OD2 
598  N  N   . ASN A 77  ? 0.44301 0.33460 0.53261 -0.09639 -0.05293 -0.01707 77  ASN A N   
599  C  CA  . ASN A 77  ? 0.41286 0.30850 0.52599 -0.07152 -0.03559 -0.03464 77  ASN A CA  
600  C  C   . ASN A 77  ? 0.32037 0.30190 0.51177 -0.00401 -0.02515 -0.03324 77  ASN A C   
601  O  O   . ASN A 77  ? 0.31315 0.27066 0.52321 -0.04548 -0.02471 -0.04330 77  ASN A O   
602  C  CB  . ASN A 77  ? 0.41817 0.35676 0.53752 -0.12682 -0.00696 -0.03838 77  ASN A CB  
603  C  CG  . ASN A 77  ? 0.46662 0.43876 0.56468 -0.12684 -0.01319 -0.00575 77  ASN A CG  
604  O  OD1 . ASN A 77  ? 0.51995 0.38469 0.58225 -0.22168 -0.01757 0.02388  77  ASN A OD1 
605  N  ND2 . ASN A 77  ? 0.45786 0.46290 0.55871 -0.05733 -0.06238 -0.02100 77  ASN A ND2 
606  N  N   . PHE A 78  ? 0.27812 0.30166 0.47860 -0.01061 -0.03135 -0.03350 78  PHE A N   
607  C  CA  . PHE A 78  ? 0.28017 0.24482 0.44678 0.00758  -0.00936 -0.02154 78  PHE A CA  
608  C  C   . PHE A 78  ? 0.25925 0.31517 0.40444 0.00851  -0.00107 -0.01970 78  PHE A C   
609  O  O   . PHE A 78  ? 0.30840 0.37876 0.41576 0.02357  0.00201  -0.00583 78  PHE A O   
610  C  CB  . PHE A 78  ? 0.28089 0.26510 0.45918 -0.01354 -0.03930 -0.00554 78  PHE A CB  
611  C  CG  . PHE A 78  ? 0.20507 0.26292 0.46765 -0.06293 -0.06844 -0.00288 78  PHE A CG  
612  C  CD1 . PHE A 78  ? 0.20558 0.29310 0.46842 -0.03381 -0.12394 0.00026  78  PHE A CD1 
613  C  CD2 . PHE A 78  ? 0.29479 0.27674 0.47604 -0.01542 -0.08564 0.01862  78  PHE A CD2 
614  C  CE1 . PHE A 78  ? 0.27769 0.31773 0.48175 -0.03367 -0.07816 0.03397  78  PHE A CE1 
615  C  CE2 . PHE A 78  ? 0.26839 0.26087 0.47748 0.01685  -0.09586 0.02207  78  PHE A CE2 
616  C  CZ  . PHE A 78  ? 0.30152 0.30656 0.48203 0.01615  -0.06500 0.06638  78  PHE A CZ  
617  N  N   . PRO A 79  ? 0.25437 0.31766 0.35694 -0.00943 0.01555  -0.03396 79  PRO A N   
618  C  CA  . PRO A 79  ? 0.25958 0.34393 0.37126 -0.04418 0.03031  -0.05806 79  PRO A CA  
619  C  C   . PRO A 79  ? 0.37499 0.34752 0.45209 -0.07046 0.05720  -0.08594 79  PRO A C   
620  O  O   . PRO A 79  ? 0.49679 0.38107 0.49570 -0.13827 0.12990  -0.07950 79  PRO A O   
621  C  CB  . PRO A 79  ? 0.29005 0.30453 0.34512 -0.03218 0.01903  0.00634  79  PRO A CB  
622  C  CG  . PRO A 79  ? 0.27353 0.28540 0.33947 -0.04110 -0.04841 -0.00519 79  PRO A CG  
623  C  CD  . PRO A 79  ? 0.23941 0.36286 0.34505 -0.03326 -0.04953 -0.03796 79  PRO A CD  
624  N  N   . ALA A 80  ? 0.38226 0.46167 0.46883 0.00099  0.03270  -0.11318 80  ALA A N   
625  C  CA  . ALA A 80  ? 0.37348 0.53700 0.45855 0.09291  -0.01214 -0.11898 80  ALA A CA  
626  C  C   . ALA A 80  ? 0.37288 0.43868 0.45559 0.06851  -0.03011 -0.12061 80  ALA A C   
627  O  O   . ALA A 80  ? 0.38874 0.49864 0.46587 0.00205  -0.05245 -0.09707 80  ALA A O   
628  C  CB  . ALA A 80  ? 0.29076 0.66801 0.44519 0.12283  -0.08091 -0.09874 80  ALA A CB  
629  N  N   . THR A 81  ? 0.37794 0.43466 0.46202 0.03299  -0.01481 -0.06510 81  THR A N   
630  C  CA  . THR A 81  ? 0.35373 0.38180 0.45392 -0.02047 -0.00776 -0.05637 81  THR A CA  
631  C  C   . THR A 81  ? 0.35798 0.39806 0.44908 0.00919  -0.00918 -0.06144 81  THR A C   
632  O  O   . THR A 81  ? 0.42369 0.33758 0.42924 -0.00725 -0.03216 -0.03308 81  THR A O   
633  C  CB  . THR A 81  ? 0.33807 0.26586 0.47954 -0.01756 0.01818  0.01460  81  THR A CB  
634  O  OG1 . THR A 81  ? 0.44099 0.30160 0.49995 -0.07276 -0.04993 0.01056  81  THR A OG1 
635  C  CG2 . THR A 81  ? 0.30727 0.26881 0.49380 -0.02830 0.06035  0.04348  81  THR A CG2 
636  N  N   . SER A 82  ? 0.33520 0.37520 0.44567 -0.00547 0.00848  -0.08079 82  SER A N   
637  C  CA  . SER A 82  ? 0.35046 0.48382 0.45849 -0.01894 0.02013  -0.05373 82  SER A CA  
638  C  C   . SER A 82  ? 0.35890 0.61268 0.46158 -0.02536 0.05276  -0.04419 82  SER A C   
639  O  O   . SER A 82  ? 0.35698 0.62230 0.45100 0.00984  0.07376  -0.08805 82  SER A O   
640  C  CB  . SER A 82  ? 0.43690 0.42144 0.47046 -0.03133 -0.03828 -0.06949 82  SER A CB  
641  O  OG  . SER A 82  ? 0.54792 0.50668 0.50275 0.00649  -0.03719 -0.09078 82  SER A OG  
642  N  N   . PRO A 83  ? 0.40425 0.68268 0.49408 -0.00740 0.05405  -0.02860 83  PRO A N   
643  C  CA  . PRO A 83  ? 0.39362 0.70312 0.51383 0.03124  0.07500  -0.00499 83  PRO A CA  
644  C  C   . PRO A 83  ? 0.38293 0.66932 0.52669 0.02001  0.08918  -0.01715 83  PRO A C   
645  O  O   . PRO A 83  ? 0.39391 0.73066 0.53159 -0.00851 0.05212  -0.01304 83  PRO A O   
646  C  CB  . PRO A 83  ? 0.38710 0.68340 0.51954 -0.02894 0.08921  0.01359  83  PRO A CB  
647  C  CG  . PRO A 83  ? 0.39992 0.69655 0.51090 -0.07400 0.09385  0.00288  83  PRO A CG  
648  C  CD  . PRO A 83  ? 0.42764 0.67034 0.49445 -0.03932 0.08643  -0.01880 83  PRO A CD  
649  N  N   . ALA A 84  ? 0.40860 0.65629 0.53197 0.07122  0.11667  -0.04292 84  ALA A N   
650  C  CA  . ALA A 84  ? 0.45894 0.60220 0.55908 0.08602  0.12248  -0.00837 84  ALA A CA  
651  C  C   . ALA A 84  ? 0.49501 0.66335 0.58894 0.07046  0.14701  0.01260  84  ALA A C   
652  O  O   . ALA A 84  ? 0.47948 0.65106 0.58053 0.05098  0.16778  0.02518  84  ALA A O   
653  C  CB  . ALA A 84  ? 0.46234 0.53638 0.56977 0.09577  0.07672  0.00720  84  ALA A CB  
654  N  N   . PHE A 85  ? 0.46590 0.74634 0.61578 0.12001  0.16896  0.01740  85  PHE A N   
655  C  CA  . PHE A 85  ? 0.52803 0.80401 0.64965 0.12741  0.19495  0.04618  85  PHE A CA  
656  C  C   . PHE A 85  ? 0.54715 0.85403 0.69541 0.06848  0.19027  0.03217  85  PHE A C   
657  O  O   . PHE A 85  ? 0.47377 0.84198 0.68926 0.05166  0.20461  0.03680  85  PHE A O   
658  C  CB  . PHE A 85  ? 0.68767 0.80597 0.64316 0.19468  0.21639  0.06242  85  PHE A CB  
659  C  CG  . PHE A 85  ? 0.80758 0.80796 0.64752 0.27956  0.22978  0.05813  85  PHE A CG  
660  C  CD1 . PHE A 85  ? 0.83854 0.77372 0.64672 0.30370  0.23236  0.07108  85  PHE A CD1 
661  C  CD2 . PHE A 85  ? 0.85903 0.80226 0.64365 0.28058  0.23233  0.05504  85  PHE A CD2 
662  C  CE1 . PHE A 85  ? 0.83041 0.75875 0.64111 0.34628  0.26104  0.07313  85  PHE A CE1 
663  C  CE2 . PHE A 85  ? 0.85418 0.77647 0.64054 0.30303  0.24771  0.05602  85  PHE A CE2 
664  C  CZ  . PHE A 85  ? 0.84685 0.76485 0.64252 0.35095  0.24470  0.06848  85  PHE A CZ  
665  N  N   . GLU A 86  ? 0.56671 0.90287 0.74614 0.04289  0.17079  0.03023  86  GLU A N   
666  C  CA  . GLU A 86  ? 0.60947 0.91666 0.79228 0.04846  0.15558  0.03190  86  GLU A CA  
667  C  C   . GLU A 86  ? 0.58034 0.93319 0.80975 0.05999  0.11790  0.01968  86  GLU A C   
668  O  O   . GLU A 86  ? 0.59155 0.95821 0.81883 0.01721  0.10038  0.02053  86  GLU A O   
669  C  CB  . GLU A 86  ? 0.69719 0.92395 0.81263 0.05572  0.18422  0.03556  86  GLU A CB  
670  C  CG  . GLU A 86  ? 0.78803 0.97463 0.83659 0.03312  0.21069  0.02026  86  GLU A CG  
671  C  CD  . GLU A 86  ? 0.85219 1.02808 0.86147 0.03269  0.21209  0.01432  86  GLU A CD  
672  O  OE1 . GLU A 86  ? 0.88571 1.05959 0.87046 0.02920  0.22060  0.02198  86  GLU A OE1 
673  O  OE2 . GLU A 86  ? 0.83551 1.02661 0.87007 0.04529  0.20514  0.00481  86  GLU A OE2 
674  N  N   . ALA A 87  ? 0.54092 0.93289 0.81272 0.15599  0.09609  -0.01404 87  ALA A N   
675  C  CA  . ALA A 87  ? 0.50479 0.87729 0.82273 0.29165  0.06025  -0.03108 87  ALA A CA  
676  C  C   . ALA A 87  ? 0.58620 0.93031 0.83286 0.30763  0.04066  -0.07696 87  ALA A C   
677  O  O   . ALA A 87  ? 0.63637 0.96923 0.83111 0.33940  0.04995  -0.08543 87  ALA A O   
678  C  CB  . ALA A 87  ? 0.51318 0.89350 0.82588 0.25054  0.02350  0.00199  87  ALA A CB  
679  N  N   . VAL A 88  ? 0.58033 0.97178 0.84316 0.20875  0.00648  -0.10168 88  VAL A N   
680  C  CA  . VAL A 88  ? 0.63166 1.01113 0.86145 0.10153  -0.00756 -0.12272 88  VAL A CA  
681  C  C   . VAL A 88  ? 0.64257 0.95946 0.88296 0.07455  -0.02953 -0.10615 88  VAL A C   
682  O  O   . VAL A 88  ? 0.64197 0.92202 0.87532 0.03908  -0.03502 -0.11383 88  VAL A O   
683  C  CB  . VAL A 88  ? 0.71813 1.07259 0.85300 0.04422  0.01324  -0.15962 88  VAL A CB  
684  C  CG1 . VAL A 88  ? 0.69715 1.09032 0.84869 0.02144  0.03592  -0.17579 88  VAL A CG1 
685  C  CG2 . VAL A 88  ? 0.73741 1.10283 0.84733 0.02380  0.01923  -0.16204 88  VAL A CG2 
686  N  N   . ARG A 89  ? 0.68734 0.96155 0.91732 0.09132  -0.04497 -0.07473 89  ARG A N   
687  C  CA  . ARG A 89  ? 0.73132 0.96256 0.95949 0.10983  -0.05505 -0.03530 89  ARG A CA  
688  C  C   . ARG A 89  ? 0.75487 1.01609 0.97632 0.11611  -0.05673 -0.04596 89  ARG A C   
689  O  O   . ARG A 89  ? 0.73913 1.03762 0.97233 0.12418  -0.06104 -0.04064 89  ARG A O   
690  C  CB  . ARG A 89  ? 0.72331 0.91292 0.98530 0.11621  -0.06229 0.01450  89  ARG A CB  
691  C  CG  . ARG A 89  ? 0.71797 0.88551 1.01639 0.10037  -0.06359 0.03052  89  ARG A CG  
692  C  CD  . ARG A 89  ? 0.70692 0.92519 1.04473 0.08295  -0.06101 0.02485  89  ARG A CD  
693  N  NE  . ARG A 89  ? 0.70943 0.98306 1.06714 0.00816  -0.04991 0.00133  89  ARG A NE  
694  C  CZ  . ARG A 89  ? 0.66153 1.02530 1.07943 -0.10168 -0.02621 -0.03507 89  ARG A CZ  
695  N  NH1 . ARG A 89  ? 0.67037 1.05502 1.07758 -0.14806 -0.00181 -0.04546 89  ARG A NH1 
696  N  NH2 . ARG A 89  ? 0.54066 1.00553 1.08356 -0.12681 -0.02520 -0.05661 89  ARG A NH2 
697  N  N   . GLU A 90  ? 0.80907 1.03487 0.99175 0.07660  -0.05645 -0.04682 90  GLU A N   
698  C  CA  . GLU A 90  ? 0.88384 1.05183 1.00589 -0.00677 -0.06297 -0.03161 90  GLU A CA  
699  C  C   . GLU A 90  ? 0.83746 0.96200 0.98106 -0.03524 -0.07251 0.01003  90  GLU A C   
700  O  O   . GLU A 90  ? 0.84351 0.95402 0.98579 -0.01580 -0.06265 -0.00828 90  GLU A O   
701  C  CB  . GLU A 90  ? 0.99130 1.13791 1.04249 -0.05997 -0.06134 -0.05484 90  GLU A CB  
702  C  CG  . GLU A 90  ? 1.10634 1.22214 1.07438 -0.09269 -0.05911 -0.07655 90  GLU A CG  
703  C  CD  . GLU A 90  ? 1.21975 1.29580 1.10261 -0.09479 -0.05330 -0.09816 90  GLU A CD  
704  O  OE1 . GLU A 90  ? 1.24739 1.31138 1.11366 -0.06329 -0.05523 -0.10441 90  GLU A OE1 
705  O  OE2 . GLU A 90  ? 1.26337 1.32188 1.11160 -0.10255 -0.04584 -0.10569 90  GLU A OE2 
706  N  N   . SER A 91  ? 0.75426 0.91636 0.95031 -0.06408 -0.09485 0.05541  91  SER A N   
707  C  CA  . SER A 91  ? 0.67928 0.84230 0.91978 -0.06865 -0.11536 0.08136  91  SER A CA  
708  C  C   . SER A 91  ? 0.57541 0.77184 0.88200 -0.02338 -0.12677 0.07888  91  SER A C   
709  O  O   . SER A 91  ? 0.49975 0.74783 0.88372 0.05518  -0.13078 0.06906  91  SER A O   
710  C  CB  . SER A 91  ? 0.69951 0.85537 0.92052 -0.06543 -0.13807 0.12900  91  SER A CB  
711  O  OG  . SER A 91  ? 0.69342 0.82858 0.92223 -0.11827 -0.15751 0.16443  91  SER A OG  
712  N  N   . PRO A 92  ? 0.46736 0.67914 0.83707 0.01574  -0.13998 0.09554  92  PRO A N   
713  C  CA  . PRO A 92  ? 0.41503 0.65231 0.80044 -0.01587 -0.12339 0.07131  92  PRO A CA  
714  C  C   . PRO A 92  ? 0.39375 0.60093 0.73831 -0.01124 -0.11709 0.04220  92  PRO A C   
715  O  O   . PRO A 92  ? 0.52863 0.60349 0.76428 -0.02130 -0.07450 0.01344  92  PRO A O   
716  C  CB  . PRO A 92  ? 0.39377 0.66640 0.81704 0.04051  -0.11922 0.09813  92  PRO A CB  
717  C  CG  . PRO A 92  ? 0.41032 0.65811 0.82964 0.05527  -0.12012 0.09879  92  PRO A CG  
718  C  CD  . PRO A 92  ? 0.41548 0.65805 0.83451 0.06038  -0.13209 0.09691  92  PRO A CD  
719  N  N   . GLN A 93  ? 0.25421 0.45156 0.63828 -0.13084 -0.10990 0.06888  93  GLN A N   
720  C  CA  . GLN A 93  ? 0.29084 0.24287 0.56697 -0.05132 -0.08120 0.01520  93  GLN A CA  
721  C  C   . GLN A 93  ? 0.32982 0.24944 0.50868 -0.04368 -0.09720 -0.00479 93  GLN A C   
722  O  O   . GLN A 93  ? 0.44244 0.30860 0.54405 -0.07121 -0.13707 0.03363  93  GLN A O   
723  C  CB  . GLN A 93  ? 0.42030 0.20942 0.55362 -0.01753 -0.04652 -0.03777 93  GLN A CB  
724  C  CG  . GLN A 93  ? 0.48387 0.20903 0.54877 -0.00051 -0.04347 -0.04044 93  GLN A CG  
725  C  CD  . GLN A 93  ? 0.62694 0.30652 0.53441 -0.03521 -0.05085 0.01508  93  GLN A CD  
726  O  OE1 . GLN A 93  ? 0.66544 0.37853 0.50535 -0.03648 -0.01085 0.05675  93  GLN A OE1 
727  N  NE2 . GLN A 93  ? 0.62974 0.34353 0.52457 -0.01536 -0.10693 0.07381  93  GLN A NE2 
728  N  N   . ALA A 94  ? 0.25703 0.25637 0.42440 0.05358  -0.08518 -0.05584 94  ALA A N   
729  C  CA  . ALA A 94  ? 0.27652 0.26625 0.36266 0.02739  -0.07173 -0.06066 94  ALA A CA  
730  C  C   . ALA A 94  ? 0.26858 0.24731 0.32089 0.05792  -0.07369 -0.02313 94  ALA A C   
731  O  O   . ALA A 94  ? 0.36278 0.22343 0.27959 -0.04144 -0.07969 0.00326  94  ALA A O   
732  C  CB  . ALA A 94  ? 0.24815 0.25735 0.34441 0.01930  -0.07461 -0.07005 94  ALA A CB  
733  N  N   . PHE A 95  ? 0.28270 0.31874 0.29883 0.01529  -0.08418 0.00946  95  PHE A N   
734  C  CA  . PHE A 95  ? 0.23870 0.28946 0.27618 0.03351  -0.02935 -0.00212 95  PHE A CA  
735  C  C   . PHE A 95  ? 0.29145 0.23916 0.25571 0.01710  -0.03218 -0.01865 95  PHE A C   
736  O  O   . PHE A 95  ? 0.32054 0.20378 0.27112 0.02102  -0.06963 -0.03921 95  PHE A O   
737  C  CB  . PHE A 95  ? 0.27215 0.27462 0.25417 -0.03199 -0.02342 -0.04488 95  PHE A CB  
738  C  CG  . PHE A 95  ? 0.23891 0.30513 0.24460 0.04549  -0.04551 -0.03697 95  PHE A CG  
739  C  CD1 . PHE A 95  ? 0.20728 0.30575 0.24476 0.00863  -0.04541 -0.03033 95  PHE A CD1 
740  C  CD2 . PHE A 95  ? 0.25901 0.29889 0.24911 0.04781  -0.02407 -0.05847 95  PHE A CD2 
741  C  CE1 . PHE A 95  ? 0.25581 0.20098 0.26669 0.07121  -0.06214 -0.01758 95  PHE A CE1 
742  C  CE2 . PHE A 95  ? 0.21046 0.26627 0.25956 0.04485  -0.03386 -0.00943 95  PHE A CE2 
743  C  CZ  . PHE A 95  ? 0.24660 0.25476 0.25626 0.07830  -0.01471 0.00109  95  PHE A CZ  
744  N  N   . ILE A 96  ? 0.30256 0.19318 0.22413 0.03779  -0.03002 0.01811  96  ILE A N   
745  C  CA  . ILE A 96  ? 0.24767 0.22922 0.24292 0.01615  -0.05507 -0.02150 96  ILE A CA  
746  C  C   . ILE A 96  ? 0.28992 0.21781 0.26503 0.03017  -0.04922 -0.02752 96  ILE A C   
747  O  O   . ILE A 96  ? 0.29579 0.23698 0.28374 0.07664  -0.02696 -0.02791 96  ILE A O   
748  C  CB  . ILE A 96  ? 0.23570 0.32299 0.24439 0.06211  -0.03444 0.00379  96  ILE A CB  
749  C  CG1 . ILE A 96  ? 0.26019 0.30532 0.22335 0.04719  -0.08530 -0.04307 96  ILE A CG1 
750  C  CG2 . ILE A 96  ? 0.23798 0.31795 0.26133 0.07407  -0.04649 -0.02097 96  ILE A CG2 
751  C  CD1 . ILE A 96  ? 0.25393 0.31619 0.21040 0.03680  -0.06922 0.00622  96  ILE A CD1 
752  N  N   . GLY A 97  ? 0.27323 0.27548 0.26774 -0.00747 -0.05225 -0.02524 97  GLY A N   
753  C  CA  . GLY A 97  ? 0.27724 0.25478 0.26418 -0.01734 -0.06550 -0.01096 97  GLY A CA  
754  C  C   . GLY A 97  ? 0.27954 0.24070 0.28423 -0.01948 -0.06324 -0.01661 97  GLY A C   
755  O  O   . GLY A 97  ? 0.34141 0.32886 0.31959 -0.01922 -0.07172 -0.00131 97  GLY A O   
756  N  N   . LEU A 98  ? 0.27583 0.26205 0.25913 -0.00456 -0.04412 -0.01195 98  LEU A N   
757  C  CA  . LEU A 98  ? 0.29457 0.26657 0.24918 0.05659  -0.09467 -0.01367 98  LEU A CA  
758  C  C   . LEU A 98  ? 0.25302 0.20079 0.25820 0.01833  -0.09204 -0.01597 98  LEU A C   
759  O  O   . LEU A 98  ? 0.30170 0.28457 0.25570 -0.01548 -0.09823 -0.03068 98  LEU A O   
760  C  CB  . LEU A 98  ? 0.33461 0.23201 0.27941 0.05988  -0.07193 0.00488  98  LEU A CB  
761  C  CG  . LEU A 98  ? 0.25959 0.20497 0.32220 0.00236  -0.07006 -0.02146 98  LEU A CG  
762  C  CD1 . LEU A 98  ? 0.25810 0.22947 0.34263 0.00132  -0.12329 0.01928  98  LEU A CD1 
763  C  CD2 . LEU A 98  ? 0.24456 0.30977 0.31169 -0.02428 -0.06953 -0.04843 98  LEU A CD2 
764  N  N   . ASP A 99  ? 0.31562 0.23642 0.26902 -0.00080 -0.06108 -0.00080 99  ASP A N   
765  C  CA  . ASP A 99  ? 0.39756 0.20702 0.26144 0.01534  -0.05080 -0.01198 99  ASP A CA  
766  C  C   . ASP A 99  ? 0.40071 0.31510 0.24594 0.04582  -0.07642 0.00986  99  ASP A C   
767  O  O   . ASP A 99  ? 0.36560 0.33666 0.22953 0.04231  -0.10977 0.02483  99  ASP A O   
768  C  CB  . ASP A 99  ? 0.40531 0.23128 0.27520 -0.00924 -0.05071 -0.02280 99  ASP A CB  
769  C  CG  . ASP A 99  ? 0.35895 0.26489 0.27191 0.02972  -0.05851 -0.02766 99  ASP A CG  
770  O  OD1 . ASP A 99  ? 0.33815 0.25955 0.27194 0.02371  -0.06941 0.00376  99  ASP A OD1 
771  O  OD2 . ASP A 99  ? 0.38935 0.27374 0.30328 0.02852  -0.06370 -0.01281 99  ASP A OD2 
772  N  N   . PRO A 100 ? 0.41452 0.32813 0.23023 0.00600  -0.04162 0.00105  100 PRO A N   
773  C  CA  . PRO A 100 ? 0.39858 0.31216 0.22448 0.03671  -0.02314 -0.00965 100 PRO A CA  
774  C  C   . PRO A 100 ? 0.59840 0.39961 0.22186 0.01338  -0.03023 -0.02634 100 PRO A C   
775  O  O   . PRO A 100 ? 0.71412 0.41071 0.25749 0.05838  -0.02017 -0.05745 100 PRO A O   
776  C  CB  . PRO A 100 ? 0.42196 0.41212 0.23977 0.02918  -0.02183 0.00328  100 PRO A CB  
777  C  CG  . PRO A 100 ? 0.44223 0.43503 0.23740 0.05430  -0.00072 0.00492  100 PRO A CG  
778  C  CD  . PRO A 100 ? 0.36447 0.44708 0.24048 -0.00094 0.00685  0.01838  100 PRO A CD  
779  N  N   . PRO A 101 ? 0.55724 0.42369 0.20771 0.01097  -0.04238 -0.01414 101 PRO A N   
780  C  CA  . PRO A 101 ? 0.53519 0.40578 0.20810 -0.01464 -0.01717 0.00236  101 PRO A CA  
781  C  C   . PRO A 101 ? 0.44649 0.35993 0.25612 -0.00242 -0.03321 0.02071  101 PRO A C   
782  O  O   . PRO A 101 ? 0.42324 0.35814 0.28017 -0.02800 -0.02567 0.00502  101 PRO A O   
783  C  CB  . PRO A 101 ? 0.58753 0.46407 0.21246 -0.03556 -0.03493 -0.00126 101 PRO A CB  
784  C  CG  . PRO A 101 ? 0.58819 0.49048 0.21541 -0.05470 -0.03920 -0.03962 101 PRO A CG  
785  C  CD  . PRO A 101 ? 0.62192 0.46868 0.20009 -0.05214 -0.04752 -0.04032 101 PRO A CD  
786  N  N   . GLU A 102 ? 0.42599 0.32322 0.25653 0.00697  -0.07189 0.01105  102 GLU A N   
787  C  CA  . GLU A 102 ? 0.40316 0.37468 0.27628 0.01996  -0.09341 0.01534  102 GLU A CA  
788  C  C   . GLU A 102 ? 0.32034 0.33717 0.27856 0.06662  -0.07710 0.02771  102 GLU A C   
789  O  O   . GLU A 102 ? 0.33589 0.36611 0.31864 0.05386  -0.05355 0.04367  102 GLU A O   
790  C  CB  . GLU A 102 ? 0.39680 0.51247 0.29239 -0.05420 -0.14916 0.01902  102 GLU A CB  
791  C  CG  . GLU A 102 ? 0.50052 0.66690 0.30259 -0.08026 -0.13575 0.04664  102 GLU A CG  
792  C  CD  . GLU A 102 ? 0.57000 0.80789 0.32723 -0.18743 -0.14729 0.01880  102 GLU A CD  
793  O  OE1 . GLU A 102 ? 0.53095 0.87093 0.35210 -0.24251 -0.11878 -0.02565 102 GLU A OE1 
794  O  OE2 . GLU A 102 ? 0.65603 0.86103 0.33608 -0.14894 -0.17138 0.01667  102 GLU A OE2 
795  N  N   . HIS A 103 ? 0.30789 0.28335 0.24743 0.07343  -0.08181 0.03936  103 HIS A N   
796  C  CA  . HIS A 103 ? 0.30249 0.24528 0.23131 0.02573  -0.06383 0.02623  103 HIS A CA  
797  C  C   . HIS A 103 ? 0.29092 0.26619 0.23141 -0.02897 -0.05157 0.00189  103 HIS A C   
798  O  O   . HIS A 103 ? 0.31551 0.27549 0.22915 -0.00281 -0.04205 -0.00510 103 HIS A O   
799  C  CB  . HIS A 103 ? 0.29904 0.28701 0.21285 0.08640  -0.06553 0.01656  103 HIS A CB  
800  C  CG  . HIS A 103 ? 0.31358 0.25640 0.23559 0.08675  -0.07430 -0.00171 103 HIS A CG  
801  N  ND1 . HIS A 103 ? 0.36402 0.26637 0.23949 0.09732  -0.06945 0.02296  103 HIS A ND1 
802  C  CD2 . HIS A 103 ? 0.37087 0.25195 0.21725 0.08506  -0.09624 -0.00968 103 HIS A CD2 
803  C  CE1 . HIS A 103 ? 0.36360 0.29541 0.22190 0.04577  -0.08729 -0.01146 103 HIS A CE1 
804  N  NE2 . HIS A 103 ? 0.38334 0.27789 0.24264 0.09420  -0.07454 -0.01999 103 HIS A NE2 
805  N  N   . GLY A 104 ? 0.29461 0.26905 0.22895 0.03250  -0.02975 -0.01503 104 GLY A N   
806  C  CA  . GLY A 104 ? 0.29001 0.34066 0.23542 0.04244  -0.02293 -0.01495 104 GLY A CA  
807  C  C   . GLY A 104 ? 0.35376 0.38010 0.22404 0.05827  -0.02149 -0.01224 104 GLY A C   
808  O  O   . GLY A 104 ? 0.38530 0.37477 0.21565 0.00551  -0.02520 -0.00824 104 GLY A O   
809  N  N   . THR A 105 ? 0.31537 0.31941 0.23001 0.08717  -0.04963 0.01447  105 THR A N   
810  C  CA  . THR A 105 ? 0.31851 0.30334 0.24279 0.07399  -0.04541 0.00904  105 THR A CA  
811  C  C   . THR A 105 ? 0.41648 0.26403 0.25810 0.03208  -0.01696 0.03440  105 THR A C   
812  O  O   . THR A 105 ? 0.47355 0.28148 0.28565 0.05403  0.00270  0.04405  105 THR A O   
813  C  CB  . THR A 105 ? 0.37349 0.39659 0.25062 0.03019  -0.02635 -0.01712 105 THR A CB  
814  O  OG1 . THR A 105 ? 0.37875 0.43792 0.26393 0.04155  -0.07794 -0.03055 105 THR A OG1 
815  C  CG2 . THR A 105 ? 0.41302 0.39661 0.23236 0.07765  -0.06221 -0.07551 105 THR A CG2 
816  N  N   . ARG A 106 ? 0.33051 0.28723 0.23919 0.02707  -0.04924 0.05404  106 ARG A N   
817  C  CA  . ARG A 106 ? 0.25919 0.26184 0.25906 0.01202  -0.03208 0.02993  106 ARG A CA  
818  C  C   . ARG A 106 ? 0.27195 0.24655 0.24855 0.04901  -0.03401 0.01986  106 ARG A C   
819  O  O   . ARG A 106 ? 0.24386 0.30942 0.26675 0.01918  -0.00620 0.00222  106 ARG A O   
820  C  CB  . ARG A 106 ? 0.21287 0.33989 0.28448 -0.03060 -0.06001 0.05156  106 ARG A CB  
821  C  CG  . ARG A 106 ? 0.30712 0.43601 0.28904 -0.06168 -0.02852 0.02175  106 ARG A CG  
822  C  CD  . ARG A 106 ? 0.27708 0.44785 0.33100 0.00599  -0.03256 0.02789  106 ARG A CD  
823  N  NE  . ARG A 106 ? 0.25939 0.44583 0.32911 0.07710  -0.09947 0.06759  106 ARG A NE  
824  C  CZ  . ARG A 106 ? 0.29117 0.35614 0.35183 0.08353  -0.06258 0.05652  106 ARG A CZ  
825  N  NH1 . ARG A 106 ? 0.31577 0.33950 0.35224 -0.00431 -0.03032 0.04216  106 ARG A NH1 
826  N  NH2 . ARG A 106 ? 0.29199 0.30436 0.37115 0.09732  -0.04450 0.05496  106 ARG A NH2 
827  N  N   . ARG A 107 ? 0.22527 0.24342 0.22505 0.01887  -0.06742 0.01409  107 ARG A N   
828  C  CA  . ARG A 107 ? 0.20157 0.20662 0.22660 0.03520  -0.05998 0.03000  107 ARG A CA  
829  C  C   . ARG A 107 ? 0.23062 0.23276 0.23759 0.02441  -0.03406 0.00638  107 ARG A C   
830  O  O   . ARG A 107 ? 0.24943 0.26305 0.24921 -0.00865 -0.05349 -0.02165 107 ARG A O   
831  C  CB  . ARG A 107 ? 0.20352 0.26799 0.20483 0.03118  -0.04067 0.02148  107 ARG A CB  
832  C  CG  . ARG A 107 ? 0.18986 0.31348 0.22431 0.08158  -0.09147 0.00974  107 ARG A CG  
833  C  CD  . ARG A 107 ? 0.21706 0.29790 0.23478 0.03662  -0.07445 0.01041  107 ARG A CD  
834  N  NE  . ARG A 107 ? 0.20421 0.36863 0.24636 0.03260  -0.07046 -0.03853 107 ARG A NE  
835  C  CZ  . ARG A 107 ? 0.24860 0.39562 0.28825 0.03529  -0.07544 -0.05483 107 ARG A CZ  
836  N  NH1 . ARG A 107 ? 0.27630 0.33314 0.25531 0.07375  -0.06291 0.01741  107 ARG A NH1 
837  N  NH2 . ARG A 107 ? 0.23775 0.45662 0.35950 0.07873  -0.05031 -0.06876 107 ARG A NH2 
838  N  N   . ARG A 108 ? 0.23280 0.28024 0.24180 0.01243  -0.00903 0.00115  108 ARG A N   
839  C  CA  . ARG A 108 ? 0.20415 0.27048 0.26585 0.02685  0.01682  -0.04251 108 ARG A CA  
840  C  C   . ARG A 108 ? 0.19338 0.26250 0.28058 0.03691  0.01663  0.01266  108 ARG A C   
841  O  O   . ARG A 108 ? 0.26903 0.33554 0.30693 -0.05929 -0.00971 -0.00829 108 ARG A O   
842  C  CB  . ARG A 108 ? 0.29517 0.28667 0.26119 0.05290  0.08349  -0.04820 108 ARG A CB  
843  C  CG  . ARG A 108 ? 0.41442 0.39360 0.27940 0.06671  0.08860  -0.04549 108 ARG A CG  
844  C  CD  . ARG A 108 ? 0.56962 0.43033 0.27837 0.06247  0.06584  -0.08088 108 ARG A CD  
845  N  NE  . ARG A 108 ? 0.63261 0.44454 0.28827 0.08612  0.09860  -0.07933 108 ARG A NE  
846  C  CZ  . ARG A 108 ? 0.64709 0.54125 0.31140 0.03135  0.09603  -0.04697 108 ARG A CZ  
847  N  NH1 . ARG A 108 ? 0.64847 0.53678 0.33523 0.07220  0.11479  -0.03307 108 ARG A NH1 
848  N  NH2 . ARG A 108 ? 0.64583 0.50449 0.31291 -0.06768 0.09349  -0.02638 108 ARG A NH2 
849  N  N   . MET A 109 ? 0.21757 0.25380 0.23766 0.03590  0.00821  -0.00667 109 MET A N   
850  C  CA  . MET A 109 ? 0.20949 0.28260 0.23744 0.00349  -0.02183 0.01737  109 MET A CA  
851  C  C   . MET A 109 ? 0.26295 0.27195 0.25435 -0.00061 -0.05255 -0.00368 109 MET A C   
852  O  O   . MET A 109 ? 0.27830 0.26250 0.27225 0.02585  -0.05163 -0.01309 109 MET A O   
853  C  CB  . MET A 109 ? 0.19748 0.30953 0.23114 0.02747  -0.03292 0.03797  109 MET A CB  
854  C  CG  . MET A 109 ? 0.16153 0.39141 0.25139 0.00620  -0.08773 0.03259  109 MET A CG  
855  S  SD  . MET A 109 ? 0.26084 0.33838 0.28976 0.01183  -0.04263 0.03211  109 MET A SD  
856  C  CE  . MET A 109 ? 0.29423 0.37674 0.27697 -0.03663 -0.06490 0.00168  109 MET A CE  
857  N  N   . THR A 110 ? 0.21882 0.29768 0.26096 0.06228  -0.03963 -0.00819 110 THR A N   
858  C  CA  . THR A 110 ? 0.25715 0.28094 0.23487 0.04306  -0.04257 -0.01001 110 THR A CA  
859  C  C   . THR A 110 ? 0.23671 0.27022 0.24217 0.03035  -0.04367 0.00397  110 THR A C   
860  O  O   . THR A 110 ? 0.28486 0.25786 0.23957 0.04212  -0.02748 -0.01392 110 THR A O   
861  C  CB  . THR A 110 ? 0.21758 0.25443 0.25487 0.11709  -0.04569 0.03981  110 THR A CB  
862  O  OG1 . THR A 110 ? 0.28557 0.30342 0.24299 0.06210  -0.01709 0.01932  110 THR A OG1 
863  C  CG2 . THR A 110 ? 0.21948 0.31195 0.29475 0.01144  -0.05723 0.00061  110 THR A CG2 
864  N  N   . ILE A 111 ? 0.28126 0.29802 0.26786 0.04048  -0.03885 -0.00556 111 ILE A N   
865  C  CA  . ILE A 111 ? 0.24243 0.29448 0.27274 0.00147  -0.02184 -0.04768 111 ILE A CA  
866  C  C   . ILE A 111 ? 0.28870 0.27320 0.27305 -0.00932 -0.05726 0.02878  111 ILE A C   
867  O  O   . ILE A 111 ? 0.29484 0.37462 0.25554 -0.05735 -0.04176 0.01995  111 ILE A O   
868  C  CB  . ILE A 111 ? 0.29605 0.31857 0.26228 -0.00126 -0.00740 -0.04491 111 ILE A CB  
869  C  CG1 . ILE A 111 ? 0.33876 0.36800 0.24767 0.05144  0.05107  -0.03960 111 ILE A CG1 
870  C  CG2 . ILE A 111 ? 0.34641 0.24714 0.28891 -0.04224 -0.04745 -0.00988 111 ILE A CG2 
871  C  CD1 . ILE A 111 ? 0.38044 0.46229 0.27105 0.06193  0.02857  -0.03504 111 ILE A CD1 
872  N  N   . SER A 112 ? 0.37535 0.24737 0.28732 0.04026  -0.02127 0.03525  112 SER A N   
873  C  CA  . SER A 112 ? 0.41585 0.30417 0.30022 0.00062  -0.00909 0.06798  112 SER A CA  
874  C  C   . SER A 112 ? 0.36553 0.26990 0.30242 -0.03172 0.00388  0.03992  112 SER A C   
875  O  O   . SER A 112 ? 0.38335 0.30375 0.31912 -0.02415 0.04471  0.01548  112 SER A O   
876  C  CB  . SER A 112 ? 0.51429 0.36800 0.32131 0.01358  -0.01386 0.07332  112 SER A CB  
877  O  OG  . SER A 112 ? 0.58211 0.49193 0.31969 0.06320  -0.07320 0.06001  112 SER A OG  
878  N  N   . GLU A 113 ? 0.31404 0.29766 0.29804 -0.02433 -0.01003 0.05886  113 GLU A N   
879  C  CA  . GLU A 113 ? 0.29901 0.30555 0.29785 0.02679  -0.02501 0.03839  113 GLU A CA  
880  C  C   . GLU A 113 ? 0.26709 0.27872 0.30431 -0.02418 -0.02404 0.02573  113 GLU A C   
881  O  O   . GLU A 113 ? 0.30584 0.28862 0.30408 0.02758  -0.05551 -0.00536 113 GLU A O   
882  C  CB  . GLU A 113 ? 0.36139 0.30910 0.31370 0.06029  0.02553  0.00940  113 GLU A CB  
883  C  CG  . GLU A 113 ? 0.47976 0.32048 0.36656 0.05801  -0.02277 0.00547  113 GLU A CG  
884  C  CD  . GLU A 113 ? 0.63737 0.50078 0.41944 0.08318  -0.03701 0.00288  113 GLU A CD  
885  O  OE1 . GLU A 113 ? 0.59523 0.48131 0.45447 0.19300  -0.03367 -0.02687 113 GLU A OE1 
886  O  OE2 . GLU A 113 ? 0.75073 0.58800 0.43414 0.05755  -0.02984 0.03832  113 GLU A OE2 
887  N  N   . PHE A 114 ? 0.24263 0.26233 0.27854 0.03698  -0.03299 0.00695  114 PHE A N   
888  C  CA  . PHE A 114 ? 0.26836 0.19630 0.27576 -0.04942 -0.02260 0.00431  114 PHE A CA  
889  C  C   . PHE A 114 ? 0.29508 0.29543 0.29257 -0.02217 -0.03201 -0.02495 114 PHE A C   
890  O  O   . PHE A 114 ? 0.33922 0.31505 0.30695 -0.01736 -0.03861 -0.02353 114 PHE A O   
891  C  CB  . PHE A 114 ? 0.28725 0.18103 0.27292 -0.02572 0.01719  0.02449  114 PHE A CB  
892  C  CG  . PHE A 114 ? 0.27070 0.23088 0.27130 0.00803  -0.01540 0.00680  114 PHE A CG  
893  C  CD1 . PHE A 114 ? 0.28614 0.27269 0.26504 -0.00905 0.02382  0.00184  114 PHE A CD1 
894  C  CD2 . PHE A 114 ? 0.24963 0.24877 0.25958 -0.01642 -0.02620 0.02002  114 PHE A CD2 
895  C  CE1 . PHE A 114 ? 0.30072 0.27934 0.26266 -0.04346 -0.02591 0.00684  114 PHE A CE1 
896  C  CE2 . PHE A 114 ? 0.34047 0.26765 0.24289 -0.03368 -0.02311 0.03735  114 PHE A CE2 
897  C  CZ  . PHE A 114 ? 0.31478 0.23119 0.24311 -0.04534 -0.05163 0.02978  114 PHE A CZ  
898  N  N   . THR A 115 ? 0.25983 0.35801 0.27653 -0.02495 0.00306  -0.02964 115 THR A N   
899  C  CA  . THR A 115 ? 0.24863 0.40216 0.28483 0.03713  -0.01792 -0.00416 115 THR A CA  
900  C  C   . THR A 115 ? 0.27620 0.42650 0.28255 -0.06186 -0.01637 -0.01737 115 THR A C   
901  O  O   . THR A 115 ? 0.31175 0.41727 0.25927 -0.06493 0.00998  -0.01848 115 THR A O   
902  C  CB  . THR A 115 ? 0.36516 0.47722 0.29225 -0.00289 0.00594  0.01070  115 THR A CB  
903  O  OG1 . THR A 115 ? 0.37366 0.54187 0.28817 -0.03928 0.03834  0.01360  115 THR A OG1 
904  C  CG2 . THR A 115 ? 0.38573 0.45783 0.27329 -0.07045 -0.03128 0.00419  115 THR A CG2 
905  N  N   . VAL A 116 ? 0.30240 0.52870 0.31432 0.03923  0.01763  -0.03061 116 VAL A N   
906  C  CA  . VAL A 116 ? 0.29729 0.55152 0.31570 0.00188  -0.00760 -0.07005 116 VAL A CA  
907  C  C   . VAL A 116 ? 0.32499 0.58565 0.32794 -0.08158 0.00956  -0.05367 116 VAL A C   
908  O  O   . VAL A 116 ? 0.34012 0.49502 0.34974 -0.17426 -0.01657 -0.06569 116 VAL A O   
909  C  CB  . VAL A 116 ? 0.46693 0.64057 0.34562 0.05413  0.04824  -0.05601 116 VAL A CB  
910  C  CG1 . VAL A 116 ? 0.53643 0.69408 0.35831 0.01879  0.06761  -0.04858 116 VAL A CG1 
911  C  CG2 . VAL A 116 ? 0.44903 0.66219 0.33265 0.09122  0.02923  -0.05278 116 VAL A CG2 
912  N  N   . LYS A 117 ? 0.39160 0.57505 0.30478 -0.16394 0.00513  0.00702  117 LYS A N   
913  C  CA  . LYS A 117 ? 0.49172 0.57394 0.30356 -0.16980 0.04114  0.04307  117 LYS A CA  
914  C  C   . LYS A 117 ? 0.49388 0.47638 0.29581 -0.24180 0.03375  0.02729  117 LYS A C   
915  O  O   . LYS A 117 ? 0.51801 0.54432 0.26716 -0.23865 0.02962  -0.00253 117 LYS A O   
916  C  CB  . LYS A 117 ? 0.61482 0.60587 0.31531 -0.14097 0.07929  0.07100  117 LYS A CB  
917  C  CG  . LYS A 117 ? 0.67214 0.71936 0.35794 -0.13952 0.12793  0.08836  117 LYS A CG  
918  C  CD  . LYS A 117 ? 0.70164 0.78835 0.40689 -0.06743 0.16606  0.07258  117 LYS A CD  
919  C  CE  . LYS A 117 ? 0.68109 0.82751 0.43217 0.01356  0.18683  0.06547  117 LYS A CE  
920  N  NZ  . LYS A 117 ? 0.64331 0.86611 0.44709 0.08488  0.19333  0.04332  117 LYS A NZ  
921  N  N   . ARG A 118 ? 0.39096 0.43701 0.30875 -0.21894 0.05849  0.04253  118 ARG A N   
922  C  CA  . ARG A 118 ? 0.51902 0.40158 0.32299 -0.20260 -0.00297 0.09947  118 ARG A CA  
923  C  C   . ARG A 118 ? 0.52067 0.36623 0.28528 -0.19616 -0.01343 0.08902  118 ARG A C   
924  O  O   . ARG A 118 ? 0.55160 0.40476 0.29413 -0.18498 -0.02118 0.05641  118 ARG A O   
925  C  CB  . ARG A 118 ? 0.58939 0.43812 0.39207 -0.16419 -0.06088 0.11201  118 ARG A CB  
926  C  CG  . ARG A 118 ? 0.72771 0.59549 0.47567 -0.19607 -0.07726 0.13897  118 ARG A CG  
927  C  CD  . ARG A 118 ? 0.83028 0.63536 0.53392 -0.18309 -0.08996 0.19898  118 ARG A CD  
928  N  NE  . ARG A 118 ? 1.00090 0.80129 0.61441 -0.11913 -0.08339 0.16911  118 ARG A NE  
929  C  CZ  . ARG A 118 ? 1.13791 0.92987 0.65908 -0.06867 -0.08982 0.13776  118 ARG A CZ  
930  N  NH1 . ARG A 118 ? 1.17470 0.96180 0.67389 -0.06421 -0.08607 0.11254  118 ARG A NH1 
931  N  NH2 . ARG A 118 ? 1.20015 0.99565 0.68282 -0.04990 -0.09561 0.10331  118 ARG A NH2 
932  N  N   . ILE A 119 ? 0.47261 0.39656 0.27723 -0.18811 -0.00132 0.06019  119 ILE A N   
933  C  CA  . ILE A 119 ? 0.42891 0.39351 0.25571 -0.14473 -0.00416 0.04281  119 ILE A CA  
934  C  C   . ILE A 119 ? 0.50644 0.50913 0.29549 -0.19185 0.02057  0.04650  119 ILE A C   
935  O  O   . ILE A 119 ? 0.54317 0.47044 0.24782 -0.16271 -0.01295 0.05087  119 ILE A O   
936  C  CB  . ILE A 119 ? 0.41013 0.42462 0.23948 -0.08319 0.02003  0.03139  119 ILE A CB  
937  C  CG1 . ILE A 119 ? 0.37271 0.51903 0.26274 -0.00385 0.04572  0.03665  119 ILE A CG1 
938  C  CG2 . ILE A 119 ? 0.37483 0.37887 0.20955 -0.03909 -0.01437 0.02385  119 ILE A CG2 
939  C  CD1 . ILE A 119 ? 0.39547 0.46611 0.29070 -0.02287 0.05962  -0.01427 119 ILE A CD1 
940  N  N   . LYS A 120 ? 0.49728 0.54286 0.34352 -0.21773 0.08795  0.01576  120 LYS A N   
941  C  CA  . LYS A 120 ? 0.51706 0.45573 0.40765 -0.28619 0.04725  -0.05882 120 LYS A CA  
942  C  C   . LYS A 120 ? 0.61969 0.48837 0.38867 -0.28718 0.06111  -0.06101 120 LYS A C   
943  O  O   . LYS A 120 ? 0.65429 0.52388 0.35887 -0.31193 0.03997  -0.07688 120 LYS A O   
944  C  CB  . LYS A 120 ? 0.56412 0.44852 0.47638 -0.28920 0.01882  -0.07373 120 LYS A CB  
945  C  CG  . LYS A 120 ? 0.62827 0.49022 0.55219 -0.24233 0.02995  -0.07933 120 LYS A CG  
946  C  CD  . LYS A 120 ? 0.64630 0.49566 0.60120 -0.21097 0.08860  -0.04334 120 LYS A CD  
947  C  CE  . LYS A 120 ? 0.69395 0.57525 0.64324 -0.17352 0.09017  -0.05813 120 LYS A CE  
948  N  NZ  . LYS A 120 ? 0.71410 0.65245 0.65552 -0.13072 0.12205  -0.06272 120 LYS A NZ  
949  N  N   . GLY A 121 ? 0.69056 0.44738 0.39074 -0.16988 0.10836  -0.01415 121 GLY A N   
950  C  CA  . GLY A 121 ? 0.74173 0.43604 0.38061 -0.08040 0.09435  0.03064  121 GLY A CA  
951  C  C   . GLY A 121 ? 0.73135 0.31037 0.35014 -0.11963 0.10513  0.05036  121 GLY A C   
952  O  O   . GLY A 121 ? 0.79036 0.44461 0.35679 -0.13078 0.06734  0.01614  121 GLY A O   
953  N  N   . MET A 122 ? 0.72617 0.34433 0.33147 -0.17237 0.05046  0.07325  122 MET A N   
954  C  CA  . MET A 122 ? 0.69381 0.31765 0.31180 -0.23003 -0.02955 0.04247  122 MET A CA  
955  C  C   . MET A 122 ? 0.74451 0.28506 0.31451 -0.17861 -0.06832 0.02075  122 MET A C   
956  O  O   . MET A 122 ? 0.78072 0.32986 0.25877 -0.10088 -0.09138 0.05802  122 MET A O   
957  C  CB  . MET A 122 ? 0.76232 0.30587 0.31340 -0.17818 -0.03619 0.00808  122 MET A CB  
958  C  CG  . MET A 122 ? 0.74191 0.34824 0.33519 -0.14718 -0.03192 -0.01064 122 MET A CG  
959  S  SD  . MET A 122 ? 0.70895 0.34841 0.35821 -0.07240 -0.01600 -0.00648 122 MET A SD  
960  C  CE  . MET A 122 ? 0.73389 0.36117 0.36095 -0.10296 -0.01607 -0.05071 122 MET A CE  
961  N  N   . ARG A 123 ? 0.65140 0.35796 0.34333 -0.23336 -0.07634 0.00163  123 ARG A N   
962  C  CA  . ARG A 123 ? 0.61763 0.49458 0.36780 -0.25315 -0.05149 -0.02115 123 ARG A CA  
963  C  C   . ARG A 123 ? 0.67864 0.43716 0.38649 -0.31083 -0.03125 0.01076  123 ARG A C   
964  O  O   . ARG A 123 ? 0.67578 0.47197 0.35098 -0.30650 -0.07909 0.02927  123 ARG A O   
965  C  CB  . ARG A 123 ? 0.52683 0.60925 0.38942 -0.21790 -0.00563 0.00529  123 ARG A CB  
966  C  CG  . ARG A 123 ? 0.53217 0.62919 0.42652 -0.24346 0.01453  0.02956  123 ARG A CG  
967  C  CD  . ARG A 123 ? 0.47348 0.60948 0.45495 -0.25091 0.01400  0.04236  123 ARG A CD  
968  N  NE  . ARG A 123 ? 0.48593 0.54600 0.45752 -0.24439 -0.03439 0.00808  123 ARG A NE  
969  C  CZ  . ARG A 123 ? 0.50755 0.48482 0.44632 -0.23800 -0.08750 0.02685  123 ARG A CZ  
970  N  NH1 . ARG A 123 ? 0.55096 0.48609 0.43541 -0.21825 -0.08488 0.02590  123 ARG A NH1 
971  N  NH2 . ARG A 123 ? 0.44060 0.50871 0.45456 -0.20862 -0.12774 -0.03759 123 ARG A NH2 
972  N  N   . PRO A 124 ? 0.78693 0.32660 0.41041 -0.23380 -0.00584 0.04060  124 PRO A N   
973  C  CA  . PRO A 124 ? 0.78940 0.31423 0.41821 -0.22288 0.00707  0.03429  124 PRO A CA  
974  C  C   . PRO A 124 ? 0.78476 0.27006 0.38671 -0.15722 -0.02064 0.06290  124 PRO A C   
975  O  O   . PRO A 124 ? 0.81047 0.28544 0.38632 -0.11136 -0.09079 0.02880  124 PRO A O   
976  C  CB  . PRO A 124 ? 0.81282 0.35165 0.43654 -0.23672 0.03171  0.06155  124 PRO A CB  
977  C  CG  . PRO A 124 ? 0.76938 0.36629 0.44432 -0.24689 0.04947  0.06155  124 PRO A CG  
978  C  CD  . PRO A 124 ? 0.72455 0.39059 0.44064 -0.27604 0.02751  0.04883  124 PRO A CD  
979  N  N   . GLU A 125 ? 0.72177 0.28811 0.36334 -0.11854 -0.06707 0.03560  125 GLU A N   
980  C  CA  . GLU A 125 ? 0.68097 0.21358 0.35280 -0.06455 -0.13320 0.02735  125 GLU A CA  
981  C  C   . GLU A 125 ? 0.62468 0.18623 0.33564 -0.00844 -0.11546 0.00008  125 GLU A C   
982  O  O   . GLU A 125 ? 0.64433 0.30103 0.32835 0.08468  -0.13443 -0.04214 125 GLU A O   
983  C  CB  . GLU A 125 ? 0.69439 0.35003 0.38273 -0.00556 -0.15791 0.05993  125 GLU A CB  
984  C  CG  . GLU A 125 ? 0.74275 0.47480 0.42944 0.01434  -0.10152 0.07917  125 GLU A CG  
985  C  CD  . GLU A 125 ? 0.77752 0.58200 0.45704 -0.03802 -0.11231 0.14056  125 GLU A CD  
986  O  OE1 . GLU A 125 ? 0.82056 0.58212 0.48158 -0.00749 -0.11751 0.15126  125 GLU A OE1 
987  O  OE2 . GLU A 125 ? 0.69604 0.62190 0.45969 -0.01796 -0.11929 0.14781  125 GLU A OE2 
988  N  N   . VAL A 126 ? 0.55886 0.21432 0.32884 0.04015  -0.09763 -0.03812 126 VAL A N   
989  C  CA  . VAL A 126 ? 0.47826 0.20515 0.30530 0.01407  -0.07364 -0.01943 126 VAL A CA  
990  C  C   . VAL A 126 ? 0.43886 0.18767 0.30682 -0.04996 -0.06365 -0.03236 126 VAL A C   
991  O  O   . VAL A 126 ? 0.43325 0.23129 0.30476 -0.02095 -0.02367 0.02805  126 VAL A O   
992  C  CB  . VAL A 126 ? 0.39890 0.21445 0.27317 -0.03250 -0.08408 0.01364  126 VAL A CB  
993  C  CG1 . VAL A 126 ? 0.33361 0.20169 0.27504 -0.02410 -0.04538 0.01192  126 VAL A CG1 
994  C  CG2 . VAL A 126 ? 0.33005 0.30727 0.27622 -0.05982 -0.06354 0.01610  126 VAL A CG2 
995  N  N   . GLU A 127 ? 0.44764 0.19034 0.30962 0.00762  -0.11487 -0.02174 127 GLU A N   
996  C  CA  . GLU A 127 ? 0.47040 0.23198 0.33893 0.02217  -0.10077 -0.01658 127 GLU A CA  
997  C  C   . GLU A 127 ? 0.44853 0.20813 0.33620 0.00247  -0.11755 -0.01986 127 GLU A C   
998  O  O   . GLU A 127 ? 0.45333 0.21497 0.32232 -0.00446 -0.12955 0.00772  127 GLU A O   
999  C  CB  . GLU A 127 ? 0.47520 0.21584 0.37131 -0.01013 -0.07453 0.02974  127 GLU A CB  
1000 C  CG  . GLU A 127 ? 0.61906 0.36426 0.43608 0.00186  -0.04696 0.05564  127 GLU A CG  
1001 C  CD  . GLU A 127 ? 0.76941 0.41906 0.48793 -0.02215 -0.05140 0.04335  127 GLU A CD  
1002 O  OE1 . GLU A 127 ? 0.79322 0.42037 0.53928 -0.01560 -0.02585 0.03798  127 GLU A OE1 
1003 O  OE2 . GLU A 127 ? 0.82356 0.40449 0.47629 -0.00992 -0.06618 0.02585  127 GLU A OE2 
1004 N  N   . GLU A 128 ? 0.46599 0.16648 0.37076 0.03334  -0.14230 -0.01826 128 GLU A N   
1005 C  CA  . GLU A 128 ? 0.48195 0.17601 0.39558 0.09196  -0.12435 -0.00700 128 GLU A CA  
1006 C  C   . GLU A 128 ? 0.58172 0.23042 0.37127 0.06874  -0.13101 -0.03543 128 GLU A C   
1007 O  O   . GLU A 128 ? 0.55839 0.23382 0.34727 0.12057  -0.16000 -0.02825 128 GLU A O   
1008 C  CB  . GLU A 128 ? 0.57530 0.19756 0.44902 0.00217  -0.14266 0.04484  128 GLU A CB  
1009 C  CG  . GLU A 128 ? 0.64820 0.36688 0.49617 0.09716  -0.16849 0.13225  128 GLU A CG  
1010 C  CD  . GLU A 128 ? 0.71334 0.48698 0.53950 0.10046  -0.15138 0.17734  128 GLU A CD  
1011 O  OE1 . GLU A 128 ? 0.71683 0.62464 0.53178 0.08367  -0.14915 0.24900  128 GLU A OE1 
1012 O  OE2 . GLU A 128 ? 0.76690 0.44773 0.56788 0.17732  -0.16833 0.16103  128 GLU A OE2 
1013 N  N   . VAL A 129 ? 0.57662 0.17770 0.35110 0.02408  -0.12801 -0.02107 129 VAL A N   
1014 C  CA  . VAL A 129 ? 0.53863 0.16617 0.32270 0.05181  -0.15736 -0.00800 129 VAL A CA  
1015 C  C   . VAL A 129 ? 0.46659 0.22255 0.31389 0.12566  -0.16051 -0.03459 129 VAL A C   
1016 O  O   . VAL A 129 ? 0.49096 0.31590 0.32667 0.15453  -0.14095 -0.07413 129 VAL A O   
1017 C  CB  . VAL A 129 ? 0.53483 0.17893 0.30229 0.05762  -0.13333 0.02563  129 VAL A CB  
1018 C  CG1 . VAL A 129 ? 0.54437 0.18555 0.30561 0.07008  -0.14812 0.01237  129 VAL A CG1 
1019 C  CG2 . VAL A 129 ? 0.54630 0.18013 0.33740 0.05882  -0.05238 0.06778  129 VAL A CG2 
1020 N  N   . VAL A 130 ? 0.44099 0.24477 0.29722 0.11504  -0.17179 -0.03419 130 VAL A N   
1021 C  CA  . VAL A 130 ? 0.40848 0.23211 0.28341 0.07856  -0.12784 -0.03167 130 VAL A CA  
1022 C  C   . VAL A 130 ? 0.42489 0.29467 0.27761 0.08518  -0.09612 -0.04572 130 VAL A C   
1023 O  O   . VAL A 130 ? 0.45237 0.31332 0.28031 0.06651  -0.10522 -0.04869 130 VAL A O   
1024 C  CB  . VAL A 130 ? 0.36204 0.22655 0.26563 0.08587  -0.09206 -0.01268 130 VAL A CB  
1025 C  CG1 . VAL A 130 ? 0.41588 0.25383 0.26009 0.06458  -0.10956 -0.04624 130 VAL A CG1 
1026 C  CG2 . VAL A 130 ? 0.44186 0.18007 0.27894 0.02020  -0.07592 -0.01454 130 VAL A CG2 
1027 N  N   . HIS A 131 ? 0.45498 0.27507 0.27911 0.03270  -0.14636 -0.03954 131 HIS A N   
1028 C  CA  . HIS A 131 ? 0.47634 0.36486 0.32383 0.03252  -0.13029 -0.06290 131 HIS A CA  
1029 C  C   . HIS A 131 ? 0.50809 0.33829 0.33988 0.04217  -0.17533 -0.08463 131 HIS A C   
1030 O  O   . HIS A 131 ? 0.54105 0.33430 0.33758 0.08346  -0.16570 -0.10040 131 HIS A O   
1031 C  CB  . HIS A 131 ? 0.44007 0.35531 0.33985 0.02723  -0.13852 -0.04740 131 HIS A CB  
1032 C  CG  . HIS A 131 ? 0.41648 0.44322 0.36740 0.03971  -0.10405 -0.00052 131 HIS A CG  
1033 N  ND1 . HIS A 131 ? 0.48603 0.47314 0.38965 0.05784  -0.08498 0.03943  131 HIS A ND1 
1034 C  CD2 . HIS A 131 ? 0.34909 0.50061 0.38423 0.08455  -0.08591 0.04485  131 HIS A CD2 
1035 C  CE1 . HIS A 131 ? 0.44390 0.47988 0.39438 0.03753  -0.07725 0.08243  131 HIS A CE1 
1036 N  NE2 . HIS A 131 ? 0.41723 0.43529 0.38800 0.04984  -0.08589 0.07784  131 HIS A NE2 
1037 N  N   . GLY A 132 ? 0.48542 0.33381 0.36870 0.08629  -0.17195 -0.09947 132 GLY A N   
1038 C  CA  . GLY A 132 ? 0.50126 0.29465 0.37621 0.14338  -0.10883 -0.11172 132 GLY A CA  
1039 C  C   . GLY A 132 ? 0.50212 0.34709 0.35678 0.14893  -0.12862 -0.12252 132 GLY A C   
1040 O  O   . GLY A 132 ? 0.54034 0.37670 0.36949 0.13100  -0.13194 -0.13028 132 GLY A O   
1041 N  N   . PHE A 133 ? 0.45427 0.26116 0.33148 0.13817  -0.08744 -0.09598 133 PHE A N   
1042 C  CA  . PHE A 133 ? 0.48806 0.31465 0.30245 0.15674  -0.11224 -0.05665 133 PHE A CA  
1043 C  C   . PHE A 133 ? 0.42515 0.38620 0.31642 0.16465  -0.15340 -0.04466 133 PHE A C   
1044 O  O   . PHE A 133 ? 0.51936 0.34962 0.32713 0.22615  -0.11356 -0.09610 133 PHE A O   
1045 C  CB  . PHE A 133 ? 0.46791 0.29882 0.26220 0.12143  -0.07061 -0.04165 133 PHE A CB  
1046 C  CG  . PHE A 133 ? 0.47541 0.28794 0.24691 0.11151  -0.03414 -0.05013 133 PHE A CG  
1047 C  CD1 . PHE A 133 ? 0.53252 0.30854 0.25643 0.13515  -0.02146 -0.00318 133 PHE A CD1 
1048 C  CD2 . PHE A 133 ? 0.50020 0.27945 0.21871 0.10532  -0.06504 0.01358  133 PHE A CD2 
1049 C  CE1 . PHE A 133 ? 0.52669 0.32800 0.24355 0.08116  -0.03896 -0.04166 133 PHE A CE1 
1050 C  CE2 . PHE A 133 ? 0.51378 0.23277 0.24641 -0.00340 -0.03131 -0.02269 133 PHE A CE2 
1051 C  CZ  . PHE A 133 ? 0.52634 0.27011 0.23880 0.01841  -0.00726 -0.03132 133 PHE A CZ  
1052 N  N   . LEU A 134 ? 0.39590 0.40703 0.32566 0.17389  -0.10902 -0.04538 134 LEU A N   
1053 C  CA  . LEU A 134 ? 0.37701 0.48871 0.35780 0.15338  -0.08218 -0.04165 134 LEU A CA  
1054 C  C   . LEU A 134 ? 0.44927 0.62022 0.34182 0.19916  -0.11557 -0.06700 134 LEU A C   
1055 O  O   . LEU A 134 ? 0.48954 0.72812 0.31516 0.21982  -0.11245 -0.09356 134 LEU A O   
1056 C  CB  . LEU A 134 ? 0.38091 0.42813 0.39017 0.16361  -0.02935 -0.01867 134 LEU A CB  
1057 C  CG  . LEU A 134 ? 0.42826 0.32560 0.42001 0.09767  0.04540  -0.02580 134 LEU A CG  
1058 C  CD1 . LEU A 134 ? 0.37828 0.34762 0.43379 0.05860  0.06691  -0.03081 134 LEU A CD1 
1059 C  CD2 . LEU A 134 ? 0.40833 0.37059 0.42249 0.09351  0.03665  0.00422  134 LEU A CD2 
1060 N  N   . ASP A 135 ? 0.55207 0.59167 0.35114 0.15430  -0.13579 -0.11158 135 ASP A N   
1061 C  CA  . ASP A 135 ? 0.61230 0.56255 0.36637 0.11700  -0.14401 -0.15750 135 ASP A CA  
1062 C  C   . ASP A 135 ? 0.60865 0.53545 0.34408 0.12528  -0.16182 -0.18722 135 ASP A C   
1063 O  O   . ASP A 135 ? 0.58386 0.59383 0.35546 0.16680  -0.15106 -0.21433 135 ASP A O   
1064 C  CB  . ASP A 135 ? 0.68488 0.56742 0.41322 0.11779  -0.10853 -0.20458 135 ASP A CB  
1065 C  CG  . ASP A 135 ? 0.72738 0.63663 0.44059 0.04957  -0.10908 -0.20840 135 ASP A CG  
1066 O  OD1 . ASP A 135 ? 0.71489 0.73830 0.43962 0.01407  -0.15841 -0.19788 135 ASP A OD1 
1067 O  OD2 . ASP A 135 ? 0.74511 0.64172 0.47099 0.02825  -0.10726 -0.18817 135 ASP A OD2 
1068 N  N   . GLU A 136 ? 0.59697 0.49550 0.35001 0.11978  -0.15664 -0.12588 136 GLU A N   
1069 C  CA  . GLU A 136 ? 0.58173 0.43736 0.35684 0.19482  -0.12285 -0.11080 136 GLU A CA  
1070 C  C   . GLU A 136 ? 0.55577 0.46751 0.35438 0.24226  -0.09164 -0.12101 136 GLU A C   
1071 O  O   . GLU A 136 ? 0.55897 0.51212 0.35574 0.26076  -0.07472 -0.16630 136 GLU A O   
1072 C  CB  . GLU A 136 ? 0.61578 0.40983 0.35963 0.18986  -0.11900 -0.09582 136 GLU A CB  
1073 C  CG  . GLU A 136 ? 0.63305 0.36477 0.34452 0.18796  -0.11955 -0.08756 136 GLU A CG  
1074 C  CD  . GLU A 136 ? 0.73482 0.42812 0.33738 0.15846  -0.08987 -0.07005 136 GLU A CD  
1075 O  OE1 . GLU A 136 ? 0.69552 0.39801 0.33999 0.11212  -0.07296 -0.05005 136 GLU A OE1 
1076 O  OE2 . GLU A 136 ? 0.79175 0.49029 0.31433 0.19397  -0.08484 -0.07580 136 GLU A OE2 
1077 N  N   . MET A 137 ? 0.56837 0.41779 0.33733 0.23863  -0.12404 -0.07089 137 MET A N   
1078 C  CA  . MET A 137 ? 0.59718 0.40655 0.32389 0.26948  -0.15542 -0.09505 137 MET A CA  
1079 C  C   . MET A 137 ? 0.67099 0.51694 0.33342 0.29548  -0.15386 -0.15490 137 MET A C   
1080 O  O   . MET A 137 ? 0.74336 0.52771 0.33442 0.32806  -0.13348 -0.13350 137 MET A O   
1081 C  CB  . MET A 137 ? 0.58357 0.41702 0.29964 0.27021  -0.16706 -0.11651 137 MET A CB  
1082 C  CG  . MET A 137 ? 0.55766 0.48635 0.30085 0.30209  -0.10767 -0.10373 137 MET A CG  
1083 S  SD  . MET A 137 ? 0.49202 0.50749 0.30365 0.26011  -0.02581 -0.06620 137 MET A SD  
1084 C  CE  . MET A 137 ? 0.54309 0.53953 0.32035 0.30382  -0.05968 -0.07241 137 MET A CE  
1085 N  N   . LEU A 138 ? 0.63364 0.62510 0.35481 0.31186  -0.16977 -0.18586 138 LEU A N   
1086 C  CA  . LEU A 138 ? 0.68365 0.67362 0.38683 0.27978  -0.20135 -0.20057 138 LEU A CA  
1087 C  C   . LEU A 138 ? 0.70632 0.71078 0.40316 0.28789  -0.21946 -0.19701 138 LEU A C   
1088 O  O   . LEU A 138 ? 0.77624 0.80239 0.40735 0.20460  -0.23410 -0.18320 138 LEU A O   
1089 C  CB  . LEU A 138 ? 0.71050 0.66168 0.40215 0.26305  -0.22196 -0.19955 138 LEU A CB  
1090 C  CG  . LEU A 138 ? 0.73932 0.64468 0.44367 0.29917  -0.21691 -0.09773 138 LEU A CG  
1091 C  CD1 . LEU A 138 ? 0.77191 0.59983 0.45540 0.33384  -0.22571 -0.09051 138 LEU A CD1 
1092 C  CD2 . LEU A 138 ? 0.77275 0.71734 0.46863 0.23358  -0.20263 -0.03826 138 LEU A CD2 
1093 N  N   . ALA A 139 ? 0.66235 0.62504 0.42119 0.31105  -0.18763 -0.21952 139 ALA A N   
1094 C  CA  . ALA A 139 ? 0.63981 0.58405 0.44877 0.30693  -0.14085 -0.21806 139 ALA A CA  
1095 C  C   . ALA A 139 ? 0.68666 0.67401 0.47079 0.27500  -0.07257 -0.22178 139 ALA A C   
1096 O  O   . ALA A 139 ? 0.74248 0.79724 0.49107 0.25131  -0.05999 -0.19010 139 ALA A O   
1097 C  CB  . ALA A 139 ? 0.67271 0.51875 0.44888 0.26738  -0.13264 -0.20066 139 ALA A CB  
1098 N  N   . ALA A 140 ? 0.71682 0.70991 0.49688 0.24078  0.00107  -0.16116 140 ALA A N   
1099 C  CA  . ALA A 140 ? 0.76495 0.73768 0.50032 0.17698  0.05411  -0.16588 140 ALA A CA  
1100 C  C   . ALA A 140 ? 0.78588 0.80112 0.50998 0.17788  0.07463  -0.15616 140 ALA A C   
1101 O  O   . ALA A 140 ? 0.83664 0.86776 0.52115 0.17144  0.10341  -0.14284 140 ALA A O   
1102 C  CB  . ALA A 140 ? 0.77115 0.74070 0.50292 0.09532  0.07197  -0.12818 140 ALA A CB  
1103 N  N   . GLY A 141 ? 0.73186 0.81788 0.49731 0.19349  0.02664  -0.14822 141 GLY A N   
1104 C  CA  . GLY A 141 ? 0.70090 0.84188 0.48485 0.19758  0.01729  -0.11151 141 GLY A CA  
1105 C  C   . GLY A 141 ? 0.69635 0.81509 0.48062 0.17777  0.03333  -0.11278 141 GLY A C   
1106 O  O   . GLY A 141 ? 0.70224 0.78028 0.46455 0.11430  0.07138  -0.09294 141 GLY A O   
1107 N  N   . PRO A 142 ? 0.69204 0.82818 0.48521 0.15434  -0.01930 -0.11171 142 PRO A N   
1108 C  CA  . PRO A 142 ? 0.66136 0.77223 0.47554 0.16196  -0.03668 -0.14406 142 PRO A CA  
1109 C  C   . PRO A 142 ? 0.60384 0.69340 0.43947 0.14477  -0.04829 -0.19287 142 PRO A C   
1110 O  O   . PRO A 142 ? 0.58642 0.64694 0.43915 0.11646  -0.04209 -0.18964 142 PRO A O   
1111 C  CB  . PRO A 142 ? 0.69186 0.81258 0.49450 0.16860  -0.01099 -0.11504 142 PRO A CB  
1112 C  CG  . PRO A 142 ? 0.72454 0.83268 0.50578 0.21296  -0.02428 -0.10685 142 PRO A CG  
1113 C  CD  . PRO A 142 ? 0.73995 0.85227 0.49427 0.18859  -0.01151 -0.12825 142 PRO A CD  
1114 N  N   . THR A 143 ? 0.53370 0.60767 0.38703 0.10862  -0.08805 -0.24794 143 THR A N   
1115 C  CA  . THR A 143 ? 0.48048 0.63110 0.36434 0.11598  -0.07917 -0.16282 143 THR A CA  
1116 C  C   . THR A 143 ? 0.43711 0.55190 0.34151 0.14376  -0.09722 -0.12931 143 THR A C   
1117 O  O   . THR A 143 ? 0.47353 0.53435 0.37934 0.16928  -0.13182 -0.16043 143 THR A O   
1118 C  CB  . THR A 143 ? 0.44552 0.71695 0.39086 0.05238  -0.03328 -0.08215 143 THR A CB  
1119 O  OG1 . THR A 143 ? 0.42759 0.70356 0.42049 -0.00390 -0.01118 -0.04525 143 THR A OG1 
1120 C  CG2 . THR A 143 ? 0.44976 0.80130 0.37690 0.03733  -0.04678 -0.11359 143 THR A CG2 
1121 N  N   . ALA A 144 ? 0.40610 0.42161 0.27703 0.09707  -0.06503 -0.09822 144 ALA A N   
1122 C  CA  . ALA A 144 ? 0.42061 0.43817 0.24277 0.05310  -0.05283 -0.06823 144 ALA A CA  
1123 C  C   . ALA A 144 ? 0.42586 0.44693 0.24639 0.09718  -0.05405 -0.09893 144 ALA A C   
1124 O  O   . ALA A 144 ? 0.41513 0.50365 0.25938 0.13192  -0.05066 -0.09889 144 ALA A O   
1125 C  CB  . ALA A 144 ? 0.48656 0.44472 0.25049 0.03005  -0.04634 0.01056  144 ALA A CB  
1126 N  N   . ASP A 145 ? 0.38147 0.38611 0.21645 0.10444  -0.00549 -0.10173 145 ASP A N   
1127 C  CA  . ASP A 145 ? 0.37517 0.36924 0.21546 0.08346  -0.02101 -0.06166 145 ASP A CA  
1128 C  C   . ASP A 145 ? 0.35031 0.33461 0.22731 0.13633  -0.01280 0.00386  145 ASP A C   
1129 O  O   . ASP A 145 ? 0.38971 0.36296 0.23511 0.14333  -0.02449 0.01152  145 ASP A O   
1130 C  CB  . ASP A 145 ? 0.37408 0.40045 0.25085 0.08674  -0.01770 -0.03377 145 ASP A CB  
1131 C  CG  . ASP A 145 ? 0.42937 0.39575 0.28576 0.12616  -0.05277 -0.03330 145 ASP A CG  
1132 O  OD1 . ASP A 145 ? 0.45819 0.36753 0.27430 0.13637  -0.01533 0.01040  145 ASP A OD1 
1133 O  OD2 . ASP A 145 ? 0.40850 0.48900 0.33087 0.10318  -0.05799 -0.03998 145 ASP A OD2 
1134 N  N   . LEU A 146 ? 0.34071 0.34088 0.21203 0.15414  -0.00466 -0.00758 146 LEU A N   
1135 C  CA  . LEU A 146 ? 0.31948 0.36071 0.19925 0.12896  -0.02078 -0.02351 146 LEU A CA  
1136 C  C   . LEU A 146 ? 0.34526 0.36151 0.20581 0.08481  -0.04540 -0.03488 146 LEU A C   
1137 O  O   . LEU A 146 ? 0.35512 0.30557 0.17520 0.06063  -0.01304 -0.03275 146 LEU A O   
1138 C  CB  . LEU A 146 ? 0.29173 0.36509 0.22028 0.11893  0.02133  -0.06429 146 LEU A CB  
1139 C  CG  . LEU A 146 ? 0.33653 0.38527 0.24569 0.08665  0.01453  -0.05927 146 LEU A CG  
1140 C  CD1 . LEU A 146 ? 0.31118 0.43011 0.22851 0.03535  -0.05736 -0.04681 146 LEU A CD1 
1141 C  CD2 . LEU A 146 ? 0.39285 0.41331 0.28038 0.19165  0.07428  -0.03915 146 LEU A CD2 
1142 N  N   . VAL A 147 ? 0.36897 0.33031 0.22050 0.09122  -0.03868 -0.01936 147 VAL A N   
1143 C  CA  . VAL A 147 ? 0.38141 0.29353 0.21665 0.08358  -0.01348 0.01493  147 VAL A CA  
1144 C  C   . VAL A 147 ? 0.40438 0.32628 0.23375 0.10750  0.02284  -0.02940 147 VAL A C   
1145 O  O   . VAL A 147 ? 0.36385 0.29755 0.24454 0.07767  -0.02488 0.01676  147 VAL A O   
1146 C  CB  . VAL A 147 ? 0.36456 0.34719 0.20143 0.09518  -0.00152 0.03992  147 VAL A CB  
1147 C  CG1 . VAL A 147 ? 0.33413 0.35433 0.19096 0.08341  0.03466  0.02430  147 VAL A CG1 
1148 C  CG2 . VAL A 147 ? 0.37587 0.38142 0.20595 0.10935  -0.01442 0.03526  147 VAL A CG2 
1149 N  N   . SER A 148 ? 0.35945 0.30227 0.24257 0.15261  0.05688  -0.04140 148 SER A N   
1150 C  CA  . SER A 148 ? 0.35920 0.35584 0.22619 0.16847  0.00122  -0.00898 148 SER A CA  
1151 C  C   . SER A 148 ? 0.37807 0.42201 0.24411 0.08101  -0.01380 -0.02677 148 SER A C   
1152 O  O   . SER A 148 ? 0.42178 0.37481 0.25795 0.13438  0.00026  -0.03772 148 SER A O   
1153 C  CB  . SER A 148 ? 0.35314 0.41721 0.20279 0.12838  0.00627  -0.00899 148 SER A CB  
1154 O  OG  . SER A 148 ? 0.36442 0.40747 0.23211 0.09131  0.00647  -0.02056 148 SER A OG  
1155 N  N   . GLN A 149 ? 0.32088 0.39078 0.23719 0.09993  -0.01762 -0.05399 149 GLN A N   
1156 C  CA  A GLN A 149 ? 0.36202 0.36620 0.23872 0.07818  -0.01097 -0.05447 149 GLN A CA  
1157 C  CA  B GLN A 149 ? 0.37518 0.36709 0.24559 0.08614  -0.02763 -0.05350 149 GLN A CA  
1158 C  C   . GLN A 149 ? 0.35739 0.31679 0.25106 0.11235  -0.00135 -0.05421 149 GLN A C   
1159 O  O   . GLN A 149 ? 0.45248 0.29548 0.25502 0.11419  -0.01124 -0.07432 149 GLN A O   
1160 C  CB  A GLN A 149 ? 0.38117 0.38518 0.23659 0.08023  -0.00915 -0.05365 149 GLN A CB  
1161 C  CB  B GLN A 149 ? 0.42795 0.37542 0.25985 0.13354  -0.05073 -0.05367 149 GLN A CB  
1162 C  CG  A GLN A 149 ? 0.38760 0.41768 0.22994 0.10229  -0.00037 -0.07708 149 GLN A CG  
1163 C  CG  B GLN A 149 ? 0.46865 0.40980 0.26153 0.16246  -0.06346 -0.10131 149 GLN A CG  
1164 C  CD  A GLN A 149 ? 0.43517 0.44400 0.23083 0.09817  0.00742  -0.07705 149 GLN A CD  
1165 C  CD  B GLN A 149 ? 0.50401 0.45815 0.27747 0.20485  -0.07612 -0.10031 149 GLN A CD  
1166 O  OE1 A GLN A 149 ? 0.49128 0.47431 0.25261 0.11326  0.01506  -0.06591 149 GLN A OE1 
1167 O  OE1 B GLN A 149 ? 0.53548 0.42626 0.30583 0.22283  -0.07948 -0.14505 149 GLN A OE1 
1168 N  NE2 A GLN A 149 ? 0.46367 0.41653 0.21038 0.07841  0.02132  -0.09455 149 GLN A NE2 
1169 N  NE2 B GLN A 149 ? 0.50290 0.47116 0.27663 0.17517  -0.06362 -0.05562 149 GLN A NE2 
1170 N  N   . PHE A 150 ? 0.30021 0.32959 0.23221 0.08996  -0.00729 -0.07471 150 PHE A N   
1171 C  CA  . PHE A 150 ? 0.29008 0.27690 0.21671 0.04014  -0.02014 -0.05709 150 PHE A CA  
1172 C  C   . PHE A 150 ? 0.30277 0.29473 0.23479 0.10511  -0.01391 -0.02713 150 PHE A C   
1173 O  O   . PHE A 150 ? 0.35511 0.22624 0.22195 0.04855  -0.02920 -0.01718 150 PHE A O   
1174 C  CB  . PHE A 150 ? 0.31743 0.28114 0.19946 0.10699  -0.02421 -0.04807 150 PHE A CB  
1175 C  CG  . PHE A 150 ? 0.37465 0.26649 0.17584 0.08950  0.00564  -0.07058 150 PHE A CG  
1176 C  CD1 . PHE A 150 ? 0.37158 0.31705 0.16663 0.05441  -0.00811 -0.06015 150 PHE A CD1 
1177 C  CD2 . PHE A 150 ? 0.42253 0.23168 0.18922 0.04809  0.01510  -0.07865 150 PHE A CD2 
1178 C  CE1 . PHE A 150 ? 0.34794 0.27720 0.17066 0.07476  -0.02648 -0.06725 150 PHE A CE1 
1179 C  CE2 . PHE A 150 ? 0.42756 0.22835 0.22456 0.04498  -0.00177 -0.05110 150 PHE A CE2 
1180 C  CZ  . PHE A 150 ? 0.42073 0.25504 0.20190 0.08042  -0.01678 0.01050  150 PHE A CZ  
1181 N  N   . ALA A 151 ? 0.32802 0.27693 0.23104 0.09397  0.01323  -0.05606 151 ALA A N   
1182 C  CA  . ALA A 151 ? 0.35583 0.22319 0.20702 0.05348  -0.01720 -0.01109 151 ALA A CA  
1183 C  C   . ALA A 151 ? 0.26458 0.26151 0.19599 0.09912  -0.01916 -0.06290 151 ALA A C   
1184 O  O   . ALA A 151 ? 0.34398 0.22981 0.20969 0.06864  -0.03930 -0.02603 151 ALA A O   
1185 C  CB  . ALA A 151 ? 0.32723 0.24715 0.21553 0.08210  -0.03342 0.02396  151 ALA A CB  
1186 N  N   . LEU A 152 ? 0.25792 0.24120 0.19155 0.08339  -0.01490 -0.01294 152 LEU A N   
1187 C  CA  . LEU A 152 ? 0.26068 0.30893 0.19739 0.05835  -0.02765 -0.02942 152 LEU A CA  
1188 C  C   . LEU A 152 ? 0.35481 0.32298 0.19785 0.10054  -0.02768 -0.04470 152 LEU A C   
1189 O  O   . LEU A 152 ? 0.34259 0.31642 0.21847 0.10685  -0.06627 -0.02892 152 LEU A O   
1190 C  CB  . LEU A 152 ? 0.31720 0.38716 0.23833 0.01137  -0.01470 -0.02198 152 LEU A CB  
1191 C  CG  . LEU A 152 ? 0.35198 0.48814 0.28889 -0.07825 0.03529  -0.11079 152 LEU A CG  
1192 C  CD1 . LEU A 152 ? 0.38775 0.45738 0.31023 -0.08480 0.03191  -0.08773 152 LEU A CD1 
1193 C  CD2 . LEU A 152 ? 0.53707 0.64087 0.35767 -0.10280 0.00538  -0.08885 152 LEU A CD2 
1194 N  N   . PRO A 153 ? 0.36261 0.28077 0.20064 0.09973  -0.01414 -0.03849 153 PRO A N   
1195 C  CA  . PRO A 153 ? 0.39533 0.30804 0.19842 0.14142  0.00531  -0.02277 153 PRO A CA  
1196 C  C   . PRO A 153 ? 0.37066 0.28965 0.21102 0.12740  -0.00982 -0.02328 153 PRO A C   
1197 O  O   . PRO A 153 ? 0.43816 0.29433 0.21654 0.10917  -0.03297 -0.01331 153 PRO A O   
1198 C  CB  . PRO A 153 ? 0.45208 0.35596 0.19609 0.11648  0.01123  -0.05278 153 PRO A CB  
1199 C  CG  . PRO A 153 ? 0.48523 0.42006 0.21197 0.16263  0.00840  -0.04274 153 PRO A CG  
1200 C  CD  . PRO A 153 ? 0.38003 0.35767 0.20474 0.17270  0.03794  -0.05200 153 PRO A CD  
1201 N  N   . VAL A 154 ? 0.36877 0.27036 0.20694 0.12288  -0.04775 -0.02819 154 VAL A N   
1202 C  CA  . VAL A 154 ? 0.34208 0.31553 0.20981 0.06564  -0.02103 -0.02803 154 VAL A CA  
1203 C  C   . VAL A 154 ? 0.34653 0.25783 0.21075 0.07553  -0.04796 -0.02406 154 VAL A C   
1204 O  O   . VAL A 154 ? 0.33102 0.22319 0.19692 0.06106  -0.06335 -0.00272 154 VAL A O   
1205 C  CB  . VAL A 154 ? 0.34783 0.23077 0.19327 0.06488  -0.01122 -0.06134 154 VAL A CB  
1206 C  CG1 . VAL A 154 ? 0.32515 0.23309 0.21924 0.08232  -0.00200 -0.04937 154 VAL A CG1 
1207 C  CG2 . VAL A 154 ? 0.41051 0.25989 0.21407 0.02310  -0.05954 -0.05418 154 VAL A CG2 
1208 N  N   . PRO A 155 ? 0.35676 0.23924 0.20924 0.04956  -0.05335 -0.00804 155 PRO A N   
1209 C  CA  . PRO A 155 ? 0.29125 0.25621 0.19653 0.09677  -0.03684 -0.01115 155 PRO A CA  
1210 C  C   . PRO A 155 ? 0.25253 0.24093 0.19822 0.07149  -0.03844 -0.04401 155 PRO A C   
1211 O  O   . PRO A 155 ? 0.30604 0.24557 0.20313 0.01606  -0.07313 0.01130  155 PRO A O   
1212 C  CB  . PRO A 155 ? 0.29889 0.23691 0.19693 0.05338  -0.00115 0.01651  155 PRO A CB  
1213 C  CG  . PRO A 155 ? 0.24983 0.19715 0.20265 0.00543  -0.02584 -0.02908 155 PRO A CG  
1214 C  CD  . PRO A 155 ? 0.34440 0.21565 0.21347 0.02886  -0.05813 -0.01358 155 PRO A CD  
1215 N  N   . SER A 156 ? 0.26794 0.26140 0.21713 0.05382  -0.00105 -0.05279 156 SER A N   
1216 C  CA  . SER A 156 ? 0.24178 0.25389 0.22800 0.08767  -0.00637 -0.01847 156 SER A CA  
1217 C  C   . SER A 156 ? 0.26959 0.28020 0.21925 0.03330  -0.00445 -0.02992 156 SER A C   
1218 O  O   . SER A 156 ? 0.33263 0.31388 0.21730 0.06450  0.00508  -0.02673 156 SER A O   
1219 C  CB  . SER A 156 ? 0.23300 0.32084 0.24570 0.04422  -0.00481 0.00835  156 SER A CB  
1220 O  OG  . SER A 156 ? 0.30414 0.44477 0.25622 0.05612  -0.03805 0.03682  156 SER A OG  
1221 N  N   . MET A 157 ? 0.33660 0.23360 0.22114 0.06760  -0.00781 -0.02268 157 MET A N   
1222 C  CA  . MET A 157 ? 0.32462 0.23087 0.23251 0.04226  -0.02715 -0.03179 157 MET A CA  
1223 C  C   . MET A 157 ? 0.26160 0.19636 0.21855 0.06988  -0.06617 0.00424  157 MET A C   
1224 O  O   . MET A 157 ? 0.29370 0.22217 0.24125 0.04518  -0.08415 -0.00840 157 MET A O   
1225 C  CB  . MET A 157 ? 0.37079 0.17571 0.27369 0.09702  -0.05667 -0.04685 157 MET A CB  
1226 C  CG  . MET A 157 ? 0.43814 0.15887 0.30549 0.05936  -0.06594 -0.04200 157 MET A CG  
1227 S  SD  . MET A 157 ? 0.51274 0.26604 0.29566 0.08604  -0.05738 -0.03490 157 MET A SD  
1228 C  CE  . MET A 157 ? 0.53564 0.30527 0.31652 0.11312  -0.09089 -0.05196 157 MET A CE  
1229 N  N   . VAL A 158 ? 0.25846 0.20696 0.20942 0.03961  -0.05339 -0.02130 158 VAL A N   
1230 C  CA  . VAL A 158 ? 0.26829 0.24848 0.20750 0.03890  -0.03870 -0.01945 158 VAL A CA  
1231 C  C   . VAL A 158 ? 0.20927 0.17722 0.20653 0.02613  -0.09067 -0.00251 158 VAL A C   
1232 O  O   . VAL A 158 ? 0.28386 0.24044 0.19036 0.04675  -0.07669 0.00746  158 VAL A O   
1233 C  CB  . VAL A 158 ? 0.27270 0.21309 0.21649 0.05286  -0.02560 -0.03542 158 VAL A CB  
1234 C  CG1 . VAL A 158 ? 0.23813 0.26381 0.23654 0.00384  0.00791  0.00530  158 VAL A CG1 
1235 C  CG2 . VAL A 158 ? 0.30754 0.18844 0.24530 -0.03051 -0.05049 -0.05461 158 VAL A CG2 
1236 N  N   . ILE A 159 ? 0.27793 0.17039 0.21249 0.01515  -0.03915 -0.03077 159 ILE A N   
1237 C  CA  . ILE A 159 ? 0.26807 0.19420 0.24059 0.04300  -0.03919 -0.05615 159 ILE A CA  
1238 C  C   . ILE A 159 ? 0.28307 0.27085 0.26385 0.03784  -0.03339 -0.05897 159 ILE A C   
1239 O  O   . ILE A 159 ? 0.24227 0.23417 0.25062 0.01573  -0.01358 -0.02102 159 ILE A O   
1240 C  CB  . ILE A 159 ? 0.27125 0.21588 0.22373 0.06828  0.01033  -0.06629 159 ILE A CB  
1241 C  CG1 . ILE A 159 ? 0.28020 0.22238 0.23816 0.06116  0.03977  -0.02390 159 ILE A CG1 
1242 C  CG2 . ILE A 159 ? 0.22650 0.27913 0.24094 0.00901  -0.00586 -0.00999 159 ILE A CG2 
1243 C  CD1 . ILE A 159 ? 0.35991 0.22917 0.24487 -0.00327 0.05275  -0.00705 159 ILE A CD1 
1244 N  N   . CYS A 160 ? 0.27936 0.20680 0.27825 0.07182  -0.03727 -0.01803 160 CYS A N   
1245 C  CA  . CYS A 160 ? 0.26801 0.19278 0.27447 0.12373  0.00476  -0.02505 160 CYS A CA  
1246 C  C   . CYS A 160 ? 0.31779 0.15638 0.28710 0.05513  -0.03451 0.00890  160 CYS A C   
1247 O  O   . CYS A 160 ? 0.31039 0.25707 0.26373 0.08459  -0.03159 0.00469  160 CYS A O   
1248 C  CB  . CYS A 160 ? 0.26375 0.29906 0.28411 0.08877  0.01241  -0.00935 160 CYS A CB  
1249 S  SG  . CYS A 160 ? 0.31394 0.43645 0.27723 0.04408  0.01119  0.03538  160 CYS A SG  
1250 N  N   . ARG A 161 ? 0.31131 0.23543 0.29744 -0.03141 -0.04082 -0.00045 161 ARG A N   
1251 C  CA  . ARG A 161 ? 0.32310 0.22548 0.29796 -0.01633 -0.05181 -0.04714 161 ARG A CA  
1252 C  C   . ARG A 161 ? 0.32612 0.21608 0.26923 -0.00034 -0.05275 -0.03742 161 ARG A C   
1253 O  O   . ARG A 161 ? 0.29768 0.25866 0.28187 -0.03748 -0.07424 0.02227  161 ARG A O   
1254 C  CB  . ARG A 161 ? 0.36046 0.29953 0.31467 -0.00782 -0.06509 -0.08626 161 ARG A CB  
1255 C  CG  . ARG A 161 ? 0.47923 0.30397 0.38885 0.08865  -0.02296 -0.01941 161 ARG A CG  
1256 C  CD  . ARG A 161 ? 0.53459 0.43880 0.44054 0.06742  -0.03351 -0.01363 161 ARG A CD  
1257 N  NE  . ARG A 161 ? 0.56283 0.44282 0.47536 -0.00270 -0.03213 -0.03378 161 ARG A NE  
1258 C  CZ  . ARG A 161 ? 0.61111 0.45937 0.48574 -0.03833 -0.03188 -0.05196 161 ARG A CZ  
1259 N  NH1 . ARG A 161 ? 0.58696 0.40004 0.49135 0.00790  -0.05573 -0.03000 161 ARG A NH1 
1260 N  NH2 . ARG A 161 ? 0.61723 0.48093 0.47471 -0.10338 -0.05212 -0.08710 161 ARG A NH2 
1261 N  N   . LEU A 162 ? 0.28721 0.20776 0.26136 0.04360  -0.03871 -0.04499 162 LEU A N   
1262 C  CA  . LEU A 162 ? 0.28248 0.20130 0.23017 0.04726  -0.02937 -0.02965 162 LEU A CA  
1263 C  C   . LEU A 162 ? 0.28381 0.22713 0.23895 -0.02668 -0.07055 -0.01918 162 LEU A C   
1264 O  O   . LEU A 162 ? 0.24503 0.28773 0.24077 0.01234  -0.06795 0.01562  162 LEU A O   
1265 C  CB  . LEU A 162 ? 0.28694 0.21517 0.24311 0.04166  -0.05030 -0.02849 162 LEU A CB  
1266 C  CG  . LEU A 162 ? 0.22988 0.30408 0.24929 0.01567  -0.05892 -0.04073 162 LEU A CG  
1267 C  CD1 . LEU A 162 ? 0.26853 0.24675 0.29102 0.03670  -0.01426 0.00085  162 LEU A CD1 
1268 C  CD2 . LEU A 162 ? 0.24469 0.33727 0.23172 -0.02937 -0.07063 -0.02562 162 LEU A CD2 
1269 N  N   . LEU A 163 ? 0.21603 0.21587 0.24556 0.01338  -0.04095 -0.01791 163 LEU A N   
1270 C  CA  . LEU A 163 ? 0.29028 0.14532 0.24180 -0.01244 -0.05773 0.01512  163 LEU A CA  
1271 C  C   . LEU A 163 ? 0.29182 0.18640 0.23433 -0.00992 -0.04530 0.03726  163 LEU A C   
1272 O  O   . LEU A 163 ? 0.25295 0.22230 0.23888 0.04074  -0.03524 0.01378  163 LEU A O   
1273 C  CB  . LEU A 163 ? 0.30884 0.18643 0.23142 -0.01013 -0.02182 0.03222  163 LEU A CB  
1274 C  CG  . LEU A 163 ? 0.37127 0.15479 0.21639 -0.00287 -0.01841 -0.00544 163 LEU A CG  
1275 C  CD1 . LEU A 163 ? 0.31311 0.22570 0.22422 -0.02893 -0.07122 0.04121  163 LEU A CD1 
1276 C  CD2 . LEU A 163 ? 0.39463 0.17778 0.21520 0.02059  -0.01696 -0.03179 163 LEU A CD2 
1277 N  N   . GLY A 164 ? 0.28204 0.17861 0.25824 0.04688  -0.01433 0.02672  164 GLY A N   
1278 C  CA  . GLY A 164 ? 0.28955 0.19968 0.26172 0.05749  -0.02373 -0.01097 164 GLY A CA  
1279 C  C   . GLY A 164 ? 0.25151 0.20733 0.27026 0.06019  -0.05158 0.01543  164 GLY A C   
1280 O  O   . GLY A 164 ? 0.29802 0.24458 0.29757 0.06521  -0.06911 0.02072  164 GLY A O   
1281 N  N   . VAL A 165 ? 0.32384 0.21309 0.24043 0.05830  -0.05511 0.00112  165 VAL A N   
1282 C  CA  . VAL A 165 ? 0.33257 0.20526 0.28130 0.06926  0.00603  -0.01123 165 VAL A CA  
1283 C  C   . VAL A 165 ? 0.27408 0.24135 0.30160 0.10751  0.00658  -0.00283 165 VAL A C   
1284 O  O   . VAL A 165 ? 0.28679 0.28728 0.32478 0.06133  -0.07110 -0.01039 165 VAL A O   
1285 C  CB  . VAL A 165 ? 0.31890 0.22672 0.28238 0.04987  0.03498  -0.04304 165 VAL A CB  
1286 C  CG1 . VAL A 165 ? 0.32171 0.27913 0.30446 0.03963  0.04986  -0.06926 165 VAL A CG1 
1287 C  CG2 . VAL A 165 ? 0.26596 0.22780 0.29389 0.05318  0.03149  -0.01933 165 VAL A CG2 
1288 N  N   . PRO A 166 ? 0.23753 0.22764 0.31633 0.06910  0.00032  0.00288  166 PRO A N   
1289 C  CA  . PRO A 166 ? 0.27805 0.22383 0.32332 0.10421  -0.02891 -0.03760 166 PRO A CA  
1290 C  C   . PRO A 166 ? 0.35419 0.30911 0.32707 0.04471  -0.06209 -0.07206 166 PRO A C   
1291 O  O   . PRO A 166 ? 0.36495 0.25634 0.35444 0.08939  -0.03548 -0.07950 166 PRO A O   
1292 C  CB  . PRO A 166 ? 0.31938 0.28615 0.33673 0.04738  -0.01047 -0.02877 166 PRO A CB  
1293 C  CG  . PRO A 166 ? 0.31681 0.30406 0.34288 0.06658  -0.00896 -0.05825 166 PRO A CG  
1294 C  CD  . PRO A 166 ? 0.24031 0.27336 0.32584 0.08330  0.00910  -0.04520 166 PRO A CD  
1295 N  N   . TYR A 167 ? 0.41749 0.24539 0.30589 0.08875  -0.07452 -0.07945 167 TYR A N   
1296 C  CA  . TYR A 167 ? 0.44474 0.31875 0.29125 0.10633  -0.10225 -0.07469 167 TYR A CA  
1297 C  C   . TYR A 167 ? 0.49758 0.37688 0.30368 0.15236  -0.08704 -0.09390 167 TYR A C   
1298 O  O   . TYR A 167 ? 0.62492 0.41496 0.28331 0.12845  -0.07651 -0.11063 167 TYR A O   
1299 C  CB  . TYR A 167 ? 0.41224 0.31315 0.29926 0.08739  -0.09944 -0.03789 167 TYR A CB  
1300 C  CG  . TYR A 167 ? 0.42190 0.37641 0.29855 0.15857  -0.05427 -0.01215 167 TYR A CG  
1301 C  CD1 . TYR A 167 ? 0.37769 0.34729 0.30733 0.13882  -0.01318 0.01372  167 TYR A CD1 
1302 C  CD2 . TYR A 167 ? 0.47085 0.41082 0.30888 0.15486  -0.01717 -0.01918 167 TYR A CD2 
1303 C  CE1 . TYR A 167 ? 0.40742 0.44357 0.29935 0.10298  -0.01728 0.02788  167 TYR A CE1 
1304 C  CE2 . TYR A 167 ? 0.45695 0.44632 0.30263 0.11552  -0.00291 -0.02636 167 TYR A CE2 
1305 C  CZ  . TYR A 167 ? 0.41767 0.39611 0.31761 0.10120  -0.05033 0.01294  167 TYR A CZ  
1306 O  OH  . TYR A 167 ? 0.33580 0.38995 0.34388 0.05953  -0.08272 -0.01032 167 TYR A OH  
1307 N  N   . ALA A 168 ? 0.50743 0.35609 0.33275 0.14405  -0.02616 -0.07351 168 ALA A N   
1308 C  CA  . ALA A 168 ? 0.52522 0.33923 0.36228 0.17519  0.00570  -0.08314 168 ALA A CA  
1309 C  C   . ALA A 168 ? 0.52216 0.38883 0.36909 0.14317  0.00587  -0.10943 168 ALA A C   
1310 O  O   . ALA A 168 ? 0.54486 0.46627 0.37494 0.10879  -0.00386 -0.06729 168 ALA A O   
1311 C  CB  . ALA A 168 ? 0.49150 0.39022 0.36111 0.14159  -0.00327 -0.08570 168 ALA A CB  
1312 N  N   . ASP A 169 ? 0.45573 0.34542 0.37181 0.14522  -0.04645 -0.09192 169 ASP A N   
1313 C  CA  . ASP A 169 ? 0.48523 0.34441 0.35543 0.15086  -0.04463 -0.08606 169 ASP A CA  
1314 C  C   . ASP A 169 ? 0.42708 0.34494 0.30943 0.11212  -0.03184 -0.06688 169 ASP A C   
1315 O  O   . ASP A 169 ? 0.43255 0.37707 0.30175 0.05275  -0.01932 -0.05205 169 ASP A O   
1316 C  CB  . ASP A 169 ? 0.46202 0.36860 0.36644 0.18045  -0.03755 -0.06973 169 ASP A CB  
1317 C  CG  . ASP A 169 ? 0.47938 0.38176 0.39835 0.12864  -0.01444 -0.04883 169 ASP A CG  
1318 O  OD1 . ASP A 169 ? 0.50505 0.46424 0.42900 0.15807  -0.02293 -0.01712 169 ASP A OD1 
1319 O  OD2 . ASP A 169 ? 0.43673 0.38678 0.41590 0.11939  -0.05607 -0.01197 169 ASP A OD2 
1320 N  N   . HIS A 170 ? 0.42877 0.39988 0.28875 0.10157  0.03266  -0.04198 170 HIS A N   
1321 C  CA  . HIS A 170 ? 0.44046 0.38586 0.28542 0.11421  0.06000  -0.07710 170 HIS A CA  
1322 C  C   . HIS A 170 ? 0.42059 0.40570 0.29844 0.09137  0.06199  -0.09666 170 HIS A C   
1323 O  O   . HIS A 170 ? 0.43684 0.36105 0.29899 0.02739  0.04385  -0.05615 170 HIS A O   
1324 C  CB  . HIS A 170 ? 0.45759 0.38625 0.28446 0.07593  0.07651  -0.07439 170 HIS A CB  
1325 C  CG  . HIS A 170 ? 0.50275 0.37981 0.28270 0.18059  0.03199  -0.09808 170 HIS A CG  
1326 N  ND1 . HIS A 170 ? 0.57449 0.41333 0.28869 0.13189  0.02533  -0.07808 170 HIS A ND1 
1327 C  CD2 . HIS A 170 ? 0.51073 0.45085 0.26672 0.19852  0.01796  -0.08565 170 HIS A CD2 
1328 C  CE1 . HIS A 170 ? 0.58890 0.50635 0.28536 0.13491  -0.00302 -0.06771 170 HIS A CE1 
1329 N  NE2 . HIS A 170 ? 0.56527 0.49653 0.28180 0.17474  -0.01982 -0.07155 170 HIS A NE2 
1330 N  N   . GLU A 171 ? 0.40693 0.44579 0.31877 0.12182  0.05006  -0.06603 171 GLU A N   
1331 C  CA  . GLU A 171 ? 0.44022 0.52205 0.33325 0.09357  0.05549  -0.10018 171 GLU A CA  
1332 C  C   . GLU A 171 ? 0.43054 0.46258 0.34534 0.09252  0.03385  -0.03322 171 GLU A C   
1333 O  O   . GLU A 171 ? 0.45410 0.44485 0.36947 0.10910  -0.01589 -0.00640 171 GLU A O   
1334 C  CB  . GLU A 171 ? 0.45657 0.59660 0.36406 0.08331  0.06485  -0.13125 171 GLU A CB  
1335 C  CG  . GLU A 171 ? 0.51587 0.68179 0.35959 0.05614  0.06405  -0.21193 171 GLU A CG  
1336 C  CD  . GLU A 171 ? 0.55195 0.77063 0.39185 0.02835  0.08343  -0.19331 171 GLU A CD  
1337 O  OE1 . GLU A 171 ? 0.60739 0.74967 0.41451 0.10667  0.10870  -0.17595 171 GLU A OE1 
1338 O  OE2 . GLU A 171 ? 0.58350 0.83369 0.39616 -0.03089 0.06673  -0.18864 171 GLU A OE2 
1339 N  N   . PHE A 172 ? 0.43768 0.46731 0.33369 0.13223  0.01069  -0.04864 172 PHE A N   
1340 C  CA  . PHE A 172 ? 0.39560 0.43169 0.32688 0.12026  0.00215  -0.03212 172 PHE A CA  
1341 C  C   . PHE A 172 ? 0.39994 0.40013 0.31008 0.16392  0.02969  0.01047  172 PHE A C   
1342 O  O   . PHE A 172 ? 0.35461 0.45300 0.32186 0.09824  0.01718  -0.00093 172 PHE A O   
1343 C  CB  . PHE A 172 ? 0.38480 0.44619 0.33537 0.14669  -0.03327 -0.02715 172 PHE A CB  
1344 C  CG  . PHE A 172 ? 0.41663 0.45277 0.35609 0.13994  -0.06503 -0.05339 172 PHE A CG  
1345 C  CD1 . PHE A 172 ? 0.46082 0.51283 0.36755 0.12194  -0.09076 -0.07672 172 PHE A CD1 
1346 C  CD2 . PHE A 172 ? 0.41093 0.43361 0.35470 0.15803  -0.06444 -0.08295 172 PHE A CD2 
1347 C  CE1 . PHE A 172 ? 0.49231 0.56240 0.37634 0.08662  -0.10082 -0.06560 172 PHE A CE1 
1348 C  CE2 . PHE A 172 ? 0.44027 0.46482 0.38499 0.12703  -0.07267 -0.07644 172 PHE A CE2 
1349 C  CZ  . PHE A 172 ? 0.48710 0.50657 0.39523 0.08327  -0.06320 -0.08698 172 PHE A CZ  
1350 N  N   . PHE A 173 ? 0.40479 0.37031 0.30062 0.09804  0.02319  -0.00230 173 PHE A N   
1351 C  CA  . PHE A 173 ? 0.32725 0.35923 0.26002 0.11131  0.03927  0.00870  173 PHE A CA  
1352 C  C   . PHE A 173 ? 0.27617 0.33419 0.25311 0.07472  0.02433  -0.01058 173 PHE A C   
1353 O  O   . PHE A 173 ? 0.36314 0.32148 0.25986 0.07779  0.04757  0.01414  173 PHE A O   
1354 C  CB  . PHE A 173 ? 0.37363 0.40552 0.26235 0.01021  -0.00906 -0.00370 173 PHE A CB  
1355 C  CG  . PHE A 173 ? 0.35279 0.36036 0.24995 0.05898  -0.00702 -0.01548 173 PHE A CG  
1356 C  CD1 . PHE A 173 ? 0.34188 0.40772 0.23559 0.04537  0.01219  -0.03448 173 PHE A CD1 
1357 C  CD2 . PHE A 173 ? 0.38623 0.38970 0.26558 0.02231  0.00482  -0.02603 173 PHE A CD2 
1358 C  CE1 . PHE A 173 ? 0.40534 0.44263 0.24723 0.04360  0.01762  -0.00762 173 PHE A CE1 
1359 C  CE2 . PHE A 173 ? 0.35729 0.37366 0.27572 0.09201  0.01096  0.01204  173 PHE A CE2 
1360 C  CZ  . PHE A 173 ? 0.37411 0.44319 0.26274 0.08363  0.02059  0.01219  173 PHE A CZ  
1361 N  N   . GLN A 174 ? 0.31701 0.41061 0.23317 0.05539  0.00186  0.01025  174 GLN A N   
1362 C  CA  . GLN A 174 ? 0.27185 0.39868 0.25148 0.02373  -0.00011 -0.02956 174 GLN A CA  
1363 C  C   . GLN A 174 ? 0.32771 0.36553 0.27116 0.07993  0.04859  -0.00964 174 GLN A C   
1364 O  O   . GLN A 174 ? 0.34645 0.37153 0.26574 0.06080  0.03877  0.05351  174 GLN A O   
1365 C  CB  . GLN A 174 ? 0.26798 0.42531 0.26887 0.00740  -0.01426 -0.02848 174 GLN A CB  
1366 C  CG  . GLN A 174 ? 0.29912 0.37841 0.27955 0.01152  0.00621  -0.02230 174 GLN A CG  
1367 C  CD  . GLN A 174 ? 0.34953 0.40794 0.29932 0.05409  0.02345  -0.00859 174 GLN A CD  
1368 O  OE1 . GLN A 174 ? 0.40454 0.44883 0.30170 0.05216  0.03931  -0.04113 174 GLN A OE1 
1369 N  NE2 . GLN A 174 ? 0.32251 0.44117 0.30738 0.09255  0.01000  0.02210  174 GLN A NE2 
1370 N  N   . ASP A 175 ? 0.26487 0.37134 0.24690 0.10609  0.06583  0.03241  175 ASP A N   
1371 C  CA  . ASP A 175 ? 0.28519 0.42478 0.25726 0.05237  0.05561  0.01647  175 ASP A CA  
1372 C  C   . ASP A 175 ? 0.27160 0.40214 0.25854 0.05962  0.03423  0.04487  175 ASP A C   
1373 O  O   . ASP A 175 ? 0.28508 0.37859 0.29524 0.04300  -0.01880 0.05798  175 ASP A O   
1374 C  CB  . ASP A 175 ? 0.34834 0.48148 0.29637 0.07321  0.08348  0.00916  175 ASP A CB  
1375 C  CG  . ASP A 175 ? 0.43348 0.55630 0.32691 0.00388  0.10938  -0.02036 175 ASP A CG  
1376 O  OD1 . ASP A 175 ? 0.51564 0.58217 0.36500 -0.08775 0.14595  -0.02753 175 ASP A OD1 
1377 O  OD2 . ASP A 175 ? 0.43098 0.58014 0.34979 0.04270  0.10892  -0.07688 175 ASP A OD2 
1378 N  N   . ALA A 176 ? 0.33378 0.41587 0.22919 0.05666  0.05125  0.02063  176 ALA A N   
1379 C  CA  . ALA A 176 ? 0.30157 0.40710 0.25137 0.05679  0.05533  0.02266  176 ALA A CA  
1380 C  C   . ALA A 176 ? 0.22229 0.34615 0.28451 0.00376  0.05149  0.00981  176 ALA A C   
1381 O  O   . ALA A 176 ? 0.33388 0.33391 0.30712 0.05782  0.02787  0.00043  176 ALA A O   
1382 C  CB  . ALA A 176 ? 0.30101 0.43300 0.25000 0.08949  0.03682  0.02352  176 ALA A CB  
1383 N  N   . SER A 177 ? 0.20310 0.33066 0.29327 0.05010  0.01433  0.03153  177 SER A N   
1384 C  CA  . SER A 177 ? 0.26984 0.32283 0.31057 0.13127  0.01805  0.07257  177 SER A CA  
1385 C  C   . SER A 177 ? 0.32505 0.35893 0.30706 0.06627  0.07335  0.05284  177 SER A C   
1386 O  O   . SER A 177 ? 0.33652 0.42426 0.33144 0.12031  0.04017  0.06006  177 SER A O   
1387 C  CB  . SER A 177 ? 0.25970 0.29847 0.34441 0.07085  0.06187  0.03773  177 SER A CB  
1388 O  OG  . SER A 177 ? 0.32987 0.37382 0.34305 0.05401  0.03856  0.03275  177 SER A OG  
1389 N  N   . LYS A 178 ? 0.32436 0.40540 0.28498 0.07903  0.05574  0.09019  178 LYS A N   
1390 C  CA  . LYS A 178 ? 0.32566 0.39239 0.30045 0.08342  0.05278  0.08276  178 LYS A CA  
1391 C  C   . LYS A 178 ? 0.35118 0.36226 0.32957 0.13228  0.04119  0.06709  178 LYS A C   
1392 O  O   . LYS A 178 ? 0.38612 0.35783 0.32929 0.05550  0.00145  0.07700  178 LYS A O   
1393 C  CB  . LYS A 178 ? 0.36625 0.44434 0.27742 0.10208  0.04390  0.07515  178 LYS A CB  
1394 C  CG  . LYS A 178 ? 0.44542 0.45407 0.28181 0.07370  0.03845  0.10208  178 LYS A CG  
1395 C  CD  . LYS A 178 ? 0.49141 0.51600 0.28139 0.01879  0.09066  0.06961  178 LYS A CD  
1396 C  CE  . LYS A 178 ? 0.54307 0.65243 0.28548 0.00761  0.10840  0.08434  178 LYS A CE  
1397 N  NZ  . LYS A 178 ? 0.57481 0.72855 0.31079 0.01475  0.10315  0.05355  178 LYS A NZ  
1398 N  N   . ARG A 179 ? 0.27699 0.38075 0.33472 0.13791  0.06844  0.04077  179 ARG A N   
1399 C  CA  . ARG A 179 ? 0.32776 0.40935 0.36741 0.04457  0.11262  0.03455  179 ARG A CA  
1400 C  C   . ARG A 179 ? 0.39574 0.39308 0.39705 0.04085  0.10525  0.04506  179 ARG A C   
1401 O  O   . ARG A 179 ? 0.50201 0.37053 0.40876 0.03920  0.08375  0.01466  179 ARG A O   
1402 C  CB  . ARG A 179 ? 0.36708 0.47193 0.38549 0.11821  0.12943  0.04779  179 ARG A CB  
1403 C  CG  . ARG A 179 ? 0.38547 0.47673 0.40410 0.11003  0.12304  0.03141  179 ARG A CG  
1404 C  CD  . ARG A 179 ? 0.39104 0.53022 0.41904 0.07124  0.11808  0.03961  179 ARG A CD  
1405 N  NE  . ARG A 179 ? 0.42012 0.59893 0.43347 0.07026  0.14907  0.01003  179 ARG A NE  
1406 C  CZ  . ARG A 179 ? 0.37681 0.67539 0.44288 0.07076  0.16303  0.02248  179 ARG A CZ  
1407 N  NH1 . ARG A 179 ? 0.32951 0.71423 0.44315 0.04873  0.15006  0.04147  179 ARG A NH1 
1408 N  NH2 . ARG A 179 ? 0.35041 0.63877 0.45786 0.12159  0.16764  -0.01822 179 ARG A NH2 
1409 N  N   . LEU A 180 ? 0.30767 0.36073 0.39960 0.06485  0.09838  0.05040  180 LEU A N   
1410 C  CA  . LEU A 180 ? 0.36717 0.36168 0.41663 0.07399  0.07477  0.05131  180 LEU A CA  
1411 C  C   . LEU A 180 ? 0.36417 0.34332 0.44362 0.06918  0.07917  0.03592  180 LEU A C   
1412 O  O   . LEU A 180 ? 0.43953 0.30806 0.45028 0.11351  0.10857  0.03350  180 LEU A O   
1413 C  CB  . LEU A 180 ? 0.37974 0.28090 0.40287 0.10184  0.10064  0.02684  180 LEU A CB  
1414 C  CG  . LEU A 180 ? 0.46154 0.31714 0.40279 -0.00628 0.06997  0.05630  180 LEU A CG  
1415 C  CD1 . LEU A 180 ? 0.44204 0.37397 0.41335 -0.07474 0.05625  0.06132  180 LEU A CD1 
1416 C  CD2 . LEU A 180 ? 0.51795 0.33199 0.41277 -0.01259 0.05181  0.05042  180 LEU A CD2 
1417 N  N   . VAL A 181 ? 0.28951 0.31930 0.45060 0.06336  0.03251  0.05426  181 VAL A N   
1418 C  CA  . VAL A 181 ? 0.34608 0.28277 0.46034 0.12312  0.05282  0.06112  181 VAL A CA  
1419 C  C   . VAL A 181 ? 0.46262 0.32520 0.45069 0.07652  0.02139  0.06550  181 VAL A C   
1420 O  O   . VAL A 181 ? 0.42742 0.34296 0.44897 0.04741  0.06831  0.02772  181 VAL A O   
1421 C  CB  . VAL A 181 ? 0.36541 0.35539 0.47615 0.06402  0.06851  0.09184  181 VAL A CB  
1422 C  CG1 . VAL A 181 ? 0.37711 0.39451 0.49134 0.06713  0.06136  0.06770  181 VAL A CG1 
1423 C  CG2 . VAL A 181 ? 0.35471 0.34371 0.47718 0.09592  0.01512  0.07905  181 VAL A CG2 
1424 N  N   . GLN A 182 ? 0.47672 0.31132 0.44890 0.03479  0.00317  0.06265  182 GLN A N   
1425 C  CA  . GLN A 182 ? 0.49933 0.34116 0.44547 -0.03575 -0.05071 0.09818  182 GLN A CA  
1426 C  C   . GLN A 182 ? 0.54522 0.44166 0.47607 -0.08139 -0.03865 0.11442  182 GLN A C   
1427 O  O   . GLN A 182 ? 0.54305 0.47543 0.49014 -0.06097 0.02534  0.11034  182 GLN A O   
1428 C  CB  . GLN A 182 ? 0.55999 0.35045 0.44115 -0.07215 -0.06094 0.03251  182 GLN A CB  
1429 C  CG  . GLN A 182 ? 0.58780 0.42821 0.42658 -0.05728 -0.07932 0.00743  182 GLN A CG  
1430 C  CD  . GLN A 182 ? 0.66053 0.50235 0.41559 -0.07351 -0.08039 0.00296  182 GLN A CD  
1431 O  OE1 . GLN A 182 ? 0.68189 0.52815 0.39723 -0.06071 -0.02689 0.02760  182 GLN A OE1 
1432 N  NE2 . GLN A 182 ? 0.64114 0.50930 0.43048 -0.08994 -0.08641 0.04613  182 GLN A NE2 
1433 N  N   . SER A 183 ? 0.56084 0.44468 0.50545 -0.11406 -0.08184 0.11945  183 SER A N   
1434 C  CA  . SER A 183 ? 0.60002 0.48910 0.54124 -0.20241 -0.09225 0.17410  183 SER A CA  
1435 C  C   . SER A 183 ? 0.58117 0.53299 0.56798 -0.15689 -0.08854 0.18692  183 SER A C   
1436 O  O   . SER A 183 ? 0.56361 0.41915 0.56287 -0.10569 -0.10660 0.17361  183 SER A O   
1437 C  CB  . SER A 183 ? 0.70427 0.59108 0.55198 -0.19416 -0.13154 0.18782  183 SER A CB  
1438 O  OG  . SER A 183 ? 0.81807 0.62276 0.54829 -0.19212 -0.17574 0.20490  183 SER A OG  
1439 N  N   . THR A 184 ? 0.55788 0.60737 0.59445 -0.19701 -0.06621 0.19326  184 THR A N   
1440 C  CA  . THR A 184 ? 0.58218 0.66873 0.61632 -0.20728 -0.04387 0.20262  184 THR A CA  
1441 C  C   . THR A 184 ? 0.53055 0.59939 0.64688 -0.15044 -0.01525 0.20078  184 THR A C   
1442 O  O   . THR A 184 ? 0.55164 0.53950 0.65855 -0.15018 -0.03537 0.20462  184 THR A O   
1443 C  CB  . THR A 184 ? 0.61563 0.84810 0.61627 -0.23702 -0.08312 0.19583  184 THR A CB  
1444 O  OG1 . THR A 184 ? 0.62582 0.92046 0.60787 -0.24850 -0.06880 0.19759  184 THR A OG1 
1445 C  CG2 . THR A 184 ? 0.63571 0.87622 0.62977 -0.24557 -0.08642 0.20800  184 THR A CG2 
1446 N  N   . ASP A 185 ? 0.49261 0.53247 0.66518 -0.09578 0.05672  0.22201  185 ASP A N   
1447 C  CA  . ASP A 185 ? 0.50476 0.56934 0.67489 -0.02798 0.06641  0.21472  185 ASP A CA  
1448 C  C   . ASP A 185 ? 0.44597 0.46521 0.68880 -0.02028 0.05813  0.20901  185 ASP A C   
1449 O  O   . ASP A 185 ? 0.41336 0.44146 0.69572 0.04347  0.06067  0.23632  185 ASP A O   
1450 C  CB  . ASP A 185 ? 0.56028 0.63746 0.67589 -0.03419 0.11889  0.20425  185 ASP A CB  
1451 C  CG  . ASP A 185 ? 0.63478 0.75524 0.68698 -0.02458 0.17447  0.15648  185 ASP A CG  
1452 O  OD1 . ASP A 185 ? 0.66596 0.78990 0.69145 -0.02301 0.21612  0.13996  185 ASP A OD1 
1453 O  OD2 . ASP A 185 ? 0.68855 0.73964 0.68478 -0.02970 0.17618  0.18275  185 ASP A OD2 
1454 N  N   . ALA A 186 ? 0.38354 0.37763 0.69305 -0.01374 0.04266  0.17293  186 ALA A N   
1455 C  CA  . ALA A 186 ? 0.40591 0.37512 0.69107 0.00192  0.02005  0.16134  186 ALA A CA  
1456 C  C   . ALA A 186 ? 0.41580 0.43726 0.69092 -0.00101 0.03416  0.13536  186 ALA A C   
1457 O  O   . ALA A 186 ? 0.39336 0.46180 0.68729 0.03608  0.00973  0.15825  186 ALA A O   
1458 C  CB  . ALA A 186 ? 0.39232 0.37214 0.69284 -0.01918 0.02267  0.13512  186 ALA A CB  
1459 N  N   . GLN A 187 ? 0.34714 0.42358 0.68664 -0.02416 0.07909  0.14375  187 GLN A N   
1460 C  CA  . GLN A 187 ? 0.44578 0.53849 0.70090 0.01183  0.10407  0.15438  187 GLN A CA  
1461 C  C   . GLN A 187 ? 0.38917 0.47010 0.65831 0.06436  0.11574  0.17113  187 GLN A C   
1462 O  O   . GLN A 187 ? 0.40402 0.43063 0.65812 0.04890  0.14097  0.17130  187 GLN A O   
1463 C  CB  . GLN A 187 ? 0.56052 0.67913 0.75263 0.03202  0.06963  0.09927  187 GLN A CB  
1464 C  CG  . GLN A 187 ? 0.70144 0.82785 0.79238 0.03588  0.04652  0.04670  187 GLN A CG  
1465 C  CD  . GLN A 187 ? 0.76812 0.97724 0.82571 0.03827  0.04286  -0.00977 187 GLN A CD  
1466 O  OE1 . GLN A 187 ? 0.77910 1.04643 0.83694 0.02195  0.02902  -0.03226 187 GLN A OE1 
1467 N  NE2 . GLN A 187 ? 0.78496 0.98385 0.83588 0.04196  0.05718  -0.03203 187 GLN A NE2 
1468 N  N   . SER A 188 ? 0.40738 0.50673 0.61044 0.04461  0.11827  0.22287  188 SER A N   
1469 C  CA  . SER A 188 ? 0.42702 0.57637 0.59976 0.04460  0.07741  0.21841  188 SER A CA  
1470 C  C   . SER A 188 ? 0.34660 0.54312 0.57609 0.04888  0.09629  0.17095  188 SER A C   
1471 O  O   . SER A 188 ? 0.35346 0.46030 0.57600 0.02093  0.11321  0.13707  188 SER A O   
1472 C  CB  . SER A 188 ? 0.56059 0.66011 0.63254 0.15456  0.01770  0.17504  188 SER A CB  
1473 O  OG  . SER A 188 ? 0.68197 0.75869 0.65061 0.16108  -0.05257 0.16717  188 SER A OG  
1474 N  N   . ALA A 189 ? 0.28709 0.49157 0.55516 -0.00136 0.06727  0.15488  189 ALA A N   
1475 C  CA  . ALA A 189 ? 0.29434 0.45756 0.54584 0.10922  0.02908  0.13864  189 ALA A CA  
1476 C  C   . ALA A 189 ? 0.28909 0.42927 0.51179 0.03914  0.02791  0.10355  189 ALA A C   
1477 O  O   . ALA A 189 ? 0.25776 0.37947 0.51009 0.01235  0.05250  0.06131  189 ALA A O   
1478 C  CB  . ALA A 189 ? 0.27819 0.48580 0.57743 0.14468  -0.01544 0.14773  189 ALA A CB  
1479 N  N   . LEU A 190 ? 0.24363 0.42054 0.49617 0.04313  0.02106  0.06161  190 LEU A N   
1480 C  CA  . LEU A 190 ? 0.24139 0.38400 0.46992 0.04822  0.02470  0.08099  190 LEU A CA  
1481 C  C   . LEU A 190 ? 0.26682 0.32715 0.45250 0.01466  0.06979  0.09558  190 LEU A C   
1482 O  O   . LEU A 190 ? 0.27476 0.42059 0.44474 -0.03733 0.06638  0.09563  190 LEU A O   
1483 C  CB  . LEU A 190 ? 0.25496 0.49204 0.49843 -0.00197 0.04216  0.01790  190 LEU A CB  
1484 C  CG  . LEU A 190 ? 0.31476 0.62402 0.52664 -0.02424 0.04385  -0.03648 190 LEU A CG  
1485 C  CD1 . LEU A 190 ? 0.34085 0.66496 0.53572 -0.01464 0.04494  -0.07011 190 LEU A CD1 
1486 C  CD2 . LEU A 190 ? 0.39304 0.67996 0.53640 0.04886  0.02822  -0.05597 190 LEU A CD2 
1487 N  N   . THR A 191 ? 0.33133 0.37118 0.46301 -0.00687 0.08411  0.06402  191 THR A N   
1488 C  CA  . THR A 191 ? 0.37499 0.36066 0.44678 0.00010  0.10434  0.06570  191 THR A CA  
1489 C  C   . THR A 191 ? 0.32385 0.36754 0.41125 0.01621  0.04833  0.07834  191 THR A C   
1490 O  O   . THR A 191 ? 0.32115 0.35382 0.41692 0.03083  0.02972  0.09706  191 THR A O   
1491 C  CB  . THR A 191 ? 0.40528 0.36409 0.47590 -0.02480 0.12306  0.02928  191 THR A CB  
1492 O  OG1 . THR A 191 ? 0.39464 0.46885 0.49005 -0.02249 0.11336  0.06350  191 THR A OG1 
1493 C  CG2 . THR A 191 ? 0.42844 0.42093 0.49979 -0.00798 0.14104  -0.02778 191 THR A CG2 
1494 N  N   . ALA A 192 ? 0.29271 0.39337 0.38709 -0.00342 0.04749  0.07187  192 ALA A N   
1495 C  CA  . ALA A 192 ? 0.30669 0.39357 0.35441 0.04530  0.04961  0.07534  192 ALA A CA  
1496 C  C   . ALA A 192 ? 0.31313 0.39161 0.35726 0.04602  0.04196  0.04250  192 ALA A C   
1497 O  O   . ALA A 192 ? 0.27719 0.32942 0.37969 0.03951  0.04759  0.03478  192 ALA A O   
1498 C  CB  . ALA A 192 ? 0.36836 0.36980 0.35434 0.12266  0.01409  0.05847  192 ALA A CB  
1499 N  N   . ARG A 193 ? 0.25859 0.37945 0.34103 0.00748  0.06479  0.04049  193 ARG A N   
1500 C  CA  . ARG A 193 ? 0.32394 0.37008 0.31839 0.02346  0.07040  0.04955  193 ARG A CA  
1501 C  C   . ARG A 193 ? 0.24046 0.36164 0.35839 0.05864  0.02748  0.04770  193 ARG A C   
1502 O  O   . ARG A 193 ? 0.28569 0.36263 0.35225 0.03591  -0.00261 0.03451  193 ARG A O   
1503 C  CB  . ARG A 193 ? 0.35980 0.40628 0.30102 0.04835  0.06664  0.00069  193 ARG A CB  
1504 C  CG  . ARG A 193 ? 0.40795 0.47861 0.31393 0.00800  0.10548  -0.02334 193 ARG A CG  
1505 C  CD  . ARG A 193 ? 0.59217 0.57510 0.34433 0.01181  0.02911  0.00867  193 ARG A CD  
1506 N  NE  . ARG A 193 ? 0.73814 0.62592 0.38473 -0.03985 -0.00848 0.02784  193 ARG A NE  
1507 C  CZ  . ARG A 193 ? 0.82929 0.61050 0.41588 -0.04343 -0.05504 0.02056  193 ARG A CZ  
1508 N  NH1 . ARG A 193 ? 0.89064 0.51142 0.42987 -0.05385 -0.08950 -0.02584 193 ARG A NH1 
1509 N  NH2 . ARG A 193 ? 0.83366 0.68362 0.43708 -0.09100 -0.07083 0.02314  193 ARG A NH2 
1510 N  N   . ASN A 194 ? 0.26752 0.30769 0.39809 0.05654  0.01577  0.03155  194 ASN A N   
1511 C  CA  . ASN A 194 ? 0.24464 0.37921 0.42918 0.00942  -0.00927 0.06649  194 ASN A CA  
1512 C  C   . ASN A 194 ? 0.25795 0.35927 0.40064 0.05833  0.01536  0.03181  194 ASN A C   
1513 O  O   . ASN A 194 ? 0.29739 0.41167 0.39724 0.08415  0.04199  0.06009  194 ASN A O   
1514 C  CB  . ASN A 194 ? 0.29140 0.48209 0.47108 -0.04671 -0.00868 0.05516  194 ASN A CB  
1515 C  CG  . ASN A 194 ? 0.48336 0.64097 0.51204 -0.09272 -0.02865 0.07163  194 ASN A CG  
1516 O  OD1 . ASN A 194 ? 0.62858 0.68487 0.52747 -0.20295 -0.06299 0.05265  194 ASN A OD1 
1517 N  ND2 . ASN A 194 ? 0.45561 0.66215 0.52787 -0.06853 0.00991  0.07297  194 ASN A ND2 
1518 N  N   . ASP A 195 ? 0.26472 0.37214 0.37957 0.01181  0.04641  0.01333  195 ASP A N   
1519 C  CA  . ASP A 195 ? 0.26479 0.36679 0.38947 -0.00035 0.04521  -0.01211 195 ASP A CA  
1520 C  C   . ASP A 195 ? 0.24160 0.24179 0.37631 0.03019  0.01536  0.01262  195 ASP A C   
1521 O  O   . ASP A 195 ? 0.30383 0.27183 0.38546 0.04327  0.07685  0.04632  195 ASP A O   
1522 C  CB  . ASP A 195 ? 0.29425 0.38670 0.41092 0.01178  0.08937  0.00135  195 ASP A CB  
1523 C  CG  . ASP A 195 ? 0.34911 0.41891 0.43504 0.05529  0.08485  0.02830  195 ASP A CG  
1524 O  OD1 . ASP A 195 ? 0.33385 0.45619 0.45470 0.06375  0.09199  0.05034  195 ASP A OD1 
1525 O  OD2 . ASP A 195 ? 0.41611 0.47930 0.42880 0.03448  0.10238  0.01223  195 ASP A OD2 
1526 N  N   . LEU A 196 ? 0.23488 0.31974 0.36929 0.04635  0.02787  -0.05081 196 LEU A N   
1527 C  CA  . LEU A 196 ? 0.17990 0.35916 0.36238 0.01838  -0.00388 -0.02844 196 LEU A CA  
1528 C  C   . LEU A 196 ? 0.16121 0.33713 0.36262 -0.01012 0.03297  0.01026  196 LEU A C   
1529 O  O   . LEU A 196 ? 0.24342 0.35385 0.38546 -0.04092 0.08061  0.01977  196 LEU A O   
1530 C  CB  . LEU A 196 ? 0.17827 0.35915 0.34986 0.04907  -0.04384 -0.04326 196 LEU A CB  
1531 C  CG  . LEU A 196 ? 0.28157 0.40031 0.35145 0.05675  -0.03228 -0.07981 196 LEU A CG  
1532 C  CD1 . LEU A 196 ? 0.26310 0.43192 0.37384 0.09372  -0.00713 -0.05756 196 LEU A CD1 
1533 C  CD2 . LEU A 196 ? 0.31972 0.42533 0.33398 0.07086  0.02569  -0.09837 196 LEU A CD2 
1534 N  N   . ALA A 197 ? 0.18780 0.29865 0.35656 0.01559  0.02544  0.02472  197 ALA A N   
1535 C  CA  . ALA A 197 ? 0.28037 0.26542 0.35729 0.01945  0.01476  0.01105  197 ALA A CA  
1536 C  C   . ALA A 197 ? 0.25730 0.31622 0.36935 0.06369  0.05433  0.03116  197 ALA A C   
1537 O  O   . ALA A 197 ? 0.31096 0.30187 0.35866 0.02676  -0.00423 0.01192  197 ALA A O   
1538 C  CB  . ALA A 197 ? 0.26589 0.27860 0.35642 -0.03797 0.01052  -0.00809 197 ALA A CB  
1539 N  N   . GLY A 198 ? 0.29844 0.28942 0.39342 0.05039  0.07923  0.00071  198 GLY A N   
1540 C  CA  . GLY A 198 ? 0.30767 0.27771 0.42218 0.03122  0.05232  -0.00965 198 GLY A CA  
1541 C  C   . GLY A 198 ? 0.26946 0.28815 0.43684 0.06705  0.05610  0.02914  198 GLY A C   
1542 O  O   . GLY A 198 ? 0.27909 0.31419 0.46810 0.09132  0.04510  0.03447  198 GLY A O   
1543 N  N   . TYR A 199 ? 0.26800 0.25765 0.43902 0.02969  0.06137  0.05076  199 TYR A N   
1544 C  CA  . TYR A 199 ? 0.20041 0.24878 0.41902 -0.03177 0.06251  0.03419  199 TYR A CA  
1545 C  C   . TYR A 199 ? 0.22658 0.28401 0.42668 0.04627  0.05601  0.02022  199 TYR A C   
1546 O  O   . TYR A 199 ? 0.27511 0.28762 0.43621 0.02936  0.04958  0.03821  199 TYR A O   
1547 C  CB  . TYR A 199 ? 0.26810 0.31612 0.42104 0.02380  0.06396  -0.00474 199 TYR A CB  
1548 C  CG  . TYR A 199 ? 0.28426 0.29975 0.40848 0.06488  0.08058  -0.04534 199 TYR A CG  
1549 C  CD1 . TYR A 199 ? 0.33469 0.29436 0.40624 0.02622  0.04255  -0.09171 199 TYR A CD1 
1550 C  CD2 . TYR A 199 ? 0.30808 0.31939 0.40122 0.04266  0.07478  -0.05053 199 TYR A CD2 
1551 C  CE1 . TYR A 199 ? 0.38793 0.31462 0.40177 0.01768  0.05877  -0.07299 199 TYR A CE1 
1552 C  CE2 . TYR A 199 ? 0.36314 0.33017 0.40026 0.00230  0.05188  -0.08409 199 TYR A CE2 
1553 C  CZ  . TYR A 199 ? 0.40770 0.31766 0.39597 0.04992  0.03782  -0.06281 199 TYR A CZ  
1554 O  OH  . TYR A 199 ? 0.47400 0.33756 0.38847 -0.02415 -0.00197 -0.04528 199 TYR A OH  
1555 N  N   . LEU A 200 ? 0.19673 0.28148 0.39833 0.05993  0.07206  -0.00517 200 LEU A N   
1556 C  CA  . LEU A 200 ? 0.15229 0.27310 0.38505 0.05031  0.05287  0.03631  200 LEU A CA  
1557 C  C   . LEU A 200 ? 0.17498 0.31750 0.41016 0.05544  0.01934  0.03455  200 LEU A C   
1558 O  O   . LEU A 200 ? 0.25677 0.31575 0.40793 0.03424  0.04430  0.02215  200 LEU A O   
1559 C  CB  . LEU A 200 ? 0.15271 0.28998 0.38416 0.06380  0.01922  0.03259  200 LEU A CB  
1560 C  CG  . LEU A 200 ? 0.26601 0.25164 0.39903 -0.00282 0.01522  -0.01538 200 LEU A CG  
1561 C  CD1 . LEU A 200 ? 0.31385 0.19710 0.38486 0.02998  0.02528  -0.01299 200 LEU A CD1 
1562 C  CD2 . LEU A 200 ? 0.28694 0.19839 0.41483 0.01745  0.04633  -0.03669 200 LEU A CD2 
1563 N  N   . ASP A 201 ? 0.16891 0.34891 0.44239 0.07391  0.00563  0.01343  201 ASP A N   
1564 C  CA  . ASP A 201 ? 0.17269 0.35081 0.47186 0.03546  -0.04209 0.03154  201 ASP A CA  
1565 C  C   . ASP A 201 ? 0.23834 0.33992 0.47986 0.05574  0.00270  0.01361  201 ASP A C   
1566 O  O   . ASP A 201 ? 0.27323 0.31167 0.47552 0.02275  -0.03063 0.02658  201 ASP A O   
1567 C  CB  . ASP A 201 ? 0.24490 0.39595 0.49685 0.02024  -0.05672 0.04918  201 ASP A CB  
1568 C  CG  . ASP A 201 ? 0.39039 0.52520 0.51078 -0.03015 -0.06319 0.06678  201 ASP A CG  
1569 O  OD1 . ASP A 201 ? 0.44835 0.49834 0.51108 -0.02331 -0.02855 0.03477  201 ASP A OD1 
1570 O  OD2 . ASP A 201 ? 0.43664 0.64005 0.52510 -0.02412 -0.06810 0.08084  201 ASP A OD2 
1571 N  N   . GLY A 202 ? 0.20931 0.26774 0.48708 0.08053  0.04184  -0.04685 202 GLY A N   
1572 C  CA  . GLY A 202 ? 0.28260 0.27479 0.49628 0.10922  0.04170  -0.04478 202 GLY A CA  
1573 C  C   . GLY A 202 ? 0.24860 0.28050 0.47979 0.09665  0.03299  -0.00800 202 GLY A C   
1574 O  O   . GLY A 202 ? 0.30111 0.28917 0.45542 0.03622  0.04937  0.01549  202 GLY A O   
1575 N  N   . LEU A 203 ? 0.22006 0.28866 0.45922 0.07396  0.02887  -0.02026 203 LEU A N   
1576 C  CA  . LEU A 203 ? 0.23390 0.31307 0.44823 0.01995  0.03128  -0.03538 203 LEU A CA  
1577 C  C   . LEU A 203 ? 0.29781 0.26676 0.41802 -0.04365 0.02291  0.00593  203 LEU A C   
1578 O  O   . LEU A 203 ? 0.27038 0.25847 0.43210 -0.00794 0.02404  0.00518  203 LEU A O   
1579 C  CB  . LEU A 203 ? 0.26964 0.35486 0.47033 -0.00406 0.02737  -0.07358 203 LEU A CB  
1580 C  CG  . LEU A 203 ? 0.29049 0.36743 0.49624 0.02793  -0.01048 -0.08793 203 LEU A CG  
1581 C  CD1 . LEU A 203 ? 0.43269 0.43160 0.50241 0.00566  -0.00041 -0.09428 203 LEU A CD1 
1582 C  CD2 . LEU A 203 ? 0.32001 0.39055 0.52091 0.10930  -0.01921 -0.07641 203 LEU A CD2 
1583 N  N   . ILE A 204 ? 0.24167 0.26289 0.37186 -0.02469 0.01661  0.00240  204 ILE A N   
1584 C  CA  . ILE A 204 ? 0.25052 0.19028 0.36995 0.04754  -0.02570 -0.00936 204 ILE A CA  
1585 C  C   . ILE A 204 ? 0.22509 0.24370 0.39327 0.02364  -0.02325 0.01691  204 ILE A C   
1586 O  O   . ILE A 204 ? 0.30540 0.25768 0.39323 -0.00621 -0.05782 0.03404  204 ILE A O   
1587 C  CB  . ILE A 204 ? 0.27996 0.19124 0.34699 0.01266  -0.00008 -0.01244 204 ILE A CB  
1588 C  CG1 . ILE A 204 ? 0.29147 0.19598 0.37899 0.03174  0.03227  -0.00181 204 ILE A CG1 
1589 C  CG2 . ILE A 204 ? 0.28644 0.30249 0.33506 -0.06140 -0.02539 -0.02168 204 ILE A CG2 
1590 C  CD1 . ILE A 204 ? 0.33937 0.23895 0.38257 0.04779  0.03897  -0.03742 204 ILE A CD1 
1591 N  N   . THR A 205 ? 0.24525 0.24800 0.40972 0.01225  -0.01585 -0.01899 205 THR A N   
1592 C  CA  . THR A 205 ? 0.21758 0.25943 0.40846 -0.03284 -0.02382 0.01134  205 THR A CA  
1593 C  C   . THR A 205 ? 0.30615 0.29066 0.39108 -0.02628 -0.04801 -0.00433 205 THR A C   
1594 O  O   . THR A 205 ? 0.33426 0.27067 0.39597 -0.00410 -0.03216 -0.01246 205 THR A O   
1595 C  CB  . THR A 205 ? 0.20595 0.26812 0.42929 -0.03342 -0.04877 -0.00526 205 THR A CB  
1596 O  OG1 . THR A 205 ? 0.36842 0.33845 0.42457 -0.04193 -0.02385 0.05020  205 THR A OG1 
1597 C  CG2 . THR A 205 ? 0.23953 0.33860 0.45509 0.05145  -0.01572 0.04538  205 THR A CG2 
1598 N  N   . GLN A 206 ? 0.30821 0.27817 0.35780 -0.00210 -0.04891 -0.01172 206 GLN A N   
1599 C  CA  . GLN A 206 ? 0.31551 0.27531 0.34880 -0.04406 -0.02982 -0.03681 206 GLN A CA  
1600 C  C   . GLN A 206 ? 0.34199 0.27474 0.35229 0.00120  -0.02236 -0.04883 206 GLN A C   
1601 O  O   . GLN A 206 ? 0.32422 0.31890 0.35641 -0.02836 -0.01204 -0.03682 206 GLN A O   
1602 C  CB  . GLN A 206 ? 0.35495 0.35959 0.35729 0.04734  -0.04237 -0.07385 206 GLN A CB  
1603 C  CG  . GLN A 206 ? 0.49669 0.46857 0.38400 -0.01667 -0.00956 -0.05828 206 GLN A CG  
1604 C  CD  . GLN A 206 ? 0.63833 0.56791 0.43016 -0.04029 -0.05051 -0.05475 206 GLN A CD  
1605 O  OE1 . GLN A 206 ? 0.74705 0.61017 0.46410 -0.03139 -0.08100 -0.05807 206 GLN A OE1 
1606 N  NE2 . GLN A 206 ? 0.63096 0.62217 0.41909 -0.03461 -0.00964 -0.08423 206 GLN A NE2 
1607 N  N   . PHE A 207 ? 0.28950 0.24226 0.33926 0.02880  -0.02054 -0.02680 207 PHE A N   
1608 C  CA  . PHE A 207 ? 0.29208 0.29473 0.29564 -0.04093 -0.07896 -0.00966 207 PHE A CA  
1609 C  C   . PHE A 207 ? 0.26818 0.33011 0.29232 0.00866  -0.06581 0.01250  207 PHE A C   
1610 O  O   . PHE A 207 ? 0.31265 0.29988 0.27999 0.02424  -0.05175 0.03017  207 PHE A O   
1611 C  CB  . PHE A 207 ? 0.29642 0.23698 0.31497 0.00530  -0.11670 0.04976  207 PHE A CB  
1612 C  CG  . PHE A 207 ? 0.43211 0.23249 0.36567 -0.02376 -0.17894 0.01917  207 PHE A CG  
1613 C  CD1 . PHE A 207 ? 0.56615 0.26548 0.40543 -0.03529 -0.23568 0.03059  207 PHE A CD1 
1614 C  CD2 . PHE A 207 ? 0.46735 0.30592 0.36933 0.01844  -0.17714 0.06285  207 PHE A CD2 
1615 C  CE1 . PHE A 207 ? 0.63126 0.24133 0.39950 0.01153  -0.21746 0.06501  207 PHE A CE1 
1616 C  CE2 . PHE A 207 ? 0.47748 0.32312 0.35592 0.03053  -0.16491 0.01442  207 PHE A CE2 
1617 C  CZ  . PHE A 207 ? 0.57628 0.20820 0.36716 -0.06833 -0.19713 0.07364  207 PHE A CZ  
1618 N  N   . GLN A 208 ? 0.28923 0.23214 0.29341 0.01189  -0.04955 -0.00390 208 GLN A N   
1619 C  CA  . GLN A 208 ? 0.33420 0.21438 0.30936 0.01337  -0.07157 -0.00935 208 GLN A CA  
1620 C  C   . GLN A 208 ? 0.34900 0.30048 0.30891 0.06104  -0.03842 -0.02374 208 GLN A C   
1621 O  O   . GLN A 208 ? 0.38833 0.30270 0.31509 0.02134  -0.05343 -0.04158 208 GLN A O   
1622 C  CB  . GLN A 208 ? 0.41308 0.17085 0.30630 0.02654  -0.04966 -0.01251 208 GLN A CB  
1623 C  CG  . GLN A 208 ? 0.34820 0.18997 0.32157 0.05729  -0.04216 -0.01042 208 GLN A CG  
1624 C  CD  . GLN A 208 ? 0.30982 0.21805 0.32995 0.04706  -0.01870 -0.00132 208 GLN A CD  
1625 O  OE1 . GLN A 208 ? 0.24395 0.37352 0.35035 -0.02777 -0.00236 -0.01923 208 GLN A OE1 
1626 N  NE2 . GLN A 208 ? 0.33546 0.27232 0.30257 0.07741  -0.04299 -0.01069 208 GLN A NE2 
1627 N  N   . THR A 209 ? 0.28443 0.27199 0.29634 0.03674  -0.07044 -0.07522 209 THR A N   
1628 C  CA  . THR A 209 ? 0.30625 0.25696 0.30307 0.00961  -0.02525 -0.01369 209 THR A CA  
1629 C  C   . THR A 209 ? 0.36584 0.31183 0.31362 0.08359  -0.08849 -0.02245 209 THR A C   
1630 O  O   . THR A 209 ? 0.39965 0.35955 0.33554 0.05957  -0.05227 -0.02146 209 THR A O   
1631 C  CB  . THR A 209 ? 0.37171 0.29203 0.30812 0.07650  0.01759  -0.02961 209 THR A CB  
1632 O  OG1 . THR A 209 ? 0.34356 0.39821 0.33735 0.02587  -0.00257 -0.00285 209 THR A OG1 
1633 C  CG2 . THR A 209 ? 0.37055 0.30187 0.29527 0.09685  -0.06130 -0.03528 209 THR A CG2 
1634 N  N   . GLU A 210 ? 0.32627 0.25133 0.33242 0.04150  -0.12064 -0.04819 210 GLU A N   
1635 C  CA  A GLU A 210 ? 0.34936 0.28851 0.35555 0.01104  -0.12184 -0.05067 210 GLU A CA  
1636 C  CA  B GLU A 210 ? 0.37194 0.30064 0.35527 0.01381  -0.10863 -0.05148 210 GLU A CA  
1637 C  C   . GLU A 210 ? 0.37529 0.24744 0.35280 -0.03269 -0.09417 -0.01412 210 GLU A C   
1638 O  O   . GLU A 210 ? 0.38471 0.24414 0.35952 -0.04326 -0.07954 0.02436  210 GLU A O   
1639 C  CB  A GLU A 210 ? 0.38946 0.39907 0.37148 -0.03872 -0.16026 -0.07191 210 GLU A CB  
1640 C  CB  B GLU A 210 ? 0.45766 0.43399 0.36987 -0.03273 -0.12277 -0.07255 210 GLU A CB  
1641 C  CG  A GLU A 210 ? 0.46792 0.50933 0.41013 -0.02885 -0.13523 -0.07351 210 GLU A CG  
1642 C  CG  B GLU A 210 ? 0.57404 0.57077 0.40297 -0.00949 -0.09308 -0.08014 210 GLU A CG  
1643 C  CD  A GLU A 210 ? 0.48077 0.55735 0.43994 0.02442  -0.12960 -0.06784 210 GLU A CD  
1644 C  CD  B GLU A 210 ? 0.64230 0.67826 0.43405 0.02536  -0.07048 -0.09290 210 GLU A CD  
1645 O  OE1 A GLU A 210 ? 0.51325 0.59513 0.45255 0.07459  -0.13147 -0.05627 210 GLU A OE1 
1646 O  OE1 B GLU A 210 ? 0.67036 0.70983 0.45850 0.01516  -0.04081 -0.09319 210 GLU A OE1 
1647 O  OE2 A GLU A 210 ? 0.44484 0.54904 0.45123 0.01601  -0.10512 -0.07593 210 GLU A OE2 
1648 O  OE2 B GLU A 210 ? 0.69704 0.73362 0.43288 0.03696  -0.06195 -0.08440 210 GLU A OE2 
1649 N  N   . PRO A 211 ? 0.39409 0.25418 0.35147 -0.01127 -0.08456 0.01906  211 PRO A N   
1650 C  CA  . PRO A 211 ? 0.29152 0.28824 0.34478 -0.00634 -0.07507 0.00841  211 PRO A CA  
1651 C  C   . PRO A 211 ? 0.34153 0.32072 0.36253 -0.01398 -0.12458 -0.05679 211 PRO A C   
1652 O  O   . PRO A 211 ? 0.37684 0.30162 0.37361 -0.02992 -0.10526 -0.06294 211 PRO A O   
1653 C  CB  . PRO A 211 ? 0.37179 0.36307 0.32980 0.02931  -0.06775 0.04823  211 PRO A CB  
1654 C  CG  . PRO A 211 ? 0.47700 0.37858 0.33300 0.07442  -0.05522 0.04854  211 PRO A CG  
1655 C  CD  . PRO A 211 ? 0.42887 0.30379 0.32676 0.04623  -0.03851 0.06055  211 PRO A CD  
1656 N  N   . GLY A 212 ? 0.39367 0.33284 0.36944 0.05170  -0.15862 -0.07413 212 GLY A N   
1657 C  CA  . GLY A 212 ? 0.43420 0.42422 0.37276 0.15842  -0.19185 -0.08939 212 GLY A CA  
1658 C  C   . GLY A 212 ? 0.44004 0.28654 0.38770 0.12816  -0.15608 -0.06173 212 GLY A C   
1659 O  O   . GLY A 212 ? 0.29111 0.26499 0.36936 0.02128  -0.11647 0.02601  212 GLY A O   
1660 N  N   . ALA A 213 ? 0.47086 0.31566 0.39829 0.13651  -0.20527 -0.06339 213 ALA A N   
1661 C  CA  . ALA A 213 ? 0.43849 0.26586 0.39116 0.10094  -0.20164 -0.05304 213 ALA A CA  
1662 C  C   . ALA A 213 ? 0.38585 0.20352 0.33661 0.02758  -0.12986 0.04968  213 ALA A C   
1663 O  O   . ALA A 213 ? 0.40826 0.38580 0.34371 0.06521  -0.06633 0.08463  213 ALA A O   
1664 C  CB  . ALA A 213 ? 0.49419 0.32301 0.41122 0.10418  -0.25556 -0.07843 213 ALA A CB  
1665 N  N   . GLY A 214 ? 0.30905 0.21954 0.30076 -0.01014 -0.07336 0.01942  214 GLY A N   
1666 C  CA  . GLY A 214 ? 0.34008 0.20962 0.29851 -0.03098 -0.07860 0.00588  214 GLY A CA  
1667 C  C   . GLY A 214 ? 0.31378 0.24618 0.26077 0.01610  -0.09356 0.01171  214 GLY A C   
1668 O  O   . GLY A 214 ? 0.38290 0.25569 0.26334 0.00995  -0.11277 0.03076  214 GLY A O   
1669 N  N   . LEU A 215 ? 0.23593 0.24706 0.25420 -0.00713 -0.04010 0.01963  215 LEU A N   
1670 C  CA  . LEU A 215 ? 0.24152 0.18374 0.23563 0.02706  -0.06108 -0.02830 215 LEU A CA  
1671 C  C   . LEU A 215 ? 0.22312 0.21414 0.24350 -0.01514 -0.01287 -0.02648 215 LEU A C   
1672 O  O   . LEU A 215 ? 0.31908 0.25907 0.24660 0.00951  -0.06026 -0.00371 215 LEU A O   
1673 C  CB  . LEU A 215 ? 0.31789 0.17912 0.24176 0.06079  -0.05211 -0.01131 215 LEU A CB  
1674 C  CG  . LEU A 215 ? 0.36350 0.22532 0.19758 0.04067  -0.04615 0.01732  215 LEU A CG  
1675 C  CD1 . LEU A 215 ? 0.32525 0.34038 0.20104 0.05466  -0.04799 0.03156  215 LEU A CD1 
1676 C  CD2 . LEU A 215 ? 0.38993 0.26087 0.20179 0.06173  -0.02203 0.04672  215 LEU A CD2 
1677 N  N   . VAL A 216 ? 0.27509 0.24227 0.24736 0.01251  -0.05867 -0.01252 216 VAL A N   
1678 C  CA  . VAL A 216 ? 0.25966 0.25485 0.25378 -0.00142 -0.04212 -0.00644 216 VAL A CA  
1679 C  C   . VAL A 216 ? 0.27461 0.18626 0.25914 0.05002  -0.04817 0.00990  216 VAL A C   
1680 O  O   . VAL A 216 ? 0.33891 0.27132 0.26359 -0.00168 -0.06391 0.01017  216 VAL A O   
1681 C  CB  . VAL A 216 ? 0.24891 0.26560 0.25811 0.05280  -0.06180 -0.00139 216 VAL A CB  
1682 C  CG1 . VAL A 216 ? 0.25997 0.27075 0.24598 -0.01306 -0.06476 0.02052  216 VAL A CG1 
1683 C  CG2 . VAL A 216 ? 0.29618 0.33703 0.27110 0.02321  -0.04183 -0.01131 216 VAL A CG2 
1684 N  N   . GLY A 217 ? 0.27898 0.16847 0.25553 0.01346  -0.02201 0.01895  217 GLY A N   
1685 C  CA  . GLY A 217 ? 0.28337 0.20323 0.23372 -0.02749 -0.07121 0.04959  217 GLY A CA  
1686 C  C   . GLY A 217 ? 0.24625 0.29062 0.24931 0.01317  -0.08505 0.01928  217 GLY A C   
1687 O  O   . GLY A 217 ? 0.29000 0.29677 0.23778 -0.00176 -0.07894 0.02499  217 GLY A O   
1688 N  N   . ALA A 218 ? 0.28091 0.25905 0.26534 0.05279  -0.06172 0.01305  218 ALA A N   
1689 C  CA  . ALA A 218 ? 0.20740 0.28466 0.25149 0.01884  -0.04164 0.00640  218 ALA A CA  
1690 C  C   . ALA A 218 ? 0.21319 0.33511 0.25247 -0.02662 -0.06365 0.00463  218 ALA A C   
1691 O  O   . ALA A 218 ? 0.26950 0.36546 0.25276 0.01611  -0.09676 -0.01364 218 ALA A O   
1692 C  CB  . ALA A 218 ? 0.26105 0.31626 0.25670 0.02474  -0.06634 0.04107  218 ALA A CB  
1693 N  N   . LEU A 219 ? 0.27333 0.23262 0.26700 0.01272  -0.06668 0.02683  219 LEU A N   
1694 C  CA  . LEU A 219 ? 0.27662 0.25454 0.26030 0.01404  -0.07070 0.01872  219 LEU A CA  
1695 C  C   . LEU A 219 ? 0.24150 0.23023 0.24862 -0.01045 -0.05518 0.01021  219 LEU A C   
1696 O  O   . LEU A 219 ? 0.28814 0.34489 0.23007 -0.01703 -0.04778 -0.00276 219 LEU A O   
1697 C  CB  . LEU A 219 ? 0.27343 0.24983 0.24148 0.03818  -0.08646 0.02200  219 LEU A CB  
1698 C  CG  . LEU A 219 ? 0.26175 0.25011 0.25154 0.05732  -0.06946 0.00120  219 LEU A CG  
1699 C  CD1 . LEU A 219 ? 0.33611 0.23584 0.24345 0.05131  -0.08718 0.02700  219 LEU A CD1 
1700 C  CD2 . LEU A 219 ? 0.29165 0.35758 0.26974 0.13088  -0.02172 -0.05185 219 LEU A CD2 
1701 N  N   . VAL A 220 ? 0.26752 0.21884 0.25383 0.02713  -0.02390 0.02296  220 VAL A N   
1702 C  CA  . VAL A 220 ? 0.24497 0.27400 0.23612 0.06578  -0.04077 0.01257  220 VAL A CA  
1703 C  C   . VAL A 220 ? 0.24444 0.25097 0.24243 -0.05137 -0.06102 0.01527  220 VAL A C   
1704 O  O   . VAL A 220 ? 0.29094 0.25800 0.24873 -0.00422 -0.06805 0.01950  220 VAL A O   
1705 C  CB  . VAL A 220 ? 0.20664 0.24454 0.20633 0.02854  -0.05998 0.02955  220 VAL A CB  
1706 C  CG1 . VAL A 220 ? 0.22883 0.28638 0.24001 0.02894  -0.04183 0.01968  220 VAL A CG1 
1707 C  CG2 . VAL A 220 ? 0.32160 0.24141 0.20251 0.02165  -0.04001 0.04603  220 VAL A CG2 
1708 N  N   . ALA A 221 ? 0.29404 0.20700 0.25922 -0.05592 -0.05384 0.04797  221 ALA A N   
1709 C  CA  . ALA A 221 ? 0.30749 0.24452 0.26007 -0.03970 -0.06526 0.02147  221 ALA A CA  
1710 C  C   . ALA A 221 ? 0.32633 0.25779 0.25916 -0.01708 -0.07250 -0.00561 221 ALA A C   
1711 O  O   . ALA A 221 ? 0.36560 0.33713 0.23698 0.03540  -0.03202 0.03509  221 ALA A O   
1712 C  CB  . ALA A 221 ? 0.36314 0.24235 0.28419 -0.03975 -0.05695 -0.00717 221 ALA A CB  
1713 N  N   . ASP A 222 ? 0.26949 0.25654 0.26870 -0.02743 -0.01685 -0.01792 222 ASP A N   
1714 C  CA  . ASP A 222 ? 0.24930 0.27943 0.27470 0.03196  -0.02416 0.00747  222 ASP A CA  
1715 C  C   . ASP A 222 ? 0.28399 0.27407 0.26114 0.03145  -0.01977 0.02742  222 ASP A C   
1716 O  O   . ASP A 222 ? 0.27031 0.30768 0.26864 0.03798  -0.05199 0.06358  222 ASP A O   
1717 C  CB  . ASP A 222 ? 0.24900 0.33672 0.29607 0.02770  -0.04150 0.03975  222 ASP A CB  
1718 C  CG  . ASP A 222 ? 0.35092 0.38739 0.32285 0.01980  -0.04651 0.07937  222 ASP A CG  
1719 O  OD1 . ASP A 222 ? 0.41549 0.37151 0.34489 0.00173  -0.08462 0.09792  222 ASP A OD1 
1720 O  OD2 . ASP A 222 ? 0.41382 0.55538 0.34665 0.00179  -0.04271 0.05448  222 ASP A OD2 
1721 N  N   . GLN A 223 ? 0.30192 0.27583 0.24622 0.01993  -0.01337 0.01075  223 GLN A N   
1722 C  CA  . GLN A 223 ? 0.23929 0.25622 0.24914 0.00997  -0.06365 0.06909  223 GLN A CA  
1723 C  C   . GLN A 223 ? 0.23246 0.28361 0.22659 0.02292  -0.06586 0.00428  223 GLN A C   
1724 O  O   . GLN A 223 ? 0.26494 0.28233 0.23436 0.01250  -0.05468 -0.00953 223 GLN A O   
1725 C  CB  . GLN A 223 ? 0.24932 0.27208 0.28242 0.03412  -0.06462 0.05867  223 GLN A CB  
1726 C  CG  . GLN A 223 ? 0.23294 0.28568 0.30364 0.02274  -0.04530 0.07475  223 GLN A CG  
1727 C  CD  . GLN A 223 ? 0.22948 0.31115 0.31793 0.05445  -0.04447 0.03792  223 GLN A CD  
1728 O  OE1 . GLN A 223 ? 0.23926 0.33541 0.33207 0.01991  -0.03613 0.06649  223 GLN A OE1 
1729 N  NE2 . GLN A 223 ? 0.29395 0.41007 0.32880 0.06326  -0.01554 0.05432  223 GLN A NE2 
1730 N  N   . LEU A 224 ? 0.23684 0.28069 0.23420 0.07013  -0.03797 0.00294  224 LEU A N   
1731 C  CA  . LEU A 224 ? 0.25638 0.24155 0.23571 0.09107  0.00320  0.02377  224 LEU A CA  
1732 C  C   . LEU A 224 ? 0.25723 0.25701 0.24118 0.04230  -0.01935 0.04904  224 LEU A C   
1733 O  O   . LEU A 224 ? 0.27555 0.34232 0.22426 0.00315  -0.03385 0.01377  224 LEU A O   
1734 C  CB  . LEU A 224 ? 0.18476 0.28880 0.24093 -0.01909 0.03671  0.03180  224 LEU A CB  
1735 C  CG  . LEU A 224 ? 0.23085 0.24394 0.24724 0.00395  0.02193  0.03675  224 LEU A CG  
1736 C  CD1 . LEU A 224 ? 0.29130 0.23317 0.25713 0.00534  -0.00903 -0.00845 224 LEU A CD1 
1737 C  CD2 . LEU A 224 ? 0.28894 0.25954 0.24005 0.03272  -0.02902 0.00114  224 LEU A CD2 
1738 N  N   . ALA A 225 ? 0.30251 0.21997 0.25942 0.01952  -0.01552 0.08522  225 ALA A N   
1739 C  CA  . ALA A 225 ? 0.29326 0.21205 0.22985 0.01137  -0.03069 0.04677  225 ALA A CA  
1740 C  C   . ALA A 225 ? 0.19977 0.26266 0.22130 0.04168  -0.05199 0.04651  225 ALA A C   
1741 O  O   . ALA A 225 ? 0.23616 0.26487 0.23442 -0.01539 -0.06004 0.04049  225 ALA A O   
1742 C  CB  . ALA A 225 ? 0.35804 0.22353 0.25090 0.00446  -0.04325 0.02015  225 ALA A CB  
1743 N  N   . ASN A 226 ? 0.19963 0.26232 0.22090 0.05406  0.01473  0.01641  226 ASN A N   
1744 C  CA  . ASN A 226 ? 0.23645 0.30143 0.23918 0.00673  -0.02114 0.00830  226 ASN A CA  
1745 C  C   . ASN A 226 ? 0.32337 0.33120 0.25127 -0.02488 -0.05294 0.01406  226 ASN A C   
1746 O  O   . ASN A 226 ? 0.34005 0.32236 0.25576 -0.05686 -0.07882 0.02811  226 ASN A O   
1747 C  CB  . ASN A 226 ? 0.26946 0.29660 0.24381 -0.03921 0.01072  0.00567  226 ASN A CB  
1748 C  CG  . ASN A 226 ? 0.29017 0.31227 0.24013 -0.08227 0.00383  0.04570  226 ASN A CG  
1749 O  OD1 . ASN A 226 ? 0.38733 0.32632 0.23553 -0.02115 0.01228  0.06640  226 ASN A OD1 
1750 N  ND2 . ASN A 226 ? 0.33410 0.30884 0.25210 -0.05595 -0.04174 0.02168  226 ASN A ND2 
1751 N  N   . GLY A 227 ? 0.26725 0.26182 0.23607 -0.02826 -0.05411 0.04322  227 GLY A N   
1752 C  CA  . GLY A 227 ? 0.25608 0.22854 0.26640 0.02879  -0.05678 0.02391  227 GLY A CA  
1753 C  C   . GLY A 227 ? 0.28582 0.23983 0.29062 0.01417  -0.06074 -0.01064 227 GLY A C   
1754 O  O   . GLY A 227 ? 0.31823 0.31166 0.32701 0.00622  -0.05562 -0.02662 227 GLY A O   
1755 N  N   . GLU A 228 ? 0.27367 0.27455 0.25251 -0.02982 -0.06740 0.00215  228 GLU A N   
1756 C  CA  . GLU A 228 ? 0.29656 0.25666 0.24898 -0.00263 -0.04580 0.04464  228 GLU A CA  
1757 C  C   . GLU A 228 ? 0.33393 0.27536 0.25589 0.08896  -0.06418 0.00795  228 GLU A C   
1758 O  O   . GLU A 228 ? 0.38063 0.25391 0.28231 0.09092  -0.08598 0.01800  228 GLU A O   
1759 C  CB  . GLU A 228 ? 0.25772 0.34855 0.25116 -0.04954 -0.03418 0.04677  228 GLU A CB  
1760 C  CG  . GLU A 228 ? 0.32835 0.40392 0.25005 -0.03136 -0.07069 0.07458  228 GLU A CG  
1761 C  CD  . GLU A 228 ? 0.38240 0.49870 0.26795 -0.06541 -0.04366 0.10033  228 GLU A CD  
1762 O  OE1 . GLU A 228 ? 0.36326 0.55143 0.27797 -0.05823 -0.06655 0.06755  228 GLU A OE1 
1763 O  OE2 . GLU A 228 ? 0.38893 0.56192 0.30894 -0.12145 -0.03465 0.05505  228 GLU A OE2 
1764 N  N   . ILE A 229 ? 0.26997 0.31152 0.24622 -0.03224 -0.03198 0.01233  229 ILE A N   
1765 C  CA  . ILE A 229 ? 0.23895 0.33584 0.25317 -0.09908 -0.03791 0.04295  229 ILE A CA  
1766 C  C   . ILE A 229 ? 0.23567 0.31416 0.26103 -0.08839 -0.04960 0.03281  229 ILE A C   
1767 O  O   . ILE A 229 ? 0.26760 0.28772 0.28861 -0.01691 -0.04547 0.00283  229 ILE A O   
1768 C  CB  . ILE A 229 ? 0.30099 0.25090 0.25646 -0.08121 -0.07282 0.05475  229 ILE A CB  
1769 C  CG1 . ILE A 229 ? 0.30789 0.29794 0.26640 -0.03484 -0.08746 0.03518  229 ILE A CG1 
1770 C  CG2 . ILE A 229 ? 0.30011 0.27808 0.25247 -0.05611 -0.08497 -0.01442 229 ILE A CG2 
1771 C  CD1 . ILE A 229 ? 0.35922 0.38717 0.27779 0.00406  -0.07984 0.02799  229 ILE A CD1 
1772 N  N   . ASP A 230 ? 0.23789 0.37893 0.26469 -0.08964 -0.03471 0.04821  230 ASP A N   
1773 C  CA  . ASP A 230 ? 0.27188 0.41556 0.27742 -0.04681 -0.05810 0.01400  230 ASP A CA  
1774 C  C   . ASP A 230 ? 0.30050 0.35682 0.29852 -0.02152 -0.02163 -0.02355 230 ASP A C   
1775 O  O   . ASP A 230 ? 0.26782 0.31995 0.29365 -0.03686 -0.02930 0.01257  230 ASP A O   
1776 C  CB  . ASP A 230 ? 0.35145 0.37953 0.30416 -0.05416 -0.03663 0.00915  230 ASP A CB  
1777 C  CG  . ASP A 230 ? 0.43157 0.41552 0.31818 -0.09280 -0.03960 0.04139  230 ASP A CG  
1778 O  OD1 . ASP A 230 ? 0.54813 0.41231 0.32285 -0.11685 -0.04327 0.04640  230 ASP A OD1 
1779 O  OD2 . ASP A 230 ? 0.38804 0.42879 0.34940 -0.07976 0.01259  -0.05003 230 ASP A OD2 
1780 N  N   . ARG A 231 ? 0.26878 0.33313 0.32583 0.00786  -0.02417 0.03311  231 ARG A N   
1781 C  CA  . ARG A 231 ? 0.25498 0.29051 0.36276 -0.00832 -0.04015 0.03281  231 ARG A CA  
1782 C  C   . ARG A 231 ? 0.24708 0.25541 0.31960 -0.02961 -0.05816 0.00240  231 ARG A C   
1783 O  O   . ARG A 231 ? 0.23150 0.29280 0.32523 -0.01570 -0.06632 -0.02291 231 ARG A O   
1784 C  CB  . ARG A 231 ? 0.26461 0.38378 0.41818 0.03092  -0.06228 0.02666  231 ARG A CB  
1785 C  CG  . ARG A 231 ? 0.24248 0.40893 0.47416 0.06909  -0.08381 0.01835  231 ARG A CG  
1786 C  CD  . ARG A 231 ? 0.27769 0.55827 0.52089 0.00296  -0.03617 -0.02076 231 ARG A CD  
1787 N  NE  . ARG A 231 ? 0.29482 0.56051 0.55370 0.00466  -0.02047 -0.05960 231 ARG A NE  
1788 C  CZ  . ARG A 231 ? 0.26517 0.59237 0.55007 0.06104  -0.02688 -0.04284 231 ARG A CZ  
1789 N  NH1 . ARG A 231 ? 0.23787 0.59555 0.54027 0.01128  -0.01039 -0.06652 231 ARG A NH1 
1790 N  NH2 . ARG A 231 ? 0.29332 0.52772 0.52025 0.03151  -0.07596 -0.10669 231 ARG A NH2 
1791 N  N   . GLU A 232 ? 0.29177 0.27180 0.29841 -0.08204 -0.05286 0.04049  232 GLU A N   
1792 C  CA  A GLU A 232 ? 0.25143 0.30205 0.30128 -0.03403 -0.04254 0.05268  232 GLU A CA  
1793 C  CA  B GLU A 232 ? 0.26934 0.32674 0.30829 -0.02248 -0.05767 0.05359  232 GLU A CA  
1794 C  C   . GLU A 232 ? 0.27195 0.30580 0.28447 -0.02217 -0.03922 0.06847  232 GLU A C   
1795 O  O   . GLU A 232 ? 0.28715 0.27852 0.25629 -0.06020 -0.00782 0.06677  232 GLU A O   
1796 C  CB  A GLU A 232 ? 0.28075 0.40285 0.32493 -0.06061 -0.01203 0.06361  232 GLU A CB  
1797 C  CB  B GLU A 232 ? 0.32696 0.44189 0.34675 -0.00610 -0.05993 0.05624  232 GLU A CB  
1798 C  CG  A GLU A 232 ? 0.40145 0.49752 0.32670 -0.02327 -0.00161 0.05118  232 GLU A CG  
1799 C  CG  B GLU A 232 ? 0.41736 0.53670 0.37082 0.03019  -0.07784 0.06048  232 GLU A CG  
1800 C  CD  A GLU A 232 ? 0.41495 0.49826 0.31132 -0.05136 0.01139  0.04244  232 GLU A CD  
1801 C  CD  B GLU A 232 ? 0.46444 0.60109 0.40071 0.07637  -0.08090 0.07445  232 GLU A CD  
1802 O  OE1 A GLU A 232 ? 0.23944 0.37981 0.24887 -0.14571 -0.04019 0.06940  232 GLU A OE1 
1803 O  OE1 B GLU A 232 ? 0.44766 0.61280 0.40833 0.08092  -0.08867 0.08945  232 GLU A OE1 
1804 O  OE2 A GLU A 232 ? 0.47436 0.50977 0.32151 -0.04329 0.03349  0.02842  232 GLU A OE2 
1805 O  OE2 B GLU A 232 ? 0.48039 0.61765 0.41040 0.12120  -0.08202 0.07589  232 GLU A OE2 
1806 N  N   . GLU A 233 ? 0.30903 0.30455 0.28589 -0.04041 -0.02167 0.03530  233 GLU A N   
1807 C  CA  . GLU A 233 ? 0.26038 0.28375 0.25742 -0.01158 -0.00782 0.00198  233 GLU A CA  
1808 C  C   . GLU A 233 ? 0.21166 0.26444 0.24422 -0.03799 -0.03146 0.01031  233 GLU A C   
1809 O  O   . GLU A 233 ? 0.22131 0.37379 0.24397 0.04500  -0.03047 0.01402  233 GLU A O   
1810 C  CB  . GLU A 233 ? 0.29901 0.28788 0.26935 -0.04839 0.00534  -0.00151 233 GLU A CB  
1811 C  CG  . GLU A 233 ? 0.41716 0.29888 0.29871 -0.03648 0.01069  0.00547  233 GLU A CG  
1812 C  CD  . GLU A 233 ? 0.48307 0.33168 0.32513 -0.05620 -0.02741 0.00323  233 GLU A CD  
1813 O  OE1 . GLU A 233 ? 0.40516 0.31954 0.32437 -0.01788 -0.02933 0.00425  233 GLU A OE1 
1814 O  OE2 . GLU A 233 ? 0.50984 0.31067 0.34541 -0.02598 -0.04429 0.00615  233 GLU A OE2 
1815 N  N   . LEU A 234 ? 0.26840 0.25288 0.24496 0.00278  -0.01914 -0.00054 234 LEU A N   
1816 C  CA  . LEU A 234 ? 0.28143 0.18305 0.24243 0.00455  -0.00840 0.02568  234 LEU A CA  
1817 C  C   . LEU A 234 ? 0.26312 0.24029 0.24917 0.01693  0.00277  0.04159  234 LEU A C   
1818 O  O   . LEU A 234 ? 0.21478 0.26628 0.25149 0.01450  -0.00779 0.02686  234 LEU A O   
1819 C  CB  . LEU A 234 ? 0.34099 0.16900 0.24542 -0.03797 -0.03590 0.02415  234 LEU A CB  
1820 C  CG  . LEU A 234 ? 0.37902 0.15047 0.25256 -0.04209 -0.07145 0.03320  234 LEU A CG  
1821 C  CD1 . LEU A 234 ? 0.37963 0.19934 0.28222 -0.00601 -0.07193 0.04729  234 LEU A CD1 
1822 C  CD2 . LEU A 234 ? 0.39638 0.28320 0.24681 -0.02138 -0.08221 -0.01500 234 LEU A CD2 
1823 N  N   . ILE A 235 ? 0.21407 0.22576 0.25806 0.04008  0.00122  0.02926  235 ILE A N   
1824 C  CA  . ILE A 235 ? 0.16932 0.28049 0.27674 0.02160  -0.00259 0.02254  235 ILE A CA  
1825 C  C   . ILE A 235 ? 0.22862 0.26904 0.26530 0.03148  -0.01191 0.04644  235 ILE A C   
1826 O  O   . ILE A 235 ? 0.23240 0.26782 0.24716 0.04092  -0.03468 0.01692  235 ILE A O   
1827 C  CB  . ILE A 235 ? 0.18414 0.23503 0.31693 0.03454  -0.03143 0.02927  235 ILE A CB  
1828 C  CG1 . ILE A 235 ? 0.15569 0.24220 0.35477 0.00410  -0.07584 0.00841  235 ILE A CG1 
1829 C  CG2 . ILE A 235 ? 0.26565 0.28816 0.31525 -0.01350 0.01043  0.03667  235 ILE A CG2 
1830 C  CD1 . ILE A 235 ? 0.15224 0.31488 0.37825 0.00991  -0.07799 -0.01638 235 ILE A CD1 
1831 N  N   . SER A 236 ? 0.25730 0.25318 0.27476 0.05144  0.01354  0.04709  236 SER A N   
1832 C  CA  . SER A 236 ? 0.17553 0.19700 0.27860 -0.01461 0.01828  0.00672  236 SER A CA  
1833 C  C   . SER A 236 ? 0.19655 0.24594 0.25451 -0.09538 -0.00869 -0.00805 236 SER A C   
1834 O  O   . SER A 236 ? 0.25720 0.31521 0.21584 -0.05992 -0.02729 -0.01047 236 SER A O   
1835 C  CB  . SER A 236 ? 0.21206 0.26840 0.31131 -0.02286 -0.04872 -0.01827 236 SER A CB  
1836 O  OG  . SER A 236 ? 0.24251 0.31923 0.34786 -0.00013 -0.03274 -0.04263 236 SER A OG  
1837 N  N   . THR A 237 ? 0.25850 0.20472 0.25350 -0.03192 -0.01224 0.00630  237 THR A N   
1838 C  CA  . THR A 237 ? 0.19680 0.20355 0.23957 -0.06307 -0.02331 -0.00583 237 THR A CA  
1839 C  C   . THR A 237 ? 0.19486 0.19920 0.22369 -0.01724 -0.03511 0.00395  237 THR A C   
1840 O  O   . THR A 237 ? 0.18734 0.22944 0.20017 0.01375  -0.02199 0.00057  237 THR A O   
1841 C  CB  . THR A 237 ? 0.16733 0.27125 0.20858 -0.01287 -0.01585 -0.00265 237 THR A CB  
1842 O  OG1 . THR A 237 ? 0.30042 0.32075 0.24292 0.00615  -0.02039 -0.02871 237 THR A OG1 
1843 C  CG2 . THR A 237 ? 0.15965 0.29320 0.22062 -0.03714 -0.02515 0.02390  237 THR A CG2 
1844 N  N   . ALA A 238 ? 0.20230 0.22160 0.24752 0.04599  0.00625  -0.00437 238 ALA A N   
1845 C  CA  . ALA A 238 ? 0.21823 0.17525 0.25520 0.03233  0.00133  -0.02192 238 ALA A CA  
1846 C  C   . ALA A 238 ? 0.19514 0.19994 0.24431 0.01202  0.01421  0.00566  238 ALA A C   
1847 O  O   . ALA A 238 ? 0.22392 0.25887 0.21969 0.01485  -0.03218 0.00947  238 ALA A O   
1848 C  CB  . ALA A 238 ? 0.27366 0.15511 0.28850 0.03567  0.00091  -0.01992 238 ALA A CB  
1849 N  N   . MET A 239 ? 0.15867 0.20353 0.25943 -0.00209 0.03765  0.03357  239 MET A N   
1850 C  CA  . MET A 239 ? 0.19241 0.25883 0.25858 -0.00285 0.02135  0.05773  239 MET A CA  
1851 C  C   . MET A 239 ? 0.21009 0.24415 0.22606 -0.00293 -0.01024 0.02177  239 MET A C   
1852 O  O   . MET A 239 ? 0.20642 0.23596 0.20471 0.00763  -0.01629 0.00309  239 MET A O   
1853 C  CB  . MET A 239 ? 0.22593 0.22846 0.27785 -0.03902 0.04675  0.03294  239 MET A CB  
1854 C  CG  . MET A 239 ? 0.20367 0.33463 0.30798 -0.02635 0.05462  0.04843  239 MET A CG  
1855 S  SD  . MET A 239 ? 0.23057 0.33241 0.33479 -0.02484 0.02416  0.06126  239 MET A SD  
1856 C  CE  . MET A 239 ? 0.20999 0.32392 0.33213 0.06386  -0.02469 0.08616  239 MET A CE  
1857 N  N   . LEU A 240 ? 0.17132 0.26247 0.19840 0.00056  0.01956  0.01834  240 LEU A N   
1858 C  CA  . LEU A 240 ? 0.17851 0.27917 0.23611 -0.02484 -0.01284 -0.01711 240 LEU A CA  
1859 C  C   . LEU A 240 ? 0.21611 0.24883 0.23857 0.01202  -0.00818 0.00264  240 LEU A C   
1860 O  O   . LEU A 240 ? 0.21382 0.22880 0.25076 0.00525  -0.00620 -0.00559 240 LEU A O   
1861 C  CB  . LEU A 240 ? 0.18384 0.32589 0.23606 0.04730  -0.00232 0.01359  240 LEU A CB  
1862 C  CG  . LEU A 240 ? 0.27290 0.36596 0.26223 0.11689  -0.03074 -0.01857 240 LEU A CG  
1863 C  CD1 . LEU A 240 ? 0.34948 0.33282 0.27670 0.13500  -0.06063 0.00246  240 LEU A CD1 
1864 C  CD2 . LEU A 240 ? 0.25491 0.32759 0.26972 0.09487  -0.02615 -0.10100 240 LEU A CD2 
1865 N  N   . LEU A 241 ? 0.24799 0.20779 0.22324 0.00314  -0.01000 -0.00394 241 LEU A N   
1866 C  CA  A LEU A 241 ? 0.22848 0.18615 0.21986 -0.00583 0.00725  0.03063  241 LEU A CA  
1867 C  CA  B LEU A 241 ? 0.20874 0.22327 0.22257 0.01923  0.00529  0.02479  241 LEU A CA  
1868 C  C   . LEU A 241 ? 0.17994 0.21189 0.21206 0.02351  0.00702  -0.00135 241 LEU A C   
1869 O  O   . LEU A 241 ? 0.18859 0.27209 0.23920 0.02389  -0.01323 -0.00466 241 LEU A O   
1870 C  CB  A LEU A 241 ? 0.24142 0.16913 0.20358 -0.01942 0.01802  0.05335  241 LEU A CB  
1871 C  CB  B LEU A 241 ? 0.17622 0.26509 0.21075 0.05842  0.01505  0.02337  241 LEU A CB  
1872 C  CG  A LEU A 241 ? 0.29354 0.15112 0.19597 -0.02147 -0.00081 0.02318  241 LEU A CG  
1873 C  CG  B LEU A 241 ? 0.24991 0.31495 0.21438 0.07868  -0.02075 -0.02622 241 LEU A CG  
1874 C  CD1 A LEU A 241 ? 0.29634 0.14838 0.18984 0.03472  -0.02024 0.02307  241 LEU A CD1 
1875 C  CD1 B LEU A 241 ? 0.30682 0.32234 0.20681 0.03290  0.00799  -0.01968 241 LEU A CD1 
1876 C  CD2 A LEU A 241 ? 0.31352 0.18497 0.19762 -0.08997 0.01252  0.05610  241 LEU A CD2 
1877 C  CD2 B LEU A 241 ? 0.23270 0.36034 0.21769 0.16110  -0.04238 -0.03657 241 LEU A CD2 
1878 N  N   . LEU A 242 ? 0.20315 0.21288 0.20688 0.04081  0.05426  -0.00260 242 LEU A N   
1879 C  CA  . LEU A 242 ? 0.21596 0.24681 0.21791 0.09220  0.01729  -0.02323 242 LEU A CA  
1880 C  C   . LEU A 242 ? 0.31888 0.29803 0.22522 0.06034  0.01369  -0.01801 242 LEU A C   
1881 O  O   . LEU A 242 ? 0.33464 0.26370 0.23405 0.04020  0.02837  0.00198  242 LEU A O   
1882 C  CB  . LEU A 242 ? 0.25844 0.28804 0.24984 0.10467  0.02377  -0.04844 242 LEU A CB  
1883 C  CG  . LEU A 242 ? 0.20712 0.33672 0.28567 0.00392  -0.02012 -0.11950 242 LEU A CG  
1884 C  CD1 . LEU A 242 ? 0.41457 0.40767 0.33897 -0.02758 0.03888  -0.13781 242 LEU A CD1 
1885 C  CD2 . LEU A 242 ? 0.20712 0.46075 0.28908 0.05842  -0.03202 -0.11768 242 LEU A CD2 
1886 N  N   . ILE A 243 ? 0.27125 0.25288 0.21828 0.05088  -0.02486 0.02218  243 ILE A N   
1887 C  CA  . ILE A 243 ? 0.21229 0.27414 0.22903 0.05926  0.01306  0.02381  243 ILE A CA  
1888 C  C   . ILE A 243 ? 0.22647 0.27555 0.21613 0.07914  0.01024  0.00776  243 ILE A C   
1889 O  O   . ILE A 243 ? 0.29028 0.31721 0.22462 0.07540  -0.00806 -0.01836 243 ILE A O   
1890 C  CB  . ILE A 243 ? 0.21977 0.38040 0.27318 0.01214  -0.01854 0.10804  243 ILE A CB  
1891 C  CG1 . ILE A 243 ? 0.23538 0.46308 0.30701 -0.06569 -0.03837 0.05287  243 ILE A CG1 
1892 C  CG2 . ILE A 243 ? 0.34125 0.49618 0.28621 -0.08192 -0.02441 0.06789  243 ILE A CG2 
1893 C  CD1 . ILE A 243 ? 0.35813 0.51246 0.34298 -0.04279 -0.03718 0.07427  243 ILE A CD1 
1894 N  N   . ALA A 244 ? 0.21105 0.23521 0.22945 -0.01376 0.04771  -0.00304 244 ALA A N   
1895 C  CA  . ALA A 244 ? 0.20615 0.23043 0.22363 -0.01322 0.01425  -0.02056 244 ALA A CA  
1896 C  C   . ALA A 244 ? 0.26583 0.21715 0.25616 0.01559  -0.02025 -0.03074 244 ALA A C   
1897 O  O   . ALA A 244 ? 0.28642 0.25256 0.28264 -0.00441 -0.02745 0.00744  244 ALA A O   
1898 C  CB  . ALA A 244 ? 0.26448 0.25519 0.21204 0.07206  0.03078  -0.00837 244 ALA A CB  
1899 N  N   . GLY A 245 ? 0.29791 0.17861 0.24349 0.04766  -0.01954 -0.01730 245 GLY A N   
1900 C  CA  . GLY A 245 ? 0.37738 0.22850 0.25811 -0.00128 -0.07240 -0.06935 245 GLY A CA  
1901 C  C   . GLY A 245 ? 0.41563 0.24423 0.24340 0.01154  -0.13978 -0.07873 245 GLY A C   
1902 O  O   . GLY A 245 ? 0.50801 0.34653 0.28937 0.01337  -0.18591 -0.07393 245 GLY A O   
1903 N  N   . HIS A 246 ? 0.43639 0.24670 0.22021 0.01441  -0.07226 -0.02397 246 HIS A N   
1904 C  CA  . HIS A 246 ? 0.46869 0.39454 0.21476 0.11753  -0.04491 0.01370  246 HIS A CA  
1905 C  C   . HIS A 246 ? 0.41883 0.28234 0.20973 0.00391  -0.05888 -0.04100 246 HIS A C   
1906 O  O   . HIS A 246 ? 0.52711 0.24881 0.22743 0.00994  -0.03442 -0.02395 246 HIS A O   
1907 C  CB  . HIS A 246 ? 0.43006 0.46425 0.19566 0.19617  0.01718  0.00258  246 HIS A CB  
1908 C  CG  . HIS A 246 ? 0.43666 0.58137 0.18596 0.16841  -0.00547 0.00228  246 HIS A CG  
1909 N  ND1 . HIS A 246 ? 0.41658 0.69913 0.24355 0.00437  -0.00818 -0.03173 246 HIS A ND1 
1910 C  CD2 . HIS A 246 ? 0.41672 0.71946 0.22759 0.06788  0.02490  0.04510  246 HIS A CD2 
1911 C  CE1 . HIS A 246 ? 0.35453 0.77007 0.24373 0.02874  -0.02035 -0.02308 246 HIS A CE1 
1912 N  NE2 . HIS A 246 ? 0.34222 0.79195 0.24032 0.10700  0.00533  0.01991  246 HIS A NE2 
1913 N  N   . GLU A 247 ? 0.32090 0.22162 0.23980 0.04694  -0.03509 -0.01172 247 GLU A N   
1914 C  CA  . GLU A 247 ? 0.25037 0.19397 0.23969 0.03551  -0.01967 0.02366  247 GLU A CA  
1915 C  C   . GLU A 247 ? 0.30507 0.27969 0.22349 0.05113  0.00793  0.03188  247 GLU A C   
1916 O  O   . GLU A 247 ? 0.31338 0.31117 0.22737 0.03029  0.00898  0.04002  247 GLU A O   
1917 C  CB  . GLU A 247 ? 0.24569 0.27277 0.26672 0.00039  0.00852  0.01456  247 GLU A CB  
1918 C  CG  . GLU A 247 ? 0.31841 0.40852 0.27647 0.09614  0.04421  0.04783  247 GLU A CG  
1919 C  CD  . GLU A 247 ? 0.37975 0.57196 0.27205 0.15542  0.04481  0.09574  247 GLU A CD  
1920 O  OE1 . GLU A 247 ? 0.35518 0.64138 0.31648 0.18359  0.05212  0.11805  247 GLU A OE1 
1921 O  OE2 . GLU A 247 ? 0.47111 0.61753 0.24541 0.20864  0.06480  0.06276  247 GLU A OE2 
1922 N  N   . THR A 248 ? 0.28407 0.23559 0.20635 0.01293  0.04213  0.00176  248 THR A N   
1923 C  CA  . THR A 248 ? 0.25870 0.26578 0.20316 0.02875  -0.00581 0.01349  248 THR A CA  
1924 C  C   . THR A 248 ? 0.27241 0.19513 0.19974 0.06032  0.00717  0.03613  248 THR A C   
1925 O  O   . THR A 248 ? 0.33863 0.17492 0.18738 0.01441  -0.00662 0.00288  248 THR A O   
1926 C  CB  . THR A 248 ? 0.28410 0.28776 0.19515 -0.04900 -0.00162 -0.00098 248 THR A CB  
1927 O  OG1 . THR A 248 ? 0.29716 0.36840 0.22300 -0.00571 0.02143  0.02288  248 THR A OG1 
1928 C  CG2 . THR A 248 ? 0.33428 0.29909 0.23998 -0.09849 0.00893  -0.04085 248 THR A CG2 
1929 N  N   . THR A 249 ? 0.26516 0.17487 0.20547 0.02137  0.00189  0.00476  249 THR A N   
1930 C  CA  . THR A 249 ? 0.28743 0.14582 0.21583 0.00326  0.01483  0.02853  249 THR A CA  
1931 C  C   . THR A 249 ? 0.27526 0.21055 0.20671 0.00385  0.04503  -0.01899 249 THR A C   
1932 O  O   . THR A 249 ? 0.32483 0.25923 0.23954 0.00888  0.01615  -0.00937 249 THR A O   
1933 C  CB  . THR A 249 ? 0.33018 0.25294 0.22555 -0.08667 0.01386  0.03000  249 THR A CB  
1934 O  OG1 . THR A 249 ? 0.35632 0.27610 0.22817 0.05677  0.05672  0.02745  249 THR A OG1 
1935 C  CG2 . THR A 249 ? 0.33753 0.23798 0.24484 0.00169  0.00873  0.02398  249 THR A CG2 
1936 N  N   . ALA A 250 ? 0.21083 0.25245 0.21004 0.01720  0.06280  0.00185  250 ALA A N   
1937 C  CA  . ALA A 250 ? 0.21902 0.21888 0.18446 0.10151  0.01213  0.00849  250 ALA A CA  
1938 C  C   . ALA A 250 ? 0.29269 0.23087 0.19198 0.07027  0.00388  -0.01943 250 ALA A C   
1939 O  O   . ALA A 250 ? 0.32787 0.24288 0.17666 0.06805  -0.00439 -0.02205 250 ALA A O   
1940 C  CB  . ALA A 250 ? 0.24533 0.24789 0.22100 0.10979  0.02043  -0.04965 250 ALA A CB  
1941 N  N   . SER A 251 ? 0.32277 0.16773 0.21903 0.00780  0.01798  -0.01803 251 SER A N   
1942 C  CA  . SER A 251 ? 0.27760 0.17529 0.24886 -0.01565 0.01397  -0.01197 251 SER A CA  
1943 C  C   . SER A 251 ? 0.28629 0.22005 0.21793 0.00109  0.01398  -0.01554 251 SER A C   
1944 O  O   . SER A 251 ? 0.29870 0.27269 0.19067 0.02517  -0.00694 0.00757  251 SER A O   
1945 C  CB  . SER A 251 ? 0.25151 0.21290 0.32588 -0.04042 0.07351  -0.00346 251 SER A CB  
1946 O  OG  . SER A 251 ? 0.34412 0.32408 0.38941 -0.02378 0.09199  0.01514  251 SER A OG  
1947 N  N   . MET A 252 ? 0.28601 0.19752 0.19436 -0.01193 0.02528  0.03029  252 MET A N   
1948 C  CA  . MET A 252 ? 0.24642 0.23888 0.20055 -0.01526 -0.00281 -0.01573 252 MET A CA  
1949 C  C   . MET A 252 ? 0.29560 0.21680 0.19621 0.07158  0.02431  -0.02172 252 MET A C   
1950 O  O   . MET A 252 ? 0.30066 0.22709 0.20577 0.03602  -0.01071 0.00163  252 MET A O   
1951 C  CB  . MET A 252 ? 0.32497 0.21708 0.17867 0.02658  0.01088  0.00419  252 MET A CB  
1952 C  CG  . MET A 252 ? 0.35091 0.18567 0.19152 0.10320  0.00334  0.01586  252 MET A CG  
1953 S  SD  . MET A 252 ? 0.28171 0.24092 0.20932 0.03158  0.02133  -0.00707 252 MET A SD  
1954 C  CE  . MET A 252 ? 0.25927 0.27350 0.23550 0.00857  -0.03794 -0.02199 252 MET A CE  
1955 N  N   . THR A 253 ? 0.33361 0.19698 0.18928 0.01828  0.02432  -0.04499 253 THR A N   
1956 C  CA  . THR A 253 ? 0.29831 0.19596 0.19719 -0.00447 -0.02047 -0.02821 253 THR A CA  
1957 C  C   . THR A 253 ? 0.28704 0.22202 0.17953 0.02817  -0.03165 0.00003  253 THR A C   
1958 O  O   . THR A 253 ? 0.31715 0.24721 0.18736 0.07368  0.00108  0.00550  253 THR A O   
1959 C  CB  . THR A 253 ? 0.31866 0.20087 0.21087 0.04785  -0.01572 -0.02162 253 THR A CB  
1960 O  OG1 . THR A 253 ? 0.29877 0.26201 0.19849 -0.00167 -0.00789 0.01435  253 THR A OG1 
1961 C  CG2 . THR A 253 ? 0.24482 0.24904 0.23376 0.07179  -0.02389 -0.04054 253 THR A CG2 
1962 N  N   . SER A 254 ? 0.27048 0.24416 0.18203 0.03891  -0.00599 -0.00176 254 SER A N   
1963 C  CA  A SER A 254 ? 0.27743 0.22144 0.20974 -0.01261 -0.01778 -0.00209 254 SER A CA  
1964 C  CA  B SER A 254 ? 0.28278 0.28403 0.19116 0.01675  -0.00863 0.01948  254 SER A CA  
1965 C  C   . SER A 254 ? 0.27674 0.24174 0.19400 0.01147  -0.03052 0.01374  254 SER A C   
1966 O  O   . SER A 254 ? 0.35323 0.25615 0.20922 0.05248  -0.02107 0.00129  254 SER A O   
1967 C  CB  A SER A 254 ? 0.28820 0.24577 0.23882 -0.01265 -0.00633 0.00832  254 SER A CB  
1968 C  CB  B SER A 254 ? 0.32614 0.37129 0.19231 0.04458  0.00971  0.05318  254 SER A CB  
1969 O  OG  A SER A 254 ? 0.32167 0.24724 0.24872 -0.00094 0.00631  0.03720  254 SER A OG  
1970 O  OG  B SER A 254 ? 0.38682 0.40692 0.18400 0.06343  0.03129  0.07568  254 SER A OG  
1971 N  N   . LEU A 255 ? 0.24056 0.23814 0.20918 0.00267  0.02017  -0.00600 255 LEU A N   
1972 C  CA  . LEU A 255 ? 0.26537 0.23161 0.19901 0.04693  -0.02738 -0.00612 255 LEU A CA  
1973 C  C   . LEU A 255 ? 0.30620 0.26672 0.20056 0.04582  -0.02534 0.01277  255 LEU A C   
1974 O  O   . LEU A 255 ? 0.31927 0.23231 0.18120 0.04681  -0.01415 0.02641  255 LEU A O   
1975 C  CB  . LEU A 255 ? 0.28053 0.21103 0.18720 -0.04377 -0.01818 -0.00804 255 LEU A CB  
1976 C  CG  . LEU A 255 ? 0.27984 0.28696 0.18175 -0.09690 0.02379  0.00382  255 LEU A CG  
1977 C  CD1 . LEU A 255 ? 0.32932 0.31062 0.21933 -0.07180 0.01587  -0.05424 255 LEU A CD1 
1978 C  CD2 . LEU A 255 ? 0.41902 0.40523 0.21396 -0.16706 0.00500  0.01097  255 LEU A CD2 
1979 N  N   . SER A 256 ? 0.27944 0.22652 0.19059 -0.02345 -0.01340 0.01015  256 SER A N   
1980 C  CA  . SER A 256 ? 0.24124 0.23614 0.18437 -0.03383 -0.04134 0.02427  256 SER A CA  
1981 C  C   . SER A 256 ? 0.25111 0.27831 0.20277 0.02253  -0.04303 -0.02443 256 SER A C   
1982 O  O   . SER A 256 ? 0.23629 0.31727 0.20414 0.03309  -0.04210 -0.01285 256 SER A O   
1983 C  CB  . SER A 256 ? 0.32572 0.27617 0.18535 0.00577  -0.00496 0.00870  256 SER A CB  
1984 O  OG  . SER A 256 ? 0.29822 0.25983 0.19839 -0.00672 0.00599  0.01080  256 SER A OG  
1985 N  N   . VAL A 257 ? 0.28273 0.24786 0.20058 0.03820  -0.04815 -0.01917 257 VAL A N   
1986 C  CA  . VAL A 257 ? 0.31776 0.26662 0.19809 0.08257  -0.02915 -0.03054 257 VAL A CA  
1987 C  C   . VAL A 257 ? 0.35826 0.26739 0.23060 0.02808  -0.02224 -0.00897 257 VAL A C   
1988 O  O   . VAL A 257 ? 0.32197 0.30018 0.23431 0.02037  -0.05922 -0.01326 257 VAL A O   
1989 C  CB  . VAL A 257 ? 0.33408 0.27136 0.18934 0.09502  -0.04545 -0.01781 257 VAL A CB  
1990 C  CG1 . VAL A 257 ? 0.25017 0.37902 0.18577 -0.00752 -0.03413 -0.04494 257 VAL A CG1 
1991 C  CG2 . VAL A 257 ? 0.36745 0.28636 0.22281 0.10452  -0.05990 0.02441  257 VAL A CG2 
1992 N  N   . ILE A 258 ? 0.37365 0.25093 0.22906 0.04026  0.00735  0.00501  258 ILE A N   
1993 C  CA  . ILE A 258 ? 0.32563 0.29073 0.22853 0.05169  0.00562  0.06312  258 ILE A CA  
1994 C  C   . ILE A 258 ? 0.36250 0.30255 0.20632 0.01669  -0.00018 0.03616  258 ILE A C   
1995 O  O   . ILE A 258 ? 0.36703 0.31141 0.19632 0.04860  -0.02852 -0.00545 258 ILE A O   
1996 C  CB  . ILE A 258 ? 0.30876 0.31125 0.23978 -0.01572 0.02430  0.04418  258 ILE A CB  
1997 C  CG1 . ILE A 258 ? 0.25592 0.37118 0.24049 -0.02143 0.01854  0.02282  258 ILE A CG1 
1998 C  CG2 . ILE A 258 ? 0.33839 0.39802 0.23171 0.01445  0.01724  0.04331  258 ILE A CG2 
1999 C  CD1 . ILE A 258 ? 0.27856 0.31831 0.26245 -0.03395 -0.00230 0.01289  258 ILE A CD1 
2000 N  N   . THR A 259 ? 0.32900 0.29733 0.19744 0.07212  -0.00159 0.00459  259 THR A N   
2001 C  CA  . THR A 259 ? 0.33391 0.28095 0.19740 0.07767  -0.04513 -0.00031 259 THR A CA  
2002 C  C   . THR A 259 ? 0.31439 0.27063 0.22738 0.04782  -0.03551 -0.00628 259 THR A C   
2003 O  O   . THR A 259 ? 0.32728 0.30123 0.22959 0.04307  -0.05826 0.01720  259 THR A O   
2004 C  CB  . THR A 259 ? 0.30991 0.28120 0.18149 0.03667  -0.03920 -0.00922 259 THR A CB  
2005 O  OG1 . THR A 259 ? 0.28848 0.24589 0.19589 0.00061  -0.00112 -0.00326 259 THR A OG1 
2006 C  CG2 . THR A 259 ? 0.29578 0.30780 0.19280 0.10292  -0.04390 -0.01932 259 THR A CG2 
2007 N  N   . LEU A 260 ? 0.30190 0.23270 0.23171 0.04056  -0.03916 -0.03607 260 LEU A N   
2008 C  CA  . LEU A 260 ? 0.34291 0.28123 0.21627 -0.01706 -0.04926 -0.01813 260 LEU A CA  
2009 C  C   . LEU A 260 ? 0.31660 0.31912 0.21565 0.06499  -0.06449 -0.05619 260 LEU A C   
2010 O  O   . LEU A 260 ? 0.33695 0.31369 0.24719 0.05914  -0.08204 -0.03864 260 LEU A O   
2011 C  CB  . LEU A 260 ? 0.34071 0.26068 0.22743 0.04935  -0.07095 0.04616  260 LEU A CB  
2012 C  CG  . LEU A 260 ? 0.24808 0.30405 0.25204 0.05020  -0.05750 0.01266  260 LEU A CG  
2013 C  CD1 . LEU A 260 ? 0.33382 0.27187 0.26314 0.04135  -0.05699 0.06872  260 LEU A CD1 
2014 C  CD2 . LEU A 260 ? 0.31051 0.32737 0.27757 0.00819  -0.06777 -0.02229 260 LEU A CD2 
2015 N  N   . LEU A 261 ? 0.34798 0.31328 0.21469 0.09525  -0.05066 -0.05041 261 LEU A N   
2016 C  CA  . LEU A 261 ? 0.33794 0.31830 0.19778 0.14193  -0.07005 -0.04000 261 LEU A CA  
2017 C  C   . LEU A 261 ? 0.38470 0.31191 0.22110 0.13673  -0.04178 -0.05802 261 LEU A C   
2018 O  O   . LEU A 261 ? 0.40624 0.35890 0.22270 0.06933  -0.06277 -0.00510 261 LEU A O   
2019 C  CB  . LEU A 261 ? 0.40347 0.29213 0.23302 0.15190  -0.04220 -0.01685 261 LEU A CB  
2020 C  CG  . LEU A 261 ? 0.43617 0.35586 0.26310 0.11214  -0.04765 -0.05660 261 LEU A CG  
2021 C  CD1 . LEU A 261 ? 0.37932 0.49543 0.26265 0.13913  -0.00752 -0.04885 261 LEU A CD1 
2022 C  CD2 . LEU A 261 ? 0.45138 0.29326 0.27056 0.03691  -0.05096 -0.03095 261 LEU A CD2 
2023 N  N   . ASP A 262 ? 0.37955 0.29280 0.24951 0.09725  -0.04364 -0.05107 262 ASP A N   
2024 C  CA  . ASP A 262 ? 0.35957 0.27072 0.26900 0.12912  -0.06685 -0.00009 262 ASP A CA  
2025 C  C   . ASP A 262 ? 0.38294 0.25364 0.25629 0.07042  -0.03361 -0.00286 262 ASP A C   
2026 O  O   . ASP A 262 ? 0.48377 0.29641 0.28268 0.02427  -0.00017 0.03667  262 ASP A O   
2027 C  CB  . ASP A 262 ? 0.36832 0.35018 0.27329 0.05875  -0.04947 0.01708  262 ASP A CB  
2028 C  CG  . ASP A 262 ? 0.44408 0.43782 0.26554 0.01034  -0.03498 0.01543  262 ASP A CG  
2029 O  OD1 . ASP A 262 ? 0.38262 0.40718 0.24852 0.02459  -0.00703 0.01359  262 ASP A OD1 
2030 O  OD2 . ASP A 262 ? 0.49542 0.42710 0.26325 0.02985  -0.02914 -0.00617 262 ASP A OD2 
2031 N  N   . HIS A 263 ? 0.32719 0.33133 0.24872 0.06345  -0.03735 -0.05857 263 HIS A N   
2032 C  CA  . HIS A 263 ? 0.40161 0.29940 0.24001 0.09815  -0.06772 -0.07759 263 HIS A CA  
2033 C  C   . HIS A 263 ? 0.38249 0.34604 0.24679 0.07458  -0.08197 -0.04402 263 HIS A C   
2034 O  O   . HIS A 263 ? 0.39733 0.33335 0.25803 0.07432  -0.08171 -0.03593 263 HIS A O   
2035 C  CB  . HIS A 263 ? 0.44584 0.22592 0.22664 0.09853  -0.10800 -0.02312 263 HIS A CB  
2036 C  CG  . HIS A 263 ? 0.45099 0.25791 0.22010 -0.00209 -0.06905 -0.05621 263 HIS A CG  
2037 N  ND1 . HIS A 263 ? 0.44953 0.25684 0.20878 0.02409  -0.05712 -0.01369 263 HIS A ND1 
2038 C  CD2 . HIS A 263 ? 0.49776 0.23071 0.24132 -0.01456 -0.09352 -0.03476 263 HIS A CD2 
2039 C  CE1 . HIS A 263 ? 0.49552 0.25570 0.22590 0.03572  -0.07736 -0.01714 263 HIS A CE1 
2040 N  NE2 . HIS A 263 ? 0.51203 0.24730 0.24343 -0.00314 -0.07891 -0.03009 263 HIS A NE2 
2041 N  N   . PRO A 264 ? 0.39419 0.37433 0.24909 0.07901  -0.11442 -0.03651 264 PRO A N   
2042 C  CA  . PRO A 264 ? 0.38362 0.41112 0.26087 -0.01065 -0.10163 -0.07097 264 PRO A CA  
2043 C  C   . PRO A 264 ? 0.39059 0.42257 0.29973 0.05606  -0.09191 -0.01914 264 PRO A C   
2044 O  O   . PRO A 264 ? 0.34753 0.49422 0.33142 0.01760  -0.11889 -0.03199 264 PRO A O   
2045 C  CB  . PRO A 264 ? 0.47559 0.39904 0.26689 0.01681  -0.10542 -0.04486 264 PRO A CB  
2046 C  CG  . PRO A 264 ? 0.52950 0.34085 0.26031 0.00017  -0.10685 -0.03253 264 PRO A CG  
2047 C  CD  . PRO A 264 ? 0.49656 0.26621 0.24192 0.02464  -0.07900 -0.03961 264 PRO A CD  
2048 N  N   . GLU A 265 ? 0.43304 0.44691 0.31804 0.10264  -0.07020 0.04898  265 GLU A N   
2049 C  CA  . GLU A 265 ? 0.44548 0.51069 0.33538 0.13494  -0.11807 0.02596  265 GLU A CA  
2050 C  C   . GLU A 265 ? 0.42822 0.47242 0.32938 0.09814  -0.12086 -0.02690 265 GLU A C   
2051 O  O   . GLU A 265 ? 0.41665 0.46607 0.33813 0.06673  -0.10536 -0.06978 265 GLU A O   
2052 C  CB  . GLU A 265 ? 0.50962 0.59057 0.37075 0.11107  -0.14208 0.08788  265 GLU A CB  
2053 C  CG  . GLU A 265 ? 0.62914 0.81563 0.43717 0.02626  -0.09529 0.08300  265 GLU A CG  
2054 C  CD  . GLU A 265 ? 0.70115 1.02413 0.48303 -0.04464 -0.05207 0.10336  265 GLU A CD  
2055 O  OE1 . GLU A 265 ? 0.70500 1.07287 0.49709 -0.04967 -0.03348 0.10818  265 GLU A OE1 
2056 O  OE2 . GLU A 265 ? 0.74162 1.12005 0.49972 -0.10116 -0.03132 0.09149  265 GLU A OE2 
2057 N  N   . GLN A 266 ? 0.41980 0.40149 0.30063 0.11865  -0.12799 -0.10028 266 GLN A N   
2058 C  CA  . GLN A 266 ? 0.40436 0.35407 0.30392 0.09556  -0.09268 -0.07524 266 GLN A CA  
2059 C  C   . GLN A 266 ? 0.37227 0.33247 0.30135 0.09206  -0.08791 -0.07178 266 GLN A C   
2060 O  O   . GLN A 266 ? 0.38664 0.33036 0.30437 -0.00415 -0.06543 -0.04378 266 GLN A O   
2061 C  CB  . GLN A 266 ? 0.42381 0.30985 0.31264 0.06235  -0.07866 -0.03927 266 GLN A CB  
2062 C  CG  . GLN A 266 ? 0.44181 0.32140 0.32313 0.08743  -0.09265 0.00653  266 GLN A CG  
2063 C  CD  . GLN A 266 ? 0.42003 0.33399 0.32966 0.07579  -0.10972 -0.00530 266 GLN A CD  
2064 O  OE1 . GLN A 266 ? 0.42986 0.33606 0.32149 0.04956  -0.05436 -0.02473 266 GLN A OE1 
2065 N  NE2 . GLN A 266 ? 0.38988 0.30922 0.33383 0.04324  -0.12072 0.02531  266 GLN A NE2 
2066 N  N   . TYR A 267 ? 0.35670 0.34494 0.28864 0.11558  -0.11577 -0.07922 267 TYR A N   
2067 C  CA  . TYR A 267 ? 0.35189 0.32002 0.30642 0.05702  -0.09115 -0.09295 267 TYR A CA  
2068 C  C   . TYR A 267 ? 0.38152 0.38056 0.32247 0.02622  -0.08424 -0.07298 267 TYR A C   
2069 O  O   . TYR A 267 ? 0.34943 0.41150 0.32522 0.03923  -0.09972 -0.06999 267 TYR A O   
2070 C  CB  . TYR A 267 ? 0.31173 0.35290 0.31552 0.09632  -0.03769 -0.07212 267 TYR A CB  
2071 C  CG  . TYR A 267 ? 0.28896 0.34257 0.31345 0.02604  -0.03138 -0.08766 267 TYR A CG  
2072 C  CD1 . TYR A 267 ? 0.34067 0.39843 0.33473 0.07385  -0.06678 -0.05155 267 TYR A CD1 
2073 C  CD2 . TYR A 267 ? 0.37192 0.43376 0.33223 0.03214  -0.03504 -0.14303 267 TYR A CD2 
2074 C  CE1 . TYR A 267 ? 0.37625 0.41503 0.32272 0.12850  -0.03442 -0.07384 267 TYR A CE1 
2075 C  CE2 . TYR A 267 ? 0.38952 0.44486 0.32974 0.10413  -0.05476 -0.07919 267 TYR A CE2 
2076 C  CZ  . TYR A 267 ? 0.34402 0.41493 0.34458 0.21695  -0.07148 -0.05059 267 TYR A CZ  
2077 O  OH  . TYR A 267 ? 0.37372 0.51728 0.35365 0.16638  -0.08971 -0.09386 267 TYR A OH  
2078 N  N   . ALA A 268 ? 0.37353 0.40370 0.32795 0.01484  -0.10037 -0.06752 268 ALA A N   
2079 C  CA  . ALA A 268 ? 0.38927 0.43110 0.33325 -0.01574 -0.13499 -0.05477 268 ALA A CA  
2080 C  C   . ALA A 268 ? 0.37626 0.42613 0.37262 -0.02730 -0.11458 -0.06001 268 ALA A C   
2081 O  O   . ALA A 268 ? 0.37593 0.47439 0.36935 -0.00030 -0.11888 -0.03504 268 ALA A O   
2082 C  CB  . ALA A 268 ? 0.47144 0.39437 0.32937 -0.05691 -0.16518 -0.00770 268 ALA A CB  
2083 N  N   . ALA A 269 ? 0.29720 0.39207 0.39177 0.03248  -0.07302 -0.05090 269 ALA A N   
2084 C  CA  . ALA A 269 ? 0.33269 0.40993 0.40470 0.03816  -0.09408 -0.01457 269 ALA A CA  
2085 C  C   . ALA A 269 ? 0.33451 0.42266 0.41281 0.03740  -0.09558 -0.00944 269 ALA A C   
2086 O  O   . ALA A 269 ? 0.36380 0.42434 0.44032 0.02103  -0.12270 -0.02193 269 ALA A O   
2087 C  CB  . ALA A 269 ? 0.29717 0.38586 0.42959 0.08088  -0.09275 0.03962  269 ALA A CB  
2088 N  N   . LEU A 270 ? 0.30926 0.40766 0.39140 0.04214  -0.16382 -0.05548 270 LEU A N   
2089 C  CA  . LEU A 270 ? 0.30100 0.42084 0.36850 0.01379  -0.12427 -0.05446 270 LEU A CA  
2090 C  C   . LEU A 270 ? 0.36931 0.47546 0.37075 0.01296  -0.15305 -0.09278 270 LEU A C   
2091 O  O   . LEU A 270 ? 0.42170 0.54543 0.37621 0.03096  -0.16940 -0.06745 270 LEU A O   
2092 C  CB  . LEU A 270 ? 0.26705 0.48460 0.36008 0.00359  -0.08674 -0.03054 270 LEU A CB  
2093 C  CG  . LEU A 270 ? 0.25956 0.40550 0.35834 0.00183  -0.04617 -0.02010 270 LEU A CG  
2094 C  CD1 . LEU A 270 ? 0.29972 0.42082 0.33358 -0.01730 -0.03566 -0.03114 270 LEU A CD1 
2095 C  CD2 . LEU A 270 ? 0.29502 0.39411 0.36923 -0.04986 -0.08467 -0.03473 270 LEU A CD2 
2096 N  N   . ARG A 271 ? 0.32834 0.40928 0.36865 0.01613  -0.15932 -0.11561 271 ARG A N   
2097 C  CA  A ARG A 271 ? 0.35706 0.44450 0.38879 -0.00763 -0.13277 -0.14043 271 ARG A CA  
2098 C  CA  B ARG A 271 ? 0.35741 0.44072 0.37839 -0.01266 -0.14774 -0.14787 271 ARG A CA  
2099 C  C   . ARG A 271 ? 0.34574 0.43968 0.40835 -0.05105 -0.12984 -0.11090 271 ARG A C   
2100 O  O   . ARG A 271 ? 0.37247 0.45134 0.43252 0.00462  -0.10287 -0.11972 271 ARG A O   
2101 C  CB  A ARG A 271 ? 0.42104 0.46138 0.40343 0.06820  -0.11732 -0.15942 271 ARG A CB  
2102 C  CB  B ARG A 271 ? 0.43013 0.45341 0.36942 0.05767  -0.16108 -0.17388 271 ARG A CB  
2103 C  CG  A ARG A 271 ? 0.46444 0.53147 0.43888 0.08602  -0.10755 -0.14665 271 ARG A CG  
2104 C  CG  B ARG A 271 ? 0.46921 0.53409 0.38644 0.06901  -0.18906 -0.16730 271 ARG A CG  
2105 C  CD  A ARG A 271 ? 0.47505 0.55548 0.46045 0.05581  -0.08135 -0.13711 271 ARG A CD  
2106 C  CD  B ARG A 271 ? 0.48589 0.57558 0.39251 0.06856  -0.19487 -0.17435 271 ARG A CD  
2107 N  NE  A ARG A 271 ? 0.45207 0.52298 0.48352 0.04507  -0.06901 -0.12176 271 ARG A NE  
2108 N  NE  B ARG A 271 ? 0.51529 0.59536 0.42339 0.05112  -0.19151 -0.13772 271 ARG A NE  
2109 C  CZ  A ARG A 271 ? 0.41256 0.53637 0.50068 0.02893  -0.08249 -0.11844 271 ARG A CZ  
2110 C  CZ  B ARG A 271 ? 0.52114 0.55672 0.45000 -0.00199 -0.16661 -0.15567 271 ARG A CZ  
2111 N  NH1 A ARG A 271 ? 0.41049 0.53446 0.53155 0.01368  -0.08247 -0.10598 271 ARG A NH1 
2112 N  NH1 B ARG A 271 ? 0.50816 0.59728 0.47870 -0.00332 -0.14974 -0.12528 271 ARG A NH1 
2113 N  NH2 A ARG A 271 ? 0.37225 0.48785 0.48640 0.02613  -0.09712 -0.12906 271 ARG A NH2 
2114 N  NH2 B ARG A 271 ? 0.53628 0.49260 0.43333 -0.02905 -0.17266 -0.21085 271 ARG A NH2 
2115 N  N   . ALA A 272 ? 0.32392 0.44064 0.42803 -0.04767 -0.14993 -0.02953 272 ALA A N   
2116 C  CA  . ALA A 272 ? 0.27361 0.50349 0.43287 -0.07450 -0.14044 -0.01881 272 ALA A CA  
2117 C  C   . ALA A 272 ? 0.33467 0.50527 0.44324 -0.05925 -0.13168 0.00269  272 ALA A C   
2118 O  O   . ALA A 272 ? 0.38514 0.54040 0.45715 -0.11464 -0.12628 0.01781  272 ALA A O   
2119 C  CB  . ALA A 272 ? 0.27685 0.50722 0.43874 -0.07562 -0.13327 -0.04637 272 ALA A CB  
2120 N  N   . ASP A 273 ? 0.32493 0.44639 0.42899 -0.07453 -0.11478 0.02628  273 ASP A N   
2121 C  CA  . ASP A 273 ? 0.32712 0.53095 0.42882 -0.06464 -0.10123 0.00613  273 ASP A CA  
2122 C  C   . ASP A 273 ? 0.29147 0.47314 0.39606 -0.01406 -0.10054 0.00875  273 ASP A C   
2123 O  O   . ASP A 273 ? 0.25274 0.48402 0.38291 -0.03288 -0.05401 0.02446  273 ASP A O   
2124 C  CB  . ASP A 273 ? 0.28874 0.60379 0.45033 -0.06624 -0.06165 0.00937  273 ASP A CB  
2125 C  CG  . ASP A 273 ? 0.35895 0.67588 0.48581 -0.10087 -0.04811 -0.01212 273 ASP A CG  
2126 O  OD1 . ASP A 273 ? 0.33996 0.65766 0.49377 -0.15191 -0.04055 0.00519  273 ASP A OD1 
2127 O  OD2 . ASP A 273 ? 0.45327 0.70152 0.49957 -0.07177 -0.01886 -0.05462 273 ASP A OD2 
2128 N  N   . ARG A 274 ? 0.34512 0.40485 0.38386 -0.03306 -0.12611 0.00103  274 ARG A N   
2129 C  CA  . ARG A 274 ? 0.30390 0.31706 0.34994 0.01805  -0.10438 -0.03036 274 ARG A CA  
2130 C  C   . ARG A 274 ? 0.30261 0.32456 0.35249 0.00894  -0.04645 -0.03691 274 ARG A C   
2131 O  O   . ARG A 274 ? 0.36561 0.34147 0.34366 -0.04774 -0.06300 -0.00479 274 ARG A O   
2132 C  CB  . ARG A 274 ? 0.35622 0.26035 0.35772 -0.00729 -0.04130 -0.01227 274 ARG A CB  
2133 C  CG  . ARG A 274 ? 0.40943 0.33933 0.36585 -0.03444 -0.06174 -0.01956 274 ARG A CG  
2134 C  CD  . ARG A 274 ? 0.39520 0.28960 0.37624 -0.00625 -0.06743 -0.06427 274 ARG A CD  
2135 N  NE  . ARG A 274 ? 0.38513 0.36870 0.38200 0.02373  -0.09253 -0.04795 274 ARG A NE  
2136 C  CZ  . ARG A 274 ? 0.36179 0.36184 0.36888 -0.02725 -0.10362 -0.08353 274 ARG A CZ  
2137 N  NH1 . ARG A 274 ? 0.40247 0.33736 0.38202 -0.02722 -0.10747 -0.05285 274 ARG A NH1 
2138 N  NH2 . ARG A 274 ? 0.41054 0.39082 0.35701 -0.09491 -0.05910 -0.07038 274 ARG A NH2 
2139 N  N   . SER A 275 ? 0.30713 0.29641 0.36868 -0.01017 0.01366  -0.01920 275 SER A N   
2140 C  CA  . SER A 275 ? 0.26769 0.34803 0.39360 -0.04159 0.02610  -0.02867 275 SER A CA  
2141 C  C   . SER A 275 ? 0.26169 0.39637 0.39065 -0.05570 0.00034  0.00322  275 SER A C   
2142 O  O   . SER A 275 ? 0.31174 0.44348 0.36355 -0.09438 -0.00883 -0.01171 275 SER A O   
2143 C  CB  . SER A 275 ? 0.28068 0.35088 0.43278 0.05006  0.00471  0.00130  275 SER A CB  
2144 O  OG  . SER A 275 ? 0.33996 0.43653 0.45680 0.00824  -0.07098 0.01915  275 SER A OG  
2145 N  N   . LEU A 276 ? 0.22784 0.40566 0.39277 -0.03589 -0.00657 0.01785  276 LEU A N   
2146 C  CA  . LEU A 276 ? 0.20167 0.33232 0.38776 -0.03404 -0.01947 0.03252  276 LEU A CA  
2147 C  C   . LEU A 276 ? 0.20617 0.30413 0.34479 0.00854  -0.05555 0.03049  276 LEU A C   
2148 O  O   . LEU A 276 ? 0.26316 0.32674 0.32222 -0.00002 -0.02548 0.00375  276 LEU A O   
2149 C  CB  . LEU A 276 ? 0.21781 0.37097 0.41930 -0.02179 -0.03340 0.01037  276 LEU A CB  
2150 C  CG  . LEU A 276 ? 0.26745 0.44685 0.43154 -0.01001 -0.05608 -0.02026 276 LEU A CG  
2151 C  CD1 . LEU A 276 ? 0.27086 0.50460 0.42938 -0.03337 -0.07776 0.03607  276 LEU A CD1 
2152 C  CD2 . LEU A 276 ? 0.31599 0.52027 0.44531 0.04056  -0.05278 -0.02068 276 LEU A CD2 
2153 N  N   . VAL A 277 ? 0.19676 0.30380 0.30626 0.03420  -0.05529 0.02994  277 VAL A N   
2154 C  CA  . VAL A 277 ? 0.19482 0.27523 0.29525 0.04728  -0.06104 0.00713  277 VAL A CA  
2155 C  C   . VAL A 277 ? 0.21447 0.26556 0.27938 -0.03652 -0.06148 -0.01018 277 VAL A C   
2156 O  O   . VAL A 277 ? 0.18901 0.28628 0.28774 -0.01134 -0.03369 -0.02797 277 VAL A O   
2157 C  CB  . VAL A 277 ? 0.20924 0.28014 0.31579 0.06721  -0.08276 -0.00015 277 VAL A CB  
2158 C  CG1 . VAL A 277 ? 0.27464 0.29874 0.33360 0.07252  -0.07790 0.04192  277 VAL A CG1 
2159 C  CG2 . VAL A 277 ? 0.27215 0.29422 0.32631 -0.01456 -0.10265 -0.01438 277 VAL A CG2 
2160 N  N   . PRO A 278 ? 0.31372 0.23723 0.27116 -0.03635 -0.02052 -0.00506 278 PRO A N   
2161 C  CA  . PRO A 278 ? 0.31437 0.24134 0.24068 -0.07682 -0.00158 0.02390  278 PRO A CA  
2162 C  C   . PRO A 278 ? 0.31434 0.31781 0.24718 -0.01898 -0.03963 0.00667  278 PRO A C   
2163 O  O   . PRO A 278 ? 0.31519 0.28605 0.21489 -0.01880 -0.00970 -0.00705 278 PRO A O   
2164 C  CB  . PRO A 278 ? 0.39042 0.26285 0.27442 -0.10851 -0.00364 0.02312  278 PRO A CB  
2165 C  CG  . PRO A 278 ? 0.38826 0.30757 0.28659 -0.14649 -0.08662 0.02319  278 PRO A CG  
2166 C  CD  . PRO A 278 ? 0.39790 0.29008 0.26739 -0.11967 -0.04874 0.02795  278 PRO A CD  
2167 N  N   . GLY A 279 ? 0.24652 0.31744 0.26139 0.01521  -0.02397 0.02300  279 GLY A N   
2168 C  CA  . GLY A 279 ? 0.26387 0.31248 0.27943 -0.03112 -0.00605 0.04275  279 GLY A CA  
2169 C  C   . GLY A 279 ? 0.28679 0.24399 0.28013 -0.02791 -0.02855 0.03209  279 GLY A C   
2170 O  O   . GLY A 279 ? 0.20928 0.31149 0.29061 0.01750  -0.00601 -0.00772 279 GLY A O   
2171 N  N   . ALA A 280 ? 0.26243 0.26125 0.27488 0.01997  -0.03757 0.02006  280 ALA A N   
2172 C  CA  . ALA A 280 ? 0.22315 0.26062 0.25456 -0.02854 -0.02873 0.01794  280 ALA A CA  
2173 C  C   . ALA A 280 ? 0.23099 0.28017 0.23895 -0.00714 -0.02753 0.01809  280 ALA A C   
2174 O  O   . ALA A 280 ? 0.22042 0.25598 0.24331 0.00867  -0.04749 0.01153  280 ALA A O   
2175 C  CB  . ALA A 280 ? 0.32058 0.24167 0.24446 -0.01421 -0.04820 -0.00358 280 ALA A CB  
2176 N  N   . VAL A 281 ? 0.18853 0.26333 0.24161 0.01109  -0.04069 0.01607  281 VAL A N   
2177 C  CA  . VAL A 281 ? 0.18981 0.23738 0.25273 -0.01690 -0.05398 0.02413  281 VAL A CA  
2178 C  C   . VAL A 281 ? 0.20013 0.23074 0.23624 -0.04452 -0.04001 0.00146  281 VAL A C   
2179 O  O   . VAL A 281 ? 0.18622 0.21518 0.24109 -0.01220 -0.06844 0.01268  281 VAL A O   
2180 C  CB  . VAL A 281 ? 0.23458 0.18570 0.27598 -0.02314 -0.08810 0.01456  281 VAL A CB  
2181 C  CG1 . VAL A 281 ? 0.26950 0.24612 0.28387 0.03198  -0.08622 -0.01139 281 VAL A CG1 
2182 C  CG2 . VAL A 281 ? 0.26500 0.18151 0.28714 -0.01378 -0.09808 0.01351  281 VAL A CG2 
2183 N  N   . GLU A 282 ? 0.23279 0.25676 0.20609 0.04882  -0.03422 0.01818  282 GLU A N   
2184 C  CA  . GLU A 282 ? 0.28340 0.19930 0.20035 0.00210  -0.02037 0.02445  282 GLU A CA  
2185 C  C   . GLU A 282 ? 0.26382 0.19379 0.21344 -0.02882 -0.03370 0.01987  282 GLU A C   
2186 O  O   . GLU A 282 ? 0.24282 0.22752 0.19015 0.00369  -0.02093 0.00887  282 GLU A O   
2187 C  CB  . GLU A 282 ? 0.17162 0.28436 0.24021 0.00711  0.02601  0.04075  282 GLU A CB  
2188 C  CG  . GLU A 282 ? 0.23352 0.30888 0.25229 0.05583  0.01309  0.02646  282 GLU A CG  
2189 C  CD  . GLU A 282 ? 0.28205 0.30604 0.24791 0.02031  -0.00763 0.00876  282 GLU A CD  
2190 O  OE1 . GLU A 282 ? 0.34098 0.26504 0.25617 -0.00702 -0.02430 0.02710  282 GLU A OE1 
2191 O  OE2 . GLU A 282 ? 0.31949 0.29441 0.23550 -0.01344 -0.02685 -0.01690 282 GLU A OE2 
2192 N  N   . GLU A 283 ? 0.23549 0.21911 0.20970 0.01162  -0.03268 0.06145  283 GLU A N   
2193 C  CA  . GLU A 283 ? 0.18473 0.27654 0.21066 0.00348  -0.03461 0.06359  283 GLU A CA  
2194 C  C   . GLU A 283 ? 0.22572 0.22948 0.22071 0.02279  0.02082  0.06743  283 GLU A C   
2195 O  O   . GLU A 283 ? 0.26360 0.28169 0.25044 0.01904  0.00794  0.06670  283 GLU A O   
2196 C  CB  . GLU A 283 ? 0.24940 0.27435 0.22801 0.02883  -0.04787 0.06247  283 GLU A CB  
2197 C  CG  . GLU A 283 ? 0.27932 0.23169 0.22367 0.00989  -0.05930 0.04646  283 GLU A CG  
2198 C  CD  . GLU A 283 ? 0.36090 0.25426 0.21962 0.10107  -0.08703 0.00602  283 GLU A CD  
2199 O  OE1 . GLU A 283 ? 0.44320 0.26469 0.26655 0.07242  -0.09239 -0.00440 283 GLU A OE1 
2200 O  OE2 . GLU A 283 ? 0.34156 0.25335 0.22129 0.04598  -0.07644 -0.00644 283 GLU A OE2 
2201 N  N   . LEU A 284 ? 0.21024 0.22597 0.21646 0.03583  -0.02823 0.02057  284 LEU A N   
2202 C  CA  . LEU A 284 ? 0.20514 0.20809 0.19338 -0.00418 -0.02306 -0.01921 284 LEU A CA  
2203 C  C   . LEU A 284 ? 0.26726 0.23785 0.18606 -0.00558 -0.03037 -0.00563 284 LEU A C   
2204 O  O   . LEU A 284 ? 0.24281 0.21932 0.20927 0.01890  -0.01481 0.00488  284 LEU A O   
2205 C  CB  . LEU A 284 ? 0.21890 0.24188 0.19559 0.01788  -0.03151 -0.02911 284 LEU A CB  
2206 C  CG  . LEU A 284 ? 0.27559 0.23058 0.20516 -0.02207 -0.03756 -0.00080 284 LEU A CG  
2207 C  CD1 . LEU A 284 ? 0.26077 0.23960 0.24370 0.00027  -0.00766 -0.01530 284 LEU A CD1 
2208 C  CD2 . LEU A 284 ? 0.25605 0.32116 0.20579 0.00306  -0.03488 -0.00281 284 LEU A CD2 
2209 N  N   . LEU A 285 ? 0.24720 0.23547 0.15899 0.08002  -0.01653 -0.00092 285 LEU A N   
2210 C  CA  . LEU A 285 ? 0.21625 0.15418 0.16489 -0.01312 -0.03805 0.04168  285 LEU A CA  
2211 C  C   . LEU A 285 ? 0.19102 0.17189 0.18398 0.00188  -0.00755 0.01301  285 LEU A C   
2212 O  O   . LEU A 285 ? 0.28573 0.17767 0.17258 -0.03122 0.00240  -0.00889 285 LEU A O   
2213 C  CB  . LEU A 285 ? 0.25783 0.14909 0.16069 0.02076  -0.03209 0.05089  285 LEU A CB  
2214 C  CG  . LEU A 285 ? 0.20557 0.15776 0.19514 -0.02573 -0.04572 0.04157  285 LEU A CG  
2215 C  CD1 . LEU A 285 ? 0.23618 0.18567 0.22970 -0.01334 -0.02915 0.06888  285 LEU A CD1 
2216 C  CD2 . LEU A 285 ? 0.22480 0.22676 0.19017 0.00066  -0.05416 0.00617  285 LEU A CD2 
2217 N  N   . ARG A 286 ? 0.23726 0.18072 0.20082 0.05692  -0.02527 0.00500  286 ARG A N   
2218 C  CA  . ARG A 286 ? 0.17604 0.16452 0.20039 0.04231  -0.02760 -0.00178 286 ARG A CA  
2219 C  C   . ARG A 286 ? 0.28180 0.19921 0.21713 0.00810  -0.01534 0.02059  286 ARG A C   
2220 O  O   . ARG A 286 ? 0.26682 0.19458 0.21464 -0.01242 0.00866  -0.00828 286 ARG A O   
2221 C  CB  . ARG A 286 ? 0.17396 0.23756 0.21642 0.07547  -0.01329 -0.02534 286 ARG A CB  
2222 C  CG  . ARG A 286 ? 0.21580 0.24136 0.20420 0.09884  -0.01986 -0.02820 286 ARG A CG  
2223 C  CD  . ARG A 286 ? 0.20779 0.28764 0.16904 0.03596  -0.06188 -0.01297 286 ARG A CD  
2224 N  NE  . ARG A 286 ? 0.26951 0.28306 0.16595 0.07516  -0.02154 0.02399  286 ARG A NE  
2225 C  CZ  . ARG A 286 ? 0.32124 0.24797 0.19175 0.08829  -0.03658 0.00731  286 ARG A CZ  
2226 N  NH1 . ARG A 286 ? 0.37462 0.21613 0.22368 0.05282  -0.01409 0.01650  286 ARG A NH1 
2227 N  NH2 . ARG A 286 ? 0.31104 0.29285 0.20539 0.02470  -0.03613 0.00171  286 ARG A NH2 
2228 N  N   . TYR A 287 ? 0.25176 0.21809 0.19634 0.03404  -0.03152 0.01579  287 TYR A N   
2229 C  CA  . TYR A 287 ? 0.23709 0.18336 0.19801 0.00047  -0.05034 -0.01053 287 TYR A CA  
2230 C  C   . TYR A 287 ? 0.16369 0.17189 0.21215 0.02616  -0.00499 -0.02690 287 TYR A C   
2231 O  O   . TYR A 287 ? 0.24177 0.18602 0.26032 -0.00578 -0.00502 0.02584  287 TYR A O   
2232 C  CB  . TYR A 287 ? 0.25673 0.18962 0.19903 0.02962  -0.05388 0.03027  287 TYR A CB  
2233 C  CG  . TYR A 287 ? 0.27652 0.19914 0.17450 0.05630  -0.04057 0.02707  287 TYR A CG  
2234 C  CD1 . TYR A 287 ? 0.27922 0.31339 0.19835 0.13120  -0.02072 0.01216  287 TYR A CD1 
2235 C  CD2 . TYR A 287 ? 0.34384 0.24505 0.17550 -0.00601 -0.04795 -0.00413 287 TYR A CD2 
2236 C  CE1 . TYR A 287 ? 0.41282 0.28915 0.19410 0.07015  -0.03027 0.04372  287 TYR A CE1 
2237 C  CE2 . TYR A 287 ? 0.33203 0.34544 0.20679 0.06032  -0.02337 0.04409  287 TYR A CE2 
2238 C  CZ  . TYR A 287 ? 0.41787 0.33489 0.19589 0.02706  -0.02110 0.07161  287 TYR A CZ  
2239 O  OH  . TYR A 287 ? 0.49275 0.38364 0.19434 -0.02083 -0.03915 0.06619  287 TYR A OH  
2240 N  N   . LEU A 288 ? 0.17060 0.19068 0.21932 0.05737  -0.00110 -0.00174 288 LEU A N   
2241 C  CA  . LEU A 288 ? 0.19617 0.19218 0.21091 0.02596  -0.04098 -0.01473 288 LEU A CA  
2242 C  C   . LEU A 288 ? 0.29684 0.20223 0.20047 -0.01256 -0.01574 -0.00251 288 LEU A C   
2243 O  O   . LEU A 288 ? 0.28131 0.24906 0.20046 0.00383  -0.00944 0.01376  288 LEU A O   
2244 C  CB  . LEU A 288 ? 0.30878 0.22468 0.20892 -0.03477 -0.01544 -0.03832 288 LEU A CB  
2245 C  CG  . LEU A 288 ? 0.35033 0.20759 0.18021 -0.06344 0.03103  0.00168  288 LEU A CG  
2246 C  CD1 . LEU A 288 ? 0.37058 0.16692 0.19999 0.00997  -0.00504 -0.00462 288 LEU A CD1 
2247 C  CD2 . LEU A 288 ? 0.42833 0.23587 0.18045 -0.03185 -0.01900 0.02551  288 LEU A CD2 
2248 N  N   . ALA A 289 ? 0.31360 0.20992 0.16742 0.00978  -0.00815 -0.01832 289 ALA A N   
2249 C  CA  . ALA A 289 ? 0.26480 0.15459 0.21435 0.01427  0.03348  -0.02336 289 ALA A CA  
2250 C  C   . ALA A 289 ? 0.26667 0.24056 0.22319 0.01980  0.04391  -0.00526 289 ALA A C   
2251 O  O   . ALA A 289 ? 0.31985 0.25906 0.21332 -0.02479 0.01415  0.01674  289 ALA A O   
2252 C  CB  . ALA A 289 ? 0.30982 0.16664 0.22058 -0.00723 0.00409  -0.00393 289 ALA A CB  
2253 N  N   . ILE A 290 ? 0.20383 0.24699 0.21410 0.07259  0.03992  0.04900  290 ILE A N   
2254 C  CA  . ILE A 290 ? 0.24032 0.25854 0.23127 0.04621  0.02260  0.01250  290 ILE A CA  
2255 C  C   . ILE A 290 ? 0.22260 0.31658 0.24859 0.05473  0.01662  0.05141  290 ILE A C   
2256 O  O   . ILE A 290 ? 0.23055 0.32423 0.27432 0.00013  0.04898  0.03489  290 ILE A O   
2257 C  CB  . ILE A 290 ? 0.22423 0.24230 0.23358 0.06584  0.00758  0.06366  290 ILE A CB  
2258 C  CG1 . ILE A 290 ? 0.33116 0.18915 0.28638 0.08736  0.05016  0.07524  290 ILE A CG1 
2259 C  CG2 . ILE A 290 ? 0.20539 0.36026 0.21952 0.00714  0.00783  0.03815  290 ILE A CG2 
2260 C  CD1 . ILE A 290 ? 0.36724 0.19090 0.33936 0.00279  0.06639  0.00535  290 ILE A CD1 
2261 N  N   . ALA A 291 ? 0.27359 0.26608 0.23349 -0.00849 0.04021  0.03877  291 ALA A N   
2262 C  CA  . ALA A 291 ? 0.26687 0.19239 0.25013 -0.01584 0.00431  0.04142  291 ALA A CA  
2263 C  C   . ALA A 291 ? 0.33604 0.23632 0.29527 0.00288  0.02794  0.02444  291 ALA A C   
2264 O  O   . ALA A 291 ? 0.40227 0.25814 0.27835 0.00017  0.09974  -0.00935 291 ALA A O   
2265 C  CB  . ALA A 291 ? 0.27430 0.19145 0.23854 0.03384  0.00781  0.02588  291 ALA A CB  
2266 N  N   . ASP A 292 ? 0.44911 0.29973 0.33216 -0.01090 0.05444  0.03091  292 ASP A N   
2267 C  CA  . ASP A 292 ? 0.43773 0.22519 0.34581 -0.01154 0.06466  0.02413  292 ASP A CA  
2268 C  C   . ASP A 292 ? 0.44000 0.25343 0.34804 -0.05085 0.11731  -0.07898 292 ASP A C   
2269 O  O   . ASP A 292 ? 0.41759 0.31728 0.37275 -0.04949 0.03541  -0.08376 292 ASP A O   
2270 C  CB  . ASP A 292 ? 0.47065 0.34332 0.39703 -0.00544 0.02524  0.00918  292 ASP A CB  
2271 C  CG  . ASP A 292 ? 0.49377 0.41770 0.44548 0.06938  0.00504  0.02262  292 ASP A CG  
2272 O  OD1 . ASP A 292 ? 0.56771 0.24635 0.42594 0.05625  0.01277  0.01958  292 ASP A OD1 
2273 O  OD2 . ASP A 292 ? 0.46259 0.50327 0.48081 -0.00652 -0.03362 0.05800  292 ASP A OD2 
2274 N  N   . ILE A 293 ? 0.42520 0.32642 0.35693 -0.12677 0.15707  -0.06812 293 ILE A N   
2275 C  CA  . ILE A 293 ? 0.56456 0.43620 0.39833 -0.08110 0.10939  -0.07991 293 ILE A CA  
2276 C  C   . ILE A 293 ? 0.57099 0.38874 0.40600 -0.08582 0.08532  -0.05992 293 ILE A C   
2277 O  O   . ILE A 293 ? 0.55898 0.42274 0.40522 -0.05410 0.01573  -0.03161 293 ILE A O   
2278 C  CB  . ILE A 293 ? 0.70047 0.55272 0.43191 -0.07390 0.09253  -0.12281 293 ILE A CB  
2279 C  CG1 . ILE A 293 ? 0.71158 0.59227 0.45608 0.04241  0.05501  -0.12993 293 ILE A CG1 
2280 C  CG2 . ILE A 293 ? 0.75453 0.65062 0.42773 -0.07641 0.10940  -0.14024 293 ILE A CG2 
2281 C  CD1 . ILE A 293 ? 0.78671 0.62397 0.47827 0.01358  0.04724  -0.12627 293 ILE A CD1 
2282 N  N   . ALA A 294 ? 0.49703 0.26405 0.40913 -0.14273 0.09966  -0.04703 294 ALA A N   
2283 C  CA  . ALA A 294 ? 0.48224 0.31495 0.42647 -0.07920 0.07519  -0.03398 294 ALA A CA  
2284 C  C   . ALA A 294 ? 0.49561 0.28509 0.41118 0.04530  0.06189  -0.03184 294 ALA A C   
2285 O  O   . ALA A 294 ? 0.66054 0.38608 0.44287 0.08621  0.07662  0.00640  294 ALA A O   
2286 C  CB  . ALA A 294 ? 0.50080 0.36571 0.45063 -0.13383 0.02412  -0.09015 294 ALA A CB  
2287 N  N   . GLY A 295 ? 0.27542 0.20763 0.37747 -0.00368 0.00463  -0.07713 295 GLY A N   
2288 C  CA  . GLY A 295 ? 0.28719 0.19977 0.36083 0.02602  -0.04621 -0.08538 295 GLY A CA  
2289 C  C   . GLY A 295 ? 0.29438 0.18853 0.31813 0.03266  -0.05084 -0.05334 295 GLY A C   
2290 O  O   . GLY A 295 ? 0.31510 0.17383 0.30699 0.03493  -0.04662 -0.01292 295 GLY A O   
2291 N  N   . GLY A 296 ? 0.25403 0.22803 0.29270 0.02282  -0.01162 -0.04521 296 GLY A N   
2292 C  CA  . GLY A 296 ? 0.27736 0.25965 0.27281 -0.01956 -0.03519 -0.04253 296 GLY A CA  
2293 C  C   . GLY A 296 ? 0.25361 0.25242 0.26866 0.00550  -0.00346 -0.00969 296 GLY A C   
2294 O  O   . GLY A 296 ? 0.26185 0.26414 0.26030 0.02367  0.02609  -0.00358 296 GLY A O   
2295 N  N   . ARG A 297 ? 0.26366 0.20906 0.24528 0.01409  0.01365  -0.07440 297 ARG A N   
2296 C  CA  . ARG A 297 ? 0.24170 0.18411 0.26282 -0.02575 0.00312  -0.03557 297 ARG A CA  
2297 C  C   . ARG A 297 ? 0.30448 0.21928 0.28605 0.02387  -0.00947 -0.01764 297 ARG A C   
2298 O  O   . ARG A 297 ? 0.27550 0.23710 0.29946 -0.03647 -0.02039 -0.02793 297 ARG A O   
2299 C  CB  . ARG A 297 ? 0.21804 0.18672 0.28417 -0.00032 0.03883  0.01446  297 ARG A CB  
2300 C  CG  . ARG A 297 ? 0.23497 0.19874 0.27071 -0.05676 0.00493  0.04087  297 ARG A CG  
2301 C  CD  . ARG A 297 ? 0.29062 0.12344 0.28084 0.00266  0.02860  0.00363  297 ARG A CD  
2302 N  NE  . ARG A 297 ? 0.29027 0.17146 0.26417 -0.04195 -0.04079 -0.01186 297 ARG A NE  
2303 C  CZ  . ARG A 297 ? 0.19695 0.18475 0.25811 -0.04838 -0.02517 0.00935  297 ARG A CZ  
2304 N  NH1 . ARG A 297 ? 0.26367 0.23514 0.23130 0.01880  -0.01933 -0.01236 297 ARG A NH1 
2305 N  NH2 . ARG A 297 ? 0.19932 0.16756 0.26888 -0.00650 -0.02771 0.02660  297 ARG A NH2 
2306 N  N   . VAL A 298 ? 0.29776 0.22248 0.29983 -0.02536 0.01446  0.00310  298 VAL A N   
2307 C  CA  . VAL A 298 ? 0.23821 0.24123 0.33168 -0.06579 -0.02147 -0.06689 298 VAL A CA  
2308 C  C   . VAL A 298 ? 0.28663 0.17537 0.31644 -0.02522 -0.01979 -0.04333 298 VAL A C   
2309 O  O   . VAL A 298 ? 0.29665 0.27170 0.32813 -0.06276 -0.07215 0.00590  298 VAL A O   
2310 C  CB  . VAL A 298 ? 0.25111 0.24202 0.38106 -0.07033 -0.06460 -0.03621 298 VAL A CB  
2311 C  CG1 . VAL A 298 ? 0.31882 0.29342 0.39303 -0.00862 -0.02879 0.03841  298 VAL A CG1 
2312 C  CG2 . VAL A 298 ? 0.24665 0.38790 0.42087 -0.03992 -0.06347 -0.05576 298 VAL A CG2 
2313 N  N   . ALA A 299 ? 0.29016 0.23538 0.30926 0.00744  -0.02374 -0.08677 299 ALA A N   
2314 C  CA  . ALA A 299 ? 0.32819 0.21662 0.31356 0.02512  -0.04627 -0.03371 299 ALA A CA  
2315 C  C   . ALA A 299 ? 0.32634 0.30135 0.33322 0.02772  -0.08762 -0.01570 299 ALA A C   
2316 O  O   . ALA A 299 ? 0.34868 0.33686 0.34236 -0.05246 -0.06735 -0.06899 299 ALA A O   
2317 C  CB  . ALA A 299 ? 0.36032 0.32169 0.30613 0.08156  -0.03206 -0.03341 299 ALA A CB  
2318 N  N   . THR A 300 ? 0.27217 0.31531 0.33672 -0.03759 -0.08214 -0.03306 300 THR A N   
2319 C  CA  . THR A 300 ? 0.34593 0.24008 0.33355 -0.08219 -0.10032 -0.06054 300 THR A CA  
2320 C  C   . THR A 300 ? 0.34511 0.32732 0.35082 0.02898  -0.08367 -0.05063 300 THR A C   
2321 O  O   . THR A 300 ? 0.37520 0.37201 0.38622 0.00772  -0.08453 -0.06969 300 THR A O   
2322 C  CB  . THR A 300 ? 0.32181 0.32206 0.34452 -0.09300 -0.08989 -0.04777 300 THR A CB  
2323 O  OG1 . THR A 300 ? 0.30708 0.34269 0.34778 -0.06297 -0.09782 -0.04739 300 THR A OG1 
2324 C  CG2 . THR A 300 ? 0.39098 0.30755 0.36860 0.01670  -0.07140 -0.09214 300 THR A CG2 
2325 N  N   . ALA A 301 ? 0.38772 0.30685 0.34636 0.05620  -0.06514 -0.04634 301 ALA A N   
2326 C  CA  . ALA A 301 ? 0.38776 0.34758 0.36156 0.06547  -0.04811 -0.11001 301 ALA A CA  
2327 C  C   . ALA A 301 ? 0.39926 0.33431 0.38640 0.07526  -0.07006 -0.11761 301 ALA A C   
2328 O  O   . ALA A 301 ? 0.43086 0.33052 0.37589 0.01552  -0.03456 -0.14077 301 ALA A O   
2329 C  CB  . ALA A 301 ? 0.44840 0.46102 0.37671 0.05165  -0.04532 -0.13261 301 ALA A CB  
2330 N  N   . ASP A 302 ? 0.41773 0.36061 0.42367 0.05415  -0.08742 -0.13657 302 ASP A N   
2331 C  CA  . ASP A 302 ? 0.39128 0.41950 0.43819 0.03711  -0.06442 -0.16197 302 ASP A CA  
2332 C  C   . ASP A 302 ? 0.34955 0.45048 0.42758 0.04801  -0.06639 -0.16499 302 ASP A C   
2333 O  O   . ASP A 302 ? 0.38268 0.42857 0.43470 0.02266  -0.07955 -0.14413 302 ASP A O   
2334 C  CB  . ASP A 302 ? 0.43975 0.38739 0.47073 0.02887  -0.05579 -0.21316 302 ASP A CB  
2335 C  CG  . ASP A 302 ? 0.51945 0.38793 0.48937 0.10650  -0.02223 -0.23825 302 ASP A CG  
2336 O  OD1 . ASP A 302 ? 0.49114 0.48060 0.46233 0.05081  -0.04252 -0.22188 302 ASP A OD1 
2337 O  OD2 . ASP A 302 ? 0.65173 0.44643 0.54349 0.13659  -0.00386 -0.26143 302 ASP A OD2 
2338 N  N   . ILE A 303 ? 0.30570 0.37327 0.40982 0.07683  -0.06119 -0.15678 303 ILE A N   
2339 C  CA  . ILE A 303 ? 0.38061 0.31006 0.41340 0.08062  -0.08050 -0.13396 303 ILE A CA  
2340 C  C   . ILE A 303 ? 0.37805 0.34190 0.45050 0.12762  -0.05446 -0.10855 303 ILE A C   
2341 O  O   . ILE A 303 ? 0.39915 0.34636 0.46357 0.03783  -0.03422 -0.09900 303 ILE A O   
2342 C  CB  . ILE A 303 ? 0.38178 0.25828 0.38987 0.05775  -0.05854 -0.10046 303 ILE A CB  
2343 C  CG1 . ILE A 303 ? 0.39433 0.28422 0.36991 0.10663  -0.05271 -0.10029 303 ILE A CG1 
2344 C  CG2 . ILE A 303 ? 0.40689 0.30430 0.39641 0.01498  -0.07900 -0.11044 303 ILE A CG2 
2345 C  CD1 . ILE A 303 ? 0.37635 0.32862 0.37440 0.05065  -0.05574 -0.10303 303 ILE A CD1 
2346 N  N   . GLU A 304 ? 0.40822 0.41631 0.47861 0.17090  -0.01490 -0.18220 304 GLU A N   
2347 C  CA  . GLU A 304 ? 0.44924 0.45863 0.52558 0.14466  0.00900  -0.20907 304 GLU A CA  
2348 C  C   . GLU A 304 ? 0.46428 0.55937 0.51072 0.15807  -0.02102 -0.17504 304 GLU A C   
2349 O  O   . GLU A 304 ? 0.43884 0.59564 0.50059 0.16527  -0.03656 -0.17256 304 GLU A O   
2350 C  CB  . GLU A 304 ? 0.49148 0.52678 0.58950 0.18247  0.03823  -0.24804 304 GLU A CB  
2351 C  CG  . GLU A 304 ? 0.66788 0.68393 0.67144 0.16128  0.05847  -0.26143 304 GLU A CG  
2352 C  CD  . GLU A 304 ? 0.83691 0.88999 0.73267 0.14199  0.07573  -0.22804 304 GLU A CD  
2353 O  OE1 . GLU A 304 ? 0.91725 0.91339 0.77473 0.14011  0.06372  -0.21528 304 GLU A OE1 
2354 O  OE2 . GLU A 304 ? 0.88647 0.99954 0.76849 0.13097  0.08548  -0.21047 304 GLU A OE2 
2355 N  N   . VAL A 305 ? 0.48557 0.53521 0.50128 0.19505  -0.03158 -0.16066 305 VAL A N   
2356 C  CA  . VAL A 305 ? 0.52806 0.54838 0.52103 0.18705  -0.03543 -0.16334 305 VAL A CA  
2357 C  C   . VAL A 305 ? 0.49071 0.60912 0.53620 0.23444  -0.04108 -0.13492 305 VAL A C   
2358 O  O   . VAL A 305 ? 0.52548 0.67879 0.54024 0.17808  -0.06756 -0.15011 305 VAL A O   
2359 C  CB  . VAL A 305 ? 0.57368 0.48491 0.50141 0.18939  -0.06680 -0.21020 305 VAL A CB  
2360 C  CG1 . VAL A 305 ? 0.59490 0.51100 0.50232 0.15659  -0.12091 -0.20124 305 VAL A CG1 
2361 C  CG2 . VAL A 305 ? 0.57107 0.42080 0.48723 0.16624  -0.06317 -0.20962 305 VAL A CG2 
2362 N  N   . GLU A 306 ? 0.49734 0.61172 0.55463 0.24835  -0.01483 -0.15075 306 GLU A N   
2363 C  CA  . GLU A 306 ? 0.51759 0.61022 0.58568 0.26065  0.00714  -0.12381 306 GLU A CA  
2364 C  C   . GLU A 306 ? 0.57732 0.65956 0.61518 0.23674  -0.00238 -0.08384 306 GLU A C   
2365 O  O   . GLU A 306 ? 0.63483 0.74096 0.62864 0.20180  -0.02813 -0.04031 306 GLU A O   
2366 C  CB  . GLU A 306 ? 0.54830 0.68612 0.60138 0.21318  0.03424  -0.09830 306 GLU A CB  
2367 C  CG  . GLU A 306 ? 0.62055 0.73549 0.61586 0.15631  0.04469  -0.08522 306 GLU A CG  
2368 C  CD  . GLU A 306 ? 0.69645 0.79033 0.63114 0.14054  0.04339  -0.06195 306 GLU A CD  
2369 O  OE1 . GLU A 306 ? 0.73765 0.78508 0.65043 0.13946  0.04693  -0.04320 306 GLU A OE1 
2370 O  OE2 . GLU A 306 ? 0.68009 0.78819 0.61794 0.13623  0.03545  -0.07065 306 GLU A OE2 
2371 N  N   . GLY A 307 ? 0.58281 0.58717 0.63761 0.29853  0.02809  -0.07521 307 GLY A N   
2372 C  CA  . GLY A 307 ? 0.63364 0.57558 0.64977 0.23097  0.01695  -0.05888 307 GLY A CA  
2373 C  C   . GLY A 307 ? 0.69261 0.53756 0.65075 0.19179  -0.00548 -0.03990 307 GLY A C   
2374 O  O   . GLY A 307 ? 0.70969 0.51105 0.66528 0.12707  -0.02037 -0.02519 307 GLY A O   
2375 N  N   . GLN A 308 ? 0.69139 0.48786 0.62256 0.25530  -0.01904 -0.02534 308 GLN A N   
2376 C  CA  A GLN A 308 ? 0.73283 0.52842 0.61661 0.21157  -0.02523 0.00209  308 GLN A CA  
2377 C  CA  B GLN A 308 ? 0.72429 0.51131 0.61517 0.18008  -0.01291 0.00040  308 GLN A CA  
2378 C  C   . GLN A 308 ? 0.70821 0.51279 0.60292 0.14050  -0.03071 -0.01447 308 GLN A C   
2379 O  O   . GLN A 308 ? 0.71490 0.54930 0.60183 0.15211  -0.05295 -0.03751 308 GLN A O   
2380 C  CB  A GLN A 308 ? 0.79035 0.59393 0.62935 0.25024  -0.02033 0.02037  308 GLN A CB  
2381 C  CB  B GLN A 308 ? 0.76705 0.53565 0.62383 0.15797  0.01546  0.01489  308 GLN A CB  
2382 C  CG  A GLN A 308 ? 0.82141 0.66445 0.64730 0.30382  -0.01358 0.03097  308 GLN A CG  
2383 C  CG  B GLN A 308 ? 0.79378 0.57592 0.63819 0.14576  0.04535  0.01906  308 GLN A CG  
2384 C  CD  A GLN A 308 ? 0.83779 0.71439 0.66658 0.34155  0.00490  0.05244  308 GLN A CD  
2385 C  CD  B GLN A 308 ? 0.79570 0.58121 0.64982 0.13446  0.08160  0.03956  308 GLN A CD  
2386 O  OE1 A GLN A 308 ? 0.86841 0.69243 0.67518 0.40597  0.01424  0.06445  308 GLN A OE1 
2387 O  OE1 B GLN A 308 ? 0.77406 0.54907 0.64904 0.08629  0.10595  0.03471  308 GLN A OE1 
2388 N  NE2 A GLN A 308 ? 0.80407 0.73891 0.67357 0.32706  0.01451  0.05440  308 GLN A NE2 
2389 N  NE2 B GLN A 308 ? 0.81282 0.58651 0.65839 0.18455  0.08872  0.06045  308 GLN A NE2 
2390 N  N   . LEU A 309 ? 0.64361 0.46080 0.58302 0.11215  -0.02671 -0.01614 309 LEU A N   
2391 C  CA  . LEU A 309 ? 0.51202 0.38479 0.56127 0.05814  -0.01798 -0.06073 309 LEU A CA  
2392 C  C   . LEU A 309 ? 0.47288 0.34415 0.52769 0.01305  0.00002  -0.06725 309 LEU A C   
2393 O  O   . LEU A 309 ? 0.47976 0.33030 0.54908 0.06235  0.03285  -0.07730 309 LEU A O   
2394 C  CB  . LEU A 309 ? 0.59943 0.30303 0.57539 -0.05274 -0.00347 -0.08391 309 LEU A CB  
2395 C  CG  . LEU A 309 ? 0.65356 0.32375 0.57317 -0.09782 -0.00556 -0.11868 309 LEU A CG  
2396 C  CD1 . LEU A 309 ? 0.69735 0.34124 0.56703 -0.04410 -0.01935 -0.13471 309 LEU A CD1 
2397 C  CD2 . LEU A 309 ? 0.69622 0.39108 0.57748 -0.12996 0.00551  -0.13055 309 LEU A CD2 
2398 N  N   . ILE A 310 ? 0.39712 0.27587 0.48301 0.00301  -0.01430 -0.07221 310 ILE A N   
2399 C  CA  . ILE A 310 ? 0.40221 0.26878 0.44370 -0.00436 -0.05698 -0.08099 310 ILE A CA  
2400 C  C   . ILE A 310 ? 0.41615 0.30238 0.46647 -0.06064 -0.08610 -0.13699 310 ILE A C   
2401 O  O   . ILE A 310 ? 0.44720 0.32512 0.45639 0.01065  -0.09026 -0.10237 310 ILE A O   
2402 C  CB  . ILE A 310 ? 0.36704 0.29433 0.40499 -0.00095 -0.08606 -0.07853 310 ILE A CB  
2403 C  CG1 . ILE A 310 ? 0.30970 0.32259 0.37875 -0.02927 -0.07961 -0.12857 310 ILE A CG1 
2404 C  CG2 . ILE A 310 ? 0.42264 0.28918 0.39098 0.05115  -0.12438 -0.01770 310 ILE A CG2 
2405 C  CD1 . ILE A 310 ? 0.32034 0.32583 0.37852 0.01512  -0.09469 -0.14514 310 ILE A CD1 
2406 N  N   . ARG A 311 ? 0.39054 0.32460 0.48372 -0.07623 -0.06967 -0.14965 311 ARG A N   
2407 C  CA  . ARG A 311 ? 0.44036 0.26897 0.49137 0.00193  -0.10905 -0.11802 311 ARG A CA  
2408 C  C   . ARG A 311 ? 0.39884 0.31421 0.45109 -0.05203 -0.10215 -0.08669 311 ARG A C   
2409 O  O   . ARG A 311 ? 0.39130 0.30244 0.44173 0.00357  -0.10504 -0.08448 311 ARG A O   
2410 C  CB  . ARG A 311 ? 0.48857 0.32824 0.53622 -0.08853 -0.10637 -0.11817 311 ARG A CB  
2411 C  CG  . ARG A 311 ? 0.57358 0.25761 0.58512 -0.04404 -0.08901 -0.04488 311 ARG A CG  
2412 C  CD  . ARG A 311 ? 0.66543 0.40598 0.63568 -0.08319 -0.07297 -0.02889 311 ARG A CD  
2413 N  NE  . ARG A 311 ? 0.67745 0.48901 0.68003 -0.11646 -0.08241 0.04125  311 ARG A NE  
2414 C  CZ  . ARG A 311 ? 0.65229 0.53736 0.70251 -0.11701 -0.09378 0.08478  311 ARG A CZ  
2415 N  NH1 . ARG A 311 ? 0.67486 0.72397 0.71287 -0.11073 -0.11582 0.07713  311 ARG A NH1 
2416 N  NH2 . ARG A 311 ? 0.59344 0.32421 0.69324 -0.12086 -0.07923 0.11261  311 ARG A NH2 
2417 N  N   . ALA A 312 ? 0.42771 0.38178 0.41349 0.00779  -0.11682 -0.11267 312 ALA A N   
2418 C  CA  . ALA A 312 ? 0.43295 0.38540 0.40332 -0.00578 -0.13166 -0.12000 312 ALA A CA  
2419 C  C   . ALA A 312 ? 0.39134 0.33190 0.42149 -0.01598 -0.12936 -0.09611 312 ALA A C   
2420 O  O   . ALA A 312 ? 0.43557 0.34014 0.43247 -0.06704 -0.12008 -0.09523 312 ALA A O   
2421 C  CB  . ALA A 312 ? 0.42495 0.44101 0.39332 -0.03411 -0.15508 -0.12776 312 ALA A CB  
2422 N  N   . GLY A 313 ? 0.35493 0.33343 0.41598 -0.00123 -0.11590 -0.10463 313 GLY A N   
2423 C  CA  . GLY A 313 ? 0.33157 0.30882 0.41203 -0.02707 -0.08955 -0.08013 313 GLY A CA  
2424 C  C   . GLY A 313 ? 0.35044 0.33910 0.42065 -0.08185 -0.03586 -0.07738 313 GLY A C   
2425 O  O   . GLY A 313 ? 0.36730 0.38201 0.45153 -0.06444 -0.00645 -0.05050 313 GLY A O   
2426 N  N   . GLU A 314 ? 0.33876 0.30687 0.39893 -0.09033 -0.03528 -0.06900 314 GLU A N   
2427 C  CA  . GLU A 314 ? 0.32225 0.20989 0.39180 -0.01123 -0.04088 -0.03115 314 GLU A CA  
2428 C  C   . GLU A 314 ? 0.31699 0.20259 0.35738 -0.06159 -0.02227 -0.05545 314 GLU A C   
2429 O  O   . GLU A 314 ? 0.32754 0.27797 0.33859 -0.06675 -0.05078 -0.06506 314 GLU A O   
2430 C  CB  . GLU A 314 ? 0.36069 0.20541 0.43717 -0.04173 -0.06577 -0.04002 314 GLU A CB  
2431 C  CG  . GLU A 314 ? 0.39933 0.30586 0.46919 -0.09088 -0.09029 -0.03672 314 GLU A CG  
2432 C  CD  . GLU A 314 ? 0.46862 0.33216 0.50072 -0.04757 -0.10148 0.00377  314 GLU A CD  
2433 O  OE1 . GLU A 314 ? 0.44283 0.37964 0.49765 -0.08411 -0.08499 -0.01696 314 GLU A OE1 
2434 O  OE2 . GLU A 314 ? 0.52180 0.44821 0.53171 -0.07840 -0.08446 0.03239  314 GLU A OE2 
2435 N  N   . GLY A 315 ? 0.33245 0.23716 0.33089 -0.05336 -0.01508 -0.06286 315 GLY A N   
2436 C  CA  . GLY A 315 ? 0.34284 0.23659 0.33101 0.00382  -0.02837 -0.04250 315 GLY A CA  
2437 C  C   . GLY A 315 ? 0.33785 0.22154 0.30631 0.00153  -0.03425 -0.00074 315 GLY A C   
2438 O  O   . GLY A 315 ? 0.34273 0.23637 0.31151 -0.04005 -0.00934 -0.02867 315 GLY A O   
2439 N  N   . VAL A 316 ? 0.34813 0.20485 0.27442 -0.04293 -0.04053 -0.02444 316 VAL A N   
2440 C  CA  . VAL A 316 ? 0.29759 0.22459 0.27263 -0.02381 -0.04439 0.00078  316 VAL A CA  
2441 C  C   . VAL A 316 ? 0.26733 0.23272 0.28092 -0.03023 -0.06517 -0.00917 316 VAL A C   
2442 O  O   . VAL A 316 ? 0.34438 0.25010 0.33460 -0.02832 -0.05504 -0.00621 316 VAL A O   
2443 C  CB  . VAL A 316 ? 0.26866 0.23400 0.26268 -0.05459 -0.06089 0.00452  316 VAL A CB  
2444 C  CG1 . VAL A 316 ? 0.21797 0.27546 0.28566 0.03826  -0.05141 -0.01648 316 VAL A CG1 
2445 C  CG2 . VAL A 316 ? 0.36729 0.25995 0.28619 -0.01496 -0.00351 0.02984  316 VAL A CG2 
2446 N  N   . ILE A 317 ? 0.24659 0.19611 0.25053 -0.01329 -0.04587 -0.04536 317 ILE A N   
2447 C  CA  . ILE A 317 ? 0.22682 0.18427 0.24547 -0.00146 -0.00298 -0.04308 317 ILE A CA  
2448 C  C   . ILE A 317 ? 0.25459 0.19757 0.24756 0.00306  0.00019  -0.00444 317 ILE A C   
2449 O  O   . ILE A 317 ? 0.29162 0.17973 0.28587 0.00329  -0.01811 -0.00177 317 ILE A O   
2450 C  CB  . ILE A 317 ? 0.26121 0.27151 0.24395 -0.01209 0.01534  -0.04120 317 ILE A CB  
2451 C  CG1 . ILE A 317 ? 0.25854 0.28149 0.25996 -0.01315 0.04042  0.02104  317 ILE A CG1 
2452 C  CG2 . ILE A 317 ? 0.38340 0.35241 0.26051 0.03058  0.01018  -0.03119 317 ILE A CG2 
2453 C  CD1 . ILE A 317 ? 0.30896 0.35860 0.29457 -0.01377 0.05779  -0.02361 317 ILE A CD1 
2454 N  N   . VAL A 318 ? 0.25465 0.17792 0.24627 -0.01962 -0.00905 -0.01696 318 VAL A N   
2455 C  CA  . VAL A 318 ? 0.22640 0.21093 0.23129 -0.00441 -0.02545 0.00059  318 VAL A CA  
2456 C  C   . VAL A 318 ? 0.30536 0.18372 0.23634 -0.02180 -0.01267 0.03436  318 VAL A C   
2457 O  O   . VAL A 318 ? 0.35763 0.19946 0.25416 0.02080  -0.01597 0.01096  318 VAL A O   
2458 C  CB  . VAL A 318 ? 0.17939 0.22478 0.21521 0.01584  -0.03867 0.00122  318 VAL A CB  
2459 C  CG1 . VAL A 318 ? 0.17342 0.28677 0.23346 -0.00345 -0.02042 0.03436  318 VAL A CG1 
2460 C  CG2 . VAL A 318 ? 0.24750 0.29073 0.22747 0.04245  0.00771  -0.01618 318 VAL A CG2 
2461 N  N   . VAL A 319 ? 0.38669 0.20110 0.23788 -0.01497 -0.01574 0.04146  319 VAL A N   
2462 C  CA  . VAL A 319 ? 0.29834 0.21378 0.21983 -0.05883 -0.00190 0.01384  319 VAL A CA  
2463 C  C   . VAL A 319 ? 0.29185 0.21365 0.25219 0.02362  -0.01247 0.02847  319 VAL A C   
2464 O  O   . VAL A 319 ? 0.33080 0.15759 0.24491 -0.01362 0.00446  -0.00358 319 VAL A O   
2465 C  CB  . VAL A 319 ? 0.31188 0.22823 0.23217 -0.03520 -0.02542 0.03414  319 VAL A CB  
2466 C  CG1 . VAL A 319 ? 0.30048 0.25476 0.22508 -0.04459 -0.02139 0.03060  319 VAL A CG1 
2467 C  CG2 . VAL A 319 ? 0.30624 0.24113 0.23345 -0.05301 -0.00932 -0.01707 319 VAL A CG2 
2468 N  N   . ASN A 320 ? 0.24755 0.21638 0.26330 -0.00625 0.00610  0.03587  320 ASN A N   
2469 C  CA  . ASN A 320 ? 0.25954 0.16933 0.24891 0.00110  -0.01508 0.04706  320 ASN A CA  
2470 C  C   . ASN A 320 ? 0.28568 0.14612 0.24813 -0.01215 0.01297  0.03803  320 ASN A C   
2471 O  O   . ASN A 320 ? 0.20284 0.25649 0.25145 -0.00599 -0.02639 0.01792  320 ASN A O   
2472 C  CB  . ASN A 320 ? 0.25377 0.17961 0.24822 0.03684  0.00255  -0.00193 320 ASN A CB  
2473 C  CG  . ASN A 320 ? 0.24840 0.19376 0.22493 0.01805  -0.03046 0.01941  320 ASN A CG  
2474 O  OD1 . ASN A 320 ? 0.32192 0.25743 0.21230 0.03795  -0.04881 0.00347  320 ASN A OD1 
2475 N  ND2 . ASN A 320 ? 0.25559 0.23674 0.22818 0.01820  -0.02386 -0.00092 320 ASN A ND2 
2476 N  N   . SER A 321 ? 0.31224 0.17072 0.25833 0.01382  -0.01911 0.03092  321 SER A N   
2477 C  CA  . SER A 321 ? 0.31464 0.20445 0.26708 0.04974  0.00524  0.04743  321 SER A CA  
2478 C  C   . SER A 321 ? 0.29234 0.15932 0.25916 0.02172  0.01588  0.03072  321 SER A C   
2479 O  O   . SER A 321 ? 0.27151 0.23403 0.24357 0.01646  -0.01873 -0.01307 321 SER A O   
2480 C  CB  . SER A 321 ? 0.28759 0.21748 0.28514 -0.05192 -0.01593 0.03016  321 SER A CB  
2481 O  OG  . SER A 321 ? 0.31914 0.19186 0.28654 -0.00204 0.03481  0.05114  321 SER A OG  
2482 N  N   . ILE A 322 ? 0.37594 0.12124 0.26822 0.01200  0.04348  -0.00660 322 ILE A N   
2483 C  CA  . ILE A 322 ? 0.36126 0.15575 0.27013 0.01624  0.05202  0.01219  322 ILE A CA  
2484 C  C   . ILE A 322 ? 0.32263 0.19060 0.25686 0.02392  0.00033  0.00443  322 ILE A C   
2485 O  O   . ILE A 322 ? 0.28552 0.19331 0.26197 0.03047  -0.03622 -0.01227 322 ILE A O   
2486 C  CB  . ILE A 322 ? 0.35607 0.15554 0.29717 0.00716  0.04466  0.02338  322 ILE A CB  
2487 C  CG1 . ILE A 322 ? 0.27291 0.19640 0.28554 0.01319  0.03806  0.03288  322 ILE A CG1 
2488 C  CG2 . ILE A 322 ? 0.41370 0.16328 0.30854 0.00941  0.04661  0.02393  322 ILE A CG2 
2489 C  CD1 . ILE A 322 ? 0.36440 0.15830 0.28785 -0.02721 0.06175  0.00848  322 ILE A CD1 
2490 N  N   . ALA A 323 ? 0.33235 0.19544 0.22187 0.04793  0.01833  0.01699  323 ALA A N   
2491 C  CA  . ALA A 323 ? 0.23952 0.21021 0.22880 0.03864  -0.03504 0.02206  323 ALA A CA  
2492 C  C   . ALA A 323 ? 0.19651 0.26098 0.25658 0.07037  -0.00236 0.01370  323 ALA A C   
2493 O  O   . ALA A 323 ? 0.22019 0.23669 0.25342 0.05349  -0.00996 0.02014  323 ALA A O   
2494 C  CB  . ALA A 323 ? 0.25775 0.25967 0.22466 0.07704  0.00333  -0.00918 323 ALA A CB  
2495 N  N   . ASN A 324 ? 0.27329 0.22300 0.22483 0.02444  -0.00121 0.01656  324 ASN A N   
2496 C  CA  . ASN A 324 ? 0.28992 0.20834 0.23768 0.07389  -0.01404 0.03200  324 ASN A CA  
2497 C  C   . ASN A 324 ? 0.29178 0.18195 0.23447 0.04794  -0.01206 0.02493  324 ASN A C   
2498 O  O   . ASN A 324 ? 0.27403 0.24924 0.22759 0.03359  -0.02622 0.03514  324 ASN A O   
2499 C  CB  . ASN A 324 ? 0.25471 0.14016 0.21359 0.04995  -0.03912 0.03427  324 ASN A CB  
2500 C  CG  . ASN A 324 ? 0.24079 0.17153 0.21271 0.06495  -0.01884 0.01330  324 ASN A CG  
2501 O  OD1 . ASN A 324 ? 0.31656 0.27133 0.22102 0.05508  -0.00376 0.03779  324 ASN A OD1 
2502 N  ND2 . ASN A 324 ? 0.25810 0.25473 0.21749 0.10765  0.03445  0.02122  324 ASN A ND2 
2503 N  N   . ARG A 325 ? 0.34185 0.15888 0.21403 0.04694  -0.00165 0.04893  325 ARG A N   
2504 C  CA  . ARG A 325 ? 0.38567 0.21069 0.23735 0.09865  -0.01095 0.02793  325 ARG A CA  
2505 C  C   . ARG A 325 ? 0.35975 0.23701 0.26225 0.06799  -0.05211 -0.01828 325 ARG A C   
2506 O  O   . ARG A 325 ? 0.40262 0.19427 0.28624 0.01345  -0.06975 0.00997  325 ARG A O   
2507 C  CB  . ARG A 325 ? 0.36273 0.27922 0.23576 0.03566  0.01362  -0.00910 325 ARG A CB  
2508 C  CG  . ARG A 325 ? 0.40852 0.24767 0.23286 0.05481  -0.04431 -0.02137 325 ARG A CG  
2509 C  CD  . ARG A 325 ? 0.42944 0.24233 0.24251 0.09941  -0.03516 -0.00881 325 ARG A CD  
2510 N  NE  . ARG A 325 ? 0.38713 0.26027 0.21368 0.04713  -0.00895 -0.02456 325 ARG A NE  
2511 C  CZ  . ARG A 325 ? 0.34834 0.22764 0.25919 0.10783  -0.01408 0.04135  325 ARG A CZ  
2512 N  NH1 . ARG A 325 ? 0.32843 0.24773 0.29713 0.05862  -0.03959 0.04996  325 ARG A NH1 
2513 N  NH2 . ARG A 325 ? 0.28534 0.21303 0.25948 0.05956  0.00091  0.05312  325 ARG A NH2 
2514 N  N   . ASP A 326 ? 0.33448 0.25729 0.25350 0.07888  -0.05117 -0.02027 326 ASP A N   
2515 C  CA  . ASP A 326 ? 0.30888 0.28338 0.25875 0.10969  -0.06804 -0.04819 326 ASP A CA  
2516 C  C   . ASP A 326 ? 0.34181 0.29720 0.29206 0.11334  -0.10292 -0.04556 326 ASP A C   
2517 O  O   . ASP A 326 ? 0.34387 0.31198 0.28993 0.09726  -0.11643 -0.07574 326 ASP A O   
2518 C  CB  . ASP A 326 ? 0.33908 0.24329 0.24642 0.12095  -0.04635 -0.08739 326 ASP A CB  
2519 C  CG  . ASP A 326 ? 0.33652 0.27633 0.27883 0.11234  -0.04387 -0.07340 326 ASP A CG  
2520 O  OD1 . ASP A 326 ? 0.32631 0.28660 0.31598 0.10669  -0.06435 -0.05347 326 ASP A OD1 
2521 O  OD2 . ASP A 326 ? 0.34952 0.27850 0.26464 0.06470  -0.03334 -0.05221 326 ASP A OD2 
2522 N  N   . GLY A 327 ? 0.29204 0.31338 0.31640 0.13445  -0.10791 -0.02394 327 GLY A N   
2523 C  CA  . GLY A 327 ? 0.30519 0.35621 0.35306 0.10662  -0.10681 -0.02432 327 GLY A CA  
2524 C  C   . GLY A 327 ? 0.30546 0.42177 0.39895 0.08868  -0.10605 -0.04420 327 GLY A C   
2525 O  O   . GLY A 327 ? 0.30937 0.44042 0.43058 0.10590  -0.11876 -0.07978 327 GLY A O   
2526 N  N   . THR A 328 ? 0.33446 0.35823 0.40290 0.12301  -0.06773 -0.04448 328 THR A N   
2527 C  CA  . THR A 328 ? 0.39916 0.40451 0.40965 0.08382  -0.06916 -0.08901 328 THR A CA  
2528 C  C   . THR A 328 ? 0.36478 0.32814 0.40948 0.06508  -0.04532 -0.07686 328 THR A C   
2529 O  O   . THR A 328 ? 0.36316 0.39906 0.44429 0.13523  -0.04617 -0.10161 328 THR A O   
2530 C  CB  . THR A 328 ? 0.33304 0.40902 0.43585 0.04868  -0.10637 -0.10126 328 THR A CB  
2531 O  OG1 . THR A 328 ? 0.32228 0.41350 0.44162 0.10421  -0.12030 -0.11200 328 THR A OG1 
2532 C  CG2 . THR A 328 ? 0.33627 0.39649 0.45422 0.02260  -0.12189 -0.08172 328 THR A CG2 
2533 N  N   . VAL A 329 ? 0.33074 0.26057 0.39400 0.11484  -0.06816 -0.09308 329 VAL A N   
2534 C  CA  . VAL A 329 ? 0.23750 0.30946 0.34911 0.13460  -0.05177 -0.10049 329 VAL A CA  
2535 C  C   . VAL A 329 ? 0.26344 0.29406 0.31316 0.08488  -0.05572 -0.09422 329 VAL A C   
2536 O  O   . VAL A 329 ? 0.32464 0.35879 0.29942 -0.01026 -0.00520 -0.04895 329 VAL A O   
2537 C  CB  . VAL A 329 ? 0.25748 0.33525 0.33662 0.04844  -0.06309 -0.09847 329 VAL A CB  
2538 C  CG1 . VAL A 329 ? 0.23367 0.32997 0.34179 0.04715  -0.02542 -0.06385 329 VAL A CG1 
2539 C  CG2 . VAL A 329 ? 0.32625 0.40903 0.34188 0.07054  -0.04785 -0.10404 329 VAL A CG2 
2540 N  N   . TYR A 330 ? 0.26229 0.28237 0.28149 0.07675  -0.05572 -0.03997 330 TYR A N   
2541 C  CA  . TYR A 330 ? 0.30666 0.27399 0.27540 0.11294  -0.06409 -0.03074 330 TYR A CA  
2542 C  C   . TYR A 330 ? 0.36563 0.29369 0.30540 0.16805  -0.07565 0.00055  330 TYR A C   
2543 O  O   . TYR A 330 ? 0.48668 0.30673 0.31990 0.05713  -0.12076 0.04829  330 TYR A O   
2544 C  CB  . TYR A 330 ? 0.29724 0.25927 0.23400 0.08679  -0.04623 -0.03919 330 TYR A CB  
2545 C  CG  . TYR A 330 ? 0.26294 0.27183 0.19157 0.07056  -0.05499 0.00871  330 TYR A CG  
2546 C  CD1 . TYR A 330 ? 0.31732 0.25263 0.19384 0.05928  -0.01551 0.00012  330 TYR A CD1 
2547 C  CD2 . TYR A 330 ? 0.28986 0.19304 0.18962 0.05983  -0.05444 -0.00790 330 TYR A CD2 
2548 C  CE1 . TYR A 330 ? 0.27837 0.29914 0.20066 0.08791  -0.01878 0.01428  330 TYR A CE1 
2549 C  CE2 . TYR A 330 ? 0.30615 0.23519 0.18525 0.09528  -0.01606 0.03994  330 TYR A CE2 
2550 C  CZ  . TYR A 330 ? 0.29270 0.25636 0.18118 0.08797  -0.02421 0.03780  330 TYR A CZ  
2551 O  OH  . TYR A 330 ? 0.28047 0.33486 0.20093 0.11907  0.00258  0.01199  330 TYR A OH  
2552 N  N   . GLU A 331 ? 0.37257 0.37063 0.32807 0.19135  -0.11238 -0.03388 331 GLU A N   
2553 C  CA  . GLU A 331 ? 0.35726 0.33444 0.34330 0.17852  -0.11770 -0.02359 331 GLU A CA  
2554 C  C   . GLU A 331 ? 0.41729 0.32254 0.33299 0.13893  -0.11565 -0.02519 331 GLU A C   
2555 O  O   . GLU A 331 ? 0.42284 0.31565 0.34079 0.12943  -0.11283 -0.02475 331 GLU A O   
2556 C  CB  . GLU A 331 ? 0.34359 0.53798 0.40363 0.19654  -0.11313 0.03283  331 GLU A CB  
2557 C  CG  . GLU A 331 ? 0.43537 0.78952 0.43620 0.19596  -0.11780 0.05166  331 GLU A CG  
2558 C  CD  . GLU A 331 ? 0.50825 0.97021 0.47954 0.10792  -0.07574 0.01698  331 GLU A CD  
2559 O  OE1 . GLU A 331 ? 0.52683 1.02259 0.51425 0.06959  -0.11532 -0.02167 331 GLU A OE1 
2560 O  OE2 . GLU A 331 ? 0.54021 1.02458 0.48257 0.07407  -0.00216 0.04614  331 GLU A OE2 
2561 N  N   . ASP A 332 ? 0.45632 0.32683 0.33091 0.12416  -0.13502 -0.00734 332 ASP A N   
2562 C  CA  A ASP A 332 ? 0.47281 0.31706 0.31453 0.07247  -0.18198 -0.01308 332 ASP A CA  
2563 C  CA  B ASP A 332 ? 0.44661 0.31164 0.32391 0.08394  -0.14242 -0.02638 332 ASP A CA  
2564 C  C   . ASP A 332 ? 0.46300 0.27041 0.30091 0.06037  -0.14276 -0.03345 332 ASP A C   
2565 O  O   . ASP A 332 ? 0.44424 0.30985 0.28585 0.02321  -0.15969 0.01521  332 ASP A O   
2566 C  CB  A ASP A 332 ? 0.51506 0.37623 0.35250 0.05586  -0.19872 -0.01587 332 ASP A CB  
2567 C  CB  B ASP A 332 ? 0.44051 0.33038 0.35582 0.08264  -0.13211 -0.05010 332 ASP A CB  
2568 C  CG  A ASP A 332 ? 0.64285 0.39216 0.38094 0.03718  -0.22195 -0.00043 332 ASP A CG  
2569 C  CG  B ASP A 332 ? 0.50488 0.34082 0.38404 0.06107  -0.12336 -0.06246 332 ASP A CG  
2570 O  OD1 A ASP A 332 ? 0.71790 0.28951 0.40048 0.07433  -0.19600 -0.00015 332 ASP A OD1 
2571 O  OD1 B ASP A 332 ? 0.55098 0.33674 0.39066 0.07572  -0.10150 -0.04836 332 ASP A OD1 
2572 O  OD2 A ASP A 332 ? 0.69781 0.41932 0.39392 -0.01117 -0.21470 -0.02792 332 ASP A OD2 
2573 O  OD2 B ASP A 332 ? 0.54519 0.36535 0.38972 0.07273  -0.14226 -0.06953 332 ASP A OD2 
2574 N  N   . PRO A 333 ? 0.44723 0.23716 0.28366 0.10210  -0.15084 -0.01590 333 PRO A N   
2575 C  CA  . PRO A 333 ? 0.41594 0.25363 0.28028 0.09058  -0.09637 -0.01089 333 PRO A CA  
2576 C  C   . PRO A 333 ? 0.47303 0.23254 0.25193 0.06633  -0.07090 -0.00771 333 PRO A C   
2577 O  O   . PRO A 333 ? 0.49539 0.27096 0.22897 0.08636  -0.09735 0.02877  333 PRO A O   
2578 C  CB  . PRO A 333 ? 0.42626 0.22083 0.27869 0.04644  -0.11838 0.01730  333 PRO A CB  
2579 C  CG  . PRO A 333 ? 0.43751 0.27867 0.29755 0.09752  -0.14984 -0.00581 333 PRO A CG  
2580 C  CD  . PRO A 333 ? 0.47476 0.21180 0.30084 0.11413  -0.13564 -0.00795 333 PRO A CD  
2581 N  N   . ASP A 334 ? 0.47816 0.27854 0.25422 0.06980  -0.05434 0.02834  334 ASP A N   
2582 C  CA  . ASP A 334 ? 0.58111 0.26156 0.25343 0.08748  -0.08844 0.00808  334 ASP A CA  
2583 C  C   . ASP A 334 ? 0.63486 0.24950 0.22098 0.04597  -0.10532 0.01040  334 ASP A C   
2584 O  O   . ASP A 334 ? 0.71197 0.23636 0.21762 0.00686  -0.07506 -0.02307 334 ASP A O   
2585 C  CB  . ASP A 334 ? 0.60857 0.29101 0.27382 -0.00260 -0.11514 0.05407  334 ASP A CB  
2586 C  CG  . ASP A 334 ? 0.60084 0.31928 0.31057 0.04898  -0.14631 0.10209  334 ASP A CG  
2587 O  OD1 . ASP A 334 ? 0.62129 0.29454 0.30712 0.03716  -0.13401 0.09953  334 ASP A OD1 
2588 O  OD2 . ASP A 334 ? 0.71365 0.40449 0.32939 -0.02170 -0.12458 0.10549  334 ASP A OD2 
2589 N  N   . ALA A 335 ? 0.58291 0.25982 0.21884 0.08125  -0.13017 0.00319  335 ALA A N   
2590 C  CA  . ALA A 335 ? 0.53703 0.30006 0.26729 0.05652  -0.15808 -0.01093 335 ALA A CA  
2591 C  C   . ALA A 335 ? 0.49359 0.23872 0.26580 0.05012  -0.11738 0.01609  335 ALA A C   
2592 O  O   . ALA A 335 ? 0.46709 0.28027 0.25494 0.06477  -0.05905 0.02024  335 ALA A O   
2593 C  CB  . ALA A 335 ? 0.53511 0.34366 0.28644 0.09039  -0.19612 0.00162  335 ALA A CB  
2594 N  N   . LEU A 336 ? 0.42823 0.23833 0.26821 0.04919  -0.07026 0.00911  336 LEU A N   
2595 C  CA  . LEU A 336 ? 0.33666 0.24497 0.25401 0.07261  -0.05793 0.00609  336 LEU A CA  
2596 C  C   . LEU A 336 ? 0.31786 0.28462 0.24204 0.08009  -0.03316 0.02443  336 LEU A C   
2597 O  O   . LEU A 336 ? 0.33712 0.35916 0.24317 0.10577  -0.08865 0.03613  336 LEU A O   
2598 C  CB  . LEU A 336 ? 0.33098 0.25168 0.23642 0.07408  -0.06971 -0.01028 336 LEU A CB  
2599 C  CG  . LEU A 336 ? 0.30094 0.26878 0.22975 -0.00262 -0.05751 -0.01652 336 LEU A CG  
2600 C  CD1 . LEU A 336 ? 0.33759 0.30321 0.22096 -0.03822 -0.05282 -0.00519 336 LEU A CD1 
2601 C  CD2 . LEU A 336 ? 0.33995 0.30001 0.26410 0.10272  -0.03126 -0.04942 336 LEU A CD2 
2602 N  N   . ASP A 337 ? 0.31185 0.29714 0.23345 0.04774  -0.00825 0.02831  337 ASP A N   
2603 C  CA  . ASP A 337 ? 0.30222 0.34479 0.24722 0.04918  -0.02978 0.03915  337 ASP A CA  
2604 C  C   . ASP A 337 ? 0.32512 0.30942 0.24974 0.06260  -0.01944 0.03256  337 ASP A C   
2605 O  O   . ASP A 337 ? 0.31456 0.35778 0.25963 0.04457  -0.02619 0.01084  337 ASP A O   
2606 C  CB  . ASP A 337 ? 0.35103 0.35151 0.27349 0.08427  -0.05022 0.02280  337 ASP A CB  
2607 C  CG  . ASP A 337 ? 0.36846 0.35354 0.29932 0.07786  -0.02474 0.00588  337 ASP A CG  
2608 O  OD1 . ASP A 337 ? 0.33456 0.39454 0.30763 0.00386  -0.03498 0.02447  337 ASP A OD1 
2609 O  OD2 . ASP A 337 ? 0.39642 0.33108 0.33575 0.09621  -0.04370 -0.00750 337 ASP A OD2 
2610 N  N   . ILE A 338 ? 0.28835 0.25301 0.24154 0.01560  -0.02929 0.00974  338 ILE A N   
2611 C  CA  . ILE A 338 ? 0.33382 0.22104 0.28721 -0.00047 -0.00627 0.03982  338 ILE A CA  
2612 C  C   . ILE A 338 ? 0.30467 0.33285 0.31906 -0.02722 -0.00829 0.02203  338 ILE A C   
2613 O  O   . ILE A 338 ? 0.32667 0.35996 0.32829 -0.01973 0.00991  0.01650  338 ILE A O   
2614 C  CB  . ILE A 338 ? 0.36578 0.33448 0.29992 0.02209  -0.03255 0.00687  338 ILE A CB  
2615 C  CG1 . ILE A 338 ? 0.43064 0.35421 0.30531 0.04360  -0.06776 -0.01948 338 ILE A CG1 
2616 C  CG2 . ILE A 338 ? 0.37078 0.31691 0.31509 0.08349  -0.02956 -0.00578 338 ILE A CG2 
2617 C  CD1 . ILE A 338 ? 0.46376 0.43501 0.31485 0.04689  -0.04843 -0.02625 338 ILE A CD1 
2618 N  N   . HIS A 339 ? 0.29612 0.42380 0.31582 0.02746  -0.05321 0.01883  339 HIS A N   
2619 C  CA  . HIS A 339 ? 0.27295 0.42705 0.33016 -0.01810 -0.06966 0.01445  339 HIS A CA  
2620 C  C   . HIS A 339 ? 0.29985 0.45662 0.31803 -0.03469 -0.02902 -0.02322 339 HIS A C   
2621 O  O   . HIS A 339 ? 0.35323 0.51400 0.34074 -0.04678 0.01096  -0.03944 339 HIS A O   
2622 C  CB  . HIS A 339 ? 0.29700 0.44228 0.36969 -0.03088 -0.09583 -0.00853 339 HIS A CB  
2623 C  CG  . HIS A 339 ? 0.37925 0.46213 0.41261 0.02625  -0.09892 -0.01034 339 HIS A CG  
2624 N  ND1 . HIS A 339 ? 0.37583 0.48753 0.43442 0.06371  -0.09393 0.01005  339 HIS A ND1 
2625 C  CD2 . HIS A 339 ? 0.47262 0.46455 0.42879 0.03798  -0.10474 -0.00183 339 HIS A CD2 
2626 C  CE1 . HIS A 339 ? 0.43955 0.50480 0.42063 0.05841  -0.08966 0.00938  339 HIS A CE1 
2627 N  NE2 . HIS A 339 ? 0.50775 0.47955 0.43415 0.02970  -0.10759 0.02142  339 HIS A NE2 
2628 N  N   . ARG A 340 ? 0.26840 0.41958 0.29261 0.01865  -0.03784 0.00816  340 ARG A N   
2629 C  CA  . ARG A 340 ? 0.27500 0.45514 0.26938 0.04540  -0.02261 0.01448  340 ARG A CA  
2630 C  C   . ARG A 340 ? 0.28949 0.49780 0.29150 0.05101  -0.03482 0.03137  340 ARG A C   
2631 O  O   . ARG A 340 ? 0.34407 0.36126 0.34437 0.06408  -0.07256 0.04663  340 ARG A O   
2632 C  CB  . ARG A 340 ? 0.18774 0.40660 0.27376 0.09988  -0.00588 0.01363  340 ARG A CB  
2633 C  CG  . ARG A 340 ? 0.26843 0.35848 0.26988 0.06620  0.00765  0.06746  340 ARG A CG  
2634 C  CD  . ARG A 340 ? 0.32675 0.30348 0.25899 0.08465  -0.00320 0.06073  340 ARG A CD  
2635 N  NE  . ARG A 340 ? 0.40398 0.25250 0.23845 0.12799  -0.04735 0.05161  340 ARG A NE  
2636 C  CZ  . ARG A 340 ? 0.41077 0.33418 0.23098 0.11189  -0.09625 0.00027  340 ARG A CZ  
2637 N  NH1 . ARG A 340 ? 0.38351 0.35572 0.25691 0.06864  -0.10652 -0.03166 340 ARG A NH1 
2638 N  NH2 . ARG A 340 ? 0.49522 0.27375 0.23181 0.11757  -0.09028 -0.03060 340 ARG A NH2 
2639 N  N   . SER A 341 ? 0.24845 0.61927 0.26358 0.07569  -0.02317 0.02219  341 SER A N   
2640 C  CA  . SER A 341 ? 0.22499 0.64339 0.24918 0.02263  0.01197  0.00845  341 SER A CA  
2641 C  C   . SER A 341 ? 0.29136 0.59158 0.25616 0.05398  0.01408  -0.01457 341 SER A C   
2642 O  O   . SER A 341 ? 0.34065 0.56768 0.28299 0.05250  -0.02332 -0.04493 341 SER A O   
2643 C  CB  . SER A 341 ? 0.29319 0.76922 0.23109 0.06000  0.00697  0.00452  341 SER A CB  
2644 O  OG  . SER A 341 ? 0.37258 0.85330 0.28183 0.00035  0.00787  0.00559  341 SER A OG  
2645 N  N   . ALA A 342 ? 0.23012 0.41343 0.25057 0.07171  0.01926  0.02723  342 ALA A N   
2646 C  CA  . ALA A 342 ? 0.21506 0.38344 0.26512 0.07955  0.01878  0.04015  342 ALA A CA  
2647 C  C   . ALA A 342 ? 0.24189 0.38966 0.25643 0.06803  0.01987  0.04852  342 ALA A C   
2648 O  O   . ALA A 342 ? 0.20027 0.38896 0.28248 0.05814  0.01555  0.05861  342 ALA A O   
2649 C  CB  . ALA A 342 ? 0.23441 0.31828 0.29351 0.03573  0.05690  0.00894  342 ALA A CB  
2650 N  N   . ARG A 343 ? 0.27721 0.43088 0.23061 0.05645  -0.00949 0.05177  343 ARG A N   
2651 C  CA  . ARG A 343 ? 0.22864 0.41694 0.23497 -0.01643 -0.01600 0.03061  343 ARG A CA  
2652 C  C   . ARG A 343 ? 0.22062 0.36114 0.22303 0.06069  0.01179  0.05941  343 ARG A C   
2653 O  O   . ARG A 343 ? 0.27382 0.39929 0.23147 0.11804  0.01770  0.08926  343 ARG A O   
2654 C  CB  . ARG A 343 ? 0.25914 0.54699 0.28362 -0.07011 0.01013  0.06943  343 ARG A CB  
2655 C  CG  . ARG A 343 ? 0.36109 0.65104 0.31187 -0.06423 0.02517  0.03509  343 ARG A CG  
2656 C  CD  . ARG A 343 ? 0.38864 0.63974 0.32369 -0.02496 0.01232  0.04789  343 ARG A CD  
2657 N  NE  . ARG A 343 ? 0.32329 0.60568 0.32668 -0.04808 -0.00682 0.03115  343 ARG A NE  
2658 C  CZ  . ARG A 343 ? 0.34059 0.53497 0.32535 -0.03862 -0.01116 0.03783  343 ARG A CZ  
2659 N  NH1 . ARG A 343 ? 0.37042 0.50543 0.34484 0.00501  0.00184  0.01123  343 ARG A NH1 
2660 N  NH2 . ARG A 343 ? 0.31286 0.55976 0.30778 0.00261  -0.05372 -0.00162 343 ARG A NH2 
2661 N  N   . HIS A 344 ? 0.21458 0.36554 0.21828 0.07734  0.03737  0.03336  344 HIS A N   
2662 C  CA  . HIS A 344 ? 0.24305 0.29677 0.22788 0.03617  0.01178  0.01369  344 HIS A CA  
2663 C  C   . HIS A 344 ? 0.29903 0.29920 0.19104 0.05222  0.00760  0.01455  344 HIS A C   
2664 O  O   . HIS A 344 ? 0.27985 0.29852 0.20215 0.08362  0.00989  0.01765  344 HIS A O   
2665 C  CB  . HIS A 344 ? 0.32818 0.35407 0.22991 0.10400  0.06152  0.01594  344 HIS A CB  
2666 C  CG  . HIS A 344 ? 0.37775 0.38753 0.26084 0.17036  0.11267  0.06778  344 HIS A CG  
2667 N  ND1 . HIS A 344 ? 0.38824 0.48852 0.29957 0.14006  0.15419  0.07254  344 HIS A ND1 
2668 C  CD2 . HIS A 344 ? 0.36795 0.46128 0.28104 0.15335  0.15097  0.06041  344 HIS A CD2 
2669 C  CE1 . HIS A 344 ? 0.38238 0.52454 0.31414 0.17149  0.14173  0.11435  344 HIS A CE1 
2670 N  NE2 . HIS A 344 ? 0.42451 0.49323 0.30999 0.13905  0.13669  0.08390  344 HIS A NE2 
2671 N  N   . HIS A 345 ? 0.22366 0.27440 0.19537 0.03903  0.00606  -0.00980 345 HIS A N   
2672 C  CA  . HIS A 345 ? 0.23190 0.25719 0.18031 0.03469  -0.00082 -0.02972 345 HIS A CA  
2673 C  C   . HIS A 345 ? 0.18000 0.22565 0.21060 0.06014  -0.00847 0.01612  345 HIS A C   
2674 O  O   . HIS A 345 ? 0.22728 0.23240 0.21171 0.01093  -0.00193 0.02041  345 HIS A O   
2675 C  CB  . HIS A 345 ? 0.26057 0.19839 0.18207 0.06213  0.01722  -0.06087 345 HIS A CB  
2676 C  CG  . HIS A 345 ? 0.21698 0.20743 0.20373 0.07154  0.00789  -0.01755 345 HIS A CG  
2677 N  ND1 . HIS A 345 ? 0.20002 0.23200 0.20896 0.05498  -0.02223 -0.03107 345 HIS A ND1 
2678 C  CD2 . HIS A 345 ? 0.27405 0.21407 0.21276 0.03928  0.00442  0.00427  345 HIS A CD2 
2679 C  CE1 . HIS A 345 ? 0.24377 0.21405 0.22410 -0.02362 -0.01807 -0.01025 345 HIS A CE1 
2680 N  NE2 . HIS A 345 ? 0.25686 0.27570 0.22533 -0.01559 -0.00521 -0.02800 345 HIS A NE2 
2681 N  N   . LEU A 346 ? 0.20918 0.20941 0.21092 -0.00201 0.00559  0.00353  346 LEU A N   
2682 C  CA  . LEU A 346 ? 0.22519 0.15455 0.19536 0.00086  -0.00429 -0.02991 346 LEU A CA  
2683 C  C   . LEU A 346 ? 0.24693 0.18228 0.19599 0.01332  0.01325  0.00199  346 LEU A C   
2684 O  O   . LEU A 346 ? 0.24829 0.21956 0.19691 0.01280  -0.00505 -0.00804 346 LEU A O   
2685 C  CB  . LEU A 346 ? 0.20977 0.16754 0.20799 -0.01010 0.03064  -0.03431 346 LEU A CB  
2686 C  CG  . LEU A 346 ? 0.30258 0.16927 0.18761 0.08297  -0.02637 -0.04547 346 LEU A CG  
2687 C  CD1 . LEU A 346 ? 0.32124 0.22869 0.21710 0.07754  0.03104  -0.02629 346 LEU A CD1 
2688 C  CD2 . LEU A 346 ? 0.31326 0.28940 0.19415 0.04014  -0.05248 -0.02396 346 LEU A CD2 
2689 N  N   . ALA A 347 ? 0.24481 0.20525 0.17590 0.01584  0.01840  0.01589  347 ALA A N   
2690 C  CA  . ALA A 347 ? 0.23738 0.21895 0.18719 0.01961  -0.00993 -0.00701 347 ALA A CA  
2691 C  C   . ALA A 347 ? 0.20899 0.19534 0.21948 0.01249  -0.03059 0.04582  347 ALA A C   
2692 O  O   . ALA A 347 ? 0.19732 0.22032 0.22956 0.02780  -0.02658 0.02818  347 ALA A O   
2693 C  CB  . ALA A 347 ? 0.25424 0.29026 0.17191 -0.02525 -0.05487 -0.05722 347 ALA A CB  
2694 N  N   . PHE A 348 ? 0.24825 0.19280 0.20491 -0.01096 -0.04014 0.03452  348 PHE A N   
2695 C  CA  . PHE A 348 ? 0.18223 0.18544 0.20868 0.02096  -0.00546 -0.02173 348 PHE A CA  
2696 C  C   . PHE A 348 ? 0.17498 0.23116 0.22566 0.04178  0.00710  -0.01105 348 PHE A C   
2697 O  O   . PHE A 348 ? 0.24129 0.20687 0.21578 -0.01064 -0.00604 -0.00630 348 PHE A O   
2698 C  CB  . PHE A 348 ? 0.20690 0.16865 0.20084 -0.02656 0.00037  -0.02918 348 PHE A CB  
2699 C  CG  . PHE A 348 ? 0.23698 0.19976 0.19628 0.01432  0.00042  -0.02132 348 PHE A CG  
2700 C  CD1 . PHE A 348 ? 0.24109 0.18054 0.18902 0.00294  0.01090  -0.01536 348 PHE A CD1 
2701 C  CD2 . PHE A 348 ? 0.25487 0.24325 0.19509 0.00402  -0.04184 0.01283  348 PHE A CD2 
2702 C  CE1 . PHE A 348 ? 0.20160 0.25305 0.19656 -0.04724 0.01357  0.00313  348 PHE A CE1 
2703 C  CE2 . PHE A 348 ? 0.23311 0.29993 0.18642 -0.03880 -0.00026 -0.00921 348 PHE A CE2 
2704 C  CZ  . PHE A 348 ? 0.20567 0.26492 0.18084 -0.02626 -0.00523 0.00870  348 PHE A CZ  
2705 N  N   . GLY A 349 ? 0.23069 0.24130 0.20524 0.01679  0.02960  -0.03959 349 GLY A N   
2706 C  CA  . GLY A 349 ? 0.31350 0.23616 0.17308 0.03815  -0.02101 -0.04374 349 GLY A CA  
2707 C  C   . GLY A 349 ? 0.29746 0.21376 0.19127 0.04674  -0.01026 -0.02957 349 GLY A C   
2708 O  O   . GLY A 349 ? 0.23868 0.25582 0.19902 0.01106  -0.00817 -0.02745 349 GLY A O   
2709 N  N   . PHE A 350 ? 0.25630 0.19677 0.17097 -0.00592 0.01927  -0.02261 350 PHE A N   
2710 C  CA  . PHE A 350 ? 0.28874 0.23626 0.18347 0.02272  -0.00149 0.00687  350 PHE A CA  
2711 C  C   . PHE A 350 ? 0.23714 0.22557 0.19701 0.01716  0.00508  0.00195  350 PHE A C   
2712 O  O   . PHE A 350 ? 0.27903 0.25128 0.21554 0.03789  -0.01864 -0.01073 350 PHE A O   
2713 C  CB  . PHE A 350 ? 0.35824 0.26409 0.20796 0.07360  -0.01966 -0.01958 350 PHE A CB  
2714 C  CG  . PHE A 350 ? 0.31143 0.21763 0.23175 0.04309  0.01681  -0.04214 350 PHE A CG  
2715 C  CD1 . PHE A 350 ? 0.25671 0.25742 0.24064 -0.00907 0.01064  -0.04693 350 PHE A CD1 
2716 C  CD2 . PHE A 350 ? 0.29441 0.21602 0.22125 0.05670  0.00677  -0.04639 350 PHE A CD2 
2717 C  CE1 . PHE A 350 ? 0.26876 0.28716 0.24779 0.08787  0.00020  -0.07393 350 PHE A CE1 
2718 C  CE2 . PHE A 350 ? 0.27540 0.26121 0.23593 -0.00951 0.01228  -0.07872 350 PHE A CE2 
2719 C  CZ  . PHE A 350 ? 0.29563 0.26118 0.25413 0.01463  -0.02778 -0.06264 350 PHE A CZ  
2720 N  N   . GLY A 351 ? 0.25509 0.23469 0.20368 0.05398  -0.02491 -0.00683 351 GLY A N   
2721 C  CA  . GLY A 351 ? 0.21223 0.29008 0.20255 0.07309  -0.06953 -0.00016 351 GLY A CA  
2722 C  C   . GLY A 351 ? 0.24567 0.31983 0.20774 0.04149  -0.04708 -0.01256 351 GLY A C   
2723 O  O   . GLY A 351 ? 0.29555 0.29380 0.20150 0.03709  -0.01436 -0.04168 351 GLY A O   
2724 N  N   . VAL A 352 ? 0.29527 0.31363 0.19334 0.07034  -0.06237 -0.03431 352 VAL A N   
2725 C  CA  . VAL A 352 ? 0.32017 0.30991 0.20775 0.10006  -0.05040 -0.01832 352 VAL A CA  
2726 C  C   . VAL A 352 ? 0.33707 0.29969 0.19961 0.05719  -0.05992 -0.03691 352 VAL A C   
2727 O  O   . VAL A 352 ? 0.32481 0.30668 0.20522 0.04905  -0.03951 0.00315  352 VAL A O   
2728 C  CB  . VAL A 352 ? 0.39600 0.31208 0.21804 0.00665  -0.03477 -0.06096 352 VAL A CB  
2729 C  CG1 . VAL A 352 ? 0.39958 0.34172 0.21546 0.09540  -0.03186 -0.07478 352 VAL A CG1 
2730 C  CG2 . VAL A 352 ? 0.36028 0.33232 0.26713 -0.07903 -0.01465 -0.04972 352 VAL A CG2 
2731 N  N   . HIS A 353 ? 0.24928 0.28530 0.20677 0.07128  -0.02032 -0.04070 353 HIS A N   
2732 C  CA  . HIS A 353 ? 0.23509 0.26153 0.22819 0.01943  -0.02343 -0.03708 353 HIS A CA  
2733 C  C   . HIS A 353 ? 0.21800 0.28885 0.22744 0.03525  0.00005  -0.03237 353 HIS A C   
2734 O  O   . HIS A 353 ? 0.21466 0.26660 0.24389 0.02759  -0.02408 -0.02239 353 HIS A O   
2735 C  CB  . HIS A 353 ? 0.18734 0.25140 0.21023 0.00318  -0.02088 0.03106  353 HIS A CB  
2736 C  CG  . HIS A 353 ? 0.17060 0.27193 0.22563 0.02003  -0.07964 -0.01400 353 HIS A CG  
2737 N  ND1 . HIS A 353 ? 0.23139 0.28653 0.22777 0.02128  -0.06318 -0.02811 353 HIS A ND1 
2738 C  CD2 . HIS A 353 ? 0.21456 0.26216 0.23095 -0.00962 -0.05455 -0.02751 353 HIS A CD2 
2739 C  CE1 . HIS A 353 ? 0.27193 0.22378 0.23889 0.00169  -0.05628 -0.03967 353 HIS A CE1 
2740 N  NE2 . HIS A 353 ? 0.21881 0.23248 0.25223 0.01699  -0.03286 -0.01790 353 HIS A NE2 
2741 N  N   . GLN A 354 ? 0.16608 0.26371 0.19785 0.05054  -0.01218 0.00980  354 GLN A N   
2742 C  CA  A GLN A 354 ? 0.19238 0.24822 0.20296 0.01981  -0.04747 0.01238  354 GLN A CA  
2743 C  CA  B GLN A 354 ? 0.18640 0.23389 0.21074 0.03759  -0.03241 0.00954  354 GLN A CA  
2744 C  C   . GLN A 354 ? 0.20842 0.20328 0.20359 0.04261  -0.04020 0.00489  354 GLN A C   
2745 O  O   . GLN A 354 ? 0.23063 0.20710 0.21492 0.03981  -0.03274 0.00072  354 GLN A O   
2746 C  CB  A GLN A 354 ? 0.23932 0.26285 0.19916 0.02186  -0.06275 0.02762  354 GLN A CB  
2747 C  CB  B GLN A 354 ? 0.20557 0.22635 0.22436 0.05431  -0.03704 0.01320  354 GLN A CB  
2748 C  CG  A GLN A 354 ? 0.17141 0.30084 0.20776 0.03726  -0.07006 0.02516  354 GLN A CG  
2749 C  CG  B GLN A 354 ? 0.17872 0.22502 0.23366 0.07415  -0.04666 0.02333  354 GLN A CG  
2750 C  CD  A GLN A 354 ? 0.21504 0.29996 0.23731 0.02966  -0.01826 0.01960  354 GLN A CD  
2751 C  CD  B GLN A 354 ? 0.22259 0.24340 0.23743 0.04257  -0.02569 0.05380  354 GLN A CD  
2752 O  OE1 A GLN A 354 ? 0.18436 0.31099 0.25698 0.02690  0.02484  -0.00221 354 GLN A OE1 
2753 O  OE1 B GLN A 354 ? 0.27032 0.26598 0.22149 0.01779  -0.03703 0.12901  354 GLN A OE1 
2754 N  NE2 A GLN A 354 ? 0.29308 0.22942 0.23531 0.02854  -0.03659 0.01056  354 GLN A NE2 
2755 N  NE2 B GLN A 354 ? 0.20276 0.25029 0.24764 0.04465  -0.02590 0.03120  354 GLN A NE2 
2756 N  N   . CYS A 355 ? 0.16021 0.19751 0.18038 0.03825  0.01106  -0.03554 355 CYS A N   
2757 C  CA  . CYS A 355 ? 0.22165 0.18185 0.19107 0.03121  0.01146  0.00387  355 CYS A CA  
2758 C  C   . CYS A 355 ? 0.19782 0.21386 0.17776 0.00388  0.01648  0.03342  355 CYS A C   
2759 O  O   . CYS A 355 ? 0.20199 0.27046 0.18886 -0.01049 0.02291  0.01150  355 CYS A O   
2760 C  CB  . CYS A 355 ? 0.22694 0.24683 0.17709 0.05499  -0.02230 -0.00745 355 CYS A CB  
2761 S  SG  . CYS A 355 ? 0.27023 0.21597 0.19140 0.01568  0.01057  0.01234  355 CYS A SG  
2762 N  N   . LEU A 356 ? 0.23958 0.20444 0.20428 0.05844  -0.04363 0.00505  356 LEU A N   
2763 C  CA  . LEU A 356 ? 0.31566 0.22195 0.23633 -0.00064 -0.08357 -0.00643 356 LEU A CA  
2764 C  C   . LEU A 356 ? 0.22232 0.19354 0.19940 0.00273  -0.03388 0.02047  356 LEU A C   
2765 O  O   . LEU A 356 ? 0.24472 0.21573 0.20357 0.00239  -0.02953 0.01461  356 LEU A O   
2766 C  CB  . LEU A 356 ? 0.36273 0.18429 0.26325 -0.00949 -0.13972 0.02792  356 LEU A CB  
2767 C  CG  . LEU A 356 ? 0.44976 0.24850 0.29459 0.05408  -0.15439 0.04573  356 LEU A CG  
2768 C  CD1 . LEU A 356 ? 0.57063 0.30561 0.28291 -0.02063 -0.10511 0.07236  356 LEU A CD1 
2769 C  CD2 . LEU A 356 ? 0.49242 0.22500 0.36390 0.02625  -0.16740 0.03519  356 LEU A CD2 
2770 N  N   . GLY A 357 ? 0.18586 0.21608 0.17336 -0.00754 -0.03069 -0.03352 357 GLY A N   
2771 C  CA  . GLY A 357 ? 0.19636 0.21756 0.21675 0.00101  -0.03994 -0.04867 357 GLY A CA  
2772 C  C   . GLY A 357 ? 0.18197 0.22122 0.20308 0.01626  -0.03197 0.01239  357 GLY A C   
2773 O  O   . GLY A 357 ? 0.21125 0.22902 0.22543 -0.02050 -0.02596 -0.05005 357 GLY A O   
2774 N  N   . GLN A 358 ? 0.17763 0.24975 0.20783 0.05255  0.00129  -0.00777 358 GLN A N   
2775 C  CA  . GLN A 358 ? 0.18207 0.24046 0.22870 -0.01337 -0.00767 0.01663  358 GLN A CA  
2776 C  C   . GLN A 358 ? 0.26367 0.25059 0.24021 0.02581  0.01537  0.00389  358 GLN A C   
2777 O  O   . GLN A 358 ? 0.29303 0.25736 0.23290 0.03939  0.02328  -0.01192 358 GLN A O   
2778 C  CB  . GLN A 358 ? 0.27075 0.23442 0.20958 0.02908  0.05217  0.01593  358 GLN A CB  
2779 C  CG  . GLN A 358 ? 0.20077 0.21884 0.21268 0.02210  0.05876  -0.03805 358 GLN A CG  
2780 C  CD  . GLN A 358 ? 0.25007 0.27486 0.25488 0.00843  0.02870  -0.02035 358 GLN A CD  
2781 O  OE1 . GLN A 358 ? 0.30546 0.30624 0.28962 0.00082  0.01569  -0.02737 358 GLN A OE1 
2782 N  NE2 . GLN A 358 ? 0.28612 0.33366 0.27608 -0.00733 0.05456  -0.02576 358 GLN A NE2 
2783 N  N   . ASN A 359 ? 0.24990 0.22143 0.25966 0.01419  0.03975  -0.05912 359 ASN A N   
2784 C  CA  . ASN A 359 ? 0.28718 0.23579 0.23750 -0.00524 0.05570  -0.03129 359 ASN A CA  
2785 C  C   . ASN A 359 ? 0.24689 0.21564 0.23270 -0.03105 0.04010  -0.06052 359 ASN A C   
2786 O  O   . ASN A 359 ? 0.23187 0.25517 0.23912 -0.03326 0.00553  -0.07221 359 ASN A O   
2787 C  CB  . ASN A 359 ? 0.28625 0.32835 0.23618 0.05697  0.05980  -0.00179 359 ASN A CB  
2788 C  CG  . ASN A 359 ? 0.26235 0.23893 0.22243 0.07593  0.04506  0.05876  359 ASN A CG  
2789 O  OD1 . ASN A 359 ? 0.30212 0.29721 0.22853 0.03794  0.00419  0.06234  359 ASN A OD1 
2790 N  ND2 . ASN A 359 ? 0.30127 0.37350 0.20852 0.01409  0.05202  0.03995  359 ASN A ND2 
2791 N  N   . LEU A 360 ? 0.20051 0.22957 0.21691 -0.02504 0.02406  -0.03719 360 LEU A N   
2792 C  CA  . LEU A 360 ? 0.23891 0.21885 0.20017 0.01257  0.02997  -0.00182 360 LEU A CA  
2793 C  C   . LEU A 360 ? 0.26900 0.18416 0.20878 0.01156  -0.00192 -0.00106 360 LEU A C   
2794 O  O   . LEU A 360 ? 0.23744 0.21600 0.25118 -0.00132 -0.00782 -0.02208 360 LEU A O   
2795 C  CB  . LEU A 360 ? 0.23681 0.20313 0.22369 0.02126  0.02275  -0.03635 360 LEU A CB  
2796 C  CG  . LEU A 360 ? 0.22305 0.18131 0.23076 0.02177  -0.00276 -0.04197 360 LEU A CG  
2797 C  CD1 . LEU A 360 ? 0.27651 0.17412 0.23116 0.01038  -0.00012 0.02413  360 LEU A CD1 
2798 C  CD2 . LEU A 360 ? 0.25900 0.35592 0.20823 0.08771  -0.02981 -0.01618 360 LEU A CD2 
2799 N  N   . ALA A 361 ? 0.20803 0.20507 0.21891 -0.01500 0.02750  0.02337  361 ALA A N   
2800 C  CA  . ALA A 361 ? 0.21510 0.21449 0.22543 -0.05785 -0.01109 0.03380  361 ALA A CA  
2801 C  C   . ALA A 361 ? 0.22357 0.28935 0.21875 -0.01973 -0.02952 0.01457  361 ALA A C   
2802 O  O   . ALA A 361 ? 0.21486 0.25169 0.20613 0.00681  -0.01921 0.02631  361 ALA A O   
2803 C  CB  . ALA A 361 ? 0.25928 0.19674 0.24556 -0.04015 0.01702  0.04169  361 ALA A CB  
2804 N  N   . ARG A 362 ? 0.23173 0.28569 0.22185 -0.02533 -0.02477 -0.01606 362 ARG A N   
2805 C  CA  . ARG A 362 ? 0.19862 0.26124 0.21878 -0.00095 -0.02747 -0.04412 362 ARG A CA  
2806 C  C   . ARG A 362 ? 0.20504 0.25247 0.23130 -0.04271 -0.04731 -0.02322 362 ARG A C   
2807 O  O   . ARG A 362 ? 0.23979 0.25812 0.25428 -0.02257 -0.04899 -0.02633 362 ARG A O   
2808 C  CB  . ARG A 362 ? 0.22334 0.23891 0.20602 -0.00324 0.02322  -0.02894 362 ARG A CB  
2809 C  CG  . ARG A 362 ? 0.20538 0.22630 0.19171 0.03488  -0.00200 -0.03541 362 ARG A CG  
2810 C  CD  . ARG A 362 ? 0.27037 0.24141 0.20101 0.05215  0.03719  -0.02273 362 ARG A CD  
2811 N  NE  . ARG A 362 ? 0.33819 0.23347 0.23612 0.00500  0.01983  -0.03735 362 ARG A NE  
2812 C  CZ  . ARG A 362 ? 0.30612 0.22658 0.20458 0.02758  -0.01083 0.02935  362 ARG A CZ  
2813 N  NH1 . ARG A 362 ? 0.42686 0.29527 0.21005 0.06628  -0.06910 -0.02890 362 ARG A NH1 
2814 N  NH2 . ARG A 362 ? 0.33733 0.23492 0.24078 0.05925  -0.01599 -0.01296 362 ARG A NH2 
2815 N  N   . LEU A 363 ? 0.25846 0.23053 0.24227 0.04330  0.01101  0.00194  363 LEU A N   
2816 C  CA  . LEU A 363 ? 0.27831 0.23020 0.23449 -0.00448 -0.00076 -0.01114 363 LEU A CA  
2817 C  C   . LEU A 363 ? 0.24010 0.22927 0.21910 -0.02234 -0.01685 -0.03611 363 LEU A C   
2818 O  O   . LEU A 363 ? 0.28677 0.22870 0.21964 -0.01373 -0.04708 -0.01291 363 LEU A O   
2819 C  CB  . LEU A 363 ? 0.28111 0.20284 0.24464 0.04848  -0.02152 0.00907  363 LEU A CB  
2820 C  CG  . LEU A 363 ? 0.30975 0.27983 0.28538 -0.01386 -0.07659 0.04589  363 LEU A CG  
2821 C  CD1 . LEU A 363 ? 0.32523 0.37353 0.29535 -0.10071 -0.08707 0.07629  363 LEU A CD1 
2822 C  CD2 . LEU A 363 ? 0.27156 0.27617 0.28498 -0.04781 -0.06819 0.03611  363 LEU A CD2 
2823 N  N   . GLU A 364 ? 0.21444 0.20686 0.22773 0.01123  0.00774  0.03362  364 GLU A N   
2824 C  CA  . GLU A 364 ? 0.21302 0.20605 0.22409 -0.03954 0.03988  0.00511  364 GLU A CA  
2825 C  C   . GLU A 364 ? 0.28624 0.16807 0.24985 0.03527  -0.03462 -0.00131 364 GLU A C   
2826 O  O   . GLU A 364 ? 0.26667 0.16604 0.24688 -0.00868 -0.01762 -0.00652 364 GLU A O   
2827 C  CB  . GLU A 364 ? 0.20571 0.19985 0.22722 0.00033  0.01887  0.03875  364 GLU A CB  
2828 C  CG  . GLU A 364 ? 0.16086 0.27301 0.24831 0.01204  -0.03072 0.06083  364 GLU A CG  
2829 C  CD  . GLU A 364 ? 0.28759 0.26197 0.28877 0.11554  -0.00314 0.06119  364 GLU A CD  
2830 O  OE1 . GLU A 364 ? 0.35018 0.34044 0.31521 0.09287  -0.03255 0.04373  364 GLU A OE1 
2831 O  OE2 . GLU A 364 ? 0.38031 0.25299 0.28786 0.14020  0.01146  0.00183  364 GLU A OE2 
2832 N  N   . LEU A 365 ? 0.18094 0.16102 0.24679 0.00895  -0.01018 0.03653  365 LEU A N   
2833 C  CA  . LEU A 365 ? 0.16207 0.17631 0.24921 0.02423  -0.02188 0.01752  365 LEU A CA  
2834 C  C   . LEU A 365 ? 0.21075 0.22296 0.23700 -0.00436 0.01825  0.03320  365 LEU A C   
2835 O  O   . LEU A 365 ? 0.28297 0.23790 0.24129 0.01860  -0.00410 -0.00637 365 LEU A O   
2836 C  CB  . LEU A 365 ? 0.19459 0.20436 0.26883 -0.04073 0.01088  0.01415  365 LEU A CB  
2837 C  CG  . LEU A 365 ? 0.28593 0.26357 0.27967 -0.05340 0.02114  -0.01068 365 LEU A CG  
2838 C  CD1 . LEU A 365 ? 0.37565 0.31439 0.29359 -0.00484 0.04532  -0.02964 365 LEU A CD1 
2839 C  CD2 . LEU A 365 ? 0.36264 0.31382 0.28404 -0.00263 0.09768  -0.00071 365 LEU A CD2 
2840 N  N   . GLU A 366 ? 0.25587 0.19726 0.26048 -0.00680 0.00090  -0.00658 366 GLU A N   
2841 C  CA  . GLU A 366 ? 0.30033 0.20214 0.25389 -0.00732 -0.05761 -0.03032 366 GLU A CA  
2842 C  C   . GLU A 366 ? 0.29886 0.19144 0.26457 -0.02067 -0.07358 -0.01853 366 GLU A C   
2843 O  O   . GLU A 366 ? 0.30138 0.22404 0.27870 -0.06055 -0.04326 -0.01880 366 GLU A O   
2844 C  CB  . GLU A 366 ? 0.23606 0.29583 0.26497 -0.04864 -0.04446 -0.01158 366 GLU A CB  
2845 C  CG  . GLU A 366 ? 0.32574 0.38362 0.29217 -0.03999 -0.07473 -0.00885 366 GLU A CG  
2846 C  CD  . GLU A 366 ? 0.42729 0.49238 0.32828 -0.04918 -0.13031 -0.03449 366 GLU A CD  
2847 O  OE1 . GLU A 366 ? 0.45217 0.54752 0.34414 0.00840  -0.13207 -0.01192 366 GLU A OE1 
2848 O  OE2 . GLU A 366 ? 0.47757 0.52226 0.34632 -0.10605 -0.11180 0.00830  366 GLU A OE2 
2849 N  N   . VAL A 367 ? 0.29150 0.19799 0.27510 -0.00533 -0.08130 -0.00571 367 VAL A N   
2850 C  CA  . VAL A 367 ? 0.31101 0.17046 0.25291 -0.00243 -0.04479 0.00722  367 VAL A CA  
2851 C  C   . VAL A 367 ? 0.31744 0.19826 0.23945 0.00468  -0.04339 -0.01410 367 VAL A C   
2852 O  O   . VAL A 367 ? 0.35521 0.22301 0.25018 -0.03015 -0.10451 -0.00562 367 VAL A O   
2853 C  CB  . VAL A 367 ? 0.31908 0.20160 0.23305 0.01725  -0.02541 -0.02144 367 VAL A CB  
2854 C  CG1 . VAL A 367 ? 0.29876 0.20812 0.27839 -0.01209 -0.00747 -0.04428 367 VAL A CG1 
2855 C  CG2 . VAL A 367 ? 0.35657 0.25094 0.20539 0.00529  -0.02099 0.01782  367 VAL A CG2 
2856 N  N   . ILE A 368 ? 0.29743 0.19403 0.22767 -0.01413 0.00097  -0.00113 368 ILE A N   
2857 C  CA  . ILE A 368 ? 0.29238 0.23279 0.20845 0.00993  -0.02077 0.01899  368 ILE A CA  
2858 C  C   . ILE A 368 ? 0.35646 0.20929 0.21577 0.01206  -0.05427 -0.03006 368 ILE A C   
2859 O  O   . ILE A 368 ? 0.36965 0.22364 0.23373 0.01375  -0.08521 -0.03532 368 ILE A O   
2860 C  CB  . ILE A 368 ? 0.24863 0.25439 0.21347 -0.03134 0.00487  0.02988  368 ILE A CB  
2861 C  CG1 . ILE A 368 ? 0.26926 0.22819 0.25907 0.03916  -0.03038 -0.03073 368 ILE A CG1 
2862 C  CG2 . ILE A 368 ? 0.30722 0.22712 0.19402 0.02342  0.02607  0.03134  368 ILE A CG2 
2863 C  CD1 . ILE A 368 ? 0.25700 0.26298 0.29964 0.01438  -0.02735 -0.00379 368 ILE A CD1 
2864 N  N   . LEU A 369 ? 0.32244 0.21342 0.21158 -0.00224 -0.05010 0.00190  369 LEU A N   
2865 C  CA  . LEU A 369 ? 0.29744 0.19974 0.23045 -0.02782 -0.06297 -0.01690 369 LEU A CA  
2866 C  C   . LEU A 369 ? 0.31968 0.23808 0.23014 -0.00865 -0.04540 0.00790  369 LEU A C   
2867 O  O   . LEU A 369 ? 0.35800 0.25626 0.23163 0.04666  -0.05365 -0.02267 369 LEU A O   
2868 C  CB  . LEU A 369 ? 0.27564 0.21607 0.24365 0.00978  -0.04404 -0.03655 369 LEU A CB  
2869 C  CG  . LEU A 369 ? 0.31192 0.24528 0.24212 -0.00160 -0.01715 -0.01605 369 LEU A CG  
2870 C  CD1 . LEU A 369 ? 0.35487 0.28115 0.25739 0.00855  -0.02548 -0.03660 369 LEU A CD1 
2871 C  CD2 . LEU A 369 ? 0.36045 0.28577 0.24355 -0.01668 -0.01348 0.02116  369 LEU A CD2 
2872 N  N   . ASN A 370 ? 0.34013 0.23085 0.24345 0.00653  -0.05530 0.01008  370 ASN A N   
2873 C  CA  . ASN A 370 ? 0.32471 0.21472 0.24529 -0.05262 -0.01423 -0.01895 370 ASN A CA  
2874 C  C   . ASN A 370 ? 0.36164 0.23874 0.25760 0.00669  -0.05931 -0.05322 370 ASN A C   
2875 O  O   . ASN A 370 ? 0.38948 0.26438 0.26913 -0.00049 -0.08572 -0.06540 370 ASN A O   
2876 C  CB  . ASN A 370 ? 0.31872 0.26918 0.26012 -0.03837 -0.03691 0.00739  370 ASN A CB  
2877 C  CG  . ASN A 370 ? 0.33073 0.26174 0.26834 0.02762  -0.06404 0.01815  370 ASN A CG  
2878 O  OD1 . ASN A 370 ? 0.36117 0.29750 0.30091 0.02093  -0.08093 -0.00710 370 ASN A OD1 
2879 N  ND2 . ASN A 370 ? 0.35916 0.26894 0.26759 -0.06827 -0.01639 -0.00919 370 ASN A ND2 
2880 N  N   . ALA A 371 ? 0.34925 0.26773 0.26363 0.04445  -0.07814 -0.03531 371 ALA A N   
2881 C  CA  . ALA A 371 ? 0.37262 0.26469 0.25652 0.02916  -0.10372 -0.01651 371 ALA A CA  
2882 C  C   . ALA A 371 ? 0.36258 0.22642 0.27339 0.02560  -0.06730 -0.05096 371 ALA A C   
2883 O  O   . ALA A 371 ? 0.33456 0.25836 0.29742 0.02560  -0.06957 -0.08751 371 ALA A O   
2884 C  CB  . ALA A 371 ? 0.44220 0.28213 0.25800 0.00663  -0.14444 -0.01074 371 ALA A CB  
2885 N  N   . LEU A 372 ? 0.36114 0.25667 0.24935 0.02322  -0.06227 -0.05307 372 LEU A N   
2886 C  CA  . LEU A 372 ? 0.36641 0.25835 0.24735 0.00832  -0.06044 -0.01506 372 LEU A CA  
2887 C  C   . LEU A 372 ? 0.38959 0.31098 0.25701 0.03486  -0.02828 -0.04260 372 LEU A C   
2888 O  O   . LEU A 372 ? 0.37519 0.30228 0.24371 0.06038  -0.07797 -0.06547 372 LEU A O   
2889 C  CB  . LEU A 372 ? 0.34853 0.27735 0.25036 -0.06453 -0.05297 -0.03115 372 LEU A CB  
2890 C  CG  . LEU A 372 ? 0.32014 0.34078 0.22522 -0.02765 -0.03617 -0.07120 372 LEU A CG  
2891 C  CD1 . LEU A 372 ? 0.32393 0.35712 0.23449 -0.03298 -0.04368 -0.01900 372 LEU A CD1 
2892 C  CD2 . LEU A 372 ? 0.35305 0.38281 0.22527 0.03682  0.01538  -0.09753 372 LEU A CD2 
2893 N  N   . MET A 373 ? 0.41543 0.26093 0.27454 -0.01607 -0.03431 -0.06103 373 MET A N   
2894 C  CA  . MET A 373 ? 0.37220 0.31747 0.27172 0.03042  -0.08502 -0.08159 373 MET A CA  
2895 C  C   . MET A 373 ? 0.43387 0.34027 0.26669 0.00192  -0.11354 -0.06417 373 MET A C   
2896 O  O   . MET A 373 ? 0.43449 0.43536 0.26610 -0.02488 -0.10300 -0.07534 373 MET A O   
2897 C  CB  . MET A 373 ? 0.36555 0.26636 0.28484 0.00369  -0.08741 -0.07665 373 MET A CB  
2898 C  CG  . MET A 373 ? 0.35734 0.32394 0.29551 0.00196  -0.05756 -0.06080 373 MET A CG  
2899 S  SD  . MET A 373 ? 0.35359 0.32803 0.28969 0.02043  -0.05427 -0.02166 373 MET A SD  
2900 C  CE  . MET A 373 ? 0.29496 0.38172 0.26283 0.00256  -0.06942 -0.06330 373 MET A CE  
2901 N  N   . ASP A 374 ? 0.45809 0.32011 0.30550 0.04158  -0.08852 -0.04812 374 ASP A N   
2902 C  CA  . ASP A 374 ? 0.48425 0.30838 0.32762 -0.01416 -0.10858 -0.10981 374 ASP A CA  
2903 C  C   . ASP A 374 ? 0.50408 0.28270 0.33570 -0.05354 -0.12466 -0.11975 374 ASP A C   
2904 O  O   . ASP A 374 ? 0.58853 0.31625 0.39312 -0.09395 -0.11554 -0.13799 374 ASP A O   
2905 C  CB  . ASP A 374 ? 0.50173 0.22455 0.34214 -0.03345 -0.09421 -0.04364 374 ASP A CB  
2906 C  CG  . ASP A 374 ? 0.58663 0.31290 0.35892 -0.10529 -0.09581 -0.03033 374 ASP A CG  
2907 O  OD1 . ASP A 374 ? 0.63859 0.31169 0.38044 -0.04773 -0.09102 -0.06273 374 ASP A OD1 
2908 O  OD2 . ASP A 374 ? 0.56076 0.40525 0.37059 -0.12192 -0.09990 0.00891  374 ASP A OD2 
2909 N  N   . ARG A 375 ? 0.52475 0.25470 0.32335 -0.02979 -0.07011 -0.09441 375 ARG A N   
2910 C  CA  . ARG A 375 ? 0.54926 0.29951 0.31796 0.01616  -0.07339 -0.09669 375 ARG A CA  
2911 C  C   . ARG A 375 ? 0.49648 0.28095 0.30468 -0.04347 -0.09933 -0.08352 375 ARG A C   
2912 O  O   . ARG A 375 ? 0.59964 0.32305 0.32146 -0.04869 -0.09029 -0.10080 375 ARG A O   
2913 C  CB  . ARG A 375 ? 0.56498 0.31975 0.33484 0.09718  -0.10621 -0.05380 375 ARG A CB  
2914 C  CG  . ARG A 375 ? 0.66039 0.42582 0.38001 0.06571  -0.08368 -0.03726 375 ARG A CG  
2915 C  CD  . ARG A 375 ? 0.69086 0.39667 0.40482 0.10982  -0.08854 -0.04515 375 ARG A CD  
2916 N  NE  . ARG A 375 ? 0.67180 0.39870 0.42447 0.19046  -0.08068 -0.07177 375 ARG A NE  
2917 C  CZ  . ARG A 375 ? 0.72060 0.44556 0.43752 0.22633  -0.08173 -0.05552 375 ARG A CZ  
2918 N  NH1 . ARG A 375 ? 0.69125 0.45752 0.41844 0.24837  -0.10817 -0.06111 375 ARG A NH1 
2919 N  NH2 . ARG A 375 ? 0.70050 0.45940 0.44700 0.25176  -0.03991 -0.06050 375 ARG A NH2 
2920 N  N   . VAL A 376 ? 0.45436 0.34227 0.28040 0.05891  -0.10775 -0.09213 376 VAL A N   
2921 C  CA  . VAL A 376 ? 0.44166 0.36746 0.27630 0.04002  -0.10715 -0.04412 376 VAL A CA  
2922 C  C   . VAL A 376 ? 0.49990 0.39883 0.24938 0.06743  -0.08220 -0.05960 376 VAL A C   
2923 O  O   . VAL A 376 ? 0.57644 0.38488 0.21782 0.10674  -0.03575 -0.06969 376 VAL A O   
2924 C  CB  . VAL A 376 ? 0.52801 0.41026 0.29193 -0.05763 -0.12659 -0.04607 376 VAL A CB  
2925 C  CG1 . VAL A 376 ? 0.58120 0.53028 0.27285 -0.06646 -0.09189 -0.02725 376 VAL A CG1 
2926 C  CG2 . VAL A 376 ? 0.57246 0.41853 0.29546 -0.06652 -0.11290 -0.04804 376 VAL A CG2 
2927 N  N   . PRO A 377 ? 0.48227 0.45579 0.26378 0.07377  -0.10767 -0.07926 377 PRO A N   
2928 C  CA  . PRO A 377 ? 0.51220 0.53768 0.27641 0.12783  -0.09100 -0.05666 377 PRO A CA  
2929 C  C   . PRO A 377 ? 0.50865 0.58391 0.27611 0.15274  -0.07820 -0.03305 377 PRO A C   
2930 O  O   . PRO A 377 ? 0.50259 0.66779 0.30717 0.21820  -0.08396 -0.01523 377 PRO A O   
2931 C  CB  . PRO A 377 ? 0.49739 0.53970 0.28650 0.15032  -0.09847 -0.07577 377 PRO A CB  
2932 C  CG  . PRO A 377 ? 0.46941 0.55564 0.27111 0.09174  -0.14911 -0.10341 377 PRO A CG  
2933 C  CD  . PRO A 377 ? 0.51107 0.55424 0.29558 0.09389  -0.10304 -0.10582 377 PRO A CD  
2934 N  N   . THR A 378 ? 0.46316 0.60792 0.27674 0.11630  -0.06650 -0.06131 378 THR A N   
2935 C  CA  . THR A 378 ? 0.48975 0.59349 0.24406 0.06423  -0.06640 -0.09039 378 THR A CA  
2936 C  C   . THR A 378 ? 0.52771 0.51837 0.23439 0.11763  -0.06159 -0.09616 378 THR A C   
2937 O  O   . THR A 378 ? 0.52330 0.55500 0.24494 0.18701  -0.06031 -0.07762 378 THR A O   
2938 C  CB  . THR A 378 ? 0.49591 0.69104 0.28798 0.04255  -0.02181 -0.09814 378 THR A CB  
2939 O  OG1 . THR A 378 ? 0.44252 0.66212 0.30365 0.09093  -0.04226 -0.13797 378 THR A OG1 
2940 C  CG2 . THR A 378 ? 0.51411 0.76103 0.27496 0.09058  0.00491  -0.08324 378 THR A CG2 
2941 N  N   . LEU A 379 ? 0.57638 0.41257 0.24024 0.14358  -0.10207 -0.08745 379 LEU A N   
2942 C  CA  . LEU A 379 ? 0.55681 0.36014 0.24451 0.16206  -0.10799 -0.04531 379 LEU A CA  
2943 C  C   . LEU A 379 ? 0.49977 0.34331 0.25022 0.16212  -0.08510 -0.00768 379 LEU A C   
2944 O  O   . LEU A 379 ? 0.49828 0.35650 0.27302 0.14860  -0.04060 -0.02882 379 LEU A O   
2945 C  CB  . LEU A 379 ? 0.63374 0.44018 0.22632 0.15781  -0.09439 -0.04407 379 LEU A CB  
2946 C  CG  . LEU A 379 ? 0.68493 0.37680 0.22779 0.07778  -0.07415 -0.03923 379 LEU A CG  
2947 C  CD1 . LEU A 379 ? 0.66796 0.42506 0.22518 0.09948  -0.05191 -0.02966 379 LEU A CD1 
2948 C  CD2 . LEU A 379 ? 0.74086 0.37176 0.25226 0.06535  -0.10597 -0.00611 379 LEU A CD2 
2949 N  N   . ARG A 380 ? 0.49575 0.41855 0.26098 0.11559  -0.06628 -0.06194 380 ARG A N   
2950 C  CA  . ARG A 380 ? 0.49780 0.41964 0.27306 0.13913  -0.09630 -0.02821 380 ARG A CA  
2951 C  C   . ARG A 380 ? 0.49089 0.39294 0.25021 0.08953  -0.07630 -0.05140 380 ARG A C   
2952 O  O   . ARG A 380 ? 0.47686 0.43772 0.25041 0.12981  -0.08483 -0.02652 380 ARG A O   
2953 C  CB  . ARG A 380 ? 0.53277 0.56909 0.30575 0.15124  -0.10976 -0.01790 380 ARG A CB  
2954 C  CG  . ARG A 380 ? 0.60417 0.79212 0.33453 0.19256  -0.13994 0.03023  380 ARG A CG  
2955 C  CD  . ARG A 380 ? 0.67876 0.99800 0.37946 0.20561  -0.14483 0.01150  380 ARG A CD  
2956 N  NE  . ARG A 380 ? 0.76191 1.10593 0.41990 0.24672  -0.16973 0.04653  380 ARG A NE  
2957 C  CZ  . ARG A 380 ? 0.85187 1.14832 0.46247 0.30211  -0.16972 0.04666  380 ARG A CZ  
2958 N  NH1 . ARG A 380 ? 0.90625 1.17326 0.49554 0.30244  -0.14931 0.04598  380 ARG A NH1 
2959 N  NH2 . ARG A 380 ? 0.84732 1.10022 0.47677 0.35281  -0.19294 0.04795  380 ARG A NH2 
2960 N  N   . LEU A 381 ? 0.47127 0.39506 0.23234 0.07948  -0.04224 -0.04856 381 LEU A N   
2961 C  CA  . LEU A 381 ? 0.42720 0.46863 0.20454 0.11767  -0.03382 -0.06930 381 LEU A CA  
2962 C  C   . LEU A 381 ? 0.47873 0.48621 0.21415 0.17906  -0.06135 -0.06547 381 LEU A C   
2963 O  O   . LEU A 381 ? 0.46065 0.47761 0.24877 0.15390  -0.09829 -0.01663 381 LEU A O   
2964 C  CB  . LEU A 381 ? 0.45936 0.47242 0.22135 0.08892  -0.03438 -0.06098 381 LEU A CB  
2965 C  CG  . LEU A 381 ? 0.51436 0.45389 0.23550 0.10187  -0.03101 -0.05018 381 LEU A CG  
2966 C  CD1 . LEU A 381 ? 0.48877 0.41828 0.24545 0.03568  -0.05997 -0.04861 381 LEU A CD1 
2967 C  CD2 . LEU A 381 ? 0.47012 0.43104 0.24160 0.08014  0.00208  -0.02792 381 LEU A CD2 
2968 N  N   . ALA A 382 ? 0.46776 0.54676 0.21604 0.15713  -0.03257 -0.07374 382 ALA A N   
2969 C  CA  . ALA A 382 ? 0.54126 0.59771 0.21224 0.14290  -0.01563 -0.10072 382 ALA A CA  
2970 C  C   . ALA A 382 ? 0.62163 0.63771 0.22173 0.09496  -0.02217 -0.06507 382 ALA A C   
2971 O  O   . ALA A 382 ? 0.67307 0.67045 0.22777 0.05651  0.00123  -0.06102 382 ALA A O   
2972 C  CB  . ALA A 382 ? 0.52421 0.58036 0.23340 0.15775  -0.04013 -0.12059 382 ALA A CB  
2973 N  N   . VAL A 383 ? 0.61102 0.65054 0.22791 0.05300  -0.03437 -0.03743 383 VAL A N   
2974 C  CA  . VAL A 383 ? 0.60319 0.64897 0.25806 0.05066  -0.01793 -0.00635 383 VAL A CA  
2975 C  C   . VAL A 383 ? 0.60445 0.56670 0.27743 0.07794  -0.00640 0.00149  383 VAL A C   
2976 O  O   . VAL A 383 ? 0.62119 0.53292 0.29791 0.03970  -0.02555 -0.00887 383 VAL A O   
2977 C  CB  . VAL A 383 ? 0.54407 0.71729 0.25792 0.03412  0.00549  -0.01682 383 VAL A CB  
2978 C  CG1 . VAL A 383 ? 0.53144 0.72414 0.27754 0.07419  0.03675  -0.02819 383 VAL A CG1 
2979 C  CG2 . VAL A 383 ? 0.50688 0.79365 0.24390 0.02269  -0.02702 0.02943  383 VAL A CG2 
2980 N  N   . PRO A 384 ? 0.65916 0.54537 0.31720 0.11280  0.04110  0.04550  384 PRO A N   
2981 C  CA  . PRO A 384 ? 0.69549 0.53564 0.32890 0.09195  -0.00867 0.09980  384 PRO A CA  
2982 C  C   . PRO A 384 ? 0.69734 0.50850 0.33337 0.03480  -0.03179 0.10144  384 PRO A C   
2983 O  O   . PRO A 384 ? 0.65957 0.56752 0.32117 -0.04426 -0.02905 0.10199  384 PRO A O   
2984 C  CB  . PRO A 384 ? 0.72667 0.57045 0.34436 0.08174  0.01737  0.09513  384 PRO A CB  
2985 C  CG  . PRO A 384 ? 0.71797 0.58129 0.34815 0.11002  0.04915  0.12348  384 PRO A CG  
2986 C  CD  . PRO A 384 ? 0.68405 0.51734 0.31654 0.14058  0.05644  0.12971  384 PRO A CD  
2987 N  N   . VAL A 385 ? 0.67417 0.44855 0.35693 0.01020  -0.06314 0.09610  385 VAL A N   
2988 C  CA  . VAL A 385 ? 0.62450 0.41871 0.40168 -0.02819 -0.07054 0.06448  385 VAL A CA  
2989 C  C   . VAL A 385 ? 0.67228 0.43471 0.44451 -0.04975 -0.09771 0.08593  385 VAL A C   
2990 O  O   . VAL A 385 ? 0.69453 0.40727 0.41206 -0.03912 -0.10142 0.02984  385 VAL A O   
2991 C  CB  . VAL A 385 ? 0.60049 0.41423 0.40310 -0.02660 -0.07088 0.01137  385 VAL A CB  
2992 C  CG1 . VAL A 385 ? 0.58901 0.41113 0.42216 -0.01251 -0.07993 0.02168  385 VAL A CG1 
2993 C  CG2 . VAL A 385 ? 0.53471 0.38349 0.38920 -0.04400 -0.05133 0.00171  385 VAL A CG2 
2994 N  N   . GLU A 386 ? 0.68617 0.52597 0.49483 -0.01500 -0.10740 0.14280  386 GLU A N   
2995 C  CA  . GLU A 386 ? 0.67633 0.57862 0.53951 -0.01340 -0.13155 0.19731  386 GLU A CA  
2996 C  C   . GLU A 386 ? 0.61063 0.56322 0.50813 -0.07638 -0.09357 0.19121  386 GLU A C   
2997 O  O   . GLU A 386 ? 0.62476 0.56088 0.52702 -0.17210 -0.10755 0.16930  386 GLU A O   
2998 C  CB  . GLU A 386 ? 0.71042 0.65837 0.60624 0.03130  -0.17904 0.23715  386 GLU A CB  
2999 C  CG  . GLU A 386 ? 0.80561 0.77377 0.66328 0.00702  -0.18886 0.22267  386 GLU A CG  
3000 C  CD  . GLU A 386 ? 0.89889 0.85463 0.69181 0.05769  -0.21531 0.25498  386 GLU A CD  
3001 O  OE1 . GLU A 386 ? 0.96634 0.86905 0.69984 0.05293  -0.23882 0.28654  386 GLU A OE1 
3002 O  OE2 . GLU A 386 ? 0.87845 0.87560 0.70800 0.11797  -0.21203 0.25435  386 GLU A OE2 
3003 N  N   . GLN A 387 ? 0.58757 0.51805 0.44360 0.04007  -0.07248 0.22380  387 GLN A N   
3004 C  CA  . GLN A 387 ? 0.56962 0.49021 0.36676 0.01940  0.00913  0.18694  387 GLN A CA  
3005 C  C   . GLN A 387 ? 0.51407 0.45742 0.31239 0.02158  0.03761  0.13695  387 GLN A C   
3006 O  O   . GLN A 387 ? 0.46420 0.48678 0.29556 -0.04012 0.04465  0.05458  387 GLN A O   
3007 C  CB  . GLN A 387 ? 0.63533 0.52757 0.34843 -0.08538 0.03540  0.15074  387 GLN A CB  
3008 C  CG  . GLN A 387 ? 0.72009 0.58460 0.36182 -0.05239 0.03646  0.12385  387 GLN A CG  
3009 C  CD  . GLN A 387 ? 0.76156 0.68011 0.38234 0.01491  0.01580  0.11092  387 GLN A CD  
3010 O  OE1 . GLN A 387 ? 0.80758 0.74794 0.39560 0.04822  -0.01025 0.09503  387 GLN A OE1 
3011 N  NE2 . GLN A 387 ? 0.77556 0.73525 0.38560 0.05700  0.01597  0.07384  387 GLN A NE2 
3012 N  N   . LEU A 388 ? 0.48782 0.47086 0.28595 -0.00753 0.05093  0.12447  388 LEU A N   
3013 C  CA  . LEU A 388 ? 0.46089 0.41729 0.27089 -0.03133 0.03665  0.09063  388 LEU A CA  
3014 C  C   . LEU A 388 ? 0.45063 0.38232 0.28574 -0.04414 0.00841  0.06497  388 LEU A C   
3015 O  O   . LEU A 388 ? 0.49922 0.34515 0.31182 -0.05294 0.04019  0.06941  388 LEU A O   
3016 C  CB  . LEU A 388 ? 0.41643 0.36130 0.26137 -0.01230 0.03848  0.05500  388 LEU A CB  
3017 C  CG  . LEU A 388 ? 0.40351 0.39824 0.25694 -0.01072 0.03645  0.07510  388 LEU A CG  
3018 C  CD1 . LEU A 388 ? 0.46190 0.40710 0.26480 -0.02273 0.04297  0.10549  388 LEU A CD1 
3019 C  CD2 . LEU A 388 ? 0.43772 0.39001 0.24888 -0.02423 -0.02888 0.04488  388 LEU A CD2 
3020 N  N   . VAL A 389 ? 0.37891 0.42048 0.24622 -0.03235 0.05622  0.01351  389 VAL A N   
3021 C  CA  . VAL A 389 ? 0.35714 0.42885 0.25701 0.00838  0.09979  0.02715  389 VAL A CA  
3022 C  C   . VAL A 389 ? 0.37989 0.40388 0.24589 0.02160  0.07751  0.01398  389 VAL A C   
3023 O  O   . VAL A 389 ? 0.41503 0.40158 0.23041 -0.00732 0.05889  0.04301  389 VAL A O   
3024 C  CB  . VAL A 389 ? 0.41148 0.44846 0.25434 0.01641  0.10483  0.01475  389 VAL A CB  
3025 C  CG1 . VAL A 389 ? 0.46659 0.40987 0.27311 -0.06416 0.08130  0.03921  389 VAL A CG1 
3026 C  CG2 . VAL A 389 ? 0.42935 0.51230 0.28037 0.06338  0.12876  0.01976  389 VAL A CG2 
3027 N  N   . LEU A 390 ? 0.36140 0.38364 0.24653 -0.02540 0.05921  0.02715  390 LEU A N   
3028 C  CA  . LEU A 390 ? 0.36435 0.36022 0.26848 -0.00397 0.01108  0.03185  390 LEU A CA  
3029 C  C   . LEU A 390 ? 0.35754 0.36280 0.28418 -0.03213 0.06476  0.04343  390 LEU A C   
3030 O  O   . LEU A 390 ? 0.40399 0.43249 0.31291 -0.10165 0.10816  0.06569  390 LEU A O   
3031 C  CB  . LEU A 390 ? 0.33869 0.29929 0.29454 -0.00287 0.02463  0.00419  390 LEU A CB  
3032 C  CG  . LEU A 390 ? 0.37957 0.27654 0.35244 -0.08623 0.00128  0.07369  390 LEU A CG  
3033 C  CD1 . LEU A 390 ? 0.42189 0.30948 0.37506 -0.01475 -0.01101 0.00817  390 LEU A CD1 
3034 C  CD2 . LEU A 390 ? 0.42092 0.36981 0.39574 -0.13157 -0.02302 0.05238  390 LEU A CD2 
3035 N  N   . ARG A 391 ? 0.32908 0.34429 0.27827 0.01284  0.03131  0.03330  391 ARG A N   
3036 C  CA  . ARG A 391 ? 0.34405 0.30299 0.29602 0.02551  0.03232  0.03849  391 ARG A CA  
3037 C  C   . ARG A 391 ? 0.35375 0.28689 0.28984 -0.00902 0.03310  0.07065  391 ARG A C   
3038 O  O   . ARG A 391 ? 0.36200 0.30063 0.29380 0.03024  0.00177  0.02420  391 ARG A O   
3039 C  CB  . ARG A 391 ? 0.37407 0.26715 0.31824 0.07265  0.02633  0.04897  391 ARG A CB  
3040 C  CG  . ARG A 391 ? 0.46663 0.17826 0.35227 0.02896  0.08047  0.06576  391 ARG A CG  
3041 C  CD  . ARG A 391 ? 0.55948 0.19832 0.36880 -0.03339 0.08152  0.06379  391 ARG A CD  
3042 N  NE  . ARG A 391 ? 0.59940 0.27068 0.38595 -0.01540 0.06165  0.08168  391 ARG A NE  
3043 C  CZ  . ARG A 391 ? 0.67012 0.35379 0.41490 -0.03106 0.07027  0.06961  391 ARG A CZ  
3044 N  NH1 . ARG A 391 ? 0.67038 0.28599 0.41864 -0.02786 0.09163  0.01817  391 ARG A NH1 
3045 N  NH2 . ARG A 391 ? 0.71991 0.34861 0.43094 -0.02018 0.04103  0.06477  391 ARG A NH2 
3046 N  N   . PRO A 392 ? 0.30280 0.41135 0.31465 -0.05105 0.00871  0.04891  392 PRO A N   
3047 C  CA  . PRO A 392 ? 0.27444 0.38641 0.32696 -0.00938 0.04576  0.05473  392 PRO A CA  
3048 C  C   . PRO A 392 ? 0.33551 0.33336 0.33502 -0.02818 0.04412  0.04278  392 PRO A C   
3049 O  O   . PRO A 392 ? 0.32131 0.28996 0.32893 -0.06021 0.06857  0.06415  392 PRO A O   
3050 C  CB  . PRO A 392 ? 0.23092 0.42548 0.34561 -0.01908 0.04844  0.04899  392 PRO A CB  
3051 C  CG  . PRO A 392 ? 0.29135 0.46547 0.34633 -0.02255 0.03030  0.06165  392 PRO A CG  
3052 C  CD  . PRO A 392 ? 0.33432 0.47259 0.34534 -0.02996 -0.00799 0.05390  392 PRO A CD  
3053 N  N   . GLY A 393 ? 0.31714 0.33734 0.33579 -0.03155 0.00432  0.01381  393 GLY A N   
3054 C  CA  . GLY A 393 ? 0.35300 0.26784 0.35089 -0.00628 0.02253  -0.02052 393 GLY A CA  
3055 C  C   . GLY A 393 ? 0.25745 0.26102 0.36041 -0.01278 0.01324  -0.00311 393 GLY A C   
3056 O  O   . GLY A 393 ? 0.32290 0.27453 0.35891 -0.03473 0.02881  -0.02896 393 GLY A O   
3057 N  N   . THR A 394 ? 0.28578 0.26098 0.36437 -0.00643 0.02151  0.01416  394 THR A N   
3058 C  CA  . THR A 394 ? 0.31425 0.26538 0.35874 -0.08268 0.04001  0.00542  394 THR A CA  
3059 C  C   . THR A 394 ? 0.29007 0.22909 0.32001 -0.09916 -0.00190 -0.00771 394 THR A C   
3060 O  O   . THR A 394 ? 0.37432 0.29429 0.30271 -0.07380 -0.01786 0.02441  394 THR A O   
3061 C  CB  . THR A 394 ? 0.33365 0.27414 0.38084 -0.04521 0.07544  0.01240  394 THR A CB  
3062 O  OG1 . THR A 394 ? 0.36130 0.32431 0.38790 -0.07514 0.07699  0.00901  394 THR A OG1 
3063 C  CG2 . THR A 394 ? 0.41933 0.28374 0.39132 -0.07247 0.04586  0.03159  394 THR A CG2 
3064 N  N   . THR A 395 ? 0.27859 0.22676 0.31059 -0.03403 0.03160  -0.00316 395 THR A N   
3065 C  CA  . THR A 395 ? 0.28007 0.25187 0.32033 -0.00713 0.04721  0.00194  395 THR A CA  
3066 C  C   . THR A 395 ? 0.22782 0.26676 0.29990 -0.01767 0.05061  0.01693  395 THR A C   
3067 O  O   . THR A 395 ? 0.25826 0.28036 0.30698 -0.01095 0.02118  0.05150  395 THR A O   
3068 C  CB  . THR A 395 ? 0.34546 0.26518 0.31263 0.00871  0.01343  0.02913  395 THR A CB  
3069 O  OG1 . THR A 395 ? 0.38738 0.28126 0.33390 0.01613  0.02379  0.05766  395 THR A OG1 
3070 C  CG2 . THR A 395 ? 0.36775 0.23949 0.28184 0.04313  0.01786  0.03212  395 THR A CG2 
3071 N  N   . ILE A 396 ? 0.25982 0.25048 0.27739 -0.05695 0.02496  0.01530  396 ILE A N   
3072 C  CA  . ILE A 396 ? 0.23300 0.24764 0.25228 -0.04645 0.02939  0.01315  396 ILE A CA  
3073 C  C   . ILE A 396 ? 0.33222 0.22335 0.25890 -0.00418 0.02644  0.06547  396 ILE A C   
3074 O  O   . ILE A 396 ? 0.32146 0.25368 0.26577 0.04612  0.07474  0.01673  396 ILE A O   
3075 C  CB  . ILE A 396 ? 0.29040 0.24882 0.25472 -0.07348 0.03124  0.02435  396 ILE A CB  
3076 C  CG1 . ILE A 396 ? 0.40324 0.30830 0.24731 0.02995  0.07039  -0.01058 396 ILE A CG1 
3077 C  CG2 . ILE A 396 ? 0.34365 0.24804 0.26265 -0.09170 0.02197  0.03615  396 ILE A CG2 
3078 C  CD1 . ILE A 396 ? 0.49606 0.54478 0.28493 0.01999  0.06174  -0.00153 396 ILE A CD1 
3079 N  N   . GLN A 397 ? 0.29523 0.18783 0.26033 0.00435  -0.02052 0.04203  397 GLN A N   
3080 C  CA  . GLN A 397 ? 0.30570 0.18469 0.22774 0.01660  -0.01767 0.03370  397 GLN A CA  
3081 C  C   . GLN A 397 ? 0.32138 0.23154 0.22348 -0.01473 0.06107  0.01095  397 GLN A C   
3082 O  O   . GLN A 397 ? 0.41198 0.23420 0.22258 -0.03380 0.02766  0.03430  397 GLN A O   
3083 C  CB  . GLN A 397 ? 0.31694 0.20780 0.22458 0.09906  -0.00094 -0.01472 397 GLN A CB  
3084 C  CG  . GLN A 397 ? 0.34873 0.19547 0.22952 0.03433  0.00296  0.00155  397 GLN A CG  
3085 C  CD  . GLN A 397 ? 0.45375 0.27744 0.26399 -0.04568 0.01437  0.01201  397 GLN A CD  
3086 O  OE1 . GLN A 397 ? 0.33320 0.29984 0.27624 -0.00815 0.06446  -0.00333 397 GLN A OE1 
3087 N  NE2 . GLN A 397 ? 0.55432 0.38899 0.30180 -0.12267 0.00528  0.01655  397 GLN A NE2 
3088 N  N   . GLY A 398 ? 0.31922 0.25554 0.22221 -0.02769 0.07631  -0.02593 398 GLY A N   
3089 C  CA  . GLY A 398 ? 0.36493 0.27600 0.22226 -0.00676 0.05813  -0.07034 398 GLY A CA  
3090 C  C   . GLY A 398 ? 0.36408 0.28760 0.21954 0.03106  0.05353  -0.01690 398 GLY A C   
3091 O  O   . GLY A 398 ? 0.37776 0.28868 0.23469 0.04777  0.05334  0.00775  398 GLY A O   
3092 N  N   . VAL A 399 ? 0.39367 0.30140 0.21742 0.03524  0.07742  -0.01140 399 VAL A N   
3093 C  CA  . VAL A 399 ? 0.32910 0.31361 0.24975 0.07520  0.06554  0.00609  399 VAL A CA  
3094 C  C   . VAL A 399 ? 0.33818 0.34189 0.28212 0.07012  0.05432  -0.01519 399 VAL A C   
3095 O  O   . VAL A 399 ? 0.39596 0.36737 0.32466 0.03124  0.00499  0.00546  399 VAL A O   
3096 C  CB  . VAL A 399 ? 0.39437 0.27452 0.27438 0.00867  -0.00409 0.03216  399 VAL A CB  
3097 C  CG1 . VAL A 399 ? 0.46179 0.33124 0.28813 0.03378  0.03164  0.03488  399 VAL A CG1 
3098 C  CG2 . VAL A 399 ? 0.38437 0.33649 0.26054 -0.00615 -0.03667 0.03807  399 VAL A CG2 
3099 N  N   . ASN A 400 ? 0.34884 0.40192 0.31062 0.09820  0.03834  0.02363  400 ASN A N   
3100 C  CA  . ASN A 400 ? 0.40387 0.39319 0.31922 0.06877  0.03874  -0.00792 400 ASN A CA  
3101 C  C   . ASN A 400 ? 0.42401 0.39091 0.30103 0.05287  0.02896  -0.02787 400 ASN A C   
3102 O  O   . ASN A 400 ? 0.39504 0.43502 0.31030 0.10218  0.03465  -0.01666 400 ASN A O   
3103 C  CB  . ASN A 400 ? 0.36687 0.45946 0.33839 0.02704  0.01885  0.00189  400 ASN A CB  
3104 C  CG  . ASN A 400 ? 0.37867 0.54923 0.34464 0.00567  0.00618  0.00122  400 ASN A CG  
3105 O  OD1 . ASN A 400 ? 0.34047 0.57624 0.34322 0.03112  0.03372  -0.03416 400 ASN A OD1 
3106 N  ND2 . ASN A 400 ? 0.35975 0.61321 0.36695 0.00348  -0.01219 0.00761  400 ASN A ND2 
3107 N  N   . GLU A 401 ? 0.37155 0.30949 0.27352 0.01544  0.04788  -0.00191 401 GLU A N   
3108 C  CA  A GLU A 401 ? 0.37616 0.35569 0.26075 0.05933  0.06883  -0.00064 401 GLU A CA  
3109 C  CA  B GLU A 401 ? 0.38830 0.35975 0.26463 0.00862  0.07293  -0.00406 401 GLU A CA  
3110 C  C   . GLU A 401 ? 0.34725 0.35552 0.24723 -0.01490 0.06798  0.01641  401 GLU A C   
3111 O  O   . GLU A 401 ? 0.43714 0.41566 0.26593 0.03989  0.06593  0.02642  401 GLU A O   
3112 C  CB  A GLU A 401 ? 0.49723 0.45248 0.28717 0.02264  0.11258  -0.03522 401 GLU A CB  
3113 C  CB  B GLU A 401 ? 0.48810 0.43316 0.29128 -0.05329 0.11870  -0.03258 401 GLU A CB  
3114 C  CG  A GLU A 401 ? 0.58764 0.55863 0.32656 0.04459  0.14237  -0.04882 401 GLU A CG  
3115 C  CG  B GLU A 401 ? 0.55598 0.48828 0.32888 -0.09765 0.16202  -0.04186 401 GLU A CG  
3116 C  CD  A GLU A 401 ? 0.66666 0.64954 0.36188 0.04723  0.15799  -0.04020 401 GLU A CD  
3117 C  CD  B GLU A 401 ? 0.61812 0.56192 0.36764 -0.15299 0.19682  -0.02996 401 GLU A CD  
3118 O  OE1 A GLU A 401 ? 0.66206 0.67322 0.38355 0.05322  0.16337  -0.01537 401 GLU A OE1 
3119 O  OE1 B GLU A 401 ? 0.66355 0.60125 0.37054 -0.14288 0.21200  -0.01582 401 GLU A OE1 
3120 O  OE2 A GLU A 401 ? 0.69223 0.65600 0.36812 0.08769  0.15060  -0.07356 401 GLU A OE2 
3121 O  OE2 B GLU A 401 ? 0.61096 0.59255 0.39243 -0.19505 0.20289  -0.01148 401 GLU A OE2 
3122 N  N   . LEU A 402 ? 0.29217 0.36896 0.23787 0.01151  0.04165  0.02126  402 LEU A N   
3123 C  CA  . LEU A 402 ? 0.32107 0.35886 0.21987 0.02564  0.02513  -0.05002 402 LEU A CA  
3124 C  C   . LEU A 402 ? 0.44357 0.40833 0.20308 0.09433  0.01602  -0.03619 402 LEU A C   
3125 O  O   . LEU A 402 ? 0.46678 0.34158 0.19819 0.14778  -0.02257 -0.03858 402 LEU A O   
3126 C  CB  . LEU A 402 ? 0.33238 0.32134 0.22058 0.06660  0.02952  -0.06870 402 LEU A CB  
3127 C  CG  . LEU A 402 ? 0.33708 0.29159 0.23344 0.07230  0.04600  -0.01108 402 LEU A CG  
3128 C  CD1 . LEU A 402 ? 0.38346 0.30520 0.23169 0.06085  0.08048  0.01211  402 LEU A CD1 
3129 C  CD2 . LEU A 402 ? 0.35301 0.38580 0.23036 0.05248  0.03842  0.00902  402 LEU A CD2 
3130 N  N   . PRO A 403 ? 0.44952 0.49962 0.20282 0.08422  0.02645  -0.04132 403 PRO A N   
3131 C  CA  . PRO A 403 ? 0.41314 0.49170 0.20097 0.12208  0.05239  -0.08828 403 PRO A CA  
3132 C  C   . PRO A 403 ? 0.47282 0.48060 0.20892 0.09190  0.01316  -0.09771 403 PRO A C   
3133 O  O   . PRO A 403 ? 0.40567 0.46052 0.23103 0.11604  0.00429  -0.08313 403 PRO A O   
3134 C  CB  . PRO A 403 ? 0.42708 0.55051 0.19396 0.08499  0.05757  -0.04032 403 PRO A CB  
3135 C  CG  . PRO A 403 ? 0.46610 0.52314 0.20392 0.05204  0.07557  -0.04572 403 PRO A CG  
3136 C  CD  . PRO A 403 ? 0.47425 0.48054 0.19337 0.08453  0.06848  0.00742  403 PRO A CD  
3137 N  N   . VAL A 404 ? 0.45108 0.41234 0.21045 0.07773  -0.01796 -0.08167 404 VAL A N   
3138 C  CA  . VAL A 404 ? 0.42546 0.39817 0.21127 0.07274  -0.06230 -0.09769 404 VAL A CA  
3139 C  C   . VAL A 404 ? 0.39665 0.44464 0.24366 0.05664  -0.08625 -0.10321 404 VAL A C   
3140 O  O   . VAL A 404 ? 0.42900 0.48875 0.27839 0.04455  -0.09259 -0.10585 404 VAL A O   
3141 C  CB  . VAL A 404 ? 0.42712 0.32304 0.18452 0.09358  -0.03699 -0.06638 404 VAL A CB  
3142 C  CG1 . VAL A 404 ? 0.48956 0.34543 0.16288 0.07017  -0.05055 -0.07529 404 VAL A CG1 
3143 C  CG2 . VAL A 404 ? 0.43479 0.36791 0.20609 0.15382  -0.08782 -0.04504 404 VAL A CG2 
3144 N  N   . THR A 405 ? 0.45409 0.37934 0.22894 0.05338  -0.12010 -0.09158 405 THR A N   
3145 C  CA  . THR A 405 ? 0.46304 0.40143 0.23613 0.11201  -0.07358 -0.12572 405 THR A CA  
3146 C  C   . THR A 405 ? 0.42645 0.37347 0.25638 0.11517  -0.10596 -0.14652 405 THR A C   
3147 O  O   . THR A 405 ? 0.47613 0.39096 0.26246 0.14923  -0.08076 -0.12253 405 THR A O   
3148 C  CB  . THR A 405 ? 0.51300 0.47340 0.27413 0.13594  -0.07853 -0.10849 405 THR A CB  
3149 O  OG1 . THR A 405 ? 0.50849 0.56136 0.30470 0.12936  -0.03195 -0.12308 405 THR A OG1 
3150 C  CG2 . THR A 405 ? 0.50458 0.56308 0.27683 0.13247  -0.08034 -0.02578 405 THR A CG2 
3151 N  N   . TRP A 406 ? 0.37930 0.45221 0.28375 0.12034  -0.14571 -0.12950 406 TRP A N   
3152 C  CA  . TRP A 406 ? 0.42619 0.54020 0.33236 0.12991  -0.14975 -0.15402 406 TRP A CA  
3153 C  C   . TRP A 406 ? 0.44276 0.59929 0.39679 0.06540  -0.12694 -0.21224 406 TRP A C   
3154 O  O   . TRP A 406 ? 0.49830 0.68105 0.36755 0.01432  -0.10985 -0.20277 406 TRP A O   
3155 C  CB  . TRP A 406 ? 0.47888 0.49130 0.33079 0.09225  -0.11771 -0.18313 406 TRP A CB  
3156 C  CG  . TRP A 406 ? 0.51165 0.44269 0.34835 0.07386  -0.12857 -0.15809 406 TRP A CG  
3157 C  CD1 . TRP A 406 ? 0.55869 0.41907 0.37918 0.08974  -0.11364 -0.13930 406 TRP A CD1 
3158 C  CD2 . TRP A 406 ? 0.46842 0.39737 0.35090 0.11095  -0.15298 -0.12632 406 TRP A CD2 
3159 N  NE1 . TRP A 406 ? 0.57120 0.46471 0.37530 0.08475  -0.14440 -0.12898 406 TRP A NE1 
3160 C  CE2 . TRP A 406 ? 0.49475 0.42676 0.37392 0.06460  -0.15812 -0.12295 406 TRP A CE2 
3161 C  CE3 . TRP A 406 ? 0.45033 0.36884 0.36740 0.04919  -0.18979 -0.09123 406 TRP A CE3 
3162 C  CZ2 . TRP A 406 ? 0.51778 0.42488 0.39327 0.12914  -0.12398 -0.13225 406 TRP A CZ2 
3163 C  CZ3 . TRP A 406 ? 0.44264 0.41391 0.39931 0.09943  -0.15845 -0.10017 406 TRP A CZ3 
3164 C  CH2 . TRP A 406 ? 0.50948 0.41411 0.39996 0.13792  -0.10953 -0.13209 406 TRP A CH2 
3165 N  N   . HIS A 407 ? 0.47678 0.63685 0.48538 0.08786  -0.13598 -0.24726 407 HIS A N   
3166 C  CA  . HIS A 407 ? 0.55043 0.59154 0.56796 0.01316  -0.17677 -0.27215 407 HIS A CA  
3167 C  C   . HIS A 407 ? 0.68159 0.71894 0.66339 0.00384  -0.17635 -0.25008 407 HIS A C   
3168 O  O   . HIS A 407 ? 0.73730 0.76610 0.68100 0.05203  -0.16244 -0.25585 407 HIS A O   
3169 C  CB  . HIS A 407 ? 0.50133 0.51628 0.55815 -0.01273 -0.19225 -0.24934 407 HIS A CB  
3170 C  CG  . HIS A 407 ? 0.51264 0.48190 0.56419 -0.11913 -0.18170 -0.19419 407 HIS A CG  
3171 N  ND1 . HIS A 407 ? 0.52070 0.55855 0.56571 -0.10502 -0.16807 -0.13324 407 HIS A ND1 
3172 C  CD2 . HIS A 407 ? 0.54185 0.49091 0.56460 -0.14605 -0.19457 -0.14567 407 HIS A CD2 
3173 C  CE1 . HIS A 407 ? 0.50660 0.51787 0.58142 -0.17721 -0.16374 -0.10473 407 HIS A CE1 
3174 N  NE2 . HIS A 407 ? 0.55900 0.61259 0.58018 -0.15569 -0.18167 -0.12317 407 HIS A NE2 
3175 N  N   . HIS A 408 ? 0.79789 0.82393 0.75433 -0.00116 -0.12182 -0.18114 408 HIS A N   
3176 C  CA  . HIS A 408 ? 0.95692 0.86128 0.83439 -0.03895 -0.10031 -0.15020 408 HIS A CA  
3177 C  C   . HIS A 408 ? 0.96154 0.79067 0.88639 -0.03462 -0.06398 -0.14367 408 HIS A C   
3178 O  O   . HIS A 408 ? 1.00658 0.77747 0.89357 -0.03041 -0.07079 -0.14604 408 HIS A O   
3179 C  CB  . HIS A 408 ? 1.10994 0.97503 0.85873 -0.06804 -0.11265 -0.11017 408 HIS A CB  
3180 C  CG  . HIS A 408 ? 1.24044 1.08026 0.87964 -0.04777 -0.11018 -0.07512 408 HIS A CG  
3181 N  ND1 . HIS A 408 ? 1.29602 1.11427 0.89019 -0.00823 -0.10349 -0.06548 408 HIS A ND1 
3182 C  CD2 . HIS A 408 ? 1.26450 1.12105 0.88415 -0.01732 -0.12261 -0.04459 408 HIS A CD2 
3183 C  CE1 . HIS A 408 ? 1.30579 1.12593 0.89394 0.00072  -0.11171 -0.05297 408 HIS A CE1 
3184 N  NE2 . HIS A 408 ? 1.28438 1.14667 0.88833 0.00566  -0.12579 -0.04038 408 HIS A NE2 
3185 N  N   . HIS A 409 ? 0.94326 0.82507 0.92925 -0.08954 -0.03671 -0.12287 409 HIS A N   
3186 C  CA  . HIS A 409 ? 0.88538 0.80509 0.95745 -0.12040 -0.01032 -0.12329 409 HIS A CA  
3187 C  C   . HIS A 409 ? 0.82450 0.66425 0.96380 -0.16959 -0.02536 -0.18391 409 HIS A C   
3188 O  O   . HIS A 409 ? 0.76264 0.56864 0.96488 -0.21277 -0.04366 -0.22641 409 HIS A O   
3189 C  CB  . HIS A 409 ? 0.88734 0.82962 0.97248 -0.06328 0.02521  -0.09944 409 HIS A CB  
3190 C  CG  . HIS A 409 ? 0.90945 0.85992 0.98958 -0.03567 0.07104  -0.09153 409 HIS A CG  
3191 N  ND1 . HIS A 409 ? 0.90790 0.86899 0.99689 -0.00482 0.10486  -0.08402 409 HIS A ND1 
3192 C  CD2 . HIS A 409 ? 0.92306 0.87183 0.99811 -0.02957 0.09143  -0.08726 409 HIS A CD2 
3193 C  CE1 . HIS A 409 ? 0.91494 0.87750 1.00294 0.01864  0.12133  -0.07427 409 HIS A CE1 
3194 N  NE2 . HIS A 409 ? 0.92124 0.88717 1.00454 0.01393  0.11266  -0.07570 409 HIS A NE2 
3195 C  CHA . HEM B .   ? 0.23762 0.21924 0.21551 0.02612  -0.05160 0.00708  501 HEM A CHA 
3196 C  CHB . HEM B .   ? 0.19067 0.24263 0.19120 -0.01417 -0.01343 0.00220  501 HEM A CHB 
3197 C  CHC . HEM B .   ? 0.26092 0.24913 0.17686 0.04968  0.00937  0.02281  501 HEM A CHC 
3198 C  CHD . HEM B .   ? 0.22685 0.22242 0.22832 -0.04108 -0.01781 -0.04632 501 HEM A CHD 
3199 C  C1A . HEM B .   ? 0.30369 0.18092 0.19880 0.00359  -0.03658 -0.02471 501 HEM A C1A 
3200 C  C2A . HEM B .   ? 0.23028 0.20468 0.20235 0.00277  -0.02983 -0.01852 501 HEM A C2A 
3201 C  C3A . HEM B .   ? 0.19166 0.26177 0.20519 0.02795  -0.00970 -0.02515 501 HEM A C3A 
3202 C  C4A . HEM B .   ? 0.24228 0.22172 0.20241 0.00268  0.02972  -0.00380 501 HEM A C4A 
3203 C  CMA . HEM B .   ? 0.25889 0.20303 0.21495 0.06111  -0.00490 -0.01274 501 HEM A CMA 
3204 C  CAA . HEM B .   ? 0.17788 0.23114 0.21710 -0.00737 -0.00244 -0.04655 501 HEM A CAA 
3205 C  CBA . HEM B .   ? 0.19717 0.26356 0.24875 -0.03620 -0.04854 -0.04404 501 HEM A CBA 
3206 C  CGA . HEM B .   ? 0.20027 0.28998 0.26431 -0.02168 -0.04939 -0.02835 501 HEM A CGA 
3207 O  O1A . HEM B .   ? 0.29428 0.23368 0.25275 0.00361  -0.02097 -0.00676 501 HEM A O1A 
3208 O  O2A . HEM B .   ? 0.22779 0.39201 0.32351 0.01148  -0.05007 -0.02412 501 HEM A O2A 
3209 C  C1B . HEM B .   ? 0.23011 0.21186 0.18881 -0.02202 0.02492  0.03568  501 HEM A C1B 
3210 C  C2B . HEM B .   ? 0.27572 0.18470 0.20005 0.03727  0.04467  -0.01695 501 HEM A C2B 
3211 C  C3B . HEM B .   ? 0.24240 0.20595 0.20008 0.02481  0.04333  -0.00984 501 HEM A C3B 
3212 C  C4B . HEM B .   ? 0.26853 0.21987 0.20096 0.05185  0.03197  -0.01428 501 HEM A C4B 
3213 C  CMB . HEM B .   ? 0.25454 0.18612 0.23056 0.06429  0.05804  0.04041  501 HEM A CMB 
3214 C  CAB . HEM B .   ? 0.28616 0.22465 0.21865 -0.05562 0.07819  -0.00573 501 HEM A CAB 
3215 C  CBB . HEM B .   ? 0.38173 0.33712 0.27369 -0.06749 0.04124  0.02159  501 HEM A CBB 
3216 C  C1C . HEM B .   ? 0.25978 0.22330 0.21017 0.06341  0.00138  -0.01453 501 HEM A C1C 
3217 C  C2C . HEM B .   ? 0.27656 0.22822 0.21566 0.03933  0.01792  -0.00537 501 HEM A C2C 
3218 C  C3C . HEM B .   ? 0.29110 0.20065 0.22156 -0.03895 0.01865  0.03372  501 HEM A C3C 
3219 C  C4C . HEM B .   ? 0.23885 0.21301 0.21981 -0.01116 0.00380  -0.01031 501 HEM A C4C 
3220 C  CMC . HEM B .   ? 0.28534 0.27001 0.24014 0.03268  0.01405  -0.05386 501 HEM A CMC 
3221 C  CAC . HEM B .   ? 0.39392 0.26406 0.24386 -0.01324 0.00699  0.02894  501 HEM A CAC 
3222 C  CBC . HEM B .   ? 0.43966 0.34372 0.31327 -0.02130 -0.00683 -0.03994 501 HEM A CBC 
3223 C  C1D . HEM B .   ? 0.29750 0.20257 0.23347 0.00304  -0.02192 -0.02982 501 HEM A C1D 
3224 C  C2D . HEM B .   ? 0.29622 0.20577 0.24508 0.01225  -0.02966 0.01148  501 HEM A C2D 
3225 C  C3D . HEM B .   ? 0.25580 0.23640 0.24139 -0.01443 -0.01587 0.03220  501 HEM A C3D 
3226 C  C4D . HEM B .   ? 0.20041 0.24474 0.21937 -0.05306 -0.03598 0.01642  501 HEM A C4D 
3227 C  CMD . HEM B .   ? 0.31205 0.25301 0.24549 0.07958  -0.03105 0.01906  501 HEM A CMD 
3228 C  CAD . HEM B .   ? 0.29325 0.24404 0.21896 0.00516  -0.08443 -0.01402 501 HEM A CAD 
3229 C  CBD . HEM B .   ? 0.26878 0.25494 0.23533 0.01660  -0.07605 -0.06372 501 HEM A CBD 
3230 C  CGD . HEM B .   ? 0.26098 0.29297 0.27311 0.02368  -0.06186 -0.02420 501 HEM A CGD 
3231 O  O1D . HEM B .   ? 0.29414 0.28475 0.25055 0.08756  -0.06282 -0.02489 501 HEM A O1D 
3232 O  O2D . HEM B .   ? 0.25126 0.28251 0.29633 0.01507  -0.07580 -0.02033 501 HEM A O2D 
3233 N  NA  . HEM B .   ? 0.25917 0.18005 0.20734 -0.01368 0.00841  -0.00191 501 HEM A NA  
3234 N  NB  . HEM B .   ? 0.25896 0.21585 0.18657 -0.01399 0.03556  0.01346  501 HEM A NB  
3235 N  NC  . HEM B .   ? 0.24207 0.21586 0.20629 0.03533  0.01176  0.01930  501 HEM A NC  
3236 N  ND  . HEM B .   ? 0.24926 0.20718 0.21908 -0.02813 -0.02594 -0.02566 501 HEM A ND  
3237 FE FE  . HEM B .   ? 0.24248 0.22266 0.21340 0.02391  0.00346  0.00369  501 HEM A FE  
3238 C  C1  . DIF C .   ? 0.60928 0.33992 0.53481 0.06708  -0.00211 -0.02295 502 DIF A C1  
3239 C  C2  . DIF C .   ? 0.62205 0.39080 0.55913 0.09150  0.00148  -0.08281 502 DIF A C2  
3240 CL CL2 . DIF C .   ? 0.64159 0.43946 0.60612 0.05301  0.00949  -0.14256 502 DIF A CL2 
3241 C  C3  . DIF C .   ? 0.61317 0.45367 0.53750 0.09909  -0.01687 -0.04782 502 DIF A C3  
3242 C  C4  . DIF C .   ? 0.62532 0.42240 0.49595 0.10140  -0.04451 -0.03287 502 DIF A C4  
3243 CL CL4 . DIF C .   ? 0.63831 0.47232 0.44760 0.12293  -0.09139 0.01684  502 DIF A CL4 
3244 C  C5  . DIF C .   ? 0.58027 0.34194 0.50295 0.10770  -0.02306 -0.04243 502 DIF A C5  
3245 C  C6  . DIF C .   ? 0.55139 0.24489 0.51194 0.12173  0.00724  -0.03258 502 DIF A C6  
3246 N  N1  . DIF C .   ? 0.57413 0.54012 0.55103 0.04259  -0.01322 -0.04471 502 DIF A N1  
3247 C  C7  . DIF C .   ? 0.51222 0.64831 0.53736 0.02745  0.02576  -0.12742 502 DIF A C7  
3248 C  C8  . DIF C .   ? 0.57429 0.62740 0.54626 0.01035  0.01829  -0.08935 502 DIF A C8  
3249 C  C9  . DIF C .   ? 0.57621 0.68167 0.55468 -0.00668 0.03105  -0.08619 502 DIF A C9  
3250 C  C10 . DIF C .   ? 0.57848 0.73323 0.55370 0.00258  0.05007  -0.10269 502 DIF A C10 
3251 C  C11 . DIF C .   ? 0.57403 0.73943 0.55318 -0.04053 0.04367  -0.10335 502 DIF A C11 
3252 C  C12 . DIF C .   ? 0.55780 0.71850 0.54882 -0.02607 0.01525  -0.11100 502 DIF A C12 
3253 C  C13 . DIF C .   ? 0.49153 0.63851 0.53165 0.04680  0.01148  -0.11315 502 DIF A C13 
3254 C  C14 . DIF C .   ? 0.49852 0.64343 0.51812 0.07627  0.01719  -0.12099 502 DIF A C14 
3255 O  O1  . DIF C .   ? 0.53887 0.70931 0.50532 0.07543  0.03838  -0.14262 502 DIF A O1  
3256 O  O2  . DIF C .   ? 0.51645 0.61529 0.52771 0.05302  -0.02788 -0.05743 502 DIF A O2  
3257 C  C   . TRS D .   ? 0.52784 0.83684 0.47939 0.00322  0.02836  -0.08064 503 TRS A C   
3258 C  C1  . TRS D .   ? 0.55775 0.84503 0.47765 -0.02087 0.08228  -0.07407 503 TRS A C1  
3259 C  C2  . TRS D .   ? 0.54675 0.76897 0.49075 0.02635  0.02563  -0.09379 503 TRS A C2  
3260 C  C3  . TRS D .   ? 0.54409 0.82045 0.48362 0.00097  0.01932  -0.07641 503 TRS A C3  
3261 N  N   . TRS D .   ? 0.48625 0.90165 0.48790 -0.00406 0.01333  -0.08040 503 TRS A N   
3262 O  O1  . TRS D .   ? 0.56446 0.82731 0.45983 -0.00468 0.15138  -0.08762 503 TRS A O1  
3263 O  O2  . TRS D .   ? 0.52998 0.70190 0.49591 0.06291  0.02172  -0.10693 503 TRS A O2  
3264 O  O3  . TRS D .   ? 0.50109 0.79679 0.47965 -0.01788 0.03053  -0.06349 503 TRS A O3  
3265 C  C1  . EDO E .   ? 0.80647 0.94255 0.88249 -0.13621 -0.23790 -0.08042 504 EDO A C1  
3266 O  O1  . EDO E .   ? 0.84533 1.04031 0.89477 -0.14576 -0.22103 -0.09210 504 EDO A O1  
3267 C  C2  . EDO E .   ? 0.73761 0.85505 0.87117 -0.15560 -0.26571 -0.08339 504 EDO A C2  
3268 O  O2  . EDO E .   ? 0.70277 0.78095 0.86604 -0.17217 -0.27428 -0.08141 504 EDO A O2  
3269 C  C1  . EDO F .   ? 0.79569 0.79666 0.71505 -0.19771 0.20052  -0.01775 505 EDO A C1  
3270 O  O1  . EDO F .   ? 0.82229 0.78935 0.72367 -0.17742 0.19204  0.01810  505 EDO A O1  
3271 C  C2  . EDO F .   ? 0.77461 0.79773 0.69827 -0.26424 0.20213  -0.03407 505 EDO A C2  
3272 O  O2  . EDO F .   ? 0.81587 0.77165 0.68652 -0.31375 0.18032  -0.03951 505 EDO A O2  
3273 O  O   . HOH G .   ? 0.52639 0.58904 0.46964 0.10172  0.04596  -0.09930 601 HOH A O   
3274 O  O   . HOH G .   ? 0.67091 0.33801 0.33191 0.16834  -0.04519 0.09953  602 HOH A O   
3275 O  O   . HOH G .   ? 0.68341 0.66920 0.44250 -0.15772 -0.06343 -0.15343 603 HOH A O   
3276 O  O   . HOH G .   ? 0.36677 0.48509 0.48668 0.01535  0.02761  0.04016  604 HOH A O   
3277 O  O   . HOH G .   ? 0.39275 0.56591 0.35320 -0.14697 0.08262  0.01654  605 HOH A O   
3278 O  O   . HOH G .   ? 0.73597 0.64107 0.57708 0.17949  -0.26874 -0.11387 606 HOH A O   
3279 O  O   . HOH G .   ? 0.80059 0.51557 0.54354 0.33452  0.25616  0.17543  607 HOH A O   
3280 O  O   . HOH G .   ? 0.84664 0.83374 0.56064 -0.01055 0.08283  0.10079  608 HOH A O   
3281 O  O   . HOH G .   ? 0.51986 0.38413 0.69194 -0.07195 -0.27055 0.14163  609 HOH A O   
3282 O  O   . HOH G .   ? 0.60537 0.56316 1.01913 -0.06153 0.38229  -0.11551 610 HOH A O   
3283 O  O   . HOH G .   ? 0.35611 0.60919 0.59079 0.13804  -0.06961 -0.10188 611 HOH A O   
3284 O  O   . HOH G .   ? 0.30920 0.55990 1.17372 -0.03268 -0.06513 -0.08893 612 HOH A O   
3285 O  O   . HOH G .   ? 0.56160 0.68810 0.90647 -0.22775 -0.21861 0.24488  613 HOH A O   
3286 O  O   . HOH G .   ? 0.53096 0.44883 0.34843 -0.10011 0.00148  0.07360  614 HOH A O   
3287 O  O   . HOH G .   ? 0.48868 0.48477 0.78397 0.06395  -0.15481 -0.13522 615 HOH A O   
3288 O  O   . HOH G .   ? 0.43337 0.37289 0.81298 -0.02703 -0.02967 -0.19365 616 HOH A O   
3289 O  O   . HOH G .   ? 0.66269 0.41388 0.28464 0.17352  -0.07394 -0.03689 617 HOH A O   
3290 O  O   . HOH G .   ? 0.35881 0.69255 0.55248 -0.12182 0.05119  0.17635  618 HOH A O   
3291 O  O   . HOH G .   ? 0.43581 1.02014 1.05136 0.10940  0.23325  0.33021  619 HOH A O   
3292 O  O   . HOH G .   ? 0.49176 1.04310 0.73498 0.09736  -0.16463 0.33382  620 HOH A O   
3293 O  O   . HOH G .   ? 0.58816 0.87093 0.86392 0.09579  0.05763  0.39399  621 HOH A O   
3294 O  O   . HOH G .   ? 0.61422 0.71101 0.36724 0.36049  0.06023  0.14426  622 HOH A O   
3295 O  O   . HOH G .   ? 1.05373 0.48257 0.65434 -0.23424 -0.17710 -0.02897 623 HOH A O   
3296 O  O   . HOH G .   ? 0.45088 0.24741 0.35721 0.09623  -0.16647 -0.09753 624 HOH A O   
3297 O  O   . HOH G .   ? 0.24824 0.33308 0.26473 0.03872  -0.06326 -0.00939 625 HOH A O   
3298 O  O   . HOH G .   ? 0.97367 0.59079 0.58562 0.31005  -0.09765 -0.24039 626 HOH A O   
3299 O  O   . HOH G .   ? 0.33703 0.23313 0.34041 0.08370  0.00487  0.01779  627 HOH A O   
3300 O  O   . HOH G .   ? 0.63122 0.45118 0.67643 0.07200  -0.18914 0.23449  628 HOH A O   
3301 O  O   . HOH G .   ? 0.82594 0.96797 0.28346 0.18168  0.00315  0.07468  629 HOH A O   
3302 O  O   . HOH G .   ? 0.41285 0.53886 0.29905 0.01835  0.03794  0.06252  630 HOH A O   
3303 O  O   . HOH G .   ? 0.37020 0.45184 0.51118 0.01634  0.02731  0.14785  631 HOH A O   
3304 O  O   . HOH G .   ? 0.77221 0.32493 0.91649 0.13366  0.12886  0.07929  632 HOH A O   
3305 O  O   . HOH G .   ? 0.63883 0.64417 0.90140 -0.08965 0.06367  0.41494  633 HOH A O   
3306 O  O   . HOH G .   ? 0.41337 0.44004 0.77140 0.15233  0.00537  0.18075  634 HOH A O   
3307 O  O   . HOH G .   ? 0.39422 0.77146 0.71331 -0.19013 -0.13898 0.40568  635 HOH A O   
3308 O  O   . HOH G .   ? 0.30236 0.46740 0.79097 -0.01513 0.01276  0.12824  636 HOH A O   
3309 O  O   . HOH G .   ? 0.31319 0.28457 0.71204 0.07083  0.01473  -0.03860 637 HOH A O   
3310 O  O   . HOH G .   ? 0.54429 0.32005 0.53610 0.00092  0.08230  0.03064  638 HOH A O   
3311 O  O   . HOH G .   ? 0.32735 0.31907 0.27798 0.07575  -0.00617 0.04615  639 HOH A O   
3312 O  O   . HOH G .   ? 0.75098 0.92541 0.57652 -0.11555 0.04960  -0.37377 640 HOH A O   
3313 O  O   . HOH G .   ? 0.58375 0.49084 0.59297 0.17516  0.15383  0.06676  641 HOH A O   
3314 O  O   . HOH G .   ? 0.69505 0.58596 0.92861 0.04803  0.23318  0.00591  642 HOH A O   
3315 O  O   . HOH G .   ? 0.24819 0.25900 0.28197 0.03081  -0.01979 -0.01528 643 HOH A O   
3316 O  O   . HOH G .   ? 0.73180 0.64122 0.49960 0.22379  -0.03486 -0.03966 644 HOH A O   
3317 O  O   . HOH G .   ? 0.79441 0.45745 0.42682 0.02552  0.03413  -0.02382 645 HOH A O   
3318 O  O   . HOH G .   ? 0.33365 0.29562 0.68417 0.00182  -0.06477 -0.07685 646 HOH A O   
3319 O  O   . HOH G .   ? 0.70862 0.38182 0.41022 -0.03631 0.00655  0.04132  647 HOH A O   
3320 O  O   . HOH G .   ? 0.68337 0.59754 0.70648 -0.19916 -0.28691 0.06358  648 HOH A O   
3321 O  O   . HOH G .   ? 0.30218 0.33785 0.27485 0.01108  -0.07034 0.01895  649 HOH A O   
3322 O  O   . HOH G .   ? 0.95293 0.79867 0.53111 0.08522  -0.03620 0.33274  650 HOH A O   
3323 O  O   . HOH G .   ? 0.88023 0.45111 0.39516 -0.11392 0.08135  -0.15299 651 HOH A O   
3324 O  O   . HOH G .   ? 0.43262 0.42103 0.31781 -0.07476 -0.01299 0.04701  652 HOH A O   
3325 O  O   . HOH G .   ? 1.03476 0.55375 0.52919 0.14126  0.25311  0.22374  653 HOH A O   
3326 O  O   . HOH G .   ? 0.76746 0.38607 0.55212 0.09224  0.02821  0.24105  654 HOH A O   
3327 O  O   . HOH G .   ? 0.65354 0.75288 0.52585 0.26467  0.08326  0.23779  655 HOH A O   
3328 O  O   . HOH G .   ? 0.27448 0.25572 0.25747 0.02894  -0.06084 -0.00792 656 HOH A O   
3329 O  O   . HOH G .   ? 0.89700 0.57622 0.45324 -0.20654 0.21818  -0.08452 657 HOH A O   
3330 O  O   . HOH G .   ? 0.46976 0.34014 0.28036 0.07701  -0.11330 -0.04048 658 HOH A O   
3331 O  O   . HOH G .   ? 0.80579 0.60644 0.33251 -0.33245 0.15738  -0.13046 659 HOH A O   
3332 O  O   . HOH G .   ? 0.68226 0.28553 0.28522 0.17997  -0.03459 -0.06490 660 HOH A O   
3333 O  O   . HOH G .   ? 0.61653 0.49291 0.46867 -0.21081 -0.12877 0.16075  661 HOH A O   
3334 O  O   . HOH G .   ? 0.71382 0.75998 0.91621 0.06200  0.34166  0.32474  662 HOH A O   
3335 O  O   . HOH G .   ? 0.33520 0.45007 0.82436 0.10334  0.21478  0.13366  663 HOH A O   
3336 O  O   . HOH G .   ? 0.80022 0.33830 0.48934 0.17246  -0.18998 -0.04464 664 HOH A O   
3337 O  O   . HOH G .   ? 0.43470 0.68580 0.55193 0.16198  -0.12749 0.05940  665 HOH A O   
3338 O  O   . HOH G .   ? 0.95289 0.42335 0.58522 -0.12198 -0.13489 0.19738  666 HOH A O   
3339 O  O   . HOH G .   ? 0.28595 1.11866 0.28528 0.05953  -0.00259 -0.02916 667 HOH A O   
3340 O  O   . HOH G .   ? 0.37856 0.41620 0.49168 0.06965  -0.05905 -0.01498 668 HOH A O   
3341 O  O   . HOH G .   ? 0.61110 0.35228 0.68446 -0.12971 -0.23156 0.21510  669 HOH A O   
3342 O  O   . HOH G .   ? 1.02143 0.67539 0.35314 -0.28297 -0.06258 0.03654  670 HOH A O   
3343 O  O   . HOH G .   ? 0.61682 0.36478 0.53386 0.01621  0.27686  0.05183  671 HOH A O   
3344 O  O   . HOH G .   ? 0.39877 0.62461 0.19026 0.20445  -0.01716 0.00488  672 HOH A O   
3345 O  O   . HOH G .   ? 0.68491 0.34494 0.34786 0.12180  0.07532  0.01875  673 HOH A O   
3346 O  O   . HOH G .   ? 0.68643 0.52705 0.45131 -0.15346 -0.24411 -0.03509 674 HOH A O   
3347 O  O   . HOH G .   ? 0.30895 0.31186 0.40691 -0.04233 -0.00875 -0.00387 675 HOH A O   
3348 O  O   . HOH G .   ? 0.72684 0.59131 0.35224 0.33852  -0.00627 0.00636  676 HOH A O   
3349 O  O   . HOH G .   ? 0.20691 0.28143 0.19925 -0.01572 0.02260  0.00853  677 HOH A O   
3350 O  O   . HOH G .   ? 0.41733 0.41422 0.61704 0.11371  -0.13652 -0.04935 678 HOH A O   
3351 O  O   . HOH G .   ? 0.63104 0.44327 0.69577 -0.01839 -0.30249 0.10521  679 HOH A O   
3352 O  O   . HOH G .   ? 0.63575 0.77767 0.43670 -0.26428 -0.07988 0.10332  680 HOH A O   
3353 O  O   . HOH G .   ? 0.69840 0.51901 0.89223 0.18849  0.23714  0.33683  681 HOH A O   
3354 O  O   . HOH G .   ? 0.45012 0.41619 0.54285 -0.01358 0.08387  0.09755  682 HOH A O   
3355 O  O   . HOH G .   ? 0.44343 0.62352 0.27730 -0.05668 -0.05072 0.13561  683 HOH A O   
3356 O  O   . HOH G .   ? 0.37206 0.29876 0.50838 -0.06407 -0.04751 0.07857  684 HOH A O   
3357 O  O   . HOH G .   ? 0.88528 0.41822 0.48300 -0.03534 -0.01593 -0.06256 685 HOH A O   
3358 O  O   . HOH G .   ? 1.09692 0.34876 0.35370 0.15916  0.05910  -0.03551 686 HOH A O   
3359 O  O   . HOH G .   ? 0.40327 0.35122 0.71337 -0.06024 0.00858  0.11879  687 HOH A O   
3360 O  O   . HOH G .   ? 1.00077 0.62603 0.45678 -0.42856 -0.12412 0.02330  688 HOH A O   
3361 O  O   . HOH G .   ? 0.43852 0.47095 1.14109 0.08546  0.25450  0.26620  689 HOH A O   
3362 O  O   . HOH G .   ? 0.89660 0.31004 0.61188 0.03734  -0.30713 -0.06953 690 HOH A O   
3363 O  O   . HOH G .   ? 0.26485 0.24450 0.26281 -0.01156 -0.01623 -0.02369 691 HOH A O   
3364 O  O   . HOH G .   ? 0.44822 0.30484 0.39520 0.02462  -0.10546 -0.04725 692 HOH A O   
3365 O  O   . HOH G .   ? 0.52017 0.63002 0.69454 0.03032  0.33954  0.00913  693 HOH A O   
3366 O  O   . HOH G .   ? 0.27951 0.25048 0.28561 0.07226  -0.04187 -0.04190 694 HOH A O   
3367 O  O   . HOH G .   ? 0.45628 1.10000 0.35751 0.19750  -0.07167 0.05993  695 HOH A O   
3368 O  O   . HOH G .   ? 0.36252 0.35012 0.37455 -0.02270 -0.05554 0.03190  696 HOH A O   
3369 O  O   . HOH G .   ? 0.26914 0.29951 0.26403 0.00747  0.00845  -0.04264 697 HOH A O   
3370 O  O   . HOH G .   ? 0.39534 0.73415 0.47835 -0.07221 -0.05624 -0.07002 698 HOH A O   
3371 O  O   . HOH G .   ? 0.72391 0.59858 0.82436 -0.07051 0.01210  0.18247  699 HOH A O   
3372 O  O   . HOH G .   ? 0.42982 0.43428 0.33742 0.13742  -0.05070 -0.05756 700 HOH A O   
3373 O  O   . HOH G .   ? 1.14063 0.33814 0.29915 -0.03618 0.00019  -0.01979 701 HOH A O   
3374 O  O   . HOH G .   ? 0.62898 0.40989 0.58192 0.08867  -0.05091 -0.18179 702 HOH A O   
3375 O  O   . HOH G .   ? 0.70074 0.40012 0.45601 0.07018  -0.21986 -0.01932 703 HOH A O   
3376 O  O   . HOH G .   ? 0.58116 0.55433 0.39765 -0.19433 0.08266  0.07365  704 HOH A O   
3377 O  O   . HOH G .   ? 0.28618 0.44455 0.26243 0.00017  -0.05806 -0.03104 705 HOH A O   
3378 O  O   . HOH G .   ? 0.74903 0.45558 0.46786 0.18746  -0.03992 -0.04637 706 HOH A O   
3379 O  O   . HOH G .   ? 0.80421 0.40964 0.62185 0.09997  -0.06162 0.04623  707 HOH A O   
3380 O  O   A HOH G .   ? 0.31794 0.33048 0.36123 -0.00042 -0.12445 0.09066  708 HOH A O   
3381 O  O   B HOH G .   ? 0.27658 0.31238 0.50746 0.09105  -0.07391 -0.12978 708 HOH A O   
3382 O  O   . HOH G .   ? 0.69493 0.36253 0.57637 0.07758  -0.32211 -0.14988 709 HOH A O   
3383 O  O   . HOH G .   ? 0.37684 0.21760 0.45560 0.02641  -0.05737 0.01888  710 HOH A O   
3384 O  O   . HOH G .   ? 0.46991 0.67920 0.54624 0.04745  -0.15497 0.12130  711 HOH A O   
3385 O  O   . HOH G .   ? 0.76748 0.35100 0.48655 -0.07202 -0.12852 -0.04233 712 HOH A O   
3386 O  O   . HOH G .   ? 0.83116 0.96868 0.56379 0.23250  -0.01191 -0.16377 713 HOH A O   
3387 O  O   . HOH G .   ? 0.27222 0.27805 0.21284 0.00085  0.01155  -0.00374 714 HOH A O   
3388 O  O   . HOH G .   ? 0.45947 0.38763 0.44695 0.02771  -0.06864 -0.02822 715 HOH A O   
3389 O  O   . HOH G .   ? 0.31714 0.30390 0.30328 -0.01251 0.06143  0.04399  716 HOH A O   
3390 O  O   . HOH G .   ? 0.59458 0.56993 1.11343 0.21866  -0.27265 -0.02561 717 HOH A O   
3391 O  O   . HOH G .   ? 0.29337 0.34724 0.28052 0.01583  -0.03247 -0.00753 718 HOH A O   
3392 O  O   . HOH G .   ? 0.44559 0.54365 0.25788 0.13649  -0.13620 -0.12374 719 HOH A O   
3393 O  O   . HOH G .   ? 0.47741 0.27470 0.36115 0.02174  0.13390  0.03101  720 HOH A O   
3394 O  O   . HOH G .   ? 0.31510 0.29966 0.24386 -0.00084 0.02565  0.04656  721 HOH A O   
3395 O  O   . HOH G .   ? 0.59998 0.46218 0.23276 0.11353  0.02563  -0.02035 722 HOH A O   
3396 O  O   . HOH G .   ? 0.62077 0.88038 0.43865 0.32433  0.08339  0.25811  723 HOH A O   
3397 O  O   . HOH G .   ? 0.73714 0.32271 0.42997 -0.00799 -0.16807 -0.06847 724 HOH A O   
3398 O  O   . HOH G .   ? 0.17496 0.23135 0.19655 -0.00147 0.00162  0.01368  725 HOH A O   
3399 O  O   . HOH G .   ? 0.25149 0.21289 0.21369 -0.02425 0.02253  -0.01923 726 HOH A O   
3400 O  O   . HOH G .   ? 0.49094 0.95682 0.60980 -0.00085 -0.10841 0.10206  727 HOH A O   
3401 O  O   . HOH G .   ? 0.60931 0.39895 0.32079 0.11970  0.02394  -0.07775 728 HOH A O   
3402 O  O   . HOH G .   ? 0.30351 0.35821 0.41580 -0.06279 -0.00628 -0.01680 729 HOH A O   
3403 O  O   . HOH G .   ? 0.58363 0.28906 0.53987 -0.09094 0.00408  0.08928  730 HOH A O   
3404 O  O   . HOH G .   ? 0.59273 0.55632 0.51716 0.12359  -0.17020 -0.23539 731 HOH A O   
3405 O  O   . HOH G .   ? 0.47822 0.73128 0.38327 -0.11022 -0.00902 0.03269  732 HOH A O   
3406 O  O   . HOH G .   ? 0.29301 0.26512 0.35933 0.02091  -0.04454 -0.04797 733 HOH A O   
3407 O  O   . HOH G .   ? 0.60542 0.68981 0.50969 0.18826  -0.27029 -0.19344 734 HOH A O   
3408 O  O   . HOH G .   ? 0.55550 0.68087 0.47295 -0.22729 -0.12935 -0.05596 735 HOH A O   
3409 O  O   . HOH G .   ? 0.54478 0.42241 0.31891 -0.03173 -0.03281 0.00879  736 HOH A O   
3410 O  O   . HOH G .   ? 0.96305 0.67976 0.31297 -0.03227 0.11171  -0.01292 737 HOH A O   
3411 O  O   . HOH G .   ? 0.45606 0.33862 0.38249 -0.03809 -0.02589 0.09806  738 HOH A O   
3412 O  O   . HOH G .   ? 0.56164 0.48713 0.38509 0.01442  -0.08340 -0.05793 739 HOH A O   
3413 O  O   . HOH G .   ? 0.80332 0.49037 0.62491 0.15591  -0.05795 0.18372  740 HOH A O   
3414 O  O   . HOH G .   ? 0.48405 0.34070 0.28734 0.02603  0.03748  0.07357  741 HOH A O   
3415 O  O   . HOH G .   ? 0.54391 0.54542 0.51532 0.15304  0.16069  -0.00304 742 HOH A O   
3416 O  O   . HOH G .   ? 0.33799 0.55658 0.39691 0.07234  0.09375  -0.00826 743 HOH A O   
3417 O  O   . HOH G .   ? 0.66772 0.30578 0.64104 0.09779  0.21403  -0.01355 744 HOH A O   
3418 O  O   . HOH G .   ? 0.60012 0.46969 0.42293 -0.05490 -0.16415 0.10088  745 HOH A O   
3419 O  O   . HOH G .   ? 0.94746 0.39789 0.54608 -0.21461 -0.12748 0.16258  746 HOH A O   
3420 O  O   . HOH G .   ? 0.63783 0.41829 0.32223 -0.03601 -0.00584 0.09550  747 HOH A O   
3421 O  O   . HOH G .   ? 0.57692 0.74719 0.85833 -0.02281 0.09794  0.15154  748 HOH A O   
3422 O  O   . HOH G .   ? 0.51566 0.66242 0.71514 -0.18867 -0.24990 0.12376  749 HOH A O   
3423 O  O   . HOH G .   ? 0.20856 0.56674 0.80736 0.02674  0.00016  0.05014  750 HOH A O   
3424 O  O   . HOH G .   ? 0.31725 0.43720 0.23736 -0.10383 -0.00189 0.04994  751 HOH A O   
3425 O  O   . HOH G .   ? 0.29250 0.33304 0.32936 -0.00713 -0.05121 -0.05093 752 HOH A O   
3426 O  O   . HOH G .   ? 0.55608 0.98926 0.53171 0.09005  -0.17853 -0.32300 753 HOH A O   
3427 O  O   . HOH G .   ? 0.84683 0.40466 0.41704 -0.17412 0.03694  0.00531  754 HOH A O   
3428 O  O   . HOH G .   ? 0.31386 0.77998 0.44933 0.18630  -0.10977 -0.06964 755 HOH A O   
3429 O  O   . HOH G .   ? 0.55729 0.36989 0.50015 0.03644  0.22303  0.00462  756 HOH A O   
3430 O  O   . HOH G .   ? 0.57451 0.77350 1.05764 -0.03195 0.12439  -0.29275 757 HOH A O   
3431 O  O   . HOH G .   ? 0.30770 0.34506 0.40389 0.00427  -0.05118 -0.04722 758 HOH A O   
3432 O  O   . HOH G .   ? 0.89636 0.37875 0.58191 -0.14484 -0.20677 -0.02236 759 HOH A O   
3433 O  O   . HOH G .   ? 1.04628 0.38248 0.41151 -0.09482 0.02432  0.01804  760 HOH A O   
3434 O  O   . HOH G .   ? 0.36305 0.32279 0.28458 -0.03878 0.00291  -0.03398 761 HOH A O   
3435 O  O   . HOH G .   ? 0.75391 0.25178 0.50333 -0.13170 -0.15897 0.05892  762 HOH A O   
3436 O  O   . HOH G .   ? 0.59427 0.48870 0.36003 0.25411  -0.05407 -0.13832 763 HOH A O   
3437 O  O   . HOH G .   ? 0.36584 0.48056 0.86297 0.12466  -0.22473 -0.27642 764 HOH A O   
3438 O  O   . HOH G .   ? 0.46636 0.47277 0.60819 0.04408  -0.02339 -0.04037 765 HOH A O   
3439 O  O   . HOH G .   ? 0.50013 0.35139 0.39301 0.00085  0.03772  0.04450  766 HOH A O   
3440 O  O   . HOH G .   ? 0.49684 0.29015 0.26119 0.08333  0.01186  0.00471  767 HOH A O   
3441 O  O   . HOH G .   ? 0.64748 0.49602 0.57345 -0.23599 -0.13987 0.23057  768 HOH A O   
3442 O  O   . HOH G .   ? 0.40634 0.24543 0.23540 0.00274  -0.02481 -0.03536 769 HOH A O   
3443 O  O   . HOH G .   ? 0.34160 0.22805 0.19770 0.01626  -0.03009 0.03207  770 HOH A O   
3444 O  O   . HOH G .   ? 0.56799 0.79397 0.47619 -0.08382 0.04845  0.13606  771 HOH A O   
3445 O  O   . HOH G .   ? 0.44571 0.47360 0.30946 -0.14607 0.00335  -0.00726 772 HOH A O   
3446 O  O   . HOH G .   ? 0.42688 0.35870 0.52911 0.08195  -0.03449 -0.05983 773 HOH A O   
3447 O  O   . HOH G .   ? 0.32449 0.78874 0.51979 0.16653  0.10805  0.34707  774 HOH A O   
3448 O  O   . HOH G .   ? 0.43700 0.71219 0.64837 0.13658  -0.06380 0.17884  775 HOH A O   
3449 O  O   . HOH G .   ? 0.46169 0.66263 0.28898 -0.02851 0.03983  0.00779  776 HOH A O   
3450 O  O   . HOH G .   ? 0.62227 0.50317 0.30865 -0.03351 -0.02792 0.01651  777 HOH A O   
3451 O  O   . HOH G .   ? 0.43222 0.45501 0.28583 -0.00819 0.02262  0.08805  778 HOH A O   
3452 O  O   . HOH G .   ? 0.33153 0.28184 0.28980 0.00979  0.03781  0.04094  779 HOH A O   
3453 O  O   . HOH G .   ? 0.46605 0.49030 0.67236 -0.20836 0.20236  -0.18132 780 HOH A O   
3454 O  O   . HOH G .   ? 0.43502 0.38730 0.37090 0.03880  -0.20963 -0.02736 781 HOH A O   
3455 O  O   . HOH G .   ? 0.83093 0.37646 0.42744 0.18540  -0.25058 -0.13998 782 HOH A O   
3456 O  O   . HOH G .   ? 0.32157 0.76565 0.41386 0.06135  -0.04706 -0.24925 783 HOH A O   
3457 O  O   . HOH G .   ? 0.50412 0.97564 0.35587 0.15317  -0.12599 -0.07022 784 HOH A O   
3458 O  O   . HOH G .   ? 0.39713 0.25089 0.30886 -0.01170 -0.10423 0.09044  785 HOH A O   
3459 O  O   . HOH G .   ? 0.96737 0.51857 0.31129 0.15616  -0.00308 0.04584  786 HOH A O   
3460 O  O   . HOH G .   ? 0.96156 0.39626 1.06906 0.20996  0.06168  -0.18275 787 HOH A O   
3461 O  O   . HOH G .   ? 0.78628 0.56722 0.75138 0.00374  -0.15924 -0.00139 788 HOH A O   
3462 O  O   . HOH G .   ? 0.37551 0.32987 0.36400 -0.06720 -0.10732 0.04448  789 HOH A O   
3463 O  O   . HOH G .   ? 0.47963 0.51864 0.49588 0.03914  -0.16582 -0.16044 790 HOH A O   
3464 O  O   . HOH G .   ? 0.41235 1.15917 0.34139 0.08681  -0.02980 0.14381  791 HOH A O   
3465 O  O   . HOH G .   ? 0.50485 0.35954 1.00891 -0.13655 -0.05897 0.14712  792 HOH A O   
3466 O  O   . HOH G .   ? 0.61236 0.43500 0.46815 -0.14205 0.15747  -0.09468 793 HOH A O   
3467 O  O   . HOH G .   ? 0.71416 0.78453 0.61101 0.02296  0.04283  0.17138  794 HOH A O   
3468 O  O   . HOH G .   ? 0.99629 0.52258 0.28857 0.22561  0.01254  0.05708  795 HOH A O   
3469 O  O   . HOH G .   ? 0.53287 0.39872 0.38039 0.23084  -0.01134 -0.05097 796 HOH A O   
3470 O  O   . HOH G .   ? 0.69796 0.86526 0.33498 0.01299  0.16571  -0.03073 797 HOH A O   
3471 O  O   . HOH G .   ? 0.32035 0.31121 0.33589 -0.00091 -0.07649 -0.05293 798 HOH A O   
3472 O  O   . HOH G .   ? 0.79004 0.53262 0.32170 -0.00886 0.15456  -0.04337 799 HOH A O   
3473 O  O   . HOH G .   ? 0.56652 0.30302 0.29881 0.14384  -0.11695 -0.05519 800 HOH A O   
3474 O  O   . HOH G .   ? 1.12111 0.31422 0.46353 0.09369  0.12345  0.06056  801 HOH A O   
3475 O  O   . HOH G .   ? 0.73283 0.39627 0.54190 0.07577  -0.12023 -0.09897 802 HOH A O   
3476 O  O   . HOH G .   ? 0.66471 0.73522 0.48704 -0.04102 -0.09069 0.19478  803 HOH A O   
3477 O  O   . HOH G .   ? 0.53502 0.61682 0.43263 0.21322  -0.13604 -0.22794 804 HOH A O   
3478 O  O   . HOH G .   ? 0.35121 0.51401 0.97119 -0.09208 -0.14398 0.19501  805 HOH A O   
3479 O  O   . HOH G .   ? 1.16376 0.48605 0.53549 0.11166  0.14681  0.15317  806 HOH A O   
3480 O  O   . HOH G .   ? 0.53950 1.21913 0.56690 -0.17146 -0.01490 0.19612  807 HOH A O   
3481 O  O   . HOH G .   ? 0.61265 0.23242 0.63862 0.03609  -0.13876 -0.04735 808 HOH A O   
3482 O  O   . HOH G .   ? 0.66532 0.32539 1.06503 -0.11596 -0.05832 -0.10650 809 HOH A O   
3483 O  O   . HOH G .   ? 0.69949 0.34438 0.99431 -0.02108 0.48543  -0.02743 810 HOH A O   
3484 O  O   . HOH G .   ? 0.67873 0.45157 0.48161 -0.04742 0.07533  0.14574  811 HOH A O   
3485 O  O   . HOH G .   ? 0.47416 0.34012 0.49158 0.15540  0.07785  0.01688  812 HOH A O   
3486 O  O   . HOH G .   ? 0.65061 0.45589 0.34187 -0.01921 -0.04772 -0.02902 813 HOH A O   
3487 O  O   . HOH G .   ? 0.89795 0.56770 0.37757 -0.39972 0.02006  -0.02544 814 HOH A O   
3488 O  O   . HOH G .   ? 0.85225 0.39391 0.36763 -0.04510 -0.01176 0.04328  815 HOH A O   
3489 O  O   . HOH G .   ? 1.16906 0.51956 0.54757 -0.16154 0.10926  -0.15323 816 HOH A O   
3490 O  O   . HOH G .   ? 0.37814 0.95264 0.89197 -0.12903 -0.00131 0.38952  817 HOH A O   
3491 O  O   . HOH G .   ? 0.82182 0.82791 0.46194 0.41426  -0.13043 -0.23067 818 HOH A O   
3492 O  O   . HOH G .   ? 0.35111 0.47833 0.81095 -0.03440 -0.16993 -0.17461 819 HOH A O   
3493 O  O   . HOH G .   ? 0.52017 0.62702 0.52135 -0.10952 0.04619  -0.05354 820 HOH A O   
3494 O  O   . HOH G .   ? 1.31289 0.62360 0.39139 0.14317  0.03524  -0.11491 821 HOH A O   
3495 O  O   . HOH G .   ? 0.28243 0.22186 0.21891 -0.00427 0.00280  0.00067  822 HOH A O   
3496 O  O   . HOH G .   ? 0.94089 0.68527 0.33592 0.09554  0.09684  -0.04006 823 HOH A O   
3497 O  O   . HOH G .   ? 0.70306 0.46124 0.39729 0.21310  0.04448  -0.08190 824 HOH A O   
3498 O  O   . HOH G .   ? 0.58246 0.39513 0.24626 0.17476  -0.06400 -0.01637 825 HOH A O   
3499 O  O   . HOH G .   ? 0.66723 0.80967 0.51555 -0.06917 0.16616  -0.27773 826 HOH A O   
3500 O  O   . HOH G .   ? 0.42192 0.51115 1.27465 0.13200  0.04125  0.05324  827 HOH A O   
3501 O  O   . HOH G .   ? 0.34671 0.72678 0.66462 -0.11744 -0.20732 0.19016  828 HOH A O   
3502 O  O   . HOH G .   ? 0.59175 0.55355 0.40414 0.20673  0.03227  0.09375  829 HOH A O   
3503 O  O   . HOH G .   ? 0.80253 0.64265 0.39633 -0.25577 -0.14075 -0.00694 830 HOH A O   
3504 O  O   . HOH G .   ? 0.65217 0.56721 0.63475 -0.01688 -0.00591 0.06736  831 HOH A O   
3505 O  O   . HOH G .   ? 0.49513 0.53909 0.64621 -0.12064 -0.02759 -0.19078 832 HOH A O   
3506 O  O   . HOH G .   ? 1.10728 0.38072 0.32093 -0.16096 -0.08023 0.02972  833 HOH A O   
3507 O  O   . HOH G .   ? 0.91000 0.95613 0.64748 0.26658  0.23492  0.20999  834 HOH A O   
3508 O  O   . HOH G .   ? 0.54975 0.46485 0.65832 0.00363  -0.05256 -0.17647 835 HOH A O   
3509 O  O   . HOH G .   ? 0.60823 0.57256 1.28019 -0.04243 0.28562  -0.11385 836 HOH A O   
3510 O  O   . HOH G .   ? 0.40755 0.75367 0.72473 0.10149  -0.08032 -0.16541 837 HOH A O   
3511 O  O   . HOH G .   ? 0.71211 0.37324 0.80876 -0.04788 -0.29219 0.02161  838 HOH A O   
3512 O  O   . HOH G .   ? 0.80410 0.49937 0.74258 0.31471  -0.03249 -0.03434 839 HOH A O   
3513 O  O   . HOH G .   ? 0.61401 0.55670 0.26865 -0.09638 0.03957  0.01005  840 HOH A O   
3514 O  O   . HOH G .   ? 0.60612 1.15630 0.40325 -0.21337 0.07135  -0.14211 841 HOH A O   
3515 O  O   . HOH G .   ? 0.98078 0.25880 0.64468 0.01295  0.07480  -0.05694 842 HOH A O   
3516 O  O   . HOH G .   ? 0.51577 0.35858 0.37407 -0.00450 0.10717  0.05099  843 HOH A O   
3517 O  O   . HOH G .   ? 0.58864 0.55886 0.72144 -0.20408 -0.14305 -0.23412 844 HOH A O   
3518 O  O   . HOH G .   ? 0.68532 0.98842 0.43592 0.07168  -0.11342 -0.10563 845 HOH A O   
3519 O  O   . HOH G .   ? 0.44618 0.59778 0.76131 0.02536  0.11166  -0.01932 846 HOH A O   
3520 O  O   . HOH G .   ? 0.47941 1.24432 0.33634 -0.10462 0.05766  -0.04409 847 HOH A O   
3521 O  O   . HOH G .   ? 1.13478 0.85462 0.52089 -0.24008 0.28042  0.04293  848 HOH A O   
3522 O  O   . HOH G .   ? 0.80017 0.51731 0.39200 0.10487  0.00361  -0.05631 849 HOH A O   
3523 O  O   . HOH G .   ? 0.61857 0.86960 0.60177 -0.06506 -0.00271 -0.14846 850 HOH A O   
3524 O  O   . HOH G .   ? 0.75288 0.60395 0.58407 -0.22704 0.07335  0.11191  851 HOH A O   
3525 O  O   . HOH G .   ? 0.70235 0.58078 0.31736 -0.09622 0.02883  -0.02371 852 HOH A O   
3526 O  O   . HOH G .   ? 0.35572 0.67041 0.55558 -0.11120 0.05677  -0.20921 853 HOH A O   
3527 O  O   . HOH G .   ? 0.76862 0.51613 0.53404 -0.34781 0.12192  -0.10239 854 HOH A O   
3528 O  O   . HOH G .   ? 0.56776 0.45426 0.37791 0.12070  0.03550  -0.05066 855 HOH A O   
3529 O  O   . HOH G .   ? 1.18947 0.54553 0.55639 0.29065  0.33719  0.04450  856 HOH A O   
3530 O  O   . HOH G .   ? 0.49805 0.40344 0.37527 0.04745  0.03728  0.05144  857 HOH A O   
3531 O  O   . HOH G .   ? 0.56969 0.49551 0.71419 0.11900  -0.25836 -0.30073 858 HOH A O   
3532 O  O   . HOH G .   ? 0.87126 0.66413 0.45409 0.11432  0.01695  0.11585  859 HOH A O   
3533 O  O   . HOH G .   ? 0.63073 0.48139 0.57391 0.10270  0.33450  0.03437  860 HOH A O   
3534 O  O   . HOH G .   ? 0.54687 0.32462 0.59020 -0.02823 0.08679  0.08270  861 HOH A O   
3535 O  O   . HOH G .   ? 0.88571 0.59027 0.41814 0.23621  -0.06350 0.07764  862 HOH A O   
3536 O  O   . HOH G .   ? 0.29719 0.31841 0.43713 -0.01987 -0.04664 0.07191  863 HOH A O   
3537 O  O   . HOH G .   ? 0.51883 0.53587 0.38360 -0.17832 -0.17488 0.07867  864 HOH A O   
3538 O  O   . HOH G .   ? 0.33723 0.87126 0.40747 -0.13351 -0.10381 0.25484  865 HOH A O   
3539 O  O   . HOH G .   ? 0.34775 0.50790 0.58047 0.05080  -0.03202 0.00437  866 HOH A O   
3540 O  O   . HOH G .   ? 0.71293 0.82871 0.76832 -0.05798 -0.10781 -0.14775 867 HOH A O   
3541 O  O   . HOH G .   ? 0.48877 0.54179 0.61402 0.23936  0.10903  0.11081  868 HOH A O   
3542 O  O   . HOH G .   ? 0.57881 0.46512 0.65400 -0.14037 -0.04505 0.10027  869 HOH A O   
3543 O  O   . HOH G .   ? 0.55875 0.98151 0.78918 -0.00742 -0.26377 0.00635  870 HOH A O   
3544 O  O   . HOH G .   ? 0.51357 0.25328 0.41263 -0.04529 -0.24520 0.07133  871 HOH A O   
3545 O  O   . HOH G .   ? 0.71786 0.72904 0.56101 -0.01140 -0.03431 -0.00380 872 HOH A O   
3546 O  O   . HOH G .   ? 0.49551 0.79866 0.96090 -0.26833 0.09950  0.21557  873 HOH A O   
3547 O  O   . HOH G .   ? 0.72075 0.60630 0.69099 -0.26768 0.24168  -0.27024 874 HOH A O   
3548 O  O   . HOH G .   ? 0.44698 0.55997 1.35424 -0.01128 -0.18961 -0.00500 875 HOH A O   
3549 O  O   . HOH G .   ? 0.80392 0.91460 0.94782 0.14009  0.50039  0.00147  876 HOH A O   
3550 O  O   . HOH G .   ? 0.54045 0.73567 0.98499 -0.01945 -0.29452 -0.30500 877 HOH A O   
3551 O  O   . HOH G .   ? 1.04132 0.51280 0.35878 -0.16551 -0.14414 0.09631  878 HOH A O   
3552 O  O   . HOH G .   ? 0.77369 0.52642 0.45496 -0.17051 0.12446  -0.06447 879 HOH A O   
3553 O  O   . HOH G .   ? 0.70359 0.76110 0.75020 0.07993  0.02322  0.19059  880 HOH A O   
3554 O  O   . HOH G .   ? 0.67655 0.81645 0.48134 0.10932  0.06762  -0.05455 881 HOH A O   
3555 O  O   . HOH G .   ? 1.04440 0.63313 0.52254 0.09123  0.17685  -0.24658 882 HOH A O   
3556 O  O   . HOH G .   ? 0.22704 0.29046 0.26906 -0.03938 0.00442  -0.00358 883 HOH A O   
3557 O  O   . HOH G .   ? 0.93063 0.83859 0.52451 0.01871  -0.13810 -0.01811 884 HOH A O   
3558 O  O   . HOH G .   ? 1.05572 0.73565 0.87050 -0.18450 0.46550  0.08888  885 HOH A O   
3559 O  O   . HOH G .   ? 0.85281 0.76381 0.69449 0.22721  -0.20156 -0.13164 886 HOH A O   
3560 O  O   . HOH G .   ? 0.80766 0.72132 0.98490 -0.03923 0.25212  0.07003  887 HOH A O   
3561 O  O   . HOH G .   ? 0.99604 0.52789 0.44922 -0.09119 -0.10782 -0.10581 888 HOH A O   
3562 O  O   . HOH G .   ? 0.57606 0.75031 0.64745 0.10147  0.27805  0.28206  889 HOH A O   
3563 O  O   . HOH G .   ? 0.50892 0.30866 0.72021 0.07777  0.00347  0.02884  890 HOH A O   
3564 O  O   . HOH G .   ? 0.60119 0.48741 0.44509 -0.08190 0.09829  -0.15432 891 HOH A O   
3565 O  O   . HOH G .   ? 0.85039 0.46717 0.34806 0.22163  -0.09068 -0.02854 892 HOH A O   
3566 O  O   . HOH G .   ? 0.48936 0.53883 1.16471 -0.19076 -0.10167 0.04554  893 HOH A O   
3567 O  O   . HOH G .   ? 0.69803 0.81784 0.61874 0.09564  0.02460  0.00797  894 HOH A O   
3568 O  O   . HOH G .   ? 0.53066 0.58162 0.55620 -0.00268 -0.24137 -0.08131 895 HOH A O   
3569 O  O   . HOH G .   ? 0.85572 0.54369 0.55447 -0.03060 -0.38568 -0.04315 896 HOH A O   
3570 O  O   . HOH G .   ? 0.75487 0.61601 0.84240 0.12066  -0.02168 0.11876  897 HOH A O   
3571 O  O   . HOH G .   ? 0.57699 0.97349 0.59627 0.30843  0.08965  0.01160  898 HOH A O   
3572 O  O   . HOH G .   ? 0.52714 0.54570 0.54915 -0.00401 -0.21455 -0.13295 899 HOH A O   
3573 O  O   . HOH G .   ? 0.55783 0.42953 0.86939 0.13910  0.08756  0.07002  900 HOH A O   
3574 O  O   . HOH G .   ? 0.57016 0.46523 0.30037 0.25355  -0.01682 -0.00085 901 HOH A O   
3575 O  O   . HOH G .   ? 0.68554 0.71268 0.85111 0.22946  -0.14707 0.15528  902 HOH A O   
3576 O  O   . HOH G .   ? 0.73799 0.46387 0.32249 -0.19618 0.03337  0.01289  903 HOH A O   
3577 O  O   . HOH G .   ? 0.49993 0.44557 0.26855 0.08314  -0.05765 0.02752  904 HOH A O   
3578 O  O   . HOH G .   ? 0.53333 0.51657 0.46032 0.03236  -0.07309 0.13268  905 HOH A O   
3579 O  O   . HOH G .   ? 0.69585 1.32461 0.56236 -0.03018 0.18333  0.02544  906 HOH A O   
3580 O  O   . HOH G .   ? 0.51756 0.49961 0.36758 0.18535  0.08625  0.03610  907 HOH A O   
3581 O  O   . HOH G .   ? 0.62366 0.51238 0.50188 0.07836  -0.25162 -0.09641 908 HOH A O   
3582 O  O   . HOH G .   ? 0.53759 0.68649 0.46080 0.04945  0.04289  -0.15935 909 HOH A O   
3583 O  O   . HOH G .   ? 0.50034 0.93032 0.65703 -0.17017 0.03379  -0.19583 910 HOH A O   
3584 O  O   . HOH G .   ? 0.63933 0.95544 0.48063 -0.31406 0.15729  0.05648  911 HOH A O   
3585 O  O   . HOH G .   ? 1.05298 0.73267 0.53130 0.30223  0.11815  0.27450  912 HOH A O   
3586 O  O   . HOH G .   ? 0.69099 0.65952 0.53662 -0.08627 0.16111  0.11829  913 HOH A O   
3587 O  O   . HOH G .   ? 0.55391 0.50240 0.59895 0.18083  0.30816  0.17565  914 HOH A O   
3588 O  O   . HOH G .   ? 0.62358 0.42106 0.69195 0.17674  -0.07086 -0.07645 915 HOH A O   
3589 O  O   . HOH G .   ? 0.46995 0.52106 0.81859 0.14912  -0.13044 0.01202  916 HOH A O   
3590 O  O   . HOH G .   ? 0.61704 0.83751 1.06415 0.03536  -0.01135 0.40586  917 HOH A O   
3591 O  O   . HOH G .   ? 0.63409 0.63589 0.39087 0.15273  -0.12564 0.07595  918 HOH A O   
3592 O  O   . HOH G .   ? 0.51710 0.53323 0.43691 -0.12802 -0.12787 -0.05875 919 HOH A O   
3593 O  O   . HOH G .   ? 0.50894 0.62766 0.56409 -0.03069 -0.05481 0.09012  920 HOH A O   
3594 O  O   . HOH G .   ? 0.94380 0.81575 0.35593 0.00808  -0.08776 -0.03720 921 HOH A O   
3595 O  O   . HOH G .   ? 0.64745 0.65686 0.67267 -0.01802 -0.05498 -0.17091 922 HOH A O   
3596 O  O   . HOH G .   ? 0.75268 0.66794 1.04697 -0.03567 0.25895  0.04423  923 HOH A O   
3597 O  O   . HOH G .   ? 0.76628 0.64597 0.55270 -0.17262 -0.16092 0.11867  924 HOH A O   
3598 O  O   . HOH G .   ? 0.35202 0.38338 0.55839 0.01577  0.01750  0.03119  925 HOH A O   
3599 O  O   . HOH G .   ? 0.59251 0.48357 0.60714 0.12029  -0.00129 -0.10711 926 HOH A O   
3600 O  O   . HOH G .   ? 0.59313 0.71635 0.90802 -0.10578 -0.05295 0.32315  927 HOH A O   
3601 O  O   . HOH G .   ? 0.73585 0.60252 0.55469 0.15128  0.25733  0.27091  928 HOH A O   
3602 O  O   . HOH G .   ? 0.46030 0.91823 0.62556 -0.05689 0.19579  -0.12913 929 HOH A O   
3603 O  O   . HOH G .   ? 0.64409 0.81019 0.69397 0.12212  0.05032  -0.08570 930 HOH A O   
3604 O  O   . HOH G .   ? 0.41040 0.67174 0.99214 0.07946  -0.15729 -0.42662 931 HOH A O   
3605 O  O   . HOH G .   ? 0.56513 0.25793 0.50589 0.01700  -0.03478 -0.06541 932 HOH A O   
3606 O  O   . HOH G .   ? 0.51904 0.78308 0.47074 0.04561  0.01818  0.13881  933 HOH A O   
3607 O  O   . HOH G .   ? 0.64728 0.63519 0.58362 0.13976  -0.32334 -0.02440 934 HOH A O   
3608 O  O   . HOH G .   ? 0.83078 0.75768 0.94107 -0.02891 0.28910  -0.05011 935 HOH A O   
3609 O  O   . HOH G .   ? 0.74238 0.63235 0.45413 0.06199  -0.11140 0.10696  936 HOH A O   
3610 O  O   . HOH G .   ? 1.07557 0.74467 0.36205 0.42700  -0.06796 -0.07953 937 HOH A O   
3611 O  O   . HOH G .   ? 0.42860 0.45708 0.22986 -0.00938 -0.06815 0.05613  938 HOH A O   
3612 O  O   . HOH G .   ? 0.34973 0.71455 0.31548 0.09351  -0.04205 -0.02672 939 HOH A O   
3613 O  O   . HOH G .   ? 0.88915 0.52366 0.61975 0.21363  0.00237  0.03650  940 HOH A O   
3614 O  O   . HOH G .   ? 0.76654 0.67472 0.66585 0.16889  -0.37347 0.03147  941 HOH A O   
3615 O  O   . HOH G .   ? 0.40943 0.31506 0.34791 -0.03135 0.01163  -0.03962 942 HOH A O   
3616 O  O   . HOH G .   ? 0.79836 0.59110 0.96636 -0.03771 -0.09831 -0.17201 943 HOH A O   
3617 O  O   . HOH G .   ? 0.45828 0.52214 0.64013 -0.00116 -0.21618 -0.13637 944 HOH A O   
3618 O  O   . HOH G .   ? 0.52304 0.39898 0.34634 -0.03560 -0.08657 -0.01933 945 HOH A O   
3619 O  O   . HOH G .   ? 0.71332 0.56162 0.32239 0.08097  -0.00683 0.01055  946 HOH A O   
3620 O  O   . HOH G .   ? 0.56605 0.61961 0.36361 -0.00080 -0.01689 0.18712  947 HOH A O   
3621 O  O   . HOH G .   ? 0.69063 0.61034 0.46800 0.29428  0.25462  0.09135  948 HOH A O   
3622 O  O   . HOH G .   ? 0.42016 0.39301 0.37193 -0.03723 -0.08885 -0.08489 949 HOH A O   
3623 O  O   . HOH G .   ? 0.50648 0.46950 0.30600 0.09687  -0.09672 -0.09025 950 HOH A O   
3624 O  O   . HOH G .   ? 0.48182 0.95058 0.36185 0.01903  -0.15651 -0.11178 951 HOH A O   
3625 O  O   . HOH G .   ? 0.74237 0.73502 0.76498 0.02567  -0.21616 0.29807  952 HOH A O   
3626 O  O   . HOH G .   ? 0.60528 0.91824 0.61134 0.17232  0.00454  0.17951  953 HOH A O   
3627 O  O   . HOH G .   ? 0.76597 0.50820 0.42648 0.23791  -0.18182 -0.09640 954 HOH A O   
3628 O  O   . HOH G .   ? 0.96066 0.36005 0.67278 0.08779  -0.16431 0.04945  955 HOH A O   
3629 O  O   . HOH G .   ? 1.03262 0.68900 0.48602 0.30147  0.06663  -0.18745 956 HOH A O   
3630 O  O   . HOH G .   ? 0.80131 1.01764 0.86998 0.36173  0.41285  0.22941  957 HOH A O   
3631 O  O   . HOH G .   ? 0.54062 1.09539 0.46286 -0.25279 0.03102  0.15713  958 HOH A O   
3632 O  O   . HOH G .   ? 0.71502 0.37209 0.86179 0.25386  0.07246  0.05338  959 HOH A O   
3633 O  O   . HOH G .   ? 0.46434 0.47006 0.33570 0.09662  -0.10347 -0.15484 960 HOH A O   
3634 O  O   . HOH G .   ? 1.23427 0.69269 0.43916 0.20150  -0.05978 -0.03392 961 HOH A O   
3635 O  O   . HOH G .   ? 0.65175 0.69842 0.65133 -0.22217 -0.06449 -0.11825 962 HOH A O   
3636 O  O   . HOH G .   ? 0.86682 0.91880 0.79651 0.29325  0.18327  0.07765  963 HOH A O   
3637 O  O   . HOH G .   ? 0.72997 0.81603 0.84376 0.15706  -0.07678 0.39996  964 HOH A O   
3638 O  O   . HOH G .   ? 0.48708 0.64307 0.32125 -0.24850 0.03815  -0.06203 965 HOH A O   
3639 O  O   . HOH G .   ? 0.76956 0.49087 0.49014 0.10592  0.25902  0.15275  966 HOH A O   
3640 O  O   . HOH G .   ? 0.86435 0.70111 0.34972 0.24420  -0.16385 -0.09917 967 HOH A O   
3641 O  O   . HOH G .   ? 0.40227 0.73638 0.27564 0.07349  -0.06533 0.04631  968 HOH A O   
3642 O  O   . HOH G .   ? 0.56441 0.88160 0.37346 -0.13007 0.05181  -0.15471 969 HOH A O   
3643 O  O   . HOH G .   ? 0.34083 0.62561 0.36078 -0.06240 -0.02653 -0.16062 970 HOH A O   
3644 O  O   . HOH G .   ? 0.59058 0.49268 0.34296 -0.10701 -0.03990 -0.05568 971 HOH A O   
3645 O  O   . HOH G .   ? 0.51049 0.50912 0.34998 0.02274  -0.00840 -0.12472 972 HOH A O   
3646 O  O   . HOH G .   ? 0.45963 0.39997 0.29680 -0.20591 -0.00016 -0.11081 973 HOH A O   
3647 O  O   . HOH G .   ? 0.55987 0.48735 0.82386 -0.01108 -0.02339 -0.06619 974 HOH A O   
3648 O  O   . HOH G .   ? 0.47075 0.28230 0.32599 -0.08125 0.04174  -0.00369 975 HOH A O   
3649 O  O   . HOH G .   ? 0.45732 0.29167 0.49475 -0.10185 0.12751  0.06207  976 HOH A O   
# 
