data_9CVO
# 
_entry.id   9CVO 
# 
_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   9CVO         pdb_00009cvo 10.2210/pdb9cvo/pdb 
WWPDB D_1000286178 ?            ?                   
# 
_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       2025-04-30 
_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                        9CVO 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-29 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              poulos@uci.edu 
_pdbx_contact_author.name_first         Thomas 
_pdbx_contact_author.name_last          Poulos 
_pdbx_contact_author.name_mi            L 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5648-3510 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, H.'       1 0000-0003-4867-367X 
'Poulos, T.L.' 2 0000-0002-5648-3510 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Bioorg.Med.Chem. 
_citation.journal_id_ASTM           BMECEP 
_citation.journal_id_CSD            1200 
_citation.journal_id_ISSN           1464-3391 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            124 
_citation.language                  ? 
_citation.page_first                118193 
_citation.page_last                 118193 
_citation.title                     
;Truncated pyridinylbenzylamines: Potent, selective, and highly membrane permeable inhibitors of human neuronal nitric oxide synthase.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bmc.2025.118193 
_citation.pdbx_database_id_PubMed   40252563 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vasu, D.'        1 ? 
primary 'Do, H.T.'        2 ? 
primary 'Li, H.'          3 ? 
primary 'Hardy, C.D.'     4 ? 
primary 'Poulos, T.L.'    5 ? 
primary 'Silverman, R.B.' 6 ? 
# 
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 'Nitric oxide synthase, brain'                                                  48726.410 1  1.14.13.39 R349A ? 
? 
2 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE'                                               616.487   1  ?          ?     ? 
? 
3 non-polymer syn 5,6,7,8-TETRAHYDROBIOPTERIN                                                     241.247   1  ?          ?     ? 
? 
4 non-polymer syn 'ZINC ION'                                                                      65.409    1  ?          ?     ? 
? 
5 non-polymer syn '(6M)-6-{5-[(dimethylamino)methyl]-2,3-difluorophenyl}-4-methylpyridin-2-amine' 277.312   1  ?          ?     ? 
? 
6 water       nat water                                                                           18.015    43 ?          ?     ? 
? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'BNOS,Constitutive NOS,NC-NOS,NOS type I,Neuronal NOS,nNOS,Peptidyl-cysteine S-nitrosylase NOS1' 
# 
_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       
;CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVATKDQLFPLAKEFLDQYYSSIKRFGSKA
HMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVATKDQLFPLAKEFLDQYYSSIKRFGSKA
HMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKG
;
_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 5,6,7,8-TETRAHYDROBIOPTERIN                                                     H4B   
4 'ZINC ION'                                                                      ZN    
5 '(6M)-6-{5-[(dimethylamino)methyl]-2,3-difluorophenyl}-4-methylpyridin-2-amine' A1A0K 
6 water                                                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   CYS n 
1 2   PRO n 
1 3   ARG n 
1 4   PHE n 
1 5   LEU n 
1 6   LYS n 
1 7   VAL n 
1 8   LYS n 
1 9   ASN n 
1 10  TRP n 
1 11  GLU n 
1 12  THR n 
1 13  ASP n 
1 14  VAL n 
1 15  VAL n 
1 16  LEU n 
1 17  THR n 
1 18  ASP n 
1 19  THR n 
1 20  LEU n 
1 21  HIS n 
1 22  LEU n 
1 23  LYS n 
1 24  SER n 
1 25  THR n 
1 26  LEU n 
1 27  GLU n 
1 28  THR n 
1 29  GLY n 
1 30  CYS n 
1 31  THR n 
1 32  GLU n 
1 33  HIS n 
1 34  ILE n 
1 35  CYS n 
1 36  MET n 
1 37  GLY n 
1 38  SER n 
1 39  ILE n 
1 40  MET n 
1 41  LEU n 
1 42  PRO n 
1 43  SER n 
1 44  GLN n 
1 45  HIS n 
1 46  THR n 
1 47  ARG n 
1 48  LYS n 
1 49  PRO n 
1 50  GLU n 
1 51  ASP n 
1 52  VAL n 
1 53  ALA n 
1 54  THR n 
1 55  LYS n 
1 56  ASP n 
1 57  GLN n 
1 58  LEU n 
1 59  PHE n 
1 60  PRO n 
1 61  LEU n 
1 62  ALA n 
1 63  LYS n 
1 64  GLU n 
1 65  PHE n 
1 66  LEU n 
1 67  ASP n 
1 68  GLN n 
1 69  TYR n 
1 70  TYR n 
1 71  SER n 
1 72  SER n 
1 73  ILE n 
1 74  LYS n 
1 75  ARG n 
1 76  PHE n 
1 77  GLY n 
1 78  SER n 
1 79  LYS n 
1 80  ALA n 
1 81  HIS n 
1 82  MET n 
1 83  ASP n 
1 84  ARG n 
1 85  LEU n 
1 86  GLU n 
1 87  GLU n 
1 88  VAL n 
1 89  ASN n 
1 90  LYS n 
1 91  GLU n 
1 92  ILE n 
1 93  GLU n 
1 94  SER n 
1 95  THR n 
1 96  SER n 
1 97  THR n 
1 98  TYR n 
1 99  GLN n 
1 100 LEU n 
1 101 LYS n 
1 102 ASP n 
1 103 THR n 
1 104 GLU n 
1 105 LEU n 
1 106 ILE n 
1 107 TYR n 
1 108 GLY n 
1 109 ALA n 
1 110 LYS n 
1 111 HIS n 
1 112 ALA n 
1 113 TRP n 
1 114 ARG n 
1 115 ASN n 
1 116 ALA n 
1 117 SER n 
1 118 ARG n 
1 119 CYS n 
1 120 VAL n 
1 121 GLY n 
1 122 ARG n 
1 123 ILE n 
1 124 GLN n 
1 125 TRP n 
1 126 SER n 
1 127 LYS n 
1 128 LEU n 
1 129 GLN n 
1 130 VAL n 
1 131 PHE n 
1 132 ASP n 
1 133 ALA n 
1 134 ARG n 
1 135 ASP n 
1 136 CYS n 
1 137 THR n 
1 138 THR n 
1 139 ALA n 
1 140 HIS n 
1 141 GLY n 
1 142 MET n 
1 143 PHE n 
1 144 ASN n 
1 145 TYR n 
1 146 ILE n 
1 147 CYS n 
1 148 ASN n 
1 149 HIS n 
1 150 VAL n 
1 151 LYS n 
1 152 TYR n 
1 153 ALA n 
1 154 THR n 
1 155 ASN n 
1 156 LYS n 
1 157 GLY n 
1 158 ASN n 
1 159 LEU n 
1 160 ARG n 
1 161 SER n 
1 162 ALA n 
1 163 ILE n 
1 164 THR n 
1 165 ILE n 
1 166 PHE n 
1 167 PRO n 
1 168 GLN n 
1 169 ARG n 
1 170 THR n 
1 171 ASP n 
1 172 GLY n 
1 173 LYS n 
1 174 HIS n 
1 175 ASP n 
1 176 PHE n 
1 177 ARG n 
1 178 VAL n 
1 179 TRP n 
1 180 ASN n 
1 181 SER n 
1 182 GLN n 
1 183 LEU n 
1 184 ILE n 
1 185 ARG n 
1 186 TYR n 
1 187 ALA n 
1 188 GLY n 
1 189 TYR n 
1 190 LYS n 
1 191 GLN n 
1 192 PRO n 
1 193 ASP n 
1 194 GLY n 
1 195 SER n 
1 196 THR n 
1 197 LEU n 
1 198 GLY n 
1 199 ASP n 
1 200 PRO n 
1 201 ALA n 
1 202 ASN n 
1 203 VAL n 
1 204 GLN n 
1 205 PHE n 
1 206 THR n 
1 207 GLU n 
1 208 ILE n 
1 209 CYS n 
1 210 ILE n 
1 211 GLN n 
1 212 GLN n 
1 213 GLY n 
1 214 TRP n 
1 215 LYS n 
1 216 ALA n 
1 217 PRO n 
1 218 ARG n 
1 219 GLY n 
1 220 ARG n 
1 221 PHE n 
1 222 ASP n 
1 223 VAL n 
1 224 LEU n 
1 225 PRO n 
1 226 LEU n 
1 227 LEU n 
1 228 LEU n 
1 229 GLN n 
1 230 ALA n 
1 231 ASN n 
1 232 GLY n 
1 233 ASN n 
1 234 ASP n 
1 235 PRO n 
1 236 GLU n 
1 237 LEU n 
1 238 PHE n 
1 239 GLN n 
1 240 ILE n 
1 241 PRO n 
1 242 PRO n 
1 243 GLU n 
1 244 LEU n 
1 245 VAL n 
1 246 LEU n 
1 247 GLU n 
1 248 VAL n 
1 249 PRO n 
1 250 ILE n 
1 251 ARG n 
1 252 HIS n 
1 253 PRO n 
1 254 LYS n 
1 255 PHE n 
1 256 ASP n 
1 257 TRP n 
1 258 PHE n 
1 259 LYS n 
1 260 ASP n 
1 261 LEU n 
1 262 GLY n 
1 263 LEU n 
1 264 LYS n 
1 265 TRP n 
1 266 TYR n 
1 267 GLY n 
1 268 LEU n 
1 269 PRO n 
1 270 ALA n 
1 271 VAL n 
1 272 SER n 
1 273 ASN n 
1 274 MET n 
1 275 LEU n 
1 276 LEU n 
1 277 GLU n 
1 278 ILE n 
1 279 GLY n 
1 280 GLY n 
1 281 LEU n 
1 282 GLU n 
1 283 PHE n 
1 284 SER n 
1 285 ALA n 
1 286 CYS n 
1 287 PRO n 
1 288 PHE n 
1 289 SER n 
1 290 GLY n 
1 291 TRP n 
1 292 TYR n 
1 293 MET n 
1 294 GLY n 
1 295 THR n 
1 296 GLU n 
1 297 ILE n 
1 298 GLY n 
1 299 VAL n 
1 300 ARG n 
1 301 ASP n 
1 302 TYR n 
1 303 CYS n 
1 304 ASP n 
1 305 ASN n 
1 306 SER n 
1 307 ARG n 
1 308 TYR n 
1 309 ASN n 
1 310 ILE n 
1 311 LEU n 
1 312 GLU n 
1 313 GLU n 
1 314 VAL n 
1 315 ALA n 
1 316 LYS n 
1 317 LYS n 
1 318 MET n 
1 319 ASP n 
1 320 LEU n 
1 321 ASP n 
1 322 MET n 
1 323 ARG n 
1 324 LYS n 
1 325 THR n 
1 326 SER n 
1 327 SER n 
1 328 LEU n 
1 329 TRP n 
1 330 LYS n 
1 331 ASP n 
1 332 GLN n 
1 333 ALA n 
1 334 LEU n 
1 335 VAL n 
1 336 GLU n 
1 337 ILE n 
1 338 ASN n 
1 339 ILE n 
1 340 ALA n 
1 341 VAL n 
1 342 LEU n 
1 343 TYR n 
1 344 SER n 
1 345 PHE n 
1 346 GLN n 
1 347 SER n 
1 348 ASP n 
1 349 LYS n 
1 350 VAL n 
1 351 THR n 
1 352 ILE n 
1 353 VAL n 
1 354 ASP n 
1 355 HIS n 
1 356 HIS n 
1 357 SER n 
1 358 ALA n 
1 359 THR n 
1 360 GLU n 
1 361 SER n 
1 362 PHE n 
1 363 ILE n 
1 364 LYS n 
1 365 HIS n 
1 366 MET n 
1 367 GLU n 
1 368 ASN n 
1 369 GLU n 
1 370 TYR n 
1 371 ARG n 
1 372 CYS n 
1 373 ARG n 
1 374 GLY n 
1 375 GLY n 
1 376 CYS n 
1 377 PRO n 
1 378 ALA n 
1 379 ASP n 
1 380 TRP n 
1 381 VAL n 
1 382 TRP n 
1 383 ILE n 
1 384 VAL n 
1 385 PRO n 
1 386 PRO n 
1 387 MET n 
1 388 SER n 
1 389 GLY n 
1 390 SER n 
1 391 ILE n 
1 392 THR n 
1 393 PRO n 
1 394 VAL n 
1 395 PHE n 
1 396 HIS n 
1 397 GLN n 
1 398 GLU n 
1 399 MET n 
1 400 LEU n 
1 401 ASN n 
1 402 TYR n 
1 403 ARG n 
1 404 LEU n 
1 405 THR n 
1 406 PRO n 
1 407 SER n 
1 408 PHE n 
1 409 GLU n 
1 410 TYR n 
1 411 GLN n 
1 412 PRO n 
1 413 ASP n 
1 414 PRO n 
1 415 TRP n 
1 416 ASN n 
1 417 THR n 
1 418 HIS n 
1 419 VAL n 
1 420 TRP n 
1 421 LYS n 
1 422 GLY 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                   422 
_entity_src_gen.gene_src_common_name               'Norway rat' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'Nos1, Bnos' 
_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      'Rattus norvegicus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     10116 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                brain 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET22b 
_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 
A1A0K non-polymer         . '(6M)-6-{5-[(dimethylamino)methyl]-2,3-difluorophenyl}-4-methylpyridin-2-amine' ?    'C15 H17 F2 N3' 
277.312 
ALA   'L-peptide linking' y ALANINE                                                                         ?    'C3 H7 N O2' 
89.093  
ARG   'L-peptide linking' y ARGININE                                                                        ?    'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                      ?    'C4 H8 N2 O3' 
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                 ?    'C4 H7 N O4' 
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                        ?    'C3 H7 N O2 S' 
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                       ?    'C5 H10 N2 O3' 
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                 ?    'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                                                         ?    'C2 H5 N O2' 
75.067  
H4B   non-polymer         . 5,6,7,8-TETRAHYDROBIOPTERIN                                                     ?    'C9 H15 N5 O3' 
241.247 
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 
TYR   'L-peptide linking' y TYROSINE                                                                        ?    'C9 H11 N O3' 
181.189 
VAL   'L-peptide linking' y VALINE                                                                          ?    'C5 H11 N O2' 
117.146 
ZN    non-polymer         . 'ZINC ION'                                                                      ?    'Zn 2' 65.409  
# 
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   CYS 1   297 ?   ?   ?   A . n 
A 1 2   PRO 2   298 ?   ?   ?   A . n 
A 1 3   ARG 3   299 299 ARG ARG A . n 
A 1 4   PHE 4   300 300 PHE PHE A . n 
A 1 5   LEU 5   301 301 LEU LEU A . n 
A 1 6   LYS 6   302 302 LYS LYS A . n 
A 1 7   VAL 7   303 303 VAL VAL A . n 
A 1 8   LYS 8   304 304 LYS LYS A . n 
A 1 9   ASN 9   305 305 ASN ASN A . n 
A 1 10  TRP 10  306 306 TRP TRP A . n 
A 1 11  GLU 11  307 307 GLU GLU A . n 
A 1 12  THR 12  308 308 THR THR A . n 
A 1 13  ASP 13  309 309 ASP ASP A . n 
A 1 14  VAL 14  310 310 VAL VAL A . n 
A 1 15  VAL 15  311 311 VAL VAL A . n 
A 1 16  LEU 16  312 312 LEU LEU A . n 
A 1 17  THR 17  313 313 THR THR A . n 
A 1 18  ASP 18  314 314 ASP ASP A . n 
A 1 19  THR 19  315 315 THR THR A . n 
A 1 20  LEU 20  316 316 LEU LEU A . n 
A 1 21  HIS 21  317 317 HIS HIS A . n 
A 1 22  LEU 22  318 318 LEU LEU A . n 
A 1 23  LYS 23  319 319 LYS LYS A . n 
A 1 24  SER 24  320 320 SER SER A . n 
A 1 25  THR 25  321 321 THR THR A . n 
A 1 26  LEU 26  322 322 LEU LEU A . n 
A 1 27  GLU 27  323 323 GLU GLU A . n 
A 1 28  THR 28  324 324 THR THR A . n 
A 1 29  GLY 29  325 325 GLY GLY A . n 
A 1 30  CYS 30  326 326 CYS CYS A . n 
A 1 31  THR 31  327 327 THR THR A . n 
A 1 32  GLU 32  328 328 GLU GLU A . n 
A 1 33  HIS 33  329 329 HIS HIS A . n 
A 1 34  ILE 34  330 330 ILE ILE A . n 
A 1 35  CYS 35  331 331 CYS CYS A . n 
A 1 36  MET 36  332 332 MET MET A . n 
A 1 37  GLY 37  333 333 GLY GLY A . n 
A 1 38  SER 38  334 334 SER SER A . n 
A 1 39  ILE 39  335 335 ILE ILE A . n 
A 1 40  MET 40  336 336 MET MET A . n 
A 1 41  LEU 41  337 337 LEU LEU A . n 
A 1 42  PRO 42  338 338 PRO PRO A . n 
A 1 43  SER 43  339 339 SER SER A . n 
A 1 44  GLN 44  340 ?   ?   ?   A . n 
A 1 45  HIS 45  341 ?   ?   ?   A . n 
A 1 46  THR 46  342 ?   ?   ?   A . n 
A 1 47  ARG 47  343 ?   ?   ?   A . n 
A 1 48  LYS 48  344 ?   ?   ?   A . n 
A 1 49  PRO 49  345 ?   ?   ?   A . n 
A 1 50  GLU 50  346 ?   ?   ?   A . n 
A 1 51  ASP 51  347 ?   ?   ?   A . n 
A 1 52  VAL 52  348 348 VAL VAL A . n 
A 1 53  ALA 53  349 349 ALA ALA A . n 
A 1 54  THR 54  350 350 THR THR A . n 
A 1 55  LYS 55  351 351 LYS LYS A . n 
A 1 56  ASP 56  352 352 ASP ASP A . n 
A 1 57  GLN 57  353 353 GLN GLN A . n 
A 1 58  LEU 58  354 354 LEU LEU A . n 
A 1 59  PHE 59  355 355 PHE PHE A . n 
A 1 60  PRO 60  356 356 PRO PRO A . n 
A 1 61  LEU 61  357 357 LEU LEU A . n 
A 1 62  ALA 62  358 358 ALA ALA A . n 
A 1 63  LYS 63  359 359 LYS LYS A . n 
A 1 64  GLU 64  360 360 GLU GLU A . n 
A 1 65  PHE 65  361 361 PHE PHE A . n 
A 1 66  LEU 66  362 362 LEU LEU A . n 
A 1 67  ASP 67  363 363 ASP ASP A . n 
A 1 68  GLN 68  364 364 GLN GLN A . n 
A 1 69  TYR 69  365 365 TYR TYR A . n 
A 1 70  TYR 70  366 366 TYR TYR A . n 
A 1 71  SER 71  367 367 SER SER A . n 
A 1 72  SER 72  368 368 SER SER A . n 
A 1 73  ILE 73  369 369 ILE ILE A . n 
A 1 74  LYS 74  370 370 LYS LYS A . n 
A 1 75  ARG 75  371 371 ARG ARG A . n 
A 1 76  PHE 76  372 372 PHE PHE A . n 
A 1 77  GLY 77  373 373 GLY GLY A . n 
A 1 78  SER 78  374 374 SER SER A . n 
A 1 79  LYS 79  375 375 LYS LYS A . n 
A 1 80  ALA 80  376 376 ALA ALA A . n 
A 1 81  HIS 81  377 377 HIS HIS A . n 
A 1 82  MET 82  378 378 MET MET A . n 
A 1 83  ASP 83  379 379 ASP ASP A . n 
A 1 84  ARG 84  380 380 ARG ARG A . n 
A 1 85  LEU 85  381 381 LEU LEU A . n 
A 1 86  GLU 86  382 382 GLU GLU A . n 
A 1 87  GLU 87  383 383 GLU GLU A . n 
A 1 88  VAL 88  384 384 VAL VAL A . n 
A 1 89  ASN 89  385 385 ASN ASN A . n 
A 1 90  LYS 90  386 386 LYS LYS A . n 
A 1 91  GLU 91  387 387 GLU GLU A . n 
A 1 92  ILE 92  388 388 ILE ILE A . n 
A 1 93  GLU 93  389 389 GLU GLU A . n 
A 1 94  SER 94  390 390 SER SER A . n 
A 1 95  THR 95  391 391 THR THR A . n 
A 1 96  SER 96  392 392 SER SER A . n 
A 1 97  THR 97  393 393 THR THR A . n 
A 1 98  TYR 98  394 394 TYR TYR A . n 
A 1 99  GLN 99  395 395 GLN GLN A . n 
A 1 100 LEU 100 396 396 LEU LEU A . n 
A 1 101 LYS 101 397 397 LYS LYS A . n 
A 1 102 ASP 102 398 398 ASP ASP A . n 
A 1 103 THR 103 399 399 THR THR A . n 
A 1 104 GLU 104 400 400 GLU GLU A . n 
A 1 105 LEU 105 401 401 LEU LEU A . n 
A 1 106 ILE 106 402 402 ILE ILE A . n 
A 1 107 TYR 107 403 403 TYR TYR A . n 
A 1 108 GLY 108 404 404 GLY GLY A . n 
A 1 109 ALA 109 405 405 ALA ALA A . n 
A 1 110 LYS 110 406 406 LYS LYS A . n 
A 1 111 HIS 111 407 407 HIS HIS A . n 
A 1 112 ALA 112 408 408 ALA ALA A . n 
A 1 113 TRP 113 409 409 TRP TRP A . n 
A 1 114 ARG 114 410 410 ARG ARG A . n 
A 1 115 ASN 115 411 411 ASN ASN A . n 
A 1 116 ALA 116 412 412 ALA ALA A . n 
A 1 117 SER 117 413 413 SER SER A . n 
A 1 118 ARG 118 414 414 ARG ARG A . n 
A 1 119 CYS 119 415 415 CYS CYS A . n 
A 1 120 VAL 120 416 416 VAL VAL A . n 
A 1 121 GLY 121 417 417 GLY GLY A . n 
A 1 122 ARG 122 418 418 ARG ARG A . n 
A 1 123 ILE 123 419 419 ILE ILE A . n 
A 1 124 GLN 124 420 420 GLN GLN A . n 
A 1 125 TRP 125 421 421 TRP TRP A . n 
A 1 126 SER 126 422 422 SER SER A . n 
A 1 127 LYS 127 423 423 LYS LYS A . n 
A 1 128 LEU 128 424 424 LEU LEU A . n 
A 1 129 GLN 129 425 425 GLN GLN A . n 
A 1 130 VAL 130 426 426 VAL VAL A . n 
A 1 131 PHE 131 427 427 PHE PHE A . n 
A 1 132 ASP 132 428 428 ASP ASP A . n 
A 1 133 ALA 133 429 429 ALA ALA A . n 
A 1 134 ARG 134 430 430 ARG ARG A . n 
A 1 135 ASP 135 431 431 ASP ASP A . n 
A 1 136 CYS 136 432 432 CYS CYS A . n 
A 1 137 THR 137 433 433 THR THR A . n 
A 1 138 THR 138 434 434 THR THR A . n 
A 1 139 ALA 139 435 435 ALA ALA A . n 
A 1 140 HIS 140 436 436 HIS HIS A . n 
A 1 141 GLY 141 437 437 GLY GLY A . n 
A 1 142 MET 142 438 438 MET MET A . n 
A 1 143 PHE 143 439 439 PHE PHE A . n 
A 1 144 ASN 144 440 440 ASN ASN A . n 
A 1 145 TYR 145 441 441 TYR TYR A . n 
A 1 146 ILE 146 442 442 ILE ILE A . n 
A 1 147 CYS 147 443 443 CYS CYS A . n 
A 1 148 ASN 148 444 444 ASN ASN A . n 
A 1 149 HIS 149 445 445 HIS HIS A . n 
A 1 150 VAL 150 446 446 VAL VAL A . n 
A 1 151 LYS 151 447 447 LYS LYS A . n 
A 1 152 TYR 152 448 448 TYR TYR A . n 
A 1 153 ALA 153 449 449 ALA ALA A . n 
A 1 154 THR 154 450 450 THR THR A . n 
A 1 155 ASN 155 451 451 ASN ASN A . n 
A 1 156 LYS 156 452 452 LYS LYS A . n 
A 1 157 GLY 157 453 453 GLY GLY A . n 
A 1 158 ASN 158 454 454 ASN ASN A . n 
A 1 159 LEU 159 455 455 LEU LEU A . n 
A 1 160 ARG 160 456 456 ARG ARG A . n 
A 1 161 SER 161 457 457 SER SER A . n 
A 1 162 ALA 162 458 458 ALA ALA A . n 
A 1 163 ILE 163 459 459 ILE ILE A . n 
A 1 164 THR 164 460 460 THR THR A . n 
A 1 165 ILE 165 461 461 ILE ILE A . n 
A 1 166 PHE 166 462 462 PHE PHE A . n 
A 1 167 PRO 167 463 463 PRO PRO A . n 
A 1 168 GLN 168 464 464 GLN GLN A . n 
A 1 169 ARG 169 465 465 ARG ARG A . n 
A 1 170 THR 170 466 466 THR THR A . n 
A 1 171 ASP 171 467 467 ASP ASP A . n 
A 1 172 GLY 172 468 468 GLY GLY A . n 
A 1 173 LYS 173 469 469 LYS LYS A . n 
A 1 174 HIS 174 470 470 HIS HIS A . n 
A 1 175 ASP 175 471 471 ASP ASP A . n 
A 1 176 PHE 176 472 472 PHE PHE A . n 
A 1 177 ARG 177 473 473 ARG ARG A . n 
A 1 178 VAL 178 474 474 VAL VAL A . n 
A 1 179 TRP 179 475 475 TRP TRP A . n 
A 1 180 ASN 180 476 476 ASN ASN A . n 
A 1 181 SER 181 477 477 SER SER A . n 
A 1 182 GLN 182 478 478 GLN GLN A . n 
A 1 183 LEU 183 479 479 LEU LEU A . n 
A 1 184 ILE 184 480 480 ILE ILE A . n 
A 1 185 ARG 185 481 481 ARG ARG A . n 
A 1 186 TYR 186 482 482 TYR TYR A . n 
A 1 187 ALA 187 483 483 ALA ALA A . n 
A 1 188 GLY 188 484 484 GLY GLY A . n 
A 1 189 TYR 189 485 485 TYR TYR A . n 
A 1 190 LYS 190 486 486 LYS LYS A . n 
A 1 191 GLN 191 487 487 GLN GLN A . n 
A 1 192 PRO 192 488 488 PRO PRO A . n 
A 1 193 ASP 193 489 489 ASP ASP A . n 
A 1 194 GLY 194 490 490 GLY GLY A . n 
A 1 195 SER 195 491 491 SER SER A . n 
A 1 196 THR 196 492 492 THR THR A . n 
A 1 197 LEU 197 493 493 LEU LEU A . n 
A 1 198 GLY 198 494 494 GLY GLY A . n 
A 1 199 ASP 199 495 495 ASP ASP A . n 
A 1 200 PRO 200 496 496 PRO PRO A . n 
A 1 201 ALA 201 497 497 ALA ALA A . n 
A 1 202 ASN 202 498 498 ASN ASN A . n 
A 1 203 VAL 203 499 499 VAL VAL A . n 
A 1 204 GLN 204 500 500 GLN GLN A . n 
A 1 205 PHE 205 501 501 PHE PHE A . n 
A 1 206 THR 206 502 502 THR THR A . n 
A 1 207 GLU 207 503 503 GLU GLU A . n 
A 1 208 ILE 208 504 504 ILE ILE A . n 
A 1 209 CYS 209 505 505 CYS CYS A . n 
A 1 210 ILE 210 506 506 ILE ILE A . n 
A 1 211 GLN 211 507 507 GLN GLN A . n 
A 1 212 GLN 212 508 508 GLN GLN A . n 
A 1 213 GLY 213 509 509 GLY GLY A . n 
A 1 214 TRP 214 510 510 TRP TRP A . n 
A 1 215 LYS 215 511 511 LYS LYS A . n 
A 1 216 ALA 216 512 512 ALA ALA A . n 
A 1 217 PRO 217 513 513 PRO PRO A . n 
A 1 218 ARG 218 514 514 ARG ARG A . n 
A 1 219 GLY 219 515 515 GLY GLY A . n 
A 1 220 ARG 220 516 516 ARG ARG A . n 
A 1 221 PHE 221 517 517 PHE PHE A . n 
A 1 222 ASP 222 518 518 ASP ASP A . n 
A 1 223 VAL 223 519 519 VAL VAL A . n 
A 1 224 LEU 224 520 520 LEU LEU A . n 
A 1 225 PRO 225 521 521 PRO PRO A . n 
A 1 226 LEU 226 522 522 LEU LEU A . n 
A 1 227 LEU 227 523 523 LEU LEU A . n 
A 1 228 LEU 228 524 524 LEU LEU A . n 
A 1 229 GLN 229 525 525 GLN GLN A . n 
A 1 230 ALA 230 526 526 ALA ALA A . n 
A 1 231 ASN 231 527 527 ASN ASN A . n 
A 1 232 GLY 232 528 528 GLY GLY A . n 
A 1 233 ASN 233 529 529 ASN ASN A . n 
A 1 234 ASP 234 530 530 ASP ASP A . n 
A 1 235 PRO 235 531 531 PRO PRO A . n 
A 1 236 GLU 236 532 532 GLU GLU A . n 
A 1 237 LEU 237 533 533 LEU LEU A . n 
A 1 238 PHE 238 534 534 PHE PHE A . n 
A 1 239 GLN 239 535 535 GLN GLN A . n 
A 1 240 ILE 240 536 536 ILE ILE A . n 
A 1 241 PRO 241 537 537 PRO PRO A . n 
A 1 242 PRO 242 538 538 PRO PRO A . n 
A 1 243 GLU 243 539 539 GLU GLU A . n 
A 1 244 LEU 244 540 540 LEU LEU A . n 
A 1 245 VAL 245 541 541 VAL VAL A . n 
A 1 246 LEU 246 542 542 LEU LEU A . n 
A 1 247 GLU 247 543 543 GLU GLU A . n 
A 1 248 VAL 248 544 544 VAL VAL A . n 
A 1 249 PRO 249 545 545 PRO PRO A . n 
A 1 250 ILE 250 546 546 ILE ILE A . n 
A 1 251 ARG 251 547 547 ARG ARG A . n 
A 1 252 HIS 252 548 548 HIS HIS A . n 
A 1 253 PRO 253 549 549 PRO PRO A . n 
A 1 254 LYS 254 550 550 LYS LYS A . n 
A 1 255 PHE 255 551 551 PHE PHE A . n 
A 1 256 ASP 256 552 552 ASP ASP A . n 
A 1 257 TRP 257 553 553 TRP TRP A . n 
A 1 258 PHE 258 554 554 PHE PHE A . n 
A 1 259 LYS 259 555 555 LYS LYS A . n 
A 1 260 ASP 260 556 556 ASP ASP A . n 
A 1 261 LEU 261 557 557 LEU LEU A . n 
A 1 262 GLY 262 558 558 GLY GLY A . n 
A 1 263 LEU 263 559 559 LEU LEU A . n 
A 1 264 LYS 264 560 560 LYS LYS A . n 
A 1 265 TRP 265 561 561 TRP TRP A . n 
A 1 266 TYR 266 562 562 TYR TYR A . n 
A 1 267 GLY 267 563 563 GLY GLY A . n 
A 1 268 LEU 268 564 564 LEU LEU A . n 
A 1 269 PRO 269 565 565 PRO PRO A . n 
A 1 270 ALA 270 566 566 ALA ALA A . n 
A 1 271 VAL 271 567 567 VAL VAL A . n 
A 1 272 SER 272 568 568 SER SER A . n 
A 1 273 ASN 273 569 569 ASN ASN A . n 
A 1 274 MET 274 570 570 MET MET A . n 
A 1 275 LEU 275 571 571 LEU LEU A . n 
A 1 276 LEU 276 572 572 LEU LEU A . n 
A 1 277 GLU 277 573 573 GLU GLU A . n 
A 1 278 ILE 278 574 574 ILE ILE A . n 
A 1 279 GLY 279 575 575 GLY GLY A . n 
A 1 280 GLY 280 576 576 GLY GLY A . n 
A 1 281 LEU 281 577 577 LEU LEU A . n 
A 1 282 GLU 282 578 578 GLU GLU A . n 
A 1 283 PHE 283 579 579 PHE PHE A . n 
A 1 284 SER 284 580 580 SER SER A . n 
A 1 285 ALA 285 581 581 ALA ALA A . n 
A 1 286 CYS 286 582 582 CYS CYS A . n 
A 1 287 PRO 287 583 583 PRO PRO A . n 
A 1 288 PHE 288 584 584 PHE PHE A . n 
A 1 289 SER 289 585 585 SER SER A . n 
A 1 290 GLY 290 586 586 GLY GLY A . n 
A 1 291 TRP 291 587 587 TRP TRP A . n 
A 1 292 TYR 292 588 588 TYR TYR A . n 
A 1 293 MET 293 589 589 MET MET A . n 
A 1 294 GLY 294 590 590 GLY GLY A . n 
A 1 295 THR 295 591 591 THR THR A . n 
A 1 296 GLU 296 592 592 GLU GLU A . n 
A 1 297 ILE 297 593 593 ILE ILE A . n 
A 1 298 GLY 298 594 594 GLY GLY A . n 
A 1 299 VAL 299 595 595 VAL VAL A . n 
A 1 300 ARG 300 596 596 ARG ARG A . n 
A 1 301 ASP 301 597 597 ASP ASP A . n 
A 1 302 TYR 302 598 598 TYR TYR A . n 
A 1 303 CYS 303 599 599 CYS CYS A . n 
A 1 304 ASP 304 600 600 ASP ASP A . n 
A 1 305 ASN 305 601 601 ASN ASN A . n 
A 1 306 SER 306 602 602 SER SER A . n 
A 1 307 ARG 307 603 603 ARG ARG A . n 
A 1 308 TYR 308 604 604 TYR TYR A . n 
A 1 309 ASN 309 605 605 ASN ASN A . n 
A 1 310 ILE 310 606 606 ILE ILE A . n 
A 1 311 LEU 311 607 607 LEU LEU A . n 
A 1 312 GLU 312 608 608 GLU GLU A . n 
A 1 313 GLU 313 609 609 GLU GLU A . n 
A 1 314 VAL 314 610 610 VAL VAL A . n 
A 1 315 ALA 315 611 611 ALA ALA A . n 
A 1 316 LYS 316 612 612 LYS LYS A . n 
A 1 317 LYS 317 613 613 LYS LYS A . n 
A 1 318 MET 318 614 614 MET MET A . n 
A 1 319 ASP 319 615 615 ASP ASP A . n 
A 1 320 LEU 320 616 616 LEU LEU A . n 
A 1 321 ASP 321 617 617 ASP ASP A . n 
A 1 322 MET 322 618 618 MET MET A . n 
A 1 323 ARG 323 619 619 ARG ARG A . n 
A 1 324 LYS 324 620 620 LYS LYS A . n 
A 1 325 THR 325 621 621 THR THR A . n 
A 1 326 SER 326 622 622 SER SER A . n 
A 1 327 SER 327 623 623 SER SER A . n 
A 1 328 LEU 328 624 624 LEU LEU A . n 
A 1 329 TRP 329 625 625 TRP TRP A . n 
A 1 330 LYS 330 626 626 LYS LYS A . n 
A 1 331 ASP 331 627 627 ASP ASP A . n 
A 1 332 GLN 332 628 628 GLN GLN A . n 
A 1 333 ALA 333 629 629 ALA ALA A . n 
A 1 334 LEU 334 630 630 LEU LEU A . n 
A 1 335 VAL 335 631 631 VAL VAL A . n 
A 1 336 GLU 336 632 632 GLU GLU A . n 
A 1 337 ILE 337 633 633 ILE ILE A . n 
A 1 338 ASN 338 634 634 ASN ASN A . n 
A 1 339 ILE 339 635 635 ILE ILE A . n 
A 1 340 ALA 340 636 636 ALA ALA A . n 
A 1 341 VAL 341 637 637 VAL VAL A . n 
A 1 342 LEU 342 638 638 LEU LEU A . n 
A 1 343 TYR 343 639 639 TYR TYR A . n 
A 1 344 SER 344 640 640 SER SER A . n 
A 1 345 PHE 345 641 641 PHE PHE A . n 
A 1 346 GLN 346 642 642 GLN GLN A . n 
A 1 347 SER 347 643 643 SER SER A . n 
A 1 348 ASP 348 644 644 ASP ASP A . n 
A 1 349 LYS 349 645 645 LYS LYS A . n 
A 1 350 VAL 350 646 646 VAL VAL A . n 
A 1 351 THR 351 647 647 THR THR A . n 
A 1 352 ILE 352 648 648 ILE ILE A . n 
A 1 353 VAL 353 649 649 VAL VAL A . n 
A 1 354 ASP 354 650 650 ASP ASP A . n 
A 1 355 HIS 355 651 651 HIS HIS A . n 
A 1 356 HIS 356 652 652 HIS HIS A . n 
A 1 357 SER 357 653 653 SER SER A . n 
A 1 358 ALA 358 654 654 ALA ALA A . n 
A 1 359 THR 359 655 655 THR THR A . n 
A 1 360 GLU 360 656 656 GLU GLU A . n 
A 1 361 SER 361 657 657 SER SER A . n 
A 1 362 PHE 362 658 658 PHE PHE A . n 
A 1 363 ILE 363 659 659 ILE ILE A . n 
A 1 364 LYS 364 660 660 LYS LYS A . n 
A 1 365 HIS 365 661 661 HIS HIS A . n 
A 1 366 MET 366 662 662 MET MET A . n 
A 1 367 GLU 367 663 663 GLU GLU A . n 
A 1 368 ASN 368 664 664 ASN ASN A . n 
A 1 369 GLU 369 665 665 GLU GLU A . n 
A 1 370 TYR 370 666 666 TYR TYR A . n 
A 1 371 ARG 371 667 667 ARG ARG A . n 
A 1 372 CYS 372 668 668 CYS CYS A . n 
A 1 373 ARG 373 669 669 ARG ARG A . n 
A 1 374 GLY 374 670 670 GLY GLY A . n 
A 1 375 GLY 375 671 671 GLY GLY A . n 
A 1 376 CYS 376 672 672 CYS CYS A . n 
A 1 377 PRO 377 673 673 PRO PRO A . n 
A 1 378 ALA 378 674 674 ALA ALA A . n 
A 1 379 ASP 379 675 675 ASP ASP A . n 
A 1 380 TRP 380 676 676 TRP TRP A . n 
A 1 381 VAL 381 677 677 VAL VAL A . n 
A 1 382 TRP 382 678 678 TRP TRP A . n 
A 1 383 ILE 383 679 679 ILE ILE A . n 
A 1 384 VAL 384 680 680 VAL VAL A . n 
A 1 385 PRO 385 681 681 PRO PRO A . n 
A 1 386 PRO 386 682 682 PRO PRO A . n 
A 1 387 MET 387 683 683 MET MET A . n 
A 1 388 SER 388 684 684 SER SER A . n 
A 1 389 GLY 389 685 685 GLY GLY A . n 
A 1 390 SER 390 686 686 SER SER A . n 
A 1 391 ILE 391 687 687 ILE ILE A . n 
A 1 392 THR 392 688 688 THR THR A . n 
A 1 393 PRO 393 689 689 PRO PRO A . n 
A 1 394 VAL 394 690 690 VAL VAL A . n 
A 1 395 PHE 395 691 691 PHE PHE A . n 
A 1 396 HIS 396 692 692 HIS HIS A . n 
A 1 397 GLN 397 693 693 GLN GLN A . n 
A 1 398 GLU 398 694 694 GLU GLU A . n 
A 1 399 MET 399 695 695 MET MET A . n 
A 1 400 LEU 400 696 696 LEU LEU A . n 
A 1 401 ASN 401 697 697 ASN ASN A . n 
A 1 402 TYR 402 698 698 TYR TYR A . n 
A 1 403 ARG 403 699 699 ARG ARG A . n 
A 1 404 LEU 404 700 700 LEU LEU A . n 
A 1 405 THR 405 701 701 THR THR A . n 
A 1 406 PRO 406 702 702 PRO PRO A . n 
A 1 407 SER 407 703 703 SER SER A . n 
A 1 408 PHE 408 704 704 PHE PHE A . n 
A 1 409 GLU 409 705 705 GLU GLU A . n 
A 1 410 TYR 410 706 706 TYR TYR A . n 
A 1 411 GLN 411 707 707 GLN GLN A . n 
A 1 412 PRO 412 708 708 PRO PRO A . n 
A 1 413 ASP 413 709 709 ASP ASP A . n 
A 1 414 PRO 414 710 710 PRO PRO A . n 
A 1 415 TRP 415 711 711 TRP TRP A . n 
A 1 416 ASN 416 712 712 ASN ASN A . n 
A 1 417 THR 417 713 713 THR THR A . n 
A 1 418 HIS 418 714 714 HIS HIS A . n 
A 1 419 VAL 419 715 715 VAL VAL A . n 
A 1 420 TRP 420 716 716 TRP TRP A . n 
A 1 421 LYS 421 717 717 LYS LYS A . n 
A 1 422 GLY 422 718 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A0K 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A0K 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 HEM   1  801 750 HEM   HEM A . 
C 3 H4B   1  802 760 H4B   BH4 A . 
D 4 ZN    1  803 900 ZN    ZN  A . 
E 5 A1A0K 1  804 800 A1A0K 2V1 A . 
F 6 HOH   1  901 31  HOH   HOH A . 
F 6 HOH   2  902 14  HOH   HOH A . 
F 6 HOH   3  903 33  HOH   HOH A . 
F 6 HOH   4  904 20  HOH   HOH A . 
F 6 HOH   5  905 22  HOH   HOH A . 
F 6 HOH   6  906 29  HOH   HOH A . 
F 6 HOH   7  907 19  HOH   HOH A . 
F 6 HOH   8  908 7   HOH   HOH A . 
F 6 HOH   9  909 12  HOH   HOH A . 
F 6 HOH   10 910 27  HOH   HOH A . 
F 6 HOH   11 911 15  HOH   HOH A . 
F 6 HOH   12 912 37  HOH   HOH A . 
F 6 HOH   13 913 42  HOH   HOH A . 
F 6 HOH   14 914 17  HOH   HOH A . 
F 6 HOH   15 915 34  HOH   HOH A . 
F 6 HOH   16 916 43  HOH   HOH A . 
F 6 HOH   17 917 6   HOH   HOH A . 
F 6 HOH   18 918 13  HOH   HOH A . 
F 6 HOH   19 919 3   HOH   HOH A . 
F 6 HOH   20 920 1   HOH   HOH A . 
F 6 HOH   21 921 11  HOH   HOH A . 
F 6 HOH   22 922 16  HOH   HOH A . 
F 6 HOH   23 923 8   HOH   HOH A . 
F 6 HOH   24 924 24  HOH   HOH A . 
F 6 HOH   25 925 35  HOH   HOH A . 
F 6 HOH   26 926 32  HOH   HOH A . 
F 6 HOH   27 927 28  HOH   HOH A . 
F 6 HOH   28 928 23  HOH   HOH A . 
F 6 HOH   29 929 4   HOH   HOH A . 
F 6 HOH   30 930 18  HOH   HOH A . 
F 6 HOH   31 931 2   HOH   HOH A . 
F 6 HOH   32 932 38  HOH   HOH A . 
F 6 HOH   33 933 21  HOH   HOH A . 
F 6 HOH   34 934 9   HOH   HOH A . 
F 6 HOH   35 935 36  HOH   HOH A . 
F 6 HOH   36 936 25  HOH   HOH A . 
F 6 HOH   37 937 5   HOH   HOH A . 
F 6 HOH   38 938 39  HOH   HOH A . 
F 6 HOH   39 939 10  HOH   HOH A . 
F 6 HOH   40 940 30  HOH   HOH A . 
F 6 HOH   41 941 26  HOH   HOH A . 
F 6 HOH   42 942 41  HOH   HOH A . 
F 6 HOH   43 943 40  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 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.11.1_2575 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CVO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.764 
_cell.length_a_esd                 ? 
_cell.length_b                     113.015 
_cell.length_b_esd                 ? 
_cell.length_c                     163.145 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9CVO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 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                   9CVO 
_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             2.48 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          50.4 
_exptl_crystal.description                  bricks 
_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              5.8 
_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    
;20-24% PEG3350, 0.1M MES
0.14-0.20M AMMONIUM ACETATE, 
10% ETHYLENE GLYCOL,
30uM SDS, 5 mM GSH
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            278 
# 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-09-17 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'DOUBLE CRYSTAL SI(III)' 
_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                        'ALS BEAMLINE 8.2.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.2.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CVO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.08 
_reflns.d_resolution_low                               46.45 
_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                                     27563 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                8.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.3 
_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                                0.209 
_reflns.pdbx_Rpim_I_all                                0.067 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       237523 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.982 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.198 
_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                                    2.08 
_reflns_shell.d_res_low                                     2.14 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           11581 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2113 
_reflns_shell.percent_possible_obs                          99.1 
_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                               5.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.7 
_reflns_shell.pdbx_Rrim_I_all                               5.930 
_reflns_shell.pdbx_Rpim_I_all                               2.530 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.243 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  5.342 
_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                               ? 
_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                                 9CVO 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.081 
_refine.ls_d_res_low                             46.45 
_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                     27290 
_refine.ls_number_reflns_R_free                  2640 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.71 
_refine.ls_percent_reflns_R_free                 5.11 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2252 
_refine.ls_R_factor_R_free                       0.2849 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2219 
_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                          0.00 
_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          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            random 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 41.35 
_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                            0.35 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        3341 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         81 
_refine_hist.number_atoms_solvent             43 
_refine_hist.number_atoms_total               3465 
_refine_hist.d_res_high                       2.081 
_refine_hist.d_res_low                        46.45 
# 
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' ? 0.008  ? 3530 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.998  ? 4804 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.968 ? 2054 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.052  ? 499  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 606  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.081  2.1185 . . 149 2410 91.00  . . . . 0.4126 . . . . . . . . . . . 0.4935 
'X-RAY DIFFRACTION' 2.1185 2.1593 . . 139 2524 98.00  . . . . 0.3999 . . . . . . . . . . . 0.4789 
'X-RAY DIFFRACTION' 2.1593 2.2033 . . 123 2641 98.00  . . . . 0.3655 . . . . . . . . . . . 0.4729 
'X-RAY DIFFRACTION' 2.2033 2.2512 . . 164 2493 99.00  . . . . 0.3517 . . . . . . . . . . . 0.4427 
'X-RAY DIFFRACTION' 2.2512 2.3036 . . 137 2616 99.00  . . . . 0.3173 . . . . . . . . . . . 0.3847 
'X-RAY DIFFRACTION' 2.3036 2.3612 . . 121 2610 99.00  . . . . 0.3170 . . . . . . . . . . . 0.4291 
'X-RAY DIFFRACTION' 2.3612 2.4251 . . 151 2543 99.00  . . . . 0.3147 . . . . . . . . . . . 0.3806 
'X-RAY DIFFRACTION' 2.4251 2.4964 . . 122 2598 99.00  . . . . 0.3009 . . . . . . . . . . . 0.3930 
'X-RAY DIFFRACTION' 2.4964 2.5770 . . 124 2623 99.00  . . . . 0.2915 . . . . . . . . . . . 0.4060 
'X-RAY DIFFRACTION' 2.5770 2.6691 . . 130 2547 99.00  . . . . 0.2970 . . . . . . . . . . . 0.3951 
'X-RAY DIFFRACTION' 2.6691 2.7759 . . 127 2577 99.00  . . . . 0.2914 . . . . . . . . . . . 0.3416 
'X-RAY DIFFRACTION' 2.7759 2.9022 . . 111 2653 99.00  . . . . 0.2673 . . . . . . . . . . . 0.3527 
'X-RAY DIFFRACTION' 2.9022 3.0552 . . 135 2625 99.00  . . . . 0.2815 . . . . . . . . . . . 0.3833 
'X-RAY DIFFRACTION' 3.0552 3.2466 . . 160 2579 100.00 . . . . 0.2718 . . . . . . . . . . . 0.3122 
'X-RAY DIFFRACTION' 3.2466 3.4972 . . 161 2544 100.00 . . . . 0.2318 . . . . . . . . . . . 0.2895 
'X-RAY DIFFRACTION' 3.4972 3.8490 . . 139 2642 100.00 . . . . 0.2000 . . . . . . . . . . . 0.2719 
'X-RAY DIFFRACTION' 3.8490 4.4056 . . 148 2613 100.00 . . . . 0.1757 . . . . . . . . . . . 0.2114 
'X-RAY DIFFRACTION' 4.4056 5.5491 . . 163 2552 100.00 . . . . 0.1566 . . . . . . . . . . . 0.2318 
'X-RAY DIFFRACTION' 5.5491 46.45  . . 136 2622 100.00 . . . . 0.1602 . . . . . . . . . . . 0.2132 
# 
_struct.entry_id                     9CVO 
_struct.title                        
;Structure of rat neuronal nitric oxide synthase R349A mutant heme domain bound with 6-(5-((dimethylamino)methyl)-2,3-difluorophenyl)-4-methylpyridin-2-amine dihydrochloride
;
_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        9CVO 
_struct_keywords.text            'nitric oxide synthase inhibitor binding, 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 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    NOS1_RAT 
_struct_ref.pdbx_db_accession          P29476 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;CPRFLKVKNWETDVVLTDTLHLKSTLETGCTEHICMGSIMLPSQHTRKPEDVRTKDQLFPLAKEFLDQYYSSIKRFGSKA
HMDRLEEVNKEIESTSTYQLKDTELIYGAKHAWRNASRCVGRIQWSKLQVFDARDCTTAHGMFNYICNHVKYATNKGNLR
SAITIFPQRTDGKHDFRVWNSQLIRYAGYKQPDGSTLGDPANVQFTEICIQQGWKAPRGRFDVLPLLLQANGNDPELFQI
PPELVLEVPIRHPKFDWFKDLGLKWYGLPAVSNMLLEIGGLEFSACPFSGWYMGTEIGVRDYCDNSRYNILEEVAKKMDL
DMRKTSSLWKDQALVEINIAVLYSFQSDKVTIVDHHSATESFIKHMENEYRCRGGCPADWVWIVPPMSGSITPVFHQEML
NYRLTPSFEYQPDPWNTHVWKG
;
_struct_ref.pdbx_align_begin           297 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9CVO 
_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                 422 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P29476 
_struct_ref_seq.db_align_beg                  297 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  718 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       297 
_struct_ref_seq.pdbx_auth_seq_align_end       718 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             9CVO 
_struct_ref_seq_dif.mon_id                       ALA 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      53 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P29476 
_struct_ref_seq_dif.db_mon_id                    ARG 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          349 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            349 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 19  ? SER A 24  ? THR A 315 SER A 320 5 ? 6  
HELX_P HELX_P2  AA2 THR A 54  ? ILE A 73  ? THR A 350 ILE A 369 1 ? 20 
HELX_P HELX_P3  AA3 SER A 78  ? SER A 96  ? SER A 374 SER A 392 1 ? 19 
HELX_P HELX_P4  AA4 LYS A 101 ? ASN A 115 ? LYS A 397 ASN A 411 1 ? 15 
HELX_P HELX_P5  AA5 GLY A 121 ? TRP A 125 ? GLY A 417 TRP A 421 5 ? 5  
HELX_P HELX_P6  AA6 THR A 138 ? ASN A 155 ? THR A 434 ASN A 451 1 ? 18 
HELX_P HELX_P7  AA7 LYS A 156 ? ASN A 158 ? LYS A 452 ASN A 454 5 ? 3  
HELX_P HELX_P8  AA8 ASN A 202 ? GLN A 212 ? ASN A 498 GLN A 508 1 ? 11 
HELX_P HELX_P9  AA9 PRO A 241 ? VAL A 245 ? PRO A 537 VAL A 541 5 ? 5  
HELX_P HELX_P10 AB1 ASP A 256 ? GLY A 262 ? ASP A 552 GLY A 558 1 ? 7  
HELX_P HELX_P11 AB2 GLY A 294 ? VAL A 299 ? GLY A 590 VAL A 595 1 ? 6  
HELX_P HELX_P12 AB3 VAL A 299 ? ASP A 304 ? VAL A 595 ASP A 600 1 ? 6  
HELX_P HELX_P13 AB4 ILE A 310 ? LYS A 317 ? ILE A 606 LYS A 613 1 ? 8  
HELX_P HELX_P14 AB5 LEU A 328 ? SER A 347 ? LEU A 624 SER A 643 1 ? 20 
HELX_P HELX_P15 AB6 ASP A 354 ? GLY A 374 ? ASP A 650 GLY A 670 1 ? 21 
HELX_P HELX_P16 AB7 ASP A 379 ? VAL A 384 ? ASP A 675 VAL A 680 1 ? 6  
HELX_P HELX_P17 AB8 SER A 388 ? THR A 392 ? SER A 684 THR A 688 5 ? 5  
HELX_P HELX_P18 AB9 ASP A 413 ? HIS A 418 ? ASP A 709 HIS A 714 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 30  SG ? ? ? 1_555 D ZN  . ZN ? ? A CYS 326 A ZN  803 1_555 ? ? ? ? ? ? ? 2.427 ? ? 
metalc2 metalc ? ? A CYS 30  SG ? ? ? 1_555 D ZN  . ZN ? ? A CYS 326 A ZN  803 3_455 ? ? ? ? ? ? ? 2.425 ? ? 
metalc3 metalc ? ? A CYS 35  SG ? ? ? 1_555 D ZN  . ZN ? ? A CYS 331 A ZN  803 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc4 metalc ? ? A CYS 35  SG ? ? ? 1_555 D ZN  . ZN ? ? A CYS 331 A ZN  803 3_455 ? ? ? ? ? ? ? 2.338 ? ? 
metalc5 metalc ? ? A CYS 119 SG ? ? ? 1_555 B HEM . FE ? ? A CYS 415 A HEM 801 1_555 ? ? ? ? ? ? ? 2.398 ? ? 
# 
_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 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 30 ? A CYS 326 ? 1_555 0.0   ? 
2  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 111.4 ? 
3  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 111.4 ? 
4  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 111.4 ? 
5  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 111.4 ? 
6  SG ? A CYS 35  ? A CYS 331 ? 1_555 ZN ? D ZN  . ? A ZN  803 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 0.0   ? 
7  SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NA ? B HEM .  ? A HEM 801 ? 1_555 99.1  ? 
8  SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NB ? B HEM .  ? A HEM 801 ? 1_555 96.7  ? 
9  NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NB ? B HEM .  ? A HEM 801 ? 1_555 85.6  ? 
10 SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NC ? B HEM .  ? A HEM 801 ? 1_555 95.3  ? 
11 NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NC ? B HEM .  ? A HEM 801 ? 1_555 165.3 ? 
12 NB ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NC ? B HEM .  ? A HEM 801 ? 1_555 90.3  ? 
13 SG ? A CYS 119 ? A CYS 415 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 99.1  ? 
14 NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 91.5  ? 
15 NB ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 164.2 ? 
16 NC ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 88.6  ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          THR 
_struct_mon_prot_cis.label_seq_id           405 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           THR 
_struct_mon_prot_cis.auth_seq_id            701 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    406 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     702 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -2.64 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 2 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
AA7 ? 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 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LYS A 6   ? LYS A 8   ? LYS A 302 LYS A 304 
AA1 2 VAL A 15  ? THR A 17  ? VAL A 311 THR A 313 
AA2 1 GLN A 129 ? ASP A 132 ? GLN A 425 ASP A 428 
AA2 2 ALA A 162 ? ILE A 165 ? ALA A 458 ILE A 461 
AA2 3 PHE A 288 ? SER A 289 ? PHE A 584 SER A 585 
AA2 4 ALA A 270 ? VAL A 271 ? ALA A 566 VAL A 567 
AA3 1 ARG A 177 ? VAL A 178 ? ARG A 473 VAL A 474 
AA3 2 LEU A 226 ? GLN A 229 ? LEU A 522 GLN A 525 
AA3 3 GLU A 236 ? PHE A 238 ? GLU A 532 PHE A 534 
AA4 1 GLY A 188 ? LYS A 190 ? GLY A 484 LYS A 486 
AA4 2 THR A 196 ? GLY A 198 ? THR A 492 GLY A 494 
AA5 1 GLU A 247 ? PRO A 249 ? GLU A 543 PRO A 545 
AA5 2 LYS A 264 ? TYR A 266 ? LYS A 560 TYR A 562 
AA6 1 LEU A 281 ? PHE A 283 ? LEU A 577 PHE A 579 
AA6 2 LEU A 275 ? ILE A 278 ? LEU A 571 ILE A 574 
AA6 3 SER A 407 ? GLU A 409 ? SER A 703 GLU A 705 
AA7 1 TYR A 292 ? MET A 293 ? TYR A 588 MET A 589 
AA7 2 ILE A 352 ? VAL A 353 ? ILE A 648 VAL A 649 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 7   ? N VAL A 303 O LEU A 16  ? O LEU A 312 
AA2 1 2 N PHE A 131 ? N PHE A 427 O ILE A 163 ? O ILE A 459 
AA2 2 3 N ALA A 162 ? N ALA A 458 O SER A 289 ? O SER A 585 
AA2 3 4 O PHE A 288 ? O PHE A 584 N VAL A 271 ? N VAL A 567 
AA3 1 2 N ARG A 177 ? N ARG A 473 O GLN A 229 ? O GLN A 525 
AA3 2 3 N LEU A 226 ? N LEU A 522 O PHE A 238 ? O PHE A 534 
AA4 1 2 N TYR A 189 ? N TYR A 485 O LEU A 197 ? O LEU A 493 
AA5 1 2 N VAL A 248 ? N VAL A 544 O TRP A 265 ? O TRP A 561 
AA6 1 2 O LEU A 281 ? O LEU A 577 N ILE A 278 ? N ILE A 574 
AA6 2 3 N LEU A 275 ? N LEU A 571 O GLU A 409 ? O GLU A 705 
AA7 1 2 N TYR A 292 ? N TYR A 588 O VAL A 353 ? O VAL A 649 
# 
_pdbx_entry_details.entry_id                   9CVO 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 309 ? ? 54.79   12.28   
2  1 THR A 321 ? ? -135.41 -46.95  
3  1 LEU A 337 ? ? -118.19 77.83   
4  1 SER A 374 ? ? -66.55  -173.82 
5  1 ALA A 412 ? ? -66.98  94.26   
6  1 THR A 466 ? ? -113.17 -81.37  
7  1 SER A 491 ? ? -67.82  -171.53 
8  1 PRO A 513 ? ? -77.44  40.81   
9  1 ARG A 514 ? ? -19.92  70.31   
10 1 ARG A 516 ? ? -89.12  -82.89  
11 1 LYS A 550 ? ? -141.93 -65.05  
12 1 CYS A 582 ? ? -150.19 53.47   
13 1 ARG A 603 ? ? -109.81 -133.28 
14 1 LYS A 613 ? ? -68.04  0.26    
15 1 ASP A 615 ? ? 54.80   84.69   
16 1 ASP A 617 ? ? -64.86  88.78   
17 1 VAL A 715 ? ? -63.97  97.22   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    ZN 
_pdbx_struct_special_symmetry.auth_seq_id     803 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   D 
_pdbx_struct_special_symmetry.label_comp_id   ZN 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -23.5421 
_pdbx_refine_tls.origin_y         -4.8820 
_pdbx_refine_tls.origin_z         22.1931 
_pdbx_refine_tls.T[1][1]          0.3744 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0501 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0741 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.3838 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0342 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.4753 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.8801 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.1789 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.0958 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.9491 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.2821 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          8.2146 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0365 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.1312 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0073 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0006 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0682 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0340 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.7298 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1649 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0612 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '(chain A and resid 299:716)' 
# 
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 CYS 297 ? A CYS 1   
2  1 Y 1 A PRO 298 ? A PRO 2   
3  1 Y 1 A GLN 340 ? A GLN 44  
4  1 Y 1 A HIS 341 ? A HIS 45  
5  1 Y 1 A THR 342 ? A THR 46  
6  1 Y 1 A ARG 343 ? A ARG 47  
7  1 Y 1 A LYS 344 ? A LYS 48  
8  1 Y 1 A PRO 345 ? A PRO 49  
9  1 Y 1 A GLU 346 ? A GLU 50  
10 1 Y 1 A ASP 347 ? A ASP 51  
11 1 Y 1 A GLY 718 ? A GLY 422 
# 
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 
A1A0K C11  C  Y N 1   
A1A0K C12  C  Y N 2   
A1A0K C13  C  Y N 3   
A1A0K C14  C  Y N 4   
A1A0K C15  C  Y N 5   
A1A0K C16  C  Y N 6   
A1A0K C17  C  N N 7   
A1A0K C02  C  Y N 8   
A1A0K C03  C  Y N 9   
A1A0K C04  C  Y N 10  
A1A0K C05  C  Y N 11  
A1A0K C06  C  Y N 12  
A1A0K C07  C  N N 13  
A1A0K C19  C  N N 14  
A1A0K C20  C  N N 15  
A1A0K F12  F  N N 16  
A1A0K F13  F  N N 17  
A1A0K N01  N  Y N 18  
A1A0K N02  N  N N 19  
A1A0K N18  N  N N 20  
A1A0K H1   H  N N 21  
A1A0K H2   H  N N 22  
A1A0K H3   H  N N 23  
A1A0K H4   H  N N 24  
A1A0K H5   H  N N 25  
A1A0K H6   H  N N 26  
A1A0K H7   H  N N 27  
A1A0K H8   H  N N 28  
A1A0K H9   H  N N 29  
A1A0K H10  H  N N 30  
A1A0K H11  H  N N 31  
A1A0K H12  H  N N 32  
A1A0K H13  H  N N 33  
A1A0K H14  H  N N 34  
A1A0K H15  H  N N 35  
A1A0K H16  H  N N 36  
A1A0K H17  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
GLN   N    N  N N 125 
GLN   CA   C  N S 126 
GLN   C    C  N N 127 
GLN   O    O  N N 128 
GLN   CB   C  N N 129 
GLN   CG   C  N N 130 
GLN   CD   C  N N 131 
GLN   OE1  O  N N 132 
GLN   NE2  N  N N 133 
GLN   OXT  O  N N 134 
GLN   H    H  N N 135 
GLN   H2   H  N N 136 
GLN   HA   H  N N 137 
GLN   HB2  H  N N 138 
GLN   HB3  H  N N 139 
GLN   HG2  H  N N 140 
GLN   HG3  H  N N 141 
GLN   HE21 H  N N 142 
GLN   HE22 H  N N 143 
GLN   HXT  H  N N 144 
GLU   N    N  N N 145 
GLU   CA   C  N S 146 
GLU   C    C  N N 147 
GLU   O    O  N N 148 
GLU   CB   C  N N 149 
GLU   CG   C  N N 150 
GLU   CD   C  N N 151 
GLU   OE1  O  N N 152 
GLU   OE2  O  N N 153 
GLU   OXT  O  N N 154 
GLU   H    H  N N 155 
GLU   H2   H  N N 156 
GLU   HA   H  N N 157 
GLU   HB2  H  N N 158 
GLU   HB3  H  N N 159 
GLU   HG2  H  N N 160 
GLU   HG3  H  N N 161 
GLU   HE2  H  N N 162 
GLU   HXT  H  N N 163 
GLY   N    N  N N 164 
GLY   CA   C  N N 165 
GLY   C    C  N N 166 
GLY   O    O  N N 167 
GLY   OXT  O  N N 168 
GLY   H    H  N N 169 
GLY   H2   H  N N 170 
GLY   HA2  H  N N 171 
GLY   HA3  H  N N 172 
GLY   HXT  H  N N 173 
H4B   N1   N  Y N 174 
H4B   C2   C  Y N 175 
H4B   N2   N  N N 176 
H4B   N3   N  Y N 177 
H4B   C4   C  Y N 178 
H4B   O4   O  N N 179 
H4B   C4A  C  Y N 180 
H4B   C8A  C  Y N 181 
H4B   N5   N  N N 182 
H4B   N8   N  N N 183 
H4B   C6   C  N R 184 
H4B   C7   C  N N 185 
H4B   C9   C  N R 186 
H4B   O9   O  N N 187 
H4B   C10  C  N S 188 
H4B   C11  C  N N 189 
H4B   O10  O  N N 190 
H4B   HN21 H  N N 191 
H4B   HN22 H  N N 192 
H4B   HN3  H  N N 193 
H4B   HN5  H  N N 194 
H4B   HN8  H  N N 195 
H4B   H6   H  N N 196 
H4B   H71  H  N N 197 
H4B   H72  H  N N 198 
H4B   H9   H  N N 199 
H4B   HO9  H  N N 200 
H4B   H10  H  N N 201 
H4B   H111 H  N N 202 
H4B   H112 H  N N 203 
H4B   H113 H  N N 204 
H4B   HO0  H  N N 205 
HEM   CHA  C  N N 206 
HEM   CHB  C  N N 207 
HEM   CHC  C  N N 208 
HEM   CHD  C  N N 209 
HEM   C1A  C  Y N 210 
HEM   C2A  C  Y N 211 
HEM   C3A  C  Y N 212 
HEM   C4A  C  Y N 213 
HEM   CMA  C  N N 214 
HEM   CAA  C  N N 215 
HEM   CBA  C  N N 216 
HEM   CGA  C  N N 217 
HEM   O1A  O  N N 218 
HEM   O2A  O  N N 219 
HEM   C1B  C  N N 220 
HEM   C2B  C  N N 221 
HEM   C3B  C  N N 222 
HEM   C4B  C  N N 223 
HEM   CMB  C  N N 224 
HEM   CAB  C  N N 225 
HEM   CBB  C  N N 226 
HEM   C1C  C  Y N 227 
HEM   C2C  C  Y N 228 
HEM   C3C  C  Y N 229 
HEM   C4C  C  Y N 230 
HEM   CMC  C  N N 231 
HEM   CAC  C  N N 232 
HEM   CBC  C  N N 233 
HEM   C1D  C  N N 234 
HEM   C2D  C  N N 235 
HEM   C3D  C  N N 236 
HEM   C4D  C  N N 237 
HEM   CMD  C  N N 238 
HEM   CAD  C  N N 239 
HEM   CBD  C  N N 240 
HEM   CGD  C  N N 241 
HEM   O1D  O  N N 242 
HEM   O2D  O  N N 243 
HEM   NA   N  Y N 244 
HEM   NB   N  N N 245 
HEM   NC   N  Y N 246 
HEM   ND   N  N N 247 
HEM   FE   FE N N 248 
HEM   HHB  H  N N 249 
HEM   HHC  H  N N 250 
HEM   HHD  H  N N 251 
HEM   HMA  H  N N 252 
HEM   HMAA H  N N 253 
HEM   HMAB H  N N 254 
HEM   HAA  H  N N 255 
HEM   HAAA H  N N 256 
HEM   HBA  H  N N 257 
HEM   HBAA H  N N 258 
HEM   HMB  H  N N 259 
HEM   HMBA H  N N 260 
HEM   HMBB H  N N 261 
HEM   HAB  H  N N 262 
HEM   HBB  H  N N 263 
HEM   HBBA H  N N 264 
HEM   HMC  H  N N 265 
HEM   HMCA H  N N 266 
HEM   HMCB H  N N 267 
HEM   HAC  H  N N 268 
HEM   HBC  H  N N 269 
HEM   HBCA H  N N 270 
HEM   HMD  H  N N 271 
HEM   HMDA H  N N 272 
HEM   HMDB H  N N 273 
HEM   HAD  H  N N 274 
HEM   HADA H  N N 275 
HEM   HBD  H  N N 276 
HEM   HBDA H  N N 277 
HEM   H2A  H  N N 278 
HEM   H2D  H  N N 279 
HEM   HHA  H  N N 280 
HIS   N    N  N N 281 
HIS   CA   C  N S 282 
HIS   C    C  N N 283 
HIS   O    O  N N 284 
HIS   CB   C  N N 285 
HIS   CG   C  Y N 286 
HIS   ND1  N  Y N 287 
HIS   CD2  C  Y N 288 
HIS   CE1  C  Y N 289 
HIS   NE2  N  Y N 290 
HIS   OXT  O  N N 291 
HIS   H    H  N N 292 
HIS   H2   H  N N 293 
HIS   HA   H  N N 294 
HIS   HB2  H  N N 295 
HIS   HB3  H  N N 296 
HIS   HD1  H  N N 297 
HIS   HD2  H  N N 298 
HIS   HE1  H  N N 299 
HIS   HE2  H  N N 300 
HIS   HXT  H  N N 301 
HOH   O    O  N N 302 
HOH   H1   H  N N 303 
HOH   H2   H  N N 304 
ILE   N    N  N N 305 
ILE   CA   C  N S 306 
ILE   C    C  N N 307 
ILE   O    O  N N 308 
ILE   CB   C  N S 309 
ILE   CG1  C  N N 310 
ILE   CG2  C  N N 311 
ILE   CD1  C  N N 312 
ILE   OXT  O  N N 313 
ILE   H    H  N N 314 
ILE   H2   H  N N 315 
ILE   HA   H  N N 316 
ILE   HB   H  N N 317 
ILE   HG12 H  N N 318 
ILE   HG13 H  N N 319 
ILE   HG21 H  N N 320 
ILE   HG22 H  N N 321 
ILE   HG23 H  N N 322 
ILE   HD11 H  N N 323 
ILE   HD12 H  N N 324 
ILE   HD13 H  N N 325 
ILE   HXT  H  N N 326 
LEU   N    N  N N 327 
LEU   CA   C  N S 328 
LEU   C    C  N N 329 
LEU   O    O  N N 330 
LEU   CB   C  N N 331 
LEU   CG   C  N N 332 
LEU   CD1  C  N N 333 
LEU   CD2  C  N N 334 
LEU   OXT  O  N N 335 
LEU   H    H  N N 336 
LEU   H2   H  N N 337 
LEU   HA   H  N N 338 
LEU   HB2  H  N N 339 
LEU   HB3  H  N N 340 
LEU   HG   H  N N 341 
LEU   HD11 H  N N 342 
LEU   HD12 H  N N 343 
LEU   HD13 H  N N 344 
LEU   HD21 H  N N 345 
LEU   HD22 H  N N 346 
LEU   HD23 H  N N 347 
LEU   HXT  H  N N 348 
LYS   N    N  N N 349 
LYS   CA   C  N S 350 
LYS   C    C  N N 351 
LYS   O    O  N N 352 
LYS   CB   C  N N 353 
LYS   CG   C  N N 354 
LYS   CD   C  N N 355 
LYS   CE   C  N N 356 
LYS   NZ   N  N N 357 
LYS   OXT  O  N N 358 
LYS   H    H  N N 359 
LYS   H2   H  N N 360 
LYS   HA   H  N N 361 
LYS   HB2  H  N N 362 
LYS   HB3  H  N N 363 
LYS   HG2  H  N N 364 
LYS   HG3  H  N N 365 
LYS   HD2  H  N N 366 
LYS   HD3  H  N N 367 
LYS   HE2  H  N N 368 
LYS   HE3  H  N N 369 
LYS   HZ1  H  N N 370 
LYS   HZ2  H  N N 371 
LYS   HZ3  H  N N 372 
LYS   HXT  H  N N 373 
MET   N    N  N N 374 
MET   CA   C  N S 375 
MET   C    C  N N 376 
MET   O    O  N N 377 
MET   CB   C  N N 378 
MET   CG   C  N N 379 
MET   SD   S  N N 380 
MET   CE   C  N N 381 
MET   OXT  O  N N 382 
MET   H    H  N N 383 
MET   H2   H  N N 384 
MET   HA   H  N N 385 
MET   HB2  H  N N 386 
MET   HB3  H  N N 387 
MET   HG2  H  N N 388 
MET   HG3  H  N N 389 
MET   HE1  H  N N 390 
MET   HE2  H  N N 391 
MET   HE3  H  N N 392 
MET   HXT  H  N N 393 
PHE   N    N  N N 394 
PHE   CA   C  N S 395 
PHE   C    C  N N 396 
PHE   O    O  N N 397 
PHE   CB   C  N N 398 
PHE   CG   C  Y N 399 
PHE   CD1  C  Y N 400 
PHE   CD2  C  Y N 401 
PHE   CE1  C  Y N 402 
PHE   CE2  C  Y N 403 
PHE   CZ   C  Y N 404 
PHE   OXT  O  N N 405 
PHE   H    H  N N 406 
PHE   H2   H  N N 407 
PHE   HA   H  N N 408 
PHE   HB2  H  N N 409 
PHE   HB3  H  N N 410 
PHE   HD1  H  N N 411 
PHE   HD2  H  N N 412 
PHE   HE1  H  N N 413 
PHE   HE2  H  N N 414 
PHE   HZ   H  N N 415 
PHE   HXT  H  N N 416 
PRO   N    N  N N 417 
PRO   CA   C  N S 418 
PRO   C    C  N N 419 
PRO   O    O  N N 420 
PRO   CB   C  N N 421 
PRO   CG   C  N N 422 
PRO   CD   C  N N 423 
PRO   OXT  O  N N 424 
PRO   H    H  N N 425 
PRO   HA   H  N N 426 
PRO   HB2  H  N N 427 
PRO   HB3  H  N N 428 
PRO   HG2  H  N N 429 
PRO   HG3  H  N N 430 
PRO   HD2  H  N N 431 
PRO   HD3  H  N N 432 
PRO   HXT  H  N N 433 
SER   N    N  N N 434 
SER   CA   C  N S 435 
SER   C    C  N N 436 
SER   O    O  N N 437 
SER   CB   C  N N 438 
SER   OG   O  N N 439 
SER   OXT  O  N N 440 
SER   H    H  N N 441 
SER   H2   H  N N 442 
SER   HA   H  N N 443 
SER   HB2  H  N N 444 
SER   HB3  H  N N 445 
SER   HG   H  N N 446 
SER   HXT  H  N N 447 
THR   N    N  N N 448 
THR   CA   C  N S 449 
THR   C    C  N N 450 
THR   O    O  N N 451 
THR   CB   C  N R 452 
THR   OG1  O  N N 453 
THR   CG2  C  N N 454 
THR   OXT  O  N N 455 
THR   H    H  N N 456 
THR   H2   H  N N 457 
THR   HA   H  N N 458 
THR   HB   H  N N 459 
THR   HG1  H  N N 460 
THR   HG21 H  N N 461 
THR   HG22 H  N N 462 
THR   HG23 H  N N 463 
THR   HXT  H  N N 464 
TRP   N    N  N N 465 
TRP   CA   C  N S 466 
TRP   C    C  N N 467 
TRP   O    O  N N 468 
TRP   CB   C  N N 469 
TRP   CG   C  Y N 470 
TRP   CD1  C  Y N 471 
TRP   CD2  C  Y N 472 
TRP   NE1  N  Y N 473 
TRP   CE2  C  Y N 474 
TRP   CE3  C  Y N 475 
TRP   CZ2  C  Y N 476 
TRP   CZ3  C  Y N 477 
TRP   CH2  C  Y N 478 
TRP   OXT  O  N N 479 
TRP   H    H  N N 480 
TRP   H2   H  N N 481 
TRP   HA   H  N N 482 
TRP   HB2  H  N N 483 
TRP   HB3  H  N N 484 
TRP   HD1  H  N N 485 
TRP   HE1  H  N N 486 
TRP   HE3  H  N N 487 
TRP   HZ2  H  N N 488 
TRP   HZ3  H  N N 489 
TRP   HH2  H  N N 490 
TRP   HXT  H  N N 491 
TYR   N    N  N N 492 
TYR   CA   C  N S 493 
TYR   C    C  N N 494 
TYR   O    O  N N 495 
TYR   CB   C  N N 496 
TYR   CG   C  Y N 497 
TYR   CD1  C  Y N 498 
TYR   CD2  C  Y N 499 
TYR   CE1  C  Y N 500 
TYR   CE2  C  Y N 501 
TYR   CZ   C  Y N 502 
TYR   OH   O  N N 503 
TYR   OXT  O  N N 504 
TYR   H    H  N N 505 
TYR   H2   H  N N 506 
TYR   HA   H  N N 507 
TYR   HB2  H  N N 508 
TYR   HB3  H  N N 509 
TYR   HD1  H  N N 510 
TYR   HD2  H  N N 511 
TYR   HE1  H  N N 512 
TYR   HE2  H  N N 513 
TYR   HH   H  N N 514 
TYR   HXT  H  N N 515 
VAL   N    N  N N 516 
VAL   CA   C  N S 517 
VAL   C    C  N N 518 
VAL   O    O  N N 519 
VAL   CB   C  N N 520 
VAL   CG1  C  N N 521 
VAL   CG2  C  N N 522 
VAL   OXT  O  N N 523 
VAL   H    H  N N 524 
VAL   H2   H  N N 525 
VAL   HA   H  N N 526 
VAL   HB   H  N N 527 
VAL   HG11 H  N N 528 
VAL   HG12 H  N N 529 
VAL   HG13 H  N N 530 
VAL   HG21 H  N N 531 
VAL   HG22 H  N N 532 
VAL   HG23 H  N N 533 
VAL   HXT  H  N N 534 
ZN    ZN   ZN N N 535 
# 
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 
A1A0K C07 C04  sing N N 1   
A1A0K C04 C05  doub Y N 2   
A1A0K C04 C03  sing Y N 3   
A1A0K C05 C06  sing Y N 4   
A1A0K C03 C02  doub Y N 5   
A1A0K F12 C12  sing N N 6   
A1A0K C06 C11  sing N N 7   
A1A0K C06 N01  doub Y N 8   
A1A0K C02 N01  sing Y N 9   
A1A0K C02 N02  sing N N 10  
A1A0K C12 C11  doub Y N 11  
A1A0K C12 C13  sing Y N 12  
A1A0K C11 C16  sing Y N 13  
A1A0K C19 N18  sing N N 14  
A1A0K F13 C13  sing N N 15  
A1A0K C13 C14  doub Y N 16  
A1A0K C16 C15  doub Y N 17  
A1A0K C14 C15  sing Y N 18  
A1A0K C15 C17  sing N N 19  
A1A0K N18 C17  sing N N 20  
A1A0K N18 C20  sing N N 21  
A1A0K C14 H1   sing N N 22  
A1A0K C16 H2   sing N N 23  
A1A0K C17 H3   sing N N 24  
A1A0K C17 H4   sing N N 25  
A1A0K C03 H5   sing N N 26  
A1A0K C05 H6   sing N N 27  
A1A0K C07 H7   sing N N 28  
A1A0K C07 H8   sing N N 29  
A1A0K C07 H9   sing N N 30  
A1A0K C19 H10  sing N N 31  
A1A0K C19 H11  sing N N 32  
A1A0K C19 H12  sing N N 33  
A1A0K C20 H13  sing N N 34  
A1A0K C20 H14  sing N N 35  
A1A0K C20 H15  sing N N 36  
A1A0K N02 H16  sing N N 37  
A1A0K N02 H17  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
GLN   N   CA   sing N N 121 
GLN   N   H    sing N N 122 
GLN   N   H2   sing N N 123 
GLN   CA  C    sing N N 124 
GLN   CA  CB   sing N N 125 
GLN   CA  HA   sing N N 126 
GLN   C   O    doub N N 127 
GLN   C   OXT  sing N N 128 
GLN   CB  CG   sing N N 129 
GLN   CB  HB2  sing N N 130 
GLN   CB  HB3  sing N N 131 
GLN   CG  CD   sing N N 132 
GLN   CG  HG2  sing N N 133 
GLN   CG  HG3  sing N N 134 
GLN   CD  OE1  doub N N 135 
GLN   CD  NE2  sing N N 136 
GLN   NE2 HE21 sing N N 137 
GLN   NE2 HE22 sing N N 138 
GLN   OXT HXT  sing N N 139 
GLU   N   CA   sing N N 140 
GLU   N   H    sing N N 141 
GLU   N   H2   sing N N 142 
GLU   CA  C    sing N N 143 
GLU   CA  CB   sing N N 144 
GLU   CA  HA   sing N N 145 
GLU   C   O    doub N N 146 
GLU   C   OXT  sing N N 147 
GLU   CB  CG   sing N N 148 
GLU   CB  HB2  sing N N 149 
GLU   CB  HB3  sing N N 150 
GLU   CG  CD   sing N N 151 
GLU   CG  HG2  sing N N 152 
GLU   CG  HG3  sing N N 153 
GLU   CD  OE1  doub N N 154 
GLU   CD  OE2  sing N N 155 
GLU   OE2 HE2  sing N N 156 
GLU   OXT HXT  sing N N 157 
GLY   N   CA   sing N N 158 
GLY   N   H    sing N N 159 
GLY   N   H2   sing N N 160 
GLY   CA  C    sing N N 161 
GLY   CA  HA2  sing N N 162 
GLY   CA  HA3  sing N N 163 
GLY   C   O    doub N N 164 
GLY   C   OXT  sing N N 165 
GLY   OXT HXT  sing N N 166 
H4B   N1  C2   doub Y N 167 
H4B   N1  C8A  sing Y N 168 
H4B   C2  N2   sing N N 169 
H4B   C2  N3   sing Y N 170 
H4B   N2  HN21 sing N N 171 
H4B   N2  HN22 sing N N 172 
H4B   N3  C4   sing Y N 173 
H4B   N3  HN3  sing N N 174 
H4B   C4  O4   doub N N 175 
H4B   C4  C4A  sing Y N 176 
H4B   C4A C8A  doub Y N 177 
H4B   C4A N5   sing N N 178 
H4B   C8A N8   sing N N 179 
H4B   N5  C6   sing N N 180 
H4B   N5  HN5  sing N N 181 
H4B   N8  C7   sing N N 182 
H4B   N8  HN8  sing N N 183 
H4B   C6  C7   sing N N 184 
H4B   C6  C9   sing N N 185 
H4B   C6  H6   sing N N 186 
H4B   C7  H71  sing N N 187 
H4B   C7  H72  sing N N 188 
H4B   C9  O9   sing N N 189 
H4B   C9  C10  sing N N 190 
H4B   C9  H9   sing N N 191 
H4B   O9  HO9  sing N N 192 
H4B   C10 C11  sing N N 193 
H4B   C10 O10  sing N N 194 
H4B   C10 H10  sing N N 195 
H4B   C11 H111 sing N N 196 
H4B   C11 H112 sing N N 197 
H4B   C11 H113 sing N N 198 
H4B   O10 HO0  sing N N 199 
HEM   CHA C1A  sing N N 200 
HEM   CHA C4D  doub N N 201 
HEM   CHA HHA  sing N N 202 
HEM   CHB C4A  sing N N 203 
HEM   CHB C1B  doub N N 204 
HEM   CHB HHB  sing N N 205 
HEM   CHC C4B  sing N N 206 
HEM   CHC C1C  doub N N 207 
HEM   CHC HHC  sing N N 208 
HEM   CHD C4C  doub N N 209 
HEM   CHD C1D  sing N N 210 
HEM   CHD HHD  sing N N 211 
HEM   C1A C2A  doub Y N 212 
HEM   C1A NA   sing Y N 213 
HEM   C2A C3A  sing Y N 214 
HEM   C2A CAA  sing N N 215 
HEM   C3A C4A  doub Y N 216 
HEM   C3A CMA  sing N N 217 
HEM   C4A NA   sing Y N 218 
HEM   CMA HMA  sing N N 219 
HEM   CMA HMAA sing N N 220 
HEM   CMA HMAB sing N N 221 
HEM   CAA CBA  sing N N 222 
HEM   CAA HAA  sing N N 223 
HEM   CAA HAAA sing N N 224 
HEM   CBA CGA  sing N N 225 
HEM   CBA HBA  sing N N 226 
HEM   CBA HBAA sing N N 227 
HEM   CGA O1A  doub N N 228 
HEM   CGA O2A  sing N N 229 
HEM   C1B C2B  sing N N 230 
HEM   C1B NB   sing N N 231 
HEM   C2B C3B  doub N N 232 
HEM   C2B CMB  sing N N 233 
HEM   C3B C4B  sing N N 234 
HEM   C3B CAB  sing N N 235 
HEM   C4B NB   doub N N 236 
HEM   CMB HMB  sing N N 237 
HEM   CMB HMBA sing N N 238 
HEM   CMB HMBB sing N N 239 
HEM   CAB CBB  doub N N 240 
HEM   CAB HAB  sing N N 241 
HEM   CBB HBB  sing N N 242 
HEM   CBB HBBA sing N N 243 
HEM   C1C C2C  sing Y N 244 
HEM   C1C NC   sing Y N 245 
HEM   C2C C3C  doub Y N 246 
HEM   C2C CMC  sing N N 247 
HEM   C3C C4C  sing Y N 248 
HEM   C3C CAC  sing N N 249 
HEM   C4C NC   sing Y N 250 
HEM   CMC HMC  sing N N 251 
HEM   CMC HMCA sing N N 252 
HEM   CMC HMCB sing N N 253 
HEM   CAC CBC  doub N N 254 
HEM   CAC HAC  sing N N 255 
HEM   CBC HBC  sing N N 256 
HEM   CBC HBCA sing N N 257 
HEM   C1D C2D  sing N N 258 
HEM   C1D ND   doub N N 259 
HEM   C2D C3D  doub N N 260 
HEM   C2D CMD  sing N N 261 
HEM   C3D C4D  sing N N 262 
HEM   C3D CAD  sing N N 263 
HEM   C4D ND   sing N N 264 
HEM   CMD HMD  sing N N 265 
HEM   CMD HMDA sing N N 266 
HEM   CMD HMDB sing N N 267 
HEM   CAD CBD  sing N N 268 
HEM   CAD HAD  sing N N 269 
HEM   CAD HADA sing N N 270 
HEM   CBD CGD  sing N N 271 
HEM   CBD HBD  sing N N 272 
HEM   CBD HBDA sing N N 273 
HEM   CGD O1D  doub N N 274 
HEM   CGD O2D  sing N N 275 
HEM   O2A H2A  sing N N 276 
HEM   O2D H2D  sing N N 277 
HEM   FE  NA   sing N N 278 
HEM   FE  NB   sing N N 279 
HEM   FE  NC   sing N N 280 
HEM   FE  ND   sing N N 281 
HIS   N   CA   sing N N 282 
HIS   N   H    sing N N 283 
HIS   N   H2   sing N N 284 
HIS   CA  C    sing N N 285 
HIS   CA  CB   sing N N 286 
HIS   CA  HA   sing N N 287 
HIS   C   O    doub N N 288 
HIS   C   OXT  sing N N 289 
HIS   CB  CG   sing N N 290 
HIS   CB  HB2  sing N N 291 
HIS   CB  HB3  sing N N 292 
HIS   CG  ND1  sing Y N 293 
HIS   CG  CD2  doub Y N 294 
HIS   ND1 CE1  doub Y N 295 
HIS   ND1 HD1  sing N N 296 
HIS   CD2 NE2  sing Y N 297 
HIS   CD2 HD2  sing N N 298 
HIS   CE1 NE2  sing Y N 299 
HIS   CE1 HE1  sing N N 300 
HIS   NE2 HE2  sing N N 301 
HIS   OXT HXT  sing N N 302 
HOH   O   H1   sing N N 303 
HOH   O   H2   sing N N 304 
ILE   N   CA   sing N N 305 
ILE   N   H    sing N N 306 
ILE   N   H2   sing N N 307 
ILE   CA  C    sing N N 308 
ILE   CA  CB   sing N N 309 
ILE   CA  HA   sing N N 310 
ILE   C   O    doub N N 311 
ILE   C   OXT  sing N N 312 
ILE   CB  CG1  sing N N 313 
ILE   CB  CG2  sing N N 314 
ILE   CB  HB   sing N N 315 
ILE   CG1 CD1  sing N N 316 
ILE   CG1 HG12 sing N N 317 
ILE   CG1 HG13 sing N N 318 
ILE   CG2 HG21 sing N N 319 
ILE   CG2 HG22 sing N N 320 
ILE   CG2 HG23 sing N N 321 
ILE   CD1 HD11 sing N N 322 
ILE   CD1 HD12 sing N N 323 
ILE   CD1 HD13 sing N N 324 
ILE   OXT HXT  sing N N 325 
LEU   N   CA   sing N N 326 
LEU   N   H    sing N N 327 
LEU   N   H2   sing N N 328 
LEU   CA  C    sing N N 329 
LEU   CA  CB   sing N N 330 
LEU   CA  HA   sing N N 331 
LEU   C   O    doub N N 332 
LEU   C   OXT  sing N N 333 
LEU   CB  CG   sing N N 334 
LEU   CB  HB2  sing N N 335 
LEU   CB  HB3  sing N N 336 
LEU   CG  CD1  sing N N 337 
LEU   CG  CD2  sing N N 338 
LEU   CG  HG   sing N N 339 
LEU   CD1 HD11 sing N N 340 
LEU   CD1 HD12 sing N N 341 
LEU   CD1 HD13 sing N N 342 
LEU   CD2 HD21 sing N N 343 
LEU   CD2 HD22 sing N N 344 
LEU   CD2 HD23 sing N N 345 
LEU   OXT HXT  sing N N 346 
LYS   N   CA   sing N N 347 
LYS   N   H    sing N N 348 
LYS   N   H2   sing N N 349 
LYS   CA  C    sing N N 350 
LYS   CA  CB   sing N N 351 
LYS   CA  HA   sing N N 352 
LYS   C   O    doub N N 353 
LYS   C   OXT  sing N N 354 
LYS   CB  CG   sing N N 355 
LYS   CB  HB2  sing N N 356 
LYS   CB  HB3  sing N N 357 
LYS   CG  CD   sing N N 358 
LYS   CG  HG2  sing N N 359 
LYS   CG  HG3  sing N N 360 
LYS   CD  CE   sing N N 361 
LYS   CD  HD2  sing N N 362 
LYS   CD  HD3  sing N N 363 
LYS   CE  NZ   sing N N 364 
LYS   CE  HE2  sing N N 365 
LYS   CE  HE3  sing N N 366 
LYS   NZ  HZ1  sing N N 367 
LYS   NZ  HZ2  sing N N 368 
LYS   NZ  HZ3  sing N N 369 
LYS   OXT HXT  sing N N 370 
MET   N   CA   sing N N 371 
MET   N   H    sing N N 372 
MET   N   H2   sing N N 373 
MET   CA  C    sing N N 374 
MET   CA  CB   sing N N 375 
MET   CA  HA   sing N N 376 
MET   C   O    doub N N 377 
MET   C   OXT  sing N N 378 
MET   CB  CG   sing N N 379 
MET   CB  HB2  sing N N 380 
MET   CB  HB3  sing N N 381 
MET   CG  SD   sing N N 382 
MET   CG  HG2  sing N N 383 
MET   CG  HG3  sing N N 384 
MET   SD  CE   sing N N 385 
MET   CE  HE1  sing N N 386 
MET   CE  HE2  sing N N 387 
MET   CE  HE3  sing N N 388 
MET   OXT HXT  sing N N 389 
PHE   N   CA   sing N N 390 
PHE   N   H    sing N N 391 
PHE   N   H2   sing N N 392 
PHE   CA  C    sing N N 393 
PHE   CA  CB   sing N N 394 
PHE   CA  HA   sing N N 395 
PHE   C   O    doub N N 396 
PHE   C   OXT  sing N N 397 
PHE   CB  CG   sing N N 398 
PHE   CB  HB2  sing N N 399 
PHE   CB  HB3  sing N N 400 
PHE   CG  CD1  doub Y N 401 
PHE   CG  CD2  sing Y N 402 
PHE   CD1 CE1  sing Y N 403 
PHE   CD1 HD1  sing N N 404 
PHE   CD2 CE2  doub Y N 405 
PHE   CD2 HD2  sing N N 406 
PHE   CE1 CZ   doub Y N 407 
PHE   CE1 HE1  sing N N 408 
PHE   CE2 CZ   sing Y N 409 
PHE   CE2 HE2  sing N N 410 
PHE   CZ  HZ   sing N N 411 
PHE   OXT HXT  sing N N 412 
PRO   N   CA   sing N N 413 
PRO   N   CD   sing N N 414 
PRO   N   H    sing N N 415 
PRO   CA  C    sing N N 416 
PRO   CA  CB   sing N N 417 
PRO   CA  HA   sing N N 418 
PRO   C   O    doub N N 419 
PRO   C   OXT  sing N N 420 
PRO   CB  CG   sing N N 421 
PRO   CB  HB2  sing N N 422 
PRO   CB  HB3  sing N N 423 
PRO   CG  CD   sing N N 424 
PRO   CG  HG2  sing N N 425 
PRO   CG  HG3  sing N N 426 
PRO   CD  HD2  sing N N 427 
PRO   CD  HD3  sing N N 428 
PRO   OXT HXT  sing N N 429 
SER   N   CA   sing N N 430 
SER   N   H    sing N N 431 
SER   N   H2   sing N N 432 
SER   CA  C    sing N N 433 
SER   CA  CB   sing N N 434 
SER   CA  HA   sing N N 435 
SER   C   O    doub N N 436 
SER   C   OXT  sing N N 437 
SER   CB  OG   sing N N 438 
SER   CB  HB2  sing N N 439 
SER   CB  HB3  sing N N 440 
SER   OG  HG   sing N N 441 
SER   OXT HXT  sing N N 442 
THR   N   CA   sing N N 443 
THR   N   H    sing N N 444 
THR   N   H2   sing N N 445 
THR   CA  C    sing N N 446 
THR   CA  CB   sing N N 447 
THR   CA  HA   sing N N 448 
THR   C   O    doub N N 449 
THR   C   OXT  sing N N 450 
THR   CB  OG1  sing N N 451 
THR   CB  CG2  sing N N 452 
THR   CB  HB   sing N N 453 
THR   OG1 HG1  sing N N 454 
THR   CG2 HG21 sing N N 455 
THR   CG2 HG22 sing N N 456 
THR   CG2 HG23 sing N N 457 
THR   OXT HXT  sing N N 458 
TRP   N   CA   sing N N 459 
TRP   N   H    sing N N 460 
TRP   N   H2   sing N N 461 
TRP   CA  C    sing N N 462 
TRP   CA  CB   sing N N 463 
TRP   CA  HA   sing N N 464 
TRP   C   O    doub N N 465 
TRP   C   OXT  sing N N 466 
TRP   CB  CG   sing N N 467 
TRP   CB  HB2  sing N N 468 
TRP   CB  HB3  sing N N 469 
TRP   CG  CD1  doub Y N 470 
TRP   CG  CD2  sing Y N 471 
TRP   CD1 NE1  sing Y N 472 
TRP   CD1 HD1  sing N N 473 
TRP   CD2 CE2  doub Y N 474 
TRP   CD2 CE3  sing Y N 475 
TRP   NE1 CE2  sing Y N 476 
TRP   NE1 HE1  sing N N 477 
TRP   CE2 CZ2  sing Y N 478 
TRP   CE3 CZ3  doub Y N 479 
TRP   CE3 HE3  sing N N 480 
TRP   CZ2 CH2  doub Y N 481 
TRP   CZ2 HZ2  sing N N 482 
TRP   CZ3 CH2  sing Y N 483 
TRP   CZ3 HZ3  sing N N 484 
TRP   CH2 HH2  sing N N 485 
TRP   OXT HXT  sing N N 486 
TYR   N   CA   sing N N 487 
TYR   N   H    sing N N 488 
TYR   N   H2   sing N N 489 
TYR   CA  C    sing N N 490 
TYR   CA  CB   sing N N 491 
TYR   CA  HA   sing N N 492 
TYR   C   O    doub N N 493 
TYR   C   OXT  sing N N 494 
TYR   CB  CG   sing N N 495 
TYR   CB  HB2  sing N N 496 
TYR   CB  HB3  sing N N 497 
TYR   CG  CD1  doub Y N 498 
TYR   CG  CD2  sing Y N 499 
TYR   CD1 CE1  sing Y N 500 
TYR   CD1 HD1  sing N N 501 
TYR   CD2 CE2  doub Y N 502 
TYR   CD2 HD2  sing N N 503 
TYR   CE1 CZ   doub Y N 504 
TYR   CE1 HE1  sing N N 505 
TYR   CE2 CZ   sing Y N 506 
TYR   CE2 HE2  sing N N 507 
TYR   CZ  OH   sing N N 508 
TYR   OH  HH   sing N N 509 
TYR   OXT HXT  sing N N 510 
VAL   N   CA   sing N N 511 
VAL   N   H    sing N N 512 
VAL   N   H2   sing N N 513 
VAL   CA  C    sing N N 514 
VAL   CA  CB   sing N N 515 
VAL   CA  HA   sing N N 516 
VAL   C   O    doub N N 517 
VAL   C   OXT  sing N N 518 
VAL   CB  CG1  sing N N 519 
VAL   CB  CG2  sing N N 520 
VAL   CB  HB   sing N N 521 
VAL   CG1 HG11 sing N N 522 
VAL   CG1 HG12 sing N N 523 
VAL   CG1 HG13 sing N N 524 
VAL   CG2 HG21 sing N N 525 
VAL   CG2 HG22 sing N N 526 
VAL   CG2 HG23 sing N N 527 
VAL   OXT HXT  sing N N 528 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM131920 
_pdbx_audit_support.ordinal                1 
# 
_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   7TS9 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CVO 
_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]   0.020507 
_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]   0.008848 
_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]   0.006130 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
FE 
N  
O  
S  
ZN 
# 
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   . ARG   A 1 3   ? -38.665 -24.961 41.749 1.00 146.73 ? 299 ARG   A N   1 
ATOM   2    C  CA  . ARG   A 1 3   ? -38.128 -24.913 40.394 1.00 144.38 ? 299 ARG   A CA  1 
ATOM   3    C  C   . ARG   A 1 3   ? -39.101 -24.187 39.461 1.00 141.67 ? 299 ARG   A C   1 
ATOM   4    O  O   . ARG   A 1 3   ? -39.322 -24.597 38.322 1.00 147.81 ? 299 ARG   A O   1 
ATOM   5    C  CB  . ARG   A 1 3   ? -37.838 -26.327 39.889 1.00 149.27 ? 299 ARG   A CB  1 
ATOM   6    C  CG  . ARG   A 1 3   ? -36.938 -26.410 38.661 1.00 148.77 ? 299 ARG   A CG  1 
ATOM   7    C  CD  . ARG   A 1 3   ? -35.508 -25.987 38.951 1.00 146.44 ? 299 ARG   A CD  1 
ATOM   8    N  NE  . ARG   A 1 3   ? -34.825 -25.550 37.733 1.00 144.70 ? 299 ARG   A NE  1 
ATOM   9    C  CZ  . ARG   A 1 3   ? -34.251 -26.366 36.852 1.00 145.13 ? 299 ARG   A CZ  1 
ATOM   10   N  NH1 . ARG   A 1 3   ? -34.269 -27.680 37.044 1.00 147.13 ? 299 ARG   A NH1 1 
ATOM   11   N  NH2 . ARG   A 1 3   ? -33.659 -25.866 35.773 1.00 142.13 ? 299 ARG   A NH2 1 
ATOM   12   N  N   . PHE   A 1 4   ? -39.703 -23.120 39.975 1.00 132.83 ? 300 PHE   A N   1 
ATOM   13   C  CA  . PHE   A 1 4   ? -40.549 -22.199 39.219 1.00 124.61 ? 300 PHE   A CA  1 
ATOM   14   C  C   . PHE   A 1 4   ? -40.348 -20.818 39.843 1.00 118.35 ? 300 PHE   A C   1 
ATOM   15   O  O   . PHE   A 1 4   ? -41.271 -20.190 40.356 1.00 122.64 ? 300 PHE   A O   1 
ATOM   16   C  CB  . PHE   A 1 4   ? -42.012 -22.639 39.243 1.00 125.99 ? 300 PHE   A CB  1 
ATOM   17   C  CG  . PHE   A 1 4   ? -42.213 -24.105 38.977 1.00 129.89 ? 300 PHE   A CG  1 
ATOM   18   C  CD1 . PHE   A 1 4   ? -42.276 -25.012 40.028 1.00 131.79 ? 300 PHE   A CD1 1 
ATOM   19   C  CD2 . PHE   A 1 4   ? -42.334 -24.582 37.679 1.00 131.13 ? 300 PHE   A CD2 1 
ATOM   20   C  CE1 . PHE   A 1 4   ? -42.458 -26.363 39.791 1.00 135.02 ? 300 PHE   A CE1 1 
ATOM   21   C  CE2 . PHE   A 1 4   ? -42.516 -25.932 37.434 1.00 135.32 ? 300 PHE   A CE2 1 
ATOM   22   C  CZ  . PHE   A 1 4   ? -42.580 -26.823 38.495 1.00 138.07 ? 300 PHE   A CZ  1 
ATOM   23   N  N   . LEU   A 1 5   ? -39.110 -20.331 39.759 1.00 108.90 ? 301 LEU   A N   1 
ATOM   24   C  CA  . LEU   A 1 5   ? -38.556 -19.374 40.712 1.00 96.25  ? 301 LEU   A CA  1 
ATOM   25   C  C   . LEU   A 1 5   ? -39.266 -18.024 40.685 1.00 92.84  ? 301 LEU   A C   1 
ATOM   26   O  O   . LEU   A 1 5   ? -39.893 -17.630 39.698 1.00 94.34  ? 301 LEU   A O   1 
ATOM   27   C  CB  . LEU   A 1 5   ? -37.072 -19.173 40.440 1.00 88.01  ? 301 LEU   A CB  1 
ATOM   28   C  CG  . LEU   A 1 5   ? -36.284 -20.455 40.679 1.00 86.58  ? 301 LEU   A CG  1 
ATOM   29   C  CD1 . LEU   A 1 5   ? -35.112 -20.549 39.737 1.00 87.97  ? 301 LEU   A CD1 1 
ATOM   30   C  CD2 . LEU   A 1 5   ? -35.823 -20.484 42.113 1.00 82.31  ? 301 LEU   A CD2 1 
ATOM   31   N  N   . LYS   A 1 6   ? -39.127 -17.306 41.798 1.00 84.01  ? 302 LYS   A N   1 
ATOM   32   C  CA  . LYS   A 1 6   ? -39.768 -16.017 42.022 1.00 80.82  ? 302 LYS   A CA  1 
ATOM   33   C  C   . LYS   A 1 6   ? -38.709 -14.927 42.104 1.00 71.86  ? 302 LYS   A C   1 
ATOM   34   O  O   . LYS   A 1 6   ? -37.693 -15.086 42.794 1.00 55.42  ? 302 LYS   A O   1 
ATOM   35   C  CB  . LYS   A 1 6   ? -40.596 -16.030 43.307 1.00 83.95  ? 302 LYS   A CB  1 
ATOM   36   C  CG  . LYS   A 1 6   ? -41.687 -17.083 43.349 1.00 90.04  ? 302 LYS   A CG  1 
ATOM   37   C  CD  . LYS   A 1 6   ? -42.924 -16.652 42.571 1.00 96.11  ? 302 LYS   A CD  1 
ATOM   38   C  CE  . LYS   A 1 6   ? -44.014 -17.729 42.597 1.00 105.29 ? 302 LYS   A CE  1 
ATOM   39   N  NZ  . LYS   A 1 6   ? -44.586 -17.979 43.955 1.00 111.89 ? 302 LYS   A NZ  1 
ATOM   40   N  N   . VAL   A 1 7   ? -38.938 -13.834 41.381 1.00 74.70  ? 303 VAL   A N   1 
ATOM   41   C  CA  . VAL   A 1 7   ? -38.081 -12.660 41.425 1.00 71.79  ? 303 VAL   A CA  1 
ATOM   42   C  C   . VAL   A 1 7   ? -38.934 -11.510 41.930 1.00 70.32  ? 303 VAL   A C   1 
ATOM   43   O  O   . VAL   A 1 7   ? -40.062 -11.313 41.461 1.00 71.98  ? 303 VAL   A O   1 
ATOM   44   C  CB  . VAL   A 1 7   ? -37.447 -12.359 40.049 1.00 76.50  ? 303 VAL   A CB  1 
ATOM   45   C  CG1 . VAL   A 1 7   ? -37.140 -13.649 39.331 1.00 81.65  ? 303 VAL   A CG1 1 
ATOM   46   C  CG2 . VAL   A 1 7   ? -38.335 -11.499 39.160 1.00 75.06  ? 303 VAL   A CG2 1 
ATOM   47   N  N   . LYS   A 1 8   ? -38.431 -10.801 42.937 1.00 68.26  ? 304 LYS   A N   1 
ATOM   48   C  CA  . LYS   A 1 8   ? -39.179 -9.728  43.565 1.00 67.81  ? 304 LYS   A CA  1 
ATOM   49   C  C   . LYS   A 1 8   ? -38.593 -8.389  43.154 1.00 60.64  ? 304 LYS   A C   1 
ATOM   50   O  O   . LYS   A 1 8   ? -37.396 -8.269  42.901 1.00 60.14  ? 304 LYS   A O   1 
ATOM   51   C  CB  . LYS   A 1 8   ? -39.150 -9.833  45.095 1.00 68.92  ? 304 LYS   A CB  1 
ATOM   52   C  CG  . LYS   A 1 8   ? -40.148 -8.914  45.794 1.00 73.93  ? 304 LYS   A CG  1 
ATOM   53   C  CD  . LYS   A 1 8   ? -40.062 -9.009  47.315 1.00 75.52  ? 304 LYS   A CD  1 
ATOM   54   C  CE  . LYS   A 1 8   ? -40.850 -7.884  47.996 1.00 81.14  ? 304 LYS   A CE  1 
ATOM   55   N  NZ  . LYS   A 1 8   ? -40.901 -8.006  49.486 1.00 85.62  ? 304 LYS   A NZ  1 
ATOM   56   N  N   . ASN   A 1 9   ? -39.446 -7.383  43.096 1.00 60.78  ? 305 ASN   A N   1 
ATOM   57   C  CA  . ASN   A 1 9   ? -39.011 -5.998  43.077 1.00 66.30  ? 305 ASN   A CA  1 
ATOM   58   C  C   . ASN   A 1 9   ? -39.236 -5.451  44.477 1.00 74.81  ? 305 ASN   A C   1 
ATOM   59   O  O   . ASN   A 1 9   ? -40.256 -5.748  45.100 1.00 76.31  ? 305 ASN   A O   1 
ATOM   60   C  CB  . ASN   A 1 9   ? -39.783 -5.185  42.033 1.00 74.13  ? 305 ASN   A CB  1 
ATOM   61   C  CG  . ASN   A 1 9   ? -39.333 -3.736  41.972 1.00 79.39  ? 305 ASN   A CG  1 
ATOM   62   O  OD1 . ASN   A 1 9   ? -39.386 -3.011  42.970 1.00 83.54  ? 305 ASN   A OD1 1 
ATOM   63   N  ND2 . ASN   A 1 9   ? -38.863 -3.310  40.801 1.00 72.75  ? 305 ASN   A ND2 1 
ATOM   64   N  N   . TRP   A 1 10  ? -38.269 -4.690  44.987 1.00 76.42  ? 306 TRP   A N   1 
ATOM   65   C  CA  . TRP   A 1 10  ? -38.364 -4.141  46.333 1.00 84.39  ? 306 TRP   A CA  1 
ATOM   66   C  C   . TRP   A 1 10  ? -38.661 -2.649  46.354 1.00 89.83  ? 306 TRP   A C   1 
ATOM   67   O  O   . TRP   A 1 10  ? -38.811 -2.080  47.437 1.00 93.18  ? 306 TRP   A O   1 
ATOM   68   C  CB  . TRP   A 1 10  ? -37.079 -4.423  47.123 1.00 77.65  ? 306 TRP   A CB  1 
ATOM   69   C  CG  . TRP   A 1 10  ? -36.809 -5.879  47.306 1.00 70.80  ? 306 TRP   A CG  1 
ATOM   70   C  CD1 . TRP   A 1 10  ? -36.149 -6.706  46.451 1.00 62.85  ? 306 TRP   A CD1 1 
ATOM   71   C  CD2 . TRP   A 1 10  ? -37.202 -6.688  48.420 1.00 71.83  ? 306 TRP   A CD2 1 
ATOM   72   N  NE1 . TRP   A 1 10  ? -36.099 -7.980  46.962 1.00 61.52  ? 306 TRP   A NE1 1 
ATOM   73   C  CE2 . TRP   A 1 10  ? -36.731 -7.994  48.176 1.00 69.09  ? 306 TRP   A CE2 1 
ATOM   74   C  CE3 . TRP   A 1 10  ? -37.890 -6.432  49.611 1.00 79.48  ? 306 TRP   A CE3 1 
ATOM   75   C  CZ2 . TRP   A 1 10  ? -36.937 -9.046  49.072 1.00 67.51  ? 306 TRP   A CZ2 1 
ATOM   76   C  CZ3 . TRP   A 1 10  ? -38.088 -7.471  50.499 1.00 79.93  ? 306 TRP   A CZ3 1 
ATOM   77   C  CH2 . TRP   A 1 10  ? -37.623 -8.764  50.223 1.00 76.16  ? 306 TRP   A CH2 1 
ATOM   78   N  N   . GLU   A 1 11  ? -38.728 -1.993  45.196 1.00 91.39  ? 307 GLU   A N   1 
ATOM   79   C  CA  . GLU   A 1 11  ? -39.239 -0.631  45.153 1.00 90.40  ? 307 GLU   A CA  1 
ATOM   80   C  C   . GLU   A 1 11  ? -40.759 -0.631  45.072 1.00 95.38  ? 307 GLU   A C   1 
ATOM   81   O  O   . GLU   A 1 11  ? -41.409 0.240   45.663 1.00 104.29 ? 307 GLU   A O   1 
ATOM   82   C  CB  . GLU   A 1 11  ? -38.635 0.120   43.963 1.00 86.96  ? 307 GLU   A CB  1 
ATOM   83   C  CG  . GLU   A 1 11  ? -38.445 1.619   44.161 1.00 82.69  ? 307 GLU   A CG  1 
ATOM   84   C  CD  . GLU   A 1 11  ? -38.628 2.418   42.858 1.00 89.22  ? 307 GLU   A CD  1 
ATOM   85   O  OE1 . GLU   A 1 11  ? -39.466 3.350   42.870 1.00 92.30  ? 307 GLU   A OE1 1 
ATOM   86   O  OE2 . GLU   A 1 11  ? -37.957 2.120   41.829 1.00 77.96  ? 307 GLU   A OE2 1 
ATOM   87   N  N   . THR   A 1 12  ? -41.333 -1.630  44.387 1.00 87.97  ? 308 THR   A N   1 
ATOM   88   C  CA  . THR   A 1 12  ? -42.763 -1.712  44.107 1.00 91.24  ? 308 THR   A CA  1 
ATOM   89   C  C   . THR   A 1 12  ? -43.459 -2.907  44.758 1.00 93.15  ? 308 THR   A C   1 
ATOM   90   O  O   . THR   A 1 12  ? -44.678 -3.046  44.601 1.00 97.02  ? 308 THR   A O   1 
ATOM   91   C  CB  . THR   A 1 12  ? -43.006 -1.775  42.581 1.00 91.37  ? 308 THR   A CB  1 
ATOM   92   O  OG1 . THR   A 1 12  ? -42.375 -2.940  42.032 1.00 82.56  ? 308 THR   A OG1 1 
ATOM   93   C  CG2 . THR   A 1 12  ? -42.463 -0.535  41.869 1.00 88.41  ? 308 THR   A CG2 1 
ATOM   94   N  N   . ASP   A 1 13  ? -42.734 -3.775  45.467 1.00 93.61  ? 309 ASP   A N   1 
ATOM   95   C  CA  . ASP   A 1 13  ? -43.224 -5.063  45.964 1.00 98.45  ? 309 ASP   A CA  1 
ATOM   96   C  C   . ASP   A 1 13  ? -43.806 -5.953  44.861 1.00 100.02 ? 309 ASP   A C   1 
ATOM   97   O  O   . ASP   A 1 13  ? -44.447 -6.965  45.161 1.00 105.25 ? 309 ASP   A O   1 
ATOM   98   C  CB  . ASP   A 1 13  ? -44.258 -4.887  47.088 1.00 111.52 ? 309 ASP   A CB  1 
ATOM   99   C  CG  . ASP   A 1 13  ? -43.622 -4.526  48.428 1.00 120.25 ? 309 ASP   A CG  1 
ATOM   100  O  OD1 . ASP   A 1 13  ? -42.687 -5.233  48.862 1.00 119.89 ? 309 ASP   A OD1 1 
ATOM   101  O  OD2 . ASP   A 1 13  ? -44.059 -3.529  49.045 1.00 124.59 ? 309 ASP   A OD2 1 
ATOM   102  N  N   . VAL   A 1 14  ? -43.594 -5.615  43.587 1.00 94.64  ? 310 VAL   A N   1 
ATOM   103  C  CA  . VAL   A 1 14  ? -44.078 -6.455  42.497 1.00 93.09  ? 310 VAL   A CA  1 
ATOM   104  C  C   . VAL   A 1 14  ? -43.283 -7.754  42.459 1.00 92.35  ? 310 VAL   A C   1 
ATOM   105  O  O   . VAL   A 1 14  ? -42.066 -7.767  42.692 1.00 95.17  ? 310 VAL   A O   1 
ATOM   106  C  CB  . VAL   A 1 14  ? -43.989 -5.698  41.162 1.00 85.73  ? 310 VAL   A CB  1 
ATOM   107  C  CG1 . VAL   A 1 14  ? -44.202 -6.638  39.988 1.00 91.10  ? 310 VAL   A CG1 1 
ATOM   108  C  CG2 . VAL   A 1 14  ? -45.006 -4.579  41.124 1.00 81.25  ? 310 VAL   A CG2 1 
ATOM   109  N  N   . VAL   A 1 15  ? -43.972 -8.863  42.194 1.00 83.49  ? 311 VAL   A N   1 
ATOM   110  C  CA  . VAL   A 1 15  ? -43.342 -10.175 42.132 1.00 82.97  ? 311 VAL   A CA  1 
ATOM   111  C  C   . VAL   A 1 15  ? -43.738 -10.841 40.825 1.00 92.69  ? 311 VAL   A C   1 
ATOM   112  O  O   . VAL   A 1 15  ? -44.894 -10.751 40.393 1.00 102.26 ? 311 VAL   A O   1 
ATOM   113  C  CB  . VAL   A 1 15  ? -43.727 -11.060 43.334 1.00 79.55  ? 311 VAL   A CB  1 
ATOM   114  C  CG1 . VAL   A 1 15  ? -42.988 -12.396 43.275 1.00 71.81  ? 311 VAL   A CG1 1 
ATOM   115  C  CG2 . VAL   A 1 15  ? -43.422 -10.338 44.636 1.00 82.74  ? 311 VAL   A CG2 1 
ATOM   116  N  N   . LEU   A 1 16  ? -42.775 -11.504 40.190 1.00 88.72  ? 312 LEU   A N   1 
ATOM   117  C  CA  . LEU   A 1 16  ? -42.998 -12.217 38.943 1.00 86.62  ? 312 LEU   A CA  1 
ATOM   118  C  C   . LEU   A 1 16  ? -42.445 -13.627 39.084 1.00 79.96  ? 312 LEU   A C   1 
ATOM   119  O  O   . LEU   A 1 16  ? -41.516 -13.868 39.865 1.00 70.68  ? 312 LEU   A O   1 
ATOM   120  C  CB  . LEU   A 1 16  ? -42.337 -11.493 37.765 1.00 84.25  ? 312 LEU   A CB  1 
ATOM   121  C  CG  . LEU   A 1 16  ? -42.939 -10.126 37.426 1.00 90.17  ? 312 LEU   A CG  1 
ATOM   122  C  CD1 . LEU   A 1 16  ? -41.966 -9.300  36.608 1.00 87.95  ? 312 LEU   A CD1 1 
ATOM   123  C  CD2 . LEU   A 1 16  ? -44.260 -10.292 36.678 1.00 96.96  ? 312 LEU   A CD2 1 
ATOM   124  N  N   . THR   A 1 17  ? -43.032 -14.559 38.334 1.00 82.25  ? 313 THR   A N   1 
ATOM   125  C  CA  . THR   A 1 17  ? -42.620 -15.956 38.360 1.00 84.45  ? 313 THR   A CA  1 
ATOM   126  C  C   . THR   A 1 17  ? -41.903 -16.312 37.071 1.00 89.21  ? 313 THR   A C   1 
ATOM   127  O  O   . THR   A 1 17  ? -42.396 -16.027 35.974 1.00 90.22  ? 313 THR   A O   1 
ATOM   128  C  CB  . THR   A 1 17  ? -43.806 -16.896 38.561 1.00 88.13  ? 313 THR   A CB  1 
ATOM   129  O  OG1 . THR   A 1 17  ? -44.486 -16.560 39.779 1.00 90.90  ? 313 THR   A OG1 1 
ATOM   130  C  CG2 . THR   A 1 17  ? -43.310 -18.342 38.635 1.00 83.92  ? 313 THR   A CG2 1 
ATOM   131  N  N   . ASP   A 1 18  ? -40.757 -16.960 37.213 1.00 87.05  ? 314 ASP   A N   1 
ATOM   132  C  CA  . ASP   A 1 18  ? -39.860 -17.262 36.107 1.00 80.28  ? 314 ASP   A CA  1 
ATOM   133  C  C   . ASP   A 1 18  ? -39.874 -18.764 35.879 1.00 79.01  ? 314 ASP   A C   1 
ATOM   134  O  O   . ASP   A 1 18  ? -39.321 -19.518 36.683 1.00 74.54  ? 314 ASP   A O   1 
ATOM   135  C  CB  . ASP   A 1 18  ? -38.452 -16.767 36.422 1.00 77.18  ? 314 ASP   A CB  1 
ATOM   136  C  CG  . ASP   A 1 18  ? -37.549 -16.758 35.206 1.00 72.09  ? 314 ASP   A CG  1 
ATOM   137  O  OD1 . ASP   A 1 18  ? -37.260 -17.856 34.692 1.00 72.76  ? 314 ASP   A OD1 1 
ATOM   138  O  OD2 . ASP   A 1 18  ? -37.134 -15.652 34.766 1.00 59.66  ? 314 ASP   A OD2 1 
ATOM   139  N  N   . THR   A 1 19  ? -40.521 -19.195 34.797 1.00 82.94  ? 315 THR   A N   1 
ATOM   140  C  CA  . THR   A 1 19  ? -40.373 -20.561 34.312 1.00 82.63  ? 315 THR   A CA  1 
ATOM   141  C  C   . THR   A 1 19  ? -39.479 -20.659 33.082 1.00 82.61  ? 315 THR   A C   1 
ATOM   142  O  O   . THR   A 1 19  ? -39.067 -21.767 32.721 1.00 82.43  ? 315 THR   A O   1 
ATOM   143  C  CB  . THR   A 1 19  ? -41.741 -21.162 33.979 1.00 82.47  ? 315 THR   A CB  1 
ATOM   144  O  OG1 . THR   A 1 19  ? -42.427 -20.290 33.077 1.00 85.95  ? 315 THR   A OG1 1 
ATOM   145  C  CG2 . THR   A 1 19  ? -42.573 -21.324 35.236 1.00 85.31  ? 315 THR   A CG2 1 
ATOM   146  N  N   . LEU   A 1 20  ? -39.165 -19.524 32.446 1.00 77.68  ? 316 LEU   A N   1 
ATOM   147  C  CA  . LEU   A 1 20  ? -38.347 -19.525 31.238 1.00 71.77  ? 316 LEU   A CA  1 
ATOM   148  C  C   . LEU   A 1 20  ? -36.964 -20.113 31.493 1.00 74.93  ? 316 LEU   A C   1 
ATOM   149  O  O   . LEU   A 1 20  ? -36.347 -20.667 30.574 1.00 77.23  ? 316 LEU   A O   1 
ATOM   150  C  CB  . LEU   A 1 20  ? -38.225 -18.097 30.687 1.00 61.86  ? 316 LEU   A CB  1 
ATOM   151  C  CG  . LEU   A 1 20  ? -37.501 -17.929 29.337 1.00 61.78  ? 316 LEU   A CG  1 
ATOM   152  C  CD1 . LEU   A 1 20  ? -38.190 -18.760 28.257 1.00 52.69  ? 316 LEU   A CD1 1 
ATOM   153  C  CD2 . LEU   A 1 20  ? -37.421 -16.464 28.922 1.00 62.47  ? 316 LEU   A CD2 1 
ATOM   154  N  N   . HIS   A 1 21  ? -36.462 -20.000 32.729 1.00 66.66  ? 317 HIS   A N   1 
ATOM   155  C  CA  . HIS   A 1 21  ? -35.120 -20.470 33.052 1.00 61.52  ? 317 HIS   A CA  1 
ATOM   156  C  C   . HIS   A 1 21  ? -34.992 -21.973 32.896 1.00 64.63  ? 317 HIS   A C   1 
ATOM   157  O  O   . HIS   A 1 21  ? -33.867 -22.486 32.841 1.00 66.47  ? 317 HIS   A O   1 
ATOM   158  C  CB  . HIS   A 1 21  ? -34.761 -20.087 34.496 1.00 70.67  ? 317 HIS   A CB  1 
ATOM   159  C  CG  . HIS   A 1 21  ? -35.527 -20.858 35.521 1.00 73.22  ? 317 HIS   A CG  1 
ATOM   160  N  ND1 . HIS   A 1 21  ? -36.808 -20.523 35.907 1.00 77.15  ? 317 HIS   A ND1 1 
ATOM   161  C  CD2 . HIS   A 1 21  ? -35.204 -21.973 36.216 1.00 78.97  ? 317 HIS   A CD2 1 
ATOM   162  C  CE1 . HIS   A 1 21  ? -37.233 -21.387 36.812 1.00 81.98  ? 317 HIS   A CE1 1 
ATOM   163  N  NE2 . HIS   A 1 21  ? -36.278 -22.275 37.019 1.00 82.28  ? 317 HIS   A NE2 1 
ATOM   164  N  N   . LEU   A 1 22  ? -36.123 -22.687 32.860 1.00 69.47  ? 318 LEU   A N   1 
ATOM   165  C  CA  . LEU   A 1 22  ? -36.117 -24.131 32.641 1.00 82.29  ? 318 LEU   A CA  1 
ATOM   166  C  C   . LEU   A 1 22  ? -35.624 -24.489 31.240 1.00 87.03  ? 318 LEU   A C   1 
ATOM   167  O  O   . LEU   A 1 22  ? -34.999 -25.544 31.052 1.00 85.53  ? 318 LEU   A O   1 
ATOM   168  C  CB  . LEU   A 1 22  ? -37.525 -24.691 32.871 1.00 85.97  ? 318 LEU   A CB  1 
ATOM   169  C  CG  . LEU   A 1 22  ? -38.152 -24.575 34.267 1.00 86.59  ? 318 LEU   A CG  1 
ATOM   170  C  CD1 . LEU   A 1 22  ? -39.606 -25.046 34.256 1.00 82.04  ? 318 LEU   A CD1 1 
ATOM   171  C  CD2 . LEU   A 1 22  ? -37.336 -25.340 35.304 1.00 84.84  ? 318 LEU   A CD2 1 
ATOM   172  N  N   . LYS   A 1 23  ? -35.903 -23.629 30.253 1.00 83.27  ? 319 LYS   A N   1 
ATOM   173  C  CA  . LYS   A 1 23  ? -35.407 -23.802 28.892 1.00 84.82  ? 319 LYS   A CA  1 
ATOM   174  C  C   . LYS   A 1 23  ? -33.918 -23.528 28.785 1.00 86.86  ? 319 LYS   A C   1 
ATOM   175  O  O   . LYS   A 1 23  ? -33.325 -23.845 27.749 1.00 91.69  ? 319 LYS   A O   1 
ATOM   176  C  CB  . LYS   A 1 23  ? -36.158 -22.883 27.914 1.00 78.02  ? 319 LYS   A CB  1 
ATOM   177  C  CG  . LYS   A 1 23  ? -37.651 -23.190 27.704 1.00 83.45  ? 319 LYS   A CG  1 
ATOM   178  C  CD  . LYS   A 1 23  ? -37.911 -24.362 26.751 1.00 95.82  ? 319 LYS   A CD  1 
ATOM   179  C  CE  . LYS   A 1 23  ? -37.694 -23.998 25.262 1.00 104.05 ? 319 LYS   A CE  1 
ATOM   180  N  NZ  . LYS   A 1 23  ? -38.706 -23.053 24.685 1.00 107.30 ? 319 LYS   A NZ  1 
ATOM   181  N  N   . SER   A 1 24  ? -33.313 -22.933 29.811 1.00 86.25  ? 320 SER   A N   1 
ATOM   182  C  CA  . SER   A 1 24  ? -31.881 -22.680 29.789 1.00 85.43  ? 320 SER   A CA  1 
ATOM   183  C  C   . SER   A 1 24  ? -31.110 -23.980 29.621 1.00 86.45  ? 320 SER   A C   1 
ATOM   184  O  O   . SER   A 1 24  ? -31.539 -25.053 30.058 1.00 88.14  ? 320 SER   A O   1 
ATOM   185  C  CB  . SER   A 1 24  ? -31.423 -21.982 31.065 1.00 86.30  ? 320 SER   A CB  1 
ATOM   186  O  OG  . SER   A 1 24  ? -30.015 -22.032 31.161 1.00 87.39  ? 320 SER   A OG  1 
ATOM   187  N  N   . THR   A 1 25  ? -29.949 -23.863 28.986 1.00 86.62  ? 321 THR   A N   1 
ATOM   188  C  CA  . THR   A 1 25  ? -29.199 -25.027 28.549 1.00 98.50  ? 321 THR   A CA  1 
ATOM   189  C  C   . THR   A 1 25  ? -27.728 -24.838 28.897 1.00 99.24  ? 321 THR   A C   1 
ATOM   190  O  O   . THR   A 1 25  ? -27.097 -25.736 29.471 1.00 101.21 ? 321 THR   A O   1 
ATOM   191  C  CB  . THR   A 1 25  ? -29.422 -25.253 27.038 1.00 96.42  ? 321 THR   A CB  1 
ATOM   192  O  OG1 . THR   A 1 25  ? -28.400 -26.105 26.511 1.00 97.57  ? 321 THR   A OG1 1 
ATOM   193  C  CG2 . THR   A 1 25  ? -29.447 -23.922 26.262 1.00 92.24  ? 321 THR   A CG2 1 
ATOM   194  N  N   . LEU   A 1 26  ? -27.189 -23.661 28.584 1.00 93.32  ? 322 LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 26  ? -25.789 -23.366 28.845 1.00 96.75  ? 322 LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 26  ? -25.545 -23.191 30.346 1.00 96.80  ? 322 LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 26  ? -26.463 -23.221 31.171 1.00 90.62  ? 322 LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 26  ? -25.362 -22.122 28.072 1.00 98.71  ? 322 LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 26  ? -24.751 -22.344 26.689 1.00 102.70 ? 322 LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 26  ? -25.205 -21.244 25.751 1.00 100.69 ? 322 LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 26  ? -23.228 -22.376 26.789 1.00 104.35 ? 322 LEU   A CD2 1 
ATOM   202  N  N   . GLU   A 1 27  ? -24.277 -23.012 30.700 1.00 97.08  ? 323 GLU   A N   1 
ATOM   203  C  CA  . GLU   A 1 27  ? -23.855 -22.898 32.084 1.00 96.05  ? 323 GLU   A CA  1 
ATOM   204  C  C   . GLU   A 1 27  ? -23.404 -21.468 32.371 1.00 90.60  ? 323 GLU   A C   1 
ATOM   205  O  O   . GLU   A 1 27  ? -22.977 -20.741 31.467 1.00 92.51  ? 323 GLU   A O   1 
ATOM   206  C  CB  . GLU   A 1 27  ? -22.740 -23.904 32.400 1.00 101.79 ? 323 GLU   A CB  1 
ATOM   207  C  CG  . GLU   A 1 27  ? -23.112 -25.344 32.037 1.00 110.50 ? 323 GLU   A CG  1 
ATOM   208  C  CD  . GLU   A 1 27  ? -22.329 -26.398 32.815 1.00 119.46 ? 323 GLU   A CD  1 
ATOM   209  O  OE1 . GLU   A 1 27  ? -21.524 -26.024 33.692 1.00 120.41 ? 323 GLU   A OE1 1 
ATOM   210  O  OE2 . GLU   A 1 27  ? -22.528 -27.607 32.549 1.00 122.99 ? 323 GLU   A OE2 1 
ATOM   211  N  N   . THR   A 1 28  ? -23.505 -21.072 33.644 1.00 76.60  ? 324 THR   A N   1 
ATOM   212  C  CA  . THR   A 1 28  ? -23.347 -19.681 34.064 1.00 69.49  ? 324 THR   A CA  1 
ATOM   213  C  C   . THR   A 1 28  ? -21.953 -19.340 34.592 1.00 66.03  ? 324 THR   A C   1 
ATOM   214  O  O   . THR   A 1 28  ? -21.514 -18.189 34.471 1.00 64.04  ? 324 THR   A O   1 
ATOM   215  C  CB  . THR   A 1 28  ? -24.357 -19.352 35.169 1.00 64.02  ? 324 THR   A CB  1 
ATOM   216  O  OG1 . THR   A 1 28  ? -24.145 -20.230 36.292 1.00 62.72  ? 324 THR   A OG1 1 
ATOM   217  C  CG2 . THR   A 1 28  ? -25.784 -19.509 34.649 1.00 57.98  ? 324 THR   A CG2 1 
ATOM   218  N  N   . GLY   A 1 29  ? -21.242 -20.307 35.165 1.00 69.16  ? 325 GLY   A N   1 
ATOM   219  C  CA  . GLY   A 1 29  ? -20.055 -20.065 35.949 1.00 69.38  ? 325 GLY   A CA  1 
ATOM   220  C  C   . GLY   A 1 29  ? -20.297 -20.297 37.423 1.00 74.25  ? 325 GLY   A C   1 
ATOM   221  O  O   . GLY   A 1 29  ? -19.365 -20.661 38.152 1.00 79.23  ? 325 GLY   A O   1 
ATOM   222  N  N   . CYS   A 1 30  ? -21.538 -20.134 37.861 1.00 72.33  ? 326 CYS   A N   1 
ATOM   223  C  CA  . CYS   A 1 30  ? -21.891 -20.291 39.259 1.00 71.97  ? 326 CYS   A CA  1 
ATOM   224  C  C   . CYS   A 1 30  ? -22.140 -21.758 39.583 1.00 71.03  ? 326 CYS   A C   1 
ATOM   225  O  O   . CYS   A 1 30  ? -22.669 -22.513 38.760 1.00 69.32  ? 326 CYS   A O   1 
ATOM   226  C  CB  . CYS   A 1 30  ? -23.129 -19.457 39.577 1.00 69.65  ? 326 CYS   A CB  1 
ATOM   227  S  SG  . CYS   A 1 30  ? -22.920 -17.674 39.327 1.00 64.49  ? 326 CYS   A SG  1 
ATOM   228  N  N   . THR   A 1 31  ? -21.734 -22.165 40.777 1.00 66.06  ? 327 THR   A N   1 
ATOM   229  C  CA  . THR   A 1 31  ? -22.072 -23.469 41.326 1.00 73.60  ? 327 THR   A CA  1 
ATOM   230  C  C   . THR   A 1 31  ? -22.947 -23.276 42.557 1.00 77.53  ? 327 THR   A C   1 
ATOM   231  O  O   . THR   A 1 31  ? -23.262 -22.152 42.951 1.00 84.38  ? 327 THR   A O   1 
ATOM   232  C  CB  . THR   A 1 31  ? -20.812 -24.260 41.658 1.00 74.78  ? 327 THR   A CB  1 
ATOM   233  O  OG1 . THR   A 1 31  ? -20.200 -23.705 42.827 1.00 72.20  ? 327 THR   A OG1 1 
ATOM   234  C  CG2 . THR   A 1 31  ? -19.830 -24.195 40.496 1.00 66.50  ? 327 THR   A CG2 1 
ATOM   235  N  N   . GLU   A 1 32  ? -23.343 -24.385 43.179 1.00 85.48  ? 328 GLU   A N   1 
ATOM   236  C  CA  . GLU   A 1 32  ? -24.152 -24.273 44.386 1.00 91.13  ? 328 GLU   A CA  1 
ATOM   237  C  C   . GLU   A 1 32  ? -23.397 -23.585 45.517 1.00 88.07  ? 328 GLU   A C   1 
ATOM   238  O  O   . GLU   A 1 32  ? -24.028 -23.075 46.449 1.00 84.54  ? 328 GLU   A O   1 
ATOM   239  C  CB  . GLU   A 1 32  ? -24.646 -25.657 44.825 1.00 104.66 ? 328 GLU   A CB  1 
ATOM   240  C  CG  . GLU   A 1 32  ? -25.905 -26.139 44.094 1.00 114.84 ? 328 GLU   A CG  1 
ATOM   241  C  CD  . GLU   A 1 32  ? -25.626 -27.223 43.060 1.00 125.06 ? 328 GLU   A CD  1 
ATOM   242  O  OE1 . GLU   A 1 32  ? -26.080 -28.376 43.258 1.00 131.35 ? 328 GLU   A OE1 1 
ATOM   243  O  OE2 . GLU   A 1 32  ? -24.953 -26.920 42.051 1.00 125.08 ? 328 GLU   A OE2 1 
ATOM   244  N  N   . HIS   A 1 33  ? -22.066 -23.517 45.433 1.00 82.79  ? 329 HIS   A N   1 
ATOM   245  C  CA  . HIS   A 1 33  ? -21.229 -23.030 46.525 1.00 82.55  ? 329 HIS   A CA  1 
ATOM   246  C  C   . HIS   A 1 33  ? -20.341 -21.852 46.126 1.00 75.83  ? 329 HIS   A C   1 
ATOM   247  O  O   . HIS   A 1 33  ? -19.422 -21.498 46.879 1.00 75.58  ? 329 HIS   A O   1 
ATOM   248  C  CB  . HIS   A 1 33  ? -20.383 -24.187 47.063 1.00 93.87  ? 329 HIS   A CB  1 
ATOM   249  C  CG  . HIS   A 1 33  ? -21.160 -25.458 47.236 1.00 103.39 ? 329 HIS   A CG  1 
ATOM   250  N  ND1 . HIS   A 1 33  ? -21.280 -26.400 46.234 1.00 105.22 ? 329 HIS   A ND1 1 
ATOM   251  C  CD2 . HIS   A 1 33  ? -21.893 -25.921 48.277 1.00 103.82 ? 329 HIS   A CD2 1 
ATOM   252  C  CE1 . HIS   A 1 33  ? -22.037 -27.397 46.657 1.00 107.70 ? 329 HIS   A CE1 1 
ATOM   253  N  NE2 . HIS   A 1 33  ? -22.422 -27.131 47.893 1.00 107.76 ? 329 HIS   A NE2 1 
ATOM   254  N  N   . ILE   A 1 34  ? -20.595 -21.235 44.972 1.00 69.24  ? 330 ILE   A N   1 
ATOM   255  C  CA  . ILE   A 1 34  ? -19.881 -20.032 44.559 1.00 63.78  ? 330 ILE   A CA  1 
ATOM   256  C  C   . ILE   A 1 34  ? -20.691 -19.344 43.471 1.00 66.44  ? 330 ILE   A C   1 
ATOM   257  O  O   . ILE   A 1 34  ? -21.238 -19.988 42.572 1.00 72.44  ? 330 ILE   A O   1 
ATOM   258  C  CB  . ILE   A 1 34  ? -18.438 -20.342 44.093 1.00 63.37  ? 330 ILE   A CB  1 
ATOM   259  C  CG1 . ILE   A 1 34  ? -17.707 -19.044 43.764 1.00 63.38  ? 330 ILE   A CG1 1 
ATOM   260  C  CG2 . ILE   A 1 34  ? -18.438 -21.232 42.853 1.00 71.19  ? 330 ILE   A CG2 1 
ATOM   261  C  CD1 . ILE   A 1 34  ? -16.230 -19.101 44.015 1.00 62.22  ? 330 ILE   A CD1 1 
ATOM   262  N  N   . CYS   A 1 35  ? -20.773 -18.026 43.570 1.00 65.82  ? 331 CYS   A N   1 
ATOM   263  C  CA  . CYS   A 1 35  ? -21.453 -17.198 42.587 1.00 64.00  ? 331 CYS   A CA  1 
ATOM   264  C  C   . CYS   A 1 35  ? -20.431 -16.312 41.897 1.00 64.91  ? 331 CYS   A C   1 
ATOM   265  O  O   . CYS   A 1 35  ? -19.587 -15.700 42.563 1.00 57.91  ? 331 CYS   A O   1 
ATOM   266  C  CB  . CYS   A 1 35  ? -22.545 -16.369 43.253 1.00 61.60  ? 331 CYS   A CB  1 
ATOM   267  S  SG  . CYS   A 1 35  ? -23.159 -15.034 42.234 1.00 57.18  ? 331 CYS   A SG  1 
ATOM   268  N  N   . MET   A 1 36  ? -20.488 -16.287 40.563 1.00 72.86  ? 332 MET   A N   1 
ATOM   269  C  CA  . MET   A 1 36  ? -19.530 -15.572 39.731 1.00 77.32  ? 332 MET   A CA  1 
ATOM   270  C  C   . MET   A 1 36  ? -20.172 -14.399 39.003 1.00 66.53  ? 332 MET   A C   1 
ATOM   271  O  O   . MET   A 1 36  ? -19.584 -13.853 38.060 1.00 61.11  ? 332 MET   A O   1 
ATOM   272  C  CB  . MET   A 1 36  ? -18.895 -16.515 38.716 1.00 87.16  ? 332 MET   A CB  1 
ATOM   273  C  CG  . MET   A 1 36  ? -18.405 -17.787 39.322 1.00 96.58  ? 332 MET   A CG  1 
ATOM   274  S  SD  . MET   A 1 36  ? -16.713 -18.124 38.843 1.00 104.13 ? 332 MET   A SD  1 
ATOM   275  C  CE  . MET   A 1 36  ? -16.353 -19.400 40.032 1.00 106.31 ? 332 MET   A CE  1 
ATOM   276  N  N   . GLY   A 1 37  ? -21.365 -13.994 39.437 1.00 55.80  ? 333 GLY   A N   1 
ATOM   277  C  CA  . GLY   A 1 37  ? -22.143 -12.947 38.803 1.00 59.56  ? 333 GLY   A CA  1 
ATOM   278  C  C   . GLY   A 1 37  ? -21.403 -11.647 38.535 1.00 58.86  ? 333 GLY   A C   1 
ATOM   279  O  O   . GLY   A 1 37  ? -22.005 -10.741 37.954 1.00 52.77  ? 333 GLY   A O   1 
ATOM   280  N  N   . SER   A 1 38  ? -20.146 -11.498 38.964 1.00 55.81  ? 334 SER   A N   1 
ATOM   281  C  CA  . SER   A 1 38  ? -19.421 -10.248 38.736 1.00 46.64  ? 334 SER   A CA  1 
ATOM   282  C  C   . SER   A 1 38  ? -18.077 -10.502 38.062 1.00 49.80  ? 334 SER   A C   1 
ATOM   283  O  O   . SER   A 1 38  ? -17.284 -9.566  37.893 1.00 56.08  ? 334 SER   A O   1 
ATOM   284  C  CB  . SER   A 1 38  ? -19.274 -9.455  40.047 1.00 56.54  ? 334 SER   A CB  1 
ATOM   285  O  OG  . SER   A 1 38  ? -18.114 -9.801  40.801 1.00 62.45  ? 334 SER   A OG  1 
ATOM   286  N  N   . ILE   A 1 39  ? -17.830 -11.743 37.637 1.00 40.81  ? 335 ILE   A N   1 
ATOM   287  C  CA  . ILE   A 1 39  ? -16.754 -12.056 36.709 1.00 51.89  ? 335 ILE   A CA  1 
ATOM   288  C  C   . ILE   A 1 39  ? -17.162 -11.604 35.309 1.00 57.94  ? 335 ILE   A C   1 
ATOM   289  O  O   . ILE   A 1 39  ? -18.230 -11.983 34.809 1.00 51.41  ? 335 ILE   A O   1 
ATOM   290  C  CB  . ILE   A 1 39  ? -16.451 -13.556 36.714 1.00 51.74  ? 335 ILE   A CB  1 
ATOM   291  C  CG1 . ILE   A 1 39  ? -16.182 -14.066 38.146 1.00 56.14  ? 335 ILE   A CG1 1 
ATOM   292  C  CG2 . ILE   A 1 39  ? -15.300 -13.837 35.792 1.00 50.40  ? 335 ILE   A CG2 1 
ATOM   293  C  CD1 . ILE   A 1 39  ? -15.060 -13.328 38.857 1.00 59.56  ? 335 ILE   A CD1 1 
ATOM   294  N  N   . MET   A 1 40  ? -16.293 -10.829 34.659 1.00 65.23  ? 336 MET   A N   1 
ATOM   295  C  CA  . MET   A 1 40  ? -16.648 -10.219 33.375 1.00 67.94  ? 336 MET   A CA  1 
ATOM   296  C  C   . MET   A 1 40  ? -16.849 -11.269 32.285 1.00 70.37  ? 336 MET   A C   1 
ATOM   297  O  O   . MET   A 1 40  ? -17.915 -11.344 31.658 1.00 73.22  ? 336 MET   A O   1 
ATOM   298  C  CB  . MET   A 1 40  ? -15.568 -9.227  32.958 1.00 77.92  ? 336 MET   A CB  1 
ATOM   299  C  CG  . MET   A 1 40  ? -16.019 -8.286  31.874 1.00 91.71  ? 336 MET   A CG  1 
ATOM   300  S  SD  . MET   A 1 40  ? -16.321 -6.655  32.551 1.00 96.91  ? 336 MET   A SD  1 
ATOM   301  C  CE  . MET   A 1 40  ? -14.697 -5.940  32.451 1.00 98.52  ? 336 MET   A CE  1 
ATOM   302  N  N   . LEU   A 1 41  ? -15.828 -12.088 32.033 1.00 75.31  ? 337 LEU   A N   1 
ATOM   303  C  CA  . LEU   A 1 41  ? -15.830 -13.039 30.922 1.00 86.67  ? 337 LEU   A CA  1 
ATOM   304  C  C   . LEU   A 1 41  ? -15.729 -14.453 31.486 1.00 104.26 ? 337 LEU   A C   1 
ATOM   305  O  O   . LEU   A 1 41  ? -14.651 -15.066 31.454 1.00 113.25 ? 337 LEU   A O   1 
ATOM   306  C  CB  . LEU   A 1 41  ? -14.678 -12.757 29.954 1.00 81.05  ? 337 LEU   A CB  1 
ATOM   307  C  CG  . LEU   A 1 41  ? -14.067 -11.344 29.900 1.00 77.85  ? 337 LEU   A CG  1 
ATOM   308  C  CD1 . LEU   A 1 41  ? -12.639 -11.374 29.359 1.00 79.50  ? 337 LEU   A CD1 1 
ATOM   309  C  CD2 . LEU   A 1 41  ? -14.924 -10.349 29.110 1.00 73.18  ? 337 LEU   A CD2 1 
ATOM   310  N  N   . PRO   A 1 42  ? -16.823 -15.009 32.003 1.00 110.54 ? 338 PRO   A N   1 
ATOM   311  C  CA  . PRO   A 1 42  ? -16.736 -16.327 32.642 1.00 112.68 ? 338 PRO   A CA  1 
ATOM   312  C  C   . PRO   A 1 42  ? -16.734 -17.445 31.607 1.00 112.49 ? 338 PRO   A C   1 
ATOM   313  O  O   . PRO   A 1 42  ? -17.452 -17.400 30.603 1.00 103.44 ? 338 PRO   A O   1 
ATOM   314  C  CB  . PRO   A 1 42  ? -17.987 -16.377 33.535 1.00 111.72 ? 338 PRO   A CB  1 
ATOM   315  C  CG  . PRO   A 1 42  ? -18.755 -15.064 33.259 1.00 111.20 ? 338 PRO   A CG  1 
ATOM   316  C  CD  . PRO   A 1 42  ? -18.204 -14.504 31.988 1.00 110.21 ? 338 PRO   A CD  1 
ATOM   317  N  N   . SER   A 1 43  ? -15.894 -18.445 31.857 1.00 113.20 ? 339 SER   A N   1 
ATOM   318  C  CA  . SER   A 1 43  ? -15.767 -19.601 30.980 1.00 112.85 ? 339 SER   A CA  1 
ATOM   319  C  C   . SER   A 1 43  ? -15.204 -20.783 31.755 1.00 113.71 ? 339 SER   A C   1 
ATOM   320  O  O   . SER   A 1 43  ? -15.552 -21.928 31.485 1.00 115.42 ? 339 SER   A O   1 
ATOM   321  C  CB  . SER   A 1 43  ? -14.872 -19.278 29.779 1.00 114.22 ? 339 SER   A CB  1 
ATOM   322  O  OG  . SER   A 1 43  ? -14.647 -20.425 28.970 1.00 115.02 ? 339 SER   A OG  1 
ATOM   323  N  N   . VAL   A 1 52  ? -13.721 -26.085 16.501 1.00 143.33 ? 348 VAL   A N   1 
ATOM   324  C  CA  . VAL   A 1 52  ? -14.622 -26.598 15.472 1.00 142.52 ? 348 VAL   A CA  1 
ATOM   325  C  C   . VAL   A 1 52  ? -15.606 -27.592 16.102 1.00 146.42 ? 348 VAL   A C   1 
ATOM   326  O  O   . VAL   A 1 52  ? -15.256 -28.312 17.042 1.00 155.65 ? 348 VAL   A O   1 
ATOM   327  C  CB  . VAL   A 1 52  ? -13.825 -27.231 14.305 1.00 138.98 ? 348 VAL   A CB  1 
ATOM   328  C  CG1 . VAL   A 1 52  ? -12.999 -28.416 14.788 1.00 139.55 ? 348 VAL   A CG1 1 
ATOM   329  C  CG2 . VAL   A 1 52  ? -14.752 -27.627 13.159 1.00 136.98 ? 348 VAL   A CG2 1 
ATOM   330  N  N   . ALA   A 1 53  ? -16.842 -27.617 15.594 1.00 137.38 ? 349 ALA   A N   1 
ATOM   331  C  CA  . ALA   A 1 53  ? -17.926 -28.398 16.179 1.00 130.01 ? 349 ALA   A CA  1 
ATOM   332  C  C   . ALA   A 1 53  ? -18.389 -29.479 15.211 1.00 127.04 ? 349 ALA   A C   1 
ATOM   333  O  O   . ALA   A 1 53  ? -18.433 -29.259 13.997 1.00 131.57 ? 349 ALA   A O   1 
ATOM   334  C  CB  . ALA   A 1 53  ? -19.104 -27.499 16.564 1.00 123.09 ? 349 ALA   A CB  1 
ATOM   335  N  N   . THR   A 1 54  ? -18.755 -30.643 15.759 1.00 122.94 ? 350 THR   A N   1 
ATOM   336  C  CA  . THR   A 1 54  ? -19.066 -31.818 14.957 1.00 118.75 ? 350 THR   A CA  1 
ATOM   337  C  C   . THR   A 1 54  ? -20.562 -31.918 14.658 1.00 117.35 ? 350 THR   A C   1 
ATOM   338  O  O   . THR   A 1 54  ? -21.381 -31.121 15.119 1.00 117.06 ? 350 THR   A O   1 
ATOM   339  C  CB  . THR   A 1 54  ? -18.601 -33.097 15.652 1.00 116.70 ? 350 THR   A CB  1 
ATOM   340  O  OG1 . THR   A 1 54  ? -19.709 -33.688 16.347 1.00 115.43 ? 350 THR   A OG1 1 
ATOM   341  C  CG2 . THR   A 1 54  ? -17.479 -32.801 16.635 1.00 116.39 ? 350 THR   A CG2 1 
ATOM   342  N  N   . LYS   A 1 55  ? -20.918 -32.944 13.884 1.00 120.17 ? 351 LYS   A N   1 
ATOM   343  C  CA  . LYS   A 1 55  ? -22.282 -33.101 13.396 1.00 121.24 ? 351 LYS   A CA  1 
ATOM   344  C  C   . LYS   A 1 55  ? -23.191 -33.717 14.443 1.00 121.35 ? 351 LYS   A C   1 
ATOM   345  O  O   . LYS   A 1 55  ? -24.396 -33.436 14.458 1.00 116.85 ? 351 LYS   A O   1 
ATOM   346  C  CB  . LYS   A 1 55  ? -22.280 -33.959 12.131 1.00 121.87 ? 351 LYS   A CB  1 
ATOM   347  C  CG  . LYS   A 1 55  ? -20.885 -34.324 11.664 1.00 123.40 ? 351 LYS   A CG  1 
ATOM   348  C  CD  . LYS   A 1 55  ? -20.923 -35.352 10.547 1.00 132.81 ? 351 LYS   A CD  1 
ATOM   349  C  CE  . LYS   A 1 55  ? -19.519 -35.783 10.141 1.00 137.59 ? 351 LYS   A CE  1 
ATOM   350  N  NZ  . LYS   A 1 55  ? -19.520 -37.043 9.342  1.00 143.89 ? 351 LYS   A NZ  1 
ATOM   351  N  N   . ASP   A 1 56  ? -22.636 -34.570 15.304 1.00 124.86 ? 352 ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 56  ? -23.404 -35.125 16.412 1.00 128.55 ? 352 ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 56  ? -23.987 -34.007 17.264 1.00 120.21 ? 352 ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 56  ? -25.202 -33.930 17.480 1.00 119.57 ? 352 ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 56  ? -22.508 -36.039 17.255 1.00 133.93 ? 352 ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 56  ? -21.614 -36.929 16.405 1.00 138.15 ? 352 ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 56  ? -22.140 -37.826 15.714 1.00 140.04 ? 352 ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 56  ? -20.383 -36.716 16.417 1.00 137.91 ? 352 ASP   A OD2 1 
ATOM   359  N  N   . GLN   A 1 57  ? -23.123 -33.112 17.737 1.00 113.41 ? 353 GLN   A N   1 
ATOM   360  C  CA  . GLN   A 1 57  ? -23.583 -31.981 18.528 1.00 109.37 ? 353 GLN   A CA  1 
ATOM   361  C  C   . GLN   A 1 57  ? -24.526 -31.085 17.736 1.00 104.48 ? 353 GLN   A C   1 
ATOM   362  O  O   . GLN   A 1 57  ? -25.361 -30.390 18.324 1.00 101.91 ? 353 GLN   A O   1 
ATOM   363  C  CB  . GLN   A 1 57  ? -22.378 -31.178 19.007 1.00 112.93 ? 353 GLN   A CB  1 
ATOM   364  C  CG  . GLN   A 1 57  ? -21.108 -32.002 19.134 1.00 123.55 ? 353 GLN   A CG  1 
ATOM   365  C  CD  . GLN   A 1 57  ? -19.871 -31.209 18.764 1.00 129.84 ? 353 GLN   A CD  1 
ATOM   366  O  OE1 . GLN   A 1 57  ? -19.885 -30.444 17.803 1.00 133.04 ? 353 GLN   A OE1 1 
ATOM   367  N  NE2 . GLN   A 1 57  ? -18.797 -31.378 19.531 1.00 131.16 ? 353 GLN   A NE2 1 
ATOM   368  N  N   . LEU   A 1 58  ? -24.425 -31.105 16.404 1.00 97.84  ? 354 LEU   A N   1 
ATOM   369  C  CA  . LEU   A 1 58  ? -25.035 -30.052 15.603 1.00 93.04  ? 354 LEU   A CA  1 
ATOM   370  C  C   . LEU   A 1 58  ? -26.541 -30.228 15.451 1.00 93.96  ? 354 LEU   A C   1 
ATOM   371  O  O   . LEU   A 1 58  ? -27.254 -29.234 15.260 1.00 91.10  ? 354 LEU   A O   1 
ATOM   372  C  CB  . LEU   A 1 58  ? -24.374 -29.999 14.228 1.00 95.53  ? 354 LEU   A CB  1 
ATOM   373  C  CG  . LEU   A 1 58  ? -24.300 -28.635 13.546 1.00 86.03  ? 354 LEU   A CG  1 
ATOM   374  C  CD1 . LEU   A 1 58  ? -23.534 -27.671 14.430 1.00 76.43  ? 354 LEU   A CD1 1 
ATOM   375  C  CD2 . LEU   A 1 58  ? -23.641 -28.776 12.163 1.00 78.14  ? 354 LEU   A CD2 1 
ATOM   376  N  N   . PHE   A 1 59  ? -27.052 -31.469 15.509 1.00 96.47  ? 355 PHE   A N   1 
ATOM   377  C  CA  . PHE   A 1 59  ? -28.476 -31.619 15.215 1.00 107.54 ? 355 PHE   A CA  1 
ATOM   378  C  C   . PHE   A 1 59  ? -29.398 -31.236 16.371 1.00 111.84 ? 355 PHE   A C   1 
ATOM   379  O  O   . PHE   A 1 59  ? -30.384 -30.527 16.126 1.00 116.09 ? 355 PHE   A O   1 
ATOM   380  C  CB  . PHE   A 1 59  ? -28.848 -33.030 14.763 1.00 121.18 ? 355 PHE   A CB  1 
ATOM   381  C  CG  . PHE   A 1 59  ? -30.266 -33.118 14.264 1.00 131.56 ? 355 PHE   A CG  1 
ATOM   382  C  CD1 . PHE   A 1 59  ? -30.631 -32.487 13.083 1.00 134.53 ? 355 PHE   A CD1 1 
ATOM   383  C  CD2 . PHE   A 1 59  ? -31.246 -33.777 14.992 1.00 136.60 ? 355 PHE   A CD2 1 
ATOM   384  C  CE1 . PHE   A 1 59  ? -31.937 -32.530 12.622 1.00 137.58 ? 355 PHE   A CE1 1 
ATOM   385  C  CE2 . PHE   A 1 59  ? -32.557 -33.828 14.532 1.00 141.05 ? 355 PHE   A CE2 1 
ATOM   386  C  CZ  . PHE   A 1 59  ? -32.900 -33.204 13.342 1.00 141.13 ? 355 PHE   A CZ  1 
ATOM   387  N  N   . PRO   A 1 60  ? -29.168 -31.691 17.620 1.00 108.70 ? 356 PRO   A N   1 
ATOM   388  C  CA  . PRO   A 1 60  ? -30.045 -31.222 18.709 1.00 103.63 ? 356 PRO   A CA  1 
ATOM   389  C  C   . PRO   A 1 60  ? -30.211 -29.720 18.701 1.00 91.54  ? 356 PRO   A C   1 
ATOM   390  O  O   . PRO   A 1 60  ? -31.322 -29.216 18.904 1.00 85.19  ? 356 PRO   A O   1 
ATOM   391  C  CB  . PRO   A 1 60  ? -29.335 -31.709 19.982 1.00 106.05 ? 356 PRO   A CB  1 
ATOM   392  C  CG  . PRO   A 1 60  ? -27.945 -32.059 19.548 1.00 109.36 ? 356 PRO   A CG  1 
ATOM   393  C  CD  . PRO   A 1 60  ? -28.093 -32.552 18.143 1.00 108.62 ? 356 PRO   A CD  1 
ATOM   394  N  N   . LEU   A 1 61  ? -29.125 -29.000 18.399 1.00 85.12  ? 357 LEU   A N   1 
ATOM   395  C  CA  . LEU   A 1 61  ? -29.152 -27.541 18.361 1.00 75.80  ? 357 LEU   A CA  1 
ATOM   396  C  C   . LEU   A 1 61  ? -29.984 -27.030 17.190 1.00 79.68  ? 357 LEU   A C   1 
ATOM   397  O  O   . LEU   A 1 61  ? -30.684 -26.018 17.318 1.00 84.66  ? 357 LEU   A O   1 
ATOM   398  C  CB  . LEU   A 1 61  ? -27.726 -27.005 18.277 1.00 69.39  ? 357 LEU   A CB  1 
ATOM   399  C  CG  . LEU   A 1 61  ? -26.725 -27.630 19.256 1.00 77.91  ? 357 LEU   A CG  1 
ATOM   400  C  CD1 . LEU   A 1 61  ? -25.411 -26.860 19.273 1.00 70.62  ? 357 LEU   A CD1 1 
ATOM   401  C  CD2 . LEU   A 1 61  ? -27.302 -27.745 20.678 1.00 85.28  ? 357 LEU   A CD2 1 
ATOM   402  N  N   . ALA   A 1 62  ? -29.926 -27.712 16.040 1.00 72.66  ? 358 ALA   A N   1 
ATOM   403  C  CA  . ALA   A 1 62  ? -30.816 -27.345 14.946 1.00 75.12  ? 358 ALA   A CA  1 
ATOM   404  C  C   . ALA   A 1 62  ? -32.263 -27.651 15.311 1.00 79.98  ? 358 ALA   A C   1 
ATOM   405  O  O   . ALA   A 1 62  ? -33.151 -26.805 15.144 1.00 73.68  ? 358 ALA   A O   1 
ATOM   406  C  CB  . ALA   A 1 62  ? -30.411 -28.074 13.663 1.00 72.49  ? 358 ALA   A CB  1 
ATOM   407  N  N   . LYS   A 1 63  ? -32.503 -28.858 15.838 1.00 88.03  ? 359 LYS   A N   1 
ATOM   408  C  CA  . LYS   A 1 63  ? -33.842 -29.298 16.233 1.00 94.87  ? 359 LYS   A CA  1 
ATOM   409  C  C   . LYS   A 1 63  ? -34.454 -28.353 17.258 1.00 96.72  ? 359 LYS   A C   1 
ATOM   410  O  O   . LYS   A 1 63  ? -35.536 -27.794 17.043 1.00 103.02 ? 359 LYS   A O   1 
ATOM   411  C  CB  . LYS   A 1 63  ? -33.767 -30.718 16.797 1.00 99.57  ? 359 LYS   A CB  1 
ATOM   412  C  CG  . LYS   A 1 63  ? -35.098 -31.282 17.247 1.00 103.89 ? 359 LYS   A CG  1 
ATOM   413  C  CD  . LYS   A 1 63  ? -34.914 -32.651 17.883 1.00 104.26 ? 359 LYS   A CD  1 
ATOM   414  C  CE  . LYS   A 1 63  ? -36.202 -33.453 17.862 1.00 103.85 ? 359 LYS   A CE  1 
ATOM   415  N  NZ  . LYS   A 1 63  ? -37.386 -32.682 18.333 1.00 100.07 ? 359 LYS   A NZ  1 
ATOM   416  N  N   . GLU   A 1 64  ? -33.775 -28.190 18.396 1.00 85.45  ? 360 GLU   A N   1 
ATOM   417  C  CA  . GLU   A 1 64  ? -34.150 -27.219 19.415 1.00 90.06  ? 360 GLU   A CA  1 
ATOM   418  C  C   . GLU   A 1 64  ? -34.533 -25.863 18.813 1.00 84.41  ? 360 GLU   A C   1 
ATOM   419  O  O   . GLU   A 1 64  ? -35.646 -25.366 19.028 1.00 85.29  ? 360 GLU   A O   1 
ATOM   420  C  CB  . GLU   A 1 64  ? -32.975 -27.088 20.390 1.00 91.95  ? 360 GLU   A CB  1 
ATOM   421  C  CG  . GLU   A 1 64  ? -33.274 -26.533 21.753 1.00 99.05  ? 360 GLU   A CG  1 
ATOM   422  C  CD  . GLU   A 1 64  ? -31.990 -26.193 22.502 1.00 101.73 ? 360 GLU   A CD  1 
ATOM   423  O  OE1 . GLU   A 1 64  ? -31.046 -27.018 22.458 1.00 102.45 ? 360 GLU   A OE1 1 
ATOM   424  O  OE2 . GLU   A 1 64  ? -31.918 -25.094 23.105 1.00 100.01 ? 360 GLU   A OE2 1 
ATOM   425  N  N   . PHE   A 1 65  ? -33.622 -25.256 18.042 1.00 75.00  ? 361 PHE   A N   1 
ATOM   426  C  CA  . PHE   A 1 65  ? -33.910 -23.954 17.440 1.00 76.05  ? 361 PHE   A CA  1 
ATOM   427  C  C   . PHE   A 1 65  ? -35.111 -24.030 16.500 1.00 79.01  ? 361 PHE   A C   1 
ATOM   428  O  O   . PHE   A 1 65  ? -36.023 -23.198 16.576 1.00 79.58  ? 361 PHE   A O   1 
ATOM   429  C  CB  . PHE   A 1 65  ? -32.678 -23.421 16.699 1.00 78.59  ? 361 PHE   A CB  1 
ATOM   430  C  CG  . PHE   A 1 65  ? -32.958 -22.216 15.824 1.00 75.28  ? 361 PHE   A CG  1 
ATOM   431  C  CD1 . PHE   A 1 65  ? -33.063 -20.950 16.377 1.00 73.06  ? 361 PHE   A CD1 1 
ATOM   432  C  CD2 . PHE   A 1 65  ? -33.116 -22.355 14.445 1.00 80.35  ? 361 PHE   A CD2 1 
ATOM   433  C  CE1 . PHE   A 1 65  ? -33.322 -19.845 15.575 1.00 74.19  ? 361 PHE   A CE1 1 
ATOM   434  C  CE2 . PHE   A 1 65  ? -33.377 -21.256 13.636 1.00 76.45  ? 361 PHE   A CE2 1 
ATOM   435  C  CZ  . PHE   A 1 65  ? -33.477 -19.997 14.203 1.00 77.35  ? 361 PHE   A CZ  1 
ATOM   436  N  N   . LEU   A 1 66  ? -35.136 -25.034 15.612 1.00 76.82  ? 362 LEU   A N   1 
ATOM   437  C  CA  . LEU   A 1 66  ? -36.242 -25.148 14.665 1.00 77.87  ? 362 LEU   A CA  1 
ATOM   438  C  C   . LEU   A 1 66  ? -37.574 -25.334 15.377 1.00 83.48  ? 362 LEU   A C   1 
ATOM   439  O  O   . LEU   A 1 66  ? -38.617 -24.899 14.873 1.00 80.84  ? 362 LEU   A O   1 
ATOM   440  C  CB  . LEU   A 1 66  ? -36.001 -26.314 13.701 1.00 84.57  ? 362 LEU   A CB  1 
ATOM   441  C  CG  . LEU   A 1 66  ? -34.917 -26.191 12.629 1.00 83.95  ? 362 LEU   A CG  1 
ATOM   442  C  CD1 . LEU   A 1 66  ? -34.935 -27.440 11.792 1.00 90.51  ? 362 LEU   A CD1 1 
ATOM   443  C  CD2 . LEU   A 1 66  ? -35.129 -24.965 11.770 1.00 80.05  ? 362 LEU   A CD2 1 
ATOM   444  N  N   . ASP   A 1 67  ? -37.554 -25.969 16.552 1.00 89.91  ? 363 ASP   A N   1 
ATOM   445  C  CA  . ASP   A 1 67  ? -38.784 -26.227 17.295 1.00 95.49  ? 363 ASP   A CA  1 
ATOM   446  C  C   . ASP   A 1 67  ? -39.378 -24.945 17.863 1.00 88.44  ? 363 ASP   A C   1 
ATOM   447  O  O   . ASP   A 1 67  ? -40.603 -24.769 17.868 1.00 90.62  ? 363 ASP   A O   1 
ATOM   448  C  CB  . ASP   A 1 67  ? -38.517 -27.233 18.414 1.00 94.98  ? 363 ASP   A CB  1 
ATOM   449  C  CG  . ASP   A 1 67  ? -38.625 -28.671 17.944 1.00 106.37 ? 363 ASP   A CG  1 
ATOM   450  O  OD1 . ASP   A 1 67  ? -39.755 -29.114 17.652 1.00 113.99 ? 363 ASP   A OD1 1 
ATOM   451  O  OD2 . ASP   A 1 67  ? -37.584 -29.359 17.864 1.00 107.39 ? 363 ASP   A OD2 1 
ATOM   452  N  N   . GLN   A 1 68  ? -38.536 -24.043 18.364 1.00 81.54  ? 364 GLN   A N   1 
ATOM   453  C  CA  . GLN   A 1 68  ? -39.088 -22.821 18.924 1.00 83.83  ? 364 GLN   A CA  1 
ATOM   454  C  C   . GLN   A 1 68  ? -39.452 -21.838 17.825 1.00 85.34  ? 364 GLN   A C   1 
ATOM   455  O  O   . GLN   A 1 68  ? -40.427 -21.093 17.964 1.00 87.76  ? 364 GLN   A O   1 
ATOM   456  C  CB  . GLN   A 1 68  ? -38.104 -22.210 19.931 1.00 79.74  ? 364 GLN   A CB  1 
ATOM   457  C  CG  . GLN   A 1 68  ? -36.703 -22.013 19.378 1.00 82.29  ? 364 GLN   A CG  1 
ATOM   458  C  CD  . GLN   A 1 68  ? -35.626 -21.993 20.455 1.00 79.69  ? 364 GLN   A CD  1 
ATOM   459  O  OE1 . GLN   A 1 68  ? -34.816 -21.057 20.530 1.00 70.69  ? 364 GLN   A OE1 1 
ATOM   460  N  NE2 . GLN   A 1 68  ? -35.594 -23.039 21.274 1.00 84.94  ? 364 GLN   A NE2 1 
ATOM   461  N  N   . TYR   A 1 69  ? -38.712 -21.854 16.714 1.00 87.61  ? 365 TYR   A N   1 
ATOM   462  C  CA  . TYR   A 1 69  ? -39.023 -20.954 15.606 1.00 87.08  ? 365 TYR   A CA  1 
ATOM   463  C  C   . TYR   A 1 69  ? -40.386 -21.261 14.997 1.00 88.26  ? 365 TYR   A C   1 
ATOM   464  O  O   . TYR   A 1 69  ? -41.134 -20.342 14.636 1.00 87.66  ? 365 TYR   A O   1 
ATOM   465  C  CB  . TYR   A 1 69  ? -37.942 -21.026 14.527 1.00 87.52  ? 365 TYR   A CB  1 
ATOM   466  C  CG  . TYR   A 1 69  ? -38.419 -20.396 13.247 1.00 89.62  ? 365 TYR   A CG  1 
ATOM   467  C  CD1 . TYR   A 1 69  ? -38.734 -19.043 13.202 1.00 90.13  ? 365 TYR   A CD1 1 
ATOM   468  C  CD2 . TYR   A 1 69  ? -38.600 -21.154 12.093 1.00 89.66  ? 365 TYR   A CD2 1 
ATOM   469  C  CE1 . TYR   A 1 69  ? -39.198 -18.463 12.045 1.00 91.82  ? 365 TYR   A CE1 1 
ATOM   470  C  CE2 . TYR   A 1 69  ? -39.064 -20.577 10.936 1.00 87.46  ? 365 TYR   A CE2 1 
ATOM   471  C  CZ  . TYR   A 1 69  ? -39.359 -19.232 10.919 1.00 89.68  ? 365 TYR   A CZ  1 
ATOM   472  O  OH  . TYR   A 1 69  ? -39.820 -18.641 9.771  1.00 92.21  ? 365 TYR   A OH  1 
ATOM   473  N  N   . TYR   A 1 70  ? -40.722 -22.540 14.845 1.00 96.26  ? 366 TYR   A N   1 
ATOM   474  C  CA  . TYR   A 1 70  ? -42.044 -22.861 14.325 1.00 105.35 ? 366 TYR   A CA  1 
ATOM   475  C  C   . TYR   A 1 70  ? -43.101 -22.662 15.398 1.00 108.12 ? 366 TYR   A C   1 
ATOM   476  O  O   . TYR   A 1 70  ? -44.223 -22.233 15.102 1.00 112.87 ? 366 TYR   A O   1 
ATOM   477  C  CB  . TYR   A 1 70  ? -42.065 -24.284 13.764 1.00 112.37 ? 366 TYR   A CB  1 
ATOM   478  C  CG  . TYR   A 1 70  ? -41.446 -24.349 12.391 1.00 112.22 ? 366 TYR   A CG  1 
ATOM   479  C  CD1 . TYR   A 1 70  ? -40.174 -24.875 12.198 1.00 108.94 ? 366 TYR   A CD1 1 
ATOM   480  C  CD2 . TYR   A 1 70  ? -42.120 -23.840 11.289 1.00 114.78 ? 366 TYR   A CD2 1 
ATOM   481  C  CE1 . TYR   A 1 70  ? -39.601 -24.911 10.938 1.00 108.95 ? 366 TYR   A CE1 1 
ATOM   482  C  CE2 . TYR   A 1 70  ? -41.558 -23.873 10.026 1.00 113.89 ? 366 TYR   A CE2 1 
ATOM   483  C  CZ  . TYR   A 1 70  ? -40.301 -24.408 9.853  1.00 109.22 ? 366 TYR   A CZ  1 
ATOM   484  O  OH  . TYR   A 1 70  ? -39.753 -24.427 8.590  1.00 102.55 ? 366 TYR   A OH  1 
ATOM   485  N  N   . SER   A 1 71  ? -42.747 -22.937 16.654 1.00 103.48 ? 367 SER   A N   1 
ATOM   486  C  CA  . SER   A 1 71  ? -43.622 -22.568 17.759 1.00 104.83 ? 367 SER   A CA  1 
ATOM   487  C  C   . SER   A 1 71  ? -43.917 -21.073 17.746 1.00 100.65 ? 367 SER   A C   1 
ATOM   488  O  O   . SER   A 1 71  ? -45.020 -20.653 18.112 1.00 109.44 ? 367 SER   A O   1 
ATOM   489  C  CB  . SER   A 1 71  ? -42.987 -22.988 19.089 1.00 103.88 ? 367 SER   A CB  1 
ATOM   490  O  OG  . SER   A 1 71  ? -43.936 -22.985 20.142 1.00 107.69 ? 367 SER   A OG  1 
ATOM   491  N  N   . SER   A 1 72  ? -42.957 -20.259 17.295 1.00 88.96  ? 368 SER   A N   1 
ATOM   492  C  CA  . SER   A 1 72  ? -43.136 -18.811 17.319 1.00 92.68  ? 368 SER   A CA  1 
ATOM   493  C  C   . SER   A 1 72  ? -44.075 -18.324 16.219 1.00 102.18 ? 368 SER   A C   1 
ATOM   494  O  O   . SER   A 1 72  ? -44.763 -17.314 16.404 1.00 107.77 ? 368 SER   A O   1 
ATOM   495  C  CB  . SER   A 1 72  ? -41.784 -18.108 17.202 1.00 91.23  ? 368 SER   A CB  1 
ATOM   496  O  OG  . SER   A 1 72  ? -41.608 -17.547 15.910 1.00 92.74  ? 368 SER   A OG  1 
ATOM   497  N  N   . ILE   A 1 73  ? -44.112 -18.999 15.068 1.00 105.66 ? 369 ILE   A N   1 
ATOM   498  C  CA  . ILE   A 1 73  ? -45.045 -18.608 14.017 1.00 110.61 ? 369 ILE   A CA  1 
ATOM   499  C  C   . ILE   A 1 73  ? -46.329 -19.414 14.178 1.00 118.81 ? 369 ILE   A C   1 
ATOM   500  O  O   . ILE   A 1 73  ? -47.155 -19.482 13.260 1.00 124.80 ? 369 ILE   A O   1 
ATOM   501  C  CB  . ILE   A 1 73  ? -44.434 -18.783 12.611 1.00 109.74 ? 369 ILE   A CB  1 
ATOM   502  C  CG1 . ILE   A 1 73  ? -43.933 -20.213 12.409 1.00 110.15 ? 369 ILE   A CG1 1 
ATOM   503  C  CG2 . ILE   A 1 73  ? -43.302 -17.775 12.382 1.00 102.78 ? 369 ILE   A CG2 1 
ATOM   504  C  CD1 . ILE   A 1 73  ? -42.973 -20.359 11.257 1.00 106.91 ? 369 ILE   A CD1 1 
ATOM   505  N  N   . LYS   A 1 74  ? -46.500 -20.021 15.354 1.00 119.31 ? 370 LYS   A N   1 
ATOM   506  C  CA  . LYS   A 1 74  ? -47.724 -20.732 15.731 1.00 125.86 ? 370 LYS   A CA  1 
ATOM   507  C  C   . LYS   A 1 74  ? -48.055 -21.847 14.740 1.00 133.87 ? 370 LYS   A C   1 
ATOM   508  O  O   . LYS   A 1 74  ? -49.219 -22.102 14.422 1.00 142.35 ? 370 LYS   A O   1 
ATOM   509  C  CB  . LYS   A 1 74  ? -48.899 -19.766 15.896 1.00 127.53 ? 370 LYS   A CB  1 
ATOM   510  C  CG  . LYS   A 1 74  ? -49.025 -19.230 17.321 1.00 128.35 ? 370 LYS   A CG  1 
ATOM   511  C  CD  . LYS   A 1 74  ? -49.263 -17.724 17.383 1.00 128.72 ? 370 LYS   A CD  1 
ATOM   512  C  CE  . LYS   A 1 74  ? -48.915 -17.180 18.771 1.00 129.72 ? 370 LYS   A CE  1 
ATOM   513  N  NZ  . LYS   A 1 74  ? -49.138 -15.711 18.911 1.00 130.12 ? 370 LYS   A NZ  1 
ATOM   514  N  N   . ARG   A 1 75  ? -47.011 -22.513 14.245 1.00 128.14 ? 371 ARG   A N   1 
ATOM   515  C  CA  . ARG   A 1 75  ? -47.111 -23.751 13.477 1.00 125.72 ? 371 ARG   A CA  1 
ATOM   516  C  C   . ARG   A 1 75  ? -46.105 -24.768 14.001 1.00 126.35 ? 371 ARG   A C   1 
ATOM   517  O  O   . ARG   A 1 75  ? -45.335 -25.375 13.254 1.00 120.82 ? 371 ARG   A O   1 
ATOM   518  C  CB  . ARG   A 1 75  ? -46.916 -23.492 11.997 1.00 121.50 ? 371 ARG   A CB  1 
ATOM   519  C  CG  . ARG   A 1 75  ? -47.855 -22.448 11.449 1.00 124.41 ? 371 ARG   A CG  1 
ATOM   520  C  CD  . ARG   A 1 75  ? -47.085 -21.475 10.588 1.00 122.01 ? 371 ARG   A CD  1 
ATOM   521  N  NE  . ARG   A 1 75  ? -47.789 -21.177 9.349  1.00 128.96 ? 371 ARG   A NE  1 
ATOM   522  C  CZ  . ARG   A 1 75  ? -47.891 -22.017 8.324  1.00 134.00 ? 371 ARG   A CZ  1 
ATOM   523  N  NH1 . ARG   A 1 75  ? -48.554 -21.655 7.234  1.00 132.97 ? 371 ARG   A NH1 1 
ATOM   524  N  NH2 . ARG   A 1 75  ? -47.336 -23.221 8.388  1.00 137.58 ? 371 ARG   A NH2 1 
ATOM   525  N  N   . PHE   A 1 76  ? -46.097 -24.921 15.328 1.00 131.44 ? 372 PHE   A N   1 
ATOM   526  C  CA  . PHE   A 1 76  ? -45.307 -25.934 16.019 1.00 136.36 ? 372 PHE   A CA  1 
ATOM   527  C  C   . PHE   A 1 76  ? -45.624 -27.325 15.482 1.00 143.90 ? 372 PHE   A C   1 
ATOM   528  O  O   . PHE   A 1 76  ? -46.790 -27.717 15.394 1.00 152.25 ? 372 PHE   A O   1 
ATOM   529  C  CB  . PHE   A 1 76  ? -45.620 -25.848 17.521 1.00 139.63 ? 372 PHE   A CB  1 
ATOM   530  C  CG  . PHE   A 1 76  ? -44.793 -26.757 18.409 1.00 140.74 ? 372 PHE   A CG  1 
ATOM   531  C  CD1 . PHE   A 1 76  ? -43.702 -27.467 17.927 1.00 138.31 ? 372 PHE   A CD1 1 
ATOM   532  C  CD2 . PHE   A 1 76  ? -45.123 -26.883 19.755 1.00 144.49 ? 372 PHE   A CD2 1 
ATOM   533  C  CE1 . PHE   A 1 76  ? -42.969 -28.289 18.761 1.00 138.10 ? 372 PHE   A CE1 1 
ATOM   534  C  CE2 . PHE   A 1 76  ? -44.393 -27.697 20.598 1.00 143.58 ? 372 PHE   A CE2 1 
ATOM   535  C  CZ  . PHE   A 1 76  ? -43.314 -28.403 20.100 1.00 142.05 ? 372 PHE   A CZ  1 
ATOM   536  N  N   . GLY   A 1 77  ? -44.579 -28.065 15.114 1.00 142.17 ? 373 GLY   A N   1 
ATOM   537  C  CA  . GLY   A 1 77  ? -44.706 -29.487 14.845 1.00 146.37 ? 373 GLY   A CA  1 
ATOM   538  C  C   . GLY   A 1 77  ? -45.562 -29.877 13.656 1.00 146.19 ? 373 GLY   A C   1 
ATOM   539  O  O   . GLY   A 1 77  ? -45.807 -31.066 13.426 1.00 153.74 ? 373 GLY   A O   1 
ATOM   540  N  N   . SER   A 1 78  ? -46.016 -28.896 12.886 1.00 136.63 ? 374 SER   A N   1 
ATOM   541  C  CA  . SER   A 1 78  ? -46.850 -29.164 11.722 1.00 130.86 ? 374 SER   A CA  1 
ATOM   542  C  C   . SER   A 1 78  ? -46.026 -29.911 10.674 1.00 125.34 ? 374 SER   A C   1 
ATOM   543  O  O   . SER   A 1 78  ? -44.879 -30.309 10.905 1.00 116.05 ? 374 SER   A O   1 
ATOM   544  C  CB  . SER   A 1 78  ? -47.424 -27.861 11.176 1.00 126.28 ? 374 SER   A CB  1 
ATOM   545  O  OG  . SER   A 1 78  ? -46.388 -26.953 10.840 1.00 120.04 ? 374 SER   A OG  1 
ATOM   546  N  N   . LYS   A 1 79  ? -46.619 -30.116 9.493  1.00 124.43 ? 375 LYS   A N   1 
ATOM   547  C  CA  . LYS   A 1 79  ? -45.867 -30.721 8.400  1.00 122.54 ? 375 LYS   A CA  1 
ATOM   548  C  C   . LYS   A 1 79  ? -44.749 -29.800 7.932  1.00 116.24 ? 375 LYS   A C   1 
ATOM   549  O  O   . LYS   A 1 79  ? -43.617 -30.251 7.724  1.00 112.95 ? 375 LYS   A O   1 
ATOM   550  C  CB  . LYS   A 1 79  ? -46.795 -31.077 7.236  1.00 127.78 ? 375 LYS   A CB  1 
ATOM   551  C  CG  . LYS   A 1 79  ? -46.076 -31.727 6.048  1.00 125.19 ? 375 LYS   A CG  1 
ATOM   552  C  CD  . LYS   A 1 79  ? -46.688 -33.076 5.679  1.00 129.67 ? 375 LYS   A CD  1 
ATOM   553  C  CE  . LYS   A 1 79  ? -45.850 -33.807 4.637  1.00 129.52 ? 375 LYS   A CE  1 
ATOM   554  N  NZ  . LYS   A 1 79  ? -44.498 -34.192 5.128  1.00 126.64 ? 375 LYS   A NZ  1 
ATOM   555  N  N   . ALA   A 1 80  ? -45.039 -28.504 7.781  1.00 118.39 ? 376 ALA   A N   1 
ATOM   556  C  CA  . ALA   A 1 80  ? -44.004 -27.569 7.349  1.00 118.31 ? 376 ALA   A CA  1 
ATOM   557  C  C   . ALA   A 1 80  ? -42.819 -27.560 8.310  1.00 114.65 ? 376 ALA   A C   1 
ATOM   558  O  O   . ALA   A 1 80  ? -41.677 -27.369 7.876  1.00 113.80 ? 376 ALA   A O   1 
ATOM   559  C  CB  . ALA   A 1 80  ? -44.592 -26.165 7.190  1.00 114.49 ? 376 ALA   A CB  1 
ATOM   560  N  N   . HIS   A 1 81  ? -43.059 -27.793 9.606  1.00 113.57 ? 377 HIS   A N   1 
ATOM   561  C  CA  . HIS   A 1 81  ? -41.952 -27.936 10.552 1.00 112.06 ? 377 HIS   A CA  1 
ATOM   562  C  C   . HIS   A 1 81  ? -41.200 -29.241 10.325 1.00 113.22 ? 377 HIS   A C   1 
ATOM   563  O  O   . HIS   A 1 81  ? -39.983 -29.242 10.110 1.00 108.60 ? 377 HIS   A O   1 
ATOM   564  C  CB  . HIS   A 1 81  ? -42.461 -27.860 11.999 1.00 113.47 ? 377 HIS   A CB  1 
ATOM   565  C  CG  . HIS   A 1 81  ? -41.423 -28.199 13.033 1.00 114.68 ? 377 HIS   A CG  1 
ATOM   566  N  ND1 . HIS   A 1 81  ? -41.753 -28.589 14.314 1.00 116.08 ? 377 HIS   A ND1 1 
ATOM   567  C  CD2 . HIS   A 1 81  ? -40.068 -28.198 12.982 1.00 111.72 ? 377 HIS   A CD2 1 
ATOM   568  C  CE1 . HIS   A 1 81  ? -40.651 -28.826 15.001 1.00 112.62 ? 377 HIS   A CE1 1 
ATOM   569  N  NE2 . HIS   A 1 81  ? -39.614 -28.596 14.217 1.00 111.40 ? 377 HIS   A NE2 1 
ATOM   570  N  N   . MET   A 1 82  ? -41.909 -30.370 10.384 1.00 119.97 ? 378 MET   A N   1 
ATOM   571  C  CA  . MET   A 1 82  ? -41.248 -31.671 10.304 1.00 121.70 ? 378 MET   A CA  1 
ATOM   572  C  C   . MET   A 1 82  ? -40.447 -31.840 9.014  1.00 115.85 ? 378 MET   A C   1 
ATOM   573  O  O   . MET   A 1 82  ? -39.399 -32.497 9.025  1.00 117.00 ? 378 MET   A O   1 
ATOM   574  C  CB  . MET   A 1 82  ? -42.282 -32.784 10.454 1.00 129.44 ? 378 MET   A CB  1 
ATOM   575  C  CG  . MET   A 1 82  ? -42.893 -32.840 11.849 1.00 136.01 ? 378 MET   A CG  1 
ATOM   576  S  SD  . MET   A 1 82  ? -41.618 -33.105 13.100 1.00 134.18 ? 378 MET   A SD  1 
ATOM   577  C  CE  . MET   A 1 82  ? -42.509 -32.699 14.611 1.00 138.76 ? 378 MET   A CE  1 
ATOM   578  N  N   . ASP   A 1 83  ? -40.899 -31.250 7.905  1.00 109.09 ? 379 ASP   A N   1 
ATOM   579  C  CA  . ASP   A 1 83  ? -40.108 -31.337 6.681  1.00 107.88 ? 379 ASP   A CA  1 
ATOM   580  C  C   . ASP   A 1 83  ? -38.866 -30.467 6.764  1.00 106.81 ? 379 ASP   A C   1 
ATOM   581  O  O   . ASP   A 1 83  ? -37.836 -30.804 6.171  1.00 107.33 ? 379 ASP   A O   1 
ATOM   582  C  CB  . ASP   A 1 83  ? -40.941 -30.950 5.461  1.00 108.16 ? 379 ASP   A CB  1 
ATOM   583  C  CG  . ASP   A 1 83  ? -41.883 -32.052 5.031  1.00 118.31 ? 379 ASP   A CG  1 
ATOM   584  O  OD1 . ASP   A 1 83  ? -43.088 -31.770 4.871  1.00 122.44 ? 379 ASP   A OD1 1 
ATOM   585  O  OD2 . ASP   A 1 83  ? -41.424 -33.205 4.869  1.00 122.59 ? 379 ASP   A OD2 1 
ATOM   586  N  N   . ARG   A 1 84  ? -38.949 -29.347 7.488  1.00 106.47 ? 380 ARG   A N   1 
ATOM   587  C  CA  . ARG   A 1 84  ? -37.771 -28.517 7.728  1.00 103.44 ? 380 ARG   A CA  1 
ATOM   588  C  C   . ARG   A 1 84  ? -36.799 -29.197 8.688  1.00 103.94 ? 380 ARG   A C   1 
ATOM   589  O  O   . ARG   A 1 84  ? -35.579 -29.042 8.561  1.00 108.20 ? 380 ARG   A O   1 
ATOM   590  C  CB  . ARG   A 1 84  ? -38.195 -27.157 8.279  1.00 97.10  ? 380 ARG   A CB  1 
ATOM   591  C  CG  . ARG   A 1 84  ? -37.049 -26.222 8.548  1.00 88.66  ? 380 ARG   A CG  1 
ATOM   592  C  CD  . ARG   A 1 84  ? -36.780 -25.335 7.356  1.00 87.89  ? 380 ARG   A CD  1 
ATOM   593  N  NE  . ARG   A 1 84  ? -35.508 -24.645 7.521  1.00 82.44  ? 380 ARG   A NE  1 
ATOM   594  C  CZ  . ARG   A 1 84  ? -34.342 -25.162 7.158  1.00 77.47  ? 380 ARG   A CZ  1 
ATOM   595  N  NH1 . ARG   A 1 84  ? -34.313 -26.358 6.598  1.00 84.15  ? 380 ARG   A NH1 1 
ATOM   596  N  NH2 . ARG   A 1 84  ? -33.209 -24.490 7.352  1.00 66.12  ? 380 ARG   A NH2 1 
ATOM   597  N  N   . LEU   A 1 85  ? -37.323 -29.932 9.670  1.00 100.63 ? 381 LEU   A N   1 
ATOM   598  C  CA  . LEU   A 1 85  ? -36.468 -30.733 10.537 1.00 98.78  ? 381 LEU   A CA  1 
ATOM   599  C  C   . LEU   A 1 85  ? -35.771 -31.827 9.737  1.00 101.37 ? 381 LEU   A C   1 
ATOM   600  O  O   . LEU   A 1 85  ? -34.552 -32.016 9.838  1.00 95.61  ? 381 LEU   A O   1 
ATOM   601  C  CB  . LEU   A 1 85  ? -37.309 -31.335 11.661 1.00 101.25 ? 381 LEU   A CB  1 
ATOM   602  C  CG  . LEU   A 1 85  ? -36.608 -31.663 12.969 1.00 101.51 ? 381 LEU   A CG  1 
ATOM   603  C  CD1 . LEU   A 1 85  ? -36.658 -30.449 13.874 1.00 96.05  ? 381 LEU   A CD1 1 
ATOM   604  C  CD2 . LEU   A 1 85  ? -37.274 -32.865 13.616 1.00 111.56 ? 381 LEU   A CD2 1 
ATOM   605  N  N   . GLU   A 1 86  ? -36.542 -32.554 8.924  1.00 111.72 ? 382 GLU   A N   1 
ATOM   606  C  CA  . GLU   A 1 86  ? -35.975 -33.558 8.029  1.00 115.85 ? 382 GLU   A CA  1 
ATOM   607  C  C   . GLU   A 1 86  ? -34.960 -32.938 7.082  1.00 107.21 ? 382 GLU   A C   1 
ATOM   608  O  O   . GLU   A 1 86  ? -33.873 -33.489 6.869  1.00 107.46 ? 382 GLU   A O   1 
ATOM   609  C  CB  . GLU   A 1 86  ? -37.098 -34.231 7.241  1.00 129.82 ? 382 GLU   A CB  1 
ATOM   610  C  CG  . GLU   A 1 86  ? -36.641 -35.257 6.218  1.00 142.55 ? 382 GLU   A CG  1 
ATOM   611  C  CD  . GLU   A 1 86  ? -37.054 -36.672 6.583  1.00 156.55 ? 382 GLU   A CD  1 
ATOM   612  O  OE1 . GLU   A 1 86  ? -36.262 -37.607 6.335  1.00 161.86 ? 382 GLU   A OE1 1 
ATOM   613  O  OE2 . GLU   A 1 86  ? -38.169 -36.848 7.120  1.00 161.63 ? 382 GLU   A OE2 1 
ATOM   614  N  N   . GLU   A 1 87  ? -35.301 -31.787 6.510  1.00 100.51 ? 383 GLU   A N   1 
ATOM   615  C  CA  . GLU   A 1 87  ? -34.418 -31.121 5.561  1.00 94.57  ? 383 GLU   A CA  1 
ATOM   616  C  C   . GLU   A 1 87  ? -33.069 -30.787 6.192  1.00 93.89  ? 383 GLU   A C   1 
ATOM   617  O  O   . GLU   A 1 87  ? -32.015 -31.086 5.619  1.00 95.20  ? 383 GLU   A O   1 
ATOM   618  C  CB  . GLU   A 1 87  ? -35.116 -29.871 5.030  1.00 90.83  ? 383 GLU   A CB  1 
ATOM   619  C  CG  . GLU   A 1 87  ? -34.264 -28.964 4.193  1.00 96.92  ? 383 GLU   A CG  1 
ATOM   620  C  CD  . GLU   A 1 87  ? -35.106 -27.966 3.420  1.00 97.12  ? 383 GLU   A CD  1 
ATOM   621  O  OE1 . GLU   A 1 87  ? -35.863 -27.207 4.075  1.00 87.83  ? 383 GLU   A OE1 1 
ATOM   622  O  OE2 . GLU   A 1 87  ? -35.025 -27.960 2.159  1.00 94.26  ? 383 GLU   A OE2 1 
ATOM   623  N  N   . VAL   A 1 88  ? -33.081 -30.189 7.389  1.00 89.91  ? 384 VAL   A N   1 
ATOM   624  C  CA  . VAL   A 1 88  ? -31.830 -29.805 8.042  1.00 86.02  ? 384 VAL   A CA  1 
ATOM   625  C  C   . VAL   A 1 88  ? -31.017 -31.041 8.407  1.00 92.18  ? 384 VAL   A C   1 
ATOM   626  O  O   . VAL   A 1 88  ? -29.803 -31.093 8.178  1.00 89.83  ? 384 VAL   A O   1 
ATOM   627  C  CB  . VAL   A 1 88  ? -32.094 -28.934 9.286  1.00 82.66  ? 384 VAL   A CB  1 
ATOM   628  C  CG1 . VAL   A 1 88  ? -30.799 -28.723 10.038 1.00 83.32  ? 384 VAL   A CG1 1 
ATOM   629  C  CG2 . VAL   A 1 88  ? -32.680 -27.597 8.897  1.00 77.89  ? 384 VAL   A CG2 1 
ATOM   630  N  N   . ASN   A 1 89  ? -31.675 -32.045 8.998  1.00 101.35 ? 385 ASN   A N   1 
ATOM   631  C  CA  . ASN   A 1 89  ? -31.004 -33.294 9.346  1.00 108.38 ? 385 ASN   A CA  1 
ATOM   632  C  C   . ASN   A 1 89  ? -30.202 -33.836 8.167  1.00 110.93 ? 385 ASN   A C   1 
ATOM   633  O  O   . ASN   A 1 89  ? -29.011 -34.143 8.296  1.00 113.27 ? 385 ASN   A O   1 
ATOM   634  C  CB  . ASN   A 1 89  ? -32.041 -34.317 9.811  1.00 117.42 ? 385 ASN   A CB  1 
ATOM   635  C  CG  . ASN   A 1 89  ? -31.416 -35.507 10.509 1.00 129.47 ? 385 ASN   A CG  1 
ATOM   636  O  OD1 . ASN   A 1 89  ? -30.403 -35.376 11.197 1.00 133.24 ? 385 ASN   A OD1 1 
ATOM   637  N  ND2 . ASN   A 1 89  ? -32.021 -36.681 10.336 1.00 134.22 ? 385 ASN   A ND2 1 
ATOM   638  N  N   . LYS   A 1 90  ? -30.839 -33.931 6.998  1.00 113.22 ? 386 LYS   A N   1 
ATOM   639  C  CA  . LYS   A 1 90  ? -30.164 -34.460 5.820  1.00 117.14 ? 386 LYS   A CA  1 
ATOM   640  C  C   . LYS   A 1 90  ? -29.025 -33.557 5.358  1.00 115.91 ? 386 LYS   A C   1 
ATOM   641  O  O   . LYS   A 1 90  ? -28.007 -34.054 4.866  1.00 119.52 ? 386 LYS   A O   1 
ATOM   642  C  CB  . LYS   A 1 90  ? -31.180 -34.659 4.699  1.00 122.51 ? 386 LYS   A CB  1 
ATOM   643  C  CG  . LYS   A 1 90  ? -32.222 -35.735 4.980  1.00 126.09 ? 386 LYS   A CG  1 
ATOM   644  C  CD  . LYS   A 1 90  ? -33.496 -35.461 4.198  1.00 126.46 ? 386 LYS   A CD  1 
ATOM   645  C  CE  . LYS   A 1 90  ? -34.267 -36.739 3.918  1.00 135.12 ? 386 LYS   A CE  1 
ATOM   646  N  NZ  . LYS   A 1 90  ? -35.533 -36.459 3.185  1.00 135.12 ? 386 LYS   A NZ  1 
ATOM   647  N  N   . GLU   A 1 91  ? -29.169 -32.238 5.506  1.00 108.67 ? 387 GLU   A N   1 
ATOM   648  C  CA  . GLU   A 1 91  ? -28.073 -31.343 5.148  1.00 105.67 ? 387 GLU   A CA  1 
ATOM   649  C  C   . GLU   A 1 91  ? -26.924 -31.430 6.150  1.00 107.78 ? 387 GLU   A C   1 
ATOM   650  O  O   . GLU   A 1 91  ? -25.767 -31.202 5.778  1.00 110.59 ? 387 GLU   A O   1 
ATOM   651  C  CB  . GLU   A 1 91  ? -28.580 -29.903 5.031  1.00 102.54 ? 387 GLU   A CB  1 
ATOM   652  C  CG  . GLU   A 1 91  ? -27.516 -28.898 4.583  1.00 95.88  ? 387 GLU   A CG  1 
ATOM   653  C  CD  . GLU   A 1 91  ? -28.055 -27.483 4.408  1.00 92.55  ? 387 GLU   A CD  1 
ATOM   654  O  OE1 . GLU   A 1 91  ? -27.320 -26.627 3.863  1.00 89.05  ? 387 GLU   A OE1 1 
ATOM   655  O  OE2 . GLU   A 1 91  ? -29.208 -27.219 4.818  1.00 91.32  ? 387 GLU   A OE2 1 
ATOM   656  N  N   . ILE   A 1 92  ? -27.216 -31.756 7.417  1.00 101.83 ? 388 ILE   A N   1 
ATOM   657  C  CA  . ILE   A 1 92  ? -26.144 -32.005 8.380  1.00 100.16 ? 388 ILE   A CA  1 
ATOM   658  C  C   . ILE   A 1 92  ? -25.510 -33.370 8.131  1.00 107.94 ? 388 ILE   A C   1 
ATOM   659  O  O   . ILE   A 1 92  ? -24.330 -33.578 8.428  1.00 111.76 ? 388 ILE   A O   1 
ATOM   660  C  CB  . ILE   A 1 92  ? -26.653 -31.882 9.831  1.00 98.35  ? 388 ILE   A CB  1 
ATOM   661  C  CG1 . ILE   A 1 92  ? -27.334 -30.534 10.069 1.00 96.54  ? 388 ILE   A CG1 1 
ATOM   662  C  CG2 . ILE   A 1 92  ? -25.499 -32.015 10.817 1.00 94.92  ? 388 ILE   A CG2 1 
ATOM   663  C  CD1 . ILE   A 1 92  ? -27.827 -30.351 11.497 1.00 93.95  ? 388 ILE   A CD1 1 
ATOM   664  N  N   . GLU   A 1 93  ? -26.275 -34.332 7.616  1.00 111.95 ? 389 GLU   A N   1 
ATOM   665  C  CA  . GLU   A 1 93  ? -25.649 -35.533 7.072  1.00 119.02 ? 389 GLU   A CA  1 
ATOM   666  C  C   . GLU   A 1 93  ? -24.758 -35.176 5.886  1.00 118.06 ? 389 GLU   A C   1 
ATOM   667  O  O   . GLU   A 1 93  ? -23.571 -35.522 5.858  1.00 118.22 ? 389 GLU   A O   1 
ATOM   668  C  CB  . GLU   A 1 93  ? -26.713 -36.550 6.650  1.00 124.44 ? 389 GLU   A CB  1 
ATOM   669  C  CG  . GLU   A 1 93  ? -27.689 -36.962 7.749  1.00 131.83 ? 389 GLU   A CG  1 
ATOM   670  C  CD  . GLU   A 1 93  ? -27.091 -37.921 8.768  1.00 136.03 ? 389 GLU   A CD  1 
ATOM   671  O  OE1 . GLU   A 1 93  ? -25.968 -38.421 8.539  1.00 138.33 ? 389 GLU   A OE1 1 
ATOM   672  O  OE2 . GLU   A 1 93  ? -27.752 -38.176 9.800  1.00 135.19 ? 389 GLU   A OE2 1 
ATOM   673  N  N   . SER   A 1 94  ? -25.313 -34.434 4.920  1.00 117.96 ? 390 SER   A N   1 
ATOM   674  C  CA  . SER   A 1 94  ? -24.641 -34.196 3.645  1.00 120.79 ? 390 SER   A CA  1 
ATOM   675  C  C   . SER   A 1 94  ? -23.383 -33.350 3.811  1.00 126.77 ? 390 SER   A C   1 
ATOM   676  O  O   . SER   A 1 94  ? -22.309 -33.723 3.326  1.00 131.07 ? 390 SER   A O   1 
ATOM   677  C  CB  . SER   A 1 94  ? -25.612 -33.529 2.678  1.00 115.04 ? 390 SER   A CB  1 
ATOM   678  O  OG  . SER   A 1 94  ? -24.918 -33.039 1.549  1.00 117.76 ? 390 SER   A OG  1 
ATOM   679  N  N   . THR   A 1 95  ? -23.497 -32.199 4.478  1.00 126.50 ? 391 THR   A N   1 
ATOM   680  C  CA  . THR   A 1 95  ? -22.396 -31.248 4.608  1.00 127.31 ? 391 THR   A CA  1 
ATOM   681  C  C   . THR   A 1 95  ? -21.785 -31.199 5.998  1.00 121.09 ? 391 THR   A C   1 
ATOM   682  O  O   . THR   A 1 95  ? -20.825 -30.449 6.205  1.00 113.38 ? 391 THR   A O   1 
ATOM   683  C  CB  . THR   A 1 95  ? -22.857 -29.832 4.237  1.00 131.49 ? 391 THR   A CB  1 
ATOM   684  O  OG1 . THR   A 1 95  ? -24.239 -29.850 3.864  1.00 138.67 ? 391 THR   A OG1 1 
ATOM   685  C  CG2 . THR   A 1 95  ? -22.013 -29.268 3.098  1.00 129.30 ? 391 THR   A CG2 1 
ATOM   686  N  N   . SER   A 1 96  ? -22.314 -31.963 6.952  1.00 126.48 ? 392 SER   A N   1 
ATOM   687  C  CA  . SER   A 1 96  ? -21.952 -31.854 8.363  1.00 124.53 ? 392 SER   A CA  1 
ATOM   688  C  C   . SER   A 1 96  ? -22.157 -30.435 8.890  1.00 118.40 ? 392 SER   A C   1 
ATOM   689  O  O   . SER   A 1 96  ? -21.508 -30.027 9.856  1.00 119.48 ? 392 SER   A O   1 
ATOM   690  C  CB  . SER   A 1 96  ? -20.517 -32.334 8.615  1.00 128.89 ? 392 SER   A CB  1 
ATOM   691  O  OG  . SER   A 1 96  ? -19.576 -31.515 7.948  1.00 128.93 ? 392 SER   A OG  1 
ATOM   692  N  N   . THR   A 1 97  ? -23.052 -29.686 8.250  1.00 107.31 ? 393 THR   A N   1 
ATOM   693  C  CA  . THR   A 1 97  ? -23.492 -28.359 8.673  1.00 90.48  ? 393 THR   A CA  1 
ATOM   694  C  C   . THR   A 1 97  ? -24.785 -28.059 7.917  1.00 85.38  ? 393 THR   A C   1 
ATOM   695  O  O   . THR   A 1 97  ? -25.342 -28.936 7.252  1.00 91.52  ? 393 THR   A O   1 
ATOM   696  C  CB  . THR   A 1 97  ? -22.393 -27.308 8.452  1.00 84.45  ? 393 THR   A CB  1 
ATOM   697  O  OG1 . THR   A 1 97  ? -22.883 -25.996 8.792  1.00 81.92  ? 393 THR   A OG1 1 
ATOM   698  C  CG2 . THR   A 1 97  ? -21.912 -27.322 7.023  1.00 80.24  ? 393 THR   A CG2 1 
ATOM   699  N  N   . TYR   A 1 98  ? -25.298 -26.839 8.044  1.00 84.20  ? 394 TYR   A N   1 
ATOM   700  C  CA  . TYR   A 1 98  ? -26.524 -26.500 7.332  1.00 84.43  ? 394 TYR   A CA  1 
ATOM   701  C  C   . TYR   A 1 98  ? -26.632 -24.984 7.206  1.00 78.37  ? 394 TYR   A C   1 
ATOM   702  O  O   . TYR   A 1 98  ? -25.815 -24.228 7.738  1.00 75.62  ? 394 TYR   A O   1 
ATOM   703  C  CB  . TYR   A 1 98  ? -27.764 -27.112 8.013  1.00 85.79  ? 394 TYR   A CB  1 
ATOM   704  C  CG  . TYR   A 1 98  ? -28.136 -26.485 9.327  1.00 82.77  ? 394 TYR   A CG  1 
ATOM   705  C  CD1 . TYR   A 1 98  ? -29.143 -25.527 9.401  1.00 84.18  ? 394 TYR   A CD1 1 
ATOM   706  C  CD2 . TYR   A 1 98  ? -27.476 -26.837 10.500 1.00 83.96  ? 394 TYR   A CD2 1 
ATOM   707  C  CE1 . TYR   A 1 98  ? -29.478 -24.930 10.609 1.00 77.89  ? 394 TYR   A CE1 1 
ATOM   708  C  CE2 . TYR   A 1 98  ? -27.804 -26.249 11.707 1.00 72.71  ? 394 TYR   A CE2 1 
ATOM   709  C  CZ  . TYR   A 1 98  ? -28.809 -25.300 11.756 1.00 73.37  ? 394 TYR   A CZ  1 
ATOM   710  O  OH  . TYR   A 1 98  ? -29.147 -24.710 12.956 1.00 75.52  ? 394 TYR   A OH  1 
ATOM   711  N  N   . GLN   A 1 99  ? -27.652 -24.549 6.480  1.00 80.24  ? 395 GLN   A N   1 
ATOM   712  C  CA  . GLN   A 1 99  ? -27.860 -23.139 6.183  1.00 76.93  ? 395 GLN   A CA  1 
ATOM   713  C  C   . GLN   A 1 99  ? -29.235 -22.718 6.665  1.00 70.16  ? 395 GLN   A C   1 
ATOM   714  O  O   . GLN   A 1 99  ? -30.210 -23.461 6.514  1.00 69.53  ? 395 GLN   A O   1 
ATOM   715  C  CB  . GLN   A 1 99  ? -27.728 -22.834 4.676  1.00 74.71  ? 395 GLN   A CB  1 
ATOM   716  C  CG  . GLN   A 1 99  ? -26.320 -22.950 4.108  1.00 76.77  ? 395 GLN   A CG  1 
ATOM   717  C  CD  . GLN   A 1 99  ? -25.356 -21.924 4.666  1.00 79.34  ? 395 GLN   A CD  1 
ATOM   718  O  OE1 . GLN   A 1 99  ? -24.376 -22.278 5.318  1.00 84.92  ? 395 GLN   A OE1 1 
ATOM   719  N  NE2 . GLN   A 1 99  ? -25.615 -20.647 4.396  1.00 82.52  ? 395 GLN   A NE2 1 
ATOM   720  N  N   . LEU   A 1 100 ? -29.306 -21.513 7.216  1.00 63.80  ? 396 LEU   A N   1 
ATOM   721  C  CA  . LEU   A 1 100 ? -30.543 -20.994 7.771  1.00 63.88  ? 396 LEU   A CA  1 
ATOM   722  C  C   . LEU   A 1 100 ? -31.377 -20.330 6.690  1.00 67.08  ? 396 LEU   A C   1 
ATOM   723  O  O   . LEU   A 1 100 ? -30.839 -19.649 5.812  1.00 67.53  ? 396 LEU   A O   1 
ATOM   724  C  CB  . LEU   A 1 100 ? -30.261 -19.972 8.869  1.00 48.34  ? 396 LEU   A CB  1 
ATOM   725  C  CG  . LEU   A 1 100 ? -29.635 -20.502 10.167 1.00 52.00  ? 396 LEU   A CG  1 
ATOM   726  C  CD1 . LEU   A 1 100 ? -28.914 -19.360 10.849 1.00 52.74  ? 396 LEU   A CD1 1 
ATOM   727  C  CD2 . LEU   A 1 100 ? -30.719 -21.041 11.075 1.00 57.21  ? 396 LEU   A CD2 1 
ATOM   728  N  N   . LYS   A 1 101 ? -32.694 -20.521 6.781  1.00 67.74  ? 397 LYS   A N   1 
ATOM   729  C  CA  . LYS   A 1 101 ? -33.639 -19.745 5.991  1.00 77.63  ? 397 LYS   A CA  1 
ATOM   730  C  C   . LYS   A 1 101 ? -33.516 -18.271 6.339  1.00 74.27  ? 397 LYS   A C   1 
ATOM   731  O  O   . LYS   A 1 101 ? -33.148 -17.912 7.457  1.00 75.78  ? 397 LYS   A O   1 
ATOM   732  C  CB  . LYS   A 1 101 ? -35.068 -20.218 6.259  1.00 86.21  ? 397 LYS   A CB  1 
ATOM   733  C  CG  . LYS   A 1 101 ? -35.374 -21.609 5.764  1.00 91.68  ? 397 LYS   A CG  1 
ATOM   734  C  CD  . LYS   A 1 101 ? -35.641 -21.581 4.278  1.00 95.03  ? 397 LYS   A CD  1 
ATOM   735  C  CE  . LYS   A 1 101 ? -35.336 -22.914 3.642  1.00 98.65  ? 397 LYS   A CE  1 
ATOM   736  N  NZ  . LYS   A 1 101 ? -35.051 -22.747 2.181  1.00 99.87  ? 397 LYS   A NZ  1 
ATOM   737  N  N   . ASP   A 1 102 ? -33.818 -17.413 5.363  1.00 66.87  ? 398 ASP   A N   1 
ATOM   738  C  CA  . ASP   A 1 102 ? -33.891 -15.979 5.632  1.00 70.50  ? 398 ASP   A CA  1 
ATOM   739  C  C   . ASP   A 1 102 ? -34.717 -15.698 6.879  1.00 72.46  ? 398 ASP   A C   1 
ATOM   740  O  O   . ASP   A 1 102 ? -34.300 -14.930 7.753  1.00 67.02  ? 398 ASP   A O   1 
ATOM   741  C  CB  . ASP   A 1 102 ? -34.493 -15.240 4.433  1.00 85.67  ? 398 ASP   A CB  1 
ATOM   742  C  CG  . ASP   A 1 102 ? -33.468 -14.915 3.353  1.00 87.26  ? 398 ASP   A CG  1 
ATOM   743  O  OD1 . ASP   A 1 102 ? -32.354 -15.486 3.378  1.00 80.47  ? 398 ASP   A OD1 1 
ATOM   744  O  OD2 . ASP   A 1 102 ? -33.785 -14.066 2.485  1.00 89.76  ? 398 ASP   A OD2 1 
ATOM   745  N  N   . THR   A 1 103 ? -35.882 -16.342 6.990  1.00 74.24  ? 399 THR   A N   1 
ATOM   746  C  CA  . THR   A 1 103 ? -36.758 -16.126 8.140  1.00 74.71  ? 399 THR   A CA  1 
ATOM   747  C  C   . THR   A 1 103 ? -36.143 -16.659 9.431  1.00 77.80  ? 399 THR   A C   1 
ATOM   748  O  O   . THR   A 1 103 ? -36.282 -16.043 10.497 1.00 75.36  ? 399 THR   A O   1 
ATOM   749  C  CB  . THR   A 1 103 ? -38.104 -16.795 7.885  1.00 76.18  ? 399 THR   A CB  1 
ATOM   750  O  OG1 . THR   A 1 103 ? -37.895 -18.187 7.613  1.00 72.22  ? 399 THR   A OG1 1 
ATOM   751  C  CG2 . THR   A 1 103 ? -38.803 -16.150 6.701  1.00 71.19  ? 399 THR   A CG2 1 
ATOM   752  N  N   . GLU   A 1 104 ? -35.482 -17.813 9.360  1.00 76.71  ? 400 GLU   A N   1 
ATOM   753  C  CA  . GLU   A 1 104 ? -34.808 -18.351 10.533 1.00 72.15  ? 400 GLU   A CA  1 
ATOM   754  C  C   . GLU   A 1 104 ? -33.651 -17.458 10.970 1.00 72.85  ? 400 GLU   A C   1 
ATOM   755  O  O   . GLU   A 1 104 ? -33.408 -17.304 12.180 1.00 76.71  ? 400 GLU   A O   1 
ATOM   756  C  CB  . GLU   A 1 104 ? -34.314 -19.764 10.243 1.00 71.75  ? 400 GLU   A CB  1 
ATOM   757  C  CG  . GLU   A 1 104 ? -35.410 -20.776 9.984  1.00 70.18  ? 400 GLU   A CG  1 
ATOM   758  C  CD  . GLU   A 1 104 ? -34.879 -22.018 9.293  1.00 75.87  ? 400 GLU   A CD  1 
ATOM   759  O  OE1 . GLU   A 1 104 ? -35.662 -22.980 9.127  1.00 74.83  ? 400 GLU   A OE1 1 
ATOM   760  O  OE2 . GLU   A 1 104 ? -33.683 -22.029 8.915  1.00 78.89  ? 400 GLU   A OE2 1 
ATOM   761  N  N   . LEU   A 1 105 ? -32.939 -16.851 10.010 1.00 60.44  ? 401 LEU   A N   1 
ATOM   762  C  CA  . LEU   A 1 105 ? -31.847 -15.950 10.373 1.00 61.48  ? 401 LEU   A CA  1 
ATOM   763  C  C   . LEU   A 1 105 ? -32.360 -14.720 11.122 1.00 63.99  ? 401 LEU   A C   1 
ATOM   764  O  O   . LEU   A 1 105 ? -31.741 -14.289 12.100 1.00 63.43  ? 401 LEU   A O   1 
ATOM   765  C  CB  . LEU   A 1 105 ? -31.061 -15.538 9.132  1.00 55.37  ? 401 LEU   A CB  1 
ATOM   766  C  CG  . LEU   A 1 105 ? -29.707 -14.872 9.366  1.00 54.45  ? 401 LEU   A CG  1 
ATOM   767  C  CD1 . LEU   A 1 105 ? -28.683 -15.819 9.996  1.00 52.40  ? 401 LEU   A CD1 1 
ATOM   768  C  CD2 . LEU   A 1 105 ? -29.203 -14.324 8.065  1.00 56.58  ? 401 LEU   A CD2 1 
ATOM   769  N  N   . ILE   A 1 106 ? -33.496 -14.158 10.695 1.00 60.47  ? 402 ILE   A N   1 
ATOM   770  C  CA  . ILE   A 1 106 ? -34.030 -12.947 11.329 1.00 56.87  ? 402 ILE   A CA  1 
ATOM   771  C  C   . ILE   A 1 106 ? -34.562 -13.265 12.727 1.00 62.01  ? 402 ILE   A C   1 
ATOM   772  O  O   . ILE   A 1 106 ? -34.293 -12.538 13.693 1.00 61.93  ? 402 ILE   A O   1 
ATOM   773  C  CB  . ILE   A 1 106 ? -35.116 -12.309 10.432 1.00 61.19  ? 402 ILE   A CB  1 
ATOM   774  C  CG1 . ILE   A 1 106 ? -34.503 -11.661 9.179  1.00 57.89  ? 402 ILE   A CG1 1 
ATOM   775  C  CG2 . ILE   A 1 106 ? -35.928 -11.282 11.188 1.00 64.14  ? 402 ILE   A CG2 1 
ATOM   776  C  CD1 . ILE   A 1 106 ? -35.378 -11.779 7.919  1.00 58.49  ? 402 ILE   A CD1 1 
ATOM   777  N  N   . TYR   A 1 107 ? -35.340 -14.342 12.843 1.00 63.47  ? 403 TYR   A N   1 
ATOM   778  C  CA  . TYR   A 1 107 ? -35.816 -14.811 14.134 1.00 67.21  ? 403 TYR   A CA  1 
ATOM   779  C  C   . TYR   A 1 107 ? -34.652 -15.078 15.087 1.00 73.64  ? 403 TYR   A C   1 
ATOM   780  O  O   . TYR   A 1 107 ? -34.617 -14.554 16.215 1.00 60.27  ? 403 TYR   A O   1 
ATOM   781  C  CB  . TYR   A 1 107 ? -36.659 -16.074 13.937 1.00 65.32  ? 403 TYR   A CB  1 
ATOM   782  C  CG  . TYR   A 1 107 ? -37.005 -16.766 15.231 1.00 77.55  ? 403 TYR   A CG  1 
ATOM   783  C  CD1 . TYR   A 1 107 ? -38.206 -16.512 15.874 1.00 84.77  ? 403 TYR   A CD1 1 
ATOM   784  C  CD2 . TYR   A 1 107 ? -36.122 -17.667 15.821 1.00 83.25  ? 403 TYR   A CD2 1 
ATOM   785  C  CE1 . TYR   A 1 107 ? -38.520 -17.137 17.072 1.00 88.78  ? 403 TYR   A CE1 1 
ATOM   786  C  CE2 . TYR   A 1 107 ? -36.420 -18.284 17.021 1.00 86.34  ? 403 TYR   A CE2 1 
ATOM   787  C  CZ  . TYR   A 1 107 ? -37.621 -18.015 17.635 1.00 86.09  ? 403 TYR   A CZ  1 
ATOM   788  O  OH  . TYR   A 1 107 ? -37.934 -18.633 18.806 1.00 85.26  ? 403 TYR   A OH  1 
ATOM   789  N  N   . GLY   A 1 108 ? -33.703 -15.915 14.654 1.00 71.22  ? 404 GLY   A N   1 
ATOM   790  C  CA  . GLY   A 1 108 ? -32.520 -16.239 15.431 1.00 60.67  ? 404 GLY   A CA  1 
ATOM   791  C  C   . GLY   A 1 108 ? -31.796 -14.998 15.904 1.00 62.06  ? 404 GLY   A C   1 
ATOM   792  O  O   . GLY   A 1 108 ? -31.555 -14.839 17.097 1.00 57.66  ? 404 GLY   A O   1 
ATOM   793  N  N   . ALA   A 1 109 ? -31.475 -14.095 14.980 1.00 61.58  ? 405 ALA   A N   1 
ATOM   794  C  CA  . ALA   A 1 109 ? -30.777 -12.872 15.348 1.00 56.19  ? 405 ALA   A CA  1 
ATOM   795  C  C   . ALA   A 1 109 ? -31.558 -12.080 16.391 1.00 58.41  ? 405 ALA   A C   1 
ATOM   796  O  O   . ALA   A 1 109 ? -30.995 -11.630 17.397 1.00 61.15  ? 405 ALA   A O   1 
ATOM   797  C  CB  . ALA   A 1 109 ? -30.533 -12.026 14.095 1.00 49.81  ? 405 ALA   A CB  1 
ATOM   798  N  N   . LYS   A 1 110 ? -32.863 -11.898 16.163 1.00 56.19  ? 406 LYS   A N   1 
ATOM   799  C  CA  . LYS   A 1 110 ? -33.663 -11.071 17.064 1.00 60.40  ? 406 LYS   A CA  1 
ATOM   800  C  C   . LYS   A 1 110 ? -33.735 -11.676 18.455 1.00 64.18  ? 406 LYS   A C   1 
ATOM   801  O  O   . LYS   A 1 110 ? -33.860 -10.949 19.451 1.00 60.98  ? 406 LYS   A O   1 
ATOM   802  C  CB  . LYS   A 1 110 ? -35.077 -10.900 16.513 1.00 59.66  ? 406 LYS   A CB  1 
ATOM   803  C  CG  . LYS   A 1 110 ? -35.230 -9.847  15.456 1.00 66.41  ? 406 LYS   A CG  1 
ATOM   804  C  CD  . LYS   A 1 110 ? -36.655 -9.850  14.955 1.00 66.71  ? 406 LYS   A CD  1 
ATOM   805  C  CE  . LYS   A 1 110 ? -36.875 -8.771  13.926 1.00 59.27  ? 406 LYS   A CE  1 
ATOM   806  N  NZ  . LYS   A 1 110 ? -38.333 -8.553  13.734 1.00 61.47  ? 406 LYS   A NZ  1 
ATOM   807  N  N   . HIS   A 1 111 ? -33.678 -13.003 18.536 1.00 63.52  ? 407 HIS   A N   1 
ATOM   808  C  CA  . HIS   A 1 111 ? -33.776 -13.707 19.798 1.00 65.53  ? 407 HIS   A CA  1 
ATOM   809  C  C   . HIS   A 1 111 ? -32.439 -13.836 20.504 1.00 67.11  ? 407 HIS   A C   1 
ATOM   810  O  O   . HIS   A 1 111 ? -32.411 -13.943 21.739 1.00 66.54  ? 407 HIS   A O   1 
ATOM   811  C  CB  . HIS   A 1 111 ? -34.445 -15.061 19.549 1.00 63.52  ? 407 HIS   A CB  1 
ATOM   812  C  CG  . HIS   A 1 111 ? -35.935 -14.967 19.545 1.00 60.75  ? 407 HIS   A CG  1 
ATOM   813  N  ND1 . HIS   A 1 111 ? -36.641 -14.424 18.494 1.00 66.37  ? 407 HIS   A ND1 1 
ATOM   814  C  CD2 . HIS   A 1 111 ? -36.848 -15.260 20.502 1.00 62.27  ? 407 HIS   A CD2 1 
ATOM   815  C  CE1 . HIS   A 1 111 ? -37.929 -14.429 18.784 1.00 66.64  ? 407 HIS   A CE1 1 
ATOM   816  N  NE2 . HIS   A 1 111 ? -38.082 -14.929 19.998 1.00 67.37  ? 407 HIS   A NE2 1 
ATOM   817  N  N   . ALA   A 1 112 ? -31.337 -13.758 19.758 1.00 61.97  ? 408 ALA   A N   1 
ATOM   818  C  CA  . ALA   A 1 112 ? -30.048 -13.528 20.395 1.00 60.36  ? 408 ALA   A CA  1 
ATOM   819  C  C   . ALA   A 1 112 ? -30.058 -12.224 21.180 1.00 64.88  ? 408 ALA   A C   1 
ATOM   820  O  O   . ALA   A 1 112 ? -29.586 -12.166 22.325 1.00 64.60  ? 408 ALA   A O   1 
ATOM   821  C  CB  . ALA   A 1 112 ? -28.940 -13.506 19.354 1.00 59.40  ? 408 ALA   A CB  1 
ATOM   822  N  N   . TRP   A 1 113 ? -30.596 -11.162 20.574 1.00 58.88  ? 409 TRP   A N   1 
ATOM   823  C  CA  . TRP   A 1 113 ? -30.722 -9.900  21.289 1.00 57.20  ? 409 TRP   A CA  1 
ATOM   824  C  C   . TRP   A 1 113 ? -31.697 -10.028 22.458 1.00 62.32  ? 409 TRP   A C   1 
ATOM   825  O  O   . TRP   A 1 113 ? -31.383 -9.629  23.582 1.00 56.73  ? 409 TRP   A O   1 
ATOM   826  C  CB  . TRP   A 1 113 ? -31.168 -8.799  20.337 1.00 54.22  ? 409 TRP   A CB  1 
ATOM   827  C  CG  . TRP   A 1 113 ? -31.326 -7.422  20.977 1.00 57.55  ? 409 TRP   A CG  1 
ATOM   828  C  CD1 . TRP   A 1 113 ? -30.957 -7.033  22.244 1.00 61.30  ? 409 TRP   A CD1 1 
ATOM   829  C  CD2 . TRP   A 1 113 ? -31.903 -6.266  20.359 1.00 60.95  ? 409 TRP   A CD2 1 
ATOM   830  N  NE1 . TRP   A 1 113 ? -31.276 -5.712  22.447 1.00 63.53  ? 409 TRP   A NE1 1 
ATOM   831  C  CE2 . TRP   A 1 113 ? -31.856 -5.217  21.305 1.00 63.26  ? 409 TRP   A CE2 1 
ATOM   832  C  CE3 . TRP   A 1 113 ? -32.463 -6.017  19.098 1.00 58.39  ? 409 TRP   A CE3 1 
ATOM   833  C  CZ2 . TRP   A 1 113 ? -32.336 -3.943  21.024 1.00 63.55  ? 409 TRP   A CZ2 1 
ATOM   834  C  CZ3 . TRP   A 1 113 ? -32.938 -4.753  18.823 1.00 62.37  ? 409 TRP   A CZ3 1 
ATOM   835  C  CH2 . TRP   A 1 113 ? -32.871 -3.730  19.779 1.00 65.51  ? 409 TRP   A CH2 1 
ATOM   836  N  N   . ARG   A 1 114 ? -32.890 -10.573 22.195 1.00 58.15  ? 410 ARG   A N   1 
ATOM   837  C  CA  . ARG   A 1 114 ? -33.897 -10.788 23.227 1.00 58.61  ? 410 ARG   A CA  1 
ATOM   838  C  C   . ARG   A 1 114 ? -33.334 -11.504 24.448 1.00 64.11  ? 410 ARG   A C   1 
ATOM   839  O  O   . ARG   A 1 114 ? -33.804 -11.294 25.573 1.00 61.18  ? 410 ARG   A O   1 
ATOM   840  C  CB  . ARG   A 1 114 ? -35.043 -11.605 22.646 1.00 60.08  ? 410 ARG   A CB  1 
ATOM   841  C  CG  . ARG   A 1 114 ? -36.228 -11.732 23.537 1.00 61.02  ? 410 ARG   A CG  1 
ATOM   842  C  CD  . ARG   A 1 114 ? -37.275 -12.650 22.938 1.00 66.11  ? 410 ARG   A CD  1 
ATOM   843  N  NE  . ARG   A 1 114 ? -38.551 -12.414 23.611 1.00 73.12  ? 410 ARG   A NE  1 
ATOM   844  C  CZ  . ARG   A 1 114 ? -39.695 -13.015 23.314 1.00 71.07  ? 410 ARG   A CZ  1 
ATOM   845  N  NH1 . ARG   A 1 114 ? -40.792 -12.720 24.000 1.00 59.77  ? 410 ARG   A NH1 1 
ATOM   846  N  NH2 . ARG   A 1 114 ? -39.745 -13.907 22.333 1.00 75.00  ? 410 ARG   A NH2 1 
ATOM   847  N  N   . ASN   A 1 115 ? -32.332 -12.349 24.244 1.00 62.34  ? 411 ASN   A N   1 
ATOM   848  C  CA  . ASN   A 1 115 ? -31.744 -13.149 25.302 1.00 58.82  ? 411 ASN   A CA  1 
ATOM   849  C  C   . ASN   A 1 115 ? -30.449 -12.562 25.833 1.00 57.76  ? 411 ASN   A C   1 
ATOM   850  O  O   . ASN   A 1 115 ? -29.840 -13.148 26.736 1.00 61.57  ? 411 ASN   A O   1 
ATOM   851  C  CB  . ASN   A 1 115 ? -31.485 -14.569 24.798 1.00 51.78  ? 411 ASN   A CB  1 
ATOM   852  C  CG  . ASN   A 1 115 ? -32.756 -15.286 24.396 1.00 65.51  ? 411 ASN   A CG  1 
ATOM   853  O  OD1 . ASN   A 1 115 ? -33.842 -14.949 24.858 1.00 73.67  ? 411 ASN   A OD1 1 
ATOM   854  N  ND2 . ASN   A 1 115 ? -32.627 -16.287 23.531 1.00 70.56  ? 411 ASN   A ND2 1 
ATOM   855  N  N   . ALA   A 1 116 ? -30.002 -11.441 25.282 1.00 54.26  ? 412 ALA   A N   1 
ATOM   856  C  CA  . ALA   A 1 116 ? -28.794 -10.797 25.763 1.00 56.52  ? 412 ALA   A CA  1 
ATOM   857  C  C   . ALA   A 1 116 ? -29.047 -10.274 27.177 1.00 56.26  ? 412 ALA   A C   1 
ATOM   858  O  O   . ALA   A 1 116 ? -29.570 -9.170  27.352 1.00 47.68  ? 412 ALA   A O   1 
ATOM   859  C  CB  . ALA   A 1 116 ? -28.387 -9.663  24.812 1.00 53.00  ? 412 ALA   A CB  1 
ATOM   860  N  N   . SER   A 1 117 ? -28.697 -11.059 28.190 1.00 57.95  ? 413 SER   A N   1 
ATOM   861  C  CA  . SER   A 1 117 ? -29.145 -10.750 29.543 1.00 58.96  ? 413 SER   A CA  1 
ATOM   862  C  C   . SER   A 1 117 ? -28.470 -9.510  30.117 1.00 54.27  ? 413 SER   A C   1 
ATOM   863  O  O   . SER   A 1 117 ? -29.002 -8.909  31.056 1.00 50.27  ? 413 SER   A O   1 
ATOM   864  C  CB  . SER   A 1 117 ? -28.914 -11.958 30.456 1.00 50.48  ? 413 SER   A CB  1 
ATOM   865  O  OG  . SER   A 1 117 ? -27.535 -12.164 30.672 1.00 52.40  ? 413 SER   A OG  1 
ATOM   866  N  N   . ARG   A 1 118 ? -27.326 -9.108  29.565 1.00 48.36  ? 414 ARG   A N   1 
ATOM   867  C  CA  . ARG   A 1 118 ? -26.659 -7.879  29.973 1.00 43.74  ? 414 ARG   A CA  1 
ATOM   868  C  C   . ARG   A 1 118 ? -27.162 -6.650  29.233 1.00 49.32  ? 414 ARG   A C   1 
ATOM   869  O  O   . ARG   A 1 118 ? -26.632 -5.569  29.478 1.00 35.46  ? 414 ARG   A O   1 
ATOM   870  C  CB  . ARG   A 1 118 ? -25.148 -7.992  29.762 1.00 47.20  ? 414 ARG   A CB  1 
ATOM   871  C  CG  . ARG   A 1 118 ? -24.482 -9.067  30.601 1.00 52.07  ? 414 ARG   A CG  1 
ATOM   872  C  CD  . ARG   A 1 118 ? -22.980 -9.144  30.374 1.00 51.69  ? 414 ARG   A CD  1 
ATOM   873  N  NE  . ARG   A 1 118 ? -22.334 -9.822  31.492 1.00 49.19  ? 414 ARG   A NE  1 
ATOM   874  C  CZ  . ARG   A 1 118 ? -21.044 -10.139 31.533 1.00 54.69  ? 414 ARG   A CZ  1 
ATOM   875  N  NH1 . ARG   A 1 118 ? -20.267 -9.861  30.501 1.00 56.18  ? 414 ARG   A NH1 1 
ATOM   876  N  NH2 . ARG   A 1 118 ? -20.530 -10.746 32.604 1.00 56.10  ? 414 ARG   A NH2 1 
ATOM   877  N  N   . CYS   A 1 119 ? -28.127 -6.792  28.304 1.00 48.34  ? 415 CYS   A N   1 
ATOM   878  C  CA  . CYS   A 1 119 ? -28.643 -5.664  27.523 1.00 47.04  ? 415 CYS   A CA  1 
ATOM   879  C  C   . CYS   A 1 119 ? -29.847 -5.021  28.199 1.00 49.82  ? 415 CYS   A C   1 
ATOM   880  O  O   . CYS   A 1 119 ? -30.859 -5.687  28.440 1.00 55.45  ? 415 CYS   A O   1 
ATOM   881  C  CB  . CYS   A 1 119 ? -29.066 -6.081  26.106 1.00 42.35  ? 415 CYS   A CB  1 
ATOM   882  S  SG  . CYS   A 1 119 ? -29.584 -4.610  25.161 1.00 43.31  ? 415 CYS   A SG  1 
ATOM   883  N  N   . VAL   A 1 120 ? -29.764 -3.712  28.441 1.00 53.13  ? 416 VAL   A N   1 
ATOM   884  C  CA  . VAL   A 1 120 ? -30.859 -2.991  29.087 1.00 56.18  ? 416 VAL   A CA  1 
ATOM   885  C  C   . VAL   A 1 120 ? -31.878 -2.443  28.089 1.00 60.94  ? 416 VAL   A C   1 
ATOM   886  O  O   . VAL   A 1 120 ? -33.009 -2.117  28.483 1.00 54.83  ? 416 VAL   A O   1 
ATOM   887  C  CB  . VAL   A 1 120 ? -30.296 -1.857  29.969 1.00 56.39  ? 416 VAL   A CB  1 
ATOM   888  C  CG1 . VAL   A 1 120 ? -29.614 -0.785  29.127 1.00 59.34  ? 416 VAL   A CG1 1 
ATOM   889  C  CG2 . VAL   A 1 120 ? -31.398 -1.255  30.883 1.00 52.08  ? 416 VAL   A CG2 1 
ATOM   890  N  N   . GLY   A 1 121 ? -31.535 -2.377  26.801 1.00 60.26  ? 417 GLY   A N   1 
ATOM   891  C  CA  . GLY   A 1 121 ? -32.430 -1.788  25.820 1.00 59.07  ? 417 GLY   A CA  1 
ATOM   892  C  C   . GLY   A 1 121 ? -33.288 -2.788  25.077 1.00 56.07  ? 417 GLY   A C   1 
ATOM   893  O  O   . GLY   A 1 121 ? -33.797 -2.490  23.989 1.00 63.94  ? 417 GLY   A O   1 
ATOM   894  N  N   . ARG   A 1 122 ? -33.487 -3.964  25.671 1.00 54.51  ? 418 ARG   A N   1 
ATOM   895  C  CA  . ARG   A 1 122 ? -34.068 -5.102  24.958 1.00 55.68  ? 418 ARG   A CA  1 
ATOM   896  C  C   . ARG   A 1 122 ? -35.551 -4.963  24.696 1.00 60.15  ? 418 ARG   A C   1 
ATOM   897  O  O   . ARG   A 1 122 ? -36.109 -5.796  23.977 1.00 66.31  ? 418 ARG   A O   1 
ATOM   898  C  CB  . ARG   A 1 122 ? -33.844 -6.407  25.718 1.00 37.58  ? 418 ARG   A CB  1 
ATOM   899  C  CG  . ARG   A 1 122 ? -32.439 -6.919  25.642 1.00 59.06  ? 418 ARG   A CG  1 
ATOM   900  C  CD  . ARG   A 1 122 ? -32.369 -8.252  26.293 1.00 57.25  ? 418 ARG   A CD  1 
ATOM   901  N  NE  . ARG   A 1 122 ? -32.196 -8.090  27.728 1.00 54.75  ? 418 ARG   A NE  1 
ATOM   902  C  CZ  . ARG   A 1 122 ? -32.358 -9.058  28.615 1.00 49.22  ? 418 ARG   A CZ  1 
ATOM   903  N  NH1 . ARG   A 1 122 ? -32.721 -10.271 28.212 1.00 47.84  ? 418 ARG   A NH1 1 
ATOM   904  N  NH2 . ARG   A 1 122 ? -32.150 -8.808  29.910 1.00 54.69  ? 418 ARG   A NH2 1 
ATOM   905  N  N   . ILE   A 1 123 ? -36.196 -3.936  25.236 1.00 60.16  ? 419 ILE   A N   1 
ATOM   906  C  CA  . ILE   A 1 123 ? -37.616 -3.715  24.995 1.00 58.49  ? 419 ILE   A CA  1 
ATOM   907  C  C   . ILE   A 1 123 ? -37.852 -3.584  23.480 1.00 66.69  ? 419 ILE   A C   1 
ATOM   908  O  O   . ILE   A 1 123 ? -38.968 -3.793  22.980 1.00 61.02  ? 419 ILE   A O   1 
ATOM   909  C  CB  . ILE   A 1 123 ? -38.101 -2.474  25.777 1.00 59.65  ? 419 ILE   A CB  1 
ATOM   910  C  CG1 . ILE   A 1 123 ? -39.618 -2.323  25.710 1.00 65.50  ? 419 ILE   A CG1 1 
ATOM   911  C  CG2 . ILE   A 1 123 ? -37.363 -1.198  25.341 1.00 54.42  ? 419 ILE   A CG2 1 
ATOM   912  C  CD1 . ILE   A 1 123 ? -40.113 -0.994  26.240 1.00 70.95  ? 419 ILE   A CD1 1 
ATOM   913  N  N   . GLN   A 1 124 ? -36.774 -3.302  22.744 1.00 69.81  ? 420 GLN   A N   1 
ATOM   914  C  CA  . GLN   A 1 124 ? -36.786 -3.044  21.312 1.00 73.56  ? 420 GLN   A CA  1 
ATOM   915  C  C   . GLN   A 1 124 ? -36.427 -4.270  20.472 1.00 71.06  ? 420 GLN   A C   1 
ATOM   916  O  O   . GLN   A 1 124 ? -36.295 -4.151  19.245 1.00 65.12  ? 420 GLN   A O   1 
ATOM   917  C  CB  . GLN   A 1 124 ? -35.814 -1.903  21.000 1.00 79.64  ? 420 GLN   A CB  1 
ATOM   918  C  CG  . GLN   A 1 124 ? -36.368 -0.514  21.238 1.00 92.67  ? 420 GLN   A CG  1 
ATOM   919  C  CD  . GLN   A 1 124 ? -37.141 0.015   20.039 1.00 106.43 ? 420 GLN   A CD  1 
ATOM   920  O  OE1 . GLN   A 1 124 ? -37.659 -0.752  19.227 1.00 107.86 ? 420 GLN   A OE1 1 
ATOM   921  N  NE2 . GLN   A 1 124 ? -37.212 1.335   19.919 1.00 113.95 ? 420 GLN   A NE2 1 
ATOM   922  N  N   . TRP   A 1 125 ? -36.277 -5.441  21.097 1.00 64.17  ? 421 TRP   A N   1 
ATOM   923  C  CA  . TRP   A 1 125 ? -35.618 -6.561  20.435 1.00 62.11  ? 421 TRP   A CA  1 
ATOM   924  C  C   . TRP   A 1 125 ? -36.329 -6.973  19.153 1.00 65.49  ? 421 TRP   A C   1 
ATOM   925  O  O   . TRP   A 1 125 ? -35.670 -7.380  18.193 1.00 65.42  ? 421 TRP   A O   1 
ATOM   926  C  CB  . TRP   A 1 125 ? -35.528 -7.754  21.374 1.00 55.69  ? 421 TRP   A CB  1 
ATOM   927  C  CG  . TRP   A 1 125 ? -36.858 -8.318  21.643 1.00 63.23  ? 421 TRP   A CG  1 
ATOM   928  C  CD1 . TRP   A 1 125 ? -37.726 -7.935  22.628 1.00 67.03  ? 421 TRP   A CD1 1 
ATOM   929  C  CD2 . TRP   A 1 125 ? -37.515 -9.345  20.902 1.00 64.02  ? 421 TRP   A CD2 1 
ATOM   930  N  NE1 . TRP   A 1 125 ? -38.874 -8.677  22.554 1.00 75.48  ? 421 TRP   A NE1 1 
ATOM   931  C  CE2 . TRP   A 1 125 ? -38.774 -9.547  21.496 1.00 72.63  ? 421 TRP   A CE2 1 
ATOM   932  C  CE3 . TRP   A 1 125 ? -37.154 -10.126 19.807 1.00 59.84  ? 421 TRP   A CE3 1 
ATOM   933  C  CZ2 . TRP   A 1 125 ? -39.672 -10.496 21.029 1.00 69.16  ? 421 TRP   A CZ2 1 
ATOM   934  C  CZ3 . TRP   A 1 125 ? -38.050 -11.066 19.340 1.00 60.87  ? 421 TRP   A CZ3 1 
ATOM   935  C  CH2 . TRP   A 1 125 ? -39.292 -11.240 19.947 1.00 70.14  ? 421 TRP   A CH2 1 
ATOM   936  N  N   . SER   A 1 126 ? -37.662 -6.879  19.109 1.00 71.51  ? 422 SER   A N   1 
ATOM   937  C  CA  . SER   A 1 126 ? -38.376 -7.295  17.901 1.00 79.72  ? 422 SER   A CA  1 
ATOM   938  C  C   . SER   A 1 126 ? -38.214 -6.298  16.756 1.00 82.40  ? 422 SER   A C   1 
ATOM   939  O  O   . SER   A 1 126 ? -38.409 -6.666  15.596 1.00 88.40  ? 422 SER   A O   1 
ATOM   940  C  CB  . SER   A 1 126 ? -39.862 -7.508  18.201 1.00 83.10  ? 422 SER   A CB  1 
ATOM   941  O  OG  . SER   A 1 126 ? -40.589 -6.293  18.135 1.00 84.50  ? 422 SER   A OG  1 
ATOM   942  N  N   . LYS   A 1 127 ? -37.885 -5.038  17.049 1.00 78.32  ? 423 LYS   A N   1 
ATOM   943  C  CA  . LYS   A 1 127 ? -37.620 -4.039  16.007 1.00 71.59  ? 423 LYS   A CA  1 
ATOM   944  C  C   . LYS   A 1 127 ? -36.125 -4.051  15.701 1.00 69.72  ? 423 LYS   A C   1 
ATOM   945  O  O   . LYS   A 1 127 ? -35.350 -3.209  16.162 1.00 71.33  ? 423 LYS   A O   1 
ATOM   946  C  CB  . LYS   A 1 127 ? -38.089 -2.655  16.444 1.00 73.91  ? 423 LYS   A CB  1 
ATOM   947  C  CG  . LYS   A 1 127 ? -39.400 -2.185  15.817 1.00 88.20  ? 423 LYS   A CG  1 
ATOM   948  C  CD  . LYS   A 1 127 ? -39.402 -0.667  15.551 1.00 92.59  ? 423 LYS   A CD  1 
ATOM   949  C  CE  . LYS   A 1 127 ? -40.544 -0.256  14.615 1.00 101.28 ? 423 LYS   A CE  1 
ATOM   950  N  NZ  . LYS   A 1 127 ? -40.339 -0.725  13.193 1.00 101.61 ? 423 LYS   A NZ  1 
ATOM   951  N  N   . LEU   A 1 128 ? -35.712 -5.042  14.917 1.00 65.36  ? 424 LEU   A N   1 
ATOM   952  C  CA  . LEU   A 1 128 ? -34.308 -5.203  14.565 1.00 61.91  ? 424 LEU   A CA  1 
ATOM   953  C  C   . LEU   A 1 128 ? -34.211 -5.483  13.073 1.00 63.56  ? 424 LEU   A C   1 
ATOM   954  O  O   . LEU   A 1 128 ? -34.902 -6.367  12.554 1.00 70.49  ? 424 LEU   A O   1 
ATOM   955  C  CB  . LEU   A 1 128 ? -33.644 -6.333  15.378 1.00 46.01  ? 424 LEU   A CB  1 
ATOM   956  C  CG  . LEU   A 1 128 ? -32.183 -6.720  15.074 1.00 48.56  ? 424 LEU   A CG  1 
ATOM   957  C  CD1 . LEU   A 1 128 ? -31.191 -5.713  15.600 1.00 43.29  ? 424 LEU   A CD1 1 
ATOM   958  C  CD2 . LEU   A 1 128 ? -31.819 -8.121  15.567 1.00 52.26  ? 424 LEU   A CD2 1 
ATOM   959  N  N   . GLN   A 1 129 ? -33.368 -4.732  12.388 1.00 66.48  ? 425 GLN   A N   1 
ATOM   960  C  CA  . GLN   A 1 129 ? -33.224 -4.858  10.940 1.00 68.44  ? 425 GLN   A CA  1 
ATOM   961  C  C   . GLN   A 1 129 ? -32.050 -5.780  10.666 1.00 64.37  ? 425 GLN   A C   1 
ATOM   962  O  O   . GLN   A 1 129 ? -30.899 -5.437  10.951 1.00 58.20  ? 425 GLN   A O   1 
ATOM   963  C  CB  . GLN   A 1 129 ? -33.028 -3.493  10.286 1.00 72.97  ? 425 GLN   A CB  1 
ATOM   964  C  CG  . GLN   A 1 129 ? -32.917 -3.531  8.778  1.00 72.24  ? 425 GLN   A CG  1 
ATOM   965  C  CD  . GLN   A 1 129 ? -34.050 -4.314  8.136  1.00 73.62  ? 425 GLN   A CD  1 
ATOM   966  O  OE1 . GLN   A 1 129 ? -35.213 -4.177  8.524  1.00 77.22  ? 425 GLN   A OE1 1 
ATOM   967  N  NE2 . GLN   A 1 129 ? -33.710 -5.159  7.168  1.00 73.30  ? 425 GLN   A NE2 1 
ATOM   968  N  N   . VAL   A 1 130 ? -32.339 -6.952  10.129 1.00 65.93  ? 426 VAL   A N   1 
ATOM   969  C  CA  . VAL   A 1 130 ? -31.311 -7.953  9.893  1.00 63.57  ? 426 VAL   A CA  1 
ATOM   970  C  C   . VAL   A 1 130 ? -30.803 -7.819  8.458  1.00 63.68  ? 426 VAL   A C   1 
ATOM   971  O  O   . VAL   A 1 130 ? -31.582 -7.853  7.500  1.00 63.17  ? 426 VAL   A O   1 
ATOM   972  C  CB  . VAL   A 1 130 ? -31.847 -9.363  10.183 1.00 60.12  ? 426 VAL   A CB  1 
ATOM   973  C  CG1 . VAL   A 1 130 ? -30.721 -10.403 10.066 1.00 50.09  ? 426 VAL   A CG1 1 
ATOM   974  C  CG2 . VAL   A 1 130 ? -32.547 -9.391  11.559 1.00 55.00  ? 426 VAL   A CG2 1 
ATOM   975  N  N   . PHE   A 1 131 ? -29.499 -7.636  8.309  1.00 61.81  ? 427 PHE   A N   1 
ATOM   976  C  CA  . PHE   A 1 131 ? -28.871 -7.548  6.996  1.00 62.24  ? 427 PHE   A CA  1 
ATOM   977  C  C   . PHE   A 1 131 ? -28.126 -8.849  6.732  1.00 60.43  ? 427 PHE   A C   1 
ATOM   978  O  O   . PHE   A 1 131 ? -27.141 -9.163  7.412  1.00 57.73  ? 427 PHE   A O   1 
ATOM   979  C  CB  . PHE   A 1 131 ? -27.924 -6.353  6.903  1.00 52.49  ? 427 PHE   A CB  1 
ATOM   980  C  CG  . PHE   A 1 131 ? -28.623 -5.042  6.776  1.00 54.12  ? 427 PHE   A CG  1 
ATOM   981  C  CD1 . PHE   A 1 131 ? -29.391 -4.756  5.666  1.00 55.42  ? 427 PHE   A CD1 1 
ATOM   982  C  CD2 . PHE   A 1 131 ? -28.494 -4.067  7.753  1.00 52.93  ? 427 PHE   A CD2 1 
ATOM   983  C  CE1 . PHE   A 1 131 ? -30.029 -3.532  5.536  1.00 55.10  ? 427 PHE   A CE1 1 
ATOM   984  C  CE2 . PHE   A 1 131 ? -29.135 -2.843  7.633  1.00 54.64  ? 427 PHE   A CE2 1 
ATOM   985  C  CZ  . PHE   A 1 131 ? -29.898 -2.576  6.530  1.00 59.82  ? 427 PHE   A CZ  1 
ATOM   986  N  N   . ASP   A 1 132 ? -28.599 -9.601  5.753  1.00 63.46  ? 428 ASP   A N   1 
ATOM   987  C  CA  . ASP   A 1 132 ? -28.003 -10.886 5.417  1.00 53.68  ? 428 ASP   A CA  1 
ATOM   988  C  C   . ASP   A 1 132 ? -26.803 -10.624 4.527  1.00 58.16  ? 428 ASP   A C   1 
ATOM   989  O  O   . ASP   A 1 132 ? -26.952 -10.286 3.356  1.00 64.03  ? 428 ASP   A O   1 
ATOM   990  C  CB  . ASP   A 1 132 ? -29.029 -11.778 4.730  1.00 47.46  ? 428 ASP   A CB  1 
ATOM   991  C  CG  . ASP   A 1 132 ? -28.513 -13.172 4.510  1.00 51.48  ? 428 ASP   A CG  1 
ATOM   992  O  OD1 . ASP   A 1 132 ? -29.337 -14.065 4.261  1.00 58.44  ? 428 ASP   A OD1 1 
ATOM   993  O  OD2 . ASP   A 1 132 ? -27.282 -13.384 4.599  1.00 52.27  ? 428 ASP   A OD2 1 
ATOM   994  N  N   . ALA   A 1 133 ? -25.604 -10.758 5.075  1.00 58.96  ? 429 ALA   A N   1 
ATOM   995  C  CA  . ALA   A 1 133 ? -24.392 -10.641 4.276  1.00 54.80  ? 429 ALA   A CA  1 
ATOM   996  C  C   . ALA   A 1 133 ? -23.716 -11.990 4.117  1.00 55.98  ? 429 ALA   A C   1 
ATOM   997  O  O   . ALA   A 1 133 ? -22.503 -12.066 3.929  1.00 61.57  ? 429 ALA   A O   1 
ATOM   998  C  CB  . ALA   A 1 133 ? -23.418 -9.631  4.881  1.00 55.77  ? 429 ALA   A CB  1 
ATOM   999  N  N   . ARG   A 1 134 ? -24.497 -13.065 4.190  1.00 50.11  ? 430 ARG   A N   1 
ATOM   1000 C  CA  . ARG   A 1 134 ? -23.910 -14.383 4.026  1.00 52.53  ? 430 ARG   A CA  1 
ATOM   1001 C  C   . ARG   A 1 134 ? -23.461 -14.687 2.595  1.00 57.76  ? 430 ARG   A C   1 
ATOM   1002 O  O   . ARG   A 1 134 ? -22.789 -15.706 2.409  1.00 59.12  ? 430 ARG   A O   1 
ATOM   1003 C  CB  . ARG   A 1 134 ? -24.885 -15.448 4.519  1.00 51.02  ? 430 ARG   A CB  1 
ATOM   1004 C  CG  . ARG   A 1 134 ? -25.033 -15.435 6.068  1.00 53.36  ? 430 ARG   A CG  1 
ATOM   1005 C  CD  . ARG   A 1 134 ? -26.113 -16.412 6.503  1.00 53.21  ? 430 ARG   A CD  1 
ATOM   1006 N  NE  . ARG   A 1 134 ? -27.381 -16.101 5.857  1.00 59.93  ? 430 ARG   A NE  1 
ATOM   1007 C  CZ  . ARG   A 1 134 ? -28.390 -16.951 5.736  1.00 62.22  ? 430 ARG   A CZ  1 
ATOM   1008 N  NH1 . ARG   A 1 134 ? -28.273 -18.182 6.218  1.00 51.39  ? 430 ARG   A NH1 1 
ATOM   1009 N  NH2 . ARG   A 1 134 ? -29.504 -16.575 5.108  1.00 69.25  ? 430 ARG   A NH2 1 
ATOM   1010 N  N   . ASP   A 1 135 ? -23.792 -13.847 1.592  1.00 54.99  ? 431 ASP   A N   1 
ATOM   1011 C  CA  . ASP   A 1 135 ? -23.222 -13.991 0.246  1.00 63.49  ? 431 ASP   A CA  1 
ATOM   1012 C  C   . ASP   A 1 135 ? -21.872 -13.291 0.104  1.00 64.41  ? 431 ASP   A C   1 
ATOM   1013 O  O   . ASP   A 1 135 ? -21.295 -13.293 -0.990 1.00 66.47  ? 431 ASP   A O   1 
ATOM   1014 C  CB  . ASP   A 1 135 ? -24.202 -13.477 -0.839 1.00 61.31  ? 431 ASP   A CB  1 
ATOM   1015 C  CG  . ASP   A 1 135 ? -24.521 -11.967 -0.716 1.00 66.95  ? 431 ASP   A CG  1 
ATOM   1016 O  OD1 . ASP   A 1 135 ? -25.111 -11.384 -1.659 1.00 64.43  ? 431 ASP   A OD1 1 
ATOM   1017 O  OD2 . ASP   A 1 135 ? -24.195 -11.347 0.318  1.00 61.43  ? 431 ASP   A OD2 1 
ATOM   1018 N  N   . CYS   A 1 136 ? -21.346 -12.725 1.191  1.00 59.12  ? 432 CYS   A N   1 
ATOM   1019 C  CA  . CYS   A 1 136 ? -20.097 -11.976 1.156  1.00 61.40  ? 432 CYS   A CA  1 
ATOM   1020 C  C   . CYS   A 1 136 ? -18.906 -12.919 1.020  1.00 67.06  ? 432 CYS   A C   1 
ATOM   1021 O  O   . CYS   A 1 136 ? -18.918 -14.046 1.524  1.00 70.30  ? 432 CYS   A O   1 
ATOM   1022 C  CB  . CYS   A 1 136 ? -19.962 -11.104 2.411  1.00 59.85  ? 432 CYS   A CB  1 
ATOM   1023 S  SG  . CYS   A 1 136 ? -18.646 -9.858  2.338  1.00 63.19  ? 432 CYS   A SG  1 
ATOM   1024 N  N   . THR   A 1 137 ? -17.882 -12.460 0.290  1.00 65.34  ? 433 THR   A N   1 
ATOM   1025 C  CA  . THR   A 1 137 ? -16.695 -13.280 0.043  1.00 60.37  ? 433 THR   A CA  1 
ATOM   1026 C  C   . THR   A 1 137 ? -15.368 -12.559 0.265  1.00 66.98  ? 433 THR   A C   1 
ATOM   1027 O  O   . THR   A 1 137 ? -14.338 -13.238 0.391  1.00 65.60  ? 433 THR   A O   1 
ATOM   1028 C  CB  . THR   A 1 137 ? -16.708 -13.843 -1.391 1.00 69.39  ? 433 THR   A CB  1 
ATOM   1029 O  OG1 . THR   A 1 137 ? -16.529 -12.783 -2.338 1.00 64.98  ? 433 THR   A OG1 1 
ATOM   1030 C  CG2 . THR   A 1 137 ? -18.017 -14.547 -1.684 1.00 69.36  ? 433 THR   A CG2 1 
ATOM   1031 N  N   . THR   A 1 138 ? -15.344 -11.225 0.341  1.00 70.50  ? 434 THR   A N   1 
ATOM   1032 C  CA  . THR   A 1 138 ? -14.108 -10.451 0.371  1.00 68.63  ? 434 THR   A CA  1 
ATOM   1033 C  C   . THR   A 1 138 ? -14.220 -9.360  1.429  1.00 65.11  ? 434 THR   A C   1 
ATOM   1034 O  O   . THR   A 1 138 ? -15.316 -8.937  1.809  1.00 63.29  ? 434 THR   A O   1 
ATOM   1035 C  CB  . THR   A 1 138 ? -13.799 -9.817  -1.004 1.00 69.07  ? 434 THR   A CB  1 
ATOM   1036 O  OG1 . THR   A 1 138 ? -14.993 -9.229  -1.546 1.00 73.02  ? 434 THR   A OG1 1 
ATOM   1037 C  CG2 . THR   A 1 138 ? -13.278 -10.858 -1.978 1.00 69.74  ? 434 THR   A CG2 1 
ATOM   1038 N  N   . ALA   A 1 139 ? -13.060 -8.906  1.907  1.00 65.86  ? 435 ALA   A N   1 
ATOM   1039 C  CA  . ALA   A 1 139 ? -13.053 -7.789  2.842  1.00 70.99  ? 435 ALA   A CA  1 
ATOM   1040 C  C   . ALA   A 1 139 ? -13.672 -6.546  2.225  1.00 70.31  ? 435 ALA   A C   1 
ATOM   1041 O  O   . ALA   A 1 139 ? -14.328 -5.769  2.929  1.00 72.76  ? 435 ALA   A O   1 
ATOM   1042 C  CB  . ALA   A 1 139 ? -11.631 -7.496  3.303  1.00 77.33  ? 435 ALA   A CB  1 
ATOM   1043 N  N   . HIS   A 1 140 ? -13.490 -6.344  0.914  1.00 70.87  ? 436 HIS   A N   1 
ATOM   1044 C  CA  . HIS   A 1 140 ? -14.145 -5.219  0.250  1.00 61.50  ? 436 HIS   A CA  1 
ATOM   1045 C  C   . HIS   A 1 140 ? -15.656 -5.350  0.316  1.00 55.17  ? 436 HIS   A C   1 
ATOM   1046 O  O   . HIS   A 1 140 ? -16.368 -4.354  0.464  1.00 54.62  ? 436 HIS   A O   1 
ATOM   1047 C  CB  . HIS   A 1 140 ? -13.699 -5.111  -1.208 1.00 72.29  ? 436 HIS   A CB  1 
ATOM   1048 C  CG  . HIS   A 1 140 ? -12.421 -4.359  -1.405 1.00 76.37  ? 436 HIS   A CG  1 
ATOM   1049 N  ND1 . HIS   A 1 140 ? -11.188 -4.901  -1.111 1.00 78.81  ? 436 HIS   A ND1 1 
ATOM   1050 C  CD2 . HIS   A 1 140 ? -12.185 -3.113  -1.881 1.00 76.13  ? 436 HIS   A CD2 1 
ATOM   1051 C  CE1 . HIS   A 1 140 ? -10.246 -4.021  -1.401 1.00 82.68  ? 436 HIS   A CE1 1 
ATOM   1052 N  NE2 . HIS   A 1 140 ? -10.824 -2.928  -1.869 1.00 80.64  ? 436 HIS   A NE2 1 
ATOM   1053 N  N   . GLY   A 1 141 ? -16.169 -6.568  0.180  1.00 54.74  ? 437 GLY   A N   1 
ATOM   1054 C  CA  . GLY   A 1 141 ? -17.595 -6.761  0.355  1.00 60.10  ? 437 GLY   A CA  1 
ATOM   1055 C  C   . GLY   A 1 141 ? -18.023 -6.490  1.779  1.00 63.43  ? 437 GLY   A C   1 
ATOM   1056 O  O   . GLY   A 1 141 ? -19.054 -5.857  2.021  1.00 66.18  ? 437 GLY   A O   1 
ATOM   1057 N  N   . MET   A 1 142 ? -17.220 -6.943  2.739  1.00 65.98  ? 438 MET   A N   1 
ATOM   1058 C  CA  . MET   A 1 142 ? -17.479 -6.633  4.139  1.00 56.24  ? 438 MET   A CA  1 
ATOM   1059 C  C   . MET   A 1 142 ? -17.596 -5.130  4.349  1.00 53.33  ? 438 MET   A C   1 
ATOM   1060 O  O   . MET   A 1 142 ? -18.643 -4.628  4.766  1.00 54.01  ? 438 MET   A O   1 
ATOM   1061 C  CB  . MET   A 1 142 ? -16.372 -7.225  5.001  1.00 54.95  ? 438 MET   A CB  1 
ATOM   1062 C  CG  . MET   A 1 142 ? -16.522 -8.701  5.192  1.00 51.81  ? 438 MET   A CG  1 
ATOM   1063 S  SD  . MET   A 1 142 ? -15.195 -9.369  6.175  1.00 64.25  ? 438 MET   A SD  1 
ATOM   1064 C  CE  . MET   A 1 142 ? -15.857 -9.092  7.825  1.00 67.86  ? 438 MET   A CE  1 
ATOM   1065 N  N   . PHE   A 1 143 ? -16.555 -4.390  3.973  1.00 55.35  ? 439 PHE   A N   1 
ATOM   1066 C  CA  . PHE   A 1 143 ? -16.591 -2.936  4.053  1.00 61.11  ? 439 PHE   A CA  1 
ATOM   1067 C  C   . PHE   A 1 143 ? -17.887 -2.379  3.492  1.00 65.31  ? 439 PHE   A C   1 
ATOM   1068 O  O   . PHE   A 1 143 ? -18.558 -1.559  4.128  1.00 63.82  ? 439 PHE   A O   1 
ATOM   1069 C  CB  . PHE   A 1 143 ? -15.392 -2.356  3.314  1.00 68.18  ? 439 PHE   A CB  1 
ATOM   1070 C  CG  . PHE   A 1 143 ? -15.440 -0.871  3.170  1.00 73.51  ? 439 PHE   A CG  1 
ATOM   1071 C  CD1 . PHE   A 1 143 ? -15.557 -0.285  1.915  1.00 77.78  ? 439 PHE   A CD1 1 
ATOM   1072 C  CD2 . PHE   A 1 143 ? -15.400 -0.063  4.285  1.00 63.68  ? 439 PHE   A CD2 1 
ATOM   1073 C  CE1 . PHE   A 1 143 ? -15.607 1.086   1.786  1.00 80.05  ? 439 PHE   A CE1 1 
ATOM   1074 C  CE2 . PHE   A 1 143 ? -15.437 1.301   4.162  1.00 72.22  ? 439 PHE   A CE2 1 
ATOM   1075 C  CZ  . PHE   A 1 143 ? -15.544 1.883   2.916  1.00 78.50  ? 439 PHE   A CZ  1 
ATOM   1076 N  N   . ASN   A 1 144 ? -18.276 -2.866  2.309  1.00 63.52  ? 440 ASN   A N   1 
ATOM   1077 C  CA  . ASN   A 1 144 ? -19.477 -2.369  1.659  1.00 59.01  ? 440 ASN   A CA  1 
ATOM   1078 C  C   . ASN   A 1 144 ? -20.747 -2.738  2.420  1.00 59.17  ? 440 ASN   A C   1 
ATOM   1079 O  O   . ASN   A 1 144 ? -21.683 -1.933  2.488  1.00 61.24  ? 440 ASN   A O   1 
ATOM   1080 C  CB  . ASN   A 1 144 ? -19.540 -2.898  0.228  1.00 62.63  ? 440 ASN   A CB  1 
ATOM   1081 C  CG  . ASN   A 1 144 ? -20.671 -2.287  -0.544 1.00 62.49  ? 440 ASN   A CG  1 
ATOM   1082 O  OD1 . ASN   A 1 144 ? -20.719 -1.071  -0.717 1.00 57.65  ? 440 ASN   A OD1 1 
ATOM   1083 N  ND2 . ASN   A 1 144 ? -21.606 -3.121  -0.987 1.00 56.33  ? 440 ASN   A ND2 1 
ATOM   1084 N  N   . TYR   A 1 145 ? -20.824 -3.954  2.974  1.00 57.95  ? 441 TYR   A N   1 
ATOM   1085 C  CA  . TYR   A 1 145 ? -21.979 -4.289  3.807  1.00 65.02  ? 441 TYR   A CA  1 
ATOM   1086 C  C   . TYR   A 1 145 ? -22.019 -3.435  5.075  1.00 62.54  ? 441 TYR   A C   1 
ATOM   1087 O  O   . TYR   A 1 145 ? -23.089 -2.948  5.466  1.00 60.70  ? 441 TYR   A O   1 
ATOM   1088 C  CB  . TYR   A 1 145 ? -21.971 -5.771  4.168  1.00 63.50  ? 441 TYR   A CB  1 
ATOM   1089 C  CG  . TYR   A 1 145 ? -22.746 -6.649  3.219  1.00 57.77  ? 441 TYR   A CG  1 
ATOM   1090 C  CD1 . TYR   A 1 145 ? -22.097 -7.582  2.432  1.00 57.31  ? 441 TYR   A CD1 1 
ATOM   1091 C  CD2 . TYR   A 1 145 ? -24.129 -6.541  3.103  1.00 50.21  ? 441 TYR   A CD2 1 
ATOM   1092 C  CE1 . TYR   A 1 145 ? -22.790 -8.403  1.563  1.00 50.93  ? 441 TYR   A CE1 1 
ATOM   1093 C  CE2 . TYR   A 1 145 ? -24.837 -7.361  2.223  1.00 50.65  ? 441 TYR   A CE2 1 
ATOM   1094 C  CZ  . TYR   A 1 145 ? -24.155 -8.288  1.452  1.00 54.53  ? 441 TYR   A CZ  1 
ATOM   1095 O  OH  . TYR   A 1 145 ? -24.829 -9.106  0.549  1.00 53.11  ? 441 TYR   A OH  1 
ATOM   1096 N  N   . ILE   A 1 146 ? -20.868 -3.250  5.728  1.00 56.93  ? 442 ILE   A N   1 
ATOM   1097 C  CA  . ILE   A 1 146 ? -20.813 -2.459  6.961  1.00 61.45  ? 442 ILE   A CA  1 
ATOM   1098 C  C   . ILE   A 1 146 ? -21.215 -1.013  6.691  1.00 65.94  ? 442 ILE   A C   1 
ATOM   1099 O  O   . ILE   A 1 146 ? -21.940 -0.393  7.487  1.00 57.76  ? 442 ILE   A O   1 
ATOM   1100 C  CB  . ILE   A 1 146 ? -19.406 -2.561  7.583  1.00 55.48  ? 442 ILE   A CB  1 
ATOM   1101 C  CG1 . ILE   A 1 146 ? -19.134 -4.002  8.022  1.00 49.58  ? 442 ILE   A CG1 1 
ATOM   1102 C  CG2 . ILE   A 1 146 ? -19.210 -1.564  8.729  1.00 44.24  ? 442 ILE   A CG2 1 
ATOM   1103 C  CD1 . ILE   A 1 146 ? -17.820 -4.192  8.788  1.00 49.89  ? 442 ILE   A CD1 1 
ATOM   1104 N  N   . CYS   A 1 147 ? -20.790 -0.467  5.543  1.00 67.13  ? 443 CYS   A N   1 
ATOM   1105 C  CA  . CYS   A 1 147 ? -21.126 0.914   5.209  1.00 62.26  ? 443 CYS   A CA  1 
ATOM   1106 C  C   . CYS   A 1 147 ? -22.623 1.088   5.064  1.00 53.99  ? 443 CYS   A C   1 
ATOM   1107 O  O   . CYS   A 1 147 ? -23.186 2.094   5.505  1.00 53.44  ? 443 CYS   A O   1 
ATOM   1108 C  CB  . CYS   A 1 147 ? -20.436 1.342   3.908  1.00 66.34  ? 443 CYS   A CB  1 
ATOM   1109 S  SG  . CYS   A 1 147 ? -18.730 1.818   4.075  1.00 66.31  ? 443 CYS   A SG  1 
ATOM   1110 N  N   . ASN   A 1 148 ? -23.280 0.137   4.404  1.00 52.20  ? 444 ASN   A N   1 
ATOM   1111 C  CA  . ASN   A 1 148 ? -24.728 0.217   4.283  1.00 56.44  ? 444 ASN   A CA  1 
ATOM   1112 C  C   . ASN   A 1 148 ? -25.376 0.056   5.656  1.00 57.37  ? 444 ASN   A C   1 
ATOM   1113 O  O   . ASN   A 1 148 ? -26.362 0.731   5.978  1.00 59.14  ? 444 ASN   A O   1 
ATOM   1114 C  CB  . ASN   A 1 148 ? -25.250 -0.851  3.318  1.00 61.25  ? 444 ASN   A CB  1 
ATOM   1115 C  CG  . ASN   A 1 148 ? -24.761 -0.664  1.872  1.00 64.10  ? 444 ASN   A CG  1 
ATOM   1116 O  OD1 . ASN   A 1 148 ? -24.362 0.432   1.464  1.00 64.51  ? 444 ASN   A OD1 1 
ATOM   1117 N  ND2 . ASN   A 1 148 ? -24.820 -1.745  1.092  1.00 55.96  ? 444 ASN   A ND2 1 
ATOM   1118 N  N   . HIS   A 1 149 ? -24.821 -0.830  6.480  1.00 57.51  ? 445 HIS   A N   1 
ATOM   1119 C  CA  . HIS   A 1 149 ? -25.278 -0.942  7.864  1.00 56.37  ? 445 HIS   A CA  1 
ATOM   1120 C  C   . HIS   A 1 149 ? -25.173 0.410   8.576  1.00 51.98  ? 445 HIS   A C   1 
ATOM   1121 O  O   . HIS   A 1 149 ? -26.173 0.944   9.071  1.00 53.68  ? 445 HIS   A O   1 
ATOM   1122 C  CB  . HIS   A 1 149 ? -24.477 -2.035  8.596  1.00 56.35  ? 445 HIS   A CB  1 
ATOM   1123 C  CG  . HIS   A 1 149 ? -24.873 -2.227  10.038 1.00 58.32  ? 445 HIS   A CG  1 
ATOM   1124 N  ND1 . HIS   A 1 149 ? -25.090 -3.471  10.597 1.00 51.45  ? 445 HIS   A ND1 1 
ATOM   1125 C  CD2 . HIS   A 1 149 ? -25.091 -1.329  11.030 1.00 53.90  ? 445 HIS   A CD2 1 
ATOM   1126 C  CE1 . HIS   A 1 149 ? -25.436 -3.332  11.865 1.00 53.59  ? 445 HIS   A CE1 1 
ATOM   1127 N  NE2 . HIS   A 1 149 ? -25.437 -2.043  12.154 1.00 57.42  ? 445 HIS   A NE2 1 
ATOM   1128 N  N   . VAL   A 1 150 ? -23.981 1.007   8.583  1.00 50.02  ? 446 VAL   A N   1 
ATOM   1129 C  CA  . VAL   A 1 150 ? -23.802 2.272   9.300  1.00 44.68  ? 446 VAL   A CA  1 
ATOM   1130 C  C   . VAL   A 1 150 ? -24.801 3.301   8.800  1.00 59.17  ? 446 VAL   A C   1 
ATOM   1131 O  O   . VAL   A 1 150 ? -25.600 3.838   9.566  1.00 65.04  ? 446 VAL   A O   1 
ATOM   1132 C  CB  . VAL   A 1 150 ? -22.357 2.779   9.169  1.00 58.43  ? 446 VAL   A CB  1 
ATOM   1133 C  CG1 . VAL   A 1 150 ? -22.268 4.236   9.649  1.00 59.06  ? 446 VAL   A CG1 1 
ATOM   1134 C  CG2 . VAL   A 1 150 ? -21.420 1.892   9.948  1.00 60.98  ? 446 VAL   A CG2 1 
ATOM   1135 N  N   . LYS   A 1 151 ? -24.828 3.528   7.490  1.00 52.36  ? 447 LYS   A N   1 
ATOM   1136 C  CA  . LYS   A 1 151 ? -25.747 4.523   6.947  1.00 62.11  ? 447 LYS   A CA  1 
ATOM   1137 C  C   . LYS   A 1 151 ? -27.193 4.198   7.301  1.00 64.74  ? 447 LYS   A C   1 
ATOM   1138 O  O   . LYS   A 1 151 ? -27.942 5.079   7.746  1.00 64.61  ? 447 LYS   A O   1 
ATOM   1139 C  CB  . LYS   A 1 151 ? -25.579 4.632   5.428  1.00 52.74  ? 447 LYS   A CB  1 
ATOM   1140 C  CG  . LYS   A 1 151 ? -26.425 5.751   4.817  1.00 57.19  ? 447 LYS   A CG  1 
ATOM   1141 C  CD  . LYS   A 1 151 ? -26.023 5.949   3.377  1.00 63.95  ? 447 LYS   A CD  1 
ATOM   1142 C  CE  . LYS   A 1 151 ? -26.381 7.329   2.827  1.00 72.06  ? 447 LYS   A CE  1 
ATOM   1143 N  NZ  . LYS   A 1 151 ? -26.063 7.346   1.360  1.00 76.05  ? 447 LYS   A NZ  1 
ATOM   1144 N  N   . TYR   A 1 152 ? -27.605 2.935   7.127  1.00 58.94  ? 448 TYR   A N   1 
ATOM   1145 C  CA  . TYR   A 1 152 ? -28.987 2.587   7.444  1.00 62.94  ? 448 TYR   A CA  1 
ATOM   1146 C  C   . TYR   A 1 152 ? -29.289 2.821   8.922  1.00 64.26  ? 448 TYR   A C   1 
ATOM   1147 O  O   . TYR   A 1 152 ? -30.234 3.542   9.266  1.00 71.37  ? 448 TYR   A O   1 
ATOM   1148 C  CB  . TYR   A 1 152 ? -29.308 1.138   7.082  1.00 62.27  ? 448 TYR   A CB  1 
ATOM   1149 C  CG  . TYR   A 1 152 ? -30.675 0.759   7.623  1.00 71.87  ? 448 TYR   A CG  1 
ATOM   1150 C  CD1 . TYR   A 1 152 ? -31.836 1.068   6.920  1.00 77.42  ? 448 TYR   A CD1 1 
ATOM   1151 C  CD2 . TYR   A 1 152 ? -30.809 0.136   8.862  1.00 69.14  ? 448 TYR   A CD2 1 
ATOM   1152 C  CE1 . TYR   A 1 152 ? -33.085 0.744   7.432  1.00 81.70  ? 448 TYR   A CE1 1 
ATOM   1153 C  CE2 . TYR   A 1 152 ? -32.043 -0.184  9.373  1.00 72.55  ? 448 TYR   A CE2 1 
ATOM   1154 C  CZ  . TYR   A 1 152 ? -33.175 0.118   8.663  1.00 78.79  ? 448 TYR   A CZ  1 
ATOM   1155 O  OH  . TYR   A 1 152 ? -34.398 -0.214  9.189  1.00 85.65  ? 448 TYR   A OH  1 
ATOM   1156 N  N   . ALA   A 1 153 ? -28.495 2.212   9.810  1.00 60.63  ? 449 ALA   A N   1 
ATOM   1157 C  CA  . ALA   A 1 153 ? -28.777 2.270   11.242 1.00 61.67  ? 449 ALA   A CA  1 
ATOM   1158 C  C   . ALA   A 1 153 ? -28.695 3.687   11.792 1.00 67.31  ? 449 ALA   A C   1 
ATOM   1159 O  O   . ALA   A 1 153 ? -29.289 3.974   12.838 1.00 79.85  ? 449 ALA   A O   1 
ATOM   1160 C  CB  . ALA   A 1 153 ? -27.814 1.341   12.003 1.00 56.46  ? 449 ALA   A CB  1 
ATOM   1161 N  N   . THR   A 1 154 ? -27.987 4.577   11.104 1.00 61.71  ? 450 THR   A N   1 
ATOM   1162 C  CA  . THR   A 1 154 ? -27.825 5.950   11.557 1.00 65.96  ? 450 THR   A CA  1 
ATOM   1163 C  C   . THR   A 1 154 ? -29.017 6.823   11.170 1.00 73.52  ? 450 THR   A C   1 
ATOM   1164 O  O   . THR   A 1 154 ? -29.428 7.680   11.956 1.00 80.84  ? 450 THR   A O   1 
ATOM   1165 C  CB  . THR   A 1 154 ? -26.527 6.519   10.990 1.00 66.52  ? 450 THR   A CB  1 
ATOM   1166 O  OG1 . THR   A 1 154 ? -25.448 5.654   11.356 1.00 56.40  ? 450 THR   A OG1 1 
ATOM   1167 C  CG2 . THR   A 1 154 ? -26.269 7.928   11.515 1.00 70.92  ? 450 THR   A CG2 1 
ATOM   1168 N  N   . ASN   A 1 155 ? -29.567 6.636   9.966  1.00 72.47  ? 451 ASN   A N   1 
ATOM   1169 C  CA  . ASN   A 1 155 ? -30.843 7.242   9.561  1.00 67.39  ? 451 ASN   A CA  1 
ATOM   1170 C  C   . ASN   A 1 155 ? -30.918 8.723   9.963  1.00 72.54  ? 451 ASN   A C   1 
ATOM   1171 O  O   . ASN   A 1 155 ? -31.882 9.190   10.571 1.00 73.45  ? 451 ASN   A O   1 
ATOM   1172 C  CB  . ASN   A 1 155 ? -32.019 6.440   10.142 1.00 70.02  ? 451 ASN   A CB  1 
ATOM   1173 C  CG  . ASN   A 1 155 ? -33.385 6.908   9.643  1.00 79.83  ? 451 ASN   A CG  1 
ATOM   1174 O  OD1 . ASN   A 1 155 ? -33.540 7.330   8.495  1.00 86.35  ? 451 ASN   A OD1 1 
ATOM   1175 N  ND2 . ASN   A 1 155 ? -34.387 6.822   10.513 1.00 82.23  ? 451 ASN   A ND2 1 
ATOM   1176 N  N   . LYS   A 1 156 ? -29.857 9.460   9.632  1.00 77.68  ? 452 LYS   A N   1 
ATOM   1177 C  CA  . LYS   A 1 156 ? -29.773 10.900  9.813  1.00 83.24  ? 452 LYS   A CA  1 
ATOM   1178 C  C   . LYS   A 1 156 ? -29.807 11.286  11.281 1.00 91.45  ? 452 LYS   A C   1 
ATOM   1179 O  O   . LYS   A 1 156 ? -30.096 12.437  11.607 1.00 107.64 ? 452 LYS   A O   1 
ATOM   1180 C  CB  . LYS   A 1 156 ? -30.885 11.650  9.058  1.00 87.39  ? 452 LYS   A CB  1 
ATOM   1181 C  CG  . LYS   A 1 156 ? -31.119 11.225  7.598  1.00 103.84 ? 452 LYS   A CG  1 
ATOM   1182 C  CD  . LYS   A 1 156 ? -31.869 12.300  6.785  1.00 115.14 ? 452 LYS   A CD  1 
ATOM   1183 C  CE  . LYS   A 1 156 ? -33.001 12.957  7.582  1.00 130.05 ? 452 LYS   A CE  1 
ATOM   1184 N  NZ  . LYS   A 1 156 ? -34.211 12.096  7.729  1.00 136.42 ? 452 LYS   A NZ  1 
ATOM   1185 N  N   . GLY   A 1 157 ? -29.524 10.336  12.175 1.00 87.24  ? 453 GLY   A N   1 
ATOM   1186 C  CA  . GLY   A 1 157 ? -29.599 10.548  13.598 1.00 79.92  ? 453 GLY   A CA  1 
ATOM   1187 C  C   . GLY   A 1 157 ? -30.802 9.907   14.258 1.00 81.05  ? 453 GLY   A C   1 
ATOM   1188 O  O   . GLY   A 1 157 ? -30.751 9.635   15.471 1.00 75.82  ? 453 GLY   A O   1 
ATOM   1189 N  N   . ASN   A 1 158 ? -31.893 9.675   13.511 1.00 81.89  ? 454 ASN   A N   1 
ATOM   1190 C  CA  . ASN   A 1 158 ? -33.020 8.889   14.020 1.00 80.37  ? 454 ASN   A CA  1 
ATOM   1191 C  C   . ASN   A 1 158 ? -32.617 7.421   13.949 1.00 76.00  ? 454 ASN   A C   1 
ATOM   1192 O  O   . ASN   A 1 158 ? -33.072 6.658   13.091 1.00 74.01  ? 454 ASN   A O   1 
ATOM   1193 C  CB  . ASN   A 1 158 ? -34.302 9.156   13.242 1.00 88.00  ? 454 ASN   A CB  1 
ATOM   1194 C  CG  . ASN   A 1 158 ? -35.479 8.318   13.753 1.00 93.53  ? 454 ASN   A CG  1 
ATOM   1195 O  OD1 . ASN   A 1 158 ? -35.455 7.798   14.882 1.00 94.75  ? 454 ASN   A OD1 1 
ATOM   1196 N  ND2 . ASN   A 1 158 ? -36.515 8.185   12.924 1.00 89.01  ? 454 ASN   A ND2 1 
ATOM   1197 N  N   . LEU   A 1 159 ? -31.757 7.025   14.895 1.00 66.77  ? 455 LEU   A N   1 
ATOM   1198 C  CA  . LEU   A 1 159 ? -31.025 5.771   14.783 1.00 66.40  ? 455 LEU   A CA  1 
ATOM   1199 C  C   . LEU   A 1 159 ? -31.976 4.579   14.730 1.00 63.62  ? 455 LEU   A C   1 
ATOM   1200 O  O   . LEU   A 1 159 ? -33.089 4.610   15.270 1.00 67.75  ? 455 LEU   A O   1 
ATOM   1201 C  CB  . LEU   A 1 159 ? -30.050 5.621   15.955 1.00 67.16  ? 455 LEU   A CB  1 
ATOM   1202 C  CG  . LEU   A 1 159 ? -28.600 6.086   15.760 1.00 67.68  ? 455 LEU   A CG  1 
ATOM   1203 C  CD1 . LEU   A 1 159 ? -28.507 7.422   15.035 1.00 72.04  ? 455 LEU   A CD1 1 
ATOM   1204 C  CD2 . LEU   A 1 159 ? -27.909 6.158   17.101 1.00 70.17  ? 455 LEU   A CD2 1 
ATOM   1205 N  N   . ARG   A 1 160 ? -31.517 3.516   14.076 1.00 52.15  ? 456 ARG   A N   1 
ATOM   1206 C  CA  . ARG   A 1 160 ? -32.296 2.301   13.914 1.00 51.67  ? 456 ARG   A CA  1 
ATOM   1207 C  C   . ARG   A 1 160 ? -31.453 1.090   14.260 1.00 52.35  ? 456 ARG   A C   1 
ATOM   1208 O  O   . ARG   A 1 160 ? -30.267 1.023   13.931 1.00 57.57  ? 456 ARG   A O   1 
ATOM   1209 C  CB  . ARG   A 1 160 ? -32.843 2.175   12.433 1.00 56.22  ? 456 ARG   A CB  1 
ATOM   1210 C  CG  . ARG   A 1 160 ? -33.819 3.265   12.101 1.00 63.70  ? 456 ARG   A CG  1 
ATOM   1211 C  CD  . ARG   A 1 160 ? -34.397 3.167   10.685 1.00 70.72  ? 456 ARG   A CD  1 
ATOM   1212 N  NE  . ARG   A 1 160 ? -33.444 3.536   9.647  1.00 68.85  ? 456 ARG   A NE  1 
ATOM   1213 C  CZ  . ARG   A 1 160 ? -33.794 3.813   8.389  1.00 74.42  ? 456 ARG   A CZ  1 
ATOM   1214 N  NH1 . ARG   A 1 160 ? -35.072 3.770   8.029  1.00 75.76  ? 456 ARG   A NH1 1 
ATOM   1215 N  NH2 . ARG   A 1 160 ? -32.872 4.153   7.497  1.00 63.75  ? 456 ARG   A NH2 1 
ATOM   1216 N  N   . SER   A 1 161 ? -32.070 0.144   14.954 1.00 62.83  ? 457 SER   A N   1 
ATOM   1217 C  CA  . SER   A 1 161 ? -31.370 -1.074  15.325 1.00 60.52  ? 457 SER   A CA  1 
ATOM   1218 C  C   . SER   A 1 161 ? -31.147 -1.919  14.085 1.00 54.13  ? 457 SER   A C   1 
ATOM   1219 O  O   . SER   A 1 161 ? -32.070 -2.094  13.277 1.00 53.86  ? 457 SER   A O   1 
ATOM   1220 C  CB  . SER   A 1 161 ? -32.172 -1.856  16.361 1.00 64.50  ? 457 SER   A CB  1 
ATOM   1221 O  OG  . SER   A 1 161 ? -32.419 -1.039  17.504 1.00 68.17  ? 457 SER   A OG  1 
ATOM   1222 N  N   . ALA   A 1 162 ? -29.928 -2.444  13.937 1.00 55.93  ? 458 ALA   A N   1 
ATOM   1223 C  CA  . ALA   A 1 162 ? -29.583 -3.261  12.779 1.00 58.27  ? 458 ALA   A CA  1 
ATOM   1224 C  C   . ALA   A 1 162 ? -28.488 -4.257  13.135 1.00 57.31  ? 458 ALA   A C   1 
ATOM   1225 O  O   . ALA   A 1 162 ? -27.717 -4.068  14.081 1.00 55.56  ? 458 ALA   A O   1 
ATOM   1226 C  CB  . ALA   A 1 162 ? -29.124 -2.401  11.589 1.00 55.37  ? 458 ALA   A CB  1 
ATOM   1227 N  N   . ILE   A 1 163 ? -28.417 -5.320  12.345 1.00 59.04  ? 459 ILE   A N   1 
ATOM   1228 C  CA  . ILE   A 1 163 ? -27.346 -6.298  12.451 1.00 56.05  ? 459 ILE   A CA  1 
ATOM   1229 C  C   . ILE   A 1 163 ? -26.995 -6.751  11.044 1.00 58.22  ? 459 ILE   A C   1 
ATOM   1230 O  O   . ILE   A 1 163 ? -27.874 -6.891  10.185 1.00 57.08  ? 459 ILE   A O   1 
ATOM   1231 C  CB  . ILE   A 1 163 ? -27.747 -7.496  13.335 1.00 54.84  ? 459 ILE   A CB  1 
ATOM   1232 C  CG1 . ILE   A 1 163 ? -26.536 -8.402  13.590 1.00 51.54  ? 459 ILE   A CG1 1 
ATOM   1233 C  CG2 . ILE   A 1 163 ? -28.897 -8.251  12.690 1.00 48.80  ? 459 ILE   A CG2 1 
ATOM   1234 C  CD1 . ILE   A 1 163 ? -26.777 -9.507  14.624 1.00 41.56  ? 459 ILE   A CD1 1 
ATOM   1235 N  N   . THR   A 1 164 ? -25.708 -6.959  10.803 1.00 55.20  ? 460 THR   A N   1 
ATOM   1236 C  CA  . THR   A 1 164 ? -25.222 -7.461  9.525  1.00 56.66  ? 460 THR   A CA  1 
ATOM   1237 C  C   . THR   A 1 164 ? -24.488 -8.764  9.781  1.00 56.00  ? 460 THR   A C   1 
ATOM   1238 O  O   . THR   A 1 164 ? -23.510 -8.783  10.535 1.00 63.19  ? 460 THR   A O   1 
ATOM   1239 C  CB  . THR   A 1 164 ? -24.305 -6.442  8.865  1.00 54.16  ? 460 THR   A CB  1 
ATOM   1240 O  OG1 . THR   A 1 164 ? -25.081 -5.296  8.482  1.00 51.70  ? 460 THR   A OG1 1 
ATOM   1241 C  CG2 . THR   A 1 164 ? -23.617 -7.061  7.642  1.00 46.52  ? 460 THR   A CG2 1 
ATOM   1242 N  N   . ILE   A 1 165 ? -24.959 -9.845  9.164  1.00 49.75  ? 461 ILE   A N   1 
ATOM   1243 C  CA  . ILE   A 1 165 ? -24.536 -11.204 9.489  1.00 45.91  ? 461 ILE   A CA  1 
ATOM   1244 C  C   . ILE   A 1 165 ? -23.713 -11.756 8.323  1.00 53.67  ? 461 ILE   A C   1 
ATOM   1245 O  O   . ILE   A 1 165 ? -24.264 -12.113 7.276  1.00 53.96  ? 461 ILE   A O   1 
ATOM   1246 C  CB  . ILE   A 1 165 ? -25.744 -12.095 9.816  1.00 47.61  ? 461 ILE   A CB  1 
ATOM   1247 C  CG1 . ILE   A 1 165 ? -26.447 -11.593 11.078 1.00 51.39  ? 461 ILE   A CG1 1 
ATOM   1248 C  CG2 . ILE   A 1 165 ? -25.301 -13.496 10.067 1.00 45.12  ? 461 ILE   A CG2 1 
ATOM   1249 C  CD1 . ILE   A 1 165 ? -27.746 -12.244 11.335 1.00 55.19  ? 461 ILE   A CD1 1 
ATOM   1250 N  N   . PHE   A 1 166 ? -22.394 -11.821 8.504  1.00 51.77  ? 462 PHE   A N   1 
ATOM   1251 C  CA  . PHE   A 1 166 ? -21.477 -12.372 7.523  1.00 53.67  ? 462 PHE   A CA  1 
ATOM   1252 C  C   . PHE   A 1 166 ? -21.475 -13.894 7.604  1.00 60.28  ? 462 PHE   A C   1 
ATOM   1253 O  O   . PHE   A 1 166 ? -22.078 -14.468 8.514  1.00 58.37  ? 462 PHE   A O   1 
ATOM   1254 C  CB  . PHE   A 1 166 ? -20.089 -11.769 7.731  1.00 47.12  ? 462 PHE   A CB  1 
ATOM   1255 C  CG  . PHE   A 1 166 ? -20.028 -10.324 7.358  1.00 54.92  ? 462 PHE   A CG  1 
ATOM   1256 C  CD1 . PHE   A 1 166 ? -20.012 -9.939  6.009  1.00 50.01  ? 462 PHE   A CD1 1 
ATOM   1257 C  CD2 . PHE   A 1 166 ? -20.068 -9.343  8.330  1.00 56.41  ? 462 PHE   A CD2 1 
ATOM   1258 C  CE1 . PHE   A 1 166 ? -19.979 -8.597  5.665  1.00 54.26  ? 462 PHE   A CE1 1 
ATOM   1259 C  CE2 . PHE   A 1 166 ? -20.040 -7.988  7.981  1.00 52.59  ? 462 PHE   A CE2 1 
ATOM   1260 C  CZ  . PHE   A 1 166 ? -19.996 -7.617  6.647  1.00 60.29  ? 462 PHE   A CZ  1 
ATOM   1261 N  N   . PRO   A 1 167 ? -20.846 -14.577 6.633  1.00 61.02  ? 463 PRO   A N   1 
ATOM   1262 C  CA  . PRO   A 1 167 ? -20.972 -16.037 6.558  1.00 64.78  ? 463 PRO   A CA  1 
ATOM   1263 C  C   . PRO   A 1 167 ? -20.592 -16.746 7.854  1.00 65.23  ? 463 PRO   A C   1 
ATOM   1264 O  O   . PRO   A 1 167 ? -19.656 -16.358 8.562  1.00 64.54  ? 463 PRO   A O   1 
ATOM   1265 C  CB  . PRO   A 1 167 ? -20.024 -16.404 5.415  1.00 61.49  ? 463 PRO   A CB  1 
ATOM   1266 C  CG  . PRO   A 1 167 ? -20.040 -15.240 4.535  1.00 65.88  ? 463 PRO   A CG  1 
ATOM   1267 C  CD  . PRO   A 1 167 ? -20.082 -14.061 5.479  1.00 63.51  ? 463 PRO   A CD  1 
ATOM   1268 N  N   . GLN   A 1 168 ? -21.328 -17.812 8.146  1.00 66.33  ? 464 GLN   A N   1 
ATOM   1269 C  CA  . GLN   A 1 168 ? -21.064 -18.577 9.351  1.00 53.61  ? 464 GLN   A CA  1 
ATOM   1270 C  C   . GLN   A 1 168 ? -19.692 -19.224 9.270  1.00 61.80  ? 464 GLN   A C   1 
ATOM   1271 O  O   . GLN   A 1 168 ? -19.153 -19.460 8.183  1.00 61.44  ? 464 GLN   A O   1 
ATOM   1272 C  CB  . GLN   A 1 168 ? -22.142 -19.642 9.563  1.00 46.25  ? 464 GLN   A CB  1 
ATOM   1273 C  CG  . GLN   A 1 168 ? -22.152 -20.735 8.489  1.00 49.79  ? 464 GLN   A CG  1 
ATOM   1274 C  CD  . GLN   A 1 168 ? -23.542 -21.317 8.279  1.00 58.41  ? 464 GLN   A CD  1 
ATOM   1275 O  OE1 . GLN   A 1 168 ? -24.544 -20.593 8.303  1.00 66.47  ? 464 GLN   A OE1 1 
ATOM   1276 N  NE2 . GLN   A 1 168 ? -23.610 -22.635 8.075  1.00 55.09  ? 464 GLN   A NE2 1 
ATOM   1277 N  N   . ARG   A 1 169 ? -19.112 -19.464 10.444 1.00 61.55  ? 465 ARG   A N   1 
ATOM   1278 C  CA  . ARG   A 1 169 ? -17.904 -20.261 10.544 1.00 65.10  ? 465 ARG   A CA  1 
ATOM   1279 C  C   . ARG   A 1 169 ? -18.175 -21.667 10.025 1.00 72.98  ? 465 ARG   A C   1 
ATOM   1280 O  O   . ARG   A 1 169 ? -19.226 -22.252 10.296 1.00 78.18  ? 465 ARG   A O   1 
ATOM   1281 C  CB  . ARG   A 1 169 ? -17.428 -20.315 12.001 1.00 68.70  ? 465 ARG   A CB  1 
ATOM   1282 C  CG  . ARG   A 1 169 ? -16.527 -21.502 12.284 1.00 72.56  ? 465 ARG   A CG  1 
ATOM   1283 C  CD  . ARG   A 1 169 ? -16.101 -21.617 13.738 1.00 84.97  ? 465 ARG   A CD  1 
ATOM   1284 N  NE  . ARG   A 1 169 ? -15.144 -20.594 14.152 1.00 88.17  ? 465 ARG   A NE  1 
ATOM   1285 C  CZ  . ARG   A 1 169 ? -15.335 -19.785 15.186 1.00 84.03  ? 465 ARG   A CZ  1 
ATOM   1286 N  NH1 . ARG   A 1 169 ? -16.444 -19.896 15.900 1.00 85.42  ? 465 ARG   A NH1 1 
ATOM   1287 N  NH2 . ARG   A 1 169 ? -14.425 -18.876 15.511 1.00 79.57  ? 465 ARG   A NH2 1 
ATOM   1288 N  N   . THR   A 1 170 ? -17.220 -22.206 9.266  1.00 77.69  ? 466 THR   A N   1 
ATOM   1289 C  CA  . THR   A 1 170 ? -17.305 -23.560 8.730  1.00 81.98  ? 466 THR   A CA  1 
ATOM   1290 C  C   . THR   A 1 170 ? -16.241 -24.436 9.369  1.00 92.11  ? 466 THR   A C   1 
ATOM   1291 O  O   . THR   A 1 170 ? -16.505 -25.177 10.321 1.00 95.21  ? 466 THR   A O   1 
ATOM   1292 C  CB  . THR   A 1 170 ? -17.105 -23.565 7.215  1.00 79.99  ? 466 THR   A CB  1 
ATOM   1293 O  OG1 . THR   A 1 170 ? -16.061 -22.643 6.882  1.00 81.89  ? 466 THR   A OG1 1 
ATOM   1294 C  CG2 . THR   A 1 170 ? -18.391 -23.202 6.462  1.00 72.17  ? 466 THR   A CG2 1 
ATOM   1295 N  N   . ASP   A 1 171 ? -15.023 -24.335 8.848  1.00 95.27  ? 467 ASP   A N   1 
ATOM   1296 C  CA  . ASP   A 1 171 ? -13.930 -25.175 9.318  1.00 98.68  ? 467 ASP   A CA  1 
ATOM   1297 C  C   . ASP   A 1 171 ? -13.278 -24.610 10.572 1.00 96.97  ? 467 ASP   A C   1 
ATOM   1298 O  O   . ASP   A 1 171 ? -12.827 -25.372 11.434 1.00 102.10 ? 467 ASP   A O   1 
ATOM   1299 C  CB  . ASP   A 1 171 ? -12.887 -25.307 8.219  1.00 104.46 ? 467 ASP   A CB  1 
ATOM   1300 C  CG  . ASP   A 1 171 ? -12.310 -23.969 7.838  1.00 110.35 ? 467 ASP   A CG  1 
ATOM   1301 O  OD1 . ASP   A 1 171 ? -13.101 -23.007 7.712  1.00 111.05 ? 467 ASP   A OD1 1 
ATOM   1302 O  OD2 . ASP   A 1 171 ? -11.075 -23.867 7.703  1.00 114.22 ? 467 ASP   A OD2 1 
ATOM   1303 N  N   . GLY   A 1 172 ? -13.207 -23.286 10.684 1.00 94.41  ? 468 GLY   A N   1 
ATOM   1304 C  CA  . GLY   A 1 172 ? -12.461 -22.651 11.752 1.00 95.29  ? 468 GLY   A CA  1 
ATOM   1305 C  C   . GLY   A 1 172 ? -11.321 -21.802 11.221 1.00 100.64 ? 468 GLY   A C   1 
ATOM   1306 O  O   . GLY   A 1 172 ? -11.067 -20.706 11.729 1.00 102.73 ? 468 GLY   A O   1 
ATOM   1307 N  N   . LYS   A 1 173 ? -10.624 -22.299 10.195 1.00 103.09 ? 469 LYS   A N   1 
ATOM   1308 C  CA  . LYS   A 1 173 ? -9.555  -21.537 9.563  1.00 104.20 ? 469 LYS   A CA  1 
ATOM   1309 C  C   . LYS   A 1 173 ? -10.074 -20.563 8.511  1.00 99.34  ? 469 LYS   A C   1 
ATOM   1310 O  O   . LYS   A 1 173 ? -9.282  -19.786 7.963  1.00 100.23 ? 469 LYS   A O   1 
ATOM   1311 C  CB  . LYS   A 1 173 ? -8.520  -22.485 8.935  1.00 111.35 ? 469 LYS   A CB  1 
ATOM   1312 C  CG  . LYS   A 1 173 ? -7.786  -23.394 9.936  1.00 116.88 ? 469 LYS   A CG  1 
ATOM   1313 C  CD  . LYS   A 1 173 ? -8.426  -24.785 10.039 1.00 121.22 ? 469 LYS   A CD  1 
ATOM   1314 C  CE  . LYS   A 1 173 ? -8.505  -25.297 11.496 1.00 125.06 ? 469 LYS   A CE  1 
ATOM   1315 N  NZ  . LYS   A 1 173 ? -7.279  -25.995 12.005 1.00 126.51 ? 469 LYS   A NZ  1 
ATOM   1316 N  N   . HIS   A 1 174 ? -11.373 -20.585 8.217  1.00 98.22  ? 470 HIS   A N   1 
ATOM   1317 C  CA  . HIS   A 1 174 ? -12.013 -19.628 7.316  1.00 99.08  ? 470 HIS   A CA  1 
ATOM   1318 C  C   . HIS   A 1 174 ? -13.110 -18.940 8.104  1.00 102.76 ? 470 HIS   A C   1 
ATOM   1319 O  O   . HIS   A 1 174 ? -14.290 -19.289 7.990  1.00 106.41 ? 470 HIS   A O   1 
ATOM   1320 C  CB  . HIS   A 1 174 ? -12.577 -20.296 6.074  1.00 99.99  ? 470 HIS   A CB  1 
ATOM   1321 C  CG  . HIS   A 1 174 ? -11.538 -20.961 5.239  1.00 102.84 ? 470 HIS   A CG  1 
ATOM   1322 N  ND1 . HIS   A 1 174 ? -11.431 -22.330 5.137  1.00 106.01 ? 470 HIS   A ND1 1 
ATOM   1323 C  CD2 . HIS   A 1 174 ? -10.531 -20.446 4.496  1.00 105.63 ? 470 HIS   A CD2 1 
ATOM   1324 C  CE1 . HIS   A 1 174 ? -10.415 -22.630 4.347  1.00 110.78 ? 470 HIS   A CE1 1 
ATOM   1325 N  NE2 . HIS   A 1 174 ? -9.853  -21.505 3.943  1.00 110.18 ? 470 HIS   A NE2 1 
ATOM   1326 N  N   . ASP   A 1 175 ? -12.710 -17.967 8.913  1.00 97.09  ? 471 ASP   A N   1 
ATOM   1327 C  CA  . ASP   A 1 175 ? -13.640 -17.148 9.667  1.00 85.34  ? 471 ASP   A CA  1 
ATOM   1328 C  C   . ASP   A 1 175 ? -13.710 -15.759 9.061  1.00 74.09  ? 471 ASP   A C   1 
ATOM   1329 O  O   . ASP   A 1 175 ? -12.691 -15.199 8.641  1.00 74.67  ? 471 ASP   A O   1 
ATOM   1330 C  CB  . ASP   A 1 175 ? -13.223 -17.050 11.132 1.00 89.37  ? 471 ASP   A CB  1 
ATOM   1331 C  CG  . ASP   A 1 175 ? -13.640 -18.254 11.920 1.00 90.71  ? 471 ASP   A CG  1 
ATOM   1332 O  OD1 . ASP   A 1 175 ? -14.414 -19.070 11.373 1.00 93.88  ? 471 ASP   A OD1 1 
ATOM   1333 O  OD2 . ASP   A 1 175 ? -13.193 -18.392 13.070 1.00 92.21  ? 471 ASP   A OD2 1 
ATOM   1334 N  N   . PHE   A 1 176 ? -14.922 -15.223 8.991  1.00 66.11  ? 472 PHE   A N   1 
ATOM   1335 C  CA  . PHE   A 1 176 ? -15.101 -13.799 8.765  1.00 62.40  ? 472 PHE   A CA  1 
ATOM   1336 C  C   . PHE   A 1 176 ? -15.039 -13.103 10.115 1.00 60.37  ? 472 PHE   A C   1 
ATOM   1337 O  O   . PHE   A 1 176 ? -15.815 -13.431 11.015 1.00 55.80  ? 472 PHE   A O   1 
ATOM   1338 C  CB  . PHE   A 1 176 ? -16.432 -13.520 8.070  1.00 60.52  ? 472 PHE   A CB  1 
ATOM   1339 C  CG  . PHE   A 1 176 ? -16.447 -13.878 6.623  1.00 59.15  ? 472 PHE   A CG  1 
ATOM   1340 C  CD1 . PHE   A 1 176 ? -16.477 -15.197 6.223  1.00 59.68  ? 472 PHE   A CD1 1 
ATOM   1341 C  CD2 . PHE   A 1 176 ? -16.448 -12.887 5.659  1.00 64.62  ? 472 PHE   A CD2 1 
ATOM   1342 C  CE1 . PHE   A 1 176 ? -16.500 -15.524 4.864  1.00 63.60  ? 472 PHE   A CE1 1 
ATOM   1343 C  CE2 . PHE   A 1 176 ? -16.467 -13.203 4.319  1.00 63.76  ? 472 PHE   A CE2 1 
ATOM   1344 C  CZ  . PHE   A 1 176 ? -16.492 -14.524 3.922  1.00 61.62  ? 472 PHE   A CZ  1 
ATOM   1345 N  N   . ARG   A 1 177 ? -14.099 -12.180 10.274 1.00 56.29  ? 473 ARG   A N   1 
ATOM   1346 C  CA  . ARG   A 1 177 ? -13.990 -11.417 11.510 1.00 65.94  ? 473 ARG   A CA  1 
ATOM   1347 C  C   . ARG   A 1 177 ? -13.861 -9.941  11.195 1.00 63.44  ? 473 ARG   A C   1 
ATOM   1348 O  O   . ARG   A 1 177 ? -13.046 -9.561  10.353 1.00 59.96  ? 473 ARG   A O   1 
ATOM   1349 C  CB  . ARG   A 1 177 ? -12.787 -11.874 12.345 1.00 67.02  ? 473 ARG   A CB  1 
ATOM   1350 C  CG  . ARG   A 1 177 ? -12.893 -13.286 12.831 1.00 65.33  ? 473 ARG   A CG  1 
ATOM   1351 C  CD  . ARG   A 1 177 ? -14.072 -13.401 13.768 1.00 68.16  ? 473 ARG   A CD  1 
ATOM   1352 N  NE  . ARG   A 1 177 ? -13.915 -12.542 14.937 1.00 69.26  ? 473 ARG   A NE  1 
ATOM   1353 C  CZ  . ARG   A 1 177 ? -13.171 -12.858 15.992 1.00 71.36  ? 473 ARG   A CZ  1 
ATOM   1354 N  NH1 . ARG   A 1 177 ? -12.517 -14.015 16.024 1.00 74.07  ? 473 ARG   A NH1 1 
ATOM   1355 N  NH2 . ARG   A 1 177 ? -13.077 -12.018 17.015 1.00 70.69  ? 473 ARG   A NH2 1 
ATOM   1356 N  N   . VAL   A 1 178 ? -14.667 -9.122  11.864 1.00 58.85  ? 474 VAL   A N   1 
ATOM   1357 C  CA  . VAL   A 1 178 ? -14.351 -7.707  12.041 1.00 55.65  ? 474 VAL   A CA  1 
ATOM   1358 C  C   . VAL   A 1 178 ? -13.389 -7.606  13.217 1.00 69.93  ? 474 VAL   A C   1 
ATOM   1359 O  O   . VAL   A 1 178 ? -13.727 -8.007  14.336 1.00 77.72  ? 474 VAL   A O   1 
ATOM   1360 C  CB  . VAL   A 1 178 ? -15.621 -6.873  12.282 1.00 54.59  ? 474 VAL   A CB  1 
ATOM   1361 C  CG1 . VAL   A 1 178 ? -15.302 -5.372  12.311 1.00 55.21  ? 474 VAL   A CG1 1 
ATOM   1362 C  CG2 . VAL   A 1 178 ? -16.683 -7.167  11.214 1.00 53.99  ? 474 VAL   A CG2 1 
ATOM   1363 N  N   . TRP   A 1 179 ? -12.181 -7.095  12.966 1.00 75.47  ? 475 TRP   A N   1 
ATOM   1364 C  CA  . TRP   A 1 179 ? -11.169 -7.046  14.017 1.00 74.07  ? 475 TRP   A CA  1 
ATOM   1365 C  C   . TRP   A 1 179 ? -11.378 -5.896  14.998 1.00 75.33  ? 475 TRP   A C   1 
ATOM   1366 O  O   . TRP   A 1 179 ? -10.827 -5.945  16.103 1.00 78.22  ? 475 TRP   A O   1 
ATOM   1367 C  CB  . TRP   A 1 179 ? -9.761  -6.962  13.415 1.00 69.80  ? 475 TRP   A CB  1 
ATOM   1368 C  CG  . TRP   A 1 179 ? -9.268  -8.267  12.870 1.00 74.09  ? 475 TRP   A CG  1 
ATOM   1369 C  CD1 . TRP   A 1 179 ? -10.012 -9.233  12.248 1.00 74.08  ? 475 TRP   A CD1 1 
ATOM   1370 C  CD2 . TRP   A 1 179 ? -7.924  -8.757  12.905 1.00 79.20  ? 475 TRP   A CD2 1 
ATOM   1371 N  NE1 . TRP   A 1 179 ? -9.209  -10.289 11.891 1.00 79.06  ? 475 TRP   A NE1 1 
ATOM   1372 C  CE2 . TRP   A 1 179 ? -7.924  -10.022 12.287 1.00 83.89  ? 475 TRP   A CE2 1 
ATOM   1373 C  CE3 . TRP   A 1 179 ? -6.721  -8.247  13.394 1.00 83.87  ? 475 TRP   A CE3 1 
ATOM   1374 C  CZ2 . TRP   A 1 179 ? -6.769  -10.782 12.148 1.00 91.35  ? 475 TRP   A CZ2 1 
ATOM   1375 C  CZ3 . TRP   A 1 179 ? -5.581  -9.003  13.261 1.00 91.37  ? 475 TRP   A CZ3 1 
ATOM   1376 C  CH2 . TRP   A 1 179 ? -5.611  -10.257 12.642 1.00 95.37  ? 475 TRP   A CH2 1 
ATOM   1377 N  N   . ASN   A 1 180 ? -12.144 -4.876  14.619 1.00 71.13  ? 476 ASN   A N   1 
ATOM   1378 C  CA  . ASN   A 1 180 ? -12.507 -3.814  15.539 1.00 68.29  ? 476 ASN   A CA  1 
ATOM   1379 C  C   . ASN   A 1 180 ? -13.454 -4.346  16.603 1.00 71.94  ? 476 ASN   A C   1 
ATOM   1380 O  O   . ASN   A 1 180 ? -14.245 -5.260  16.354 1.00 67.21  ? 476 ASN   A O   1 
ATOM   1381 C  CB  . ASN   A 1 180 ? -13.208 -2.664  14.813 1.00 73.61  ? 476 ASN   A CB  1 
ATOM   1382 C  CG  . ASN   A 1 180 ? -12.486 -2.221  13.568 1.00 77.92  ? 476 ASN   A CG  1 
ATOM   1383 O  OD1 . ASN   A 1 180 ? -12.150 -3.040  12.710 1.00 76.97  ? 476 ASN   A OD1 1 
ATOM   1384 N  ND2 . ASN   A 1 180 ? -12.238 -0.914  13.459 1.00 77.96  ? 476 ASN   A ND2 1 
ATOM   1385 N  N   . SER   A 1 181 ? -13.384 -3.753  17.800 1.00 64.55  ? 477 SER   A N   1 
ATOM   1386 C  CA  . SER   A 1 181 ? -14.372 -4.114  18.811 1.00 61.29  ? 477 SER   A CA  1 
ATOM   1387 C  C   . SER   A 1 181 ? -15.721 -3.468  18.518 1.00 62.00  ? 477 SER   A C   1 
ATOM   1388 O  O   . SER   A 1 181 ? -16.766 -4.082  18.762 1.00 54.15  ? 477 SER   A O   1 
ATOM   1389 C  CB  . SER   A 1 181 ? -13.871 -3.753  20.218 1.00 54.48  ? 477 SER   A CB  1 
ATOM   1390 O  OG  . SER   A 1 181 ? -13.136 -2.539  20.259 1.00 63.46  ? 477 SER   A OG  1 
ATOM   1391 N  N   . GLN   A 1 182 ? -15.714 -2.258  17.960 1.00 68.67  ? 478 GLN   A N   1 
ATOM   1392 C  CA  . GLN   A 1 182 ? -16.910 -1.588  17.467 1.00 68.88  ? 478 GLN   A CA  1 
ATOM   1393 C  C   . GLN   A 1 182 ? -16.596 -0.989  16.105 1.00 72.02  ? 478 GLN   A C   1 
ATOM   1394 O  O   . GLN   A 1 182 ? -15.480 -0.511  15.882 1.00 78.90  ? 478 GLN   A O   1 
ATOM   1395 C  CB  . GLN   A 1 182 ? -17.389 -0.458  18.402 1.00 70.87  ? 478 GLN   A CB  1 
ATOM   1396 C  CG  . GLN   A 1 182 ? -17.814 -0.849  19.812 1.00 74.39  ? 478 GLN   A CG  1 
ATOM   1397 C  CD  . GLN   A 1 182 ? -17.926 0.375   20.734 1.00 77.19  ? 478 GLN   A CD  1 
ATOM   1398 O  OE1 . GLN   A 1 182 ? -18.480 1.417   20.353 1.00 78.79  ? 478 GLN   A OE1 1 
ATOM   1399 N  NE2 . GLN   A 1 182 ? -17.377 0.258   21.938 1.00 70.50  ? 478 GLN   A NE2 1 
ATOM   1400 N  N   . LEU   A 1 183 ? -17.588 -1.002  15.209 1.00 65.02  ? 479 LEU   A N   1 
ATOM   1401 C  CA  . LEU   A 1 183 ? -17.426 -0.394  13.892 1.00 63.14  ? 479 LEU   A CA  1 
ATOM   1402 C  C   . LEU   A 1 183 ? -16.850 1.013   13.985 1.00 60.56  ? 479 LEU   A C   1 
ATOM   1403 O  O   . LEU   A 1 183 ? -15.971 1.389   13.203 1.00 66.77  ? 479 LEU   A O   1 
ATOM   1404 C  CB  . LEU   A 1 183 ? -18.772 -0.361  13.167 1.00 60.79  ? 479 LEU   A CB  1 
ATOM   1405 C  CG  . LEU   A 1 183 ? -19.549 -1.663  12.936 1.00 60.97  ? 479 LEU   A CG  1 
ATOM   1406 C  CD1 . LEU   A 1 183 ? -20.804 -1.412  12.076 1.00 64.13  ? 479 LEU   A CD1 1 
ATOM   1407 C  CD2 . LEU   A 1 183 ? -18.658 -2.752  12.323 1.00 50.37  ? 479 LEU   A CD2 1 
ATOM   1408 N  N   . ILE   A 1 184 ? -17.334 1.813   14.924 1.00 67.59  ? 480 ILE   A N   1 
ATOM   1409 C  CA  . ILE   A 1 184 ? -16.857 3.179   15.114 1.00 48.83  ? 480 ILE   A CA  1 
ATOM   1410 C  C   . ILE   A 1 184 ? -16.268 3.311   16.516 1.00 66.03  ? 480 ILE   A C   1 
ATOM   1411 O  O   . ILE   A 1 184 ? -16.992 3.206   17.516 1.00 71.04  ? 480 ILE   A O   1 
ATOM   1412 C  CB  . ILE   A 1 184 ? -17.971 4.192   14.867 1.00 50.54  ? 480 ILE   A CB  1 
ATOM   1413 C  CG1 . ILE   A 1 184 ? -18.341 4.165   13.364 1.00 58.24  ? 480 ILE   A CG1 1 
ATOM   1414 C  CG2 . ILE   A 1 184 ? -17.474 5.596   15.156 1.00 57.74  ? 480 ILE   A CG2 1 
ATOM   1415 C  CD1 . ILE   A 1 184 ? -19.614 4.868   13.065 1.00 58.45  ? 480 ILE   A CD1 1 
ATOM   1416 N  N   . ARG   A 1 185 ? -14.951 3.516   16.582 1.00 66.45  ? 481 ARG   A N   1 
ATOM   1417 C  CA  . ARG   A 1 185 ? -14.233 3.812   17.812 1.00 74.76  ? 481 ARG   A CA  1 
ATOM   1418 C  C   . ARG   A 1 185 ? -13.169 4.858   17.522 1.00 80.93  ? 481 ARG   A C   1 
ATOM   1419 O  O   . ARG   A 1 185 ? -12.654 4.951   16.403 1.00 84.77  ? 481 ARG   A O   1 
ATOM   1420 C  CB  . ARG   A 1 185 ? -13.558 2.574   18.423 1.00 70.01  ? 481 ARG   A CB  1 
ATOM   1421 C  CG  . ARG   A 1 185 ? -14.505 1.459   18.767 1.00 71.13  ? 481 ARG   A CG  1 
ATOM   1422 C  CD  . ARG   A 1 185 ? -14.011 0.606   19.953 1.00 74.38  ? 481 ARG   A CD  1 
ATOM   1423 N  NE  . ARG   A 1 185 ? -14.063 1.357   21.207 1.00 76.60  ? 481 ARG   A NE  1 
ATOM   1424 C  CZ  . ARG   A 1 185 ? -13.847 0.835   22.410 1.00 75.54  ? 481 ARG   A CZ  1 
ATOM   1425 N  NH1 . ARG   A 1 185 ? -13.567 -0.461  22.550 1.00 60.13  ? 481 ARG   A NH1 1 
ATOM   1426 N  NH2 . ARG   A 1 185 ? -13.921 1.618   23.480 1.00 86.03  ? 481 ARG   A NH2 1 
ATOM   1427 N  N   . TYR   A 1 186 ? -12.847 5.642   18.545 1.00 74.97  ? 482 TYR   A N   1 
ATOM   1428 C  CA  . TYR   A 1 186 ? -11.768 6.612   18.469 1.00 81.65  ? 482 TYR   A CA  1 
ATOM   1429 C  C   . TYR   A 1 186 ? -10.428 5.931   18.733 1.00 84.24  ? 482 TYR   A C   1 
ATOM   1430 O  O   . TYR   A 1 186 ? -10.349 4.883   19.380 1.00 78.33  ? 482 TYR   A O   1 
ATOM   1431 C  CB  . TYR   A 1 186 ? -12.009 7.763   19.457 1.00 81.41  ? 482 TYR   A CB  1 
ATOM   1432 C  CG  . TYR   A 1 186 ? -13.280 8.538   19.129 1.00 86.46  ? 482 TYR   A CG  1 
ATOM   1433 C  CD1 . TYR   A 1 186 ? -14.348 8.594   20.019 1.00 85.28  ? 482 TYR   A CD1 1 
ATOM   1434 C  CD2 . TYR   A 1 186 ? -13.427 9.177   17.899 1.00 83.06  ? 482 TYR   A CD2 1 
ATOM   1435 C  CE1 . TYR   A 1 186 ? -15.512 9.297   19.704 1.00 83.46  ? 482 TYR   A CE1 1 
ATOM   1436 C  CE2 . TYR   A 1 186 ? -14.579 9.881   17.581 1.00 85.64  ? 482 TYR   A CE2 1 
ATOM   1437 C  CZ  . TYR   A 1 186 ? -15.623 9.929   18.482 1.00 83.08  ? 482 TYR   A CZ  1 
ATOM   1438 O  OH  . TYR   A 1 186 ? -16.775 10.618  18.151 1.00 77.14  ? 482 TYR   A OH  1 
ATOM   1439 N  N   . ALA   A 1 187 ? -9.373  6.526   18.196 1.00 92.27  ? 483 ALA   A N   1 
ATOM   1440 C  CA  . ALA   A 1 187 ? -8.050  5.935   18.238 1.00 92.51  ? 483 ALA   A CA  1 
ATOM   1441 C  C   . ALA   A 1 187 ? -7.417  6.120   19.611 1.00 95.07  ? 483 ALA   A C   1 
ATOM   1442 O  O   . ALA   A 1 187 ? -7.780  7.013   20.377 1.00 90.63  ? 483 ALA   A O   1 
ATOM   1443 C  CB  . ALA   A 1 187 ? -7.151  6.550   17.170 1.00 90.03  ? 483 ALA   A CB  1 
ATOM   1444 N  N   . GLY   A 1 188 ? -6.440  5.266   19.903 1.00 97.55  ? 484 GLY   A N   1 
ATOM   1445 C  CA  . GLY   A 1 188 ? -5.733  5.332   21.164 1.00 103.52 ? 484 GLY   A CA  1 
ATOM   1446 C  C   . GLY   A 1 188 ? -4.233  5.372   20.999 1.00 107.38 ? 484 GLY   A C   1 
ATOM   1447 O  O   . GLY   A 1 188 ? -3.605  4.356   20.686 1.00 109.81 ? 484 GLY   A O   1 
ATOM   1448 N  N   . TYR   A 1 189 ? -3.647  6.542   21.210 1.00 106.38 ? 485 TYR   A N   1 
ATOM   1449 C  CA  . TYR   A 1 189 ? -2.215  6.741   21.040 1.00 109.98 ? 485 TYR   A CA  1 
ATOM   1450 C  C   . TYR   A 1 189 ? -1.589  6.973   22.402 1.00 116.21 ? 485 TYR   A C   1 
ATOM   1451 O  O   . TYR   A 1 189 ? -1.841  8.000   23.041 1.00 113.07 ? 485 TYR   A O   1 
ATOM   1452 C  CB  . TYR   A 1 189 ? -1.906  7.920   20.121 1.00 110.85 ? 485 TYR   A CB  1 
ATOM   1453 C  CG  . TYR   A 1 189 ? -2.742  7.997   18.872 1.00 99.61  ? 485 TYR   A CG  1 
ATOM   1454 C  CD1 . TYR   A 1 189 ? -3.859  8.815   18.829 1.00 97.10  ? 485 TYR   A CD1 1 
ATOM   1455 C  CD2 . TYR   A 1 189 ? -2.407  7.274   17.741 1.00 103.52 ? 485 TYR   A CD2 1 
ATOM   1456 C  CE1 . TYR   A 1 189 ? -4.627  8.907   17.707 1.00 102.48 ? 485 TYR   A CE1 1 
ATOM   1457 C  CE2 . TYR   A 1 189 ? -3.182  7.360   16.591 1.00 100.60 ? 485 TYR   A CE2 1 
ATOM   1458 C  CZ  . TYR   A 1 189 ? -4.287  8.189   16.583 1.00 97.81  ? 485 TYR   A CZ  1 
ATOM   1459 O  OH  . TYR   A 1 189 ? -5.087  8.309   15.485 1.00 87.39  ? 485 TYR   A OH  1 
ATOM   1460 N  N   . LYS   A 1 190 ? -0.774  6.019   22.834 1.00 123.98 ? 486 LYS   A N   1 
ATOM   1461 C  CA  . LYS   A 1 190 ? 0.167   6.279   23.909 1.00 131.47 ? 486 LYS   A CA  1 
ATOM   1462 C  C   . LYS   A 1 190 ? 1.127   7.388   23.483 1.00 139.52 ? 486 LYS   A C   1 
ATOM   1463 O  O   . LYS   A 1 190 ? 1.238   7.735   22.303 1.00 143.69 ? 486 LYS   A O   1 
ATOM   1464 C  CB  . LYS   A 1 190 ? 0.925   5.001   24.258 1.00 132.47 ? 486 LYS   A CB  1 
ATOM   1465 C  CG  . LYS   A 1 190 ? 1.213   4.142   23.031 1.00 132.12 ? 486 LYS   A CG  1 
ATOM   1466 C  CD  . LYS   A 1 190 ? 2.243   3.060   23.307 1.00 131.37 ? 486 LYS   A CD  1 
ATOM   1467 C  CE  . LYS   A 1 190 ? 1.608   1.808   23.881 1.00 123.16 ? 486 LYS   A CE  1 
ATOM   1468 N  NZ  . LYS   A 1 190 ? 2.527   0.642   23.758 1.00 122.78 ? 486 LYS   A NZ  1 
ATOM   1469 N  N   . GLN   A 1 191 ? 1.826   7.951   24.456 1.00 141.38 ? 487 GLN   A N   1 
ATOM   1470 C  CA  . GLN   A 1 191 ? 2.711   9.075   24.213 1.00 146.72 ? 487 GLN   A CA  1 
ATOM   1471 C  C   . GLN   A 1 191 ? 4.156   8.716   24.538 1.00 153.67 ? 487 GLN   A C   1 
ATOM   1472 O  O   . GLN   A 1 191 ? 4.424   7.699   25.191 1.00 153.77 ? 487 GLN   A O   1 
ATOM   1473 C  CB  . GLN   A 1 191 ? 2.279   10.291  25.047 1.00 148.11 ? 487 GLN   A CB  1 
ATOM   1474 C  CG  . GLN   A 1 191 ? 0.949   10.904  24.623 1.00 145.44 ? 487 GLN   A CG  1 
ATOM   1475 C  CD  . GLN   A 1 191 ? 0.989   11.548  23.240 1.00 149.42 ? 487 GLN   A CD  1 
ATOM   1476 O  OE1 . GLN   A 1 191 ? 1.373   10.924  22.249 1.00 150.36 ? 487 GLN   A OE1 1 
ATOM   1477 N  NE2 . GLN   A 1 191 ? 0.573   12.804  23.170 1.00 150.94 ? 487 GLN   A NE2 1 
ATOM   1478 N  N   . PRO   A 1 192 ? 5.122   9.519   24.078 1.00 159.94 ? 488 PRO   A N   1 
ATOM   1479 C  CA  . PRO   A 1 192 ? 6.500   9.325   24.561 1.00 166.52 ? 488 PRO   A CA  1 
ATOM   1480 C  C   . PRO   A 1 192 ? 6.640   9.569   26.054 1.00 167.74 ? 488 PRO   A C   1 
ATOM   1481 O  O   . PRO   A 1 192 ? 7.401   8.863   26.730 1.00 168.86 ? 488 PRO   A O   1 
ATOM   1482 C  CB  . PRO   A 1 192 ? 7.307   10.330  23.730 1.00 173.29 ? 488 PRO   A CB  1 
ATOM   1483 C  CG  . PRO   A 1 192 ? 6.299   11.312  23.211 1.00 170.72 ? 488 PRO   A CG  1 
ATOM   1484 C  CD  . PRO   A 1 192 ? 5.052   10.524  23.004 1.00 162.74 ? 488 PRO   A CD  1 
ATOM   1485 N  N   . ASP   A 1 193 ? 5.910   10.541  26.597 1.00 167.39 ? 489 ASP   A N   1 
ATOM   1486 C  CA  . ASP   A 1 193 ? 5.924   10.791  28.032 1.00 167.38 ? 489 ASP   A CA  1 
ATOM   1487 C  C   . ASP   A 1 193 ? 5.027   9.832   28.808 1.00 157.04 ? 489 ASP   A C   1 
ATOM   1488 O  O   . ASP   A 1 193 ? 4.637   10.147  29.940 1.00 154.74 ? 489 ASP   A O   1 
ATOM   1489 C  CB  . ASP   A 1 193 ? 5.516   12.237  28.324 1.00 173.19 ? 489 ASP   A CB  1 
ATOM   1490 C  CG  . ASP   A 1 193 ? 4.129   12.564  27.819 1.00 169.94 ? 489 ASP   A CG  1 
ATOM   1491 O  OD1 . ASP   A 1 193 ? 3.925   12.549  26.583 1.00 166.83 ? 489 ASP   A OD1 1 
ATOM   1492 O  OD2 . ASP   A 1 193 ? 3.244   12.825  28.665 1.00 166.94 ? 489 ASP   A OD2 1 
ATOM   1493 N  N   . GLY   A 1 194 ? 4.687   8.687   28.227 1.00 153.00 ? 490 GLY   A N   1 
ATOM   1494 C  CA  . GLY   A 1 194 ? 3.929   7.648   28.902 1.00 150.50 ? 490 GLY   A CA  1 
ATOM   1495 C  C   . GLY   A 1 194 ? 2.416   7.692   28.784 1.00 149.89 ? 490 GLY   A C   1 
ATOM   1496 O  O   . GLY   A 1 194 ? 1.783   6.647   28.619 1.00 151.22 ? 490 GLY   A O   1 
ATOM   1497 N  N   . SER   A 1 195 ? 1.824   8.883   28.857 1.00 149.61 ? 491 SER   A N   1 
ATOM   1498 C  CA  . SER   A 1 195 ? 0.372   9.030   28.911 1.00 144.51 ? 491 SER   A CA  1 
ATOM   1499 C  C   . SER   A 1 195 ? -0.266  8.605   27.579 1.00 139.94 ? 491 SER   A C   1 
ATOM   1500 O  O   . SER   A 1 195 ? 0.389   8.061   26.684 1.00 142.23 ? 491 SER   A O   1 
ATOM   1501 C  CB  . SER   A 1 195 ? 0.008   10.461  29.294 1.00 144.70 ? 491 SER   A CB  1 
ATOM   1502 O  OG  . SER   A 1 195 ? 0.605   11.393  28.409 1.00 149.38 ? 491 SER   A OG  1 
ATOM   1503 N  N   . THR   A 1 196 ? -1.571  8.856   27.436 1.00 133.01 ? 492 THR   A N   1 
ATOM   1504 C  CA  . THR   A 1 196 ? -2.340  8.335   26.306 1.00 126.29 ? 492 THR   A CA  1 
ATOM   1505 C  C   . THR   A 1 196 ? -3.235  9.415   25.708 1.00 124.98 ? 492 THR   A C   1 
ATOM   1506 O  O   . THR   A 1 196 ? -4.062  10.004  26.410 1.00 126.23 ? 492 THR   A O   1 
ATOM   1507 C  CB  . THR   A 1 196 ? -3.195  7.134   26.733 1.00 114.21 ? 492 THR   A CB  1 
ATOM   1508 O  OG1 . THR   A 1 196 ? -2.350  6.064   27.181 1.00 108.99 ? 492 THR   A OG1 1 
ATOM   1509 C  CG2 . THR   A 1 196 ? -4.066  6.660   25.564 1.00 107.90 ? 492 THR   A CG2 1 
ATOM   1510 N  N   . LEU   A 1 197 ? -3.089  9.650   24.406 1.00 123.15 ? 493 LEU   A N   1 
ATOM   1511 C  CA  . LEU   A 1 197 ? -4.019  10.472  23.645 1.00 118.17 ? 493 LEU   A CA  1 
ATOM   1512 C  C   . LEU   A 1 197 ? -5.114  9.589   23.063 1.00 108.24 ? 493 LEU   A C   1 
ATOM   1513 O  O   . LEU   A 1 197 ? -4.921  8.388   22.855 1.00 102.22 ? 493 LEU   A O   1 
ATOM   1514 C  CB  . LEU   A 1 197 ? -3.288  11.235  22.532 1.00 123.23 ? 493 LEU   A CB  1 
ATOM   1515 C  CG  . LEU   A 1 197 ? -4.037  12.246  21.650 1.00 125.36 ? 493 LEU   A CG  1 
ATOM   1516 C  CD1 . LEU   A 1 197 ? -4.926  13.159  22.471 1.00 126.99 ? 493 LEU   A CD1 1 
ATOM   1517 C  CD2 . LEU   A 1 197 ? -3.060  13.080  20.826 1.00 132.68 ? 493 LEU   A CD2 1 
ATOM   1518 N  N   . GLY   A 1 198 ? -6.281  10.187  22.831 1.00 109.81 ? 494 GLY   A N   1 
ATOM   1519 C  CA  . GLY   A 1 198 ? -7.380  9.485   22.186 1.00 109.69 ? 494 GLY   A CA  1 
ATOM   1520 C  C   . GLY   A 1 198 ? -8.180  8.604   23.123 1.00 107.62 ? 494 GLY   A C   1 
ATOM   1521 O  O   . GLY   A 1 198 ? -8.842  9.109   24.029 1.00 116.92 ? 494 GLY   A O   1 
ATOM   1522 N  N   . ASP   A 1 199 ? -8.130  7.292   22.921 1.00 96.28  ? 495 ASP   A N   1 
ATOM   1523 C  CA  . ASP   A 1 199 ? -8.891  6.343   23.735 1.00 88.40  ? 495 ASP   A CA  1 
ATOM   1524 C  C   . ASP   A 1 199 ? -7.958  5.238   24.209 1.00 88.10  ? 495 ASP   A C   1 
ATOM   1525 O  O   . ASP   A 1 199 ? -7.546  4.392   23.390 1.00 75.46  ? 495 ASP   A O   1 
ATOM   1526 C  CB  . ASP   A 1 199 ? -10.072 5.769   22.954 1.00 87.59  ? 495 ASP   A CB  1 
ATOM   1527 C  CG  . ASP   A 1 199 ? -11.074 5.042   23.847 1.00 89.29  ? 495 ASP   A CG  1 
ATOM   1528 O  OD1 . ASP   A 1 199 ? -10.691 4.590   24.951 1.00 82.72  ? 495 ASP   A OD1 1 
ATOM   1529 O  OD2 . ASP   A 1 199 ? -12.256 4.922   23.438 1.00 88.59  ? 495 ASP   A OD2 1 
ATOM   1530 N  N   . PRO   A 1 200 ? -7.609  5.196   25.505 1.00 93.63  ? 496 PRO   A N   1 
ATOM   1531 C  CA  . PRO   A 1 200 ? -6.696  4.142   25.985 1.00 89.05  ? 496 PRO   A CA  1 
ATOM   1532 C  C   . PRO   A 1 200 ? -7.199  2.733   25.724 1.00 81.94  ? 496 PRO   A C   1 
ATOM   1533 O  O   . PRO   A 1 200 ? -6.386  1.813   25.597 1.00 82.93  ? 496 PRO   A O   1 
ATOM   1534 C  CB  . PRO   A 1 200 ? -6.574  4.441   27.486 1.00 94.36  ? 496 PRO   A CB  1 
ATOM   1535 C  CG  . PRO   A 1 200 ? -6.901  5.902   27.619 1.00 97.49  ? 496 PRO   A CG  1 
ATOM   1536 C  CD  . PRO   A 1 200 ? -7.950  6.167   26.556 1.00 92.85  ? 496 PRO   A CD  1 
ATOM   1537 N  N   . ALA   A 1 201 ? -8.515  2.543   25.611 1.00 82.53  ? 497 ALA   A N   1 
ATOM   1538 C  CA  . ALA   A 1 201 ? -9.068  1.213   25.370 1.00 82.61  ? 497 ALA   A CA  1 
ATOM   1539 C  C   . ALA   A 1 201 ? -8.471  0.557   24.131 1.00 88.50  ? 497 ALA   A C   1 
ATOM   1540 O  O   . ALA   A 1 201 ? -8.216  -0.653  24.122 1.00 84.42  ? 497 ALA   A O   1 
ATOM   1541 C  CB  . ALA   A 1 201 ? -10.589 1.297   25.227 1.00 76.19  ? 497 ALA   A CB  1 
ATOM   1542 N  N   . ASN   A 1 202 ? -8.220  1.347   23.083 1.00 94.79  ? 498 ASN   A N   1 
ATOM   1543 C  CA  . ASN   A 1 202 ? -7.928  0.837   21.749 1.00 93.49  ? 498 ASN   A CA  1 
ATOM   1544 C  C   . ASN   A 1 202 ? -6.451  0.931   21.387 1.00 92.61  ? 498 ASN   A C   1 
ATOM   1545 O  O   . ASN   A 1 202 ? -6.110  0.827   20.202 1.00 95.11  ? 498 ASN   A O   1 
ATOM   1546 C  CB  . ASN   A 1 202 ? -8.745  1.601   20.704 1.00 92.86  ? 498 ASN   A CB  1 
ATOM   1547 C  CG  . ASN   A 1 202 ? -10.190 1.783   21.110 1.00 87.05  ? 498 ASN   A CG  1 
ATOM   1548 O  OD1 . ASN   A 1 202 ? -10.837 0.844   21.573 1.00 83.18  ? 498 ASN   A OD1 1 
ATOM   1549 N  ND2 . ASN   A 1 202 ? -10.706 2.998   20.940 1.00 86.98  ? 498 ASN   A ND2 1 
ATOM   1550 N  N   . VAL   A 1 203 ? -5.571  1.143   22.371 1.00 80.78  ? 499 VAL   A N   1 
ATOM   1551 C  CA  . VAL   A 1 203 ? -4.186  1.486   22.055 1.00 82.06  ? 499 VAL   A CA  1 
ATOM   1552 C  C   . VAL   A 1 203 ? -3.488  0.330   21.357 1.00 85.95  ? 499 VAL   A C   1 
ATOM   1553 O  O   . VAL   A 1 203 ? -2.636  0.540   20.483 1.00 89.62  ? 499 VAL   A O   1 
ATOM   1554 C  CB  . VAL   A 1 203 ? -3.429  1.921   23.321 1.00 89.78  ? 499 VAL   A CB  1 
ATOM   1555 C  CG1 . VAL   A 1 203 ? -1.973  2.200   22.985 1.00 90.33  ? 499 VAL   A CG1 1 
ATOM   1556 C  CG2 . VAL   A 1 203 ? -4.066  3.156   23.906 1.00 96.28  ? 499 VAL   A CG2 1 
ATOM   1557 N  N   . GLN   A 1 204 ? -3.837  -0.907  21.708 1.00 84.45  ? 500 GLN   A N   1 
ATOM   1558 C  CA  . GLN   A 1 204 ? -3.278  -2.017  20.947 1.00 96.79  ? 500 GLN   A CA  1 
ATOM   1559 C  C   . GLN   A 1 204 ? -3.891  -2.070  19.556 1.00 97.31  ? 500 GLN   A C   1 
ATOM   1560 O  O   . GLN   A 1 204 ? -3.171  -2.194  18.558 1.00 100.57 ? 500 GLN   A O   1 
ATOM   1561 C  CB  . GLN   A 1 204 ? -3.472  -3.354  21.665 1.00 102.54 ? 500 GLN   A CB  1 
ATOM   1562 C  CG  . GLN   A 1 204 ? -2.902  -4.509  20.831 1.00 110.73 ? 500 GLN   A CG  1 
ATOM   1563 C  CD  . GLN   A 1 204 ? -2.910  -5.855  21.529 1.00 115.92 ? 500 GLN   A CD  1 
ATOM   1564 O  OE1 . GLN   A 1 204 ? -3.622  -6.059  22.512 1.00 116.21 ? 500 GLN   A OE1 1 
ATOM   1565 N  NE2 . GLN   A 1 204 ? -2.113  -6.788  21.014 1.00 120.77 ? 500 GLN   A NE2 1 
ATOM   1566 N  N   . PHE   A 1 205 ? -5.221  -1.959  19.470 1.00 91.23  ? 501 PHE   A N   1 
ATOM   1567 C  CA  . PHE   A 1 205 ? -5.883  -2.024  18.170 1.00 86.22  ? 501 PHE   A CA  1 
ATOM   1568 C  C   . PHE   A 1 205 ? -5.404  -0.910  17.247 1.00 89.20  ? 501 PHE   A C   1 
ATOM   1569 O  O   . PHE   A 1 205 ? -5.167  -1.139  16.053 1.00 88.42  ? 501 PHE   A O   1 
ATOM   1570 C  CB  . PHE   A 1 205 ? -7.400  -1.960  18.329 1.00 80.28  ? 501 PHE   A CB  1 
ATOM   1571 C  CG  . PHE   A 1 205 ? -8.131  -2.022  17.022 1.00 90.76  ? 501 PHE   A CG  1 
ATOM   1572 C  CD1 . PHE   A 1 205 ? -8.249  -3.224  16.341 1.00 95.54  ? 501 PHE   A CD1 1 
ATOM   1573 C  CD2 . PHE   A 1 205 ? -8.667  -0.875  16.453 1.00 93.90  ? 501 PHE   A CD2 1 
ATOM   1574 C  CE1 . PHE   A 1 205 ? -8.904  -3.289  15.123 1.00 94.87  ? 501 PHE   A CE1 1 
ATOM   1575 C  CE2 . PHE   A 1 205 ? -9.324  -0.934  15.244 1.00 96.66  ? 501 PHE   A CE2 1 
ATOM   1576 C  CZ  . PHE   A 1 205 ? -9.439  -2.143  14.575 1.00 95.30  ? 501 PHE   A CZ  1 
ATOM   1577 N  N   . THR   A 1 206 ? -5.264  0.305   17.782 1.00 88.71  ? 502 THR   A N   1 
ATOM   1578 C  CA  . THR   A 1 206 ? -4.708  1.402   17.002 1.00 89.30  ? 502 THR   A CA  1 
ATOM   1579 C  C   . THR   A 1 206 ? -3.315  1.050   16.491 1.00 97.95  ? 502 THR   A C   1 
ATOM   1580 O  O   . THR   A 1 206 ? -2.943  1.420   15.370 1.00 99.17  ? 502 THR   A O   1 
ATOM   1581 C  CB  . THR   A 1 206 ? -4.682  2.676   17.851 1.00 84.98  ? 502 THR   A CB  1 
ATOM   1582 O  OG1 . THR   A 1 206 ? -6.006  2.962   18.321 1.00 88.42  ? 502 THR   A OG1 1 
ATOM   1583 C  CG2 . THR   A 1 206 ? -4.160  3.875   17.058 1.00 80.62  ? 502 THR   A CG2 1 
ATOM   1584 N  N   . GLU   A 1 207 ? -2.540  0.314   17.290 1.00 103.38 ? 503 GLU   A N   1 
ATOM   1585 C  CA  . GLU   A 1 207 ? -1.204  -0.087  16.861 1.00 112.11 ? 503 GLU   A CA  1 
ATOM   1586 C  C   . GLU   A 1 207 ? -1.265  -1.132  15.761 1.00 107.33 ? 503 GLU   A C   1 
ATOM   1587 O  O   . GLU   A 1 207 ? -0.473  -1.086  14.811 1.00 114.14 ? 503 GLU   A O   1 
ATOM   1588 C  CB  . GLU   A 1 207 ? -0.407  -0.614  18.050 1.00 120.75 ? 503 GLU   A CB  1 
ATOM   1589 C  CG  . GLU   A 1 207 ? 0.511   0.420   18.655 1.00 133.60 ? 503 GLU   A CG  1 
ATOM   1590 C  CD  . GLU   A 1 207 ? 0.592   0.318   20.161 1.00 141.70 ? 503 GLU   A CD  1 
ATOM   1591 O  OE1 . GLU   A 1 207 ? 0.456   -0.805  20.689 1.00 142.40 ? 503 GLU   A OE1 1 
ATOM   1592 O  OE2 . GLU   A 1 207 ? 0.781   1.366   20.816 1.00 145.41 ? 503 GLU   A OE2 1 
ATOM   1593 N  N   . ILE   A 1 208 ? -2.186  -2.090  15.881 1.00 101.08 ? 504 ILE   A N   1 
ATOM   1594 C  CA  . ILE   A 1 208 ? -2.323  -3.127  14.862 1.00 103.44 ? 504 ILE   A CA  1 
ATOM   1595 C  C   . ILE   A 1 208 ? -2.642  -2.496  13.515 1.00 101.01 ? 504 ILE   A C   1 
ATOM   1596 O  O   . ILE   A 1 208 ? -2.034  -2.830  12.495 1.00 99.16  ? 504 ILE   A O   1 
ATOM   1597 C  CB  . ILE   A 1 208 ? -3.397  -4.149  15.270 1.00 100.14 ? 504 ILE   A CB  1 
ATOM   1598 C  CG1 . ILE   A 1 208 ? -3.014  -4.825  16.582 1.00 103.45 ? 504 ILE   A CG1 1 
ATOM   1599 C  CG2 . ILE   A 1 208 ? -3.561  -5.194  14.180 1.00 99.46  ? 504 ILE   A CG2 1 
ATOM   1600 C  CD1 . ILE   A 1 208 ? -4.175  -5.492  17.301 1.00 104.50 ? 504 ILE   A CD1 1 
ATOM   1601 N  N   . CYS   A 1 209 ? -3.593  -1.556  13.502 1.00 100.52 ? 505 CYS   A N   1 
ATOM   1602 C  CA  . CYS   A 1 209 ? -3.915  -0.816  12.289 1.00 100.72 ? 505 CYS   A CA  1 
ATOM   1603 C  C   . CYS   A 1 209 ? -2.682  -0.134  11.711 1.00 110.52 ? 505 CYS   A C   1 
ATOM   1604 O  O   . CYS   A 1 209 ? -2.511  -0.077  10.485 1.00 110.67 ? 505 CYS   A O   1 
ATOM   1605 C  CB  . CYS   A 1 209 ? -5.011  0.211   12.580 1.00 93.80  ? 505 CYS   A CB  1 
ATOM   1606 S  SG  . CYS   A 1 209 ? -6.605  -0.520  13.005 1.00 88.84  ? 505 CYS   A SG  1 
ATOM   1607 N  N   . ILE   A 1 210 ? -1.798  0.375   12.577 1.00 111.78 ? 506 ILE   A N   1 
ATOM   1608 C  CA  . ILE   A 1 210 ? -0.578  1.007   12.082 1.00 117.33 ? 506 ILE   A CA  1 
ATOM   1609 C  C   . ILE   A 1 210 ? 0.372   -0.040  11.509 1.00 120.65 ? 506 ILE   A C   1 
ATOM   1610 O  O   . ILE   A 1 210 ? 0.992   0.172   10.457 1.00 117.24 ? 506 ILE   A O   1 
ATOM   1611 C  CB  . ILE   A 1 210 ? 0.088   1.833   13.195 1.00 116.42 ? 506 ILE   A CB  1 
ATOM   1612 C  CG1 . ILE   A 1 210 ? -0.817  2.987   13.620 1.00 113.77 ? 506 ILE   A CG1 1 
ATOM   1613 C  CG2 . ILE   A 1 210 ? 1.413   2.387   12.720 1.00 126.32 ? 506 ILE   A CG2 1 
ATOM   1614 C  CD1 . ILE   A 1 210 ? -0.431  3.573   14.982 1.00 117.88 ? 506 ILE   A CD1 1 
ATOM   1615 N  N   . GLN   A 1 211 ? 0.494   -1.188  12.184 1.00 121.28 ? 507 GLN   A N   1 
ATOM   1616 C  CA  . GLN   A 1 211 ? 1.336   -2.271  11.683 1.00 125.98 ? 507 GLN   A CA  1 
ATOM   1617 C  C   . GLN   A 1 211 ? 0.837   -2.830  10.353 1.00 120.09 ? 507 GLN   A C   1 
ATOM   1618 O  O   . GLN   A 1 211 ? 1.636   -3.381  9.586  1.00 120.00 ? 507 GLN   A O   1 
ATOM   1619 C  CB  . GLN   A 1 211 ? 1.430   -3.384  12.736 1.00 128.23 ? 507 GLN   A CB  1 
ATOM   1620 C  CG  . GLN   A 1 211 ? 2.329   -4.563  12.344 1.00 134.65 ? 507 GLN   A CG  1 
ATOM   1621 C  CD  . GLN   A 1 211 ? 3.281   -4.996  13.453 1.00 139.43 ? 507 GLN   A CD  1 
ATOM   1622 O  OE1 . GLN   A 1 211 ? 3.751   -4.177  14.243 1.00 143.49 ? 507 GLN   A OE1 1 
ATOM   1623 N  NE2 . GLN   A 1 211 ? 3.574   -6.294  13.507 1.00 138.42 ? 507 GLN   A NE2 1 
ATOM   1624 N  N   . GLN   A 1 212 ? -0.457  -2.709  10.060 1.00 116.64 ? 508 GLN   A N   1 
ATOM   1625 C  CA  . GLN   A 1 212 ? -0.988  -3.088  8.754  1.00 114.11 ? 508 GLN   A CA  1 
ATOM   1626 C  C   . GLN   A 1 212 ? -0.999  -1.927  7.773  1.00 114.50 ? 508 GLN   A C   1 
ATOM   1627 O  O   . GLN   A 1 212 ? -1.418  -2.110  6.625  1.00 109.23 ? 508 GLN   A O   1 
ATOM   1628 C  CB  . GLN   A 1 212 ? -2.403  -3.653  8.886  1.00 110.15 ? 508 GLN   A CB  1 
ATOM   1629 C  CG  . GLN   A 1 212 ? -2.536  -4.784  9.896  1.00 117.03 ? 508 GLN   A CG  1 
ATOM   1630 C  CD  . GLN   A 1 212 ? -1.887  -6.081  9.433  1.00 124.79 ? 508 GLN   A CD  1 
ATOM   1631 O  OE1 . GLN   A 1 212 ? -2.575  -7.029  9.049  1.00 127.91 ? 508 GLN   A OE1 1 
ATOM   1632 N  NE2 . GLN   A 1 212 ? -0.564  -6.133  9.482  1.00 129.75 ? 508 GLN   A NE2 1 
ATOM   1633 N  N   . GLY   A 1 213 ? -0.572  -0.746  8.199  1.00 118.38 ? 509 GLY   A N   1 
ATOM   1634 C  CA  . GLY   A 1 213 ? -0.404  0.384   7.322  1.00 123.31 ? 509 GLY   A CA  1 
ATOM   1635 C  C   . GLY   A 1 213 ? -1.324  1.570   7.529  1.00 122.79 ? 509 GLY   A C   1 
ATOM   1636 O  O   . GLY   A 1 213 ? -1.498  2.356   6.588  1.00 120.86 ? 509 GLY   A O   1 
ATOM   1637 N  N   . TRP   A 1 214 ? -1.921  1.729   8.702  1.00 129.70 ? 510 TRP   A N   1 
ATOM   1638 C  CA  . TRP   A 1 214 ? -2.703  2.934   8.925  1.00 124.38 ? 510 TRP   A CA  1 
ATOM   1639 C  C   . TRP   A 1 214 ? -1.778  4.136   9.043  1.00 127.09 ? 510 TRP   A C   1 
ATOM   1640 O  O   . TRP   A 1 214 ? -0.631  4.031   9.491  1.00 132.15 ? 510 TRP   A O   1 
ATOM   1641 C  CB  . TRP   A 1 214 ? -3.568  2.826   10.185 1.00 117.92 ? 510 TRP   A CB  1 
ATOM   1642 C  CG  . TRP   A 1 214 ? -4.703  3.827   10.191 1.00 113.28 ? 510 TRP   A CG  1 
ATOM   1643 C  CD1 . TRP   A 1 214 ? -5.490  4.168   9.131  1.00 108.97 ? 510 TRP   A CD1 1 
ATOM   1644 C  CD2 . TRP   A 1 214 ? -5.151  4.631   11.296 1.00 113.85 ? 510 TRP   A CD2 1 
ATOM   1645 N  NE1 . TRP   A 1 214 ? -6.413  5.112   9.508  1.00 108.14 ? 510 TRP   A NE1 1 
ATOM   1646 C  CE2 . TRP   A 1 214 ? -6.223  5.421   10.828 1.00 108.88 ? 510 TRP   A CE2 1 
ATOM   1647 C  CE3 . TRP   A 1 214 ? -4.754  4.754   12.633 1.00 116.53 ? 510 TRP   A CE3 1 
ATOM   1648 C  CZ2 . TRP   A 1 214 ? -6.905  6.320   11.650 1.00 109.66 ? 510 TRP   A CZ2 1 
ATOM   1649 C  CZ3 . TRP   A 1 214 ? -5.434  5.649   13.451 1.00 114.99 ? 510 TRP   A CZ3 1 
ATOM   1650 C  CH2 . TRP   A 1 214 ? -6.497  6.418   12.956 1.00 113.97 ? 510 TRP   A CH2 1 
ATOM   1651 N  N   . LYS   A 1 215 ? -2.285  5.284   8.620  1.00 120.72 ? 511 LYS   A N   1 
ATOM   1652 C  CA  . LYS   A 1 215 ? -1.613  6.560   8.830  1.00 124.31 ? 511 LYS   A CA  1 
ATOM   1653 C  C   . LYS   A 1 215 ? -2.441  7.350   9.833  1.00 116.07 ? 511 LYS   A C   1 
ATOM   1654 O  O   . LYS   A 1 215 ? -3.513  7.868   9.499  1.00 113.27 ? 511 LYS   A O   1 
ATOM   1655 C  CB  . LYS   A 1 215 ? -1.421  7.311   7.515  1.00 127.71 ? 511 LYS   A CB  1 
ATOM   1656 C  CG  . LYS   A 1 215 ? -0.224  6.810   6.700  1.00 133.26 ? 511 LYS   A CG  1 
ATOM   1657 C  CD  . LYS   A 1 215 ? 1.022   7.693   6.888  1.00 141.92 ? 511 LYS   A CD  1 
ATOM   1658 C  CE  . LYS   A 1 215 ? 1.651   7.566   8.282  1.00 145.19 ? 511 LYS   A CE  1 
ATOM   1659 N  NZ  . LYS   A 1 215 ? 2.720   8.574   8.542  1.00 150.41 ? 511 LYS   A NZ  1 
ATOM   1660 N  N   . ALA   A 1 216 ? -1.953  7.421   11.046 1.00 111.29 ? 512 ALA   A N   1 
ATOM   1661 C  CA  . ALA   A 1 216 ? -2.751  7.928   12.150 1.00 109.23 ? 512 ALA   A CA  1 
ATOM   1662 C  C   . ALA   A 1 216 ? -2.698  9.452   12.190 1.00 115.68 ? 512 ALA   A C   1 
ATOM   1663 O  O   . ALA   A 1 216 ? -1.603  10.028  12.154 1.00 121.30 ? 512 ALA   A O   1 
ATOM   1664 C  CB  . ALA   A 1 216 ? -2.252  7.353   13.467 1.00 106.05 ? 512 ALA   A CB  1 
ATOM   1665 N  N   . PRO   A 1 217 ? -3.854  10.137  12.248 1.00 109.83 ? 513 PRO   A N   1 
ATOM   1666 C  CA  . PRO   A 1 217 ? -3.847  11.590  12.487 1.00 113.06 ? 513 PRO   A CA  1 
ATOM   1667 C  C   . PRO   A 1 217 ? -3.603  11.938  13.945 1.00 124.49 ? 513 PRO   A C   1 
ATOM   1668 O  O   . PRO   A 1 217 ? -4.228  12.868  14.465 1.00 130.15 ? 513 PRO   A O   1 
ATOM   1669 C  CB  . PRO   A 1 217 ? -5.251  12.029  12.046 1.00 109.24 ? 513 PRO   A CB  1 
ATOM   1670 C  CG  . PRO   A 1 217 ? -6.088  10.806  12.100 1.00 101.59 ? 513 PRO   A CG  1 
ATOM   1671 C  CD  . PRO   A 1 217 ? -5.185  9.634   11.862 1.00 103.47 ? 513 PRO   A CD  1 
ATOM   1672 N  N   . ARG   A 1 218 ? -2.678  11.207  14.583 1.00 129.92 ? 514 ARG   A N   1 
ATOM   1673 C  CA  . ARG   A 1 218 ? -2.446  11.162  16.028 1.00 122.13 ? 514 ARG   A CA  1 
ATOM   1674 C  C   . ARG   A 1 218 ? -3.006  12.356  16.793 1.00 118.94 ? 514 ARG   A C   1 
ATOM   1675 O  O   . ARG   A 1 218 ? -2.257  13.212  17.277 1.00 126.93 ? 514 ARG   A O   1 
ATOM   1676 C  CB  . ARG   A 1 218 ? -0.949  11.008  16.305 1.00 126.36 ? 514 ARG   A CB  1 
ATOM   1677 C  CG  . ARG   A 1 218 ? -0.373  9.715   15.747 1.00 128.34 ? 514 ARG   A CG  1 
ATOM   1678 C  CD  . ARG   A 1 218 ? 1.010   9.439   16.300 1.00 137.49 ? 514 ARG   A CD  1 
ATOM   1679 N  NE  . ARG   A 1 218 ? 1.102   8.090   16.853 1.00 139.86 ? 514 ARG   A NE  1 
ATOM   1680 C  CZ  . ARG   A 1 218 ? 1.833   7.107   16.337 1.00 143.55 ? 514 ARG   A CZ  1 
ATOM   1681 N  NH1 . ARG   A 1 218 ? 1.841   5.913   16.914 1.00 143.63 ? 514 ARG   A NH1 1 
ATOM   1682 N  NH2 . ARG   A 1 218 ? 2.565   7.316   15.255 1.00 148.10 ? 514 ARG   A NH2 1 
ATOM   1683 N  N   . GLY   A 1 219 ? -4.337  12.416  16.876 1.00 112.42 ? 515 GLY   A N   1 
ATOM   1684 C  CA  . GLY   A 1 219 ? -5.048  13.318  17.760 1.00 112.99 ? 515 GLY   A CA  1 
ATOM   1685 C  C   . GLY   A 1 219 ? -5.990  12.560  18.679 1.00 109.94 ? 515 GLY   A C   1 
ATOM   1686 O  O   . GLY   A 1 219 ? -5.737  11.401  19.025 1.00 102.42 ? 515 GLY   A O   1 
ATOM   1687 N  N   . ARG   A 1 220 ? -7.100  13.185  19.062 1.00 113.86 ? 516 ARG   A N   1 
ATOM   1688 C  CA  . ARG   A 1 220 ? -8.007  12.566  20.020 1.00 111.20 ? 516 ARG   A CA  1 
ATOM   1689 C  C   . ARG   A 1 220 ? -9.054  11.703  19.343 1.00 111.27 ? 516 ARG   A C   1 
ATOM   1690 O  O   . ARG   A 1 220 ? -8.911  10.480  19.237 1.00 110.25 ? 516 ARG   A O   1 
ATOM   1691 C  CB  . ARG   A 1 220 ? -8.723  13.630  20.840 1.00 114.35 ? 516 ARG   A CB  1 
ATOM   1692 C  CG  . ARG   A 1 220 ? -9.169  13.148  22.184 1.00 110.19 ? 516 ARG   A CG  1 
ATOM   1693 C  CD  . ARG   A 1 220 ? -8.345  13.836  23.237 1.00 113.45 ? 516 ARG   A CD  1 
ATOM   1694 N  NE  . ARG   A 1 220 ? -9.175  14.705  24.057 1.00 113.62 ? 516 ARG   A NE  1 
ATOM   1695 C  CZ  . ARG   A 1 220 ? -9.446  14.475  25.332 1.00 114.65 ? 516 ARG   A CZ  1 
ATOM   1696 N  NH1 . ARG   A 1 220 ? -8.926  13.414  25.931 1.00 117.05 ? 516 ARG   A NH1 1 
ATOM   1697 N  NH2 . ARG   A 1 220 ? -10.222 15.308  26.010 1.00 115.84 ? 516 ARG   A NH2 1 
ATOM   1698 N  N   . PHE   A 1 221 ? -10.113 12.364  18.880 1.00 109.90 ? 517 PHE   A N   1 
ATOM   1699 C  CA  . PHE   A 1 221 ? -11.317 11.707  18.388 1.00 102.12 ? 517 PHE   A CA  1 
ATOM   1700 C  C   . PHE   A 1 221 ? -11.159 11.321  16.910 1.00 108.14 ? 517 PHE   A C   1 
ATOM   1701 O  O   . PHE   A 1 221 ? -11.955 11.667  16.033 1.00 109.68 ? 517 PHE   A O   1 
ATOM   1702 C  CB  . PHE   A 1 221 ? -12.519 12.611  18.641 1.00 95.79  ? 517 PHE   A CB  1 
ATOM   1703 C  CG  . PHE   A 1 221 ? -12.755 12.938  20.115 1.00 90.71  ? 517 PHE   A CG  1 
ATOM   1704 C  CD1 . PHE   A 1 221 ? -12.568 14.221  20.599 1.00 92.56  ? 517 PHE   A CD1 1 
ATOM   1705 C  CD2 . PHE   A 1 221 ? -13.171 11.960  21.000 1.00 80.61  ? 517 PHE   A CD2 1 
ATOM   1706 C  CE1 . PHE   A 1 221 ? -12.790 14.521  21.931 1.00 92.71  ? 517 PHE   A CE1 1 
ATOM   1707 C  CE2 . PHE   A 1 221 ? -13.403 12.258  22.329 1.00 79.03  ? 517 PHE   A CE2 1 
ATOM   1708 C  CZ  . PHE   A 1 221 ? -13.207 13.538  22.799 1.00 80.97  ? 517 PHE   A CZ  1 
ATOM   1709 N  N   . ASP   A 1 222 ? -10.095 10.562  16.657 1.00 106.00 ? 518 ASP   A N   1 
ATOM   1710 C  CA  . ASP   A 1 222 ? -9.781  10.043  15.334 1.00 94.40  ? 518 ASP   A CA  1 
ATOM   1711 C  C   . ASP   A 1 222 ? -10.510 8.719   15.138 1.00 96.89  ? 518 ASP   A C   1 
ATOM   1712 O  O   . ASP   A 1 222 ? -10.217 7.740   15.832 1.00 101.75 ? 518 ASP   A O   1 
ATOM   1713 C  CB  . ASP   A 1 222 ? -8.272  9.853   15.177 1.00 89.85  ? 518 ASP   A CB  1 
ATOM   1714 C  CG  . ASP   A 1 222 ? -7.479  11.132  15.437 1.00 97.14  ? 518 ASP   A CG  1 
ATOM   1715 O  OD1 . ASP   A 1 222 ? -8.098  12.196  15.673 1.00 99.68  ? 518 ASP   A OD1 1 
ATOM   1716 O  OD2 . ASP   A 1 222 ? -6.227  11.070  15.405 1.00 100.61 ? 518 ASP   A OD2 1 
ATOM   1717 N  N   . VAL   A 1 223 ? -11.460 8.694   14.205 1.00 91.18  ? 519 VAL   A N   1 
ATOM   1718 C  CA  . VAL   A 1 223 ? -12.219 7.480   13.909 1.00 84.50  ? 519 VAL   A CA  1 
ATOM   1719 C  C   . VAL   A 1 223 ? -11.273 6.434   13.337 1.00 84.79  ? 519 VAL   A C   1 
ATOM   1720 O  O   . VAL   A 1 223 ? -10.633 6.661   12.304 1.00 84.21  ? 519 VAL   A O   1 
ATOM   1721 C  CB  . VAL   A 1 223 ? -13.366 7.772   12.926 1.00 85.46  ? 519 VAL   A CB  1 
ATOM   1722 C  CG1 . VAL   A 1 223 ? -14.235 6.538   12.744 1.00 80.95  ? 519 VAL   A CG1 1 
ATOM   1723 C  CG2 . VAL   A 1 223 ? -14.197 8.969   13.378 1.00 83.43  ? 519 VAL   A CG2 1 
ATOM   1724 N  N   . LEU   A 1 224 ? -11.206 5.274   13.982 1.00 77.66  ? 520 LEU   A N   1 
ATOM   1725 C  CA  . LEU   A 1 224 ? -10.311 4.240   13.506 1.00 79.85  ? 520 LEU   A CA  1 
ATOM   1726 C  C   . LEU   A 1 224 ? -10.806 3.673   12.181 1.00 82.03  ? 520 LEU   A C   1 
ATOM   1727 O  O   . LEU   A 1 224 ? -11.990 3.767   11.854 1.00 83.80  ? 520 LEU   A O   1 
ATOM   1728 C  CB  . LEU   A 1 224 ? -10.190 3.103   14.513 1.00 68.00  ? 520 LEU   A CB  1 
ATOM   1729 C  CG  . LEU   A 1 224 ? -9.430  3.383   15.818 1.00 71.60  ? 520 LEU   A CG  1 
ATOM   1730 C  CD1 . LEU   A 1 224 ? -10.176 2.660   16.895 1.00 61.71  ? 520 LEU   A CD1 1 
ATOM   1731 C  CD2 . LEU   A 1 224 ? -7.974  2.907   15.755 1.00 73.30  ? 520 LEU   A CD2 1 
ATOM   1732 N  N   . PRO   A 1 225 ? -9.916  3.065   11.407 1.00 82.29  ? 521 PRO   A N   1 
ATOM   1733 C  CA  . PRO   A 1 225 ? -10.338 2.374   10.190 1.00 83.69  ? 521 PRO   A CA  1 
ATOM   1734 C  C   . PRO   A 1 225 ? -10.804 0.965   10.522 1.00 80.33  ? 521 PRO   A C   1 
ATOM   1735 O  O   . PRO   A 1 225 ? -10.446 0.396   11.554 1.00 82.02  ? 521 PRO   A O   1 
ATOM   1736 C  CB  . PRO   A 1 225 ? -9.052  2.346   9.355  1.00 88.79  ? 521 PRO   A CB  1 
ATOM   1737 C  CG  . PRO   A 1 225 ? -7.977  2.237   10.385 1.00 90.94  ? 521 PRO   A CG  1 
ATOM   1738 C  CD  . PRO   A 1 225 ? -8.452  3.009   11.590 1.00 84.59  ? 521 PRO   A CD  1 
ATOM   1739 N  N   . LEU   A 1 226 ? -11.621 0.415   9.629  1.00 76.12  ? 522 LEU   A N   1 
ATOM   1740 C  CA  . LEU   A 1 226 ? -12.098 -0.949  9.796  1.00 72.79  ? 522 LEU   A CA  1 
ATOM   1741 C  C   . LEU   A 1 226 ? -11.001 -1.938  9.434  1.00 73.74  ? 522 LEU   A C   1 
ATOM   1742 O  O   . LEU   A 1 226 ? -10.278 -1.742  8.460  1.00 72.29  ? 522 LEU   A O   1 
ATOM   1743 C  CB  . LEU   A 1 226 ? -13.333 -1.201  8.933  1.00 64.59  ? 522 LEU   A CB  1 
ATOM   1744 C  CG  . LEU   A 1 226 ? -14.568 -0.367  9.286  1.00 70.43  ? 522 LEU   A CG  1 
ATOM   1745 C  CD1 . LEU   A 1 226 ? -15.650 -0.498  8.206  1.00 71.88  ? 522 LEU   A CD1 1 
ATOM   1746 C  CD2 . LEU   A 1 226 ? -15.120 -0.734  10.681 1.00 61.77  ? 522 LEU   A CD2 1 
ATOM   1747 N  N   . LEU   A 1 227 ? -10.866 -2.995  10.240 1.00 74.35  ? 523 LEU   A N   1 
ATOM   1748 C  CA  . LEU   A 1 227 ? -9.950  -4.107  9.965  1.00 77.53  ? 523 LEU   A CA  1 
ATOM   1749 C  C   . LEU   A 1 227 ? -10.806 -5.344  9.715  1.00 74.89  ? 523 LEU   A C   1 
ATOM   1750 O  O   . LEU   A 1 227 ? -11.281 -5.982  10.656 1.00 71.02  ? 523 LEU   A O   1 
ATOM   1751 C  CB  . LEU   A 1 227 ? -8.974  -4.339  11.114 1.00 75.00  ? 523 LEU   A CB  1 
ATOM   1752 C  CG  . LEU   A 1 227 ? -7.472  -4.238  10.835 1.00 82.01  ? 523 LEU   A CG  1 
ATOM   1753 C  CD1 . LEU   A 1 227 ? -6.703  -5.008  11.898 1.00 84.95  ? 523 LEU   A CD1 1 
ATOM   1754 C  CD2 . LEU   A 1 227 ? -7.064  -4.675  9.426  1.00 75.93  ? 523 LEU   A CD2 1 
ATOM   1755 N  N   . LEU   A 1 228 ? -10.981 -5.690  8.442  1.00 74.63  ? 524 LEU   A N   1 
ATOM   1756 C  CA  . LEU   A 1 228 ? -11.931 -6.710  8.027  1.00 70.61  ? 524 LEU   A CA  1 
ATOM   1757 C  C   . LEU   A 1 228 ? -11.175 -7.921  7.504  1.00 70.23  ? 524 LEU   A C   1 
ATOM   1758 O  O   . LEU   A 1 228 ? -10.398 -7.806  6.549  1.00 62.57  ? 524 LEU   A O   1 
ATOM   1759 C  CB  . LEU   A 1 228 ? -12.879 -6.159  6.965  1.00 67.79  ? 524 LEU   A CB  1 
ATOM   1760 C  CG  . LEU   A 1 228 ? -13.481 -4.823  7.392  1.00 62.59  ? 524 LEU   A CG  1 
ATOM   1761 C  CD1 . LEU   A 1 228 ? -14.285 -4.269  6.261  1.00 55.01  ? 524 LEU   A CD1 1 
ATOM   1762 C  CD2 . LEU   A 1 228 ? -14.344 -4.971  8.659  1.00 55.51  ? 524 LEU   A CD2 1 
ATOM   1763 N  N   . GLN   A 1 229 ? -11.405 -9.066  8.137  1.00 69.35  ? 525 GLN   A N   1 
ATOM   1764 C  CA  . GLN   A 1 229 ? -10.875 -10.354 7.714  1.00 76.91  ? 525 GLN   A CA  1 
ATOM   1765 C  C   . GLN   A 1 229 ? -12.006 -11.146 7.062  1.00 77.40  ? 525 GLN   A C   1 
ATOM   1766 O  O   . GLN   A 1 229 ? -13.054 -11.357 7.682  1.00 76.56  ? 525 GLN   A O   1 
ATOM   1767 C  CB  . GLN   A 1 229 ? -10.295 -11.111 8.911  1.00 73.97  ? 525 GLN   A CB  1 
ATOM   1768 C  CG  . GLN   A 1 229 ? -10.280 -12.608 8.735  1.00 73.35  ? 525 GLN   A CG  1 
ATOM   1769 C  CD  . GLN   A 1 229 ? -9.785  -13.352 9.944  1.00 77.04  ? 525 GLN   A CD  1 
ATOM   1770 O  OE1 . GLN   A 1 229 ? -9.632  -12.789 11.037 1.00 81.91  ? 525 GLN   A OE1 1 
ATOM   1771 N  NE2 . GLN   A 1 229 ? -9.537  -14.640 9.763  1.00 74.95  ? 525 GLN   A NE2 1 
ATOM   1772 N  N   . ALA   A 1 230 ? -11.807 -11.576 5.815  1.00 76.29  ? 526 ALA   A N   1 
ATOM   1773 C  CA  . ALA   A 1 230 ? -12.814 -12.350 5.097  1.00 74.20  ? 526 ALA   A CA  1 
ATOM   1774 C  C   . ALA   A 1 230 ? -12.287 -13.753 4.814  1.00 70.88  ? 526 ALA   A C   1 
ATOM   1775 O  O   . ALA   A 1 230 ? -11.126 -13.915 4.421  1.00 68.11  ? 526 ALA   A O   1 
ATOM   1776 C  CB  . ALA   A 1 230 ? -13.221 -11.660 3.793  1.00 74.18  ? 526 ALA   A CB  1 
ATOM   1777 N  N   . ASN   A 1 231 ? -13.134 -14.758 5.054  1.00 71.16  ? 527 ASN   A N   1 
ATOM   1778 C  CA  . ASN   A 1 231 ? -12.851 -16.164 4.744  1.00 80.03  ? 527 ASN   A CA  1 
ATOM   1779 C  C   . ASN   A 1 231 ? -11.492 -16.602 5.292  1.00 82.16  ? 527 ASN   A C   1 
ATOM   1780 O  O   . ASN   A 1 231 ? -10.725 -17.315 4.643  1.00 79.61  ? 527 ASN   A O   1 
ATOM   1781 C  CB  . ASN   A 1 231 ? -12.955 -16.415 3.235  1.00 89.49  ? 527 ASN   A CB  1 
ATOM   1782 C  CG  . ASN   A 1 231 ? -12.955 -17.891 2.880  1.00 98.05  ? 527 ASN   A CG  1 
ATOM   1783 O  OD1 . ASN   A 1 231 ? -11.972 -18.405 2.338  1.00 104.40 ? 527 ASN   A OD1 1 
ATOM   1784 N  ND2 . ASN   A 1 231 ? -14.050 -18.576 3.176  1.00 96.22  ? 527 ASN   A ND2 1 
ATOM   1785 N  N   . GLY   A 1 232 ? -11.193 -16.171 6.515  1.00 88.98  ? 528 GLY   A N   1 
ATOM   1786 C  CA  . GLY   A 1 232 ? -9.918  -16.488 7.125  1.00 95.38  ? 528 GLY   A CA  1 
ATOM   1787 C  C   . GLY   A 1 232 ? -8.716  -15.737 6.585  1.00 102.53 ? 528 GLY   A C   1 
ATOM   1788 O  O   . GLY   A 1 232 ? -7.622  -15.890 7.142  1.00 111.01 ? 528 GLY   A O   1 
ATOM   1789 N  N   . ASN   A 1 233 ? -8.870  -14.925 5.536  1.00 92.02  ? 529 ASN   A N   1 
ATOM   1790 C  CA  . ASN   A 1 233 ? -7.728  -14.224 4.957  1.00 91.21  ? 529 ASN   A CA  1 
ATOM   1791 C  C   . ASN   A 1 233 ? -7.243  -13.094 5.868  1.00 91.28  ? 529 ASN   A C   1 
ATOM   1792 O  O   . ASN   A 1 233 ? -7.982  -12.560 6.698  1.00 94.31  ? 529 ASN   A O   1 
ATOM   1793 C  CB  . ASN   A 1 233 ? -8.072  -13.657 3.577  1.00 84.19  ? 529 ASN   A CB  1 
ATOM   1794 C  CG  . ASN   A 1 233 ? -8.020  -14.710 2.485  1.00 83.15  ? 529 ASN   A CG  1 
ATOM   1795 O  OD1 . ASN   A 1 233 ? -7.059  -14.773 1.710  1.00 94.30  ? 529 ASN   A OD1 1 
ATOM   1796 N  ND2 . ASN   A 1 233 ? -9.057  -15.539 2.410  1.00 71.18  ? 529 ASN   A ND2 1 
ATOM   1797 N  N   . ASP   A 1 234 ? -5.974  -12.732 5.699  1.00 93.09  ? 530 ASP   A N   1 
ATOM   1798 C  CA  . ASP   A 1 234 ? -5.385  -11.663 6.496  1.00 100.09 ? 530 ASP   A CA  1 
ATOM   1799 C  C   . ASP   A 1 234 ? -6.175  -10.367 6.301  1.00 99.14  ? 530 ASP   A C   1 
ATOM   1800 O  O   . ASP   A 1 234 ? -6.471  -9.992  5.157  1.00 105.33 ? 530 ASP   A O   1 
ATOM   1801 C  CB  . ASP   A 1 234 ? -3.910  -11.468 6.126  1.00 108.22 ? 530 ASP   A CB  1 
ATOM   1802 C  CG  . ASP   A 1 234 ? -3.076  -12.742 6.315  1.00 116.41 ? 530 ASP   A CG  1 
ATOM   1803 O  OD1 . ASP   A 1 234 ? -2.097  -12.937 5.562  1.00 123.25 ? 530 ASP   A OD1 1 
ATOM   1804 O  OD2 . ASP   A 1 234 ? -3.402  -13.561 7.199  1.00 118.04 ? 530 ASP   A OD2 1 
ATOM   1805 N  N   . PRO   A 1 235 ? -6.530  -9.661  7.375  1.00 90.90  ? 531 PRO   A N   1 
ATOM   1806 C  CA  . PRO   A 1 235 ? -7.497  -8.566  7.256  1.00 84.66  ? 531 PRO   A CA  1 
ATOM   1807 C  C   . PRO   A 1 235 ? -6.909  -7.333  6.591  1.00 82.82  ? 531 PRO   A C   1 
ATOM   1808 O  O   . PRO   A 1 235 ? -5.694  -7.169  6.466  1.00 88.94  ? 531 PRO   A O   1 
ATOM   1809 C  CB  . PRO   A 1 235 ? -7.875  -8.276  8.713  1.00 82.25  ? 531 PRO   A CB  1 
ATOM   1810 C  CG  . PRO   A 1 235 ? -6.638  -8.577  9.446  1.00 82.80  ? 531 PRO   A CG  1 
ATOM   1811 C  CD  . PRO   A 1 235 ? -6.050  -9.797  8.762  1.00 88.65  ? 531 PRO   A CD  1 
ATOM   1812 N  N   . GLU   A 1 236 ? -7.811  -6.438  6.184  1.00 83.41  ? 532 GLU   A N   1 
ATOM   1813 C  CA  . GLU   A 1 236 ? -7.481  -5.311  5.317  1.00 83.90  ? 532 GLU   A CA  1 
ATOM   1814 C  C   . GLU   A 1 236 ? -8.151  -4.044  5.833  1.00 81.38  ? 532 GLU   A C   1 
ATOM   1815 O  O   . GLU   A 1 236 ? -9.271  -4.081  6.345  1.00 79.85  ? 532 GLU   A O   1 
ATOM   1816 C  CB  . GLU   A 1 236 ? -7.922  -5.575  3.863  1.00 79.44  ? 532 GLU   A CB  1 
ATOM   1817 C  CG  . GLU   A 1 236 ? -7.595  -6.969  3.372  1.00 77.89  ? 532 GLU   A CG  1 
ATOM   1818 C  CD  . GLU   A 1 236 ? -8.377  -7.359  2.128  1.00 81.85  ? 532 GLU   A CD  1 
ATOM   1819 O  OE1 . GLU   A 1 236 ? -8.982  -6.466  1.485  1.00 79.77  ? 532 GLU   A OE1 1 
ATOM   1820 O  OE2 . GLU   A 1 236 ? -8.388  -8.571  1.813  1.00 77.16  ? 532 GLU   A OE2 1 
ATOM   1821 N  N   . LEU   A 1 237 ? -7.473  -2.914  5.664  1.00 82.93  ? 533 LEU   A N   1 
ATOM   1822 C  CA  . LEU   A 1 237 ? -7.928  -1.656  6.241  1.00 85.01  ? 533 LEU   A CA  1 
ATOM   1823 C  C   . LEU   A 1 237 ? -8.857  -0.920  5.285  1.00 88.17  ? 533 LEU   A C   1 
ATOM   1824 O  O   . LEU   A 1 237 ? -8.602  -0.859  4.080  1.00 92.97  ? 533 LEU   A O   1 
ATOM   1825 C  CB  . LEU   A 1 237 ? -6.729  -0.774  6.594  1.00 84.15  ? 533 LEU   A CB  1 
ATOM   1826 C  CG  . LEU   A 1 237 ? -5.975  -1.233  7.845  1.00 80.10  ? 533 LEU   A CG  1 
ATOM   1827 C  CD1 . LEU   A 1 237 ? -4.511  -0.834  7.816  1.00 82.98  ? 533 LEU   A CD1 1 
ATOM   1828 C  CD2 . LEU   A 1 237 ? -6.640  -0.671  9.087  1.00 74.04  ? 533 LEU   A CD2 1 
ATOM   1829 N  N   . PHE   A 1 238 ? -9.943  -0.362  5.829  1.00 85.69  ? 534 PHE   A N   1 
ATOM   1830 C  CA  . PHE   A 1 238 ? -10.854 0.473   5.054  1.00 86.51  ? 534 PHE   A CA  1 
ATOM   1831 C  C   . PHE   A 1 238 ? -11.343 1.624   5.918  1.00 83.04  ? 534 PHE   A C   1 
ATOM   1832 O  O   . PHE   A 1 238 ? -11.641 1.439   7.100  1.00 82.43  ? 534 PHE   A O   1 
ATOM   1833 C  CB  . PHE   A 1 238 ? -12.078 -0.293  4.528  1.00 77.51  ? 534 PHE   A CB  1 
ATOM   1834 C  CG  . PHE   A 1 238 ? -11.752 -1.577  3.834  1.00 79.54  ? 534 PHE   A CG  1 
ATOM   1835 C  CD1 . PHE   A 1 238 ? -11.508 -2.731  4.568  1.00 81.15  ? 534 PHE   A CD1 1 
ATOM   1836 C  CD2 . PHE   A 1 238 ? -11.719 -1.642  2.453  1.00 79.37  ? 534 PHE   A CD2 1 
ATOM   1837 C  CE1 . PHE   A 1 238 ? -11.209 -3.918  3.928  1.00 83.90  ? 534 PHE   A CE1 1 
ATOM   1838 C  CE2 . PHE   A 1 238 ? -11.428 -2.829  1.811  1.00 76.00  ? 534 PHE   A CE2 1 
ATOM   1839 C  CZ  . PHE   A 1 238 ? -11.171 -3.969  2.541  1.00 73.85  ? 534 PHE   A CZ  1 
ATOM   1840 N  N   . GLN   A 1 239 ? -11.467 2.800   5.301  1.00 85.41  ? 535 GLN   A N   1 
ATOM   1841 C  CA  . GLN   A 1 239 ? -11.860 4.035   5.971  1.00 89.21  ? 535 GLN   A CA  1 
ATOM   1842 C  C   . GLN   A 1 239 ? -13.317 4.348   5.640  1.00 88.33  ? 535 GLN   A C   1 
ATOM   1843 O  O   . GLN   A 1 239 ? -13.637 4.721   4.504  1.00 91.83  ? 535 GLN   A O   1 
ATOM   1844 C  CB  . GLN   A 1 239 ? -10.933 5.174   5.551  1.00 99.41  ? 535 GLN   A CB  1 
ATOM   1845 C  CG  . GLN   A 1 239 ? -11.092 6.431   6.370  1.00 109.79 ? 535 GLN   A CG  1 
ATOM   1846 C  CD  . GLN   A 1 239 ? -11.595 7.588   5.543  1.00 115.60 ? 535 GLN   A CD  1 
ATOM   1847 O  OE1 . GLN   A 1 239 ? -12.646 8.157   5.829  1.00 118.02 ? 535 GLN   A OE1 1 
ATOM   1848 N  NE2 . GLN   A 1 239 ? -10.846 7.944   4.508  1.00 119.29 ? 535 GLN   A NE2 1 
ATOM   1849 N  N   . ILE   A 1 240 ? -14.194 4.180   6.628  1.00 85.28  ? 536 ILE   A N   1 
ATOM   1850 C  CA  . ILE   A 1 240 ? -15.597 4.583   6.554  1.00 82.57  ? 536 ILE   A CA  1 
ATOM   1851 C  C   . ILE   A 1 240 ? -15.658 6.021   6.069  1.00 87.78  ? 536 ILE   A C   1 
ATOM   1852 O  O   . ILE   A 1 240 ? -15.023 6.899   6.672  1.00 84.54  ? 536 ILE   A O   1 
ATOM   1853 C  CB  . ILE   A 1 240 ? -16.301 4.476   7.916  1.00 79.37  ? 536 ILE   A CB  1 
ATOM   1854 C  CG1 . ILE   A 1 240 ? -16.020 3.129   8.580  1.00 77.28  ? 536 ILE   A CG1 1 
ATOM   1855 C  CG2 . ILE   A 1 240 ? -17.801 4.733   7.783  1.00 71.27  ? 536 ILE   A CG2 1 
ATOM   1856 C  CD1 . ILE   A 1 240 ? -15.675 3.251   10.049 1.00 78.03  ? 536 ILE   A CD1 1 
ATOM   1857 N  N   . PRO   A 1 241 ? -16.402 6.306   5.005  1.00 79.15  ? 537 PRO   A N   1 
ATOM   1858 C  CA  . PRO   A 1 241 ? -16.511 7.680   4.525  1.00 80.59  ? 537 PRO   A CA  1 
ATOM   1859 C  C   . PRO   A 1 241 ? -16.999 8.586   5.640  1.00 79.27  ? 537 PRO   A C   1 
ATOM   1860 O  O   . PRO   A 1 241 ? -18.053 8.334   6.244  1.00 76.10  ? 537 PRO   A O   1 
ATOM   1861 C  CB  . PRO   A 1 241 ? -17.532 7.575   3.379  1.00 75.41  ? 537 PRO   A CB  1 
ATOM   1862 C  CG  . PRO   A 1 241 ? -17.463 6.139   2.963  1.00 67.43  ? 537 PRO   A CG  1 
ATOM   1863 C  CD  . PRO   A 1 241 ? -17.249 5.385   4.233  1.00 75.39  ? 537 PRO   A CD  1 
ATOM   1864 N  N   . PRO   A 1 242 ? -16.239 9.632   5.965  1.00 82.63  ? 538 PRO   A N   1 
ATOM   1865 C  CA  . PRO   A 1 242 ? -16.561 10.431  7.155  1.00 86.44  ? 538 PRO   A CA  1 
ATOM   1866 C  C   . PRO   A 1 242 ? -17.964 11.003  7.146  1.00 89.17  ? 538 PRO   A C   1 
ATOM   1867 O  O   . PRO   A 1 242 ? -18.463 11.393  8.209  1.00 96.69  ? 538 PRO   A O   1 
ATOM   1868 C  CB  . PRO   A 1 242 ? -15.502 11.539  7.121  1.00 87.59  ? 538 PRO   A CB  1 
ATOM   1869 C  CG  . PRO   A 1 242 ? -14.367 10.925  6.366  1.00 90.18  ? 538 PRO   A CG  1 
ATOM   1870 C  CD  . PRO   A 1 242 ? -15.021 10.112  5.298  1.00 86.66  ? 538 PRO   A CD  1 
ATOM   1871 N  N   . GLU   A 1 243 ? -18.625 11.057  5.988  1.00 74.52  ? 539 GLU   A N   1 
ATOM   1872 C  CA  . GLU   A 1 243 ? -20.005 11.521  5.961  1.00 78.84  ? 539 GLU   A CA  1 
ATOM   1873 C  C   . GLU   A 1 243 ? -20.952 10.500  6.579  1.00 78.40  ? 539 GLU   A C   1 
ATOM   1874 O  O   . GLU   A 1 243 ? -22.080 10.850  6.950  1.00 74.15  ? 539 GLU   A O   1 
ATOM   1875 C  CB  . GLU   A 1 243 ? -20.426 11.872  4.524  1.00 89.28  ? 539 GLU   A CB  1 
ATOM   1876 C  CG  . GLU   A 1 243 ? -20.418 10.711  3.526  1.00 90.05  ? 539 GLU   A CG  1 
ATOM   1877 C  CD  . GLU   A 1 243 ? -19.111 10.588  2.744  1.00 95.46  ? 539 GLU   A CD  1 
ATOM   1878 O  OE1 . GLU   A 1 243 ? -18.034 10.806  3.352  1.00 93.58  ? 539 GLU   A OE1 1 
ATOM   1879 O  OE2 . GLU   A 1 243 ? -19.160 10.274  1.522  1.00 91.58  ? 539 GLU   A OE2 1 
ATOM   1880 N  N   . LEU   A 1 244 ? -20.510 9.251   6.707  1.00 74.32  ? 540 LEU   A N   1 
ATOM   1881 C  CA  . LEU   A 1 244 ? -21.288 8.204   7.344  1.00 73.56  ? 540 LEU   A CA  1 
ATOM   1882 C  C   . LEU   A 1 244 ? -21.091 8.139   8.847  1.00 66.54  ? 540 LEU   A C   1 
ATOM   1883 O  O   . LEU   A 1 244 ? -21.917 7.519   9.525  1.00 69.55  ? 540 LEU   A O   1 
ATOM   1884 C  CB  . LEU   A 1 244 ? -20.915 6.842   6.756  1.00 71.99  ? 540 LEU   A CB  1 
ATOM   1885 C  CG  . LEU   A 1 244 ? -21.290 6.718   5.296  1.00 70.87  ? 540 LEU   A CG  1 
ATOM   1886 C  CD1 . LEU   A 1 244 ? -21.126 5.263   4.859  1.00 63.05  ? 540 LEU   A CD1 1 
ATOM   1887 C  CD2 . LEU   A 1 244 ? -22.716 7.257   5.076  1.00 63.41  ? 540 LEU   A CD2 1 
ATOM   1888 N  N   . VAL   A 1 245 ? -20.022 8.741   9.371  1.00 71.28  ? 541 VAL   A N   1 
ATOM   1889 C  CA  . VAL   A 1 245 ? -19.689 8.670   10.800 1.00 76.39  ? 541 VAL   A CA  1 
ATOM   1890 C  C   . VAL   A 1 245 ? -20.345 9.874   11.467 1.00 81.65  ? 541 VAL   A C   1 
ATOM   1891 O  O   . VAL   A 1 245 ? -19.801 10.984  11.449 1.00 65.73  ? 541 VAL   A O   1 
ATOM   1892 C  CB  . VAL   A 1 245 ? -18.176 8.660   11.041 1.00 81.23  ? 541 VAL   A CB  1 
ATOM   1893 C  CG1 . VAL   A 1 245 ? -17.866 8.273   12.497 1.00 78.29  ? 541 VAL   A CG1 1 
ATOM   1894 C  CG2 . VAL   A 1 245 ? -17.469 7.714   10.054 1.00 80.65  ? 541 VAL   A CG2 1 
ATOM   1895 N  N   . LEU   A 1 246 ? -21.528 9.665   12.038 1.00 69.51  ? 542 LEU   A N   1 
ATOM   1896 C  CA  . LEU   A 1 246 ? -22.265 10.769  12.640 1.00 71.84  ? 542 LEU   A CA  1 
ATOM   1897 C  C   . LEU   A 1 246 ? -21.774 11.023  14.063 1.00 72.05  ? 542 LEU   A C   1 
ATOM   1898 O  O   . LEU   A 1 246 ? -21.838 10.139  14.925 1.00 79.65  ? 542 LEU   A O   1 
ATOM   1899 C  CB  . LEU   A 1 246 ? -23.763 10.481  12.637 1.00 73.60  ? 542 LEU   A CB  1 
ATOM   1900 C  CG  . LEU   A 1 246 ? -24.577 11.447  13.517 1.00 80.31  ? 542 LEU   A CG  1 
ATOM   1901 C  CD1 . LEU   A 1 246 ? -24.474 12.887  13.006 1.00 78.61  ? 542 LEU   A CD1 1 
ATOM   1902 C  CD2 . LEU   A 1 246 ? -26.039 11.009  13.648 1.00 76.84  ? 542 LEU   A CD2 1 
ATOM   1903 N  N   . GLU   A 1 247 ? -21.349 12.247  14.316 1.00 73.51  ? 543 GLU   A N   1 
ATOM   1904 C  CA  . GLU   A 1 247 ? -20.727 12.638  15.570 1.00 77.55  ? 543 GLU   A CA  1 
ATOM   1905 C  C   . GLU   A 1 247 ? -21.509 13.769  16.237 1.00 88.17  ? 543 GLU   A C   1 
ATOM   1906 O  O   . GLU   A 1 247 ? -22.081 14.631  15.562 1.00 100.24 ? 543 GLU   A O   1 
ATOM   1907 C  CB  . GLU   A 1 247 ? -19.273 13.048  15.324 1.00 81.26  ? 543 GLU   A CB  1 
ATOM   1908 C  CG  . GLU   A 1 247 ? -18.381 11.887  14.910 1.00 81.00  ? 543 GLU   A CG  1 
ATOM   1909 C  CD  . GLU   A 1 247 ? -16.959 12.317  14.657 1.00 94.69  ? 543 GLU   A CD  1 
ATOM   1910 O  OE1 . GLU   A 1 247 ? -16.712 12.933  13.594 1.00 110.67 ? 543 GLU   A OE1 1 
ATOM   1911 O  OE2 . GLU   A 1 247 ? -16.099 12.054  15.521 1.00 88.96  ? 543 GLU   A OE2 1 
ATOM   1912 N  N   . VAL   A 1 248 ? -21.532 13.756  17.571 1.00 85.45  ? 544 VAL   A N   1 
ATOM   1913 C  CA  . VAL   A 1 248 ? -22.274 14.738  18.362 1.00 91.84  ? 544 VAL   A CA  1 
ATOM   1914 C  C   . VAL   A 1 248 ? -21.304 15.548  19.223 1.00 92.19  ? 544 VAL   A C   1 
ATOM   1915 O  O   . VAL   A 1 248 ? -20.676 14.984  20.127 1.00 83.84  ? 544 VAL   A O   1 
ATOM   1916 C  CB  . VAL   A 1 248 ? -23.332 14.063  19.256 1.00 86.00  ? 544 VAL   A CB  1 
ATOM   1917 C  CG1 . VAL   A 1 248 ? -24.042 15.116  20.134 1.00 82.95  ? 544 VAL   A CG1 1 
ATOM   1918 C  CG2 . VAL   A 1 248 ? -24.338 13.254  18.435 1.00 84.40  ? 544 VAL   A CG2 1 
ATOM   1919 N  N   . PRO   A 1 249 ? -21.142 16.855  18.998 1.00 94.79  ? 545 PRO   A N   1 
ATOM   1920 C  CA  . PRO   A 1 249 ? -20.268 17.651  19.876 1.00 97.65  ? 545 PRO   A CA  1 
ATOM   1921 C  C   . PRO   A 1 249 ? -20.966 17.955  21.199 1.00 103.55 ? 545 PRO   A C   1 
ATOM   1922 O  O   . PRO   A 1 249 ? -22.097 18.449  21.219 1.00 108.11 ? 545 PRO   A O   1 
ATOM   1923 C  CB  . PRO   A 1 249 ? -20.011 18.924  19.055 1.00 94.32  ? 545 PRO   A CB  1 
ATOM   1924 C  CG  . PRO   A 1 249 ? -21.226 19.074  18.253 1.00 95.79  ? 545 PRO   A CG  1 
ATOM   1925 C  CD  . PRO   A 1 249 ? -21.669 17.662  17.881 1.00 93.37  ? 545 PRO   A CD  1 
ATOM   1926 N  N   . ILE   A 1 250 ? -20.286 17.649  22.306 1.00 106.02 ? 546 ILE   A N   1 
ATOM   1927 C  CA  . ILE   A 1 250 ? -20.881 17.751  23.639 1.00 92.66  ? 546 ILE   A CA  1 
ATOM   1928 C  C   . ILE   A 1 250 ? -20.845 19.198  24.116 1.00 101.53 ? 546 ILE   A C   1 
ATOM   1929 O  O   . ILE   A 1 250 ? -19.769 19.787  24.276 1.00 106.91 ? 546 ILE   A O   1 
ATOM   1930 C  CB  . ILE   A 1 250 ? -20.154 16.842  24.640 1.00 93.09  ? 546 ILE   A CB  1 
ATOM   1931 C  CG1 . ILE   A 1 250 ? -19.931 15.449  24.049 1.00 81.97  ? 546 ILE   A CG1 1 
ATOM   1932 C  CG2 . ILE   A 1 250 ? -20.927 16.773  25.971 1.00 89.53  ? 546 ILE   A CG2 1 
ATOM   1933 C  CD1 . ILE   A 1 250 ? -21.202 14.772  23.632 1.00 84.74  ? 546 ILE   A CD1 1 
ATOM   1934 N  N   . ARG   A 1 251 ? -22.019 19.763  24.389 1.00 102.99 ? 547 ARG   A N   1 
ATOM   1935 C  CA  . ARG   A 1 251 ? -22.110 21.050  25.058 1.00 111.43 ? 547 ARG   A CA  1 
ATOM   1936 C  C   . ARG   A 1 251 ? -22.986 20.907  26.292 1.00 109.35 ? 547 ARG   A C   1 
ATOM   1937 O  O   . ARG   A 1 251 ? -23.849 20.024  26.369 1.00 105.01 ? 547 ARG   A O   1 
ATOM   1938 C  CB  . ARG   A 1 251 ? -22.668 22.167  24.141 1.00 115.53 ? 547 ARG   A CB  1 
ATOM   1939 C  CG  . ARG   A 1 251 ? -24.088 21.951  23.636 1.00 112.75 ? 547 ARG   A CG  1 
ATOM   1940 C  CD  . ARG   A 1 251 ? -24.080 21.594  22.154 1.00 112.46 ? 547 ARG   A CD  1 
ATOM   1941 N  NE  . ARG   A 1 251 ? -25.423 21.403  21.617 1.00 110.13 ? 547 ARG   A NE  1 
ATOM   1942 C  CZ  . ARG   A 1 251 ? -25.741 20.443  20.760 1.00 107.33 ? 547 ARG   A CZ  1 
ATOM   1943 N  NH1 . ARG   A 1 251 ? -26.981 20.332  20.324 1.00 112.95 ? 547 ARG   A NH1 1 
ATOM   1944 N  NH2 . ARG   A 1 251 ? -24.817 19.588  20.344 1.00 104.38 ? 547 ARG   A NH2 1 
ATOM   1945 N  N   . HIS   A 1 252 ? -22.741 21.764  27.250 1.00 113.93 ? 548 HIS   A N   1 
ATOM   1946 C  CA  . HIS   A 1 252 ? -23.619 21.753  28.399 1.00 115.62 ? 548 HIS   A CA  1 
ATOM   1947 C  C   . HIS   A 1 252 ? -24.675 22.836  28.251 1.00 121.61 ? 548 HIS   A C   1 
ATOM   1948 O  O   . HIS   A 1 252 ? -24.431 23.858  27.606 1.00 124.98 ? 548 HIS   A O   1 
ATOM   1949 C  CB  . HIS   A 1 252 ? -22.836 21.971  29.692 1.00 106.90 ? 548 HIS   A CB  1 
ATOM   1950 C  CG  . HIS   A 1 252 ? -23.561 21.493  30.907 1.00 118.95 ? 548 HIS   A CG  1 
ATOM   1951 N  ND1 . HIS   A 1 252 ? -24.463 22.279  31.593 1.00 123.00 ? 548 HIS   A ND1 1 
ATOM   1952 C  CD2 . HIS   A 1 252 ? -23.543 20.297  31.541 1.00 113.77 ? 548 HIS   A CD2 1 
ATOM   1953 C  CE1 . HIS   A 1 252 ? -24.967 21.589  32.597 1.00 115.62 ? 548 HIS   A CE1 1 
ATOM   1954 N  NE2 . HIS   A 1 252 ? -24.423 20.385  32.589 1.00 112.12 ? 548 HIS   A NE2 1 
ATOM   1955 N  N   . PRO   A 1 253 ? -25.881 22.624  28.799 1.00 121.43 ? 549 PRO   A N   1 
ATOM   1956 C  CA  . PRO   A 1 253 ? -26.916 23.665  28.704 1.00 127.96 ? 549 PRO   A CA  1 
ATOM   1957 C  C   . PRO   A 1 253 ? -26.744 24.774  29.735 1.00 141.45 ? 549 PRO   A C   1 
ATOM   1958 O  O   . PRO   A 1 253 ? -27.692 25.511  30.023 1.00 147.97 ? 549 PRO   A O   1 
ATOM   1959 C  CB  . PRO   A 1 253 ? -28.224 22.886  28.911 1.00 121.69 ? 549 PRO   A CB  1 
ATOM   1960 C  CG  . PRO   A 1 253 ? -27.832 21.635  29.634 1.00 113.57 ? 549 PRO   A CG  1 
ATOM   1961 C  CD  . PRO   A 1 253 ? -26.412 21.330  29.282 1.00 105.85 ? 549 PRO   A CD  1 
ATOM   1962 N  N   . LYS   A 1 254 ? -25.536 24.901  30.292 1.00 148.46 ? 550 LYS   A N   1 
ATOM   1963 C  CA  . LYS   A 1 254 ? -25.197 25.982  31.211 1.00 151.18 ? 550 LYS   A CA  1 
ATOM   1964 C  C   . LYS   A 1 254 ? -23.774 26.460  30.968 1.00 151.48 ? 550 LYS   A C   1 
ATOM   1965 O  O   . LYS   A 1 254 ? -23.549 27.600  30.552 1.00 169.67 ? 550 LYS   A O   1 
ATOM   1966 C  CB  . LYS   A 1 254 ? -25.309 25.536  32.670 1.00 152.41 ? 550 LYS   A CB  1 
ATOM   1967 C  CG  . LYS   A 1 254 ? -26.565 24.798  33.043 1.00 150.44 ? 550 LYS   A CG  1 
ATOM   1968 C  CD  . LYS   A 1 254 ? -27.751 25.719  33.170 1.00 155.17 ? 550 LYS   A CD  1 
ATOM   1969 C  CE  . LYS   A 1 254 ? -28.914 24.974  33.790 1.00 152.29 ? 550 LYS   A CE  1 
ATOM   1970 N  NZ  . LYS   A 1 254 ? -30.225 25.599  33.481 1.00 157.32 ? 550 LYS   A NZ  1 
ATOM   1971 N  N   . PHE   A 1 255 ? -22.812 25.577  31.224 1.00 135.95 ? 551 PHE   A N   1 
ATOM   1972 C  CA  . PHE   A 1 255 ? -21.401 25.939  31.303 1.00 135.48 ? 551 PHE   A CA  1 
ATOM   1973 C  C   . PHE   A 1 255 ? -20.815 26.062  29.901 1.00 139.61 ? 551 PHE   A C   1 
ATOM   1974 O  O   . PHE   A 1 255 ? -20.606 25.055  29.221 1.00 120.11 ? 551 PHE   A O   1 
ATOM   1975 C  CB  . PHE   A 1 255 ? -20.642 24.893  32.114 1.00 130.96 ? 551 PHE   A CB  1 
ATOM   1976 C  CG  . PHE   A 1 255 ? -21.215 24.645  33.493 1.00 129.82 ? 551 PHE   A CG  1 
ATOM   1977 C  CD1 . PHE   A 1 255 ? -22.224 23.716  33.685 1.00 127.08 ? 551 PHE   A CD1 1 
ATOM   1978 C  CD2 . PHE   A 1 255 ? -20.732 25.329  34.590 1.00 135.34 ? 551 PHE   A CD2 1 
ATOM   1979 C  CE1 . PHE   A 1 255 ? -22.745 23.480  34.933 1.00 128.56 ? 551 PHE   A CE1 1 
ATOM   1980 C  CE2 . PHE   A 1 255 ? -21.250 25.099  35.853 1.00 135.81 ? 551 PHE   A CE2 1 
ATOM   1981 C  CZ  . PHE   A 1 255 ? -22.258 24.175  36.024 1.00 133.33 ? 551 PHE   A CZ  1 
ATOM   1982 N  N   . ASP   A 1 256 ? -20.521 27.290  29.477 1.00 143.84 ? 552 ASP   A N   1 
ATOM   1983 C  CA  . ASP   A 1 256 ? -19.969 27.507  28.148 1.00 153.23 ? 552 ASP   A CA  1 
ATOM   1984 C  C   . ASP   A 1 256 ? -18.500 27.123  28.037 1.00 146.95 ? 552 ASP   A C   1 
ATOM   1985 O  O   . ASP   A 1 256 ? -17.995 27.013  26.915 1.00 147.55 ? 552 ASP   A O   1 
ATOM   1986 C  CB  . ASP   A 1 256 ? -20.154 28.967  27.727 1.00 171.71 ? 552 ASP   A CB  1 
ATOM   1987 C  CG  . ASP   A 1 256 ? -21.543 29.241  27.171 1.00 178.58 ? 552 ASP   A CG  1 
ATOM   1988 O  OD1 . ASP   A 1 256 ? -22.477 29.438  27.978 1.00 179.44 ? 552 ASP   A OD1 1 
ATOM   1989 O  OD2 . ASP   A 1 256 ? -21.701 29.257  25.928 1.00 179.76 ? 552 ASP   A OD2 1 
ATOM   1990 N  N   . TRP   A 1 257 ? -17.796 26.926  29.153 1.00 138.72 ? 553 TRP   A N   1 
ATOM   1991 C  CA  . TRP   A 1 257 ? -16.482 26.306  29.048 1.00 138.52 ? 553 TRP   A CA  1 
ATOM   1992 C  C   . TRP   A 1 257 ? -16.584 24.843  28.650 1.00 134.67 ? 553 TRP   A C   1 
ATOM   1993 O  O   . TRP   A 1 257 ? -15.560 24.232  28.326 1.00 130.40 ? 553 TRP   A O   1 
ATOM   1994 C  CB  . TRP   A 1 257 ? -15.719 26.431  30.362 1.00 140.76 ? 553 TRP   A CB  1 
ATOM   1995 C  CG  . TRP   A 1 257 ? -16.505 25.937  31.527 1.00 139.31 ? 553 TRP   A CG  1 
ATOM   1996 C  CD1 . TRP   A 1 257 ? -17.313 26.678  32.334 1.00 144.02 ? 553 TRP   A CD1 1 
ATOM   1997 C  CD2 . TRP   A 1 257 ? -16.583 24.586  32.012 1.00 132.88 ? 553 TRP   A CD2 1 
ATOM   1998 N  NE1 . TRP   A 1 257 ? -17.878 25.882  33.298 1.00 137.99 ? 553 TRP   A NE1 1 
ATOM   1999 C  CE2 . TRP   A 1 257 ? -17.448 24.593  33.122 1.00 129.58 ? 553 TRP   A CE2 1 
ATOM   2000 C  CE3 . TRP   A 1 257 ? -16.003 23.376  31.617 1.00 123.83 ? 553 TRP   A CE3 1 
ATOM   2001 C  CZ2 . TRP   A 1 257 ? -17.751 23.444  33.837 1.00 122.30 ? 553 TRP   A CZ2 1 
ATOM   2002 C  CZ3 . TRP   A 1 257 ? -16.300 22.239  32.332 1.00 118.35 ? 553 TRP   A CZ3 1 
ATOM   2003 C  CH2 . TRP   A 1 257 ? -17.166 22.280  33.431 1.00 119.65 ? 553 TRP   A CH2 1 
ATOM   2004 N  N   . PHE   A 1 258 ? -17.795 24.275  28.682 1.00 143.70 ? 554 PHE   A N   1 
ATOM   2005 C  CA  . PHE   A 1 258 ? -18.001 22.912  28.208 1.00 144.05 ? 554 PHE   A CA  1 
ATOM   2006 C  C   . PHE   A 1 258 ? -17.809 22.809  26.702 1.00 142.56 ? 554 PHE   A C   1 
ATOM   2007 O  O   . PHE   A 1 258 ? -17.409 21.751  26.205 1.00 145.79 ? 554 PHE   A O   1 
ATOM   2008 C  CB  . PHE   A 1 258 ? -19.394 22.425  28.593 1.00 144.20 ? 554 PHE   A CB  1 
ATOM   2009 C  CG  . PHE   A 1 258 ? -19.439 20.991  28.957 1.00 142.28 ? 554 PHE   A CG  1 
ATOM   2010 C  CD1 . PHE   A 1 258 ? -19.487 20.607  30.284 1.00 140.65 ? 554 PHE   A CD1 1 
ATOM   2011 C  CD2 . PHE   A 1 258 ? -19.408 20.016  27.978 1.00 139.60 ? 554 PHE   A CD2 1 
ATOM   2012 C  CE1 . PHE   A 1 258 ? -19.514 19.279  30.630 1.00 136.03 ? 554 PHE   A CE1 1 
ATOM   2013 C  CE2 . PHE   A 1 258 ? -19.435 18.682  28.318 1.00 132.99 ? 554 PHE   A CE2 1 
ATOM   2014 C  CZ  . PHE   A 1 258 ? -19.490 18.312  29.641 1.00 133.93 ? 554 PHE   A CZ  1 
ATOM   2015 N  N   . LYS   A 1 259 ? -18.111 23.877  25.958 1.00 140.65 ? 555 LYS   A N   1 
ATOM   2016 C  CA  . LYS   A 1 259 ? -17.704 23.927  24.557 1.00 143.97 ? 555 LYS   A CA  1 
ATOM   2017 C  C   . LYS   A 1 259 ? -16.197 23.755  24.438 1.00 139.20 ? 555 LYS   A C   1 
ATOM   2018 O  O   . LYS   A 1 259 ? -15.710 22.935  23.652 1.00 125.98 ? 555 LYS   A O   1 
ATOM   2019 C  CB  . LYS   A 1 259 ? -18.135 25.251  23.916 1.00 153.30 ? 555 LYS   A CB  1 
ATOM   2020 C  CG  . LYS   A 1 259 ? -19.527 25.725  24.287 1.00 156.30 ? 555 LYS   A CG  1 
ATOM   2021 C  CD  . LYS   A 1 259 ? -19.889 27.019  23.574 1.00 163.75 ? 555 LYS   A CD  1 
ATOM   2022 C  CE  . LYS   A 1 259 ? -21.390 27.220  23.596 1.00 163.45 ? 555 LYS   A CE  1 
ATOM   2023 N  NZ  . LYS   A 1 259 ? -22.070 25.949  23.989 1.00 154.66 ? 555 LYS   A NZ  1 
ATOM   2024 N  N   . ASP   A 1 260 ? -15.442 24.515  25.239 1.00 146.31 ? 556 ASP   A N   1 
ATOM   2025 C  CA  . ASP   A 1 260 ? -13.987 24.492  25.167 1.00 146.63 ? 556 ASP   A CA  1 
ATOM   2026 C  C   . ASP   A 1 260 ? -13.404 23.195  25.699 1.00 135.24 ? 556 ASP   A C   1 
ATOM   2027 O  O   . ASP   A 1 260 ? -12.248 22.884  25.390 1.00 124.25 ? 556 ASP   A O   1 
ATOM   2028 C  CB  . ASP   A 1 260 ? -13.403 25.685  25.925 1.00 156.59 ? 556 ASP   A CB  1 
ATOM   2029 C  CG  . ASP   A 1 260 ? -13.458 26.967  25.116 1.00 161.67 ? 556 ASP   A CG  1 
ATOM   2030 O  OD1 . ASP   A 1 260 ? -13.072 26.929  23.927 1.00 161.81 ? 556 ASP   A OD1 1 
ATOM   2031 O  OD2 . ASP   A 1 260 ? -13.892 28.005  25.662 1.00 166.35 ? 556 ASP   A OD2 1 
ATOM   2032 N  N   . LEU   A 1 261 ? -14.171 22.442  26.498 1.00 138.69 ? 557 LEU   A N   1 
ATOM   2033 C  CA  . LEU   A 1 261 ? -13.787 21.071  26.816 1.00 137.94 ? 557 LEU   A CA  1 
ATOM   2034 C  C   . LEU   A 1 261 ? -13.432 20.308  25.547 1.00 144.46 ? 557 LEU   A C   1 
ATOM   2035 O  O   . LEU   A 1 261 ? -12.494 19.504  25.535 1.00 145.54 ? 557 LEU   A O   1 
ATOM   2036 C  CB  . LEU   A 1 261 ? -14.913 20.367  27.575 1.00 130.29 ? 557 LEU   A CB  1 
ATOM   2037 C  CG  . LEU   A 1 261 ? -15.018 20.628  29.080 1.00 131.61 ? 557 LEU   A CG  1 
ATOM   2038 C  CD1 . LEU   A 1 261 ? -16.073 19.733  29.742 1.00 122.55 ? 557 LEU   A CD1 1 
ATOM   2039 C  CD2 . LEU   A 1 261 ? -13.665 20.425  29.735 1.00 134.94 ? 557 LEU   A CD2 1 
ATOM   2040 N  N   . GLY   A 1 262 ? -14.155 20.572  24.461 1.00 148.82 ? 558 GLY   A N   1 
ATOM   2041 C  CA  . GLY   A 1 262 ? -13.796 20.048  23.160 1.00 150.88 ? 558 GLY   A CA  1 
ATOM   2042 C  C   . GLY   A 1 262 ? -14.018 18.560  23.041 1.00 140.05 ? 558 GLY   A C   1 
ATOM   2043 O  O   . GLY   A 1 262 ? -13.126 17.826  22.607 1.00 143.29 ? 558 GLY   A O   1 
ATOM   2044 N  N   . LEU   A 1 263 ? -15.202 18.099  23.424 1.00 126.64 ? 559 LEU   A N   1 
ATOM   2045 C  CA  . LEU   A 1 263 ? -15.511 16.682  23.385 1.00 112.71 ? 559 LEU   A CA  1 
ATOM   2046 C  C   . LEU   A 1 263 ? -16.634 16.405  22.395 1.00 105.32 ? 559 LEU   A C   1 
ATOM   2047 O  O   . LEU   A 1 263 ? -17.470 17.268  22.106 1.00 98.80  ? 559 LEU   A O   1 
ATOM   2048 C  CB  . LEU   A 1 263 ? -15.897 16.161  24.766 1.00 108.45 ? 559 LEU   A CB  1 
ATOM   2049 C  CG  . LEU   A 1 263 ? -14.832 16.413  25.839 1.00 109.92 ? 559 LEU   A CG  1 
ATOM   2050 C  CD1 . LEU   A 1 263 ? -15.269 15.817  27.141 1.00 104.33 ? 559 LEU   A CD1 1 
ATOM   2051 C  CD2 . LEU   A 1 263 ? -13.467 15.865  25.435 1.00 112.08 ? 559 LEU   A CD2 1 
ATOM   2052 N  N   . LYS   A 1 264 ? -16.628 15.180  21.879 1.00 98.91  ? 560 LYS   A N   1 
ATOM   2053 C  CA  . LYS   A 1 264 ? -17.654 14.689  20.978 1.00 91.80  ? 560 LYS   A CA  1 
ATOM   2054 C  C   . LYS   A 1 264 ? -17.658 13.179  21.071 1.00 89.51  ? 560 LYS   A C   1 
ATOM   2055 O  O   . LYS   A 1 264 ? -16.645 12.558  21.401 1.00 86.84  ? 560 LYS   A O   1 
ATOM   2056 C  CB  . LYS   A 1 264 ? -17.407 15.103  19.522 1.00 88.10  ? 560 LYS   A CB  1 
ATOM   2057 C  CG  . LYS   A 1 264 ? -16.049 14.658  18.996 1.00 93.21  ? 560 LYS   A CG  1 
ATOM   2058 C  CD  . LYS   A 1 264 ? -15.908 14.899  17.490 1.00 99.61  ? 560 LYS   A CD  1 
ATOM   2059 C  CE  . LYS   A 1 264 ? -14.439 15.065  17.084 1.00 104.07 ? 560 LYS   A CE  1 
ATOM   2060 N  NZ  . LYS   A 1 264 ? -14.209 15.283  15.625 1.00 93.55  ? 560 LYS   A NZ  1 
ATOM   2061 N  N   . TRP   A 1 265 ? -18.801 12.591  20.753 1.00 81.57  ? 561 TRP   A N   1 
ATOM   2062 C  CA  . TRP   A 1 265 ? -18.893 11.152  20.631 1.00 77.16  ? 561 TRP   A CA  1 
ATOM   2063 C  C   . TRP   A 1 265 ? -19.578 10.807  19.314 1.00 80.91  ? 561 TRP   A C   1 
ATOM   2064 O  O   . TRP   A 1 265 ? -20.204 11.658  18.674 1.00 86.51  ? 561 TRP   A O   1 
ATOM   2065 C  CB  . TRP   A 1 265 ? -19.639 10.535  21.806 1.00 62.27  ? 561 TRP   A CB  1 
ATOM   2066 C  CG  . TRP   A 1 265 ? -19.208 9.124   22.061 1.00 67.43  ? 561 TRP   A CG  1 
ATOM   2067 C  CD1 . TRP   A 1 265 ? -19.960 8.001   21.901 1.00 72.40  ? 561 TRP   A CD1 1 
ATOM   2068 C  CD2 . TRP   A 1 265 ? -17.916 8.682   22.500 1.00 75.95  ? 561 TRP   A CD2 1 
ATOM   2069 N  NE1 . TRP   A 1 265 ? -19.230 6.886   22.229 1.00 77.92  ? 561 TRP   A NE1 1 
ATOM   2070 C  CE2 . TRP   A 1 265 ? -17.970 7.275   22.601 1.00 76.22  ? 561 TRP   A CE2 1 
ATOM   2071 C  CE3 . TRP   A 1 265 ? -16.725 9.337   22.832 1.00 78.91  ? 561 TRP   A CE3 1 
ATOM   2072 C  CZ2 . TRP   A 1 265 ? -16.876 6.510   23.021 1.00 66.59  ? 561 TRP   A CZ2 1 
ATOM   2073 C  CZ3 . TRP   A 1 265 ? -15.635 8.564   23.247 1.00 77.33  ? 561 TRP   A CZ3 1 
ATOM   2074 C  CH2 . TRP   A 1 265 ? -15.723 7.172   23.336 1.00 62.38  ? 561 TRP   A CH2 1 
ATOM   2075 N  N   . TYR   A 1 266 ? -19.433 9.550   18.910 1.00 72.06  ? 562 TYR   A N   1 
ATOM   2076 C  CA  . TYR   A 1 266 ? -20.105 9.055   17.717 1.00 65.23  ? 562 TYR   A CA  1 
ATOM   2077 C  C   . TYR   A 1 266 ? -21.510 8.582   18.060 1.00 67.13  ? 562 TYR   A C   1 
ATOM   2078 O  O   . TYR   A 1 266 ? -21.759 8.014   19.136 1.00 68.94  ? 562 TYR   A O   1 
ATOM   2079 C  CB  . TYR   A 1 266 ? -19.303 7.933   17.073 1.00 62.99  ? 562 TYR   A CB  1 
ATOM   2080 C  CG  . TYR   A 1 266 ? -18.813 6.857   18.023 1.00 69.27  ? 562 TYR   A CG  1 
ATOM   2081 C  CD1 . TYR   A 1 266 ? -19.554 5.707   18.237 1.00 67.62  ? 562 TYR   A CD1 1 
ATOM   2082 C  CD2 . TYR   A 1 266 ? -17.588 6.976   18.672 1.00 64.73  ? 562 TYR   A CD2 1 
ATOM   2083 C  CE1 . TYR   A 1 266 ? -19.105 4.725   19.082 1.00 68.70  ? 562 TYR   A CE1 1 
ATOM   2084 C  CE2 . TYR   A 1 266 ? -17.127 5.984   19.520 1.00 67.58  ? 562 TYR   A CE2 1 
ATOM   2085 C  CZ  . TYR   A 1 266 ? -17.891 4.871   19.728 1.00 71.40  ? 562 TYR   A CZ  1 
ATOM   2086 O  OH  . TYR   A 1 266 ? -17.443 3.882   20.567 1.00 80.66  ? 562 TYR   A OH  1 
ATOM   2087 N  N   . GLY   A 1 267 ? -22.440 8.849   17.148 1.00 62.67  ? 563 GLY   A N   1 
ATOM   2088 C  CA  . GLY   A 1 267 ? -23.825 8.544   17.428 1.00 64.60  ? 563 GLY   A CA  1 
ATOM   2089 C  C   . GLY   A 1 267 ? -24.098 7.058   17.506 1.00 66.54  ? 563 GLY   A C   1 
ATOM   2090 O  O   . GLY   A 1 267 ? -25.044 6.639   18.180 1.00 71.44  ? 563 GLY   A O   1 
ATOM   2091 N  N   . LEU   A 1 268 ? -23.268 6.241   16.847 1.00 69.99  ? 564 LEU   A N   1 
ATOM   2092 C  CA  . LEU   A 1 268 ? -23.646 4.866   16.556 1.00 64.75  ? 564 LEU   A CA  1 
ATOM   2093 C  C   . LEU   A 1 268 ? -22.852 3.908   17.426 1.00 63.36  ? 564 LEU   A C   1 
ATOM   2094 O  O   . LEU   A 1 268 ? -21.645 3.707   17.177 1.00 63.68  ? 564 LEU   A O   1 
ATOM   2095 C  CB  . LEU   A 1 268 ? -23.422 4.544   15.080 1.00 66.36  ? 564 LEU   A CB  1 
ATOM   2096 C  CG  . LEU   A 1 268 ? -24.212 3.340   14.551 1.00 65.46  ? 564 LEU   A CG  1 
ATOM   2097 C  CD1 . LEU   A 1 268 ? -25.700 3.652   14.376 1.00 62.59  ? 564 LEU   A CD1 1 
ATOM   2098 C  CD2 . LEU   A 1 268 ? -23.620 2.867   13.249 1.00 61.57  ? 564 LEU   A CD2 1 
ATOM   2099 N  N   . PRO   A 1 269 ? -23.472 3.272   18.430 1.00 57.66  ? 565 PRO   A N   1 
ATOM   2100 C  CA  . PRO   A 1 269 ? -22.789 2.171   19.108 1.00 55.36  ? 565 PRO   A CA  1 
ATOM   2101 C  C   . PRO   A 1 269 ? -23.068 0.898   18.343 1.00 49.89  ? 565 PRO   A C   1 
ATOM   2102 O  O   . PRO   A 1 269 ? -24.233 0.527   18.173 1.00 63.15  ? 565 PRO   A O   1 
ATOM   2103 C  CB  . PRO   A 1 269 ? -23.422 2.158   20.509 1.00 57.35  ? 565 PRO   A CB  1 
ATOM   2104 C  CG  . PRO   A 1 269 ? -24.832 2.774   20.311 1.00 58.25  ? 565 PRO   A CG  1 
ATOM   2105 C  CD  . PRO   A 1 269 ? -24.876 3.380   18.865 1.00 53.97  ? 565 PRO   A CD  1 
ATOM   2106 N  N   . ALA   A 1 270 ? -22.022 0.213   17.886 1.00 50.31  ? 566 ALA   A N   1 
ATOM   2107 C  CA  . ALA   A 1 270 ? -22.191 -0.943  17.001 1.00 47.21  ? 566 ALA   A CA  1 
ATOM   2108 C  C   . ALA   A 1 270 ? -21.087 -1.930  17.346 1.00 54.89  ? 566 ALA   A C   1 
ATOM   2109 O  O   . ALA   A 1 270 ? -19.926 -1.715  16.989 1.00 57.41  ? 566 ALA   A O   1 
ATOM   2110 C  CB  . ALA   A 1 270 ? -22.153 -0.525  15.522 1.00 44.18  ? 566 ALA   A CB  1 
ATOM   2111 N  N   . VAL   A 1 271 ? -21.455 -2.991  18.060 1.00 46.71  ? 567 VAL   A N   1 
ATOM   2112 C  CA  . VAL   A 1 271 ? -20.490 -3.963  18.548 1.00 53.96  ? 567 VAL   A CA  1 
ATOM   2113 C  C   . VAL   A 1 271 ? -20.171 -4.934  17.433 1.00 52.94  ? 567 VAL   A C   1 
ATOM   2114 O  O   . VAL   A 1 271 ? -21.071 -5.544  16.845 1.00 63.57  ? 567 VAL   A O   1 
ATOM   2115 C  CB  . VAL   A 1 271 ? -21.036 -4.713  19.771 1.00 51.52  ? 567 VAL   A CB  1 
ATOM   2116 C  CG1 . VAL   A 1 271 ? -20.401 -6.115  19.867 1.00 51.25  ? 567 VAL   A CG1 1 
ATOM   2117 C  CG2 . VAL   A 1 271 ? -20.797 -3.901  21.030 1.00 48.30  ? 567 VAL   A CG2 1 
ATOM   2118 N  N   . SER   A 1 272 ? -18.891 -5.107  17.156 1.00 58.71  ? 568 SER   A N   1 
ATOM   2119 C  CA  . SER   A 1 272 ? -18.492 -5.881  15.995 1.00 63.14  ? 568 SER   A CA  1 
ATOM   2120 C  C   . SER   A 1 272 ? -17.708 -7.138  16.332 1.00 65.62  ? 568 SER   A C   1 
ATOM   2121 O  O   . SER   A 1 272 ? -17.437 -7.933  15.424 1.00 62.68  ? 568 SER   A O   1 
ATOM   2122 C  CB  . SER   A 1 272 ? -17.670 -5.000  15.054 1.00 63.11  ? 568 SER   A CB  1 
ATOM   2123 O  OG  . SER   A 1 272 ? -16.546 -4.473  15.730 1.00 64.81  ? 568 SER   A OG  1 
ATOM   2124 N  N   . ASN   A 1 273 ? -17.356 -7.355  17.603 1.00 61.20  ? 569 ASN   A N   1 
ATOM   2125 C  CA  . ASN   A 1 273 ? -16.372 -8.368  17.961 1.00 62.08  ? 569 ASN   A CA  1 
ATOM   2126 C  C   . ASN   A 1 273 ? -16.988 -9.592  18.616 1.00 62.88  ? 569 ASN   A C   1 
ATOM   2127 O  O   . ASN   A 1 273 ? -16.252 -10.485 19.038 1.00 65.64  ? 569 ASN   A O   1 
ATOM   2128 C  CB  . ASN   A 1 273 ? -15.288 -7.787  18.874 1.00 58.86  ? 569 ASN   A CB  1 
ATOM   2129 C  CG  . ASN   A 1 273 ? -15.841 -7.242  20.202 1.00 61.11  ? 569 ASN   A CG  1 
ATOM   2130 O  OD1 . ASN   A 1 273 ? -17.037 -7.333  20.496 1.00 58.64  ? 569 ASN   A OD1 1 
ATOM   2131 N  ND2 . ASN   A 1 273 ? -14.948 -6.671  21.009 1.00 58.49  ? 569 ASN   A ND2 1 
ATOM   2132 N  N   . MET   A 1 274 ? -18.310 -9.669  18.694 1.00 56.30  ? 570 MET   A N   1 
ATOM   2133 C  CA  . MET   A 1 274 ? -18.957 -10.774 19.366 1.00 56.56  ? 570 MET   A CA  1 
ATOM   2134 C  C   . MET   A 1 274 ? -19.386 -11.829 18.360 1.00 59.37  ? 570 MET   A C   1 
ATOM   2135 O  O   . MET   A 1 274 ? -19.202 -11.690 17.153 1.00 63.02  ? 570 MET   A O   1 
ATOM   2136 C  CB  . MET   A 1 274 ? -20.125 -10.261 20.199 1.00 55.67  ? 570 MET   A CB  1 
ATOM   2137 C  CG  . MET   A 1 274 ? -19.653 -9.417  21.419 1.00 58.27  ? 570 MET   A CG  1 
ATOM   2138 S  SD  . MET   A 1 274 ? -21.085 -9.095  22.411 1.00 48.22  ? 570 MET   A SD  1 
ATOM   2139 C  CE  . MET   A 1 274 ? -21.477 -10.737 22.991 1.00 46.88  ? 570 MET   A CE  1 
ATOM   2140 N  N   . LEU   A 1 275 ? -19.937 -12.920 18.874 1.00 58.85  ? 571 LEU   A N   1 
ATOM   2141 C  CA  . LEU   A 1 275 ? -20.262 -14.085 18.069 1.00 57.84  ? 571 LEU   A CA  1 
ATOM   2142 C  C   . LEU   A 1 275 ? -21.736 -14.394 18.242 1.00 61.86  ? 571 LEU   A C   1 
ATOM   2143 O  O   . LEU   A 1 275 ? -22.203 -14.583 19.367 1.00 60.21  ? 571 LEU   A O   1 
ATOM   2144 C  CB  . LEU   A 1 275 ? -19.402 -15.286 18.460 1.00 54.59  ? 571 LEU   A CB  1 
ATOM   2145 C  CG  . LEU   A 1 275 ? -19.493 -16.496 17.522 1.00 59.07  ? 571 LEU   A CG  1 
ATOM   2146 C  CD1 . LEU   A 1 275 ? -18.128 -17.129 17.383 1.00 63.92  ? 571 LEU   A CD1 1 
ATOM   2147 C  CD2 . LEU   A 1 275 ? -20.509 -17.518 18.004 1.00 59.23  ? 571 LEU   A CD2 1 
ATOM   2148 N  N   . LEU   A 1 276 ? -22.451 -14.444 17.129 1.00 55.85  ? 572 LEU   A N   1 
ATOM   2149 C  CA  . LEU   A 1 276 ? -23.873 -14.750 17.097 1.00 62.76  ? 572 LEU   A CA  1 
ATOM   2150 C  C   . LEU   A 1 276 ? -24.056 -16.243 16.873 1.00 68.56  ? 572 LEU   A C   1 
ATOM   2151 O  O   . LEU   A 1 276 ? -23.494 -16.809 15.929 1.00 71.77  ? 572 LEU   A O   1 
ATOM   2152 C  CB  . LEU   A 1 276 ? -24.575 -13.965 15.979 1.00 65.90  ? 572 LEU   A CB  1 
ATOM   2153 C  CG  . LEU   A 1 276 ? -25.993 -14.383 15.579 1.00 60.53  ? 572 LEU   A CG  1 
ATOM   2154 C  CD1 . LEU   A 1 276 ? -26.925 -14.210 16.753 1.00 56.10  ? 572 LEU   A CD1 1 
ATOM   2155 C  CD2 . LEU   A 1 276 ? -26.507 -13.574 14.420 1.00 51.50  ? 572 LEU   A CD2 1 
ATOM   2156 N  N   . GLU   A 1 277 ? -24.863 -16.865 17.727 1.00 56.89  ? 573 GLU   A N   1 
ATOM   2157 C  CA  . GLU   A 1 277 ? -25.113 -18.299 17.698 1.00 61.28  ? 573 GLU   A CA  1 
ATOM   2158 C  C   . GLU   A 1 277 ? -26.580 -18.523 17.367 1.00 66.80  ? 573 GLU   A C   1 
ATOM   2159 O  O   . GLU   A 1 277 ? -27.458 -18.023 18.081 1.00 64.93  ? 573 GLU   A O   1 
ATOM   2160 C  CB  . GLU   A 1 277 ? -24.764 -18.936 19.045 1.00 67.21  ? 573 GLU   A CB  1 
ATOM   2161 C  CG  . GLU   A 1 277 ? -24.142 -20.295 18.947 1.00 80.63  ? 573 GLU   A CG  1 
ATOM   2162 C  CD  . GLU   A 1 277 ? -24.907 -21.342 19.717 1.00 87.66  ? 573 GLU   A CD  1 
ATOM   2163 O  OE1 . GLU   A 1 277 ? -26.063 -21.652 19.335 1.00 80.78  ? 573 GLU   A OE1 1 
ATOM   2164 O  OE2 . GLU   A 1 277 ? -24.343 -21.852 20.708 1.00 96.73  ? 573 GLU   A OE2 1 
ATOM   2165 N  N   . ILE   A 1 278 ? -26.843 -19.241 16.275 1.00 61.09  ? 574 ILE   A N   1 
ATOM   2166 C  CA  . ILE   A 1 278 ? -28.194 -19.625 15.880 1.00 62.69  ? 574 ILE   A CA  1 
ATOM   2167 C  C   . ILE   A 1 278 ? -28.184 -21.101 15.517 1.00 64.87  ? 574 ILE   A C   1 
ATOM   2168 O  O   . ILE   A 1 278 ? -27.406 -21.524 14.654 1.00 75.86  ? 574 ILE   A O   1 
ATOM   2169 C  CB  . ILE   A 1 278 ? -28.722 -18.812 14.685 1.00 64.47  ? 574 ILE   A CB  1 
ATOM   2170 C  CG1 . ILE   A 1 278 ? -28.563 -17.311 14.915 1.00 64.35  ? 574 ILE   A CG1 1 
ATOM   2171 C  CG2 . ILE   A 1 278 ? -30.173 -19.182 14.414 1.00 66.43  ? 574 ILE   A CG2 1 
ATOM   2172 C  CD1 . ILE   A 1 278 ? -28.937 -16.481 13.698 1.00 64.10  ? 574 ILE   A CD1 1 
ATOM   2173 N  N   . GLY   A 1 279 ? -29.059 -21.872 16.159 1.00 60.30  ? 575 GLY   A N   1 
ATOM   2174 C  CA  . GLY   A 1 279 ? -29.223 -23.288 15.904 1.00 65.23  ? 575 GLY   A CA  1 
ATOM   2175 C  C   . GLY   A 1 279 ? -27.924 -24.050 15.759 1.00 72.97  ? 575 GLY   A C   1 
ATOM   2176 O  O   . GLY   A 1 279 ? -27.804 -24.921 14.893 1.00 84.75  ? 575 GLY   A O   1 
ATOM   2177 N  N   . GLY   A 1 280 ? -26.939 -23.729 16.590 1.00 71.65  ? 576 GLY   A N   1 
ATOM   2178 C  CA  . GLY   A 1 280 ? -25.649 -24.375 16.521 1.00 70.40  ? 576 GLY   A CA  1 
ATOM   2179 C  C   . GLY   A 1 280 ? -24.677 -23.762 15.538 1.00 69.95  ? 576 GLY   A C   1 
ATOM   2180 O  O   . GLY   A 1 280 ? -23.496 -24.125 15.551 1.00 71.13  ? 576 GLY   A O   1 
ATOM   2181 N  N   . LEU   A 1 281 ? -25.126 -22.835 14.699 1.00 70.94  ? 577 LEU   A N   1 
ATOM   2182 C  CA  . LEU   A 1 281 ? -24.264 -22.213 13.705 1.00 71.65  ? 577 LEU   A CA  1 
ATOM   2183 C  C   . LEU   A 1 281 ? -23.601 -20.972 14.286 1.00 69.03  ? 577 LEU   A C   1 
ATOM   2184 O  O   . LEU   A 1 281 ? -24.239 -20.183 14.987 1.00 69.59  ? 577 LEU   A O   1 
ATOM   2185 C  CB  . LEU   A 1 281 ? -25.068 -21.848 12.465 1.00 64.02  ? 577 LEU   A CB  1 
ATOM   2186 C  CG  . LEU   A 1 281 ? -25.736 -23.022 11.754 1.00 66.34  ? 577 LEU   A CG  1 
ATOM   2187 C  CD1 . LEU   A 1 281 ? -26.401 -22.494 10.484 1.00 61.61  ? 577 LEU   A CD1 1 
ATOM   2188 C  CD2 . LEU   A 1 281 ? -24.723 -24.125 11.441 1.00 72.49  ? 577 LEU   A CD2 1 
ATOM   2189 N  N   . GLU   A 1 282 ? -22.319 -20.796 13.980 1.00 70.08  ? 578 GLU   A N   1 
ATOM   2190 C  CA  . GLU   A 1 282 ? -21.496 -19.774 14.614 1.00 66.31  ? 578 GLU   A CA  1 
ATOM   2191 C  C   . GLU   A 1 282 ? -21.175 -18.669 13.622 1.00 64.44  ? 578 GLU   A C   1 
ATOM   2192 O  O   . GLU   A 1 282 ? -20.500 -18.907 12.610 1.00 66.99  ? 578 GLU   A O   1 
ATOM   2193 C  CB  . GLU   A 1 282 ? -20.214 -20.384 15.179 1.00 69.50  ? 578 GLU   A CB  1 
ATOM   2194 C  CG  . GLU   A 1 282 ? -20.450 -21.300 16.368 1.00 77.35  ? 578 GLU   A CG  1 
ATOM   2195 C  CD  . GLU   A 1 282 ? -19.159 -21.710 17.039 1.00 78.55  ? 578 GLU   A CD  1 
ATOM   2196 O  OE1 . GLU   A 1 282 ? -18.137 -21.796 16.317 1.00 70.31  ? 578 GLU   A OE1 1 
ATOM   2197 O  OE2 . GLU   A 1 282 ? -19.168 -21.930 18.280 1.00 83.73  ? 578 GLU   A OE2 1 
ATOM   2198 N  N   . PHE   A 1 283 ? -21.655 -17.471 13.920 1.00 61.58  ? 579 PHE   A N   1 
ATOM   2199 C  CA  . PHE   A 1 283 ? -21.453 -16.289 13.092 1.00 57.98  ? 579 PHE   A CA  1 
ATOM   2200 C  C   . PHE   A 1 283 ? -20.426 -15.402 13.789 1.00 55.91  ? 579 PHE   A C   1 
ATOM   2201 O  O   . PHE   A 1 283 ? -20.761 -14.649 14.705 1.00 63.14  ? 579 PHE   A O   1 
ATOM   2202 C  CB  . PHE   A 1 283 ? -22.777 -15.576 12.853 1.00 53.88  ? 579 PHE   A CB  1 
ATOM   2203 C  CG  . PHE   A 1 283 ? -23.765 -16.389 12.058 1.00 61.33  ? 579 PHE   A CG  1 
ATOM   2204 C  CD1 . PHE   A 1 283 ? -24.791 -17.077 12.681 1.00 61.50  ? 579 PHE   A CD1 1 
ATOM   2205 C  CD2 . PHE   A 1 283 ? -23.655 -16.472 10.678 1.00 61.10  ? 579 PHE   A CD2 1 
ATOM   2206 C  CE1 . PHE   A 1 283 ? -25.698 -17.824 11.941 1.00 67.30  ? 579 PHE   A CE1 1 
ATOM   2207 C  CE2 . PHE   A 1 283 ? -24.562 -17.208 9.932  1.00 66.79  ? 579 PHE   A CE2 1 
ATOM   2208 C  CZ  . PHE   A 1 283 ? -25.585 -17.885 10.564 1.00 69.62  ? 579 PHE   A CZ  1 
ATOM   2209 N  N   . SER   A 1 284 ? -19.170 -15.498 13.348 1.00 60.66  ? 580 SER   A N   1 
ATOM   2210 C  CA  . SER   A 1 284 ? -18.042 -14.796 13.948 1.00 58.95  ? 580 SER   A CA  1 
ATOM   2211 C  C   . SER   A 1 284 ? -17.954 -13.327 13.554 1.00 58.87  ? 580 SER   A C   1 
ATOM   2212 O  O   . SER   A 1 284 ? -17.134 -12.599 14.122 1.00 64.99  ? 580 SER   A O   1 
ATOM   2213 C  CB  . SER   A 1 284 ? -16.754 -15.492 13.538 1.00 65.30  ? 580 SER   A CB  1 
ATOM   2214 O  OG  . SER   A 1 284 ? -16.738 -15.689 12.124 1.00 64.71  ? 580 SER   A OG  1 
ATOM   2215 N  N   . ALA   A 1 285 ? -18.746 -12.883 12.580 1.00 61.25  ? 581 ALA   A N   1 
ATOM   2216 C  CA  . ALA   A 1 285 ? -18.785 -11.483 12.167 1.00 51.49  ? 581 ALA   A CA  1 
ATOM   2217 C  C   . ALA   A 1 285 ? -20.253 -11.108 12.063 1.00 57.15  ? 581 ALA   A C   1 
ATOM   2218 O  O   . ALA   A 1 285 ? -20.943 -11.538 11.134 1.00 64.05  ? 581 ALA   A O   1 
ATOM   2219 C  CB  . ALA   A 1 285 ? -18.053 -11.252 10.846 1.00 58.33  ? 581 ALA   A CB  1 
ATOM   2220 N  N   . CYS   A 1 286 ? -20.730 -10.333 13.027 1.00 53.98  ? 582 CYS   A N   1 
ATOM   2221 C  CA  . CYS   A 1 286 ? -22.140 -9.975  13.108 1.00 52.67  ? 582 CYS   A CA  1 
ATOM   2222 C  C   . CYS   A 1 286 ? -22.352 -8.605  13.756 1.00 59.79  ? 582 CYS   A C   1 
ATOM   2223 O  O   . CYS   A 1 286 ? -23.147 -8.495  14.701 1.00 68.98  ? 582 CYS   A O   1 
ATOM   2224 C  CB  . CYS   A 1 286 ? -22.895 -11.043 13.900 1.00 55.15  ? 582 CYS   A CB  1 
ATOM   2225 S  SG  . CYS   A 1 286 ? -22.173 -11.344 15.569 1.00 55.31  ? 582 CYS   A SG  1 
ATOM   2226 N  N   . PRO   A 1 287 ? -21.703 -7.542  13.271 1.00 58.24  ? 583 PRO   A N   1 
ATOM   2227 C  CA  . PRO   A 1 287 ? -21.870 -6.232  13.913 1.00 51.18  ? 583 PRO   A CA  1 
ATOM   2228 C  C   . PRO   A 1 287 ? -23.335 -5.846  14.061 1.00 53.71  ? 583 PRO   A C   1 
ATOM   2229 O  O   . PRO   A 1 287 ? -24.137 -5.992  13.129 1.00 42.55  ? 583 PRO   A O   1 
ATOM   2230 C  CB  . PRO   A 1 287 ? -21.115 -5.280  12.980 1.00 51.45  ? 583 PRO   A CB  1 
ATOM   2231 C  CG  . PRO   A 1 287 ? -21.027 -6.034  11.650 1.00 61.08  ? 583 PRO   A CG  1 
ATOM   2232 C  CD  . PRO   A 1 287 ? -20.856 -7.450  12.071 1.00 62.20  ? 583 PRO   A CD  1 
ATOM   2233 N  N   . PHE   A 1 288 ? -23.686 -5.393  15.281 1.00 48.10  ? 584 PHE   A N   1 
ATOM   2234 C  CA  . PHE   A 1 288 ? -25.043 -4.977  15.621 1.00 45.54  ? 584 PHE   A CA  1 
ATOM   2235 C  C   . PHE   A 1 288 ? -25.015 -3.624  16.309 1.00 53.93  ? 584 PHE   A C   1 
ATOM   2236 O  O   . PHE   A 1 288 ? -24.089 -3.318  17.064 1.00 47.84  ? 584 PHE   A O   1 
ATOM   2237 C  CB  . PHE   A 1 288 ? -25.763 -5.993  16.528 1.00 46.92  ? 584 PHE   A CB  1 
ATOM   2238 C  CG  . PHE   A 1 288 ? -25.011 -6.337  17.811 1.00 55.88  ? 584 PHE   A CG  1 
ATOM   2239 C  CD1 . PHE   A 1 288 ? -25.210 -5.610  18.974 1.00 49.34  ? 584 PHE   A CD1 1 
ATOM   2240 C  CD2 . PHE   A 1 288 ? -24.158 -7.442  17.859 1.00 57.35  ? 584 PHE   A CD2 1 
ATOM   2241 C  CE1 . PHE   A 1 288 ? -24.546 -5.948  20.147 1.00 45.04  ? 584 PHE   A CE1 1 
ATOM   2242 C  CE2 . PHE   A 1 288 ? -23.493 -7.778  19.010 1.00 52.03  ? 584 PHE   A CE2 1 
ATOM   2243 C  CZ  . PHE   A 1 288 ? -23.700 -7.021  20.167 1.00 47.94  ? 584 PHE   A CZ  1 
ATOM   2244 N  N   . SER   A 1 289 ? -26.048 -2.831  16.067 1.00 58.54  ? 585 SER   A N   1 
ATOM   2245 C  CA  . SER   A 1 289 ? -26.064 -1.446  16.493 1.00 59.83  ? 585 SER   A CA  1 
ATOM   2246 C  C   . SER   A 1 289 ? -27.423 -1.102  17.065 1.00 45.47  ? 585 SER   A C   1 
ATOM   2247 O  O   . SER   A 1 289 ? -28.457 -1.585  16.593 1.00 53.01  ? 585 SER   A O   1 
ATOM   2248 C  CB  . SER   A 1 289 ? -25.755 -0.486  15.322 1.00 71.85  ? 585 SER   A CB  1 
ATOM   2249 O  OG  . SER   A 1 289 ? -26.797 -0.524  14.357 1.00 70.21  ? 585 SER   A OG  1 
ATOM   2250 N  N   . GLY   A 1 290 ? -27.413 -0.243  18.077 1.00 43.21  ? 586 GLY   A N   1 
ATOM   2251 C  CA  . GLY   A 1 290 ? -28.649 0.391   18.465 1.00 46.01  ? 586 GLY   A CA  1 
ATOM   2252 C  C   . GLY   A 1 290 ? -28.454 1.883   18.621 1.00 55.39  ? 586 GLY   A C   1 
ATOM   2253 O  O   . GLY   A 1 290 ? -28.077 2.584   17.682 1.00 57.14  ? 586 GLY   A O   1 
ATOM   2254 N  N   . TRP   A 1 291 ? -28.724 2.375   19.823 1.00 58.20  ? 587 TRP   A N   1 
ATOM   2255 C  CA  . TRP   A 1 291 ? -28.402 3.737   20.196 1.00 59.31  ? 587 TRP   A CA  1 
ATOM   2256 C  C   . TRP   A 1 291 ? -27.882 3.698   21.622 1.00 57.98  ? 587 TRP   A C   1 
ATOM   2257 O  O   . TRP   A 1 291 ? -27.962 2.670   22.302 1.00 56.35  ? 587 TRP   A O   1 
ATOM   2258 C  CB  . TRP   A 1 291 ? -29.609 4.670   20.035 1.00 59.39  ? 587 TRP   A CB  1 
ATOM   2259 C  CG  . TRP   A 1 291 ? -30.850 4.123   20.638 1.00 69.49  ? 587 TRP   A CG  1 
ATOM   2260 C  CD1 . TRP   A 1 291 ? -31.236 4.200   21.961 1.00 71.00  ? 587 TRP   A CD1 1 
ATOM   2261 C  CD2 . TRP   A 1 291 ? -31.888 3.409   19.960 1.00 73.12  ? 587 TRP   A CD2 1 
ATOM   2262 N  NE1 . TRP   A 1 291 ? -32.450 3.579   22.133 1.00 72.95  ? 587 TRP   A NE1 1 
ATOM   2263 C  CE2 . TRP   A 1 291 ? -32.872 3.084   20.924 1.00 76.80  ? 587 TRP   A CE2 1 
ATOM   2264 C  CE3 . TRP   A 1 291 ? -32.088 3.013   18.627 1.00 77.14  ? 587 TRP   A CE3 1 
ATOM   2265 C  CZ2 . TRP   A 1 291 ? -34.033 2.374   20.598 1.00 82.53  ? 587 TRP   A CZ2 1 
ATOM   2266 C  CZ3 . TRP   A 1 291 ? -33.241 2.316   18.304 1.00 79.46  ? 587 TRP   A CZ3 1 
ATOM   2267 C  CH2 . TRP   A 1 291 ? -34.199 2.002   19.284 1.00 84.28  ? 587 TRP   A CH2 1 
ATOM   2268 N  N   . TYR   A 1 292 ? -27.323 4.822   22.049 1.00 62.75  ? 588 TYR   A N   1 
ATOM   2269 C  CA  . TYR   A 1 292 ? -26.627 4.884   23.320 1.00 63.78  ? 588 TYR   A CA  1 
ATOM   2270 C  C   . TYR   A 1 292 ? -27.595 5.208   24.447 1.00 66.57  ? 588 TYR   A C   1 
ATOM   2271 O  O   . TYR   A 1 292 ? -28.479 6.065   24.309 1.00 57.74  ? 588 TYR   A O   1 
ATOM   2272 C  CB  . TYR   A 1 292 ? -25.534 5.949   23.274 1.00 65.17  ? 588 TYR   A CB  1 
ATOM   2273 C  CG  . TYR   A 1 292 ? -24.134 5.492   22.908 1.00 65.81  ? 588 TYR   A CG  1 
ATOM   2274 C  CD1 . TYR   A 1 292 ? -23.512 5.966   21.755 1.00 65.51  ? 588 TYR   A CD1 1 
ATOM   2275 C  CD2 . TYR   A 1 292 ? -23.412 4.626   23.734 1.00 62.84  ? 588 TYR   A CD2 1 
ATOM   2276 C  CE1 . TYR   A 1 292 ? -22.222 5.585   21.417 1.00 65.49  ? 588 TYR   A CE1 1 
ATOM   2277 C  CE2 . TYR   A 1 292 ? -22.107 4.237   23.402 1.00 66.10  ? 588 TYR   A CE2 1 
ATOM   2278 C  CZ  . TYR   A 1 292 ? -21.523 4.721   22.232 1.00 68.15  ? 588 TYR   A CZ  1 
ATOM   2279 O  OH  . TYR   A 1 292 ? -20.239 4.356   21.873 1.00 67.19  ? 588 TYR   A OH  1 
ATOM   2280 N  N   . MET   A 1 293 ? -27.432 4.509   25.562 1.00 63.89  ? 589 MET   A N   1 
ATOM   2281 C  CA  . MET   A 1 293 ? -27.798 5.092   26.841 1.00 68.54  ? 589 MET   A CA  1 
ATOM   2282 C  C   . MET   A 1 293 ? -26.703 6.078   27.207 1.00 61.79  ? 589 MET   A C   1 
ATOM   2283 O  O   . MET   A 1 293 ? -25.525 5.846   26.916 1.00 61.83  ? 589 MET   A O   1 
ATOM   2284 C  CB  . MET   A 1 293 ? -27.955 4.019   27.920 1.00 65.63  ? 589 MET   A CB  1 
ATOM   2285 C  CG  . MET   A 1 293 ? -28.679 4.493   29.180 1.00 61.32  ? 589 MET   A CG  1 
ATOM   2286 S  SD  . MET   A 1 293 ? -28.977 3.089   30.254 1.00 56.39  ? 589 MET   A SD  1 
ATOM   2287 C  CE  . MET   A 1 293 ? -27.295 2.508   30.444 1.00 47.08  ? 589 MET   A CE  1 
ATOM   2288 N  N   . GLY   A 1 294 ? -27.098 7.209   27.796 1.00 57.04  ? 590 GLY   A N   1 
ATOM   2289 C  CA  . GLY   A 1 294 ? -26.134 8.268   28.020 1.00 60.92  ? 590 GLY   A CA  1 
ATOM   2290 C  C   . GLY   A 1 294 ? -24.946 7.811   28.850 1.00 65.70  ? 590 GLY   A C   1 
ATOM   2291 O  O   . GLY   A 1 294 ? -23.823 8.280   28.655 1.00 71.23  ? 590 GLY   A O   1 
ATOM   2292 N  N   . THR   A 1 295 ? -25.178 6.898   29.798 1.00 67.48  ? 591 THR   A N   1 
ATOM   2293 C  CA  . THR   A 1 295 ? -24.151 6.628   30.799 1.00 61.66  ? 591 THR   A CA  1 
ATOM   2294 C  C   . THR   A 1 295 ? -22.918 5.972   30.193 1.00 58.78  ? 591 THR   A C   1 
ATOM   2295 O  O   . THR   A 1 295 ? -21.797 6.220   30.658 1.00 58.23  ? 591 THR   A O   1 
ATOM   2296 C  CB  . THR   A 1 295 ? -24.719 5.776   31.926 1.00 51.20  ? 591 THR   A CB  1 
ATOM   2297 O  OG1 . THR   A 1 295 ? -25.216 4.536   31.429 1.00 51.95  ? 591 THR   A OG1 1 
ATOM   2298 C  CG2 . THR   A 1 295 ? -25.850 6.554   32.634 1.00 56.92  ? 591 THR   A CG2 1 
ATOM   2299 N  N   . GLU   A 1 296 ? -23.087 5.140   29.160 1.00 50.53  ? 592 GLU   A N   1 
ATOM   2300 C  CA  . GLU   A 1 296 ? -21.903 4.509   28.592 1.00 54.76  ? 592 GLU   A CA  1 
ATOM   2301 C  C   . GLU   A 1 296 ? -20.927 5.553   28.072 1.00 65.26  ? 592 GLU   A C   1 
ATOM   2302 O  O   . GLU   A 1 296 ? -19.711 5.359   28.154 1.00 73.49  ? 592 GLU   A O   1 
ATOM   2303 C  CB  . GLU   A 1 296 ? -22.282 3.544   27.481 1.00 51.16  ? 592 GLU   A CB  1 
ATOM   2304 C  CG  . GLU   A 1 296 ? -23.650 2.907   27.592 1.00 52.90  ? 592 GLU   A CG  1 
ATOM   2305 C  CD  . GLU   A 1 296 ? -24.087 2.296   26.255 1.00 63.33  ? 592 GLU   A CD  1 
ATOM   2306 O  OE1 . GLU   A 1 296 ? -23.262 1.601   25.608 1.00 58.21  ? 592 GLU   A OE1 1 
ATOM   2307 O  OE2 . GLU   A 1 296 ? -25.248 2.532   25.849 1.00 58.01  ? 592 GLU   A OE2 1 
ATOM   2308 N  N   . ILE   A 1 297 ? -21.435 6.681   27.587 1.00 68.08  ? 593 ILE   A N   1 
ATOM   2309 C  CA  . ILE   A 1 297 ? -20.557 7.777   27.179 1.00 73.04  ? 593 ILE   A CA  1 
ATOM   2310 C  C   . ILE   A 1 297 ? -20.144 8.614   28.383 1.00 72.48  ? 593 ILE   A C   1 
ATOM   2311 O  O   . ILE   A 1 297 ? -18.955 8.712   28.718 1.00 71.22  ? 593 ILE   A O   1 
ATOM   2312 C  CB  . ILE   A 1 297 ? -21.234 8.668   26.124 1.00 73.62  ? 593 ILE   A CB  1 
ATOM   2313 C  CG1 . ILE   A 1 297 ? -21.878 7.834   25.037 1.00 68.19  ? 593 ILE   A CG1 1 
ATOM   2314 C  CG2 . ILE   A 1 297 ? -20.207 9.608   25.504 1.00 73.42  ? 593 ILE   A CG2 1 
ATOM   2315 C  CD1 . ILE   A 1 297 ? -22.468 8.707   23.949 1.00 64.41  ? 593 ILE   A CD1 1 
ATOM   2316 N  N   . GLY   A 1 298 ? -21.134 9.246   29.028 1.00 77.12  ? 594 GLY   A N   1 
ATOM   2317 C  CA  . GLY   A 1 298 ? -20.842 10.240  30.049 1.00 75.53  ? 594 GLY   A CA  1 
ATOM   2318 C  C   . GLY   A 1 298 ? -20.083 9.665   31.231 1.00 75.26  ? 594 GLY   A C   1 
ATOM   2319 O  O   . GLY   A 1 298 ? -19.115 10.259  31.705 1.00 72.48  ? 594 GLY   A O   1 
ATOM   2320 N  N   . VAL   A 1 299 ? -20.494 8.482   31.702 1.00 76.51  ? 595 VAL   A N   1 
ATOM   2321 C  CA  . VAL   A 1 299 ? -19.881 7.843   32.872 1.00 72.88  ? 595 VAL   A CA  1 
ATOM   2322 C  C   . VAL   A 1 299 ? -18.660 7.019   32.485 1.00 71.56  ? 595 VAL   A C   1 
ATOM   2323 O  O   . VAL   A 1 299 ? -17.543 7.294   32.929 1.00 69.48  ? 595 VAL   A O   1 
ATOM   2324 C  CB  . VAL   A 1 299 ? -20.859 6.909   33.600 1.00 63.74  ? 595 VAL   A CB  1 
ATOM   2325 C  CG1 . VAL   A 1 299 ? -20.210 6.462   34.886 1.00 52.53  ? 595 VAL   A CG1 1 
ATOM   2326 C  CG2 . VAL   A 1 299 ? -22.248 7.517   33.789 1.00 54.80  ? 595 VAL   A CG2 1 
ATOM   2327 N  N   . ARG   A 1 300 ? -18.891 5.961   31.703 1.00 61.36  ? 596 ARG   A N   1 
ATOM   2328 C  CA  . ARG   A 1 300 ? -17.847 4.982   31.422 1.00 67.05  ? 596 ARG   A CA  1 
ATOM   2329 C  C   . ARG   A 1 300 ? -16.806 5.530   30.440 1.00 73.46  ? 596 ARG   A C   1 
ATOM   2330 O  O   . ARG   A 1 300 ? -15.624 5.658   30.782 1.00 75.60  ? 596 ARG   A O   1 
ATOM   2331 C  CB  . ARG   A 1 300 ? -18.485 3.700   30.878 1.00 46.99  ? 596 ARG   A CB  1 
ATOM   2332 C  CG  . ARG   A 1 300 ? -19.611 3.139   31.719 1.00 45.10  ? 596 ARG   A CG  1 
ATOM   2333 C  CD  . ARG   A 1 300 ? -19.064 2.888   33.202 1.00 59.91  ? 596 ARG   A CD  1 
ATOM   2334 N  NE  . ARG   A 1 300 ? -17.811 2.132   33.179 1.00 53.66  ? 596 ARG   A NE  1 
ATOM   2335 C  CZ  . ARG   A 1 300 ? -17.749 0.840   32.862 1.00 60.21  ? 596 ARG   A CZ  1 
ATOM   2336 N  NH1 . ARG   A 1 300 ? -18.862 0.164   32.584 1.00 57.19  ? 596 ARG   A NH1 1 
ATOM   2337 N  NH2 . ARG   A 1 300 ? -16.578 0.228   32.814 1.00 63.94  ? 596 ARG   A NH2 1 
ATOM   2338 N  N   . ASP   A 1 301 ? -17.222 5.835   29.198 1.00 64.08  ? 597 ASP   A N   1 
ATOM   2339 C  CA  . ASP   A 1 301 ? -16.271 6.325   28.198 1.00 68.07  ? 597 ASP   A CA  1 
ATOM   2340 C  C   . ASP   A 1 301 ? -15.480 7.512   28.727 1.00 69.62  ? 597 ASP   A C   1 
ATOM   2341 O  O   . ASP   A 1 301 ? -14.243 7.494   28.757 1.00 74.60  ? 597 ASP   A O   1 
ATOM   2342 C  CB  . ASP   A 1 301 ? -17.006 6.712   26.901 1.00 72.61  ? 597 ASP   A CB  1 
ATOM   2343 C  CG  . ASP   A 1 301 ? -17.596 5.509   26.180 1.00 70.80  ? 597 ASP   A CG  1 
ATOM   2344 O  OD1 . ASP   A 1 301 ? -17.008 4.412   26.230 1.00 64.06  ? 597 ASP   A OD1 1 
ATOM   2345 O  OD2 . ASP   A 1 301 ? -18.670 5.654   25.565 1.00 74.82  ? 597 ASP   A OD2 1 
ATOM   2346 N  N   . TYR   A 1 302 ? -16.180 8.541   29.186 1.00 69.37  ? 598 TYR   A N   1 
ATOM   2347 C  CA  . TYR   A 1 302 ? -15.516 9.772   29.601 1.00 79.99  ? 598 TYR   A CA  1 
ATOM   2348 C  C   . TYR   A 1 302 ? -14.815 9.660   30.971 1.00 84.11  ? 598 TYR   A C   1 
ATOM   2349 O  O   . TYR   A 1 302 ? -13.753 10.269  31.172 1.00 87.54  ? 598 TYR   A O   1 
ATOM   2350 C  CB  . TYR   A 1 302 ? -16.539 10.910  29.605 1.00 91.21  ? 598 TYR   A CB  1 
ATOM   2351 C  CG  . TYR   A 1 302 ? -16.918 11.441  28.222 1.00 95.15  ? 598 TYR   A CG  1 
ATOM   2352 C  CD1 . TYR   A 1 302 ? -18.096 12.161  28.036 1.00 96.26  ? 598 TYR   A CD1 1 
ATOM   2353 C  CD2 . TYR   A 1 302 ? -16.095 11.238  27.114 1.00 94.86  ? 598 TYR   A CD2 1 
ATOM   2354 C  CE1 . TYR   A 1 302 ? -18.452 12.657  26.789 1.00 93.89  ? 598 TYR   A CE1 1 
ATOM   2355 C  CE2 . TYR   A 1 302 ? -16.446 11.736  25.852 1.00 94.00  ? 598 TYR   A CE2 1 
ATOM   2356 C  CZ  . TYR   A 1 302 ? -17.621 12.447  25.710 1.00 92.44  ? 598 TYR   A CZ  1 
ATOM   2357 O  OH  . TYR   A 1 302 ? -17.980 12.955  24.487 1.00 87.34  ? 598 TYR   A OH  1 
ATOM   2358 N  N   . CYS   A 1 303 ? -15.371 8.899   31.926 1.00 73.33  ? 599 CYS   A N   1 
ATOM   2359 C  CA  . CYS   A 1 303 ? -14.901 8.963   33.315 1.00 72.29  ? 599 CYS   A CA  1 
ATOM   2360 C  C   . CYS   A 1 303 ? -14.345 7.665   33.889 1.00 70.47  ? 599 CYS   A C   1 
ATOM   2361 O  O   . CYS   A 1 303 ? -13.934 7.658   35.064 1.00 66.22  ? 599 CYS   A O   1 
ATOM   2362 C  CB  . CYS   A 1 303 ? -16.027 9.452   34.228 1.00 74.46  ? 599 CYS   A CB  1 
ATOM   2363 S  SG  . CYS   A 1 303 ? -16.547 11.128  33.894 1.00 73.16  ? 599 CYS   A SG  1 
ATOM   2364 N  N   . ASP   A 1 304 ? -14.339 6.561   33.137 1.00 73.55  ? 600 ASP   A N   1 
ATOM   2365 C  CA  . ASP   A 1 304 ? -13.488 5.445   33.533 1.00 82.37  ? 600 ASP   A CA  1 
ATOM   2366 C  C   . ASP   A 1 304 ? -12.065 5.958   33.684 1.00 89.58  ? 600 ASP   A C   1 
ATOM   2367 O  O   . ASP   A 1 304 ? -11.606 6.798   32.906 1.00 99.35  ? 600 ASP   A O   1 
ATOM   2368 C  CB  . ASP   A 1 304 ? -13.516 4.312   32.503 1.00 82.37  ? 600 ASP   A CB  1 
ATOM   2369 C  CG  . ASP   A 1 304 ? -14.525 3.229   32.826 1.00 76.08  ? 600 ASP   A CG  1 
ATOM   2370 O  OD1 . ASP   A 1 304 ? -15.351 3.425   33.741 1.00 65.96  ? 600 ASP   A OD1 1 
ATOM   2371 O  OD2 . ASP   A 1 304 ? -14.494 2.175   32.136 1.00 79.12  ? 600 ASP   A OD2 1 
ATOM   2372 N  N   . ASN   A 1 305 ? -11.375 5.472   34.710 1.00 90.30  ? 601 ASN   A N   1 
ATOM   2373 C  CA  . ASN   A 1 305 ? -10.027 5.959   34.975 1.00 89.27  ? 601 ASN   A CA  1 
ATOM   2374 C  C   . ASN   A 1 305 ? -9.082  5.625   33.831 1.00 83.52  ? 601 ASN   A C   1 
ATOM   2375 O  O   . ASN   A 1 305 ? -8.226  6.440   33.464 1.00 81.83  ? 601 ASN   A O   1 
ATOM   2376 C  CB  . ASN   A 1 305 ? -9.504  5.365   36.278 1.00 91.25  ? 601 ASN   A CB  1 
ATOM   2377 C  CG  . ASN   A 1 305 ? -9.701  6.288   37.452 1.00 100.36 ? 601 ASN   A CG  1 
ATOM   2378 O  OD1 . ASN   A 1 305 ? -9.718  7.508   37.295 1.00 109.26 ? 601 ASN   A OD1 1 
ATOM   2379 N  ND2 . ASN   A 1 305 ? -9.829  5.716   38.640 1.00 96.99  ? 601 ASN   A ND2 1 
ATOM   2380 N  N   . SER   A 1 306 ? -9.204  4.420   33.274 1.00 81.30  ? 602 SER   A N   1 
ATOM   2381 C  CA  . SER   A 1 306 ? -8.373  3.994   32.162 1.00 92.27  ? 602 SER   A CA  1 
ATOM   2382 C  C   . SER   A 1 306 ? -9.036  4.250   30.808 1.00 89.99  ? 602 SER   A C   1 
ATOM   2383 O  O   . SER   A 1 306 ? -8.610  3.676   29.800 1.00 84.18  ? 602 SER   A O   1 
ATOM   2384 C  CB  . SER   A 1 306 ? -7.995  2.518   32.317 1.00 100.14 ? 602 SER   A CB  1 
ATOM   2385 O  OG  . SER   A 1 306 ? -9.135  1.692   32.466 1.00 101.42 ? 602 SER   A OG  1 
ATOM   2386 N  N   . ARG   A 1 307 ? -10.063 5.089   30.769 1.00 86.79  ? 603 ARG   A N   1 
ATOM   2387 C  CA  . ARG   A 1 307 ? -10.643 5.581   29.523 1.00 84.02  ? 603 ARG   A CA  1 
ATOM   2388 C  C   . ARG   A 1 307 ? -10.293 7.071   29.389 1.00 88.85  ? 603 ARG   A C   1 
ATOM   2389 O  O   . ARG   A 1 307 ? -9.127  7.413   29.607 1.00 91.71  ? 603 ARG   A O   1 
ATOM   2390 C  CB  . ARG   A 1 307 ? -12.125 5.251   29.482 1.00 78.93  ? 603 ARG   A CB  1 
ATOM   2391 C  CG  . ARG   A 1 307 ? -12.372 3.754   29.373 1.00 76.61  ? 603 ARG   A CG  1 
ATOM   2392 C  CD  . ARG   A 1 307 ? -11.879 3.215   28.030 1.00 78.16  ? 603 ARG   A CD  1 
ATOM   2393 N  NE  . ARG   A 1 307 ? -12.515 3.919   26.927 1.00 72.65  ? 603 ARG   A NE  1 
ATOM   2394 C  CZ  . ARG   A 1 307 ? -13.798 3.788   26.618 1.00 72.66  ? 603 ARG   A CZ  1 
ATOM   2395 N  NH1 . ARG   A 1 307 ? -14.568 2.987   27.334 1.00 59.99  ? 603 ARG   A NH1 1 
ATOM   2396 N  NH2 . ARG   A 1 307 ? -14.317 4.454   25.596 1.00 84.80  ? 603 ARG   A NH2 1 
ATOM   2397 N  N   . TYR   A 1 308 ? -11.237 7.959   29.050 1.00 89.55  ? 604 TYR   A N   1 
ATOM   2398 C  CA  . TYR   A 1 308 ? -10.888 9.361   28.796 1.00 86.13  ? 604 TYR   A CA  1 
ATOM   2399 C  C   . TYR   A 1 308 ? -10.538 10.134  30.060 1.00 90.48  ? 604 TYR   A C   1 
ATOM   2400 O  O   . TYR   A 1 308 ? -9.793  11.122  29.979 1.00 86.70  ? 604 TYR   A O   1 
ATOM   2401 C  CB  . TYR   A 1 308 ? -12.023 10.078  28.072 1.00 81.28  ? 604 TYR   A CB  1 
ATOM   2402 C  CG  . TYR   A 1 308 ? -11.918 9.908   26.577 1.00 87.48  ? 604 TYR   A CG  1 
ATOM   2403 C  CD1 . TYR   A 1 308 ? -12.118 8.670   25.992 1.00 86.24  ? 604 TYR   A CD1 1 
ATOM   2404 C  CD2 . TYR   A 1 308 ? -11.596 10.978  25.756 1.00 96.29  ? 604 TYR   A CD2 1 
ATOM   2405 C  CE1 . TYR   A 1 308 ? -12.012 8.502   24.630 1.00 88.35  ? 604 TYR   A CE1 1 
ATOM   2406 C  CE2 . TYR   A 1 308 ? -11.483 10.818  24.384 1.00 97.93  ? 604 TYR   A CE2 1 
ATOM   2407 C  CZ  . TYR   A 1 308 ? -11.698 9.579   23.827 1.00 94.48  ? 604 TYR   A CZ  1 
ATOM   2408 O  OH  . TYR   A 1 308 ? -11.589 9.410   22.461 1.00 95.62  ? 604 TYR   A OH  1 
ATOM   2409 N  N   . ASN   A 1 309 ? -11.074 9.729   31.212 1.00 78.73  ? 605 ASN   A N   1 
ATOM   2410 C  CA  . ASN   A 1 309 ? -10.544 10.182  32.493 1.00 86.59  ? 605 ASN   A CA  1 
ATOM   2411 C  C   . ASN   A 1 309 ? -10.658 11.702  32.634 1.00 95.93  ? 605 ASN   A C   1 
ATOM   2412 O  O   . ASN   A 1 309 ? -9.687  12.393  32.959 1.00 102.45 ? 605 ASN   A O   1 
ATOM   2413 C  CB  . ASN   A 1 309 ? -9.092  9.725   32.637 1.00 90.82  ? 605 ASN   A CB  1 
ATOM   2414 C  CG  . ASN   A 1 309 ? -8.646  9.683   34.050 1.00 91.13  ? 605 ASN   A CG  1 
ATOM   2415 O  OD1 . ASN   A 1 309 ? -9.472  9.628   34.961 1.00 89.71  ? 605 ASN   A OD1 1 
ATOM   2416 N  ND2 . ASN   A 1 309 ? -7.333  9.705   34.259 1.00 93.25  ? 605 ASN   A ND2 1 
ATOM   2417 N  N   . ILE   A 1 310 ? -11.862 12.221  32.377 1.00 94.79  ? 606 ILE   A N   1 
ATOM   2418 C  CA  . ILE   A 1 310 ? -12.087 13.660  32.279 1.00 98.89  ? 606 ILE   A CA  1 
ATOM   2419 C  C   . ILE   A 1 310 ? -12.695 14.239  33.555 1.00 102.39 ? 606 ILE   A C   1 
ATOM   2420 O  O   . ILE   A 1 310 ? -13.040 15.424  33.585 1.00 104.75 ? 606 ILE   A O   1 
ATOM   2421 C  CB  . ILE   A 1 310 ? -12.960 14.005  31.059 1.00 98.29  ? 606 ILE   A CB  1 
ATOM   2422 C  CG1 . ILE   A 1 310 ? -14.402 13.565  31.306 1.00 92.92  ? 606 ILE   A CG1 1 
ATOM   2423 C  CG2 . ILE   A 1 310 ? -12.416 13.335  29.800 1.00 92.52  ? 606 ILE   A CG2 1 
ATOM   2424 C  CD1 . ILE   A 1 310 ? -15.394 14.173  30.381 1.00 85.41  ? 606 ILE   A CD1 1 
ATOM   2425 N  N   . LEU   A 1 311 ? -12.833 13.434  34.614 1.00 99.52  ? 607 LEU   A N   1 
ATOM   2426 C  CA  . LEU   A 1 311 ? -13.276 13.993  35.890 1.00 97.43  ? 607 LEU   A CA  1 
ATOM   2427 C  C   . LEU   A 1 311 ? -12.312 15.065  36.380 1.00 102.19 ? 607 LEU   A C   1 
ATOM   2428 O  O   . LEU   A 1 311 ? -12.744 16.082  36.932 1.00 102.08 ? 607 LEU   A O   1 
ATOM   2429 C  CB  . LEU   A 1 311 ? -13.430 12.894  36.941 1.00 82.24  ? 607 LEU   A CB  1 
ATOM   2430 C  CG  . LEU   A 1 311 ? -14.710 12.057  36.912 1.00 75.90  ? 607 LEU   A CG  1 
ATOM   2431 C  CD1 . LEU   A 1 311 ? -14.693 11.002  38.020 1.00 79.17  ? 607 LEU   A CD1 1 
ATOM   2432 C  CD2 . LEU   A 1 311 ? -15.945 12.930  37.021 1.00 77.92  ? 607 LEU   A CD2 1 
ATOM   2433 N  N   . GLU   A 1 312 ? -11.006 14.857  36.171 1.00 111.74 ? 608 GLU   A N   1 
ATOM   2434 C  CA  . GLU   A 1 312 ? -9.987  15.844  36.534 1.00 126.01 ? 608 GLU   A CA  1 
ATOM   2435 C  C   . GLU   A 1 312 ? -10.347 17.242  36.039 1.00 122.51 ? 608 GLU   A C   1 
ATOM   2436 O  O   . GLU   A 1 312 ? -10.445 18.195  36.821 1.00 120.32 ? 608 GLU   A O   1 
ATOM   2437 C  CB  . GLU   A 1 312 ? -8.633  15.426  35.951 1.00 137.45 ? 608 GLU   A CB  1 
ATOM   2438 C  CG  . GLU   A 1 312 ? -7.936  14.271  36.655 1.00 137.40 ? 608 GLU   A CG  1 
ATOM   2439 C  CD  . GLU   A 1 312 ? -7.004  14.743  37.751 1.00 142.96 ? 608 GLU   A CD  1 
ATOM   2440 O  OE1 . GLU   A 1 312 ? -7.435  15.582  38.565 1.00 145.94 ? 608 GLU   A OE1 1 
ATOM   2441 O  OE2 . GLU   A 1 312 ? -5.839  14.292  37.790 1.00 144.51 ? 608 GLU   A OE2 1 
ATOM   2442 N  N   . GLU   A 1 313 ? -10.536 17.377  34.728 1.00 118.99 ? 609 GLU   A N   1 
ATOM   2443 C  CA  . GLU   A 1 313 ? -10.709 18.697  34.137 1.00 127.87 ? 609 GLU   A CA  1 
ATOM   2444 C  C   . GLU   A 1 313 ? -12.101 19.260  34.378 1.00 122.17 ? 609 GLU   A C   1 
ATOM   2445 O  O   . GLU   A 1 313 ? -12.251 20.465  34.608 1.00 126.58 ? 609 GLU   A O   1 
ATOM   2446 C  CB  . GLU   A 1 313 ? -10.413 18.646  32.640 1.00 138.41 ? 609 GLU   A CB  1 
ATOM   2447 C  CG  . GLU   A 1 313 ? -8.962  18.937  32.292 1.00 151.41 ? 609 GLU   A CG  1 
ATOM   2448 C  CD  . GLU   A 1 313 ? -8.578  20.402  32.496 1.00 163.51 ? 609 GLU   A CD  1 
ATOM   2449 O  OE1 . GLU   A 1 313 ? -8.574  20.885  33.654 1.00 162.65 ? 609 GLU   A OE1 1 
ATOM   2450 O  OE2 . GLU   A 1 313 ? -8.280  21.075  31.482 1.00 168.67 ? 609 GLU   A OE2 1 
ATOM   2451 N  N   . VAL   A 1 314 ? -13.133 18.421  34.320 1.00 112.21 ? 610 VAL   A N   1 
ATOM   2452 C  CA  . VAL   A 1 314 ? -14.472 18.962  34.510 1.00 109.92 ? 610 VAL   A CA  1 
ATOM   2453 C  C   . VAL   A 1 314 ? -14.652 19.450  35.947 1.00 113.15 ? 610 VAL   A C   1 
ATOM   2454 O  O   . VAL   A 1 314 ? -15.362 20.435  36.191 1.00 109.90 ? 610 VAL   A O   1 
ATOM   2455 C  CB  . VAL   A 1 314 ? -15.529 17.921  34.103 1.00 104.72 ? 610 VAL   A CB  1 
ATOM   2456 C  CG1 . VAL   A 1 314 ? -16.927 18.483  34.293 1.00 99.67  ? 610 VAL   A CG1 1 
ATOM   2457 C  CG2 . VAL   A 1 314 ? -15.322 17.511  32.645 1.00 107.92 ? 610 VAL   A CG2 1 
ATOM   2458 N  N   . ALA   A 1 315 ? -14.001 18.800  36.915 1.00 112.26 ? 611 ALA   A N   1 
ATOM   2459 C  CA  . ALA   A 1 315 ? -14.024 19.319  38.277 1.00 117.75 ? 611 ALA   A CA  1 
ATOM   2460 C  C   . ALA   A 1 315 ? -13.311 20.657  38.356 1.00 124.06 ? 611 ALA   A C   1 
ATOM   2461 O  O   . ALA   A 1 315 ? -13.740 21.554  39.089 1.00 131.18 ? 611 ALA   A O   1 
ATOM   2462 C  CB  . ALA   A 1 315 ? -13.383 18.326  39.240 1.00 101.19 ? 611 ALA   A CB  1 
ATOM   2463 N  N   . LYS   A 1 316 ? -12.209 20.798  37.620 1.00 123.96 ? 612 LYS   A N   1 
ATOM   2464 C  CA  . LYS   A 1 316 ? -11.440 22.032  37.608 1.00 131.06 ? 612 LYS   A CA  1 
ATOM   2465 C  C   . LYS   A 1 316 ? -12.338 23.211  37.274 1.00 138.15 ? 612 LYS   A C   1 
ATOM   2466 O  O   . LYS   A 1 316 ? -12.596 24.070  38.129 1.00 134.57 ? 612 LYS   A O   1 
ATOM   2467 C  CB  . LYS   A 1 316 ? -10.291 21.949  36.600 1.00 130.75 ? 612 LYS   A CB  1 
ATOM   2468 C  CG  . LYS   A 1 316 ? -8.997  21.409  37.172 1.00 131.40 ? 612 LYS   A CG  1 
ATOM   2469 C  CD  . LYS   A 1 316 ? -7.798  22.013  36.442 1.00 139.29 ? 612 LYS   A CD  1 
ATOM   2470 C  CE  . LYS   A 1 316 ? -7.822  23.543  36.490 1.00 146.68 ? 612 LYS   A CE  1 
ATOM   2471 N  NZ  . LYS   A 1 316 ? -6.623  24.194  35.875 1.00 150.38 ? 612 LYS   A NZ  1 
ATOM   2472 N  N   . LYS   A 1 317 ? -12.847 23.228  36.044 1.00 122.83 ? 613 LYS   A N   1 
ATOM   2473 C  CA  . LYS   A 1 317 ? -13.606 24.344  35.494 1.00 134.38 ? 613 LYS   A CA  1 
ATOM   2474 C  C   . LYS   A 1 317 ? -14.961 24.543  36.161 1.00 131.39 ? 613 LYS   A C   1 
ATOM   2475 O  O   . LYS   A 1 317 ? -15.698 25.451  35.760 1.00 132.48 ? 613 LYS   A O   1 
ATOM   2476 C  CB  . LYS   A 1 317 ? -13.780 24.151  33.984 1.00 124.99 ? 613 LYS   A CB  1 
ATOM   2477 C  CG  . LYS   A 1 317 ? -12.544 24.501  33.185 1.00 133.28 ? 613 LYS   A CG  1 
ATOM   2478 C  CD  . LYS   A 1 317 ? -12.253 23.436  32.163 1.00 126.16 ? 613 LYS   A CD  1 
ATOM   2479 C  CE  . LYS   A 1 317 ? -10.835 23.535  31.633 1.00 129.09 ? 613 LYS   A CE  1 
ATOM   2480 N  NZ  . LYS   A 1 317 ? -10.570 22.452  30.632 1.00 121.95 ? 613 LYS   A NZ  1 
ATOM   2481 N  N   . MET   A 1 318 ? -15.315 23.722  37.146 1.00 141.69 ? 614 MET   A N   1 
ATOM   2482 C  CA  . MET   A 1 318 ? -16.410 24.041  38.048 1.00 147.36 ? 614 MET   A CA  1 
ATOM   2483 C  C   . MET   A 1 318 ? -15.924 24.677  39.340 1.00 158.60 ? 614 MET   A C   1 
ATOM   2484 O  O   . MET   A 1 318 ? -16.751 25.163  40.118 1.00 167.89 ? 614 MET   A O   1 
ATOM   2485 C  CB  . MET   A 1 318 ? -17.218 22.781  38.372 1.00 139.08 ? 614 MET   A CB  1 
ATOM   2486 C  CG  . MET   A 1 318 ? -17.824 22.110  37.159 1.00 135.41 ? 614 MET   A CG  1 
ATOM   2487 S  SD  . MET   A 1 318 ? -18.619 20.536  37.544 1.00 124.93 ? 614 MET   A SD  1 
ATOM   2488 C  CE  . MET   A 1 318 ? -19.928 21.084  38.636 1.00 126.81 ? 614 MET   A CE  1 
ATOM   2489 N  N   . ASP   A 1 319 ? -14.606 24.697  39.567 1.00 161.49 ? 615 ASP   A N   1 
ATOM   2490 C  CA  . ASP   A 1 319 ? -14.000 25.132  40.824 1.00 165.57 ? 615 ASP   A CA  1 
ATOM   2491 C  C   . ASP   A 1 319 ? -14.589 24.340  41.984 1.00 156.08 ? 615 ASP   A C   1 
ATOM   2492 O  O   . ASP   A 1 319 ? -15.537 24.789  42.637 1.00 160.60 ? 615 ASP   A O   1 
ATOM   2493 C  CB  . ASP   A 1 319 ? -14.183 26.640  41.027 1.00 174.56 ? 615 ASP   A CB  1 
ATOM   2494 C  CG  . ASP   A 1 319 ? -12.888 27.342  41.412 1.00 181.88 ? 615 ASP   A CG  1 
ATOM   2495 O  OD1 . ASP   A 1 319 ? -11.873 27.160  40.705 1.00 181.94 ? 615 ASP   A OD1 1 
ATOM   2496 O  OD2 . ASP   A 1 319 ? -12.893 28.096  42.408 1.00 186.84 ? 615 ASP   A OD2 1 
ATOM   2497 N  N   . LEU   A 1 320 ? -14.036 23.157  42.243 1.00 145.38 ? 616 LEU   A N   1 
ATOM   2498 C  CA  . LEU   A 1 320 ? -14.566 22.243  43.244 1.00 133.22 ? 616 LEU   A CA  1 
ATOM   2499 C  C   . LEU   A 1 320 ? -13.471 21.854  44.225 1.00 135.92 ? 616 LEU   A C   1 
ATOM   2500 O  O   . LEU   A 1 320 ? -12.282 21.880  43.894 1.00 139.32 ? 616 LEU   A O   1 
ATOM   2501 C  CB  . LEU   A 1 320 ? -15.153 20.977  42.592 1.00 116.72 ? 616 LEU   A CB  1 
ATOM   2502 C  CG  . LEU   A 1 320 ? -16.389 21.196  41.722 1.00 117.93 ? 616 LEU   A CG  1 
ATOM   2503 C  CD1 . LEU   A 1 320 ? -16.929 19.864  41.227 1.00 115.06 ? 616 LEU   A CD1 1 
ATOM   2504 C  CD2 . LEU   A 1 320 ? -17.460 21.972  42.471 1.00 120.78 ? 616 LEU   A CD2 1 
ATOM   2505 N  N   . ASP   A 1 321 ? -13.887 21.486  45.438 1.00 133.69 ? 617 ASP   A N   1 
ATOM   2506 C  CA  . ASP   A 1 321 ? -12.948 21.033  46.456 1.00 136.39 ? 617 ASP   A CA  1 
ATOM   2507 C  C   . ASP   A 1 321 ? -12.301 19.736  45.997 1.00 123.60 ? 617 ASP   A C   1 
ATOM   2508 O  O   . ASP   A 1 321 ? -12.805 18.650  46.297 1.00 114.75 ? 617 ASP   A O   1 
ATOM   2509 C  CB  . ASP   A 1 321 ? -13.656 20.835  47.804 1.00 142.19 ? 617 ASP   A CB  1 
ATOM   2510 C  CG  . ASP   A 1 321 ? -12.689 20.514  48.945 1.00 149.86 ? 617 ASP   A CG  1 
ATOM   2511 O  OD1 . ASP   A 1 321 ? -13.160 20.290  50.083 1.00 148.56 ? 617 ASP   A OD1 1 
ATOM   2512 O  OD2 . ASP   A 1 321 ? -11.461 20.501  48.715 1.00 154.64 ? 617 ASP   A OD2 1 
ATOM   2513 N  N   . MET   A 1 322 ? -11.190 19.830  45.268 1.00 126.11 ? 618 MET   A N   1 
ATOM   2514 C  CA  . MET   A 1 322 ? -10.475 18.635  44.841 1.00 134.81 ? 618 MET   A CA  1 
ATOM   2515 C  C   . MET   A 1 322 ? -9.398  18.208  45.829 1.00 148.43 ? 618 MET   A C   1 
ATOM   2516 O  O   . MET   A 1 322 ? -8.793  17.146  45.642 1.00 147.38 ? 618 MET   A O   1 
ATOM   2517 C  CB  . MET   A 1 322 ? -9.857  18.844  43.448 1.00 133.16 ? 618 MET   A CB  1 
ATOM   2518 C  CG  . MET   A 1 322 ? -10.871 18.763  42.316 1.00 129.89 ? 618 MET   A CG  1 
ATOM   2519 S  SD  . MET   A 1 322 ? -10.181 18.894  40.652 1.00 132.11 ? 618 MET   A SD  1 
ATOM   2520 C  CE  . MET   A 1 322 ? -8.930  17.610  40.651 1.00 129.63 ? 618 MET   A CE  1 
ATOM   2521 N  N   . ARG   A 1 323 ? -9.153  19.006  46.873 1.00 159.89 ? 619 ARG   A N   1 
ATOM   2522 C  CA  . ARG   A 1 323 ? -8.214  18.605  47.914 1.00 162.66 ? 619 ARG   A CA  1 
ATOM   2523 C  C   . ARG   A 1 323 ? -8.640  17.292  48.557 1.00 156.65 ? 619 ARG   A C   1 
ATOM   2524 O  O   . ARG   A 1 323 ? -7.817  16.393  48.764 1.00 159.73 ? 619 ARG   A O   1 
ATOM   2525 C  CB  . ARG   A 1 323 ? -8.112  19.699  48.981 1.00 171.41 ? 619 ARG   A CB  1 
ATOM   2526 C  CG  . ARG   A 1 323 ? -7.689  21.066  48.480 1.00 180.47 ? 619 ARG   A CG  1 
ATOM   2527 C  CD  . ARG   A 1 323 ? -8.421  22.178  49.231 1.00 185.90 ? 619 ARG   A CD  1 
ATOM   2528 N  NE  . ARG   A 1 323 ? -9.584  22.656  48.486 1.00 186.95 ? 619 ARG   A NE  1 
ATOM   2529 C  CZ  . ARG   A 1 323 ? -10.328 23.700  48.841 1.00 190.53 ? 619 ARG   A CZ  1 
ATOM   2530 N  NH1 . ARG   A 1 323 ? -10.034 24.381  49.940 1.00 194.05 ? 619 ARG   A NH1 1 
ATOM   2531 N  NH2 . ARG   A 1 323 ? -11.363 24.064  48.092 1.00 188.97 ? 619 ARG   A NH2 1 
ATOM   2532 N  N   . LYS   A 1 324 ? -9.924  17.161  48.870 1.00 145.83 ? 620 LYS   A N   1 
ATOM   2533 C  CA  . LYS   A 1 324 ? -10.428 16.072  49.684 1.00 132.32 ? 620 LYS   A CA  1 
ATOM   2534 C  C   . LYS   A 1 324 ? -11.226 15.096  48.832 1.00 124.80 ? 620 LYS   A C   1 
ATOM   2535 O  O   . LYS   A 1 324 ? -11.726 15.428  47.752 1.00 128.15 ? 620 LYS   A O   1 
ATOM   2536 C  CB  . LYS   A 1 324 ? -11.294 16.603  50.832 1.00 132.27 ? 620 LYS   A CB  1 
ATOM   2537 C  CG  . LYS   A 1 324 ? -10.506 17.048  52.069 1.00 136.13 ? 620 LYS   A CG  1 
ATOM   2538 C  CD  . LYS   A 1 324 ? -9.626  18.275  51.810 1.00 139.91 ? 620 LYS   A CD  1 
ATOM   2539 C  CE  . LYS   A 1 324 ? -8.621  18.526  52.937 1.00 138.92 ? 620 LYS   A CE  1 
ATOM   2540 N  NZ  . LYS   A 1 324 ? -7.595  19.532  52.537 1.00 139.66 ? 620 LYS   A NZ  1 
ATOM   2541 N  N   . THR   A 1 325 ? -11.322 13.870  49.335 1.00 112.15 ? 621 THR   A N   1 
ATOM   2542 C  CA  . THR   A 1 325 ? -12.108 12.839  48.669 1.00 105.54 ? 621 THR   A CA  1 
ATOM   2543 C  C   . THR   A 1 325 ? -13.597 12.985  48.984 1.00 106.74 ? 621 THR   A C   1 
ATOM   2544 O  O   . THR   A 1 325 ? -14.447 12.816  48.098 1.00 83.88  ? 621 THR   A O   1 
ATOM   2545 C  CB  . THR   A 1 325 ? -11.585 11.455  49.086 1.00 99.64  ? 621 THR   A CB  1 
ATOM   2546 O  OG1 . THR   A 1 325 ? -12.481 10.429  48.651 1.00 90.53  ? 621 THR   A OG1 1 
ATOM   2547 C  CG2 . THR   A 1 325 ? -11.383 11.373  50.633 1.00 110.30 ? 621 THR   A CG2 1 
ATOM   2548 N  N   . SER   A 1 326 ? -13.918 13.345  50.232 1.00 110.22 ? 622 SER   A N   1 
ATOM   2549 C  CA  . SER   A 1 326 ? -15.274 13.373  50.769 1.00 99.22  ? 622 SER   A CA  1 
ATOM   2550 C  C   . SER   A 1 326 ? -16.076 14.575  50.299 1.00 98.26  ? 622 SER   A C   1 
ATOM   2551 O  O   . SER   A 1 326 ? -17.248 14.701  50.672 1.00 90.36  ? 622 SER   A O   1 
ATOM   2552 C  CB  . SER   A 1 326 ? -15.205 13.350  52.293 1.00 90.63  ? 622 SER   A CB  1 
ATOM   2553 O  OG  . SER   A 1 326 ? -13.884 13.646  52.698 1.00 95.47  ? 622 SER   A OG  1 
ATOM   2554 N  N   . SER   A 1 327 ? -15.473 15.461  49.509 1.00 105.17 ? 623 SER   A N   1 
ATOM   2555 C  CA  . SER   A 1 327 ? -16.196 16.574  48.911 1.00 111.39 ? 623 SER   A CA  1 
ATOM   2556 C  C   . SER   A 1 327 ? -17.105 16.145  47.767 1.00 98.24  ? 623 SER   A C   1 
ATOM   2557 O  O   . SER   A 1 327 ? -17.870 16.980  47.270 1.00 96.26  ? 623 SER   A O   1 
ATOM   2558 C  CB  . SER   A 1 327 ? -15.203 17.613  48.405 1.00 120.83 ? 623 SER   A CB  1 
ATOM   2559 O  OG  . SER   A 1 327 ? -14.321 17.031  47.458 1.00 117.02 ? 623 SER   A OG  1 
ATOM   2560 N  N   . LEU   A 1 328 ? -17.015 14.885  47.326 1.00 98.94  ? 624 LEU   A N   1 
ATOM   2561 C  CA  . LEU   A 1 328 ? -17.832 14.345  46.226 1.00 93.46  ? 624 LEU   A CA  1 
ATOM   2562 C  C   . LEU   A 1 328 ? -17.688 15.175  44.953 1.00 98.46  ? 624 LEU   A C   1 
ATOM   2563 O  O   . LEU   A 1 328 ? -18.613 15.270  44.140 1.00 96.51  ? 624 LEU   A O   1 
ATOM   2564 C  CB  . LEU   A 1 328 ? -19.305 14.217  46.633 1.00 87.97  ? 624 LEU   A CB  1 
ATOM   2565 C  CG  . LEU   A 1 328 ? -19.579 13.361  47.878 1.00 88.36  ? 624 LEU   A CG  1 
ATOM   2566 C  CD1 . LEU   A 1 328 ? -21.029 12.909  47.918 1.00 81.68  ? 624 LEU   A CD1 1 
ATOM   2567 C  CD2 . LEU   A 1 328 ? -18.648 12.171  47.906 1.00 87.49  ? 624 LEU   A CD2 1 
ATOM   2568 N  N   . TRP   A 1 329 ? -16.516 15.783  44.769 1.00 99.74  ? 625 TRP   A N   1 
ATOM   2569 C  CA  . TRP   A 1 329 ? -16.295 16.556  43.558 1.00 104.58 ? 625 TRP   A CA  1 
ATOM   2570 C  C   . TRP   A 1 329 ? -16.388 15.666  42.328 1.00 103.22 ? 625 TRP   A C   1 
ATOM   2571 O  O   . TRP   A 1 329 ? -16.846 16.109  41.273 1.00 101.25 ? 625 TRP   A O   1 
ATOM   2572 C  CB  . TRP   A 1 329 ? -14.944 17.259  43.614 1.00 108.70 ? 625 TRP   A CB  1 
ATOM   2573 C  CG  . TRP   A 1 329 ? -13.785 16.331  43.744 1.00 109.56 ? 625 TRP   A CG  1 
ATOM   2574 C  CD1 . TRP   A 1 329 ? -13.237 15.879  44.893 1.00 111.58 ? 625 TRP   A CD1 1 
ATOM   2575 C  CD2 . TRP   A 1 329 ? -13.020 15.748  42.678 1.00 114.17 ? 625 TRP   A CD2 1 
ATOM   2576 N  NE1 . TRP   A 1 329 ? -12.178 15.046  44.624 1.00 112.16 ? 625 TRP   A NE1 1 
ATOM   2577 C  CE2 . TRP   A 1 329 ? -12.024 14.949  43.269 1.00 115.25 ? 625 TRP   A CE2 1 
ATOM   2578 C  CE3 . TRP   A 1 329 ? -13.085 15.818  41.285 1.00 105.99 ? 625 TRP   A CE3 1 
ATOM   2579 C  CZ2 . TRP   A 1 329 ? -11.099 14.226  42.516 1.00 112.50 ? 625 TRP   A CZ2 1 
ATOM   2580 C  CZ3 . TRP   A 1 329 ? -12.159 15.112  40.540 1.00 105.82 ? 625 TRP   A CZ3 1 
ATOM   2581 C  CH2 . TRP   A 1 329 ? -11.181 14.327  41.157 1.00 106.97 ? 625 TRP   A CH2 1 
ATOM   2582 N  N   . LYS   A 1 330 ? -15.973 14.401  42.455 1.00 100.51 ? 626 LYS   A N   1 
ATOM   2583 C  CA  . LYS   A 1 330 ? -16.084 13.457  41.344 1.00 98.83  ? 626 LYS   A CA  1 
ATOM   2584 C  C   . LYS   A 1 330 ? -17.541 13.197  40.981 1.00 92.90  ? 626 LYS   A C   1 
ATOM   2585 O  O   . LYS   A 1 330 ? -17.901 13.183  39.801 1.00 99.05  ? 626 LYS   A O   1 
ATOM   2586 C  CB  . LYS   A 1 330 ? -15.379 12.141  41.693 1.00 100.94 ? 626 LYS   A CB  1 
ATOM   2587 C  CG  . LYS   A 1 330 ? -13.879 12.162  41.476 1.00 97.31  ? 626 LYS   A CG  1 
ATOM   2588 C  CD  . LYS   A 1 330 ? -13.241 10.792  41.643 1.00 83.54  ? 626 LYS   A CD  1 
ATOM   2589 C  CE  . LYS   A 1 330 ? -11.738 10.912  41.446 1.00 82.00  ? 626 LYS   A CE  1 
ATOM   2590 N  NZ  . LYS   A 1 330 ? -10.950 9.713   41.835 1.00 82.62  ? 626 LYS   A NZ  1 
ATOM   2591 N  N   . ASP   A 1 331 ? -18.394 12.975  41.985 1.00 88.83  ? 627 ASP   A N   1 
ATOM   2592 C  CA  . ASP   A 1 331 ? -19.811 12.739  41.722 1.00 84.78  ? 627 ASP   A CA  1 
ATOM   2593 C  C   . ASP   A 1 331 ? -20.439 13.935  41.032 1.00 86.81  ? 627 ASP   A C   1 
ATOM   2594 O  O   . ASP   A 1 331 ? -21.113 13.790  40.001 1.00 88.66  ? 627 ASP   A O   1 
ATOM   2595 C  CB  . ASP   A 1 331 ? -20.549 12.441  43.026 1.00 87.88  ? 627 ASP   A CB  1 
ATOM   2596 C  CG  . ASP   A 1 331 ? -19.984 11.230  43.745 1.00 85.45  ? 627 ASP   A CG  1 
ATOM   2597 O  OD1 . ASP   A 1 331 ? -18.866 11.344  44.274 1.00 71.26  ? 627 ASP   A OD1 1 
ATOM   2598 O  OD2 . ASP   A 1 331 ? -20.630 10.161  43.734 1.00 73.40  ? 627 ASP   A OD2 1 
ATOM   2599 N  N   . GLN   A 1 332 ? -20.218 15.126  41.598 1.00 82.76  ? 628 GLN   A N   1 
ATOM   2600 C  CA  . GLN   A 1 332 ? -20.751 16.372  41.053 1.00 99.58  ? 628 GLN   A CA  1 
ATOM   2601 C  C   . GLN   A 1 332 ? -20.380 16.551  39.586 1.00 97.93  ? 628 GLN   A C   1 
ATOM   2602 O  O   . GLN   A 1 332 ? -21.235 16.868  38.750 1.00 93.97  ? 628 GLN   A O   1 
ATOM   2603 C  CB  . GLN   A 1 332 ? -20.220 17.539  41.888 1.00 116.41 ? 628 GLN   A CB  1 
ATOM   2604 C  CG  . GLN   A 1 332 ? -20.996 18.838  41.763 1.00 125.45 ? 628 GLN   A CG  1 
ATOM   2605 C  CD  . GLN   A 1 332 ? -22.131 18.925  42.765 1.00 125.58 ? 628 GLN   A CD  1 
ATOM   2606 O  OE1 . GLN   A 1 332 ? -22.032 19.623  43.797 1.00 99.85  ? 628 GLN   A OE1 1 
ATOM   2607 N  NE2 . GLN   A 1 332 ? -23.226 18.208  42.469 1.00 113.73 ? 628 GLN   A NE2 1 
ATOM   2608 N  N   . ALA   A 1 333 ? -19.097 16.372  39.263 1.00 99.17  ? 629 ALA   A N   1 
ATOM   2609 C  CA  . ALA   A 1 333 ? -18.632 16.531  37.895 1.00 100.09 ? 629 ALA   A CA  1 
ATOM   2610 C  C   . ALA   A 1 333 ? -19.207 15.454  36.983 1.00 105.76 ? 629 ALA   A C   1 
ATOM   2611 O  O   . ALA   A 1 333 ? -19.338 15.670  35.774 1.00 105.70 ? 629 ALA   A O   1 
ATOM   2612 C  CB  . ALA   A 1 333 ? -17.103 16.508  37.856 1.00 96.76  ? 629 ALA   A CB  1 
ATOM   2613 N  N   . LEU   A 1 334 ? -19.572 14.302  37.543 1.00 102.22 ? 630 LEU   A N   1 
ATOM   2614 C  CA  . LEU   A 1 334 ? -20.145 13.242  36.728 1.00 94.09  ? 630 LEU   A CA  1 
ATOM   2615 C  C   . LEU   A 1 334 ? -21.560 13.598  36.283 1.00 94.12  ? 630 LEU   A C   1 
ATOM   2616 O  O   . LEU   A 1 334 ? -21.905 13.448  35.103 1.00 104.92 ? 630 LEU   A O   1 
ATOM   2617 C  CB  . LEU   A 1 334 ? -20.136 11.925  37.501 1.00 94.33  ? 630 LEU   A CB  1 
ATOM   2618 C  CG  . LEU   A 1 334 ? -20.475 10.677  36.681 1.00 96.77  ? 630 LEU   A CG  1 
ATOM   2619 C  CD1 . LEU   A 1 334 ? -19.220 10.045  36.121 1.00 99.12  ? 630 LEU   A CD1 1 
ATOM   2620 C  CD2 . LEU   A 1 334 ? -21.251 9.679   37.515 1.00 94.58  ? 630 LEU   A CD2 1 
ATOM   2621 N  N   . VAL   A 1 335 ? -22.390 14.086  37.211 1.00 85.32  ? 631 VAL   A N   1 
ATOM   2622 C  CA  . VAL   A 1 335 ? -23.782 14.402  36.889 1.00 88.43  ? 631 VAL   A CA  1 
ATOM   2623 C  C   . VAL   A 1 335 ? -23.881 15.475  35.801 1.00 92.24  ? 631 VAL   A C   1 
ATOM   2624 O  O   . VAL   A 1 335 ? -24.763 15.400  34.933 1.00 92.77  ? 631 VAL   A O   1 
ATOM   2625 C  CB  . VAL   A 1 335 ? -24.547 14.814  38.164 1.00 98.13  ? 631 VAL   A CB  1 
ATOM   2626 C  CG1 . VAL   A 1 335 ? -25.943 15.290  37.812 1.00 105.69 ? 631 VAL   A CG1 1 
ATOM   2627 C  CG2 . VAL   A 1 335 ? -24.647 13.649  39.116 1.00 94.26  ? 631 VAL   A CG2 1 
ATOM   2628 N  N   . GLU   A 1 336 ? -22.981 16.469  35.814 1.00 87.38  ? 632 GLU   A N   1 
ATOM   2629 C  CA  . GLU   A 1 336 ? -22.986 17.523  34.791 1.00 102.65 ? 632 GLU   A CA  1 
ATOM   2630 C  C   . GLU   A 1 336 ? -22.616 16.969  33.423 1.00 98.02  ? 632 GLU   A C   1 
ATOM   2631 O  O   . GLU   A 1 336 ? -23.286 17.248  32.421 1.00 97.38  ? 632 GLU   A O   1 
ATOM   2632 C  CB  . GLU   A 1 336 ? -22.000 18.635  35.156 1.00 111.04 ? 632 GLU   A CB  1 
ATOM   2633 C  CG  . GLU   A 1 336 ? -22.126 19.186  36.541 1.00 118.81 ? 632 GLU   A CG  1 
ATOM   2634 C  CD  . GLU   A 1 336 ? -23.325 20.081  36.694 1.00 125.98 ? 632 GLU   A CD  1 
ATOM   2635 O  OE1 . GLU   A 1 336 ? -23.896 20.505  35.658 1.00 127.13 ? 632 GLU   A OE1 1 
ATOM   2636 O  OE2 . GLU   A 1 336 ? -23.690 20.359  37.860 1.00 126.57 ? 632 GLU   A OE2 1 
ATOM   2637 N  N   . ILE   A 1 337 ? -21.507 16.227  33.374 1.00 93.57  ? 633 ILE   A N   1 
ATOM   2638 C  CA  . ILE   A 1 337 ? -21.037 15.562  32.166 1.00 89.95  ? 633 ILE   A CA  1 
ATOM   2639 C  C   . ILE   A 1 337 ? -22.172 14.806  31.497 1.00 95.23  ? 633 ILE   A C   1 
ATOM   2640 O  O   . ILE   A 1 337 ? -22.339 14.865  30.276 1.00 89.51  ? 633 ILE   A O   1 
ATOM   2641 C  CB  . ILE   A 1 337 ? -19.854 14.632  32.497 1.00 81.07  ? 633 ILE   A CB  1 
ATOM   2642 C  CG1 . ILE   A 1 337 ? -18.628 15.475  32.862 1.00 84.64  ? 633 ILE   A CG1 1 
ATOM   2643 C  CG2 . ILE   A 1 337 ? -19.532 13.716  31.311 1.00 85.35  ? 633 ILE   A CG2 1 
ATOM   2644 C  CD1 . ILE   A 1 337 ? -17.413 14.651  33.240 1.00 83.74  ? 633 ILE   A CD1 1 
ATOM   2645 N  N   . ASN   A 1 338 ? -22.998 14.124  32.289 1.00 95.07  ? 634 ASN   A N   1 
ATOM   2646 C  CA  . ASN   A 1 338 ? -24.058 13.313  31.710 1.00 83.47  ? 634 ASN   A CA  1 
ATOM   2647 C  C   . ASN   A 1 338 ? -25.276 14.142  31.290 1.00 85.47  ? 634 ASN   A C   1 
ATOM   2648 O  O   . ASN   A 1 338 ? -25.948 13.781  30.314 1.00 77.36  ? 634 ASN   A O   1 
ATOM   2649 C  CB  . ASN   A 1 338 ? -24.430 12.200  32.687 1.00 75.53  ? 634 ASN   A CB  1 
ATOM   2650 C  CG  . ASN   A 1 338 ? -23.500 10.992  32.552 1.00 80.59  ? 634 ASN   A CG  1 
ATOM   2651 O  OD1 . ASN   A 1 338 ? -23.779 10.061  31.800 1.00 83.87  ? 634 ASN   A OD1 1 
ATOM   2652 N  ND2 . ASN   A 1 338 ? -22.367 11.037  33.232 1.00 73.99  ? 634 ASN   A ND2 1 
ATOM   2653 N  N   . ILE   A 1 339 ? -25.582 15.246  31.989 1.00 96.45  ? 635 ILE   A N   1 
ATOM   2654 C  CA  . ILE   A 1 339 ? -26.597 16.166  31.477 1.00 92.90  ? 635 ILE   A CA  1 
ATOM   2655 C  C   . ILE   A 1 339 ? -26.172 16.687  30.112 1.00 87.85  ? 635 ILE   A C   1 
ATOM   2656 O  O   . ILE   A 1 339 ? -26.995 16.828  29.202 1.00 94.19  ? 635 ILE   A O   1 
ATOM   2657 C  CB  . ILE   A 1 339 ? -26.855 17.315  32.471 1.00 96.09  ? 635 ILE   A CB  1 
ATOM   2658 C  CG1 . ILE   A 1 339 ? -27.514 16.768  33.734 1.00 83.47  ? 635 ILE   A CG1 1 
ATOM   2659 C  CG2 . ILE   A 1 339 ? -27.731 18.404  31.842 1.00 89.19  ? 635 ILE   A CG2 1 
ATOM   2660 C  CD1 . ILE   A 1 339 ? -27.862 17.796  34.744 1.00 87.69  ? 635 ILE   A CD1 1 
ATOM   2661 N  N   . ALA   A 1 340 ? -24.861 16.894  29.932 1.00 84.54  ? 636 ALA   A N   1 
ATOM   2662 C  CA  . ALA   A 1 340 ? -24.334 17.491  28.709 1.00 93.29  ? 636 ALA   A CA  1 
ATOM   2663 C  C   . ALA   A 1 340 ? -24.378 16.503  27.548 1.00 91.89  ? 636 ALA   A C   1 
ATOM   2664 O  O   . ALA   A 1 340 ? -24.808 16.850  26.440 1.00 95.37  ? 636 ALA   A O   1 
ATOM   2665 C  CB  . ALA   A 1 340 ? -22.907 17.982  28.948 1.00 92.32  ? 636 ALA   A CB  1 
ATOM   2666 N  N   . VAL   A 1 341 ? -23.912 15.274  27.779 1.00 93.11  ? 637 VAL   A N   1 
ATOM   2667 C  CA  . VAL   A 1 341 ? -24.009 14.235  26.758 1.00 87.87  ? 637 VAL   A CA  1 
ATOM   2668 C  C   . VAL   A 1 341 ? -25.446 14.125  26.274 1.00 90.92  ? 637 VAL   A C   1 
ATOM   2669 O  O   . VAL   A 1 341 ? -25.730 14.267  25.078 1.00 95.37  ? 637 VAL   A O   1 
ATOM   2670 C  CB  . VAL   A 1 341 ? -23.479 12.897  27.302 1.00 83.60  ? 637 VAL   A CB  1 
ATOM   2671 C  CG1 . VAL   A 1 341 ? -23.985 11.732  26.465 1.00 74.30  ? 637 VAL   A CG1 1 
ATOM   2672 C  CG2 . VAL   A 1 341 ? -21.960 12.905  27.320 1.00 83.92  ? 637 VAL   A CG2 1 
ATOM   2673 N  N   . LEU   A 1 342 ? -26.383 13.939  27.209 1.00 85.08  ? 638 LEU   A N   1 
ATOM   2674 C  CA  . LEU   A 1 342 ? -27.795 13.885  26.846 1.00 81.63  ? 638 LEU   A CA  1 
ATOM   2675 C  C   . LEU   A 1 342 ? -28.193 15.107  26.030 1.00 85.71  ? 638 LEU   A C   1 
ATOM   2676 O  O   . LEU   A 1 342 ? -28.615 14.985  24.872 1.00 75.36  ? 638 LEU   A O   1 
ATOM   2677 C  CB  . LEU   A 1 342 ? -28.666 13.771  28.098 1.00 81.64  ? 638 LEU   A CB  1 
ATOM   2678 C  CG  . LEU   A 1 342 ? -28.484 12.453  28.858 1.00 76.68  ? 638 LEU   A CG  1 
ATOM   2679 C  CD1 . LEU   A 1 342 ? -29.579 12.253  29.877 1.00 79.47  ? 638 LEU   A CD1 1 
ATOM   2680 C  CD2 . LEU   A 1 342 ? -28.442 11.305  27.877 1.00 65.37  ? 638 LEU   A CD2 1 
ATOM   2681 N  N   . TYR   A 1 343 ? -28.023 16.298  26.620 1.00 94.67  ? 639 TYR   A N   1 
ATOM   2682 C  CA  . TYR   A 1 343 ? -28.468 17.540  25.995 1.00 107.43 ? 639 TYR   A CA  1 
ATOM   2683 C  C   . TYR   A 1 343 ? -27.972 17.651  24.555 1.00 101.95 ? 639 TYR   A C   1 
ATOM   2684 O  O   . TYR   A 1 343 ? -28.763 17.837  23.626 1.00 106.27 ? 639 TYR   A O   1 
ATOM   2685 C  CB  . TYR   A 1 343 ? -28.007 18.743  26.828 1.00 113.69 ? 639 TYR   A CB  1 
ATOM   2686 C  CG  . TYR   A 1 343 ? -28.331 20.066  26.171 1.00 117.06 ? 639 TYR   A CG  1 
ATOM   2687 C  CD1 . TYR   A 1 343 ? -29.624 20.568  26.180 1.00 120.06 ? 639 TYR   A CD1 1 
ATOM   2688 C  CD2 . TYR   A 1 343 ? -27.349 20.797  25.523 1.00 122.49 ? 639 TYR   A CD2 1 
ATOM   2689 C  CE1 . TYR   A 1 343 ? -29.929 21.766  25.576 1.00 127.60 ? 639 TYR   A CE1 1 
ATOM   2690 C  CE2 . TYR   A 1 343 ? -27.642 21.997  24.912 1.00 129.62 ? 639 TYR   A CE2 1 
ATOM   2691 C  CZ  . TYR   A 1 343 ? -28.933 22.478  24.941 1.00 133.62 ? 639 TYR   A CZ  1 
ATOM   2692 O  OH  . TYR   A 1 343 ? -29.225 23.678  24.332 1.00 144.78 ? 639 TYR   A OH  1 
ATOM   2693 N  N   . SER   A 1 344 ? -26.659 17.502  24.357 1.00 98.84  ? 640 SER   A N   1 
ATOM   2694 C  CA  . SER   A 1 344 ? -26.069 17.588  23.022 1.00 93.35  ? 640 SER   A CA  1 
ATOM   2695 C  C   . SER   A 1 344 ? -26.741 16.637  22.044 1.00 93.53  ? 640 SER   A C   1 
ATOM   2696 O  O   . SER   A 1 344 ? -27.127 17.037  20.932 1.00 91.12  ? 640 SER   A O   1 
ATOM   2697 C  CB  . SER   A 1 344 ? -24.572 17.290  23.100 1.00 89.42  ? 640 SER   A CB  1 
ATOM   2698 O  OG  . SER   A 1 344 ? -23.969 18.041  24.147 1.00 98.09  ? 640 SER   A OG  1 
ATOM   2699 N  N   . PHE   A 1 345 ? -26.880 15.366  22.443 1.00 87.30  ? 641 PHE   A N   1 
ATOM   2700 C  CA  . PHE   A 1 345 ? -27.465 14.367  21.553 1.00 88.58  ? 641 PHE   A CA  1 
ATOM   2701 C  C   . PHE   A 1 345 ? -28.905 14.720  21.184 1.00 99.15  ? 641 PHE   A C   1 
ATOM   2702 O  O   . PHE   A 1 345 ? -29.345 14.456  20.060 1.00 100.86 ? 641 PHE   A O   1 
ATOM   2703 C  CB  . PHE   A 1 345 ? -27.412 12.983  22.206 1.00 81.45  ? 641 PHE   A CB  1 
ATOM   2704 C  CG  . PHE   A 1 345 ? -26.186 12.158  21.849 1.00 67.51  ? 641 PHE   A CG  1 
ATOM   2705 C  CD1 . PHE   A 1 345 ? -24.909 12.561  22.229 1.00 74.81  ? 641 PHE   A CD1 1 
ATOM   2706 C  CD2 . PHE   A 1 345 ? -26.326 10.950  21.182 1.00 69.20  ? 641 PHE   A CD2 1 
ATOM   2707 C  CE1 . PHE   A 1 345 ? -23.794 11.785  21.911 1.00 67.97  ? 641 PHE   A CE1 1 
ATOM   2708 C  CE2 . PHE   A 1 345 ? -25.225 10.161  20.890 1.00 59.08  ? 641 PHE   A CE2 1 
ATOM   2709 C  CZ  . PHE   A 1 345 ? -23.957 10.578  21.231 1.00 64.22  ? 641 PHE   A CZ  1 
ATOM   2710 N  N   . GLN   A 1 346 ? -29.660 15.318  22.114 1.00 101.59 ? 642 GLN   A N   1 
ATOM   2711 C  CA  . GLN   A 1 346 ? -31.070 15.556  21.819 1.00 95.28  ? 642 GLN   A CA  1 
ATOM   2712 C  C   . GLN   A 1 346 ? -31.287 16.847  21.050 1.00 95.66  ? 642 GLN   A C   1 
ATOM   2713 O  O   . GLN   A 1 346 ? -32.205 16.921  20.232 1.00 90.45  ? 642 GLN   A O   1 
ATOM   2714 C  CB  . GLN   A 1 346 ? -31.897 15.593  23.091 1.00 93.99  ? 642 GLN   A CB  1 
ATOM   2715 C  CG  . GLN   A 1 346 ? -31.789 14.362  23.932 1.00 97.21  ? 642 GLN   A CG  1 
ATOM   2716 C  CD  . GLN   A 1 346 ? -32.151 14.657  25.363 1.00 106.32 ? 642 GLN   A CD  1 
ATOM   2717 O  OE1 . GLN   A 1 346 ? -31.517 15.488  26.010 1.00 106.57 ? 642 GLN   A OE1 1 
ATOM   2718 N  NE2 . GLN   A 1 346 ? -33.198 14.008  25.857 1.00 109.42 ? 642 GLN   A NE2 1 
ATOM   2719 N  N   . SER   A 1 347 ? -30.505 17.893  21.339 1.00 95.97  ? 643 SER   A N   1 
ATOM   2720 C  CA  . SER   A 1 347 ? -30.619 19.110  20.551 1.00 100.38 ? 643 SER   A CA  1 
ATOM   2721 C  C   . SER   A 1 347 ? -30.054 18.932  19.137 1.00 102.37 ? 643 SER   A C   1 
ATOM   2722 O  O   . SER   A 1 347 ? -30.089 19.885  18.345 1.00 107.00 ? 643 SER   A O   1 
ATOM   2723 C  CB  . SER   A 1 347 ? -29.916 20.281  21.261 1.00 96.92  ? 643 SER   A CB  1 
ATOM   2724 O  OG  . SER   A 1 347 ? -30.433 20.535  22.571 1.00 104.20 ? 643 SER   A OG  1 
ATOM   2725 N  N   . ASP   A 1 348 ? -29.535 17.741  18.820 1.00 106.94 ? 644 ASP   A N   1 
ATOM   2726 C  CA  . ASP   A 1 348 ? -29.076 17.376  17.485 1.00 108.76 ? 644 ASP   A CA  1 
ATOM   2727 C  C   . ASP   A 1 348 ? -29.973 16.339  16.820 1.00 113.91 ? 644 ASP   A C   1 
ATOM   2728 O  O   . ASP   A 1 348 ? -29.633 15.847  15.740 1.00 107.38 ? 644 ASP   A O   1 
ATOM   2729 C  CB  . ASP   A 1 348 ? -27.639 16.849  17.550 1.00 100.39 ? 644 ASP   A CB  1 
ATOM   2730 C  CG  . ASP   A 1 348 ? -26.609 17.953  17.626 1.00 105.96 ? 644 ASP   A CG  1 
ATOM   2731 O  OD1 . ASP   A 1 348 ? -26.998 19.134  17.766 1.00 113.18 ? 644 ASP   A OD1 1 
ATOM   2732 O  OD2 . ASP   A 1 348 ? -25.405 17.641  17.541 1.00 104.66 ? 644 ASP   A OD2 1 
ATOM   2733 N  N   . LYS   A 1 349 ? -31.100 15.989  17.445 1.00 125.09 ? 645 LYS   A N   1 
ATOM   2734 C  CA  . LYS   A 1 349 ? -32.022 14.962  16.951 1.00 125.64 ? 645 LYS   A CA  1 
ATOM   2735 C  C   . LYS   A 1 349 ? -31.337 13.610  16.752 1.00 114.95 ? 645 LYS   A C   1 
ATOM   2736 O  O   . LYS   A 1 349 ? -31.756 12.808  15.916 1.00 114.75 ? 645 LYS   A O   1 
ATOM   2737 C  CB  . LYS   A 1 349 ? -32.713 15.406  15.658 1.00 132.01 ? 645 LYS   A CB  1 
ATOM   2738 C  CG  . LYS   A 1 349 ? -34.207 15.130  15.643 1.00 137.17 ? 645 LYS   A CG  1 
ATOM   2739 C  CD  . LYS   A 1 349 ? -35.006 16.410  15.418 1.00 144.66 ? 645 LYS   A CD  1 
ATOM   2740 C  CE  . LYS   A 1 349 ? -36.473 16.226  15.790 1.00 147.90 ? 645 LYS   A CE  1 
ATOM   2741 N  NZ  . LYS   A 1 349 ? -36.642 15.919  17.243 1.00 148.54 ? 645 LYS   A NZ  1 
ATOM   2742 N  N   . VAL   A 1 350 ? -30.294 13.328  17.526 1.00 107.27 ? 646 VAL   A N   1 
ATOM   2743 C  CA  . VAL   A 1 350 ? -29.611 12.040  17.482 1.00 91.25  ? 646 VAL   A CA  1 
ATOM   2744 C  C   . VAL   A 1 350 ? -30.137 11.186  18.627 1.00 83.28  ? 646 VAL   A C   1 
ATOM   2745 O  O   . VAL   A 1 350 ? -30.100 11.605  19.794 1.00 83.61  ? 646 VAL   A O   1 
ATOM   2746 C  CB  . VAL   A 1 350 ? -28.086 12.210  17.556 1.00 83.75  ? 646 VAL   A CB  1 
ATOM   2747 C  CG1 . VAL   A 1 350 ? -27.401 10.847  17.575 1.00 74.60  ? 646 VAL   A CG1 1 
ATOM   2748 C  CG2 . VAL   A 1 350 ? -27.603 13.037  16.372 1.00 78.81  ? 646 VAL   A CG2 1 
ATOM   2749 N  N   . THR   A 1 351 ? -30.629 9.994   18.284 1.00 75.35  ? 647 THR   A N   1 
ATOM   2750 C  CA  . THR   A 1 351 ? -31.306 9.116   19.232 1.00 78.63  ? 647 THR   A CA  1 
ATOM   2751 C  C   . THR   A 1 351 ? -30.408 8.826   20.427 1.00 75.84  ? 647 THR   A C   1 
ATOM   2752 O  O   . THR   A 1 351 ? -29.230 8.498   20.270 1.00 77.67  ? 647 THR   A O   1 
ATOM   2753 C  CB  . THR   A 1 351 ? -31.709 7.797   18.542 1.00 76.71  ? 647 THR   A CB  1 
ATOM   2754 O  OG1 . THR   A 1 351 ? -32.427 8.071   17.325 1.00 84.54  ? 647 THR   A OG1 1 
ATOM   2755 C  CG2 . THR   A 1 351 ? -32.581 6.921   19.485 1.00 71.64  ? 647 THR   A CG2 1 
ATOM   2756 N  N   . ILE   A 1 352 ? -30.961 8.976   21.631 1.00 80.95  ? 648 ILE   A N   1 
ATOM   2757 C  CA  . ILE   A 1 352 ? -30.242 8.645   22.858 1.00 68.73  ? 648 ILE   A CA  1 
ATOM   2758 C  C   . ILE   A 1 352 ? -31.286 8.436   23.946 1.00 73.69  ? 648 ILE   A C   1 
ATOM   2759 O  O   . ILE   A 1 352 ? -32.420 8.917   23.843 1.00 73.78  ? 648 ILE   A O   1 
ATOM   2760 C  CB  . ILE   A 1 352 ? -29.213 9.746   23.238 1.00 69.98  ? 648 ILE   A CB  1 
ATOM   2761 C  CG1 . ILE   A 1 352 ? -28.153 9.193   24.209 1.00 74.50  ? 648 ILE   A CG1 1 
ATOM   2762 C  CG2 . ILE   A 1 352 ? -29.894 10.921  23.885 1.00 64.45  ? 648 ILE   A CG2 1 
ATOM   2763 C  CD1 . ILE   A 1 352 ? -26.938 10.108  24.416 1.00 70.97  ? 648 ILE   A CD1 1 
ATOM   2764 N  N   . VAL   A 1 353 ? -30.913 7.691   24.990 1.00 64.74  ? 649 VAL   A N   1 
ATOM   2765 C  CA  . VAL   A 1 353 ? -31.811 7.393   26.092 1.00 72.83  ? 649 VAL   A CA  1 
ATOM   2766 C  C   . VAL   A 1 353 ? -31.061 7.674   27.393 1.00 75.21  ? 649 VAL   A C   1 
ATOM   2767 O  O   . VAL   A 1 353 ? -29.856 7.415   27.501 1.00 70.87  ? 649 VAL   A O   1 
ATOM   2768 C  CB  . VAL   A 1 353 ? -32.351 5.939   26.007 1.00 79.93  ? 649 VAL   A CB  1 
ATOM   2769 C  CG1 . VAL   A 1 353 ? -31.259 4.896   26.212 1.00 77.63  ? 649 VAL   A CG1 1 
ATOM   2770 C  CG2 . VAL   A 1 353 ? -33.533 5.719   26.951 1.00 73.70  ? 649 VAL   A CG2 1 
ATOM   2771 N  N   . ASP   A 1 354 ? -31.755 8.288   28.345 1.00 79.45  ? 650 ASP   A N   1 
ATOM   2772 C  CA  . ASP   A 1 354 ? -31.196 8.565   29.661 1.00 75.11  ? 650 ASP   A CA  1 
ATOM   2773 C  C   . ASP   A 1 354 ? -31.341 7.314   30.522 1.00 76.83  ? 650 ASP   A C   1 
ATOM   2774 O  O   . ASP   A 1 354 ? -32.238 6.496   30.300 1.00 81.29  ? 650 ASP   A O   1 
ATOM   2775 C  CB  . ASP   A 1 354 ? -31.900 9.756   30.295 1.00 76.41  ? 650 ASP   A CB  1 
ATOM   2776 C  CG  . ASP   A 1 354 ? -33.362 9.482   30.618 1.00 86.55  ? 650 ASP   A CG  1 
ATOM   2777 O  OD1 . ASP   A 1 354 ? -34.248 10.173  30.075 1.00 88.73  ? 650 ASP   A OD1 1 
ATOM   2778 O  OD2 . ASP   A 1 354 ? -33.633 8.581   31.439 1.00 88.24  ? 650 ASP   A OD2 1 
ATOM   2779 N  N   . HIS   A 1 355 ? -30.433 7.147   31.487 1.00 72.57  ? 651 HIS   A N   1 
ATOM   2780 C  CA  . HIS   A 1 355 ? -30.442 5.922   32.290 1.00 64.39  ? 651 HIS   A CA  1 
ATOM   2781 C  C   . HIS   A 1 355 ? -31.743 5.721   33.075 1.00 64.65  ? 651 HIS   A C   1 
ATOM   2782 O  O   . HIS   A 1 355 ? -32.039 4.585   33.468 1.00 63.03  ? 651 HIS   A O   1 
ATOM   2783 C  CB  . HIS   A 1 355 ? -29.245 5.898   33.236 1.00 66.82  ? 651 HIS   A CB  1 
ATOM   2784 C  CG  . HIS   A 1 355 ? -29.048 7.167   34.005 1.00 70.41  ? 651 HIS   A CG  1 
ATOM   2785 N  ND1 . HIS   A 1 355 ? -28.573 8.320   33.420 1.00 68.08  ? 651 HIS   A ND1 1 
ATOM   2786 C  CD2 . HIS   A 1 355 ? -29.243 7.463   35.313 1.00 72.96  ? 651 HIS   A CD2 1 
ATOM   2787 C  CE1 . HIS   A 1 355 ? -28.485 9.274   34.331 1.00 76.01  ? 651 HIS   A CE1 1 
ATOM   2788 N  NE2 . HIS   A 1 355 ? -28.894 8.784   35.487 1.00 74.26  ? 651 HIS   A NE2 1 
ATOM   2789 N  N   . HIS   A 1 356 ? -32.535 6.780   33.302 1.00 65.45  ? 652 HIS   A N   1 
ATOM   2790 C  CA  . HIS   A 1 356 ? -33.837 6.608   33.948 1.00 69.65  ? 652 HIS   A CA  1 
ATOM   2791 C  C   . HIS   A 1 356 ? -34.869 6.029   32.989 1.00 70.15  ? 652 HIS   A C   1 
ATOM   2792 O  O   . HIS   A 1 356 ? -35.491 4.993   33.270 1.00 59.86  ? 652 HIS   A O   1 
ATOM   2793 C  CB  . HIS   A 1 356 ? -34.317 7.937   34.510 1.00 73.23  ? 652 HIS   A CB  1 
ATOM   2794 C  CG  . HIS   A 1 356 ? -33.340 8.553   35.452 1.00 77.97  ? 652 HIS   A CG  1 
ATOM   2795 N  ND1 . HIS   A 1 356 ? -33.102 8.039   36.706 1.00 80.57  ? 652 HIS   A ND1 1 
ATOM   2796 C  CD2 . HIS   A 1 356 ? -32.497 9.601   35.306 1.00 80.39  ? 652 HIS   A CD2 1 
ATOM   2797 C  CE1 . HIS   A 1 356 ? -32.177 8.765   37.306 1.00 82.09  ? 652 HIS   A CE1 1 
ATOM   2798 N  NE2 . HIS   A 1 356 ? -31.793 9.720   36.477 1.00 83.12  ? 652 HIS   A NE2 1 
ATOM   2799 N  N   . SER   A 1 357 ? -35.067 6.698   31.845 1.00 75.89  ? 653 SER   A N   1 
ATOM   2800 C  CA  . SER   A 1 357 ? -35.986 6.206   30.828 1.00 76.50  ? 653 SER   A CA  1 
ATOM   2801 C  C   . SER   A 1 357 ? -35.674 4.768   30.441 1.00 63.64  ? 653 SER   A C   1 
ATOM   2802 O  O   . SER   A 1 357 ? -36.581 3.943   30.322 1.00 62.36  ? 653 SER   A O   1 
ATOM   2803 C  CB  . SER   A 1 357 ? -35.929 7.105   29.594 1.00 79.55  ? 653 SER   A CB  1 
ATOM   2804 O  OG  . SER   A 1 357 ? -37.093 6.896   28.828 1.00 87.96  ? 653 SER   A OG  1 
ATOM   2805 N  N   . ALA   A 1 358 ? -34.393 4.447   30.259 1.00 64.23  ? 654 ALA   A N   1 
ATOM   2806 C  CA  . ALA   A 1 358 ? -34.026 3.121   29.770 1.00 63.82  ? 654 ALA   A CA  1 
ATOM   2807 C  C   . ALA   A 1 358 ? -34.252 2.050   30.835 1.00 65.46  ? 654 ALA   A C   1 
ATOM   2808 O  O   . ALA   A 1 358 ? -34.631 0.912   30.515 1.00 58.58  ? 654 ALA   A O   1 
ATOM   2809 C  CB  . ALA   A 1 358 ? -32.569 3.127   29.306 1.00 60.03  ? 654 ALA   A CB  1 
ATOM   2810 N  N   . THR   A 1 359 ? -34.017 2.381   32.115 1.00 59.28  ? 655 THR   A N   1 
ATOM   2811 C  CA  . THR   A 1 359 ? -34.212 1.345   33.120 1.00 56.26  ? 655 THR   A CA  1 
ATOM   2812 C  C   . THR   A 1 359 ? -35.697 1.148   33.405 1.00 55.55  ? 655 THR   A C   1 
ATOM   2813 O  O   . THR   A 1 359 ? -36.131 0.022   33.665 1.00 59.81  ? 655 THR   A O   1 
ATOM   2814 C  CB  . THR   A 1 359 ? -33.422 1.663   34.400 1.00 55.91  ? 655 THR   A CB  1 
ATOM   2815 O  OG1 . THR   A 1 359 ? -33.758 2.969   34.878 1.00 59.62  ? 655 THR   A OG1 1 
ATOM   2816 C  CG2 . THR   A 1 359 ? -31.934 1.627   34.113 1.00 55.51  ? 655 THR   A CG2 1 
ATOM   2817 N  N   . GLU   A 1 360 ? -36.505 2.202   33.300 1.00 61.83  ? 656 GLU   A N   1 
ATOM   2818 C  CA  . GLU   A 1 360 ? -37.946 2.004   33.424 1.00 77.29  ? 656 GLU   A CA  1 
ATOM   2819 C  C   . GLU   A 1 360 ? -38.461 1.117   32.298 1.00 78.34  ? 656 GLU   A C   1 
ATOM   2820 O  O   . GLU   A 1 360 ? -39.259 0.202   32.528 1.00 85.05  ? 656 GLU   A O   1 
ATOM   2821 C  CB  . GLU   A 1 360 ? -38.685 3.340   33.430 1.00 86.04  ? 656 GLU   A CB  1 
ATOM   2822 C  CG  . GLU   A 1 360 ? -40.101 3.222   33.977 1.00 97.91  ? 656 GLU   A CG  1 
ATOM   2823 C  CD  . GLU   A 1 360 ? -41.105 4.059   33.215 1.00 109.68 ? 656 GLU   A CD  1 
ATOM   2824 O  OE1 . GLU   A 1 360 ? -42.131 3.495   32.774 1.00 115.90 ? 656 GLU   A OE1 1 
ATOM   2825 O  OE2 . GLU   A 1 360 ? -40.867 5.276   33.051 1.00 117.03 ? 656 GLU   A OE2 1 
ATOM   2826 N  N   . SER   A 1 361 ? -38.003 1.372   31.068 1.00 75.85  ? 657 SER   A N   1 
ATOM   2827 C  CA  A SER   A 1 361 ? -38.434 0.553   29.939 0.49 69.54  ? 657 SER   A CA  1 
ATOM   2828 C  CA  B SER   A 1 361 ? -38.426 0.551   29.935 0.51 69.60  ? 657 SER   A CA  1 
ATOM   2829 C  C   . SER   A 1 361 ? -38.051 -0.907  30.151 1.00 67.45  ? 657 SER   A C   1 
ATOM   2830 O  O   . SER   A 1 361 ? -38.811 -1.817  29.799 1.00 65.69  ? 657 SER   A O   1 
ATOM   2831 C  CB  A SER   A 1 361 ? -37.828 1.086   28.639 0.49 62.16  ? 657 SER   A CB  1 
ATOM   2832 C  CB  B SER   A 1 361 ? -37.801 1.071   28.640 0.51 62.04  ? 657 SER   A CB  1 
ATOM   2833 O  OG  A SER   A 1 361 ? -38.023 2.486   28.513 0.49 59.48  ? 657 SER   A OG  1 
ATOM   2834 O  OG  B SER   A 1 361 ? -36.588 0.391   28.347 0.51 58.07  ? 657 SER   A OG  1 
ATOM   2835 N  N   . PHE   A 1 362 ? -36.886 -1.148  30.749 1.00 62.32  ? 658 PHE   A N   1 
ATOM   2836 C  CA  . PHE   A 1 362 ? -36.470 -2.515  31.001 1.00 64.77  ? 658 PHE   A CA  1 
ATOM   2837 C  C   . PHE   A 1 362 ? -37.388 -3.209  32.005 1.00 67.07  ? 658 PHE   A C   1 
ATOM   2838 O  O   . PHE   A 1 362 ? -37.672 -4.402  31.861 1.00 72.00  ? 658 PHE   A O   1 
ATOM   2839 C  CB  . PHE   A 1 362 ? -35.025 -2.549  31.475 1.00 65.29  ? 658 PHE   A CB  1 
ATOM   2840 C  CG  . PHE   A 1 362 ? -34.502 -3.929  31.590 1.00 66.73  ? 658 PHE   A CG  1 
ATOM   2841 C  CD1 . PHE   A 1 362 ? -34.331 -4.707  30.457 1.00 55.76  ? 658 PHE   A CD1 1 
ATOM   2842 C  CD2 . PHE   A 1 362 ? -34.233 -4.479  32.833 1.00 70.81  ? 658 PHE   A CD2 1 
ATOM   2843 C  CE1 . PHE   A 1 362 ? -33.859 -5.988  30.560 1.00 62.57  ? 658 PHE   A CE1 1 
ATOM   2844 C  CE2 . PHE   A 1 362 ? -33.766 -5.763  32.941 1.00 72.71  ? 658 PHE   A CE2 1 
ATOM   2845 C  CZ  . PHE   A 1 362 ? -33.576 -6.523  31.801 1.00 64.75  ? 658 PHE   A CZ  1 
ATOM   2846 N  N   . ILE   A 1 363 ? -37.865 -2.487  33.029 1.00 65.65  ? 659 ILE   A N   1 
ATOM   2847 C  CA  . ILE   A 1 363 ? -38.831 -3.088  33.946 1.00 73.01  ? 659 ILE   A CA  1 
ATOM   2848 C  C   . ILE   A 1 363 ? -40.137 -3.362  33.215 1.00 76.40  ? 659 ILE   A C   1 
ATOM   2849 O  O   . ILE   A 1 363 ? -40.722 -4.444  33.341 1.00 80.55  ? 659 ILE   A O   1 
ATOM   2850 C  CB  . ILE   A 1 363 ? -39.040 -2.198  35.193 1.00 76.47  ? 659 ILE   A CB  1 
ATOM   2851 C  CG1 . ILE   A 1 363 ? -37.734 -2.052  35.971 1.00 72.36  ? 659 ILE   A CG1 1 
ATOM   2852 C  CG2 . ILE   A 1 363 ? -40.078 -2.809  36.147 1.00 74.41  ? 659 ILE   A CG2 1 
ATOM   2853 C  CD1 . ILE   A 1 363 ? -37.293 -3.339  36.627 1.00 72.51  ? 659 ILE   A CD1 1 
ATOM   2854 N  N   . LYS   A 1 364 ? -40.593 -2.404  32.407 1.00 83.32  ? 660 LYS   A N   1 
ATOM   2855 C  CA  . LYS   A 1 364 ? -41.769 -2.634  31.573 1.00 80.12  ? 660 LYS   A CA  1 
ATOM   2856 C  C   . LYS   A 1 364 ? -41.546 -3.826  30.655 1.00 73.33  ? 660 LYS   A C   1 
ATOM   2857 O  O   . LYS   A 1 364 ? -42.426 -4.683  30.520 1.00 73.82  ? 660 LYS   A O   1 
ATOM   2858 C  CB  . LYS   A 1 364 ? -42.101 -1.370  30.776 1.00 79.45  ? 660 LYS   A CB  1 
ATOM   2859 C  CG  . LYS   A 1 364 ? -43.577 -1.204  30.408 1.00 89.78  ? 660 LYS   A CG  1 
ATOM   2860 C  CD  . LYS   A 1 364 ? -43.950 0.275   30.385 1.00 99.80  ? 660 LYS   A CD  1 
ATOM   2861 C  CE  . LYS   A 1 364 ? -45.042 0.589   29.369 1.00 108.44 ? 660 LYS   A CE  1 
ATOM   2862 N  NZ  . LYS   A 1 364 ? -44.582 0.523   27.936 1.00 112.49 ? 660 LYS   A NZ  1 
ATOM   2863 N  N   . HIS   A 1 365 ? -40.344 -3.923  30.061 1.00 70.95  ? 661 HIS   A N   1 
ATOM   2864 C  CA  . HIS   A 1 365 ? -39.985 -5.048  29.194 1.00 69.20  ? 661 HIS   A CA  1 
ATOM   2865 C  C   . HIS   A 1 365 ? -39.918 -6.351  29.971 1.00 68.17  ? 661 HIS   A C   1 
ATOM   2866 O  O   . HIS   A 1 365 ? -40.328 -7.401  29.465 1.00 67.01  ? 661 HIS   A O   1 
ATOM   2867 C  CB  . HIS   A 1 365 ? -38.642 -4.784  28.507 1.00 68.56  ? 661 HIS   A CB  1 
ATOM   2868 C  CG  . HIS   A 1 365 ? -38.067 -5.981  27.801 1.00 73.51  ? 661 HIS   A CG  1 
ATOM   2869 N  ND1 . HIS   A 1 365 ? -38.702 -6.607  26.748 1.00 78.19  ? 661 HIS   A ND1 1 
ATOM   2870 C  CD2 . HIS   A 1 365 ? -36.899 -6.647  27.981 1.00 72.98  ? 661 HIS   A CD2 1 
ATOM   2871 C  CE1 . HIS   A 1 365 ? -37.957 -7.613  26.319 1.00 75.00  ? 661 HIS   A CE1 1 
ATOM   2872 N  NE2 . HIS   A 1 365 ? -36.859 -7.662  27.053 1.00 72.65  ? 661 HIS   A NE2 1 
ATOM   2873 N  N   . MET   A 1 366 ? -39.376 -6.308  31.190 1.00 65.06  ? 662 MET   A N   1 
ATOM   2874 C  CA  . MET   A 1 366 ? -39.351 -7.502  32.023 1.00 63.23  ? 662 MET   A CA  1 
ATOM   2875 C  C   . MET   A 1 366 ? -40.755 -8.045  32.248 1.00 65.48  ? 662 MET   A C   1 
ATOM   2876 O  O   . MET   A 1 366 ? -40.973 -9.260  32.165 1.00 64.27  ? 662 MET   A O   1 
ATOM   2877 C  CB  . MET   A 1 366 ? -38.674 -7.198  33.364 1.00 61.66  ? 662 MET   A CB  1 
ATOM   2878 C  CG  . MET   A 1 366 ? -37.444 -8.036  33.613 1.00 52.65  ? 662 MET   A CG  1 
ATOM   2879 S  SD  . MET   A 1 366 ? -36.540 -7.457  35.057 1.00 58.85  ? 662 MET   A SD  1 
ATOM   2880 C  CE  . MET   A 1 366 ? -36.179 -9.054  35.808 1.00 59.09  ? 662 MET   A CE  1 
ATOM   2881 N  N   . GLU   A 1 367 ? -41.719 -7.158  32.532 1.00 69.65  ? 663 GLU   A N   1 
ATOM   2882 C  CA  . GLU   A 1 367 ? -43.101 -7.588  32.742 1.00 83.40  ? 663 GLU   A CA  1 
ATOM   2883 C  C   . GLU   A 1 367 ? -43.634 -8.319  31.519 1.00 84.97  ? 663 GLU   A C   1 
ATOM   2884 O  O   . GLU   A 1 367 ? -44.189 -9.419  31.621 1.00 85.49  ? 663 GLU   A O   1 
ATOM   2885 C  CB  . GLU   A 1 367 ? -43.993 -6.385  33.051 1.00 96.22  ? 663 GLU   A CB  1 
ATOM   2886 C  CG  . GLU   A 1 367 ? -43.671 -5.623  34.329 1.00 101.37 ? 663 GLU   A CG  1 
ATOM   2887 C  CD  . GLU   A 1 367 ? -44.419 -4.298  34.403 1.00 108.43 ? 663 GLU   A CD  1 
ATOM   2888 O  OE1 . GLU   A 1 367 ? -45.487 -4.159  33.753 1.00 112.03 ? 663 GLU   A OE1 1 
ATOM   2889 O  OE2 . GLU   A 1 367 ? -43.931 -3.390  35.103 1.00 108.19 ? 663 GLU   A OE2 1 
ATOM   2890 N  N   . ASN   A 1 368 ? -43.494 -7.698  30.352 1.00 85.81  ? 664 ASN   A N   1 
ATOM   2891 C  CA  . ASN   A 1 368 ? -43.880 -8.338  29.100 1.00 83.75  ? 664 ASN   A CA  1 
ATOM   2892 C  C   . ASN   A 1 368 ? -43.264 -9.731  28.975 1.00 77.89  ? 664 ASN   A C   1 
ATOM   2893 O  O   . ASN   A 1 368 ? -43.962 -10.709 28.679 1.00 76.51  ? 664 ASN   A O   1 
ATOM   2894 C  CB  . ASN   A 1 368 ? -43.465 -7.435  27.940 1.00 78.83  ? 664 ASN   A CB  1 
ATOM   2895 C  CG  . ASN   A 1 368 ? -44.064 -6.039  28.049 1.00 80.79  ? 664 ASN   A CG  1 
ATOM   2896 O  OD1 . ASN   A 1 368 ? -45.201 -5.875  28.500 1.00 86.36  ? 664 ASN   A OD1 1 
ATOM   2897 N  ND2 . ASN   A 1 368 ? -43.301 -5.025  27.636 1.00 75.44  ? 664 ASN   A ND2 1 
ATOM   2898 N  N   . GLU   A 1 369 ? -41.960 -9.845  29.255 1.00 71.42  ? 665 GLU   A N   1 
ATOM   2899 C  CA  . GLU   A 1 369 ? -41.276 -11.128 29.127 1.00 71.92  ? 665 GLU   A CA  1 
ATOM   2900 C  C   . GLU   A 1 369 ? -41.853 -12.176 30.075 1.00 82.48  ? 665 GLU   A C   1 
ATOM   2901 O  O   . GLU   A 1 369 ? -42.136 -13.303 29.662 1.00 87.22  ? 665 GLU   A O   1 
ATOM   2902 C  CB  . GLU   A 1 369 ? -39.780 -10.947 29.370 1.00 72.57  ? 665 GLU   A CB  1 
ATOM   2903 C  CG  . GLU   A 1 369 ? -39.036 -10.275 28.243 1.00 78.76  ? 665 GLU   A CG  1 
ATOM   2904 C  CD  . GLU   A 1 369 ? -38.810 -11.207 27.071 1.00 82.12  ? 665 GLU   A CD  1 
ATOM   2905 O  OE1 . GLU   A 1 369 ? -37.882 -12.047 27.148 1.00 94.95  ? 665 GLU   A OE1 1 
ATOM   2906 O  OE2 . GLU   A 1 369 ? -39.581 -11.117 26.099 1.00 64.49  ? 665 GLU   A OE2 1 
ATOM   2907 N  N   . TYR   A 1 370 ? -42.025 -11.835 31.360 1.00 86.04  ? 666 TYR   A N   1 
ATOM   2908 C  CA  . TYR   A 1 370 ? -42.549 -12.826 32.302 1.00 86.42  ? 666 TYR   A CA  1 
ATOM   2909 C  C   . TYR   A 1 370 ? -43.975 -13.245 31.953 1.00 92.99  ? 666 TYR   A C   1 
ATOM   2910 O  O   . TYR   A 1 370 ? -44.345 -14.410 32.150 1.00 93.31  ? 666 TYR   A O   1 
ATOM   2911 C  CB  . TYR   A 1 370 ? -42.470 -12.298 33.739 1.00 80.48  ? 666 TYR   A CB  1 
ATOM   2912 C  CG  . TYR   A 1 370 ? -41.087 -12.453 34.327 1.00 70.41  ? 666 TYR   A CG  1 
ATOM   2913 C  CD1 . TYR   A 1 370 ? -40.090 -11.524 34.057 1.00 65.20  ? 666 TYR   A CD1 1 
ATOM   2914 C  CD2 . TYR   A 1 370 ? -40.765 -13.545 35.110 1.00 74.20  ? 666 TYR   A CD2 1 
ATOM   2915 C  CE1 . TYR   A 1 370 ? -38.821 -11.667 34.559 1.00 67.96  ? 666 TYR   A CE1 1 
ATOM   2916 C  CE2 . TYR   A 1 370 ? -39.491 -13.693 35.631 1.00 76.89  ? 666 TYR   A CE2 1 
ATOM   2917 C  CZ  . TYR   A 1 370 ? -38.523 -12.749 35.354 1.00 74.25  ? 666 TYR   A CZ  1 
ATOM   2918 O  OH  . TYR   A 1 370 ? -37.249 -12.885 35.865 1.00 72.27  ? 666 TYR   A OH  1 
ATOM   2919 N  N   . ARG   A 1 371 ? -44.774 -12.328 31.411 1.00 96.34  ? 667 ARG   A N   1 
ATOM   2920 C  CA  . ARG   A 1 371 ? -46.140 -12.635 31.003 1.00 105.94 ? 667 ARG   A CA  1 
ATOM   2921 C  C   . ARG   A 1 371 ? -46.167 -13.522 29.758 1.00 107.02 ? 667 ARG   A C   1 
ATOM   2922 O  O   . ARG   A 1 371 ? -46.555 -14.694 29.832 1.00 108.44 ? 667 ARG   A O   1 
ATOM   2923 C  CB  . ARG   A 1 371 ? -46.909 -11.329 30.776 1.00 113.83 ? 667 ARG   A CB  1 
ATOM   2924 C  CG  . ARG   A 1 371 ? -48.281 -11.468 30.129 1.00 125.94 ? 667 ARG   A CG  1 
ATOM   2925 C  CD  . ARG   A 1 371 ? -49.123 -10.204 30.335 1.00 133.62 ? 667 ARG   A CD  1 
ATOM   2926 N  NE  . ARG   A 1 371 ? -48.310 -8.992  30.453 1.00 135.11 ? 667 ARG   A NE  1 
ATOM   2927 C  CZ  . ARG   A 1 371 ? -47.793 -8.328  29.422 1.00 136.37 ? 667 ARG   A CZ  1 
ATOM   2928 N  NH1 . ARG   A 1 371 ? -47.991 -8.763  28.184 1.00 137.82 ? 667 ARG   A NH1 1 
ATOM   2929 N  NH2 . ARG   A 1 371 ? -47.071 -7.234  29.629 1.00 135.22 ? 667 ARG   A NH2 1 
ATOM   2930 N  N   . CYS   A 1 372 ? -45.737 -12.990 28.616 1.00 103.79 ? 668 CYS   A N   1 
ATOM   2931 C  CA  . CYS   A 1 372 ? -45.894 -13.709 27.359 1.00 105.93 ? 668 CYS   A CA  1 
ATOM   2932 C  C   . CYS   A 1 372 ? -44.779 -14.717 27.089 1.00 99.77  ? 668 CYS   A C   1 
ATOM   2933 O  O   . CYS   A 1 372 ? -44.820 -15.388 26.052 1.00 107.72 ? 668 CYS   A O   1 
ATOM   2934 C  CB  . CYS   A 1 372 ? -45.997 -12.706 26.198 1.00 110.67 ? 668 CYS   A CB  1 
ATOM   2935 S  SG  . CYS   A 1 372 ? -44.486 -11.757 25.795 1.00 109.11 ? 668 CYS   A SG  1 
ATOM   2936 N  N   . ARG   A 1 373 ? -43.798 -14.852 27.985 1.00 85.56  ? 669 ARG   A N   1 
ATOM   2937 C  CA  . ARG   A 1 373 ? -42.657 -15.738 27.746 1.00 80.45  ? 669 ARG   A CA  1 
ATOM   2938 C  C   . ARG   A 1 373 ? -42.220 -16.540 28.962 1.00 88.84  ? 669 ARG   A C   1 
ATOM   2939 O  O   . ARG   A 1 373 ? -41.434 -17.482 28.802 1.00 85.09  ? 669 ARG   A O   1 
ATOM   2940 C  CB  . ARG   A 1 373 ? -41.453 -14.933 27.237 1.00 76.74  ? 669 ARG   A CB  1 
ATOM   2941 C  CG  . ARG   A 1 373 ? -40.368 -15.755 26.560 1.00 81.84  ? 669 ARG   A CG  1 
ATOM   2942 C  CD  . ARG   A 1 373 ? -39.155 -14.908 26.211 1.00 80.79  ? 669 ARG   A CD  1 
ATOM   2943 N  NE  . ARG   A 1 373 ? -38.192 -15.673 25.425 1.00 81.91  ? 669 ARG   A NE  1 
ATOM   2944 C  CZ  . ARG   A 1 373 ? -36.904 -15.369 25.307 1.00 77.75  ? 669 ARG   A CZ  1 
ATOM   2945 N  NH1 . ARG   A 1 373 ? -36.404 -14.309 25.928 1.00 72.56  ? 669 ARG   A NH1 1 
ATOM   2946 N  NH2 . ARG   A 1 373 ? -36.114 -16.136 24.569 1.00 78.42  ? 669 ARG   A NH2 1 
ATOM   2947 N  N   . GLY   A 1 374 ? -42.675 -16.208 30.169 1.00 95.11  ? 670 GLY   A N   1 
ATOM   2948 C  CA  . GLY   A 1 374 ? -42.301 -16.935 31.361 1.00 100.21 ? 670 GLY   A CA  1 
ATOM   2949 C  C   . GLY   A 1 374 ? -41.016 -16.497 32.028 1.00 100.49 ? 670 GLY   A C   1 
ATOM   2950 O  O   . GLY   A 1 374 ? -40.516 -17.221 32.897 1.00 107.90 ? 670 GLY   A O   1 
ATOM   2951 N  N   . GLY   A 1 375 ? -40.464 -15.355 31.662 1.00 93.39  ? 671 GLY   A N   1 
ATOM   2952 C  CA  . GLY   A 1 375 ? -39.240 -14.886 32.281 1.00 83.70  ? 671 GLY   A CA  1 
ATOM   2953 C  C   . GLY   A 1 375 ? -38.454 -13.998 31.337 1.00 79.45  ? 671 GLY   A C   1 
ATOM   2954 O  O   . GLY   A 1 375 ? -38.826 -13.783 30.186 1.00 83.70  ? 671 GLY   A O   1 
ATOM   2955 N  N   . CYS   A 1 376 ? -37.340 -13.494 31.860 1.00 71.63  ? 672 CYS   A N   1 
ATOM   2956 C  CA  . CYS   A 1 376 ? -36.420 -12.611 31.156 1.00 64.52  ? 672 CYS   A CA  1 
ATOM   2957 C  C   . CYS   A 1 376 ? -35.053 -12.727 31.811 1.00 66.06  ? 672 CYS   A C   1 
ATOM   2958 O  O   . CYS   A 1 376 ? -34.879 -12.256 32.937 1.00 63.79  ? 672 CYS   A O   1 
ATOM   2959 C  CB  . CYS   A 1 376 ? -36.909 -11.157 31.203 1.00 61.29  ? 672 CYS   A CB  1 
ATOM   2960 S  SG  . CYS   A 1 376 ? -35.856 -9.931  30.348 1.00 55.84  ? 672 CYS   A SG  1 
ATOM   2961 N  N   . PRO   A 1 377 ? -34.073 -13.359 31.170 1.00 63.73  ? 673 PRO   A N   1 
ATOM   2962 C  CA  . PRO   A 1 377 ? -32.728 -13.376 31.753 1.00 49.22  ? 673 PRO   A CA  1 
ATOM   2963 C  C   . PRO   A 1 377 ? -32.192 -11.974 31.886 1.00 52.63  ? 673 PRO   A C   1 
ATOM   2964 O  O   . PRO   A 1 377 ? -32.341 -11.139 30.989 1.00 41.75  ? 673 PRO   A O   1 
ATOM   2965 C  CB  . PRO   A 1 377 ? -31.903 -14.189 30.752 1.00 54.71  ? 673 PRO   A CB  1 
ATOM   2966 C  CG  . PRO   A 1 377 ? -32.696 -14.149 29.481 1.00 51.93  ? 673 PRO   A CG  1 
ATOM   2967 C  CD  . PRO   A 1 377 ? -34.133 -14.089 29.891 1.00 49.89  ? 673 PRO   A CD  1 
ATOM   2968 N  N   . ALA   A 1 378 ? -31.550 -11.716 33.013 1.00 50.31  ? 674 ALA   A N   1 
ATOM   2969 C  CA  . ALA   A 1 378 ? -31.062 -10.371 33.254 1.00 47.63  ? 674 ALA   A CA  1 
ATOM   2970 C  C   . ALA   A 1 378 ? -29.862 -10.433 34.188 1.00 43.40  ? 674 ALA   A C   1 
ATOM   2971 O  O   . ALA   A 1 378 ? -29.827 -11.251 35.108 1.00 51.18  ? 674 ALA   A O   1 
ATOM   2972 C  CB  . ALA   A 1 378 ? -32.191 -9.490  33.789 1.00 43.93  ? 674 ALA   A CB  1 
ATOM   2973 N  N   . ASP   A 1 379 ? -28.859 -9.621  33.879 1.00 35.10  ? 675 ASP   A N   1 
ATOM   2974 C  CA  . ASP   A 1 379 ? -27.604 -9.526  34.592 1.00 35.04  ? 675 ASP   A CA  1 
ATOM   2975 C  C   . ASP   A 1 379 ? -27.643 -8.180  35.294 1.00 52.39  ? 675 ASP   A C   1 
ATOM   2976 O  O   . ASP   A 1 379 ? -27.368 -7.137  34.692 1.00 53.97  ? 675 ASP   A O   1 
ATOM   2977 C  CB  . ASP   A 1 379 ? -26.418 -9.659  33.654 1.00 41.63  ? 675 ASP   A CB  1 
ATOM   2978 C  CG  . ASP   A 1 379 ? -25.118 -9.794  34.389 1.00 51.01  ? 675 ASP   A CG  1 
ATOM   2979 O  OD1 . ASP   A 1 379 ? -24.163 -10.362 33.818 1.00 49.42  ? 675 ASP   A OD1 1 
ATOM   2980 O  OD2 . ASP   A 1 379 ? -25.041 -9.326  35.536 1.00 55.54  ? 675 ASP   A OD2 1 
ATOM   2981 N  N   . TRP   A 1 380 ? -28.010 -8.229  36.574 1.00 47.82  ? 676 TRP   A N   1 
ATOM   2982 C  CA  . TRP   A 1 380 ? -28.148 -7.031  37.385 1.00 40.13  ? 676 TRP   A CA  1 
ATOM   2983 C  C   . TRP   A 1 380 ? -26.841 -6.252  37.463 1.00 42.88  ? 676 TRP   A C   1 
ATOM   2984 O  O   . TRP   A 1 380 ? -26.848 -5.010  37.482 1.00 48.45  ? 676 TRP   A O   1 
ATOM   2985 C  CB  . TRP   A 1 380 ? -28.618 -7.458  38.770 1.00 45.58  ? 676 TRP   A CB  1 
ATOM   2986 C  CG  . TRP   A 1 380 ? -28.980 -6.394  39.722 1.00 35.45  ? 676 TRP   A CG  1 
ATOM   2987 C  CD1 . TRP   A 1 380 ? -30.229 -6.124  40.184 1.00 49.37  ? 676 TRP   A CD1 1 
ATOM   2988 C  CD2 . TRP   A 1 380 ? -28.085 -5.500  40.422 1.00 37.56  ? 676 TRP   A CD2 1 
ATOM   2989 N  NE1 . TRP   A 1 380 ? -30.182 -5.111  41.109 1.00 49.24  ? 676 TRP   A NE1 1 
ATOM   2990 C  CE2 . TRP   A 1 380 ? -28.882 -4.714  41.289 1.00 45.62  ? 676 TRP   A CE2 1 
ATOM   2991 C  CE3 . TRP   A 1 380 ? -26.698 -5.292  40.414 1.00 36.64  ? 676 TRP   A CE3 1 
ATOM   2992 C  CZ2 . TRP   A 1 380 ? -28.341 -3.708  42.125 1.00 48.91  ? 676 TRP   A CZ2 1 
ATOM   2993 C  CZ3 . TRP   A 1 380 ? -26.160 -4.291  41.264 1.00 52.07  ? 676 TRP   A CZ3 1 
ATOM   2994 C  CH2 . TRP   A 1 380 ? -26.983 -3.528  42.100 1.00 37.56  ? 676 TRP   A CH2 1 
ATOM   2995 N  N   . VAL   A 1 381 ? -25.705 -6.958  37.510 1.00 42.31  ? 677 VAL   A N   1 
ATOM   2996 C  CA  . VAL   A 1 381 ? -24.408 -6.276  37.488 1.00 44.35  ? 677 VAL   A CA  1 
ATOM   2997 C  C   . VAL   A 1 381 ? -24.312 -5.333  36.301 1.00 52.42  ? 677 VAL   A C   1 
ATOM   2998 O  O   . VAL   A 1 381 ? -23.819 -4.207  36.423 1.00 45.92  ? 677 VAL   A O   1 
ATOM   2999 C  CB  . VAL   A 1 381 ? -23.257 -7.293  37.471 1.00 46.23  ? 677 VAL   A CB  1 
ATOM   3000 C  CG1 . VAL   A 1 381 ? -21.963 -6.559  37.257 1.00 48.48  ? 677 VAL   A CG1 1 
ATOM   3001 C  CG2 . VAL   A 1 381 ? -23.210 -8.063  38.770 1.00 46.41  ? 677 VAL   A CG2 1 
ATOM   3002 N  N   . TRP   A 1 382 ? -24.779 -5.785  35.133 1.00 50.16  ? 678 TRP   A N   1 
ATOM   3003 C  CA  . TRP   A 1 382 ? -24.702 -5.035  33.885 1.00 47.80  ? 678 TRP   A CA  1 
ATOM   3004 C  C   . TRP   A 1 382 ? -25.908 -4.141  33.632 1.00 44.92  ? 678 TRP   A C   1 
ATOM   3005 O  O   . TRP   A 1 382 ? -25.760 -3.089  33.009 1.00 47.59  ? 678 TRP   A O   1 
ATOM   3006 C  CB  . TRP   A 1 382 ? -24.526 -6.006  32.703 1.00 44.00  ? 678 TRP   A CB  1 
ATOM   3007 C  CG  . TRP   A 1 382 ? -23.091 -6.365  32.483 1.00 51.82  ? 678 TRP   A CG  1 
ATOM   3008 C  CD1 . TRP   A 1 382 ? -22.298 -7.113  33.314 1.00 57.07  ? 678 TRP   A CD1 1 
ATOM   3009 C  CD2 . TRP   A 1 382 ? -22.259 -5.968  31.381 1.00 56.21  ? 678 TRP   A CD2 1 
ATOM   3010 N  NE1 . TRP   A 1 382 ? -21.030 -7.217  32.786 1.00 58.92  ? 678 TRP   A NE1 1 
ATOM   3011 C  CE2 . TRP   A 1 382 ? -20.980 -6.521  31.604 1.00 60.58  ? 678 TRP   A CE2 1 
ATOM   3012 C  CE3 . TRP   A 1 382 ? -22.476 -5.217  30.227 1.00 55.13  ? 678 TRP   A CE3 1 
ATOM   3013 C  CZ2 . TRP   A 1 382 ? -19.923 -6.338  30.719 1.00 61.10  ? 678 TRP   A CZ2 1 
ATOM   3014 C  CZ3 . TRP   A 1 382 ? -21.419 -5.034  29.346 1.00 61.22  ? 678 TRP   A CZ3 1 
ATOM   3015 C  CH2 . TRP   A 1 382 ? -20.162 -5.596  29.597 1.00 64.04  ? 678 TRP   A CH2 1 
ATOM   3016 N  N   . ILE   A 1 383 ? -27.084 -4.503  34.150 1.00 50.54  ? 679 ILE   A N   1 
ATOM   3017 C  CA  . ILE   A 1 383 ? -28.295 -3.733  33.870 1.00 42.91  ? 679 ILE   A CA  1 
ATOM   3018 C  C   . ILE   A 1 383 ? -28.342 -2.458  34.708 1.00 54.95  ? 679 ILE   A C   1 
ATOM   3019 O  O   . ILE   A 1 383 ? -28.859 -1.435  34.243 1.00 53.09  ? 679 ILE   A O   1 
ATOM   3020 C  CB  . ILE   A 1 383 ? -29.544 -4.611  34.101 1.00 51.64  ? 679 ILE   A CB  1 
ATOM   3021 C  CG1 . ILE   A 1 383 ? -29.598 -5.778  33.100 1.00 45.08  ? 679 ILE   A CG1 1 
ATOM   3022 C  CG2 . ILE   A 1 383 ? -30.835 -3.789  34.084 1.00 49.96  ? 679 ILE   A CG2 1 
ATOM   3023 C  CD1 . ILE   A 1 383 ? -30.148 -5.420  31.695 1.00 56.80  ? 679 ILE   A CD1 1 
ATOM   3024 N  N   . VAL   A 1 384 ? -27.835 -2.486  35.944 1.00 40.54  ? 680 VAL   A N   1 
ATOM   3025 C  CA  . VAL   A 1 384 ? -27.910 -1.263  36.757 1.00 46.50  ? 680 VAL   A CA  1 
ATOM   3026 C  C   . VAL   A 1 384 ? -26.959 -0.234  36.170 1.00 43.37  ? 680 VAL   A C   1 
ATOM   3027 O  O   . VAL   A 1 384 ? -25.774 -0.538  35.965 1.00 45.89  ? 680 VAL   A O   1 
ATOM   3028 C  CB  . VAL   A 1 384 ? -27.566 -1.555  38.220 1.00 45.28  ? 680 VAL   A CB  1 
ATOM   3029 C  CG1 . VAL   A 1 384 ? -27.470 -0.218  39.057 1.00 40.31  ? 680 VAL   A CG1 1 
ATOM   3030 C  CG2 . VAL   A 1 384 ? -28.595 -2.470  38.787 1.00 56.73  ? 680 VAL   A CG2 1 
ATOM   3031 N  N   . PRO   A 1 385 ? -27.435 0.951   35.804 1.00 56.12  ? 681 PRO   A N   1 
ATOM   3032 C  CA  . PRO   A 1 385 ? -26.542 1.952   35.211 1.00 46.87  ? 681 PRO   A CA  1 
ATOM   3033 C  C   . PRO   A 1 385 ? -25.372 2.247   36.148 1.00 57.80  ? 681 PRO   A C   1 
ATOM   3034 O  O   . PRO   A 1 385 ? -25.506 2.138   37.381 1.00 57.62  ? 681 PRO   A O   1 
ATOM   3035 C  CB  . PRO   A 1 385 ? -27.447 3.179   35.032 1.00 53.09  ? 681 PRO   A CB  1 
ATOM   3036 C  CG  . PRO   A 1 385 ? -28.681 2.886   35.882 1.00 65.21  ? 681 PRO   A CG  1 
ATOM   3037 C  CD  . PRO   A 1 385 ? -28.832 1.401   35.849 1.00 60.40  ? 681 PRO   A CD  1 
ATOM   3038 N  N   . PRO   A 1 386 ? -24.222 2.618   35.589 1.00 57.75  ? 682 PRO   A N   1 
ATOM   3039 C  CA  . PRO   A 1 386 ? -23.019 2.812   36.409 1.00 46.19  ? 682 PRO   A CA  1 
ATOM   3040 C  C   . PRO   A 1 386 ? -22.986 4.124   37.178 1.00 61.59  ? 682 PRO   A C   1 
ATOM   3041 O  O   . PRO   A 1 386 ? -21.951 4.484   37.750 1.00 66.85  ? 682 PRO   A O   1 
ATOM   3042 C  CB  . PRO   A 1 386 ? -21.920 2.748   35.350 1.00 47.24  ? 682 PRO   A CB  1 
ATOM   3043 C  CG  . PRO   A 1 386 ? -22.584 3.510   34.133 1.00 44.73  ? 682 PRO   A CG  1 
ATOM   3044 C  CD  . PRO   A 1 386 ? -24.051 3.174   34.221 1.00 55.81  ? 682 PRO   A CD  1 
ATOM   3045 N  N   . MET   A 1 387 ? -24.102 4.816   37.265 1.00 59.48  ? 683 MET   A N   1 
ATOM   3046 C  CA  . MET   A 1 387 ? -24.213 5.969   38.137 1.00 52.66  ? 683 MET   A CA  1 
ATOM   3047 C  C   . MET   A 1 387 ? -25.628 5.980   38.674 1.00 65.52  ? 683 MET   A C   1 
ATOM   3048 O  O   . MET   A 1 387 ? -26.539 5.455   38.030 1.00 66.03  ? 683 MET   A O   1 
ATOM   3049 C  CB  . MET   A 1 387 ? -23.910 7.274   37.386 1.00 60.94  ? 683 MET   A CB  1 
ATOM   3050 C  CG  . MET   A 1 387 ? -24.988 7.704   36.399 1.00 70.72  ? 683 MET   A CG  1 
ATOM   3051 S  SD  . MET   A 1 387 ? -24.709 9.352   35.671 1.00 81.59  ? 683 MET   A SD  1 
ATOM   3052 C  CE  . MET   A 1 387 ? -24.882 10.375  37.127 1.00 77.91  ? 683 MET   A CE  1 
ATOM   3053 N  N   . SER   A 1 388 ? -25.812 6.577   39.854 1.00 70.95  ? 684 SER   A N   1 
ATOM   3054 C  CA  . SER   A 1 388 ? -27.142 6.718   40.451 1.00 66.36  ? 684 SER   A CA  1 
ATOM   3055 C  C   . SER   A 1 388 ? -27.892 5.387   40.472 1.00 59.60  ? 684 SER   A C   1 
ATOM   3056 O  O   . SER   A 1 388 ? -29.102 5.324   40.239 1.00 63.77  ? 684 SER   A O   1 
ATOM   3057 C  CB  . SER   A 1 388 ? -27.953 7.765   39.699 1.00 67.92  ? 684 SER   A CB  1 
ATOM   3058 O  OG  . SER   A 1 388 ? -27.138 8.863   39.361 1.00 78.55  ? 684 SER   A OG  1 
ATOM   3059 N  N   . GLY   A 1 389 ? -27.163 4.313   40.740 1.00 54.89  ? 685 GLY   A N   1 
ATOM   3060 C  CA  . GLY   A 1 389 ? -27.769 3.002   40.869 1.00 55.36  ? 685 GLY   A CA  1 
ATOM   3061 C  C   . GLY   A 1 389 ? -29.186 2.975   41.410 1.00 59.10  ? 685 GLY   A C   1 
ATOM   3062 O  O   . GLY   A 1 389 ? -30.136 2.697   40.676 1.00 65.54  ? 685 GLY   A O   1 
ATOM   3063 N  N   . SER   A 1 390 ? -29.345 3.307   42.688 1.00 60.97  ? 686 SER   A N   1 
ATOM   3064 C  CA  . SER   A 1 390 ? -30.579 2.993   43.397 1.00 65.02  ? 686 SER   A CA  1 
ATOM   3065 C  C   . SER   A 1 390 ? -31.691 3.986   43.141 1.00 66.28  ? 686 SER   A C   1 
ATOM   3066 O  O   . SER   A 1 390 ? -32.801 3.789   43.653 1.00 65.51  ? 686 SER   A O   1 
ATOM   3067 C  CB  . SER   A 1 390 ? -30.322 2.901   44.908 1.00 60.59  ? 686 SER   A CB  1 
ATOM   3068 O  OG  . SER   A 1 390 ? -29.620 4.038   45.327 1.00 66.84  ? 686 SER   A OG  1 
ATOM   3069 N  N   . ILE   A 1 391 ? -31.436 5.057   42.384 1.00 64.52  ? 687 ILE   A N   1 
ATOM   3070 C  CA  . ILE   A 1 391 ? -32.533 5.932   42.004 1.00 70.41  ? 687 ILE   A CA  1 
ATOM   3071 C  C   . ILE   A 1 391 ? -33.131 5.532   40.674 1.00 68.96  ? 687 ILE   A C   1 
ATOM   3072 O  O   . ILE   A 1 391 ? -34.035 6.221   40.193 1.00 77.41  ? 687 ILE   A O   1 
ATOM   3073 C  CB  . ILE   A 1 391 ? -32.122 7.422   41.999 1.00 72.62  ? 687 ILE   A CB  1 
ATOM   3074 C  CG1 . ILE   A 1 391 ? -31.296 7.780   40.768 1.00 80.31  ? 687 ILE   A CG1 1 
ATOM   3075 C  CG2 . ILE   A 1 391 ? -31.366 7.796   43.276 1.00 73.74  ? 687 ILE   A CG2 1 
ATOM   3076 C  CD1 . ILE   A 1 391 ? -31.025 9.268   40.679 1.00 78.72  ? 687 ILE   A CD1 1 
ATOM   3077 N  N   . THR   A 1 392 ? -32.657 4.428   40.068 1.00 70.47  ? 688 THR   A N   1 
ATOM   3078 C  CA  . THR   A 1 392 ? -33.213 3.773   38.893 1.00 69.51  ? 688 THR   A CA  1 
ATOM   3079 C  C   . THR   A 1 392 ? -33.916 2.481   39.298 1.00 70.58  ? 688 THR   A C   1 
ATOM   3080 O  O   . THR   A 1 392 ? -33.420 1.744   40.159 1.00 74.22  ? 688 THR   A O   1 
ATOM   3081 C  CB  . THR   A 1 392 ? -32.136 3.458   37.840 1.00 69.64  ? 688 THR   A CB  1 
ATOM   3082 O  OG1 . THR   A 1 392 ? -31.266 2.417   38.312 1.00 60.88  ? 688 THR   A OG1 1 
ATOM   3083 C  CG2 . THR   A 1 392 ? -31.313 4.708   37.489 1.00 64.21  ? 688 THR   A CG2 1 
ATOM   3084 N  N   . PRO   A 1 393 ? -35.075 2.189   38.704 1.00 68.80  ? 689 PRO   A N   1 
ATOM   3085 C  CA  . PRO   A 1 393 ? -35.902 1.079   39.199 1.00 68.18  ? 689 PRO   A CA  1 
ATOM   3086 C  C   . PRO   A 1 393 ? -35.275 -0.300  39.024 1.00 67.27  ? 689 PRO   A C   1 
ATOM   3087 O  O   . PRO   A 1 393 ? -35.751 -1.244  39.668 1.00 74.58  ? 689 PRO   A O   1 
ATOM   3088 C  CB  . PRO   A 1 393 ? -37.186 1.207   38.372 1.00 78.62  ? 689 PRO   A CB  1 
ATOM   3089 C  CG  . PRO   A 1 393 ? -36.720 1.833   37.074 1.00 81.12  ? 689 PRO   A CG  1 
ATOM   3090 C  CD  . PRO   A 1 393 ? -35.641 2.813   37.488 1.00 79.14  ? 689 PRO   A CD  1 
ATOM   3091 N  N   . VAL   A 1 394 ? -34.240 -0.463  38.195 1.00 59.69  ? 690 VAL   A N   1 
ATOM   3092 C  CA  . VAL   A 1 394 ? -33.645 -1.791  38.066 1.00 60.25  ? 690 VAL   A CA  1 
ATOM   3093 C  C   . VAL   A 1 394 ? -32.774 -2.139  39.286 1.00 57.16  ? 690 VAL   A C   1 
ATOM   3094 O  O   . VAL   A 1 394 ? -32.552 -3.326  39.578 1.00 52.53  ? 690 VAL   A O   1 
ATOM   3095 C  CB  . VAL   A 1 394 ? -32.833 -1.911  36.762 1.00 52.40  ? 690 VAL   A CB  1 
ATOM   3096 C  CG1 . VAL   A 1 394 ? -33.758 -1.883  35.522 1.00 55.39  ? 690 VAL   A CG1 1 
ATOM   3097 C  CG2 . VAL   A 1 394 ? -31.777 -0.817  36.697 1.00 53.97  ? 690 VAL   A CG2 1 
ATOM   3098 N  N   . PHE   A 1 395 ? -32.220 -1.134  39.971 1.00 55.60  ? 691 PHE   A N   1 
ATOM   3099 C  CA  . PHE   A 1 395 ? -31.433 -1.418  41.181 1.00 58.47  ? 691 PHE   A CA  1 
ATOM   3100 C  C   . PHE   A 1 395 ? -32.223 -2.261  42.166 1.00 60.68  ? 691 PHE   A C   1 
ATOM   3101 O  O   . PHE   A 1 395 ? -31.663 -3.143  42.829 1.00 55.97  ? 691 PHE   A O   1 
ATOM   3102 C  CB  . PHE   A 1 395 ? -30.974 -0.121  41.862 1.00 48.74  ? 691 PHE   A CB  1 
ATOM   3103 C  CG  . PHE   A 1 395 ? -30.210 -0.338  43.184 1.00 49.87  ? 691 PHE   A CG  1 
ATOM   3104 C  CD1 . PHE   A 1 395 ? -28.826 -0.219  43.239 1.00 51.82  ? 691 PHE   A CD1 1 
ATOM   3105 C  CD2 . PHE   A 1 395 ? -30.880 -0.668  44.343 1.00 49.70  ? 691 PHE   A CD2 1 
ATOM   3106 C  CE1 . PHE   A 1 395 ? -28.130 -0.418  44.440 1.00 58.35  ? 691 PHE   A CE1 1 
ATOM   3107 C  CE2 . PHE   A 1 395 ? -30.192 -0.883  45.548 1.00 59.12  ? 691 PHE   A CE2 1 
ATOM   3108 C  CZ  . PHE   A 1 395 ? -28.816 -0.753  45.588 1.00 53.11  ? 691 PHE   A CZ  1 
ATOM   3109 N  N   . HIS   A 1 396 ? -33.521 -1.986  42.278 1.00 68.08  ? 692 HIS   A N   1 
ATOM   3110 C  CA  . HIS   A 1 396 ? -34.440 -2.586  43.236 1.00 63.46  ? 692 HIS   A CA  1 
ATOM   3111 C  C   . HIS   A 1 396 ? -35.138 -3.825  42.694 1.00 62.58  ? 692 HIS   A C   1 
ATOM   3112 O  O   . HIS   A 1 396 ? -36.063 -4.337  43.329 1.00 63.76  ? 692 HIS   A O   1 
ATOM   3113 C  CB  . HIS   A 1 396 ? -35.464 -1.533  43.634 1.00 65.81  ? 692 HIS   A CB  1 
ATOM   3114 C  CG  . HIS   A 1 396 ? -34.838 -0.248  44.068 1.00 69.82  ? 692 HIS   A CG  1 
ATOM   3115 N  ND1 . HIS   A 1 396 ? -34.235 -0.101  45.296 1.00 70.15  ? 692 HIS   A ND1 1 
ATOM   3116 C  CD2 . HIS   A 1 396 ? -34.676 0.932   43.426 1.00 69.32  ? 692 HIS   A CD2 1 
ATOM   3117 C  CE1 . HIS   A 1 396 ? -33.755 1.125   45.408 1.00 72.87  ? 692 HIS   A CE1 1 
ATOM   3118 N  NE2 . HIS   A 1 396 ? -34.001 1.770   44.281 1.00 73.55  ? 692 HIS   A NE2 1 
ATOM   3119 N  N   . GLN   A 1 397 ? -34.721 -4.306  41.531 1.00 65.99  ? 693 GLN   A N   1 
ATOM   3120 C  CA  . GLN   A 1 397 ? -35.388 -5.398  40.835 1.00 62.56  ? 693 GLN   A CA  1 
ATOM   3121 C  C   . GLN   A 1 397 ? -34.503 -6.630  40.855 1.00 54.70  ? 693 GLN   A C   1 
ATOM   3122 O  O   . GLN   A 1 397 ? -33.440 -6.640  40.228 1.00 56.16  ? 693 GLN   A O   1 
ATOM   3123 C  CB  . GLN   A 1 397 ? -35.715 -4.998  39.397 1.00 67.71  ? 693 GLN   A CB  1 
ATOM   3124 C  CG  . GLN   A 1 397 ? -36.222 -6.142  38.546 1.00 67.00  ? 693 GLN   A CG  1 
ATOM   3125 C  CD  . GLN   A 1 397 ? -37.584 -6.629  38.990 1.00 62.42  ? 693 GLN   A CD  1 
ATOM   3126 O  OE1 . GLN   A 1 397 ? -38.502 -5.834  39.185 1.00 58.93  ? 693 GLN   A OE1 1 
ATOM   3127 N  NE2 . GLN   A 1 397 ? -37.724 -7.941  39.154 1.00 61.54  ? 693 GLN   A NE2 1 
ATOM   3128 N  N   . GLU   A 1 398 ? -34.929 -7.658  41.587 1.00 54.26  ? 694 GLU   A N   1 
ATOM   3129 C  CA  . GLU   A 1 398 ? -34.269 -8.951  41.490 1.00 58.64  ? 694 GLU   A CA  1 
ATOM   3130 C  C   . GLU   A 1 398 ? -34.360 -9.506  40.071 1.00 62.49  ? 694 GLU   A C   1 
ATOM   3131 O  O   . GLU   A 1 398 ? -35.413 -9.463  39.430 1.00 58.42  ? 694 GLU   A O   1 
ATOM   3132 C  CB  . GLU   A 1 398 ? -34.884 -9.940  42.474 1.00 59.53  ? 694 GLU   A CB  1 
ATOM   3133 C  CG  . GLU   A 1 398 ? -34.654 -9.571  43.950 1.00 59.92  ? 694 GLU   A CG  1 
ATOM   3134 C  CD  . GLU   A 1 398 ? -35.440 -10.445 44.899 1.00 67.24  ? 694 GLU   A CD  1 
ATOM   3135 O  OE1 . GLU   A 1 398 ? -35.490 -10.112 46.108 1.00 67.91  ? 694 GLU   A OE1 1 
ATOM   3136 O  OE2 . GLU   A 1 398 ? -36.006 -11.471 44.436 1.00 66.06  ? 694 GLU   A OE2 1 
ATOM   3137 N  N   . MET   A 1 399 ? -33.254 -10.067 39.600 1.00 62.41  ? 695 MET   A N   1 
ATOM   3138 C  CA  . MET   A 1 399 ? -33.172 -10.619 38.256 1.00 61.94  ? 695 MET   A CA  1 
ATOM   3139 C  C   . MET   A 1 399 ? -32.523 -11.990 38.304 1.00 61.49  ? 695 MET   A C   1 
ATOM   3140 O  O   . MET   A 1 399 ? -31.406 -12.125 38.807 1.00 63.81  ? 695 MET   A O   1 
ATOM   3141 C  CB  . MET   A 1 399 ? -32.368 -9.697  37.328 1.00 47.78  ? 695 MET   A CB  1 
ATOM   3142 C  CG  . MET   A 1 399 ? -33.005 -8.342  37.027 1.00 42.08  ? 695 MET   A CG  1 
ATOM   3143 S  SD  . MET   A 1 399 ? -31.743 -7.199  36.493 1.00 51.96  ? 695 MET   A SD  1 
ATOM   3144 C  CE  . MET   A 1 399 ? -32.604 -5.636  36.670 1.00 48.82  ? 695 MET   A CE  1 
ATOM   3145 N  N   . LEU   A 1 400 ? -33.201 -12.986 37.740 1.00 60.16  ? 696 LEU   A N   1 
ATOM   3146 C  CA  . LEU   A 1 400 ? -32.588 -14.280 37.446 1.00 61.49  ? 696 LEU   A CA  1 
ATOM   3147 C  C   . LEU   A 1 400 ? -31.769 -14.194 36.157 1.00 62.59  ? 696 LEU   A C   1 
ATOM   3148 O  O   . LEU   A 1 400 ? -32.301 -13.817 35.103 1.00 56.93  ? 696 LEU   A O   1 
ATOM   3149 C  CB  . LEU   A 1 400 ? -33.663 -15.352 37.308 1.00 62.22  ? 696 LEU   A CB  1 
ATOM   3150 C  CG  . LEU   A 1 400 ? -34.458 -15.660 38.571 1.00 65.05  ? 696 LEU   A CG  1 
ATOM   3151 C  CD1 . LEU   A 1 400 ? -35.479 -16.745 38.289 1.00 69.10  ? 696 LEU   A CD1 1 
ATOM   3152 C  CD2 . LEU   A 1 400 ? -33.508 -16.070 39.665 1.00 64.96  ? 696 LEU   A CD2 1 
ATOM   3153 N  N   . ASN   A 1 401 ? -30.484 -14.541 36.235 1.00 60.05  ? 697 ASN   A N   1 
ATOM   3154 C  CA  . ASN   A 1 401 ? -29.618 -14.623 35.068 1.00 53.41  ? 697 ASN   A CA  1 
ATOM   3155 C  C   . ASN   A 1 401 ? -29.466 -16.076 34.646 1.00 59.49  ? 697 ASN   A C   1 
ATOM   3156 O  O   . ASN   A 1 401 ? -29.157 -16.943 35.469 1.00 53.14  ? 697 ASN   A O   1 
ATOM   3157 C  CB  . ASN   A 1 401 ? -28.241 -14.023 35.332 1.00 54.21  ? 697 ASN   A CB  1 
ATOM   3158 C  CG  . ASN   A 1 401 ? -27.436 -13.816 34.046 1.00 50.84  ? 697 ASN   A CG  1 
ATOM   3159 O  OD1 . ASN   A 1 401 ? -28.006 -13.699 32.950 1.00 55.70  ? 697 ASN   A OD1 1 
ATOM   3160 N  ND2 . ASN   A 1 401 ? -26.107 -13.782 34.173 1.00 40.35  ? 697 ASN   A ND2 1 
ATOM   3161 N  N   . TYR   A 1 402 ? -29.683 -16.330 33.357 1.00 53.99  ? 698 TYR   A N   1 
ATOM   3162 C  CA  . TYR   A 1 402 ? -29.499 -17.651 32.788 1.00 50.22  ? 698 TYR   A CA  1 
ATOM   3163 C  C   . TYR   A 1 402 ? -29.304 -17.494 31.280 1.00 61.80  ? 698 TYR   A C   1 
ATOM   3164 O  O   . TYR   A 1 402 ? -29.637 -16.462 30.694 1.00 49.66  ? 698 TYR   A O   1 
ATOM   3165 C  CB  . TYR   A 1 402 ? -30.672 -18.573 33.137 1.00 54.47  ? 698 TYR   A CB  1 
ATOM   3166 C  CG  . TYR   A 1 402 ? -32.050 -17.971 32.932 1.00 61.08  ? 698 TYR   A CG  1 
ATOM   3167 C  CD1 . TYR   A 1 402 ? -32.699 -18.105 31.711 1.00 62.54  ? 698 TYR   A CD1 1 
ATOM   3168 C  CD2 . TYR   A 1 402 ? -32.703 -17.267 33.952 1.00 61.11  ? 698 TYR   A CD2 1 
ATOM   3169 C  CE1 . TYR   A 1 402 ? -33.951 -17.566 31.501 1.00 62.43  ? 698 TYR   A CE1 1 
ATOM   3170 C  CE2 . TYR   A 1 402 ? -33.973 -16.722 33.753 1.00 62.64  ? 698 TYR   A CE2 1 
ATOM   3171 C  CZ  . TYR   A 1 402 ? -34.593 -16.884 32.515 1.00 65.34  ? 698 TYR   A CZ  1 
ATOM   3172 O  OH  . TYR   A 1 402 ? -35.848 -16.356 32.271 1.00 63.75  ? 698 TYR   A OH  1 
ATOM   3173 N  N   . ARG   A 1 403 ? -28.748 -18.529 30.672 1.00 60.90  ? 699 ARG   A N   1 
ATOM   3174 C  CA  . ARG   A 1 403 ? -28.174 -18.451 29.338 1.00 69.79  ? 699 ARG   A CA  1 
ATOM   3175 C  C   . ARG   A 1 403 ? -29.080 -19.183 28.353 1.00 71.84  ? 699 ARG   A C   1 
ATOM   3176 O  O   . ARG   A 1 403 ? -28.943 -20.387 28.142 1.00 78.44  ? 699 ARG   A O   1 
ATOM   3177 C  CB  . ARG   A 1 403 ? -26.772 -19.035 29.335 1.00 81.39  ? 699 ARG   A CB  1 
ATOM   3178 C  CG  . ARG   A 1 403 ? -25.963 -18.714 30.578 1.00 95.04  ? 699 ARG   A CG  1 
ATOM   3179 C  CD  . ARG   A 1 403 ? -24.698 -17.957 30.221 1.00 103.80 ? 699 ARG   A CD  1 
ATOM   3180 N  NE  . ARG   A 1 403 ? -23.998 -18.585 29.106 1.00 112.94 ? 699 ARG   A NE  1 
ATOM   3181 C  CZ  . ARG   A 1 403 ? -23.865 -18.042 27.899 1.00 115.73 ? 699 ARG   A CZ  1 
ATOM   3182 N  NH1 . ARG   A 1 403 ? -24.373 -16.840 27.640 1.00 110.91 ? 699 ARG   A NH1 1 
ATOM   3183 N  NH2 . ARG   A 1 403 ? -23.212 -18.705 26.954 1.00 120.49 ? 699 ARG   A NH2 1 
ATOM   3184 N  N   . LEU   A 1 404 ? -30.003 -18.446 27.751 1.00 69.09  ? 700 LEU   A N   1 
ATOM   3185 C  CA  . LEU   A 1 404 ? -30.804 -18.990 26.671 1.00 63.34  ? 700 LEU   A CA  1 
ATOM   3186 C  C   . LEU   A 1 404 ? -30.069 -18.846 25.342 1.00 63.99  ? 700 LEU   A C   1 
ATOM   3187 O  O   . LEU   A 1 404 ? -29.042 -18.170 25.235 1.00 56.42  ? 700 LEU   A O   1 
ATOM   3188 C  CB  . LEU   A 1 404 ? -32.153 -18.286 26.593 1.00 61.98  ? 700 LEU   A CB  1 
ATOM   3189 C  CG  . LEU   A 1 404 ? -33.081 -18.250 27.802 1.00 61.64  ? 700 LEU   A CG  1 
ATOM   3190 C  CD1 . LEU   A 1 404 ? -34.310 -17.411 27.468 1.00 49.96  ? 700 LEU   A CD1 1 
ATOM   3191 C  CD2 . LEU   A 1 404 ? -33.468 -19.659 28.274 1.00 70.30  ? 700 LEU   A CD2 1 
ATOM   3192 N  N   . THR   A 1 405 ? -30.613 -19.503 24.321 1.00 67.80  ? 701 THR   A N   1 
ATOM   3193 C  CA  . THR   A 1 405 ? -30.097 -19.453 22.965 1.00 64.52  ? 701 THR   A CA  1 
ATOM   3194 C  C   . THR   A 1 405 ? -31.284 -19.309 22.022 1.00 67.50  ? 701 THR   A C   1 
ATOM   3195 O  O   . THR   A 1 405 ? -32.405 -19.692 22.380 1.00 70.03  ? 701 THR   A O   1 
ATOM   3196 C  CB  . THR   A 1 405 ? -29.266 -20.708 22.635 1.00 66.55  ? 701 THR   A CB  1 
ATOM   3197 O  OG1 . THR   A 1 405 ? -28.335 -20.413 21.601 1.00 64.01  ? 701 THR   A OG1 1 
ATOM   3198 C  CG2 . THR   A 1 405 ? -30.140 -21.860 22.205 1.00 56.30  ? 701 THR   A CG2 1 
ATOM   3199 N  N   . PRO   A 1 406 ? -31.094 -18.691 20.839 1.00 67.69  ? 702 PRO   A N   1 
ATOM   3200 C  CA  . PRO   A 1 406 ? -29.913 -18.041 20.246 1.00 65.28  ? 702 PRO   A CA  1 
ATOM   3201 C  C   . PRO   A 1 406 ? -29.314 -16.931 21.118 1.00 65.70  ? 702 PRO   A C   1 
ATOM   3202 O  O   . PRO   A 1 406 ? -30.030 -16.360 21.948 1.00 63.51  ? 702 PRO   A O   1 
ATOM   3203 C  CB  . PRO   A 1 406 ? -30.466 -17.468 18.928 1.00 61.30  ? 702 PRO   A CB  1 
ATOM   3204 C  CG  . PRO   A 1 406 ? -31.618 -18.360 18.589 1.00 62.54  ? 702 PRO   A CG  1 
ATOM   3205 C  CD  . PRO   A 1 406 ? -32.247 -18.671 19.916 1.00 61.77  ? 702 PRO   A CD  1 
ATOM   3206 N  N   . SER   A 1 407 ? -28.025 -16.636 20.936 1.00 64.22  ? 703 SER   A N   1 
ATOM   3207 C  CA  . SER   A 1 407 ? -27.313 -15.803 21.893 1.00 64.37  ? 703 SER   A CA  1 
ATOM   3208 C  C   . SER   A 1 407 ? -26.131 -15.110 21.235 1.00 65.83  ? 703 SER   A C   1 
ATOM   3209 O  O   . SER   A 1 407 ? -25.538 -15.626 20.283 1.00 63.24  ? 703 SER   A O   1 
ATOM   3210 C  CB  . SER   A 1 407 ? -26.803 -16.640 23.069 1.00 61.65  ? 703 SER   A CB  1 
ATOM   3211 O  OG  . SER   A 1 407 ? -25.760 -17.494 22.638 1.00 66.15  ? 703 SER   A OG  1 
ATOM   3212 N  N   . PHE   A 1 408 ? -25.791 -13.939 21.766 1.00 65.74  ? 704 PHE   A N   1 
ATOM   3213 C  CA  . PHE   A 1 408 ? -24.534 -13.286 21.436 1.00 63.62  ? 704 PHE   A CA  1 
ATOM   3214 C  C   . PHE   A 1 408 ? -23.482 -13.757 22.431 1.00 62.20  ? 704 PHE   A C   1 
ATOM   3215 O  O   . PHE   A 1 408 ? -23.759 -13.856 23.626 1.00 63.61  ? 704 PHE   A O   1 
ATOM   3216 C  CB  . PHE   A 1 408 ? -24.675 -11.763 21.460 1.00 59.92  ? 704 PHE   A CB  1 
ATOM   3217 C  CG  . PHE   A 1 408 ? -25.501 -11.221 20.327 1.00 55.68  ? 704 PHE   A CG  1 
ATOM   3218 C  CD1 . PHE   A 1 408 ? -26.808 -10.802 20.549 1.00 49.71  ? 704 PHE   A CD1 1 
ATOM   3219 C  CD2 . PHE   A 1 408 ? -24.979 -11.145 19.031 1.00 56.62  ? 704 PHE   A CD2 1 
ATOM   3220 C  CE1 . PHE   A 1 408 ? -27.590 -10.314 19.511 1.00 56.74  ? 704 PHE   A CE1 1 
ATOM   3221 C  CE2 . PHE   A 1 408 ? -25.758 -10.647 17.969 1.00 51.27  ? 704 PHE   A CE2 1 
ATOM   3222 C  CZ  . PHE   A 1 408 ? -27.062 -10.233 18.213 1.00 53.71  ? 704 PHE   A CZ  1 
ATOM   3223 N  N   . GLU   A 1 409 ? -22.297 -14.095 21.934 1.00 58.28  ? 705 GLU   A N   1 
ATOM   3224 C  CA  . GLU   A 1 409 ? -21.253 -14.676 22.758 1.00 55.79  ? 705 GLU   A CA  1 
ATOM   3225 C  C   . GLU   A 1 409 ? -19.948 -13.944 22.529 1.00 60.74  ? 705 GLU   A C   1 
ATOM   3226 O  O   . GLU   A 1 409 ? -19.639 -13.534 21.407 1.00 64.58  ? 705 GLU   A O   1 
ATOM   3227 C  CB  . GLU   A 1 409 ? -21.055 -16.182 22.488 1.00 63.46  ? 705 GLU   A CB  1 
ATOM   3228 C  CG  . GLU   A 1 409 ? -22.240 -17.105 22.829 1.00 74.69  ? 705 GLU   A CG  1 
ATOM   3229 C  CD  . GLU   A 1 409 ? -22.685 -17.040 24.293 1.00 88.17  ? 705 GLU   A CD  1 
ATOM   3230 O  OE1 . GLU   A 1 409 ? -21.908 -16.581 25.168 1.00 92.67  ? 705 GLU   A OE1 1 
ATOM   3231 O  OE2 . GLU   A 1 409 ? -23.835 -17.451 24.563 1.00 94.32  ? 705 GLU   A OE2 1 
ATOM   3232 N  N   . TYR   A 1 410 ? -19.194 -13.776 23.609 1.00 55.07  ? 706 TYR   A N   1 
ATOM   3233 C  CA  . TYR   A 1 410 ? -17.850 -13.245 23.510 1.00 49.50  ? 706 TYR   A CA  1 
ATOM   3234 C  C   . TYR   A 1 410 ? -16.973 -14.208 22.738 1.00 52.98  ? 706 TYR   A C   1 
ATOM   3235 O  O   . TYR   A 1 410 ? -17.215 -15.419 22.696 1.00 59.68  ? 706 TYR   A O   1 
ATOM   3236 C  CB  . TYR   A 1 410 ? -17.245 -13.054 24.900 1.00 55.02  ? 706 TYR   A CB  1 
ATOM   3237 C  CG  . TYR   A 1 410 ? -17.677 -11.828 25.653 1.00 62.84  ? 706 TYR   A CG  1 
ATOM   3238 C  CD1 . TYR   A 1 410 ? -18.034 -11.923 26.999 1.00 71.58  ? 706 TYR   A CD1 1 
ATOM   3239 C  CD2 . TYR   A 1 410 ? -17.662 -10.566 25.060 1.00 70.87  ? 706 TYR   A CD2 1 
ATOM   3240 C  CE1 . TYR   A 1 410 ? -18.400 -10.813 27.725 1.00 70.31  ? 706 TYR   A CE1 1 
ATOM   3241 C  CE2 . TYR   A 1 410 ? -18.031 -9.440  25.785 1.00 79.32  ? 706 TYR   A CE2 1 
ATOM   3242 C  CZ  . TYR   A 1 410 ? -18.396 -9.580  27.123 1.00 80.58  ? 706 TYR   A CZ  1 
ATOM   3243 O  OH  . TYR   A 1 410 ? -18.764 -8.485  27.869 1.00 88.37  ? 706 TYR   A OH  1 
ATOM   3244 N  N   . GLN   A 1 411 ? -15.922 -13.665 22.139 1.00 51.86  ? 707 GLN   A N   1 
ATOM   3245 C  CA  . GLN   A 1 411 ? -15.030 -14.518 21.376 1.00 54.24  ? 707 GLN   A CA  1 
ATOM   3246 C  C   . GLN   A 1 411 ? -13.655 -13.888 21.402 1.00 58.29  ? 707 GLN   A C   1 
ATOM   3247 O  O   . GLN   A 1 411 ? -13.542 -12.660 21.517 1.00 67.32  ? 707 GLN   A O   1 
ATOM   3248 C  CB  . GLN   A 1 411 ? -15.529 -14.708 19.934 1.00 60.60  ? 707 GLN   A CB  1 
ATOM   3249 C  CG  . GLN   A 1 411 ? -15.207 -13.551 19.016 1.00 63.10  ? 707 GLN   A CG  1 
ATOM   3250 C  CD  . GLN   A 1 411 ? -15.838 -13.692 17.650 1.00 70.93  ? 707 GLN   A CD  1 
ATOM   3251 O  OE1 . GLN   A 1 411 ? -15.951 -14.802 17.113 1.00 75.85  ? 707 GLN   A OE1 1 
ATOM   3252 N  NE2 . GLN   A 1 411 ? -16.253 -12.561 17.073 1.00 64.76  ? 707 GLN   A NE2 1 
ATOM   3253 N  N   . PRO   A 1 412 ? -12.597 -14.689 21.335 1.00 64.74  ? 708 PRO   A N   1 
ATOM   3254 C  CA  . PRO   A 1 412 ? -11.245 -14.127 21.443 1.00 74.69  ? 708 PRO   A CA  1 
ATOM   3255 C  C   . PRO   A 1 412 ? -10.944 -13.168 20.300 1.00 79.09  ? 708 PRO   A C   1 
ATOM   3256 O  O   . PRO   A 1 412 ? -11.488 -13.283 19.200 1.00 82.85  ? 708 PRO   A O   1 
ATOM   3257 C  CB  . PRO   A 1 412 ? -10.341 -15.366 21.394 1.00 78.90  ? 708 PRO   A CB  1 
ATOM   3258 C  CG  . PRO   A 1 412 ? -11.176 -16.419 20.696 1.00 79.51  ? 708 PRO   A CG  1 
ATOM   3259 C  CD  . PRO   A 1 412 ? -12.582 -16.153 21.166 1.00 71.43  ? 708 PRO   A CD  1 
ATOM   3260 N  N   . ASP   A 1 413 ? -10.083 -12.199 20.585 1.00 82.58  ? 709 ASP   A N   1 
ATOM   3261 C  CA  . ASP   A 1 413 ? -9.645  -11.275 19.554 1.00 87.30  ? 709 ASP   A CA  1 
ATOM   3262 C  C   . ASP   A 1 413 ? -8.973  -12.046 18.423 1.00 90.92  ? 709 ASP   A C   1 
ATOM   3263 O  O   . ASP   A 1 413 ? -8.238  -13.008 18.680 1.00 89.31  ? 709 ASP   A O   1 
ATOM   3264 C  CB  . ASP   A 1 413 ? -8.674  -10.250 20.130 1.00 93.96  ? 709 ASP   A CB  1 
ATOM   3265 C  CG  . ASP   A 1 413 ? -9.336  -9.317  21.114 1.00 97.24  ? 709 ASP   A CG  1 
ATOM   3266 O  OD1 . ASP   A 1 413 ? -10.470 -8.866  20.837 1.00 92.72  ? 709 ASP   A OD1 1 
ATOM   3267 O  OD2 . ASP   A 1 413 ? -8.723  -9.040  22.167 1.00 103.19 ? 709 ASP   A OD2 1 
ATOM   3268 N  N   . PRO   A 1 414 ? -9.195  -11.653 17.165 1.00 95.69  ? 710 PRO   A N   1 
ATOM   3269 C  CA  . PRO   A 1 414 ? -8.670  -12.454 16.046 1.00 98.67  ? 710 PRO   A CA  1 
ATOM   3270 C  C   . PRO   A 1 414 ? -7.161  -12.436 15.941 1.00 105.26 ? 710 PRO   A C   1 
ATOM   3271 O  O   . PRO   A 1 414 ? -6.597  -13.348 15.327 1.00 114.91 ? 710 PRO   A O   1 
ATOM   3272 C  CB  . PRO   A 1 414 ? -9.312  -11.812 14.802 1.00 91.76  ? 710 PRO   A CB  1 
ATOM   3273 C  CG  . PRO   A 1 414 ? -10.331 -10.834 15.302 1.00 91.58  ? 710 PRO   A CG  1 
ATOM   3274 C  CD  . PRO   A 1 414 ? -9.921  -10.457 16.705 1.00 96.09  ? 710 PRO   A CD  1 
ATOM   3275 N  N   . TRP   A 1 415 ? -6.487  -11.431 16.500 1.00 101.48 ? 711 TRP   A N   1 
ATOM   3276 C  CA  . TRP   A 1 415 ? -5.038  -11.357 16.373 1.00 104.55 ? 711 TRP   A CA  1 
ATOM   3277 C  C   . TRP   A 1 415 ? -4.306  -12.258 17.361 1.00 103.62 ? 711 TRP   A C   1 
ATOM   3278 O  O   . TRP   A 1 415 ? -3.095  -12.451 17.215 1.00 104.97 ? 711 TRP   A O   1 
ATOM   3279 C  CB  . TRP   A 1 415 ? -4.566  -9.905  16.522 1.00 105.87 ? 711 TRP   A CB  1 
ATOM   3280 C  CG  . TRP   A 1 415 ? -4.953  -9.245  17.811 1.00 100.77 ? 711 TRP   A CG  1 
ATOM   3281 C  CD1 . TRP   A 1 415 ? -4.255  -9.277  18.983 1.00 100.48 ? 711 TRP   A CD1 1 
ATOM   3282 C  CD2 . TRP   A 1 415 ? -6.118  -8.439  18.059 1.00 98.04  ? 711 TRP   A CD2 1 
ATOM   3283 N  NE1 . TRP   A 1 415 ? -4.914  -8.552  19.948 1.00 94.98  ? 711 TRP   A NE1 1 
ATOM   3284 C  CE2 . TRP   A 1 415 ? -6.060  -8.029  19.408 1.00 96.14  ? 711 TRP   A CE2 1 
ATOM   3285 C  CE3 . TRP   A 1 415 ? -7.205  -8.029  17.274 1.00 97.51  ? 711 TRP   A CE3 1 
ATOM   3286 C  CZ2 . TRP   A 1 415 ? -7.040  -7.224  19.989 1.00 92.99  ? 711 TRP   A CZ2 1 
ATOM   3287 C  CZ3 . TRP   A 1 415 ? -8.184  -7.234  17.856 1.00 93.53  ? 711 TRP   A CZ3 1 
ATOM   3288 C  CH2 . TRP   A 1 415 ? -8.095  -6.844  19.201 1.00 94.58  ? 711 TRP   A CH2 1 
ATOM   3289 N  N   . ASN   A 1 416 ? -4.999  -12.815 18.358 1.00 100.82 ? 712 ASN   A N   1 
ATOM   3290 C  CA  . ASN   A 1 416 ? -4.407  -13.877 19.164 1.00 104.26 ? 712 ASN   A CA  1 
ATOM   3291 C  C   . ASN   A 1 416 ? -4.581  -15.235 18.506 1.00 102.51 ? 712 ASN   A C   1 
ATOM   3292 O  O   . ASN   A 1 416 ? -3.796  -16.156 18.773 1.00 105.84 ? 712 ASN   A O   1 
ATOM   3293 C  CB  . ASN   A 1 416 ? -5.024  -13.912 20.568 1.00 100.48 ? 712 ASN   A CB  1 
ATOM   3294 C  CG  . ASN   A 1 416 ? -5.155  -12.534 21.188 1.00 100.09 ? 712 ASN   A CG  1 
ATOM   3295 O  OD1 . ASN   A 1 416 ? -4.353  -11.638 20.922 1.00 105.02 ? 712 ASN   A OD1 1 
ATOM   3296 N  ND2 . ASN   A 1 416 ? -6.177  -12.357 22.025 1.00 94.11  ? 712 ASN   A ND2 1 
ATOM   3297 N  N   . THR   A 1 417 ? -5.581  -15.363 17.638 1.00 98.68  ? 713 THR   A N   1 
ATOM   3298 C  CA  . THR   A 1 417 ? -5.988  -16.635 17.065 1.00 101.82 ? 713 THR   A CA  1 
ATOM   3299 C  C   . THR   A 1 417 ? -5.480  -16.862 15.648 1.00 108.06 ? 713 THR   A C   1 
ATOM   3300 O  O   . THR   A 1 417 ? -5.376  -18.020 15.227 1.00 112.42 ? 713 THR   A O   1 
ATOM   3301 C  CB  . THR   A 1 417 ? -7.517  -16.719 17.042 1.00 97.04  ? 713 THR   A CB  1 
ATOM   3302 O  OG1 . THR   A 1 417 ? -8.068  -15.482 17.516 1.00 93.56  ? 713 THR   A OG1 1 
ATOM   3303 C  CG2 . THR   A 1 417 ? -8.021  -17.862 17.904 1.00 98.50  ? 713 THR   A CG2 1 
ATOM   3304 N  N   . HIS   A 1 418 ? -5.157  -15.796 14.913 1.00 110.11 ? 714 HIS   A N   1 
ATOM   3305 C  CA  . HIS   A 1 418 ? -5.036  -15.862 13.460 1.00 112.63 ? 714 HIS   A CA  1 
ATOM   3306 C  C   . HIS   A 1 418 ? -3.710  -16.480 13.032 1.00 117.66 ? 714 HIS   A C   1 
ATOM   3307 O  O   . HIS   A 1 418 ? -2.640  -15.878 13.192 1.00 118.60 ? 714 HIS   A O   1 
ATOM   3308 C  CB  . HIS   A 1 418 ? -5.205  -14.472 12.862 1.00 109.43 ? 714 HIS   A CB  1 
ATOM   3309 C  CG  . HIS   A 1 418 ? -5.291  -14.468 11.370 1.00 106.11 ? 714 HIS   A CG  1 
ATOM   3310 N  ND1 . HIS   A 1 418 ? -5.947  -15.450 10.658 1.00 105.37 ? 714 HIS   A ND1 1 
ATOM   3311 C  CD2 . HIS   A 1 418 ? -4.802  -13.599 10.455 1.00 107.25 ? 714 HIS   A CD2 1 
ATOM   3312 C  CE1 . HIS   A 1 418 ? -5.856  -15.183 9.367  1.00 105.65 ? 714 HIS   A CE1 1 
ATOM   3313 N  NE2 . HIS   A 1 418 ? -5.168  -14.066 9.218  1.00 106.02 ? 714 HIS   A NE2 1 
ATOM   3314 N  N   . VAL   A 1 419 ? -3.795  -17.673 12.446 1.00 120.22 ? 715 VAL   A N   1 
ATOM   3315 C  CA  . VAL   A 1 419 ? -2.668  -18.277 11.753 1.00 127.02 ? 715 VAL   A CA  1 
ATOM   3316 C  C   . VAL   A 1 419 ? -2.338  -17.382 10.568 1.00 129.14 ? 715 VAL   A C   1 
ATOM   3317 O  O   . VAL   A 1 419 ? -2.969  -17.465 9.508  1.00 124.72 ? 715 VAL   A O   1 
ATOM   3318 C  CB  . VAL   A 1 419 ? -2.977  -19.722 11.326 1.00 125.28 ? 715 VAL   A CB  1 
ATOM   3319 C  CG1 . VAL   A 1 419 ? -1.862  -20.267 10.450 1.00 127.63 ? 715 VAL   A CG1 1 
ATOM   3320 C  CG2 . VAL   A 1 419 ? -3.167  -20.602 12.561 1.00 121.02 ? 715 VAL   A CG2 1 
ATOM   3321 N  N   . TRP   A 1 420 ? -1.352  -16.514 10.756 1.00 138.45 ? 716 TRP   A N   1 
ATOM   3322 C  CA  . TRP   A 1 420 ? -1.045  -15.411 9.859  1.00 142.79 ? 716 TRP   A CA  1 
ATOM   3323 C  C   . TRP   A 1 420 ? -0.052  -15.811 8.765  1.00 154.66 ? 716 TRP   A C   1 
ATOM   3324 O  O   . TRP   A 1 420 ? 0.558   -16.884 8.796  1.00 155.33 ? 716 TRP   A O   1 
ATOM   3325 C  CB  . TRP   A 1 420 ? -0.496  -14.246 10.681 1.00 143.61 ? 716 TRP   A CB  1 
ATOM   3326 C  CG  . TRP   A 1 420 ? -1.007  -12.905 10.263 1.00 142.28 ? 716 TRP   A CG  1 
ATOM   3327 C  CD1 . TRP   A 1 420 ? -1.212  -12.466 8.990  1.00 142.33 ? 716 TRP   A CD1 1 
ATOM   3328 C  CD2 . TRP   A 1 420 ? -1.396  -11.833 11.124 1.00 140.81 ? 716 TRP   A CD2 1 
ATOM   3329 N  NE1 . TRP   A 1 420 ? -1.696  -11.180 9.003  1.00 140.22 ? 716 TRP   A NE1 1 
ATOM   3330 C  CE2 . TRP   A 1 420 ? -1.818  -10.768 10.302 1.00 138.61 ? 716 TRP   A CE2 1 
ATOM   3331 C  CE3 . TRP   A 1 420 ? -1.426  -11.670 12.509 1.00 140.62 ? 716 TRP   A CE3 1 
ATOM   3332 C  CZ2 . TRP   A 1 420 ? -2.262  -9.559  10.820 1.00 137.58 ? 716 TRP   A CZ2 1 
ATOM   3333 C  CZ3 . TRP   A 1 420 ? -1.865  -10.472 13.022 1.00 140.28 ? 716 TRP   A CZ3 1 
ATOM   3334 C  CH2 . TRP   A 1 420 ? -2.278  -9.430  12.180 1.00 139.51 ? 716 TRP   A CH2 1 
ATOM   3335 N  N   . LYS   A 1 421 ? 0.105   -14.917 7.781  1.00 79.73  ? 717 LYS   A N   1 
ATOM   3336 C  CA  . LYS   A 1 421 ? 1.181   -15.035 6.785  1.00 89.56  ? 717 LYS   A CA  1 
ATOM   3337 C  C   . LYS   A 1 421 ? 1.775   -13.653 6.455  1.00 91.54  ? 717 LYS   A C   1 
ATOM   3338 O  O   . LYS   A 1 421 ? 1.900   -13.272 5.299  1.00 87.09  ? 717 LYS   A O   1 
ATOM   3339 C  CB  . LYS   A 1 421 ? 0.655   -15.676 5.489  1.00 89.86  ? 717 LYS   A CB  1 
ATOM   3340 C  CG  . LYS   A 1 421 ? 0.365   -17.148 5.648  1.00 94.02  ? 717 LYS   A CG  1 
ATOM   3341 C  CD  . LYS   A 1 421 ? 1.274   -17.974 4.756  1.00 100.48 ? 717 LYS   A CD  1 
ATOM   3342 C  CE  . LYS   A 1 421 ? 0.737   -19.410 4.552  1.00 102.15 ? 717 LYS   A CE  1 
ATOM   3343 N  NZ  . LYS   A 1 421 ? 1.706   -20.498 4.972  1.00 101.71 ? 717 LYS   A NZ  1 
HETATM 3344 C  CHA . HEM   B 2 .   ? -24.999 -4.357  26.111 1.00 56.29  ? 801 HEM   A CHA 1 
HETATM 3345 C  CHB . HEM   B 2 .   ? -28.183 -0.740  25.761 1.00 64.79  ? 801 HEM   A CHB 1 
HETATM 3346 C  CHC . HEM   B 2 .   ? -29.213 -2.398  21.282 1.00 61.61  ? 801 HEM   A CHC 1 
HETATM 3347 C  CHD . HEM   B 2 .   ? -27.271 -6.693  22.437 1.00 58.86  ? 801 HEM   A CHD 1 
HETATM 3348 C  C1A . HEM   B 2 .   ? -25.620 -3.145  26.348 1.00 57.59  ? 801 HEM   A C1A 1 
HETATM 3349 C  C2A . HEM   B 2 .   ? -25.262 -2.120  27.316 1.00 66.40  ? 801 HEM   A C2A 1 
HETATM 3350 C  C3A . HEM   B 2 .   ? -26.139 -1.109  27.215 1.00 66.14  ? 801 HEM   A C3A 1 
HETATM 3351 C  C4A . HEM   B 2 .   ? -27.098 -1.472  26.191 1.00 62.80  ? 801 HEM   A C4A 1 
HETATM 3352 C  CMA . HEM   B 2 .   ? -26.165 0.209   28.028 1.00 65.28  ? 801 HEM   A CMA 1 
HETATM 3353 C  CAA . HEM   B 2 .   ? -24.043 -2.177  28.254 1.00 58.25  ? 801 HEM   A CAA 1 
HETATM 3354 C  CBA . HEM   B 2 .   ? -22.879 -1.767  27.352 1.00 51.04  ? 801 HEM   A CBA 1 
HETATM 3355 C  CGA . HEM   B 2 .   ? -21.682 -1.627  28.227 1.00 58.98  ? 801 HEM   A CGA 1 
HETATM 3356 O  O1A . HEM   B 2 .   ? -21.824 -1.095  29.382 1.00 54.32  ? 801 HEM   A O1A 1 
HETATM 3357 O  O2A . HEM   B 2 .   ? -20.601 -2.054  27.748 1.00 61.90  ? 801 HEM   A O2A 1 
HETATM 3358 C  C1B . HEM   B 2 .   ? -28.748 -0.842  24.503 1.00 68.34  ? 801 HEM   A C1B 1 
HETATM 3359 C  C2B . HEM   B 2 .   ? -29.708 0.071   23.912 1.00 65.29  ? 801 HEM   A C2B 1 
HETATM 3360 C  C3B . HEM   B 2 .   ? -30.015 -0.381  22.694 1.00 66.59  ? 801 HEM   A C3B 1 
HETATM 3361 C  C4B . HEM   B 2 .   ? -29.242 -1.604  22.430 1.00 67.43  ? 801 HEM   A C4B 1 
HETATM 3362 C  CMB . HEM   B 2 .   ? -30.298 1.326   24.604 1.00 63.16  ? 801 HEM   A CMB 1 
HETATM 3363 C  CAB . HEM   B 2 .   ? -31.016 0.353   21.766 1.00 74.26  ? 801 HEM   A CAB 1 
HETATM 3364 C  CBB . HEM   B 2 .   ? -31.555 -0.220  20.690 1.00 80.99  ? 801 HEM   A CBB 1 
HETATM 3365 C  C1C . HEM   B 2 .   ? -28.767 -3.703  21.148 1.00 58.68  ? 801 HEM   A C1C 1 
HETATM 3366 C  C2C . HEM   B 2 .   ? -28.850 -4.555  19.952 1.00 56.12  ? 801 HEM   A C2C 1 
HETATM 3367 C  C3C . HEM   B 2 .   ? -28.311 -5.761  20.256 1.00 57.45  ? 801 HEM   A C3C 1 
HETATM 3368 C  C4C . HEM   B 2 .   ? -27.870 -5.709  21.653 1.00 54.34  ? 801 HEM   A C4C 1 
HETATM 3369 C  CMC . HEM   B 2 .   ? -29.467 -4.043  18.646 1.00 56.93  ? 801 HEM   A CMC 1 
HETATM 3370 C  CAC . HEM   B 2 .   ? -28.148 -7.031  19.380 1.00 50.87  ? 801 HEM   A CAC 1 
HETATM 3371 C  CBC . HEM   B 2 .   ? -28.616 -7.135  18.131 1.00 57.10  ? 801 HEM   A CBC 1 
HETATM 3372 C  C1D . HEM   B 2 .   ? -26.358 -6.393  23.429 1.00 61.69  ? 801 HEM   A C1D 1 
HETATM 3373 C  C2D . HEM   B 2 .   ? -25.151 -7.114  23.779 1.00 64.97  ? 801 HEM   A C2D 1 
HETATM 3374 C  C3D . HEM   B 2 .   ? -24.544 -6.467  24.788 1.00 64.87  ? 801 HEM   A C3D 1 
HETATM 3375 C  C4D . HEM   B 2 .   ? -25.312 -5.289  25.120 1.00 61.46  ? 801 HEM   A C4D 1 
HETATM 3376 C  CMD . HEM   B 2 .   ? -24.652 -8.413  23.121 1.00 68.98  ? 801 HEM   A CMD 1 
HETATM 3377 C  CAD . HEM   B 2 .   ? -23.212 -6.830  25.467 1.00 56.98  ? 801 HEM   A CAD 1 
HETATM 3378 C  CBD . HEM   B 2 .   ? -23.191 -8.085  26.310 1.00 64.17  ? 801 HEM   A CBD 1 
HETATM 3379 C  CGD . HEM   B 2 .   ? -21.746 -8.225  26.746 1.00 65.18  ? 801 HEM   A CGD 1 
HETATM 3380 O  O1D . HEM   B 2 .   ? -21.408 -9.268  27.381 1.00 58.93  ? 801 HEM   A O1D 1 
HETATM 3381 O  O2D . HEM   B 2 .   ? -20.931 -7.294  26.435 1.00 61.33  ? 801 HEM   A O2D 1 
HETATM 3382 N  NA  . HEM   B 2 .   ? -26.751 -2.712  25.705 1.00 61.13  ? 801 HEM   A NA  1 
HETATM 3383 N  NB  . HEM   B 2 .   ? -28.488 -1.841  23.578 1.00 64.47  ? 801 HEM   A NB  1 
HETATM 3384 N  NC  . HEM   B 2 .   ? -28.175 -4.451  22.124 1.00 58.53  ? 801 HEM   A NC  1 
HETATM 3385 N  ND  . HEM   B 2 .   ? -26.413 -5.286  24.263 1.00 57.06  ? 801 HEM   A ND  1 
HETATM 3386 FE FE  . HEM   B 2 .   ? -27.653 -3.717  24.054 1.00 56.70  ? 801 HEM   A FE  1 
HETATM 3387 N  N1  . H4B   C 3 .   ? -21.920 -3.217  33.555 1.00 60.60  ? 802 H4B   A N1  1 
HETATM 3388 C  C2  . H4B   C 3 .   ? -21.920 -2.640  32.315 1.00 55.47  ? 802 H4B   A C2  1 
HETATM 3389 N  N2  . H4B   C 3 .   ? -23.103 -2.238  31.773 1.00 45.57  ? 802 H4B   A N2  1 
HETATM 3390 N  N3  . H4B   C 3 .   ? -20.762 -2.456  31.632 1.00 45.78  ? 802 H4B   A N3  1 
HETATM 3391 C  C4  . H4B   C 3 .   ? -19.586 -2.859  32.155 1.00 50.02  ? 802 H4B   A C4  1 
HETATM 3392 O  O4  . H4B   C 3 .   ? -18.517 -2.699  31.530 1.00 48.87  ? 802 H4B   A O4  1 
HETATM 3393 C  C4A . H4B   C 3 .   ? -19.573 -3.453  33.399 1.00 51.22  ? 802 H4B   A C4A 1 
HETATM 3394 C  C8A . H4B   C 3 .   ? -20.758 -3.635  34.110 1.00 55.52  ? 802 H4B   A C8A 1 
HETATM 3395 N  N5  . H4B   C 3 .   ? -18.408 -3.878  33.920 1.00 50.42  ? 802 H4B   A N5  1 
HETATM 3396 N  N8  . H4B   C 3 .   ? -20.760 -4.220  35.326 1.00 56.07  ? 802 H4B   A N8  1 
HETATM 3397 C  C6  . H4B   C 3 .   ? -18.481 -4.901  34.967 1.00 58.99  ? 802 H4B   A C6  1 
HETATM 3398 C  C7  . H4B   C 3 .   ? -19.514 -4.521  36.017 1.00 56.33  ? 802 H4B   A C7  1 
HETATM 3399 C  C9  . H4B   C 3 .   ? -17.157 -5.095  35.698 1.00 57.23  ? 802 H4B   A C9  1 
HETATM 3400 O  O9  . H4B   C 3 .   ? -16.777 -3.786  36.129 1.00 55.28  ? 802 H4B   A O9  1 
HETATM 3401 C  C10 . H4B   C 3 .   ? -17.324 -6.042  36.905 1.00 60.22  ? 802 H4B   A C10 1 
HETATM 3402 C  C11 . H4B   C 3 .   ? -16.054 -6.171  37.753 1.00 52.45  ? 802 H4B   A C11 1 
HETATM 3403 O  O10 . H4B   C 3 .   ? -17.768 -7.344  36.478 1.00 63.69  ? 802 H4B   A O10 1 
HETATM 3404 ZN ZN  . ZN    D 4 .   ? -24.382 -16.401 40.788 0.47 59.25  ? 803 ZN    A ZN  1 
HETATM 3405 C  C11 . A1A0K E 5 .   ? -22.220 -1.511  23.637 1.00 89.13  ? 804 A1A0K A C11 1 
HETATM 3406 C  C12 . A1A0K E 5 .   ? -21.232 -0.550  23.547 1.00 98.50  ? 804 A1A0K A C12 1 
HETATM 3407 C  C13 . A1A0K E 5 .   ? -19.957 -0.823  24.001 1.00 104.60 ? 804 A1A0K A C13 1 
HETATM 3408 C  C14 . A1A0K E 5 .   ? -19.666 -2.073  24.560 1.00 100.26 ? 804 A1A0K A C14 1 
HETATM 3409 C  C15 . A1A0K E 5 .   ? -20.651 -3.062  24.656 1.00 94.03  ? 804 A1A0K A C15 1 
HETATM 3410 C  C16 . A1A0K E 5 .   ? -21.936 -2.759  24.191 1.00 88.88  ? 804 A1A0K A C16 1 
HETATM 3411 C  C17 . A1A0K E 5 .   ? -20.414 -4.445  25.266 1.00 93.16  ? 804 A1A0K A C17 1 
HETATM 3412 C  C02 . A1A0K E 5 .   ? -25.481 0.205   23.279 1.00 75.44  ? 804 A1A0K A C02 1 
HETATM 3413 C  C03 . A1A0K E 5 .   ? -26.054 -0.467  22.198 1.00 73.59  ? 804 A1A0K A C03 1 
HETATM 3414 C  C04 . A1A0K E 5 .   ? -25.357 -1.497  21.580 1.00 73.92  ? 804 A1A0K A C04 1 
HETATM 3415 C  C05 . A1A0K E 5 .   ? -24.104 -1.848  22.048 1.00 76.10  ? 804 A1A0K A C05 1 
HETATM 3416 C  C06 . A1A0K E 5 .   ? -23.571 -1.164  23.131 1.00 81.52  ? 804 A1A0K A C06 1 
HETATM 3417 C  C07 . A1A0K E 5 .   ? -25.931 -2.236  20.405 1.00 77.66  ? 804 A1A0K A C07 1 
HETATM 3418 C  C19 . A1A0K E 5 .   ? -18.747 -5.313  23.640 1.00 93.78  ? 804 A1A0K A C19 1 
HETATM 3419 C  C20 . A1A0K E 5 .   ? -18.019 -4.630  25.866 1.00 91.23  ? 804 A1A0K A C20 1 
HETATM 3420 F  F12 . A1A0K E 5 .   ? -21.502 0.653   23.011 1.00 100.84 ? 804 A1A0K A F12 1 
HETATM 3421 F  F13 . A1A0K E 5 .   ? -19.019 0.139   23.895 1.00 111.09 ? 804 A1A0K A F13 1 
HETATM 3422 N  N01 . A1A0K E 5 .   ? -24.253 -0.148  23.714 1.00 77.13  ? 804 A1A0K A N01 1 
HETATM 3423 N  N02 . A1A0K E 5 .   ? -26.146 1.207   23.901 1.00 77.99  ? 804 A1A0K A N02 1 
HETATM 3424 N  N18 . A1A0K E 5 .   ? -19.132 -5.178  25.062 1.00 94.22  ? 804 A1A0K A N18 1 
HETATM 3425 O  O   . HOH   F 6 .   ? -15.719 -18.894 4.687  1.00 59.67  ? 901 HOH   A O   1 
HETATM 3426 O  O   . HOH   F 6 .   ? -29.819 -12.810 40.300 1.00 69.82  ? 902 HOH   A O   1 
HETATM 3427 O  O   . HOH   F 6 .   ? -13.316 -9.750  16.548 1.00 57.56  ? 903 HOH   A O   1 
HETATM 3428 O  O   . HOH   F 6 .   ? -35.675 -36.390 0.799  1.00 92.96  ? 904 HOH   A O   1 
HETATM 3429 O  O   . HOH   F 6 .   ? -25.052 -4.325  5.934  1.00 54.56  ? 905 HOH   A O   1 
HETATM 3430 O  O   . HOH   F 6 .   ? -14.822 -21.029 9.627  1.00 63.18  ? 906 HOH   A O   1 
HETATM 3431 O  O   . HOH   F 6 .   ? -26.390 -34.694 13.786 1.00 84.64  ? 907 HOH   A O   1 
HETATM 3432 O  O   . HOH   F 6 .   ? -27.040 -3.208  30.046 1.00 59.32  ? 908 HOH   A O   1 
HETATM 3433 O  O   . HOH   F 6 .   ? -40.914 -5.746  38.666 1.00 63.23  ? 909 HOH   A O   1 
HETATM 3434 O  O   . HOH   F 6 .   ? -23.349 6.718   12.123 1.00 56.03  ? 910 HOH   A O   1 
HETATM 3435 O  O   . HOH   F 6 .   ? -19.891 -8.592  34.534 1.00 60.74  ? 911 HOH   A O   1 
HETATM 3436 O  O   . HOH   F 6 .   ? -34.983 6.614   37.642 1.00 59.31  ? 912 HOH   A O   1 
HETATM 3437 O  O   . HOH   F 6 .   ? -34.876 -11.990 35.690 1.00 51.04  ? 913 HOH   A O   1 
HETATM 3438 O  O   . HOH   F 6 .   ? -24.463 -11.200 37.450 1.00 55.16  ? 914 HOH   A O   1 
HETATM 3439 O  O   . HOH   F 6 .   ? -10.217 12.506  35.550 1.00 76.46  ? 915 HOH   A O   1 
HETATM 3440 O  O   . HOH   F 6 .   ? -35.845 -10.282 26.829 1.00 59.88  ? 916 HOH   A O   1 
HETATM 3441 O  O   . HOH   F 6 .   ? -23.500 -0.687  34.692 1.00 70.39  ? 917 HOH   A O   1 
HETATM 3442 O  O   . HOH   F 6 .   ? -29.763 -15.501 27.883 1.00 72.03  ? 918 HOH   A O   1 
HETATM 3443 O  O   . HOH   F 6 .   ? -20.619 1.438   25.771 1.00 60.70  ? 919 HOH   A O   1 
HETATM 3444 O  O   . HOH   F 6 .   ? -21.968 -14.983 -2.934 1.00 55.06  ? 920 HOH   A O   1 
HETATM 3445 O  O   . HOH   F 6 .   ? -38.051 -0.773  40.951 1.00 64.82  ? 921 HOH   A O   1 
HETATM 3446 O  O   . HOH   F 6 .   ? -21.694 -10.477 35.003 1.00 58.99  ? 922 HOH   A O   1 
HETATM 3447 O  O   . HOH   F 6 .   ? -21.787 1.570   29.931 1.00 48.40  ? 923 HOH   A O   1 
HETATM 3448 O  O   . HOH   F 6 .   ? -19.866 -14.521 10.677 1.00 71.89  ? 924 HOH   A O   1 
HETATM 3449 O  O   . HOH   F 6 .   ? -29.653 22.618  18.453 1.00 68.84  ? 925 HOH   A O   1 
HETATM 3450 O  O   . HOH   F 6 .   ? -17.444 12.260  10.675 1.00 81.01  ? 926 HOH   A O   1 
HETATM 3451 O  O   . HOH   F 6 .   ? -37.391 2.895   9.320  1.00 64.65  ? 927 HOH   A O   1 
HETATM 3452 O  O   . HOH   F 6 .   ? -23.677 -18.405 6.736  1.00 57.57  ? 928 HOH   A O   1 
HETATM 3453 O  O   . HOH   F 6 .   ? -18.519 3.127   24.052 1.00 60.84  ? 929 HOH   A O   1 
HETATM 3454 O  O   . HOH   F 6 .   ? -28.533 -10.805 37.914 1.00 68.02  ? 930 HOH   A O   1 
HETATM 3455 O  O   . HOH   F 6 .   ? -18.008 -18.228 21.650 1.00 60.85  ? 931 HOH   A O   1 
HETATM 3456 O  O   . HOH   F 6 .   ? -43.425 -14.920 23.257 1.00 77.24  ? 932 HOH   A O   1 
HETATM 3457 O  O   . HOH   F 6 .   ? -36.875 -7.570  10.185 1.00 73.38  ? 933 HOH   A O   1 
HETATM 3458 O  O   . HOH   F 6 .   ? -17.048 -3.394  28.616 1.00 78.23  ? 934 HOH   A O   1 
HETATM 3459 O  O   . HOH   F 6 .   ? -27.541 23.862  20.346 1.00 84.51  ? 935 HOH   A O   1 
HETATM 3460 O  O   . HOH   F 6 .   ? -28.368 -14.369 0.741  1.00 96.66  ? 936 HOH   A O   1 
HETATM 3461 O  O   . HOH   F 6 .   ? -17.292 0.971   28.975 1.00 61.52  ? 937 HOH   A O   1 
HETATM 3462 O  O   . HOH   F 6 .   ? -38.620 -19.031 23.770 1.00 80.71  ? 938 HOH   A O   1 
HETATM 3463 O  O   . HOH   F 6 .   ? -34.112 2.556   25.362 1.00 85.86  ? 939 HOH   A O   1 
HETATM 3464 O  O   . HOH   F 6 .   ? 2.786   -0.179  16.613 1.00 70.39  ? 940 HOH   A O   1 
HETATM 3465 O  O   . HOH   F 6 .   ? -27.400 -17.663 1.958  1.00 69.13  ? 941 HOH   A O   1 
HETATM 3466 O  O   . HOH   F 6 .   ? -46.280 -19.078 29.096 1.00 101.20 ? 942 HOH   A O   1 
HETATM 3467 O  O   . HOH   F 6 .   ? -48.445 -17.880 27.323 1.00 83.86  ? 943 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   . ARG A 3   ? 1.9450 1.9298 1.7004 -0.5355 0.0327  0.0265  299 ARG A N   
2    C CA  . ARG A 3   ? 1.9235 1.8758 1.6867 -0.5176 0.0242  0.0172  299 ARG A CA  
3    C C   . ARG A 3   ? 1.8300 1.9024 1.6505 -0.5254 0.0221  0.0103  299 ARG A C   
4    O O   . ARG A 3   ? 1.9168 1.9768 1.7227 -0.5361 0.0169  0.0042  299 ARG A O   
5    C CB  . ARG A 3   ? 2.0541 1.8852 1.7322 -0.5419 0.0214  0.0170  299 ARG A CB  
6    C CG  . ARG A 3   ? 2.0715 1.8381 1.7429 -0.5170 0.0136  0.0088  299 ARG A CG  
7    C CD  . ARG A 3   ? 2.0562 1.7683 1.7397 -0.4559 0.0104  0.0089  299 ARG A CD  
8    N NE  . ARG A 3   ? 2.0249 1.7350 1.7378 -0.4202 0.0032  -0.0002 299 ARG A NE  
9    C CZ  . ARG A 3   ? 2.0783 1.6973 1.7386 -0.4197 -0.0006 -0.0043 299 ARG A CZ  
10   N NH1 . ARG A 3   ? 2.1698 1.6819 1.7386 -0.4512 0.0015  -0.0005 299 ARG A NH1 
11   N NH2 . ARG A 3   ? 2.0251 1.6563 1.7188 -0.3861 -0.0064 -0.0122 299 ARG A NH2 
12   N N   . PHE A 4   ? 1.6600 1.8470 1.5402 -0.5067 0.0259  0.0111  300 PHE A N   
13   C CA  . PHE A 4   ? 1.4952 1.8051 1.4344 -0.4979 0.0241  0.0052  300 PHE A CA  
14   C C   . PHE A 4   ? 1.3784 1.7469 1.3715 -0.4359 0.0252  0.0045  300 PHE A C   
15   O O   . PHE A 4   ? 1.3873 1.8616 1.4107 -0.4319 0.0308  0.0065  300 PHE A O   
16   C CB  . PHE A 4   ? 1.4922 1.8784 1.4165 -0.5316 0.0272  0.0075  300 PHE A CB  
17   C CG  . PHE A 4   ? 1.5945 1.8974 1.4433 -0.5788 0.0257  0.0091  300 PHE A CG  
18   C CD1 . PHE A 4   ? 1.6562 1.9026 1.4488 -0.6090 0.0307  0.0167  300 PHE A CD1 
19   C CD2 . PHE A 4   ? 1.6254 1.9030 1.4541 -0.5921 0.0192  0.0028  300 PHE A CD2 
20   C CE1 . PHE A 4   ? 1.7507 1.9145 1.4651 -0.6509 0.0288  0.0175  300 PHE A CE1 
21   C CE2 . PHE A 4   ? 1.7308 1.9280 1.4827 -0.6346 0.0180  0.0039  300 PHE A CE2 
22   C CZ  . PHE A 4   ? 1.8048 1.9437 1.4975 -0.6638 0.0226  0.0110  300 PHE A CZ  
23   N N   . LEU A 5   ? 1.2794 1.5780 1.2802 -0.3865 0.0196  0.0011  301 LEU A N   
24   C CA  . LEU A 5   ? 1.1109 1.4123 1.1339 -0.3371 0.0207  0.0024  301 LEU A CA  
25   C C   . LEU A 5   ? 1.0161 1.4234 1.0879 -0.3028 0.0217  -0.0012 301 LEU A C   
26   O O   . LEU A 5   ? 1.0056 1.4767 1.1021 -0.3016 0.0190  -0.0061 301 LEU A O   
27   C CB  . LEU A 5   ? 1.0377 1.2494 1.0569 -0.2988 0.0132  -0.0007 301 LEU A CB  
28   C CG  . LEU A 5   ? 1.0738 1.1778 1.0381 -0.3193 0.0129  0.0038  301 LEU A CG  
29   C CD1 . LEU A 5   ? 1.1161 1.1514 1.0751 -0.2947 0.0049  -0.0013 301 LEU A CD1 
30   C CD2 . LEU A 5   ? 1.0357 1.1086 0.9832 -0.3057 0.0165  0.0107  301 LEU A CD2 
31   N N   . LYS A 6   ? 0.8974 1.3174 0.9771 -0.2711 0.0252  0.0013  302 LYS A N   
32   C CA  . LYS A 6   ? 0.8177 1.3239 0.9293 -0.2319 0.0273  -0.0016 302 LYS A CA  
33   C C   . LYS A 6   ? 0.7190 1.1730 0.8382 -0.1785 0.0209  -0.0062 302 LYS A C   
34   O O   . LYS A 6   ? 0.5418 0.9205 0.6433 -0.1712 0.0190  -0.0040 302 LYS A O   
35   C CB  . LYS A 6   ? 0.8383 1.4062 0.9450 -0.2398 0.0377  0.0047  302 LYS A CB  
36   C CG  . LYS A 6   ? 0.8992 1.5273 0.9947 -0.2997 0.0449  0.0106  302 LYS A CG  
37   C CD  . LYS A 6   ? 0.9240 1.6776 1.0503 -0.3019 0.0463  0.0077  302 LYS A CD  
38   C CE  . LYS A 6   ? 1.0217 1.8439 1.1350 -0.3709 0.0529  0.0139  302 LYS A CE  
39   N NZ  . LYS A 6   ? 1.0959 1.9604 1.1950 -0.3880 0.0639  0.0223  302 LYS A NZ  
40   N N   . VAL A 7   ? 0.7348 1.2278 0.8757 -0.1433 0.0170  -0.0122 303 VAL A N   
41   C CA  . VAL A 7   ? 0.7128 1.1608 0.8541 -0.0963 0.0110  -0.0167 303 VAL A CA  
42   C C   . VAL A 7   ? 0.6707 1.1854 0.8157 -0.0577 0.0153  -0.0184 303 VAL A C   
43   O O   . VAL A 7   ? 0.6580 1.2598 0.8172 -0.0537 0.0186  -0.0192 303 VAL A O   
44   C CB  . VAL A 7   ? 0.7811 1.1942 0.9313 -0.0867 0.0021  -0.0221 303 VAL A CB  
45   C CG1 . VAL A 7   ? 0.8586 1.2386 1.0050 -0.1278 0.0003  -0.0208 303 VAL A CG1 
46   C CG2 . VAL A 7   ? 0.7349 1.2162 0.9010 -0.0630 0.0010  -0.0264 303 VAL A CG2 
47   N N   . LYS A 8   ? 0.6628 1.1399 0.7909 -0.0290 0.0154  -0.0187 304 LYS A N   
48   C CA  . LYS A 8   ? 0.6435 1.1697 0.7632 0.0122  0.0201  -0.0206 304 LYS A CA  
49   C C   . LYS A 8   ? 0.5755 1.0499 0.6786 0.0569  0.0123  -0.0271 304 LYS A C   
50   O O   . LYS A 8   ? 0.5990 0.9918 0.6941 0.0532  0.0042  -0.0289 304 LYS A O   
51   C CB  . LYS A 8   ? 0.6659 1.1848 0.7681 0.0129  0.0265  -0.0167 304 LYS A CB  
52   C CG  . LYS A 8   ? 0.7106 1.2964 0.8021 0.0537  0.0339  -0.0181 304 LYS A CG  
53   C CD  . LYS A 8   ? 0.7413 1.3152 0.8130 0.0547  0.0403  -0.0145 304 LYS A CD  
54   C CE  . LYS A 8   ? 0.8036 1.4246 0.8547 0.1071  0.0464  -0.0177 304 LYS A CE  
55   N NZ  . LYS A 8   ? 0.8669 1.4877 0.8986 0.1080  0.0539  -0.0141 304 LYS A NZ  
56   N N   . ASN A 9   ? 0.5646 1.0873 0.6575 0.0994  0.0149  -0.0303 305 ASN A N   
57   C CA  . ASN A 9   ? 0.6661 1.1290 0.7240 0.1462  0.0093  -0.0359 305 ASN A CA  
58   C C   . ASN A 9   ? 0.7851 1.2447 0.8126 0.1735  0.0150  -0.0362 305 ASN A C   
59   O O   . ASN A 9   ? 0.7735 1.3162 0.8098 0.1773  0.0248  -0.0331 305 ASN A O   
60   C CB  . ASN A 9   ? 0.7528 1.2574 0.8065 0.1833  0.0078  -0.0394 305 ASN A CB  
61   C CG  . ASN A 9   ? 0.8624 1.2883 0.8657 0.2309  0.0018  -0.0449 305 ASN A CG  
62   O OD1 . ASN A 9   ? 0.9370 1.3357 0.9015 0.2620  0.0043  -0.0469 305 ASN A OD1 
63   N ND2 . ASN A 9   ? 0.7950 1.1768 0.7922 0.2347  -0.0063 -0.0473 305 ASN A ND2 
64   N N   . TRP A 10  ? 0.8490 1.2154 0.8393 0.1887  0.0088  -0.0397 306 TRP A N   
65   C CA  . TRP A 10  ? 0.9678 1.3168 0.9220 0.2137  0.0130  -0.0409 306 TRP A CA  
66   C C   . TRP A 10  ? 1.0665 1.3811 0.9657 0.2720  0.0113  -0.0476 306 TRP A C   
67   O O   . TRP A 10  ? 1.1282 1.4239 0.9882 0.2993  0.0149  -0.0498 306 TRP A O   
68   C CB  . TRP A 10  ? 0.9127 1.1815 0.8564 0.1860  0.0073  -0.0400 306 TRP A CB  
69   C CG  . TRP A 10  ? 0.8048 1.0972 0.7882 0.1370  0.0099  -0.0330 306 TRP A CG  
70   C CD1 . TRP A 10  ? 0.7003 0.9754 0.7122 0.1018  0.0046  -0.0305 306 TRP A CD1 
71   C CD2 . TRP A 10  ? 0.8027 1.1332 0.7931 0.1197  0.0186  -0.0273 306 TRP A CD2 
72   N NE1 . TRP A 10  ? 0.6716 0.9637 0.7021 0.0656  0.0092  -0.0239 306 TRP A NE1 
73   C CE2 . TRP A 10  ? 0.7608 1.0858 0.7785 0.0736  0.0177  -0.0214 306 TRP A CE2 
74   C CE3 . TRP A 10  ? 0.8947 1.2596 0.8656 0.1398  0.0274  -0.0264 306 TRP A CE3 
75   C CZ2 . TRP A 10  ? 0.7321 1.0785 0.7544 0.0451  0.0250  -0.0141 306 TRP A CZ2 
76   C CZ3 . TRP A 10  ? 0.8867 1.2817 0.8688 0.1096  0.0349  -0.0191 306 TRP A CZ3 
77   C CH2 . TRP A 10  ? 0.8350 1.2180 0.8408 0.0617  0.0336  -0.0127 306 TRP A CH2 
78   N N   . GLU A 11  ? 1.0956 1.3931 0.9835 0.2928  0.0059  -0.0508 307 GLU A N   
79   C CA  . GLU A 11  ? 1.1122 1.3827 0.9400 0.3544  0.0057  -0.0562 307 GLU A CA  
80   C C   . GLU A 11  ? 1.1312 1.5207 0.9721 0.3926  0.0160  -0.0548 307 GLU A C   
81   O O   . GLU A 11  ? 1.2587 1.6531 1.0509 0.4483  0.0209  -0.0580 307 GLU A O   
82   C CB  . GLU A 11  ? 1.1032 1.2969 0.9040 0.3619  -0.0047 -0.0595 307 GLU A CB  
83   C CG  . GLU A 11  ? 1.1126 1.2049 0.8242 0.4099  -0.0093 -0.0657 307 GLU A CG  
84   C CD  . GLU A 11  ? 1.2157 1.2775 0.8967 0.4396  -0.0147 -0.0675 307 GLU A CD  
85   O OE1 . GLU A 11  ? 1.2739 1.3336 0.8993 0.5022  -0.0116 -0.0705 307 GLU A OE1 
86   O OE2 . GLU A 11  ? 1.0711 1.1116 0.7796 0.4044  -0.0216 -0.0657 307 GLU A OE2 
87   N N   . THR A 12  ? 0.9835 1.4722 0.8868 0.3625  0.0194  -0.0500 308 THR A N   
88   C CA  . THR A 12  ? 0.9742 1.5942 0.8982 0.3903  0.0278  -0.0479 308 THR A CA  
89   C C   . THR A 12  ? 0.9444 1.6767 0.9181 0.3515  0.0382  -0.0415 308 THR A C   
90   O O   . THR A 12  ? 0.9446 1.8028 0.9388 0.3678  0.0458  -0.0389 308 THR A O   
91   C CB  . THR A 12  ? 0.9568 1.6095 0.9054 0.3875  0.0221  -0.0478 308 THR A CB  
92   O OG1 . THR A 12  ? 0.8307 1.4767 0.8294 0.3194  0.0181  -0.0447 308 THR A OG1 
93   C CG2 . THR A 12  ? 0.9730 1.5205 0.8657 0.4289  0.0128  -0.0532 308 THR A CG2 
94   N N   . ASP A 13  ? 0.9576 1.6510 0.9481 0.3001  0.0387  -0.0382 309 ASP A N   
95   C CA  . ASP A 13  ? 0.9768 1.7546 1.0092 0.2499  0.0472  -0.0310 309 ASP A CA  
96   C C   . ASP A 13  ? 0.9533 1.8148 1.0323 0.2110  0.0471  -0.0275 309 ASP A C   
97   O O   . ASP A 13  ? 0.9822 1.9274 1.0894 0.1691  0.0548  -0.0213 309 ASP A O   
98   C CB  . ASP A 13  ? 1.1159 1.9836 1.1377 0.2778  0.0600  -0.0286 309 ASP A CB  
99   C CG  . ASP A 13  ? 1.2658 2.0542 1.2492 0.2911  0.0617  -0.0300 309 ASP A CG  
100  O OD1 . ASP A 13  ? 1.2817 2.0015 1.2719 0.2456  0.0583  -0.0274 309 ASP A OD1 
101  O OD2 . ASP A 13  ? 1.3327 2.1265 1.2748 0.3496  0.0661  -0.0340 309 ASP A OD2 
102  N N   . VAL A 14  ? 0.8914 1.7295 0.9748 0.2202  0.0384  -0.0311 310 VAL A N   
103  C CA  . VAL A 14  ? 0.8347 1.7437 0.9584 0.1813  0.0370  -0.0288 310 VAL A CA  
104  C C   . VAL A 14  ? 0.8366 1.6924 0.9801 0.1116  0.0345  -0.0253 310 VAL A C   
105  O O   . VAL A 14  ? 0.9144 1.6585 1.0431 0.1029  0.0288  -0.0265 310 VAL A O   
106  C CB  . VAL A 14  ? 0.7505 1.6387 0.8683 0.2129  0.0280  -0.0337 310 VAL A CB  
107  C CG1 . VAL A 14  ? 0.7902 1.7248 0.9464 0.1654  0.0243  -0.0322 310 VAL A CG1 
108  C CG2 . VAL A 14  ? 0.6773 1.6369 0.7730 0.2828  0.0314  -0.0359 310 VAL A CG2 
109  N N   . VAL A 15  ? 0.6883 1.6242 0.8599 0.0616  0.0387  -0.0206 311 VAL A N   
110  C CA  . VAL A 15  ? 0.6967 1.5797 0.8760 -0.0034 0.0370  -0.0170 311 VAL A CA  
111  C C   . VAL A 15  ? 0.7984 1.7239 0.9994 -0.0392 0.0328  -0.0176 311 VAL A C   
112  O O   . VAL A 15  ? 0.8752 1.9169 1.0933 -0.0366 0.0358  -0.0171 311 VAL A O   
113  C CB  . VAL A 15  ? 0.6435 1.5597 0.8192 -0.0418 0.0471  -0.0097 311 VAL A CB  
114  C CG1 . VAL A 15  ? 0.5732 1.4127 0.7426 -0.1032 0.0447  -0.0059 311 VAL A CG1 
115  C CG2 . VAL A 15  ? 0.7026 1.5853 0.8558 -0.0028 0.0513  -0.0096 311 VAL A CG2 
116  N N   . LEU A 16  ? 0.7792 1.6143 0.9777 -0.0708 0.0257  -0.0188 312 LEU A N   
117  C CA  . LEU A 16  ? 0.7416 1.5963 0.9533 -0.1079 0.0209  -0.0202 312 LEU A CA  
118  C C   . LEU A 16  ? 0.6845 1.4717 0.8817 -0.1685 0.0212  -0.0166 312 LEU A C   
119  O O   . LEU A 16  ? 0.6023 1.3022 0.7810 -0.1696 0.0217  -0.0144 312 LEU A O   
120  C CB  . LEU A 16  ? 0.7279 1.5308 0.9426 -0.0759 0.0111  -0.0266 312 LEU A CB  
121  C CG  . LEU A 16  ? 0.7823 1.6430 1.0006 -0.0152 0.0098  -0.0300 312 LEU A CG  
122  C CD1 . LEU A 16  ? 0.7872 1.5600 0.9945 0.0179  0.0008  -0.0350 312 LEU A CD1 
123  C CD2 . LEU A 16  ? 0.8184 1.8077 1.0580 -0.0242 0.0110  -0.0298 312 LEU A CD2 
124  N N   . THR A 17  ? 0.6998 1.5259 0.8996 -0.2182 0.0205  -0.0160 313 THR A N   
125  C CA  . THR A 17  ? 0.7602 1.5154 0.9332 -0.2773 0.0206  -0.0129 313 THR A CA  
126  C C   . THR A 17  ? 0.8461 1.5303 1.0133 -0.2862 0.0115  -0.0184 313 THR A C   
127  O O   . THR A 17  ? 0.8348 1.5731 1.0201 -0.2831 0.0068  -0.0229 313 THR A O   
128  C CB  . THR A 17  ? 0.7855 1.6158 0.9471 -0.3352 0.0267  -0.0077 313 THR A CB  
129  O OG1 . THR A 17  ? 0.7970 1.6952 0.9615 -0.3237 0.0357  -0.0022 313 THR A OG1 
130  C CG2 . THR A 17  ? 0.7816 1.5096 0.8972 -0.3922 0.0264  -0.0044 313 THR A CG2 
131  N N   . ASP A 18  ? 0.8667 1.4342 1.0066 -0.2955 0.0091  -0.0177 314 ASP A N   
132  C CA  . ASP A 18  ? 0.8102 1.2992 0.9408 -0.2948 0.0012  -0.0227 314 ASP A CA  
133  C C   . ASP A 18  ? 0.8265 1.2601 0.9153 -0.3531 0.0017  -0.0209 314 ASP A C   
134  O O   . ASP A 18  ? 0.8070 1.1648 0.8604 -0.3680 0.0048  -0.0161 314 ASP A O   
135  C CB  . ASP A 18  ? 0.8011 1.2026 0.9290 -0.2530 -0.0022 -0.0235 314 ASP A CB  
136  C CG  . ASP A 18  ? 0.7560 1.0997 0.8835 -0.2406 -0.0100 -0.0290 314 ASP A CG  
137  O OD1 . ASP A 18  ? 0.7924 1.0807 0.8916 -0.2718 -0.0115 -0.0296 314 ASP A OD1 
138  O OD2 . ASP A 18  ? 0.5889 0.9390 0.7388 -0.1999 -0.0143 -0.0326 314 ASP A OD2 
139  N N   . THR A 19  ? 0.8657 1.3334 0.9522 -0.3860 -0.0016 -0.0248 315 THR A N   
140  C CA  . THR A 19  ? 0.9050 1.2945 0.9401 -0.4350 -0.0032 -0.0251 315 THR A CA  
141  C C   . THR A 19  ? 0.9302 1.2500 0.9584 -0.4205 -0.0111 -0.0324 315 THR A C   
142  O O   . THR A 19  ? 0.9759 1.2040 0.9521 -0.4476 -0.0126 -0.0332 315 THR A O   
143  C CB  . THR A 19  ? 0.8915 1.3372 0.9047 -0.4692 -0.0011 -0.0232 315 THR A CB  
144  O OG1 . THR A 19  ? 0.8906 1.4304 0.9447 -0.4466 -0.0047 -0.0277 315 THR A OG1 
145  C CG2 . THR A 19  ? 0.9132 1.4106 0.9176 -0.4876 0.0070  -0.0154 315 THR A CG2 
146  N N   . LEU A 20  ? 0.8423 1.1954 0.9136 -0.3720 -0.0156 -0.0370 316 LEU A N   
147  C CA  . LEU A 20  ? 0.7876 1.0844 0.8550 -0.3548 -0.0225 -0.0433 316 LEU A CA  
148  C C   . LEU A 20  ? 0.8789 1.0567 0.9114 -0.3407 -0.0227 -0.0422 316 LEU A C   
149  O O   . LEU A 20  ? 0.9377 1.0517 0.9450 -0.3428 -0.0267 -0.0467 316 LEU A O   
150  C CB  . LEU A 20  ? 0.6281 0.9785 0.7436 -0.3039 -0.0263 -0.0467 316 LEU A CB  
151  C CG  . LEU A 20  ? 0.6396 0.9509 0.7569 -0.2858 -0.0330 -0.0529 316 LEU A CG  
152  C CD1 . LEU A 20  ? 0.5262 0.8510 0.6246 -0.3285 -0.0364 -0.0577 316 LEU A CD1 
153  C CD2 . LEU A 20  ? 0.6196 0.9777 0.7760 -0.2378 -0.0361 -0.0546 316 LEU A CD2 
154  N N   . HIS A 21  ? 0.7843 0.9352 0.8133 -0.3235 -0.0186 -0.0363 317 HIS A N   
155  C CA  . HIS A 21  ? 0.7623 0.8140 0.7613 -0.3031 -0.0192 -0.0345 317 HIS A CA  
156  C C   . HIS A 21  ? 0.8534 0.8168 0.7856 -0.3393 -0.0184 -0.0339 317 HIS A C   
157  O O   . HIS A 21  ? 0.9162 0.7936 0.8157 -0.3185 -0.0198 -0.0336 317 HIS A O   
158  C CB  . HIS A 21  ? 0.8765 0.9261 0.8825 -0.2825 -0.0153 -0.0279 317 HIS A CB  
159  C CG  . HIS A 21  ? 0.9190 0.9686 0.8944 -0.3208 -0.0088 -0.0216 317 HIS A CG  
160  N ND1 . HIS A 21  ? 0.9311 1.0718 0.9284 -0.3433 -0.0045 -0.0197 317 HIS A ND1 
161  C CD2 . HIS A 21  ? 1.0370 1.0067 0.9569 -0.3411 -0.0057 -0.0161 317 HIS A CD2 
162  C CE1 . HIS A 21  ? 1.0116 1.1321 0.9711 -0.3800 0.0014  -0.0132 317 HIS A CE1 
163  N NE2 . HIS A 21  ? 1.0686 1.0797 0.9781 -0.3797 0.0007  -0.0108 317 HIS A NE2 
164  N N   . LEU A 22  ? 0.9169 0.8997 0.8229 -0.3929 -0.0160 -0.0333 318 LEU A N   
165  C CA  . LEU A 22  ? 1.1365 1.0247 0.9653 -0.4347 -0.0156 -0.0332 318 LEU A CA  
166  C C   . LEU A 22  ? 1.2209 1.0575 1.0282 -0.4289 -0.0215 -0.0415 318 LEU A C   
167  O O   . LEU A 22  ? 1.2621 0.9875 1.0000 -0.4343 -0.0220 -0.0422 318 LEU A O   
168  C CB  . LEU A 22  ? 1.1737 1.1105 0.9825 -0.4861 -0.0116 -0.0295 318 LEU A CB  
169  C CG  . LEU A 22  ? 1.1633 1.1475 0.9795 -0.5007 -0.0045 -0.0209 318 LEU A CG  
170  C CD1 . LEU A 22  ? 1.0891 1.1389 0.8893 -0.5420 -0.0012 -0.0181 318 LEU A CD1 
171  C CD2 . LEU A 22  ? 1.1959 1.0721 0.9557 -0.5001 -0.0010 -0.0143 318 LEU A CD2 
172  N N   . LYS A 23  ? 1.1305 1.0429 0.9907 -0.4153 -0.0259 -0.0476 319 LYS A N   
173  C CA  . LYS A 23  ? 1.1668 1.0413 1.0148 -0.4044 -0.0314 -0.0556 319 LYS A CA  
174  C C   . LYS A 23  ? 1.2098 1.0281 1.0623 -0.3474 -0.0324 -0.0558 319 LYS A C   
175  O O   . LYS A 23  ? 1.2939 1.0650 1.1249 -0.3350 -0.0357 -0.0616 319 LYS A O   
176  C CB  . LYS A 23  ? 1.0274 1.0054 0.9317 -0.4041 -0.0357 -0.0610 319 LYS A CB  
177  C CG  . LYS A 23  ? 1.0738 1.1222 0.9746 -0.4465 -0.0346 -0.0597 319 LYS A CG  
178  C CD  . LYS A 23  ? 1.2708 1.2596 1.1102 -0.4751 -0.0360 -0.0626 319 LYS A CD  
179  C CE  . LYS A 23  ? 1.3654 1.3657 1.2224 -0.4605 -0.0428 -0.0713 319 LYS A CE  
180  N NZ  . LYS A 23  ? 1.3466 1.4699 1.2603 -0.4577 -0.0454 -0.0725 319 LYS A NZ  
181  N N   . SER A 24  ? 1.1896 1.0182 1.0693 -0.3137 -0.0299 -0.0498 320 SER A N   
182  C CA  . SER A 24  ? 1.1915 0.9787 1.0757 -0.2636 -0.0311 -0.0492 320 SER A CA  
183  C C   . SER A 24  ? 1.2666 0.9422 1.0759 -0.2608 -0.0306 -0.0496 320 SER A C   
184  O O   . SER A 24  ? 1.3297 0.9426 1.0767 -0.2941 -0.0280 -0.0474 320 SER A O   
185  C CB  . SER A 24  ? 1.1844 0.9958 1.0988 -0.2368 -0.0289 -0.0423 320 SER A CB  
186  O OG  . SER A 24  ? 1.2167 0.9819 1.1217 -0.1962 -0.0302 -0.0407 320 SER A OG  
187  N N   . THR A 25  ? 1.2767 0.9267 1.0876 -0.2195 -0.0327 -0.0522 321 THR A N   
188  C CA  . THR A 25  ? 1.4852 1.0341 1.2232 -0.2072 -0.0325 -0.0543 321 THR A CA  
189  C C   . THR A 25  ? 1.4976 1.0317 1.2416 -0.1512 -0.0323 -0.0504 321 THR A C   
190  O O   . THR A 25  ? 1.5680 1.0249 1.2524 -0.1337 -0.0303 -0.0464 321 THR A O   
191  C CB  . THR A 25  ? 1.4668 1.0055 1.1911 -0.2182 -0.0356 -0.0635 321 THR A CB  
192  O OG1 . THR A 25  ? 1.5309 0.9820 1.1944 -0.1874 -0.0353 -0.0662 321 THR A OG1 
193  C CG2 . THR A 25  ? 1.3545 0.9909 1.1594 -0.2030 -0.0387 -0.0668 321 THR A CG2 
194  N N   . LEU A 26  ? 1.3746 0.9843 1.1868 -0.1238 -0.0345 -0.0509 322 LEU A N   
195  C CA  . LEU A 26  ? 1.4117 1.0275 1.2367 -0.0758 -0.0350 -0.0471 322 LEU A CA  
196  C C   . LEU A 26  ? 1.4073 1.0308 1.2397 -0.0675 -0.0339 -0.0389 322 LEU A C   
197  O O   . LEU A 26  ? 1.3283 0.9551 1.1597 -0.0973 -0.0321 -0.0360 322 LEU A O   
198  C CB  . LEU A 26  ? 1.3890 1.0822 1.2792 -0.0592 -0.0378 -0.0495 322 LEU A CB  
199  C CG  . LEU A 26  ? 1.4478 1.1286 1.3258 -0.0405 -0.0386 -0.0552 322 LEU A CG  
200  C CD1 . LEU A 26  ? 1.3820 1.1296 1.3141 -0.0524 -0.0411 -0.0593 322 LEU A CD1 
201  C CD2 . LEU A 26  ? 1.4687 1.1524 1.3437 0.0061  -0.0382 -0.0514 322 LEU A CD2 
202  N N   . GLU A 27  ? 1.4055 1.0379 1.2450 -0.0267 -0.0350 -0.0348 323 GLU A N   
203  C CA  . GLU A 27  ? 1.3896 1.0279 1.2318 -0.0135 -0.0349 -0.0271 323 GLU A CA  
204  C C   . GLU A 27  ? 1.2685 0.9932 1.1807 -0.0035 -0.0383 -0.0254 323 GLU A C   
205  O O   . GLU A 27  ? 1.2662 1.0351 1.2136 0.0055  -0.0406 -0.0288 323 GLU A O   
206  C CB  . GLU A 27  ? 1.5013 1.0802 1.2862 0.0262  -0.0343 -0.0229 323 GLU A CB  
207  C CG  . GLU A 27  ? 1.6756 1.1490 1.3740 0.0189  -0.0312 -0.0250 323 GLU A CG  
208  C CD  . GLU A 27  ? 1.8385 1.2360 1.4646 0.0541  -0.0299 -0.0186 323 GLU A CD  
209  O OE1 . GLU A 27  ? 1.8298 1.2664 1.4788 0.0835  -0.0316 -0.0121 323 GLU A OE1 
210  O OE2 . GLU A 27  ? 1.9459 1.2407 1.4864 0.0524  -0.0275 -0.0200 323 GLU A OE2 
211  N N   . THR A 28  ? 1.0805 0.8235 1.0066 -0.0072 -0.0386 -0.0201 324 THR A N   
212  C CA  . THR A 28  ? 0.9485 0.7611 0.9305 -0.0070 -0.0419 -0.0191 324 THR A CA  
213  C C   . THR A 28  ? 0.8920 0.7320 0.8846 0.0233  -0.0458 -0.0144 324 THR A C   
214  O O   . THR A 28  ? 0.8351 0.7299 0.8682 0.0244  -0.0497 -0.0150 324 THR A O   
215  C CB  . THR A 28  ? 0.8738 0.6951 0.8636 -0.0302 -0.0400 -0.0169 324 THR A CB  
216  O OG1 . THR A 28  ? 0.8852 0.6628 0.8351 -0.0240 -0.0380 -0.0106 324 THR A OG1 
217  C CG2 . THR A 28  ? 0.7984 0.6176 0.7868 -0.0629 -0.0365 -0.0212 324 THR A CG2 
218  N N   . GLY A 29  ? 0.9573 0.7607 0.9099 0.0473  -0.0454 -0.0095 325 GLY A N   
219  C CA  . GLY A 29  ? 0.9467 0.7829 0.9066 0.0741  -0.0495 -0.0039 325 GLY A CA  
220  C C   . GLY A 29  ? 1.0213 0.8370 0.9630 0.0712  -0.0492 0.0019  325 GLY A C   
221  O O   . GLY A 29  ? 1.0898 0.9072 1.0133 0.0990  -0.0518 0.0077  325 GLY A O   
222  N N   . CYS A 30  ? 1.0013 0.8014 0.9456 0.0398  -0.0460 0.0007  326 CYS A N   
223  C CA  . CYS A 30  ? 1.0075 0.7913 0.9358 0.0332  -0.0448 0.0061  326 CYS A CA  
224  C C   . CYS A 30  ? 1.0447 0.7477 0.9066 0.0360  -0.0401 0.0104  326 CYS A C   
225  O O   . CYS A 30  ? 1.0491 0.7048 0.8800 0.0241  -0.0365 0.0073  326 CYS A O   
226  C CB  . CYS A 30  ? 0.9597 0.7691 0.9174 0.0005  -0.0424 0.0032  326 CYS A CB  
227  S SG  . CYS A 30  ? 0.8499 0.7330 0.8675 -0.0021 -0.0479 -0.0015 326 CYS A SG  
228  N N   . THR A 31  ? 0.9981 0.6802 0.8318 0.0511  -0.0407 0.0177  327 THR A N   
229  C CA  . THR A 31  ? 1.1458 0.7426 0.9081 0.0496  -0.0361 0.0233  327 THR A CA  
230  C C   . THR A 31  ? 1.1951 0.7929 0.9579 0.0220  -0.0328 0.0275  327 THR A C   
231  O O   . THR A 31  ? 1.2424 0.9048 1.0587 0.0092  -0.0343 0.0254  327 THR A O   
232  C CB  . THR A 31  ? 1.1875 0.7503 0.9034 0.0976  -0.0391 0.0294  327 THR A CB  
233  O OG1 . THR A 31  ? 1.1319 0.7412 0.8700 0.1134  -0.0436 0.0349  327 THR A OG1 
234  C CG2 . THR A 31  ? 1.0691 0.6593 0.7984 0.1296  -0.0424 0.0252  327 THR A CG2 
235  N N   . GLU A 32  ? 1.3436 0.8644 1.0398 0.0133  -0.0281 0.0338  328 GLU A N   
236  C CA  . GLU A 32  ? 1.4156 0.9387 1.1081 -0.0130 -0.0241 0.0388  328 GLU A CA  
237  C C   . GLU A 32  ? 1.3531 0.9215 1.0718 0.0124  -0.0290 0.0430  328 GLU A C   
238  O O   . GLU A 32  ? 1.2933 0.8892 1.0295 -0.0069 -0.0266 0.0450  328 GLU A O   
239  C CB  . GLU A 32  ? 1.6490 1.0726 1.2549 -0.0298 -0.0180 0.0459  328 GLU A CB  
240  C CG  . GLU A 32  ? 1.7952 1.1888 1.3796 -0.0796 -0.0119 0.0423  328 GLU A CG  
241  C CD  . GLU A 32  ? 1.9753 1.2821 1.4944 -0.0735 -0.0120 0.0401  328 GLU A CD  
242  O OE1 . GLU A 32  ? 2.1150 1.3259 1.5497 -0.0967 -0.0075 0.0449  328 GLU A OE1 
243  O OE2 . GLU A 32  ? 1.9584 1.2888 1.5051 -0.0464 -0.0164 0.0335  328 GLU A OE2 
244  N N   . HIS A 33  ? 1.2796 0.8638 1.0023 0.0545  -0.0360 0.0441  329 HIS A N   
245  C CA  . HIS A 33  ? 1.2587 0.8821 0.9956 0.0788  -0.0420 0.0488  329 HIS A CA  
246  C C   . HIS A 33  ? 1.1241 0.8334 0.9238 0.0934  -0.0502 0.0436  329 HIS A C   
247  O O   . HIS A 33  ? 1.1053 0.8525 0.9140 0.1154  -0.0570 0.0472  329 HIS A O   
248  C CB  . HIS A 33  ? 1.4448 1.0081 1.1139 0.1170  -0.0434 0.0578  329 HIS A CB  
249  C CG  . HIS A 33  ? 1.6258 1.0856 1.2171 0.1016  -0.0355 0.0630  329 HIS A CG  
250  N ND1 . HIS A 33  ? 1.6894 1.0781 1.2306 0.1032  -0.0321 0.0611  329 HIS A ND1 
251  C CD2 . HIS A 33  ? 1.6606 1.0732 1.2110 0.0792  -0.0301 0.0699  329 HIS A CD2 
252  C CE1 . HIS A 33  ? 1.7754 1.0726 1.2439 0.0801  -0.0256 0.0667  329 HIS A CE1 
253  N NE2 . HIS A 33  ? 1.7692 1.0818 1.2434 0.0646  -0.0239 0.0726  329 HIS A NE2 
254  N N   . ILE A 34  ? 1.0169 0.7577 0.8563 0.0791  -0.0500 0.0357  330 ILE A N   
255  C CA  . ILE A 34  ? 0.9043 0.7208 0.7984 0.0836  -0.0571 0.0309  330 ILE A CA  
256  C C   . ILE A 34  ? 0.9203 0.7543 0.8497 0.0571  -0.0544 0.0226  330 ILE A C   
257  O O   . ILE A 34  ? 1.0136 0.8118 0.9271 0.0494  -0.0494 0.0201  330 ILE A O   
258  C CB  . ILE A 34  ? 0.8922 0.7337 0.7819 0.1214  -0.0630 0.0332  330 ILE A CB  
259  C CG1 . ILE A 34  ? 0.8469 0.7710 0.7903 0.1168  -0.0704 0.0292  330 ILE A CG1 
260  C CG2 . ILE A 34  ? 1.0135 0.8138 0.8775 0.1337  -0.0587 0.0310  330 ILE A CG2 
261  C CD1 . ILE A 34  ? 0.8147 0.7908 0.7587 0.1489  -0.0781 0.0341  330 ILE A CD1 
262  N N   . CYS A 35  ? 0.8816 0.7664 0.8529 0.0433  -0.0581 0.0184  331 CYS A N   
263  C CA  . CYS A 35  ? 0.8409 0.7464 0.8442 0.0235  -0.0567 0.0111  331 CYS A CA  
264  C C   . CYS A 35  ? 0.8269 0.7798 0.8595 0.0306  -0.0638 0.0083  331 CYS A C   
265  O O   . CYS A 35  ? 0.7247 0.7103 0.7654 0.0357  -0.0705 0.0103  331 CYS A O   
266  C CB  . CYS A 35  ? 0.8032 0.7183 0.8189 0.0026  -0.0540 0.0086  331 CYS A CB  
267  S SG  . CYS A 35  ? 0.7247 0.6721 0.7759 -0.0118 -0.0548 0.0002  331 CYS A SG  
268  N N   . MET A 36  ? 0.9220 0.8792 0.9671 0.0282  -0.0625 0.0041  332 MET A N   
269  C CA  . MET A 36  ? 0.9559 0.9568 1.0250 0.0324  -0.0679 0.0022  332 MET A CA  
270  C C   . MET A 36  ? 0.8066 0.8212 0.9000 0.0112  -0.0681 -0.0039 332 MET A C   
271  O O   . MET A 36  ? 0.7236 0.7653 0.8329 0.0095  -0.0711 -0.0058 332 MET A O   
272  C CB  . MET A 36  ? 1.0860 1.0814 1.1443 0.0530  -0.0662 0.0029  332 MET A CB  
273  C CG  . MET A 36  ? 1.2277 1.1933 1.2486 0.0800  -0.0649 0.0087  332 MET A CG  
274  S SD  . MET A 36  ? 1.3078 1.3213 1.3275 0.1170  -0.0695 0.0124  332 MET A SD  
275  C CE  . MET A 36  ? 1.3664 1.3379 1.3349 0.1502  -0.0690 0.0203  332 MET A CE  
276  N N   . GLY A 37  ? 0.6763 0.6744 0.7694 -0.0031 -0.0648 -0.0064 333 GLY A N   
277  C CA  . GLY A 37  ? 0.7167 0.7219 0.8244 -0.0166 -0.0644 -0.0119 333 GLY A CA  
278  C C   . GLY A 37  ? 0.6972 0.7250 0.8144 -0.0224 -0.0713 -0.0135 333 GLY A C   
279  O O   . GLY A 37  ? 0.6197 0.6446 0.7406 -0.0303 -0.0712 -0.0176 333 GLY A O   
280  N N   . SER A 38  ? 0.6514 0.7016 0.7678 -0.0202 -0.0775 -0.0100 334 SER A N   
281  C CA  . SER A 38  ? 0.5277 0.5981 0.6462 -0.0345 -0.0845 -0.0111 334 SER A CA  
282  C C   . SER A 38  ? 0.5501 0.6625 0.6797 -0.0318 -0.0881 -0.0077 334 SER A C   
283  O O   . SER A 38  ? 0.6211 0.7590 0.7507 -0.0489 -0.0943 -0.0072 334 SER A O   
284  C CB  . SER A 38  ? 0.6602 0.7254 0.7625 -0.0439 -0.0899 -0.0108 334 SER A CB  
285  O OG  . SER A 38  ? 0.7249 0.8217 0.8264 -0.0411 -0.0956 -0.0060 334 SER A OG  
286  N N   . ILE A 39  ? 0.4328 0.5513 0.5666 -0.0113 -0.0840 -0.0055 335 ILE A N   
287  C CA  . ILE A 39  ? 0.5561 0.7154 0.7000 -0.0021 -0.0851 -0.0032 335 ILE A CA  
288  C C   . ILE A 39  ? 0.6317 0.7847 0.7850 -0.0124 -0.0823 -0.0074 335 ILE A C   
289  O O   . ILE A 39  ? 0.5622 0.6781 0.7132 -0.0096 -0.0767 -0.0112 335 ILE A O   
290  C CB  . ILE A 39  ? 0.5596 0.7133 0.6929 0.0294  -0.0811 -0.0002 335 ILE A CB  
291  C CG1 . ILE A 39  ? 0.6217 0.7721 0.7394 0.0424  -0.0835 0.0045  335 ILE A CG1 
292  C CG2 . ILE A 39  ? 0.5236 0.7264 0.6649 0.0447  -0.0818 0.0021  335 ILE A CG2 
293  C CD1 . ILE A 39  ? 0.6426 0.8517 0.7688 0.0351  -0.0922 0.0083  335 ILE A CD1 
294  N N   . MET A 40  ? 0.7078 0.9008 0.8699 -0.0258 -0.0862 -0.0062 336 MET A N   
295  C CA  . MET A 40  ? 0.7432 0.9281 0.9101 -0.0382 -0.0842 -0.0094 336 MET A CA  
296  C C   . MET A 40  ? 0.7739 0.9536 0.9461 -0.0177 -0.0778 -0.0112 336 MET A C   
297  O O   . MET A 40  ? 0.8226 0.9661 0.9932 -0.0189 -0.0739 -0.0157 336 MET A O   
298  C CB  . MET A 40  ? 0.8540 1.0834 1.0234 -0.0609 -0.0895 -0.0064 336 MET A CB  
299  C CG  . MET A 40  ? 1.0378 1.2451 1.2017 -0.0795 -0.0888 -0.0091 336 MET A CG  
300  S SD  . MET A 40  ? 1.1266 1.2947 1.2608 -0.1118 -0.0954 -0.0102 336 MET A SD  
301  C CE  . MET A 40  ? 1.1287 1.3565 1.2581 -0.1444 -0.1024 -0.0042 336 MET A CE  
302  N N   . LEU A 41  ? 0.8231 1.0403 0.9981 0.0027  -0.0769 -0.0078 337 LEU A N   
303  C CA  . LEU A 41  ? 0.9700 1.1809 1.1421 0.0240  -0.0712 -0.0098 337 LEU A CA  
304  C C   . LEU A 41  ? 1.2070 1.3955 1.3588 0.0557  -0.0683 -0.0084 337 LEU A C   
305  O O   . LEU A 41  ? 1.3102 1.5359 1.4566 0.0822  -0.0683 -0.0046 337 LEU A O   
306  C CB  . LEU A 41  ? 0.8744 1.1468 1.0583 0.0256  -0.0716 -0.0072 337 LEU A CB  
307  C CG  . LEU A 41  ? 0.8152 1.1318 1.0111 -0.0078 -0.0770 -0.0042 337 LEU A CG  
308  C CD1 . LEU A 41  ? 0.8049 1.2042 1.0116 -0.0024 -0.0774 0.0011  337 LEU A CD1 
309  C CD2 . LEU A 41  ? 0.7688 1.0486 0.9630 -0.0337 -0.0766 -0.0080 337 LEU A CD2 
310  N N   . PRO A 42  ? 1.3118 1.4407 1.4473 0.0549  -0.0657 -0.0110 338 PRO A N   
311  C CA  . PRO A 42  ? 1.3605 1.4553 1.4655 0.0816  -0.0632 -0.0087 338 PRO A CA  
312  C C   . PRO A 42  ? 1.3780 1.4395 1.4566 0.1040  -0.0580 -0.0116 338 PRO A C   
313  O O   . PRO A 42  ? 1.2702 1.3095 1.3506 0.0908  -0.0553 -0.0171 338 PRO A O   
314  C CB  . PRO A 42  ? 1.3681 1.4132 1.4636 0.0635  -0.0619 -0.0100 338 PRO A CB  
315  C CG  . PRO A 42  ? 1.3483 1.4058 1.4708 0.0329  -0.0635 -0.0138 338 PRO A CG  
316  C CD  . PRO A 42  ? 1.3189 1.4103 1.4582 0.0307  -0.0644 -0.0156 338 PRO A CD  
317  N N   . SER A 43  ? 1.3982 1.4554 1.4475 0.1406  -0.0570 -0.0079 339 SER A N   
318  C CA  . SER A 43  ? 1.4210 1.4359 1.4310 0.1693  -0.0521 -0.0106 339 SER A CA  
319  C C   . SER A 43  ? 1.4601 1.4398 1.4207 0.2096  -0.0512 -0.0058 339 SER A C   
320  O O   . SER A 43  ? 1.5261 1.4271 1.4320 0.2265  -0.0471 -0.0081 339 SER A O   
321  C CB  . SER A 43  ? 1.4120 1.4867 1.4410 0.1833  -0.0514 -0.0116 339 SER A CB  
322  O OG  . SER A 43  ? 1.4510 1.4838 1.4355 0.2178  -0.0466 -0.0144 339 SER A OG  
323  N N   . VAL A 52  ? 2.0289 1.7592 1.6576 0.4201  -0.0040 -0.0810 348 VAL A N   
324  C CA  . VAL A 52  ? 2.0646 1.7057 1.6449 0.3990  -0.0042 -0.0926 348 VAL A CA  
325  C C   . VAL A 52  ? 2.1834 1.6901 1.6897 0.3787  -0.0075 -0.0974 348 VAL A C   
326  O O   . VAL A 52  ? 2.3333 1.7901 1.7906 0.4090  -0.0068 -0.0933 348 VAL A O   
327  C CB  . VAL A 52  ? 2.0412 1.6712 1.5680 0.4533  0.0024  -0.0984 348 VAL A CB  
328  C CG1 . VAL A 52  ? 2.0975 1.6666 1.5382 0.5230  0.0067  -0.0974 348 VAL A CG1 
329  C CG2 . VAL A 52  ? 2.0584 1.6055 1.5406 0.4259  0.0013  -0.1109 348 VAL A CG2 
330  N N   . ALA A 53  ? 2.0903 1.5424 1.5872 0.3253  -0.0114 -0.1053 349 ALA A N   
331  C CA  . ALA A 53  ? 2.0542 1.3945 1.4912 0.2888  -0.0152 -0.1091 349 ALA A CA  
332  C C   . ALA A 53  ? 2.0890 1.3106 1.4273 0.2868  -0.0150 -0.1214 349 ALA A C   
333  O O   . ALA A 53  ? 2.1368 1.3790 1.4834 0.2842  -0.0145 -0.1284 349 ALA A O   
334  C CB  . ALA A 53  ? 1.9276 1.3126 1.4365 0.2203  -0.0210 -0.1074 349 ALA A CB  
335  N N   . THR A 54  ? 2.1133 1.2051 1.3527 0.2849  -0.0156 -0.1240 350 THR A N   
336  C CA  . THR A 54  ? 2.1247 1.1170 1.2701 0.2777  -0.0162 -0.1274 350 THR A CA  
337  C C   . THR A 54  ? 2.1265 1.0722 1.2602 0.1995  -0.0222 -0.1347 350 THR A C   
338  O O   . THR A 54  ? 2.0899 1.0751 1.2828 0.1522  -0.0261 -0.1376 350 THR A O   
339  C CB  . THR A 54  ? 2.1555 1.0670 1.2117 0.3071  -0.0148 -0.1159 350 THR A CB  
340  O OG1 . THR A 54  ? 2.1793 1.0134 1.1932 0.2492  -0.0186 -0.1133 350 THR A OG1 
341  C CG2 . THR A 54  ? 2.1198 1.0939 1.2087 0.3620  -0.0115 -0.1060 350 THR A CG2 
342  N N   . LYS A 55  ? 2.2157 1.0807 1.2694 0.1856  -0.0234 -0.1363 351 LYS A N   
343  C CA  . LYS A 55  ? 2.2433 1.0785 1.2848 0.1128  -0.0291 -0.1424 351 LYS A CA  
344  C C   . LYS A 55  ? 2.2732 1.0569 1.2805 0.0622  -0.0315 -0.1345 351 LYS A C   
345  O O   . LYS A 55  ? 2.1993 1.0052 1.2353 -0.0039 -0.0361 -0.1374 351 LYS A O   
346  C CB  . LYS A 55  ? 2.2975 1.0686 1.2644 0.1181  -0.0295 -0.1466 351 LYS A CB  
347  C CG  . LYS A 55  ? 2.3321 1.0934 1.2630 0.1977  -0.0238 -0.1439 351 LYS A CG  
348  C CD  . LYS A 55  ? 2.5096 1.1875 1.3492 0.2024  -0.0246 -0.1459 351 LYS A CD  
349  C CE  . LYS A 55  ? 2.5861 1.2573 1.3845 0.2846  -0.0192 -0.1412 351 LYS A CE  
350  N NZ  . LYS A 55  ? 2.7405 1.3025 1.4241 0.2938  -0.0204 -0.1396 351 LYS A NZ  
351  N N   . ASP A 56  ? 2.3596 1.0807 1.3039 0.0931  -0.0284 -0.1239 352 ASP A N   
352  C CA  . ASP A 56  ? 2.4330 1.1081 1.3434 0.0494  -0.0295 -0.1155 352 ASP A CA  
353  C C   . ASP A 56  ? 2.2661 1.0274 1.2740 0.0138  -0.0313 -0.1158 352 ASP A C   
354  O O   . ASP A 56  ? 2.2483 1.0229 1.2720 -0.0524 -0.0345 -0.1158 352 ASP A O   
355  C CB  . ASP A 56  ? 2.5495 1.1554 1.3838 0.1002  -0.0259 -0.1045 352 ASP A CB  
356  C CG  . ASP A 56  ? 2.6533 1.1937 1.4022 0.1556  -0.0239 -0.1038 352 ASP A CG  
357  O OD1 . ASP A 56  ? 2.7323 1.1898 1.3988 0.1295  -0.0257 -0.1048 352 ASP A OD1 
358  O OD2 . ASP A 56  ? 2.6330 1.2101 1.3968 0.2254  -0.0206 -0.1016 352 ASP A OD2 
359  N N   . GLN A 57  ? 2.1359 0.9633 1.2100 0.0585  -0.0292 -0.1154 353 GLN A N   
360  C CA  . GLN A 57  ? 2.0287 0.9347 1.1921 0.0301  -0.0312 -0.1155 353 GLN A CA  
361  C C   . GLN A 57  ? 1.9240 0.8950 1.1509 -0.0198 -0.0363 -0.1255 353 GLN A C   
362  O O   . GLN A 57  ? 1.8524 0.8813 1.1385 -0.0645 -0.0393 -0.1238 353 GLN A O   
363  C CB  . GLN A 57  ? 2.0367 1.0009 1.2533 0.0920  -0.0283 -0.1135 353 GLN A CB  
364  C CG  . GLN A 57  ? 2.2043 1.1288 1.3613 0.1621  -0.0235 -0.1064 353 GLN A CG  
365  C CD  . GLN A 57  ? 2.2382 1.2450 1.4500 0.2257  -0.0204 -0.1081 353 GLN A CD  
366  O OE1 . GLN A 57  ? 2.2339 1.3152 1.5058 0.2189  -0.0209 -0.1131 353 GLN A OE1 
367  N NE2 . GLN A 57  ? 2.2499 1.2766 1.4569 0.2811  -0.0172 -0.0983 353 GLN A NE2 
368  N N   . LEU A 58  ? 1.8437 0.8139 1.0598 -0.0121 -0.0373 -0.1345 354 LEU A N   
369  C CA  . LEU A 58  ? 1.7260 0.7884 1.0209 -0.0427 -0.0417 -0.1410 354 LEU A CA  
370  C C   . LEU A 58  ? 1.7415 0.8002 1.0284 -0.1189 -0.0477 -0.1447 354 LEU A C   
371  O O   . LEU A 58  ? 1.6445 0.8035 1.0134 -0.1498 -0.0517 -0.1449 354 LEU A O   
372  C CB  . LEU A 58  ? 1.7585 0.8263 1.0449 -0.0064 -0.0405 -0.1486 354 LEU A CB  
373  C CG  . LEU A 58  ? 1.5571 0.7590 0.9528 -0.0029 -0.0415 -0.1469 354 LEU A CG  
374  C CD1 . LEU A 58  ? 1.3769 0.6712 0.8560 0.0285  -0.0381 -0.1348 354 LEU A CD1 
375  C CD2 . LEU A 58  ? 1.4692 0.6606 0.8391 0.0319  -0.0394 -0.1548 354 LEU A CD2 
376  N N   . PHE A 59  ? 1.8238 0.8082 1.0334 -0.1447 -0.0467 -0.1393 355 PHE A N   
377  C CA  . PHE A 59  ? 1.9538 0.9648 1.1676 -0.2140 -0.0512 -0.1395 355 PHE A CA  
378  C C   . PHE A 59  ? 1.9733 1.0423 1.2339 -0.2579 -0.0519 -0.1318 355 PHE A C   
379  O O   . PHE A 59  ? 1.9771 1.1348 1.2990 -0.2987 -0.0563 -0.1340 355 PHE A O   
380  C CB  . PHE A 59  ? 2.1920 1.1082 1.3039 -0.2352 -0.0505 -0.1367 355 PHE A CB  
381  C CG  . PHE A 59  ? 2.3080 1.2638 1.4270 -0.3034 -0.0552 -0.1377 355 PHE A CG  
382  C CD1 . PHE A 59  ? 2.3102 1.3282 1.4729 -0.3153 -0.0603 -0.1473 355 PHE A CD1 
383  C CD2 . PHE A 59  ? 2.3885 1.3290 1.4729 -0.3547 -0.0543 -0.1287 355 PHE A CD2 
384  C CE1 . PHE A 59  ? 2.3290 1.3962 1.5022 -0.3742 -0.0648 -0.1474 355 PHE A CE1 
385  C CE2 . PHE A 59  ? 2.4251 1.4156 1.5184 -0.4155 -0.0580 -0.1289 355 PHE A CE2 
386  C CZ  . PHE A 59  ? 2.3891 1.4451 1.5282 -0.4239 -0.0634 -0.1380 355 PHE A CZ  
387  N N   . PRO A 60  ? 1.9566 0.9842 1.1893 -0.2506 -0.0477 -0.1223 356 PRO A N   
388  C CA  . PRO A 60  ? 1.8536 0.9469 1.1371 -0.2904 -0.0478 -0.1154 356 PRO A CA  
389  C C   . PRO A 60  ? 1.6266 0.8348 1.0166 -0.2913 -0.0514 -0.1196 356 PRO A C   
390  O O   . PRO A 60  ? 1.5014 0.7934 0.9421 -0.3342 -0.0537 -0.1173 356 PRO A O   
391  C CB  . PRO A 60  ? 1.9177 0.9490 1.1629 -0.2615 -0.0427 -0.1064 356 PRO A CB  
392  C CG  . PRO A 60  ? 1.9969 0.9600 1.1984 -0.1957 -0.0405 -0.1094 356 PRO A CG  
393  C CD  . PRO A 60  ? 2.0120 0.9433 1.1717 -0.2019 -0.0426 -0.1168 356 PRO A CD  
394  N N   . LEU A 61  ? 1.5329 0.7485 0.9528 -0.2424 -0.0520 -0.1256 357 LEU A N   
395  C CA  . LEU A 61  ? 1.3323 0.6817 0.8662 -0.2279 -0.0529 -0.1216 357 LEU A CA  
396  C C   . LEU A 61  ? 1.3483 0.7626 0.9167 -0.2568 -0.0585 -0.1288 357 LEU A C   
397  O O   . LEU A 61  ? 1.3511 0.8696 0.9959 -0.2721 -0.0608 -0.1256 357 LEU A O   
398  C CB  . LEU A 61  ? 1.2330 0.6028 0.8005 -0.1607 -0.0490 -0.1179 357 LEU A CB  
399  C CG  . LEU A 61  ? 1.3782 0.6805 0.9014 -0.1221 -0.0440 -0.1118 357 LEU A CG  
400  C CD1 . LEU A 61  ? 1.2486 0.6090 0.8256 -0.0624 -0.0409 -0.1066 357 LEU A CD1 
401  C CD2 . LEU A 61  ? 1.4728 0.7709 0.9965 -0.1501 -0.0430 -0.1040 357 LEU A CD2 
402  N N   . ALA A 62  ? 1.2996 0.6526 0.8084 -0.2617 -0.0610 -0.1386 358 ALA A N   
403  C CA  . ALA A 62  ? 1.3037 0.7142 0.8364 -0.2946 -0.0674 -0.1458 358 ALA A CA  
404  C C   . ALA A 62  ? 1.3521 0.8010 0.8856 -0.3539 -0.0695 -0.1413 358 ALA A C   
405  O O   . ALA A 62  ? 1.2157 0.7698 0.8141 -0.3759 -0.0736 -0.1408 358 ALA A O   
406  C CB  . ALA A 62  ? 1.3193 0.6521 0.7829 -0.2851 -0.0690 -0.1567 358 ALA A CB  
407  N N   . LYS A 63  ? 1.5023 0.8765 0.9657 -0.3728 -0.0652 -0.1349 359 LYS A N   
408  C CA  . LYS A 63  ? 1.5797 0.9895 1.0353 -0.4262 -0.0647 -0.1276 359 LYS A CA  
409  C C   . LYS A 63  ? 1.5432 1.0556 1.0761 -0.4374 -0.0641 -0.1210 359 LYS A C   
410  O O   . LYS A 63  ? 1.5730 1.1864 1.1550 -0.4642 -0.0668 -0.1197 359 LYS A O   
411  C CB  . LYS A 63  ? 1.7089 1.0071 1.0674 -0.4393 -0.0595 -0.1209 359 LYS A CB  
412  C CG  . LYS A 63  ? 1.7625 1.0866 1.0984 -0.4975 -0.0581 -0.1130 359 LYS A CG  
413  C CD  . LYS A 63  ? 1.8416 1.0461 1.0737 -0.5085 -0.0532 -0.1059 359 LYS A CD  
414  C CE  . LYS A 63  ? 1.8523 1.0597 1.0338 -0.5724 -0.0525 -0.1004 359 LYS A CE  
415  N NZ  . LYS A 63  ? 1.7351 1.0753 0.9919 -0.6075 -0.0527 -0.0964 359 LYS A NZ  
416  N N   . GLU A 64  ? 1.4062 0.8939 0.9467 -0.4142 -0.0602 -0.1163 360 GLU A N   
417  C CA  . GLU A 64  ? 1.4106 0.9878 1.0234 -0.4163 -0.0593 -0.1105 360 GLU A CA  
418  C C   . GLU A 64  ? 1.2718 0.9656 0.9697 -0.4099 -0.0647 -0.1147 360 GLU A C   
419  O O   . GLU A 64  ? 1.2357 1.0267 0.9781 -0.4320 -0.0652 -0.1103 360 GLU A O   
420  C CB  . GLU A 64  ? 1.4540 0.9769 1.0628 -0.3790 -0.0559 -0.1081 360 GLU A CB  
421  C CG  . GLU A 64  ? 1.5117 1.0878 1.1641 -0.3846 -0.0530 -0.0997 360 GLU A CG  
422  C CD  . GLU A 64  ? 1.5512 1.0970 1.2172 -0.3318 -0.0494 -0.0952 360 GLU A CD  
423  O OE1 . GLU A 64  ? 1.6152 1.0600 1.2174 -0.3067 -0.0474 -0.0962 360 GLU A OE1 
424  O OE2 . GLU A 64  ? 1.4770 1.1059 1.2170 -0.3092 -0.0481 -0.0894 360 GLU A OE2 
425  N N   . PHE A 65  ? 1.1480 0.8356 0.8660 -0.3749 -0.0680 -0.1221 361 PHE A N   
426  C CA  . PHE A 65  ? 1.0983 0.8955 0.8955 -0.3557 -0.0711 -0.1218 361 PHE A CA  
427  C C   . PHE A 65  ? 1.1176 0.9697 0.9146 -0.3958 -0.0775 -0.1273 361 PHE A C   
428  O O   . PHE A 65  ? 1.0707 1.0292 0.9239 -0.4012 -0.0793 -0.1234 361 PHE A O   
429  C CB  . PHE A 65  ? 1.1295 0.9114 0.9450 -0.3009 -0.0699 -0.1229 361 PHE A CB  
430  C CG  . PHE A 65  ? 1.0369 0.9095 0.9140 -0.2849 -0.0738 -0.1237 361 PHE A CG  
431  C CD1 . PHE A 65  ? 0.9605 0.9118 0.9037 -0.2624 -0.0729 -0.1163 361 PHE A CD1 
432  C CD2 . PHE A 65  ? 1.1069 0.9782 0.9679 -0.2914 -0.0786 -0.1317 361 PHE A CD2 
433  C CE1 . PHE A 65  ? 0.9364 0.9583 0.9243 -0.2453 -0.0766 -0.1165 361 PHE A CE1 
434  C CE2 . PHE A 65  ? 1.0145 0.9641 0.9262 -0.2751 -0.0824 -0.1317 361 PHE A CE2 
435  C CZ  . PHE A 65  ? 0.9811 1.0034 0.9543 -0.2513 -0.0813 -0.1237 361 PHE A CZ  
436  N N   . LEU A 66  ? 1.1324 0.9184 0.8679 -0.4109 -0.0784 -0.1322 362 LEU A N   
437  C CA  . LEU A 66  ? 1.1269 0.9683 0.8636 -0.4392 -0.0824 -0.1335 362 LEU A CA  
438  C C   . LEU A 66  ? 1.1730 1.0801 0.9189 -0.4754 -0.0793 -0.1242 362 LEU A C   
439  O O   . LEU A 66  ? 1.0981 1.0979 0.8757 -0.4899 -0.0822 -0.1231 362 LEU A O   
440  C CB  . LEU A 66  ? 1.2697 1.0157 0.9281 -0.4518 -0.0831 -0.1397 362 LEU A CB  
441  C CG  . LEU A 66  ? 1.2848 0.9778 0.9269 -0.4187 -0.0863 -0.1505 362 LEU A CG  
442  C CD1 . LEU A 66  ? 1.4253 1.0294 0.9844 -0.4353 -0.0861 -0.1547 362 LEU A CD1 
443  C CD2 . LEU A 66  ? 1.1809 0.9713 0.8894 -0.4059 -0.0930 -0.1552 362 LEU A CD2 
444  N N   . ASP A 67  ? 1.2796 1.1415 0.9950 -0.4885 -0.0732 -0.1174 363 ASP A N   
445  C CA  . ASP A 67  ? 1.3311 1.2506 1.0465 -0.5253 -0.0692 -0.1086 363 ASP A CA  
446  C C   . ASP A 67  ? 1.1729 1.2171 0.9701 -0.5099 -0.0691 -0.1042 363 ASP A C   
447  O O   . ASP A 67  ? 1.1646 1.2988 0.9799 -0.5320 -0.0683 -0.0999 363 ASP A O   
448  C CB  . ASP A 67  ? 1.3738 1.2055 1.0297 -0.5410 -0.0628 -0.1025 363 ASP A CB  
449  C CG  . ASP A 67  ? 1.5826 1.3154 1.1436 -0.5738 -0.0617 -0.1029 363 ASP A CG  
450  O OD1 . ASP A 67  ? 1.6736 1.4448 1.2127 -0.6173 -0.0615 -0.1001 363 ASP A OD1 
451  O OD2 . ASP A 67  ? 1.6533 1.2699 1.1572 -0.5550 -0.0608 -0.1057 363 ASP A OD2 
452  N N   . GLN A 68  ? 1.0682 1.1192 0.9106 -0.4711 -0.0695 -0.1048 364 GLN A N   
453  C CA  . GLN A 68  ? 1.0370 1.1989 0.9491 -0.4526 -0.0691 -0.1001 364 GLN A CA  
454  C C   . GLN A 68  ? 1.0141 1.2575 0.9710 -0.4324 -0.0753 -0.1040 364 GLN A C   
455  O O   . GLN A 68  ? 0.9975 1.3434 0.9937 -0.4265 -0.0749 -0.0997 364 GLN A O   
456  C CB  . GLN A 68  ? 0.9835 1.1233 0.9228 -0.4215 -0.0671 -0.0983 364 GLN A CB  
457  C CG  . GLN A 68  ? 1.0404 1.1110 0.9753 -0.3929 -0.0707 -0.1058 364 GLN A CG  
458  C CD  . GLN A 68  ? 1.0288 1.0388 0.9602 -0.3642 -0.0650 -0.1007 364 GLN A CD  
459  O OE1 . GLN A 68  ? 0.8980 0.9197 0.8684 -0.3161 -0.0635 -0.0975 364 GLN A OE1 
460  N NE2 . GLN A 68  ? 1.1352 1.0770 1.0152 -0.3919 -0.0614 -0.0985 364 GLN A NE2 
461  N N   . TYR A 69  ? 1.0616 1.2598 1.0072 -0.4202 -0.0807 -0.1122 365 TYR A N   
462  C CA  . TYR A 69  ? 1.0189 1.2884 1.0012 -0.4008 -0.0871 -0.1157 365 TYR A CA  
463  C C   . TYR A 69  ? 1.0151 1.3498 0.9887 -0.4291 -0.0879 -0.1138 365 TYR A C   
464  O O   . TYR A 69  ? 0.9618 1.3932 0.9756 -0.4119 -0.0903 -0.1117 365 TYR A O   
465  C CB  . TYR A 69  ? 1.0527 1.2558 1.0168 -0.3862 -0.0922 -0.1253 365 TYR A CB  
466  C CG  . TYR A 69  ? 1.0506 1.3178 1.0368 -0.3762 -0.0988 -0.1289 365 TYR A CG  
467  C CD1 . TYR A 69  ? 1.0081 1.3662 1.0502 -0.3433 -0.1015 -0.1255 365 TYR A CD1 
468  C CD2 . TYR A 69  ? 1.0753 1.3102 1.0210 -0.3977 -0.1024 -0.1351 365 TYR A CD2 
469  C CE1 . TYR A 69  ? 1.0057 1.4201 1.0629 -0.3309 -0.1076 -0.1277 365 TYR A CE1 
470  C CE2 . TYR A 69  ? 1.0208 1.3165 0.9859 -0.3885 -0.1086 -0.1379 365 TYR A CE2 
471  C CZ  . TYR A 69  ? 1.0003 1.3859 1.0212 -0.3545 -0.1112 -0.1339 365 TYR A CZ  
472  O OH  . TYR A 69  ? 1.0083 1.4514 1.0439 -0.3415 -0.1174 -0.1358 365 TYR A OH  
473  N N   . TYR A 70  ? 1.1534 1.4348 1.0693 -0.4712 -0.0857 -0.1143 366 TYR A N   
474  C CA  . TYR A 70  ? 1.2500 1.5982 1.1547 -0.5036 -0.0858 -0.1120 366 TYR A CA  
475  C C   . TYR A 70  ? 1.2510 1.6822 1.1750 -0.5162 -0.0796 -0.1029 366 TYR A C   
476  O O   . TYR A 70  ? 1.2697 1.8034 1.2153 -0.5206 -0.0796 -0.1000 366 TYR A O   
477  C CB  . TYR A 70  ? 1.3926 1.6545 1.2225 -0.5469 -0.0857 -0.1153 366 TYR A CB  
478  C CG  . TYR A 70  ? 1.4111 1.6274 1.2254 -0.5356 -0.0925 -0.1249 366 TYR A CG  
479  C CD1 . TYR A 70  ? 1.4217 1.5206 1.1968 -0.5225 -0.0932 -0.1313 366 TYR A CD1 
480  C CD2 . TYR A 70  ? 1.4099 1.7034 1.2478 -0.5339 -0.0980 -0.1274 366 TYR A CD2 
481  C CE1 . TYR A 70  ? 1.4405 1.5003 1.1990 -0.5100 -0.0990 -0.1407 366 TYR A CE1 
482  C CE2 . TYR A 70  ? 1.4166 1.6707 1.2399 -0.5232 -0.1045 -0.1364 366 TYR A CE2 
483  C CZ  . TYR A 70  ? 1.4095 1.5471 1.1931 -0.5120 -0.1049 -0.1433 366 TYR A CZ  
484  O OH  . TYR A 70  ? 1.3430 1.4443 1.1093 -0.4999 -0.1108 -0.1528 366 TYR A OH  
485  N N   . SER A 71  ? 1.2085 1.5995 1.1238 -0.5193 -0.0740 -0.0984 367 SER A N   
486  C CA  . SER A 71  ? 1.1903 1.6631 1.1298 -0.5228 -0.0681 -0.0903 367 SER A CA  
487  C C   . SER A 71  ? 1.0808 1.6564 1.0870 -0.4759 -0.0699 -0.0890 367 SER A C   
488  O O   . SER A 71  ? 1.1527 1.8276 1.1779 -0.4762 -0.0664 -0.0838 367 SER A O   
489  C CB  . SER A 71  ? 1.2065 1.6115 1.1290 -0.5263 -0.0627 -0.0863 367 SER A CB  
490  O OG  . SER A 71  ? 1.2308 1.7025 1.1583 -0.5434 -0.0564 -0.0785 367 SER A OG  
491  N N   . SER A 72  ? 0.9305 1.4831 0.9664 -0.4343 -0.0751 -0.0937 368 SER A N   
492  C CA  . SER A 72  ? 0.9325 1.5669 1.0218 -0.3858 -0.0768 -0.0918 368 SER A CA  
493  C C   . SER A 72  ? 1.0209 1.7394 1.1221 -0.3774 -0.0805 -0.0927 368 SER A C   
494  O O   . SER A 72  ? 1.0520 1.8588 1.1839 -0.3450 -0.0793 -0.0888 368 SER A O   
495  C CB  . SER A 72  ? 0.9252 1.5054 1.0357 -0.3476 -0.0812 -0.0959 368 SER A CB  
496  O OG  . SER A 72  ? 0.9360 1.5303 1.0573 -0.3263 -0.0884 -0.1008 368 SER A OG  
497  N N   . ILE A 73  ? 1.0832 1.7743 1.1570 -0.4027 -0.0849 -0.0979 369 ILE A N   
498  C CA  . ILE A 73  ? 1.1158 1.8889 1.1980 -0.3979 -0.0882 -0.0985 369 ILE A CA  
499  C C   . ILE A 73  ? 1.2097 2.0388 1.2658 -0.4445 -0.0831 -0.0945 369 ILE A C   
500  O O   . ILE A 73  ? 1.2682 2.1560 1.3176 -0.4574 -0.0852 -0.0954 369 ILE A O   
501  C CB  . ILE A 73  ? 1.1257 1.8496 1.1944 -0.3977 -0.0962 -0.1064 369 ILE A CB  
502  C CG1 . ILE A 73  ? 1.1827 1.8044 1.1981 -0.4442 -0.0962 -0.1111 369 ILE A CG1 
503  C CG2 . ILE A 73  ? 1.0383 1.7311 1.1356 -0.3485 -0.1013 -0.1095 369 ILE A CG2 
504  C CD1 . ILE A 73  ? 1.1708 1.7211 1.1703 -0.4361 -0.1034 -0.1201 369 ILE A CD1 
505  N N   . LYS A 74  ? 1.2270 2.0402 1.2661 -0.4710 -0.0763 -0.0898 370 LYS A N   
506  C CA  . LYS A 74  ? 1.2993 2.1713 1.3115 -0.5166 -0.0705 -0.0846 370 LYS A CA  
507  C C   . LYS A 74  ? 1.4272 2.2687 1.3905 -0.5680 -0.0730 -0.0879 370 LYS A C   
508  O O   . LYS A 74  ? 1.5122 2.4344 1.4620 -0.5977 -0.0710 -0.0851 370 LYS A O   
509  C CB  . LYS A 74  ? 1.2632 2.2734 1.3089 -0.4910 -0.0675 -0.0798 370 LYS A CB  
510  C CG  . LYS A 74  ? 1.2553 2.2992 1.3224 -0.4687 -0.0612 -0.0739 370 LYS A CG  
511  C CD  . LYS A 74  ? 1.2184 2.3421 1.3302 -0.4034 -0.0615 -0.0725 370 LYS A CD  
512  C CE  . LYS A 74  ? 1.2271 2.3437 1.3580 -0.3752 -0.0568 -0.0685 370 LYS A CE  
513  N NZ  . LYS A 74  ? 1.1994 2.3819 1.3628 -0.3091 -0.0566 -0.0668 370 LYS A NZ  
514  N N   . ARG A 75  ? 1.4039 2.1280 1.3368 -0.5777 -0.0771 -0.0938 371 ARG A N   
515  C CA  . ARG A 75  ? 1.4147 2.0757 1.2863 -0.6281 -0.0788 -0.0971 371 ARG A CA  
516  C C   . ARG A 75  ? 1.4863 2.0078 1.3066 -0.6464 -0.0771 -0.0985 371 ARG A C   
517  O O   . ARG A 75  ? 1.4613 1.8856 1.2437 -0.6516 -0.0811 -0.1050 371 ARG A O   
518  C CB  . ARG A 75  ? 1.3592 2.0203 1.2368 -0.6145 -0.0867 -0.1044 371 ARG A CB  
519  C CG  . ARG A 75  ? 1.3361 2.1303 1.2607 -0.5899 -0.0884 -0.1027 371 ARG A CG  
520  C CD  . ARG A 75  ? 1.2960 2.0826 1.2574 -0.5379 -0.0960 -0.1087 371 ARG A CD  
521  N NE  . ARG A 75  ? 1.3582 2.2156 1.3261 -0.5368 -0.1007 -0.1110 371 ARG A NE  
522  C CZ  . ARG A 75  ? 1.4472 2.2692 1.3749 -0.5734 -0.1047 -0.1160 371 ARG A CZ  
523  N NH1 . ARG A 75  ? 1.4064 2.3014 1.3443 -0.5694 -0.1090 -0.1176 371 ARG A NH1 
524  N NH2 . ARG A 75  ? 1.5479 2.2587 1.4207 -0.6123 -0.1041 -0.1191 371 ARG A NH2 
525  N N   . PHE A 76  ? 1.5552 2.0667 1.3722 -0.6518 -0.0708 -0.0924 372 PHE A N   
526  C CA  . PHE A 76  ? 1.6776 2.0640 1.4394 -0.6706 -0.0677 -0.0916 372 PHE A CA  
527  C C   . PHE A 76  ? 1.8247 2.1402 1.5025 -0.7264 -0.0674 -0.0921 372 PHE A C   
528  O O   . PHE A 76  ? 1.9170 2.2957 1.5724 -0.7700 -0.0653 -0.0877 372 PHE A O   
529  C CB  . PHE A 76  ? 1.7057 2.1221 1.4776 -0.6749 -0.0607 -0.0835 372 PHE A CB  
530  C CG  . PHE A 76  ? 1.7782 2.0718 1.4975 -0.6871 -0.0570 -0.0816 372 PHE A CG  
531  C CD1 . PHE A 76  ? 1.8068 1.9704 1.4778 -0.6826 -0.0596 -0.0870 372 PHE A CD1 
532  C CD2 . PHE A 76  ? 1.8213 2.1319 1.5368 -0.6997 -0.0507 -0.0740 372 PHE A CD2 
533  C CE1 . PHE A 76  ? 1.8592 1.9113 1.4768 -0.6884 -0.0558 -0.0844 372 PHE A CE1 
534  C CE2 . PHE A 76  ? 1.8636 2.0632 1.5285 -0.7086 -0.0473 -0.0715 372 PHE A CE2 
535  C CZ  . PHE A 76  ? 1.9044 1.9737 1.5191 -0.7017 -0.0498 -0.0765 372 PHE A CZ  
536  N N   . GLY A 77  ? 1.8639 2.0475 1.4905 -0.7240 -0.0695 -0.0972 373 GLY A N   
537  C CA  . GLY A 77  ? 1.9809 2.0681 1.5122 -0.7733 -0.0682 -0.0964 373 GLY A CA  
538  C C   . GLY A 77  ? 1.9767 2.0983 1.4797 -0.8115 -0.0716 -0.0986 373 GLY A C   
539  O O   . GLY A 77  ? 2.1258 2.1725 1.5433 -0.8588 -0.0704 -0.0970 373 GLY A O   
540  N N   . SER A 78  ? 1.7973 2.0280 1.3659 -0.7914 -0.0759 -0.1019 374 SER A N   
541  C CA  . SER A 78  ? 1.7160 1.9915 1.2645 -0.8248 -0.0795 -0.1040 374 SER A CA  
542  C C   . SER A 78  ? 1.7068 1.8590 1.1965 -0.8271 -0.0843 -0.1122 374 SER A C   
543  O O   . SER A 78  ? 1.6397 1.6725 1.0972 -0.8051 -0.0840 -0.1154 374 SER A O   
544  C CB  . SER A 78  ? 1.5828 1.9998 1.2153 -0.7927 -0.0830 -0.1055 374 SER A CB  
545  O OG  . SER A 78  ? 1.4931 1.8914 1.1766 -0.7328 -0.0880 -0.1121 374 SER A OG  
546  N N   . LYS A 79  ? 1.6911 1.8732 1.1634 -0.8525 -0.0887 -0.1156 375 LYS A N   
547  C CA  . LYS A 79  ? 1.7208 1.7942 1.1408 -0.8501 -0.0939 -0.1243 375 LYS A CA  
548  C C   . LYS A 79  ? 1.6272 1.6870 1.1026 -0.7848 -0.0992 -0.1331 375 LYS A C   
549  O O   . LYS A 79  ? 1.6391 1.5788 1.0737 -0.7635 -0.1002 -0.1391 375 LYS A O   
550  C CB  . LYS A 79  ? 1.7819 1.8989 1.1744 -0.8926 -0.0978 -0.1260 375 LYS A CB  
551  C CG  . LYS A 79  ? 1.8063 1.8107 1.1396 -0.8914 -0.1034 -0.1354 375 LYS A CG  
552  C CD  . LYS A 79  ? 1.9193 1.8571 1.1503 -0.9592 -0.1020 -0.1323 375 LYS A CD  
553  C CE  . LYS A 79  ? 1.9856 1.7898 1.1459 -0.9529 -0.1066 -0.1413 375 LYS A CE  
554  N NZ  . LYS A 79  ? 2.0080 1.6738 1.1300 -0.9131 -0.1041 -0.1440 375 LYS A NZ  
555  N N   . ALA A 80  ? 1.5848 1.7657 1.1478 -0.7510 -0.1023 -0.1336 376 ALA A N   
556  C CA  . ALA A 80  ? 1.5702 1.7425 1.1825 -0.6922 -0.1075 -0.1412 376 ALA A CA  
557  C C   . ALA A 80  ? 1.5523 1.6405 1.1634 -0.6603 -0.1038 -0.1413 376 ALA A C   
558  O O   . ALA A 80  ? 1.5637 1.5864 1.1736 -0.6238 -0.1069 -0.1491 376 ALA A O   
559  C CB  . ALA A 80  ? 1.4455 1.7602 1.1443 -0.6614 -0.1105 -0.1392 376 ALA A CB  
560  N N   . HIS A 81  ? 1.5395 1.6287 1.1470 -0.6740 -0.0969 -0.1329 377 HIS A N   
561  C CA  . HIS A 81  ? 1.5532 1.5550 1.1497 -0.6480 -0.0930 -0.1324 377 HIS A CA  
562  C C   . HIS A 81  ? 1.6490 1.5008 1.1519 -0.6608 -0.0914 -0.1359 377 HIS A C   
563  O O   . HIS A 81  ? 1.6219 1.3926 1.1118 -0.6233 -0.0925 -0.1424 377 HIS A O   
564  C CB  . HIS A 81  ? 1.5513 1.5950 1.1653 -0.6602 -0.0862 -0.1222 377 HIS A CB  
565  C CG  . HIS A 81  ? 1.6062 1.5541 1.1970 -0.6411 -0.0816 -0.1205 377 HIS A CG  
566  N ND1 . HIS A 81  ? 1.6314 1.5736 1.2056 -0.6613 -0.0750 -0.1118 377 HIS A ND1 
567  C CD2 . HIS A 81  ? 1.6025 1.4603 1.1820 -0.6027 -0.0824 -0.1263 377 HIS A CD2 
568  C CE1 . HIS A 81  ? 1.6249 1.4753 1.1788 -0.6357 -0.0724 -0.1119 377 HIS A CE1 
569  N NE2 . HIS A 81  ? 1.6255 1.4249 1.1822 -0.5994 -0.0765 -0.1206 377 HIS A NE2 
570  N N   . MET A 82  ? 1.7720 1.5838 1.2026 -0.7127 -0.0885 -0.1311 378 MET A N   
571  C CA  . MET A 82  ? 1.8782 1.5385 1.2074 -0.7239 -0.0862 -0.1322 378 MET A CA  
572  C C   . MET A 82  ? 1.8370 1.4275 1.1373 -0.6989 -0.0913 -0.1431 378 MET A C   
573  O O   . MET A 82  ? 1.9129 1.3801 1.1524 -0.6750 -0.0892 -0.1460 378 MET A O   
574  C CB  . MET A 82  ? 2.0091 1.6473 1.2618 -0.7897 -0.0830 -0.1247 378 MET A CB  
575  C CG  . MET A 82  ? 2.0763 1.7552 1.3363 -0.8137 -0.0767 -0.1140 378 MET A CG  
576  S SD  . MET A 82  ? 2.0978 1.6664 1.3339 -0.7740 -0.0715 -0.1113 378 MET A SD  
577  C CE  . MET A 82  ? 2.1079 1.7754 1.3889 -0.7963 -0.0657 -0.1004 378 MET A CE  
578  N N   . ASP A 83  ? 1.7122 1.3802 1.0526 -0.7003 -0.0977 -0.1491 379 ASP A N   
579  C CA  . ASP A 83  ? 1.7255 1.3320 1.0413 -0.6737 -0.1026 -0.1601 379 ASP A CA  
580  C C   . ASP A 83  ? 1.6984 1.2967 1.0633 -0.6111 -0.1033 -0.1665 379 ASP A C   
581  O O   . ASP A 83  ? 1.7497 1.2565 1.0720 -0.5807 -0.1036 -0.1743 379 ASP A O   
582  C CB  . ASP A 83  ? 1.6918 1.3837 1.0341 -0.6929 -0.1096 -0.1647 379 ASP A CB  
583  C CG  . ASP A 83  ? 1.8549 1.5183 1.1220 -0.7541 -0.1094 -0.1613 379 ASP A CG  
584  O OD1 . ASP A 83  ? 1.8604 1.6328 1.1589 -0.7893 -0.1110 -0.1570 379 ASP A OD1 
585  O OD2 . ASP A 83  ? 1.9847 1.5165 1.1567 -0.7663 -0.1072 -0.1623 379 ASP A OD2 
586  N N   . ARG A 84  ? 1.6341 1.3274 1.0839 -0.5910 -0.1032 -0.1629 380 ARG A N   
587  C CA  . ARG A 84  ? 1.5844 1.2693 1.0766 -0.5370 -0.1031 -0.1674 380 ARG A CA  
588  C C   . ARG A 84  ? 1.6433 1.2192 1.0870 -0.5188 -0.0961 -0.1648 380 ARG A C   
589  O O   . ARG A 84  ? 1.7192 1.2371 1.1548 -0.4748 -0.0949 -0.1709 380 ARG A O   
590  C CB  . ARG A 84  ? 1.4292 1.2421 1.0180 -0.5232 -0.1048 -0.1628 380 ARG A CB  
591  C CG  . ARG A 84  ? 1.3082 1.1198 0.9407 -0.4736 -0.1049 -0.1664 380 ARG A CG  
592  C CD  . ARG A 84  ? 1.2714 1.1295 0.9386 -0.4489 -0.1119 -0.1746 380 ARG A CD  
593  N NE  . ARG A 84  ? 1.2038 1.0369 0.8916 -0.4054 -0.1109 -0.1790 380 ARG A NE  
594  C CZ  . ARG A 84  ? 1.1921 0.9241 0.8273 -0.3818 -0.1082 -0.1869 380 ARG A CZ  
595  N NH1 . ARG A 84  ? 1.3306 0.9761 0.8906 -0.3950 -0.1068 -0.1907 380 ARG A NH1 
596  N NH2 . ARG A 84  ? 1.0380 0.7677 0.7067 -0.3285 -0.1019 -0.1825 380 ARG A NH2 
597  N N   . LEU A 85  ? 1.6212 1.1717 1.0303 -0.5503 -0.0909 -0.1554 381 LEU A N   
598  C CA  . LEU A 85  ? 1.6553 1.0934 1.0043 -0.5344 -0.0845 -0.1518 381 LEU A CA  
599  C C   . LEU A 85  ? 1.7629 1.0722 1.0164 -0.5237 -0.0837 -0.1570 381 LEU A C   
600  O O   . LEU A 85  ? 1.7265 0.9557 0.9506 -0.4773 -0.0805 -0.1600 381 LEU A O   
601  C CB  . LEU A 85  ? 1.6945 1.1341 1.0183 -0.5763 -0.0797 -0.1402 381 LEU A CB  
602  C CG  . LEU A 85  ? 1.7277 1.1015 1.0280 -0.5567 -0.0734 -0.1338 381 LEU A CG  
603  C CD1 . LEU A 85  ? 1.5929 1.0679 0.9888 -0.5396 -0.0729 -0.1307 381 LEU A CD1 
604  C CD2 . LEU A 85  ? 1.9022 1.2156 1.1212 -0.6030 -0.0690 -0.1244 381 LEU A CD2 
605  N N   . GLU A 86  ? 1.9175 1.2081 1.1191 -0.5645 -0.0862 -0.1577 382 GLU A N   
606  C CA  . GLU A 86  ? 2.0405 1.2125 1.1489 -0.5554 -0.0862 -0.1628 382 GLU A CA  
607  C C   . GLU A 86  ? 1.9232 1.0926 1.0579 -0.5022 -0.0888 -0.1745 382 GLU A C   
608  O O   . GLU A 86  ? 1.9799 1.0481 1.0552 -0.4609 -0.0853 -0.1777 382 GLU A O   
609  C CB  . GLU A 86  ? 2.2324 1.4065 1.2936 -0.6134 -0.0896 -0.1620 382 GLU A CB  
610  C CG  . GLU A 86  ? 2.4669 1.5210 1.4285 -0.6088 -0.0903 -0.1671 382 GLU A CG  
611  C CD  . GLU A 86  ? 2.7183 1.6649 1.5651 -0.6515 -0.0867 -0.1580 382 GLU A CD  
612  O OE1 . GLU A 86  ? 2.8617 1.6753 1.6128 -0.6277 -0.0843 -0.1583 382 GLU A OE1 
613  O OE2 . GLU A 86  ? 2.7662 1.7613 1.6136 -0.7078 -0.0861 -0.1498 382 GLU A OE2 
614  N N   . GLU A 87  ? 1.7721 1.0545 0.9921 -0.5001 -0.0946 -0.1803 383 GLU A N   
615  C CA  . GLU A 87  ? 1.6865 0.9756 0.9313 -0.4544 -0.0973 -0.1915 383 GLU A CA  
616  C C   . GLU A 87  ? 1.6878 0.9375 0.9421 -0.3971 -0.0917 -0.1926 383 GLU A C   
617  O O   . GLU A 87  ? 1.7431 0.9206 0.9537 -0.3540 -0.0887 -0.1990 383 GLU A O   
618  C CB  . GLU A 87  ? 1.5637 0.9882 0.8992 -0.4646 -0.1047 -0.1948 383 GLU A CB  
619  C CG  . GLU A 87  ? 1.6211 1.0696 0.9918 -0.4201 -0.1077 -0.2050 383 GLU A CG  
620  C CD  . GLU A 87  ? 1.5613 1.1298 0.9990 -0.4353 -0.1162 -0.2073 383 GLU A CD  
621  O OE1 . GLU A 87  ? 1.3881 1.0560 0.8931 -0.4499 -0.1181 -0.1998 383 GLU A OE1 
622  O OE2 . GLU A 87  ? 1.5327 1.0961 0.9525 -0.4299 -0.1207 -0.2159 383 GLU A OE2 
623  N N   . VAL A 88  ? 1.6033 0.9012 0.9117 -0.3941 -0.0895 -0.1859 384 VAL A N   
624  C CA  . VAL A 88  ? 1.5594 0.8286 0.8805 -0.3417 -0.0843 -0.1863 384 VAL A CA  
625  C C   . VAL A 88  ? 1.7106 0.8520 0.9399 -0.3160 -0.0771 -0.1828 384 VAL A C   
626  O O   . VAL A 88  ? 1.7056 0.7967 0.9108 -0.2609 -0.0728 -0.1869 384 VAL A O   
627  C CB  . VAL A 88  ? 1.4662 0.8129 0.8615 -0.3481 -0.0839 -0.1791 384 VAL A CB  
628  C CG1 . VAL A 88  ? 1.4891 0.7928 0.8839 -0.2970 -0.0780 -0.1784 384 VAL A CG1 
629  C CG2 . VAL A 88  ? 1.3343 0.8063 0.8187 -0.3584 -0.0907 -0.1817 384 VAL A CG2 
630  N N   . ASN A 89  ? 1.8620 0.9530 1.0360 -0.3530 -0.0753 -0.1740 385 ASN A N   
631  C CA  . ASN A 89  ? 2.0262 0.9904 1.1013 -0.3312 -0.0694 -0.1687 385 ASN A CA  
632  C C   . ASN A 89  ? 2.1045 0.9940 1.1164 -0.2933 -0.0685 -0.1761 385 ASN A C   
633  O O   . ASN A 89  ? 2.1672 0.9945 1.1418 -0.2351 -0.0631 -0.1755 385 ASN A O   
634  C CB  . ASN A 89  ? 2.1759 1.0970 1.1886 -0.3889 -0.0693 -0.1594 385 ASN A CB  
635  C CG  . ASN A 89  ? 2.4035 1.1991 1.3166 -0.3686 -0.0634 -0.1510 385 ASN A CG  
636  O OD1 . ASN A 89  ? 2.4578 1.2294 1.3753 -0.3176 -0.0590 -0.1486 385 ASN A OD1 
637  N ND2 . ASN A 89  ? 2.5225 1.2370 1.3402 -0.4082 -0.0635 -0.1458 385 ASN A ND2 
638  N N   . LYS A 90  ? 2.1326 1.0353 1.1338 -0.3228 -0.0737 -0.1827 386 LYS A N   
639  C CA  . LYS A 90  ? 2.2262 1.0595 1.1652 -0.2898 -0.0730 -0.1898 386 LYS A CA  
640  C C   . LYS A 90  ? 2.1811 1.0535 1.1695 -0.2267 -0.0706 -0.1982 386 LYS A C   
641  O O   . LYS A 90  ? 2.2674 1.0728 1.2009 -0.1746 -0.0658 -0.2003 386 LYS A O   
642  C CB  . LYS A 90  ? 2.2935 1.1436 1.2179 -0.3396 -0.0798 -0.1951 386 LYS A CB  
643  C CG  . LYS A 90  ? 2.3804 1.1767 1.2339 -0.4010 -0.0810 -0.1865 386 LYS A CG  
644  C CD  . LYS A 90  ? 2.3490 1.2223 1.2337 -0.4601 -0.0884 -0.1902 386 LYS A CD  
645  C CE  . LYS A 90  ? 2.5202 1.3106 1.3030 -0.5125 -0.0893 -0.1848 386 LYS A CE  
646  N NZ  . LYS A 90  ? 2.4805 1.3570 1.2964 -0.5704 -0.0962 -0.1875 386 LYS A NZ  
647  N N   . GLU A 91  ? 2.0201 1.0016 1.1074 -0.2291 -0.0735 -0.2022 387 GLU A N   
648  C CA  . GLU A 91  ? 1.9557 0.9742 1.0851 -0.1716 -0.0704 -0.2091 387 GLU A CA  
649  C C   . GLU A 91  ? 1.9960 0.9818 1.1174 -0.1171 -0.0621 -0.2028 387 GLU A C   
650  O O   . GLU A 91  ? 2.0328 1.0166 1.1524 -0.0567 -0.0563 -0.2061 387 GLU A O   
651  C CB  . GLU A 91  ? 1.8438 0.9812 1.0709 -0.1922 -0.0768 -0.2139 387 GLU A CB  
652  C CG  . GLU A 91  ? 1.7245 0.9162 1.0024 -0.1363 -0.0728 -0.2165 387 GLU A CG  
653  C CD  . GLU A 91  ? 1.5972 0.9299 0.9892 -0.1510 -0.0766 -0.2093 387 GLU A CD  
654  O OE1 . GLU A 91  ? 1.5129 0.9110 0.9595 -0.1109 -0.0722 -0.2048 387 GLU A OE1 
655  O OE2 . GLU A 91  ? 1.5562 0.9343 0.9792 -0.2015 -0.0838 -0.2077 387 GLU A OE2 
656  N N   . ILE A 92  ? 1.9280 0.8956 1.0454 -0.1357 -0.0609 -0.1929 388 ILE A N   
657  C CA  . ILE A 92  ? 1.9255 0.8552 1.0247 -0.0835 -0.0534 -0.1856 388 ILE A CA  
658  C C   . ILE A 92  ? 2.0961 0.9151 1.0902 -0.0496 -0.0487 -0.1809 388 ILE A C   
659  O O   . ILE A 92  ? 2.1597 0.9545 1.1323 0.0136  -0.0422 -0.1766 388 ILE A O   
660  C CB  . ILE A 92  ? 1.8873 0.8344 1.0152 -0.1132 -0.0538 -0.1763 388 ILE A CB  
661  C CG1 . ILE A 92  ? 1.7939 0.8518 1.0222 -0.1466 -0.0593 -0.1796 388 ILE A CG1 
662  C CG2 . ILE A 92  ? 1.8566 0.7764 0.9734 -0.0558 -0.0468 -0.1690 388 ILE A CG2 
663  C CD1 . ILE A 92  ? 1.7420 0.8251 1.0027 -0.1735 -0.0592 -0.1700 388 ILE A CD1 
664  N N   . GLU A 93  ? 2.1924 0.9449 1.1161 -0.0899 -0.0521 -0.1802 389 GLU A N   
665  C CA  . GLU A 93  ? 2.3525 0.9986 1.1709 -0.0549 -0.0488 -0.1775 389 GLU A CA  
666  C C   . GLU A 93  ? 2.3300 0.9981 1.1577 -0.0021 -0.0463 -0.1862 389 GLU A C   
667  O O   . GLU A 93  ? 2.3541 0.9915 1.1463 0.0653  -0.0401 -0.1825 389 GLU A O   
668  C CB  . GLU A 93  ? 2.4721 1.0442 1.2118 -0.1143 -0.0535 -0.1757 389 GLU A CB  
669  C CG  . GLU A 93  ? 2.5767 1.1314 1.3009 -0.1724 -0.0552 -0.1662 389 GLU A CG  
670  C CD  . GLU A 93  ? 2.6886 1.1483 1.3315 -0.1432 -0.0503 -0.1541 389 GLU A CD  
671  O OE1 . GLU A 93  ? 2.7572 1.1554 1.3431 -0.0785 -0.0463 -0.1523 389 GLU A OE1 
672  O OE2 . GLU A 93  ? 2.6839 1.1345 1.3182 -0.1838 -0.0504 -0.1460 389 GLU A OE2 
673  N N   . SER A 94  ? 2.2903 1.0225 1.1691 -0.0303 -0.0509 -0.1972 390 SER A N   
674  C CA  . SER A 94  ? 2.3218 1.0689 1.1988 0.0103  -0.0488 -0.2059 390 SER A CA  
675  C C   . SER A 94  ? 2.3566 1.1705 1.2895 0.0781  -0.0413 -0.2063 390 SER A C   
676  O O   . SER A 94  ? 2.4308 1.2226 1.3265 0.1396  -0.0349 -0.2046 390 SER A O   
677  C CB  . SER A 94  ? 2.2140 1.0213 1.1357 -0.0399 -0.0564 -0.2168 390 SER A CB  
678  O OG  . SER A 94  ? 2.2323 1.0733 1.1687 0.0012  -0.0538 -0.2255 390 SER A OG  
679  N N   . THR A 95  ? 2.2947 1.1957 1.3161 0.0680  -0.0421 -0.2074 391 THR A N   
680  C CA  . THR A 95  ? 2.2594 1.2372 1.3407 0.1250  -0.0353 -0.2078 391 THR A CA  
681  C C   . THR A 95  ? 2.1714 1.1581 1.2712 0.1534  -0.0306 -0.1975 391 THR A C   
682  O O   . THR A 95  ? 2.0324 1.0914 1.1841 0.2011  -0.0244 -0.1952 391 THR A O   
683  C CB  . THR A 95  ? 2.2414 1.3327 1.4221 0.0973  -0.0395 -0.2115 391 THR A CB  
684  O OG1 . THR A 95  ? 2.3377 1.4176 1.5134 0.0277  -0.0500 -0.2187 391 THR A OG1 
685  C CG2 . THR A 95  ? 2.1808 1.3391 1.3931 0.1404  -0.0337 -0.2121 391 THR A CG2 
686  N N   . SER A 96  ? 2.2738 1.1972 1.3348 0.1242  -0.0333 -0.1897 392 SER A N   
687  C CA  . SER A 96  ? 2.2383 1.1722 1.3210 0.1397  -0.0305 -0.1801 392 SER A CA  
688  C C   . SER A 96  ? 2.0906 1.1295 1.2787 0.1228  -0.0324 -0.1813 392 SER A C   
689  O O   . SER A 96  ? 2.0709 1.1621 1.3067 0.1506  -0.0285 -0.1702 392 SER A O   
690  C CB  . SER A 96  ? 2.3080 1.2308 1.3586 0.2178  -0.0223 -0.1713 392 SER A CB  
691  O OG  . SER A 96  ? 2.2629 1.2713 1.3647 0.2662  -0.0167 -0.1751 392 SER A OG  
692  N N   . THR A 97  ? 1.9078 1.0135 1.1558 0.0744  -0.0384 -0.1840 393 THR A N   
693  C CA  . THR A 97  ? 1.6133 0.8452 0.9792 0.0465  -0.0413 -0.1747 393 THR A CA  
694  C C   . THR A 97  ? 1.5352 0.7905 0.9183 -0.0126 -0.0498 -0.1816 393 THR A C   
695  O O   . THR A 97  ? 1.6670 0.8392 0.9711 -0.0378 -0.0539 -0.1929 393 THR A O   
696  C CB  . THR A 97  ? 1.4748 0.8136 0.9203 0.0925  -0.0353 -0.1663 393 THR A CB  
697  O OG1 . THR A 97  ? 1.3734 0.8192 0.9201 0.0633  -0.0388 -0.1581 393 THR A OG1 
698  C CG2 . THR A 97  ? 1.4259 0.7703 0.8526 0.1182  -0.0327 -0.1734 393 THR A CG2 
699  N N   . TYR A 98  ? 1.4511 0.8166 0.9314 -0.0354 -0.0531 -0.1749 394 TYR A N   
700  C CA  . TYR A 98  ? 1.4357 0.8369 0.9355 -0.0855 -0.0615 -0.1805 394 TYR A CA  
701  C C   . TYR A 98  ? 1.2826 0.8082 0.8868 -0.0830 -0.0626 -0.1722 394 TYR A C   
702  O O   . TYR A 98  ? 1.2130 0.7901 0.8703 -0.0508 -0.0573 -0.1623 394 TYR A O   
703  C CB  . TYR A 98  ? 1.4769 0.8392 0.9436 -0.1444 -0.0679 -0.1832 394 TYR A CB  
704  C CG  . TYR A 98  ? 1.3976 0.8200 0.9273 -0.1587 -0.0676 -0.1723 394 TYR A CG  
705  C CD1 . TYR A 98  ? 1.3586 0.8791 0.9606 -0.1912 -0.0731 -0.1687 394 TYR A CD1 
706  C CD2 . TYR A 98  ? 1.4312 0.8135 0.9455 -0.1355 -0.0618 -0.1654 394 TYR A CD2 
707  C CE1 . TYR A 98  ? 1.2429 0.8174 0.8989 -0.2000 -0.0723 -0.1591 394 TYR A CE1 
708  C CE2 . TYR A 98  ? 1.2519 0.6886 0.8223 -0.1477 -0.0615 -0.1557 394 TYR A CE2 
709  C CZ  . TYR A 98  ? 1.2056 0.7366 0.8456 -0.1802 -0.0665 -0.1528 394 TYR A CZ  
710  O OH  . TYR A 98  ? 1.1984 0.7814 0.8894 -0.1891 -0.0658 -0.1437 394 TYR A OH  
711  N N   . GLN A 99  ? 1.2837 0.8545 0.9106 -0.1178 -0.0701 -0.1762 395 GLN A N   
712  C CA  . GLN A 99  ? 1.1791 0.8547 0.8893 -0.1145 -0.0720 -0.1694 395 GLN A CA  
713  C C   . GLN A 99  ? 1.0638 0.7929 0.8090 -0.1582 -0.0796 -0.1676 395 GLN A C   
714  O O   . GLN A 99  ? 1.0783 0.7803 0.7831 -0.2002 -0.0859 -0.1753 395 GLN A O   
715  C CB  . GLN A 99  ? 1.1452 0.8404 0.8532 -0.1039 -0.0737 -0.1748 395 GLN A CB  
716  C CG  . GLN A 99  ? 1.1848 0.8574 0.8746 -0.0553 -0.0650 -0.1745 395 GLN A CG  
717  C CD  . GLN A 99  ? 1.1758 0.9107 0.9280 -0.0229 -0.0583 -0.1616 395 GLN A CD  
718  O OE1 . GLN A 99  ? 1.2582 0.9702 0.9983 0.0065  -0.0513 -0.1577 395 GLN A OE1 
719  N NE2 . GLN A 99  ? 1.1699 0.9820 0.9834 -0.0281 -0.0607 -0.1548 395 GLN A NE2 
720  N N   . LEU A 100 ? 0.9337 0.7404 0.7499 -0.1484 -0.0791 -0.1575 396 LEU A N   
721  C CA  . LEU A 100 ? 0.9018 0.7700 0.7551 -0.1795 -0.0850 -0.1544 396 LEU A CA  
722  C C   . LEU A 100 ? 0.9136 0.8454 0.7896 -0.1905 -0.0924 -0.1573 396 LEU A C   
723  O O   . LEU A 100 ? 0.9071 0.8588 0.7998 -0.1639 -0.0914 -0.1558 396 LEU A O   
724  C CB  . LEU A 100 ? 0.6703 0.5859 0.5807 -0.1596 -0.0812 -0.1427 396 LEU A CB  
725  C CG  . LEU A 100 ? 0.7362 0.6061 0.6334 -0.1520 -0.0752 -0.1383 396 LEU A CG  
726  C CD1 . LEU A 100 ? 0.7139 0.6262 0.6639 -0.1218 -0.0711 -0.1277 396 LEU A CD1 
727  C CD2 . LEU A 100 ? 0.8068 0.6746 0.6923 -0.1911 -0.0782 -0.1390 396 LEU A CD2 
728  N N   . LYS A 101 ? 0.9100 0.8784 0.7855 -0.2303 -0.0998 -0.1606 397 LYS A N   
729  C CA  . LYS A 101 ? 0.9979 1.0476 0.9040 -0.2381 -0.1077 -0.1612 397 LYS A CA  
730  C C   . LYS A 101 ? 0.9133 1.0281 0.8803 -0.2037 -0.1058 -0.1501 397 LYS A C   
731  O O   . LYS A 101 ? 0.9254 1.0389 0.9151 -0.1901 -0.1004 -0.1426 397 LYS A O   
732  C CB  . LYS A 101 ? 1.0950 1.1873 0.9934 -0.2875 -0.1154 -0.1651 397 LYS A CB  
733  C CG  . LYS A 101 ? 1.2089 1.2372 1.0375 -0.3314 -0.1196 -0.1768 397 LYS A CG  
734  C CD  . LYS A 101 ? 1.2510 1.2956 1.0640 -0.3360 -0.1269 -0.1848 397 LYS A CD  
735  C CE  . LYS A 101 ? 1.3585 1.3009 1.0890 -0.3602 -0.1280 -0.1970 397 LYS A CE  
736  N NZ  . LYS A 101 ? 1.3795 1.3186 1.0965 -0.3431 -0.1313 -0.2035 397 LYS A NZ  
737  N N   . ASP A 102 ? 0.7963 0.9616 0.7828 -0.1894 -0.1105 -0.1492 398 ASP A N   
738  C CA  . ASP A 102 ? 0.8089 1.0295 0.8403 -0.1590 -0.1100 -0.1391 398 ASP A CA  
739  C C   . ASP A 102 ? 0.8096 1.0765 0.8669 -0.1678 -0.1108 -0.1342 398 ASP A C   
740  O O   . ASP A 102 ? 0.7326 1.0005 0.8135 -0.1445 -0.1059 -0.1258 398 ASP A O   
741  C CB  . ASP A 102 ? 0.9810 1.2543 1.0196 -0.1490 -0.1173 -0.1396 398 ASP A CB  
742  C CG  . ASP A 102 ? 1.0172 1.2548 1.0435 -0.1248 -0.1141 -0.1391 398 ASP A CG  
743  O OD1 . ASP A 102 ? 0.9579 1.1341 0.9656 -0.1199 -0.1070 -0.1406 398 ASP A OD1 
744  O OD2 . ASP A 102 ? 1.0341 1.3089 1.0676 -0.1086 -0.1186 -0.1365 398 ASP A OD2 
745  N N   . THR A 103 ? 0.8214 1.1277 0.8715 -0.2039 -0.1167 -0.1394 399 THR A N   
746  C CA  . THR A 103 ? 0.8007 1.1631 0.8750 -0.2141 -0.1169 -0.1348 399 THR A CA  
747  C C   . THR A 103 ? 0.8604 1.1672 0.9285 -0.2206 -0.1091 -0.1320 399 THR A C   
748  O O   . THR A 103 ? 0.8114 1.1456 0.9063 -0.2066 -0.1058 -0.1248 399 THR A O   
749  C CB  . THR A 103 ? 0.8019 1.2260 0.8665 -0.2583 -0.1249 -0.1411 399 THR A CB  
750  O OG1 . THR A 103 ? 0.7911 1.1459 0.8071 -0.2996 -0.1254 -0.1500 399 THR A OG1 
751  C CG2 . THR A 103 ? 0.7113 1.2068 0.7868 -0.2472 -0.1336 -0.1427 399 THR A CG2 
752  N N   . GLU A 104 ? 0.8871 1.1131 0.9146 -0.2395 -0.1062 -0.1376 400 GLU A N   
753  C CA  . GLU A 104 ? 0.8529 1.0199 0.8684 -0.2404 -0.0989 -0.1345 400 GLU A CA  
754  C C   . GLU A 104 ? 0.8590 1.0082 0.9007 -0.1959 -0.0926 -0.1265 400 GLU A C   
755  O O   . GLU A 104 ? 0.9056 1.0485 0.9606 -0.1893 -0.0880 -0.1205 400 GLU A O   
756  C CB  . GLU A 104 ? 0.8982 0.9744 0.8535 -0.2627 -0.0976 -0.1424 400 GLU A CB  
757  C CG  . GLU A 104 ? 0.8911 0.9682 0.8072 -0.3172 -0.1038 -0.1503 400 GLU A CG  
758  C CD  . GLU A 104 ? 1.0207 0.9971 0.8650 -0.3325 -0.1039 -0.1599 400 GLU A CD  
759  O OE1 . GLU A 104 ? 1.0306 0.9854 0.8272 -0.3827 -0.1089 -0.1669 400 GLU A OE1 
760  O OE2 . GLU A 104 ? 1.0822 1.0016 0.9138 -0.2947 -0.0989 -0.1603 400 GLU A OE2 
761  N N   . LEU A 105 ? 0.7019 0.8453 0.7492 -0.1682 -0.0923 -0.1260 401 LEU A N   
762  C CA  . LEU A 105 ? 0.7115 0.8439 0.7805 -0.1330 -0.0869 -0.1180 401 LEU A CA  
763  C C   . LEU A 105 ? 0.7137 0.8989 0.8187 -0.1190 -0.0878 -0.1101 401 LEU A C   
764  O O   . LEU A 105 ? 0.7071 0.8785 0.8245 -0.1049 -0.0833 -0.1038 401 LEU A O   
765  C CB  . LEU A 105 ? 0.6395 0.7608 0.7036 -0.1121 -0.0863 -0.1185 401 LEU A CB  
766  C CG  . LEU A 105 ? 0.6303 0.7325 0.7059 -0.0840 -0.0800 -0.1110 401 LEU A CG  
767  C CD1 . LEU A 105 ? 0.6278 0.6789 0.6844 -0.0805 -0.0737 -0.1116 401 LEU A CD1 
768  C CD2 . LEU A 105 ? 0.6568 0.7639 0.7290 -0.0689 -0.0801 -0.1106 401 LEU A CD2 
769  N N   . ILE A 106 ? 0.6447 0.8905 0.7622 -0.1209 -0.0938 -0.1106 402 ILE A N   
770  C CA  . ILE A 106 ? 0.5754 0.8678 0.7177 -0.0998 -0.0948 -0.1035 402 ILE A CA  
771  C C   . ILE A 106 ? 0.6316 0.9408 0.7836 -0.1133 -0.0924 -0.1017 402 ILE A C   
772  O O   . ILE A 106 ? 0.6277 0.9335 0.7920 -0.0945 -0.0890 -0.0954 402 ILE A O   
773  C CB  . ILE A 106 ? 0.6067 0.9637 0.7547 -0.0916 -0.1020 -0.1045 402 ILE A CB  
774  C CG1 . ILE A 106 ? 0.5748 0.9118 0.7129 -0.0702 -0.1035 -0.1034 402 ILE A CG1 
775  C CG2 . ILE A 106 ? 0.6206 1.0308 0.7857 -0.0693 -0.1032 -0.0985 402 ILE A CG2 
776  C CD1 . ILE A 106 ? 0.5695 0.9520 0.7008 -0.0765 -0.1113 -0.1088 402 ILE A CD1 
777  N N   . TYR A 107 ? 0.6478 0.9738 0.7900 -0.1489 -0.0943 -0.1072 403 TYR A N   
778  C CA  . TYR A 107 ? 0.6900 1.0279 0.8358 -0.1683 -0.0913 -0.1054 403 TYR A CA  
779  C C   . TYR A 107 ? 0.7970 1.0653 0.9357 -0.1607 -0.0844 -0.1018 403 TYR A C   
780  O O   . TYR A 107 ? 0.6193 0.8969 0.7737 -0.1480 -0.0810 -0.0960 403 TYR A O   
781  C CB  . TYR A 107 ? 0.6694 1.0196 0.7929 -0.2165 -0.0943 -0.1121 403 TYR A CB  
782  C CG  . TYR A 107 ? 0.8281 1.1739 0.9447 -0.2440 -0.0903 -0.1100 403 TYR A CG  
783  C CD1 . TYR A 107 ? 0.8843 1.3151 1.0214 -0.2568 -0.0912 -0.1072 403 TYR A CD1 
784  C CD2 . TYR A 107 ? 0.9389 1.1981 1.0261 -0.2543 -0.0851 -0.1102 403 TYR A CD2 
785  C CE1 . TYR A 107 ? 0.9384 1.3669 1.0678 -0.2839 -0.0867 -0.1045 403 TYR A CE1 
786  C CE2 . TYR A 107 ? 0.9849 1.2344 1.0611 -0.2788 -0.0812 -0.1074 403 TYR A CE2 
787  C CZ  . TYR A 107 ? 0.9465 1.2802 1.0444 -0.2958 -0.0819 -0.1045 403 TYR A CZ  
788  O OH  . TYR A 107 ? 0.9426 1.2691 1.0279 -0.3228 -0.0775 -0.1012 403 TYR A OH  
789  N N   . GLY A 108 ? 0.7980 0.9982 0.9100 -0.1664 -0.0824 -0.1055 404 GLY A N   
790  C CA  . GLY A 108 ? 0.6879 0.8271 0.7901 -0.1550 -0.0764 -0.1022 404 GLY A CA  
791  C C   . GLY A 108 ? 0.6937 0.8416 0.8228 -0.1218 -0.0741 -0.0947 404 GLY A C   
792  O O   . GLY A 108 ? 0.6376 0.7787 0.7746 -0.1169 -0.0709 -0.0899 404 GLY A O   
793  N N   . ALA A 109 ? 0.6802 0.8408 0.8187 -0.1016 -0.0761 -0.0936 405 ALA A N   
794  C CA  . ALA A 109 ? 0.6069 0.7675 0.7606 -0.0760 -0.0745 -0.0864 405 ALA A CA  
795  C C   . ALA A 109 ? 0.6190 0.8127 0.7877 -0.0694 -0.0752 -0.0822 405 ALA A C   
796  O O   . ALA A 109 ? 0.6576 0.8348 0.8308 -0.0599 -0.0724 -0.0772 405 ALA A O   
797  C CB  . ALA A 109 ? 0.5238 0.6919 0.6768 -0.0606 -0.0770 -0.0857 405 ALA A CB  
798  N N   . LYS A 110 ? 0.5718 0.8167 0.7465 -0.0731 -0.0789 -0.0842 406 LYS A N   
799  C CA  . LYS A 110 ? 0.6085 0.8922 0.7944 -0.0594 -0.0791 -0.0803 406 LYS A CA  
800  C C   . LYS A 110 ? 0.6568 0.9353 0.8464 -0.0738 -0.0749 -0.0790 406 LYS A C   
801  O O   . LYS A 110 ? 0.6118 0.8985 0.8069 -0.0579 -0.0732 -0.0747 406 LYS A O   
802  C CB  . LYS A 110 ? 0.5735 0.9277 0.7655 -0.0593 -0.0838 -0.0828 406 LYS A CB  
803  C CG  . LYS A 110 ? 0.6562 1.0244 0.8427 -0.0318 -0.0883 -0.0816 406 LYS A CG  
804  C CD  . LYS A 110 ? 0.6307 1.0799 0.8241 -0.0321 -0.0934 -0.0843 406 LYS A CD  
805  C CE  . LYS A 110 ? 0.5354 0.9984 0.7184 0.0009  -0.0982 -0.0823 406 LYS A CE  
806  N NZ  . LYS A 110 ? 0.5296 1.0856 0.7203 0.0117  -0.1031 -0.0831 406 LYS A NZ  
807  N N   . HIS A 111 ? 0.6580 0.9172 0.8382 -0.1032 -0.0733 -0.0826 407 HIS A N   
808  C CA  . HIS A 111 ? 0.6883 0.9366 0.8649 -0.1202 -0.0693 -0.0810 407 HIS A CA  
809  C C   . HIS A 111 ? 0.7307 0.9187 0.9005 -0.1102 -0.0655 -0.0776 407 HIS A C   
810  O O   . HIS A 111 ? 0.7252 0.9070 0.8961 -0.1122 -0.0623 -0.0740 407 HIS A O   
811  C CB  . HIS A 111 ? 0.6685 0.9182 0.8267 -0.1595 -0.0699 -0.0861 407 HIS A CB  
812  C CG  . HIS A 111 ? 0.6028 0.9330 0.7726 -0.1762 -0.0724 -0.0872 407 HIS A CG  
813  N ND1 . HIS A 111 ? 0.6516 1.0379 0.8322 -0.1689 -0.0778 -0.0898 407 HIS A ND1 
814  C CD2 . HIS A 111 ? 0.6060 0.9801 0.7799 -0.1967 -0.0701 -0.0851 407 HIS A CD2 
815  C CE1 . HIS A 111 ? 0.6246 1.0912 0.8163 -0.1839 -0.0791 -0.0896 407 HIS A CE1 
816  N NE2 . HIS A 111 ? 0.6363 1.0986 0.8248 -0.2022 -0.0741 -0.0866 407 HIS A NE2 
817  N N   . ALA A 112 ? 0.6797 0.8315 0.8434 -0.0978 -0.0658 -0.0780 408 ALA A N   
818  C CA  . ALA A 112 ? 0.6714 0.7873 0.8348 -0.0825 -0.0630 -0.0734 408 ALA A CA  
819  C C   . ALA A 112 ? 0.7181 0.8514 0.8957 -0.0655 -0.0635 -0.0682 408 ALA A C   
820  O O   . ALA A 112 ? 0.7193 0.8377 0.8974 -0.0624 -0.0613 -0.0644 408 ALA A O   
821  C CB  . ALA A 112 ? 0.6690 0.7616 0.8262 -0.0716 -0.0631 -0.0742 408 ALA A CB  
822  N N   . TRP A 113 ? 0.6317 0.7912 0.8144 -0.0527 -0.0665 -0.0679 409 TRP A N   
823  C CA  . TRP A 113 ? 0.6085 0.7734 0.7916 -0.0343 -0.0672 -0.0636 409 TRP A CA  
824  C C   . TRP A 113 ? 0.6621 0.8550 0.8507 -0.0365 -0.0653 -0.0632 409 TRP A C   
825  O O   . TRP A 113 ? 0.5972 0.7753 0.7831 -0.0297 -0.0636 -0.0599 409 TRP A O   
826  C CB  . TRP A 113 ? 0.5683 0.7471 0.7445 -0.0163 -0.0709 -0.0633 409 TRP A CB  
827  C CG  . TRP A 113 ? 0.6187 0.7880 0.7801 0.0069  -0.0720 -0.0593 409 TRP A CG  
828  C CD1 . TRP A 113 ? 0.6756 0.8230 0.8305 0.0106  -0.0703 -0.0563 409 TRP A CD1 
829  C CD2 . TRP A 113 ? 0.6666 0.8402 0.8090 0.0313  -0.0753 -0.0581 409 TRP A CD2 
830  N NE1 . TRP A 113 ? 0.7171 0.8501 0.8467 0.0347  -0.0723 -0.0540 409 TRP A NE1 
831  C CE2 . TRP A 113 ? 0.7126 0.8590 0.8321 0.0497  -0.0752 -0.0547 409 TRP A CE2 
832  C CE3 . TRP A 113 ? 0.6289 0.8235 0.7662 0.0414  -0.0786 -0.0595 409 TRP A CE3 
833  C CZ2 . TRP A 113 ? 0.7326 0.8637 0.8182 0.0796  -0.0780 -0.0526 409 TRP A CZ2 
834  C CZ3 . TRP A 113 ? 0.6916 0.8779 0.8002 0.0719  -0.0815 -0.0568 409 TRP A CZ3 
835  C CH2 . TRP A 113 ? 0.7527 0.9036 0.8327 0.0919  -0.0811 -0.0534 409 TRP A CH2 
836  N N   . ARG A 114 ? 0.5920 0.8302 0.7870 -0.0478 -0.0657 -0.0664 410 ARG A N   
837  C CA  . ARG A 114 ? 0.5825 0.8607 0.7836 -0.0541 -0.0631 -0.0657 410 ARG A CA  
838  C C   . ARG A 114 ? 0.6643 0.9097 0.8619 -0.0681 -0.0589 -0.0633 410 ARG A C   
839  O O   . ARG A 114 ? 0.6201 0.8845 0.8201 -0.0645 -0.0560 -0.0608 410 ARG A O   
840  C CB  . ARG A 114 ? 0.5817 0.9128 0.7881 -0.0777 -0.0642 -0.0696 410 ARG A CB  
841  C CG  . ARG A 114 ? 0.5705 0.9631 0.7849 -0.0857 -0.0615 -0.0683 410 ARG A CG  
842  C CD  . ARG A 114 ? 0.6160 1.0634 0.8327 -0.1195 -0.0632 -0.0720 410 ARG A CD  
843  N NE  . ARG A 114 ? 0.6721 1.2053 0.9010 -0.1193 -0.0611 -0.0699 410 ARG A NE  
844  C CZ  . ARG A 114 ? 0.6192 1.2277 0.8535 -0.1490 -0.0624 -0.0718 410 ARG A CZ  
845  N NH1 . ARG A 114 ? 0.4424 1.1390 0.6896 -0.1447 -0.0596 -0.0690 410 ARG A NH1 
846  N NH2 . ARG A 114 ? 0.6756 1.2745 0.8996 -0.1836 -0.0663 -0.0765 410 ARG A NH2 
847  N N   . ASN A 115 ? 0.6608 0.8579 0.8498 -0.0807 -0.0582 -0.0640 411 ASN A N   
848  C CA  . ASN A 115 ? 0.6312 0.7928 0.8109 -0.0913 -0.0547 -0.0615 411 ASN A CA  
849  C C   . ASN A 115 ? 0.6297 0.7562 0.8089 -0.0727 -0.0549 -0.0577 411 ASN A C   
850  O O   . ASN A 115 ? 0.6898 0.7888 0.8610 -0.0764 -0.0526 -0.0550 411 ASN A O   
851  C CB  . ASN A 115 ? 0.5600 0.6871 0.7202 -0.1136 -0.0538 -0.0645 411 ASN A CB  
852  C CG  . ASN A 115 ? 0.7258 0.8838 0.8793 -0.1426 -0.0541 -0.0683 411 ASN A CG  
853  O OD1 . ASN A 115 ? 0.8069 1.0193 0.9728 -0.1489 -0.0534 -0.0672 411 ASN A OD1 
854  N ND2 . ASN A 115 ? 0.8083 0.9342 0.9386 -0.1609 -0.0552 -0.0727 411 ASN A ND2 
855  N N   . ALA A 116 ? 0.5839 0.7104 0.7673 -0.0551 -0.0578 -0.0570 412 ALA A N   
856  C CA  . ALA A 116 ? 0.6226 0.7221 0.8027 -0.0442 -0.0588 -0.0532 412 ALA A CA  
857  C C   . ALA A 116 ? 0.6196 0.7207 0.7973 -0.0386 -0.0578 -0.0504 412 ALA A C   
858  O O   . ALA A 116 ? 0.5095 0.6199 0.6821 -0.0251 -0.0592 -0.0501 412 ALA A O   
859  C CB  . ALA A 116 ? 0.5804 0.6761 0.7571 -0.0330 -0.0622 -0.0527 412 ALA A CB  
860  N N   . SER A 117 ? 0.6459 0.7341 0.8217 -0.0462 -0.0554 -0.0484 413 SER A N   
861  C CA  . SER A 117 ? 0.6577 0.7520 0.8307 -0.0430 -0.0536 -0.0462 413 SER A CA  
862  C C   . SER A 117 ? 0.6068 0.6841 0.7710 -0.0298 -0.0567 -0.0440 413 SER A C   
863  O O   . SER A 117 ? 0.5573 0.6388 0.7138 -0.0215 -0.0559 -0.0434 413 SER A O   
864  C CB  . SER A 117 ? 0.5570 0.6362 0.7248 -0.0552 -0.0503 -0.0439 413 SER A CB  
865  O OG  . SER A 117 ? 0.5921 0.6437 0.7550 -0.0507 -0.0521 -0.0413 413 SER A OG  
866  N N   . ARG A 118 ? 0.5392 0.5979 0.7002 -0.0294 -0.0602 -0.0428 414 ARG A N   
867  C CA  . ARG A 118 ? 0.4929 0.5312 0.6377 -0.0248 -0.0641 -0.0408 414 ARG A CA  
868  C C   . ARG A 118 ? 0.5725 0.6015 0.7000 -0.0143 -0.0665 -0.0423 414 ARG A C   
869  O O   . ARG A 118 ? 0.4150 0.4147 0.5175 -0.0135 -0.0702 -0.0408 414 ARG A O   
870  C CB  . ARG A 118 ? 0.5387 0.5694 0.6851 -0.0339 -0.0669 -0.0379 414 ARG A CB  
871  C CG  . ARG A 118 ? 0.5960 0.6316 0.7508 -0.0371 -0.0654 -0.0355 414 ARG A CG  
872  C CD  . ARG A 118 ? 0.5877 0.6313 0.7451 -0.0413 -0.0682 -0.0322 414 ARG A CD  
873  N NE  . ARG A 118 ? 0.5544 0.6022 0.7122 -0.0391 -0.0684 -0.0291 414 ARG A NE  
874  C CZ  . ARG A 118 ? 0.6166 0.6834 0.7778 -0.0378 -0.0704 -0.0255 414 ARG A CZ  
875  N NH1 . ARG A 118 ? 0.6275 0.7136 0.7937 -0.0411 -0.0717 -0.0246 414 ARG A NH1 
876  N NH2 . ARG A 118 ? 0.6338 0.7055 0.7924 -0.0317 -0.0710 -0.0223 414 ARG A NH2 
877  N N   . CYS A 119 ? 0.5506 0.6007 0.6855 -0.0074 -0.0652 -0.0450 415 CYS A N   
878  C CA  . CYS A 119 ? 0.5440 0.5850 0.6582 0.0079  -0.0677 -0.0458 415 CYS A CA  
879  C C   . CYS A 119 ? 0.5814 0.6317 0.6798 0.0303  -0.0665 -0.0471 415 CYS A C   
880  O O   . CYS A 119 ? 0.6317 0.7261 0.7491 0.0331  -0.0629 -0.0488 415 CYS A O   
881  C CB  . CYS A 119 ? 0.4721 0.5369 0.6001 0.0075  -0.0676 -0.0479 415 CYS A CB  
882  S SG  . CYS A 119 ? 0.5017 0.5477 0.5960 0.0306  -0.0713 -0.0476 415 CYS A SG  
883  N N   . VAL A 120 ? 0.6505 0.6594 0.7089 0.0462  -0.0693 -0.0463 416 VAL A N   
884  C CA  . VAL A 120 ? 0.6961 0.7085 0.7298 0.0757  -0.0680 -0.0477 416 VAL A CA  
885  C C   . VAL A 120 ? 0.7546 0.7856 0.7750 0.1032  -0.0687 -0.0489 416 VAL A C   
886  O O   . VAL A 120 ? 0.6708 0.7314 0.6810 0.1323  -0.0664 -0.0502 416 VAL A O   
887  C CB  . VAL A 120 ? 0.7371 0.6842 0.7214 0.0825  -0.0708 -0.0468 416 VAL A CB  
888  C CG1 . VAL A 120 ? 0.8097 0.6950 0.7498 0.0809  -0.0761 -0.0452 416 VAL A CG1 
889  C CG2 . VAL A 120 ? 0.6906 0.6412 0.6471 0.1169  -0.0682 -0.0488 416 VAL A CG2 
890  N N   . GLY A 121 ? 0.7487 0.7711 0.7699 0.0967  -0.0715 -0.0482 417 GLY A N   
891  C CA  . GLY A 121 ? 0.7348 0.7712 0.7384 0.1248  -0.0732 -0.0488 417 GLY A CA  
892  C C   . GLY A 121 ? 0.6563 0.7702 0.7038 0.1205  -0.0716 -0.0510 417 GLY A C   
893  O O   . GLY A 121 ? 0.7529 0.8832 0.7934 0.1359  -0.0741 -0.0513 417 GLY A O   
894  N N   . ARG A 122 ? 0.6081 0.7676 0.6953 0.0985  -0.0679 -0.0524 418 ARG A N   
895  C CA  . ARG A 122 ? 0.5902 0.8108 0.7144 0.0801  -0.0671 -0.0548 418 ARG A CA  
896  C C   . ARG A 122 ? 0.6210 0.9145 0.7499 0.1022  -0.0669 -0.0562 418 ARG A C   
897  O O   . ARG A 122 ? 0.6728 1.0197 0.8268 0.0849  -0.0675 -0.0585 418 ARG A O   
898  C CB  . ARG A 122 ? 0.3466 0.5820 0.4992 0.0479  -0.0632 -0.0554 418 ARG A CB  
899  C CG  . ARG A 122 ? 0.6343 0.8191 0.7905 0.0249  -0.0636 -0.0544 418 ARG A CG  
900  C CD  . ARG A 122 ? 0.6012 0.7976 0.7764 -0.0011 -0.0600 -0.0548 418 ARG A CD  
901  N NE  . ARG A 122 ? 0.5760 0.7590 0.7452 0.0021  -0.0574 -0.0524 418 ARG A NE  
902  C CZ  . ARG A 122 ? 0.4994 0.6931 0.6777 -0.0152 -0.0535 -0.0516 418 ARG A CZ  
903  N NH1 . ARG A 122 ? 0.4720 0.6847 0.6608 -0.0390 -0.0518 -0.0531 418 ARG A NH1 
904  N NH2 . ARG A 122 ? 0.5760 0.7554 0.7465 -0.0100 -0.0516 -0.0491 418 ARG A NH2 
905  N N   . ILE A 123 ? 0.6286 0.9272 0.7300 0.1405  -0.0664 -0.0551 419 ILE A N   
906  C CA  . ILE A 123 ? 0.5795 0.9593 0.6834 0.1693  -0.0662 -0.0559 419 ILE A CA  
907  C C   . ILE A 123 ? 0.6778 1.0749 0.7811 0.1759  -0.0714 -0.0567 419 ILE A C   
908  O O   . ILE A 123 ? 0.5726 1.0549 0.6912 0.1859  -0.0725 -0.0578 419 ILE A O   
909  C CB  . ILE A 123 ? 0.6135 0.9786 0.6745 0.2196  -0.0648 -0.0545 419 ILE A CB  
910  C CG1 . ILE A 123 ? 0.6515 1.1190 0.7181 0.2541  -0.0635 -0.0548 419 ILE A CG1 
911  C CG2 . ILE A 123 ? 0.5991 0.8652 0.6034 0.2456  -0.0693 -0.0529 419 ILE A CG2 
912  C CD1 . ILE A 123 ? 0.7455 1.1922 0.7580 0.3158  -0.0626 -0.0537 419 ILE A CD1 
913  N N   . GLN A 124 ? 0.7476 1.0702 0.8347 0.1665  -0.0747 -0.0559 420 GLN A N   
914  C CA  . GLN A 124 ? 0.7986 1.1191 0.8771 0.1736  -0.0795 -0.0560 420 GLN A CA  
915  C C   . GLN A 124 ? 0.7479 1.0887 0.8634 0.1311  -0.0804 -0.0588 420 GLN A C   
916  O O   . GLN A 124 ? 0.6767 1.0112 0.7863 0.1323  -0.0842 -0.0592 420 GLN A O   
917  C CB  . GLN A 124 ? 0.9246 1.1472 0.9542 0.1885  -0.0820 -0.0526 420 GLN A CB  
918  C CG  . GLN A 124 ? 1.1186 1.3112 1.0912 0.2403  -0.0835 -0.0501 420 GLN A CG  
919  C CD  . GLN A 124 ? 1.2911 1.5100 1.2429 0.2743  -0.0879 -0.0492 420 GLN A CD  
920  O OE1 . GLN A 124 ? 1.2718 1.5638 1.2624 0.2618  -0.0896 -0.0513 420 GLN A OE1 
921  N NE2 . GLN A 124 ? 1.4305 1.5846 1.3145 0.3172  -0.0903 -0.0459 420 GLN A NE2 
922  N N   . TRP A 125 ? 0.6440 1.0034 0.7907 0.0954  -0.0769 -0.0609 421 TRP A N   
923  C CA  . TRP A 125 ? 0.6155 0.9623 0.7820 0.0572  -0.0772 -0.0636 421 TRP A CA  
924  C C   . TRP A 125 ? 0.6382 1.0358 0.8143 0.0509  -0.0813 -0.0670 421 TRP A C   
925  O O   . TRP A 125 ? 0.6468 1.0159 0.8231 0.0349  -0.0830 -0.0689 421 TRP A O   
926  C CB  . TRP A 125 ? 0.5246 0.8798 0.7115 0.0244  -0.0728 -0.0649 421 TRP A CB  
927  C CG  . TRP A 125 ? 0.5877 1.0239 0.7907 0.0146  -0.0719 -0.0667 421 TRP A CG  
928  C CD1 . TRP A 125 ? 0.6192 1.1035 0.8241 0.0312  -0.0691 -0.0647 421 TRP A CD1 
929  C CD2 . TRP A 125 ? 0.5769 1.0622 0.7934 -0.0159 -0.0739 -0.0707 421 TRP A CD2 
930  N NE1 . TRP A 125 ? 0.6921 1.2611 0.9149 0.0107  -0.0688 -0.0666 421 TRP A NE1 
931  C CE2 . TRP A 125 ? 0.6542 1.2229 0.8826 -0.0209 -0.0723 -0.0704 421 TRP A CE2 
932  C CE3 . TRP A 125 ? 0.5305 0.9967 0.7463 -0.0411 -0.0769 -0.0748 421 TRP A CE3 
933  C CZ2 . TRP A 125 ? 0.5845 1.2193 0.8239 -0.0558 -0.0742 -0.0737 421 TRP A CZ2 
934  C CZ3 . TRP A 125 ? 0.5228 1.0446 0.7454 -0.0731 -0.0790 -0.0788 421 TRP A CZ3 
935  C CH2 . TRP A 125 ? 0.6083 1.2143 0.8425 -0.0829 -0.0780 -0.0781 421 TRP A CH2 
936  N N   . SER A 126 ? 0.6851 1.1633 0.8686 0.0636  -0.0829 -0.0679 422 SER A N   
937  C CA  . SER A 126 ? 0.7670 1.3023 0.9598 0.0544  -0.0880 -0.0714 422 SER A CA  
938  C C   . SER A 126 ? 0.8160 1.3289 0.9860 0.0868  -0.0928 -0.0698 422 SER A C   
939  O O   . SER A 126 ? 0.8830 1.4188 1.0571 0.0759  -0.0973 -0.0728 422 SER A O   
940  C CB  . SER A 126 ? 0.7682 1.4121 0.9771 0.0558  -0.0887 -0.0722 422 SER A CB  
941  O OG  . SER A 126 ? 0.7782 1.4608 0.9716 0.1082  -0.0908 -0.0691 422 SER A OG  
942  N N   . LYS A 127 ? 0.7906 1.2546 0.9303 0.1254  -0.0924 -0.0650 423 LYS A N   
943  C CA  . LYS A 127 ? 0.7297 1.1540 0.8363 0.1543  -0.0965 -0.0623 423 LYS A CA  
944  C C   . LYS A 127 ? 0.7392 1.0744 0.8356 0.1326  -0.0949 -0.0608 423 LYS A C   
945  O O   . LYS A 127 ? 0.7928 1.0578 0.8597 0.1438  -0.0932 -0.0566 423 LYS A O   
946  C CB  . LYS A 127 ? 0.7780 1.1869 0.8434 0.2072  -0.0972 -0.0577 423 LYS A CB  
947  C CG  . LYS A 127 ? 0.9367 1.4225 0.9922 0.2477  -0.1019 -0.0573 423 LYS A CG  
948  C CD  . LYS A 127 ? 1.0343 1.4581 1.0256 0.3032  -0.1044 -0.0519 423 LYS A CD  
949  C CE  . LYS A 127 ? 1.1249 1.6203 1.1031 0.3451  -0.1104 -0.0510 423 LYS A CE  
950  N NZ  . LYS A 127 ? 1.1207 1.6272 1.1129 0.3219  -0.1153 -0.0526 423 LYS A NZ  
951  N N   . LEU A 128 ? 0.6749 1.0156 0.7929 0.0998  -0.0953 -0.0646 424 LEU A N   
952  C CA  . LEU A 128 ? 0.6553 0.9290 0.7680 0.0797  -0.0931 -0.0635 424 LEU A CA  
953  C C   . LEU A 128 ? 0.6744 0.9549 0.7858 0.0728  -0.0963 -0.0658 424 LEU A C   
954  O O   . LEU A 128 ? 0.7385 1.0710 0.8689 0.0580  -0.0988 -0.0714 424 LEU A O   
955  C CB  . LEU A 128 ? 0.4493 0.7120 0.5867 0.0467  -0.0883 -0.0661 424 LEU A CB  
956  C CG  . LEU A 128 ? 0.4993 0.7097 0.6360 0.0273  -0.0854 -0.0654 424 LEU A CG  
957  C CD1 . LEU A 128 ? 0.4575 0.6140 0.5732 0.0356  -0.0837 -0.0591 424 LEU A CD1 
958  C CD2 . LEU A 128 ? 0.5388 0.7507 0.6960 -0.0005 -0.0819 -0.0696 424 LEU A CD2 
959  N N   . GLN A 129 ? 0.7375 0.9654 0.8229 0.0806  -0.0964 -0.0614 425 GLN A N   
960  C CA  . GLN A 129 ? 0.7638 0.9938 0.8429 0.0774  -0.0990 -0.0627 425 GLN A CA  
961  C C   . GLN A 129 ? 0.7159 0.9206 0.8094 0.0472  -0.0947 -0.0651 425 GLN A C   
962  O O   . GLN A 129 ? 0.6562 0.8148 0.7402 0.0411  -0.0907 -0.0606 425 GLN A O   
963  C CB  . GLN A 129 ? 0.8497 1.0371 0.8856 0.1038  -0.1012 -0.0556 425 GLN A CB  
964  C CG  . GLN A 129 ? 0.8431 1.0327 0.8689 0.1030  -0.1039 -0.0560 425 GLN A CG  
965  C CD  . GLN A 129 ? 0.8287 1.0914 0.8771 0.1026  -0.1090 -0.0630 425 GLN A CD  
966  O OE1 . GLN A 129 ? 0.8552 1.1699 0.9089 0.1208  -0.1127 -0.0642 425 GLN A OE1 
967  N NE2 . GLN A 129 ? 0.8182 1.0889 0.8780 0.0807  -0.1092 -0.0680 425 GLN A NE2 
968  N N   . VAL A 130 ? 0.7190 0.9550 0.8310 0.0285  -0.0957 -0.0724 426 VAL A N   
969  C CA  . VAL A 130 ? 0.6950 0.9062 0.8142 0.0059  -0.0913 -0.0757 426 VAL A CA  
970  C C   . VAL A 130 ? 0.7055 0.9042 0.8099 0.0079  -0.0919 -0.0757 426 VAL A C   
971  O O   . VAL A 130 ? 0.6914 0.9180 0.7906 0.0121  -0.0970 -0.0791 426 VAL A O   
972  C CB  . VAL A 130 ? 0.6384 0.8732 0.7727 -0.0171 -0.0916 -0.0840 426 VAL A CB  
973  C CG1 . VAL A 130 ? 0.5249 0.7220 0.6563 -0.0328 -0.0865 -0.0872 426 VAL A CG1 
974  C CG2 . VAL A 130 ? 0.5618 0.8186 0.7094 -0.0189 -0.0911 -0.0830 426 VAL A CG2 
975  N N   . PHE A 131 ? 0.6961 0.8591 0.7933 0.0048  -0.0867 -0.0715 427 PHE A N   
976  C CA  . PHE A 131 ? 0.7097 0.8624 0.7927 0.0051  -0.0856 -0.0708 427 PHE A CA  
977  C C   . PHE A 131 ? 0.6857 0.8339 0.7763 -0.0086 -0.0810 -0.0771 427 PHE A C   
978  O O   . PHE A 131 ? 0.6544 0.7876 0.7514 -0.0132 -0.0755 -0.0751 427 PHE A O   
979  C CB  . PHE A 131 ? 0.6032 0.7246 0.6665 0.0099  -0.0827 -0.0606 427 PHE A CB  
980  C CG  . PHE A 131 ? 0.6367 0.7458 0.6738 0.0278  -0.0875 -0.0546 427 PHE A CG  
981  C CD1 . PHE A 131 ? 0.6538 0.7763 0.6754 0.0415  -0.0924 -0.0555 427 PHE A CD1 
982  C CD2 . PHE A 131 ? 0.6371 0.7163 0.6579 0.0335  -0.0873 -0.0479 427 PHE A CD2 
983  C CE1 . PHE A 131 ? 0.6661 0.7723 0.6551 0.0649  -0.0969 -0.0494 427 PHE A CE1 
984  C CE2 . PHE A 131 ? 0.6789 0.7344 0.6628 0.0555  -0.0916 -0.0424 427 PHE A CE2 
985  C CZ  . PHE A 131 ? 0.7456 0.8142 0.7129 0.0733  -0.0963 -0.0428 427 PHE A CZ  
986  N N   . ASP A 132 ? 0.7222 0.8821 0.8070 -0.0129 -0.0837 -0.0848 428 ASP A N   
987  C CA  . ASP A 132 ? 0.6051 0.7503 0.6844 -0.0219 -0.0799 -0.0922 428 ASP A CA  
988  C C   . ASP A 132 ? 0.6692 0.8034 0.7374 -0.0142 -0.0742 -0.0884 428 ASP A C   
989  O O   . ASP A 132 ? 0.7455 0.8862 0.8012 -0.0101 -0.0762 -0.0886 428 ASP A O   
990  C CB  . ASP A 132 ? 0.5257 0.6825 0.5949 -0.0335 -0.0857 -0.1026 428 ASP A CB  
991  C CG  . ASP A 132 ? 0.5933 0.7189 0.6438 -0.0426 -0.0822 -0.1113 428 ASP A CG  
992  O OD1 . ASP A 132 ? 0.6869 0.8106 0.7228 -0.0598 -0.0869 -0.1204 428 ASP A OD1 
993  O OD2 . ASP A 132 ? 0.6124 0.7152 0.6582 -0.0323 -0.0747 -0.1088 428 ASP A OD2 
994  N N   . ALA A 133 ? 0.6812 0.8052 0.7539 -0.0120 -0.0672 -0.0843 429 ALA A N   
995  C CA  . ALA A 133 ? 0.6307 0.7571 0.6945 -0.0059 -0.0607 -0.0806 429 ALA A CA  
996  C C   . ALA A 133 ? 0.6522 0.7687 0.7062 0.0007  -0.0553 -0.0879 429 ALA A C   
997  O O   . ALA A 133 ? 0.7202 0.8471 0.7721 0.0097  -0.0481 -0.0842 429 ALA A O   
998  C CB  . ALA A 133 ? 0.6380 0.7713 0.7097 -0.0081 -0.0566 -0.0689 429 ALA A CB  
999  N N   . ARG A 134 ? 0.5884 0.6845 0.6309 -0.0036 -0.0589 -0.0983 430 ARG A N   
1000 C CA  . ARG A 134 ? 0.6360 0.7057 0.6543 0.0056  -0.0542 -0.1060 430 ARG A CA  
1001 C C   . ARG A 134 ? 0.7111 0.7786 0.7051 0.0165  -0.0510 -0.1104 430 ARG A C   
1002 O O   . ARG A 134 ? 0.7449 0.7888 0.7125 0.0316  -0.0457 -0.1161 430 ARG A O   
1003 C CB  . ARG A 134 ? 0.6336 0.6701 0.6347 -0.0079 -0.0591 -0.1155 430 ARG A CB  
1004 C CG  . ARG A 134 ? 0.6579 0.6919 0.6774 -0.0142 -0.0594 -0.1112 430 ARG A CG  
1005 C CD  . ARG A 134 ? 0.6722 0.6774 0.6723 -0.0345 -0.0643 -0.1197 430 ARG A CD  
1006 N NE  . ARG A 134 ? 0.7481 0.7769 0.7519 -0.0532 -0.0723 -0.1236 430 ARG A NE  
1007 C CZ  . ARG A 134 ? 0.7899 0.8037 0.7706 -0.0773 -0.0778 -0.1325 430 ARG A CZ  
1008 N NH1 . ARG A 134 ? 0.6822 0.6432 0.6272 -0.0866 -0.0759 -0.1383 430 ARG A NH1 
1009 N NH2 . ARG A 134 ? 0.8639 0.9152 0.8520 -0.0926 -0.0855 -0.1352 430 ARG A NH2 
1010 N N   . ASP A 135 ? 0.6679 0.7564 0.6651 0.0127  -0.0539 -0.1079 431 ASP A N   
1011 C CA  . ASP A 135 ? 0.7815 0.8735 0.7575 0.0241  -0.0496 -0.1102 431 ASP A CA  
1012 C C   . ASP A 135 ? 0.7786 0.9027 0.7658 0.0353  -0.0406 -0.0992 431 ASP A C   
1013 O O   . ASP A 135 ? 0.8058 0.9420 0.7779 0.0450  -0.0356 -0.0992 431 ASP A O   
1014 C CB  . ASP A 135 ? 0.7535 0.8533 0.7227 0.0149  -0.0571 -0.1126 431 ASP A CB  
1015 C CG  . ASP A 135 ? 0.8092 0.9345 0.8001 0.0094  -0.0604 -0.1008 431 ASP A CG  
1016 O OD1 . ASP A 135 ? 0.7772 0.9116 0.7593 0.0085  -0.0653 -0.1000 431 ASP A OD1 
1017 O OD2 . ASP A 135 ? 0.7306 0.8621 0.7413 0.0073  -0.0586 -0.0923 431 ASP A OD2 
1018 N N   . CYS A 136 ? 0.6981 0.8390 0.7093 0.0320  -0.0382 -0.0900 432 CYS A N   
1019 C CA  . CYS A 136 ? 0.7107 0.8896 0.7326 0.0339  -0.0306 -0.0785 432 CYS A CA  
1020 C C   . CYS A 136 ? 0.7798 0.9765 0.7917 0.0567  -0.0213 -0.0809 432 CYS A C   
1021 O O   . CYS A 136 ? 0.8334 1.0045 0.8331 0.0718  -0.0207 -0.0889 432 CYS A O   
1022 C CB  . CYS A 136 ? 0.6800 0.8687 0.7254 0.0198  -0.0324 -0.0689 432 CYS A CB  
1023 S SG  . CYS A 136 ? 0.7050 0.9384 0.7575 0.0065  -0.0259 -0.0532 432 CYS A SG  
1024 N N   . THR A 137 ? 0.7437 0.9838 0.7550 0.0606  -0.0136 -0.0736 433 THR A N   
1025 C CA  . THR A 137 ? 0.6740 0.9452 0.6747 0.0881  -0.0036 -0.0749 433 THR A CA  
1026 C C   . THR A 137 ? 0.7270 1.0702 0.7476 0.0835  0.0042  -0.0614 433 THR A C   
1027 O O   . THR A 137 ? 0.6974 1.0798 0.7152 0.1096  0.0122  -0.0613 433 THR A O   
1028 C CB  . THR A 137 ? 0.8017 1.0636 0.7711 0.1052  0.0001  -0.0828 433 THR A CB  
1029 O OG1 . THR A 137 ? 0.7338 1.0277 0.7074 0.0887  0.0021  -0.0743 433 THR A OG1 
1030 C CG2 . THR A 137 ? 0.8316 1.0267 0.7772 0.1032  -0.0086 -0.0964 433 THR A CG2 
1031 N N   . THR A 138 ? 0.7604 1.1224 0.7959 0.0513  0.0021  -0.0500 434 THR A N   
1032 C CA  . THR A 138 ? 0.7097 1.1411 0.7569 0.0364  0.0092  -0.0366 434 THR A CA  
1033 C C   . THR A 138 ? 0.6621 1.0875 0.7241 0.0028  0.0033  -0.0271 434 THR A C   
1034 O O   . THR A 138 ? 0.6590 1.0271 0.7185 -0.0091 -0.0056 -0.0295 434 THR A O   
1035 C CB  . THR A 138 ? 0.7123 1.1682 0.7439 0.0252  0.0145  -0.0307 434 THR A CB  
1036 O OG1 . THR A 138 ? 0.7874 1.1829 0.8041 0.0107  0.0065  -0.0328 434 THR A OG1 
1037 C CG2 . THR A 138 ? 0.7169 1.1995 0.7336 0.0605  0.0232  -0.0380 434 THR A CG2 
1038 N N   . ALA A 139 ? 0.6463 1.1352 0.7208 -0.0123 0.0081  -0.0165 435 ALA A N   
1039 C CA  . ALA A 139 ? 0.7124 1.1930 0.7919 -0.0489 0.0026  -0.0072 435 ALA A CA  
1040 C C   . ALA A 139 ? 0.7278 1.1617 0.7821 -0.0793 -0.0016 -0.0011 435 ALA A C   
1041 O O   . ALA A 139 ? 0.7785 1.1615 0.8245 -0.0979 -0.0093 0.0012  435 ALA A O   
1042 C CB  . ALA A 139 ? 0.7599 1.3257 0.8526 -0.0658 0.0085  0.0036  435 ALA A CB  
1043 N N   . HIS A 140 ? 0.7364 1.1831 0.7731 -0.0815 0.0036  0.0016  436 HIS A N   
1044 C CA  . HIS A 140 ? 0.6462 1.0397 0.6510 -0.1047 -0.0007 0.0073  436 HIS A CA  
1045 C C   . HIS A 140 ? 0.5925 0.9123 0.5914 -0.0867 -0.0103 -0.0024 436 HIS A C   
1046 O O   . HIS A 140 ? 0.6114 0.8770 0.5870 -0.1017 -0.0171 0.0020  436 HIS A O   
1047 C CB  . HIS A 140 ? 0.7794 1.2013 0.7658 -0.1065 0.0069  0.0113  436 HIS A CB  
1048 C CG  . HIS A 140 ? 0.8141 1.2964 0.7912 -0.1423 0.0148  0.0259  436 HIS A CG  
1049 N ND1 . HIS A 140 ? 0.8058 1.3803 0.8085 -0.1397 0.0231  0.0287  436 HIS A ND1 
1050 C CD2 . HIS A 140 ? 0.8288 1.2944 0.7695 -0.1830 0.0155  0.0390  436 HIS A CD2 
1051 C CE1 . HIS A 140 ? 0.8440 1.4662 0.8313 -0.1809 0.0287  0.0429  436 HIS A CE1 
1052 N NE2 . HIS A 140 ? 0.8551 1.4067 0.8020 -0.2102 0.0243  0.0495  436 HIS A NE2 
1053 N N   . GLY A 141 ? 0.5829 0.8999 0.5971 -0.0545 -0.0109 -0.0155 437 GLY A N   
1054 C CA  . GLY A 141 ? 0.6701 0.9314 0.6822 -0.0421 -0.0203 -0.0246 437 GLY A CA  
1055 C C   . GLY A 141 ? 0.7162 0.9533 0.7406 -0.0490 -0.0265 -0.0242 437 GLY A C   
1056 O O   . GLY A 141 ? 0.7693 0.9628 0.7825 -0.0519 -0.0342 -0.0242 437 GLY A O   
1057 N N   . MET A 142 ? 0.7309 0.9997 0.7764 -0.0490 -0.0230 -0.0234 438 MET A N   
1058 C CA  . MET A 142 ? 0.6105 0.8601 0.6663 -0.0577 -0.0283 -0.0219 438 MET A CA  
1059 C C   . MET A 142 ? 0.5922 0.8106 0.6234 -0.0850 -0.0323 -0.0116 438 MET A C   
1060 O O   . MET A 142 ? 0.6208 0.7907 0.6406 -0.0830 -0.0395 -0.0132 438 MET A O   
1061 C CB  . MET A 142 ? 0.5708 0.8686 0.6486 -0.0553 -0.0233 -0.0203 438 MET A CB  
1062 C CG  . MET A 142 ? 0.5254 0.8266 0.6166 -0.0242 -0.0217 -0.0314 438 MET A CG  
1063 S SD  . MET A 142 ? 0.6573 1.0161 0.7678 -0.0134 -0.0161 -0.0285 438 MET A SD  
1064 C CE  . MET A 142 ? 0.7116 1.0332 0.8336 -0.0245 -0.0242 -0.0286 438 MET A CE  
1065 N N   . PHE A 143 ? 0.6145 0.8583 0.6303 -0.1103 -0.0274 -0.0007 439 PHE A N   
1066 C CA  . PHE A 143 ? 0.7149 0.9154 0.6916 -0.1404 -0.0310 0.0098  439 PHE A CA  
1067 C C   . PHE A 143 ? 0.8001 0.9348 0.7467 -0.1277 -0.0374 0.0076  439 PHE A C   
1068 O O   . PHE A 143 ? 0.8082 0.8873 0.7295 -0.1309 -0.0440 0.0097  439 PHE A O   
1069 C CB  . PHE A 143 ? 0.7983 1.0363 0.7559 -0.1711 -0.0239 0.0212  439 PHE A CB  
1070 C CG  . PHE A 143 ? 0.9040 1.0831 0.8061 -0.2050 -0.0272 0.0324  439 PHE A CG  
1071 C CD1 . PHE A 143 ? 0.9790 1.1333 0.8431 -0.2121 -0.0252 0.0382  439 PHE A CD1 
1072 C CD2 . PHE A 143 ? 0.8000 0.9396 0.6800 -0.2285 -0.0325 0.0370  439 PHE A CD2 
1073 C CE1 . PHE A 143 ? 1.0516 1.1378 0.8523 -0.2426 -0.0283 0.0490  439 PHE A CE1 
1074 C CE2 . PHE A 143 ? 0.9528 1.0231 0.7681 -0.2596 -0.0357 0.0470  439 PHE A CE2 
1075 C CZ  . PHE A 143 ? 1.0564 1.0966 0.8295 -0.2665 -0.0336 0.0534  439 PHE A CZ  
1076 N N   . ASN A 144 ? 0.7742 0.9172 0.7219 -0.1092 -0.0358 0.0029  440 ASN A N   
1077 C CA  . ASN A 144 ? 0.7433 0.8361 0.6627 -0.0947 -0.0422 0.0013  440 ASN A CA  
1078 C C   . ASN A 144 ? 0.7470 0.8184 0.6826 -0.0712 -0.0500 -0.0082 440 ASN A C   
1079 O O   . ASN A 144 ? 0.7981 0.8239 0.7049 -0.0625 -0.0566 -0.0064 440 ASN A O   
1080 C CB  . ASN A 144 ? 0.7819 0.8967 0.7009 -0.0820 -0.0389 -0.0023 440 ASN A CB  
1081 C CG  . ASN A 144 ? 0.8060 0.8765 0.6920 -0.0682 -0.0457 -0.0022 440 ASN A CG  
1082 O OD1 . ASN A 144 ? 0.7754 0.7998 0.6154 -0.0797 -0.0478 0.0080  440 ASN A OD1 
1083 N ND2 . ASN A 144 ? 0.7184 0.7998 0.6221 -0.0436 -0.0499 -0.0135 440 ASN A ND2 
1084 N N   . TYR A 145 ? 0.7071 0.8108 0.6838 -0.0590 -0.0491 -0.0180 441 TYR A N   
1085 C CA  . TYR A 145 ? 0.7967 0.8856 0.7881 -0.0434 -0.0558 -0.0258 441 TYR A CA  
1086 C C   . TYR A 145 ? 0.7785 0.8381 0.7595 -0.0523 -0.0589 -0.0202 441 TYR A C   
1087 O O   . TYR A 145 ? 0.7694 0.7997 0.7373 -0.0395 -0.0652 -0.0215 441 TYR A O   
1088 C CB  . TYR A 145 ? 0.7552 0.8748 0.7827 -0.0335 -0.0538 -0.0364 441 TYR A CB  
1089 C CG  . TYR A 145 ? 0.6793 0.8062 0.7095 -0.0193 -0.0559 -0.0465 441 TYR A CG  
1090 C CD1 . TYR A 145 ? 0.6654 0.8133 0.6990 -0.0148 -0.0502 -0.0513 441 TYR A CD1 
1091 C CD2 . TYR A 145 ? 0.5888 0.7044 0.6146 -0.0100 -0.0638 -0.0513 441 TYR A CD2 
1092 C CE1 . TYR A 145 ? 0.5863 0.7337 0.6150 -0.0049 -0.0528 -0.0613 441 TYR A CE1 
1093 C CE2 . TYR A 145 ? 0.5906 0.7172 0.6167 -0.0026 -0.0668 -0.0608 441 TYR A CE2 
1094 C CZ  . TYR A 145 ? 0.6364 0.7736 0.6617 -0.0019 -0.0614 -0.0661 441 TYR A CZ  
1095 O OH  . TYR A 145 ? 0.6199 0.7605 0.6376 0.0026  -0.0649 -0.0763 441 TYR A OH  
1096 N N   . ILE A 146 ? 0.7025 0.7736 0.6872 -0.0730 -0.0546 -0.0142 442 ILE A N   
1097 C CA  . ILE A 146 ? 0.7746 0.8153 0.7451 -0.0849 -0.0577 -0.0094 442 ILE A CA  
1098 C C   . ILE A 146 ? 0.8710 0.8494 0.7848 -0.0904 -0.0619 -0.0016 442 ILE A C   
1099 O O   . ILE A 146 ? 0.7889 0.7244 0.6813 -0.0815 -0.0672 -0.0016 442 ILE A O   
1100 C CB  . ILE A 146 ? 0.6830 0.7580 0.6669 -0.1096 -0.0528 -0.0042 442 ILE A CB  
1101 C CG1 . ILE A 146 ? 0.5756 0.7009 0.6073 -0.0948 -0.0494 -0.0122 442 ILE A CG1 
1102 C CG2 . ILE A 146 ? 0.5616 0.5995 0.5197 -0.1298 -0.0565 0.0019  442 ILE A CG2 
1103 C CD1 . ILE A 146 ? 0.5595 0.7285 0.6077 -0.1114 -0.0455 -0.0075 442 ILE A CD1 
1104 N N   . CYS A 147 ? 0.8998 0.8682 0.7826 -0.1022 -0.0594 0.0053  443 CYS A N   
1105 C CA  . CYS A 147 ? 0.8841 0.7811 0.7002 -0.1069 -0.0632 0.0137  443 CYS A CA  
1106 C C   . CYS A 147 ? 0.7944 0.6605 0.5965 -0.0689 -0.0700 0.0085  443 CYS A C   
1107 O O   . CYS A 147 ? 0.8250 0.6279 0.5776 -0.0595 -0.0750 0.0123  443 CYS A O   
1108 C CB  . CYS A 147 ? 0.9466 0.8418 0.7320 -0.1261 -0.0587 0.0221  443 CYS A CB  
1109 S SG  . CYS A 147 ? 0.9454 0.8591 0.7152 -0.1796 -0.0521 0.0335  443 CYS A SG  
1110 N N   . ASN A 148 ? 0.7445 0.6548 0.5840 -0.0464 -0.0705 0.0000  444 ASN A N   
1111 C CA  . ASN A 148 ? 0.8037 0.7043 0.6363 -0.0117 -0.0775 -0.0052 444 ASN A CA  
1112 C C   . ASN A 148 ? 0.8085 0.7109 0.6604 0.0007  -0.0807 -0.0103 444 ASN A C   
1113 O O   . ASN A 148 ? 0.8506 0.7232 0.6732 0.0259  -0.0862 -0.0098 444 ASN A O   
1114 C CB  . ASN A 148 ? 0.8350 0.7883 0.7037 0.0021  -0.0779 -0.0139 444 ASN A CB  
1115 C CG  . ASN A 148 ? 0.8794 0.8308 0.7254 -0.0048 -0.0750 -0.0092 444 ASN A CG  
1116 O OD1 . ASN A 148 ? 0.9177 0.8215 0.7119 -0.0139 -0.0743 0.0013  444 ASN A OD1 
1117 N ND2 . ASN A 148 ? 0.7497 0.7480 0.6287 -0.0012 -0.0735 -0.0173 444 ASN A ND2 
1118 N N   . HIS A 149 ? 0.7831 0.7212 0.6807 -0.0140 -0.0772 -0.0149 445 HIS A N   
1119 C CA  . HIS A 149 ? 0.7639 0.7009 0.6769 -0.0069 -0.0793 -0.0184 445 HIS A CA  
1120 C C   . HIS A 149 ? 0.7485 0.6196 0.6071 -0.0094 -0.0817 -0.0107 445 HIS A C   
1121 O O   . HIS A 149 ? 0.7861 0.6317 0.6216 0.0164  -0.0862 -0.0118 445 HIS A O   
1122 C CB  . HIS A 149 ? 0.7341 0.7116 0.6955 -0.0244 -0.0746 -0.0226 445 HIS A CB  
1123 C CG  . HIS A 149 ? 0.7533 0.7312 0.7313 -0.0195 -0.0763 -0.0259 445 HIS A CG  
1124 N ND1 . HIS A 149 ? 0.6383 0.6558 0.6609 -0.0173 -0.0749 -0.0336 445 HIS A ND1 
1125 C CD2 . HIS A 149 ? 0.7198 0.6583 0.6700 -0.0165 -0.0790 -0.0225 445 HIS A CD2 
1126 C CE1 . HIS A 149 ? 0.6673 0.6758 0.6932 -0.0138 -0.0764 -0.0343 445 HIS A CE1 
1127 N NE2 . HIS A 149 ? 0.7451 0.7076 0.7288 -0.0121 -0.0789 -0.0280 445 HIS A NE2 
1128 N N   . VAL A 150 ? 0.7424 0.5846 0.5736 -0.0403 -0.0787 -0.0027 446 VAL A N   
1129 C CA  . VAL A 150 ? 0.7198 0.4885 0.4894 -0.0496 -0.0814 0.0042  446 VAL A CA  
1130 C C   . VAL A 150 ? 0.9459 0.6512 0.6513 -0.0193 -0.0863 0.0073  446 VAL A C   
1131 O O   . VAL A 150 ? 1.0425 0.7099 0.7186 0.0061  -0.0903 0.0058  446 VAL A O   
1132 C CB  . VAL A 150 ? 0.9083 0.6599 0.6517 -0.0951 -0.0778 0.0132  446 VAL A CB  
1133 C CG1 . VAL A 150 ? 0.9771 0.6321 0.6348 -0.1081 -0.0817 0.0209  446 VAL A CG1 
1134 C CG2 . VAL A 150 ? 0.9009 0.7149 0.7011 -0.1179 -0.0741 0.0106  446 VAL A CG2 
1135 N N   . LYS A 151 ? 0.8697 0.5673 0.5524 -0.0162 -0.0860 0.0112  447 LYS A N   
1136 C CA  . LYS A 151 ? 1.0365 0.6718 0.6515 0.0168  -0.0910 0.0151  447 LYS A CA  
1137 C C   . LYS A 151 ? 1.0515 0.7190 0.6894 0.0649  -0.0956 0.0071  447 LYS A C   
1138 O O   . LYS A 151 ? 1.0864 0.6994 0.6691 0.0966  -0.0998 0.0089  447 LYS A O   
1139 C CB  . LYS A 151 ? 0.9241 0.5593 0.5205 0.0139  -0.0898 0.0199  447 LYS A CB  
1140 C CG  . LYS A 151 ? 1.0324 0.5939 0.5468 0.0491  -0.0951 0.0258  447 LYS A CG  
1141 C CD  . LYS A 151 ? 1.1300 0.6817 0.6183 0.0373  -0.0932 0.0325  447 LYS A CD  
1142 C CE  . LYS A 151 ? 1.3035 0.7504 0.6841 0.0572  -0.0971 0.0428  447 LYS A CE  
1143 N NZ  . LYS A 151 ? 1.3574 0.8091 0.7230 0.0472  -0.0949 0.0486  447 LYS A NZ  
1144 N N   . TYR A 152 ? 0.9232 0.6791 0.6373 0.0706  -0.0948 -0.0018 448 TYR A N   
1145 C CA  . TYR A 152 ? 0.9515 0.7509 0.6891 0.1094  -0.0992 -0.0089 448 TYR A CA  
1146 C C   . TYR A 152 ? 0.9743 0.7586 0.7088 0.1191  -0.0997 -0.0108 448 TYR A C   
1147 O O   . TYR A 152 ? 1.0858 0.8457 0.7804 0.1576  -0.1036 -0.0101 448 TYR A O   
1148 C CB  . TYR A 152 ? 0.8876 0.7776 0.7010 0.1035  -0.0983 -0.0183 448 TYR A CB  
1149 C CG  . TYR A 152 ? 0.9831 0.9255 0.8221 0.1335  -0.1025 -0.0251 448 TYR A CG  
1150 C CD1 . TYR A 152 ? 1.0512 1.0179 0.8725 0.1695  -0.1082 -0.0257 448 TYR A CD1 
1151 C CD2 . TYR A 152 ? 0.9257 0.8975 0.8038 0.1260  -0.1006 -0.0303 448 TYR A CD2 
1152 C CE1 . TYR A 152 ? 1.0767 1.1054 0.9223 0.1951  -0.1118 -0.0312 448 TYR A CE1 
1153 C CE2 . TYR A 152 ? 0.9437 0.9692 0.8435 0.1495  -0.1036 -0.0355 448 TYR A CE2 
1154 C CZ  . TYR A 152 ? 1.0169 1.0750 0.9019 0.1830  -0.1091 -0.0360 448 TYR A CZ  
1155 O OH  . TYR A 152 ? 1.0730 1.1993 0.9821 0.2040  -0.1118 -0.0407 448 TYR A OH  
1156 N N   . ALA A 153 ? 0.9097 0.7102 0.6836 0.0878  -0.0957 -0.0132 449 ALA A N   
1157 C CA  . ALA A 153 ? 0.9230 0.7183 0.7019 0.0950  -0.0959 -0.0159 449 ALA A CA  
1158 C C   . ALA A 153 ? 1.0530 0.7545 0.7500 0.1058  -0.0981 -0.0095 449 ALA A C   
1159 O O   . ALA A 153 ? 1.2204 0.9095 0.9042 0.1278  -0.0994 -0.0119 449 ALA A O   
1160 C CB  . ALA A 153 ? 0.8284 0.6562 0.6607 0.0586  -0.0914 -0.0188 449 ALA A CB  
1161 N N   . THR A 154 ? 1.0258 0.6574 0.6616 0.0900  -0.0984 -0.0015 450 THR A N   
1162 C CA  . THR A 154 ? 1.1466 0.6709 0.6887 0.0941  -0.1009 0.0049  450 THR A CA  
1163 C C   . THR A 154 ? 1.2798 0.7580 0.7554 0.1500  -0.1054 0.0066  450 THR A C   
1164 O O   . THR A 154 ? 1.4164 0.8269 0.8282 0.1761  -0.1077 0.0075  450 THR A O   
1165 C CB  . THR A 154 ? 1.1874 0.6547 0.6854 0.0467  -0.0992 0.0136  450 THR A CB  
1166 O OG1 . THR A 154 ? 1.0174 0.5442 0.5813 0.0013  -0.0949 0.0120  450 THR A OG1 
1167 C CG2 . THR A 154 ? 1.3204 0.6638 0.7105 0.0408  -0.1021 0.0202  450 THR A CG2 
1168 N N   . ASN A 155 ? 1.2521 0.7648 0.7367 0.1716  -0.1068 0.0072  451 ASN A N   
1169 C CA  . ASN A 155 ? 1.2079 0.7072 0.6455 0.2328  -0.1116 0.0079  451 ASN A CA  
1170 C C   . ASN A 155 ? 1.3561 0.7254 0.6746 0.2580  -0.1142 0.0145  451 ASN A C   
1171 O O   . ASN A 155 ? 1.3846 0.7387 0.6673 0.3100  -0.1168 0.0124  451 ASN A O   
1172 C CB  . ASN A 155 ? 1.1851 0.7857 0.6898 0.2672  -0.1125 -0.0011 451 ASN A CB  
1173 C CG  . ASN A 155 ? 1.3146 0.9337 0.7849 0.3323  -0.1175 -0.0007 451 ASN A CG  
1174 O OD1 . ASN A 155 ? 1.4175 1.0145 0.8490 0.3487  -0.1205 0.0042  451 ASN A OD1 
1175 N ND2 . ASN A 155 ? 1.3241 0.9911 0.8090 0.3710  -0.1184 -0.0055 451 ASN A ND2 
1176 N N   . LYS A 156 ? 1.4755 0.7487 0.7272 0.2191  -0.1134 0.0227  452 LYS A N   
1177 C CA  . LYS A 156 ? 1.6382 0.7659 0.7587 0.2328  -0.1162 0.0302  452 LYS A CA  
1178 C C   . LYS A 156 ? 1.7687 0.8478 0.8581 0.2381  -0.1166 0.0265  452 LYS A C   
1179 O O   . LYS A 156 ? 2.0510 1.0117 1.0273 0.2682  -0.1196 0.0300  452 LYS A O   
1180 C CB  . LYS A 156 ? 1.7300 0.8149 0.7757 0.3016  -0.1207 0.0338  452 LYS A CB  
1181 C CG  . LYS A 156 ? 1.9066 1.0525 0.9863 0.3087  -0.1215 0.0363  452 LYS A CG  
1182 C CD  . LYS A 156 ? 2.1142 1.1760 1.0845 0.3672  -0.1264 0.0438  452 LYS A CD  
1183 C CE  . LYS A 156 ? 2.3213 1.3688 1.2512 0.4314  -0.1251 0.0340  452 LYS A CE  
1184 N NZ  . LYS A 156 ? 2.3267 1.5140 1.3427 0.4805  -0.1274 0.0273  452 LYS A NZ  
1185 N N   . GLY A 157 ? 1.6562 0.8199 0.8385 0.2115  -0.1137 0.0193  453 GLY A N   
1186 C CA  . GLY A 157 ? 1.5784 0.7134 0.7449 0.2169  -0.1138 0.0149  453 GLY A CA  
1187 C C   . GLY A 157 ? 1.5412 0.7685 0.7698 0.2679  -0.1133 0.0064  453 GLY A C   
1188 O O   . GLY A 157 ? 1.4604 0.7049 0.7156 0.2609  -0.1118 0.0013  453 GLY A O   
1189 N N   . ASN A 158 ? 1.5238 0.8141 0.7735 0.3175  -0.1147 0.0052  454 ASN A N   
1190 C CA  . ASN A 158 ? 1.4418 0.8468 0.7651 0.3558  -0.1139 -0.0025 454 ASN A CA  
1191 C C   . ASN A 158 ? 1.3076 0.8279 0.7523 0.3083  -0.1106 -0.0076 454 ASN A C   
1192 O O   . ASN A 158 ? 1.2337 0.8411 0.7371 0.3123  -0.1110 -0.0097 454 ASN A O   
1193 C CB  . ASN A 158 ? 1.5334 0.9749 0.8353 0.4219  -0.1173 -0.0017 454 ASN A CB  
1194 C CG  . ASN A 158 ? 1.5328 1.1081 0.9130 0.4548  -0.1164 -0.0091 454 ASN A CG  
1195 O OD1 . ASN A 158 ? 1.5200 1.1337 0.9463 0.4399  -0.1130 -0.0142 454 ASN A OD1 
1196 N ND2 . ASN A 158 ? 1.4460 1.0960 0.8398 0.4976  -0.1195 -0.0092 454 ASN A ND2 
1197 N N   . LEU A 159 ? 1.1814 0.6979 0.6577 0.2643  -0.1075 -0.0097 455 LEU A N   
1198 C CA  . LEU A 159 ? 1.1199 0.7139 0.6893 0.2140  -0.1042 -0.0127 455 LEU A CA  
1199 C C   . LEU A 159 ? 1.0156 0.7308 0.6709 0.2294  -0.1032 -0.0197 455 LEU A C   
1200 O O   . LEU A 159 ? 1.0543 0.8076 0.7122 0.2697  -0.1039 -0.0230 455 LEU A O   
1201 C CB  . LEU A 159 ? 1.1333 0.7041 0.7144 0.1738  -0.1019 -0.0136 455 LEU A CB  
1202 C CG  . LEU A 159 ? 1.1746 0.6772 0.7199 0.1225  -0.1017 -0.0075 455 LEU A CG  
1203 C CD1 . LEU A 159 ? 1.3005 0.6953 0.7413 0.1317  -0.1049 0.0000  455 LEU A CD1 
1204 C CD2 . LEU A 159 ? 1.2158 0.6926 0.7575 0.0950  -0.1011 -0.0087 455 LEU A CD2 
1205 N N   . ARG A 160 ? 0.8280 0.6039 0.5495 0.1954  -0.1014 -0.0219 456 ARG A N   
1206 C CA  . ARG A 160 ? 0.7620 0.6431 0.5581 0.1984  -0.1008 -0.0285 456 ARG A CA  
1207 C C   . ARG A 160 ? 0.7365 0.6550 0.5975 0.1527  -0.0967 -0.0322 456 ARG A C   
1208 O O   . ARG A 160 ? 0.8131 0.7007 0.6735 0.1200  -0.0948 -0.0293 456 ARG A O   
1209 C CB  . ARG A 160 ? 0.8067 0.7238 0.6058 0.2130  -0.1041 -0.0284 456 ARG A CB  
1210 C CG  . ARG A 160 ? 0.9302 0.8231 0.6669 0.2666  -0.1085 -0.0249 456 ARG A CG  
1211 C CD  . ARG A 160 ? 1.0053 0.9383 0.7435 0.2837  -0.1127 -0.0244 456 ARG A CD  
1212 N NE  . ARG A 160 ? 1.0130 0.8838 0.7190 0.2621  -0.1126 -0.0189 456 ARG A NE  
1213 C CZ  . ARG A 160 ? 1.0905 0.9645 0.7725 0.2808  -0.1164 -0.0161 456 ARG A CZ  
1214 N NH1 . ARG A 160 ? 1.0836 1.0235 0.7713 0.3226  -0.1213 -0.0186 456 ARG A NH1 
1215 N NH2 . ARG A 160 ? 0.9849 0.8013 0.6360 0.2579  -0.1153 -0.0104 456 ARG A NH2 
1216 N N   . SER A 161 ? 0.8298 0.8154 0.7421 0.1518  -0.0952 -0.0380 457 SER A N   
1217 C CA  . SER A 161 ? 0.7723 0.7884 0.7388 0.1142  -0.0915 -0.0415 457 SER A CA  
1218 C C   . SER A 161 ? 0.6708 0.7199 0.6661 0.0966  -0.0915 -0.0440 457 SER A C   
1219 O O   . SER A 161 ? 0.6515 0.7422 0.6527 0.1120  -0.0946 -0.0467 457 SER A O   
1220 C CB  . SER A 161 ? 0.7914 0.8636 0.7956 0.1167  -0.0898 -0.0465 457 SER A CB  
1221 O OG  . SER A 161 ? 0.8579 0.9002 0.8322 0.1369  -0.0894 -0.0445 457 SER A OG  
1222 N N   . ALA A 162 ? 0.6932 0.7276 0.7043 0.0663  -0.0883 -0.0434 458 ALA A N   
1223 C CA  . ALA A 162 ? 0.7076 0.7661 0.7401 0.0514  -0.0874 -0.0461 458 ALA A CA  
1224 C C   . ALA A 162 ? 0.6841 0.7473 0.7460 0.0243  -0.0827 -0.0478 458 ALA A C   
1225 O O   . ALA A 162 ? 0.6698 0.7112 0.7300 0.0142  -0.0805 -0.0447 458 ALA A O   
1226 C CB  . ALA A 162 ? 0.6947 0.7184 0.6907 0.0546  -0.0886 -0.0407 458 ALA A CB  
1227 N N   . ILE A 163 ? 0.6894 0.7803 0.7735 0.0146  -0.0815 -0.0529 459 ILE A N   
1228 C CA  . ILE A 163 ? 0.6445 0.7372 0.7477 -0.0033 -0.0768 -0.0545 459 ILE A CA  
1229 C C   . ILE A 163 ? 0.6699 0.7706 0.7715 -0.0067 -0.0758 -0.0568 459 ILE A C   
1230 O O   . ILE A 163 ? 0.6510 0.7681 0.7498 -0.0002 -0.0793 -0.0609 459 ILE A O   
1231 C CB  . ILE A 163 ? 0.6149 0.7265 0.7424 -0.0099 -0.0756 -0.0604 459 ILE A CB  
1232 C CG1 . ILE A 163 ? 0.5723 0.6765 0.7095 -0.0208 -0.0707 -0.0609 459 ILE A CG1 
1233 C CG2 . ILE A 163 ? 0.5264 0.6671 0.6607 -0.0106 -0.0785 -0.0677 459 ILE A CG2 
1234 C CD1 . ILE A 163 ? 0.4406 0.5477 0.5908 -0.0268 -0.0691 -0.0649 459 ILE A CD1 
1235 N N   . THR A 164 ? 0.6335 0.7280 0.7357 -0.0159 -0.0712 -0.0541 460 THR A N   
1236 C CA  . THR A 164 ? 0.6500 0.7534 0.7495 -0.0173 -0.0687 -0.0564 460 THR A CA  
1237 C C   . THR A 164 ? 0.6341 0.7459 0.7477 -0.0205 -0.0639 -0.0609 460 THR A C   
1238 O O   . THR A 164 ? 0.7225 0.8359 0.8425 -0.0238 -0.0604 -0.0567 460 THR A O   
1239 C CB  . THR A 164 ? 0.6283 0.7213 0.7082 -0.0221 -0.0666 -0.0479 460 THR A CB  
1240 O OG1 . THR A 164 ? 0.6122 0.6852 0.6668 -0.0148 -0.0714 -0.0440 460 THR A OG1 
1241 C CG2 . THR A 164 ? 0.5264 0.6354 0.6058 -0.0229 -0.0623 -0.0499 460 THR A CG2 
1242 N N   . ILE A 165 ? 0.5542 0.6690 0.6671 -0.0187 -0.0643 -0.0695 461 ILE A N   
1243 C CA  . ILE A 165 ? 0.5079 0.6151 0.6213 -0.0179 -0.0607 -0.0753 461 ILE A CA  
1244 C C   . ILE A 165 ? 0.6104 0.7185 0.7103 -0.0104 -0.0563 -0.0779 461 ILE A C   
1245 O O   . ILE A 165 ? 0.6197 0.7239 0.7066 -0.0106 -0.0584 -0.0842 461 ILE A O   
1246 C CB  . ILE A 165 ? 0.5331 0.6319 0.6441 -0.0256 -0.0646 -0.0835 461 ILE A CB  
1247 C CG1 . ILE A 165 ? 0.5739 0.6794 0.6992 -0.0303 -0.0674 -0.0803 461 ILE A CG1 
1248 C CG2 . ILE A 165 ? 0.5147 0.5885 0.6113 -0.0249 -0.0610 -0.0893 461 ILE A CG2 
1249 C CD1 . ILE A 165 ? 0.6200 0.7321 0.7448 -0.0420 -0.0713 -0.0867 461 ILE A CD1 
1250 N N   . PHE A 166 ? 0.5821 0.7008 0.6841 -0.0030 -0.0502 -0.0731 462 PHE A N   
1251 C CA  . PHE A 166 ? 0.6075 0.7352 0.6965 0.0095  -0.0444 -0.0749 462 PHE A CA  
1252 C C   . PHE A 166 ? 0.7074 0.8070 0.7760 0.0222  -0.0424 -0.0843 462 PHE A C   
1253 O O   . PHE A 166 ? 0.6923 0.7668 0.7585 0.0172  -0.0452 -0.0878 462 PHE A O   
1254 C CB  . PHE A 166 ? 0.5093 0.6726 0.6086 0.0118  -0.0388 -0.0651 462 PHE A CB  
1255 C CG  . PHE A 166 ? 0.6022 0.7795 0.7049 -0.0044 -0.0404 -0.0563 462 PHE A CG  
1256 C CD1 . PHE A 166 ? 0.5424 0.7257 0.6321 -0.0054 -0.0391 -0.0555 462 PHE A CD1 
1257 C CD2 . PHE A 166 ? 0.6192 0.7940 0.7299 -0.0187 -0.0435 -0.0491 462 PHE A CD2 
1258 C CE1 . PHE A 166 ? 0.5984 0.7827 0.6807 -0.0208 -0.0407 -0.0467 462 PHE A CE1 
1259 C CE2 . PHE A 166 ? 0.5758 0.7470 0.6754 -0.0342 -0.0453 -0.0410 462 PHE A CE2 
1260 C CZ  . PHE A 166 ? 0.6776 0.8516 0.7615 -0.0354 -0.0439 -0.0394 462 PHE A CZ  
1261 N N   . PRO A 167 ? 0.7249 0.8222 0.7715 0.0386  -0.0375 -0.0886 463 PRO A N   
1262 C CA  . PRO A 167 ? 0.7994 0.8515 0.8103 0.0515  -0.0363 -0.0989 463 PRO A CA  
1263 C C   . PRO A 167 ? 0.8137 0.8462 0.8187 0.0617  -0.0345 -0.0979 463 PRO A C   
1264 O O   . PRO A 167 ? 0.7867 0.8536 0.8120 0.0717  -0.0309 -0.0896 463 PRO A O   
1265 C CB  . PRO A 167 ? 0.7614 0.8242 0.7506 0.0750  -0.0296 -0.1009 463 PRO A CB  
1266 C CG  . PRO A 167 ? 0.7972 0.8990 0.8068 0.0632  -0.0302 -0.0953 463 PRO A CG  
1267 C CD  . PRO A 167 ? 0.7459 0.8756 0.7915 0.0456  -0.0329 -0.0848 463 PRO A CD  
1268 N N   . GLN A 168 ? 0.8572 0.8332 0.8297 0.0570  -0.0372 -0.1064 464 GLN A N   
1269 C CA  . GLN A 168 ? 0.7115 0.6569 0.6687 0.0666  -0.0356 -0.1056 464 GLN A CA  
1270 C C   . GLN A 168 ? 0.8232 0.7690 0.7561 0.1062  -0.0280 -0.1044 464 GLN A C   
1271 O O   . GLN A 168 ? 0.8236 0.7744 0.7365 0.1257  -0.0239 -0.1078 464 GLN A O   
1272 C CB  . GLN A 168 ? 0.6551 0.5316 0.5706 0.0489  -0.0398 -0.1149 464 GLN A CB  
1273 C CG  . GLN A 168 ? 0.7390 0.5586 0.5943 0.0587  -0.0386 -0.1258 464 GLN A CG  
1274 C CD  . GLN A 168 ? 0.8740 0.6463 0.6988 0.0221  -0.0457 -0.1350 464 GLN A CD  
1275 O OE1 . GLN A 168 ? 0.9516 0.7614 0.8126 -0.0082 -0.0516 -0.1337 464 GLN A OE1 
1276 N NE2 . GLN A 168 ? 0.8836 0.5734 0.6363 0.0247  -0.0452 -0.1441 464 GLN A NE2 
1277 N N   . ARG A 169 ? 0.8185 0.7662 0.7538 0.1205  -0.0261 -0.0991 465 ARG A N   
1278 C CA  . ARG A 169 ? 0.8748 0.8195 0.7792 0.1640  -0.0194 -0.0982 465 ARG A CA  
1279 C C   . ARG A 169 ? 1.0290 0.8851 0.8591 0.1816  -0.0182 -0.1094 465 ARG A C   
1280 O O   . ARG A 169 ? 1.1280 0.9152 0.9275 0.1572  -0.0229 -0.1157 465 ARG A O   
1281 C CB  . ARG A 169 ? 0.9126 0.8688 0.8290 0.1738  -0.0193 -0.0908 465 ARG A CB  
1282 C CG  . ARG A 169 ? 0.9896 0.9136 0.8540 0.2217  -0.0141 -0.0919 465 ARG A CG  
1283 C CD  . ARG A 169 ? 1.1412 1.0740 1.0132 0.2329  -0.0147 -0.0846 465 ARG A CD  
1284 N NE  . ARG A 169 ? 1.1289 1.1632 1.0580 0.2357  -0.0137 -0.0739 465 ARG A NE  
1285 C CZ  . ARG A 169 ? 1.0518 1.1173 1.0236 0.2088  -0.0182 -0.0671 465 ARG A CZ  
1286 N NH1 . ARG A 169 ? 1.0898 1.0988 1.0570 0.1816  -0.0229 -0.0697 465 ARG A NH1 
1287 N NH2 . ARG A 169 ? 0.9515 1.1049 0.9668 0.2073  -0.0178 -0.0580 465 ARG A NH2 
1288 N N   . THR A 170 ? 1.0992 0.9571 0.8955 0.2230  -0.0116 -0.1118 466 THR A N   
1289 C CA  . THR A 170 ? 1.2127 0.9775 0.9249 0.2475  -0.0096 -0.1228 466 THR A CA  
1290 C C   . THR A 170 ? 1.3630 1.1066 1.0304 0.3018  -0.0037 -0.1203 466 THR A C   
1291 O O   . THR A 170 ? 1.4384 1.1133 1.0660 0.3044  -0.0057 -0.1210 466 THR A O   
1292 C CB  . THR A 170 ? 1.1901 0.9639 0.8852 0.2595  -0.0063 -0.1292 466 THR A CB  
1293 O OG1 . THR A 170 ? 1.1607 1.0412 0.9096 0.2772  -0.0006 -0.1200 466 THR A OG1 
1294 C CG2 . THR A 170 ? 1.0945 0.8485 0.7991 0.2107  -0.0135 -0.1360 466 THR A CG2 
1295 N N   . ASP A 171 ? 1.3797 1.1876 1.0524 0.3464  0.0038  -0.1168 467 ASP A N   
1296 C CA  . ASP A 171 ? 1.4409 1.2409 1.0677 0.4083  0.0100  -0.1144 467 ASP A CA  
1297 C C   . ASP A 171 ? 1.3750 1.2535 1.0559 0.4133  0.0096  -0.1018 467 ASP A C   
1298 O O   . ASP A 171 ? 1.4645 1.3098 1.1051 0.4503  0.0108  -0.0996 467 ASP A O   
1299 C CB  . ASP A 171 ? 1.5027 1.3533 1.1131 0.4570  0.0187  -0.1156 467 ASP A CB  
1300 C CG  . ASP A 171 ? 1.5025 1.4903 1.2001 0.4392  0.0211  -0.1060 467 ASP A CG  
1301 O OD1 . ASP A 171 ? 1.4871 1.4945 1.2377 0.3826  0.0154  -0.1044 467 ASP A OD1 
1302 O OD2 . ASP A 171 ? 1.5177 1.5945 1.2276 0.4810  0.0285  -0.0994 467 ASP A OD2 
1303 N N   . GLY A 172 ? 1.2813 1.2591 1.0466 0.3771  0.0075  -0.0933 468 GLY A N   
1304 C CA  . GLY A 172 ? 1.2469 1.3102 1.0633 0.3796  0.0071  -0.0815 468 GLY A CA  
1305 C C   . GLY A 172 ? 1.2558 1.4473 1.1207 0.3898  0.0123  -0.0732 468 GLY A C   
1306 O O   . GLY A 172 ? 1.2349 1.5068 1.1616 0.3583  0.0096  -0.0638 468 GLY A O   
1307 N N   . LYS A 173 ? 1.2912 1.5020 1.1238 0.4323  0.0200  -0.0765 469 LYS A N   
1308 C CA  . LYS A 173 ? 1.2487 1.5868 1.1237 0.4396  0.0261  -0.0685 469 LYS A CA  
1309 C C   . LYS A 173 ? 1.1693 1.5267 1.0785 0.3918  0.0254  -0.0693 469 LYS A C   
1310 O O   . LYS A 173 ? 1.1343 1.5945 1.0797 0.3854  0.0301  -0.0617 469 LYS A O   
1311 C CB  . LYS A 173 ? 1.3481 1.7100 1.1727 0.5117  0.0359  -0.0710 469 LYS A CB  
1312 C CG  . LYS A 173 ? 1.4315 1.7907 1.2188 0.5685  0.0371  -0.0677 469 LYS A CG  
1313 C CD  . LYS A 173 ? 1.5694 1.7723 1.2641 0.5974  0.0348  -0.0779 469 LYS A CD  
1314 C CE  . LYS A 173 ? 1.6411 1.7953 1.3153 0.6051  0.0291  -0.0735 469 LYS A CE  
1315 N NZ  . LYS A 173 ? 1.6589 1.8507 1.2973 0.6504  0.0284  -0.0618 469 LYS A NZ  
1316 N N   . HIS A 174 ? 1.1903 1.4552 1.0863 0.3576  0.0195  -0.0777 470 HIS A N   
1317 C CA  . HIS A 174 ? 1.1877 1.4631 1.1138 0.3123  0.0171  -0.0781 470 HIS A CA  
1318 C C   . HIS A 174 ? 1.2357 1.4757 1.1930 0.2614  0.0076  -0.0768 470 HIS A C   
1319 O O   . HIS A 174 ? 1.3167 1.4743 1.2520 0.2431  0.0022  -0.0854 470 HIS A O   
1320 C CB  . HIS A 174 ? 1.2380 1.4452 1.1160 0.3230  0.0187  -0.0901 470 HIS A CB  
1321 C CG  . HIS A 174 ? 1.2759 1.5141 1.1176 0.3767  0.0287  -0.0922 470 HIS A CG  
1322 N ND1 . HIS A 174 ? 1.3662 1.5277 1.1341 0.4263  0.0319  -0.1019 470 HIS A ND1 
1323 C CD2 . HIS A 174 ? 1.2703 1.6088 1.1346 0.3903  0.0368  -0.0855 470 HIS A CD2 
1324 C CE1 . HIS A 174 ? 1.4161 1.6301 1.1631 0.4733  0.0417  -0.1017 470 HIS A CE1 
1325 N NE2 . HIS A 174 ? 1.3501 1.6780 1.1583 0.4513  0.0450  -0.0916 470 HIS A NE2 
1326 N N   . ASP A 175 ? 1.1260 1.4316 1.1313 0.2386  0.0055  -0.0660 471 ASP A N   
1327 C CA  . ASP A 175 ? 0.9749 1.2574 1.0102 0.1936  -0.0028 -0.0636 471 ASP A CA  
1328 C C   . ASP A 175 ? 0.8056 1.1339 0.8754 0.1554  -0.0041 -0.0572 471 ASP A C   
1329 O O   . ASP A 175 ? 0.7819 1.1874 0.8678 0.1557  0.0009  -0.0495 471 ASP A O   
1330 C CB  . ASP A 175 ? 1.0118 1.3180 1.0657 0.1941  -0.0053 -0.0568 471 ASP A CB  
1331 C CG  . ASP A 175 ? 1.0659 1.2979 1.0828 0.2177  -0.0069 -0.0630 471 ASP A CG  
1332 O OD1 . ASP A 175 ? 1.1453 1.2998 1.1219 0.2238  -0.0072 -0.0730 471 ASP A OD1 
1333 O OD2 . ASP A 175 ? 1.0772 1.3258 1.1005 0.2281  -0.0080 -0.0579 471 ASP A OD2 
1334 N N   . PHE A 176 ? 0.7184 0.9990 0.7944 0.1234  -0.0107 -0.0602 472 PHE A N   
1335 C CA  . PHE A 176 ? 0.6536 0.9616 0.7558 0.0868  -0.0137 -0.0529 472 PHE A CA  
1336 C C   . PHE A 176 ? 0.6159 0.9365 0.7413 0.0665  -0.0183 -0.0458 472 PHE A C   
1337 O O   . PHE A 176 ? 0.5736 0.8488 0.6977 0.0645  -0.0230 -0.0496 472 PHE A O   
1338 C CB  . PHE A 176 ? 0.6501 0.9054 0.7441 0.0687  -0.0189 -0.0591 472 PHE A CB  
1339 C CG  . PHE A 176 ? 0.6411 0.8923 0.7143 0.0805  -0.0152 -0.0645 472 PHE A CG  
1340 C CD1 . PHE A 176 ? 0.6697 0.8870 0.7109 0.1091  -0.0123 -0.0744 472 PHE A CD1 
1341 C CD2 . PHE A 176 ? 0.7011 0.9746 0.7795 0.0626  -0.0148 -0.0597 472 PHE A CD2 
1342 C CE1 . PHE A 176 ? 0.7297 0.9396 0.7471 0.1201  -0.0091 -0.0803 472 PHE A CE1 
1343 C CE2 . PHE A 176 ? 0.6978 0.9685 0.7563 0.0735  -0.0114 -0.0646 472 PHE A CE2 
1344 C CZ  . PHE A 176 ? 0.6903 0.9312 0.7198 0.1024  -0.0086 -0.0753 472 PHE A CZ  
1345 N N   . ARG A 177 ? 0.5378 0.9203 0.6807 0.0496  -0.0168 -0.0355 473 ARG A N   
1346 C CA  . ARG A 177 ? 0.6511 1.0437 0.8105 0.0261  -0.0217 -0.0289 473 ARG A CA  
1347 C C   . ARG A 177 ? 0.6131 1.0219 0.7755 -0.0129 -0.0238 -0.0205 473 ARG A C   
1348 O O   . ARG A 177 ? 0.5528 1.0115 0.7139 -0.0210 -0.0189 -0.0148 473 ARG A O   
1349 C CB  . ARG A 177 ? 0.6410 1.0948 0.8105 0.0430  -0.0190 -0.0240 473 ARG A CB  
1350 C CG  . ARG A 177 ? 0.6338 1.0588 0.7898 0.0832  -0.0176 -0.0311 473 ARG A CG  
1351 C CD  . ARG A 177 ? 0.6945 1.0476 0.8479 0.0731  -0.0240 -0.0358 473 ARG A CD  
1352 N NE  . ARG A 177 ? 0.6959 1.0675 0.8681 0.0483  -0.0290 -0.0289 473 ARG A NE  
1353 C CZ  . ARG A 177 ? 0.7092 1.1142 0.8879 0.0602  -0.0295 -0.0249 473 ARG A CZ  
1354 N NH1 . ARG A 177 ? 0.7419 1.1645 0.9080 0.1006  -0.0250 -0.0266 473 ARG A NH1 
1355 N NH2 . ARG A 177 ? 0.6918 1.1097 0.8843 0.0340  -0.0347 -0.0194 473 ARG A NH2 
1356 N N   . VAL A 178 ? 0.5707 0.9340 0.7312 -0.0362 -0.0306 -0.0196 474 VAL A N   
1357 C CA  . VAL A 178 ? 0.5302 0.9006 0.6836 -0.0740 -0.0336 -0.0104 474 VAL A CA  
1358 C C   . VAL A 178 ? 0.6914 1.1084 0.8571 -0.0845 -0.0348 -0.0045 474 VAL A C   
1359 O O   . VAL A 178 ? 0.7942 1.1912 0.9677 -0.0744 -0.0383 -0.0078 474 VAL A O   
1360 C CB  . VAL A 178 ? 0.5466 0.8438 0.6838 -0.0877 -0.0404 -0.0122 474 VAL A CB  
1361 C CG1 . VAL A 178 ? 0.5665 0.8520 0.6792 -0.1257 -0.0433 -0.0029 474 VAL A CG1 
1362 C CG2 . VAL A 178 ? 0.5544 0.8138 0.6832 -0.0719 -0.0403 -0.0192 474 VAL A CG2 
1363 N N   . TRP A 179 ? 0.7386 1.2234 0.9053 -0.1062 -0.0318 0.0044  475 TRP A N   
1364 C CA  . TRP A 179 ? 0.6963 1.2422 0.8760 -0.1171 -0.0333 0.0102  475 TRP A CA  
1365 C C   . TRP A 179 ? 0.7298 1.2383 0.8940 -0.1568 -0.0413 0.0144  475 TRP A C   
1366 O O   . TRP A 179 ? 0.7519 1.2938 0.9261 -0.1630 -0.0446 0.0169  475 TRP A O   
1367 C CB  . TRP A 179 ? 0.6055 1.2539 0.7928 -0.1280 -0.0273 0.0186  475 TRP A CB  
1368 C CG  . TRP A 179 ? 0.6369 1.3389 0.8392 -0.0791 -0.0195 0.0148  475 TRP A CG  
1369 C CD1 . TRP A 179 ? 0.6550 1.3076 0.8520 -0.0390 -0.0163 0.0051  475 TRP A CD1 
1370 C CD2 . TRP A 179 ? 0.6591 1.4728 0.8773 -0.0631 -0.0141 0.0203  475 TRP A CD2 
1371 N NE1 . TRP A 179 ? 0.6957 1.4101 0.8980 0.0026  -0.0091 0.0038  475 TRP A NE1 
1372 C CE2 . TRP A 179 ? 0.7175 1.5354 0.9347 -0.0078 -0.0073 0.0133  475 TRP A CE2 
1373 C CE3 . TRP A 179 ? 0.6809 1.5946 0.9111 -0.0904 -0.0147 0.0305  475 TRP A CE3 
1374 C CZ2 . TRP A 179 ? 0.7762 1.6927 1.0021 0.0281  -0.0005 0.0162  475 TRP A CZ2 
1375 C CZ3 . TRP A 179 ? 0.7374 1.7546 0.9797 -0.0573 -0.0081 0.0337  475 TRP A CZ3 
1376 C CH2 . TRP A 179 ? 0.7853 1.8100 1.0284 0.0045  -0.0009 0.0267  475 TRP A CH2 
1377 N N   . ASN A 180 ? 0.7097 1.1480 0.8448 -0.1808 -0.0446 0.0151  476 ASN A N   
1378 C CA  . ASN A 180 ? 0.7012 1.0836 0.8099 -0.2111 -0.0521 0.0174  476 ASN A CA  
1379 C C   . ASN A 180 ? 0.7590 1.0954 0.8789 -0.1842 -0.0560 0.0095  476 ASN A C   
1380 O O   . ASN A 180 ? 0.7003 1.0175 0.8360 -0.1489 -0.0537 0.0019  476 ASN A O   
1381 C CB  . ASN A 180 ? 0.8080 1.1152 0.8735 -0.2324 -0.0543 0.0195  476 ASN A CB  
1382 C CG  . ASN A 180 ? 0.8564 1.1971 0.9070 -0.2559 -0.0493 0.0268  476 ASN A CG  
1383 O OD1 . ASN A 180 ? 0.8178 1.2128 0.8939 -0.2341 -0.0426 0.0255  476 ASN A OD1 
1384 N ND2 . ASN A 180 ? 0.8852 1.1889 0.8879 -0.3013 -0.0525 0.0348  476 ASN A ND2 
1385 N N   . SER A 181 ? 0.6760 0.9932 0.7833 -0.2043 -0.0620 0.0114  477 SER A N   
1386 C CA  . SER A 181 ? 0.6490 0.9180 0.7619 -0.1817 -0.0654 0.0046  477 SER A CA  
1387 C C   . SER A 181 ? 0.6950 0.8806 0.7802 -0.1764 -0.0677 0.0007  477 SER A C   
1388 O O   . SER A 181 ? 0.6003 0.7589 0.6982 -0.1479 -0.0676 -0.0063 477 SER A O   
1389 C CB  . SER A 181 ? 0.5615 0.8390 0.6694 -0.2010 -0.0709 0.0073  477 SER A CB  
1390 O OG  . SER A 181 ? 0.6864 0.9639 0.7608 -0.2476 -0.0748 0.0146  477 SER A OG  
1391 N N   . GLN A 182 ? 0.8062 0.9527 0.8501 -0.2030 -0.0698 0.0055  478 GLN A N   
1392 C CA  . GLN A 182 ? 0.8447 0.9168 0.8557 -0.1927 -0.0716 0.0030  478 GLN A CA  
1393 C C   . GLN A 182 ? 0.8948 0.9614 0.8801 -0.2092 -0.0693 0.0085  478 GLN A C   
1394 O O   . GLN A 182 ? 0.9772 1.0722 0.9483 -0.2444 -0.0684 0.0161  478 GLN A O   
1395 C CB  . GLN A 182 ? 0.9101 0.9092 0.8733 -0.2050 -0.0779 0.0038  478 GLN A CB  
1396 C CG  . GLN A 182 ? 0.9509 0.9451 0.9305 -0.1900 -0.0806 -0.0012 478 GLN A CG  
1397 C CD  . GLN A 182 ? 1.0278 0.9538 0.9514 -0.2093 -0.0867 0.0006  478 GLN A CD  
1398 O OE1 . GLN A 182 ? 1.0905 0.9444 0.9587 -0.2109 -0.0891 0.0020  478 GLN A OE1 
1399 N NE2 . GLN A 182 ? 0.9342 0.8786 0.8658 -0.2225 -0.0895 0.0007  478 GLN A NE2 
1400 N N   . LEU A 183 ? 0.8196 0.8534 0.7973 -0.1857 -0.0684 0.0050  479 LEU A N   
1401 C CA  . LEU A 183 ? 0.8107 0.8299 0.7585 -0.1980 -0.0664 0.0102  479 LEU A CA  
1402 C C   . LEU A 183 ? 0.8150 0.7854 0.7005 -0.2395 -0.0696 0.0194  479 LEU A C   
1403 O O   . LEU A 183 ? 0.8924 0.8836 0.7610 -0.2698 -0.0666 0.0269  479 LEU A O   
1404 C CB  . LEU A 183 ? 0.7989 0.7753 0.7357 -0.1659 -0.0676 0.0052  479 LEU A CB  
1405 C CG  . LEU A 183 ? 0.7728 0.7849 0.7587 -0.1303 -0.0656 -0.0043 479 LEU A CG  
1406 C CD1 . LEU A 183 ? 0.8307 0.8077 0.7981 -0.1063 -0.0679 -0.0075 479 LEU A CD1 
1407 C CD2 . LEU A 183 ? 0.6026 0.6836 0.6277 -0.1302 -0.0594 -0.0053 479 LEU A CD2 
1408 N N   . ILE A 184 ? 0.9406 0.8425 0.7851 -0.2431 -0.0754 0.0189  480 ILE A N   
1409 C CA  . ILE A 184 ? 0.7498 0.5854 0.5201 -0.2843 -0.0794 0.0268  480 ILE A CA  
1410 C C   . ILE A 184 ? 0.9657 0.8083 0.7349 -0.3084 -0.0835 0.0268  480 ILE A C   
1411 O O   . ILE A 184 ? 1.0374 0.8514 0.8102 -0.2841 -0.0867 0.0205  480 ILE A O   
1412 C CB  . ILE A 184 ? 0.8307 0.5587 0.5310 -0.2652 -0.0834 0.0266  480 ILE A CB  
1413 C CG1 . ILE A 184 ? 0.9302 0.6570 0.6256 -0.2494 -0.0799 0.0287  480 ILE A CG1 
1414 C CG2 . ILE A 184 ? 0.9813 0.6223 0.5903 -0.3086 -0.0880 0.0343  480 ILE A CG2 
1415 C CD1 . ILE A 184 ? 0.9791 0.6208 0.6211 -0.2140 -0.0835 0.0270  480 ILE A CD1 
1416 N N   . ARG A 185 ? 0.9567 0.8457 0.7223 -0.3567 -0.0831 0.0339  481 ARG A N   
1417 C CA  . ARG A 185 ? 1.0628 0.9606 0.8170 -0.3904 -0.0881 0.0354  481 ARG A CA  
1418 C C   . ARG A 185 ? 1.1655 1.0498 0.8597 -0.4565 -0.0902 0.0458  481 ARG A C   
1419 O O   . ARG A 185 ? 1.2049 1.1203 0.8957 -0.4762 -0.0855 0.0524  481 ARG A O   
1420 C CB  . ARG A 185 ? 0.9382 0.9494 0.7726 -0.3798 -0.0858 0.0328  481 ARG A CB  
1421 C CG  . ARG A 185 ? 0.9297 0.9543 0.8185 -0.3223 -0.0836 0.0233  481 ARG A CG  
1422 C CD  . ARG A 185 ? 0.9333 1.0232 0.8697 -0.3152 -0.0847 0.0206  481 ARG A CD  
1423 N NE  . ARG A 185 ? 0.9913 1.0298 0.8892 -0.3356 -0.0920 0.0201  481 ARG A NE  
1424 C CZ  . ARG A 185 ? 0.9577 1.0294 0.8830 -0.3290 -0.0946 0.0174  481 ARG A CZ  
1425 N NH1 . ARG A 185 ? 0.7146 0.8668 0.7033 -0.3007 -0.0906 0.0153  481 ARG A NH1 
1426 N NH2 . ARG A 185 ? 1.1232 1.1402 1.0056 -0.3493 -0.1014 0.0167  481 ARG A NH2 
1427 N N   . TYR A 186 ? 1.1220 0.9604 0.7660 -0.4893 -0.0966 0.0472  482 TYR A N   
1428 C CA  . TYR A 186 ? 1.2265 1.0631 0.8130 -0.5345 -0.0955 0.0566  482 TYR A CA  
1429 C C   . TYR A 186 ? 1.1939 1.1672 0.8395 -0.5509 -0.0916 0.0606  482 TYR A C   
1430 O O   . TYR A 186 ? 1.0701 1.1189 0.7871 -0.5256 -0.0911 0.0557  482 TYR A O   
1431 C CB  . TYR A 186 ? 1.2875 1.0168 0.7887 -0.5470 -0.1020 0.0560  482 TYR A CB  
1432 C CG  . TYR A 186 ? 1.4221 1.0123 0.8508 -0.5237 -0.1051 0.0529  482 TYR A CG  
1433 C CD1 . TYR A 186 ? 1.4365 0.9539 0.8498 -0.4876 -0.1097 0.0446  482 TYR A CD1 
1434 C CD2 . TYR A 186 ? 1.4153 0.9505 0.7903 -0.5327 -0.1032 0.0583  482 TYR A CD2 
1435 C CE1 . TYR A 186 ? 1.4772 0.8728 0.8209 -0.4570 -0.1120 0.0419  482 TYR A CE1 
1436 C CE2 . TYR A 186 ? 1.5135 0.9226 0.8176 -0.5037 -0.1059 0.0560  482 TYR A CE2 
1437 C CZ  . TYR A 186 ? 1.5084 0.8506 0.7978 -0.4631 -0.1101 0.0479  482 TYR A CZ  
1438 O OH  . TYR A 186 ? 1.4963 0.7211 0.7136 -0.4246 -0.1121 0.0458  482 TYR A OH  
1439 N N   . ALA A 187 ? 1.2968 1.3015 0.9076 -0.5911 -0.0892 0.0695  483 ALA A N   
1440 C CA  . ALA A 187 ? 1.2391 1.3778 0.8980 -0.6047 -0.0850 0.0743  483 ALA A CA  
1441 C C   . ALA A 187 ? 1.2678 1.4276 0.9169 -0.6205 -0.0894 0.0747  483 ALA A C   
1442 O O   . ALA A 187 ? 1.2644 1.3291 0.8499 -0.6358 -0.0956 0.0735  483 ALA A O   
1443 C CB  . ALA A 187 ? 1.2117 1.3783 0.8309 -0.6449 -0.0819 0.0835  483 ALA A CB  
1444 N N   . GLY A 188 ? 1.2372 1.5231 0.9460 -0.6145 -0.0858 0.0767  484 GLY A N   
1445 C CA  . GLY A 188 ? 1.3019 1.6241 1.0071 -0.6289 -0.0894 0.0780  484 GLY A CA  
1446 C C   . GLY A 188 ? 1.3146 1.7468 1.0184 -0.6610 -0.0867 0.0869  484 GLY A C   
1447 O O   . GLY A 188 ? 1.2859 1.8336 1.0528 -0.6368 -0.0808 0.0880  484 GLY A O   
1448 N N   . TYR A 189 ? 1.3398 1.7364 0.9660 -0.7146 -0.0911 0.0932  485 TYR A N   
1449 C CA  . TYR A 189 ? 1.3566 1.8541 0.9682 -0.7542 -0.0899 0.1022  485 TYR A CA  
1450 C C   . TYR A 189 ? 1.4334 1.9545 1.0274 -0.7761 -0.0944 0.1042  485 TYR A C   
1451 O O   . TYR A 189 ? 1.4505 1.8738 0.9719 -0.8088 -0.1008 0.1046  485 TYR A O   
1452 C CB  . TYR A 189 ? 1.4117 1.8594 0.9407 -0.8070 -0.0922 0.1085  485 TYR A CB  
1453 C CG  . TYR A 189 ? 1.2918 1.6765 0.8162 -0.7913 -0.0895 0.1061  485 TYR A CG  
1454 C CD1 . TYR A 189 ? 1.3302 1.5656 0.7937 -0.7922 -0.0939 0.1022  485 TYR A CD1 
1455 C CD2 . TYR A 189 ? 1.2949 1.7680 0.8704 -0.7741 -0.0826 0.1080  485 TYR A CD2 
1456 C CE1 . TYR A 189 ? 1.4206 1.5975 0.8757 -0.7776 -0.0915 0.1006  485 TYR A CE1 
1457 C CE2 . TYR A 189 ? 1.2794 1.6942 0.8489 -0.7616 -0.0799 0.1063  485 TYR A CE2 
1458 C CZ  . TYR A 189 ? 1.3135 1.5802 0.8225 -0.7647 -0.0844 0.1029  485 TYR A CZ  
1459 O OH  . TYR A 189 ? 1.2062 1.4104 0.7038 -0.7517 -0.0820 0.1017  485 TYR A OH  
1460 N N   . LYS A 190 ? 1.4688 2.1174 1.1244 -0.7564 -0.0908 0.1057  486 LYS A N   
1461 C CA  . LYS A 190 ? 1.5528 2.2548 1.1877 -0.7873 -0.0941 0.1107  486 LYS A CA  
1462 C C   . LYS A 190 ? 1.6765 2.3911 1.2334 -0.8563 -0.0967 0.1204  486 LYS A C   
1463 O O   . LYS A 190 ? 1.7387 2.4491 1.2717 -0.8740 -0.0952 0.1235  486 LYS A O   
1464 C CB  . LYS A 190 ? 1.4917 2.3371 1.2044 -0.7488 -0.0889 0.1112  486 LYS A CB  
1465 C CG  . LYS A 190 ? 1.4418 2.3736 1.2047 -0.7162 -0.0812 0.1120  486 LYS A CG  
1466 C CD  . LYS A 190 ? 1.3645 2.4453 1.1817 -0.6851 -0.0762 0.1148  486 LYS A CD  
1467 C CE  . LYS A 190 ? 1.2358 2.3224 1.1211 -0.6171 -0.0741 0.1062  486 LYS A CE  
1468 N NZ  . LYS A 190 ? 1.1689 2.3932 1.1028 -0.5748 -0.0676 0.1085  486 LYS A NZ  
1469 N N   . GLN A 191 ? 1.7093 2.4393 1.2233 -0.8976 -0.1011 0.1253  487 GLN A N   
1470 C CA  . GLN A 191 ? 1.8044 2.5373 1.2330 -0.9700 -0.1051 0.1344  487 GLN A CA  
1471 C C   . GLN A 191 ? 1.8330 2.7251 1.2807 -0.9917 -0.1030 0.1426  487 GLN A C   
1472 O O   . GLN A 191 ? 1.7805 2.7634 1.2986 -0.9506 -0.0992 0.1409  487 GLN A O   
1473 C CB  . GLN A 191 ? 1.8984 2.4943 1.2348 -1.0116 -0.1130 0.1341  487 GLN A CB  
1474 C CG  . GLN A 191 ? 1.9341 2.3659 1.2260 -0.9985 -0.1158 0.1275  487 GLN A CG  
1475 C CD  . GLN A 191 ? 2.0138 2.4093 1.2540 -1.0265 -0.1162 0.1305  487 GLN A CD  
1476 O OE1 . GLN A 191 ? 1.9780 2.4656 1.2694 -1.0128 -0.1110 0.1323  487 GLN A OE1 
1477 N NE2 . GLN A 191 ? 2.1149 2.3712 1.2488 -1.0640 -0.1227 0.1308  487 GLN A NE2 
1478 N N   . PRO A 192 ? 1.9207 2.8527 1.3035 -1.0555 -0.1057 0.1515  488 PRO A N   
1479 C CA  . PRO A 192 ? 1.9529 3.0332 1.3410 -1.0836 -0.1047 0.1600  488 PRO A CA  
1480 C C   . PRO A 192 ? 1.9801 3.0449 1.3485 -1.1010 -0.1081 0.1610  488 PRO A C   
1481 O O   . PRO A 192 ? 1.9376 3.1259 1.3525 -1.0862 -0.1048 0.1639  488 PRO A O   
1482 C CB  . PRO A 192 ? 2.0603 3.1575 1.3667 -1.1568 -0.1089 0.1686  488 PRO A CB  
1483 C CG  . PRO A 192 ? 2.1092 3.0321 1.3451 -1.1767 -0.1141 0.1643  488 PRO A CG  
1484 C CD  . PRO A 192 ? 2.0057 2.8654 1.3123 -1.1016 -0.1095 0.1542  488 PRO A CD  
1485 N N   . ASP A 193 ? 2.0494 2.9635 1.3472 -1.1292 -0.1144 0.1584  489 ASP A N   
1486 C CA  . ASP A 193 ? 2.0658 2.9509 1.3430 -1.1432 -0.1180 0.1584  489 ASP A CA  
1487 C C   . ASP A 193 ? 1.9159 2.7780 1.2728 -1.0716 -0.1160 0.1485  489 ASP A C   
1488 O O   . ASP A 193 ? 1.9180 2.7098 1.2516 -1.0765 -0.1204 0.1457  489 ASP A O   
1489 C CB  . ASP A 193 ? 2.2308 2.9589 1.3908 -1.2008 -0.1259 0.1598  489 ASP A CB  
1490 C CG  . ASP A 193 ? 2.2499 2.8184 1.3886 -1.1705 -0.1278 0.1511  489 ASP A CG  
1491 O OD1 . ASP A 193 ? 2.2122 2.7723 1.3543 -1.1624 -0.1259 0.1503  489 ASP A OD1 
1492 O OD2 . ASP A 193 ? 2.2563 2.7118 1.3748 -1.1534 -0.1313 0.1452  489 ASP A OD2 
1493 N N   . GLY A 194 ? 1.8175 2.7336 1.2623 -1.0070 -0.1101 0.1429  490 GLY A N   
1494 C CA  . GLY A 194 ? 1.7618 2.6725 1.2841 -0.9390 -0.1084 0.1336  490 GLY A CA  
1495 C C   . GLY A 194 ? 1.8005 2.5682 1.3265 -0.9030 -0.1107 0.1233  490 GLY A C   
1496 O O   . GLY A 194 ? 1.7878 2.5702 1.3878 -0.8415 -0.1073 0.1159  490 GLY A O   
1497 N N   . SER A 195 ? 1.8711 2.5005 1.3130 -0.9396 -0.1164 0.1229  491 SER A N   
1498 C CA  . SER A 195 ? 1.8554 2.3453 1.2899 -0.9062 -0.1191 0.1133  491 SER A CA  
1499 C C   . SER A 195 ? 1.7905 2.2665 1.2599 -0.8715 -0.1146 0.1096  491 SER A C   
1500 O O   . SER A 195 ? 1.7725 2.3504 1.2813 -0.8665 -0.1090 0.1135  491 SER A O   
1501 C CB  . SER A 195 ? 1.9424 2.2900 1.2656 -0.9529 -0.1261 0.1147  491 SER A CB  
1502 O OG  . SER A 195 ? 2.0317 2.3647 1.2794 -1.0078 -0.1268 0.1228  491 SER A OG  
1503 N N   . THR A 196 ? 1.7506 2.1002 1.2031 -0.8461 -0.1167 0.1020  492 THR A N   
1504 C CA  . THR A 196 ? 1.6571 1.9907 1.1507 -0.8066 -0.1124 0.0973  492 THR A CA  
1505 C C   . THR A 196 ? 1.7163 1.9031 1.1291 -0.8208 -0.1156 0.0957  492 THR A C   
1506 O O   . THR A 196 ? 1.7866 1.8586 1.1511 -0.8162 -0.1206 0.0910  492 THR A O   
1507 C CB  . THR A 196 ? 1.4709 1.8188 1.0498 -0.7418 -0.1107 0.0876  492 THR A CB  
1508 O OG1 . THR A 196 ? 1.3357 1.8194 0.9860 -0.7226 -0.1075 0.0890  492 THR A OG1 
1509 C CG2 . THR A 196 ? 1.3880 1.7104 1.0015 -0.7051 -0.1065 0.0829  492 THR A CG2 
1510 N N   . LEU A 197 ? 1.6975 1.8877 1.0939 -0.8340 -0.1126 0.0994  493 LEU A N   
1511 C CA  . LEU A 197 ? 1.7000 1.7589 1.0309 -0.8354 -0.1146 0.0972  493 LEU A CA  
1512 C C   . LEU A 197 ? 1.5550 1.6028 0.9550 -0.7762 -0.1103 0.0895  493 LEU A C   
1513 O O   . LEU A 197 ? 1.4124 1.5669 0.9048 -0.7440 -0.1049 0.0879  493 LEU A O   
1514 C CB  . LEU A 197 ? 1.7826 1.8467 1.0528 -0.8842 -0.1147 0.1049  493 LEU A CB  
1515 C CG  . LEU A 197 ? 1.8838 1.8118 1.0677 -0.8948 -0.1175 0.1039  493 LEU A CG  
1516 C CD1 . LEU A 197 ? 1.9828 1.7589 1.0834 -0.8916 -0.1239 0.0996  493 LEU A CD1 
1517 C CD2 . LEU A 197 ? 1.9954 1.9373 1.1083 -0.9558 -0.1197 0.1118  493 LEU A CD2 
1518 N N   . GLY A 198 ? 1.6357 1.5516 0.9850 -0.7604 -0.1129 0.0848  494 GLY A N   
1519 C CA  . GLY A 198 ? 1.6237 1.5191 1.0250 -0.7099 -0.1094 0.0782  494 GLY A CA  
1520 C C   . GLY A 198 ? 1.5745 1.4750 1.0395 -0.6622 -0.1102 0.0692  494 GLY A C   
1521 O O   . GLY A 198 ? 1.7366 1.5475 1.1582 -0.6542 -0.1153 0.0647  494 GLY A O   
1522 N N   . ASP A 199 ? 1.3643 1.3669 0.9268 -0.6295 -0.1055 0.0663  495 ASP A N   
1523 C CA  . ASP A 199 ? 1.2403 1.2536 0.8649 -0.5845 -0.1068 0.0571  495 ASP A CA  
1524 C C   . ASP A 199 ? 1.1654 1.3145 0.8675 -0.5750 -0.1040 0.0582  495 ASP A C   
1525 O O   . ASP A 199 ? 0.9564 1.1956 0.7151 -0.5600 -0.0980 0.0599  495 ASP A O   
1526 C CB  . ASP A 199 ? 1.2297 1.2105 0.8876 -0.5442 -0.1049 0.0505  495 ASP A CB  
1527 C CG  . ASP A 199 ? 1.2443 1.2058 0.9424 -0.5028 -0.1084 0.0403  495 ASP A CG  
1528 O OD1 . ASP A 199 ? 1.1354 1.1444 0.8631 -0.4987 -0.1105 0.0384  495 ASP A OD1 
1529 O OD2 . ASP A 199 ? 1.2567 1.1556 0.9537 -0.4746 -0.1094 0.0341  495 ASP A OD2 
1530 N N   . PRO A 200 ? 1.2292 1.3956 0.9327 -0.5796 -0.1079 0.0572  496 PRO A N   
1531 C CA  . PRO A 200 ? 1.1060 1.4003 0.8772 -0.5662 -0.1054 0.0586  496 PRO A CA  
1532 C C   . PRO A 200 ? 0.9706 1.3191 0.8235 -0.5133 -0.1022 0.0522  496 PRO A C   
1533 O O   . PRO A 200 ? 0.9294 1.3876 0.8340 -0.4967 -0.0977 0.0548  496 PRO A O   
1534 C CB  . PRO A 200 ? 1.1877 1.4606 0.9370 -0.5770 -0.1116 0.0570  496 PRO A CB  
1535 C CG  . PRO A 200 ? 1.2989 1.4518 0.9533 -0.6139 -0.1161 0.0589  496 PRO A CG  
1536 C CD  . PRO A 200 ? 1.2743 1.3441 0.9096 -0.5980 -0.1146 0.0555  496 PRO A CD  
1537 N N   . ALA A 201 ? 1.0007 1.2745 0.8607 -0.4855 -0.1043 0.0441  497 ALA A N   
1538 C CA  . ALA A 201 ? 0.9634 1.2817 0.8937 -0.4383 -0.1021 0.0380  497 ALA A CA  
1539 C C   . ALA A 201 ? 0.9974 1.3995 0.9657 -0.4276 -0.0943 0.0421  497 ALA A C   
1540 O O   . ALA A 201 ? 0.9000 1.3820 0.9257 -0.3921 -0.0910 0.0404  497 ALA A O   
1541 C CB  . ALA A 201 ? 0.9182 1.1390 0.8377 -0.4185 -0.1057 0.0297  497 ALA A CB  
1542 N N   . ASN A 202 ? 1.0960 1.4786 1.0271 -0.4565 -0.0911 0.0477  498 ASN A N   
1543 C CA  . ASN A 202 ? 1.0503 1.4917 1.0101 -0.4457 -0.0838 0.0504  498 ASN A CA  
1544 C C   . ASN A 202 ? 1.0083 1.5454 0.9650 -0.4684 -0.0785 0.0597  498 ASN A C   
1545 O O   . ASN A 202 ? 1.0249 1.6014 0.9876 -0.4700 -0.0724 0.0635  498 ASN A O   
1546 C CB  . ASN A 202 ? 1.0848 1.4390 1.0044 -0.4600 -0.0838 0.0504  498 ASN A CB  
1547 C CG  . ASN A 202 ? 1.0517 1.3003 0.9555 -0.4436 -0.0901 0.0420  498 ASN A CG  
1548 O OD1 . ASN A 202 ? 0.9831 1.2444 0.9331 -0.4079 -0.0920 0.0345  498 ASN A OD1 
1549 N ND2 . ASN A 202 ? 1.1105 1.2519 0.9424 -0.4678 -0.0935 0.0434  498 ASN A ND2 
1550 N N   . VAL A 203 ? 0.8490 1.4263 0.7938 -0.4869 -0.0809 0.0636  499 VAL A N   
1551 C CA  . VAL A 203 ? 0.8440 1.5038 0.7702 -0.5188 -0.0774 0.0732  499 VAL A CA  
1552 C C   . VAL A 203 ? 0.8361 1.6127 0.8168 -0.4830 -0.0694 0.0747  499 VAL A C   
1553 O O   . VAL A 203 ? 0.8665 1.7038 0.8349 -0.5021 -0.0647 0.0816  499 VAL A O   
1554 C CB  . VAL A 203 ? 0.9429 1.6241 0.8441 -0.5460 -0.0821 0.0768  499 VAL A CB  
1555 C CG1 . VAL A 203 ? 0.9231 1.7029 0.8062 -0.5792 -0.0788 0.0868  499 VAL A CG1 
1556 C CG2 . VAL A 203 ? 1.0882 1.6471 0.9229 -0.5821 -0.0895 0.0756  499 VAL A CG2 
1557 N N   . GLN A 204 ? 0.7886 1.5958 0.8243 -0.4294 -0.0679 0.0683  500 GLN A N   
1558 C CA  . GLN A 204 ? 0.8994 1.8014 0.9768 -0.3886 -0.0598 0.0690  500 GLN A CA  
1559 C C   . GLN A 204 ? 0.9137 1.7876 0.9961 -0.3807 -0.0551 0.0672  500 GLN A C   
1560 O O   . GLN A 204 ? 0.9328 1.8724 1.0162 -0.3809 -0.0486 0.0720  500 GLN A O   
1561 C CB  . GLN A 204 ? 0.9463 1.8797 1.0702 -0.3308 -0.0595 0.0628  500 GLN A CB  
1562 C CG  . GLN A 204 ? 1.0109 2.0304 1.1658 -0.2829 -0.0507 0.0631  500 GLN A CG  
1563 C CD  . GLN A 204 ? 1.0554 2.1063 1.2428 -0.2232 -0.0500 0.0584  500 GLN A CD  
1564 O OE1 . GLN A 204 ? 1.0733 2.0727 1.2693 -0.2128 -0.0562 0.0533  500 GLN A OE1 
1565 N NE2 . GLN A 204 ? 1.0857 2.2180 1.2852 -0.1817 -0.0425 0.0601  500 GLN A NE2 
1566 N N   . PHE A 205 ? 0.8680 1.6469 0.9512 -0.3742 -0.0587 0.0603  501 PHE A N   
1567 C CA  . PHE A 205 ? 0.8123 1.5634 0.9002 -0.3664 -0.0547 0.0583  501 PHE A CA  
1568 C C   . PHE A 205 ? 0.8685 1.6104 0.9101 -0.4146 -0.0526 0.0665  501 PHE A C   
1569 O O   . PHE A 205 ? 0.8427 1.6243 0.8926 -0.4082 -0.0459 0.0689  501 PHE A O   
1570 C CB  . PHE A 205 ? 0.7707 1.4203 0.8591 -0.3569 -0.0605 0.0501  501 PHE A CB  
1571 C CG  . PHE A 205 ? 0.9118 1.5332 1.0035 -0.3498 -0.0572 0.0479  501 PHE A CG  
1572 C CD1 . PHE A 205 ? 0.9437 1.6102 1.0761 -0.3006 -0.0504 0.0433  501 PHE A CD1 
1573 C CD2 . PHE A 205 ? 0.9955 1.5338 1.0386 -0.3869 -0.0597 0.0506  501 PHE A CD2 
1574 C CE1 . PHE A 205 ? 0.9531 1.5751 1.0766 -0.2843 -0.0452 0.0404  501 PHE A CE1 
1575 C CE2 . PHE A 205 ? 1.0458 1.5444 1.0823 -0.3689 -0.0548 0.0486  501 PHE A CE2 
1576 C CZ  . PHE A 205 ? 0.9997 1.5428 1.0785 -0.3183 -0.0475 0.0433  501 PHE A CZ  
1577 N N   . THR A 206 ? 0.8992 1.5849 0.8865 -0.4628 -0.0585 0.0709  502 THR A N   
1578 C CA  . THR A 206 ? 0.9287 1.6030 0.8612 -0.5122 -0.0577 0.0793  502 THR A CA  
1579 C C   . THR A 206 ? 0.9919 1.7919 0.9380 -0.5161 -0.0517 0.0863  502 THR A C   
1580 O O   . THR A 206 ? 1.0074 1.8273 0.9332 -0.5367 -0.0481 0.0916  502 THR A O   
1581 C CB  . THR A 206 ? 0.9227 1.5179 0.7881 -0.5597 -0.0657 0.0822  502 THR A CB  
1582 O OG1 . THR A 206 ? 1.0103 1.4889 0.8602 -0.5489 -0.0712 0.0751  502 THR A OG1 
1583 C CG2 . THR A 206 ? 0.8995 1.4682 0.6955 -0.6136 -0.0665 0.0905  502 THR A CG2 
1584 N N   . GLU A 207 ? 1.0211 1.9079 0.9991 -0.4942 -0.0508 0.0864  503 GLU A N   
1585 C CA  . GLU A 207 ? 1.0861 2.0986 1.0748 -0.4916 -0.0456 0.0929  503 GLU A CA  
1586 C C   . GLU A 207 ? 0.9938 2.0597 1.0247 -0.4434 -0.0371 0.0902  503 GLU A C   
1587 O O   . GLU A 207 ? 1.0593 2.1951 1.0823 -0.4525 -0.0326 0.0959  503 GLU A O   
1588 C CB  . GLU A 207 ? 1.1649 2.2516 1.1714 -0.4766 -0.0470 0.0938  503 GLU A CB  
1589 C CG  . GLU A 207 ? 1.3370 2.4452 1.2940 -0.5349 -0.0522 0.1018  503 GLU A CG  
1590 C CD  . GLU A 207 ? 1.4390 2.5444 1.4005 -0.5319 -0.0570 0.1000  503 GLU A CD  
1591 O OE1 . GLU A 207 ? 1.4206 2.5599 1.4301 -0.4784 -0.0548 0.0948  503 GLU A OE1 
1592 O OE2 . GLU A 207 ? 1.5159 2.5806 1.4282 -0.5830 -0.0632 0.1037  503 GLU A OE2 
1593 N N   . ILE A 208 ? 0.9112 1.9460 0.9836 -0.3922 -0.0353 0.0813  504 ILE A N   
1594 C CA  . ILE A 208 ? 0.9161 1.9913 1.0230 -0.3432 -0.0272 0.0776  504 ILE A CA  
1595 C C   . ILE A 208 ? 0.9024 1.9467 0.9887 -0.3691 -0.0240 0.0804  504 ILE A C   
1596 O O   . ILE A 208 ? 0.8543 1.9672 0.9460 -0.3569 -0.0172 0.0834  504 ILE A O   
1597 C CB  . ILE A 208 ? 0.8768 1.9065 1.0217 -0.2908 -0.0276 0.0671  504 ILE A CB  
1598 C CG1 . ILE A 208 ? 0.9021 1.9646 1.0638 -0.2632 -0.0306 0.0651  504 ILE A CG1 
1599 C CG2 . ILE A 208 ? 0.8486 1.9107 1.0197 -0.2408 -0.0192 0.0627  504 ILE A CG2 
1600 C CD1 . ILE A 208 ? 0.9297 1.9251 1.1157 -0.2292 -0.0350 0.0555  504 ILE A CD1 
1601 N N   . CYS A 209 ? 0.9410 1.8795 0.9986 -0.4042 -0.0291 0.0796  505 CYS A N   
1602 C CA  . CYS A 209 ? 0.9676 1.8644 0.9951 -0.4338 -0.0269 0.0833  505 CYS A CA  
1603 C C   . CYS A 209 ? 1.0822 2.0426 1.0745 -0.4748 -0.0256 0.0933  505 CYS A C   
1604 O O   . CYS A 209 ? 1.0776 2.0628 1.0643 -0.4792 -0.0202 0.0966  505 CYS A O   
1605 C CB  . CYS A 209 ? 0.9373 1.7029 0.9238 -0.4665 -0.0343 0.0819  505 CYS A CB  
1606 S SG  . CYS A 209 ? 0.8870 1.5779 0.9107 -0.4224 -0.0376 0.0699  505 CYS A SG  
1607 N N   . ILE A 210 ? 1.0960 2.0880 1.0632 -0.5062 -0.0310 0.0982  506 ILE A N   
1608 C CA  . ILE A 210 ? 1.1547 2.2167 1.0865 -0.5485 -0.0317 0.1074  506 ILE A CA  
1609 C C   . ILE A 210 ? 1.1390 2.3346 1.1105 -0.5092 -0.0246 0.1089  506 ILE A C   
1610 O O   . ILE A 210 ? 1.0825 2.3321 1.0400 -0.5255 -0.0221 0.1142  506 ILE A O   
1611 C CB  . ILE A 210 ? 1.1574 2.2184 1.0476 -0.5947 -0.0399 0.1120  506 ILE A CB  
1612 C CG1 . ILE A 210 ? 1.1895 2.1082 1.0249 -0.6340 -0.0473 0.1107  506 ILE A CG1 
1613 C CG2 . ILE A 210 ? 1.2653 2.4140 1.1204 -0.6388 -0.0417 0.1211  506 ILE A CG2 
1614 C CD1 . ILE A 210 ? 1.2582 2.1601 1.0608 -0.6647 -0.0548 0.1123  506 ILE A CD1 
1615 N N   . GLN A 211 ? 1.1147 2.3618 1.1314 -0.4547 -0.0216 0.1040  507 GLN A N   
1616 C CA  . GLN A 211 ? 1.1256 2.4885 1.1727 -0.4068 -0.0149 0.1045  507 GLN A CA  
1617 C C   . GLN A 211 ? 1.0463 2.4041 1.1125 -0.3730 -0.0070 0.1009  507 GLN A C   
1618 O O   . GLN A 211 ? 1.0121 2.4615 1.0860 -0.3481 -0.0021 0.1035  507 GLN A O   
1619 C CB  . GLN A 211 ? 1.1317 2.5272 1.2132 -0.3518 -0.0139 0.0992  507 GLN A CB  
1620 C CG  . GLN A 211 ? 1.1689 2.6762 1.2711 -0.2944 -0.0075 0.0996  507 GLN A CG  
1621 C CD  . GLN A 211 ? 1.2026 2.7887 1.3066 -0.2781 -0.0097 0.1024  507 GLN A CD  
1622 O OE1 . GLN A 211 ? 1.2574 2.8553 1.3393 -0.3267 -0.0157 0.1079  507 GLN A OE1 
1623 N NE2 . GLN A 211 ? 1.1658 2.8032 1.2903 -0.2084 -0.0047 0.0987  507 GLN A NE2 
1624 N N   . GLN A 212 ? 1.0347 2.2905 1.1064 -0.3703 -0.0060 0.0952  508 GLN A N   
1625 C CA  . GLN A 212 ? 1.0023 2.2474 1.0861 -0.3466 0.0017  0.0923  508 GLN A CA  
1626 C C   . GLN A 212 ? 1.0308 2.2448 1.0748 -0.4030 0.0010  0.0994  508 GLN A C   
1627 O O   . GLN A 212 ? 0.9656 2.1699 1.0148 -0.3899 0.0077  0.0983  508 GLN A O   
1628 C CB  . GLN A 212 ? 0.9718 2.1315 1.0820 -0.3116 0.0033  0.0822  508 GLN A CB  
1629 C CG  . GLN A 212 ? 1.0436 2.2156 1.1873 -0.2575 0.0025  0.0743  508 GLN A CG  
1630 C CD  . GLN A 212 ? 1.1078 2.3619 1.2715 -0.1941 0.0103  0.0712  508 GLN A CD  
1631 O OE1 . GLN A 212 ? 1.1493 2.3784 1.3321 -0.1439 0.0151  0.0623  508 GLN A OE1 
1632 N NE2 . GLN A 212 ? 1.1425 2.4918 1.2957 -0.1949 0.0107  0.0781  508 GLN A NE2 
1633 N N   . GLY A 213 ? 1.1020 2.2944 1.1017 -0.4646 -0.0071 0.1063  509 GLY A N   
1634 C CA  . GLY A 213 ? 1.1899 2.3545 1.1410 -0.5206 -0.0093 0.1135  509 GLY A CA  
1635 C C   . GLY A 213 ? 1.2455 2.2736 1.1465 -0.5670 -0.0157 0.1142  509 GLY A C   
1636 O O   . GLY A 213 ? 1.2500 2.2316 1.1106 -0.6012 -0.0157 0.1186  509 GLY A O   
1637 N N   . TRP A 214 ? 1.3575 2.3156 1.2549 -0.5669 -0.0213 0.1102  510 TRP A N   
1638 C CA  . TRP A 214 ? 1.3548 2.1795 1.1917 -0.6095 -0.0284 0.1112  510 TRP A CA  
1639 C C   . TRP A 214 ? 1.4125 2.2350 1.1814 -0.6738 -0.0363 0.1186  510 TRP A C   
1640 O O   . TRP A 214 ? 1.4430 2.3614 1.2166 -0.6865 -0.0385 0.1220  510 TRP A O   
1641 C CB  . TRP A 214 ? 1.2945 2.0448 1.1410 -0.5919 -0.0334 0.1045  510 TRP A CB  
1642 C CG  . TRP A 214 ? 1.3046 1.9056 1.0940 -0.6151 -0.0389 0.1037  510 TRP A CG  
1643 C CD1 . TRP A 214 ? 1.2818 1.8122 1.0465 -0.6180 -0.0361 0.1050  510 TRP A CD1 
1644 C CD2 . TRP A 214 ? 1.3604 1.8624 1.1029 -0.6354 -0.0481 0.1018  510 TRP A CD2 
1645 N NE1 . TRP A 214 ? 1.3380 1.7293 1.0414 -0.6350 -0.0433 0.1040  510 TRP A NE1 
1646 C CE2 . TRP A 214 ? 1.3594 1.7302 1.0473 -0.6453 -0.0508 0.1016  510 TRP A CE2 
1647 C CE3 . TRP A 214 ? 1.3932 1.9034 1.1310 -0.6437 -0.0540 0.1004  510 TRP A CE3 
1648 C CZ2 . TRP A 214 ? 1.4312 1.6777 1.0577 -0.6587 -0.0594 0.0992  510 TRP A CZ2 
1649 C CZ3 . TRP A 214 ? 1.4331 1.8224 1.1137 -0.6610 -0.0621 0.0982  510 TRP A CZ3 
1650 C CH2 . TRP A 214 ? 1.4823 1.7410 1.1070 -0.6663 -0.0648 0.0973  510 TRP A CH2 
1651 N N   . LYS A 215 ? 1.3923 2.1028 1.0920 -0.7141 -0.0410 0.1210  511 LYS A N   
1652 C CA  . LYS A 215 ? 1.4762 2.1518 1.0953 -0.7784 -0.0505 0.1261  511 LYS A CA  
1653 C C   . LYS A 215 ? 1.4350 1.9740 1.0011 -0.7911 -0.0582 0.1226  511 LYS A C   
1654 O O   . LYS A 215 ? 1.4540 1.8689 0.9810 -0.7880 -0.0593 0.1205  511 LYS A O   
1655 C CB  . LYS A 215 ? 1.5441 2.1956 1.1127 -0.8154 -0.0509 0.1310  511 LYS A CB  
1656 C CG  . LYS A 215 ? 1.5534 2.3536 1.1563 -0.8196 -0.0467 0.1358  511 LYS A CG  
1657 C CD  . LYS A 215 ? 1.6669 2.5132 1.2121 -0.8843 -0.0561 0.1415  511 LYS A CD  
1658 C CE  . LYS A 215 ? 1.6891 2.5866 1.2409 -0.8899 -0.0610 0.1416  511 LYS A CE  
1659 N NZ  . LYS A 215 ? 1.7706 2.6925 1.2517 -0.9604 -0.0711 0.1473  511 LYS A NZ  
1660 N N   . ALA A 216 ? 1.3678 1.9304 0.9303 -0.8019 -0.0631 0.1222  512 ALA A N   
1661 C CA  . ALA A 216 ? 1.3916 1.8399 0.9185 -0.8014 -0.0692 0.1179  512 ALA A CA  
1662 C C   . ALA A 216 ? 1.5481 1.8841 0.9629 -0.8588 -0.0785 0.1205  512 ALA A C   
1663 O O   . ALA A 216 ? 1.6176 2.0014 0.9899 -0.9088 -0.0830 0.1258  512 ALA A O   
1664 C CB  . ALA A 216 ? 1.3139 1.8332 0.8824 -0.7880 -0.0702 0.1164  512 ALA A CB  
1665 N N   . PRO A 217 ? 1.5430 1.7283 0.9019 -0.8522 -0.0822 0.1165  513 PRO A N   
1666 C CA  . PRO A 217 ? 1.6632 1.7276 0.9050 -0.9003 -0.0918 0.1173  513 PRO A CA  
1667 C C   . PRO A 217 ? 1.8240 1.8685 1.0377 -0.9153 -0.0979 0.1162  513 PRO A C   
1668 O O   . PRO A 217 ? 1.9678 1.8778 1.0994 -0.9242 -0.1044 0.1133  513 PRO A O   
1669 C CB  . PRO A 217 ? 1.6788 1.5947 0.8771 -0.8723 -0.0923 0.1129  513 PRO A CB  
1670 C CG  . PRO A 217 ? 1.5376 1.4898 0.8325 -0.8107 -0.0849 0.1090  513 PRO A CG  
1671 C CD  . PRO A 217 ? 1.4726 1.5939 0.8650 -0.8011 -0.0775 0.1117  513 PRO A CD  
1672 N N   . ARG A 218 ? 1.8276 2.0047 1.1041 -0.9165 -0.0956 0.1188  514 ARG A N   
1673 C CA  . ARG A 218 ? 1.7239 1.9125 1.0041 -0.9184 -0.0989 0.1179  514 ARG A CA  
1674 C C   . ARG A 218 ? 1.7677 1.8049 0.9465 -0.9411 -0.1073 0.1156  514 ARG A C   
1675 O O   . ARG A 218 ? 1.8982 1.9215 1.0032 -0.9939 -0.1136 0.1197  514 ARG A O   
1676 C CB  . ARG A 218 ? 1.7273 2.0534 1.0205 -0.9558 -0.0993 0.1247  514 ARG A CB  
1677 C CG  . ARG A 218 ? 1.6663 2.1487 1.0614 -0.9220 -0.0907 0.1263  514 ARG A CG  
1678 C CD  . ARG A 218 ? 1.7300 2.3508 1.1431 -0.9459 -0.0911 0.1323  514 ARG A CD  
1679 N NE  . ARG A 218 ? 1.6936 2.4158 1.2045 -0.8897 -0.0844 0.1296  514 ARG A NE  
1680 C CZ  . ARG A 218 ? 1.6723 2.5333 1.2486 -0.8635 -0.0780 0.1319  514 ARG A CZ  
1681 N NH1 . ARG A 218 ? 1.6229 2.5577 1.2767 -0.8091 -0.0726 0.1283  514 ARG A NH1 
1682 N NH2 . ARG A 218 ? 1.7144 2.6389 1.2739 -0.8901 -0.0773 0.1373  514 ARG A NH2 
1683 N N   . GLY A 219 ? 1.7258 1.6493 0.8962 -0.9002 -0.1074 0.1090  515 GLY A N   
1684 C CA  . GLY A 219 ? 1.8069 1.5908 0.8953 -0.9018 -0.1142 0.1052  515 GLY A CA  
1685 C C   . GLY A 219 ? 1.7517 1.5221 0.9035 -0.8456 -0.1123 0.0984  515 GLY A C   
1686 O O   . GLY A 219 ? 1.5848 1.4692 0.8373 -0.8198 -0.1075 0.0974  515 GLY A O   
1687 N N   . ARG A 220 ? 1.8677 1.4994 0.9590 -0.8233 -0.1164 0.0930  516 ARG A N   
1688 C CA  . ARG A 220 ? 1.8234 1.4368 0.9648 -0.7736 -0.1161 0.0859  516 ARG A CA  
1689 C C   . ARG A 220 ? 1.8009 1.4164 1.0105 -0.7192 -0.1112 0.0806  516 ARG A C   
1690 O O   . ARG A 220 ? 1.7167 1.4428 1.0296 -0.6960 -0.1059 0.0793  516 ARG A O   
1691 C CB  . ARG A 220 ? 1.9452 1.4128 0.9867 -0.7707 -0.1230 0.0822  516 ARG A CB  
1692 C CG  . ARG A 220 ? 1.8777 1.3493 0.9598 -0.7402 -0.1243 0.0766  516 ARG A CG  
1693 C CD  . ARG A 220 ? 1.9412 1.4044 0.9649 -0.7844 -0.1294 0.0805  516 ARG A CD  
1694 N NE  . ARG A 220 ? 2.0180 1.3442 0.9546 -0.7700 -0.1348 0.0762  516 ARG A NE  
1695 C CZ  . ARG A 220 ? 2.0265 1.3482 0.9814 -0.7519 -0.1369 0.0721  516 ARG A CZ  
1696 N NH1 . ARG A 220 ? 1.9825 1.4272 1.0378 -0.7479 -0.1344 0.0715  516 ARG A NH1 
1697 N NH2 . ARG A 220 ? 2.1127 1.3069 0.9818 -0.7360 -0.1414 0.0683  516 ARG A NH2 
1698 N N   . PHE A 221 ? 1.8473 1.3369 0.9915 -0.6978 -0.1132 0.0776  517 PHE A N   
1699 C CA  . PHE A 221 ? 1.7414 1.2074 0.9315 -0.6438 -0.1101 0.0722  517 PHE A CA  
1700 C C   . PHE A 221 ? 1.7911 1.3049 1.0129 -0.6469 -0.1043 0.0765  517 PHE A C   
1701 O O   . PHE A 221 ? 1.8499 1.2850 1.0324 -0.6277 -0.1038 0.0762  517 PHE A O   
1702 C CB  . PHE A 221 ? 1.7422 1.0549 0.8427 -0.6135 -0.1149 0.0672  517 PHE A CB  
1703 C CG  . PHE A 221 ? 1.7028 0.9695 0.7741 -0.6051 -0.1199 0.0626  517 PHE A CG  
1704 C CD1 . PHE A 221 ? 1.7974 0.9650 0.7543 -0.6307 -0.1255 0.0641  517 PHE A CD1 
1705 C CD2 . PHE A 221 ? 1.5298 0.8496 0.6832 -0.5721 -0.1192 0.0564  517 PHE A CD2 
1706 C CE1 . PHE A 221 ? 1.8236 0.9480 0.7510 -0.6226 -0.1296 0.0604  517 PHE A CE1 
1707 C CE2 . PHE A 221 ? 1.5332 0.8107 0.6591 -0.5639 -0.1235 0.0522  517 PHE A CE2 
1708 C CZ  . PHE A 221 ? 1.6271 0.8083 0.6412 -0.5887 -0.1284 0.0546  517 PHE A CZ  
1709 N N   . ASP A 222 ? 1.6944 1.3444 0.9886 -0.6682 -0.0996 0.0807  518 ASP A N   
1710 C CA  . ASP A 222 ? 1.5099 1.2304 0.8463 -0.6713 -0.0930 0.0850  518 ASP A CA  
1711 C C   . ASP A 222 ? 1.4902 1.2667 0.9244 -0.6226 -0.0879 0.0799  518 ASP A C   
1712 O O   . ASP A 222 ? 1.4945 1.3643 1.0074 -0.6069 -0.0864 0.0762  518 ASP A O   
1713 C CB  . ASP A 222 ? 1.4019 1.2473 0.7649 -0.7121 -0.0903 0.0915  518 ASP A CB  
1714 C CG  . ASP A 222 ? 1.5431 1.3407 0.8072 -0.7676 -0.0969 0.0960  518 ASP A CG  
1715 O OD1 . ASP A 222 ? 1.6520 1.3133 0.8222 -0.7735 -0.1030 0.0939  518 ASP A OD1 
1716 O OD2 . ASP A 222 ? 1.5495 1.4473 0.8259 -0.8044 -0.0962 0.1014  518 ASP A OD2 
1717 N N   . VAL A 223 ? 1.4413 1.1581 0.8651 -0.5985 -0.0860 0.0792  519 VAL A N   
1718 C CA  . VAL A 223 ? 1.3139 1.0759 0.8207 -0.5565 -0.0826 0.0738  519 VAL A CA  
1719 C C   . VAL A 223 ? 1.2393 1.1510 0.8311 -0.5620 -0.0749 0.0765  519 VAL A C   
1720 O O   . VAL A 223 ? 1.2256 1.1707 0.8034 -0.5857 -0.0696 0.0840  519 VAL A O   
1721 C CB  . VAL A 223 ? 1.3694 1.0395 0.8381 -0.5239 -0.0818 0.0735  519 VAL A CB  
1722 C CG1 . VAL A 223 ? 1.2642 0.9915 0.8201 -0.4530 -0.0782 0.0631  519 VAL A CG1 
1723 C CG2 . VAL A 223 ? 1.4307 0.9438 0.7953 -0.5203 -0.0892 0.0731  519 VAL A CG2 
1724 N N   . LEU A 224 ? 1.0913 1.0919 0.7675 -0.5355 -0.0741 0.0698  520 LEU A N   
1725 C CA  . LEU A 224 ? 1.0472 1.1884 0.7985 -0.5295 -0.0665 0.0715  520 LEU A CA  
1726 C C   . LEU A 224 ? 1.0623 1.2156 0.8390 -0.4902 -0.0591 0.0695  520 LEU A C   
1727 O O   . LEU A 224 ? 1.1186 1.1882 0.8773 -0.4530 -0.0605 0.0640  520 LEU A O   
1728 C CB  . LEU A 224 ? 0.8463 1.0660 0.6716 -0.4955 -0.0671 0.0638  520 LEU A CB  
1729 C CG  . LEU A 224 ? 0.8884 1.1288 0.7032 -0.5134 -0.0711 0.0651  520 LEU A CG  
1730 C CD1 . LEU A 224 ? 0.7532 0.9832 0.6084 -0.4781 -0.0759 0.0554  520 LEU A CD1 
1731 C CD2 . LEU A 224 ? 0.8554 1.2254 0.7041 -0.5220 -0.0652 0.0708  520 LEU A CD2 
1732 N N   . PRO A 225 ? 1.0156 1.2776 0.8335 -0.4951 -0.0511 0.0738  521 PRO A N   
1733 C CA  . PRO A 225 ? 1.0176 1.2986 0.8638 -0.4534 -0.0439 0.0704  521 PRO A CA  
1734 C C   . PRO A 225 ? 0.9370 1.2620 0.8533 -0.3910 -0.0422 0.0586  521 PRO A C   
1735 O O   . PRO A 225 ? 0.9302 1.3039 0.8825 -0.3827 -0.0441 0.0554  521 PRO A O   
1736 C CB  . PRO A 225 ? 1.0443 1.4295 0.8998 -0.4883 -0.0358 0.0805  521 PRO A CB  
1737 C CG  . PRO A 225 ? 1.0366 1.5053 0.9134 -0.5137 -0.0378 0.0835  521 PRO A CG  
1738 C CD  . PRO A 225 ? 1.0029 1.3748 0.8364 -0.5296 -0.0481 0.0811  521 PRO A CD  
1739 N N   . LEU A 226 ? 0.8866 1.1893 0.8163 -0.3488 -0.0389 0.0523  522 LEU A N   
1740 C CA  . LEU A 226 ? 0.8154 1.1495 0.8007 -0.2939 -0.0370 0.0411  522 LEU A CA  
1741 C C   . LEU A 226 ? 0.7745 1.2236 0.8039 -0.2822 -0.0288 0.0421  522 LEU A C   
1742 O O   . LEU A 226 ? 0.7423 1.2403 0.7642 -0.3001 -0.0224 0.0490  522 LEU A O   
1743 C CB  . LEU A 226 ? 0.7334 1.0078 0.7130 -0.2577 -0.0370 0.0338  522 LEU A CB  
1744 C CG  . LEU A 226 ? 0.8560 1.0247 0.7952 -0.2544 -0.0449 0.0316  522 LEU A CG  
1745 C CD1 . LEU A 226 ? 0.8912 1.0188 0.8212 -0.2238 -0.0448 0.0266  522 LEU A CD1 
1746 C CD2 . LEU A 226 ? 0.7457 0.8959 0.7054 -0.2363 -0.0503 0.0244  522 LEU A CD2 
1747 N N   . LEU A 227 ? 0.7541 1.2459 0.8250 -0.2501 -0.0287 0.0356  523 LEU A N   
1748 C CA  . LEU A 227 ? 0.7482 1.3409 0.8567 -0.2230 -0.0210 0.0348  523 LEU A CA  
1749 C C   . LEU A 227 ? 0.7187 1.2805 0.8462 -0.1671 -0.0193 0.0224  523 LEU A C   
1750 O O   . LEU A 227 ? 0.6731 1.2101 0.8153 -0.1433 -0.0231 0.0156  523 LEU A O   
1751 C CB  . LEU A 227 ? 0.6834 1.3516 0.8146 -0.2306 -0.0224 0.0384  523 LEU A CB  
1752 C CG  . LEU A 227 ? 0.7275 1.5192 0.8695 -0.2538 -0.0165 0.0487  523 LEU A CG  
1753 C CD1 . LEU A 227 ? 0.7264 1.6000 0.9012 -0.2326 -0.0173 0.0484  523 LEU A CD1 
1754 C CD2 . LEU A 227 ? 0.6307 1.4765 0.7777 -0.2352 -0.0062 0.0499  523 LEU A CD2 
1755 N N   . LEU A 228 ? 0.7168 1.2792 0.8397 -0.1494 -0.0136 0.0198  524 LEU A N   
1756 C CA  . LEU A 228 ? 0.6791 1.1965 0.8073 -0.1060 -0.0132 0.0078  524 LEU A CA  
1757 C C   . LEU A 228 ? 0.6475 1.2305 0.7905 -0.0681 -0.0047 0.0042  524 LEU A C   
1758 O O   . LEU A 228 ? 0.5323 1.1731 0.6719 -0.0720 0.0025  0.0094  524 LEU A O   
1759 C CB  . LEU A 228 ? 0.6725 1.1270 0.7760 -0.1127 -0.0148 0.0061  524 LEU A CB  
1760 C CG  . LEU A 228 ? 0.6367 1.0276 0.7139 -0.1471 -0.0223 0.0114  524 LEU A CG  
1761 C CD1 . LEU A 228 ? 0.5678 0.9060 0.6165 -0.1490 -0.0234 0.0112  524 LEU A CD1 
1762 C CD2 . LEU A 228 ? 0.5610 0.9022 0.6461 -0.1368 -0.0298 0.0053  524 LEU A CD2 
1763 N N   . GLN A 229 ? 0.6371 1.2076 0.7905 -0.0307 -0.0054 -0.0043 525 GLN A N   
1764 C CA  . GLN A 229 ? 0.7204 1.3274 0.8746 0.0152  0.0019  -0.0099 525 GLN A CA  
1765 C C   . GLN A 229 ? 0.7589 1.2872 0.8949 0.0404  0.0008  -0.0223 525 GLN A C   
1766 O O   . GLN A 229 ? 0.7720 1.2315 0.9054 0.0401  -0.0059 -0.0287 525 GLN A O   
1767 C CB  . GLN A 229 ? 0.6682 1.3075 0.8347 0.0400  0.0016  -0.0101 525 GLN A CB  
1768 C CG  . GLN A 229 ? 0.6707 1.2942 0.8220 0.0952  0.0061  -0.0197 525 GLN A CG  
1769 C CD  . GLN A 229 ? 0.7095 1.3526 0.8650 0.1230  0.0052  -0.0195 525 GLN A CD  
1770 O OE1 . GLN A 229 ? 0.7592 1.4200 0.9330 0.0995  -0.0002 -0.0136 525 GLN A OE1 
1771 N NE2 . GLN A 229 ? 0.6940 1.3279 0.8259 0.1753  0.0102  -0.0261 525 GLN A NE2 
1772 N N   . ALA A 230 ? 0.7452 1.2867 0.8668 0.0596  0.0073  -0.0256 526 ALA A N   
1773 C CA  . ALA A 230 ? 0.7499 1.2204 0.8489 0.0800  0.0059  -0.0378 526 ALA A CA  
1774 C C   . ALA A 230 ? 0.7123 1.1904 0.7906 0.1292  0.0126  -0.0455 526 ALA A C   
1775 O O   . ALA A 230 ? 0.6522 1.2045 0.7311 0.1490  0.0211  -0.0408 526 ALA A O   
1776 C CB  . ALA A 230 ? 0.7568 1.2164 0.8453 0.0615  0.0064  -0.0369 526 ALA A CB  
1777 N N   . ASN A 231 ? 0.7491 1.1504 0.8044 0.1487  0.0089  -0.0570 527 ASN A N   
1778 C CA  . ASN A 231 ? 0.8825 1.2586 0.8997 0.1960  0.0140  -0.0663 527 ASN A CA  
1779 C C   . ASN A 231 ? 0.8854 1.3314 0.9050 0.2317  0.0212  -0.0605 527 ASN A C   
1780 O O   . ASN A 231 ? 0.8525 1.3259 0.8465 0.2733  0.0294  -0.0631 527 ASN A O   
1781 C CB  . ASN A 231 ? 1.0150 1.3799 1.0054 0.2074  0.0184  -0.0727 527 ASN A CB  
1782 C CG  . ASN A 231 ? 1.1605 1.4682 1.0966 0.2529  0.0219  -0.0852 527 ASN A CG  
1783 O OD1 . ASN A 231 ? 1.2347 1.5822 1.1500 0.2929  0.0310  -0.0854 527 ASN A OD1 
1784 N ND2 . ASN A 231 ? 1.1780 1.3920 1.0858 0.2469  0.0147  -0.0954 527 ASN A ND2 
1785 N N   . GLY A 232 ? 0.9515 1.4295 0.9999 0.2177  0.0177  -0.0527 528 GLY A N   
1786 C CA  . GLY A 232 ? 1.0039 1.5607 1.0592 0.2488  0.0231  -0.0460 528 GLY A CA  
1787 C C   . GLY A 232 ? 1.0460 1.7230 1.1268 0.2417  0.0301  -0.0350 528 GLY A C   
1788 O O   . GLY A 232 ? 1.1212 1.8831 1.2135 0.2634  0.0339  -0.0280 528 GLY A O   
1789 N N   . ASN A 233 ? 0.9054 1.5971 0.9937 0.2108  0.0320  -0.0324 529 ASN A N   
1790 C CA  . ASN A 233 ? 0.8506 1.6571 0.9580 0.1988  0.0395  -0.0212 529 ASN A CA  
1791 C C   . ASN A 233 ? 0.8185 1.6884 0.9613 0.1511  0.0351  -0.0085 529 ASN A C   
1792 O O   . ASN A 233 ? 0.8730 1.6852 1.0251 0.1185  0.0259  -0.0083 529 ASN A O   
1793 C CB  . ASN A 233 ? 0.7685 1.5630 0.8673 0.1764  0.0425  -0.0215 529 ASN A CB  
1794 C CG  . ASN A 233 ? 0.7731 1.5497 0.8366 0.2261  0.0502  -0.0314 529 ASN A CG  
1795 O OD1 . ASN A 233 ? 0.8871 1.7479 0.9478 0.2455  0.0603  -0.0271 529 ASN A OD1 
1796 N ND2 . ASN A 233 ? 0.6680 1.3356 0.7007 0.2453  0.0454  -0.0448 529 ASN A ND2 
1797 N N   . ASP A 234 ? 0.7951 1.7879 0.9542 0.1464  0.0420  0.0023  530 ASP A N   
1798 C CA  . ASP A 234 ? 0.8518 1.9131 1.0381 0.0959  0.0379  0.0147  530 ASP A CA  
1799 C C   . ASP A 234 ? 0.8620 1.8589 1.0460 0.0316  0.0314  0.0184  530 ASP A C   
1800 O O   . ASP A 234 ? 0.9522 1.9275 1.1221 0.0181  0.0348  0.0184  530 ASP A O   
1801 C CB  . ASP A 234 ? 0.9112 2.1002 1.1004 0.0935  0.0445  0.0258  530 ASP A CB  
1802 C CG  . ASP A 234 ? 1.0109 2.2325 1.1796 0.1601  0.0469  0.0230  530 ASP A CG  
1803 O OD1 . ASP A 234 ? 1.0805 2.3699 1.2325 0.1768  0.0512  0.0279  530 ASP A OD1 
1804 O OD2 . ASP A 234 ? 1.0479 2.2245 1.2124 0.1968  0.0437  0.0163  530 ASP A OD2 
1805 N N   . PRO A 235 ? 0.7667 1.7283 0.9587 -0.0058 0.0220  0.0215  531 PRO A N   
1806 C CA  . PRO A 235 ? 0.7215 1.5954 0.8997 -0.0534 0.0150  0.0225  531 PRO A CA  
1807 C C   . PRO A 235 ? 0.6862 1.6057 0.8548 -0.1077 0.0176  0.0348  531 PRO A C   
1808 O O   . PRO A 235 ? 0.7230 1.7542 0.9020 -0.1214 0.0236  0.0442  531 PRO A O   
1809 C CB  . PRO A 235 ? 0.7019 1.5355 0.8876 -0.0701 0.0052  0.0223  531 PRO A CB  
1810 C CG  . PRO A 235 ? 0.6664 1.6073 0.8724 -0.0627 0.0074  0.0285  531 PRO A CG  
1811 C CD  . PRO A 235 ? 0.7195 1.7198 0.9290 -0.0043 0.0172  0.0245  531 PRO A CD  
1812 N N   . GLU A 236 ? 0.7313 1.5621 0.8757 -0.1396 0.0129  0.0352  532 GLU A N   
1813 C CA  . GLU A 236 ? 0.7413 1.5847 0.8619 -0.1879 0.0157  0.0459  532 GLU A CA  
1814 C C   . GLU A 236 ? 0.7492 1.5029 0.8398 -0.2360 0.0061  0.0502  532 GLU A C   
1815 O O   . GLU A 236 ? 0.7624 1.4239 0.8476 -0.2213 -0.0015 0.0422  532 GLU A O   
1816 C CB  . GLU A 236 ? 0.6984 1.5157 0.8043 -0.1666 0.0216  0.0418  532 GLU A CB  
1817 C CG  . GLU A 236 ? 0.6555 1.5244 0.7797 -0.1073 0.0297  0.0334  532 GLU A CG  
1818 C CD  . GLU A 236 ? 0.7305 1.5427 0.8366 -0.0816 0.0324  0.0252  532 GLU A CD  
1819 O OE1 . GLU A 236 ? 0.7312 1.4864 0.8134 -0.1117 0.0295  0.0286  532 GLU A OE1 
1820 O OE2 . GLU A 236 ? 0.6669 1.4874 0.7772 -0.0301 0.0368  0.0152  532 GLU A OE2 
1821 N N   . LEU A 237 ? 0.7690 1.5480 0.8341 -0.2937 0.0067  0.0630  533 LEU A N   
1822 C CA  . LEU A 237 ? 0.8380 1.5299 0.8622 -0.3418 -0.0023 0.0680  533 LEU A CA  
1823 C C   . LEU A 237 ? 0.9271 1.5175 0.9056 -0.3499 -0.0037 0.0687  533 LEU A C   
1824 O O   . LEU A 237 ? 0.9834 1.5983 0.9508 -0.3534 0.0034  0.0730  533 LEU A O   
1825 C CB  . LEU A 237 ? 0.8104 1.5693 0.8175 -0.4064 -0.0019 0.0817  533 LEU A CB  
1826 C CG  . LEU A 237 ? 0.7231 1.5573 0.7632 -0.4021 -0.0050 0.0808  533 LEU A CG  
1827 C CD1 . LEU A 237 ? 0.7404 1.6530 0.7594 -0.4293 -0.0045 0.0894  533 LEU A CD1 
1828 C CD2 . LEU A 237 ? 0.6818 1.4279 0.7036 -0.4203 -0.0162 0.0780  533 LEU A CD2 
1829 N N   . PHE A 238 ? 0.9422 1.4211 0.8925 -0.3496 -0.0129 0.0647  534 PHE A N   
1830 C CA  . PHE A 238 ? 1.0036 1.3812 0.9022 -0.3557 -0.0158 0.0664  534 PHE A CA  
1831 C C   . PHE A 238 ? 1.0100 1.2887 0.8564 -0.3855 -0.0252 0.0697  534 PHE A C   
1832 O O   . PHE A 238 ? 1.0024 1.2647 0.8650 -0.3748 -0.0311 0.0640  534 PHE A O   
1833 C CB  . PHE A 238 ? 0.8980 1.2325 0.8145 -0.2992 -0.0170 0.0542  534 PHE A CB  
1834 C CG  . PHE A 238 ? 0.8822 1.2955 0.8447 -0.2620 -0.0090 0.0477  534 PHE A CG  
1835 C CD1 . PHE A 238 ? 0.8684 1.3359 0.8790 -0.2306 -0.0078 0.0397  534 PHE A CD1 
1836 C CD2 . PHE A 238 ? 0.8800 1.3049 0.8307 -0.2556 -0.0029 0.0493  534 PHE A CD2 
1837 C CE1 . PHE A 238 ? 0.8737 1.4003 0.9139 -0.1926 -0.0005 0.0333  534 PHE A CE1 
1838 C CE2 . PHE A 238 ? 0.8045 1.2938 0.7894 -0.2187 0.0045  0.0424  534 PHE A CE2 
1839 C CZ  . PHE A 238 ? 0.7473 1.2843 0.7741 -0.1863 0.0057  0.0342  534 PHE A CZ  
1840 N N   . GLN A 239 ? 1.0873 1.2930 0.8648 -0.4196 -0.0265 0.0788  535 GLN A N   
1841 C CA  . GLN A 239 ? 1.1954 1.2918 0.9024 -0.4499 -0.0349 0.0832  535 GLN A CA  
1842 C C   . GLN A 239 ? 1.2320 1.2195 0.9045 -0.4089 -0.0403 0.0776  535 GLN A C   
1843 O O   . GLN A 239 ? 1.3008 1.2509 0.9375 -0.4050 -0.0381 0.0817  535 GLN A O   
1844 C CB  . GLN A 239 ? 1.3521 1.4337 0.9914 -0.5195 -0.0330 0.0984  535 GLN A CB  
1845 C CG  . GLN A 239 ? 1.5483 1.5179 1.1052 -0.5597 -0.0416 0.1034  535 GLN A CG  
1846 C CD  . GLN A 239 ? 1.6956 1.5416 1.1552 -0.5757 -0.0434 0.1114  535 GLN A CD  
1847 O OE1 . GLN A 239 ? 1.7830 1.5108 1.1903 -0.5493 -0.0504 0.1077  535 GLN A OE1 
1848 N NE2 . GLN A 239 ? 1.7426 1.6162 1.1736 -0.6168 -0.0366 0.1228  535 GLN A NE2 
1849 N N   . ILE A 240 ? 1.2041 1.1483 0.8879 -0.3771 -0.0470 0.0685  536 ILE A N   
1850 C CA  . ILE A 240 ? 1.2143 1.0610 0.8619 -0.3384 -0.0532 0.0635  536 ILE A CA  
1851 C C   . ILE A 240 ? 1.3494 1.0903 0.8957 -0.3682 -0.0559 0.0744  536 ILE A C   
1852 O O   . ILE A 240 ? 1.3412 1.0387 0.8324 -0.4160 -0.0583 0.0819  536 ILE A O   
1853 C CB  . ILE A 240 ? 1.1806 0.9952 0.8400 -0.3149 -0.0598 0.0552  536 ILE A CB  
1854 C CG1 . ILE A 240 ? 1.0919 1.0044 0.8401 -0.2965 -0.0572 0.0465  536 ILE A CG1 
1855 C CG2 . ILE A 240 ? 1.1122 0.8509 0.7450 -0.2667 -0.0652 0.0494  536 ILE A CG2 
1856 C CD1 . ILE A 240 ? 1.1003 1.0120 0.8525 -0.3138 -0.0613 0.0454  536 ILE A CD1 
1857 N N   . PRO A 241 ? 1.2675 0.9597 0.7801 -0.3427 -0.0560 0.0757  537 PRO A N   
1858 C CA  . PRO A 241 ? 1.3597 0.9378 0.7646 -0.3659 -0.0587 0.0866  537 PRO A CA  
1859 C C   . PRO A 241 ? 1.4009 0.8725 0.7386 -0.3659 -0.0668 0.0862  537 PRO A C   
1860 O O   . PRO A 241 ? 1.3614 0.8127 0.7175 -0.3156 -0.0717 0.0765  537 PRO A O   
1861 C CB  . PRO A 241 ? 1.3048 0.8588 0.7018 -0.3173 -0.0591 0.0843  537 PRO A CB  
1862 C CG  . PRO A 241 ? 1.1288 0.8042 0.6291 -0.2923 -0.0538 0.0752  537 PRO A CG  
1863 C CD  . PRO A 241 ? 1.1887 0.9216 0.7541 -0.2897 -0.0546 0.0668  537 PRO A CD  
1864 N N   . PRO A 242 ? 1.4931 0.8970 0.7496 -0.4235 -0.0683 0.0962  538 PRO A N   
1865 C CA  . PRO A 242 ? 1.5964 0.9006 0.7873 -0.4277 -0.0760 0.0947  538 PRO A CA  
1866 C C   . PRO A 242 ? 1.6887 0.8818 0.8177 -0.3678 -0.0820 0.0910  538 PRO A C   
1867 O O   . PRO A 242 ? 1.8166 0.9453 0.9118 -0.3506 -0.0878 0.0861  538 PRO A O   
1868 C CB  . PRO A 242 ? 1.6650 0.9029 0.7601 -0.5063 -0.0763 0.1081  538 PRO A CB  
1869 C CG  . PRO A 242 ? 1.6354 0.9986 0.7926 -0.5478 -0.0677 0.1141  538 PRO A CG  
1870 C CD  . PRO A 242 ? 1.5519 0.9705 0.7704 -0.4917 -0.0631 0.1094  538 PRO A CD  
1871 N N   . GLU A 243 ? 1.5149 0.6889 0.6277 -0.3322 -0.0808 0.0930  539 GLU A N   
1872 C CA  . GLU A 243 ? 1.6156 0.7032 0.6768 -0.2671 -0.0866 0.0892  539 GLU A CA  
1873 C C   . GLU A 243 ? 1.5519 0.7188 0.7083 -0.2087 -0.0883 0.0751  539 GLU A C   
1874 O O   . GLU A 243 ? 1.5285 0.6387 0.6503 -0.1556 -0.0935 0.0706  539 GLU A O   
1875 C CB  . GLU A 243 ? 1.7754 0.8260 0.7906 -0.2458 -0.0855 0.0960  539 GLU A CB  
1876 C CG  . GLU A 243 ? 1.7089 0.8863 0.8261 -0.2309 -0.0800 0.0920  539 GLU A CG  
1877 C CD  . GLU A 243 ? 1.7566 0.9852 0.8852 -0.2927 -0.0722 0.1011  539 GLU A CD  
1878 O OE1 . GLU A 243 ? 1.7330 0.9698 0.8529 -0.3516 -0.0700 0.1059  539 GLU A OE1 
1879 O OE2 . GLU A 243 ? 1.6893 0.9555 0.8349 -0.2824 -0.0683 0.1036  539 GLU A OE2 
1880 N N   . LEU A 244 ? 1.4193 0.7153 0.6892 -0.2174 -0.0837 0.0686  540 LEU A N   
1881 C CA  . LEU A 244 ? 1.3549 0.7266 0.7133 -0.1729 -0.0848 0.0558  540 LEU A CA  
1882 C C   . LEU A 244 ? 1.2612 0.6327 0.6345 -0.1839 -0.0870 0.0511  540 LEU A C   
1883 O O   . LEU A 244 ? 1.2706 0.6778 0.6941 -0.1440 -0.0888 0.0415  540 LEU A O   
1884 C CB  . LEU A 244 ? 1.2582 0.7563 0.7208 -0.1747 -0.0789 0.0508  540 LEU A CB  
1885 C CG  . LEU A 244 ? 1.2411 0.7508 0.7007 -0.1551 -0.0771 0.0528  540 LEU A CG  
1886 C CD1 . LEU A 244 ? 1.0694 0.6967 0.6296 -0.1470 -0.0722 0.0447  540 LEU A CD1 
1887 C CD2 . LEU A 244 ? 1.1836 0.6300 0.5959 -0.1001 -0.0836 0.0507  540 LEU A CD2 
1888 N N   . VAL A 245 ? 1.3468 0.6837 0.6778 -0.2394 -0.0870 0.0577  541 VAL A N   
1889 C CA  . VAL A 245 ? 1.4049 0.7472 0.7502 -0.2563 -0.0895 0.0536  541 VAL A CA  
1890 C C   . VAL A 245 ? 1.5512 0.7596 0.7916 -0.2409 -0.0959 0.0544  541 VAL A C   
1891 O O   . VAL A 245 ? 1.4154 0.5255 0.5564 -0.2813 -0.0983 0.0628  541 VAL A O   
1892 C CB  . VAL A 245 ? 1.4484 0.8345 0.8035 -0.3256 -0.0869 0.0599  541 VAL A CB  
1893 C CG1 . VAL A 245 ? 1.3860 0.8080 0.7806 -0.3357 -0.0893 0.0539  541 VAL A CG1 
1894 C CG2 . VAL A 245 ? 1.3769 0.8785 0.8089 -0.3385 -0.0794 0.0618  541 VAL A CG2 
1895 N N   . LEU A 246 ? 1.3944 0.5962 0.6504 -0.1823 -0.0986 0.0458  542 LEU A N   
1896 C CA  . LEU A 246 ? 1.4994 0.5766 0.6536 -0.1545 -0.1042 0.0457  542 LEU A CA  
1897 C C   . LEU A 246 ? 1.5181 0.5660 0.6536 -0.1833 -0.1071 0.0430  542 LEU A C   
1898 O O   . LEU A 246 ? 1.5587 0.6895 0.7780 -0.1744 -0.1061 0.0353  542 LEU A O   
1899 C CB  . LEU A 246 ? 1.5091 0.6021 0.6854 -0.0773 -0.1055 0.0382  542 LEU A CB  
1900 C CG  . LEU A 246 ? 1.6607 0.6455 0.7454 -0.0377 -0.1104 0.0360  542 LEU A CG  
1901 C CD1 . LEU A 246 ? 1.7389 0.5700 0.6779 -0.0438 -0.1138 0.0454  542 LEU A CD1 
1902 C CD2 . LEU A 246 ? 1.5872 0.6207 0.7117 0.0381  -0.1110 0.0281  542 LEU A CD2 
1903 N N   . GLU A 247 ? 1.6176 0.5400 0.6355 -0.2161 -0.1111 0.0492  543 GLU A N   
1904 C CA  . GLU A 247 ? 1.6880 0.5819 0.6768 -0.2528 -0.1143 0.0466  543 GLU A CA  
1905 C C   . GLU A 247 ? 1.8901 0.6800 0.7799 -0.2119 -0.1179 0.0405  543 GLU A C   
1906 O O   . GLU A 247 ? 2.0966 0.8076 0.9045 -0.1819 -0.1186 0.0406  543 GLU A O   
1907 C CB  . GLU A 247 ? 1.7330 0.6506 0.7038 -0.3288 -0.1132 0.0526  543 GLU A CB  
1908 C CG  . GLU A 247 ? 1.6525 0.6960 0.7292 -0.3691 -0.1086 0.0571  543 GLU A CG  
1909 C CD  . GLU A 247 ? 1.8189 0.9008 0.8781 -0.4375 -0.1072 0.0633  543 GLU A CD  
1910 O OE1 . GLU A 247 ? 2.0514 1.0972 1.0564 -0.4553 -0.1059 0.0692  543 GLU A OE1 
1911 O OE2 . GLU A 247 ? 1.7111 0.8609 0.8083 -0.4713 -0.1078 0.0623  543 GLU A OE2 
1912 N N   . VAL A 248 ? 1.8526 0.6453 0.7489 -0.2094 -0.1200 0.0344  544 VAL A N   
1913 C CA  . VAL A 248 ? 1.9930 0.6964 0.8001 -0.1694 -0.1228 0.0282  544 VAL A CA  
1914 C C   . VAL A 248 ? 2.0314 0.6958 0.7757 -0.2232 -0.1259 0.0289  544 VAL A C   
1915 O O   . VAL A 248 ? 1.8852 0.6119 0.6884 -0.2545 -0.1264 0.0286  544 VAL A O   
1916 C CB  . VAL A 248 ? 1.8903 0.6263 0.7509 -0.1098 -0.1225 0.0206  544 VAL A CB  
1917 C CG1 . VAL A 248 ? 1.9119 0.5625 0.6772 -0.0696 -0.1244 0.0148  544 VAL A CG1 
1918 C CG2 . VAL A 248 ? 1.8352 0.6160 0.7554 -0.0543 -0.1204 0.0203  544 VAL A CG2 
1919 N N   . PRO A 249 ? 2.1387 0.7015 0.7613 -0.2355 -0.1287 0.0294  545 PRO A N   
1920 C CA  . PRO A 249 ? 2.2124 0.7322 0.7657 -0.2857 -0.1327 0.0305  545 PRO A CA  
1921 C C   . PRO A 249 ? 2.3137 0.7890 0.8317 -0.2459 -0.1348 0.0245  545 PRO A C   
1922 O O   . PRO A 249 ? 2.4131 0.8215 0.8729 -0.1826 -0.1346 0.0189  545 PRO A O   
1923 C CB  . PRO A 249 ? 2.2473 0.6629 0.6735 -0.3066 -0.1353 0.0316  545 PRO A CB  
1924 C CG  . PRO A 249 ? 2.2893 0.6598 0.6906 -0.2379 -0.1331 0.0271  545 PRO A CG  
1925 C CD  . PRO A 249 ? 2.1755 0.6578 0.7144 -0.2088 -0.1285 0.0288  545 PRO A CD  
1926 N N   . ILE A 250 ? 2.3184 0.8374 0.8726 -0.2813 -0.1364 0.0256  546 ILE A N   
1927 C CA  . ILE A 250 ? 2.1628 0.6563 0.7014 -0.2469 -0.1378 0.0204  546 ILE A CA  
1928 C C   . ILE A 250 ? 2.3672 0.7337 0.7566 -0.2532 -0.1424 0.0206  546 ILE A C   
1929 O O   . ILE A 250 ? 2.4623 0.8027 0.7971 -0.3169 -0.1460 0.0259  546 ILE A O   
1930 C CB  . ILE A 250 ? 2.1046 0.6937 0.7387 -0.2820 -0.1379 0.0211  546 ILE A CB  
1931 C CG1 . ILE A 250 ? 1.8775 0.5894 0.6476 -0.2892 -0.1339 0.0214  546 ILE A CG1 
1932 C CG2 . ILE A 250 ? 2.0656 0.6377 0.6983 -0.2380 -0.1386 0.0146  546 ILE A CG2 
1933 C CD1 . ILE A 250 ? 1.8897 0.6193 0.7107 -0.2213 -0.1307 0.0155  546 ILE A CD1 
1934 N N   . ARG A 251 ? 2.4339 0.7247 0.7544 -0.1865 -0.1423 0.0148  547 ARG A N   
1935 C CA  . ARG A 251 ? 2.6291 0.7978 0.8070 -0.1832 -0.1465 0.0142  547 ARG A CA  
1936 C C   . ARG A 251 ? 2.6008 0.7678 0.7861 -0.1288 -0.1458 0.0095  547 ARG A C   
1937 O O   . ARG A 251 ? 2.4913 0.7309 0.7678 -0.0763 -0.1416 0.0047  547 ARG A O   
1938 C CB  . ARG A 251 ? 2.7582 0.8165 0.8148 -0.1525 -0.1468 0.0114  547 ARG A CB  
1939 C CG  . ARG A 251 ? 2.7154 0.7804 0.7880 -0.0652 -0.1424 0.0048  547 ARG A CG  
1940 C CD  . ARG A 251 ? 2.6879 0.7861 0.7991 -0.0669 -0.1399 0.0053  547 ARG A CD  
1941 N NE  . ARG A 251 ? 2.6483 0.7603 0.7756 0.0158  -0.1356 -0.0006 547 ARG A NE  
1942 C CZ  . ARG A 251 ? 2.5480 0.7494 0.7805 0.0340  -0.1318 0.0002  547 ARG A CZ  
1943 N NH1 . ARG A 251 ? 2.6109 0.8287 0.8520 0.1097  -0.1282 -0.0048 547 ARG A NH1 
1944 N NH2 . ARG A 251 ? 2.4532 0.7323 0.7806 -0.0232 -0.1316 0.0064  547 ARG A NH2 
1945 N N   . HIS A 252 ? 2.7187 0.8042 0.8060 -0.1438 -0.1499 0.0111  548 HIS A N   
1946 C CA  . HIS A 252 ? 2.7456 0.8201 0.8273 -0.0887 -0.1490 0.0069  548 HIS A CA  
1947 C C   . HIS A 252 ? 2.8844 0.8654 0.8709 -0.0235 -0.1466 0.0021  548 HIS A C   
1948 O O   . HIS A 252 ? 2.9856 0.8809 0.8820 -0.0391 -0.1475 0.0032  548 HIS A O   
1949 C CB  . HIS A 252 ? 2.6481 0.7058 0.7078 -0.1349 -0.1530 0.0107  548 HIS A CB  
1950 C CG  . HIS A 252 ? 2.7773 0.8656 0.8768 -0.0887 -0.1517 0.0065  548 HIS A CG  
1951 N ND1 . HIS A 252 ? 2.8793 0.8930 0.9012 -0.0324 -0.1507 0.0029  548 HIS A ND1 
1952 C CD2 . HIS A 252 ? 2.6312 0.8299 0.8616 -0.0881 -0.1491 0.0031  548 HIS A CD2 
1953 C CE1 . HIS A 252 ? 2.7506 0.8157 0.8267 -0.0003 -0.1497 0.0001  548 HIS A CE1 
1954 N NE2 . HIS A 252 ? 2.6237 0.8027 0.8337 -0.0340 -0.1481 -0.0011 548 HIS A NE2 
1955 N N   . PRO A 253 ? 2.8701 0.8699 0.8738 0.0518  -0.1431 -0.0033 549 PRO A N   
1956 C CA  . PRO A 253 ? 3.0100 0.9295 0.9225 0.1178  -0.1404 -0.0073 549 PRO A CA  
1957 C C   . PRO A 253 ? 3.2508 1.0669 1.0567 0.1104  -0.1432 -0.0060 549 PRO A C   
1958 O O   . PRO A 253 ? 3.3754 1.1346 1.1124 0.1727  -0.1410 -0.0093 549 PRO A O   
1959 C CB  . PRO A 253 ? 2.8784 0.8818 0.8635 0.1974  -0.1352 -0.0127 549 PRO A CB  
1960 C CG  . PRO A 253 ? 2.7087 0.8075 0.7989 0.1708  -0.1365 -0.0119 549 PRO A CG  
1961 C CD  . PRO A 253 ? 2.5998 0.7080 0.7141 0.0831  -0.1410 -0.0061 549 PRO A CD  
1962 N N   . LYS A 254 ? 3.3522 1.1463 1.1423 0.0348  -0.1483 -0.0010 550 LYS A N   
1963 C CA  . LYS A 254 ? 3.4576 1.1470 1.1397 0.0154  -0.1520 0.0011  550 LYS A CA  
1964 C C   . LYS A 254 ? 3.4909 1.1374 1.1273 -0.0766 -0.1572 0.0073  550 LYS A C   
1965 O O   . LYS A 254 ? 3.7940 1.3342 1.3183 -0.0924 -0.1591 0.0083  550 LYS A O   
1966 C CB  . LYS A 254 ? 3.4503 1.1730 1.1677 0.0244  -0.1528 0.0008  550 LYS A CB  
1967 C CG  . LYS A 254 ? 3.3779 1.1733 1.1648 0.1039  -0.1478 -0.0047 550 LYS A CG  
1968 C CD  . LYS A 254 ? 3.4900 1.2146 1.1911 0.1816  -0.1447 -0.0086 550 LYS A CD  
1969 C CE  . LYS A 254 ? 3.4016 1.2106 1.1739 0.2539  -0.1397 -0.0132 550 LYS A CE  
1970 N NZ  . LYS A 254 ? 3.4914 1.2745 1.2115 0.3384  -0.1349 -0.0169 550 LYS A NZ  
1971 N N   . PHE A 255 ? 3.2368 0.9699 0.9589 -0.1374 -0.1593 0.0115  551 PHE A N   
1972 C CA  . PHE A 255 ? 3.2480 0.9625 0.9372 -0.2280 -0.1642 0.0182  551 PHE A CA  
1973 C C   . PHE A 255 ? 3.2996 1.0195 0.9852 -0.2676 -0.1640 0.0206  551 PHE A C   
1974 O O   . PHE A 255 ? 2.9852 0.8063 0.7720 -0.2790 -0.1620 0.0215  551 PHE A O   
1975 C CB  . PHE A 255 ? 3.1231 0.9419 0.9109 -0.2722 -0.1658 0.0221  551 PHE A CB  
1976 C CG  . PHE A 255 ? 3.1030 0.9255 0.9043 -0.2337 -0.1659 0.0194  551 PHE A CG  
1977 C CD1 . PHE A 255 ? 3.0177 0.9089 0.9019 -0.1686 -0.1619 0.0141  551 PHE A CD1 
1978 C CD2 . PHE A 255 ? 3.2180 0.9766 0.9478 -0.2643 -0.1700 0.0222  551 PHE A CD2 
1979 C CE1 . PHE A 255 ? 3.0303 0.9278 0.9265 -0.1339 -0.1618 0.0115  551 PHE A CE1 
1980 C CE2 . PHE A 255 ? 3.2193 0.9805 0.9604 -0.2290 -0.1700 0.0197  551 PHE A CE2 
1981 C CZ  . PHE A 255 ? 3.1366 0.9680 0.9614 -0.1634 -0.1658 0.0143  551 PHE A CZ  
1982 N N   . ASP A 256 ? 3.4303 1.0392 0.9959 -0.2908 -0.1664 0.0218  552 ASP A N   
1983 C CA  . ASP A 256 ? 3.5559 1.1599 1.1063 -0.3292 -0.1664 0.0238  552 ASP A CA  
1984 C C   . ASP A 256 ? 3.4373 1.1136 1.0326 -0.4222 -0.1693 0.0311  552 ASP A C   
1985 O O   . ASP A 256 ? 3.4293 1.1350 1.0418 -0.4555 -0.1687 0.0331  552 ASP A O   
1986 C CB  . ASP A 256 ? 3.8896 1.3453 1.2891 -0.3231 -0.1681 0.0223  552 ASP A CB  
1987 C CG  . ASP A 256 ? 4.0026 1.4107 1.3719 -0.2323 -0.1637 0.0154  552 ASP A CG  
1988 O OD1 . ASP A 256 ? 4.0327 1.4079 1.3772 -0.1690 -0.1622 0.0117  552 ASP A OD1 
1989 O OD2 . ASP A 256 ? 4.0170 1.4253 1.3878 -0.2234 -0.1614 0.0138  552 ASP A OD2 
1990 N N   . TRP A 257 ? 3.3158 1.0253 0.9297 -0.4645 -0.1723 0.0353  553 TRP A N   
1991 C CA  . TRP A 257 ? 3.2556 1.0685 0.9392 -0.5432 -0.1739 0.0424  553 TRP A CA  
1992 C C   . TRP A 257 ? 3.1117 1.0645 0.9406 -0.5275 -0.1701 0.0422  553 TRP A C   
1993 O O   . TRP A 257 ? 3.0025 1.0538 0.8983 -0.5851 -0.1702 0.0479  553 TRP A O   
1994 C CB  . TRP A 257 ? 3.2865 1.1062 0.9554 -0.5899 -0.1778 0.0471  553 TRP A CB  
1995 C CG  . TRP A 257 ? 3.2511 1.0832 0.9588 -0.5361 -0.1769 0.0435  553 TRP A CG  
1996 C CD1 . TRP A 257 ? 3.3735 1.1009 0.9978 -0.4895 -0.1779 0.0394  553 TRP A CD1 
1997 C CD2 . TRP A 257 ? 3.0856 1.0411 0.9222 -0.5217 -0.1748 0.0434  553 TRP A CD2 
1998 N NE1 . TRP A 257 ? 3.2555 1.0365 0.9508 -0.4481 -0.1765 0.0368  553 TRP A NE1 
1999 C CE2 . TRP A 257 ? 3.0606 0.9782 0.8846 -0.4677 -0.1748 0.0390  553 TRP A CE2 
2000 C CE3 . TRP A 257 ? 2.8849 0.9776 0.8423 -0.5486 -0.1729 0.0468  553 TRP A CE3 
2001 C CZ2 . TRP A 257 ? 2.9041 0.9126 0.8300 -0.4422 -0.1732 0.0375  553 TRP A CZ2 
2002 C CZ3 . TRP A 257 ? 2.7512 0.9331 0.8124 -0.5220 -0.1712 0.0449  553 TRP A CZ3 
2003 C CH2 . TRP A 257 ? 2.7877 0.9261 0.8325 -0.4705 -0.1715 0.0400  553 TRP A CH2 
2004 N N   . PHE A 258 ? 3.2061 1.1718 1.0821 -0.4505 -0.1666 0.0360  554 PHE A N   
2005 C CA  . PHE A 258 ? 3.1282 1.2136 1.1315 -0.4318 -0.1633 0.0354  554 PHE A CA  
2006 C C   . PHE A 258 ? 3.0968 1.2041 1.1156 -0.4450 -0.1613 0.0362  554 PHE A C   
2007 O O   . PHE A 258 ? 3.0624 1.2845 1.1927 -0.4625 -0.1588 0.0383  554 PHE A O   
2008 C CB  . PHE A 258 ? 3.1184 1.2047 1.1561 -0.3460 -0.1603 0.0282  554 PHE A CB  
2009 C CG  . PHE A 258 ? 2.9972 1.2183 1.1906 -0.3353 -0.1568 0.0259  554 PHE A CG  
2010 C CD1 . PHE A 258 ? 2.9541 1.2046 1.1853 -0.3285 -0.1574 0.0241  554 PHE A CD1 
2011 C CD2 . PHE A 258 ? 2.8935 1.2123 1.1982 -0.3332 -0.1525 0.0249  554 PHE A CD2 
2012 C CE1 . PHE A 258 ? 2.8068 1.1800 1.1815 -0.3193 -0.1541 0.0201  554 PHE A CE1 
2013 C CE2 . PHE A 258 ? 2.7222 1.1620 1.1687 -0.3240 -0.1491 0.0218  554 PHE A CE2 
2014 C CZ  . PHE A 258 ? 2.7140 1.1804 1.1944 -0.3171 -0.1500 0.0188  554 PHE A CZ  
2015 N N   . LYS A 259 ? 3.1399 1.1439 1.0603 -0.4333 -0.1614 0.0338  555 LYS A N   
2016 C CA  . LYS A 259 ? 3.1776 1.1941 1.0986 -0.4604 -0.1603 0.0355  555 LYS A CA  
2017 C C   . LYS A 259 ? 3.0847 1.1719 1.0324 -0.5499 -0.1625 0.0435  555 LYS A C   
2018 O O   . LYS A 259 ? 2.8574 1.0425 0.8866 -0.5741 -0.1607 0.0466  555 LYS A O   
2019 C CB  . LYS A 259 ? 3.3836 1.2645 1.1768 -0.4420 -0.1608 0.0321  555 LYS A CB  
2020 C CG  . LYS A 259 ? 3.4670 1.2648 1.2068 -0.3563 -0.1589 0.0249  555 LYS A CG  
2021 C CD  . LYS A 259 ? 3.6481 1.3146 1.2591 -0.3391 -0.1593 0.0220  555 LYS A CD  
2022 C CE  . LYS A 259 ? 3.6682 1.2877 1.2543 -0.2422 -0.1556 0.0148  555 LYS A CE  
2023 N NZ  . LYS A 259 ? 3.4785 1.2094 1.1884 -0.1950 -0.1523 0.0125  555 LYS A NZ  
2024 N N   . ASP A 260 ? 3.2121 1.2555 1.0914 -0.5990 -0.1665 0.0472  556 ASP A N   
2025 C CA  . ASP A 260 ? 3.1895 1.2994 1.0823 -0.6849 -0.1687 0.0550  556 ASP A CA  
2026 C C   . ASP A 260 ? 2.9528 1.2126 0.9730 -0.7049 -0.1673 0.0595  556 ASP A C   
2027 O O   . ASP A 260 ? 2.7698 1.1207 0.8304 -0.7667 -0.1675 0.0660  556 ASP A O   
2028 C CB  . ASP A 260 ? 3.3852 1.4018 1.1626 -0.7301 -0.1737 0.0577  556 ASP A CB  
2029 C CG  . ASP A 260 ? 3.5354 1.4233 1.1841 -0.7416 -0.1757 0.0559  556 ASP A CG  
2030 O OD1 . ASP A 260 ? 3.5252 1.4396 1.1834 -0.7668 -0.1747 0.0572  556 ASP A OD1 
2031 O OD2 . ASP A 260 ? 3.6753 1.4341 1.2113 -0.7245 -0.1783 0.0532  556 ASP A OD2 
2032 N N   . LEU A 261 ? 2.9665 1.2554 1.0477 -0.6533 -0.1658 0.0562  557 LEU A N   
2033 C CA  . LEU A 261 ? 2.8548 1.2971 1.0891 -0.6571 -0.1620 0.0574  557 LEU A CA  
2034 C C   . LEU A 261 ? 2.8737 1.4155 1.1995 -0.6677 -0.1575 0.0588  557 LEU A C   
2035 O O   . LEU A 261 ? 2.8126 1.4831 1.2342 -0.7045 -0.1552 0.0632  557 LEU A O   
2036 C CB  . LEU A 261 ? 2.7307 1.1858 1.0340 -0.5860 -0.1594 0.0498  557 LEU A CB  
2037 C CG  . LEU A 261 ? 2.7716 1.1887 1.0404 -0.5811 -0.1625 0.0489  557 LEU A CG  
2038 C CD1 . LEU A 261 ? 2.6146 1.0698 0.9721 -0.5131 -0.1594 0.0405  557 LEU A CD1 
2039 C CD2 . LEU A 261 ? 2.7766 1.2738 1.0766 -0.6505 -0.1645 0.0559  557 LEU A CD2 
2040 N N   . GLY A 262 ? 2.9592 1.4431 1.2522 -0.6347 -0.1561 0.0554  558 GLY A N   
2041 C CA  . GLY A 262 ? 2.9397 1.4975 1.2956 -0.6494 -0.1523 0.0577  558 GLY A CA  
2042 C C   . GLY A 262 ? 2.7058 1.3951 1.2204 -0.6186 -0.1461 0.0561  558 GLY A C   
2043 O O   . GLY A 262 ? 2.6795 1.4864 1.2785 -0.6538 -0.1431 0.0608  558 GLY A O   
2044 N N   . LEU A 263 ? 2.5290 1.2013 1.0814 -0.5523 -0.1443 0.0492  559 LEU A N   
2045 C CA  . LEU A 263 ? 2.2678 1.0533 0.9613 -0.5219 -0.1392 0.0464  559 LEU A CA  
2046 C C   . LEU A 263 ? 2.1771 0.9369 0.8876 -0.4658 -0.1359 0.0423  559 LEU A C   
2047 O O   . LEU A 263 ? 2.1624 0.8117 0.7797 -0.4307 -0.1375 0.0393  559 LEU A O   
2048 C CB  . LEU A 263 ? 2.1903 0.9997 0.9305 -0.4951 -0.1400 0.0410  559 LEU A CB  
2049 C CG  . LEU A 263 ? 2.2058 1.0408 0.9297 -0.5469 -0.1434 0.0452  559 LEU A CG  
2050 C CD1 . LEU A 263 ? 2.1091 0.9702 0.8849 -0.5171 -0.1439 0.0391  559 LEU A CD1 
2051 C CD2 . LEU A 263 ? 2.1707 1.1268 0.9611 -0.6045 -0.1415 0.0522  559 LEU A CD2 
2052 N N   . LYS A 264 ? 2.0216 0.8871 0.8496 -0.4569 -0.1313 0.0423  560 LYS A N   
2053 C CA  . LYS A 264 ? 1.9216 0.7828 0.7837 -0.4056 -0.1280 0.0393  560 LYS A CA  
2054 C C   . LYS A 264 ? 1.8071 0.7893 0.8048 -0.3955 -0.1245 0.0368  560 LYS A C   
2055 O O   . LYS A 264 ? 1.7188 0.7980 0.7827 -0.4359 -0.1235 0.0393  560 LYS A O   
2056 C CB  . LYS A 264 ? 1.8950 0.7334 0.7193 -0.4235 -0.1264 0.0448  560 LYS A CB  
2057 C CG  . LYS A 264 ? 1.9075 0.8475 0.7865 -0.4864 -0.1239 0.0521  560 LYS A CG  
2058 C CD  . LYS A 264 ? 2.0005 0.9283 0.8558 -0.4988 -0.1215 0.0571  560 LYS A CD  
2059 C CE  . LYS A 264 ? 2.0355 1.0284 0.8904 -0.5697 -0.1209 0.0644  560 LYS A CE  
2060 N NZ  . LYS A 264 ? 1.9107 0.8993 0.7446 -0.5866 -0.1183 0.0691  560 LYS A NZ  
2061 N N   . TRP A 265 ? 1.6955 0.6736 0.7302 -0.3395 -0.1229 0.0315  561 TRP A N   
2062 C CA  . TRP A 265 ? 1.5656 0.6477 0.7186 -0.3296 -0.1203 0.0279  561 TRP A CA  
2063 C C   . TRP A 265 ? 1.6095 0.6868 0.7781 -0.2997 -0.1178 0.0292  561 TRP A C   
2064 O O   . TRP A 265 ? 1.7361 0.7253 0.8257 -0.2732 -0.1181 0.0318  561 TRP A O   
2065 C CB  . TRP A 265 ? 1.3582 0.4544 0.5533 -0.2911 -0.1222 0.0179  561 TRP A CB  
2066 C CG  . TRP A 265 ? 1.3359 0.5705 0.6557 -0.2975 -0.1192 0.0148  561 TRP A CG  
2067 C CD1 . TRP A 265 ? 1.3393 0.6599 0.7515 -0.2482 -0.1140 0.0095  561 TRP A CD1 
2068 C CD2 . TRP A 265 ? 1.4029 0.7157 0.7672 -0.3520 -0.1203 0.0176  561 TRP A CD2 
2069 N NE1 . TRP A 265 ? 1.3405 0.7747 0.8452 -0.2659 -0.1116 0.0087  561 TRP A NE1 
2070 C CE2 . TRP A 265 ? 1.3264 0.7632 0.8064 -0.3259 -0.1153 0.0137  561 TRP A CE2 
2071 C CE3 . TRP A 265 ? 1.4497 0.7705 0.7780 -0.4034 -0.1211 0.0249  561 TRP A CE3 
2072 C CZ2 . TRP A 265 ? 1.1489 0.6872 0.6940 -0.3585 -0.1150 0.0153  561 TRP A CZ2 
2073 C CZ3 . TRP A 265 ? 1.3667 0.8030 0.7683 -0.4344 -0.1200 0.0270  561 TRP A CZ3 
2074 C CH2 . TRP A 265 ? 1.1109 0.6448 0.6144 -0.4164 -0.1188 0.0214  561 TRP A CH2 
2075 N N   . TYR A 266 ? 1.4141 0.6243 0.6995 -0.2902 -0.1124 0.0274  562 TYR A N   
2076 C CA  . TYR A 266 ? 1.3011 0.5504 0.6270 -0.2508 -0.1077 0.0275  562 TYR A CA  
2077 C C   . TYR A 266 ? 1.3089 0.5723 0.6695 -0.1809 -0.1070 0.0187  562 TYR A C   
2078 O O   . TYR A 266 ? 1.3028 0.6066 0.7099 -0.1660 -0.1072 0.0121  562 TYR A O   
2079 C CB  . TYR A 266 ? 1.1976 0.5743 0.6216 -0.2728 -0.1022 0.0292  562 TYR A CB  
2080 C CG  . TYR A 266 ? 1.2142 0.6912 0.7267 -0.2796 -0.1009 0.0241  562 TYR A CG  
2081 C CD1 . TYR A 266 ? 1.1424 0.6900 0.7369 -0.2339 -0.0979 0.0162  562 TYR A CD1 
2082 C CD2 . TYR A 266 ? 1.1489 0.6516 0.6591 -0.3335 -0.1030 0.0279  562 TYR A CD2 
2083 C CE1 . TYR A 266 ? 1.1055 0.7340 0.7709 -0.2384 -0.0966 0.0125  562 TYR A CE1 
2084 C CE2 . TYR A 266 ? 1.1283 0.7234 0.7159 -0.3351 -0.1021 0.0240  562 TYR A CE2 
2085 C CZ  . TYR A 266 ? 1.1332 0.7846 0.7949 -0.2859 -0.0988 0.0164  562 TYR A CZ  
2086 O OH  . TYR A 266 ? 1.2010 0.9335 0.9303 -0.2853 -0.0979 0.0131  562 TYR A OH  
2087 N N   . GLY A 267 ? 1.2717 0.5036 0.6059 -0.1389 -0.1064 0.0193  563 GLY A N   
2088 C CA  . GLY A 267 ? 1.2836 0.5307 0.6400 -0.0738 -0.1062 0.0120  563 GLY A CA  
2089 C C   . GLY A 267 ? 1.2249 0.6013 0.7019 -0.0589 -0.1021 0.0055  563 GLY A C   
2090 O O   . GLY A 267 ? 1.2666 0.6730 0.7748 -0.0197 -0.1017 -0.0011 563 GLY A O   
2091 N N   . LEU A 268 ? 1.2221 0.6744 0.7629 -0.0904 -0.0986 0.0075  564 LEU A N   
2092 C CA  . LEU A 268 ? 1.0884 0.6456 0.7261 -0.0711 -0.0946 0.0017  564 LEU A CA  
2093 C C   . LEU A 268 ? 1.0257 0.6517 0.7300 -0.0965 -0.0925 -0.0010 564 LEU A C   
2094 O O   . LEU A 268 ? 1.0143 0.6706 0.7345 -0.1361 -0.0907 0.0034  564 LEU A O   
2095 C CB  . LEU A 268 ? 1.0912 0.6819 0.7482 -0.0768 -0.0919 0.0049  564 LEU A CB  
2096 C CG  . LEU A 268 ? 1.0281 0.7003 0.7589 -0.0464 -0.0894 -0.0020 564 LEU A CG  
2097 C CD1 . LEU A 268 ? 1.0051 0.6590 0.7142 0.0031  -0.0923 -0.0054 564 LEU A CD1 
2098 C CD2 . LEU A 268 ? 0.9571 0.6694 0.7130 -0.0627 -0.0860 0.0007  564 LEU A CD2 
2099 N N   . PRO A 269 ? 0.9296 0.5876 0.6735 -0.0739 -0.0922 -0.0076 565 PRO A N   
2100 C CA  . PRO A 269 ? 0.8546 0.5834 0.6655 -0.0915 -0.0897 -0.0100 565 PRO A CA  
2101 C C   . PRO A 269 ? 0.7382 0.5413 0.6162 -0.0772 -0.0855 -0.0139 565 PRO A C   
2102 O O   . PRO A 269 ? 0.8960 0.7132 0.7903 -0.0453 -0.0852 -0.0188 565 PRO A O   
2103 C CB  . PRO A 269 ? 0.8841 0.6005 0.6946 -0.0733 -0.0913 -0.0148 565 PRO A CB  
2104 C CG  . PRO A 269 ? 0.9219 0.5972 0.6942 -0.0304 -0.0926 -0.0173 565 PRO A CG  
2105 C CD  . PRO A 269 ? 0.8904 0.5347 0.6254 -0.0281 -0.0933 -0.0128 565 PRO A CD  
2106 N N   . ALA A 270 ? 0.7151 0.5677 0.6286 -0.1002 -0.0824 -0.0119 566 ALA A N   
2107 C CA  . ALA A 270 ? 0.6403 0.5499 0.6036 -0.0877 -0.0785 -0.0156 566 ALA A CA  
2108 C C   . ALA A 270 ? 0.7043 0.6707 0.7108 -0.1035 -0.0751 -0.0155 566 ALA A C   
2109 O O   . ALA A 270 ? 0.7319 0.7162 0.7332 -0.1285 -0.0737 -0.0098 566 ALA A O   
2110 C CB  . ALA A 270 ? 0.6128 0.5116 0.5541 -0.0895 -0.0777 -0.0123 566 ALA A CB  
2111 N N   . VAL A 271 ? 0.5782 0.5737 0.6230 -0.0883 -0.0738 -0.0211 567 VAL A N   
2112 C CA  . VAL A 271 ? 0.6431 0.6854 0.7218 -0.0951 -0.0710 -0.0210 567 VAL A CA  
2113 C C   . VAL A 271 ? 0.6093 0.6900 0.7121 -0.0872 -0.0665 -0.0230 567 VAL A C   
2114 O O   . VAL A 271 ? 0.7415 0.8201 0.8540 -0.0699 -0.0655 -0.0287 567 VAL A O   
2115 C CB  . VAL A 271 ? 0.6037 0.6503 0.7034 -0.0814 -0.0713 -0.0256 567 VAL A CB  
2116 C CG1 . VAL A 271 ? 0.5746 0.6648 0.7079 -0.0746 -0.0674 -0.0275 567 VAL A CG1 
2117 C CG2 . VAL A 271 ? 0.5779 0.6003 0.6570 -0.0937 -0.0751 -0.0227 567 VAL A CG2 
2118 N N   . SER A 272 ? 0.6669 0.7864 0.7775 -0.0999 -0.0637 -0.0186 568 SER A N   
2119 C CA  . SER A 272 ? 0.7068 0.8603 0.8318 -0.0906 -0.0588 -0.0200 568 SER A CA  
2120 C C   . SER A 272 ? 0.7147 0.9133 0.8653 -0.0766 -0.0549 -0.0217 568 SER A C   
2121 O O   . SER A 272 ? 0.6676 0.8886 0.8253 -0.0621 -0.0503 -0.0243 568 SER A O   
2122 C CB  . SER A 272 ? 0.7086 0.8749 0.8144 -0.1125 -0.0574 -0.0127 568 SER A CB  
2123 O OG  . SER A 272 ? 0.7228 0.9158 0.8239 -0.1379 -0.0582 -0.0056 568 SER A OG  
2124 N N   . ASN A 273 ? 0.6524 0.8611 0.8119 -0.0771 -0.0565 -0.0205 569 ASN A N   
2125 C CA  . ASN A 273 ? 0.6422 0.8980 0.8185 -0.0625 -0.0532 -0.0197 569 ASN A CA  
2126 C C   . ASN A 273 ? 0.6575 0.8912 0.8403 -0.0376 -0.0524 -0.0262 569 ASN A C   
2127 O O   . ASN A 273 ? 0.6814 0.9425 0.8700 -0.0199 -0.0501 -0.0256 569 ASN A O   
2128 C CB  . ASN A 273 ? 0.5875 0.8826 0.7663 -0.0818 -0.0557 -0.0123 569 ASN A CB  
2129 C CG  . ASN A 273 ? 0.6309 0.8884 0.8025 -0.0932 -0.0614 -0.0125 569 ASN A CG  
2130 O OD1 . ASN A 273 ? 0.6177 0.8255 0.7849 -0.0839 -0.0628 -0.0178 569 ASN A OD1 
2131 N ND2 . ASN A 273 ? 0.5888 0.8757 0.7577 -0.1143 -0.0648 -0.0067 569 ASN A ND2 
2132 N N   . MET A 274 ? 0.5916 0.7781 0.7694 -0.0357 -0.0543 -0.0317 570 MET A N   
2133 C CA  . MET A 274 ? 0.6028 0.7651 0.7812 -0.0204 -0.0537 -0.0370 570 MET A CA  
2134 C C   . MET A 274 ? 0.6466 0.7929 0.8164 -0.0058 -0.0504 -0.0437 570 MET A C   
2135 O O   . MET A 274 ? 0.6903 0.8471 0.8569 -0.0048 -0.0486 -0.0446 570 MET A O   
2136 C CB  . MET A 274 ? 0.6026 0.7331 0.7797 -0.0300 -0.0575 -0.0385 570 MET A CB  
2137 C CG  . MET A 274 ? 0.6330 0.7698 0.8110 -0.0417 -0.0608 -0.0330 570 MET A CG  
2138 S SD  . MET A 274 ? 0.5193 0.6200 0.6927 -0.0436 -0.0636 -0.0360 570 MET A SD  
2139 C CE  . MET A 274 ? 0.5036 0.5960 0.6816 -0.0300 -0.0603 -0.0401 570 MET A CE  
2140 N N   . LEU A 275 ? 0.6529 0.7697 0.8134 0.0038  -0.0497 -0.0484 571 LEU A N   
2141 C CA  . LEU A 275 ? 0.6556 0.7460 0.7963 0.0156  -0.0470 -0.0553 571 LEU A CA  
2142 C C   . LEU A 275 ? 0.7204 0.7759 0.8541 0.0020  -0.0494 -0.0610 571 LEU A C   
2143 O O   . LEU A 275 ? 0.7041 0.7457 0.8381 -0.0036 -0.0505 -0.0601 571 LEU A O   
2144 C CB  . LEU A 275 ? 0.6239 0.7052 0.7451 0.0401  -0.0433 -0.0554 571 LEU A CB  
2145 C CG  . LEU A 275 ? 0.7041 0.7489 0.7912 0.0564  -0.0400 -0.0627 571 LEU A CG  
2146 C CD1 . LEU A 275 ? 0.7645 0.8279 0.8362 0.0899  -0.0354 -0.0604 571 LEU A CD1 
2147 C CD2 . LEU A 275 ? 0.7369 0.7196 0.7941 0.0494  -0.0410 -0.0684 571 LEU A CD2 
2148 N N   . LEU A 276 ? 0.6489 0.6969 0.7762 -0.0043 -0.0503 -0.0664 572 LEU A N   
2149 C CA  . LEU A 276 ? 0.7447 0.7742 0.8657 -0.0201 -0.0531 -0.0720 572 LEU A CA  
2150 C C   . LEU A 276 ? 0.8439 0.8306 0.9303 -0.0195 -0.0513 -0.0787 572 LEU A C   
2151 O O   . LEU A 276 ? 0.8962 0.8688 0.9619 -0.0072 -0.0491 -0.0822 572 LEU A O   
2152 C CB  . LEU A 276 ? 0.7753 0.8239 0.9048 -0.0277 -0.0562 -0.0741 572 LEU A CB  
2153 C CG  . LEU A 276 ? 0.7114 0.7555 0.8330 -0.0434 -0.0595 -0.0808 572 LEU A CG  
2154 C CD1 . LEU A 276 ? 0.6489 0.7018 0.7809 -0.0546 -0.0612 -0.0792 572 LEU A CD1 
2155 C CD2 . LEU A 276 ? 0.5868 0.6548 0.7152 -0.0443 -0.0628 -0.0819 572 LEU A CD2 
2156 N N   . GLU A 277 ? 0.7083 0.6709 0.7824 -0.0338 -0.0521 -0.0803 573 GLU A N   
2157 C CA  . GLU A 277 ? 0.7974 0.7046 0.8263 -0.0395 -0.0508 -0.0860 573 GLU A CA  
2158 C C   . GLU A 277 ? 0.8701 0.7763 0.8917 -0.0713 -0.0544 -0.0917 573 GLU A C   
2159 O O   . GLU A 277 ? 0.8289 0.7649 0.8732 -0.0878 -0.0564 -0.0892 573 GLU A O   
2160 C CB  . GLU A 277 ? 0.8886 0.7648 0.9002 -0.0339 -0.0484 -0.0820 573 GLU A CB  
2161 C CG  . GLU A 277 ? 1.0991 0.9100 1.0546 -0.0176 -0.0452 -0.0850 573 GLU A CG  
2162 C CD  . GLU A 277 ? 1.2224 0.9740 1.1341 -0.0390 -0.0451 -0.0867 573 GLU A CD  
2163 O OE1 . GLU A 277 ? 1.1446 0.8831 1.0415 -0.0728 -0.0476 -0.0921 573 GLU A OE1 
2164 O OE2 . GLU A 277 ? 1.3549 1.0754 1.2448 -0.0235 -0.0427 -0.0821 573 GLU A OE2 
2165 N N   . ILE A 278 ? 0.8179 0.6959 0.8072 -0.0794 -0.0556 -0.0994 574 ILE A N   
2166 C CA  . ILE A 278 ? 0.8426 0.7213 0.8178 -0.1142 -0.0598 -0.1055 574 ILE A CA  
2167 C C   . ILE A 278 ? 0.9188 0.7195 0.8266 -0.1261 -0.0592 -0.1129 574 ILE A C   
2168 O O   . ILE A 278 ? 1.0793 0.8447 0.9583 -0.1055 -0.0575 -0.1170 574 ILE A O   
2169 C CB  . ILE A 278 ? 0.8399 0.7688 0.8408 -0.1177 -0.0642 -0.1085 574 ILE A CB  
2170 C CG1 . ILE A 278 ? 0.8014 0.7894 0.8541 -0.1002 -0.0645 -0.1010 574 ILE A CG1 
2171 C CG2 . ILE A 278 ? 0.8625 0.8085 0.8530 -0.1554 -0.0694 -0.1141 574 ILE A CG2 
2172 C CD1 . ILE A 278 ? 0.7793 0.8070 0.8490 -0.0971 -0.0684 -0.1028 574 ILE A CD1 
2173 N N   . GLY A 279 ? 0.8808 0.6523 0.7581 -0.1601 -0.0604 -0.1145 575 GLY A N   
2174 C CA  . GLY A 279 ? 0.9979 0.6824 0.7980 -0.1805 -0.0605 -0.1215 575 GLY A CA  
2175 C C   . GLY A 279 ? 1.1388 0.7456 0.8883 -0.1424 -0.0559 -0.1227 575 GLY A C   
2176 O O   . GLY A 279 ? 1.3303 0.8715 1.0185 -0.1434 -0.0564 -0.1308 575 GLY A O   
2177 N N   . GLY A 280 ? 1.1117 0.7275 0.8830 -0.1066 -0.0515 -0.1149 576 GLY A N   
2178 C CA  . GLY A 280 ? 1.1289 0.6886 0.8574 -0.0629 -0.0468 -0.1147 576 GLY A CA  
2179 C C   . GLY A 280 ? 1.0994 0.7019 0.8566 -0.0259 -0.0449 -0.1151 576 GLY A C   
2180 O O   . GLY A 280 ? 1.1293 0.7101 0.8632 0.0167  -0.0403 -0.1133 576 GLY A O   
2181 N N   . LEU A 281 ? 1.0746 0.7412 0.8798 -0.0393 -0.0480 -0.1168 577 LEU A N   
2182 C CA  . LEU A 281 ? 1.0614 0.7695 0.8916 -0.0100 -0.0460 -0.1166 577 LEU A CA  
2183 C C   . LEU A 281 ? 0.9808 0.7648 0.8773 0.0060  -0.0444 -0.1064 577 LEU A C   
2184 O O   . LEU A 281 ? 0.9610 0.7842 0.8990 -0.0143 -0.0473 -0.1018 577 LEU A O   
2185 C CB  . LEU A 281 ? 0.9536 0.6851 0.7937 -0.0326 -0.0504 -0.1230 577 LEU A CB  
2186 C CG  . LEU A 281 ? 1.0301 0.6891 0.8015 -0.0543 -0.0532 -0.1342 577 LEU A CG  
2187 C CD1 . LEU A 281 ? 0.9506 0.6496 0.7408 -0.0720 -0.0580 -0.1396 577 LEU A CD1 
2188 C CD2 . LEU A 281 ? 1.1577 0.7378 0.8588 -0.0194 -0.0480 -0.1386 577 LEU A CD2 
2189 N N   . GLU A 282 ? 0.9848 0.7909 0.8870 0.0417  -0.0399 -0.1030 578 GLU A N   
2190 C CA  . GLU A 282 ? 0.8985 0.7695 0.8513 0.0548  -0.0384 -0.0931 578 GLU A CA  
2191 C C   . GLU A 282 ? 0.8424 0.7734 0.8325 0.0550  -0.0383 -0.0908 578 GLU A C   
2192 O O   . GLU A 282 ? 0.8786 0.8141 0.8527 0.0750  -0.0348 -0.0933 578 GLU A O   
2193 C CB  . GLU A 282 ? 0.9487 0.8122 0.8800 0.0929  -0.0334 -0.0890 578 GLU A CB  
2194 C CG  . GLU A 282 ? 1.0793 0.8846 0.9749 0.0941  -0.0336 -0.0886 578 GLU A CG  
2195 C CD  . GLU A 282 ? 1.0970 0.9092 0.9783 0.1358  -0.0296 -0.0827 578 GLU A CD  
2196 O OE1 . GLU A 282 ? 0.9857 0.8252 0.8604 0.1692  -0.0256 -0.0825 578 GLU A OE1 
2197 O OE2 . GLU A 282 ? 1.1693 0.9659 1.0462 0.1362  -0.0305 -0.0781 578 GLU A OE2 
2198 N N   . PHE A 283 ? 0.7778 0.7505 0.8114 0.0342  -0.0419 -0.0859 579 PHE A N   
2199 C CA  . PHE A 283 ? 0.7065 0.7270 0.7695 0.0299  -0.0425 -0.0823 579 PHE A CA  
2200 C C   . PHE A 283 ? 0.6556 0.7216 0.7472 0.0358  -0.0408 -0.0724 579 PHE A C   
2201 O O   . PHE A 283 ? 0.7366 0.8131 0.8494 0.0216  -0.0440 -0.0678 579 PHE A O   
2202 C CB  . PHE A 283 ? 0.6478 0.6734 0.7261 0.0048  -0.0482 -0.0842 579 PHE A CB  
2203 C CG  . PHE A 283 ? 0.7617 0.7556 0.8130 -0.0062 -0.0508 -0.0939 579 PHE A CG  
2204 C CD1 . PHE A 283 ? 0.7781 0.7437 0.8150 -0.0247 -0.0538 -0.0983 579 PHE A CD1 
2205 C CD2 . PHE A 283 ? 0.7631 0.7577 0.8006 -0.0013 -0.0504 -0.0984 579 PHE A CD2 
2206 C CE1 . PHE A 283 ? 0.8698 0.8095 0.8780 -0.0419 -0.0570 -0.1073 579 PHE A CE1 
2207 C CE2 . PHE A 283 ? 0.8540 0.8201 0.8635 -0.0148 -0.0538 -0.1079 579 PHE A CE2 
2208 C CZ  . PHE A 283 ? 0.9040 0.8431 0.8982 -0.0370 -0.0575 -0.1124 579 PHE A CZ  
2209 N N   . SER A 284 ? 0.7067 0.8024 0.7957 0.0561  -0.0359 -0.0693 580 SER A N   
2210 C CA  . SER A 284 ? 0.6599 0.8081 0.7718 0.0593  -0.0342 -0.0598 580 SER A CA  
2211 C C   . SER A 284 ? 0.6391 0.8236 0.7742 0.0362  -0.0361 -0.0534 580 SER A C   
2212 O O   . SER A 284 ? 0.6980 0.9224 0.8488 0.0285  -0.0361 -0.0454 580 SER A O   
2213 C CB  . SER A 284 ? 0.7349 0.9129 0.8333 0.0907  -0.0279 -0.0587 580 SER A CB  
2214 O OG  . SER A 284 ? 0.7329 0.9095 0.8163 0.0984  -0.0246 -0.0633 580 SER A OG  
2215 N N   . ALA A 285 ? 0.6753 0.8449 0.8071 0.0244  -0.0381 -0.0566 581 ALA A N   
2216 C CA  . ALA A 285 ? 0.5424 0.7300 0.6840 0.0039  -0.0402 -0.0504 581 ALA A CA  
2217 C C   . ALA A 285 ? 0.6268 0.7790 0.7655 -0.0070 -0.0459 -0.0546 581 ALA A C   
2218 O O   . ALA A 285 ? 0.7229 0.8597 0.8510 -0.0034 -0.0466 -0.0611 581 ALA A O   
2219 C CB  . ALA A 285 ? 0.6210 0.8385 0.7568 0.0065  -0.0357 -0.0481 581 ALA A CB  
2220 N N   . CYS A 286 ? 0.5875 0.7304 0.7332 -0.0186 -0.0500 -0.0512 582 CYS A N   
2221 C CA  . CYS A 286 ? 0.5793 0.6991 0.7229 -0.0235 -0.0551 -0.0546 582 CYS A CA  
2222 C C   . CYS A 286 ? 0.6729 0.7851 0.8139 -0.0332 -0.0587 -0.0481 582 CYS A C   
2223 O O   . CYS A 286 ? 0.7922 0.8922 0.9363 -0.0330 -0.0616 -0.0494 582 CYS A O   
2224 C CB  . CYS A 286 ? 0.6151 0.7191 0.7614 -0.0204 -0.0560 -0.0609 582 CYS A CB  
2225 S SG  . CYS A 286 ? 0.6140 0.7185 0.7689 -0.0188 -0.0544 -0.0568 582 CYS A SG  
2226 N N   . PRO A 287 ? 0.6565 0.7709 0.7854 -0.0423 -0.0586 -0.0412 583 PRO A N   
2227 C CA  . PRO A 287 ? 0.5805 0.6716 0.6927 -0.0521 -0.0623 -0.0354 583 PRO A CA  
2228 C C   . PRO A 287 ? 0.6233 0.6907 0.7266 -0.0410 -0.0668 -0.0389 583 PRO A C   
2229 O O   . PRO A 287 ? 0.4822 0.5518 0.5827 -0.0317 -0.0682 -0.0427 583 PRO A O   
2230 C CB  . PRO A 287 ? 0.5920 0.6808 0.6819 -0.0658 -0.0613 -0.0283 583 PRO A CB  
2231 C CG  . PRO A 287 ? 0.7040 0.8149 0.8017 -0.0571 -0.0578 -0.0320 583 PRO A CG  
2232 C CD  . PRO A 287 ? 0.7026 0.8356 0.8251 -0.0454 -0.0549 -0.0384 583 PRO A CD  
2233 N N   . PHE A 288 ? 0.5594 0.6102 0.6581 -0.0406 -0.0692 -0.0377 584 PHE A N   
2234 C CA  . PHE A 288 ? 0.5345 0.5717 0.6241 -0.0260 -0.0729 -0.0403 584 PHE A CA  
2235 C C   . PHE A 288 ? 0.6656 0.6629 0.7205 -0.0262 -0.0757 -0.0349 584 PHE A C   
2236 O O   . PHE A 288 ? 0.5948 0.5799 0.6430 -0.0417 -0.0753 -0.0310 584 PHE A O   
2237 C CB  . PHE A 288 ? 0.5365 0.5941 0.6519 -0.0208 -0.0722 -0.0461 584 PHE A CB  
2238 C CG  . PHE A 288 ? 0.6470 0.7033 0.7731 -0.0295 -0.0704 -0.0444 584 PHE A CG  
2239 C CD1 . PHE A 288 ? 0.5743 0.6120 0.6883 -0.0279 -0.0722 -0.0420 584 PHE A CD1 
2240 C CD2 . PHE A 288 ? 0.6540 0.7269 0.7983 -0.0354 -0.0669 -0.0456 584 PHE A CD2 
2241 C CE1 . PHE A 288 ? 0.5162 0.5554 0.6396 -0.0357 -0.0711 -0.0406 584 PHE A CE1 
2242 C CE2 . PHE A 288 ? 0.5832 0.6584 0.7354 -0.0395 -0.0658 -0.0436 584 PHE A CE2 
2243 C CZ  . PHE A 288 ? 0.5393 0.5993 0.6829 -0.0414 -0.0681 -0.0410 584 PHE A CZ  
2244 N N   . SER A 289 ? 0.7399 0.7163 0.7682 -0.0075 -0.0790 -0.0350 585 SER A N   
2245 C CA  . SER A 289 ? 0.7912 0.7128 0.7691 -0.0031 -0.0819 -0.0300 585 SER A CA  
2246 C C   . SER A 289 ? 0.6147 0.5325 0.5803 0.0271  -0.0843 -0.0330 585 SER A C   
2247 O O   . SER A 289 ? 0.6907 0.6476 0.6759 0.0454  -0.0848 -0.0372 585 SER A O   
2248 C CB  . SER A 289 ? 0.9709 0.8542 0.9048 -0.0061 -0.0834 -0.0243 585 SER A CB  
2249 O OG  . SER A 289 ? 0.9460 0.8435 0.8780 0.0188  -0.0851 -0.0268 585 SER A OG  
2250 N N   . GLY A 290 ? 0.6129 0.4863 0.5425 0.0320  -0.0858 -0.0308 586 GLY A N   
2251 C CA  . GLY A 290 ? 0.6623 0.5227 0.5633 0.0677  -0.0879 -0.0324 586 GLY A CA  
2252 C C   . GLY A 290 ? 0.8361 0.6099 0.6586 0.0766  -0.0909 -0.0274 586 GLY A C   
2253 O O   . GLY A 290 ? 0.8867 0.6166 0.6677 0.0717  -0.0927 -0.0227 586 GLY A O   
2254 N N   . TRP A 291 ? 0.8910 0.6340 0.6863 0.0891  -0.0916 -0.0284 587 TRP A N   
2255 C CA  . TRP A 291 ? 0.9651 0.6117 0.6766 0.0918  -0.0946 -0.0245 587 TRP A CA  
2256 C C   . TRP A 291 ? 0.9527 0.5848 0.6654 0.0736  -0.0944 -0.0261 587 TRP A C   
2257 O O   . TRP A 291 ? 0.8893 0.5864 0.6651 0.0680  -0.0915 -0.0298 587 TRP A O   
2258 C CB  . TRP A 291 ? 0.9995 0.6070 0.6501 0.1444  -0.0968 -0.0247 587 TRP A CB  
2259 C CG  . TRP A 291 ? 1.0912 0.7687 0.7805 0.1813  -0.0947 -0.0301 587 TRP A CG  
2260 C CD1 . TRP A 291 ? 1.1124 0.7892 0.7961 0.1965  -0.0932 -0.0332 587 TRP A CD1 
2261 C CD2 . TRP A 291 ? 1.0917 0.8563 0.8301 0.2048  -0.0937 -0.0328 587 TRP A CD2 
2262 N NE1 . TRP A 291 ? 1.0940 0.8563 0.8215 0.2276  -0.0908 -0.0370 587 TRP A NE1 
2263 C CE2 . TRP A 291 ? 1.1127 0.9313 0.8741 0.2313  -0.0914 -0.0369 587 TRP A CE2 
2264 C CE3 . TRP A 291 ? 1.1210 0.9259 0.8842 0.2041  -0.0948 -0.0322 587 TRP A CE3 
2265 C CZ2 . TRP A 291 ? 1.1370 1.0531 0.9459 0.2524  -0.0903 -0.0401 587 TRP A CZ2 
2266 C CZ3 . TRP A 291 ? 1.1049 1.0009 0.9133 0.2263  -0.0945 -0.0360 587 TRP A CZ3 
2267 C CH2 . TRP A 291 ? 1.1394 1.0924 0.9704 0.2482  -0.0924 -0.0397 587 TRP A CH2 
2268 N N   . TYR A 292 ? 1.0686 0.6101 0.7054 0.0619  -0.0977 -0.0229 588 TYR A N   
2269 C CA  . TYR A 292 ? 1.0907 0.6119 0.7208 0.0365  -0.0987 -0.0239 588 TYR A CA  
2270 C C   . TYR A 292 ? 1.1412 0.6429 0.7452 0.0753  -0.0984 -0.0285 588 TYR A C   
2271 O O   . TYR A 292 ? 1.0674 0.5175 0.6089 0.1171  -0.0995 -0.0289 588 TYR A O   
2272 C CB  . TYR A 292 ? 1.1635 0.5951 0.7178 -0.0020 -0.1031 -0.0186 588 TYR A CB  
2273 C CG  . TYR A 292 ? 1.1469 0.6157 0.7378 -0.0572 -0.1030 -0.0143 588 TYR A CG  
2274 C CD1 . TYR A 292 ? 1.1626 0.6041 0.7223 -0.0824 -0.1038 -0.0081 588 TYR A CD1 
2275 C CD2 . TYR A 292 ? 1.0680 0.6001 0.7194 -0.0826 -0.1021 -0.0158 588 TYR A CD2 
2276 C CE1 . TYR A 292 ? 1.1370 0.6226 0.7287 -0.1314 -0.1031 -0.0036 588 TYR A CE1 
2277 C CE2 . TYR A 292 ? 1.0849 0.6598 0.7668 -0.1278 -0.1019 -0.0114 588 TYR A CE2 
2278 C CZ  . TYR A 292 ? 1.1268 0.6824 0.7803 -0.1520 -0.1022 -0.0053 588 TYR A CZ  
2279 O OH  . TYR A 292 ? 1.0868 0.6957 0.7703 -0.1950 -0.1013 -0.0005 588 TYR A OH  
2280 N N   . MET A 293 ? 1.0777 0.6225 0.7272 0.0646  -0.0967 -0.0316 589 MET A N   
2281 C CA  . MET A 293 ? 1.1673 0.6661 0.7708 0.0832  -0.0976 -0.0347 589 MET A CA  
2282 C C   . MET A 293 ? 1.1380 0.5425 0.6673 0.0468  -0.1031 -0.0321 589 MET A C   
2283 O O   . MET A 293 ? 1.1279 0.5442 0.6770 -0.0016 -0.1050 -0.0284 589 MET A O   
2284 C CB  . MET A 293 ? 1.0823 0.6560 0.7552 0.0810  -0.0939 -0.0382 589 MET A CB  
2285 C CG  . MET A 293 ? 1.0502 0.5952 0.6845 0.1126  -0.0930 -0.0421 589 MET A CG  
2286 S SD  . MET A 293 ? 0.9259 0.5693 0.6475 0.1093  -0.0876 -0.0449 589 MET A SD  
2287 C CE  . MET A 293 ? 0.7944 0.4448 0.5498 0.0494  -0.0908 -0.0418 589 MET A CE  
2288 N N   . GLY A 294 ? 1.1400 0.4501 0.5773 0.0703  -0.1058 -0.0338 590 GLY A N   
2289 C CA  . GLY A 294 ? 1.2540 0.4580 0.6025 0.0325  -0.1119 -0.0313 590 GLY A CA  
2290 C C   . GLY A 294 ? 1.2925 0.5270 0.6766 -0.0222 -0.1144 -0.0311 590 GLY A C   
2291 O O   . GLY A 294 ? 1.3880 0.5824 0.7360 -0.0738 -0.1192 -0.0269 590 GLY A O   
2292 N N   . THR A 295 ? 1.2675 0.5762 0.7200 -0.0124 -0.1114 -0.0349 591 THR A N   
2293 C CA  . THR A 295 ? 1.1831 0.5076 0.6522 -0.0553 -0.1147 -0.0351 591 THR A CA  
2294 C C   . THR A 295 ? 1.1057 0.4953 0.6325 -0.1051 -0.1158 -0.0298 591 THR A C   
2295 O O   . THR A 295 ? 1.1085 0.4872 0.6167 -0.1521 -0.1211 -0.0276 591 THR A O   
2296 C CB  . THR A 295 ? 1.0110 0.3978 0.5365 -0.0306 -0.1107 -0.0396 591 THR A CB  
2297 O OG1 . THR A 295 ? 0.9563 0.4433 0.5744 -0.0130 -0.1043 -0.0392 591 THR A OG1 
2298 C CG2 . THR A 295 ? 1.1275 0.4493 0.5860 0.0181  -0.1096 -0.0447 591 THR A CG2 
2299 N N   . GLU A 296 ? 0.9550 0.4160 0.5489 -0.0956 -0.1110 -0.0278 592 GLU A N   
2300 C CA  . GLU A 296 ? 0.9705 0.4952 0.6151 -0.1370 -0.1112 -0.0230 592 GLU A CA  
2301 C C   . GLU A 296 ? 1.1461 0.6104 0.7229 -0.1826 -0.1166 -0.0176 592 GLU A C   
2302 O O   . GLU A 296 ? 1.2305 0.7356 0.8260 -0.2281 -0.1192 -0.0137 592 GLU A O   
2303 C CB  . GLU A 296 ? 0.8784 0.4740 0.5914 -0.1177 -0.1053 -0.0223 592 GLU A CB  
2304 C CG  . GLU A 296 ? 0.8782 0.5043 0.6274 -0.0692 -0.1003 -0.0273 592 GLU A CG  
2305 C CD  . GLU A 296 ? 0.9814 0.6529 0.7719 -0.0544 -0.0963 -0.0267 592 GLU A CD  
2306 O OE1 . GLU A 296 ? 0.8856 0.6068 0.7192 -0.0776 -0.0950 -0.0240 592 GLU A OE1 
2307 O OE2 . GLU A 296 ? 0.9228 0.5820 0.6992 -0.0181 -0.0948 -0.0290 592 GLU A OE2 
2308 N N   . ILE A 297 ? 1.2426 0.6095 0.7347 -0.1718 -0.1185 -0.0170 593 ILE A N   
2309 C CA  . ILE A 297 ? 1.3584 0.6488 0.7679 -0.2200 -0.1239 -0.0115 593 ILE A CA  
2310 C C   . ILE A 297 ? 1.4022 0.6158 0.7360 -0.2477 -0.1309 -0.0135 593 ILE A C   
2311 O O   . ILE A 297 ? 1.3740 0.6208 0.7112 -0.2989 -0.1333 -0.0084 593 ILE A O   
2312 C CB  . ILE A 297 ? 1.4191 0.6226 0.7554 -0.1973 -0.1234 -0.0091 593 ILE A CB  
2313 C CG1 . ILE A 297 ? 1.3014 0.5791 0.7104 -0.1614 -0.1170 -0.0088 593 ILE A CG1 
2314 C CG2 . ILE A 297 ? 1.4630 0.6026 0.7241 -0.2555 -0.1276 -0.0015 593 ILE A CG2 
2315 C CD1 . ILE A 297 ? 1.3041 0.5020 0.6410 -0.1397 -0.1171 -0.0056 593 ILE A CD1 
2316 N N   . GLY A 298 ? 1.5105 0.6393 0.7803 -0.2064 -0.1317 -0.0190 594 GLY A N   
2317 C CA  . GLY A 298 ? 1.5369 0.6026 0.7304 -0.2198 -0.1343 -0.0169 594 GLY A CA  
2318 C C   . GLY A 298 ? 1.4971 0.6248 0.7378 -0.2503 -0.1370 -0.0188 594 GLY A C   
2319 O O   . GLY A 298 ? 1.4765 0.5963 0.6812 -0.2936 -0.1396 -0.0126 594 GLY A O   
2320 N N   . VAL A 299 ? 1.4640 0.6581 0.7850 -0.2285 -0.1367 -0.0269 595 VAL A N   
2321 C CA  . VAL A 299 ? 1.3807 0.6387 0.7497 -0.2491 -0.1392 -0.0287 595 VAL A CA  
2322 C C   . VAL A 299 ? 1.3023 0.6687 0.7481 -0.2926 -0.1398 -0.0228 595 VAL A C   
2323 O O   . VAL A 299 ? 1.2707 0.6622 0.7069 -0.3362 -0.1428 -0.0172 595 VAL A O   
2324 C CB  . VAL A 299 ? 1.2239 0.5389 0.6591 -0.1953 -0.1329 -0.0339 595 VAL A CB  
2325 C CG1 . VAL A 299 ? 1.0591 0.4160 0.5209 -0.2175 -0.1366 -0.0354 595 VAL A CG1 
2326 C CG2 . VAL A 299 ? 1.1548 0.3939 0.5336 -0.1386 -0.1296 -0.0392 595 VAL A CG2 
2327 N N   . ARG A 300 ? 1.1148 0.5691 0.6476 -0.2679 -0.1326 -0.0209 596 ARG A N   
2328 C CA  . ARG A 300 ? 1.1232 0.6892 0.7352 -0.2939 -0.1317 -0.0161 596 ARG A CA  
2329 C C   . ARG A 300 ? 1.2126 0.7807 0.7979 -0.3445 -0.1345 -0.0091 596 ARG A C   
2330 O O   . ARG A 300 ? 1.2244 0.8373 0.8108 -0.3858 -0.1370 -0.0036 596 ARG A O   
2331 C CB  . ARG A 300 ? 0.8144 0.4574 0.5137 -0.2501 -0.1230 -0.0171 596 ARG A CB  
2332 C CG  . ARG A 300 ? 0.7815 0.4263 0.5057 -0.2035 -0.1191 -0.0231 596 ARG A CG  
2333 C CD  . ARG A 300 ? 0.9595 0.6256 0.6911 -0.2178 -0.1234 -0.0244 596 ARG A CD  
2334 N NE  . ARG A 300 ? 0.8341 0.5874 0.6174 -0.2466 -0.1252 -0.0196 596 ARG A NE  
2335 C CZ  . ARG A 300 ? 0.8654 0.6993 0.7229 -0.2266 -0.1195 -0.0182 596 ARG A CZ  
2336 N NH1 . ARG A 300 ? 0.8156 0.6530 0.7042 -0.1859 -0.1124 -0.0214 596 ARG A NH1 
2337 N NH2 . ARG A 300 ? 0.8743 0.7852 0.7698 -0.2471 -0.1211 -0.0135 596 ARG A NH2 
2338 N N   . ASP A 301 ? 1.1099 0.6468 0.6780 -0.3338 -0.1307 -0.0069 597 ASP A N   
2339 C CA  . ASP A 301 ? 1.1652 0.7108 0.7105 -0.3784 -0.1309 0.0013  597 ASP A CA  
2340 C C   . ASP A 301 ? 1.2248 0.7260 0.6945 -0.4151 -0.1325 0.0081  597 ASP A C   
2341 O O   . ASP A 301 ? 1.2596 0.8298 0.7449 -0.4538 -0.1317 0.0155  597 ASP A O   
2342 C CB  . ASP A 301 ? 1.2515 0.7407 0.7665 -0.3588 -0.1277 0.0022  597 ASP A CB  
2343 C CG  . ASP A 301 ? 1.1717 0.7419 0.7764 -0.3126 -0.1196 0.0005  597 ASP A CG  
2344 O OD1 . ASP A 301 ? 1.0251 0.6993 0.7096 -0.3146 -0.1168 0.0012  597 ASP A OD1 
2345 O OD2 . ASP A 301 ? 1.2414 0.7693 0.8321 -0.2726 -0.1164 -0.0019 597 ASP A OD2 
2346 N N   . TYR A 302 ? 1.2880 0.6759 0.6718 -0.4013 -0.1347 0.0059  598 TYR A N   
2347 C CA  . TYR A 302 ? 1.4714 0.8004 0.7674 -0.4372 -0.1370 0.0127  598 TYR A CA  
2348 C C   . TYR A 302 ? 1.5073 0.8746 0.8138 -0.4592 -0.1404 0.0127  598 TYR A C   
2349 O O   . TYR A 302 ? 1.5600 0.9371 0.8289 -0.5051 -0.1419 0.0207  598 TYR A O   
2350 C CB  . TYR A 302 ? 1.6935 0.8852 0.8867 -0.4088 -0.1382 0.0107  598 TYR A CB  
2351 C CG  . TYR A 302 ? 1.7757 0.9140 0.9256 -0.4002 -0.1358 0.0143  598 TYR A CG  
2352 C CD1 . TYR A 302 ? 1.8498 0.8812 0.9265 -0.3548 -0.1359 0.0108  598 TYR A CD1 
2353 C CD2 . TYR A 302 ? 1.7426 0.9400 0.9216 -0.4344 -0.1332 0.0214  598 TYR A CD2 
2354 C CE1 . TYR A 302 ? 1.8507 0.8325 0.8841 -0.3439 -0.1341 0.0142  598 TYR A CE1 
2355 C CE2 . TYR A 302 ? 1.7634 0.9088 0.8993 -0.4272 -0.1313 0.0247  598 TYR A CE2 
2356 C CZ  . TYR A 302 ? 1.8048 0.8403 0.8671 -0.3823 -0.1321 0.0210  598 TYR A CZ  
2357 O OH  . TYR A 302 ? 1.7736 0.7561 0.7890 -0.3719 -0.1306 0.0242  598 TYR A OH  
2358 N N   . CYS A 303 ? 1.3476 0.7374 0.7011 -0.4290 -0.1420 0.0041  599 CYS A N   
2359 C CA  . CYS A 303 ? 1.3331 0.7348 0.6789 -0.4443 -0.1460 0.0033  599 CYS A CA  
2360 C C   . CYS A 303 ? 1.2370 0.7597 0.6808 -0.4457 -0.1468 0.0012  599 CYS A C   
2361 O O   . CYS A 303 ? 1.1792 0.7174 0.6197 -0.4575 -0.1505 0.0005  599 CYS A O   
2362 C CB  . CYS A 303 ? 1.4124 0.7150 0.7016 -0.4077 -0.1481 -0.0046 599 CYS A CB  
2363 S SG  . CYS A 303 ? 1.4911 0.6444 0.6443 -0.4034 -0.1483 -0.0007 599 CYS A SG  
2364 N N   . ASP A 304 ? 1.2206 0.8269 0.7471 -0.4316 -0.1439 0.0002  600 ASP A N   
2365 C CA  . ASP A 304 ? 1.2643 0.9928 0.8724 -0.4384 -0.1443 0.0019  600 ASP A CA  
2366 C C   . ASP A 304 ? 1.3468 1.1220 0.9348 -0.4848 -0.1443 0.0118  600 ASP A C   
2367 O O   . ASP A 304 ? 1.4952 1.2442 1.0354 -0.5137 -0.1421 0.0189  600 ASP A O   
2368 C CB  . ASP A 304 ? 1.2109 1.0206 0.8981 -0.4200 -0.1402 0.0020  600 ASP A CB  
2369 C CG  . ASP A 304 ? 1.1095 0.9317 0.8496 -0.3768 -0.1409 -0.0063 600 ASP A CG  
2370 O OD1 . ASP A 304 ? 1.0096 0.7723 0.7244 -0.3531 -0.1418 -0.0121 600 ASP A OD1 
2371 O OD2 . ASP A 304 ? 1.0999 0.9972 0.9089 -0.3513 -0.1341 -0.0043 600 ASP A OD2 
2372 N N   . ASN A 305 ? 1.3228 1.1660 0.9422 -0.4925 -0.1472 0.0124  601 ASN A N   
2373 C CA  . ASN A 305 ? 1.3010 1.1925 0.8984 -0.5370 -0.1476 0.0217  601 ASN A CA  
2374 C C   . ASN A 305 ? 1.1855 1.1682 0.8195 -0.5525 -0.1420 0.0299  601 ASN A C   
2375 O O   . ASN A 305 ? 1.1788 1.1642 0.7662 -0.5946 -0.1407 0.0386  601 ASN A O   
2376 C CB  . ASN A 305 ? 1.2932 1.2497 0.9242 -0.5360 -0.1518 0.0205  601 ASN A CB  
2377 C CG  . ASN A 305 ? 1.4605 1.3326 1.0202 -0.5529 -0.1573 0.0184  601 ASN A CG  
2378 O OD1 . ASN A 305 ? 1.6299 1.4150 1.1067 -0.5802 -0.1577 0.0220  601 ASN A OD1 
2379 N ND2 . ASN A 305 ? 1.4012 1.2965 0.9875 -0.5366 -0.1619 0.0131  601 ASN A ND2 
2380 N N   . SER A 306 ? 1.1057 1.1646 0.8188 -0.5195 -0.1385 0.0276  602 SER A N   
2381 C CA  . SER A 306 ? 1.2025 1.3503 0.9528 -0.5259 -0.1323 0.0345  602 SER A CA  
2382 C C   . SER A 306 ? 1.1946 1.2918 0.9326 -0.5193 -0.1284 0.0339  602 SER A C   
2383 O O   . SER A 306 ? 1.0835 1.2518 0.8630 -0.5130 -0.1228 0.0374  602 SER A O   
2384 C CB  . SER A 306 ? 1.2352 1.4980 1.0718 -0.4915 -0.1303 0.0335  602 SER A CB  
2385 O OG  . SER A 306 ? 1.2472 1.4844 1.1218 -0.4488 -0.1320 0.0246  602 SER A OG  
2386 N N   . ARG A 307 ? 1.2140 1.1906 0.8929 -0.5176 -0.1309 0.0296  603 ARG A N   
2387 C CA  . ARG A 307 ? 1.2096 1.1246 0.8580 -0.5162 -0.1279 0.0302  603 ARG A CA  
2388 C C   . ARG A 307 ? 1.3310 1.1644 0.8806 -0.5583 -0.1294 0.0369  603 ARG A C   
2389 O O   . ARG A 307 ? 1.3565 1.2392 0.8888 -0.5973 -0.1295 0.0447  603 ARG A O   
2390 C CB  . ARG A 307 ? 1.1645 1.0117 0.8226 -0.4735 -0.1293 0.0203  603 ARG A CB  
2391 C CG  . ARG A 307 ? 1.0757 1.0087 0.8265 -0.4385 -0.1277 0.0156  603 ARG A CG  
2392 C CD  . ARG A 307 ? 1.0569 1.0627 0.8503 -0.4390 -0.1215 0.0205  603 ARG A CD  
2393 N NE  . ARG A 307 ? 1.0271 0.9566 0.7768 -0.4420 -0.1198 0.0210  603 ARG A NE  
2394 C CZ  . ARG A 307 ? 1.0498 0.9148 0.7963 -0.4123 -0.1213 0.0138  603 ARG A CZ  
2395 N NH1 . ARG A 307 ? 0.8728 0.7464 0.6601 -0.3680 -0.1199 0.0071  603 ARG A NH1 
2396 N NH2 . ARG A 307 ? 1.2412 1.0376 0.9434 -0.4130 -0.1198 0.0150  603 ARG A NH2 
2397 N N   . TYR A 308 ? 1.4038 1.1156 0.8832 -0.5510 -0.1308 0.0345  604 TYR A N   
2398 C CA  . TYR A 308 ? 1.4220 1.0517 0.7989 -0.5898 -0.1324 0.0416  604 TYR A CA  
2399 C C   . TYR A 308 ? 1.5134 1.0974 0.8271 -0.6151 -0.1375 0.0431  604 TYR A C   
2400 O O   . TYR A 308 ? 1.5006 1.0542 0.7393 -0.6610 -0.1391 0.0512  604 TYR A O   
2401 C CB  . TYR A 308 ? 1.4222 0.9309 0.7351 -0.5673 -0.1324 0.0388  604 TYR A CB  
2402 C CG  . TYR A 308 ? 1.4853 1.0216 0.8168 -0.5704 -0.1278 0.0428  604 TYR A CG  
2403 C CD1 . TYR A 308 ? 1.4090 1.0310 0.8368 -0.5431 -0.1237 0.0394  604 TYR A CD1 
2404 C CD2 . TYR A 308 ? 1.6447 1.1205 0.8933 -0.6022 -0.1279 0.0499  604 TYR A CD2 
2405 C CE1 . TYR A 308 ? 1.4215 1.0697 0.8656 -0.5462 -0.1193 0.0432  604 TYR A CE1 
2406 C CE2 . TYR A 308 ? 1.6512 1.1535 0.9161 -0.6061 -0.1236 0.0536  604 TYR A CE2 
2407 C CZ  . TYR A 308 ? 1.5455 1.1347 0.9097 -0.5775 -0.1191 0.0503  604 TYR A CZ  
2408 O OH  . TYR A 308 ? 1.5460 1.1617 0.9254 -0.5812 -0.1146 0.0542  604 TYR A OH  
2409 N N   . ASN A 309 ? 1.3599 0.9350 0.6967 -0.5881 -0.1405 0.0356  605 ASN A N   
2410 C CA  . ASN A 309 ? 1.4756 1.0399 0.7745 -0.6135 -0.1450 0.0373  605 ASN A CA  
2411 C C   . ASN A 309 ? 1.6793 1.1142 0.8514 -0.6396 -0.1483 0.0414  605 ASN A C   
2412 O O   . ASN A 309 ? 1.7792 1.2157 0.8978 -0.6893 -0.1506 0.0494  605 ASN A O   
2413 C CB  . ASN A 309 ? 1.4712 1.1629 0.8165 -0.6509 -0.1439 0.0449  605 ASN A CB  
2414 C CG  . ASN A 309 ? 1.4678 1.1824 0.8122 -0.6635 -0.1483 0.0443  605 ASN A CG  
2415 O OD1 . ASN A 309 ? 1.4709 1.1293 0.8083 -0.6356 -0.1517 0.0363  605 ASN A OD1 
2416 N ND2 . ASN A 309 ? 1.4642 1.2646 0.8142 -0.7053 -0.1481 0.0528  605 ASN A ND2 
2417 N N   . ILE A 310 ? 1.7205 1.0420 0.8392 -0.6045 -0.1487 0.0362  606 ILE A N   
2418 C CA  . ILE A 310 ? 1.8596 1.0484 0.8494 -0.6200 -0.1514 0.0402  606 ILE A CA  
2419 C C   . ILE A 310 ? 1.9562 1.0529 0.8813 -0.6026 -0.1556 0.0357  606 ILE A C   
2420 O O   . ILE A 310 ? 2.0652 1.0393 0.8755 -0.6053 -0.1581 0.0380  606 ILE A O   
2421 C CB  . ILE A 310 ? 1.8869 1.0047 0.8429 -0.5906 -0.1489 0.0387  606 ILE A CB  
2422 C CG1 . ILE A 310 ? 1.8241 0.9008 0.8055 -0.5230 -0.1478 0.0280  606 ILE A CG1 
2423 C CG2 . ILE A 310 ? 1.7588 0.9712 0.7853 -0.6045 -0.1444 0.0426  606 ILE A CG2 
2424 C CD1 . ILE A 310 ? 1.7812 0.7627 0.7014 -0.4881 -0.1464 0.0265  606 ILE A CD1 
2425 N N   . LEU A 311 ? 1.8799 1.0304 0.8710 -0.5833 -0.1566 0.0292  607 LEU A N   
2426 C CA  . LEU A 311 ? 1.9011 0.9712 0.8297 -0.5717 -0.1606 0.0256  607 LEU A CA  
2427 C C   . LEU A 311 ? 2.0073 1.0328 0.8425 -0.6298 -0.1647 0.0352  607 LEU A C   
2428 O O   . LEU A 311 ? 2.0806 0.9872 0.8107 -0.6258 -0.1678 0.0357  607 LEU A O   
2429 C CB  . LEU A 311 ? 1.6535 0.8003 0.6711 -0.5485 -0.1615 0.0174  607 LEU A CB  
2430 C CG  . LEU A 311 ? 1.5529 0.7022 0.6288 -0.4847 -0.1590 0.0059  607 LEU A CG  
2431 C CD1 . LEU A 311 ? 1.5428 0.7687 0.6966 -0.4716 -0.1610 -0.0013 607 LEU A CD1 
2432 C CD2 . LEU A 311 ? 1.6517 0.6702 0.6386 -0.4419 -0.1587 0.0017  607 LEU A CD2 
2433 N N   . GLU A 312 ? 2.0859 1.2062 0.9535 -0.6832 -0.1645 0.0432  608 GLU A N   
2434 C CA  . GLU A 312 ? 2.3062 1.3961 1.0854 -0.7463 -0.1681 0.0533  608 GLU A CA  
2435 C C   . GLU A 312 ? 2.3577 1.2999 0.9974 -0.7577 -0.1701 0.0579  608 GLU A C   
2436 O O   . GLU A 312 ? 2.3990 1.2376 0.9349 -0.7710 -0.1743 0.0601  608 GLU A O   
2437 C CB  . GLU A 312 ? 2.3904 1.6088 1.2233 -0.7962 -0.1659 0.0618  608 GLU A CB  
2438 C CG  . GLU A 312 ? 2.3050 1.6675 1.2481 -0.7981 -0.1652 0.0603  608 GLU A CG  
2439 C CD  . GLU A 312 ? 2.3859 1.7611 1.2850 -0.8476 -0.1694 0.0664  608 GLU A CD  
2440 O OE1 . GLU A 312 ? 2.4903 1.7528 1.3019 -0.8508 -0.1737 0.0654  608 GLU A OE1 
2441 O OE2 . GLU A 312 ? 2.3481 1.8462 1.2964 -0.8824 -0.1682 0.0727  608 GLU A OE2 
2442 N N   . GLU A 313 ? 2.3205 1.2490 0.9516 -0.7521 -0.1672 0.0594  609 GLU A N   
2443 C CA  . GLU A 313 ? 2.5228 1.3189 1.0169 -0.7691 -0.1696 0.0643  609 GLU A CA  
2444 C C   . GLU A 313 ? 2.5196 1.1806 0.9415 -0.7092 -0.1707 0.0575  609 GLU A C   
2445 O O   . GLU A 313 ? 2.6639 1.1952 0.9504 -0.7207 -0.1747 0.0611  609 GLU A O   
2446 C CB  . GLU A 313 ? 2.6403 1.4702 1.1484 -0.7836 -0.1665 0.0677  609 GLU A CB  
2447 C CG  . GLU A 313 ? 2.7906 1.6841 1.2782 -0.8600 -0.1674 0.0783  609 GLU A CG  
2448 C CD  . GLU A 313 ? 3.0388 1.8082 1.3657 -0.9107 -0.1732 0.0855  609 GLU A CD  
2449 O OE1 . GLU A 313 ? 3.0673 1.7779 1.3349 -0.9209 -0.1771 0.0866  609 GLU A OE1 
2450 O OE2 . GLU A 313 ? 3.1420 1.8692 1.3973 -0.9415 -0.1741 0.0898  609 GLU A OE2 
2451 N N   . VAL A 314 ? 2.3570 1.0454 0.8608 -0.6442 -0.1672 0.0479  610 VAL A N   
2452 C CA  . VAL A 314 ? 2.3908 0.9605 0.8249 -0.5830 -0.1676 0.0418  610 VAL A CA  
2453 C C   . VAL A 314 ? 2.4746 0.9778 0.8468 -0.5781 -0.1714 0.0409  610 VAL A C   
2454 O O   . VAL A 314 ? 2.5153 0.8886 0.7718 -0.5511 -0.1736 0.0408  610 VAL A O   
2455 C CB  . VAL A 314 ? 2.2731 0.8961 0.8096 -0.5169 -0.1627 0.0321  610 VAL A CB  
2456 C CG1 . VAL A 314 ? 2.2701 0.7823 0.7345 -0.4494 -0.1623 0.0262  610 VAL A CG1 
2457 C CG2 . VAL A 314 ? 2.2777 0.9572 0.8654 -0.5247 -0.1590 0.0341  610 VAL A CG2 
2458 N N   . ALA A 315 ? 2.4115 1.0003 0.8535 -0.6029 -0.1726 0.0404  611 ALA A N   
2459 C CA  . ALA A 315 ? 2.5236 1.0493 0.9013 -0.6074 -0.1767 0.0406  611 ALA A CA  
2460 C C   . ALA A 315 ? 2.6838 1.1097 0.9200 -0.6640 -0.1813 0.0514  611 ALA A C   
2461 O O   . ALA A 315 ? 2.8507 1.1570 0.9767 -0.6523 -0.1847 0.0524  611 ALA A O   
2462 C CB  . ALA A 315 ? 2.2392 0.8839 0.7215 -0.6262 -0.1773 0.0377  611 ALA A CB  
2463 N N   . LYS A 316 ? 2.6675 1.1414 0.9011 -0.7261 -0.1816 0.0597  612 LYS A N   
2464 C CA  . LYS A 316 ? 2.8319 1.2185 0.9291 -0.7887 -0.1861 0.0703  612 LYS A CA  
2465 C C   . LYS A 316 ? 3.0242 1.2433 0.9816 -0.7568 -0.1880 0.0693  612 LYS A C   
2466 O O   . LYS A 316 ? 3.0450 1.1583 0.9099 -0.7514 -0.1914 0.0680  612 LYS A O   
2467 C CB  . LYS A 316 ? 2.7928 1.2619 0.9131 -0.8507 -0.1850 0.0780  612 LYS A CB  
2468 C CG  . LYS A 316 ? 2.7350 1.3335 0.9242 -0.9091 -0.1854 0.0836  612 LYS A CG  
2469 C CD  . LYS A 316 ? 2.8486 1.4661 0.9779 -0.9863 -0.1867 0.0947  612 LYS A CD  
2470 C CE  . LYS A 316 ? 3.0477 1.5069 1.0185 -1.0141 -0.1918 0.0963  612 LYS A CE  
2471 N NZ  . LYS A 316 ? 3.1039 1.5840 1.0261 -1.0909 -0.1936 0.1031  612 LYS A NZ  
2472 N N   . LYS A 317 ? 2.8330 1.0384 0.7957 -0.7278 -0.1851 0.0660  613 LYS A N   
2473 C CA  . LYS A 317 ? 3.0612 1.1290 0.9157 -0.6951 -0.1856 0.0613  613 LYS A CA  
2474 C C   . LYS A 317 ? 3.0627 1.0463 0.8832 -0.6157 -0.1849 0.0536  613 LYS A C   
2475 O O   . LYS A 317 ? 3.1438 1.0153 0.8744 -0.5783 -0.1847 0.0494  613 LYS A O   
2476 C CB  . LYS A 317 ? 2.9240 1.0172 0.8078 -0.6838 -0.1822 0.0599  613 LYS A CB  
2477 C CG  . LYS A 317 ? 3.0247 1.1501 0.8894 -0.7602 -0.1835 0.0666  613 LYS A CG  
2478 C CD  . LYS A 317 ? 2.8547 1.1072 0.8315 -0.7654 -0.1794 0.0683  613 LYS A CD  
2479 C CE  . LYS A 317 ? 2.8660 1.1904 0.8486 -0.8466 -0.1804 0.0762  613 LYS A CE  
2480 N NZ  . LYS A 317 ? 2.6955 1.1484 0.7895 -0.8471 -0.1760 0.0779  613 LYS A NZ  
2481 N N   . MET A 318 ? 3.1528 1.1897 1.0410 -0.5872 -0.1843 0.0517  614 MET A N   
2482 C CA  . MET A 318 ? 3.2666 1.2230 1.1095 -0.5230 -0.1844 0.0456  614 MET A CA  
2483 C C   . MET A 318 ? 3.4519 1.3503 1.2237 -0.5562 -0.1891 0.0487  614 MET A C   
2484 O O   . MET A 318 ? 3.6176 1.4318 1.3296 -0.5077 -0.1897 0.0442  614 MET A O   
2485 C CB  . MET A 318 ? 3.0940 1.1383 1.0520 -0.4655 -0.1808 0.0397  614 MET A CB  
2486 C CG  . MET A 318 ? 3.0004 1.1050 1.0397 -0.4255 -0.1756 0.0341  614 MET A CG  
2487 S SD  . MET A 318 ? 2.7678 1.0023 0.9768 -0.3674 -0.1700 0.0220  614 MET A SD  
2488 C CE  . MET A 318 ? 2.8509 0.9870 0.9803 -0.2928 -0.1701 0.0170  614 MET A CE  
2489 N N   . ASP A 319 ? 3.4721 1.4165 1.2475 -0.6370 -0.1923 0.0564  615 ASP A N   
2490 C CA  . ASP A 319 ? 3.5524 1.4635 1.2752 -0.6778 -0.1969 0.0603  615 ASP A CA  
2491 C C   . ASP A 319 ? 3.3998 1.3475 1.1828 -0.6346 -0.1964 0.0566  615 ASP A C   
2492 O O   . ASP A 319 ? 3.5059 1.3644 1.2318 -0.5796 -0.1968 0.0512  615 ASP A O   
2493 C CB  . ASP A 319 ? 3.7717 1.5217 1.3392 -0.6805 -0.2006 0.0598  615 ASP A CB  
2494 C CG  . ASP A 319 ? 3.8950 1.6229 1.3926 -0.7698 -0.2058 0.0679  615 ASP A CG  
2495 O OD1 . ASP A 319 ? 3.8593 1.6633 1.3902 -0.8315 -0.2058 0.0737  615 ASP A OD1 
2496 O OD2 . ASP A 319 ? 4.0198 1.6538 1.4254 -0.7780 -0.2100 0.0685  615 ASP A OD2 
2497 N N   . LEU A 320 ? 3.1731 1.2634 1.0874 -0.6547 -0.1950 0.0558  616 LEU A N   
2498 C CA  . LEU A 320 ? 2.9658 1.1199 0.9761 -0.6111 -0.1936 0.0457  616 LEU A CA  
2499 C C   . LEU A 320 ? 2.9574 1.1917 1.0151 -0.6684 -0.1968 0.0478  616 LEU A C   
2500 O O   . LEU A 320 ? 2.9773 1.2711 1.0453 -0.7365 -0.1981 0.0558  616 LEU A O   
2501 C CB  . LEU A 320 ? 2.6708 0.9388 0.8253 -0.5626 -0.1878 0.0357  616 LEU A CB  
2502 C CG  . LEU A 320 ? 2.7167 0.9221 0.8420 -0.4954 -0.1840 0.0316  616 LEU A CG  
2503 C CD1 . LEU A 320 ? 2.5923 0.9159 0.8635 -0.4529 -0.1786 0.0218  616 LEU A CD1 
2504 C CD2 . LEU A 320 ? 2.8292 0.9092 0.8507 -0.4390 -0.1850 0.0295  616 LEU A CD2 
2505 N N   . ASP A 321 ? 2.9178 1.1579 1.0038 -0.6387 -0.1980 0.0404  617 ASP A N   
2506 C CA  . ASP A 321 ? 2.9080 1.2290 1.0452 -0.6847 -0.2013 0.0406  617 ASP A CA  
2507 C C   . ASP A 321 ? 2.6377 1.1309 0.9275 -0.7004 -0.1987 0.0373  617 ASP A C   
2508 O O   . ASP A 321 ? 2.4635 1.0364 0.8601 -0.6567 -0.1967 0.0265  617 ASP A O   
2509 C CB  . ASP A 321 ? 2.9901 1.2823 1.1301 -0.6413 -0.2029 0.0314  617 ASP A CB  
2510 C CG  . ASP A 321 ? 3.0533 1.4131 1.2275 -0.6900 -0.2075 0.0316  617 ASP A CG  
2511 O OD1 . ASP A 321 ? 3.0386 1.3851 1.2208 -0.6598 -0.2093 0.0235  617 ASP A OD1 
2512 O OD2 . ASP A 321 ? 3.0855 1.5140 1.2760 -0.7577 -0.2094 0.0398  617 ASP A OD2 
2513 N N   . MET A 322 ? 2.6478 1.1993 0.9445 -0.7613 -0.1988 0.0469  618 MET A N   
2514 C CA  . MET A 322 ? 2.6568 1.3745 1.0911 -0.7764 -0.1963 0.0454  618 MET A CA  
2515 C C   . MET A 322 ? 2.7814 1.5963 1.2621 -0.8218 -0.1998 0.0475  618 MET A C   
2516 O O   . MET A 322 ? 2.6815 1.6408 1.2774 -0.8283 -0.1982 0.0461  618 MET A O   
2517 C CB  . MET A 322 ? 2.6275 1.3754 1.0565 -0.8116 -0.1934 0.0543  618 MET A CB  
2518 C CG  . MET A 322 ? 2.5969 1.3046 1.0339 -0.7591 -0.1890 0.0497  618 MET A CG  
2519 S SD  . MET A 322 ? 2.6092 1.3604 1.0499 -0.7964 -0.1856 0.0584  618 MET A SD  
2520 C CE  . MET A 322 ? 2.4620 1.4159 1.0473 -0.8308 -0.1837 0.0602  618 MET A CE  
2521 N N   . ARG A 323 ? 2.9818 1.7207 1.3727 -0.8510 -0.2047 0.0509  619 ARG A N   
2522 C CA  . ARG A 323 ? 2.9728 1.8015 1.4060 -0.8897 -0.2086 0.0518  619 ARG A CA  
2523 C C   . ARG A 323 ? 2.8233 1.7485 1.3801 -0.8395 -0.2086 0.0387  619 ARG A C   
2524 O O   . ARG A 323 ? 2.7842 1.8492 1.4358 -0.8577 -0.2093 0.0387  619 ARG A O   
2525 C CB  . ARG A 323 ? 3.1643 1.8754 1.4732 -0.9203 -0.2141 0.0560  619 ARG A CB  
2526 C CG  . ARG A 323 ? 3.3637 1.9631 1.5301 -0.9741 -0.2153 0.0695  619 ARG A CG  
2527 C CD  . ARG A 323 ? 3.5383 1.9600 1.5649 -0.9595 -0.2190 0.0697  619 ARG A CD  
2528 N NE  . ARG A 323 ? 3.6105 1.9162 1.5765 -0.9035 -0.2162 0.0674  619 ARG A NE  
2529 C CZ  . ARG A 323 ? 3.7556 1.8962 1.5874 -0.8807 -0.2184 0.0691  619 ARG A CZ  
2530 N NH1 . ARG A 323 ? 3.8552 1.9205 1.5976 -0.9115 -0.2237 0.0729  619 ARG A NH1 
2531 N NH2 . ARG A 323 ? 3.7815 1.8329 1.5655 -0.8255 -0.2155 0.0671  619 ARG A NH2 
2532 N N   . LYS A 324 ? 2.7114 1.5653 1.2642 -0.7749 -0.2078 0.0280  620 LYS A N   
2533 C CA  . LYS A 324 ? 2.4881 1.4077 1.1318 -0.7293 -0.2087 0.0152  620 LYS A CA  
2534 C C   . LYS A 324 ? 2.3452 1.3171 1.0794 -0.6743 -0.2034 0.0074  620 LYS A C   
2535 O O   . LYS A 324 ? 2.4120 1.3355 1.1216 -0.6574 -0.1991 0.0096  620 LYS A O   
2536 C CB  . LYS A 324 ? 2.5498 1.3559 1.1198 -0.6973 -0.2114 0.0083  620 LYS A CB  
2537 C CG  . LYS A 324 ? 2.6178 1.4139 1.1404 -0.7437 -0.2180 0.0114  620 LYS A CG  
2538 C CD  . LYS A 324 ? 2.7239 1.4540 1.1381 -0.8121 -0.2200 0.0261  620 LYS A CD  
2539 C CE  . LYS A 324 ? 2.7115 1.4672 1.0996 -0.8685 -0.2264 0.0301  620 LYS A CE  
2540 N NZ  . LYS A 324 ? 2.7614 1.4847 1.0603 -0.9444 -0.2276 0.0456  620 LYS A NZ  
2541 N N   . THR A 325 ? 2.1176 1.1897 0.9540 -0.6479 -0.2044 -0.0016 621 THR A N   
2542 C CA  . THR A 325 ? 1.9882 1.1115 0.9104 -0.5965 -0.2000 -0.0096 621 THR A CA  
2543 C C   . THR A 325 ? 2.0476 1.0742 0.9338 -0.5342 -0.1974 -0.0199 621 THR A C   
2544 O O   . THR A 325 ? 1.7603 0.7662 0.6604 -0.4953 -0.1921 -0.0230 621 THR A O   
2545 C CB  . THR A 325 ? 1.8275 1.0942 0.8640 -0.5941 -0.2025 -0.0137 621 THR A CB  
2546 O OG1 . THR A 325 ? 1.6762 0.9783 0.7852 -0.5420 -0.1992 -0.0224 621 THR A OG1 
2547 C CG2 . THR A 325 ? 1.9647 1.2361 0.9901 -0.5998 -0.2090 -0.0183 621 THR A CG2 
2548 N N   . SER A 326 ? 2.1284 1.0956 0.9639 -0.5236 -0.2006 -0.0247 622 SER A N   
2549 C CA  . SER A 326 ? 2.0230 0.9167 0.8303 -0.4613 -0.1977 -0.0350 622 SER A CA  
2550 C C   . SER A 326 ? 2.0913 0.8499 0.7923 -0.4365 -0.1939 -0.0313 622 SER A C   
2551 O O   . SER A 326 ? 2.0221 0.7188 0.6922 -0.3789 -0.1903 -0.0385 622 SER A O   
2552 C CB  . SER A 326 ? 1.9236 0.8078 0.7121 -0.4620 -0.2025 -0.0405 622 SER A CB  
2553 O OG  . SER A 326 ? 1.9773 0.8961 0.7541 -0.5265 -0.2089 -0.0324 622 SER A OG  
2554 N N   . SER A 327 ? 2.2140 0.9277 0.8543 -0.4765 -0.1946 -0.0198 623 SER A N   
2555 C CA  . SER A 327 ? 2.3695 0.9572 0.9057 -0.4521 -0.1917 -0.0150 623 SER A CA  
2556 C C   . SER A 327 ? 2.1835 0.7863 0.7627 -0.4028 -0.1853 -0.0189 623 SER A C   
2557 O O   . SER A 327 ? 2.2185 0.7229 0.7162 -0.3700 -0.1827 -0.0161 623 SER A O   
2558 C CB  . SER A 327 ? 2.5335 1.0707 0.9869 -0.5157 -0.1949 -0.0010 623 SER A CB  
2559 O OG  . SER A 327 ? 2.4243 1.0668 0.9550 -0.5551 -0.1940 0.0036  623 SER A OG  
2560 N N   . LEU A 328 ? 2.1124 0.8346 0.8122 -0.3973 -0.1831 -0.0246 624 LEU A N   
2561 C CA  . LEU A 328 ? 2.0173 0.7655 0.7681 -0.3544 -0.1771 -0.0288 624 LEU A CA  
2562 C C   . LEU A 328 ? 2.1178 0.8119 0.8113 -0.3695 -0.1756 -0.0193 624 LEU A C   
2563 O O   . LEU A 328 ? 2.1074 0.7687 0.7909 -0.3246 -0.1710 -0.0213 624 LEU A O   
2564 C CB  . LEU A 328 ? 1.9656 0.6716 0.7053 -0.2794 -0.1721 -0.0387 624 LEU A CB  
2565 C CG  . LEU A 328 ? 1.9361 0.6929 0.7282 -0.2591 -0.1726 -0.0491 624 LEU A CG  
2566 C CD1 . LEU A 328 ? 1.8460 0.6000 0.6576 -0.1847 -0.1652 -0.0590 624 LEU A CD1 
2567 C CD2 . LEU A 328 ? 1.8479 0.7298 0.7467 -0.2980 -0.1761 -0.0508 624 LEU A CD2 
2568 N N   . TRP A 329 ? 2.1497 0.8371 0.8028 -0.4335 -0.1795 -0.0086 625 TRP A N   
2569 C CA  . TRP A 329 ? 2.2468 0.8852 0.8416 -0.4533 -0.1784 0.0006  625 TRP A CA  
2570 C C   . TRP A 329 ? 2.1688 0.8943 0.8588 -0.4416 -0.1740 -0.0017 625 TRP A C   
2571 O O   . TRP A 329 ? 2.1723 0.8494 0.8253 -0.4241 -0.1712 0.0009  625 TRP A O   
2572 C CB  . TRP A 329 ? 2.3197 0.9506 0.8597 -0.5296 -0.1829 0.0124  625 TRP A CB  
2573 C CG  . TRP A 329 ? 2.2501 1.0207 0.8919 -0.5754 -0.1842 0.0138  625 TRP A CG  
2574 C CD1 . TRP A 329 ? 2.2437 1.0724 0.9235 -0.5947 -0.1878 0.0114  625 TRP A CD1 
2575 C CD2 . TRP A 329 ? 2.2498 1.1227 0.9653 -0.6043 -0.1818 0.0184  625 TRP A CD2 
2576 N NE1 . TRP A 329 ? 2.1754 1.1389 0.9474 -0.6314 -0.1879 0.0146  625 TRP A NE1 
2577 C CE2 . TRP A 329 ? 2.1967 1.1900 0.9921 -0.6373 -0.1839 0.0191  625 TRP A CE2 
2578 C CE3 . TRP A 329 ? 2.1437 1.0195 0.8639 -0.6031 -0.1780 0.0221  625 TRP A CE3 
2579 C CZ2 . TRP A 329 ? 2.0930 1.2105 0.9711 -0.6656 -0.1819 0.0238  625 TRP A CZ2 
2580 C CZ3 . TRP A 329 ? 2.0742 1.0699 0.8766 -0.6350 -0.1761 0.0264  625 TRP A CZ3 
2581 C CH2 . TRP A 329 ? 2.0230 1.1388 0.9027 -0.6642 -0.1777 0.0275  625 TRP A CH2 
2582 N N   . LYS A 330 ? 2.0527 0.9045 0.8618 -0.4492 -0.1736 -0.0064 626 LYS A N   
2583 C CA  . LYS A 330 ? 1.9724 0.9084 0.8743 -0.4360 -0.1696 -0.0087 626 LYS A CA  
2584 C C   . LYS A 330 ? 1.9064 0.8059 0.8172 -0.3673 -0.1649 -0.0176 626 LYS A C   
2585 O O   . LYS A 330 ? 1.9827 0.8786 0.9020 -0.3521 -0.1614 -0.0163 626 LYS A O   
2586 C CB  . LYS A 330 ? 1.9147 0.9878 0.9328 -0.4531 -0.1709 -0.0116 626 LYS A CB  
2587 C CG  . LYS A 330 ? 1.8376 0.9856 0.8741 -0.5164 -0.1730 -0.0012 626 LYS A CG  
2588 C CD  . LYS A 330 ? 1.5765 0.8674 0.7301 -0.5223 -0.1736 -0.0033 626 LYS A CD  
2589 C CE  . LYS A 330 ? 1.5279 0.8963 0.6915 -0.5810 -0.1747 0.0079  626 LYS A CE  
2590 N NZ  . LYS A 330 ? 1.4566 0.9638 0.7189 -0.5872 -0.1760 0.0078  626 LYS A NZ  
2591 N N   . ASP A 331 ? 1.8629 0.7402 0.7722 -0.3245 -0.1645 -0.0265 627 ASP A N   
2592 C CA  . ASP A 331 ? 1.8183 0.6692 0.7336 -0.2562 -0.1590 -0.0347 627 ASP A CA  
2593 C C   . ASP A 331 ? 1.9134 0.6571 0.7280 -0.2310 -0.1570 -0.0296 627 ASP A C   
2594 O O   . ASP A 331 ? 1.9309 0.6767 0.7612 -0.1983 -0.1528 -0.0309 627 ASP A O   
2595 C CB  . ASP A 331 ? 1.8599 0.7026 0.7767 -0.2171 -0.1584 -0.0441 627 ASP A CB  
2596 C CG  . ASP A 331 ? 1.7640 0.7089 0.7739 -0.2387 -0.1612 -0.0495 627 ASP A CG  
2597 O OD1 . ASP A 331 ? 1.5767 0.5457 0.5851 -0.2897 -0.1668 -0.0444 627 ASP A OD1 
2598 O OD2 . ASP A 331 ? 1.5678 0.5712 0.6498 -0.2055 -0.1581 -0.0583 627 ASP A OD2 
2599 N N   . GLN A 332 ? 1.9303 0.5779 0.6362 -0.2456 -0.1605 -0.0234 628 GLN A N   
2600 C CA  . GLN A 332 ? 2.2201 0.7530 0.8105 -0.2230 -0.1601 -0.0175 628 GLN A CA  
2601 C C   . GLN A 332 ? 2.1977 0.7356 0.7876 -0.2460 -0.1593 -0.0113 628 GLN A C   
2602 O O   . GLN A 332 ? 2.1716 0.6687 0.7300 -0.2023 -0.1561 -0.0118 628 GLN A O   
2603 C CB  . GLN A 332 ? 2.5042 0.9398 0.9790 -0.2548 -0.1656 -0.0100 628 GLN A CB  
2604 C CG  . GLN A 332 ? 2.7094 1.0098 1.0472 -0.2164 -0.1659 -0.0055 628 GLN A CG  
2605 C CD  . GLN A 332 ? 2.7328 0.9958 1.0430 -0.1496 -0.1637 -0.0117 628 GLN A CD  
2606 O OE1 . GLN A 332 ? 2.4587 0.6477 0.6874 -0.1548 -0.1673 -0.0088 628 GLN A OE1 
2607 N NE2 . GLN A 332 ? 2.5422 0.8597 0.9193 -0.0861 -0.1574 -0.0200 628 GLN A NE2 
2608 N N   . ALA A 333 ? 2.1847 0.7764 0.8069 -0.3134 -0.1620 -0.0051 629 ALA A N   
2609 C CA  . ALA A 333 ? 2.1926 0.7954 0.8149 -0.3406 -0.1610 0.0013  629 ALA A CA  
2610 C C   . ALA A 333 ? 2.2031 0.8865 0.9289 -0.3062 -0.1560 -0.0050 629 ALA A C   
2611 O O   . ALA A 333 ? 2.2114 0.8804 0.9242 -0.3025 -0.1540 -0.0018 629 ALA A O   
2612 C CB  . ALA A 333 ? 2.1257 0.7852 0.7656 -0.4188 -0.1643 0.0096  629 ALA A CB  
2613 N N   . LEU A 334 ? 2.0991 0.8629 0.9220 -0.2814 -0.1541 -0.0139 630 LEU A N   
2614 C CA  . LEU A 334 ? 1.9410 0.7771 0.8570 -0.2501 -0.1496 -0.0199 630 LEU A CA  
2615 C C   . LEU A 334 ? 1.9758 0.7500 0.8505 -0.1816 -0.1454 -0.0240 630 LEU A C   
2616 O O   . LEU A 334 ? 2.1030 0.8874 0.9959 -0.1657 -0.1425 -0.0232 630 LEU A O   
2617 C CB  . LEU A 334 ? 1.8774 0.8098 0.8970 -0.2447 -0.1495 -0.0282 630 LEU A CB  
2618 C CG  . LEU A 334 ? 1.8457 0.8639 0.9671 -0.2265 -0.1461 -0.0332 630 LEU A CG  
2619 C CD1 . LEU A 334 ? 1.8223 0.9319 1.0121 -0.2809 -0.1479 -0.0272 630 LEU A CD1 
2620 C CD2 . LEU A 334 ? 1.7844 0.8449 0.9644 -0.1876 -0.1446 -0.0444 630 LEU A CD2 
2621 N N   . VAL A 335 ? 1.9034 0.6176 0.7207 -0.1382 -0.1448 -0.0279 631 VAL A N   
2622 C CA  . VAL A 335 ? 1.9692 0.6410 0.7498 -0.0655 -0.1402 -0.0315 631 VAL A CA  
2623 C C   . VAL A 335 ? 2.0739 0.6659 0.7650 -0.0616 -0.1409 -0.0240 631 VAL A C   
2624 O O   . VAL A 335 ? 2.0769 0.6732 0.7748 -0.0148 -0.1369 -0.0259 631 VAL A O   
2625 C CB  . VAL A 335 ? 2.1249 0.7508 0.8529 -0.0218 -0.1394 -0.0354 631 VAL A CB  
2626 C CG1 . VAL A 335 ? 2.2495 0.8374 0.9289 0.0549  -0.1346 -0.0370 631 VAL A CG1 
2627 C CG2 . VAL A 335 ? 2.0172 0.7269 0.8375 -0.0160 -0.1375 -0.0446 631 VAL A CG2 
2628 N N   . GLU A 336 ? 2.0651 0.5856 0.6694 -0.1110 -0.1459 -0.0155 632 GLU A N   
2629 C CA  . GLU A 336 ? 2.3186 0.7552 0.8263 -0.1132 -0.1472 -0.0088 632 GLU A CA  
2630 C C   . GLU A 336 ? 2.2182 0.7146 0.7915 -0.1354 -0.1452 -0.0070 632 GLU A C   
2631 O O   . GLU A 336 ? 2.2285 0.6970 0.7746 -0.0998 -0.1429 -0.0071 632 GLU A O   
2632 C CB  . GLU A 336 ? 2.4894 0.8403 0.8893 -0.1700 -0.1531 -0.0001 632 GLU A CB  
2633 C CG  . GLU A 336 ? 2.6307 0.9203 0.9632 -0.1617 -0.1560 -0.0001 632 GLU A CG  
2634 C CD  . GLU A 336 ? 2.7899 0.9800 1.0167 -0.0926 -0.1552 -0.0011 632 GLU A CD  
2635 O OE1 . GLU A 336 ? 2.8316 0.9841 1.0146 -0.0606 -0.1535 -0.0006 632 GLU A OE1 
2636 O OE2 . GLU A 336 ? 2.8237 0.9757 1.0097 -0.0689 -0.1562 -0.0024 632 GLU A OE2 
2637 N N   . ILE A 337 ? 2.1071 0.6863 0.7617 -0.1946 -0.1463 -0.0049 633 ILE A N   
2638 C CA  . ILE A 337 ? 2.0131 0.6635 0.7412 -0.2196 -0.1443 -0.0027 633 ILE A CA  
2639 C C   . ILE A 337 ? 2.0459 0.7352 0.8371 -0.1594 -0.1394 -0.0094 633 ILE A C   
2640 O O   . ILE A 337 ? 1.9752 0.6609 0.7649 -0.1524 -0.1376 -0.0069 633 ILE A O   
2641 C CB  . ILE A 337 ? 1.8333 0.5901 0.6569 -0.2766 -0.1455 -0.0013 633 ILE A CB  
2642 C CG1 . ILE A 337 ? 1.9117 0.6370 0.6672 -0.3417 -0.1500 0.0076  633 ILE A CG1 
2643 C CG2 . ILE A 337 ? 1.8276 0.6730 0.7424 -0.2904 -0.1425 -0.0002 633 ILE A CG2 
2644 C CD1 . ILE A 337 ? 1.8339 0.6715 0.6764 -0.3949 -0.1510 0.0101  633 ILE A CD1 
2645 N N   . ASN A 338 ? 2.0152 0.7403 0.8569 -0.1142 -0.1371 -0.0178 634 ASN A N   
2646 C CA  . ASN A 338 ? 1.8301 0.6045 0.7370 -0.0593 -0.1322 -0.0241 634 ASN A CA  
2647 C C   . ASN A 338 ? 1.9039 0.6104 0.7331 0.0063  -0.1297 -0.0244 634 ASN A C   
2648 O O   . ASN A 338 ? 1.7806 0.5165 0.6422 0.0410  -0.1265 -0.0256 634 ASN A O   
2649 C CB  . ASN A 338 ? 1.6767 0.5245 0.6684 -0.0397 -0.1303 -0.0332 634 ASN A CB  
2650 C CG  . ASN A 338 ? 1.6743 0.6175 0.7701 -0.0886 -0.1318 -0.0343 634 ASN A CG  
2651 O OD1 . ASN A 338 ? 1.6717 0.6750 0.8401 -0.0767 -0.1296 -0.0373 634 ASN A OD1 
2652 N ND2 . ASN A 338 ? 1.5846 0.5435 0.6833 -0.1435 -0.1359 -0.0310 634 ASN A ND2 
2653 N N   . ILE A 339 ? 2.1070 0.7263 0.8316 0.0259  -0.1315 -0.0230 635 ILE A N   
2654 C CA  . ILE A 339 ? 2.1141 0.6652 0.7503 0.0839  -0.1300 -0.0222 635 ILE A CA  
2655 C C   . ILE A 339 ? 2.0773 0.5889 0.6716 0.0596  -0.1315 -0.0164 635 ILE A C   
2656 O O   . ILE A 339 ? 2.1635 0.6711 0.7441 0.1059  -0.1288 -0.0174 635 ILE A O   
2657 C CB  . ILE A 339 ? 2.2261 0.6805 0.7444 0.1030  -0.1326 -0.0208 635 ILE A CB  
2658 C CG1 . ILE A 339 ? 2.0363 0.5366 0.5984 0.1406  -0.1298 -0.0270 635 ILE A CG1 
2659 C CG2 . ILE A 339 ? 2.2029 0.5752 0.6106 0.1565  -0.1320 -0.0193 635 ILE A CG2 
2660 C CD1 . ILE A 339 ? 2.1556 0.5680 0.6082 0.1660  -0.1319 -0.0254 635 ILE A CD1 
2661 N N   . ALA A 340 ? 2.0451 0.5404 0.6268 -0.0146 -0.1354 -0.0103 636 ALA A N   
2662 C CA  . ALA A 340 ? 2.1874 0.6394 0.7178 -0.0455 -0.1369 -0.0044 636 ALA A CA  
2663 C C   . ALA A 340 ? 2.1084 0.6445 0.7386 -0.0447 -0.1335 -0.0047 636 ALA A C   
2664 O O   . ALA A 340 ? 2.1731 0.6807 0.7699 -0.0213 -0.1322 -0.0036 636 ALA A O   
2665 C CB  . ALA A 340 ? 2.1981 0.6220 0.6876 -0.1265 -0.1416 0.0026  636 ALA A CB  
2666 N N   . VAL A 341 ? 2.0507 0.6879 0.7992 -0.0709 -0.1323 -0.0063 637 VAL A N   
2667 C CA  . VAL A 341 ? 1.9258 0.6430 0.7698 -0.0671 -0.1293 -0.0068 637 VAL A CA  
2668 C C   . VAL A 341 ? 1.9635 0.6812 0.8098 0.0110  -0.1258 -0.0113 637 VAL A C   
2669 O O   . VAL A 341 ? 2.0272 0.7352 0.8612 0.0262  -0.1247 -0.0085 637 VAL A O   
2670 C CB  . VAL A 341 ? 1.7976 0.6188 0.7600 -0.0954 -0.1288 -0.0104 637 VAL A CB  
2671 C CG1 . VAL A 341 ? 1.6236 0.5202 0.6793 -0.0705 -0.1258 -0.0137 637 VAL A CG1 
2672 C CG2 . VAL A 341 ? 1.7883 0.6376 0.7629 -0.1739 -0.1315 -0.0038 637 VAL A CG2 
2673 N N   . LEU A 342 ? 1.8814 0.6133 0.7379 0.0627  -0.1239 -0.0179 638 LEU A N   
2674 C CA  . LEU A 342 ? 1.8312 0.5810 0.6895 0.1401  -0.1200 -0.0216 638 LEU A CA  
2675 C C   . LEU A 342 ? 1.9470 0.6126 0.6970 0.1661  -0.1206 -0.0183 638 LEU A C   
2676 O O   . LEU A 342 ? 1.8053 0.4894 0.5684 0.1890  -0.1191 -0.0168 638 LEU A O   
2677 C CB  . LEU A 342 ? 1.8226 0.5933 0.6862 0.1879  -0.1175 -0.0281 638 LEU A CB  
2678 C CG  . LEU A 342 ? 1.6933 0.5535 0.6667 0.1734  -0.1160 -0.0337 638 LEU A CG  
2679 C CD1 . LEU A 342 ? 1.7123 0.6091 0.6984 0.2312  -0.1118 -0.0400 638 LEU A CD1 
2680 C CD2 . LEU A 342 ? 1.4914 0.4310 0.5614 0.1668  -0.1148 -0.0341 638 LEU A CD2 
2681 N N   . TYR A 343 ? 2.1305 0.6989 0.7677 0.1609  -0.1233 -0.0172 639 TYR A N   
2682 C CA  . TYR A 343 ? 2.3635 0.8384 0.8799 0.1907  -0.1241 -0.0162 639 TYR A CA  
2683 C C   . TYR A 343 ? 2.3012 0.7615 0.8109 0.1618  -0.1248 -0.0120 639 TYR A C   
2684 O O   . TYR A 343 ? 2.3624 0.8212 0.8540 0.2084  -0.1224 -0.0136 639 TYR A O   
2685 C CB  . TYR A 343 ? 2.5214 0.8846 0.9137 0.1689  -0.1283 -0.0144 639 TYR A CB  
2686 C CG  . TYR A 343 ? 2.6478 0.8992 0.9007 0.1929  -0.1297 -0.0143 639 TYR A CG  
2687 C CD1 . TYR A 343 ? 2.7113 0.9415 0.9088 0.2731  -0.1265 -0.0191 639 TYR A CD1 
2688 C CD2 . TYR A 343 ? 2.7677 0.9409 0.9454 0.1355  -0.1335 -0.0098 639 TYR A CD2 
2689 C CE1 . TYR A 343 ? 2.8693 1.0107 0.9683 0.2954  -0.1253 -0.0195 639 TYR A CE1 
2690 C CE2 . TYR A 343 ? 2.9257 1.0030 0.9961 0.1560  -0.1329 -0.0108 639 TYR A CE2 
2691 C CZ  . TYR A 343 ? 2.9946 1.0544 1.0280 0.2369  -0.1287 -0.0157 639 TYR A CZ  
2692 O OH  . TYR A 343 ? 3.2030 1.1667 1.1314 0.2588  -0.1278 -0.0166 639 TYR A OH  
2693 N N   . SER A 344 ? 2.2559 0.7151 0.7844 0.0850  -0.1276 -0.0065 640 SER A N   
2694 C CA  . SER A 344 ? 2.1910 0.6412 0.7148 0.0502  -0.1280 -0.0015 640 SER A CA  
2695 C C   . SER A 344 ? 2.1358 0.6674 0.7505 0.0872  -0.1243 -0.0020 640 SER A C   
2696 O O   . SER A 344 ? 2.1278 0.6308 0.7036 0.1105  -0.1234 -0.0012 640 SER A O   
2697 C CB  . SER A 344 ? 2.1206 0.5967 0.6803 -0.0370 -0.1304 0.0046  640 SER A CB  
2698 O OG  . SER A 344 ? 2.2742 0.6911 0.7617 -0.0710 -0.1342 0.0055  640 SER A OG  
2699 N N   . PHE A 345 ? 1.9839 0.6160 0.7169 0.0924  -0.1226 -0.0036 641 PHE A N   
2700 C CA  . PHE A 345 ? 1.9436 0.6571 0.7650 0.1232  -0.1201 -0.0032 641 PHE A CA  
2701 C C   . PHE A 345 ? 2.0879 0.8014 0.8780 0.2053  -0.1178 -0.0071 641 PHE A C   
2702 O O   . PHE A 345 ? 2.0911 0.8361 0.9050 0.2297  -0.1169 -0.0047 641 PHE A O   
2703 C CB  . PHE A 345 ? 1.7808 0.5926 0.7213 0.1167  -0.1192 -0.0064 641 PHE A CB  
2704 C CG  . PHE A 345 ? 1.5660 0.4227 0.5763 0.0471  -0.1203 -0.0025 641 PHE A CG  
2705 C CD1 . PHE A 345 ? 1.6763 0.5065 0.6595 -0.0226 -0.1222 0.0010  641 PHE A CD1 
2706 C CD2 . PHE A 345 ? 1.5033 0.4927 0.6334 0.0499  -0.1160 -0.0030 641 PHE A CD2 
2707 C CE1 . PHE A 345 ? 1.5456 0.4385 0.5983 -0.0842 -0.1224 0.0043  641 PHE A CE1 
2708 C CE2 . PHE A 345 ? 1.3237 0.3901 0.5309 -0.0086 -0.1144 -0.0004 641 PHE A CE2 
2709 C CZ  . PHE A 345 ? 1.4158 0.4383 0.5861 -0.0732 -0.1174 0.0036  641 PHE A CZ  
2710 N N   . GLN A 346 ? 2.1461 0.8316 0.8824 0.2493  -0.1166 -0.0128 642 GLN A N   
2711 C CA  . GLN A 346 ? 2.0641 0.7744 0.7817 0.3286  -0.1133 -0.0172 642 GLN A CA  
2712 C C   . GLN A 346 ? 2.1423 0.7546 0.7378 0.3487  -0.1136 -0.0177 642 GLN A C   
2713 O O   . GLN A 346 ? 2.0678 0.7089 0.6601 0.4008  -0.1110 -0.0198 642 GLN A O   
2714 C CB  . GLN A 346 ? 2.0404 0.7759 0.7549 0.3731  -0.1109 -0.0231 642 GLN A CB  
2715 C CG  . GLN A 346 ? 2.0129 0.8410 0.8398 0.3591  -0.1099 -0.0248 642 GLN A CG  
2716 C CD  . GLN A 346 ? 2.1421 0.9581 0.9396 0.3797  -0.1085 -0.0292 642 GLN A CD  
2717 O OE1 . GLN A 346 ? 2.2033 0.9267 0.9193 0.3513  -0.1115 -0.0281 642 GLN A OE1 
2718 N NE2 . GLN A 346 ? 2.1285 1.0407 0.9883 0.4288  -0.1041 -0.0335 642 GLN A NE2 
2719 N N   . SER A 347 ? 2.2194 0.7176 0.7094 0.3101  -0.1166 -0.0168 643 SER A N   
2720 C CA  . SER A 347 ? 2.3507 0.7459 0.7173 0.3241  -0.1171 -0.0183 643 SER A CA  
2721 C C   . SER A 347 ? 2.3687 0.7651 0.7558 0.2905  -0.1176 -0.0135 643 SER A C   
2722 O O   . SER A 347 ? 2.4884 0.7999 0.7772 0.2980  -0.1178 -0.0152 643 SER A O   
2723 C CB  . SER A 347 ? 2.3907 0.6605 0.6311 0.2884  -0.1211 -0.0183 643 SER A CB  
2724 O OG  . SER A 347 ? 2.4975 0.7553 0.7065 0.3209  -0.1209 -0.0215 643 SER A OG  
2725 N N   . ASP A 348 ? 2.3565 0.8433 0.8634 0.2545  -0.1179 -0.0076 644 ASP A N   
2726 C CA  . ASP A 348 ? 2.3611 0.8680 0.9032 0.2271  -0.1180 -0.0014 644 ASP A CA  
2727 C C   . ASP A 348 ? 2.3567 0.9728 0.9987 0.2755  -0.1159 -0.0002 644 ASP A C   
2728 O O   . ASP A 348 ? 2.2493 0.8963 0.9343 0.2553  -0.1165 0.0066  644 ASP A O   
2729 C CB  . ASP A 348 ? 2.2330 0.7566 0.8246 0.1412  -0.1202 0.0061  644 ASP A CB  
2730 C CG  . ASP A 348 ? 2.3724 0.7941 0.8594 0.0825  -0.1229 0.0074  644 ASP A CG  
2731 O OD1 . ASP A 348 ? 2.5360 0.8599 0.9045 0.1082  -0.1238 0.0019  644 ASP A OD1 
2732 O OD2 . ASP A 348 ? 2.3378 0.7807 0.8581 0.0103  -0.1241 0.0136  644 ASP A OD2 
2733 N N   . LYS A 349 ? 2.4641 1.1453 1.1433 0.3365  -0.1138 -0.0060 645 LYS A N   
2734 C CA  . LYS A 349 ? 2.3978 1.2001 1.1758 0.3814  -0.1126 -0.0056 645 LYS A CA  
2735 C C   . LYS A 349 ? 2.1978 1.0794 1.0903 0.3379  -0.1153 0.0016  645 LYS A C   
2736 O O   . LYS A 349 ? 2.1448 1.1088 1.1065 0.3568  -0.1167 0.0052  645 LYS A O   
2737 C CB  . LYS A 349 ? 2.4920 1.2904 1.2334 0.4228  -0.1113 -0.0058 645 LYS A CB  
2738 C CG  . LYS A 349 ? 2.5127 1.4086 1.2904 0.4980  -0.1081 -0.0119 645 LYS A CG  
2739 C CD  . LYS A 349 ? 2.6690 1.4955 1.3319 0.5520  -0.1042 -0.0192 645 LYS A CD  
2740 C CE  . LYS A 349 ? 2.6674 1.5940 1.3580 0.6233  -0.0995 -0.0261 645 LYS A CE  
2741 N NZ  . LYS A 349 ? 2.6546 1.6156 1.3738 0.6255  -0.0983 -0.0289 645 LYS A NZ  
2742 N N   . VAL A 350 ? 2.1009 0.9623 1.0126 0.2802  -0.1166 0.0033  646 VAL A N   
2743 C CA  . VAL A 350 ? 1.8300 0.7820 0.8552 0.2345  -0.1165 0.0056  646 VAL A CA  
2744 C C   . VAL A 350 ? 1.6684 0.7177 0.7783 0.2518  -0.1138 -0.0031 646 VAL A C   
2745 O O   . VAL A 350 ? 1.7046 0.7004 0.7720 0.2556  -0.1144 -0.0063 646 VAL A O   
2746 C CB  . VAL A 350 ? 1.7576 0.6592 0.7655 0.1525  -0.1172 0.0102  646 VAL A CB  
2747 C CG1 . VAL A 350 ? 1.5516 0.5883 0.6944 0.1057  -0.1134 0.0076  646 VAL A CG1 
2748 C CG2 . VAL A 350 ? 1.7538 0.5640 0.6766 0.1321  -0.1191 0.0197  646 VAL A CG2 
2749 N N   . THR A 351 ? 1.4839 0.6714 0.7078 0.2600  -0.1108 -0.0067 647 THR A N   
2750 C CA  . THR A 351 ? 1.4653 0.7531 0.7692 0.2794  -0.1077 -0.0141 647 THR A CA  
2751 C C   . THR A 351 ? 1.4250 0.7049 0.7518 0.2328  -0.1065 -0.0167 647 THR A C   
2752 O O   . THR A 351 ? 1.4386 0.7198 0.7929 0.1738  -0.1064 -0.0141 647 THR A O   
2753 C CB  . THR A 351 ? 1.3567 0.7833 0.7745 0.2753  -0.1052 -0.0168 647 THR A CB  
2754 O OG1 . THR A 351 ? 1.4598 0.8959 0.8563 0.3122  -0.1073 -0.0140 647 THR A OG1 
2755 C CG2 . THR A 351 ? 1.2342 0.7630 0.7248 0.2969  -0.1019 -0.0237 647 THR A CG2 
2756 N N   . ILE A 352 ? 1.4963 0.7708 0.8087 0.2615  -0.1056 -0.0214 648 ILE A N   
2757 C CA  . ILE A 352 ? 1.3326 0.6089 0.6701 0.2234  -0.1047 -0.0244 648 ILE A CA  
2758 C C   . ILE A 352 ? 1.3752 0.6957 0.7292 0.2693  -0.1017 -0.0303 648 ILE A C   
2759 O O   . ILE A 352 ? 1.3906 0.7075 0.7053 0.3310  -0.1012 -0.0313 648 ILE A O   
2760 C CB  . ILE A 352 ? 1.4265 0.5686 0.6636 0.1880  -0.1091 -0.0212 648 ILE A CB  
2761 C CG1 . ILE A 352 ? 1.4596 0.6278 0.7433 0.1312  -0.1091 -0.0228 648 ILE A CG1 
2762 C CG2 . ILE A 352 ? 1.4300 0.4646 0.5541 0.2374  -0.1111 -0.0230 648 ILE A CG2 
2763 C CD1 . ILE A 352 ? 1.4792 0.5382 0.6790 0.0780  -0.1142 -0.0189 648 ILE A CD1 
2764 N N   . VAL A 353 ? 1.2259 0.5953 0.6388 0.2411  -0.0994 -0.0337 649 VAL A N   
2765 C CA  . VAL A 353 ? 1.3046 0.7233 0.7393 0.2767  -0.0957 -0.0387 649 VAL A CA  
2766 C C   . VAL A 353 ? 1.3646 0.7246 0.7685 0.2496  -0.0970 -0.0408 649 VAL A C   
2767 O O   . VAL A 353 ? 1.3075 0.6546 0.7305 0.1926  -0.0992 -0.0390 649 VAL A O   
2768 C CB  . VAL A 353 ? 1.3081 0.8694 0.8593 0.2722  -0.0909 -0.0409 649 VAL A CB  
2769 C CG1 . VAL A 353 ? 1.2411 0.8432 0.8653 0.2113  -0.0901 -0.0406 649 VAL A CG1 
2770 C CG2 . VAL A 353 ? 1.2035 0.8259 0.7709 0.3158  -0.0863 -0.0450 649 VAL A CG2 
2771 N N   . ASP A 354 ? 1.4498 0.7713 0.7975 0.2926  -0.0959 -0.0444 650 ASP A N   
2772 C CA  . ASP A 354 ? 1.4240 0.6917 0.7383 0.2730  -0.0971 -0.0474 650 ASP A CA  
2773 C C   . ASP A 354 ? 1.3743 0.7550 0.7897 0.2598  -0.0921 -0.0500 650 ASP A C   
2774 O O   . ASP A 354 ? 1.3730 0.8577 0.8580 0.2833  -0.0870 -0.0507 650 ASP A O   
2775 C CB  . ASP A 354 ? 1.5092 0.6815 0.7125 0.3287  -0.0977 -0.0506 650 ASP A CB  
2776 C CG  . ASP A 354 ? 1.6008 0.8568 0.8308 0.3964  -0.0912 -0.0537 650 ASP A CG  
2777 O OD1 . ASP A 354 ? 1.6486 0.8948 0.8279 0.4471  -0.0901 -0.0519 650 ASP A OD1 
2778 O OD2 . ASP A 354 ? 1.5656 0.9152 0.8718 0.3908  -0.0863 -0.0562 650 ASP A OD2 
2779 N N   . HIS A 355 ? 1.3254 0.6858 0.7461 0.2188  -0.0940 -0.0511 651 HIS A N   
2780 C CA  . HIS A 355 ? 1.1588 0.6175 0.6704 0.2024  -0.0896 -0.0526 651 HIS A CA  
2781 C C   . HIS A 355 ? 1.1403 0.6526 0.6636 0.2529  -0.0831 -0.0561 651 HIS A C   
2782 O O   . HIS A 355 ? 1.0605 0.6694 0.6648 0.2442  -0.0780 -0.0563 651 HIS A O   
2783 C CB  . HIS A 355 ? 1.2039 0.6268 0.7083 0.1548  -0.0937 -0.0528 651 HIS A CB  
2784 C CG  . HIS A 355 ? 1.3242 0.6301 0.7212 0.1622  -0.0984 -0.0557 651 HIS A CG  
2785 N ND1 . HIS A 355 ? 1.3623 0.5577 0.6666 0.1520  -0.1045 -0.0542 651 HIS A ND1 
2786 C CD2 . HIS A 355 ? 1.3788 0.6540 0.7393 0.1763  -0.0980 -0.0601 651 HIS A CD2 
2787 C CE1 . HIS A 355 ? 1.5273 0.6229 0.7380 0.1587  -0.1081 -0.0579 651 HIS A CE1 
2788 N NE2 . HIS A 355 ? 1.4780 0.6214 0.7220 0.1754  -0.1042 -0.0619 651 HIS A NE2 
2789 N N   . HIS A 356 ? 1.1978 0.6507 0.6384 0.3062  -0.0827 -0.0587 652 HIS A N   
2790 C CA  . HIS A 356 ? 1.2246 0.7442 0.6775 0.3593  -0.0756 -0.0615 652 HIS A CA  
2791 C C   . HIS A 356 ? 1.1767 0.8013 0.6874 0.3864  -0.0714 -0.0596 652 HIS A C   
2792 O O   . HIS A 356 ? 0.9824 0.7205 0.5715 0.3840  -0.0655 -0.0596 652 HIS A O   
2793 C CB  . HIS A 356 ? 1.3407 0.7621 0.6796 0.4133  -0.0763 -0.0650 652 HIS A CB  
2794 C CG  . HIS A 356 ? 1.4592 0.7713 0.7318 0.3840  -0.0813 -0.0676 652 HIS A CG  
2795 N ND1 . HIS A 356 ? 1.4719 0.8133 0.7761 0.3644  -0.0790 -0.0701 652 HIS A ND1 
2796 C CD2 . HIS A 356 ? 1.5677 0.7432 0.7437 0.3646  -0.0891 -0.0678 652 HIS A CD2 
2797 C CE1 . HIS A 356 ? 1.5524 0.7834 0.7834 0.3368  -0.0856 -0.0723 652 HIS A CE1 
2798 N NE2 . HIS A 356 ? 1.6262 0.7546 0.7773 0.3339  -0.0918 -0.0710 652 HIS A NE2 
2799 N N   . SER A 357 ? 1.2766 0.8628 0.7442 0.4099  -0.0749 -0.0577 653 SER A N   
2800 C CA  . SER A 357 ? 1.2348 0.9189 0.7529 0.4331  -0.0726 -0.0558 653 SER A CA  
2801 C C   . SER A 357 ? 1.0031 0.7852 0.6299 0.3796  -0.0710 -0.0544 653 SER A C   
2802 O O   . SER A 357 ? 0.9280 0.8235 0.6178 0.3888  -0.0665 -0.0545 653 SER A O   
2803 C CB  . SER A 357 ? 1.3187 0.9311 0.7727 0.4540  -0.0779 -0.0532 653 SER A CB  
2804 O OG  . SER A 357 ? 1.3854 1.0898 0.8670 0.4967  -0.0758 -0.0522 653 SER A OG  
2805 N N   . ALA A 358 ? 1.0185 0.7586 0.6635 0.3233  -0.0746 -0.0528 654 ALA A N   
2806 C CA  . ALA A 358 ? 0.9571 0.7754 0.6923 0.2779  -0.0734 -0.0515 654 ALA A CA  
2807 C C   . ALA A 358 ? 0.9330 0.8251 0.7289 0.2611  -0.0680 -0.0529 654 ALA A C   
2808 O O   . ALA A 358 ? 0.7941 0.7735 0.6582 0.2437  -0.0648 -0.0526 654 ALA A O   
2809 C CB  . ALA A 358 ? 0.9305 0.6878 0.6627 0.2287  -0.0784 -0.0491 654 ALA A CB  
2810 N N   . THR A 359 ? 0.8776 0.7307 0.6442 0.2637  -0.0669 -0.0544 655 THR A N   
2811 C CA  . THR A 359 ? 0.7988 0.7188 0.6199 0.2466  -0.0615 -0.0548 655 THR A CA  
2812 C C   . THR A 359 ? 0.7555 0.7627 0.5926 0.2851  -0.0548 -0.0558 655 THR A C   
2813 O O   . THR A 359 ? 0.7609 0.8531 0.6586 0.2655  -0.0498 -0.0549 655 THR A O   
2814 C CB  . THR A 359 ? 0.8257 0.6831 0.6154 0.2328  -0.0628 -0.0559 655 THR A CB  
2815 O OG1 . THR A 359 ? 0.9239 0.7106 0.6310 0.2739  -0.0640 -0.0585 655 THR A OG1 
2816 C CG2 . THR A 359 ? 0.8398 0.6404 0.6289 0.1867  -0.0692 -0.0540 655 THR A CG2 
2817 N N   . GLU A 360 ? 0.8592 0.8500 0.6399 0.3396  -0.0545 -0.0572 656 GLU A N   
2818 C CA  . GLU A 360 ? 1.0141 1.1080 0.8145 0.3786  -0.0482 -0.0575 656 GLU A CA  
2819 C C   . GLU A 360 ? 0.9752 1.1629 0.8385 0.3613  -0.0481 -0.0558 656 GLU A C   
2820 O O   . GLU A 360 ? 1.0069 1.3009 0.9236 0.3510  -0.0427 -0.0550 656 GLU A O   
2821 C CB  . GLU A 360 ? 1.1635 1.2212 0.8845 0.4486  -0.0483 -0.0591 656 GLU A CB  
2822 C CG  . GLU A 360 ? 1.2726 1.4404 1.0070 0.4939  -0.0404 -0.0595 656 GLU A CG  
2823 C CD  . GLU A 360 ? 1.4273 1.6212 1.1189 0.5608  -0.0411 -0.0593 656 GLU A CD  
2824 O OE1 . GLU A 360 ? 1.4492 1.7665 1.1880 0.5606  -0.0376 -0.0569 656 GLU A OE1 
2825 O OE2 . GLU A 360 ? 1.5874 1.6696 1.1898 0.5889  -0.0451 -0.0594 656 GLU A OE2 
2826 N N   . SER A 361 ? 0.9599 1.1080 0.8139 0.3544  -0.0542 -0.0550 657 SER A N   
2827 C CA  A SER A 361 ? 0.8349 1.0642 0.7432 0.3366  -0.0551 -0.0541 657 SER A CA  
2828 C CA  B SER A 361 ? 0.8358 1.0646 0.7441 0.3363  -0.0551 -0.0540 657 SER A CA  
2829 C C   . SER A 361 ? 0.7701 1.0456 0.7472 0.2774  -0.0526 -0.0537 657 SER A C   
2830 O O   . SER A 361 ? 0.7003 1.0705 0.7250 0.2623  -0.0503 -0.0536 657 SER A O   
2831 C CB  A SER A 361 ? 0.7715 0.9368 0.6536 0.3357  -0.0620 -0.0531 657 SER A CB  
2832 C CB  B SER A 361 ? 0.7700 0.9343 0.6528 0.3345  -0.0620 -0.0531 657 SER A CB  
2833 O OG  A SER A 361 ? 0.7875 0.8825 0.5900 0.3880  -0.0647 -0.0529 657 SER A OG  
2834 O OG  B SER A 361 ? 0.7223 0.8489 0.6353 0.2795  -0.0643 -0.0525 657 SER A OG  
2835 N N   . PHE A 362 ? 0.7272 0.9360 0.7046 0.2438  -0.0534 -0.0534 658 PHE A N   
2836 C CA  . PHE A 362 ? 0.7299 0.9701 0.7612 0.1941  -0.0510 -0.0526 658 PHE A CA  
2837 C C   . PHE A 362 ? 0.7242 1.0424 0.7818 0.1914  -0.0439 -0.0521 658 PHE A C   
2838 O O   . PHE A 362 ? 0.7530 1.1291 0.8537 0.1571  -0.0413 -0.0514 658 PHE A O   
2839 C CB  . PHE A 362 ? 0.7667 0.9253 0.7886 0.1658  -0.0537 -0.0518 658 PHE A CB  
2840 C CG  . PHE A 362 ? 0.7624 0.9426 0.8305 0.1216  -0.0520 -0.0507 658 PHE A CG  
2841 C CD1 . PHE A 362 ? 0.6072 0.8071 0.7044 0.0984  -0.0537 -0.0509 658 PHE A CD1 
2842 C CD2 . PHE A 362 ? 0.8118 0.9901 0.8887 0.1059  -0.0485 -0.0495 658 PHE A CD2 
2843 C CE1 . PHE A 362 ? 0.6803 0.8887 0.8082 0.0623  -0.0520 -0.0502 658 PHE A CE1 
2844 C CE2 . PHE A 362 ? 0.8213 1.0106 0.9307 0.0696  -0.0469 -0.0480 658 PHE A CE2 
2845 C CZ  . PHE A 362 ? 0.7089 0.9101 0.8412 0.0487  -0.0486 -0.0484 658 PHE A CZ  
2846 N N   . ILE A 363 ? 0.7165 1.0343 0.7434 0.2258  -0.0403 -0.0525 659 ILE A N   
2847 C CA  . ILE A 363 ? 0.7735 1.1764 0.8241 0.2252  -0.0326 -0.0513 659 ILE A CA  
2848 C C   . ILE A 363 ? 0.7711 1.2846 0.8472 0.2367  -0.0305 -0.0510 659 ILE A C   
2849 O O   . ILE A 363 ? 0.7831 1.3774 0.8999 0.2035  -0.0262 -0.0494 659 ILE A O   
2850 C CB  . ILE A 363 ? 0.8401 1.2178 0.8477 0.2640  -0.0289 -0.0522 659 ILE A CB  
2851 C CG1 . ILE A 363 ? 0.8287 1.1062 0.8146 0.2437  -0.0318 -0.0525 659 ILE A CG1 
2852 C CG2 . ILE A 363 ? 0.7730 1.2487 0.8057 0.2639  -0.0197 -0.0503 659 ILE A CG2 
2853 C CD1 . ILE A 363 ? 0.8103 1.1060 0.8385 0.1947  -0.0287 -0.0499 659 ILE A CD1 
2854 N N   . LYS A 364 ? 0.8667 1.3840 0.9150 0.2814  -0.0340 -0.0523 660 LYS A N   
2855 C CA  . LYS A 364 ? 0.7813 1.4089 0.8541 0.2930  -0.0337 -0.0519 660 LYS A CA  
2856 C C   . LYS A 364 ? 0.6707 1.3251 0.7902 0.2363  -0.0367 -0.0519 660 LYS A C   
2857 O O   . LYS A 364 ? 0.6306 1.3879 0.7864 0.2120  -0.0340 -0.0511 660 LYS A O   
2858 C CB  . LYS A 364 ? 0.7947 1.4022 0.8218 0.3531  -0.0384 -0.0528 660 LYS A CB  
2859 C CG  . LYS A 364 ? 0.8819 1.6139 0.9154 0.3907  -0.0361 -0.0519 660 LYS A CG  
2860 C CD  . LYS A 364 ? 1.0538 1.7295 1.0086 0.4567  -0.0361 -0.0517 660 LYS A CD  
2861 C CE  . LYS A 364 ? 1.1481 1.8862 1.0860 0.4779  -0.0365 -0.0503 660 LYS A CE  
2862 N NZ  . LYS A 364 ? 1.2047 1.9162 1.1531 0.4653  -0.0443 -0.0510 660 LYS A NZ  
2863 N N   . HIS A 365 ? 0.6731 1.2347 0.7881 0.2121  -0.0421 -0.0528 661 HIS A N   
2864 C CA  . HIS A 365 ? 0.6365 1.2060 0.7868 0.1616  -0.0449 -0.0535 661 HIS A CA  
2865 C C   . HIS A 365 ? 0.6067 1.1975 0.7859 0.1121  -0.0399 -0.0523 661 HIS A C   
2866 O O   . HIS A 365 ? 0.5661 1.2083 0.7718 0.0739  -0.0399 -0.0527 661 HIS A O   
2867 C CB  . HIS A 365 ? 0.6679 1.1343 0.8027 0.1525  -0.0506 -0.0542 661 HIS A CB  
2868 C CG  . HIS A 365 ? 0.7236 1.1819 0.8877 0.1035  -0.0524 -0.0552 661 HIS A CG  
2869 N ND1 . HIS A 365 ? 0.7559 1.2738 0.9413 0.0868  -0.0546 -0.0570 661 HIS A ND1 
2870 C CD2 . HIS A 365 ? 0.7359 1.1312 0.9058 0.0710  -0.0525 -0.0549 661 HIS A CD2 
2871 C CE1 . HIS A 365 ? 0.7224 1.2059 0.9213 0.0463  -0.0557 -0.0582 661 HIS A CE1 
2872 N NE2 . HIS A 365 ? 0.7196 1.1310 0.9099 0.0386  -0.0542 -0.0567 661 HIS A NE2 
2873 N N   . MET A 366 ? 0.5864 1.1311 0.7546 0.1105  -0.0362 -0.0507 662 MET A N   
2874 C CA  . MET A 366 ? 0.5516 1.1116 0.7393 0.0676  -0.0311 -0.0486 662 MET A CA  
2875 C C   . MET A 366 ? 0.5352 1.2100 0.7427 0.0559  -0.0256 -0.0471 662 MET A C   
2876 O O   . MET A 366 ? 0.5045 1.2076 0.7297 0.0071  -0.0239 -0.0461 662 MET A O   
2877 C CB  . MET A 366 ? 0.5574 1.0590 0.7265 0.0760  -0.0281 -0.0469 662 MET A CB  
2878 C CG  . MET A 366 ? 0.4662 0.8953 0.6390 0.0397  -0.0294 -0.0458 662 MET A CG  
2879 S SD  . MET A 366 ? 0.5763 0.9360 0.7238 0.0544  -0.0284 -0.0442 662 MET A SD  
2880 C CE  . MET A 366 ? 0.5766 0.9294 0.7393 0.0066  -0.0242 -0.0403 662 MET A CE  
2881 N N   . GLU A 367 ? 0.5682 1.3104 0.7679 0.1000  -0.0229 -0.0468 663 GLU A N   
2882 C CA  . GLU A 367 ? 0.6924 1.5636 0.9127 0.0915  -0.0174 -0.0448 663 GLU A CA  
2883 C C   . GLU A 367 ? 0.6835 1.6175 0.9274 0.0576  -0.0217 -0.0460 663 GLU A C   
2884 O O   . GLU A 367 ? 0.6671 1.6552 0.9260 0.0066  -0.0185 -0.0441 663 GLU A O   
2885 C CB  . GLU A 367 ? 0.8392 1.7739 1.0427 0.1568  -0.0147 -0.0447 663 GLU A CB  
2886 C CG  . GLU A 367 ? 0.9322 1.8145 1.1050 0.1931  -0.0099 -0.0442 663 GLU A CG  
2887 C CD  . GLU A 367 ? 1.0199 1.9389 1.1609 0.2681  -0.0086 -0.0453 663 GLU A CD  
2888 O OE1 . GLU A 367 ? 1.0447 2.0334 1.1786 0.2793  -0.0087 -0.0438 663 GLU A OE1 
2889 O OE2 . GLU A 367 ? 1.0578 1.8962 1.1568 0.3065  -0.0080 -0.0467 663 GLU A OE2 
2890 N N   . ASN A 368 ? 0.7016 1.6191 0.9397 0.0840  -0.0289 -0.0490 664 ASN A N   
2891 C CA  . ASN A 368 ? 0.6576 1.6144 0.9101 0.0527  -0.0338 -0.0507 664 ASN A CA  
2892 C C   . ASN A 368 ? 0.5929 1.5083 0.8580 -0.0150 -0.0348 -0.0517 664 ASN A C   
2893 O O   . ASN A 368 ? 0.5635 1.5161 0.8276 -0.0601 -0.0327 -0.0505 664 ASN A O   
2894 C CB  . ASN A 368 ? 0.6115 1.5305 0.8533 0.0917  -0.0421 -0.0537 664 ASN A CB  
2895 C CG  . ASN A 368 ? 0.6403 1.5773 0.8520 0.1614  -0.0407 -0.0524 664 ASN A CG  
2896 O OD1 . ASN A 368 ? 0.6924 1.6976 0.8912 0.1754  -0.0341 -0.0496 664 ASN A OD1 
2897 N ND2 . ASN A 368 ? 0.6077 1.4649 0.7937 0.2027  -0.0463 -0.0538 664 ASN A ND2 
2898 N N   . GLU A 369 ? 0.5550 1.3524 0.8065 -0.0210 -0.0353 -0.0520 665 GLU A N   
2899 C CA  . GLU A 369 ? 0.5815 1.3193 0.8316 -0.0753 -0.0357 -0.0526 665 GLU A CA  
2900 C C   . GLU A 369 ? 0.7018 1.4786 0.9534 -0.1204 -0.0291 -0.0492 665 GLU A C   
2901 O O   . GLU A 369 ? 0.7589 1.5472 1.0079 -0.1719 -0.0299 -0.0500 665 GLU A O   
2902 C CB  . GLU A 369 ? 0.6345 1.2532 0.8697 -0.0647 -0.0370 -0.0527 665 GLU A CB  
2903 C CG  . GLU A 369 ? 0.7314 1.2997 0.9614 -0.0406 -0.0437 -0.0557 665 GLU A CG  
2904 C CD  . GLU A 369 ? 0.7782 1.3310 1.0108 -0.0750 -0.0478 -0.0590 665 GLU A CD  
2905 O OE1 . GLU A 369 ? 0.9673 1.4499 1.1906 -0.1003 -0.0474 -0.0592 665 GLU A OE1 
2906 O OE2 . GLU A 369 ? 0.5325 1.1447 0.7732 -0.0748 -0.0515 -0.0615 665 GLU A OE2 
2907 N N   . TYR A 370 ? 0.7428 1.5341 0.9923 -0.1041 -0.0226 -0.0453 666 TYR A N   
2908 C CA  . TYR A 370 ? 0.7371 1.5623 0.9843 -0.1489 -0.0156 -0.0411 666 TYR A CA  
2909 C C   . TYR A 370 ? 0.7866 1.7124 1.0343 -0.1736 -0.0132 -0.0393 666 TYR A C   
2910 O O   . TYR A 370 ? 0.7995 1.7182 1.0276 -0.2263 -0.0099 -0.0363 666 TYR A O   
2911 C CB  . TYR A 370 ? 0.6653 1.4855 0.9070 -0.1218 -0.0087 -0.0371 666 TYR A CB  
2912 C CG  . TYR A 370 ? 0.5846 1.2825 0.8084 -0.1203 -0.0093 -0.0364 666 TYR A CG  
2913 C CD1 . TYR A 370 ? 0.5444 1.1706 0.7623 -0.0796 -0.0146 -0.0393 666 TYR A CD1 
2914 C CD2 . TYR A 370 ? 0.6517 1.3069 0.8607 -0.1614 -0.0052 -0.0324 666 TYR A CD2 
2915 C CE1 . TYR A 370 ? 0.6164 1.1455 0.8202 -0.0801 -0.0159 -0.0384 666 TYR A CE1 
2916 C CE2 . TYR A 370 ? 0.7256 1.2777 0.9181 -0.1559 -0.0064 -0.0315 666 TYR A CE2 
2917 C CZ  . TYR A 370 ? 0.7108 1.2067 0.9038 -0.1155 -0.0119 -0.0346 666 TYR A CZ  
2918 O OH  . TYR A 370 ? 0.7198 1.1275 0.8986 -0.1115 -0.0138 -0.0333 666 TYR A OH  
2919 N N   . ARG A 371 ? 0.8051 1.7979 1.0573 -0.1324 -0.0145 -0.0402 667 ARG A N   
2920 C CA  . ARG A 371 ? 0.9038 1.9779 1.1437 -0.1484 -0.0124 -0.0380 667 ARG A CA  
2921 C C   . ARG A 371 ? 0.9284 1.9793 1.1588 -0.1911 -0.0178 -0.0408 667 ARG A C   
2922 O O   . ARG A 371 ? 0.9541 2.0018 1.1644 -0.2464 -0.0155 -0.0387 667 ARG A O   
2923 C CB  . ARG A 371 ? 0.9797 2.1248 1.2204 -0.0857 -0.0126 -0.0382 667 ARG A CB  
2924 C CG  . ARG A 371 ? 1.1066 2.3437 1.3350 -0.0938 -0.0122 -0.0368 667 ARG A CG  
2925 C CD  . ARG A 371 ? 1.1826 2.4926 1.4018 -0.0286 -0.0102 -0.0355 667 ARG A CD  
2926 N NE  . ARG A 371 ? 1.2202 2.4735 1.4398 0.0333  -0.0124 -0.0380 667 ARG A NE  
2927 C CZ  . ARG A 371 ? 1.2508 2.4614 1.4693 0.0640  -0.0190 -0.0419 667 ARG A CZ  
2928 N NH1 . ARG A 371 ? 1.2641 2.4861 1.4862 0.0397  -0.0238 -0.0439 667 ARG A NH1 
2929 N NH2 . ARG A 371 ? 1.2587 2.4112 1.4679 0.1180  -0.0210 -0.0436 667 ARG A NH2 
2930 N N   . CYS A 372 ? 0.8919 1.9206 1.1311 -0.1662 -0.0249 -0.0455 668 CYS A N   
2931 C CA  . CYS A 372 ? 0.9260 1.9439 1.1548 -0.2000 -0.0298 -0.0485 668 CYS A CA  
2932 C C   . CYS A 372 ? 0.8859 1.8006 1.1045 -0.2410 -0.0332 -0.0515 668 CYS A C   
2933 O O   . CYS A 372 ? 0.9986 1.8916 1.2026 -0.2695 -0.0372 -0.0545 668 CYS A O   
2934 C CB  . CYS A 372 ? 0.9746 2.0173 1.2130 -0.1550 -0.0358 -0.0519 668 CYS A CB  
2935 S SG  . CYS A 372 ? 0.9772 1.9371 1.2315 -0.1105 -0.0435 -0.0565 668 CYS A SG  
2936 N N   . ARG A 373 ? 0.7265 1.5766 0.9477 -0.2432 -0.0316 -0.0508 669 ARG A N   
2937 C CA  . ARG A 373 ? 0.7016 1.4483 0.9069 -0.2742 -0.0348 -0.0539 669 ARG A CA  
2938 C C   . ARG A 373 ? 0.8322 1.5248 1.0187 -0.3038 -0.0292 -0.0500 669 ARG A C   
2939 O O   . ARG A 373 ? 0.8239 1.4263 0.9830 -0.3331 -0.0307 -0.0517 669 ARG A O   
2940 C CB  . ARG A 373 ? 0.6634 1.3637 0.8886 -0.2378 -0.0418 -0.0591 669 ARG A CB  
2941 C CG  . ARG A 373 ? 0.7713 1.3657 0.9725 -0.2588 -0.0454 -0.0630 669 ARG A CG  
2942 C CD  . ARG A 373 ? 0.7795 1.3049 0.9852 -0.2112 -0.0480 -0.0641 669 ARG A CD  
2943 N NE  . ARG A 373 ? 0.8298 1.2693 1.0132 -0.2262 -0.0509 -0.0678 669 ARG A NE  
2944 C CZ  . ARG A 373 ? 0.8034 1.1683 0.9824 -0.1990 -0.0517 -0.0677 669 ARG A CZ  
2945 N NH1 . ARG A 373 ? 0.7351 1.0937 0.9279 -0.1608 -0.0504 -0.0644 669 ARG A NH1 
2946 N NH2 . ARG A 373 ? 0.8417 1.1395 0.9985 -0.2109 -0.0536 -0.0711 669 ARG A NH2 
2947 N N   . GLY A 374 ? 0.8930 1.6325 1.0881 -0.2945 -0.0226 -0.0448 670 GLY A N   
2948 C CA  . GLY A 374 ? 0.9803 1.6712 1.1559 -0.3218 -0.0169 -0.0403 670 GLY A CA  
2949 C C   . GLY A 374 ? 1.0081 1.6221 1.1880 -0.2907 -0.0169 -0.0402 670 GLY A C   
2950 O O   . GLY A 374 ? 1.1325 1.6806 1.2865 -0.3104 -0.0129 -0.0362 670 GLY A O   
2951 N N   . GLY A 375 ? 0.9158 1.5181 1.1145 -0.2374 -0.0208 -0.0430 671 GLY A N   
2952 C CA  . GLY A 375 ? 0.8230 1.3415 1.0156 -0.2037 -0.0207 -0.0418 671 GLY A CA  
2953 C C   . GLY A 375 ? 0.7780 1.2611 0.9796 -0.1653 -0.0273 -0.0461 671 GLY A C   
2954 O O   . GLY A 375 ? 0.8177 1.3338 1.0288 -0.1628 -0.0318 -0.0500 671 GLY A O   
2955 N N   . CYS A 376 ? 0.7031 1.1194 0.8990 -0.1382 -0.0280 -0.0450 672 CYS A N   
2956 C CA  . CYS A 376 ? 0.6264 1.0001 0.8251 -0.1056 -0.0336 -0.0476 672 CYS A CA  
2957 C C   . CYS A 376 ? 0.6765 0.9707 0.8627 -0.0999 -0.0340 -0.0454 672 CYS A C   
2958 O O   . CYS A 376 ? 0.6514 0.9383 0.8339 -0.0852 -0.0316 -0.0426 672 CYS A O   
2959 C CB  . CYS A 376 ? 0.5693 0.9842 0.7751 -0.0636 -0.0346 -0.0483 672 CYS A CB  
2960 S SG  . CYS A 376 ? 0.5222 0.8793 0.7201 -0.0278 -0.0414 -0.0506 672 CYS A SG  
2961 N N   . PRO A 377 ? 0.6684 0.9068 0.8461 -0.1096 -0.0369 -0.0466 673 PRO A N   
2962 C CA  . PRO A 377 ? 0.5083 0.6854 0.6763 -0.0990 -0.0379 -0.0441 673 PRO A CA  
2963 C C   . PRO A 377 ? 0.5511 0.7233 0.7251 -0.0681 -0.0412 -0.0441 673 PRO A C   
2964 O O   . PRO A 377 ? 0.4068 0.5930 0.5865 -0.0534 -0.0445 -0.0468 673 PRO A O   
2965 C CB  . PRO A 377 ? 0.5955 0.7294 0.7539 -0.1085 -0.0405 -0.0462 673 PRO A CB  
2966 C CG  . PRO A 377 ? 0.5459 0.7146 0.7124 -0.1165 -0.0425 -0.0507 673 PRO A CG  
2967 C CD  . PRO A 377 ? 0.4964 0.7286 0.6706 -0.1288 -0.0395 -0.0504 673 PRO A CD  
2968 N N   . ALA A 378 ? 0.5327 0.6797 0.6992 -0.0597 -0.0407 -0.0410 674 ALA A N   
2969 C CA  . ALA A 378 ? 0.5045 0.6388 0.6665 -0.0359 -0.0443 -0.0412 674 ALA A CA  
2970 C C   . ALA A 378 ? 0.4669 0.5624 0.6198 -0.0357 -0.0460 -0.0381 674 ALA A C   
2971 O O   . ALA A 378 ? 0.5689 0.6582 0.7176 -0.0454 -0.0428 -0.0351 674 ALA A O   
2972 C CB  . ALA A 378 ? 0.4468 0.6172 0.6051 -0.0185 -0.0418 -0.0420 674 ALA A CB  
2973 N N   . ASP A 379 ? 0.3717 0.4427 0.5192 -0.0271 -0.0512 -0.0382 675 ASP A N   
2974 C CA  . ASP A 379 ? 0.3823 0.4270 0.5222 -0.0281 -0.0546 -0.0354 675 ASP A CA  
2975 C C   . ASP A 379 ? 0.6125 0.6444 0.7335 -0.0168 -0.0574 -0.0361 675 ASP A C   
2976 O O   . ASP A 379 ? 0.6421 0.6582 0.7503 -0.0116 -0.0615 -0.0377 675 ASP A O   
2977 C CB  . ASP A 379 ? 0.4674 0.5019 0.6124 -0.0321 -0.0585 -0.0348 675 ASP A CB  
2978 C CG  . ASP A 379 ? 0.5911 0.6151 0.7318 -0.0340 -0.0618 -0.0311 675 ASP A CG  
2979 O OD1 . ASP A 379 ? 0.5680 0.5948 0.7147 -0.0353 -0.0631 -0.0296 675 ASP A OD1 
2980 O OD2 . ASP A 379 ? 0.6546 0.6715 0.7843 -0.0326 -0.0632 -0.0299 675 ASP A OD2 
2981 N N   . TRP A 380 ? 0.5570 0.5899 0.6699 -0.0136 -0.0548 -0.0350 676 TRP A N   
2982 C CA  . TRP A 380 ? 0.4744 0.4891 0.5612 -0.0008 -0.0568 -0.0364 676 TRP A CA  
2983 C C   . TRP A 380 ? 0.5270 0.5069 0.5952 -0.0075 -0.0646 -0.0360 676 TRP A C   
2984 O O   . TRP A 380 ? 0.6183 0.5679 0.6548 -0.0001 -0.0682 -0.0383 676 TRP A O   
2985 C CB  . TRP A 380 ? 0.5413 0.5658 0.6247 0.0010  -0.0523 -0.0347 676 TRP A CB  
2986 C CG  . TRP A 380 ? 0.4282 0.4368 0.4820 0.0174  -0.0526 -0.0368 676 TRP A CG  
2987 C CD1 . TRP A 380 ? 0.5991 0.6317 0.6451 0.0352  -0.0465 -0.0383 676 TRP A CD1 
2988 C CD2 . TRP A 380 ? 0.4792 0.4456 0.5023 0.0173  -0.0591 -0.0376 676 TRP A CD2 
2989 N NE1 . TRP A 380 ? 0.6200 0.6215 0.6294 0.0510  -0.0484 -0.0405 676 TRP A NE1 
2990 C CE2 . TRP A 380 ? 0.5947 0.5510 0.5875 0.0378  -0.0565 -0.0404 676 TRP A CE2 
2991 C CE3 . TRP A 380 ? 0.4784 0.4192 0.4945 0.0008  -0.0670 -0.0363 676 TRP A CE3 
2992 C CZ2 . TRP A 380 ? 0.6668 0.5752 0.6163 0.0413  -0.0620 -0.0427 676 TRP A CZ2 
2993 C CZ3 . TRP A 380 ? 0.6999 0.6018 0.6768 -0.0007 -0.0730 -0.0381 676 TRP A CZ3 
2994 C CH2 . TRP A 380 ? 0.5349 0.4153 0.4769 0.0187  -0.0706 -0.0416 676 TRP A CH2 
2995 N N   . VAL A 381 ? 0.5141 0.4975 0.5961 -0.0216 -0.0673 -0.0327 677 VAL A N   
2996 C CA  . VAL A 381 ? 0.5501 0.5168 0.6182 -0.0333 -0.0749 -0.0316 677 VAL A CA  
2997 C C   . VAL A 381 ? 0.6620 0.6126 0.7172 -0.0361 -0.0779 -0.0334 677 VAL A C   
2998 O O   . VAL A 381 ? 0.6011 0.5202 0.6234 -0.0443 -0.0836 -0.0341 677 VAL A O   
2999 C CB  . VAL A 381 ? 0.5592 0.5488 0.6486 -0.0423 -0.0766 -0.0273 677 VAL A CB  
3000 C CG1 . VAL A 381 ? 0.5910 0.5810 0.6702 -0.0575 -0.0842 -0.0258 677 VAL A CG1 
3001 C CG2 . VAL A 381 ? 0.5595 0.5541 0.6499 -0.0388 -0.0750 -0.0246 677 VAL A CG2 
3002 N N   . TRP A 382 ? 0.6211 0.5885 0.6964 -0.0316 -0.0744 -0.0342 678 TRP A N   
3003 C CA  . TRP A 382 ? 0.5988 0.5536 0.6637 -0.0333 -0.0767 -0.0353 678 TRP A CA  
3004 C C   . TRP A 382 ? 0.5773 0.5120 0.6175 -0.0144 -0.0752 -0.0386 678 TRP A C   
3005 O O   . TRP A 382 ? 0.6326 0.5341 0.6416 -0.0141 -0.0788 -0.0390 678 TRP A O   
3006 C CB  . TRP A 382 ? 0.5304 0.5144 0.6270 -0.0364 -0.0741 -0.0346 678 TRP A CB  
3007 C CG  . TRP A 382 ? 0.6214 0.6193 0.7283 -0.0507 -0.0771 -0.0311 678 TRP A CG  
3008 C CD1 . TRP A 382 ? 0.6786 0.6936 0.7962 -0.0539 -0.0777 -0.0282 678 TRP A CD1 
3009 C CD2 . TRP A 382 ? 0.6757 0.6787 0.7813 -0.0616 -0.0796 -0.0295 678 TRP A CD2 
3010 N NE1 . TRP A 382 ? 0.6921 0.7296 0.8171 -0.0635 -0.0806 -0.0251 678 TRP A NE1 
3011 C CE2 . TRP A 382 ? 0.7170 0.7491 0.8358 -0.0704 -0.0815 -0.0258 678 TRP A CE2 
3012 C CE3 . TRP A 382 ? 0.6710 0.6597 0.7639 -0.0636 -0.0803 -0.0304 678 TRP A CE3 
3013 C CZ2 . TRP A 382 ? 0.7148 0.7695 0.8372 -0.0826 -0.0834 -0.0229 678 TRP A CZ2 
3014 C CZ3 . TRP A 382 ? 0.7432 0.7456 0.8373 -0.0784 -0.0823 -0.0274 678 TRP A CZ3 
3015 C CH2 . TRP A 382 ? 0.7613 0.8003 0.8718 -0.0885 -0.0835 -0.0238 678 TRP A CH2 
3016 N N   . ILE A 383 ? 0.6391 0.5937 0.6874 0.0022  -0.0701 -0.0404 679 ILE A N   
3017 C CA  . ILE A 383 ? 0.5508 0.5016 0.5780 0.0269  -0.0682 -0.0433 679 ILE A CA  
3018 C C   . ILE A 383 ? 0.7373 0.6383 0.7123 0.0408  -0.0710 -0.0448 679 ILE A C   
3019 O O   . ILE A 383 ? 0.7367 0.6073 0.6733 0.0615  -0.0723 -0.0466 679 ILE A O   
3020 C CB  . ILE A 383 ? 0.6341 0.6383 0.6897 0.0370  -0.0613 -0.0441 679 ILE A CB  
3021 C CG1 . ILE A 383 ? 0.5262 0.5667 0.6199 0.0218  -0.0593 -0.0436 679 ILE A CG1 
3022 C CG2 . ILE A 383 ? 0.6166 0.6319 0.6497 0.0685  -0.0589 -0.0466 679 ILE A CG2 
3023 C CD1 . ILE A 383 ? 0.6704 0.7233 0.7647 0.0316  -0.0604 -0.0455 679 ILE A CD1 
3024 N N   . VAL A 384 ? 0.5628 0.4493 0.5283 0.0321  -0.0722 -0.0443 680 VAL A N   
3025 C CA  . VAL A 384 ? 0.6763 0.5072 0.5834 0.0452  -0.0752 -0.0468 680 VAL A CA  
3026 C C   . VAL A 384 ? 0.6715 0.4417 0.5348 0.0287  -0.0829 -0.0464 680 VAL A C   
3027 O O   . VAL A 384 ? 0.6960 0.4718 0.5758 -0.0028 -0.0871 -0.0435 680 VAL A O   
3028 C CB  . VAL A 384 ? 0.6613 0.4918 0.5673 0.0373  -0.0753 -0.0465 680 VAL A CB  
3029 C CG1 . VAL A 384 ? 0.6457 0.4053 0.4804 0.0465  -0.0798 -0.0499 680 VAL A CG1 
3030 C CG2 . VAL A 384 ? 0.7770 0.6618 0.7168 0.0520  -0.0670 -0.0462 680 VAL A CG2 
3031 N N   . PRO A 385 ? 0.8709 0.5855 0.6760 0.0489  -0.0846 -0.0486 681 PRO A N   
3032 C CA  . PRO A 385 ? 0.7931 0.4409 0.5467 0.0277  -0.0919 -0.0475 681 PRO A CA  
3033 C C   . PRO A 385 ? 0.9510 0.5661 0.6792 -0.0067 -0.0984 -0.0470 681 PRO A C   
3034 O O   . PRO A 385 ? 0.9505 0.5654 0.6733 -0.0010 -0.0979 -0.0492 681 PRO A O   
3035 C CB  . PRO A 385 ? 0.9191 0.4994 0.5986 0.0644  -0.0920 -0.0505 681 PRO A CB  
3036 C CG  . PRO A 385 ? 1.0567 0.6732 0.7479 0.1047  -0.0852 -0.0538 681 PRO A CG  
3037 C CD  . PRO A 385 ? 0.9336 0.6470 0.7145 0.0937  -0.0798 -0.0517 681 PRO A CD  
3038 N N   . PRO A 386 ? 0.9629 0.5562 0.6751 -0.0442 -0.1046 -0.0440 682 PRO A N   
3039 C CA  . PRO A 386 ? 0.8265 0.4072 0.5214 -0.0833 -0.1117 -0.0428 682 PRO A CA  
3040 C C   . PRO A 386 ? 1.0848 0.5691 0.6863 -0.0885 -0.1178 -0.0465 682 PRO A C   
3041 O O   . PRO A 386 ? 1.1674 0.6317 0.7409 -0.1279 -0.1253 -0.0458 682 PRO A O   
3042 C CB  . PRO A 386 ? 0.8267 0.4298 0.5382 -0.1205 -0.1151 -0.0377 682 PRO A CB  
3043 C CG  . PRO A 386 ? 0.8252 0.3771 0.4970 -0.1035 -0.1134 -0.0378 682 PRO A CG  
3044 C CD  . PRO A 386 ? 0.9552 0.5206 0.6447 -0.0520 -0.1062 -0.0415 682 PRO A CD  
3045 N N   . MET A 387 ? 1.0946 0.5211 0.6442 -0.0483 -0.1148 -0.0507 683 MET A N   
3046 C CA  . MET A 387 ? 1.0727 0.4011 0.5270 -0.0436 -0.1195 -0.0554 683 MET A CA  
3047 C C   . MET A 387 ? 1.2392 0.5659 0.6843 0.0158  -0.1120 -0.0600 683 MET A C   
3048 O O   . MET A 387 ? 1.2120 0.5931 0.7036 0.0496  -0.1047 -0.0590 683 MET A O   
3049 C CB  . MET A 387 ? 1.2447 0.4673 0.6036 -0.0592 -0.1255 -0.0549 683 MET A CB  
3050 C CG  . MET A 387 ? 1.3884 0.5791 0.7197 -0.0123 -0.1204 -0.0551 683 MET A CG  
3051 S SD  . MET A 387 ? 1.6224 0.6615 0.8163 -0.0253 -0.1276 -0.0544 683 MET A SD  
3052 C CE  . MET A 387 ? 1.6371 0.5883 0.7346 -0.0128 -0.1300 -0.0570 683 MET A CE  
3053 N N   . SER A 388 ? 1.3475 0.6167 0.7316 0.0275  -0.1139 -0.0650 684 SER A N   
3054 C CA  . SER A 388 ? 1.2970 0.5631 0.6613 0.0867  -0.1064 -0.0695 684 SER A CA  
3055 C C   . SER A 388 ? 1.1361 0.5243 0.6041 0.1079  -0.0968 -0.0672 684 SER A C   
3056 O O   . SER A 388 ? 1.1758 0.5950 0.6522 0.1551  -0.0892 -0.0682 684 SER A O   
3057 C CB  . SER A 388 ? 1.3680 0.5584 0.6541 0.1294  -0.1053 -0.0715 684 SER A CB  
3058 O OG  . SER A 388 ? 1.5714 0.6480 0.7651 0.0985  -0.1145 -0.0717 684 SER A OG  
3059 N N   . GLY A 389 ? 1.0281 0.4865 0.5710 0.0721  -0.0973 -0.0636 685 GLY A N   
3060 C CA  . GLY A 389 ? 0.9711 0.5312 0.6010 0.0842  -0.0888 -0.0612 685 GLY A CA  
3061 C C   . GLY A 389 ? 1.0107 0.5977 0.6369 0.1333  -0.0798 -0.0639 685 GLY A C   
3062 O O   . GLY A 389 ? 1.0669 0.7019 0.7213 0.1601  -0.0736 -0.0631 685 GLY A O   
3063 N N   . SER A 390 ? 1.0563 0.6159 0.6444 0.1458  -0.0791 -0.0674 686 SER A N   
3064 C CA  . SER A 390 ? 1.0861 0.6969 0.6874 0.1860  -0.0692 -0.0687 686 SER A CA  
3065 C C   . SER A 390 ? 1.1329 0.7122 0.6732 0.2414  -0.0653 -0.0727 686 SER A C   
3066 O O   . SER A 390 ? 1.1017 0.7354 0.6519 0.2795  -0.0563 -0.0736 686 SER A O   
3067 C CB  . SER A 390 ? 1.0389 0.6386 0.6246 0.1798  -0.0692 -0.0706 686 SER A CB  
3068 O OG  . SER A 390 ? 1.1806 0.6771 0.6821 0.1718  -0.0781 -0.0753 686 SER A OG  
3069 N N   . ILE A 391 ? 1.1617 0.6554 0.6344 0.2488  -0.0717 -0.0748 687 ILE A N   
3070 C CA  . ILE A 391 ? 1.2650 0.7318 0.6786 0.3086  -0.0678 -0.0777 687 ILE A CA  
3071 C C   . ILE A 391 ? 1.2078 0.7412 0.6713 0.3211  -0.0647 -0.0739 687 ILE A C   
3072 O O   . ILE A 391 ? 1.3338 0.8548 0.7526 0.3729  -0.0621 -0.0754 687 ILE A O   
3073 C CB  . ILE A 391 ? 1.3824 0.7038 0.6732 0.3201  -0.0758 -0.0822 687 ILE A CB  
3074 C CG1 . ILE A 391 ? 1.5031 0.7705 0.7777 0.2857  -0.0838 -0.0792 687 ILE A CG1 
3075 C CG2 . ILE A 391 ? 1.4373 0.6879 0.6765 0.2958  -0.0810 -0.0864 687 ILE A CG2 
3076 C CD1 . ILE A 391 ? 1.5775 0.6941 0.7193 0.2974  -0.0910 -0.0829 687 ILE A CD1 
3077 N N   . THR A 392 ? 1.1743 0.7778 0.7254 0.2779  -0.0650 -0.0692 688 THR A N   
3078 C CA  . THR A 392 ? 1.1155 0.7979 0.7277 0.2817  -0.0616 -0.0658 688 THR A CA  
3079 C C   . THR A 392 ? 1.0621 0.8624 0.7571 0.2774  -0.0531 -0.0636 688 THR A C   
3080 O O   . THR A 392 ? 1.0908 0.9100 0.8191 0.2468  -0.0520 -0.0623 688 THR A O   
3081 C CB  . THR A 392 ? 1.1124 0.7796 0.7538 0.2348  -0.0681 -0.0625 688 THR A CB  
3082 O OG1 . THR A 392 ? 0.9697 0.6727 0.6707 0.1877  -0.0689 -0.0601 688 THR A OG1 
3083 C CG2 . THR A 392 ? 1.1116 0.6600 0.6679 0.2265  -0.0768 -0.0636 688 THR A CG2 
3084 N N   . PRO A 393 ? 1.0030 0.8836 0.7276 0.3060  -0.0472 -0.0626 689 PRO A N   
3085 C CA  . PRO A 393 ? 0.9369 0.9279 0.7259 0.3019  -0.0385 -0.0605 689 PRO A CA  
3086 C C   . PRO A 393 ? 0.8873 0.9200 0.7486 0.2460  -0.0386 -0.0567 689 PRO A C   
3087 O O   . PRO A 393 ? 0.9430 1.0448 0.8457 0.2332  -0.0319 -0.0544 689 PRO A O   
3088 C CB  . PRO A 393 ? 1.0413 1.1067 0.8390 0.3412  -0.0343 -0.0602 689 PRO A CB  
3089 C CG  . PRO A 393 ? 1.1017 1.1076 0.8731 0.3434  -0.0421 -0.0605 689 PRO A CG  
3090 C CD  . PRO A 393 ? 1.1427 1.0205 0.8436 0.3384  -0.0489 -0.0628 689 PRO A CD  
3091 N N   . VAL A 394 ? 0.8009 0.7932 0.6739 0.2136  -0.0455 -0.0555 690 VAL A N   
3092 C CA  . VAL A 394 ? 0.7763 0.8036 0.7095 0.1680  -0.0451 -0.0522 690 VAL A CA  
3093 C C   . VAL A 394 ? 0.7472 0.7451 0.6794 0.1444  -0.0461 -0.0510 690 VAL A C   
3094 O O   . VAL A 394 ? 0.6623 0.6962 0.6374 0.1164  -0.0434 -0.0478 690 VAL A O   
3095 C CB  . VAL A 394 ? 0.6800 0.6837 0.6271 0.1452  -0.0513 -0.0512 690 VAL A CB  
3096 C CG1 . VAL A 394 ? 0.6982 0.7476 0.6586 0.1632  -0.0499 -0.0517 690 VAL A CG1 
3097 C CG2 . VAL A 394 ? 0.7476 0.6606 0.6425 0.1423  -0.0591 -0.0524 690 VAL A CG2 
3098 N N   . PHE A 395 ? 0.7689 0.6961 0.6475 0.1536  -0.0506 -0.0535 691 PHE A N   
3099 C CA  . PHE A 395 ? 0.8138 0.7186 0.6893 0.1328  -0.0523 -0.0526 691 PHE A CA  
3100 C C   . PHE A 395 ? 0.8122 0.7779 0.7154 0.1370  -0.0435 -0.0507 691 PHE A C   
3101 O O   . PHE A 395 ? 0.7406 0.7169 0.6690 0.1109  -0.0431 -0.0474 691 PHE A O   
3102 C CB  . PHE A 395 ? 0.7423 0.5637 0.5458 0.1449  -0.0580 -0.0567 691 PHE A CB  
3103 C CG  . PHE A 395 ? 0.7657 0.5674 0.5619 0.1248  -0.0606 -0.0563 691 PHE A CG  
3104 C CD1 . PHE A 395 ? 0.8073 0.5673 0.5943 0.0903  -0.0699 -0.0554 691 PHE A CD1 
3105 C CD2 . PHE A 395 ? 0.7525 0.5847 0.5513 0.1398  -0.0537 -0.0563 691 PHE A CD2 
3106 C CE1 . PHE A 395 ? 0.8959 0.6450 0.6761 0.0731  -0.0731 -0.0549 691 PHE A CE1 
3107 C CE2 . PHE A 395 ? 0.8802 0.6951 0.6712 0.1225  -0.0563 -0.0557 691 PHE A CE2 
3108 C CZ  . PHE A 395 ? 0.8210 0.5942 0.6027 0.0900  -0.0664 -0.0551 691 PHE A CZ  
3109 N N   . HIS A 396 ? 0.8944 0.9025 0.7897 0.1708  -0.0362 -0.0521 692 HIS A N   
3110 C CA  . HIS A 396 ? 0.8088 0.8808 0.7217 0.1783  -0.0267 -0.0502 692 HIS A CA  
3111 C C   . HIS A 396 ? 0.7501 0.9074 0.7203 0.1579  -0.0204 -0.0459 692 HIS A C   
3112 O O   . HIS A 396 ? 0.7382 0.9609 0.7235 0.1606  -0.0116 -0.0435 692 HIS A O   
3113 C CB  . HIS A 396 ? 0.8516 0.9297 0.7190 0.2293  -0.0221 -0.0541 692 HIS A CB  
3114 C CG  . HIS A 396 ? 0.9592 0.9383 0.7554 0.2496  -0.0288 -0.0592 692 HIS A CG  
3115 N ND1 . HIS A 396 ? 0.9876 0.9215 0.7564 0.2410  -0.0306 -0.0604 692 HIS A ND1 
3116 C CD2 . HIS A 396 ? 0.9948 0.9039 0.7351 0.2737  -0.0349 -0.0633 692 HIS A CD2 
3117 C CE1 . HIS A 396 ? 1.0767 0.9177 0.7745 0.2572  -0.0376 -0.0656 692 HIS A CE1 
3118 N NE2 . HIS A 396 ? 1.0992 0.9193 0.7759 0.2766  -0.0402 -0.0672 692 HIS A NE2 
3119 N N   . GLN A 397 ? 0.7841 0.9411 0.7820 0.1353  -0.0247 -0.0448 693 GLN A N   
3120 C CA  . GLN A 397 ? 0.7026 0.9297 0.7449 0.1143  -0.0202 -0.0419 693 GLN A CA  
3121 C C   . GLN A 397 ? 0.6005 0.8094 0.6687 0.0719  -0.0218 -0.0382 693 GLN A C   
3122 O O   . GLN A 397 ? 0.6343 0.7958 0.7038 0.0596  -0.0288 -0.0387 693 GLN A O   
3123 C CB  . GLN A 397 ? 0.7614 1.0023 0.8089 0.1263  -0.0236 -0.0443 693 GLN A CB  
3124 C CG  . GLN A 397 ? 0.7179 1.0203 0.8074 0.0978  -0.0212 -0.0422 693 GLN A CG  
3125 C CD  . GLN A 397 ? 0.6236 1.0187 0.7295 0.0979  -0.0123 -0.0401 693 GLN A CD  
3126 O OE1 . GLN A 397 ? 0.5694 1.0088 0.6610 0.1352  -0.0089 -0.0416 693 GLN A OE1 
3127 N NE2 . GLN A 397 ? 0.5941 1.0192 0.7250 0.0562  -0.0084 -0.0363 693 GLN A NE2 
3128 N N   . GLU A 398 ? 0.5775 0.8231 0.6610 0.0510  -0.0150 -0.0340 694 GLU A N   
3129 C CA  . GLU A 398 ? 0.6335 0.8611 0.7337 0.0141  -0.0157 -0.0300 694 GLU A CA  
3130 C C   . GLU A 398 ? 0.6706 0.9122 0.7914 -0.0025 -0.0179 -0.0310 694 GLU A C   
3131 O O   . GLU A 398 ? 0.5963 0.8948 0.7288 0.0001  -0.0150 -0.0323 694 GLU A O   
3132 C CB  . GLU A 398 ? 0.6326 0.8934 0.7357 -0.0067 -0.0074 -0.0247 694 GLU A CB  
3133 C CG  . GLU A 398 ? 0.6512 0.8925 0.7329 0.0061  -0.0052 -0.0231 694 GLU A CG  
3134 C CD  . GLU A 398 ? 0.7301 1.0126 0.8122 -0.0131 0.0044  -0.0173 694 GLU A CD  
3135 O OE1 . GLU A 398 ? 0.7452 1.0249 0.8101 -0.0004 0.0077  -0.0160 694 GLU A OE1 
3136 O OE2 . GLU A 398 ? 0.6999 1.0150 0.7950 -0.0437 0.0086  -0.0140 694 GLU A OE2 
3137 N N   . MET A 399 ? 0.6845 0.8785 0.8083 -0.0187 -0.0231 -0.0302 695 MET A N   
3138 C CA  . MET A 399 ? 0.6731 0.8691 0.8111 -0.0334 -0.0255 -0.0317 695 MET A CA  
3139 C C   . MET A 399 ? 0.6791 0.8425 0.8146 -0.0607 -0.0251 -0.0282 695 MET A C   
3140 O O   . MET A 399 ? 0.7264 0.8453 0.8525 -0.0581 -0.0283 -0.0261 695 MET A O   
3141 C CB  . MET A 399 ? 0.5049 0.6695 0.6412 -0.0167 -0.0330 -0.0352 695 MET A CB  
3142 C CG  . MET A 399 ? 0.4300 0.6119 0.5569 0.0128  -0.0342 -0.0388 695 MET A CG  
3143 S SD  . MET A 399 ? 0.5826 0.7017 0.6898 0.0258  -0.0430 -0.0409 695 MET A SD  
3144 C CE  . MET A 399 ? 0.5537 0.6733 0.6280 0.0647  -0.0430 -0.0441 695 MET A CE  
3145 N N   . LEU A 400 ? 0.6544 0.8382 0.7932 -0.0858 -0.0218 -0.0277 696 LEU A N   
3146 C CA  . LEU A 400 ? 0.6907 0.8295 0.8160 -0.1087 -0.0222 -0.0257 696 LEU A CA  
3147 C C   . LEU A 400 ? 0.7113 0.8243 0.8426 -0.1013 -0.0283 -0.0294 696 LEU A C   
3148 O O   . LEU A 400 ? 0.6252 0.7681 0.7699 -0.1004 -0.0299 -0.0335 696 LEU A O   
3149 C CB  . LEU A 400 ? 0.6952 0.8575 0.8112 -0.1436 -0.0168 -0.0242 696 LEU A CB  
3150 C CG  . LEU A 400 ? 0.7255 0.9145 0.8316 -0.1587 -0.0095 -0.0190 696 LEU A CG  
3151 C CD1 . LEU A 400 ? 0.7735 0.9860 0.8660 -0.2021 -0.0048 -0.0173 696 LEU A CD1 
3152 C CD2 . LEU A 400 ? 0.7514 0.8814 0.8353 -0.1538 -0.0092 -0.0140 696 LEU A CD2 
3153 N N   . ASN A 401 ? 0.6992 0.7627 0.8198 -0.0943 -0.0316 -0.0277 697 ASN A N   
3154 C CA  . ASN A 401 ? 0.6215 0.6630 0.7449 -0.0878 -0.0362 -0.0305 697 ASN A CA  
3155 C C   . ASN A 401 ? 0.7196 0.7226 0.8183 -0.1046 -0.0344 -0.0298 697 ASN A C   
3156 O O   . ASN A 401 ? 0.6598 0.6266 0.7327 -0.1094 -0.0321 -0.0254 697 ASN A O   
3157 C CB  . ASN A 401 ? 0.6373 0.6594 0.7632 -0.0675 -0.0411 -0.0290 697 ASN A CB  
3158 C CG  . ASN A 401 ? 0.5937 0.6104 0.7276 -0.0599 -0.0453 -0.0317 697 ASN A CG  
3159 O OD1 . ASN A 401 ? 0.6477 0.6790 0.7896 -0.0647 -0.0454 -0.0356 697 ASN A OD1 
3160 N ND2 . ASN A 401 ? 0.4666 0.4687 0.5980 -0.0482 -0.0489 -0.0293 697 ASN A ND2 
3161 N N   . TYR A 402 ? 0.6489 0.6535 0.7490 -0.1121 -0.0356 -0.0343 698 TYR A N   
3162 C CA  . TYR A 402 ? 0.6276 0.5851 0.6953 -0.1261 -0.0346 -0.0351 698 TYR A CA  
3163 C C   . TYR A 402 ? 0.7698 0.7319 0.8465 -0.1217 -0.0380 -0.0408 698 TYR A C   
3164 O O   . TYR A 402 ? 0.5913 0.5977 0.6980 -0.1150 -0.0403 -0.0436 698 TYR A O   
3165 C CB  . TYR A 402 ? 0.6913 0.6445 0.7339 -0.1614 -0.0300 -0.0341 698 TYR A CB  
3166 C CG  . TYR A 402 ? 0.7424 0.7668 0.8114 -0.1786 -0.0288 -0.0364 698 TYR A CG  
3167 C CD1 . TYR A 402 ? 0.7521 0.7994 0.8248 -0.1949 -0.0307 -0.0417 698 TYR A CD1 
3168 C CD2 . TYR A 402 ? 0.7203 0.7935 0.8083 -0.1757 -0.0258 -0.0333 698 TYR A CD2 
3169 C CE1 . TYR A 402 ? 0.7175 0.8404 0.8142 -0.2070 -0.0300 -0.0434 698 TYR A CE1 
3170 C CE2 . TYR A 402 ? 0.7075 0.8550 0.8175 -0.1850 -0.0242 -0.0351 698 TYR A CE2 
3171 C CZ  . TYR A 402 ? 0.7307 0.9060 0.8459 -0.2004 -0.0266 -0.0400 698 TYR A CZ  
3172 O OH  . TYR A 402 ? 0.6752 0.9346 0.8125 -0.2064 -0.0257 -0.0415 698 TYR A OH  
3173 N N   . ARG A 403 ? 0.7861 0.6973 0.8307 -0.1227 -0.0380 -0.0423 699 ARG A N   
3174 C CA  . ARG A 403 ? 0.8990 0.8054 0.9474 -0.1105 -0.0408 -0.0469 699 ARG A CA  
3175 C C   . ARG A 403 ? 0.9358 0.8309 0.9630 -0.1376 -0.0407 -0.0525 699 ARG A C   
3176 O O   . ARG A 403 ? 1.0553 0.8900 1.0350 -0.1476 -0.0393 -0.0539 699 ARG A O   
3177 C CB  . ARG A 403 ? 1.0689 0.9303 1.0934 -0.0848 -0.0411 -0.0449 699 ARG A CB  
3178 C CG  . ARG A 403 ? 1.2381 1.1033 1.2698 -0.0657 -0.0413 -0.0385 699 ARG A CG  
3179 C CD  . ARG A 403 ? 1.3321 1.2241 1.3878 -0.0388 -0.0445 -0.0374 699 ARG A CD  
3180 N NE  . ARG A 403 ? 1.4613 1.3318 1.4981 -0.0242 -0.0444 -0.0403 699 ARG A NE  
3181 C CZ  . ARG A 403 ? 1.4816 1.3776 1.5380 -0.0222 -0.0458 -0.0443 699 ARG A CZ  
3182 N NH1 . ARG A 403 ? 1.3943 1.3334 1.4864 -0.0329 -0.0480 -0.0454 699 ARG A NH1 
3183 N NH2 . ARG A 403 ? 1.5563 1.4309 1.5907 -0.0066 -0.0449 -0.0469 699 ARG A NH2 
3184 N N   . LEU A 404 ? 0.8724 0.8233 0.9294 -0.1486 -0.0424 -0.0558 700 LEU A N   
3185 C CA  . LEU A 404 ? 0.8038 0.7567 0.8460 -0.1738 -0.0438 -0.0617 700 LEU A CA  
3186 C C   . LEU A 404 ? 0.8157 0.7561 0.8595 -0.1556 -0.0468 -0.0663 700 LEU A C   
3187 O O   . LEU A 404 ? 0.7123 0.6563 0.7752 -0.1256 -0.0476 -0.0644 700 LEU A O   
3188 C CB  . LEU A 404 ? 0.7509 0.7801 0.8238 -0.1905 -0.0447 -0.0628 700 LEU A CB  
3189 C CG  . LEU A 404 ? 0.7328 0.7982 0.8112 -0.2082 -0.0412 -0.0584 700 LEU A CG  
3190 C CD1 . LEU A 404 ? 0.5443 0.6982 0.6557 -0.2130 -0.0426 -0.0600 700 LEU A CD1 
3191 C CD2 . LEU A 404 ? 0.8735 0.8929 0.9044 -0.2470 -0.0380 -0.0571 700 LEU A CD2 
3192 N N   . THR A 405 ? 0.8758 0.8036 0.8968 -0.1772 -0.0485 -0.0723 701 THR A N   
3193 C CA  . THR A 405 ? 0.8384 0.7562 0.8568 -0.1640 -0.0510 -0.0775 701 THR A CA  
3194 C C   . THR A 405 ? 0.8586 0.8205 0.8856 -0.1894 -0.0547 -0.0830 701 THR A C   
3195 O O   . THR A 405 ? 0.8862 0.8693 0.9051 -0.2231 -0.0548 -0.0835 701 THR A O   
3196 C CB  . THR A 405 ? 0.9107 0.7449 0.8730 -0.1586 -0.0494 -0.0802 701 THR A CB  
3197 O OG1 . THR A 405 ? 0.8769 0.7093 0.8460 -0.1303 -0.0503 -0.0828 701 THR A OG1 
3198 C CG2 . THR A 405 ? 0.8123 0.6039 0.7231 -0.1976 -0.0503 -0.0860 701 THR A CG2 
3199 N N   . PRO A 406 ? 0.8470 0.8327 0.8924 -0.1746 -0.0578 -0.0865 702 PRO A N   
3200 C CA  . PRO A 406 ? 0.8133 0.7933 0.8738 -0.1399 -0.0578 -0.0855 702 PRO A CA  
3201 C C   . PRO A 406 ? 0.7988 0.8043 0.8932 -0.1155 -0.0565 -0.0783 702 PRO A C   
3202 O O   . PRO A 406 ? 0.7528 0.7935 0.8668 -0.1207 -0.0566 -0.0752 702 PRO A O   
3203 C CB  . PRO A 406 ? 0.7444 0.7645 0.8202 -0.1422 -0.0621 -0.0900 702 PRO A CB  
3204 C CG  . PRO A 406 ? 0.7682 0.7892 0.8190 -0.1792 -0.0645 -0.0958 702 PRO A CG  
3205 C CD  . PRO A 406 ? 0.7567 0.7848 0.8054 -0.1992 -0.0621 -0.0919 702 PRO A CD  
3206 N N   . SER A 407 ? 0.7838 0.7743 0.8818 -0.0903 -0.0554 -0.0759 703 SER A N   
3207 C CA  . SER A 407 ? 0.7743 0.7781 0.8933 -0.0736 -0.0546 -0.0692 703 SER A CA  
3208 C C   . SER A 407 ? 0.7861 0.7987 0.9163 -0.0533 -0.0549 -0.0670 703 SER A C   
3209 O O   . SER A 407 ? 0.7630 0.7607 0.8790 -0.0459 -0.0539 -0.0699 703 SER A O   
3210 C CB  . SER A 407 ? 0.7580 0.7268 0.8575 -0.0712 -0.0516 -0.0659 703 SER A CB  
3211 O OG  . SER A 407 ? 0.8364 0.7676 0.9092 -0.0559 -0.0497 -0.0670 703 SER A OG  
3212 N N   . PHE A 408 ? 0.7703 0.8061 0.9213 -0.0461 -0.0562 -0.0619 704 PHE A N   
3213 C CA  . PHE A 408 ? 0.7378 0.7836 0.8959 -0.0336 -0.0563 -0.0580 704 PHE A CA  
3214 C C   . PHE A 408 ? 0.7238 0.7619 0.8775 -0.0242 -0.0545 -0.0538 704 PHE A C   
3215 O O   . PHE A 408 ? 0.7441 0.7751 0.8976 -0.0275 -0.0545 -0.0517 704 PHE A O   
3216 C CB  . PHE A 408 ? 0.6801 0.7454 0.8511 -0.0349 -0.0593 -0.0546 704 PHE A CB  
3217 C CG  . PHE A 408 ? 0.6232 0.6980 0.7945 -0.0368 -0.0613 -0.0576 704 PHE A CG  
3218 C CD1 . PHE A 408 ? 0.5430 0.6289 0.7168 -0.0390 -0.0633 -0.0593 704 PHE A CD1 
3219 C CD2 . PHE A 408 ? 0.6350 0.7133 0.8030 -0.0339 -0.0611 -0.0584 704 PHE A CD2 
3220 C CE1 . PHE A 408 ? 0.6276 0.7282 0.8000 -0.0366 -0.0658 -0.0617 704 PHE A CE1 
3221 C CE2 . PHE A 408 ? 0.5651 0.6519 0.7309 -0.0341 -0.0635 -0.0609 704 PHE A CE2 
3222 C CZ  . PHE A 408 ? 0.5916 0.6898 0.7594 -0.0346 -0.0662 -0.0625 704 PHE A CZ  
3223 N N   . GLU A 409 ? 0.6740 0.7176 0.8227 -0.0105 -0.0527 -0.0524 705 GLU A N   
3224 C CA  . GLU A 409 ? 0.6450 0.6885 0.7863 0.0044  -0.0512 -0.0485 705 GLU A CA  
3225 C C   . GLU A 409 ? 0.6885 0.7752 0.8441 0.0113  -0.0517 -0.0432 705 GLU A C   
3226 O O   . GLU A 409 ? 0.7292 0.8349 0.8895 0.0105  -0.0510 -0.0437 705 GLU A O   
3227 C CB  . GLU A 409 ? 0.7652 0.7720 0.8739 0.0207  -0.0477 -0.0520 705 GLU A CB  
3228 C CG  . GLU A 409 ? 0.9325 0.8896 1.0157 0.0077  -0.0471 -0.0565 705 GLU A CG  
3229 C CD  . GLU A 409 ? 1.1042 1.0548 1.1909 -0.0018 -0.0479 -0.0527 705 GLU A CD  
3230 O OE1 . GLU A 409 ? 1.1492 1.1222 1.2495 0.0080  -0.0489 -0.0470 705 GLU A OE1 
3231 O OE2 . GLU A 409 ? 1.1939 1.1210 1.2689 -0.0213 -0.0476 -0.0555 705 GLU A OE2 
3232 N N   . TYR A 410 ? 0.6085 0.7142 0.7696 0.0153  -0.0530 -0.0378 706 TYR A N   
3233 C CA  . TYR A 410 ? 0.5172 0.6740 0.6895 0.0189  -0.0537 -0.0321 706 TYR A CA  
3234 C C   . TYR A 410 ? 0.5595 0.7329 0.7205 0.0456  -0.0494 -0.0326 706 TYR A C   
3235 O O   . TYR A 410 ? 0.6653 0.8004 0.8020 0.0657  -0.0465 -0.0365 706 TYR A O   
3236 C CB  . TYR A 410 ? 0.5790 0.7553 0.7561 0.0187  -0.0567 -0.0267 706 TYR A CB  
3237 C CG  . TYR A 410 ? 0.6767 0.8491 0.8618 -0.0066 -0.0614 -0.0249 706 TYR A CG  
3238 C CD1 . TYR A 410 ? 0.7946 0.9488 0.9762 -0.0076 -0.0635 -0.0240 706 TYR A CD1 
3239 C CD2 . TYR A 410 ? 0.7739 0.9562 0.9627 -0.0281 -0.0638 -0.0237 706 TYR A CD2 
3240 C CE1 . TYR A 410 ? 0.7810 0.9273 0.9633 -0.0270 -0.0675 -0.0230 706 TYR A CE1 
3241 C CE2 . TYR A 410 ? 0.8880 1.0542 1.0715 -0.0478 -0.0682 -0.0224 706 TYR A CE2 
3242 C CZ  . TYR A 410 ? 0.9105 1.0598 1.0912 -0.0459 -0.0700 -0.0224 706 TYR A CZ  
3243 O OH  . TYR A 410 ? 1.0199 1.1486 1.1893 -0.0619 -0.0742 -0.0219 706 TYR A OH  
3244 N N   . GLN A 411 ? 0.5226 0.7521 0.6957 0.0456  -0.0487 -0.0284 707 GLN A N   
3245 C CA  . GLN A 411 ? 0.5478 0.8034 0.7097 0.0757  -0.0439 -0.0286 707 GLN A CA  
3246 C C   . GLN A 411 ? 0.5647 0.9050 0.7451 0.0740  -0.0442 -0.0208 707 GLN A C   
3247 O O   . GLN A 411 ? 0.6647 1.0312 0.8618 0.0406  -0.0478 -0.0167 707 GLN A O   
3248 C CB  . GLN A 411 ? 0.6393 0.8717 0.7916 0.0768  -0.0405 -0.0346 707 GLN A CB  
3249 C CG  . GLN A 411 ? 0.6507 0.9258 0.8212 0.0548  -0.0406 -0.0314 707 GLN A CG  
3250 C CD  . GLN A 411 ? 0.7622 1.0102 0.9224 0.0547  -0.0381 -0.0375 707 GLN A CD  
3251 O OE1 . GLN A 411 ? 0.8414 1.0614 0.9790 0.0791  -0.0345 -0.0434 707 GLN A OE1 
3252 N NE2 . GLN A 411 ? 0.6799 0.9305 0.8502 0.0278  -0.0403 -0.0361 707 GLN A NE2 
3253 N N   . PRO A 412 ? 0.6343 1.0186 0.8069 0.1088  -0.0406 -0.0184 708 PRO A N   
3254 C CA  . PRO A 412 ? 0.7208 1.2038 0.9132 0.1058  -0.0412 -0.0101 708 PRO A CA  
3255 C C   . PRO A 412 ? 0.7577 1.2833 0.9641 0.0782  -0.0394 -0.0078 708 PRO A C   
3256 O O   . PRO A 412 ? 0.8198 1.3108 1.0175 0.0799  -0.0358 -0.0127 708 PRO A O   
3257 C CB  . PRO A 412 ? 0.7690 1.2854 0.9435 0.1598  -0.0364 -0.0092 708 PRO A CB  
3258 C CG  . PRO A 412 ? 0.8173 1.2463 0.9574 0.1856  -0.0319 -0.0182 708 PRO A CG  
3259 C CD  . PRO A 412 ? 0.7431 1.0888 0.8822 0.1537  -0.0361 -0.0229 708 PRO A CD  
3260 N N   . ASP A 413 ? 0.7714 1.3705 0.9958 0.0491  -0.0425 0.0001  709 ASP A N   
3261 C CA  . ASP A 413 ? 0.8135 1.4579 1.0454 0.0191  -0.0405 0.0042  709 ASP A CA  
3262 C C   . ASP A 413 ? 0.8438 1.5378 1.0729 0.0545  -0.0322 0.0038  709 ASP A C   
3263 O O   . ASP A 413 ? 0.8092 1.5485 1.0355 0.0976  -0.0291 0.0047  709 ASP A O   
3264 C CB  . ASP A 413 ? 0.8679 1.5899 1.1123 -0.0200 -0.0452 0.0134  709 ASP A CB  
3265 C CG  . ASP A 413 ? 0.9305 1.5954 1.1688 -0.0585 -0.0534 0.0134  709 ASP A CG  
3266 O OD1 . ASP A 413 ? 0.9056 1.4859 1.1314 -0.0723 -0.0545 0.0086  709 ASP A OD1 
3267 O OD2 . ASP A 413 ? 0.9900 1.6970 1.2336 -0.0727 -0.0588 0.0180  709 ASP A OD2 
3268 N N   . PRO A 414 ? 0.9082 1.5939 1.1337 0.0410  -0.0283 0.0026  710 PRO A N   
3269 C CA  . PRO A 414 ? 0.9361 1.6586 1.1541 0.0787  -0.0197 0.0007  710 PRO A CA  
3270 C C   . PRO A 414 ? 0.9723 1.8227 1.2042 0.0883  -0.0156 0.0095  710 PRO A C   
3271 O O   . PRO A 414 ? 1.0850 1.9739 1.3074 0.1354  -0.0083 0.0079  710 PRO A O   
3272 C CB  . PRO A 414 ? 0.8634 1.5477 1.0753 0.0529  -0.0178 -0.0016 710 PRO A CB  
3273 C CG  . PRO A 414 ? 0.8848 1.4986 1.0964 0.0109  -0.0254 -0.0022 710 PRO A CG  
3274 C CD  . PRO A 414 ? 0.9296 1.5694 1.1520 -0.0056 -0.0314 0.0030  710 PRO A CD  
3275 N N   . TRP A 415 ? 0.8954 1.8149 1.1453 0.0453  -0.0200 0.0185  711 TRP A N   
3276 C CA  . TRP A 415 ? 0.8993 1.9248 1.1483 0.0465  -0.0153 0.0271  711 TRP A CA  
3277 C C   . TRP A 415 ? 0.8803 1.9369 1.1200 0.0888  -0.0152 0.0282  711 TRP A C   
3278 O O   . TRP A 415 ? 0.8762 2.0091 1.1029 0.1023  -0.0103 0.0340  711 TRP A O   
3279 C CB  . TRP A 415 ? 0.9083 1.9597 1.1544 -0.0227 -0.0189 0.0359  711 TRP A CB  
3280 C CG  . TRP A 415 ? 0.8566 1.8678 1.1046 -0.0574 -0.0287 0.0367  711 TRP A CG  
3281 C CD1 . TRP A 415 ? 0.8430 1.8874 1.0873 -0.0583 -0.0321 0.0405  711 TRP A CD1 
3282 C CD2 . TRP A 415 ? 0.8487 1.7786 1.0979 -0.0950 -0.0365 0.0335  711 TRP A CD2 
3283 N NE1 . TRP A 415 ? 0.7928 1.7795 1.0365 -0.0940 -0.0412 0.0396  711 TRP A NE1 
3284 C CE2 . TRP A 415 ? 0.8313 1.7456 1.0759 -0.1160 -0.0441 0.0353  711 TRP A CE2 
3285 C CE3 . TRP A 415 ? 0.8710 1.7217 1.1120 -0.1091 -0.0367 0.0289  711 TRP A CE3 
3286 C CZ2 . TRP A 415 ? 0.8199 1.6559 1.0573 -0.1509 -0.0528 0.0326  711 TRP A CZ2 
3287 C CZ3 . TRP A 415 ? 0.8579 1.6135 1.0822 -0.1392 -0.0439 0.0263  711 TRP A CZ3 
3288 C CH2 . TRP A 415 ? 0.8731 1.6240 1.0963 -0.1591 -0.0518 0.0281  711 TRP A CH2 
3289 N N   . ASN A 416 ? 0.8621 1.8638 1.1048 0.1105  -0.0208 0.0234  712 ASN A N   
3290 C CA  . ASN A 416 ? 0.9062 1.9234 1.1318 0.1615  -0.0196 0.0236  712 ASN A CA  
3291 C C   . ASN A 416 ? 0.9050 1.8860 1.1041 0.2284  -0.0128 0.0168  712 ASN A C   
3292 O O   . ASN A 416 ? 0.9491 1.9526 1.1196 0.2761  -0.0091 0.0181  712 ASN A O   
3293 C CB  . ASN A 416 ? 0.8716 1.8418 1.1045 0.1565  -0.0286 0.0222  712 ASN A CB  
3294 C CG  . ASN A 416 ? 0.8587 1.8346 1.1098 0.0886  -0.0364 0.0266  712 ASN A CG  
3295 O OD1 . ASN A 416 ? 0.9030 1.9342 1.1531 0.0488  -0.0350 0.0331  712 ASN A OD1 
3296 N ND2 . ASN A 416 ? 0.8008 1.7135 1.0614 0.0752  -0.0449 0.0229  712 ASN A ND2 
3297 N N   . THR A 417 ? 0.8755 1.7971 1.0768 0.2324  -0.0112 0.0092  713 THR A N   
3298 C CA  . THR A 417 ? 0.9505 1.8035 1.1146 0.2901  -0.0055 0.0004  713 THR A CA  
3299 C C   . THR A 417 ? 1.0225 1.9108 1.1723 0.3106  0.0037  -0.0008 713 THR A C   
3300 O O   . THR A 417 ? 1.1060 1.9535 1.2118 0.3660  0.0092  -0.0064 713 THR A O   
3301 C CB  . THR A 417 ? 0.9426 1.6551 1.0894 0.2676  -0.0089 -0.0090 713 THR A CB  
3302 O OG1 . THR A 417 ? 0.8914 1.5945 1.0688 0.2051  -0.0160 -0.0060 713 THR A OG1 
3303 C CG2 . THR A 417 ? 1.0029 1.6271 1.1126 0.3044  -0.0108 -0.0142 713 THR A CG2 
3304 N N   . HIS A 418 ? 1.0191 1.9695 1.1949 0.2652  0.0053  0.0045  714 HIS A N   
3305 C CA  . HIS A 418 ? 1.0498 2.0144 1.2153 0.2749  0.0133  0.0020  714 HIS A CA  
3306 C C   . HIS A 418 ? 1.1016 2.1325 1.2362 0.3138  0.0197  0.0067  714 HIS A C   
3307 O O   . HIS A 418 ? 1.0801 2.2023 1.2239 0.2900  0.0193  0.0168  714 HIS A O   
3308 C CB  . HIS A 418 ? 0.9869 1.9862 1.1849 0.2098  0.0121  0.0070  714 HIS A CB  
3309 C CG  . HIS A 418 ? 0.9464 1.9493 1.1357 0.2151  0.0199  0.0040  714 HIS A CG  
3310 N ND1 . HIS A 418 ? 0.9779 1.8938 1.1317 0.2561  0.0237  -0.0073 714 HIS A ND1 
3311 C CD2 . HIS A 418 ? 0.9382 2.0005 1.1363 0.1789  0.0238  0.0108  714 HIS A CD2 
3312 C CE1 . HIS A 418 ? 0.9760 1.9124 1.1260 0.2495  0.0300  -0.0076 714 HIS A CE1 
3313 N NE2 . HIS A 418 ? 0.9386 1.9706 1.1190 0.2048  0.0309  0.0037  714 HIS A NE2 
3314 N N   . VAL A 419 ? 1.1649 2.1462 1.2566 0.3728  0.0249  -0.0008 715 VAL A N   
3315 C CA  . VAL A 419 ? 1.2442 2.2813 1.3008 0.4133  0.0304  0.0027  715 VAL A CA  
3316 C C   . VAL A 419 ? 1.2409 2.3461 1.3197 0.3778  0.0346  0.0072  715 VAL A C   
3317 O O   . VAL A 419 ? 1.2011 2.2639 1.2738 0.3821  0.0392  0.0001  715 VAL A O   
3318 C CB  . VAL A 419 ? 1.2728 2.2190 1.2682 0.4803  0.0338  -0.0070 715 VAL A CB  
3319 C CG1 . VAL A 419 ? 1.2956 2.3002 1.2534 0.5214  0.0384  -0.0029 715 VAL A CG1 
3320 C CG2 . VAL A 419 ? 1.2515 2.1308 1.2157 0.5129  0.0294  -0.0093 715 VAL A CG2 
3321 N N   . TRP A 420 ? 1.3177 2.5254 1.4176 0.3406  0.0330  0.0188  716 TRP A N   
3322 C CA  . TRP A 420 ? 1.3440 2.6151 1.4661 0.2901  0.0351  0.0254  716 TRP A CA  
3323 C C   . TRP A 420 ? 1.4799 2.8206 1.5757 0.3220  0.0405  0.0291  716 TRP A C   
3324 O O   . TRP A 420 ? 1.4967 2.8489 1.5562 0.3826  0.0416  0.0283  716 TRP A O   
3325 C CB  . TRP A 420 ? 1.3247 2.6595 1.4722 0.2285  0.0294  0.0359  716 TRP A CB  
3326 C CG  . TRP A 420 ? 1.3024 2.6286 1.4749 0.1577  0.0279  0.0392  716 TRP A CG  
3327 C CD1 . TRP A 420 ? 1.3019 2.6310 1.4752 0.1393  0.0328  0.0394  716 TRP A CD1 
3328 C CD2 . TRP A 420 ? 1.2845 2.5886 1.4770 0.0970  0.0208  0.0429  716 TRP A CD2 
3329 N NE1 . TRP A 420 ? 1.2765 2.5850 1.4662 0.0706  0.0291  0.0436  716 TRP A NE1 
3330 C CE2 . TRP A 420 ? 1.2593 2.5489 1.4586 0.0439  0.0214  0.0456  716 TRP A CE2 
3331 C CE3 . TRP A 420 ? 1.2840 2.5749 1.4841 0.0832  0.0137  0.0442  716 TRP A CE3 
3332 C CZ2 . TRP A 420 ? 1.2554 2.5100 1.4622 -0.0207 0.0146  0.0496  716 TRP A CZ2 
3333 C CZ3 . TRP A 420 ? 1.2859 2.5465 1.4976 0.0190  0.0071  0.0476  716 TRP A CZ3 
3334 C CH2 . TRP A 420 ? 1.2833 2.5222 1.4951 -0.0317 0.0073  0.0503  716 TRP A CH2 
# 
