data_9CVN
# 
_entry.id   9CVN 
# 
_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   9CVN         pdb_00009cvn 10.2210/pdb9cvn/pdb 
WWPDB D_1000286177 ?            ?                   
# 
_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                        9CVN 
_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 nat 'PROTOPORPHYRIN IX CONTAINING FE'                                             616.487   1  ?          ?     ? ? 
3 non-polymer syn 5,6,7,8-TETRAHYDROBIOPTERIN                                                   241.247   1  ?          ?     ? ? 
4 non-polymer syn '(6M)-6-{2,3-difluoro-5-[(methylamino)methyl]phenyl}-4-methylpyridin-2-amine' 263.286   1  ?          ?     ? ? 
5 non-polymer syn 'ACETATE ION'                                                                 59.044    1  ?          ?     ? ? 
6 non-polymer syn 'ZINC ION'                                                                    65.409    1  ?          ?     ? ? 
7 water       nat water                                                                         18.015    30 ?          ?     ? ? 
# 
_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 '(6M)-6-{2,3-difluoro-5-[(methylamino)methyl]phenyl}-4-methylpyridin-2-amine' A1A0B 
5 'ACETATE ION'                                                                 ACT   
6 'ZINC ION'                                                                    ZN    
7 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 
A1A0B non-polymer         . '(6M)-6-{2,3-difluoro-5-[(methylamino)methyl]phenyl}-4-methylpyridin-2-amine' ?    'C14 H15 F2 N3'    
263.286 
ACT   non-polymer         . 'ACETATE ION'                                                                 ?    'C2 H3 O2 -1'      
59.044  
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 ?   ?   ?   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 422 718 718 GLY GLY A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1A0B 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1A0B 
_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 A1A0B 1  803 800 A1A0B 3V0 A . 
E 5 ACT   1  804 860 ACT   ACT A . 
F 6 ZN    1  805 900 ZN    ZN  A . 
G 7 HOH   1  901 26  HOH   HOH A . 
G 7 HOH   2  902 15  HOH   HOH A . 
G 7 HOH   3  903 20  HOH   HOH A . 
G 7 HOH   4  904 21  HOH   HOH A . 
G 7 HOH   5  905 13  HOH   HOH A . 
G 7 HOH   6  906 2   HOH   HOH A . 
G 7 HOH   7  907 29  HOH   HOH A . 
G 7 HOH   8  908 16  HOH   HOH A . 
G 7 HOH   9  909 19  HOH   HOH A . 
G 7 HOH   10 910 10  HOH   HOH A . 
G 7 HOH   11 911 6   HOH   HOH A . 
G 7 HOH   12 912 22  HOH   HOH A . 
G 7 HOH   13 913 14  HOH   HOH A . 
G 7 HOH   14 914 8   HOH   HOH A . 
G 7 HOH   15 915 17  HOH   HOH A . 
G 7 HOH   16 916 7   HOH   HOH A . 
G 7 HOH   17 917 18  HOH   HOH A . 
G 7 HOH   18 918 25  HOH   HOH A . 
G 7 HOH   19 919 23  HOH   HOH A . 
G 7 HOH   20 920 30  HOH   HOH A . 
G 7 HOH   21 921 5   HOH   HOH A . 
G 7 HOH   22 922 1   HOH   HOH A . 
G 7 HOH   23 923 27  HOH   HOH A . 
G 7 HOH   24 924 12  HOH   HOH A . 
G 7 HOH   25 925 9   HOH   HOH A . 
G 7 HOH   26 926 11  HOH   HOH A . 
G 7 HOH   27 927 28  HOH   HOH A . 
G 7 HOH   28 928 3   HOH   HOH A . 
G 7 HOH   29 929 4   HOH   HOH A . 
G 7 HOH   30 930 24  HOH   HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.11.1_2575 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           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                     9CVN 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.010 
_cell.length_a_esd                 ? 
_cell.length_b                     113.845 
_cell.length_b_esd                 ? 
_cell.length_c                     164.367 
_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                         9CVN 
_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                   9CVN 
_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                      mirrors 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-11-13 
_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   0.979 
_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                        'SSRL BEAMLINE BL12-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.979 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL12-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CVN 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.85 
_reflns.d_resolution_low                               39.48 
_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                                     39793 
_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                           99.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.096 
_reflns.pdbx_Rpim_I_all                                0.032 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       268272 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.090 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.85 
_reflns_shell.d_res_low                                     1.89 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           11908 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2297 
_reflns_shell.percent_possible_obs                          93.7 
_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                               5.2 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.1 
_reflns_shell.pdbx_Rrim_I_all                               7.248 
_reflns_shell.pdbx_Rpim_I_all                               3.087 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.375 
_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                                  6.526 
_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                                 9CVN 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.85 
_refine.ls_d_res_low                             39.48 
_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                     37605 
_refine.ls_number_reflns_R_free                  3635 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.74 
_refine.ls_percent_reflns_R_free                 5.10 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2181 
_refine.ls_R_factor_R_free                       0.2564 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2160 
_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                          0.04 
_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                 44.74 
_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                            0.27 
_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        3334 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         84 
_refine_hist.number_atoms_solvent             30 
_refine_hist.number_atoms_total               3448 
_refine_hist.d_res_high                       1.85 
_refine_hist.d_res_low                        39.48 
# 
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  ? 3525 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.044  ? 4796 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 18.938 ? 2047 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.050  ? 497  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.006  ? 605  ? 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' 1.850  1.8727 . . 117 2010 72.00  . . . . 0.4816 . . . . . . . . . . . 0.5285 
'X-RAY DIFFRACTION' 1.8727 1.8983 . . 112 2179 79.00  . . . . 0.4799 . . . . . . . . . . . 0.5852 
'X-RAY DIFFRACTION' 1.8983 1.9255 . . 107 2279 82.00  . . . . 0.4588 . . . . . . . . . . . 0.4684 
'X-RAY DIFFRACTION' 1.9255 1.9542 . . 128 2346 83.00  . . . . 0.4503 . . . . . . . . . . . 0.4890 
'X-RAY DIFFRACTION' 1.9542 1.9847 . . 164 2380 88.00  . . . . 0.4507 . . . . . . . . . . . 0.4377 
'X-RAY DIFFRACTION' 1.9847 2.0173 . . 121 2497 90.00  . . . . 0.4132 . . . . . . . . . . . 0.4481 
'X-RAY DIFFRACTION' 2.0173 2.0520 . . 128 2580 92.00  . . . . 0.3893 . . . . . . . . . . . 0.5383 
'X-RAY DIFFRACTION' 2.0520 2.0894 . . 93  2607 95.00  . . . . 0.3729 . . . . . . . . . . . 0.4070 
'X-RAY DIFFRACTION' 2.0894 2.1295 . . 191 2675 96.00  . . . . 0.3757 . . . . . . . . . . . 0.4014 
'X-RAY DIFFRACTION' 2.1295 2.1730 . . 148 2618 96.00  . . . . 0.3502 . . . . . . . . . . . 0.4561 
'X-RAY DIFFRACTION' 2.1730 2.2203 . . 127 2722 95.00  . . . . 0.3376 . . . . . . . . . . . 0.3612 
'X-RAY DIFFRACTION' 2.2203 2.2719 . . 172 2588 96.00  . . . . 0.3056 . . . . . . . . . . . 0.4005 
'X-RAY DIFFRACTION' 2.2719 2.3287 . . 133 2667 96.00  . . . . 0.2945 . . . . . . . . . . . 0.3516 
'X-RAY DIFFRACTION' 2.3287 2.3917 . . 148 2653 95.00  . . . . 0.2985 . . . . . . . . . . . 0.3819 
'X-RAY DIFFRACTION' 2.3917 2.4620 . . 132 2696 97.00  . . . . 0.2976 . . . . . . . . . . . 0.3530 
'X-RAY DIFFRACTION' 2.4620 2.5415 . . 125 2689 97.00  . . . . 0.2770 . . . . . . . . . . . 0.3951 
'X-RAY DIFFRACTION' 2.5415 2.6323 . . 125 2726 97.00  . . . . 0.2675 . . . . . . . . . . . 0.2951 
'X-RAY DIFFRACTION' 2.6323 2.7377 . . 146 2762 98.00  . . . . 0.2589 . . . . . . . . . . . 0.3442 
'X-RAY DIFFRACTION' 2.7377 2.8622 . . 137 2714 98.00  . . . . 0.2550 . . . . . . . . . . . 0.2744 
'X-RAY DIFFRACTION' 2.8622 3.0131 . . 119 2763 99.00  . . . . 0.2652 . . . . . . . . . . . 0.2959 
'X-RAY DIFFRACTION' 3.0131 3.2018 . . 158 2746 99.00  . . . . 0.2598 . . . . . . . . . . . 0.3164 
'X-RAY DIFFRACTION' 3.2018 3.4489 . . 180 2752 99.00  . . . . 0.2238 . . . . . . . . . . . 0.2615 
'X-RAY DIFFRACTION' 3.4489 3.7957 . . 151 2745 100.00 . . . . 0.1966 . . . . . . . . . . . 0.1961 
'X-RAY DIFFRACTION' 3.7957 4.3443 . . 161 2744 100.00 . . . . 0.1670 . . . . . . . . . . . 0.2233 
'X-RAY DIFFRACTION' 4.3443 5.4711 . . 162 2776 100.00 . . . . 0.1473 . . . . . . . . . . . 0.1827 
'X-RAY DIFFRACTION' 5.4711 39.480 . . 150 2768 100.00 . . . . 0.1495 . . . . . . . . . . . 0.1843 
# 
_struct.entry_id                     9CVN 
_struct.title                        
;Structure of rat neuronal nitric oxide synthase bound with 6-(2,3-difluoro-5-((methylamino)methyl)phenyl)-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        9CVN 
_struct_keywords.text            'nitric oxide synthase inhibitor binding, OXIDOREDUCTASE, OXIDOREDUCTASE-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
# 
_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              9CVN 
_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             9CVN 
_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_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 9820  ? 
1 MORE         -143  ? 
1 'SSA (A^2)'  33990 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z         1.0000000000  0.0000000000 0.0000000000 0.0000000000   0.0000000000 
1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 3_455 -x-1,y,-z+1/2 -1.0000000000 0.0000000000 0.0000000000 -49.0100000000 0.0000000000 
1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 82.1835000000 
# 
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  ? THR A 95  ? SER A 374 THR A 391 1 ? 18 
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 LYS A 324 ? SER A 327 ? LYS A 620 SER A 623 5 ? 4  
HELX_P HELX_P15 AB6 LEU A 328 ? SER A 347 ? LEU A 624 SER A 643 1 ? 20 
HELX_P HELX_P16 AB7 ASP A 354 ? GLY A 374 ? ASP A 650 GLY A 670 1 ? 21 
HELX_P HELX_P17 AB8 ASP A 379 ? VAL A 384 ? ASP A 675 VAL A 680 1 ? 6  
HELX_P HELX_P18 AB9 SER A 388 ? GLN A 397 ? SER A 684 GLN A 693 5 ? 10 
HELX_P HELX_P19 AC1 ASP A 413 ? THR A 417 ? ASP A 709 THR A 713 5 ? 5  
# 
_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 F ZN  . ZN ? ? A CYS 326 A ZN  805 1_555 ? ? ? ? ? ? ? 2.388 ? ? 
metalc2 metalc ? ? A CYS 30  SG ? ? ? 1_555 F ZN  . ZN ? ? A CYS 326 A ZN  805 3_455 ? ? ? ? ? ? ? 2.384 ? ? 
metalc3 metalc ? ? A CYS 35  SG ? ? ? 1_555 F ZN  . ZN ? ? A CYS 331 A ZN  805 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc4 metalc ? ? A CYS 35  SG ? ? ? 1_555 F ZN  . ZN ? ? A CYS 331 A ZN  805 3_455 ? ? ? ? ? ? ? 2.319 ? ? 
metalc5 metalc ? ? A CYS 119 SG ? ? ? 1_555 B HEM . FE ? ? A CYS 415 A HEM 801 1_555 ? ? ? ? ? ? ? 2.360 ? ? 
# 
_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 ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 30 ? A CYS 326 ? 1_555 0.0   ? 
2  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 112.6 ? 
3  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 112.6 ? 
4  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 112.6 ? 
5  SG ? A CYS 30  ? A CYS 326 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 1_555 SG ? A CYS 35 ? A CYS 331 ? 1_555 112.6 ? 
6  SG ? A CYS 35  ? A CYS 331 ? 1_555 ZN ? F ZN  . ? A ZN  805 ? 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_555 105.4 ? 
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_555 101.0 ? 
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 87.7  ? 
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 98.5  ? 
11 NA ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 NC ? B HEM .  ? A HEM 801 ? 1_555 155.7 ? 
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 83.4  ? 
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_555 106.7 ? 
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 90.0  ? 
15 NB ? B HEM .   ? A HEM 801 ? 1_555 FE ? B HEM . ? A HEM 801 ? 1_555 ND ? B HEM .  ? A HEM 801 ? 1_555 151.7 ? 
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 87.3  ? 
# 
_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       -5.55 
# 
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 GLU A 277 ? N GLU A 573 O SER A 407 ? O SER A 703 
AA7 1 2 N TYR A 292 ? N TYR A 588 O VAL A 353 ? O VAL A 649 
# 
_pdbx_entry_details.entry_id                   9CVN 
_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 THR A 321 ? ? -127.74 -54.12  
2  1 THR A 466 ? ? -118.43 -94.96  
3  1 SER A 491 ? ? -79.91  -159.95 
4  1 PRO A 513 ? ? -78.73  49.25   
5  1 ARG A 514 ? ? -28.09  72.57   
6  1 ARG A 516 ? ? -91.98  -82.36  
7  1 LYS A 550 ? ? -135.55 -43.39  
8  1 CYS A 582 ? ? -150.08 59.13   
9  1 ARG A 603 ? ? -111.06 -131.88 
10 1 ASP A 615 ? ? 52.13   78.24   
11 1 ASP A 617 ? ? -63.59  87.24   
12 1 VAL A 715 ? ? -58.73  95.34   
13 1 LYS A 717 ? ? -149.26 -104.67 
# 
_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     805 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   F 
_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         -23.6598 
_pdbx_refine_tls.origin_y         -4.8496 
_pdbx_refine_tls.origin_z         22.2991 
_pdbx_refine_tls.T[1][1]          0.4408 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0422 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0649 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.4644 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0012 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.5314 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.8629 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0069 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          0.5308 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.2247 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.0285 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          8.7657 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0486 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.1505 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0055 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.0068 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0701 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0579 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.9214 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.2978 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0690 
_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 ARG 299 ? A ARG 3  
4  1 Y 1 A GLN 340 ? A GLN 44 
5  1 Y 1 A HIS 341 ? A HIS 45 
6  1 Y 1 A THR 342 ? A THR 46 
7  1 Y 1 A ARG 343 ? A ARG 47 
8  1 Y 1 A LYS 344 ? A LYS 48 
9  1 Y 1 A PRO 345 ? A PRO 49 
10 1 Y 1 A GLU 346 ? A GLU 50 
11 1 Y 1 A ASP 347 ? A ASP 51 
# 
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 
A1A0B C11  C  Y N 1   
A1A0B C12  C  Y N 2   
A1A0B C13  C  Y N 3   
A1A0B C14  C  Y N 4   
A1A0B C15  C  Y N 5   
A1A0B C16  C  Y N 6   
A1A0B C17  C  N N 7   
A1A0B C02  C  Y N 8   
A1A0B C03  C  Y N 9   
A1A0B C04  C  Y N 10  
A1A0B C05  C  Y N 11  
A1A0B C06  C  Y N 12  
A1A0B C07  C  N N 13  
A1A0B C19  C  N N 14  
A1A0B F12  F  N N 15  
A1A0B F13  F  N N 16  
A1A0B N01  N  Y N 17  
A1A0B N02  N  N N 18  
A1A0B N18  N  N N 19  
A1A0B H1   H  N N 20  
A1A0B H2   H  N N 21  
A1A0B H3   H  N N 22  
A1A0B H4   H  N N 23  
A1A0B H5   H  N N 24  
A1A0B H6   H  N N 25  
A1A0B H7   H  N N 26  
A1A0B H8   H  N N 27  
A1A0B H9   H  N N 28  
A1A0B H10  H  N N 29  
A1A0B H11  H  N N 30  
A1A0B H12  H  N N 31  
A1A0B H13  H  N N 32  
A1A0B H14  H  N N 33  
A1A0B H15  H  N N 34  
ACT   C    C  N N 35  
ACT   O    O  N N 36  
ACT   OXT  O  N N 37  
ACT   CH3  C  N N 38  
ACT   H1   H  N N 39  
ACT   H2   H  N N 40  
ACT   H3   H  N N 41  
ALA   N    N  N N 42  
ALA   CA   C  N S 43  
ALA   C    C  N N 44  
ALA   O    O  N N 45  
ALA   CB   C  N N 46  
ALA   OXT  O  N N 47  
ALA   H    H  N N 48  
ALA   H2   H  N N 49  
ALA   HA   H  N N 50  
ALA   HB1  H  N N 51  
ALA   HB2  H  N N 52  
ALA   HB3  H  N N 53  
ALA   HXT  H  N N 54  
ARG   N    N  N N 55  
ARG   CA   C  N S 56  
ARG   C    C  N N 57  
ARG   O    O  N N 58  
ARG   CB   C  N N 59  
ARG   CG   C  N N 60  
ARG   CD   C  N N 61  
ARG   NE   N  N N 62  
ARG   CZ   C  N N 63  
ARG   NH1  N  N N 64  
ARG   NH2  N  N N 65  
ARG   OXT  O  N N 66  
ARG   H    H  N N 67  
ARG   H2   H  N N 68  
ARG   HA   H  N N 69  
ARG   HB2  H  N N 70  
ARG   HB3  H  N N 71  
ARG   HG2  H  N N 72  
ARG   HG3  H  N N 73  
ARG   HD2  H  N N 74  
ARG   HD3  H  N N 75  
ARG   HE   H  N N 76  
ARG   HH11 H  N N 77  
ARG   HH12 H  N N 78  
ARG   HH21 H  N N 79  
ARG   HH22 H  N N 80  
ARG   HXT  H  N N 81  
ASN   N    N  N N 82  
ASN   CA   C  N S 83  
ASN   C    C  N N 84  
ASN   O    O  N N 85  
ASN   CB   C  N N 86  
ASN   CG   C  N N 87  
ASN   OD1  O  N N 88  
ASN   ND2  N  N N 89  
ASN   OXT  O  N N 90  
ASN   H    H  N N 91  
ASN   H2   H  N N 92  
ASN   HA   H  N N 93  
ASN   HB2  H  N N 94  
ASN   HB3  H  N N 95  
ASN   HD21 H  N N 96  
ASN   HD22 H  N N 97  
ASN   HXT  H  N N 98  
ASP   N    N  N N 99  
ASP   CA   C  N S 100 
ASP   C    C  N N 101 
ASP   O    O  N N 102 
ASP   CB   C  N N 103 
ASP   CG   C  N N 104 
ASP   OD1  O  N N 105 
ASP   OD2  O  N N 106 
ASP   OXT  O  N N 107 
ASP   H    H  N N 108 
ASP   H2   H  N N 109 
ASP   HA   H  N N 110 
ASP   HB2  H  N N 111 
ASP   HB3  H  N N 112 
ASP   HD2  H  N N 113 
ASP   HXT  H  N N 114 
CYS   N    N  N N 115 
CYS   CA   C  N R 116 
CYS   C    C  N N 117 
CYS   O    O  N N 118 
CYS   CB   C  N N 119 
CYS   SG   S  N N 120 
CYS   OXT  O  N N 121 
CYS   H    H  N N 122 
CYS   H2   H  N N 123 
CYS   HA   H  N N 124 
CYS   HB2  H  N N 125 
CYS   HB3  H  N N 126 
CYS   HG   H  N N 127 
CYS   HXT  H  N N 128 
GLN   N    N  N N 129 
GLN   CA   C  N S 130 
GLN   C    C  N N 131 
GLN   O    O  N N 132 
GLN   CB   C  N N 133 
GLN   CG   C  N N 134 
GLN   CD   C  N N 135 
GLN   OE1  O  N N 136 
GLN   NE2  N  N N 137 
GLN   OXT  O  N N 138 
GLN   H    H  N N 139 
GLN   H2   H  N N 140 
GLN   HA   H  N N 141 
GLN   HB2  H  N N 142 
GLN   HB3  H  N N 143 
GLN   HG2  H  N N 144 
GLN   HG3  H  N N 145 
GLN   HE21 H  N N 146 
GLN   HE22 H  N N 147 
GLN   HXT  H  N N 148 
GLU   N    N  N N 149 
GLU   CA   C  N S 150 
GLU   C    C  N N 151 
GLU   O    O  N N 152 
GLU   CB   C  N N 153 
GLU   CG   C  N N 154 
GLU   CD   C  N N 155 
GLU   OE1  O  N N 156 
GLU   OE2  O  N N 157 
GLU   OXT  O  N N 158 
GLU   H    H  N N 159 
GLU   H2   H  N N 160 
GLU   HA   H  N N 161 
GLU   HB2  H  N N 162 
GLU   HB3  H  N N 163 
GLU   HG2  H  N N 164 
GLU   HG3  H  N N 165 
GLU   HE2  H  N N 166 
GLU   HXT  H  N N 167 
GLY   N    N  N N 168 
GLY   CA   C  N N 169 
GLY   C    C  N N 170 
GLY   O    O  N N 171 
GLY   OXT  O  N N 172 
GLY   H    H  N N 173 
GLY   H2   H  N N 174 
GLY   HA2  H  N N 175 
GLY   HA3  H  N N 176 
GLY   HXT  H  N N 177 
H4B   N1   N  Y N 178 
H4B   C2   C  Y N 179 
H4B   N2   N  N N 180 
H4B   N3   N  Y N 181 
H4B   C4   C  Y N 182 
H4B   O4   O  N N 183 
H4B   C4A  C  Y N 184 
H4B   C8A  C  Y N 185 
H4B   N5   N  N N 186 
H4B   N8   N  N N 187 
H4B   C6   C  N R 188 
H4B   C7   C  N N 189 
H4B   C9   C  N R 190 
H4B   O9   O  N N 191 
H4B   C10  C  N S 192 
H4B   C11  C  N N 193 
H4B   O10  O  N N 194 
H4B   HN21 H  N N 195 
H4B   HN22 H  N N 196 
H4B   HN3  H  N N 197 
H4B   HN5  H  N N 198 
H4B   HN8  H  N N 199 
H4B   H6   H  N N 200 
H4B   H71  H  N N 201 
H4B   H72  H  N N 202 
H4B   H9   H  N N 203 
H4B   HO9  H  N N 204 
H4B   H10  H  N N 205 
H4B   H111 H  N N 206 
H4B   H112 H  N N 207 
H4B   H113 H  N N 208 
H4B   HO0  H  N N 209 
HEM   CHA  C  N N 210 
HEM   CHB  C  N N 211 
HEM   CHC  C  N N 212 
HEM   CHD  C  N N 213 
HEM   C1A  C  Y N 214 
HEM   C2A  C  Y N 215 
HEM   C3A  C  Y N 216 
HEM   C4A  C  Y N 217 
HEM   CMA  C  N N 218 
HEM   CAA  C  N N 219 
HEM   CBA  C  N N 220 
HEM   CGA  C  N N 221 
HEM   O1A  O  N N 222 
HEM   O2A  O  N N 223 
HEM   C1B  C  N N 224 
HEM   C2B  C  N N 225 
HEM   C3B  C  N N 226 
HEM   C4B  C  N N 227 
HEM   CMB  C  N N 228 
HEM   CAB  C  N N 229 
HEM   CBB  C  N N 230 
HEM   C1C  C  Y N 231 
HEM   C2C  C  Y N 232 
HEM   C3C  C  Y N 233 
HEM   C4C  C  Y N 234 
HEM   CMC  C  N N 235 
HEM   CAC  C  N N 236 
HEM   CBC  C  N N 237 
HEM   C1D  C  N N 238 
HEM   C2D  C  N N 239 
HEM   C3D  C  N N 240 
HEM   C4D  C  N N 241 
HEM   CMD  C  N N 242 
HEM   CAD  C  N N 243 
HEM   CBD  C  N N 244 
HEM   CGD  C  N N 245 
HEM   O1D  O  N N 246 
HEM   O2D  O  N N 247 
HEM   NA   N  Y N 248 
HEM   NB   N  N N 249 
HEM   NC   N  Y N 250 
HEM   ND   N  N N 251 
HEM   FE   FE N N 252 
HEM   HHB  H  N N 253 
HEM   HHC  H  N N 254 
HEM   HHD  H  N N 255 
HEM   HMA  H  N N 256 
HEM   HMAA H  N N 257 
HEM   HMAB H  N N 258 
HEM   HAA  H  N N 259 
HEM   HAAA H  N N 260 
HEM   HBA  H  N N 261 
HEM   HBAA H  N N 262 
HEM   HMB  H  N N 263 
HEM   HMBA H  N N 264 
HEM   HMBB H  N N 265 
HEM   HAB  H  N N 266 
HEM   HBB  H  N N 267 
HEM   HBBA H  N N 268 
HEM   HMC  H  N N 269 
HEM   HMCA H  N N 270 
HEM   HMCB H  N N 271 
HEM   HAC  H  N N 272 
HEM   HBC  H  N N 273 
HEM   HBCA H  N N 274 
HEM   HMD  H  N N 275 
HEM   HMDA H  N N 276 
HEM   HMDB H  N N 277 
HEM   HAD  H  N N 278 
HEM   HADA H  N N 279 
HEM   HBD  H  N N 280 
HEM   HBDA H  N N 281 
HEM   H2A  H  N N 282 
HEM   H2D  H  N N 283 
HEM   HHA  H  N N 284 
HIS   N    N  N N 285 
HIS   CA   C  N S 286 
HIS   C    C  N N 287 
HIS   O    O  N N 288 
HIS   CB   C  N N 289 
HIS   CG   C  Y N 290 
HIS   ND1  N  Y N 291 
HIS   CD2  C  Y N 292 
HIS   CE1  C  Y N 293 
HIS   NE2  N  Y N 294 
HIS   OXT  O  N N 295 
HIS   H    H  N N 296 
HIS   H2   H  N N 297 
HIS   HA   H  N N 298 
HIS   HB2  H  N N 299 
HIS   HB3  H  N N 300 
HIS   HD1  H  N N 301 
HIS   HD2  H  N N 302 
HIS   HE1  H  N N 303 
HIS   HE2  H  N N 304 
HIS   HXT  H  N N 305 
HOH   O    O  N N 306 
HOH   H1   H  N N 307 
HOH   H2   H  N N 308 
ILE   N    N  N N 309 
ILE   CA   C  N S 310 
ILE   C    C  N N 311 
ILE   O    O  N N 312 
ILE   CB   C  N S 313 
ILE   CG1  C  N N 314 
ILE   CG2  C  N N 315 
ILE   CD1  C  N N 316 
ILE   OXT  O  N N 317 
ILE   H    H  N N 318 
ILE   H2   H  N N 319 
ILE   HA   H  N N 320 
ILE   HB   H  N N 321 
ILE   HG12 H  N N 322 
ILE   HG13 H  N N 323 
ILE   HG21 H  N N 324 
ILE   HG22 H  N N 325 
ILE   HG23 H  N N 326 
ILE   HD11 H  N N 327 
ILE   HD12 H  N N 328 
ILE   HD13 H  N N 329 
ILE   HXT  H  N N 330 
LEU   N    N  N N 331 
LEU   CA   C  N S 332 
LEU   C    C  N N 333 
LEU   O    O  N N 334 
LEU   CB   C  N N 335 
LEU   CG   C  N N 336 
LEU   CD1  C  N N 337 
LEU   CD2  C  N N 338 
LEU   OXT  O  N N 339 
LEU   H    H  N N 340 
LEU   H2   H  N N 341 
LEU   HA   H  N N 342 
LEU   HB2  H  N N 343 
LEU   HB3  H  N N 344 
LEU   HG   H  N N 345 
LEU   HD11 H  N N 346 
LEU   HD12 H  N N 347 
LEU   HD13 H  N N 348 
LEU   HD21 H  N N 349 
LEU   HD22 H  N N 350 
LEU   HD23 H  N N 351 
LEU   HXT  H  N N 352 
LYS   N    N  N N 353 
LYS   CA   C  N S 354 
LYS   C    C  N N 355 
LYS   O    O  N N 356 
LYS   CB   C  N N 357 
LYS   CG   C  N N 358 
LYS   CD   C  N N 359 
LYS   CE   C  N N 360 
LYS   NZ   N  N N 361 
LYS   OXT  O  N N 362 
LYS   H    H  N N 363 
LYS   H2   H  N N 364 
LYS   HA   H  N N 365 
LYS   HB2  H  N N 366 
LYS   HB3  H  N N 367 
LYS   HG2  H  N N 368 
LYS   HG3  H  N N 369 
LYS   HD2  H  N N 370 
LYS   HD3  H  N N 371 
LYS   HE2  H  N N 372 
LYS   HE3  H  N N 373 
LYS   HZ1  H  N N 374 
LYS   HZ2  H  N N 375 
LYS   HZ3  H  N N 376 
LYS   HXT  H  N N 377 
MET   N    N  N N 378 
MET   CA   C  N S 379 
MET   C    C  N N 380 
MET   O    O  N N 381 
MET   CB   C  N N 382 
MET   CG   C  N N 383 
MET   SD   S  N N 384 
MET   CE   C  N N 385 
MET   OXT  O  N N 386 
MET   H    H  N N 387 
MET   H2   H  N N 388 
MET   HA   H  N N 389 
MET   HB2  H  N N 390 
MET   HB3  H  N N 391 
MET   HG2  H  N N 392 
MET   HG3  H  N N 393 
MET   HE1  H  N N 394 
MET   HE2  H  N N 395 
MET   HE3  H  N N 396 
MET   HXT  H  N N 397 
PHE   N    N  N N 398 
PHE   CA   C  N S 399 
PHE   C    C  N N 400 
PHE   O    O  N N 401 
PHE   CB   C  N N 402 
PHE   CG   C  Y N 403 
PHE   CD1  C  Y N 404 
PHE   CD2  C  Y N 405 
PHE   CE1  C  Y N 406 
PHE   CE2  C  Y N 407 
PHE   CZ   C  Y N 408 
PHE   OXT  O  N N 409 
PHE   H    H  N N 410 
PHE   H2   H  N N 411 
PHE   HA   H  N N 412 
PHE   HB2  H  N N 413 
PHE   HB3  H  N N 414 
PHE   HD1  H  N N 415 
PHE   HD2  H  N N 416 
PHE   HE1  H  N N 417 
PHE   HE2  H  N N 418 
PHE   HZ   H  N N 419 
PHE   HXT  H  N N 420 
PRO   N    N  N N 421 
PRO   CA   C  N S 422 
PRO   C    C  N N 423 
PRO   O    O  N N 424 
PRO   CB   C  N N 425 
PRO   CG   C  N N 426 
PRO   CD   C  N N 427 
PRO   OXT  O  N N 428 
PRO   H    H  N N 429 
PRO   HA   H  N N 430 
PRO   HB2  H  N N 431 
PRO   HB3  H  N N 432 
PRO   HG2  H  N N 433 
PRO   HG3  H  N N 434 
PRO   HD2  H  N N 435 
PRO   HD3  H  N N 436 
PRO   HXT  H  N N 437 
SER   N    N  N N 438 
SER   CA   C  N S 439 
SER   C    C  N N 440 
SER   O    O  N N 441 
SER   CB   C  N N 442 
SER   OG   O  N N 443 
SER   OXT  O  N N 444 
SER   H    H  N N 445 
SER   H2   H  N N 446 
SER   HA   H  N N 447 
SER   HB2  H  N N 448 
SER   HB3  H  N N 449 
SER   HG   H  N N 450 
SER   HXT  H  N N 451 
THR   N    N  N N 452 
THR   CA   C  N S 453 
THR   C    C  N N 454 
THR   O    O  N N 455 
THR   CB   C  N R 456 
THR   OG1  O  N N 457 
THR   CG2  C  N N 458 
THR   OXT  O  N N 459 
THR   H    H  N N 460 
THR   H2   H  N N 461 
THR   HA   H  N N 462 
THR   HB   H  N N 463 
THR   HG1  H  N N 464 
THR   HG21 H  N N 465 
THR   HG22 H  N N 466 
THR   HG23 H  N N 467 
THR   HXT  H  N N 468 
TRP   N    N  N N 469 
TRP   CA   C  N S 470 
TRP   C    C  N N 471 
TRP   O    O  N N 472 
TRP   CB   C  N N 473 
TRP   CG   C  Y N 474 
TRP   CD1  C  Y N 475 
TRP   CD2  C  Y N 476 
TRP   NE1  N  Y N 477 
TRP   CE2  C  Y N 478 
TRP   CE3  C  Y N 479 
TRP   CZ2  C  Y N 480 
TRP   CZ3  C  Y N 481 
TRP   CH2  C  Y N 482 
TRP   OXT  O  N N 483 
TRP   H    H  N N 484 
TRP   H2   H  N N 485 
TRP   HA   H  N N 486 
TRP   HB2  H  N N 487 
TRP   HB3  H  N N 488 
TRP   HD1  H  N N 489 
TRP   HE1  H  N N 490 
TRP   HE3  H  N N 491 
TRP   HZ2  H  N N 492 
TRP   HZ3  H  N N 493 
TRP   HH2  H  N N 494 
TRP   HXT  H  N N 495 
TYR   N    N  N N 496 
TYR   CA   C  N S 497 
TYR   C    C  N N 498 
TYR   O    O  N N 499 
TYR   CB   C  N N 500 
TYR   CG   C  Y N 501 
TYR   CD1  C  Y N 502 
TYR   CD2  C  Y N 503 
TYR   CE1  C  Y N 504 
TYR   CE2  C  Y N 505 
TYR   CZ   C  Y N 506 
TYR   OH   O  N N 507 
TYR   OXT  O  N N 508 
TYR   H    H  N N 509 
TYR   H2   H  N N 510 
TYR   HA   H  N N 511 
TYR   HB2  H  N N 512 
TYR   HB3  H  N N 513 
TYR   HD1  H  N N 514 
TYR   HD2  H  N N 515 
TYR   HE1  H  N N 516 
TYR   HE2  H  N N 517 
TYR   HH   H  N N 518 
TYR   HXT  H  N N 519 
VAL   N    N  N N 520 
VAL   CA   C  N S 521 
VAL   C    C  N N 522 
VAL   O    O  N N 523 
VAL   CB   C  N N 524 
VAL   CG1  C  N N 525 
VAL   CG2  C  N N 526 
VAL   OXT  O  N N 527 
VAL   H    H  N N 528 
VAL   H2   H  N N 529 
VAL   HA   H  N N 530 
VAL   HB   H  N N 531 
VAL   HG11 H  N N 532 
VAL   HG12 H  N N 533 
VAL   HG13 H  N N 534 
VAL   HG21 H  N N 535 
VAL   HG22 H  N N 536 
VAL   HG23 H  N N 537 
VAL   HXT  H  N N 538 
ZN    ZN   ZN N N 539 
# 
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 
A1A0B C17 N18  sing N N 1   
A1A0B C17 C15  sing N N 2   
A1A0B N18 C19  sing N N 3   
A1A0B C07 C04  sing N N 4   
A1A0B C16 C15  doub Y N 5   
A1A0B C16 C11  sing Y N 6   
A1A0B C15 C14  sing Y N 7   
A1A0B C04 C05  doub Y N 8   
A1A0B C04 C03  sing Y N 9   
A1A0B C05 C06  sing Y N 10  
A1A0B C03 C02  doub Y N 11  
A1A0B C06 C11  sing N N 12  
A1A0B C06 N01  doub Y N 13  
A1A0B C11 C12  doub Y N 14  
A1A0B C14 C13  doub Y N 15  
A1A0B C02 N01  sing Y N 16  
A1A0B C02 N02  sing N N 17  
A1A0B C12 C13  sing Y N 18  
A1A0B C12 F12  sing N N 19  
A1A0B C13 F13  sing N N 20  
A1A0B C14 H1   sing N N 21  
A1A0B C16 H2   sing N N 22  
A1A0B C17 H3   sing N N 23  
A1A0B C17 H4   sing N N 24  
A1A0B C03 H5   sing N N 25  
A1A0B C05 H6   sing N N 26  
A1A0B C07 H7   sing N N 27  
A1A0B C07 H8   sing N N 28  
A1A0B C07 H9   sing N N 29  
A1A0B C19 H10  sing N N 30  
A1A0B C19 H11  sing N N 31  
A1A0B C19 H12  sing N N 32  
A1A0B N02 H13  sing N N 33  
A1A0B N02 H14  sing N N 34  
A1A0B N18 H15  sing N N 35  
ACT   C   O    doub N N 36  
ACT   C   OXT  sing N N 37  
ACT   C   CH3  sing N N 38  
ACT   CH3 H1   sing N N 39  
ACT   CH3 H2   sing N N 40  
ACT   CH3 H3   sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
GLN   N   CA   sing N N 124 
GLN   N   H    sing N N 125 
GLN   N   H2   sing N N 126 
GLN   CA  C    sing N N 127 
GLN   CA  CB   sing N N 128 
GLN   CA  HA   sing N N 129 
GLN   C   O    doub N N 130 
GLN   C   OXT  sing N N 131 
GLN   CB  CG   sing N N 132 
GLN   CB  HB2  sing N N 133 
GLN   CB  HB3  sing N N 134 
GLN   CG  CD   sing N N 135 
GLN   CG  HG2  sing N N 136 
GLN   CG  HG3  sing N N 137 
GLN   CD  OE1  doub N N 138 
GLN   CD  NE2  sing N N 139 
GLN   NE2 HE21 sing N N 140 
GLN   NE2 HE22 sing N N 141 
GLN   OXT HXT  sing N N 142 
GLU   N   CA   sing N N 143 
GLU   N   H    sing N N 144 
GLU   N   H2   sing N N 145 
GLU   CA  C    sing N N 146 
GLU   CA  CB   sing N N 147 
GLU   CA  HA   sing N N 148 
GLU   C   O    doub N N 149 
GLU   C   OXT  sing N N 150 
GLU   CB  CG   sing N N 151 
GLU   CB  HB2  sing N N 152 
GLU   CB  HB3  sing N N 153 
GLU   CG  CD   sing N N 154 
GLU   CG  HG2  sing N N 155 
GLU   CG  HG3  sing N N 156 
GLU   CD  OE1  doub N N 157 
GLU   CD  OE2  sing N N 158 
GLU   OE2 HE2  sing N N 159 
GLU   OXT HXT  sing N N 160 
GLY   N   CA   sing N N 161 
GLY   N   H    sing N N 162 
GLY   N   H2   sing N N 163 
GLY   CA  C    sing N N 164 
GLY   CA  HA2  sing N N 165 
GLY   CA  HA3  sing N N 166 
GLY   C   O    doub N N 167 
GLY   C   OXT  sing N N 168 
GLY   OXT HXT  sing N N 169 
H4B   N1  C2   doub Y N 170 
H4B   N1  C8A  sing Y N 171 
H4B   C2  N2   sing N N 172 
H4B   C2  N3   sing Y N 173 
H4B   N2  HN21 sing N N 174 
H4B   N2  HN22 sing N N 175 
H4B   N3  C4   sing Y N 176 
H4B   N3  HN3  sing N N 177 
H4B   C4  O4   doub N N 178 
H4B   C4  C4A  sing Y N 179 
H4B   C4A C8A  doub Y N 180 
H4B   C4A N5   sing N N 181 
H4B   C8A N8   sing N N 182 
H4B   N5  C6   sing N N 183 
H4B   N5  HN5  sing N N 184 
H4B   N8  C7   sing N N 185 
H4B   N8  HN8  sing N N 186 
H4B   C6  C7   sing N N 187 
H4B   C6  C9   sing N N 188 
H4B   C6  H6   sing N N 189 
H4B   C7  H71  sing N N 190 
H4B   C7  H72  sing N N 191 
H4B   C9  O9   sing N N 192 
H4B   C9  C10  sing N N 193 
H4B   C9  H9   sing N N 194 
H4B   O9  HO9  sing N N 195 
H4B   C10 C11  sing N N 196 
H4B   C10 O10  sing N N 197 
H4B   C10 H10  sing N N 198 
H4B   C11 H111 sing N N 199 
H4B   C11 H112 sing N N 200 
H4B   C11 H113 sing N N 201 
H4B   O10 HO0  sing N N 202 
HEM   CHA C1A  sing N N 203 
HEM   CHA C4D  doub N N 204 
HEM   CHA HHA  sing N N 205 
HEM   CHB C4A  sing N N 206 
HEM   CHB C1B  doub N N 207 
HEM   CHB HHB  sing N N 208 
HEM   CHC C4B  sing N N 209 
HEM   CHC C1C  doub N N 210 
HEM   CHC HHC  sing N N 211 
HEM   CHD C4C  doub N N 212 
HEM   CHD C1D  sing N N 213 
HEM   CHD HHD  sing N N 214 
HEM   C1A C2A  doub Y N 215 
HEM   C1A NA   sing Y N 216 
HEM   C2A C3A  sing Y N 217 
HEM   C2A CAA  sing N N 218 
HEM   C3A C4A  doub Y N 219 
HEM   C3A CMA  sing N N 220 
HEM   C4A NA   sing Y N 221 
HEM   CMA HMA  sing N N 222 
HEM   CMA HMAA sing N N 223 
HEM   CMA HMAB sing N N 224 
HEM   CAA CBA  sing N N 225 
HEM   CAA HAA  sing N N 226 
HEM   CAA HAAA sing N N 227 
HEM   CBA CGA  sing N N 228 
HEM   CBA HBA  sing N N 229 
HEM   CBA HBAA sing N N 230 
HEM   CGA O1A  doub N N 231 
HEM   CGA O2A  sing N N 232 
HEM   C1B C2B  sing N N 233 
HEM   C1B NB   sing N N 234 
HEM   C2B C3B  doub N N 235 
HEM   C2B CMB  sing N N 236 
HEM   C3B C4B  sing N N 237 
HEM   C3B CAB  sing N N 238 
HEM   C4B NB   doub N N 239 
HEM   CMB HMB  sing N N 240 
HEM   CMB HMBA sing N N 241 
HEM   CMB HMBB sing N N 242 
HEM   CAB CBB  doub N N 243 
HEM   CAB HAB  sing N N 244 
HEM   CBB HBB  sing N N 245 
HEM   CBB HBBA sing N N 246 
HEM   C1C C2C  sing Y N 247 
HEM   C1C NC   sing Y N 248 
HEM   C2C C3C  doub Y N 249 
HEM   C2C CMC  sing N N 250 
HEM   C3C C4C  sing Y N 251 
HEM   C3C CAC  sing N N 252 
HEM   C4C NC   sing Y N 253 
HEM   CMC HMC  sing N N 254 
HEM   CMC HMCA sing N N 255 
HEM   CMC HMCB sing N N 256 
HEM   CAC CBC  doub N N 257 
HEM   CAC HAC  sing N N 258 
HEM   CBC HBC  sing N N 259 
HEM   CBC HBCA sing N N 260 
HEM   C1D C2D  sing N N 261 
HEM   C1D ND   doub N N 262 
HEM   C2D C3D  doub N N 263 
HEM   C2D CMD  sing N N 264 
HEM   C3D C4D  sing N N 265 
HEM   C3D CAD  sing N N 266 
HEM   C4D ND   sing N N 267 
HEM   CMD HMD  sing N N 268 
HEM   CMD HMDA sing N N 269 
HEM   CMD HMDB sing N N 270 
HEM   CAD CBD  sing N N 271 
HEM   CAD HAD  sing N N 272 
HEM   CAD HADA sing N N 273 
HEM   CBD CGD  sing N N 274 
HEM   CBD HBD  sing N N 275 
HEM   CBD HBDA sing N N 276 
HEM   CGD O1D  doub N N 277 
HEM   CGD O2D  sing N N 278 
HEM   O2A H2A  sing N N 279 
HEM   O2D H2D  sing N N 280 
HEM   FE  NA   sing N N 281 
HEM   FE  NB   sing N N 282 
HEM   FE  NC   sing N N 283 
HEM   FE  ND   sing N N 284 
HIS   N   CA   sing N N 285 
HIS   N   H    sing N N 286 
HIS   N   H2   sing N N 287 
HIS   CA  C    sing N N 288 
HIS   CA  CB   sing N N 289 
HIS   CA  HA   sing N N 290 
HIS   C   O    doub N N 291 
HIS   C   OXT  sing N N 292 
HIS   CB  CG   sing N N 293 
HIS   CB  HB2  sing N N 294 
HIS   CB  HB3  sing N N 295 
HIS   CG  ND1  sing Y N 296 
HIS   CG  CD2  doub Y N 297 
HIS   ND1 CE1  doub Y N 298 
HIS   ND1 HD1  sing N N 299 
HIS   CD2 NE2  sing Y N 300 
HIS   CD2 HD2  sing N N 301 
HIS   CE1 NE2  sing Y N 302 
HIS   CE1 HE1  sing N N 303 
HIS   NE2 HE2  sing N N 304 
HIS   OXT HXT  sing N N 305 
HOH   O   H1   sing N N 306 
HOH   O   H2   sing N N 307 
ILE   N   CA   sing N N 308 
ILE   N   H    sing N N 309 
ILE   N   H2   sing N N 310 
ILE   CA  C    sing N N 311 
ILE   CA  CB   sing N N 312 
ILE   CA  HA   sing N N 313 
ILE   C   O    doub N N 314 
ILE   C   OXT  sing N N 315 
ILE   CB  CG1  sing N N 316 
ILE   CB  CG2  sing N N 317 
ILE   CB  HB   sing N N 318 
ILE   CG1 CD1  sing N N 319 
ILE   CG1 HG12 sing N N 320 
ILE   CG1 HG13 sing N N 321 
ILE   CG2 HG21 sing N N 322 
ILE   CG2 HG22 sing N N 323 
ILE   CG2 HG23 sing N N 324 
ILE   CD1 HD11 sing N N 325 
ILE   CD1 HD12 sing N N 326 
ILE   CD1 HD13 sing N N 327 
ILE   OXT HXT  sing N N 328 
LEU   N   CA   sing N N 329 
LEU   N   H    sing N N 330 
LEU   N   H2   sing N N 331 
LEU   CA  C    sing N N 332 
LEU   CA  CB   sing N N 333 
LEU   CA  HA   sing N N 334 
LEU   C   O    doub N N 335 
LEU   C   OXT  sing N N 336 
LEU   CB  CG   sing N N 337 
LEU   CB  HB2  sing N N 338 
LEU   CB  HB3  sing N N 339 
LEU   CG  CD1  sing N N 340 
LEU   CG  CD2  sing N N 341 
LEU   CG  HG   sing N N 342 
LEU   CD1 HD11 sing N N 343 
LEU   CD1 HD12 sing N N 344 
LEU   CD1 HD13 sing N N 345 
LEU   CD2 HD21 sing N N 346 
LEU   CD2 HD22 sing N N 347 
LEU   CD2 HD23 sing N N 348 
LEU   OXT HXT  sing N N 349 
LYS   N   CA   sing N N 350 
LYS   N   H    sing N N 351 
LYS   N   H2   sing N N 352 
LYS   CA  C    sing N N 353 
LYS   CA  CB   sing N N 354 
LYS   CA  HA   sing N N 355 
LYS   C   O    doub N N 356 
LYS   C   OXT  sing N N 357 
LYS   CB  CG   sing N N 358 
LYS   CB  HB2  sing N N 359 
LYS   CB  HB3  sing N N 360 
LYS   CG  CD   sing N N 361 
LYS   CG  HG2  sing N N 362 
LYS   CG  HG3  sing N N 363 
LYS   CD  CE   sing N N 364 
LYS   CD  HD2  sing N N 365 
LYS   CD  HD3  sing N N 366 
LYS   CE  NZ   sing N N 367 
LYS   CE  HE2  sing N N 368 
LYS   CE  HE3  sing N N 369 
LYS   NZ  HZ1  sing N N 370 
LYS   NZ  HZ2  sing N N 371 
LYS   NZ  HZ3  sing N N 372 
LYS   OXT HXT  sing N N 373 
MET   N   CA   sing N N 374 
MET   N   H    sing N N 375 
MET   N   H2   sing N N 376 
MET   CA  C    sing N N 377 
MET   CA  CB   sing N N 378 
MET   CA  HA   sing N N 379 
MET   C   O    doub N N 380 
MET   C   OXT  sing N N 381 
MET   CB  CG   sing N N 382 
MET   CB  HB2  sing N N 383 
MET   CB  HB3  sing N N 384 
MET   CG  SD   sing N N 385 
MET   CG  HG2  sing N N 386 
MET   CG  HG3  sing N N 387 
MET   SD  CE   sing N N 388 
MET   CE  HE1  sing N N 389 
MET   CE  HE2  sing N N 390 
MET   CE  HE3  sing N N 391 
MET   OXT HXT  sing N N 392 
PHE   N   CA   sing N N 393 
PHE   N   H    sing N N 394 
PHE   N   H2   sing N N 395 
PHE   CA  C    sing N N 396 
PHE   CA  CB   sing N N 397 
PHE   CA  HA   sing N N 398 
PHE   C   O    doub N N 399 
PHE   C   OXT  sing N N 400 
PHE   CB  CG   sing N N 401 
PHE   CB  HB2  sing N N 402 
PHE   CB  HB3  sing N N 403 
PHE   CG  CD1  doub Y N 404 
PHE   CG  CD2  sing Y N 405 
PHE   CD1 CE1  sing Y N 406 
PHE   CD1 HD1  sing N N 407 
PHE   CD2 CE2  doub Y N 408 
PHE   CD2 HD2  sing N N 409 
PHE   CE1 CZ   doub Y N 410 
PHE   CE1 HE1  sing N N 411 
PHE   CE2 CZ   sing Y N 412 
PHE   CE2 HE2  sing N N 413 
PHE   CZ  HZ   sing N N 414 
PHE   OXT HXT  sing N N 415 
PRO   N   CA   sing N N 416 
PRO   N   CD   sing N N 417 
PRO   N   H    sing N N 418 
PRO   CA  C    sing N N 419 
PRO   CA  CB   sing N N 420 
PRO   CA  HA   sing N N 421 
PRO   C   O    doub N N 422 
PRO   C   OXT  sing N N 423 
PRO   CB  CG   sing N N 424 
PRO   CB  HB2  sing N N 425 
PRO   CB  HB3  sing N N 426 
PRO   CG  CD   sing N N 427 
PRO   CG  HG2  sing N N 428 
PRO   CG  HG3  sing N N 429 
PRO   CD  HD2  sing N N 430 
PRO   CD  HD3  sing N N 431 
PRO   OXT HXT  sing N N 432 
SER   N   CA   sing N N 433 
SER   N   H    sing N N 434 
SER   N   H2   sing N N 435 
SER   CA  C    sing N N 436 
SER   CA  CB   sing N N 437 
SER   CA  HA   sing N N 438 
SER   C   O    doub N N 439 
SER   C   OXT  sing N N 440 
SER   CB  OG   sing N N 441 
SER   CB  HB2  sing N N 442 
SER   CB  HB3  sing N N 443 
SER   OG  HG   sing N N 444 
SER   OXT HXT  sing N N 445 
THR   N   CA   sing N N 446 
THR   N   H    sing N N 447 
THR   N   H2   sing N N 448 
THR   CA  C    sing N N 449 
THR   CA  CB   sing N N 450 
THR   CA  HA   sing N N 451 
THR   C   O    doub N N 452 
THR   C   OXT  sing N N 453 
THR   CB  OG1  sing N N 454 
THR   CB  CG2  sing N N 455 
THR   CB  HB   sing N N 456 
THR   OG1 HG1  sing N N 457 
THR   CG2 HG21 sing N N 458 
THR   CG2 HG22 sing N N 459 
THR   CG2 HG23 sing N N 460 
THR   OXT HXT  sing N N 461 
TRP   N   CA   sing N N 462 
TRP   N   H    sing N N 463 
TRP   N   H2   sing N N 464 
TRP   CA  C    sing N N 465 
TRP   CA  CB   sing N N 466 
TRP   CA  HA   sing N N 467 
TRP   C   O    doub N N 468 
TRP   C   OXT  sing N N 469 
TRP   CB  CG   sing N N 470 
TRP   CB  HB2  sing N N 471 
TRP   CB  HB3  sing N N 472 
TRP   CG  CD1  doub Y N 473 
TRP   CG  CD2  sing Y N 474 
TRP   CD1 NE1  sing Y N 475 
TRP   CD1 HD1  sing N N 476 
TRP   CD2 CE2  doub Y N 477 
TRP   CD2 CE3  sing Y N 478 
TRP   NE1 CE2  sing Y N 479 
TRP   NE1 HE1  sing N N 480 
TRP   CE2 CZ2  sing Y N 481 
TRP   CE3 CZ3  doub Y N 482 
TRP   CE3 HE3  sing N N 483 
TRP   CZ2 CH2  doub Y N 484 
TRP   CZ2 HZ2  sing N N 485 
TRP   CZ3 CH2  sing Y N 486 
TRP   CZ3 HZ3  sing N N 487 
TRP   CH2 HH2  sing N N 488 
TRP   OXT HXT  sing N N 489 
TYR   N   CA   sing N N 490 
TYR   N   H    sing N N 491 
TYR   N   H2   sing N N 492 
TYR   CA  C    sing N N 493 
TYR   CA  CB   sing N N 494 
TYR   CA  HA   sing N N 495 
TYR   C   O    doub N N 496 
TYR   C   OXT  sing N N 497 
TYR   CB  CG   sing N N 498 
TYR   CB  HB2  sing N N 499 
TYR   CB  HB3  sing N N 500 
TYR   CG  CD1  doub Y N 501 
TYR   CG  CD2  sing Y N 502 
TYR   CD1 CE1  sing Y N 503 
TYR   CD1 HD1  sing N N 504 
TYR   CD2 CE2  doub Y N 505 
TYR   CD2 HD2  sing N N 506 
TYR   CE1 CZ   doub Y N 507 
TYR   CE1 HE1  sing N N 508 
TYR   CE2 CZ   sing Y N 509 
TYR   CE2 HE2  sing N N 510 
TYR   CZ  OH   sing N N 511 
TYR   OH  HH   sing N N 512 
TYR   OXT HXT  sing N N 513 
VAL   N   CA   sing N N 514 
VAL   N   H    sing N N 515 
VAL   N   H2   sing N N 516 
VAL   CA  C    sing N N 517 
VAL   CA  CB   sing N N 518 
VAL   CA  HA   sing N N 519 
VAL   C   O    doub N N 520 
VAL   C   OXT  sing N N 521 
VAL   CB  CG1  sing N N 522 
VAL   CB  CG2  sing N N 523 
VAL   CB  HB   sing N N 524 
VAL   CG1 HG11 sing N N 525 
VAL   CG1 HG12 sing N N 526 
VAL   CG1 HG13 sing N N 527 
VAL   CG2 HG21 sing N N 528 
VAL   CG2 HG22 sing N N 529 
VAL   CG2 HG23 sing N N 530 
VAL   OXT HXT  sing N N 531 
# 
_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                    9CVN 
_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]   0.020404 
_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]   0.008784 
_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]   0.006084 
_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   . PHE   A 1 4   ? -39.933 -23.340 40.007 1.00 100.78 ? 300 PHE   A N   1 
ATOM   2    C  CA  . PHE   A 1 4   ? -40.802 -22.260 39.539 1.00 105.94 ? 300 PHE   A CA  1 
ATOM   3    C  C   . PHE   A 1 4   ? -40.574 -20.990 40.358 1.00 107.99 ? 300 PHE   A C   1 
ATOM   4    O  O   . PHE   A 1 4   ? -41.484 -20.517 41.035 1.00 111.77 ? 300 PHE   A O   1 
ATOM   5    C  CB  . PHE   A 1 4   ? -42.266 -22.680 39.623 1.00 110.30 ? 300 PHE   A CB  1 
ATOM   6    C  CG  . PHE   A 1 4   ? -42.469 -24.167 39.572 1.00 119.35 ? 300 PHE   A CG  1 
ATOM   7    C  CD1 . PHE   A 1 4   ? -42.515 -24.912 40.743 1.00 124.65 ? 300 PHE   A CD1 1 
ATOM   8    C  CD2 . PHE   A 1 4   ? -42.615 -24.821 38.357 1.00 124.88 ? 300 PHE   A CD2 1 
ATOM   9    C  CE1 . PHE   A 1 4   ? -42.704 -26.283 40.708 1.00 128.35 ? 300 PHE   A CE1 1 
ATOM   10   C  CE2 . PHE   A 1 4   ? -42.805 -26.194 38.317 1.00 129.95 ? 300 PHE   A CE2 1 
ATOM   11   C  CZ  . PHE   A 1 4   ? -42.850 -26.925 39.499 1.00 131.20 ? 300 PHE   A CZ  1 
ATOM   12   N  N   . LEU   A 1 5   ? -39.371 -20.424 40.248 1.00 101.84 ? 301 LEU   A N   1 
ATOM   13   C  CA  . LEU   A 1 5   ? -38.845 -19.469 41.221 1.00 92.81  ? 301 LEU   A CA  1 
ATOM   14   C  C   . LEU   A 1 5   ? -39.513 -18.101 41.121 1.00 89.37  ? 301 LEU   A C   1 
ATOM   15   O  O   . LEU   A 1 5   ? -40.106 -17.736 40.103 1.00 86.26  ? 301 LEU   A O   1 
ATOM   16   C  CB  . LEU   A 1 5   ? -37.344 -19.287 41.024 1.00 85.52  ? 301 LEU   A CB  1 
ATOM   17   C  CG  . LEU   A 1 5   ? -36.577 -20.574 40.751 1.00 87.16  ? 301 LEU   A CG  1 
ATOM   18   C  CD1 . LEU   A 1 5   ? -35.514 -20.290 39.714 1.00 88.19  ? 301 LEU   A CD1 1 
ATOM   19   C  CD2 . LEU   A 1 5   ? -35.971 -21.134 42.025 1.00 86.09  ? 301 LEU   A CD2 1 
ATOM   20   N  N   . LYS   A 1 6   ? -39.361 -17.318 42.192 1.00 87.20  ? 302 LYS   A N   1 
ATOM   21   C  CA  . LYS   A 1 6   ? -39.976 -16.003 42.313 1.00 86.96  ? 302 LYS   A CA  1 
ATOM   22   C  C   . LYS   A 1 6   ? -38.914 -14.917 42.430 1.00 81.15  ? 302 LYS   A C   1 
ATOM   23   O  O   . LYS   A 1 6   ? -37.880 -15.106 43.082 1.00 72.40  ? 302 LYS   A O   1 
ATOM   24   C  CB  . LYS   A 1 6   ? -40.900 -15.946 43.527 1.00 93.33  ? 302 LYS   A CB  1 
ATOM   25   C  CG  . LYS   A 1 6   ? -41.836 -17.136 43.646 1.00 104.72 ? 302 LYS   A CG  1 
ATOM   26   C  CD  . LYS   A 1 6   ? -43.191 -16.850 43.024 1.00 110.12 ? 302 LYS   A CD  1 
ATOM   27   C  CE  . LYS   A 1 6   ? -44.081 -18.089 43.055 1.00 115.42 ? 302 LYS   A CE  1 
ATOM   28   N  NZ  . LYS   A 1 6   ? -44.143 -18.705 44.411 1.00 118.52 ? 302 LYS   A NZ  1 
ATOM   29   N  N   . VAL   A 1 7   ? -39.178 -13.780 41.792 1.00 77.97  ? 303 VAL   A N   1 
ATOM   30   C  CA  . VAL   A 1 7   ? -38.339 -12.595 41.901 1.00 76.69  ? 303 VAL   A CA  1 
ATOM   31   C  C   . VAL   A 1 7   ? -39.212 -11.441 42.370 1.00 79.00  ? 303 VAL   A C   1 
ATOM   32   O  O   . VAL   A 1 7   ? -40.322 -11.242 41.860 1.00 80.84  ? 303 VAL   A O   1 
ATOM   33   C  CB  . VAL   A 1 7   ? -37.618 -12.262 40.577 1.00 73.96  ? 303 VAL   A CB  1 
ATOM   34   C  CG1 . VAL   A 1 7   ? -36.876 -13.480 40.080 1.00 71.50  ? 303 VAL   A CG1 1 
ATOM   35   C  CG2 . VAL   A 1 7   ? -38.567 -11.719 39.509 1.00 80.41  ? 303 VAL   A CG2 1 
ATOM   36   N  N   . LYS   A 1 8   ? -38.723 -10.710 43.367 1.00 67.22  ? 304 LYS   A N   1 
ATOM   37   C  CA  . LYS   A 1 8   ? -39.460 -9.626  43.992 1.00 66.90  ? 304 LYS   A CA  1 
ATOM   38   C  C   . LYS   A 1 8   ? -38.837 -8.292  43.608 1.00 69.10  ? 304 LYS   A C   1 
ATOM   39   O  O   . LYS   A 1 8   ? -37.638 -8.203  43.335 1.00 73.61  ? 304 LYS   A O   1 
ATOM   40   C  CB  . LYS   A 1 8   ? -39.474 -9.788  45.523 1.00 72.49  ? 304 LYS   A CB  1 
ATOM   41   C  CG  . LYS   A 1 8   ? -40.301 -8.749  46.281 1.00 80.48  ? 304 LYS   A CG  1 
ATOM   42   C  CD  . LYS   A 1 8   ? -40.455 -9.109  47.769 1.00 76.99  ? 304 LYS   A CD  1 
ATOM   43   C  CE  . LYS   A 1 8   ? -41.109 -7.984  48.585 1.00 84.83  ? 304 LYS   A CE  1 
ATOM   44   N  NZ  . LYS   A 1 8   ? -41.219 -8.330  50.048 1.00 87.60  ? 304 LYS   A NZ  1 
ATOM   45   N  N   . ASN   A 1 9   ? -39.667 -7.260  43.556 1.00 71.11  ? 305 ASN   A N   1 
ATOM   46   C  CA  . ASN   A 1 9   ? -39.195 -5.885  43.499 1.00 76.27  ? 305 ASN   A CA  1 
ATOM   47   C  C   . ASN   A 1 9   ? -39.350 -5.311  44.904 1.00 77.26  ? 305 ASN   A C   1 
ATOM   48   O  O   . ASN   A 1 9   ? -40.441 -5.362  45.476 1.00 83.47  ? 305 ASN   A O   1 
ATOM   49   C  CB  . ASN   A 1 9   ? -39.978 -5.071  42.462 1.00 79.77  ? 305 ASN   A CB  1 
ATOM   50   C  CG  . ASN   A 1 9   ? -39.475 -3.638  42.332 1.00 80.38  ? 305 ASN   A CG  1 
ATOM   51   O  OD1 . ASN   A 1 9   ? -39.431 -2.891  43.311 1.00 85.80  ? 305 ASN   A OD1 1 
ATOM   52   N  ND2 . ASN   A 1 9   ? -39.094 -3.246  41.111 1.00 75.53  ? 305 ASN   A ND2 1 
ATOM   53   N  N   . TRP   A 1 10  ? -38.254 -4.807  45.473 1.00 74.89  ? 306 TRP   A N   1 
ATOM   54   C  CA  . TRP   A 1 10  ? -38.260 -4.287  46.837 1.00 82.90  ? 306 TRP   A CA  1 
ATOM   55   C  C   . TRP   A 1 10  ? -38.529 -2.787  46.902 1.00 90.11  ? 306 TRP   A C   1 
ATOM   56   O  O   . TRP   A 1 10  ? -38.182 -2.144  47.899 1.00 99.36  ? 306 TRP   A O   1 
ATOM   57   C  CB  . TRP   A 1 10  ? -36.935 -4.613  47.530 1.00 82.59  ? 306 TRP   A CB  1 
ATOM   58   C  CG  . TRP   A 1 10  ? -36.738 -6.072  47.731 1.00 78.60  ? 306 TRP   A CG  1 
ATOM   59   C  CD1 . TRP   A 1 10  ? -36.076 -6.926  46.907 1.00 72.74  ? 306 TRP   A CD1 1 
ATOM   60   C  CD2 . TRP   A 1 10  ? -37.218 -6.857  48.822 1.00 78.02  ? 306 TRP   A CD2 1 
ATOM   61   N  NE1 . TRP   A 1 10  ? -36.113 -8.198  47.412 1.00 66.59  ? 306 TRP   A NE1 1 
ATOM   62   C  CE2 . TRP   A 1 10  ? -36.803 -8.183  48.594 1.00 78.41  ? 306 TRP   A CE2 1 
ATOM   63   C  CE3 . TRP   A 1 10  ? -37.957 -6.571  49.968 1.00 77.43  ? 306 TRP   A CE3 1 
ATOM   64   C  CZ2 . TRP   A 1 10  ? -37.099 -9.219  49.473 1.00 74.87  ? 306 TRP   A CZ2 1 
ATOM   65   C  CZ3 . TRP   A 1 10  ? -38.254 -7.600  50.837 1.00 80.90  ? 306 TRP   A CZ3 1 
ATOM   66   C  CH2 . TRP   A 1 10  ? -37.827 -8.910  50.582 1.00 80.42  ? 306 TRP   A CH2 1 
ATOM   67   N  N   . GLU   A 1 11  ? -39.115 -2.213  45.858 1.00 97.06  ? 307 GLU   A N   1 
ATOM   68   C  CA  . GLU   A 1 11  ? -39.625 -0.849  45.881 1.00 98.39  ? 307 GLU   A CA  1 
ATOM   69   C  C   . GLU   A 1 11  ? -41.135 -0.794  45.717 1.00 104.97 ? 307 GLU   A C   1 
ATOM   70   O  O   . GLU   A 1 11  ? -41.780 0.059   46.342 1.00 105.66 ? 307 GLU   A O   1 
ATOM   71   C  CB  . GLU   A 1 11  ? -38.954 -0.005  44.777 1.00 90.41  ? 307 GLU   A CB  1 
ATOM   72   C  CG  . GLU   A 1 11  ? -39.181 1.518   44.830 1.00 90.98  ? 307 GLU   A CG  1 
ATOM   73   C  CD  . GLU   A 1 11  ? -39.067 2.171   43.436 1.00 96.56  ? 307 GLU   A CD  1 
ATOM   74   O  OE1 . GLU   A 1 11  ? -39.844 3.112   43.143 1.00 97.64  ? 307 GLU   A OE1 1 
ATOM   75   O  OE2 . GLU   A 1 11  ? -38.209 1.738   42.635 1.00 92.79  ? 307 GLU   A OE2 1 
ATOM   76   N  N   . THR   A 1 12  ? -41.715 -1.710  44.932 1.00 98.27  ? 308 THR   A N   1 
ATOM   77   C  CA  . THR   A 1 12  ? -43.151 -1.795  44.693 1.00 100.95 ? 308 THR   A CA  1 
ATOM   78   C  C   . THR   A 1 12  ? -43.805 -3.028  45.306 1.00 102.54 ? 308 THR   A C   1 
ATOM   79   O  O   . THR   A 1 12  ? -45.029 -3.171  45.208 1.00 106.55 ? 308 THR   A O   1 
ATOM   80   C  CB  . THR   A 1 12  ? -43.427 -1.810  43.192 1.00 96.69  ? 308 THR   A CB  1 
ATOM   81   O  OG1 . THR   A 1 12  ? -42.927 -3.040  42.651 1.00 88.67  ? 308 THR   A OG1 1 
ATOM   82   C  CG2 . THR   A 1 12  ? -42.725 -0.651  42.520 1.00 102.39 ? 308 THR   A CG2 1 
ATOM   83   N  N   . ASP   A 1 13  ? -43.026 -3.939  45.888 1.00 102.51 ? 309 ASP   A N   1 
ATOM   84   C  CA  . ASP   A 1 13  ? -43.516 -5.196  46.457 1.00 110.64 ? 309 ASP   A CA  1 
ATOM   85   C  C   . ASP   A 1 13  ? -44.101 -6.131  45.397 1.00 106.80 ? 309 ASP   A C   1 
ATOM   86   O  O   . ASP   A 1 13  ? -44.825 -7.072  45.732 1.00 113.39 ? 309 ASP   A O   1 
ATOM   87   C  CB  . ASP   A 1 13  ? -44.545 -4.947  47.573 1.00 122.86 ? 309 ASP   A CB  1 
ATOM   88   C  CG  . ASP   A 1 13  ? -43.919 -4.369  48.839 1.00 128.42 ? 309 ASP   A CG  1 
ATOM   89   O  OD1 . ASP   A 1 13  ? -43.150 -5.094  49.505 1.00 129.28 ? 309 ASP   A OD1 1 
ATOM   90   O  OD2 . ASP   A 1 13  ? -44.188 -3.190  49.166 1.00 130.89 ? 309 ASP   A OD2 1 
ATOM   91   N  N   . VAL   A 1 14  ? -43.795 -5.908  44.120 1.00 102.21 ? 310 VAL   A N   1 
ATOM   92   C  CA  . VAL   A 1 14  ? -44.324 -6.750  43.049 1.00 98.96  ? 310 VAL   A CA  1 
ATOM   93   C  C   . VAL   A 1 14  ? -43.536 -8.051  42.985 1.00 98.78  ? 310 VAL   A C   1 
ATOM   94   O  O   . VAL   A 1 14  ? -42.301 -8.055  43.070 1.00 101.45 ? 310 VAL   A O   1 
ATOM   95   C  CB  . VAL   A 1 14  ? -44.276 -6.017  41.696 1.00 90.30  ? 310 VAL   A CB  1 
ATOM   96   C  CG1 . VAL   A 1 14  ? -44.457 -7.007  40.571 1.00 85.96  ? 310 VAL   A CG1 1 
ATOM   97   C  CG2 . VAL   A 1 14  ? -45.351 -4.952  41.619 1.00 90.99  ? 310 VAL   A CG2 1 
ATOM   98   N  N   . VAL   A 1 15  ? -44.244 -9.165  42.818 1.00 99.00  ? 311 VAL   A N   1 
ATOM   99   C  CA  . VAL   A 1 15  ? -43.611 -10.460 42.619 1.00 96.37  ? 311 VAL   A CA  1 
ATOM   100  C  C   . VAL   A 1 15  ? -43.998 -10.998 41.249 1.00 93.74  ? 311 VAL   A C   1 
ATOM   101  O  O   . VAL   A 1 15  ? -45.137 -10.831 40.796 1.00 100.34 ? 311 VAL   A O   1 
ATOM   102  C  CB  . VAL   A 1 15  ? -43.992 -11.459 43.726 1.00 95.67  ? 311 VAL   A CB  1 
ATOM   103  C  CG1 . VAL   A 1 15  ? -43.301 -12.794 43.490 1.00 93.84  ? 311 VAL   A CG1 1 
ATOM   104  C  CG2 . VAL   A 1 15  ? -43.608 -10.893 45.080 1.00 97.76  ? 311 VAL   A CG2 1 
ATOM   105  N  N   . LEU   A 1 16  ? -43.038 -11.627 40.582 1.00 83.45  ? 312 LEU   A N   1 
ATOM   106  C  CA  . LEU   A 1 16  ? -43.285 -12.332 39.335 1.00 90.46  ? 312 LEU   A CA  1 
ATOM   107  C  C   . LEU   A 1 16  ? -42.669 -13.718 39.438 1.00 85.35  ? 312 LEU   A C   1 
ATOM   108  O  O   . LEU   A 1 16  ? -41.703 -13.925 40.180 1.00 78.85  ? 312 LEU   A O   1 
ATOM   109  C  CB  . LEU   A 1 16  ? -42.713 -11.565 38.139 1.00 84.82  ? 312 LEU   A CB  1 
ATOM   110  C  CG  . LEU   A 1 16  ? -43.311 -10.169 37.994 1.00 93.02  ? 312 LEU   A CG  1 
ATOM   111  C  CD1 . LEU   A 1 16  ? -42.251 -9.217  37.504 1.00 92.39  ? 312 LEU   A CD1 1 
ATOM   112  C  CD2 . LEU   A 1 16  ? -44.509 -10.189 37.054 1.00 105.36 ? 312 LEU   A CD2 1 
ATOM   113  N  N   . THR   A 1 17  ? -43.237 -14.667 38.698 1.00 80.22  ? 313 THR   A N   1 
ATOM   114  C  CA  . THR   A 1 17  ? -42.840 -16.067 38.772 1.00 78.32  ? 313 THR   A CA  1 
ATOM   115  C  C   . THR   A 1 17  ? -42.140 -16.480 37.487 1.00 84.13  ? 313 THR   A C   1 
ATOM   116  O  O   . THR   A 1 17  ? -42.686 -16.302 36.392 1.00 92.62  ? 313 THR   A O   1 
ATOM   117  C  CB  . THR   A 1 17  ? -44.047 -16.970 39.012 1.00 85.61  ? 313 THR   A CB  1 
ATOM   118  O  OG1 . THR   A 1 17  ? -44.703 -16.577 40.227 1.00 85.03  ? 313 THR   A OG1 1 
ATOM   119  C  CG2 . THR   A 1 17  ? -43.603 -18.432 39.118 1.00 88.21  ? 313 THR   A CG2 1 
ATOM   120  N  N   . ASP   A 1 18  ? -40.947 -17.057 37.625 1.00 74.84  ? 314 ASP   A N   1 
ATOM   121  C  CA  . ASP   A 1 18  ? -40.085 -17.381 36.489 1.00 81.92  ? 314 ASP   A CA  1 
ATOM   122  C  C   . ASP   A 1 18  ? -40.121 -18.883 36.249 1.00 81.33  ? 314 ASP   A C   1 
ATOM   123  O  O   . ASP   A 1 18  ? -39.670 -19.656 37.098 1.00 78.98  ? 314 ASP   A O   1 
ATOM   124  C  CB  . ASP   A 1 18  ? -38.651 -16.912 36.750 1.00 75.44  ? 314 ASP   A CB  1 
ATOM   125  C  CG  . ASP   A 1 18  ? -37.779 -16.940 35.495 1.00 72.97  ? 314 ASP   A CG  1 
ATOM   126  O  OD1 . ASP   A 1 18  ? -37.462 -18.049 35.022 1.00 71.21  ? 314 ASP   A OD1 1 
ATOM   127  O  OD2 . ASP   A 1 18  ? -37.404 -15.855 34.991 1.00 73.37  ? 314 ASP   A OD2 1 
ATOM   128  N  N   . THR   A 1 19  ? -40.665 -19.300 35.104 1.00 81.09  ? 315 THR   A N   1 
ATOM   129  C  CA  . THR   A 1 19  ? -40.483 -20.673 34.651 1.00 78.35  ? 315 THR   A CA  1 
ATOM   130  C  C   . THR   A 1 19  ? -39.657 -20.774 33.378 1.00 81.80  ? 315 THR   A C   1 
ATOM   131  O  O   . THR   A 1 19  ? -39.234 -21.881 33.028 1.00 77.23  ? 315 THR   A O   1 
ATOM   132  C  CB  . THR   A 1 19  ? -41.830 -21.372 34.429 1.00 87.22  ? 315 THR   A CB  1 
ATOM   133  O  OG1 . THR   A 1 19  ? -42.685 -20.545 33.632 1.00 86.13  ? 315 THR   A OG1 1 
ATOM   134  C  CG2 . THR   A 1 19  ? -42.503 -21.678 35.768 1.00 87.98  ? 315 THR   A CG2 1 
ATOM   135  N  N   . LEU   A 1 20  ? -39.392 -19.651 32.703 1.00 74.25  ? 316 LEU   A N   1 
ATOM   136  C  CA  . LEU   A 1 20  ? -38.586 -19.670 31.488 1.00 80.60  ? 316 LEU   A CA  1 
ATOM   137  C  C   . LEU   A 1 20  ? -37.196 -20.242 31.746 1.00 79.96  ? 316 LEU   A C   1 
ATOM   138  O  O   . LEU   A 1 20  ? -36.580 -20.814 30.833 1.00 73.82  ? 316 LEU   A O   1 
ATOM   139  C  CB  . LEU   A 1 20  ? -38.488 -18.255 30.913 1.00 72.28  ? 316 LEU   A CB  1 
ATOM   140  C  CG  . LEU   A 1 20  ? -37.834 -18.141 29.537 1.00 70.58  ? 316 LEU   A CG  1 
ATOM   141  C  CD1 . LEU   A 1 20  ? -38.671 -18.881 28.507 1.00 70.75  ? 316 LEU   A CD1 1 
ATOM   142  C  CD2 . LEU   A 1 20  ? -37.659 -16.683 29.161 1.00 65.44  ? 316 LEU   A CD2 1 
ATOM   143  N  N   . HIS   A 1 21  ? -36.700 -20.108 32.982 1.00 72.06  ? 317 HIS   A N   1 
ATOM   144  C  CA  . HIS   A 1 21  ? -35.386 -20.622 33.356 1.00 66.63  ? 317 HIS   A CA  1 
ATOM   145  C  C   . HIS   A 1 21  ? -35.288 -22.130 33.181 1.00 67.17  ? 317 HIS   A C   1 
ATOM   146  O  O   . HIS   A 1 21  ? -34.175 -22.658 33.071 1.00 68.23  ? 317 HIS   A O   1 
ATOM   147  C  CB  . HIS   A 1 21  ? -35.066 -20.232 34.814 1.00 67.44  ? 317 HIS   A CB  1 
ATOM   148  C  CG  . HIS   A 1 21  ? -35.837 -21.004 35.842 1.00 68.92  ? 317 HIS   A CG  1 
ATOM   149  N  ND1 . HIS   A 1 21  ? -37.048 -20.578 36.346 1.00 73.28  ? 317 HIS   A ND1 1 
ATOM   150  C  CD2 . HIS   A 1 21  ? -35.558 -22.169 36.474 1.00 73.63  ? 317 HIS   A CD2 1 
ATOM   151  C  CE1 . HIS   A 1 21  ? -37.487 -21.454 37.234 1.00 77.91  ? 317 HIS   A CE1 1 
ATOM   152  N  NE2 . HIS   A 1 21  ? -36.603 -22.431 37.328 1.00 75.39  ? 317 HIS   A NE2 1 
ATOM   153  N  N   . LEU   A 1 22  ? -36.427 -22.830 33.145 1.00 68.89  ? 318 LEU   A N   1 
ATOM   154  C  CA  . LEU   A 1 22  ? -36.415 -24.269 32.911 1.00 80.45  ? 318 LEU   A CA  1 
ATOM   155  C  C   . LEU   A 1 22  ? -35.951 -24.606 31.494 1.00 81.43  ? 318 LEU   A C   1 
ATOM   156  O  O   . LEU   A 1 22  ? -35.377 -25.680 31.266 1.00 76.60  ? 318 LEU   A O   1 
ATOM   157  C  CB  . LEU   A 1 22  ? -37.807 -24.849 33.180 1.00 88.34  ? 318 LEU   A CB  1 
ATOM   158  C  CG  . LEU   A 1 22  ? -38.326 -24.613 34.604 1.00 88.16  ? 318 LEU   A CG  1 
ATOM   159  C  CD1 . LEU   A 1 22  ? -39.785 -25.030 34.771 1.00 94.26  ? 318 LEU   A CD1 1 
ATOM   160  C  CD2 . LEU   A 1 22  ? -37.435 -25.318 35.619 1.00 84.94  ? 318 LEU   A CD2 1 
ATOM   161  N  N   . LYS   A 1 23  ? -36.180 -23.708 30.535 1.00 88.51  ? 319 LYS   A N   1 
ATOM   162  C  CA  . LYS   A 1 23  ? -35.668 -23.931 29.185 1.00 92.02  ? 319 LYS   A CA  1 
ATOM   163  C  C   . LYS   A 1 23  ? -34.191 -23.582 29.069 1.00 94.01  ? 319 LYS   A C   1 
ATOM   164  O  O   . LYS   A 1 23  ? -33.606 -23.791 28.000 1.00 100.59 ? 319 LYS   A O   1 
ATOM   165  C  CB  . LYS   A 1 23  ? -36.468 -23.124 28.146 1.00 84.24  ? 319 LYS   A CB  1 
ATOM   166  C  CG  . LYS   A 1 23  ? -37.993 -23.278 28.210 1.00 86.23  ? 319 LYS   A CG  1 
ATOM   167  C  CD  . LYS   A 1 23  ? -38.450 -24.725 28.064 1.00 99.69  ? 319 LYS   A CD  1 
ATOM   168  C  CE  . LYS   A 1 23  ? -38.813 -25.072 26.628 1.00 107.90 ? 319 LYS   A CE  1 
ATOM   169  N  NZ  . LYS   A 1 23  ? -40.032 -24.348 26.163 1.00 113.71 ? 319 LYS   A NZ  1 
ATOM   170  N  N   . SER   A 1 24  ? -33.582 -23.062 30.136 1.00 80.33  ? 320 SER   A N   1 
ATOM   171  C  CA  . SER   A 1 24  ? -32.169 -22.708 30.106 1.00 80.83  ? 320 SER   A CA  1 
ATOM   172  C  C   . SER   A 1 24  ? -31.311 -23.943 29.885 1.00 90.83  ? 320 SER   A C   1 
ATOM   173  O  O   . SER   A 1 24  ? -31.640 -25.051 30.320 1.00 87.33  ? 320 SER   A O   1 
ATOM   174  C  CB  . SER   A 1 24  ? -31.741 -22.023 31.402 1.00 83.47  ? 320 SER   A CB  1 
ATOM   175  O  OG  . SER   A 1 24  ? -30.328 -22.007 31.504 1.00 89.23  ? 320 SER   A OG  1 
ATOM   176  N  N   . THR   A 1 25  ? -30.182 -23.732 29.217 1.00 107.57 ? 321 THR   A N   1 
ATOM   177  C  CA  . THR   A 1 25  ? -29.400 -24.843 28.702 1.00 118.87 ? 321 THR   A CA  1 
ATOM   178  C  C   . THR   A 1 25  ? -27.946 -24.744 29.145 1.00 113.09 ? 321 THR   A C   1 
ATOM   179  O  O   . THR   A 1 25  ? -27.411 -25.685 29.745 1.00 110.20 ? 321 THR   A O   1 
ATOM   180  C  CB  . THR   A 1 25  ? -29.523 -24.885 27.170 1.00 126.41 ? 321 THR   A CB  1 
ATOM   181  O  OG1 . THR   A 1 25  ? -28.475 -25.688 26.614 1.00 131.92 ? 321 THR   A OG1 1 
ATOM   182  C  CG2 . THR   A 1 25  ? -29.489 -23.469 26.567 1.00 123.76 ? 321 THR   A CG2 1 
ATOM   183  N  N   . LEU   A 1 26  ? -27.314 -23.605 28.872 1.00 109.61 ? 322 LEU   A N   1 
ATOM   184  C  CA  . LEU   A 1 26  ? -25.903 -23.403 29.159 1.00 110.20 ? 322 LEU   A CA  1 
ATOM   185  C  C   . LEU   A 1 26  ? -25.670 -23.196 30.654 1.00 106.68 ? 322 LEU   A C   1 
ATOM   186  O  O   . LEU   A 1 26  ? -26.601 -23.019 31.444 1.00 106.43 ? 322 LEU   A O   1 
ATOM   187  C  CB  . LEU   A 1 26  ? -25.369 -22.204 28.375 1.00 110.30 ? 322 LEU   A CB  1 
ATOM   188  C  CG  . LEU   A 1 26  ? -24.964 -22.420 26.916 1.00 111.71 ? 322 LEU   A CG  1 
ATOM   189  C  CD1 . LEU   A 1 26  ? -25.221 -21.151 26.124 1.00 107.10 ? 322 LEU   A CD1 1 
ATOM   190  C  CD2 . LEU   A 1 26  ? -23.494 -22.832 26.818 1.00 112.86 ? 322 LEU   A CD2 1 
ATOM   191  N  N   . GLU   A 1 27  ? -24.395 -23.210 31.032 1.00 101.68 ? 323 GLU   A N   1 
ATOM   192  C  CA  . GLU   A 1 27  ? -23.976 -23.056 32.414 1.00 98.64  ? 323 GLU   A CA  1 
ATOM   193  C  C   . GLU   A 1 27  ? -23.521 -21.622 32.680 1.00 93.52  ? 323 GLU   A C   1 
ATOM   194  O  O   . GLU   A 1 27  ? -23.035 -20.925 31.783 1.00 93.87  ? 323 GLU   A O   1 
ATOM   195  C  CB  . GLU   A 1 27  ? -22.869 -24.058 32.756 1.00 103.06 ? 323 GLU   A CB  1 
ATOM   196  C  CG  . GLU   A 1 27  ? -23.244 -25.492 32.382 1.00 114.05 ? 323 GLU   A CG  1 
ATOM   197  C  CD  . GLU   A 1 27  ? -22.447 -26.551 33.131 1.00 127.13 ? 323 GLU   A CD  1 
ATOM   198  O  OE1 . GLU   A 1 27  ? -21.800 -26.216 34.148 1.00 130.30 ? 323 GLU   A OE1 1 
ATOM   199  O  OE2 . GLU   A 1 27  ? -22.477 -27.727 32.700 1.00 133.74 ? 323 GLU   A OE2 1 
ATOM   200  N  N   . THR   A 1 28  ? -23.698 -21.188 33.934 1.00 81.81  ? 324 THR   A N   1 
ATOM   201  C  CA  . THR   A 1 28  ? -23.529 -19.796 34.337 1.00 77.65  ? 324 THR   A CA  1 
ATOM   202  C  C   . THR   A 1 28  ? -22.156 -19.475 34.920 1.00 71.46  ? 324 THR   A C   1 
ATOM   203  O  O   . THR   A 1 28  ? -21.746 -18.309 34.893 1.00 75.38  ? 324 THR   A O   1 
ATOM   204  C  CB  . THR   A 1 28  ? -24.586 -19.421 35.388 1.00 73.10  ? 324 THR   A CB  1 
ATOM   205  O  OG1 . THR   A 1 28  ? -24.424 -20.255 36.549 1.00 67.84  ? 324 THR   A OG1 1 
ATOM   206  C  CG2 . THR   A 1 28  ? -25.987 -19.602 34.823 1.00 78.54  ? 324 THR   A CG2 1 
ATOM   207  N  N   . GLY   A 1 29  ? -21.435 -20.464 35.425 1.00 69.45  ? 325 GLY   A N   1 
ATOM   208  C  CA  . GLY   A 1 29  ? -20.241 -20.233 36.202 1.00 74.76  ? 325 GLY   A CA  1 
ATOM   209  C  C   . GLY   A 1 29  ? -20.440 -20.431 37.687 1.00 78.58  ? 325 GLY   A C   1 
ATOM   210  O  O   . GLY   A 1 29  ? -19.469 -20.712 38.407 1.00 83.43  ? 325 GLY   A O   1 
ATOM   211  N  N   . CYS   A 1 30  ? -21.673 -20.312 38.159 1.00 74.53  ? 326 CYS   A N   1 
ATOM   212  C  CA  . CYS   A 1 30  ? -21.938 -20.486 39.575 1.00 70.98  ? 326 CYS   A CA  1 
ATOM   213  C  C   . CYS   A 1 30  ? -22.148 -21.962 39.893 1.00 76.69  ? 326 CYS   A C   1 
ATOM   214  O  O   . CYS   A 1 30  ? -22.544 -22.760 39.040 1.00 78.32  ? 326 CYS   A O   1 
ATOM   215  C  CB  . CYS   A 1 30  ? -23.163 -19.674 39.994 1.00 61.03  ? 326 CYS   A CB  1 
ATOM   216  S  SG  . CYS   A 1 30  ? -23.065 -17.890 39.664 1.00 68.67  ? 326 CYS   A SG  1 
ATOM   217  N  N   . THR   A 1 31  ? -21.854 -22.325 41.128 1.00 79.50  ? 327 THR   A N   1 
ATOM   218  C  CA  . THR   A 1 31  ? -22.188 -23.645 41.651 1.00 80.67  ? 327 THR   A CA  1 
ATOM   219  C  C   . THR   A 1 31  ? -23.133 -23.465 42.838 1.00 81.38  ? 327 THR   A C   1 
ATOM   220  O  O   . THR   A 1 31  ? -23.595 -22.360 43.128 1.00 86.54  ? 327 THR   A O   1 
ATOM   221  C  CB  . THR   A 1 31  ? -20.923 -24.412 42.037 1.00 78.11  ? 327 THR   A CB  1 
ATOM   222  O  OG1 . THR   A 1 31  ? -20.338 -23.808 43.197 1.00 77.95  ? 327 THR   A OG1 1 
ATOM   223  C  CG2 . THR   A 1 31  ? -19.918 -24.381 40.902 1.00 71.62  ? 327 THR   A CG2 1 
ATOM   224  N  N   . GLU   A 1 32  ? -23.424 -24.557 43.537 1.00 89.65  ? 328 GLU   A N   1 
ATOM   225  C  CA  . GLU   A 1 32  ? -24.217 -24.417 44.753 1.00 95.59  ? 328 GLU   A CA  1 
ATOM   226  C  C   . GLU   A 1 32  ? -23.453 -23.685 45.853 1.00 92.89  ? 328 GLU   A C   1 
ATOM   227  O  O   . GLU   A 1 32  ? -24.075 -23.202 46.803 1.00 95.12  ? 328 GLU   A O   1 
ATOM   228  C  CB  . GLU   A 1 32  ? -24.684 -25.790 45.251 1.00 107.65 ? 328 GLU   A CB  1 
ATOM   229  C  CG  . GLU   A 1 32  ? -25.874 -26.379 44.482 1.00 121.92 ? 328 GLU   A CG  1 
ATOM   230  C  CD  . GLU   A 1 32  ? -25.458 -27.305 43.343 1.00 133.98 ? 328 GLU   A CD  1 
ATOM   231  O  OE1 . GLU   A 1 32  ? -25.757 -28.520 43.411 1.00 141.26 ? 328 GLU   A OE1 1 
ATOM   232  O  OE2 . GLU   A 1 32  ? -24.829 -26.818 42.381 1.00 135.73 ? 328 GLU   A OE2 1 
ATOM   233  N  N   . HIS   A 1 33  ? -22.129 -23.565 45.730 1.00 88.65  ? 329 HIS   A N   1 
ATOM   234  C  CA  . HIS   A 1 33  ? -21.278 -23.074 46.806 1.00 89.29  ? 329 HIS   A CA  1 
ATOM   235  C  C   . HIS   A 1 33  ? -20.435 -21.869 46.409 1.00 78.75  ? 329 HIS   A C   1 
ATOM   236  O  O   . HIS   A 1 33  ? -19.589 -21.434 47.200 1.00 78.16  ? 329 HIS   A O   1 
ATOM   237  C  CB  . HIS   A 1 33  ? -20.373 -24.201 47.301 1.00 106.16 ? 329 HIS   A CB  1 
ATOM   238  C  CG  . HIS   A 1 33  ? -21.071 -25.520 47.421 1.00 122.02 ? 329 HIS   A CG  1 
ATOM   239  N  ND1 . HIS   A 1 33  ? -21.777 -25.891 48.547 1.00 126.77 ? 329 HIS   A ND1 1 
ATOM   240  C  CD2 . HIS   A 1 33  ? -21.190 -26.548 46.547 1.00 128.11 ? 329 HIS   A CD2 1 
ATOM   241  C  CE1 . HIS   A 1 33  ? -22.294 -27.093 48.363 1.00 130.36 ? 329 HIS   A CE1 1 
ATOM   242  N  NE2 . HIS   A 1 33  ? -21.953 -27.514 47.158 1.00 129.65 ? 329 HIS   A NE2 1 
ATOM   243  N  N   . ILE   A 1 34  ? -20.637 -21.313 45.217 1.00 69.95  ? 330 ILE   A N   1 
ATOM   244  C  CA  . ILE   A 1 34  ? -19.935 -20.104 44.810 1.00 68.86  ? 330 ILE   A CA  1 
ATOM   245  C  C   . ILE   A 1 34  ? -20.743 -19.417 43.720 1.00 65.38  ? 330 ILE   A C   1 
ATOM   246  O  O   . ILE   A 1 34  ? -21.309 -20.064 42.837 1.00 67.45  ? 330 ILE   A O   1 
ATOM   247  C  CB  . ILE   A 1 34  ? -18.498 -20.402 44.339 1.00 75.00  ? 330 ILE   A CB  1 
ATOM   248  C  CG1 . ILE   A 1 34  ? -17.777 -19.090 44.053 1.00 74.09  ? 330 ILE   A CG1 1 
ATOM   249  C  CG2 . ILE   A 1 34  ? -18.504 -21.270 43.091 1.00 84.49  ? 330 ILE   A CG2 1 
ATOM   250  C  CD1 . ILE   A 1 34  ? -16.304 -19.155 44.260 1.00 75.65  ? 330 ILE   A CD1 1 
ATOM   251  N  N   . CYS   A 1 35  ? -20.817 -18.096 43.805 1.00 61.07  ? 331 CYS   A N   1 
ATOM   252  C  CA  . CYS   A 1 35  ? -21.556 -17.293 42.848 1.00 59.64  ? 331 CYS   A CA  1 
ATOM   253  C  C   . CYS   A 1 35  ? -20.552 -16.418 42.126 1.00 62.04  ? 331 CYS   A C   1 
ATOM   254  O  O   . CYS   A 1 35  ? -19.708 -15.782 42.767 1.00 56.85  ? 331 CYS   A O   1 
ATOM   255  C  CB  . CYS   A 1 35  ? -22.621 -16.448 43.533 1.00 65.04  ? 331 CYS   A CB  1 
ATOM   256  S  SG  . CYS   A 1 35  ? -23.337 -15.211 42.488 1.00 60.64  ? 331 CYS   A SG  1 
ATOM   257  N  N   . MET   A 1 36  ? -20.611 -16.435 40.794 1.00 62.01  ? 332 MET   A N   1 
ATOM   258  C  CA  . MET   A 1 36  ? -19.671 -15.703 39.961 1.00 69.50  ? 332 MET   A CA  1 
ATOM   259  C  C   . MET   A 1 36  ? -20.345 -14.570 39.211 1.00 68.71  ? 332 MET   A C   1 
ATOM   260  O  O   . MET   A 1 36  ? -19.818 -14.089 38.202 1.00 65.54  ? 332 MET   A O   1 
ATOM   261  C  CB  . MET   A 1 36  ? -18.989 -16.663 38.999 1.00 82.66  ? 332 MET   A CB  1 
ATOM   262  C  CG  . MET   A 1 36  ? -18.347 -17.801 39.736 1.00 93.23  ? 332 MET   A CG  1 
ATOM   263  S  SD  . MET   A 1 36  ? -16.902 -18.381 38.871 1.00 104.27 ? 332 MET   A SD  1 
ATOM   264  C  CE  . MET   A 1 36  ? -15.983 -19.065 40.236 1.00 105.78 ? 332 MET   A CE  1 
ATOM   265  N  N   . GLY   A 1 37  ? -21.493 -14.116 39.700 1.00 63.06  ? 333 GLY   A N   1 
ATOM   266  C  CA  . GLY   A 1 37  ? -22.204 -13.062 39.017 1.00 60.61  ? 333 GLY   A CA  1 
ATOM   267  C  C   . GLY   A 1 37  ? -21.485 -11.731 38.914 1.00 62.73  ? 333 GLY   A C   1 
ATOM   268  O  O   . GLY   A 1 37  ? -22.041 -10.825 38.297 1.00 60.73  ? 333 GLY   A O   1 
ATOM   269  N  N   . SER   A 1 38  ? -20.305 -11.546 39.515 1.00 49.71  ? 334 SER   A N   1 
ATOM   270  C  CA  . SER   A 1 38  ? -19.540 -10.333 39.235 1.00 57.83  ? 334 SER   A CA  1 
ATOM   271  C  C   . SER   A 1 38  ? -18.300 -10.598 38.387 1.00 56.08  ? 334 SER   A C   1 
ATOM   272  O  O   . SER   A 1 38  ? -17.512 -9.675  38.171 1.00 55.41  ? 334 SER   A O   1 
ATOM   273  C  CB  . SER   A 1 38  ? -19.149 -9.601  40.519 1.00 60.28  ? 334 SER   A CB  1 
ATOM   274  O  OG  . SER   A 1 38  ? -18.185 -10.305 41.307 1.00 57.86  ? 334 SER   A OG  1 
ATOM   275  N  N   . ILE   A 1 39  ? -18.096 -11.840 37.912 1.00 53.00  ? 335 ILE   A N   1 
ATOM   276  C  CA  . ILE   A 1 39  ? -16.998 -12.136 36.993 1.00 59.63  ? 335 ILE   A CA  1 
ATOM   277  C  C   . ILE   A 1 39  ? -17.395 -11.679 35.594 1.00 63.73  ? 335 ILE   A C   1 
ATOM   278  O  O   . ILE   A 1 39  ? -18.512 -11.951 35.132 1.00 66.99  ? 335 ILE   A O   1 
ATOM   279  C  CB  . ILE   A 1 39  ? -16.666 -13.641 37.020 1.00 53.96  ? 335 ILE   A CB  1 
ATOM   280  C  CG1 . ILE   A 1 39  ? -16.392 -14.133 38.465 1.00 53.40  ? 335 ILE   A CG1 1 
ATOM   281  C  CG2 . ILE   A 1 39  ? -15.473 -13.964 36.120 1.00 51.81  ? 335 ILE   A CG2 1 
ATOM   282  C  CD1 . ILE   A 1 39  ? -15.362 -13.313 39.238 1.00 65.39  ? 335 ILE   A CD1 1 
ATOM   283  N  N   . MET   A 1 40  ? -16.467 -11.005 34.891 1.00 69.32  ? 336 MET   A N   1 
ATOM   284  C  CA  . MET   A 1 40  ? -16.790 -10.358 33.613 1.00 74.81  ? 336 MET   A CA  1 
ATOM   285  C  C   . MET   A 1 40  ? -16.969 -11.366 32.478 1.00 73.61  ? 336 MET   A C   1 
ATOM   286  O  O   . MET   A 1 40  ? -17.925 -11.264 31.693 1.00 66.43  ? 336 MET   A O   1 
ATOM   287  C  CB  . MET   A 1 40  ? -15.697 -9.350  33.243 1.00 81.81  ? 336 MET   A CB  1 
ATOM   288  C  CG  . MET   A 1 40  ? -16.004 -8.519  31.997 1.00 90.66  ? 336 MET   A CG  1 
ATOM   289  S  SD  . MET   A 1 40  ? -16.618 -6.854  32.379 1.00 95.60  ? 336 MET   A SD  1 
ATOM   290  C  CE  . MET   A 1 40  ? -15.095 -5.964  32.675 1.00 93.85  ? 336 MET   A CE  1 
ATOM   291  N  N   . LEU   A 1 41  ? -16.063 -12.335 32.363 1.00 83.86  ? 337 LEU   A N   1 
ATOM   292  C  CA  . LEU   A 1 41  ? -16.153 -13.361 31.325 1.00 97.11  ? 337 LEU   A CA  1 
ATOM   293  C  C   . LEU   A 1 41  ? -15.790 -14.724 31.898 1.00 105.09 ? 337 LEU   A C   1 
ATOM   294  O  O   . LEU   A 1 41  ? -14.631 -15.152 31.841 1.00 114.27 ? 337 LEU   A O   1 
ATOM   295  C  CB  . LEU   A 1 41  ? -15.263 -13.021 30.126 1.00 103.37 ? 337 LEU   A CB  1 
ATOM   296  C  CG  . LEU   A 1 41  ? -13.817 -12.526 30.302 1.00 106.73 ? 337 LEU   A CG  1 
ATOM   297  C  CD1 . LEU   A 1 41  ? -12.797 -13.598 29.920 1.00 113.30 ? 337 LEU   A CD1 1 
ATOM   298  C  CD2 . LEU   A 1 41  ? -13.577 -11.258 29.490 1.00 102.97 ? 337 LEU   A CD2 1 
ATOM   299  N  N   . PRO   A 1 42  ? -16.759 -15.438 32.467 1.00 103.83 ? 338 PRO   A N   1 
ATOM   300  C  CA  . PRO   A 1 42  ? -16.550 -16.850 32.796 1.00 105.43 ? 338 PRO   A CA  1 
ATOM   301  C  C   . PRO   A 1 42  ? -16.882 -17.737 31.600 1.00 107.25 ? 338 PRO   A C   1 
ATOM   302  O  O   . PRO   A 1 42  ? -17.623 -17.354 30.687 1.00 105.99 ? 338 PRO   A O   1 
ATOM   303  C  CB  . PRO   A 1 42  ? -17.518 -17.092 33.971 1.00 103.19 ? 338 PRO   A CB  1 
ATOM   304  C  CG  . PRO   A 1 42  ? -18.522 -15.938 33.936 1.00 99.57  ? 338 PRO   A CG  1 
ATOM   305  C  CD  . PRO   A 1 42  ? -18.114 -14.984 32.827 1.00 97.49  ? 338 PRO   A CD  1 
ATOM   306  N  N   . SER   A 1 43  ? -16.288 -18.927 31.602 1.00 111.65 ? 339 SER   A N   1 
ATOM   307  C  CA  . SER   A 1 43  ? -16.463 -19.860 30.491 1.00 112.48 ? 339 SER   A CA  1 
ATOM   308  C  C   . SER   A 1 43  ? -17.894 -20.397 30.443 1.00 114.25 ? 339 SER   A C   1 
ATOM   309  O  O   . SER   A 1 43  ? -18.749 -19.856 29.733 1.00 111.92 ? 339 SER   A O   1 
ATOM   310  C  CB  . SER   A 1 43  ? -15.459 -21.012 30.591 1.00 110.90 ? 339 SER   A CB  1 
ATOM   311  O  OG  . SER   A 1 43  ? -15.411 -21.535 31.905 1.00 106.82 ? 339 SER   A OG  1 
ATOM   312  N  N   . VAL   A 1 52  ? -13.765 -26.603 17.078 1.00 143.73 ? 348 VAL   A N   1 
ATOM   313  C  CA  . VAL   A 1 52  ? -14.648 -26.924 15.958 1.00 141.38 ? 348 VAL   A CA  1 
ATOM   314  C  C   . VAL   A 1 52  ? -15.812 -27.786 16.460 1.00 146.68 ? 348 VAL   A C   1 
ATOM   315  O  O   . VAL   A 1 52  ? -15.666 -28.529 17.434 1.00 153.66 ? 348 VAL   A O   1 
ATOM   316  C  CB  . VAL   A 1 52  ? -13.861 -27.618 14.798 1.00 134.47 ? 348 VAL   A CB  1 
ATOM   317  C  CG1 . VAL   A 1 52  ? -13.419 -29.029 15.185 1.00 136.22 ? 348 VAL   A CG1 1 
ATOM   318  C  CG2 . VAL   A 1 52  ? -14.679 -27.628 13.516 1.00 127.00 ? 348 VAL   A CG2 1 
ATOM   319  N  N   . ALA   A 1 53  ? -16.971 -27.663 15.815 1.00 140.49 ? 349 ALA   A N   1 
ATOM   320  C  CA  . ALA   A 1 53  ? -18.163 -28.427 16.157 1.00 135.74 ? 349 ALA   A CA  1 
ATOM   321  C  C   . ALA   A 1 53  ? -18.251 -29.694 15.311 1.00 142.12 ? 349 ALA   A C   1 
ATOM   322  O  O   . ALA   A 1 53  ? -17.602 -29.818 14.270 1.00 153.69 ? 349 ALA   A O   1 
ATOM   323  C  CB  . ALA   A 1 53  ? -19.423 -27.581 15.966 1.00 126.14 ? 349 ALA   A CB  1 
ATOM   324  N  N   . THR   A 1 54  ? -19.066 -30.644 15.774 1.00 132.01 ? 350 THR   A N   1 
ATOM   325  C  CA  . THR   A 1 54  ? -19.272 -31.911 15.078 1.00 122.70 ? 350 THR   A CA  1 
ATOM   326  C  C   . THR   A 1 54  ? -20.746 -32.096 14.729 1.00 114.93 ? 350 THR   A C   1 
ATOM   327  O  O   . THR   A 1 54  ? -21.629 -31.386 15.220 1.00 105.84 ? 350 THR   A O   1 
ATOM   328  C  CB  . THR   A 1 54  ? -18.779 -33.109 15.906 1.00 123.80 ? 350 THR   A CB  1 
ATOM   329  O  OG1 . THR   A 1 54  ? -19.787 -33.505 16.846 1.00 122.26 ? 350 THR   A OG1 1 
ATOM   330  C  CG2 . THR   A 1 54  ? -17.502 -32.758 16.659 1.00 124.14 ? 350 THR   A CG2 1 
ATOM   331  N  N   . LYS   A 1 55  ? -21.000 -33.078 13.862 1.00 119.79 ? 351 LYS   A N   1 
ATOM   332  C  CA  . LYS   A 1 55  ? -22.341 -33.320 13.346 1.00 119.97 ? 351 LYS   A CA  1 
ATOM   333  C  C   . LYS   A 1 55  ? -23.235 -34.031 14.347 1.00 123.69 ? 351 LYS   A C   1 
ATOM   334  O  O   . LYS   A 1 55  ? -24.464 -33.947 14.228 1.00 113.47 ? 351 LYS   A O   1 
ATOM   335  C  CB  . LYS   A 1 55  ? -22.255 -34.139 12.054 1.00 125.55 ? 351 LYS   A CB  1 
ATOM   336  C  CG  . LYS   A 1 55  ? -20.967 -34.932 11.931 1.00 127.30 ? 351 LYS   A CG  1 
ATOM   337  C  CD  . LYS   A 1 55  ? -20.991 -35.856 10.725 1.00 130.80 ? 351 LYS   A CD  1 
ATOM   338  C  CE  . LYS   A 1 55  ? -19.735 -36.718 10.681 1.00 130.95 ? 351 LYS   A CE  1 
ATOM   339  N  NZ  . LYS   A 1 55  ? -19.956 -38.039 10.019 1.00 129.78 ? 351 LYS   A NZ  1 
ATOM   340  N  N   . ASP   A 1 56  ? -22.640 -34.733 15.314 1.00 139.28 ? 352 ASP   A N   1 
ATOM   341  C  CA  . ASP   A 1 56  ? -23.413 -35.381 16.368 1.00 147.45 ? 352 ASP   A CA  1 
ATOM   342  C  C   . ASP   A 1 56  ? -24.073 -34.346 17.264 1.00 138.83 ? 352 ASP   A C   1 
ATOM   343  O  O   . ASP   A 1 56  ? -25.271 -34.430 17.556 1.00 141.16 ? 352 ASP   A O   1 
ATOM   344  C  CB  . ASP   A 1 56  ? -22.498 -36.290 17.190 1.00 160.18 ? 352 ASP   A CB  1 
ATOM   345  C  CG  . ASP   A 1 56  ? -21.402 -36.918 16.352 1.00 172.05 ? 352 ASP   A CG  1 
ATOM   346  O  OD1 . ASP   A 1 56  ? -21.621 -38.023 15.814 1.00 178.49 ? 352 ASP   A OD1 1 
ATOM   347  O  OD2 . ASP   A 1 56  ? -20.331 -36.290 16.211 1.00 173.32 ? 352 ASP   A OD2 1 
ATOM   348  N  N   . GLN   A 1 57  ? -23.295 -33.365 17.718 1.00 126.38 ? 353 GLN   A N   1 
ATOM   349  C  CA  . GLN   A 1 57  ? -23.816 -32.300 18.559 1.00 116.40 ? 353 GLN   A CA  1 
ATOM   350  C  C   . GLN   A 1 57  ? -24.817 -31.412 17.833 1.00 108.94 ? 353 GLN   A C   1 
ATOM   351  O  O   . GLN   A 1 57  ? -25.589 -30.706 18.494 1.00 102.47 ? 353 GLN   A O   1 
ATOM   352  C  CB  . GLN   A 1 57  ? -22.662 -31.437 19.062 1.00 119.55 ? 353 GLN   A CB  1 
ATOM   353  C  CG  . GLN   A 1 57  ? -21.374 -32.198 19.292 1.00 131.70 ? 353 GLN   A CG  1 
ATOM   354  C  CD  . GLN   A 1 57  ? -20.151 -31.399 18.883 1.00 137.05 ? 353 GLN   A CD  1 
ATOM   355  O  OE1 . GLN   A 1 57  ? -20.230 -30.510 18.033 1.00 135.55 ? 353 GLN   A OE1 1 
ATOM   356  N  NE2 . GLN   A 1 57  ? -19.010 -31.717 19.484 1.00 142.40 ? 353 GLN   A NE2 1 
ATOM   357  N  N   . LEU   A 1 58  ? -24.828 -31.442 16.493 1.00 101.93 ? 354 LEU   A N   1 
ATOM   358  C  CA  . LEU   A 1 58  ? -25.474 -30.387 15.724 1.00 95.10  ? 354 LEU   A CA  1 
ATOM   359  C  C   . LEU   A 1 58  ? -26.979 -30.582 15.560 1.00 95.54  ? 354 LEU   A C   1 
ATOM   360  O  O   . LEU   A 1 58  ? -27.712 -29.587 15.518 1.00 93.54  ? 354 LEU   A O   1 
ATOM   361  C  CB  . LEU   A 1 58  ? -24.819 -30.284 14.344 1.00 97.75  ? 354 LEU   A CB  1 
ATOM   362  C  CG  . LEU   A 1 58  ? -24.644 -28.883 13.768 1.00 92.21  ? 354 LEU   A CG  1 
ATOM   363  C  CD1 . LEU   A 1 58  ? -23.702 -28.079 14.647 1.00 86.84  ? 354 LEU   A CD1 1 
ATOM   364  C  CD2 . LEU   A 1 58  ? -24.133 -28.953 12.322 1.00 97.79  ? 354 LEU   A CD2 1 
ATOM   365  N  N   . PHE   A 1 59  ? -27.470 -31.834 15.438 1.00 96.27  ? 355 PHE   A N   1 
ATOM   366  C  CA  . PHE   A 1 59  ? -28.906 -31.988 15.199 1.00 104.49 ? 355 PHE   A CA  1 
ATOM   367  C  C   . PHE   A 1 59  ? -29.769 -31.620 16.407 1.00 109.62 ? 355 PHE   A C   1 
ATOM   368  O  O   . PHE   A 1 59  ? -30.809 -30.973 16.224 1.00 113.13 ? 355 PHE   A O   1 
ATOM   369  C  CB  . PHE   A 1 59  ? -29.269 -33.404 14.746 1.00 122.36 ? 355 PHE   A CB  1 
ATOM   370  C  CG  . PHE   A 1 59  ? -30.729 -33.550 14.390 1.00 135.10 ? 355 PHE   A CG  1 
ATOM   371  C  CD1 . PHE   A 1 59  ? -31.229 -32.999 13.218 1.00 138.67 ? 355 PHE   A CD1 1 
ATOM   372  C  CD2 . PHE   A 1 59  ? -31.609 -34.203 15.240 1.00 141.64 ? 355 PHE   A CD2 1 
ATOM   373  C  CE1 . PHE   A 1 59  ? -32.572 -33.108 12.899 1.00 142.54 ? 355 PHE   A CE1 1 
ATOM   374  C  CE2 . PHE   A 1 59  ? -32.953 -34.321 14.919 1.00 145.32 ? 355 PHE   A CE2 1 
ATOM   375  C  CZ  . PHE   A 1 59  ? -33.433 -33.772 13.748 1.00 145.59 ? 355 PHE   A CZ  1 
ATOM   376  N  N   . PRO   A 1 60  ? -29.419 -32.026 17.640 1.00 109.64 ? 356 PRO   A N   1 
ATOM   377  C  CA  . PRO   A 1 60  ? -30.197 -31.553 18.803 1.00 100.57 ? 356 PRO   A CA  1 
ATOM   378  C  C   . PRO   A 1 60  ? -30.341 -30.041 18.883 1.00 89.69  ? 356 PRO   A C   1 
ATOM   379  O  O   . PRO   A 1 60  ? -31.445 -29.541 19.129 1.00 93.13  ? 356 PRO   A O   1 
ATOM   380  C  CB  . PRO   A 1 60  ? -29.408 -32.112 20.000 1.00 108.82 ? 356 PRO   A CB  1 
ATOM   381  C  CG  . PRO   A 1 60  ? -28.101 -32.612 19.423 1.00 108.61 ? 356 PRO   A CG  1 
ATOM   382  C  CD  . PRO   A 1 60  ? -28.433 -33.039 18.048 1.00 110.68 ? 356 PRO   A CD  1 
ATOM   383  N  N   . LEU   A 1 61  ? -29.246 -29.301 18.695 1.00 80.78  ? 357 LEU   A N   1 
ATOM   384  C  CA  . LEU   A 1 61  ? -29.312 -27.842 18.643 1.00 74.60  ? 357 LEU   A CA  1 
ATOM   385  C  C   . LEU   A 1 61  ? -30.224 -27.359 17.514 1.00 84.99  ? 357 LEU   A C   1 
ATOM   386  O  O   . LEU   A 1 61  ? -31.028 -26.435 17.701 1.00 87.04  ? 357 LEU   A O   1 
ATOM   387  C  CB  . LEU   A 1 61  ? -27.906 -27.280 18.467 1.00 75.86  ? 357 LEU   A CB  1 
ATOM   388  C  CG  . LEU   A 1 61  ? -26.893 -27.494 19.588 1.00 86.08  ? 357 LEU   A CG  1 
ATOM   389  C  CD1 . LEU   A 1 61  ? -25.471 -27.456 19.039 1.00 89.47  ? 357 LEU   A CD1 1 
ATOM   390  C  CD2 . LEU   A 1 61  ? -27.088 -26.422 20.643 1.00 84.50  ? 357 LEU   A CD2 1 
ATOM   391  N  N   . ALA   A 1 62  ? -30.096 -27.957 16.323 1.00 81.25  ? 358 ALA   A N   1 
ATOM   392  C  CA  . ALA   A 1 62  ? -30.948 -27.573 15.198 1.00 81.49  ? 358 ALA   A CA  1 
ATOM   393  C  C   . ALA   A 1 62  ? -32.415 -27.869 15.491 1.00 84.18  ? 358 ALA   A C   1 
ATOM   394  O  O   . ALA   A 1 62  ? -33.294 -27.030 15.241 1.00 76.40  ? 358 ALA   A O   1 
ATOM   395  C  CB  . ALA   A 1 62  ? -30.507 -28.309 13.927 1.00 81.49  ? 358 ALA   A CB  1 
ATOM   396  N  N   . LYS   A 1 63  ? -32.688 -29.072 16.013 1.00 91.85  ? 359 LYS   A N   1 
ATOM   397  C  CA  . LYS   A 1 63  ? -34.045 -29.487 16.364 1.00 98.80  ? 359 LYS   A CA  1 
ATOM   398  C  C   . LYS   A 1 63  ? -34.661 -28.551 17.396 1.00 100.40 ? 359 LYS   A C   1 
ATOM   399  O  O   . LYS   A 1 63  ? -35.780 -28.055 17.216 1.00 110.17 ? 359 LYS   A O   1 
ATOM   400  C  CB  . LYS   A 1 63  ? -34.022 -30.923 16.899 1.00 102.18 ? 359 LYS   A CB  1 
ATOM   401  C  CG  . LYS   A 1 63  ? -35.386 -31.470 17.278 1.00 105.19 ? 359 LYS   A CG  1 
ATOM   402  C  CD  . LYS   A 1 63  ? -35.289 -32.810 17.988 1.00 108.08 ? 359 LYS   A CD  1 
ATOM   403  C  CE  . LYS   A 1 63  ? -36.547 -33.630 17.740 1.00 109.49 ? 359 LYS   A CE  1 
ATOM   404  N  NZ  . LYS   A 1 63  ? -37.773 -32.809 17.956 1.00 111.46 ? 359 LYS   A NZ  1 
ATOM   405  N  N   . GLU   A 1 64  ? -33.942 -28.307 18.492 1.00 87.64  ? 360 GLU   A N   1 
ATOM   406  C  CA  . GLU   A 1 64  ? -34.433 -27.401 19.525 1.00 97.02  ? 360 GLU   A CA  1 
ATOM   407  C  C   . GLU   A 1 64  ? -34.794 -26.038 18.935 1.00 91.66  ? 360 GLU   A C   1 
ATOM   408  O  O   . GLU   A 1 64  ? -35.903 -25.534 19.142 1.00 94.85  ? 360 GLU   A O   1 
ATOM   409  C  CB  . GLU   A 1 64  ? -33.385 -27.278 20.637 1.00 101.63 ? 360 GLU   A CB  1 
ATOM   410  C  CG  . GLU   A 1 64  ? -33.673 -26.234 21.709 1.00 111.60 ? 360 GLU   A CG  1 
ATOM   411  C  CD  . GLU   A 1 64  ? -32.457 -25.956 22.598 1.00 121.83 ? 360 GLU   A CD  1 
ATOM   412  O  OE1 . GLU   A 1 64  ? -31.429 -26.651 22.435 1.00 126.08 ? 360 GLU   A OE1 1 
ATOM   413  O  OE2 . GLU   A 1 64  ? -32.528 -25.042 23.455 1.00 121.25 ? 360 GLU   A OE2 1 
ATOM   414  N  N   . PHE   A 1 65  ? -33.878 -25.434 18.173 1.00 80.77  ? 361 PHE   A N   1 
ATOM   415  C  CA  . PHE   A 1 65  ? -34.169 -24.128 17.588 1.00 74.21  ? 361 PHE   A CA  1 
ATOM   416  C  C   . PHE   A 1 65  ? -35.366 -24.191 16.649 1.00 77.96  ? 361 PHE   A C   1 
ATOM   417  O  O   . PHE   A 1 65  ? -36.199 -23.277 16.636 1.00 79.59  ? 361 PHE   A O   1 
ATOM   418  C  CB  . PHE   A 1 65  ? -32.952 -23.589 16.841 1.00 72.79  ? 361 PHE   A CB  1 
ATOM   419  C  CG  . PHE   A 1 65  ? -33.243 -22.352 16.035 1.00 71.94  ? 361 PHE   A CG  1 
ATOM   420  C  CD1 . PHE   A 1 65  ? -33.357 -21.119 16.663 1.00 72.96  ? 361 PHE   A CD1 1 
ATOM   421  C  CD2 . PHE   A 1 65  ? -33.417 -22.417 14.662 1.00 71.48  ? 361 PHE   A CD2 1 
ATOM   422  C  CE1 . PHE   A 1 65  ? -33.632 -19.977 15.935 1.00 72.98  ? 361 PHE   A CE1 1 
ATOM   423  C  CE2 . PHE   A 1 65  ? -33.693 -21.274 13.921 1.00 68.90  ? 361 PHE   A CE2 1 
ATOM   424  C  CZ  . PHE   A 1 65  ? -33.799 -20.053 14.560 1.00 61.04  ? 361 PHE   A CZ  1 
ATOM   425  N  N   . LEU   A 1 66  ? -35.460 -25.251 15.841 1.00 73.57  ? 362 LEU   A N   1 
ATOM   426  C  CA  . LEU   A 1 66  ? -36.567 -25.359 14.898 1.00 79.62  ? 362 LEU   A CA  1 
ATOM   427  C  C   . LEU   A 1 66  ? -37.892 -25.574 15.614 1.00 86.12  ? 362 LEU   A C   1 
ATOM   428  O  O   . LEU   A 1 66  ? -38.928 -25.064 15.176 1.00 84.88  ? 362 LEU   A O   1 
ATOM   429  C  CB  . LEU   A 1 66  ? -36.305 -26.495 13.906 1.00 87.49  ? 362 LEU   A CB  1 
ATOM   430  C  CG  . LEU   A 1 66  ? -35.279 -26.194 12.806 1.00 82.56  ? 362 LEU   A CG  1 
ATOM   431  C  CD1 . LEU   A 1 66  ? -35.239 -27.317 11.827 1.00 87.80  ? 362 LEU   A CD1 1 
ATOM   432  C  CD2 . LEU   A 1 66  ? -35.582 -24.876 12.123 1.00 82.17  ? 362 LEU   A CD2 1 
ATOM   433  N  N   . ASP   A 1 67  ? -37.880 -26.337 16.709 1.00 90.58  ? 363 ASP   A N   1 
ATOM   434  C  CA  . ASP   A 1 67  ? -39.106 -26.586 17.463 1.00 95.16  ? 363 ASP   A CA  1 
ATOM   435  C  C   . ASP   A 1 67  ? -39.659 -25.298 18.067 1.00 89.78  ? 363 ASP   A C   1 
ATOM   436  O  O   . ASP   A 1 67  ? -40.880 -25.130 18.176 1.00 92.14  ? 363 ASP   A O   1 
ATOM   437  C  CB  . ASP   A 1 67  ? -38.847 -27.624 18.561 1.00 104.55 ? 363 ASP   A CB  1 
ATOM   438  C  CG  . ASP   A 1 67  ? -38.957 -29.055 18.061 1.00 119.28 ? 363 ASP   A CG  1 
ATOM   439  O  OD1 . ASP   A 1 67  ? -40.093 -29.551 17.899 1.00 128.79 ? 363 ASP   A OD1 1 
ATOM   440  O  OD2 . ASP   A 1 67  ? -37.908 -29.691 17.832 1.00 123.89 ? 363 ASP   A OD2 1 
ATOM   441  N  N   . GLN   A 1 68  ? -38.782 -24.383 18.484 1.00 82.79  ? 364 GLN   A N   1 
ATOM   442  C  CA  . GLN   A 1 68  ? -39.276 -23.136 19.051 1.00 84.43  ? 364 GLN   A CA  1 
ATOM   443  C  C   . GLN   A 1 68  ? -39.605 -22.119 17.971 1.00 81.93  ? 364 GLN   A C   1 
ATOM   444  O  O   . GLN   A 1 68  ? -40.476 -21.268 18.183 1.00 84.22  ? 364 GLN   A O   1 
ATOM   445  C  CB  . GLN   A 1 68  ? -38.274 -22.556 20.073 1.00 83.61  ? 364 GLN   A CB  1 
ATOM   446  C  CG  . GLN   A 1 68  ? -36.849 -22.360 19.556 1.00 87.87  ? 364 GLN   A CG  1 
ATOM   447  C  CD  . GLN   A 1 68  ? -35.849 -21.995 20.652 1.00 87.46  ? 364 GLN   A CD  1 
ATOM   448  O  OE1 . GLN   A 1 68  ? -35.406 -20.843 20.748 1.00 87.97  ? 364 GLN   A OE1 1 
ATOM   449  N  NE2 . GLN   A 1 68  ? -35.471 -22.978 21.465 1.00 87.32  ? 364 GLN   A NE2 1 
ATOM   450  N  N   . TYR   A 1 69  ? -38.977 -22.219 16.797 1.00 90.06  ? 365 TYR   A N   1 
ATOM   451  C  CA  . TYR   A 1 69  ? -39.330 -21.316 15.709 1.00 85.20  ? 365 TYR   A CA  1 
ATOM   452  C  C   . TYR   A 1 69  ? -40.726 -21.613 15.177 1.00 90.82  ? 365 TYR   A C   1 
ATOM   453  O  O   . TYR   A 1 69  ? -41.554 -20.705 15.035 1.00 88.06  ? 365 TYR   A O   1 
ATOM   454  C  CB  . TYR   A 1 69  ? -38.307 -21.402 14.579 1.00 80.67  ? 365 TYR   A CB  1 
ATOM   455  C  CG  . TYR   A 1 69  ? -38.795 -20.685 13.351 1.00 83.71  ? 365 TYR   A CG  1 
ATOM   456  C  CD1 . TYR   A 1 69  ? -39.123 -19.337 13.409 1.00 84.05  ? 365 TYR   A CD1 1 
ATOM   457  C  CD2 . TYR   A 1 69  ? -38.963 -21.356 12.144 1.00 83.18  ? 365 TYR   A CD2 1 
ATOM   458  C  CE1 . TYR   A 1 69  ? -39.590 -18.675 12.309 1.00 85.74  ? 365 TYR   A CE1 1 
ATOM   459  C  CE2 . TYR   A 1 69  ? -39.435 -20.698 11.027 1.00 85.56  ? 365 TYR   A CE2 1 
ATOM   460  C  CZ  . TYR   A 1 69  ? -39.743 -19.353 11.120 1.00 86.88  ? 365 TYR   A CZ  1 
ATOM   461  O  OH  . TYR   A 1 69  ? -40.212 -18.665 10.034 1.00 93.14  ? 365 TYR   A OH  1 
ATOM   462  N  N   . TYR   A 1 70  ? -41.000 -22.880 14.859 1.00 96.94  ? 366 TYR   A N   1 
ATOM   463  C  CA  . TYR   A 1 70  ? -42.332 -23.247 14.396 1.00 96.98  ? 366 TYR   A CA  1 
ATOM   464  C  C   . TYR   A 1 70  ? -43.364 -23.103 15.504 1.00 101.03 ? 366 TYR   A C   1 
ATOM   465  O  O   . TYR   A 1 70  ? -44.526 -22.779 15.231 1.00 108.85 ? 366 TYR   A O   1 
ATOM   466  C  CB  . TYR   A 1 70  ? -42.313 -24.668 13.833 1.00 101.88 ? 366 TYR   A CB  1 
ATOM   467  C  CG  . TYR   A 1 70  ? -41.697 -24.710 12.453 1.00 98.87  ? 366 TYR   A CG  1 
ATOM   468  C  CD1 . TYR   A 1 70  ? -40.364 -25.069 12.263 1.00 95.30  ? 366 TYR   A CD1 1 
ATOM   469  C  CD2 . TYR   A 1 70  ? -42.440 -24.338 11.338 1.00 100.34 ? 366 TYR   A CD2 1 
ATOM   470  C  CE1 . TYR   A 1 70  ? -39.797 -25.082 10.974 1.00 93.13  ? 366 TYR   A CE1 1 
ATOM   471  C  CE2 . TYR   A 1 70  ? -41.887 -24.345 10.065 1.00 98.95  ? 366 TYR   A CE2 1 
ATOM   472  C  CZ  . TYR   A 1 70  ? -40.568 -24.715 9.885  1.00 94.74  ? 366 TYR   A CZ  1 
ATOM   473  O  OH  . TYR   A 1 70  ? -40.037 -24.711 8.600  1.00 86.37  ? 366 TYR   A OH  1 
ATOM   474  N  N   . SER   A 1 71  ? -42.965 -23.325 16.755 1.00 96.98  ? 367 SER   A N   1 
ATOM   475  C  CA  . SER   A 1 71  ? -43.859 -23.000 17.859 1.00 96.40  ? 367 SER   A CA  1 
ATOM   476  C  C   . SER   A 1 71  ? -44.216 -21.519 17.847 1.00 99.06  ? 367 SER   A C   1 
ATOM   477  O  O   . SER   A 1 71  ? -45.339 -21.145 18.200 1.00 110.75 ? 367 SER   A O   1 
ATOM   478  C  CB  . SER   A 1 71  ? -43.216 -23.395 19.191 1.00 92.22  ? 367 SER   A CB  1 
ATOM   479  O  OG  . SER   A 1 71  ? -44.164 -23.376 20.242 1.00 89.83  ? 367 SER   A OG  1 
ATOM   480  N  N   . SER   A 1 72  ? -43.292 -20.668 17.397 1.00 91.35  ? 368 SER   A N   1 
ATOM   481  C  CA  . SER   A 1 72  ? -43.517 -19.227 17.419 1.00 90.51  ? 368 SER   A CA  1 
ATOM   482  C  C   . SER   A 1 72  ? -44.480 -18.763 16.325 1.00 98.80  ? 368 SER   A C   1 
ATOM   483  O  O   . SER   A 1 72  ? -45.289 -17.858 16.564 1.00 102.46 ? 368 SER   A O   1 
ATOM   484  C  CB  . SER   A 1 72  ? -42.182 -18.488 17.303 1.00 88.27  ? 368 SER   A CB  1 
ATOM   485  O  OG  . SER   A 1 72  ? -42.088 -17.789 16.070 1.00 91.89  ? 368 SER   A OG  1 
ATOM   486  N  N   . ILE   A 1 73  ? -44.417 -19.346 15.119 1.00 95.15  ? 369 ILE   A N   1 
ATOM   487  C  CA  . ILE   A 1 73  ? -45.300 -18.911 14.037 1.00 98.45  ? 369 ILE   A CA  1 
ATOM   488  C  C   . ILE   A 1 73  ? -46.637 -19.640 14.139 1.00 107.46 ? 369 ILE   A C   1 
ATOM   489  O  O   . ILE   A 1 73  ? -47.440 -19.622 13.196 1.00 111.55 ? 369 ILE   A O   1 
ATOM   490  C  CB  . ILE   A 1 73  ? -44.663 -19.126 12.644 1.00 100.30 ? 369 ILE   A CB  1 
ATOM   491  C  CG1 . ILE   A 1 73  ? -44.302 -20.595 12.422 1.00 101.60 ? 369 ILE   A CG1 1 
ATOM   492  C  CG2 . ILE   A 1 73  ? -43.436 -18.225 12.454 1.00 96.29  ? 369 ILE   A CG2 1 
ATOM   493  C  CD1 . ILE   A 1 73  ? -43.582 -20.849 11.109 1.00 100.22 ? 369 ILE   A CD1 1 
ATOM   494  N  N   . LYS   A 1 74  ? -46.875 -20.285 15.285 1.00 111.62 ? 370 LYS   A N   1 
ATOM   495  C  CA  . LYS   A 1 74  ? -48.123 -20.981 15.602 1.00 123.05 ? 370 LYS   A CA  1 
ATOM   496  C  C   . LYS   A 1 74  ? -48.385 -22.160 14.667 1.00 124.90 ? 370 LYS   A C   1 
ATOM   497  O  O   . LYS   A 1 74  ? -49.541 -22.508 14.402 1.00 132.75 ? 370 LYS   A O   1 
ATOM   498  C  CB  . LYS   A 1 74  ? -49.316 -20.016 15.614 1.00 128.62 ? 370 LYS   A CB  1 
ATOM   499  C  CG  . LYS   A 1 74  ? -48.977 -18.677 16.249 1.00 125.99 ? 370 LYS   A CG  1 
ATOM   500  C  CD  . LYS   A 1 74  ? -50.180 -17.963 16.826 1.00 129.57 ? 370 LYS   A CD  1 
ATOM   501  C  CE  . LYS   A 1 74  ? -49.760 -16.604 17.359 1.00 125.58 ? 370 LYS   A CE  1 
ATOM   502  N  NZ  . LYS   A 1 74  ? -50.828 -15.940 18.140 1.00 126.46 ? 370 LYS   A NZ  1 
ATOM   503  N  N   . ARG   A 1 75  ? -47.318 -22.787 14.171 1.00 117.14 ? 371 ARG   A N   1 
ATOM   504  C  CA  . ARG   A 1 75  ? -47.383 -24.046 13.435 1.00 118.13 ? 371 ARG   A CA  1 
ATOM   505  C  C   . ARG   A 1 75  ? -46.385 -25.051 14.008 1.00 120.91 ? 371 ARG   A C   1 
ATOM   506  O  O   . ARG   A 1 75  ? -45.558 -25.618 13.289 1.00 120.99 ? 371 ARG   A O   1 
ATOM   507  C  CB  . ARG   A 1 75  ? -47.133 -23.831 11.949 1.00 112.93 ? 371 ARG   A CB  1 
ATOM   508  C  CG  . ARG   A 1 75  ? -48.133 -22.912 11.283 1.00 119.03 ? 371 ARG   A CG  1 
ATOM   509  C  CD  . ARG   A 1 75  ? -47.433 -21.685 10.730 1.00 121.34 ? 371 ARG   A CD  1 
ATOM   510  N  NE  . ARG   A 1 75  ? -47.746 -21.458 9.324  1.00 126.67 ? 371 ARG   A NE  1 
ATOM   511  C  CZ  . ARG   A 1 75  ? -47.105 -22.042 8.315  1.00 134.47 ? 371 ARG   A CZ  1 
ATOM   512  N  NH1 . ARG   A 1 75  ? -47.445 -21.773 7.056  1.00 134.77 ? 371 ARG   A NH1 1 
ATOM   513  N  NH2 . ARG   A 1 75  ? -46.124 -22.899 8.565  1.00 136.85 ? 371 ARG   A NH2 1 
ATOM   514  N  N   . PHE   A 1 76  ? -46.451 -25.262 15.328 1.00 121.76 ? 372 PHE   A N   1 
ATOM   515  C  CA  . PHE   A 1 76  ? -45.683 -26.309 16.002 1.00 123.86 ? 372 PHE   A CA  1 
ATOM   516  C  C   . PHE   A 1 76  ? -46.164 -27.670 15.515 1.00 131.28 ? 372 PHE   A C   1 
ATOM   517  O  O   . PHE   A 1 76  ? -47.341 -28.009 15.668 1.00 138.93 ? 372 PHE   A O   1 
ATOM   518  C  CB  . PHE   A 1 76  ? -45.851 -26.178 17.525 1.00 126.59 ? 372 PHE   A CB  1 
ATOM   519  C  CG  . PHE   A 1 76  ? -44.970 -27.111 18.370 1.00 126.77 ? 372 PHE   A CG  1 
ATOM   520  C  CD1 . PHE   A 1 76  ? -44.616 -28.385 17.946 1.00 127.98 ? 372 PHE   A CD1 1 
ATOM   521  C  CD2 . PHE   A 1 76  ? -44.527 -26.699 19.621 1.00 131.70 ? 372 PHE   A CD2 1 
ATOM   522  C  CE1 . PHE   A 1 76  ? -43.830 -29.214 18.723 1.00 128.78 ? 372 PHE   A CE1 1 
ATOM   523  C  CE2 . PHE   A 1 76  ? -43.737 -27.533 20.412 1.00 132.37 ? 372 PHE   A CE2 1 
ATOM   524  C  CZ  . PHE   A 1 76  ? -43.391 -28.790 19.958 1.00 131.90 ? 372 PHE   A CZ  1 
ATOM   525  N  N   . GLY   A 1 77  ? -45.250 -28.457 14.951 1.00 133.51 ? 373 GLY   A N   1 
ATOM   526  C  CA  . GLY   A 1 77  ? -45.543 -29.831 14.596 1.00 139.18 ? 373 GLY   A CA  1 
ATOM   527  C  C   . GLY   A 1 77  ? -46.367 -30.023 13.343 1.00 141.39 ? 373 GLY   A C   1 
ATOM   528  O  O   . GLY   A 1 77  ? -46.707 -31.169 13.013 1.00 145.15 ? 373 GLY   A O   1 
ATOM   529  N  N   . SER   A 1 78  ? -46.696 -28.950 12.627 1.00 140.01 ? 374 SER   A N   1 
ATOM   530  C  CA  . SER   A 1 78  ? -47.410 -29.069 11.366 1.00 139.03 ? 374 SER   A CA  1 
ATOM   531  C  C   . SER   A 1 78  ? -46.584 -29.881 10.378 1.00 134.22 ? 374 SER   A C   1 
ATOM   532  O  O   . SER   A 1 78  ? -45.450 -30.271 10.684 1.00 131.81 ? 374 SER   A O   1 
ATOM   533  C  CB  . SER   A 1 78  ? -47.727 -27.683 10.801 1.00 136.51 ? 374 SER   A CB  1 
ATOM   534  O  OG  . SER   A 1 78  ? -46.551 -26.897 10.695 1.00 131.03 ? 374 SER   A OG  1 
ATOM   535  N  N   . LYS   A 1 79  ? -47.146 -30.161 9.199  1.00 127.87 ? 375 LYS   A N   1 
ATOM   536  C  CA  . LYS   A 1 79  ? -46.357 -30.801 8.153  1.00 124.90 ? 375 LYS   A CA  1 
ATOM   537  C  C   . LYS   A 1 79  ? -45.109 -29.984 7.845  1.00 115.46 ? 375 LYS   A C   1 
ATOM   538  O  O   . LYS   A 1 79  ? -44.020 -30.544 7.668  1.00 113.38 ? 375 LYS   A O   1 
ATOM   539  C  CB  . LYS   A 1 79  ? -47.198 -30.993 6.890  1.00 128.56 ? 375 LYS   A CB  1 
ATOM   540  C  CG  . LYS   A 1 79  ? -46.531 -31.850 5.806  1.00 130.34 ? 375 LYS   A CG  1 
ATOM   541  C  CD  . LYS   A 1 79  ? -46.961 -33.315 5.891  1.00 134.27 ? 375 LYS   A CD  1 
ATOM   542  C  CE  . LYS   A 1 79  ? -46.151 -34.208 4.956  1.00 128.67 ? 375 LYS   A CE  1 
ATOM   543  N  NZ  . LYS   A 1 79  ? -44.778 -34.466 5.475  1.00 124.26 ? 375 LYS   A NZ  1 
ATOM   544  N  N   . ALA   A 1 80  ? -45.245 -28.655 7.811  1.00 116.82 ? 376 ALA   A N   1 
ATOM   545  C  CA  . ALA   A 1 80  ? -44.113 -27.796 7.476  1.00 114.43 ? 376 ALA   A CA  1 
ATOM   546  C  C   . ALA   A 1 80  ? -42.963 -27.983 8.460  1.00 110.22 ? 376 ALA   A C   1 
ATOM   547  O  O   . ALA   A 1 80  ? -41.800 -28.077 8.051  1.00 111.06 ? 376 ALA   A O   1 
ATOM   548  C  CB  . ALA   A 1 80  ? -44.563 -26.334 7.429  1.00 109.26 ? 376 ALA   A CB  1 
ATOM   549  N  N   . HIS   A 1 81  ? -43.271 -28.055 9.760  1.00 108.19 ? 377 HIS   A N   1 
ATOM   550  C  CA  . HIS   A 1 81  ? -42.237 -28.266 10.774 1.00 105.09 ? 377 HIS   A CA  1 
ATOM   551  C  C   . HIS   A 1 81  ? -41.598 -29.644 10.638 1.00 102.82 ? 377 HIS   A C   1 
ATOM   552  O  O   . HIS   A 1 81  ? -40.371 -29.782 10.716 1.00 98.62  ? 377 HIS   A O   1 
ATOM   553  C  CB  . HIS   A 1 81  ? -42.836 -28.090 12.170 1.00 107.19 ? 377 HIS   A CB  1 
ATOM   554  C  CG  . HIS   A 1 81  ? -41.902 -28.444 13.293 1.00 114.20 ? 377 HIS   A CG  1 
ATOM   555  N  ND1 . HIS   A 1 81  ? -42.350 -28.689 14.574 1.00 117.55 ? 377 HIS   A ND1 1 
ATOM   556  C  CD2 . HIS   A 1 81  ? -40.553 -28.575 13.338 1.00 112.82 ? 377 HIS   A CD2 1 
ATOM   557  C  CE1 . HIS   A 1 81  ? -41.321 -28.966 15.355 1.00 115.95 ? 377 HIS   A CE1 1 
ATOM   558  N  NE2 . HIS   A 1 81  ? -40.219 -28.903 14.631 1.00 114.29 ? 377 HIS   A NE2 1 
ATOM   559  N  N   . MET   A 1 82  ? -42.415 -30.681 10.459 1.00 105.33 ? 378 MET   A N   1 
ATOM   560  C  CA  . MET   A 1 82  ? -41.866 -32.027 10.335 1.00 116.24 ? 378 MET   A CA  1 
ATOM   561  C  C   . MET   A 1 82  ? -40.974 -32.159 9.105  1.00 117.13 ? 378 MET   A C   1 
ATOM   562  O  O   . MET   A 1 82  ? -39.930 -32.821 9.158  1.00 117.87 ? 378 MET   A O   1 
ATOM   563  C  CB  . MET   A 1 82  ? -42.999 -33.050 10.298 1.00 127.13 ? 378 MET   A CB  1 
ATOM   564  C  CG  . MET   A 1 82  ? -43.709 -33.204 11.632 1.00 138.20 ? 378 MET   A CG  1 
ATOM   565  S  SD  . MET   A 1 82  ? -42.577 -33.673 12.966 1.00 141.35 ? 378 MET   A SD  1 
ATOM   566  C  CE  . MET   A 1 82  ? -42.455 -32.156 13.915 1.00 139.89 ? 378 MET   A CE  1 
ATOM   567  N  N   . ASP   A 1 83  ? -41.359 -31.527 7.990  1.00 112.69 ? 379 ASP   A N   1 
ATOM   568  C  CA  . ASP   A 1 83  ? -40.542 -31.616 6.782  1.00 110.25 ? 379 ASP   A CA  1 
ATOM   569  C  C   . ASP   A 1 83  ? -39.238 -30.845 6.934  1.00 106.24 ? 379 ASP   A C   1 
ATOM   570  O  O   . ASP   A 1 83  ? -38.194 -31.288 6.443  1.00 104.19 ? 379 ASP   A O   1 
ATOM   571  C  CB  . ASP   A 1 83  ? -41.314 -31.103 5.566  1.00 116.42 ? 379 ASP   A CB  1 
ATOM   572  C  CG  . ASP   A 1 83  ? -42.258 -32.139 4.993  1.00 127.88 ? 379 ASP   A CG  1 
ATOM   573  O  OD1 . ASP   A 1 83  ? -43.432 -31.792 4.747  1.00 131.74 ? 379 ASP   A OD1 1 
ATOM   574  O  OD2 . ASP   A 1 83  ? -41.832 -33.298 4.794  1.00 133.82 ? 379 ASP   A OD2 1 
ATOM   575  N  N   . ARG   A 1 84  ? -39.285 -29.679 7.589  1.00 96.03  ? 380 ARG   A N   1 
ATOM   576  C  CA  . ARG   A 1 84  ? -38.077 -28.884 7.802  1.00 97.86  ? 380 ARG   A CA  1 
ATOM   577  C  C   . ARG   A 1 84  ? -37.118 -29.560 8.774  1.00 100.40 ? 380 ARG   A C   1 
ATOM   578  O  O   . ARG   A 1 84  ? -35.897 -29.399 8.652  1.00 101.17 ? 380 ARG   A O   1 
ATOM   579  C  CB  . ARG   A 1 84  ? -38.446 -27.495 8.323  1.00 93.35  ? 380 ARG   A CB  1 
ATOM   580  C  CG  . ARG   A 1 84  ? -37.254 -26.619 8.661  1.00 91.37  ? 380 ARG   A CG  1 
ATOM   581  C  CD  . ARG   A 1 84  ? -37.019 -25.597 7.581  1.00 94.48  ? 380 ARG   A CD  1 
ATOM   582  N  NE  . ARG   A 1 84  ? -35.743 -24.907 7.740  1.00 92.13  ? 380 ARG   A NE  1 
ATOM   583  C  CZ  . ARG   A 1 84  ? -34.644 -25.232 7.069  1.00 85.44  ? 380 ARG   A CZ  1 
ATOM   584  N  NH1 . ARG   A 1 84  ? -34.682 -26.234 6.215  1.00 81.94  ? 380 ARG   A NH1 1 
ATOM   585  N  NH2 . ARG   A 1 84  ? -33.510 -24.565 7.252  1.00 79.09  ? 380 ARG   A NH2 1 
ATOM   586  N  N   . LEU   A 1 85  ? -37.645 -30.288 9.761  1.00 98.56  ? 381 LEU   A N   1 
ATOM   587  C  CA  . LEU   A 1 85  ? -36.794 -31.102 10.616 1.00 97.80  ? 381 LEU   A CA  1 
ATOM   588  C  C   . LEU   A 1 85  ? -36.052 -32.146 9.794  1.00 105.37 ? 381 LEU   A C   1 
ATOM   589  O  O   . LEU   A 1 85  ? -34.820 -32.229 9.828  1.00 105.88 ? 381 LEU   A O   1 
ATOM   590  C  CB  . LEU   A 1 85  ? -37.640 -31.771 11.697 1.00 108.25 ? 381 LEU   A CB  1 
ATOM   591  C  CG  . LEU   A 1 85  ? -36.986 -31.889 13.073 1.00 105.95 ? 381 LEU   A CG  1 
ATOM   592  C  CD1 . LEU   A 1 85  ? -36.852 -30.514 13.690 1.00 101.62 ? 381 LEU   A CD1 1 
ATOM   593  C  CD2 . LEU   A 1 85  ? -37.792 -32.819 13.961 1.00 114.37 ? 381 LEU   A CD2 1 
ATOM   594  N  N   . GLU   A 1 86  ? -36.803 -32.949 9.034  1.00 114.09 ? 382 GLU   A N   1 
ATOM   595  C  CA  . GLU   A 1 86  ? -36.202 -33.984 8.197  1.00 116.89 ? 382 GLU   A CA  1 
ATOM   596  C  C   . GLU   A 1 86  ? -35.225 -33.387 7.193  1.00 104.24 ? 382 GLU   A C   1 
ATOM   597  O  O   . GLU   A 1 86  ? -34.151 -33.949 6.947  1.00 105.81 ? 382 GLU   A O   1 
ATOM   598  C  CB  . GLU   A 1 86  ? -37.304 -34.764 7.480  1.00 133.16 ? 382 GLU   A CB  1 
ATOM   599  C  CG  . GLU   A 1 86  ? -36.829 -35.992 6.719  1.00 152.87 ? 382 GLU   A CG  1 
ATOM   600  C  CD  . GLU   A 1 86  ? -36.498 -37.179 7.616  1.00 170.80 ? 382 GLU   A CD  1 
ATOM   601  O  OE1 . GLU   A 1 86  ? -35.973 -38.187 7.092  1.00 179.47 ? 382 GLU   A OE1 1 
ATOM   602  O  OE2 . GLU   A 1 86  ? -36.765 -37.113 8.837  1.00 176.12 ? 382 GLU   A OE2 1 
ATOM   603  N  N   . GLU   A 1 87  ? -35.575 -32.236 6.619  1.00 99.51  ? 383 GLU   A N   1 
ATOM   604  C  CA  . GLU   A 1 87  ? -34.716 -31.571 5.643  1.00 93.86  ? 383 GLU   A CA  1 
ATOM   605  C  C   . GLU   A 1 87  ? -33.381 -31.144 6.258  1.00 94.12  ? 383 GLU   A C   1 
ATOM   606  O  O   . GLU   A 1 87  ? -32.315 -31.369 5.668  1.00 83.53  ? 383 GLU   A O   1 
ATOM   607  C  CB  . GLU   A 1 87  ? -35.462 -30.369 5.064  1.00 96.82  ? 383 GLU   A CB  1 
ATOM   608  C  CG  . GLU   A 1 87  ? -34.615 -29.471 4.203  1.00 104.69 ? 383 GLU   A CG  1 
ATOM   609  C  CD  . GLU   A 1 87  ? -35.409 -28.325 3.603  1.00 105.00 ? 383 GLU   A CD  1 
ATOM   610  O  OE1 . GLU   A 1 87  ? -36.077 -27.588 4.368  1.00 101.85 ? 383 GLU   A OE1 1 
ATOM   611  O  OE2 . GLU   A 1 87  ? -35.366 -28.170 2.362  1.00 95.20  ? 383 GLU   A OE2 1 
ATOM   612  N  N   . VAL   A 1 88  ? -33.421 -30.506 7.437  1.00 85.37  ? 384 VAL   A N   1 
ATOM   613  C  CA  . VAL   A 1 88  ? -32.193 -30.063 8.102  1.00 86.48  ? 384 VAL   A CA  1 
ATOM   614  C  C   . VAL   A 1 88  ? -31.398 -31.260 8.611  1.00 93.48  ? 384 VAL   A C   1 
ATOM   615  O  O   . VAL   A 1 88  ? -30.161 -31.265 8.571  1.00 89.36  ? 384 VAL   A O   1 
ATOM   616  C  CB  . VAL   A 1 88  ? -32.521 -29.081 9.245  1.00 87.00  ? 384 VAL   A CB  1 
ATOM   617  C  CG1 . VAL   A 1 88  ? -31.273 -28.766 10.072 1.00 77.75  ? 384 VAL   A CG1 1 
ATOM   618  C  CG2 . VAL   A 1 88  ? -33.121 -27.794 8.703  1.00 92.04  ? 384 VAL   A CG2 1 
ATOM   619  N  N   . ASN   A 1 89  ? -32.095 -32.279 9.124  1.00 107.10 ? 385 ASN   A N   1 
ATOM   620  C  CA  . ASN   A 1 89  ? -31.446 -33.535 9.491  1.00 121.24 ? 385 ASN   A CA  1 
ATOM   621  C  C   . ASN   A 1 89  ? -30.613 -34.074 8.332  1.00 125.23 ? 385 ASN   A C   1 
ATOM   622  O  O   . ASN   A 1 89  ? -29.416 -34.347 8.480  1.00 134.30 ? 385 ASN   A O   1 
ATOM   623  C  CB  . ASN   A 1 89  ? -32.509 -34.556 9.910  1.00 132.20 ? 385 ASN   A CB  1 
ATOM   624  C  CG  . ASN   A 1 89  ? -31.918 -35.790 10.574 1.00 141.54 ? 385 ASN   A CG  1 
ATOM   625  O  OD1 . ASN   A 1 89  ? -31.076 -35.687 11.470 1.00 142.79 ? 385 ASN   A OD1 1 
ATOM   626  N  ND2 . ASN   A 1 89  ? -32.366 -36.969 10.139 1.00 143.76 ? 385 ASN   A ND2 1 
ATOM   627  N  N   . LYS   A 1 90  ? -31.232 -34.210 7.159  1.00 112.01 ? 386 LYS   A N   1 
ATOM   628  C  CA  . LYS   A 1 90  ? -30.531 -34.766 6.008  1.00 117.76 ? 386 LYS   A CA  1 
ATOM   629  C  C   . LYS   A 1 90  ? -29.421 -33.844 5.511  1.00 117.43 ? 386 LYS   A C   1 
ATOM   630  O  O   . LYS   A 1 90  ? -28.421 -34.325 4.965  1.00 114.04 ? 386 LYS   A O   1 
ATOM   631  C  CB  . LYS   A 1 90  ? -31.529 -35.046 4.882  1.00 121.42 ? 386 LYS   A CB  1 
ATOM   632  C  CG  . LYS   A 1 90  ? -32.558 -36.124 5.202  1.00 127.47 ? 386 LYS   A CG  1 
ATOM   633  C  CD  . LYS   A 1 90  ? -33.788 -35.985 4.313  1.00 130.04 ? 386 LYS   A CD  1 
ATOM   634  C  CE  . LYS   A 1 90  ? -34.612 -37.266 4.283  1.00 133.67 ? 386 LYS   A CE  1 
ATOM   635  N  NZ  . LYS   A 1 90  ? -35.949 -37.040 3.663  1.00 132.15 ? 386 LYS   A NZ  1 
ATOM   636  N  N   . GLU   A 1 91  ? -29.577 -32.525 5.674  1.00 111.30 ? 387 GLU   A N   1 
ATOM   637  C  CA  . GLU   A 1 91  ? -28.507 -31.619 5.271  1.00 105.68 ? 387 GLU   A CA  1 
ATOM   638  C  C   . GLU   A 1 91  ? -27.315 -31.718 6.214  1.00 103.01 ? 387 GLU   A C   1 
ATOM   639  O  O   . GLU   A 1 91  ? -26.171 -31.520 5.788  1.00 99.23  ? 387 GLU   A O   1 
ATOM   640  C  CB  . GLU   A 1 91  ? -29.017 -30.178 5.208  1.00 101.63 ? 387 GLU   A CB  1 
ATOM   641  C  CG  . GLU   A 1 91  ? -27.951 -29.179 4.767  1.00 97.25  ? 387 GLU   A CG  1 
ATOM   642  C  CD  . GLU   A 1 91  ? -28.486 -27.776 4.567  1.00 99.28  ? 387 GLU   A CD  1 
ATOM   643  O  OE1 . GLU   A 1 91  ? -27.727 -26.930 4.047  1.00 99.98  ? 387 GLU   A OE1 1 
ATOM   644  O  OE2 . GLU   A 1 91  ? -29.652 -27.513 4.932  1.00 104.25 ? 387 GLU   A OE2 1 
ATOM   645  N  N   . ILE   A 1 92  ? -27.564 -32.015 7.493  1.00 106.72 ? 388 ILE   A N   1 
ATOM   646  C  CA  . ILE   A 1 92  ? -26.479 -32.311 8.419  1.00 100.80 ? 388 ILE   A CA  1 
ATOM   647  C  C   . ILE   A 1 92  ? -25.878 -33.691 8.157  1.00 106.09 ? 388 ILE   A C   1 
ATOM   648  O  O   . ILE   A 1 92  ? -24.713 -33.931 8.496  1.00 105.77 ? 388 ILE   A O   1 
ATOM   649  C  CB  . ILE   A 1 92  ? -26.963 -32.185 9.874  1.00 96.06  ? 388 ILE   A CB  1 
ATOM   650  C  CG1 . ILE   A 1 92  ? -27.571 -30.798 10.129 1.00 91.24  ? 388 ILE   A CG1 1 
ATOM   651  C  CG2 . ILE   A 1 92  ? -25.812 -32.401 10.825 1.00 97.19  ? 388 ILE   A CG2 1 
ATOM   652  C  CD1 . ILE   A 1 92  ? -28.227 -30.642 11.502 1.00 83.56  ? 388 ILE   A CD1 1 
ATOM   653  N  N   . GLU   A 1 93  ? -26.625 -34.613 7.553  1.00 114.40 ? 389 GLU   A N   1 
ATOM   654  C  CA  . GLU   A 1 93  ? -25.982 -35.821 7.048  1.00 121.95 ? 389 GLU   A CA  1 
ATOM   655  C  C   . GLU   A 1 93  ? -25.059 -35.480 5.885  1.00 118.61 ? 389 GLU   A C   1 
ATOM   656  O  O   . GLU   A 1 93  ? -23.863 -35.796 5.912  1.00 110.02 ? 389 GLU   A O   1 
ATOM   657  C  CB  . GLU   A 1 93  ? -27.033 -36.850 6.622  1.00 130.94 ? 389 GLU   A CB  1 
ATOM   658  C  CG  . GLU   A 1 93  ? -27.963 -37.313 7.736  1.00 140.30 ? 389 GLU   A CG  1 
ATOM   659  C  CD  . GLU   A 1 93  ? -27.308 -38.300 8.688  1.00 148.56 ? 389 GLU   A CD  1 
ATOM   660  O  OE1 . GLU   A 1 93  ? -26.215 -38.810 8.360  1.00 150.91 ? 389 GLU   A OE1 1 
ATOM   661  O  OE2 . GLU   A 1 93  ? -27.889 -38.568 9.766  1.00 150.77 ? 389 GLU   A OE2 1 
ATOM   662  N  N   . SER   A 1 94  ? -25.596 -34.780 4.882  1.00 129.19 ? 390 SER   A N   1 
ATOM   663  C  CA  . SER   A 1 94  ? -24.895 -34.565 3.621  1.00 137.19 ? 390 SER   A CA  1 
ATOM   664  C  C   . SER   A 1 94  ? -23.654 -33.700 3.809  1.00 137.55 ? 390 SER   A C   1 
ATOM   665  O  O   . SER   A 1 94  ? -22.551 -34.083 3.400  1.00 135.52 ? 390 SER   A O   1 
ATOM   666  C  CB  . SER   A 1 94  ? -25.851 -33.931 2.609  1.00 137.58 ? 390 SER   A CB  1 
ATOM   667  O  OG  . SER   A 1 94  ? -25.346 -32.695 2.139  1.00 138.05 ? 390 SER   A OG  1 
ATOM   668  N  N   . THR   A 1 95  ? -23.816 -32.528 4.435  1.00 137.81 ? 391 THR   A N   1 
ATOM   669  C  CA  . THR   A 1 95  ? -22.740 -31.550 4.572  1.00 137.55 ? 391 THR   A CA  1 
ATOM   670  C  C   . THR   A 1 95  ? -22.109 -31.522 5.955  1.00 129.67 ? 391 THR   A C   1 
ATOM   671  O  O   . THR   A 1 95  ? -21.067 -30.878 6.124  1.00 121.45 ? 391 THR   A O   1 
ATOM   672  C  CB  . THR   A 1 95  ? -23.246 -30.133 4.257  1.00 140.60 ? 391 THR   A CB  1 
ATOM   673  O  OG1 . THR   A 1 95  ? -24.494 -30.204 3.558  1.00 146.87 ? 391 THR   A OG1 1 
ATOM   674  C  CG2 . THR   A 1 95  ? -22.228 -29.377 3.406  1.00 138.27 ? 391 THR   A CG2 1 
ATOM   675  N  N   . SER   A 1 96  ? -22.714 -32.187 6.941  1.00 135.18 ? 392 SER   A N   1 
ATOM   676  C  CA  . SER   A 1 96  ? -22.343 -32.084 8.353  1.00 136.30 ? 392 SER   A CA  1 
ATOM   677  C  C   . SER   A 1 96  ? -22.480 -30.656 8.875  1.00 123.67 ? 392 SER   A C   1 
ATOM   678  O  O   . SER   A 1 96  ? -21.809 -30.272 9.838  1.00 127.81 ? 392 SER   A O   1 
ATOM   679  C  CB  . SER   A 1 96  ? -20.932 -32.626 8.613  1.00 147.44 ? 392 SER   A CB  1 
ATOM   680  O  OG  . SER   A 1 96  ? -19.942 -31.794 8.039  1.00 151.08 ? 392 SER   A OG  1 
ATOM   681  N  N   . THR   A 1 97  ? -23.339 -29.869 8.234  1.00 107.51 ? 393 THR   A N   1 
ATOM   682  C  CA  . THR   A 1 97  ? -23.756 -28.542 8.677  1.00 88.28  ? 393 THR   A CA  1 
ATOM   683  C  C   . THR   A 1 97  ? -25.144 -28.299 8.092  1.00 87.86  ? 393 THR   A C   1 
ATOM   684  O  O   . THR   A 1 97  ? -25.749 -29.204 7.512  1.00 90.59  ? 393 THR   A O   1 
ATOM   685  C  CB  . THR   A 1 97  ? -22.749 -27.468 8.245  1.00 82.01  ? 393 THR   A CB  1 
ATOM   686  O  OG1 . THR   A 1 97  ? -23.068 -26.228 8.887  1.00 87.01  ? 393 THR   A OG1 1 
ATOM   687  C  CG2 . THR   A 1 97  ? -22.810 -27.260 6.726  1.00 81.90  ? 393 THR   A CG2 1 
ATOM   688  N  N   . TYR   A 1 98  ? -25.663 -27.082 8.225  1.00 79.37  ? 394 TYR   A N   1 
ATOM   689  C  CA  . TYR   A 1 98  ? -26.888 -26.762 7.501  1.00 81.27  ? 394 TYR   A CA  1 
ATOM   690  C  C   . TYR   A 1 98  ? -26.993 -25.248 7.319  1.00 74.08  ? 394 TYR   A C   1 
ATOM   691  O  O   . TYR   A 1 98  ? -26.138 -24.481 7.770  1.00 77.98  ? 394 TYR   A O   1 
ATOM   692  C  CB  . TYR   A 1 98  ? -28.114 -27.365 8.198  1.00 75.30  ? 394 TYR   A CB  1 
ATOM   693  C  CG  . TYR   A 1 98  ? -28.484 -26.710 9.490  1.00 75.38  ? 394 TYR   A CG  1 
ATOM   694  C  CD1 . TYR   A 1 98  ? -29.459 -25.722 9.533  1.00 73.72  ? 394 TYR   A CD1 1 
ATOM   695  C  CD2 . TYR   A 1 98  ? -27.860 -27.077 10.688 1.00 78.78  ? 394 TYR   A CD2 1 
ATOM   696  C  CE1 . TYR   A 1 98  ? -29.800 -25.104 10.729 1.00 73.87  ? 394 TYR   A CE1 1 
ATOM   697  C  CE2 . TYR   A 1 98  ? -28.202 -26.477 11.882 1.00 67.13  ? 394 TYR   A CE2 1 
ATOM   698  C  CZ  . TYR   A 1 98  ? -29.172 -25.494 11.901 1.00 69.32  ? 394 TYR   A CZ  1 
ATOM   699  O  OH  . TYR   A 1 98  ? -29.501 -24.888 13.091 1.00 73.80  ? 394 TYR   A OH  1 
ATOM   700  N  N   . GLN   A 1 99  ? -28.038 -24.826 6.609  1.00 82.00  ? 395 GLN   A N   1 
ATOM   701  C  CA  . GLN   A 1 99  ? -28.255 -23.424 6.267  1.00 75.18  ? 395 GLN   A CA  1 
ATOM   702  C  C   . GLN   A 1 99  ? -29.613 -22.968 6.787  1.00 73.89  ? 395 GLN   A C   1 
ATOM   703  O  O   . GLN   A 1 99  ? -30.601 -23.707 6.716  1.00 76.45  ? 395 GLN   A O   1 
ATOM   704  C  CB  . GLN   A 1 99  ? -28.168 -23.189 4.743  1.00 79.40  ? 395 GLN   A CB  1 
ATOM   705  C  CG  . GLN   A 1 99  ? -26.805 -23.503 4.124  1.00 66.64  ? 395 GLN   A CG  1 
ATOM   706  C  CD  . GLN   A 1 99  ? -25.711 -22.570 4.610  1.00 76.92  ? 395 GLN   A CD  1 
ATOM   707  O  OE1 . GLN   A 1 99  ? -25.915 -21.362 4.722  1.00 82.83  ? 395 GLN   A OE1 1 
ATOM   708  N  NE2 . GLN   A 1 99  ? -24.543 -23.130 4.907  1.00 77.97  ? 395 GLN   A NE2 1 
ATOM   709  N  N   . LEU   A 1 100 ? -29.659 -21.742 7.300  1.00 63.95  ? 396 LEU   A N   1 
ATOM   710  C  CA  . LEU   A 1 100 ? -30.885 -21.181 7.850  1.00 65.81  ? 396 LEU   A CA  1 
ATOM   711  C  C   . LEU   A 1 100 ? -31.717 -20.518 6.757  1.00 70.49  ? 396 LEU   A C   1 
ATOM   712  O  O   . LEU   A 1 100 ? -31.173 -19.887 5.847  1.00 73.38  ? 396 LEU   A O   1 
ATOM   713  C  CB  . LEU   A 1 100 ? -30.570 -20.156 8.941  1.00 60.75  ? 396 LEU   A CB  1 
ATOM   714  C  CG  . LEU   A 1 100 ? -29.951 -20.674 10.242 1.00 68.12  ? 396 LEU   A CG  1 
ATOM   715  C  CD1 . LEU   A 1 100 ? -29.358 -19.525 11.025 1.00 66.93  ? 396 LEU   A CD1 1 
ATOM   716  C  CD2 . LEU   A 1 100 ? -30.987 -21.393 11.084 1.00 68.40  ? 396 LEU   A CD2 1 
ATOM   717  N  N   . LYS   A 1 101 ? -33.042 -20.666 6.862  1.00 69.59  ? 397 LYS   A N   1 
ATOM   718  C  CA  . LYS   A 1 101 ? -33.972 -19.880 6.062  1.00 75.40  ? 397 LYS   A CA  1 
ATOM   719  C  C   . LYS   A 1 101 ? -33.878 -18.409 6.447  1.00 81.58  ? 397 LYS   A C   1 
ATOM   720  O  O   . LYS   A 1 101 ? -33.520 -18.068 7.575  1.00 83.37  ? 397 LYS   A O   1 
ATOM   721  C  CB  . LYS   A 1 101 ? -35.406 -20.364 6.271  1.00 76.91  ? 397 LYS   A CB  1 
ATOM   722  C  CG  . LYS   A 1 101 ? -35.666 -21.761 5.772  1.00 85.01  ? 397 LYS   A CG  1 
ATOM   723  C  CD  . LYS   A 1 101 ? -35.378 -21.819 4.305  1.00 83.15  ? 397 LYS   A CD  1 
ATOM   724  C  CE  . LYS   A 1 101 ? -35.539 -23.205 3.751  1.00 93.59  ? 397 LYS   A CE  1 
ATOM   725  N  NZ  . LYS   A 1 101 ? -35.262 -23.152 2.285  1.00 91.63  ? 397 LYS   A NZ  1 
ATOM   726  N  N   . ASP   A 1 102 ? -34.196 -17.534 5.489  1.00 70.65  ? 398 ASP   A N   1 
ATOM   727  C  CA  . ASP   A 1 102 ? -34.258 -16.100 5.778  1.00 69.26  ? 398 ASP   A CA  1 
ATOM   728  C  C   . ASP   A 1 102 ? -35.117 -15.818 7.003  1.00 64.47  ? 398 ASP   A C   1 
ATOM   729  O  O   . ASP   A 1 102 ? -34.714 -15.073 7.908  1.00 67.55  ? 398 ASP   A O   1 
ATOM   730  C  CB  . ASP   A 1 102 ? -34.823 -15.343 4.573  1.00 86.16  ? 398 ASP   A CB  1 
ATOM   731  C  CG  . ASP   A 1 102 ? -33.797 -15.104 3.492  1.00 92.47  ? 398 ASP   A CG  1 
ATOM   732  O  OD1 . ASP   A 1 102 ? -32.667 -15.634 3.583  1.00 92.39  ? 398 ASP   A OD1 1 
ATOM   733  O  OD2 . ASP   A 1 102 ? -34.133 -14.365 2.547  1.00 98.19  ? 398 ASP   A OD2 1 
ATOM   734  N  N   . THR   A 1 103 ? -36.315 -16.403 7.047  1.00 65.32  ? 399 THR   A N   1 
ATOM   735  C  CA  . THR   A 1 103 ? -37.176 -16.222 8.217  1.00 69.17  ? 399 THR   A CA  1 
ATOM   736  C  C   . THR   A 1 103 ? -36.526 -16.771 9.486  1.00 72.49  ? 399 THR   A C   1 
ATOM   737  O  O   . THR   A 1 103 ? -36.670 -16.191 10.571 1.00 64.49  ? 399 THR   A O   1 
ATOM   738  C  CB  . THR   A 1 103 ? -38.524 -16.900 7.978  1.00 79.44  ? 399 THR   A CB  1 
ATOM   739  O  OG1 . THR   A 1 103 ? -38.303 -18.259 7.589  1.00 76.68  ? 399 THR   A OG1 1 
ATOM   740  C  CG2 . THR   A 1 103 ? -39.302 -16.188 6.876  1.00 78.73  ? 399 THR   A CG2 1 
ATOM   741  N  N   . GLU   A 1 104 ? -35.802 -17.888 9.374  1.00 77.17  ? 400 GLU   A N   1 
ATOM   742  C  CA  . GLU   A 1 104 ? -35.162 -18.482 10.547 1.00 69.91  ? 400 GLU   A CA  1 
ATOM   743  C  C   . GLU   A 1 104 ? -34.018 -17.608 11.051 1.00 67.40  ? 400 GLU   A C   1 
ATOM   744  O  O   . GLU   A 1 104 ? -33.810 -17.472 12.274 1.00 64.25  ? 400 GLU   A O   1 
ATOM   745  C  CB  . GLU   A 1 104 ? -34.672 -19.893 10.204 1.00 71.30  ? 400 GLU   A CB  1 
ATOM   746  C  CG  . GLU   A 1 104 ? -35.805 -20.893 9.973  1.00 70.00  ? 400 GLU   A CG  1 
ATOM   747  C  CD  . GLU   A 1 104 ? -35.365 -22.192 9.311  1.00 81.38  ? 400 GLU   A CD  1 
ATOM   748  O  OE1 . GLU   A 1 104 ? -36.248 -23.041 9.060  1.00 88.36  ? 400 GLU   A OE1 1 
ATOM   749  O  OE2 . GLU   A 1 104 ? -34.156 -22.369 9.030  1.00 81.15  ? 400 GLU   A OE2 1 
ATOM   750  N  N   . LEU   A 1 105 ? -33.265 -17.007 10.122 1.00 58.41  ? 401 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 105 ? -32.183 -16.097 10.494 1.00 63.70  ? 401 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 105 ? -32.714 -14.854 11.208 1.00 64.29  ? 401 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 105 ? -32.101 -14.374 12.172 1.00 54.71  ? 401 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 105 ? -31.375 -15.711 9.243  1.00 64.73  ? 401 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 105 ? -30.032 -14.985 9.414  1.00 61.40  ? 401 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 105 ? -28.931 -15.901 9.963  1.00 58.06  ? 401 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 105 ? -29.624 -14.401 8.084  1.00 68.96  ? 401 LEU   A CD2 1 
ATOM   758  N  N   . ILE   A 1 106 ? -33.870 -14.338 10.786 1.00 56.47  ? 402 ILE   A N   1 
ATOM   759  C  CA  . ILE   A 1 106 ? -34.402 -13.123 11.411 1.00 51.68  ? 402 ILE   A CA  1 
ATOM   760  C  C   . ILE   A 1 106 ? -34.922 -13.433 12.814 1.00 58.77  ? 402 ILE   A C   1 
ATOM   761  O  O   . ILE   A 1 106 ? -34.671 -12.687 13.771 1.00 62.19  ? 402 ILE   A O   1 
ATOM   762  C  CB  . ILE   A 1 106 ? -35.474 -12.510 10.481 1.00 62.01  ? 402 ILE   A CB  1 
ATOM   763  C  CG1 . ILE   A 1 106 ? -34.799 -11.917 9.234  1.00 60.61  ? 402 ILE   A CG1 1 
ATOM   764  C  CG2 . ILE   A 1 106 ? -36.290 -11.452 11.162 1.00 65.45  ? 402 ILE   A CG2 1 
ATOM   765  C  CD1 . ILE   A 1 106 ? -35.753 -11.627 8.064  1.00 60.58  ? 402 ILE   A CD1 1 
ATOM   766  N  N   . TYR   A 1 107 ? -35.634 -14.550 12.952 1.00 67.36  ? 403 TYR   A N   1 
ATOM   767  C  CA  . TYR   A 1 107 ? -36.091 -15.023 14.246 1.00 66.92  ? 403 TYR   A CA  1 
ATOM   768  C  C   . TYR   A 1 107 ? -34.913 -15.260 15.185 1.00 68.34  ? 403 TYR   A C   1 
ATOM   769  O  O   . TYR   A 1 107 ? -34.913 -14.795 16.330 1.00 56.04  ? 403 TYR   A O   1 
ATOM   770  C  CB  . TYR   A 1 107 ? -36.905 -16.300 14.051 1.00 71.35  ? 403 TYR   A CB  1 
ATOM   771  C  CG  . TYR   A 1 107 ? -37.282 -16.974 15.342 1.00 77.94  ? 403 TYR   A CG  1 
ATOM   772  C  CD1 . TYR   A 1 107 ? -38.501 -16.713 15.948 1.00 78.76  ? 403 TYR   A CD1 1 
ATOM   773  C  CD2 . TYR   A 1 107 ? -36.414 -17.865 15.968 1.00 79.35  ? 403 TYR   A CD2 1 
ATOM   774  C  CE1 . TYR   A 1 107 ? -38.850 -17.326 17.134 1.00 76.45  ? 403 TYR   A CE1 1 
ATOM   775  C  CE2 . TYR   A 1 107 ? -36.747 -18.470 17.155 1.00 75.32  ? 403 TYR   A CE2 1 
ATOM   776  C  CZ  . TYR   A 1 107 ? -37.967 -18.199 17.734 1.00 79.47  ? 403 TYR   A CZ  1 
ATOM   777  O  OH  . TYR   A 1 107 ? -38.305 -18.806 18.919 1.00 76.66  ? 403 TYR   A OH  1 
ATOM   778  N  N   . GLY   A 1 108 ? -33.896 -15.989 14.714 1.00 66.22  ? 404 GLY   A N   1 
ATOM   779  C  CA  . GLY   A 1 108 ? -32.753 -16.287 15.569 1.00 56.84  ? 404 GLY   A CA  1 
ATOM   780  C  C   . GLY   A 1 108 ? -32.040 -15.039 16.050 1.00 62.07  ? 404 GLY   A C   1 
ATOM   781  O  O   . GLY   A 1 108 ? -31.691 -14.924 17.222 1.00 54.87  ? 404 GLY   A O   1 
ATOM   782  N  N   . ALA   A 1 109 ? -31.817 -14.082 15.150 1.00 68.06  ? 405 ALA   A N   1 
ATOM   783  C  CA  . ALA   A 1 109 ? -31.150 -12.848 15.549 1.00 60.69  ? 405 ALA   A CA  1 
ATOM   784  C  C   . ALA   A 1 109 ? -31.988 -12.076 16.558 1.00 62.33  ? 405 ALA   A C   1 
ATOM   785  O  O   . ALA   A 1 109 ? -31.476 -11.621 17.595 1.00 61.97  ? 405 ALA   A O   1 
ATOM   786  C  CB  . ALA   A 1 109 ? -30.862 -11.987 14.320 1.00 58.59  ? 405 ALA   A CB  1 
ATOM   787  N  N   . LYS   A 1 110 ? -33.287 -11.920 16.282 1.00 56.95  ? 406 LYS   A N   1 
ATOM   788  C  CA  . LYS   A 1 110 ? -34.113 -11.119 17.182 1.00 62.38  ? 406 LYS   A CA  1 
ATOM   789  C  C   . LYS   A 1 110 ? -34.162 -11.722 18.576 1.00 61.06  ? 406 LYS   A C   1 
ATOM   790  O  O   . LYS   A 1 110 ? -34.346 -10.993 19.562 1.00 64.19  ? 406 LYS   A O   1 
ATOM   791  C  CB  . LYS   A 1 110 ? -35.523 -10.968 16.626 1.00 63.25  ? 406 LYS   A CB  1 
ATOM   792  C  CG  . LYS   A 1 110 ? -35.667 -9.842  15.637 1.00 66.10  ? 406 LYS   A CG  1 
ATOM   793  C  CD  . LYS   A 1 110 ? -37.051 -9.832  15.018 1.00 67.08  ? 406 LYS   A CD  1 
ATOM   794  C  CE  . LYS   A 1 110 ? -37.164 -8.709  14.012 1.00 66.72  ? 406 LYS   A CE  1 
ATOM   795  N  NZ  . LYS   A 1 110 ? -38.578 -8.460  13.622 1.00 74.63  ? 406 LYS   A NZ  1 
ATOM   796  N  N   . HIS   A 1 111 ? -33.995 -13.041 18.682 1.00 55.95  ? 407 HIS   A N   1 
ATOM   797  C  CA  . HIS   A 1 111 ? -34.065 -13.705 19.979 1.00 61.05  ? 407 HIS   A CA  1 
ATOM   798  C  C   . HIS   A 1 111 ? -32.719 -13.787 20.682 1.00 66.15  ? 407 HIS   A C   1 
ATOM   799  O  O   . HIS   A 1 111 ? -32.681 -13.815 21.919 1.00 57.26  ? 407 HIS   A O   1 
ATOM   800  C  CB  . HIS   A 1 111 ? -34.673 -15.092 19.816 1.00 63.86  ? 407 HIS   A CB  1 
ATOM   801  C  CG  . HIS   A 1 111 ? -36.156 -15.054 19.645 1.00 63.12  ? 407 HIS   A CG  1 
ATOM   802  N  ND1 . HIS   A 1 111 ? -37.029 -15.300 20.686 1.00 63.09  ? 407 HIS   A ND1 1 
ATOM   803  C  CD2 . HIS   A 1 111 ? -36.923 -14.739 18.573 1.00 62.14  ? 407 HIS   A CD2 1 
ATOM   804  C  CE1 . HIS   A 1 111 ? -38.270 -15.167 20.255 1.00 65.60  ? 407 HIS   A CE1 1 
ATOM   805  N  NE2 . HIS   A 1 111 ? -38.233 -14.824 18.978 1.00 67.16  ? 407 HIS   A NE2 1 
ATOM   806  N  N   . ALA   A 1 112 ? -31.617 -13.815 19.928 1.00 61.29  ? 408 ALA   A N   1 
ATOM   807  C  CA  . ALA   A 1 112 ? -30.308 -13.578 20.529 1.00 56.51  ? 408 ALA   A CA  1 
ATOM   808  C  C   . ALA   A 1 112 ? -30.307 -12.275 21.339 1.00 60.61  ? 408 ALA   A C   1 
ATOM   809  O  O   . ALA   A 1 112 ? -29.877 -12.246 22.504 1.00 57.47  ? 408 ALA   A O   1 
ATOM   810  C  CB  . ALA   A 1 112 ? -29.239 -13.554 19.434 1.00 53.11  ? 408 ALA   A CB  1 
ATOM   811  N  N   . TRP   A 1 113 ? -30.823 -11.190 20.748 1.00 50.08  ? 409 TRP   A N   1 
ATOM   812  C  CA  . TRP   A 1 113 ? -30.982 -9.938  21.490 1.00 48.78  ? 409 TRP   A CA  1 
ATOM   813  C  C   . TRP   A 1 113 ? -31.943 -10.110 22.664 1.00 55.83  ? 409 TRP   A C   1 
ATOM   814  O  O   . TRP   A 1 113 ? -31.617 -9.759  23.816 1.00 51.24  ? 409 TRP   A O   1 
ATOM   815  C  CB  . TRP   A 1 113 ? -31.491 -8.845  20.549 1.00 52.05  ? 409 TRP   A CB  1 
ATOM   816  C  CG  . TRP   A 1 113 ? -31.629 -7.488  21.143 1.00 52.71  ? 409 TRP   A CG  1 
ATOM   817  C  CD1 . TRP   A 1 113 ? -31.229 -7.081  22.391 1.00 56.69  ? 409 TRP   A CD1 1 
ATOM   818  C  CD2 . TRP   A 1 113 ? -32.219 -6.347  20.518 1.00 57.04  ? 409 TRP   A CD2 1 
ATOM   819  N  NE1 . TRP   A 1 113 ? -31.532 -5.754  22.574 1.00 55.84  ? 409 TRP   A NE1 1 
ATOM   820  C  CE2 . TRP   A 1 113 ? -32.129 -5.277  21.431 1.00 53.82  ? 409 TRP   A CE2 1 
ATOM   821  C  CE3 . TRP   A 1 113 ? -32.791 -6.119  19.256 1.00 62.48  ? 409 TRP   A CE3 1 
ATOM   822  C  CZ2 . TRP   A 1 113 ? -32.612 -4.005  21.138 1.00 52.93  ? 409 TRP   A CZ2 1 
ATOM   823  C  CZ3 . TRP   A 1 113 ? -33.269 -4.859  18.960 1.00 62.58  ? 409 TRP   A CZ3 1 
ATOM   824  C  CH2 . TRP   A 1 113 ? -33.180 -3.813  19.906 1.00 62.06  ? 409 TRP   A CH2 1 
ATOM   825  N  N   . ARG   A 1 114 ? -33.143 -10.630 22.388 1.00 52.37  ? 410 ARG   A N   1 
ATOM   826  C  CA  . ARG   A 1 114 ? -34.149 -10.835 23.424 1.00 55.43  ? 410 ARG   A CA  1 
ATOM   827  C  C   . ARG   A 1 114 ? -33.587 -11.571 24.634 1.00 61.13  ? 410 ARG   A C   1 
ATOM   828  O  O   . ARG   A 1 114 ? -34.009 -11.315 25.769 1.00 51.67  ? 410 ARG   A O   1 
ATOM   829  C  CB  . ARG   A 1 114 ? -35.327 -11.614 22.842 1.00 59.66  ? 410 ARG   A CB  1 
ATOM   830  C  CG  . ARG   A 1 114 ? -36.539 -11.628 23.737 1.00 61.61  ? 410 ARG   A CG  1 
ATOM   831  C  CD  . ARG   A 1 114 ? -37.638 -12.495 23.152 1.00 65.64  ? 410 ARG   A CD  1 
ATOM   832  N  NE  . ARG   A 1 114 ? -38.857 -12.385 23.952 1.00 73.97  ? 410 ARG   A NE  1 
ATOM   833  C  CZ  . ARG   A 1 114 ? -40.026 -12.909 23.607 1.00 76.84  ? 410 ARG   A CZ  1 
ATOM   834  N  NH1 . ARG   A 1 114 ? -41.087 -12.755 24.388 1.00 66.83  ? 410 ARG   A NH1 1 
ATOM   835  N  NH2 . ARG   A 1 114 ? -40.133 -13.581 22.470 1.00 79.64  ? 410 ARG   A NH2 1 
ATOM   836  N  N   . ASN   A 1 115 ? -32.617 -12.451 24.412 1.00 60.27  ? 411 ASN   A N   1 
ATOM   837  C  CA  . ASN   A 1 115 ? -32.045 -13.312 25.431 1.00 62.11  ? 411 ASN   A CA  1 
ATOM   838  C  C   . ASN   A 1 115 ? -30.791 -12.744 26.083 1.00 57.56  ? 411 ASN   A C   1 
ATOM   839  O  O   . ASN   A 1 115 ? -30.208 -13.396 26.965 1.00 46.39  ? 411 ASN   A O   1 
ATOM   840  C  CB  . ASN   A 1 115 ? -31.714 -14.654 24.808 1.00 54.78  ? 411 ASN   A CB  1 
ATOM   841  C  CG  . ASN   A 1 115 ? -32.939 -15.434 24.474 1.00 62.07  ? 411 ASN   A CG  1 
ATOM   842  O  OD1 . ASN   A 1 115 ? -34.015 -15.161 25.004 1.00 64.56  ? 411 ASN   A OD1 1 
ATOM   843  N  ND2 . ASN   A 1 115 ? -32.799 -16.415 23.584 1.00 62.04  ? 411 ASN   A ND2 1 
ATOM   844  N  N   . ALA   A 1 116 ? -30.346 -11.574 25.650 1.00 55.68  ? 412 ALA   A N   1 
ATOM   845  C  CA  . ALA   A 1 116 ? -29.091 -10.983 26.099 1.00 59.21  ? 412 ALA   A CA  1 
ATOM   846  C  C   . ALA   A 1 116 ? -29.317 -10.396 27.485 1.00 56.99  ? 412 ALA   A C   1 
ATOM   847  O  O   . ALA   A 1 116 ? -29.856 -9.299  27.627 1.00 50.51  ? 412 ALA   A O   1 
ATOM   848  C  CB  . ALA   A 1 116 ? -28.632 -9.928  25.094 1.00 54.85  ? 412 ALA   A CB  1 
ATOM   849  N  N   . SER   A 1 117 ? -28.899 -11.118 28.531 1.00 55.91  ? 413 SER   A N   1 
ATOM   850  C  CA  . SER   A 1 117 ? -29.308 -10.733 29.873 1.00 57.51  ? 413 SER   A CA  1 
ATOM   851  C  C   . SER   A 1 117 ? -28.594 -9.478  30.373 1.00 56.51  ? 413 SER   A C   1 
ATOM   852  O  O   . SER   A 1 117 ? -29.086 -8.835  31.305 1.00 52.77  ? 413 SER   A O   1 
ATOM   853  C  CB  . SER   A 1 117 ? -29.107 -11.913 30.833 1.00 54.41  ? 413 SER   A CB  1 
ATOM   854  O  OG  . SER   A 1 117 ? -27.768 -12.370 30.848 1.00 54.54  ? 413 SER   A OG  1 
ATOM   855  N  N   . ARG   A 1 118 ? -27.462 -9.112  29.777 1.00 45.89  ? 414 ARG   A N   1 
ATOM   856  C  CA  . ARG   A 1 118 ? -26.756 -7.884  30.104 1.00 47.67  ? 414 ARG   A CA  1 
ATOM   857  C  C   . ARG   A 1 118 ? -27.291 -6.645  29.392 1.00 50.28  ? 414 ARG   A C   1 
ATOM   858  O  O   . ARG   A 1 118 ? -26.755 -5.560  29.617 1.00 47.81  ? 414 ARG   A O   1 
ATOM   859  C  CB  . ARG   A 1 118 ? -25.266 -8.040  29.815 1.00 54.53  ? 414 ARG   A CB  1 
ATOM   860  C  CG  . ARG   A 1 118 ? -24.615 -9.095  30.719 1.00 51.55  ? 414 ARG   A CG  1 
ATOM   861  C  CD  . ARG   A 1 118 ? -23.098 -9.184  30.570 1.00 52.07  ? 414 ARG   A CD  1 
ATOM   862  N  NE  . ARG   A 1 118 ? -22.530 -9.934  31.690 1.00 58.56  ? 414 ARG   A NE  1 
ATOM   863  C  CZ  . ARG   A 1 118 ? -21.266 -10.336 31.777 1.00 64.09  ? 414 ARG   A CZ  1 
ATOM   864  N  NH1 . ARG   A 1 118 ? -20.411 -10.085 30.803 1.00 68.60  ? 414 ARG   A NH1 1 
ATOM   865  N  NH2 . ARG   A 1 118 ? -20.865 -11.012 32.840 1.00 63.08  ? 414 ARG   A NH2 1 
ATOM   866  N  N   . CYS   A 1 119 ? -28.334 -6.745  28.563 1.00 47.43  ? 415 CYS   A N   1 
ATOM   867  C  CA  . CYS   A 1 119 ? -28.787 -5.596  27.789 1.00 50.23  ? 415 CYS   A CA  1 
ATOM   868  C  C   . CYS   A 1 119 ? -30.006 -4.952  28.433 1.00 52.67  ? 415 CYS   A C   1 
ATOM   869  O  O   . CYS   A 1 119 ? -31.061 -5.588  28.539 1.00 58.43  ? 415 CYS   A O   1 
ATOM   870  C  CB  . CYS   A 1 119 ? -29.109 -6.000  26.344 1.00 44.22  ? 415 CYS   A CB  1 
ATOM   871  S  SG  . CYS   A 1 119 ? -29.865 -4.685  25.322 1.00 50.51  ? 415 CYS   A SG  1 
ATOM   872  N  N   . VAL   A 1 120 ? -29.883 -3.661  28.783 1.00 56.65  ? 416 VAL   A N   1 
ATOM   873  C  CA  . VAL   A 1 120 ? -31.003 -2.899  29.347 1.00 53.02  ? 416 VAL   A CA  1 
ATOM   874  C  C   . VAL   A 1 120 ? -31.964 -2.393  28.277 1.00 58.33  ? 416 VAL   A C   1 
ATOM   875  O  O   . VAL   A 1 120 ? -33.046 -1.891  28.603 1.00 54.35  ? 416 VAL   A O   1 
ATOM   876  C  CB  . VAL   A 1 120 ? -30.488 -1.726  30.219 1.00 51.58  ? 416 VAL   A CB  1 
ATOM   877  C  CG1 . VAL   A 1 120 ? -30.088 -0.489  29.359 1.00 45.09  ? 416 VAL   A CG1 1 
ATOM   878  C  CG2 . VAL   A 1 120 ? -31.531 -1.324  31.302 1.00 53.22  ? 416 VAL   A CG2 1 
ATOM   879  N  N   . GLY   A 1 121 ? -31.642 -2.545  27.004 1.00 60.10  ? 417 GLY   A N   1 
ATOM   880  C  CA  . GLY   A 1 121 ? -32.489 -1.951  25.980 1.00 47.63  ? 417 GLY   A CA  1 
ATOM   881  C  C   . GLY   A 1 121 ? -33.438 -2.909  25.296 1.00 58.62  ? 417 GLY   A C   1 
ATOM   882  O  O   . GLY   A 1 121 ? -33.909 -2.617  24.188 1.00 62.90  ? 417 GLY   A O   1 
ATOM   883  N  N   . ARG   A 1 122 ? -33.741 -4.050  25.914 1.00 51.50  ? 418 ARG   A N   1 
ATOM   884  C  CA  . ARG   A 1 122 ? -34.370 -5.132  25.159 1.00 57.59  ? 418 ARG   A CA  1 
ATOM   885  C  C   . ARG   A 1 122 ? -35.857 -4.929  24.929 1.00 58.94  ? 418 ARG   A C   1 
ATOM   886  O  O   . ARG   A 1 122 ? -36.475 -5.744  24.230 1.00 57.86  ? 418 ARG   A O   1 
ATOM   887  C  CB  . ARG   A 1 122 ? -34.149 -6.467  25.852 1.00 54.56  ? 418 ARG   A CB  1 
ATOM   888  C  CG  . ARG   A 1 122 ? -32.744 -6.978  25.720 1.00 51.49  ? 418 ARG   A CG  1 
ATOM   889  C  CD  . ARG   A 1 122 ? -32.615 -8.282  26.437 1.00 53.04  ? 418 ARG   A CD  1 
ATOM   890  N  NE  . ARG   A 1 122 ? -32.419 -8.070  27.869 1.00 57.22  ? 418 ARG   A NE  1 
ATOM   891  C  CZ  . ARG   A 1 122 ? -32.569 -9.014  28.785 1.00 56.78  ? 418 ARG   A CZ  1 
ATOM   892  N  NH1 . ARG   A 1 122 ? -32.935 -10.240 28.427 1.00 50.29  ? 418 ARG   A NH1 1 
ATOM   893  N  NH2 . ARG   A 1 122 ? -32.348 -8.732  30.067 1.00 62.62  ? 418 ARG   A NH2 1 
ATOM   894  N  N   . ILE   A 1 123 ? -36.464 -3.877  25.488 1.00 57.76  ? 419 ILE   A N   1 
ATOM   895  C  CA  . ILE   A 1 123 ? -37.867 -3.638  25.187 1.00 60.72  ? 419 ILE   A CA  1 
ATOM   896  C  C   . ILE   A 1 123 ? -38.068 -3.470  23.669 1.00 65.37  ? 419 ILE   A C   1 
ATOM   897  O  O   . ILE   A 1 123 ? -39.192 -3.596  23.164 1.00 61.06  ? 419 ILE   A O   1 
ATOM   898  C  CB  . ILE   A 1 123 ? -38.389 -2.417  25.971 1.00 67.89  ? 419 ILE   A CB  1 
ATOM   899  C  CG1 . ILE   A 1 123 ? -39.917 -2.465  26.069 1.00 80.24  ? 419 ILE   A CG1 1 
ATOM   900  C  CG2 . ILE   A 1 123 ? -37.893 -1.113  25.340 1.00 65.70  ? 419 ILE   A CG2 1 
ATOM   901  C  CD1 . ILE   A 1 123 ? -40.538 -1.154  26.491 1.00 86.60  ? 419 ILE   A CD1 1 
ATOM   902  N  N   . GLN   A 1 124 ? -36.988 -3.223  22.931 1.00 68.80  ? 420 GLN   A N   1 
ATOM   903  C  CA  . GLN   A 1 124 ? -37.018 -2.979  21.495 1.00 71.91  ? 420 GLN   A CA  1 
ATOM   904  C  C   . GLN   A 1 124 ? -36.731 -4.230  20.661 1.00 66.40  ? 420 GLN   A C   1 
ATOM   905  O  O   . GLN   A 1 124 ? -36.661 -4.140  19.427 1.00 60.99  ? 420 GLN   A O   1 
ATOM   906  C  CB  . GLN   A 1 124 ? -36.009 -1.874  21.155 1.00 82.65  ? 420 GLN   A CB  1 
ATOM   907  C  CG  . GLN   A 1 124 ? -36.517 -0.453  21.385 1.00 95.46  ? 420 GLN   A CG  1 
ATOM   908  C  CD  . GLN   A 1 124 ? -37.287 0.096   20.179 1.00 102.86 ? 420 GLN   A CD  1 
ATOM   909  O  OE1 . GLN   A 1 124 ? -37.843 -0.660  19.385 1.00 107.93 ? 420 GLN   A OE1 1 
ATOM   910  N  NE2 . GLN   A 1 124 ? -37.317 1.413   20.045 1.00 109.46 ? 420 GLN   A NE2 1 
ATOM   911  N  N   . TRP   A 1 125 ? -36.604 -5.397  21.298 1.00 62.12  ? 421 TRP   A N   1 
ATOM   912  C  CA  . TRP   A 1 125 ? -35.953 -6.539  20.658 1.00 55.01  ? 421 TRP   A CA  1 
ATOM   913  C  C   . TRP   A 1 125 ? -36.677 -6.992  19.398 1.00 61.42  ? 421 TRP   A C   1 
ATOM   914  O  O   . TRP   A 1 125 ? -36.035 -7.503  18.476 1.00 63.30  ? 421 TRP   A O   1 
ATOM   915  C  CB  . TRP   A 1 125 ? -35.842 -7.702  21.644 1.00 52.49  ? 421 TRP   A CB  1 
ATOM   916  C  CG  . TRP   A 1 125 ? -37.153 -8.329  21.914 1.00 59.22  ? 421 TRP   A CG  1 
ATOM   917  C  CD1 . TRP   A 1 125 ? -38.021 -8.019  22.919 1.00 67.80  ? 421 TRP   A CD1 1 
ATOM   918  C  CD2 . TRP   A 1 125 ? -37.775 -9.367  21.152 1.00 66.56  ? 421 TRP   A CD2 1 
ATOM   919  N  NE1 . TRP   A 1 125 ? -39.145 -8.801  22.829 1.00 67.02  ? 421 TRP   A NE1 1 
ATOM   920  C  CE2 . TRP   A 1 125 ? -39.018 -9.639  21.754 1.00 70.64  ? 421 TRP   A CE2 1 
ATOM   921  C  CE3 . TRP   A 1 125 ? -37.404 -10.086 20.017 1.00 58.94  ? 421 TRP   A CE3 1 
ATOM   922  C  CZ2 . TRP   A 1 125 ? -39.887 -10.605 21.261 1.00 72.44  ? 421 TRP   A CZ2 1 
ATOM   923  C  CZ3 . TRP   A 1 125 ? -38.259 -11.054 19.543 1.00 57.80  ? 421 TRP   A CZ3 1 
ATOM   924  C  CH2 . TRP   A 1 125 ? -39.489 -11.295 20.148 1.00 61.87  ? 421 TRP   A CH2 1 
ATOM   925  N  N   . SER   A 1 126 ? -38.000 -6.821  19.331 1.00 62.91  ? 422 SER   A N   1 
ATOM   926  C  CA  . SER   A 1 126 ? -38.735 -7.245  18.140 1.00 74.91  ? 422 SER   A CA  1 
ATOM   927  C  C   . SER   A 1 126 ? -38.632 -6.245  16.985 1.00 76.46  ? 422 SER   A C   1 
ATOM   928  O  O   . SER   A 1 126 ? -38.956 -6.594  15.841 1.00 79.53  ? 422 SER   A O   1 
ATOM   929  C  CB  . SER   A 1 126 ? -40.206 -7.502  18.505 1.00 76.64  ? 422 SER   A CB  1 
ATOM   930  O  OG  . SER   A 1 126 ? -40.899 -6.306  18.811 1.00 78.84  ? 422 SER   A OG  1 
ATOM   931  N  N   . LYS   A 1 127 ? -38.186 -5.016  17.252 1.00 72.63  ? 423 LYS   A N   1 
ATOM   932  C  CA  . LYS   A 1 127 ? -37.894 -4.033  16.208 1.00 72.73  ? 423 LYS   A CA  1 
ATOM   933  C  C   . LYS   A 1 127 ? -36.398 -4.097  15.918 1.00 75.98  ? 423 LYS   A C   1 
ATOM   934  O  O   . LYS   A 1 127 ? -35.583 -3.349  16.466 1.00 71.40  ? 423 LYS   A O   1 
ATOM   935  C  CB  . LYS   A 1 127 ? -38.321 -2.635  16.633 1.00 75.62  ? 423 LYS   A CB  1 
ATOM   936  C  CG  . LYS   A 1 127 ? -39.794 -2.328  16.465 1.00 87.18  ? 423 LYS   A CG  1 
ATOM   937  C  CD  . LYS   A 1 127 ? -39.970 -1.022  15.675 1.00 100.27 ? 423 LYS   A CD  1 
ATOM   938  C  CE  . LYS   A 1 127 ? -41.160 -1.079  14.731 1.00 106.14 ? 423 LYS   A CE  1 
ATOM   939  N  NZ  . LYS   A 1 127 ? -41.122 0.045   13.755 1.00 111.97 ? 423 LYS   A NZ  1 
ATOM   940  N  N   . LEU   A 1 128 ? -36.036 -5.033  15.052 1.00 74.34  ? 424 LEU   A N   1 
ATOM   941  C  CA  . LEU   A 1 128 ? -34.647 -5.231  14.683 1.00 66.89  ? 424 LEU   A CA  1 
ATOM   942  C  C   . LEU   A 1 128 ? -34.599 -5.490  13.184 1.00 66.14  ? 424 LEU   A C   1 
ATOM   943  O  O   . LEU   A 1 128 ? -35.410 -6.250  12.646 1.00 64.16  ? 424 LEU   A O   1 
ATOM   944  C  CB  . LEU   A 1 128 ? -34.005 -6.382  15.482 1.00 59.77  ? 424 LEU   A CB  1 
ATOM   945  C  CG  . LEU   A 1 128 ? -32.556 -6.729  15.096 1.00 54.30  ? 424 LEU   A CG  1 
ATOM   946  C  CD1 . LEU   A 1 128 ? -31.589 -5.589  15.451 1.00 54.81  ? 424 LEU   A CD1 1 
ATOM   947  C  CD2 . LEU   A 1 128 ? -32.101 -8.034  15.741 1.00 51.91  ? 424 LEU   A CD2 1 
ATOM   948  N  N   . GLN   A 1 129 ? -33.683 -4.804  12.514 1.00 63.60  ? 425 GLN   A N   1 
ATOM   949  C  CA  . GLN   A 1 129 ? -33.515 -4.896  11.069 1.00 72.00  ? 425 GLN   A CA  1 
ATOM   950  C  C   . GLN   A 1 129 ? -32.334 -5.813  10.795 1.00 70.56  ? 425 GLN   A C   1 
ATOM   951  O  O   . GLN   A 1 129 ? -31.222 -5.568  11.275 1.00 66.36  ? 425 GLN   A O   1 
ATOM   952  C  CB  . GLN   A 1 129 ? -33.293 -3.511  10.469 1.00 75.51  ? 425 GLN   A CB  1 
ATOM   953  C  CG  . GLN   A 1 129 ? -32.979 -3.515  8.995  1.00 77.14  ? 425 GLN   A CG  1 
ATOM   954  C  CD  . GLN   A 1 129 ? -34.101 -4.097  8.162  1.00 81.33  ? 425 GLN   A CD  1 
ATOM   955  O  OE1 . GLN   A 1 129 ? -35.275 -4.046  8.548  1.00 83.62  ? 425 GLN   A OE1 1 
ATOM   956  N  NE2 . GLN   A 1 129 ? -33.746 -4.661  7.015  1.00 84.02  ? 425 GLN   A NE2 1 
ATOM   957  N  N   . VAL   A 1 130 ? -32.581 -6.888  10.065 1.00 62.13  ? 426 VAL   A N   1 
ATOM   958  C  CA  . VAL   A 1 130 ? -31.597 -7.941  9.881  1.00 58.86  ? 426 VAL   A CA  1 
ATOM   959  C  C   . VAL   A 1 130 ? -31.091 -7.848  8.452  1.00 58.71  ? 426 VAL   A C   1 
ATOM   960  O  O   . VAL   A 1 130 ? -31.889 -7.788  7.513  1.00 56.96  ? 426 VAL   A O   1 
ATOM   961  C  CB  . VAL   A 1 130 ? -32.199 -9.321  10.192 1.00 56.50  ? 426 VAL   A CB  1 
ATOM   962  C  CG1 . VAL   A 1 130 ? -31.168 -10.445 9.994  1.00 61.10  ? 426 VAL   A CG1 1 
ATOM   963  C  CG2 . VAL   A 1 130 ? -32.794 -9.329  11.618 1.00 51.24  ? 426 VAL   A CG2 1 
ATOM   964  N  N   . PHE   A 1 131 ? -29.776 -7.783  8.291  1.00 58.24  ? 427 PHE   A N   1 
ATOM   965  C  CA  . PHE   A 1 131 ? -29.152 -7.651  6.976  1.00 55.99  ? 427 PHE   A CA  1 
ATOM   966  C  C   . PHE   A 1 131 ? -28.388 -8.938  6.711  1.00 56.85  ? 427 PHE   A C   1 
ATOM   967  O  O   . PHE   A 1 131 ? -27.419 -9.248  7.413  1.00 53.56  ? 427 PHE   A O   1 
ATOM   968  C  CB  . PHE   A 1 131 ? -28.225 -6.434  6.920  1.00 50.45  ? 427 PHE   A CB  1 
ATOM   969  C  CG  . PHE   A 1 131 ? -28.951 -5.102  6.847  1.00 52.39  ? 427 PHE   A CG  1 
ATOM   970  C  CD1 . PHE   A 1 131 ? -29.763 -4.776  5.777  1.00 58.80  ? 427 PHE   A CD1 1 
ATOM   971  C  CD2 . PHE   A 1 131 ? -28.795 -4.171  7.845  1.00 61.45  ? 427 PHE   A CD2 1 
ATOM   972  C  CE1 . PHE   A 1 131 ? -30.413 -3.534  5.716  1.00 55.00  ? 427 PHE   A CE1 1 
ATOM   973  C  CE2 . PHE   A 1 131 ? -29.441 -2.961  7.804  1.00 62.58  ? 427 PHE   A CE2 1 
ATOM   974  C  CZ  . PHE   A 1 131 ? -30.248 -2.632  6.748  1.00 58.11  ? 427 PHE   A CZ  1 
ATOM   975  N  N   . ASP   A 1 132 ? -28.849 -9.705  5.726  1.00 56.58  ? 428 ASP   A N   1 
ATOM   976  C  CA  . ASP   A 1 132 ? -28.313 -11.029 5.444  1.00 54.33  ? 428 ASP   A CA  1 
ATOM   977  C  C   . ASP   A 1 132 ? -27.121 -10.832 4.522  1.00 57.09  ? 428 ASP   A C   1 
ATOM   978  O  O   . ASP   A 1 132 ? -27.286 -10.600 3.324  1.00 62.07  ? 428 ASP   A O   1 
ATOM   979  C  CB  . ASP   A 1 132 ? -29.398 -11.907 4.825  1.00 57.71  ? 428 ASP   A CB  1 
ATOM   980  C  CG  . ASP   A 1 132 ? -28.906 -13.300 4.475  1.00 67.15  ? 428 ASP   A CG  1 
ATOM   981  O  OD1 . ASP   A 1 132 ? -29.732 -14.129 4.026  1.00 69.67  ? 428 ASP   A OD1 1 
ATOM   982  O  OD2 . ASP   A 1 132 ? -27.708 -13.578 4.669  1.00 69.25  ? 428 ASP   A OD2 1 
ATOM   983  N  N   . ALA   A 1 133 ? -25.914 -10.887 5.080  1.00 53.62  ? 429 ALA   A N   1 
ATOM   984  C  CA  . ALA   A 1 133 ? -24.689 -10.814 4.290  1.00 53.48  ? 429 ALA   A CA  1 
ATOM   985  C  C   . ALA   A 1 133 ? -24.034 -12.180 4.137  1.00 54.03  ? 429 ALA   A C   1 
ATOM   986  O  O   . ALA   A 1 133 ? -22.809 -12.279 3.992  1.00 56.64  ? 429 ALA   A O   1 
ATOM   987  C  CB  . ALA   A 1 133 ? -23.702 -9.826  4.914  1.00 54.35  ? 429 ALA   A CB  1 
ATOM   988  N  N   . ARG   A 1 134 ? -24.822 -13.246 4.192  1.00 55.27  ? 430 ARG   A N   1 
ATOM   989  C  CA  . ARG   A 1 134 ? -24.251 -14.573 4.016  1.00 59.20  ? 430 ARG   A CA  1 
ATOM   990  C  C   . ARG   A 1 134 ? -23.789 -14.859 2.585  1.00 60.25  ? 430 ARG   A C   1 
ATOM   991  O  O   . ARG   A 1 134 ? -23.150 -15.894 2.380  1.00 62.92  ? 430 ARG   A O   1 
ATOM   992  C  CB  . ARG   A 1 134 ? -25.261 -15.610 4.492  1.00 57.49  ? 430 ARG   A CB  1 
ATOM   993  C  CG  . ARG   A 1 134 ? -25.430 -15.588 6.028  1.00 61.32  ? 430 ARG   A CG  1 
ATOM   994  C  CD  . ARG   A 1 134 ? -26.521 -16.556 6.485  1.00 61.69  ? 430 ARG   A CD  1 
ATOM   995  N  NE  . ARG   A 1 134 ? -27.803 -16.253 5.851  1.00 64.08  ? 430 ARG   A NE  1 
ATOM   996  C  CZ  . ARG   A 1 134 ? -28.834 -17.091 5.772  1.00 65.67  ? 430 ARG   A CZ  1 
ATOM   997  N  NH1 . ARG   A 1 134 ? -28.743 -18.309 6.290  1.00 70.80  ? 430 ARG   A NH1 1 
ATOM   998  N  NH2 . ARG   A 1 134 ? -29.952 -16.709 5.166  1.00 65.38  ? 430 ARG   A NH2 1 
ATOM   999  N  N   . ASP   A 1 135 ? -24.063 -13.985 1.602  1.00 58.73  ? 431 ASP   A N   1 
ATOM   1000 C  CA  . ASP   A 1 135 ? -23.484 -14.135 0.262  1.00 65.98  ? 431 ASP   A CA  1 
ATOM   1001 C  C   . ASP   A 1 135 ? -22.140 -13.427 0.115  1.00 66.91  ? 431 ASP   A C   1 
ATOM   1002 O  O   . ASP   A 1 135 ? -21.569 -13.424 -0.980 1.00 70.37  ? 431 ASP   A O   1 
ATOM   1003 C  CB  . ASP   A 1 135 ? -24.461 -13.621 -0.834 1.00 70.55  ? 431 ASP   A CB  1 
ATOM   1004 C  CG  . ASP   A 1 135 ? -24.772 -12.110 -0.715 1.00 77.51  ? 431 ASP   A CG  1 
ATOM   1005 O  OD1 . ASP   A 1 135 ? -25.520 -11.570 -1.561 1.00 73.05  ? 431 ASP   A OD1 1 
ATOM   1006 O  OD2 . ASP   A 1 135 ? -24.288 -11.452 0.230  1.00 73.80  ? 431 ASP   A OD2 1 
ATOM   1007 N  N   . CYS   A 1 136 ? -21.638 -12.806 1.180  1.00 65.28  ? 432 CYS   A N   1 
ATOM   1008 C  CA  . CYS   A 1 136 ? -20.365 -12.097 1.132  1.00 66.10  ? 432 CYS   A CA  1 
ATOM   1009 C  C   . CYS   A 1 136 ? -19.193 -13.071 1.005  1.00 72.14  ? 432 CYS   A C   1 
ATOM   1010 O  O   . CYS   A 1 136 ? -19.186 -14.151 1.611  1.00 81.00  ? 432 CYS   A O   1 
ATOM   1011 C  CB  . CYS   A 1 136 ? -20.209 -11.250 2.405  1.00 57.53  ? 432 CYS   A CB  1 
ATOM   1012 S  SG  . CYS   A 1 136 ? -18.963 -9.950  2.296  1.00 65.81  ? 432 CYS   A SG  1 
ATOM   1013 N  N   . THR   A 1 137 ? -18.176 -12.668 0.233  1.00 62.72  ? 433 THR   A N   1 
ATOM   1014 C  CA  . THR   A 1 137 ? -16.996 -13.498 -0.005 1.00 55.35  ? 433 THR   A CA  1 
ATOM   1015 C  C   . THR   A 1 137 ? -15.654 -12.784 0.214  1.00 61.00  ? 433 THR   A C   1 
ATOM   1016 O  O   . THR   A 1 137 ? -14.626 -13.466 0.304  1.00 71.87  ? 433 THR   A O   1 
ATOM   1017 C  CB  . THR   A 1 137 ? -17.012 -14.074 -1.438 1.00 66.84  ? 433 THR   A CB  1 
ATOM   1018 O  OG1 . THR   A 1 137 ? -17.018 -13.000 -2.379 1.00 69.15  ? 433 THR   A OG1 1 
ATOM   1019 C  CG2 . THR   A 1 137 ? -18.245 -14.963 -1.678 1.00 63.20  ? 433 THR   A CG2 1 
ATOM   1020 N  N   . THR   A 1 138 ? -15.619 -11.454 0.312  1.00 68.39  ? 434 THR   A N   1 
ATOM   1021 C  CA  . THR   A 1 138 ? -14.368 -10.697 0.358  1.00 69.40  ? 434 THR   A CA  1 
ATOM   1022 C  C   . THR   A 1 138 ? -14.457 -9.603  1.413  1.00 66.85  ? 434 THR   A C   1 
ATOM   1023 O  O   . THR   A 1 138 ? -15.546 -9.180  1.804  1.00 68.14  ? 434 THR   A O   1 
ATOM   1024 C  CB  . THR   A 1 138 ? -14.027 -10.027 -0.995 1.00 74.26  ? 434 THR   A CB  1 
ATOM   1025 O  OG1 . THR   A 1 138 ? -15.187 -9.353  -1.492 1.00 79.93  ? 434 THR   A OG1 1 
ATOM   1026 C  CG2 . THR   A 1 138 ? -13.522 -11.039 -2.025 1.00 76.01  ? 434 THR   A CG2 1 
ATOM   1027 N  N   . ALA   A 1 139 ? -13.281 -9.126  1.841  1.00 73.88  ? 435 ALA   A N   1 
ATOM   1028 C  CA  . ALA   A 1 139 ? -13.215 -8.016  2.791  1.00 65.93  ? 435 ALA   A CA  1 
ATOM   1029 C  C   . ALA   A 1 139 ? -13.858 -6.753  2.229  1.00 73.53  ? 435 ALA   A C   1 
ATOM   1030 O  O   . ALA   A 1 139 ? -14.485 -5.985  2.971  1.00 74.78  ? 435 ALA   A O   1 
ATOM   1031 C  CB  . ALA   A 1 139 ? -11.760 -7.738  3.163  1.00 72.83  ? 435 ALA   A CB  1 
ATOM   1032 N  N   . HIS   A 1 140 ? -13.694 -6.512  0.921  1.00 70.63  ? 436 HIS   A N   1 
ATOM   1033 C  CA  . HIS   A 1 140 ? -14.370 -5.392  0.268  1.00 75.25  ? 436 HIS   A CA  1 
ATOM   1034 C  C   . HIS   A 1 140 ? -15.880 -5.537  0.361  1.00 70.63  ? 436 HIS   A C   1 
ATOM   1035 O  O   . HIS   A 1 140 ? -16.594 -4.564  0.618  1.00 71.03  ? 436 HIS   A O   1 
ATOM   1036 C  CB  . HIS   A 1 140 ? -13.957 -5.293  -1.204 1.00 76.33  ? 436 HIS   A CB  1 
ATOM   1037 C  CG  . HIS   A 1 140 ? -12.668 -4.568  -1.434 1.00 80.58  ? 436 HIS   A CG  1 
ATOM   1038 N  ND1 . HIS   A 1 140 ? -11.449 -5.088  -1.060 1.00 85.11  ? 436 HIS   A ND1 1 
ATOM   1039 C  CD2 . HIS   A 1 140 ? -12.406 -3.369  -2.013 1.00 81.75  ? 436 HIS   A CD2 1 
ATOM   1040 C  CE1 . HIS   A 1 140 ? -10.489 -4.248  -1.410 1.00 89.03  ? 436 HIS   A CE1 1 
ATOM   1041 N  NE2 . HIS   A 1 140 ? -11.044 -3.191  -1.978 1.00 83.40  ? 436 HIS   A NE2 1 
ATOM   1042 N  N   . GLY   A 1 141 ? -16.391 -6.738  0.098  1.00 74.59  ? 437 GLY   A N   1 
ATOM   1043 C  CA  . GLY   A 1 141 ? -17.817 -6.967  0.257  1.00 73.26  ? 437 GLY   A CA  1 
ATOM   1044 C  C   . GLY   A 1 141 ? -18.288 -6.690  1.670  1.00 69.02  ? 437 GLY   A C   1 
ATOM   1045 O  O   . GLY   A 1 141 ? -19.356 -6.107  1.873  1.00 63.78  ? 437 GLY   A O   1 
ATOM   1046 N  N   . MET   A 1 142 ? -17.491 -7.106  2.668  1.00 70.50  ? 438 MET   A N   1 
ATOM   1047 C  CA  . MET   A 1 142 ? -17.781 -6.782  4.063  1.00 65.81  ? 438 MET   A CA  1 
ATOM   1048 C  C   . MET   A 1 142 ? -17.824 -5.273  4.279  1.00 65.42  ? 438 MET   A C   1 
ATOM   1049 O  O   . MET   A 1 142 ? -18.757 -4.749  4.895  1.00 71.38  ? 438 MET   A O   1 
ATOM   1050 C  CB  . MET   A 1 142 ? -16.735 -7.414  4.994  1.00 64.66  ? 438 MET   A CB  1 
ATOM   1051 C  CG  . MET   A 1 142 ? -16.677 -8.941  5.026  1.00 60.11  ? 438 MET   A CG  1 
ATOM   1052 S  SD  . MET   A 1 142 ? -15.373 -9.530  6.147  1.00 60.71  ? 438 MET   A SD  1 
ATOM   1053 C  CE  . MET   A 1 142 ? -16.054 -9.008  7.716  1.00 62.43  ? 438 MET   A CE  1 
ATOM   1054 N  N   . PHE   A 1 143 ? -16.818 -4.555  3.776  1.00 66.10  ? 439 PHE   A N   1 
ATOM   1055 C  CA  . PHE   A 1 143 ? -16.833 -3.099  3.887  1.00 65.66  ? 439 PHE   A CA  1 
ATOM   1056 C  C   . PHE   A 1 143 ? -18.128 -2.512  3.337  1.00 70.36  ? 439 PHE   A C   1 
ATOM   1057 O  O   . PHE   A 1 143 ? -18.779 -1.692  3.988  1.00 64.17  ? 439 PHE   A O   1 
ATOM   1058 C  CB  . PHE   A 1 143 ? -15.630 -2.515  3.159  1.00 65.00  ? 439 PHE   A CB  1 
ATOM   1059 C  CG  . PHE   A 1 143 ? -15.607 -1.013  3.151  1.00 73.92  ? 439 PHE   A CG  1 
ATOM   1060 C  CD1 . PHE   A 1 143 ? -15.716 -0.308  1.970  1.00 75.45  ? 439 PHE   A CD1 1 
ATOM   1061 C  CD2 . PHE   A 1 143 ? -15.498 -0.307  4.343  1.00 70.25  ? 439 PHE   A CD2 1 
ATOM   1062 C  CE1 . PHE   A 1 143 ? -15.700 1.075   1.971  1.00 77.39  ? 439 PHE   A CE1 1 
ATOM   1063 C  CE2 . PHE   A 1 143 ? -15.478 1.068   4.345  1.00 73.75  ? 439 PHE   A CE2 1 
ATOM   1064 C  CZ  . PHE   A 1 143 ? -15.585 1.764   3.154  1.00 75.85  ? 439 PHE   A CZ  1 
ATOM   1065 N  N   . ASN   A 1 144 ? -18.530 -2.939  2.142  1.00 66.73  ? 440 ASN   A N   1 
ATOM   1066 C  CA  . ASN   A 1 144 ? -19.767 -2.437  1.560  1.00 59.78  ? 440 ASN   A CA  1 
ATOM   1067 C  C   . ASN   A 1 144 ? -20.975 -2.757  2.437  1.00 55.55  ? 440 ASN   A C   1 
ATOM   1068 O  O   . ASN   A 1 144 ? -21.811 -1.889  2.701  1.00 70.71  ? 440 ASN   A O   1 
ATOM   1069 C  CB  . ASN   A 1 144 ? -19.963 -3.030  0.175  1.00 67.40  ? 440 ASN   A CB  1 
ATOM   1070 C  CG  . ASN   A 1 144 ? -20.994 -2.284  -0.621 1.00 65.36  ? 440 ASN   A CG  1 
ATOM   1071 O  OD1 . ASN   A 1 144 ? -20.808 -1.106  -0.927 1.00 75.66  ? 440 ASN   A OD1 1 
ATOM   1072 N  ND2 . ASN   A 1 144 ? -22.079 -2.965  -0.981 1.00 62.04  ? 440 ASN   A ND2 1 
ATOM   1073 N  N   . TYR   A 1 145 ? -21.103 -4.009  2.872  1.00 56.69  ? 441 TYR   A N   1 
ATOM   1074 C  CA  . TYR   A 1 145 ? -22.205 -4.354  3.773  1.00 61.32  ? 441 TYR   A CA  1 
ATOM   1075 C  C   . TYR   A 1 145 ? -22.175 -3.522  5.047  1.00 63.92  ? 441 TYR   A C   1 
ATOM   1076 O  O   . TYR   A 1 145 ? -23.220 -3.041  5.515  1.00 62.40  ? 441 TYR   A O   1 
ATOM   1077 C  CB  . TYR   A 1 145 ? -22.166 -5.836  4.117  1.00 51.72  ? 441 TYR   A CB  1 
ATOM   1078 C  CG  . TYR   A 1 145 ? -22.979 -6.712  3.188  1.00 53.28  ? 441 TYR   A CG  1 
ATOM   1079 C  CD1 . TYR   A 1 145 ? -22.358 -7.601  2.326  1.00 49.98  ? 441 TYR   A CD1 1 
ATOM   1080 C  CD2 . TYR   A 1 145 ? -24.368 -6.662  3.180  1.00 60.83  ? 441 TYR   A CD2 1 
ATOM   1081 C  CE1 . TYR   A 1 145 ? -23.082 -8.417  1.497  1.00 59.36  ? 441 TYR   A CE1 1 
ATOM   1082 C  CE2 . TYR   A 1 145 ? -25.111 -7.471  2.342  1.00 63.61  ? 441 TYR   A CE2 1 
ATOM   1083 C  CZ  . TYR   A 1 145 ? -24.456 -8.348  1.494  1.00 62.91  ? 441 TYR   A CZ  1 
ATOM   1084 O  OH  . TYR   A 1 145 ? -25.167 -9.162  0.638  1.00 69.17  ? 441 TYR   A OH  1 
ATOM   1085 N  N   . ILE   A 1 146 ? -20.992 -3.356  5.638  1.00 67.49  ? 442 ILE   A N   1 
ATOM   1086 C  CA  . ILE   A 1 146 ? -20.901 -2.612  6.890  1.00 65.34  ? 442 ILE   A CA  1 
ATOM   1087 C  C   . ILE   A 1 146 ? -21.273 -1.155  6.664  1.00 67.87  ? 442 ILE   A C   1 
ATOM   1088 O  O   . ILE   A 1 146 ? -21.966 -0.552  7.487  1.00 65.84  ? 442 ILE   A O   1 
ATOM   1089 C  CB  . ILE   A 1 146 ? -19.494 -2.763  7.492  1.00 59.35  ? 442 ILE   A CB  1 
ATOM   1090 C  CG1 . ILE   A 1 146 ? -19.340 -4.176  8.050  1.00 54.50  ? 442 ILE   A CG1 1 
ATOM   1091 C  CG2 . ILE   A 1 146 ? -19.222 -1.705  8.559  1.00 59.26  ? 442 ILE   A CG2 1 
ATOM   1092 C  CD1 . ILE   A 1 146 ? -17.950 -4.519  8.536  1.00 59.94  ? 442 ILE   A CD1 1 
ATOM   1093 N  N   . CYS   A 1 147 ? -20.880 -0.587  5.510  1.00 64.82  ? 443 CYS   A N   1 
ATOM   1094 C  CA  . CYS   A 1 147 ? -21.211 0.808   5.206  1.00 58.02  ? 443 CYS   A CA  1 
ATOM   1095 C  C   . CYS   A 1 147 ? -22.711 1.014   5.117  1.00 61.09  ? 443 CYS   A C   1 
ATOM   1096 O  O   . CYS   A 1 147 ? -23.246 1.983   5.666  1.00 70.98  ? 443 CYS   A O   1 
ATOM   1097 C  CB  . CYS   A 1 147 ? -20.568 1.267   3.910  1.00 63.31  ? 443 CYS   A CB  1 
ATOM   1098 S  SG  . CYS   A 1 147 ? -18.915 1.890   4.032  1.00 76.63  ? 443 CYS   A SG  1 
ATOM   1099 N  N   . ASN   A 1 148 ? -23.409 0.118   4.423  1.00 52.29  ? 444 ASN   A N   1 
ATOM   1100 C  CA  . ASN   A 1 148 ? -24.853 0.256   4.325  1.00 63.46  ? 444 ASN   A CA  1 
ATOM   1101 C  C   . ASN   A 1 148 ? -25.537 0.052   5.667  1.00 58.37  ? 444 ASN   A C   1 
ATOM   1102 O  O   . ASN   A 1 148 ? -26.594 0.644   5.913  1.00 62.27  ? 444 ASN   A O   1 
ATOM   1103 C  CB  . ASN   A 1 148 ? -25.388 -0.720  3.290  1.00 70.45  ? 444 ASN   A CB  1 
ATOM   1104 C  CG  . ASN   A 1 148 ? -24.949 -0.363  1.891  1.00 71.60  ? 444 ASN   A CG  1 
ATOM   1105 O  OD1 . ASN   A 1 148 ? -24.514 0.767   1.635  1.00 69.28  ? 444 ASN   A OD1 1 
ATOM   1106 N  ND2 . ASN   A 1 148 ? -25.067 -1.319  0.971  1.00 68.38  ? 444 ASN   A ND2 1 
ATOM   1107 N  N   . HIS   A 1 149 ? -24.961 -0.781  6.544  1.00 55.74  ? 445 HIS   A N   1 
ATOM   1108 C  CA  . HIS   A 1 149 ? -25.485 -0.904  7.907  1.00 60.37  ? 445 HIS   A CA  1 
ATOM   1109 C  C   . HIS   A 1 149 ? -25.356 0.420   8.658  1.00 60.89  ? 445 HIS   A C   1 
ATOM   1110 O  O   . HIS   A 1 149 ? -26.324 0.893   9.263  1.00 59.82  ? 445 HIS   A O   1 
ATOM   1111 C  CB  . HIS   A 1 149 ? -24.767 -2.057  8.629  1.00 56.34  ? 445 HIS   A CB  1 
ATOM   1112 C  CG  . HIS   A 1 149 ? -25.083 -2.197  10.102 1.00 59.56  ? 445 HIS   A CG  1 
ATOM   1113 N  ND1 . HIS   A 1 149 ? -25.340 -3.421  10.683 1.00 55.11  ? 445 HIS   A ND1 1 
ATOM   1114 C  CD2 . HIS   A 1 149 ? -25.127 -1.290  11.112 1.00 60.80  ? 445 HIS   A CD2 1 
ATOM   1115 C  CE1 . HIS   A 1 149 ? -25.548 -3.260  11.984 1.00 56.48  ? 445 HIS   A CE1 1 
ATOM   1116 N  NE2 . HIS   A 1 149 ? -25.427 -1.976  12.265 1.00 58.95  ? 445 HIS   A NE2 1 
ATOM   1117 N  N   . VAL   A 1 150 ? -24.161 1.029   8.637  1.00 62.02  ? 446 VAL   A N   1 
ATOM   1118 C  CA  . VAL   A 1 150 ? -23.949 2.302   9.330  1.00 61.72  ? 446 VAL   A CA  1 
ATOM   1119 C  C   . VAL   A 1 150 ? -24.936 3.345   8.829  1.00 68.02  ? 446 VAL   A C   1 
ATOM   1120 O  O   . VAL   A 1 150 ? -25.570 4.054   9.616  1.00 75.43  ? 446 VAL   A O   1 
ATOM   1121 C  CB  . VAL   A 1 150 ? -22.496 2.779   9.146  1.00 61.00  ? 446 VAL   A CB  1 
ATOM   1122 C  CG1 . VAL   A 1 150 ? -22.255 4.192   9.742  1.00 58.30  ? 446 VAL   A CG1 1 
ATOM   1123 C  CG2 . VAL   A 1 150 ? -21.538 1.773   9.746  1.00 54.84  ? 446 VAL   A CG2 1 
ATOM   1124 N  N   . LYS   A 1 151 ? -25.083 3.458   7.503  1.00 64.03  ? 447 LYS   A N   1 
ATOM   1125 C  CA  . LYS   A 1 151 ? -25.964 4.486   6.958  1.00 68.01  ? 447 LYS   A CA  1 
ATOM   1126 C  C   . LYS   A 1 151 ? -27.412 4.231   7.361  1.00 73.09  ? 447 LYS   A C   1 
ATOM   1127 O  O   . LYS   A 1 151 ? -28.120 5.151   7.795  1.00 74.61  ? 447 LYS   A O   1 
ATOM   1128 C  CB  . LYS   A 1 151 ? -25.829 4.547   5.433  1.00 69.01  ? 447 LYS   A CB  1 
ATOM   1129 C  CG  . LYS   A 1 151 ? -26.513 5.770   4.842  1.00 77.11  ? 447 LYS   A CG  1 
ATOM   1130 C  CD  . LYS   A 1 151 ? -26.177 5.917   3.383  1.00 72.11  ? 447 LYS   A CD  1 
ATOM   1131 C  CE  . LYS   A 1 151 ? -26.292 7.345   2.874  1.00 80.08  ? 447 LYS   A CE  1 
ATOM   1132 N  NZ  . LYS   A 1 151 ? -26.053 7.353   1.395  1.00 75.93  ? 447 LYS   A NZ  1 
ATOM   1133 N  N   . TYR   A 1 152 ? -27.862 2.977   7.251  1.00 67.43  ? 448 TYR   A N   1 
ATOM   1134 C  CA  . TYR   A 1 152 ? -29.249 2.669   7.576  1.00 67.08  ? 448 TYR   A CA  1 
ATOM   1135 C  C   . TYR   A 1 152 ? -29.536 2.916   9.054  1.00 67.02  ? 448 TYR   A C   1 
ATOM   1136 O  O   . TYR   A 1 152 ? -30.534 3.558   9.399  1.00 74.96  ? 448 TYR   A O   1 
ATOM   1137 C  CB  . TYR   A 1 152 ? -29.593 1.224   7.201  1.00 66.20  ? 448 TYR   A CB  1 
ATOM   1138 C  CG  . TYR   A 1 152 ? -30.937 0.799   7.759  1.00 71.52  ? 448 TYR   A CG  1 
ATOM   1139 C  CD1 . TYR   A 1 152 ? -32.116 1.042   7.075  1.00 79.83  ? 448 TYR   A CD1 1 
ATOM   1140 C  CD2 . TYR   A 1 152 ? -31.025 0.147   8.976  1.00 70.71  ? 448 TYR   A CD2 1 
ATOM   1141 C  CE1 . TYR   A 1 152 ? -33.351 0.670   7.595  1.00 80.77  ? 448 TYR   A CE1 1 
ATOM   1142 C  CE2 . TYR   A 1 152 ? -32.251 -0.225  9.504  1.00 73.51  ? 448 TYR   A CE2 1 
ATOM   1143 C  CZ  . TYR   A 1 152 ? -33.402 0.031   8.810  1.00 79.36  ? 448 TYR   A CZ  1 
ATOM   1144 O  OH  . TYR   A 1 152 ? -34.607 -0.354  9.348  1.00 88.68  ? 448 TYR   A OH  1 
ATOM   1145 N  N   . ALA   A 1 153 ? -28.669 2.410   9.947  1.00 65.84  ? 449 ALA   A N   1 
ATOM   1146 C  CA  . ALA   A 1 153 ? -28.940 2.521   11.373 1.00 69.11  ? 449 ALA   A CA  1 
ATOM   1147 C  C   . ALA   A 1 153 ? -28.834 3.961   11.851 1.00 71.35  ? 449 ALA   A C   1 
ATOM   1148 O  O   . ALA   A 1 153 ? -29.460 4.328   12.856 1.00 73.73  ? 449 ALA   A O   1 
ATOM   1149 C  CB  . ALA   A 1 153 ? -27.982 1.634   12.185 1.00 66.98  ? 449 ALA   A CB  1 
ATOM   1150 N  N   . THR   A 1 154 ? -28.032 4.783   11.173 1.00 64.68  ? 450 THR   A N   1 
ATOM   1151 C  CA  . THR   A 1 154 ? -27.903 6.164   11.619 1.00 72.64  ? 450 THR   A CA  1 
ATOM   1152 C  C   . THR   A 1 154 ? -29.136 6.977   11.239 1.00 81.02  ? 450 THR   A C   1 
ATOM   1153 O  O   . THR   A 1 154 ? -29.681 7.702   12.074 1.00 82.38  ? 450 THR   A O   1 
ATOM   1154 C  CB  . THR   A 1 154 ? -26.624 6.781   11.065 1.00 73.33  ? 450 THR   A CB  1 
ATOM   1155 O  OG1 . THR   A 1 154 ? -25.498 6.111   11.643 1.00 72.94  ? 450 THR   A OG1 1 
ATOM   1156 C  CG2 . THR   A 1 154 ? -26.553 8.245   11.417 1.00 78.21  ? 450 THR   A CG2 1 
ATOM   1157 N  N   . ASN   A 1 155 ? -29.601 6.861   9.987  1.00 79.98  ? 451 ASN   A N   1 
ATOM   1158 C  CA  . ASN   A 1 155 ? -30.904 7.402   9.587  1.00 76.08  ? 451 ASN   A CA  1 
ATOM   1159 C  C   . ASN   A 1 155 ? -31.057 8.865   10.007 1.00 79.93  ? 451 ASN   A C   1 
ATOM   1160 O  O   . ASN   A 1 155 ? -32.082 9.275   10.554 1.00 94.32  ? 451 ASN   A O   1 
ATOM   1161 C  CB  . ASN   A 1 155 ? -32.039 6.544   10.158 1.00 84.75  ? 451 ASN   A CB  1 
ATOM   1162 C  CG  . ASN   A 1 155 ? -33.419 6.964   9.661  1.00 87.57  ? 451 ASN   A CG  1 
ATOM   1163 O  OD1 . ASN   A 1 155 ? -33.576 7.452   8.530  1.00 88.15  ? 451 ASN   A OD1 1 
ATOM   1164 N  ND2 . ASN   A 1 155 ? -34.429 6.781   10.510 1.00 85.89  ? 451 ASN   A ND2 1 
ATOM   1165 N  N   . LYS   A 1 156 ? -30.010 9.655   9.773  1.00 78.50  ? 452 LYS   A N   1 
ATOM   1166 C  CA  . LYS   A 1 156 ? -30.051 11.096  9.972  1.00 90.06  ? 452 LYS   A CA  1 
ATOM   1167 C  C   . LYS   A 1 156 ? -30.178 11.459  11.449 1.00 95.52  ? 452 LYS   A C   1 
ATOM   1168 O  O   . LYS   A 1 156 ? -30.739 12.500  11.781 1.00 107.80 ? 452 LYS   A O   1 
ATOM   1169 C  CB  . LYS   A 1 156 ? -31.196 11.749  9.186  1.00 99.04  ? 452 LYS   A CB  1 
ATOM   1170 C  CG  . LYS   A 1 156 ? -31.091 11.710  7.676  1.00 108.38 ? 452 LYS   A CG  1 
ATOM   1171 C  CD  . LYS   A 1 156 ? -32.204 12.546  7.048  1.00 117.39 ? 452 LYS   A CD  1 
ATOM   1172 C  CE  . LYS   A 1 156 ? -33.394 11.703  6.621  1.00 113.74 ? 452 LYS   A CE  1 
ATOM   1173 N  NZ  . LYS   A 1 156 ? -33.121 11.038  5.325  1.00 120.73 ? 452 LYS   A NZ  1 
ATOM   1174 N  N   . GLY   A 1 157 ? -29.678 10.598  12.339 1.00 85.41  ? 453 GLY   A N   1 
ATOM   1175 C  CA  . GLY   A 1 157 ? -29.827 10.769  13.764 1.00 90.89  ? 453 GLY   A CA  1 
ATOM   1176 C  C   . GLY   A 1 157 ? -31.080 10.152  14.352 1.00 84.55  ? 453 GLY   A C   1 
ATOM   1177 O  O   . GLY   A 1 157 ? -31.189 10.047  15.577 1.00 76.79  ? 453 GLY   A O   1 
ATOM   1178 N  N   . ASN   A 1 158 ? -32.042 9.754   13.522 1.00 80.93  ? 454 ASN   A N   1 
ATOM   1179 C  CA  . ASN   A 1 158 ? -33.200 9.005   14.006 1.00 82.80  ? 454 ASN   A CA  1 
ATOM   1180 C  C   . ASN   A 1 158 ? -32.848 7.519   13.989 1.00 81.15  ? 454 ASN   A C   1 
ATOM   1181 O  O   . ASN   A 1 158 ? -33.333 6.733   13.171 1.00 89.18  ? 454 ASN   A O   1 
ATOM   1182 C  CB  . ASN   A 1 158 ? -34.435 9.320   13.174 1.00 91.56  ? 454 ASN   A CB  1 
ATOM   1183 C  CG  . ASN   A 1 158 ? -35.690 8.663   13.720 1.00 99.09  ? 454 ASN   A CG  1 
ATOM   1184 O  OD1 . ASN   A 1 158 ? -35.624 7.764   14.566 1.00 109.78 ? 454 ASN   A OD1 1 
ATOM   1185 N  ND2 . ASN   A 1 158 ? -36.845 9.112   13.240 1.00 99.50  ? 454 ASN   A ND2 1 
ATOM   1186 N  N   . LEU   A 1 159 ? -31.981 7.151   14.934 1.00 73.95  ? 455 LEU   A N   1 
ATOM   1187 C  CA  . LEU   A 1 159 ? -31.293 5.868   14.889 1.00 72.40  ? 455 LEU   A CA  1 
ATOM   1188 C  C   . LEU   A 1 159 ? -32.280 4.707   14.888 1.00 74.29  ? 455 LEU   A C   1 
ATOM   1189 O  O   . LEU   A 1 159 ? -33.350 4.762   15.510 1.00 75.36  ? 455 LEU   A O   1 
ATOM   1190 C  CB  . LEU   A 1 159 ? -30.326 5.748   16.082 1.00 73.81  ? 455 LEU   A CB  1 
ATOM   1191 C  CG  . LEU   A 1 159 ? -28.875 6.253   15.960 1.00 75.19  ? 455 LEU   A CG  1 
ATOM   1192 C  CD1 . LEU   A 1 159 ? -28.776 7.483   15.087 1.00 82.52  ? 455 LEU   A CD1 1 
ATOM   1193 C  CD2 . LEU   A 1 159 ? -28.278 6.553   17.340 1.00 75.14  ? 455 LEU   A CD2 1 
ATOM   1194 N  N   . ARG   A 1 160 ? -31.892 3.648   14.184 1.00 63.63  ? 456 ARG   A N   1 
ATOM   1195 C  CA  . ARG   A 1 160 ? -32.662 2.420   14.027 1.00 59.75  ? 456 ARG   A CA  1 
ATOM   1196 C  C   . ARG   A 1 160 ? -31.773 1.228   14.337 1.00 58.09  ? 456 ARG   A C   1 
ATOM   1197 O  O   . ARG   A 1 160 ? -30.607 1.197   13.930 1.00 71.60  ? 456 ARG   A O   1 
ATOM   1198 C  CB  . ARG   A 1 160 ? -33.217 2.257   12.562 1.00 57.75  ? 456 ARG   A CB  1 
ATOM   1199 C  CG  . ARG   A 1 160 ? -34.069 3.405   12.047 1.00 68.51  ? 456 ARG   A CG  1 
ATOM   1200 C  CD  . ARG   A 1 160 ? -34.581 3.155   10.629 1.00 74.07  ? 456 ARG   A CD  1 
ATOM   1201 N  NE  . ARG   A 1 160 ? -33.589 3.490   9.624  1.00 76.26  ? 456 ARG   A NE  1 
ATOM   1202 C  CZ  . ARG   A 1 160 ? -33.886 3.784   8.361  1.00 82.91  ? 456 ARG   A CZ  1 
ATOM   1203 N  NH1 . ARG   A 1 160 ? -35.151 3.785   7.957  1.00 85.88  ? 456 ARG   A NH1 1 
ATOM   1204 N  NH2 . ARG   A 1 160 ? -32.926 4.092   7.503  1.00 75.99  ? 456 ARG   A NH2 1 
ATOM   1205 N  N   . SER   A 1 161 ? -32.335 0.222   15.002 1.00 60.54  ? 457 SER   A N   1 
ATOM   1206 C  CA  . SER   A 1 161 ? -31.554 -0.946  15.386 1.00 58.28  ? 457 SER   A CA  1 
ATOM   1207 C  C   . SER   A 1 161 ? -31.374 -1.885  14.213 1.00 55.67  ? 457 SER   A C   1 
ATOM   1208 O  O   . SER   A 1 161 ? -32.279 -2.049  13.382 1.00 63.82  ? 457 SER   A O   1 
ATOM   1209 C  CB  . SER   A 1 161 ? -32.219 -1.699  16.549 1.00 56.59  ? 457 SER   A CB  1 
ATOM   1210 O  OG  . SER   A 1 161 ? -32.710 -0.780  17.525 1.00 58.94  ? 457 SER   A OG  1 
ATOM   1211 N  N   . ALA   A 1 162 ? -30.201 -2.520  14.154 1.00 52.62  ? 458 ALA   A N   1 
ATOM   1212 C  CA  . ALA   A 1 162 ? -29.878 -3.340  12.991 1.00 55.86  ? 458 ALA   A CA  1 
ATOM   1213 C  C   . ALA   A 1 162 ? -28.752 -4.310  13.323 1.00 56.53  ? 458 ALA   A C   1 
ATOM   1214 O  O   . ALA   A 1 162 ? -27.954 -4.079  14.233 1.00 60.11  ? 458 ALA   A O   1 
ATOM   1215 C  CB  . ALA   A 1 162 ? -29.480 -2.474  11.783 1.00 60.80  ? 458 ALA   A CB  1 
ATOM   1216 N  N   . ILE   A 1 163 ? -28.685 -5.392  12.542 1.00 53.63  ? 459 ILE   A N   1 
ATOM   1217 C  CA  . ILE   A 1 163 ? -27.603 -6.361  12.622 1.00 55.03  ? 459 ILE   A CA  1 
ATOM   1218 C  C   . ILE   A 1 163 ? -27.296 -6.864  11.214 1.00 54.93  ? 459 ILE   A C   1 
ATOM   1219 O  O   . ILE   A 1 163 ? -28.202 -7.008  10.388 1.00 62.07  ? 459 ILE   A O   1 
ATOM   1220 C  CB  . ILE   A 1 163 ? -27.972 -7.526  13.565 1.00 55.12  ? 459 ILE   A CB  1 
ATOM   1221 C  CG1 . ILE   A 1 163 ? -26.789 -8.468  13.721 1.00 47.15  ? 459 ILE   A CG1 1 
ATOM   1222 C  CG2 . ILE   A 1 163 ? -29.208 -8.276  13.033 1.00 51.92  ? 459 ILE   A CG2 1 
ATOM   1223 C  CD1 . ILE   A 1 163 ? -27.008 -9.590  14.723 1.00 45.73  ? 459 ILE   A CD1 1 
ATOM   1224 N  N   . THR   A 1 164 ? -26.012 -7.062  10.917 1.00 50.25  ? 460 THR   A N   1 
ATOM   1225 C  CA  . THR   A 1 164 ? -25.571 -7.585  9.618  1.00 49.40  ? 460 THR   A CA  1 
ATOM   1226 C  C   . THR   A 1 164 ? -24.842 -8.896  9.867  1.00 58.00  ? 460 THR   A C   1 
ATOM   1227 O  O   . THR   A 1 164 ? -23.917 -8.941  10.684 1.00 60.19  ? 460 THR   A O   1 
ATOM   1228 C  CB  . THR   A 1 164 ? -24.665 -6.595  8.903  1.00 48.91  ? 460 THR   A CB  1 
ATOM   1229 O  OG1 . THR   A 1 164 ? -25.377 -5.367  8.731  1.00 51.13  ? 460 THR   A OG1 1 
ATOM   1230 C  CG2 . THR   A 1 164 ? -24.266 -7.118  7.482  1.00 54.19  ? 460 THR   A CG2 1 
ATOM   1231 N  N   . ILE   A 1 165 ? -25.272 -9.962  9.200  1.00 51.22  ? 461 ILE   A N   1 
ATOM   1232 C  CA  . ILE   A 1 165 ? -24.835 -11.313 9.525  1.00 47.76  ? 461 ILE   A CA  1 
ATOM   1233 C  C   . ILE   A 1 165 ? -24.022 -11.870 8.364  1.00 56.40  ? 461 ILE   A C   1 
ATOM   1234 O  O   . ILE   A 1 165 ? -24.559 -12.108 7.277  1.00 57.08  ? 461 ILE   A O   1 
ATOM   1235 C  CB  . ILE   A 1 165 ? -26.027 -12.214 9.850  1.00 50.69  ? 461 ILE   A CB  1 
ATOM   1236 C  CG1 . ILE   A 1 165 ? -26.700 -11.711 11.141 1.00 48.65  ? 461 ILE   A CG1 1 
ATOM   1237 C  CG2 . ILE   A 1 165 ? -25.555 -13.608 10.038 1.00 48.54  ? 461 ILE   A CG2 1 
ATOM   1238 C  CD1 . ILE   A 1 165 ? -28.057 -12.304 11.428 1.00 48.93  ? 461 ILE   A CD1 1 
ATOM   1239 N  N   . PHE   A 1 166 ? -22.735 -12.096 8.604  1.00 60.37  ? 462 PHE   A N   1 
ATOM   1240 C  CA  . PHE   A 1 166 ? -21.797 -12.593 7.605  1.00 57.47  ? 462 PHE   A CA  1 
ATOM   1241 C  C   . PHE   A 1 166 ? -21.765 -14.112 7.626  1.00 60.02  ? 462 PHE   A C   1 
ATOM   1242 O  O   . PHE   A 1 166 ? -22.397 -14.736 8.486  1.00 63.43  ? 462 PHE   A O   1 
ATOM   1243 C  CB  . PHE   A 1 166 ? -20.425 -11.982 7.860  1.00 54.54  ? 462 PHE   A CB  1 
ATOM   1244 C  CG  . PHE   A 1 166 ? -20.356 -10.525 7.506  1.00 61.25  ? 462 PHE   A CG  1 
ATOM   1245 C  CD1 . PHE   A 1 166 ? -20.429 -10.116 6.174  1.00 61.81  ? 462 PHE   A CD1 1 
ATOM   1246 C  CD2 . PHE   A 1 166 ? -20.251 -9.557  8.501  1.00 57.72  ? 462 PHE   A CD2 1 
ATOM   1247 C  CE1 . PHE   A 1 166 ? -20.371 -8.768  5.835  1.00 65.28  ? 462 PHE   A CE1 1 
ATOM   1248 C  CE2 . PHE   A 1 166 ? -20.191 -8.197  8.160  1.00 55.86  ? 462 PHE   A CE2 1 
ATOM   1249 C  CZ  . PHE   A 1 166 ? -20.260 -7.805  6.822  1.00 59.55  ? 462 PHE   A CZ  1 
ATOM   1250 N  N   . PRO   A 1 167 ? -21.099 -14.753 6.649  1.00 58.44  ? 463 PRO   A N   1 
ATOM   1251 C  CA  . PRO   A 1 167 ? -21.152 -16.221 6.574  1.00 62.02  ? 463 PRO   A CA  1 
ATOM   1252 C  C   . PRO   A 1 167 ? -20.796 -16.907 7.894  1.00 66.27  ? 463 PRO   A C   1 
ATOM   1253 O  O   . PRO   A 1 167 ? -19.968 -16.433 8.680  1.00 71.28  ? 463 PRO   A O   1 
ATOM   1254 C  CB  . PRO   A 1 167 ? -20.145 -16.552 5.471  1.00 57.84  ? 463 PRO   A CB  1 
ATOM   1255 C  CG  . PRO   A 1 167 ? -20.254 -15.399 4.557  1.00 56.29  ? 463 PRO   A CG  1 
ATOM   1256 C  CD  . PRO   A 1 167 ? -20.475 -14.191 5.428  1.00 55.31  ? 463 PRO   A CD  1 
ATOM   1257 N  N   . GLN   A 1 168 ? -21.453 -18.034 8.135  1.00 65.54  ? 464 GLN   A N   1 
ATOM   1258 C  CA  . GLN   A 1 168 ? -21.243 -18.743 9.382  1.00 60.96  ? 464 GLN   A CA  1 
ATOM   1259 C  C   . GLN   A 1 168 ? -19.903 -19.468 9.351  1.00 64.56  ? 464 GLN   A C   1 
ATOM   1260 O  O   . GLN   A 1 168 ? -19.338 -19.736 8.292  1.00 59.12  ? 464 GLN   A O   1 
ATOM   1261 C  CB  . GLN   A 1 168 ? -22.373 -19.745 9.625  1.00 50.01  ? 464 GLN   A CB  1 
ATOM   1262 C  CG  . GLN   A 1 168 ? -22.385 -20.918 8.622  1.00 55.78  ? 464 GLN   A CG  1 
ATOM   1263 C  CD  . GLN   A 1 168 ? -23.764 -21.527 8.452  1.00 63.34  ? 464 GLN   A CD  1 
ATOM   1264 O  OE1 . GLN   A 1 168 ? -24.766 -20.815 8.400  1.00 72.10  ? 464 GLN   A OE1 1 
ATOM   1265 N  NE2 . GLN   A 1 168 ? -23.822 -22.853 8.366  1.00 70.84  ? 464 GLN   A NE2 1 
ATOM   1266 N  N   . ARG   A 1 169 ? -19.382 -19.769 10.539 1.00 62.63  ? 465 ARG   A N   1 
ATOM   1267 C  CA  . ARG   A 1 169 ? -18.174 -20.573 10.628 1.00 65.21  ? 465 ARG   A CA  1 
ATOM   1268 C  C   . ARG   A 1 169 ? -18.423 -21.926 9.975  1.00 71.59  ? 465 ARG   A C   1 
ATOM   1269 O  O   . ARG   A 1 169 ? -19.534 -22.461 10.032 1.00 72.28  ? 465 ARG   A O   1 
ATOM   1270 C  CB  . ARG   A 1 169 ? -17.765 -20.735 12.093 1.00 75.35  ? 465 ARG   A CB  1 
ATOM   1271 C  CG  . ARG   A 1 169 ? -16.563 -21.622 12.333 1.00 80.16  ? 465 ARG   A CG  1 
ATOM   1272 C  CD  . ARG   A 1 169 ? -16.253 -21.700 13.821 1.00 83.15  ? 465 ARG   A CD  1 
ATOM   1273 N  NE  . ARG   A 1 169 ? -15.383 -20.616 14.269 1.00 83.37  ? 465 ARG   A NE  1 
ATOM   1274 C  CZ  . ARG   A 1 169 ? -15.745 -19.674 15.133 1.00 80.16  ? 465 ARG   A CZ  1 
ATOM   1275 N  NH1 . ARG   A 1 169 ? -16.969 -19.680 15.653 1.00 76.18  ? 465 ARG   A NH1 1 
ATOM   1276 N  NH2 . ARG   A 1 169 ? -14.885 -18.719 15.476 1.00 70.10  ? 465 ARG   A NH2 1 
ATOM   1277 N  N   . THR   A 1 170 ? -17.398 -22.459 9.295  1.00 77.33  ? 466 THR   A N   1 
ATOM   1278 C  CA  . THR   A 1 170 ? -17.475 -23.798 8.733  1.00 80.76  ? 466 THR   A CA  1 
ATOM   1279 C  C   . THR   A 1 170 ? -16.387 -24.634 9.395  1.00 88.87  ? 466 THR   A C   1 
ATOM   1280 O  O   . THR   A 1 170 ? -16.598 -25.165 10.494 1.00 89.45  ? 466 THR   A O   1 
ATOM   1281 C  CB  . THR   A 1 170 ? -17.363 -23.775 7.199  1.00 86.12  ? 466 THR   A CB  1 
ATOM   1282 O  OG1 . THR   A 1 170 ? -16.258 -22.955 6.800  1.00 80.60  ? 466 THR   A OG1 1 
ATOM   1283 C  CG2 . THR   A 1 170 ? -18.648 -23.255 6.568  1.00 80.53  ? 466 THR   A CG2 1 
ATOM   1284 N  N   . ASP   A 1 171 ? -15.211 -24.757 8.781  1.00 89.99  ? 467 ASP   A N   1 
ATOM   1285 C  CA  . ASP   A 1 171 ? -14.174 -25.626 9.331  1.00 104.06 ? 467 ASP   A CA  1 
ATOM   1286 C  C   . ASP   A 1 171 ? -13.539 -25.039 10.584 1.00 105.10 ? 467 ASP   A C   1 
ATOM   1287 O  O   . ASP   A 1 171 ? -13.053 -25.788 11.437 1.00 113.14 ? 467 ASP   A O   1 
ATOM   1288 C  CB  . ASP   A 1 171 ? -13.098 -25.875 8.276  1.00 117.35 ? 467 ASP   A CB  1 
ATOM   1289 C  CG  . ASP   A 1 171 ? -12.296 -24.624 7.962  1.00 125.38 ? 467 ASP   A CG  1 
ATOM   1290 O  OD1 . ASP   A 1 171 ? -12.882 -23.518 7.981  1.00 125.30 ? 467 ASP   A OD1 1 
ATOM   1291 O  OD2 . ASP   A 1 171 ? -11.078 -24.740 7.716  1.00 131.61 ? 467 ASP   A OD2 1 
ATOM   1292 N  N   . GLY   A 1 172 ? -13.527 -23.713 10.708 1.00 100.48 ? 468 GLY   A N   1 
ATOM   1293 C  CA  . GLY   A 1 172 ? -12.802 -23.042 11.771 1.00 97.74  ? 468 GLY   A CA  1 
ATOM   1294 C  C   . GLY   A 1 172 ? -11.720 -22.097 11.276 1.00 103.99 ? 468 GLY   A C   1 
ATOM   1295 O  O   . GLY   A 1 172 ? -11.591 -20.982 11.786 1.00 103.22 ? 468 GLY   A O   1 
ATOM   1296 N  N   . LYS   A 1 173 ? -10.930 -22.523 10.289 1.00 108.60 ? 469 LYS   A N   1 
ATOM   1297 C  CA  . LYS   A 1 173 ? -9.870  -21.687 9.738  1.00 110.06 ? 469 LYS   A CA  1 
ATOM   1298 C  C   . LYS   A 1 173 ? -10.360 -20.758 8.633  1.00 110.22 ? 469 LYS   A C   1 
ATOM   1299 O  O   . LYS   A 1 173 ? -9.560  -19.993 8.084  1.00 113.17 ? 469 LYS   A O   1 
ATOM   1300 C  CB  . LYS   A 1 173 ? -8.717  -22.563 9.223  1.00 115.83 ? 469 LYS   A CB  1 
ATOM   1301 C  CG  . LYS   A 1 173 ? -7.950  -23.263 10.346 1.00 119.95 ? 469 LYS   A CG  1 
ATOM   1302 C  CD  . LYS   A 1 173 ? -6.852  -24.181 9.832  1.00 126.02 ? 469 LYS   A CD  1 
ATOM   1303 C  CE  . LYS   A 1 173 ? -5.664  -23.397 9.294  1.00 132.27 ? 469 LYS   A CE  1 
ATOM   1304 N  NZ  . LYS   A 1 173 ? -4.605  -24.301 8.748  1.00 139.30 ? 469 LYS   A NZ  1 
ATOM   1305 N  N   . HIS   A 1 174 ? -11.645 -20.803 8.299  1.00 104.89 ? 470 HIS   A N   1 
ATOM   1306 C  CA  . HIS   A 1 174 ? -12.264 -19.876 7.355  1.00 107.89 ? 470 HIS   A CA  1 
ATOM   1307 C  C   . HIS   A 1 174 ? -13.328 -19.120 8.133  1.00 110.90 ? 470 HIS   A C   1 
ATOM   1308 O  O   . HIS   A 1 174 ? -14.513 -19.462 8.092  1.00 116.36 ? 470 HIS   A O   1 
ATOM   1309 C  CB  . HIS   A 1 174 ? -12.847 -20.591 6.163  1.00 102.64 ? 470 HIS   A CB  1 
ATOM   1310 C  CG  . HIS   A 1 174 ? -11.833 -21.347 5.374  1.00 108.58 ? 470 HIS   A CG  1 
ATOM   1311 N  ND1 . HIS   A 1 174 ? -11.797 -22.723 5.333  1.00 112.60 ? 470 HIS   A ND1 1 
ATOM   1312 C  CD2 . HIS   A 1 174 ? -10.795 -20.919 4.619  1.00 111.89 ? 470 HIS   A CD2 1 
ATOM   1313 C  CE1 . HIS   A 1 174 ? -10.794 -23.111 4.566  1.00 118.16 ? 470 HIS   A CE1 1 
ATOM   1314 N  NE2 . HIS   A 1 174 ? -10.167 -22.036 4.123  1.00 116.73 ? 470 HIS   A NE2 1 
ATOM   1315 N  N   . ASP   A 1 175 ? -12.895 -18.097 8.853  1.00 102.69 ? 471 ASP   A N   1 
ATOM   1316 C  CA  . ASP   A 1 175 ? -13.775 -17.311 9.696  1.00 86.85  ? 471 ASP   A CA  1 
ATOM   1317 C  C   . ASP   A 1 175 ? -13.907 -15.906 9.144  1.00 78.51  ? 471 ASP   A C   1 
ATOM   1318 O  O   . ASP   A 1 175 ? -12.918 -15.292 8.735  1.00 84.84  ? 471 ASP   A O   1 
ATOM   1319 C  CB  . ASP   A 1 175 ? -13.254 -17.240 11.125 1.00 93.82  ? 471 ASP   A CB  1 
ATOM   1320 C  CG  . ASP   A 1 175 ? -13.677 -18.420 11.947 1.00 93.48  ? 471 ASP   A CG  1 
ATOM   1321 O  OD1 . ASP   A 1 175 ? -14.289 -19.353 11.390 1.00 99.78  ? 471 ASP   A OD1 1 
ATOM   1322 O  OD2 . ASP   A 1 175 ? -13.400 -18.411 13.155 1.00 97.89  ? 471 ASP   A OD2 1 
ATOM   1323 N  N   . PHE   A 1 176 ? -15.130 -15.399 9.144  1.00 70.82  ? 472 PHE   A N   1 
ATOM   1324 C  CA  . PHE   A 1 176 ? -15.360 -13.988 8.884  1.00 68.29  ? 472 PHE   A CA  1 
ATOM   1325 C  C   . PHE   A 1 176 ? -15.298 -13.253 10.210 1.00 64.26  ? 472 PHE   A C   1 
ATOM   1326 O  O   . PHE   A 1 176 ? -16.013 -13.610 11.150 1.00 65.73  ? 472 PHE   A O   1 
ATOM   1327 C  CB  . PHE   A 1 176 ? -16.704 -13.764 8.195  1.00 61.44  ? 472 PHE   A CB  1 
ATOM   1328 C  CG  . PHE   A 1 176 ? -16.673 -14.044 6.731  1.00 60.33  ? 472 PHE   A CG  1 
ATOM   1329 C  CD1 . PHE   A 1 176 ? -16.591 -15.342 6.262  1.00 64.70  ? 472 PHE   A CD1 1 
ATOM   1330 C  CD2 . PHE   A 1 176 ? -16.718 -13.005 5.823  1.00 57.53  ? 472 PHE   A CD2 1 
ATOM   1331 C  CE1 . PHE   A 1 176 ? -16.572 -15.614 4.881  1.00 70.14  ? 472 PHE   A CE1 1 
ATOM   1332 C  CE2 . PHE   A 1 176 ? -16.686 -13.269 4.437  1.00 63.95  ? 472 PHE   A CE2 1 
ATOM   1333 C  CZ  . PHE   A 1 176 ? -16.604 -14.576 3.981  1.00 66.76  ? 472 PHE   A CZ  1 
ATOM   1334 N  N   . ARG   A 1 177 ? -14.446 -12.235 10.292 1.00 60.23  ? 473 ARG   A N   1 
ATOM   1335 C  CA  . ARG   A 1 177 ? -14.295 -11.514 11.552 1.00 67.19  ? 473 ARG   A CA  1 
ATOM   1336 C  C   . ARG   A 1 177 ? -14.095 -10.031 11.288 1.00 67.76  ? 473 ARG   A C   1 
ATOM   1337 O  O   . ARG   A 1 177 ? -13.300 -9.655  10.422 1.00 70.21  ? 473 ARG   A O   1 
ATOM   1338 C  CB  . ARG   A 1 177 ? -13.108 -12.056 12.362 1.00 75.96  ? 473 ARG   A CB  1 
ATOM   1339 C  CG  . ARG   A 1 177 ? -13.322 -13.421 12.979 1.00 75.29  ? 473 ARG   A CG  1 
ATOM   1340 C  CD  . ARG   A 1 177 ? -14.385 -13.369 14.074 1.00 78.31  ? 473 ARG   A CD  1 
ATOM   1341 N  NE  . ARG   A 1 177 ? -14.180 -12.281 15.032 1.00 80.23  ? 473 ARG   A NE  1 
ATOM   1342 C  CZ  . ARG   A 1 177 ? -13.424 -12.369 16.126 1.00 81.51  ? 473 ARG   A CZ  1 
ATOM   1343 N  NH1 . ARG   A 1 177 ? -12.780 -13.498 16.407 1.00 74.62  ? 473 ARG   A NH1 1 
ATOM   1344 N  NH2 . ARG   A 1 177 ? -13.312 -11.324 16.941 1.00 82.02  ? 473 ARG   A NH2 1 
ATOM   1345 N  N   . VAL   A 1 178 ? -14.815 -9.193  12.030 1.00 58.71  ? 474 VAL   A N   1 
ATOM   1346 C  CA  . VAL   A 1 178 ? -14.458 -7.783  12.162 1.00 63.49  ? 474 VAL   A CA  1 
ATOM   1347 C  C   . VAL   A 1 178 ? -13.494 -7.676  13.338 1.00 65.52  ? 474 VAL   A C   1 
ATOM   1348 O  O   . VAL   A 1 178 ? -13.844 -8.043  14.466 1.00 66.10  ? 474 VAL   A O   1 
ATOM   1349 C  CB  . VAL   A 1 178 ? -15.700 -6.897  12.372 1.00 53.45  ? 474 VAL   A CB  1 
ATOM   1350 C  CG1 . VAL   A 1 178 ? -15.306 -5.433  12.457 1.00 56.94  ? 474 VAL   A CG1 1 
ATOM   1351 C  CG2 . VAL   A 1 178 ? -16.721 -7.100  11.227 1.00 56.92  ? 474 VAL   A CG2 1 
ATOM   1352 N  N   . TRP   A 1 179 ? -12.268 -7.198  13.076 1.00 69.32  ? 475 TRP   A N   1 
ATOM   1353 C  CA  . TRP   A 1 179 ? -11.252 -7.126  14.129 1.00 69.80  ? 475 TRP   A CA  1 
ATOM   1354 C  C   . TRP   A 1 179 ? -11.494 -5.978  15.107 1.00 70.82  ? 475 TRP   A C   1 
ATOM   1355 O  O   . TRP   A 1 179 ? -11.006 -6.036  16.248 1.00 66.28  ? 475 TRP   A O   1 
ATOM   1356 C  CB  . TRP   A 1 179 ? -9.849  -7.012  13.518 1.00 71.14  ? 475 TRP   A CB  1 
ATOM   1357 C  CG  . TRP   A 1 179 ? -9.333  -8.329  12.989 1.00 76.31  ? 475 TRP   A CG  1 
ATOM   1358 C  CD1 . TRP   A 1 179 ? -10.069 -9.316  12.400 1.00 77.62  ? 475 TRP   A CD1 1 
ATOM   1359 C  CD2 . TRP   A 1 179 ? -7.983  -8.811  13.030 1.00 76.46  ? 475 TRP   A CD2 1 
ATOM   1360 N  NE1 . TRP   A 1 179 ? -9.260  -10.379 12.064 1.00 78.47  ? 475 TRP   A NE1 1 
ATOM   1361 C  CE2 . TRP   A 1 179 ? -7.977  -10.095 12.449 1.00 79.17  ? 475 TRP   A CE2 1 
ATOM   1362 C  CE3 . TRP   A 1 179 ? -6.781  -8.284  13.501 1.00 83.36  ? 475 TRP   A CE3 1 
ATOM   1363 C  CZ2 . TRP   A 1 179 ? -6.819  -10.852 12.326 1.00 88.27  ? 475 TRP   A CZ2 1 
ATOM   1364 C  CZ3 . TRP   A 1 179 ? -5.635  -9.040  13.382 1.00 88.10  ? 475 TRP   A CZ3 1 
ATOM   1365 C  CH2 . TRP   A 1 179 ? -5.661  -10.307 12.799 1.00 90.15  ? 475 TRP   A CH2 1 
ATOM   1366 N  N   . ASN   A 1 180 ? -12.229 -4.951  14.689 1.00 66.74  ? 476 ASN   A N   1 
ATOM   1367 C  CA  . ASN   A 1 180 ? -12.650 -3.895  15.590 1.00 74.48  ? 476 ASN   A CA  1 
ATOM   1368 C  C   . ASN   A 1 180 ? -13.627 -4.436  16.621 1.00 71.73  ? 476 ASN   A C   1 
ATOM   1369 O  O   . ASN   A 1 180 ? -14.435 -5.323  16.339 1.00 63.89  ? 476 ASN   A O   1 
ATOM   1370 C  CB  . ASN   A 1 180 ? -13.331 -2.764  14.830 1.00 78.72  ? 476 ASN   A CB  1 
ATOM   1371 C  CG  . ASN   A 1 180 ? -12.479 -2.210  13.739 1.00 83.29  ? 476 ASN   A CG  1 
ATOM   1372 O  OD1 . ASN   A 1 180 ? -11.942 -2.956  12.919 1.00 89.74  ? 476 ASN   A OD1 1 
ATOM   1373 N  ND2 . ASN   A 1 180 ? -12.327 -0.895  13.723 1.00 85.76  ? 476 ASN   A ND2 1 
ATOM   1374 N  N   . SER   A 1 181 ? -13.558 -3.873  17.828 1.00 66.03  ? 477 SER   A N   1 
ATOM   1375 C  CA  . SER   A 1 181 ? -14.500 -4.268  18.869 1.00 61.36  ? 477 SER   A CA  1 
ATOM   1376 C  C   . SER   A 1 181 ? -15.839 -3.564  18.705 1.00 59.24  ? 477 SER   A C   1 
ATOM   1377 O  O   . SER   A 1 181 ? -16.885 -4.113  19.084 1.00 55.24  ? 477 SER   A O   1 
ATOM   1378 C  CB  . SER   A 1 181 ? -13.902 -3.984  20.243 1.00 61.13  ? 477 SER   A CB  1 
ATOM   1379 O  OG  . SER   A 1 181 ? -13.206 -2.742  20.230 1.00 74.26  ? 477 SER   A OG  1 
ATOM   1380 N  N   . GLN   A 1 182 ? -15.817 -2.354  18.154 1.00 63.98  ? 478 GLN   A N   1 
ATOM   1381 C  CA  . GLN   A 1 182 ? -17.007 -1.654  17.703 1.00 61.00  ? 478 GLN   A CA  1 
ATOM   1382 C  C   . GLN   A 1 182 ? -16.702 -1.051  16.343 1.00 59.16  ? 478 GLN   A C   1 
ATOM   1383 O  O   . GLN   A 1 182 ? -15.567 -0.651  16.084 1.00 65.75  ? 478 GLN   A O   1 
ATOM   1384 C  CB  . GLN   A 1 182 ? -17.435 -0.523  18.639 1.00 66.00  ? 478 GLN   A CB  1 
ATOM   1385 C  CG  . GLN   A 1 182 ? -17.767 -0.925  20.082 1.00 77.28  ? 478 GLN   A CG  1 
ATOM   1386 C  CD  . GLN   A 1 182 ? -17.850 0.283   21.012 1.00 89.30  ? 478 GLN   A CD  1 
ATOM   1387 O  OE1 . GLN   A 1 182 ? -18.684 1.170   20.809 1.00 95.39  ? 478 GLN   A OE1 1 
ATOM   1388 N  NE2 . GLN   A 1 182 ? -16.973 0.331   22.027 1.00 87.96  ? 478 GLN   A NE2 1 
ATOM   1389 N  N   . LEU   A 1 183 ? -17.737 -0.939  15.505 1.00 58.73  ? 479 LEU   A N   1 
ATOM   1390 C  CA  . LEU   A 1 183 ? -17.565 -0.406  14.156 1.00 65.15  ? 479 LEU   A CA  1 
ATOM   1391 C  C   . LEU   A 1 183 ? -16.959 0.991   14.181 1.00 69.02  ? 479 LEU   A C   1 
ATOM   1392 O  O   . LEU   A 1 183 ? -16.104 1.322   13.354 1.00 74.22  ? 479 LEU   A O   1 
ATOM   1393 C  CB  . LEU   A 1 183 ? -18.909 -0.387  13.422 1.00 65.13  ? 479 LEU   A CB  1 
ATOM   1394 C  CG  . LEU   A 1 183 ? -19.598 -1.694  12.985 1.00 68.13  ? 479 LEU   A CG  1 
ATOM   1395 C  CD1 . LEU   A 1 183 ? -20.808 -1.417  12.074 1.00 61.61  ? 479 LEU   A CD1 1 
ATOM   1396 C  CD2 . LEU   A 1 183 ? -18.631 -2.642  12.274 1.00 73.61  ? 479 LEU   A CD2 1 
ATOM   1397 N  N   . ILE   A 1 184 ? -17.378 1.830   15.126 1.00 64.51  ? 480 ILE   A N   1 
ATOM   1398 C  CA  . ILE   A 1 184 ? -16.901 3.199   15.213 1.00 59.65  ? 480 ILE   A CA  1 
ATOM   1399 C  C   . ILE   A 1 184 ? -16.274 3.385   16.594 1.00 69.56  ? 480 ILE   A C   1 
ATOM   1400 O  O   . ILE   A 1 184 ? -16.957 3.277   17.625 1.00 70.12  ? 480 ILE   A O   1 
ATOM   1401 C  CB  . ILE   A 1 184 ? -18.022 4.212   14.958 1.00 71.18  ? 480 ILE   A CB  1 
ATOM   1402 C  CG1 . ILE   A 1 184 ? -18.622 4.014   13.573 1.00 79.41  ? 480 ILE   A CG1 1 
ATOM   1403 C  CG2 . ILE   A 1 184 ? -17.479 5.614   15.003 1.00 67.78  ? 480 ILE   A CG2 1 
ATOM   1404 C  CD1 . ILE   A 1 184 ? -19.799 4.910   13.318 1.00 78.68  ? 480 ILE   A CD1 1 
ATOM   1405 N  N   . ARG   A 1 185 ? -14.965 3.622   16.611 1.00 78.91  ? 481 ARG   A N   1 
ATOM   1406 C  CA  . ARG   A 1 185 ? -14.218 3.882   17.827 1.00 77.88  ? 481 ARG   A CA  1 
ATOM   1407 C  C   . ARG   A 1 185 ? -13.171 4.943   17.544 1.00 86.43  ? 481 ARG   A C   1 
ATOM   1408 O  O   . ARG   A 1 185 ? -12.684 5.072   16.418 1.00 97.63  ? 481 ARG   A O   1 
ATOM   1409 C  CB  . ARG   A 1 185 ? -13.514 2.634   18.368 1.00 84.78  ? 481 ARG   A CB  1 
ATOM   1410 C  CG  . ARG   A 1 185 ? -14.429 1.502   18.745 1.00 86.96  ? 481 ARG   A CG  1 
ATOM   1411 C  CD  . ARG   A 1 185 ? -13.922 0.757   19.977 1.00 83.44  ? 481 ARG   A CD  1 
ATOM   1412 N  NE  . ARG   A 1 185 ? -14.157 1.509   21.207 1.00 87.31  ? 481 ARG   A NE  1 
ATOM   1413 C  CZ  . ARG   A 1 185 ? -13.941 1.025   22.425 1.00 88.36  ? 481 ARG   A CZ  1 
ATOM   1414 N  NH1 . ARG   A 1 185 ? -13.484 -0.213  22.579 1.00 78.10  ? 481 ARG   A NH1 1 
ATOM   1415 N  NH2 . ARG   A 1 185 ? -14.182 1.776   23.492 1.00 95.85  ? 481 ARG   A NH2 1 
ATOM   1416 N  N   . TYR   A 1 186 ? -12.833 5.697   18.586 1.00 83.52  ? 482 TYR   A N   1 
ATOM   1417 C  CA  . TYR   A 1 186 ? -11.770 6.685   18.542 1.00 91.78  ? 482 TYR   A CA  1 
ATOM   1418 C  C   . TYR   A 1 186 ? -10.422 6.035   18.836 1.00 93.89  ? 482 TYR   A C   1 
ATOM   1419 O  O   . TYR   A 1 186 ? -10.310 5.167   19.708 1.00 89.72  ? 482 TYR   A O   1 
ATOM   1420 C  CB  . TYR   A 1 186 ? -12.055 7.801   19.554 1.00 94.53  ? 482 TYR   A CB  1 
ATOM   1421 C  CG  . TYR   A 1 186 ? -13.294 8.610   19.210 1.00 99.92  ? 482 TYR   A CG  1 
ATOM   1422 C  CD1 . TYR   A 1 186 ? -14.258 8.901   20.165 1.00 103.23 ? 482 TYR   A CD1 1 
ATOM   1423 C  CD2 . TYR   A 1 186 ? -13.508 9.067   17.913 1.00 93.09  ? 482 TYR   A CD2 1 
ATOM   1424 C  CE1 . TYR   A 1 186 ? -15.393 9.638   19.845 1.00 105.18 ? 482 TYR   A CE1 1 
ATOM   1425 C  CE2 . TYR   A 1 186 ? -14.637 9.807   17.588 1.00 95.08  ? 482 TYR   A CE2 1 
ATOM   1426 C  CZ  . TYR   A 1 186 ? -15.578 10.084  18.558 1.00 103.19 ? 482 TYR   A CZ  1 
ATOM   1427 O  OH  . TYR   A 1 186 ? -16.704 10.818  18.237 1.00 101.43 ? 482 TYR   A OH  1 
ATOM   1428 N  N   . ALA   A 1 187 ? -9.400  6.476   18.110 1.00 92.75  ? 483 ALA   A N   1 
ATOM   1429 C  CA  . ALA   A 1 187 ? -8.059  5.929   18.236 1.00 91.30  ? 483 ALA   A CA  1 
ATOM   1430 C  C   . ALA   A 1 187 ? -7.474  6.228   19.607 1.00 102.58 ? 483 ALA   A C   1 
ATOM   1431 O  O   . ALA   A 1 187 ? -7.825  7.210   20.261 1.00 93.14  ? 483 ALA   A O   1 
ATOM   1432 C  CB  . ALA   A 1 187 ? -7.140  6.508   17.169 1.00 101.24 ? 483 ALA   A CB  1 
ATOM   1433 N  N   . GLY   A 1 188 ? -6.545  5.372   20.021 1.00 107.07 ? 484 GLY   A N   1 
ATOM   1434 C  CA  . GLY   A 1 188 ? -5.762  5.605   21.210 1.00 114.62 ? 484 GLY   A CA  1 
ATOM   1435 C  C   . GLY   A 1 188 ? -4.279  5.448   20.958 1.00 120.76 ? 484 GLY   A C   1 
ATOM   1436 O  O   . GLY   A 1 188 ? -3.814  4.376   20.563 1.00 123.49 ? 484 GLY   A O   1 
ATOM   1437 N  N   . TYR   A 1 189 ? -3.524  6.515   21.180 1.00 123.00 ? 485 TYR   A N   1 
ATOM   1438 C  CA  . TYR   A 1 189 ? -2.081  6.490   21.013 1.00 124.01 ? 485 TYR   A CA  1 
ATOM   1439 C  C   . TYR   A 1 189 ? -1.409  6.814   22.336 1.00 124.64 ? 485 TYR   A C   1 
ATOM   1440 O  O   . TYR   A 1 189 ? -1.783  7.773   23.023 1.00 117.52 ? 485 TYR   A O   1 
ATOM   1441 C  CB  . TYR   A 1 189 ? -1.603  7.494   19.957 1.00 123.51 ? 485 TYR   A CB  1 
ATOM   1442 C  CG  . TYR   A 1 189 ? -2.518  7.700   18.777 1.00 117.98 ? 485 TYR   A CG  1 
ATOM   1443 C  CD1 . TYR   A 1 189 ? -3.552  8.624   18.835 1.00 117.54 ? 485 TYR   A CD1 1 
ATOM   1444 C  CD2 . TYR   A 1 189 ? -2.327  7.002   17.595 1.00 114.11 ? 485 TYR   A CD2 1 
ATOM   1445 C  CE1 . TYR   A 1 189 ? -4.383  8.836   17.759 1.00 118.25 ? 485 TYR   A CE1 1 
ATOM   1446 C  CE2 . TYR   A 1 189 ? -3.154  7.209   16.508 1.00 118.04 ? 485 TYR   A CE2 1 
ATOM   1447 C  CZ  . TYR   A 1 189 ? -4.177  8.130   16.595 1.00 116.12 ? 485 TYR   A CZ  1 
ATOM   1448 O  OH  . TYR   A 1 189 ? -5.006  8.348   15.522 1.00 111.88 ? 485 TYR   A OH  1 
ATOM   1449 N  N   . LYS   A 1 190 ? -0.402  6.018   22.678 1.00 135.21 ? 486 LYS   A N   1 
ATOM   1450 C  CA  . LYS   A 1 190 ? 0.482   6.351   23.781 1.00 145.03 ? 486 LYS   A CA  1 
ATOM   1451 C  C   . LYS   A 1 190 ? 1.305   7.593   23.423 1.00 156.63 ? 486 LYS   A C   1 
ATOM   1452 O  O   . LYS   A 1 190 ? 1.213   8.143   22.323 1.00 159.80 ? 486 LYS   A O   1 
ATOM   1453 C  CB  . LYS   A 1 190 ? 1.364   5.151   24.108 1.00 147.47 ? 486 LYS   A CB  1 
ATOM   1454 C  CG  . LYS   A 1 190 ? 1.555   4.227   22.915 1.00 147.80 ? 486 LYS   A CG  1 
ATOM   1455 C  CD  . LYS   A 1 190 ? 2.500   3.080   23.216 1.00 150.39 ? 486 LYS   A CD  1 
ATOM   1456 C  CE  . LYS   A 1 190 ? 1.789   1.927   23.897 1.00 143.75 ? 486 LYS   A CE  1 
ATOM   1457 N  NZ  . LYS   A 1 190 ? 2.638   0.703   23.897 1.00 145.39 ? 486 LYS   A NZ  1 
ATOM   1458 N  N   . GLN   A 1 191 ? 2.125   8.046   24.363 1.00 159.98 ? 487 GLN   A N   1 
ATOM   1459 C  CA  . GLN   A 1 191 ? 2.845   9.303   24.227 1.00 160.19 ? 487 GLN   A CA  1 
ATOM   1460 C  C   . GLN   A 1 191 ? 4.351   9.104   24.350 1.00 162.59 ? 487 GLN   A C   1 
ATOM   1461 O  O   . GLN   A 1 191 ? 4.811   8.068   24.845 1.00 159.39 ? 487 GLN   A O   1 
ATOM   1462 C  CB  . GLN   A 1 191 ? 2.371   10.307  25.289 1.00 161.30 ? 487 GLN   A CB  1 
ATOM   1463 C  CG  . GLN   A 1 191 ? 1.032   10.952  24.981 1.00 158.09 ? 487 GLN   A CG  1 
ATOM   1464 C  CD  . GLN   A 1 191 ? 1.063   11.787  23.715 1.00 163.14 ? 487 GLN   A CD  1 
ATOM   1465 O  OE1 . GLN   A 1 191 ? 1.024   11.261  22.601 1.00 161.52 ? 487 GLN   A OE1 1 
ATOM   1466 N  NE2 . GLN   A 1 191 ? 1.131   13.101  23.881 1.00 171.32 ? 487 GLN   A NE2 1 
ATOM   1467 N  N   . PRO   A 1 192 ? 5.152   10.074  23.898 1.00 168.91 ? 488 PRO   A N   1 
ATOM   1468 C  CA  . PRO   A 1 192 ? 6.584   10.033  24.229 1.00 175.69 ? 488 PRO   A CA  1 
ATOM   1469 C  C   . PRO   A 1 192 ? 6.845   10.164  25.716 1.00 179.14 ? 488 PRO   A C   1 
ATOM   1470 O  O   . PRO   A 1 192 ? 7.796   9.564   26.232 1.00 184.96 ? 488 PRO   A O   1 
ATOM   1471 C  CB  . PRO   A 1 192 ? 7.158   11.222  23.446 1.00 182.21 ? 488 PRO   A CB  1 
ATOM   1472 C  CG  . PRO   A 1 192 ? 5.997   12.129  23.227 1.00 180.69 ? 488 PRO   A CG  1 
ATOM   1473 C  CD  . PRO   A 1 192 ? 4.824   11.218  23.029 1.00 172.73 ? 488 PRO   A CD  1 
ATOM   1474 N  N   . ASP   A 1 193 ? 6.016   10.929  26.428 1.00 174.78 ? 489 ASP   A N   1 
ATOM   1475 C  CA  . ASP   A 1 193 ? 6.146   11.105  27.866 1.00 172.36 ? 489 ASP   A CA  1 
ATOM   1476 C  C   . ASP   A 1 193 ? 5.400   10.041  28.658 1.00 163.51 ? 489 ASP   A C   1 
ATOM   1477 O  O   . ASP   A 1 193 ? 5.177   10.218  29.863 1.00 161.87 ? 489 ASP   A O   1 
ATOM   1478 C  CB  . ASP   A 1 193 ? 5.654   12.494  28.274 1.00 175.75 ? 489 ASP   A CB  1 
ATOM   1479 C  CG  . ASP   A 1 193 ? 4.241   12.763  27.815 1.00 172.79 ? 489 ASP   A CG  1 
ATOM   1480 O  OD1 . ASP   A 1 193 ? 4.013   12.831  26.588 1.00 171.95 ? 489 ASP   A OD1 1 
ATOM   1481 O  OD2 . ASP   A 1 193 ? 3.357   12.893  28.686 1.00 171.59 ? 489 ASP   A OD2 1 
ATOM   1482 N  N   . GLY   A 1 194 ? 4.995   8.949   28.011 1.00 162.03 ? 490 GLY   A N   1 
ATOM   1483 C  CA  . GLY   A 1 194 ? 4.394   7.828   28.693 1.00 159.55 ? 490 GLY   A CA  1 
ATOM   1484 C  C   . GLY   A 1 194 ? 2.881   7.853   28.798 1.00 157.82 ? 490 GLY   A C   1 
ATOM   1485 O  O   . GLY   A 1 194 ? 2.274   6.790   28.956 1.00 155.56 ? 490 GLY   A O   1 
ATOM   1486 N  N   . SER   A 1 195 ? 2.250   9.027   28.717 1.00 159.30 ? 491 SER   A N   1 
ATOM   1487 C  CA  . SER   A 1 195 ? 0.801   9.106   28.886 1.00 155.27 ? 491 SER   A CA  1 
ATOM   1488 C  C   . SER   A 1 195 ? 0.055   8.705   27.614 1.00 152.77 ? 491 SER   A C   1 
ATOM   1489 O  O   . SER   A 1 195 ? 0.618   8.027   26.746 1.00 150.69 ? 491 SER   A O   1 
ATOM   1490 C  CB  . SER   A 1 195 ? 0.392   10.513  29.325 1.00 157.14 ? 491 SER   A CB  1 
ATOM   1491 O  OG  . SER   A 1 195 ? 0.834   11.482  28.394 1.00 163.34 ? 491 SER   A OG  1 
ATOM   1492 N  N   . THR   A 1 196 ? -1.211  9.113   27.489 1.00 150.73 ? 492 THR   A N   1 
ATOM   1493 C  CA  . THR   A 1 196 ? -2.069  8.604   26.424 1.00 143.90 ? 492 THR   A CA  1 
ATOM   1494 C  C   . THR   A 1 196 ? -3.009  9.687   25.908 1.00 145.17 ? 492 THR   A C   1 
ATOM   1495 O  O   . THR   A 1 196 ? -3.666  10.375  26.695 1.00 148.26 ? 492 THR   A O   1 
ATOM   1496 C  CB  . THR   A 1 196 ? -2.883  7.395   26.914 1.00 131.78 ? 492 THR   A CB  1 
ATOM   1497 O  OG1 . THR   A 1 196 ? -2.010  6.277   27.130 1.00 127.14 ? 492 THR   A OG1 1 
ATOM   1498 C  CG2 . THR   A 1 196 ? -3.951  7.009   25.895 1.00 123.51 ? 492 THR   A CG2 1 
ATOM   1499 N  N   . LEU   A 1 197 ? -3.068  9.817   24.581 1.00 132.53 ? 493 LEU   A N   1 
ATOM   1500 C  CA  . LEU   A 1 197 ? -4.029  10.650  23.874 1.00 125.86 ? 493 LEU   A CA  1 
ATOM   1501 C  C   . LEU   A 1 197 ? -5.046  9.763   23.165 1.00 115.73 ? 493 LEU   A C   1 
ATOM   1502 O  O   . LEU   A 1 197 ? -4.723  8.662   22.710 1.00 102.96 ? 493 LEU   A O   1 
ATOM   1503 C  CB  . LEU   A 1 197 ? -3.321  11.555  22.851 1.00 129.61 ? 493 LEU   A CB  1 
ATOM   1504 C  CG  . LEU   A 1 197 ? -4.112  12.401  21.843 1.00 124.99 ? 493 LEU   A CG  1 
ATOM   1505 C  CD1 . LEU   A 1 197 ? -5.113  13.320  22.523 1.00 123.32 ? 493 LEU   A CD1 1 
ATOM   1506 C  CD2 . LEU   A 1 197 ? -3.165  13.214  20.956 1.00 129.54 ? 493 LEU   A CD2 1 
ATOM   1507 N  N   . GLY   A 1 198 ? -6.274  10.244  23.085 1.00 120.52 ? 494 GLY   A N   1 
ATOM   1508 C  CA  . GLY   A 1 198 ? -7.328  9.539   22.360 1.00 121.95 ? 494 GLY   A CA  1 
ATOM   1509 C  C   . GLY   A 1 198 ? -8.154  8.663   23.290 1.00 116.47 ? 494 GLY   A C   1 
ATOM   1510 O  O   . GLY   A 1 198 ? -8.757  9.165   24.227 1.00 125.82 ? 494 GLY   A O   1 
ATOM   1511 N  N   . ASP   A 1 199 ? -8.166  7.363   23.023 1.00 100.26 ? 495 ASP   A N   1 
ATOM   1512 C  CA  . ASP   A 1 199 ? -8.889  6.397   23.851 1.00 92.29  ? 495 ASP   A CA  1 
ATOM   1513 C  C   . ASP   A 1 199 ? -7.930  5.303   24.304 1.00 91.89  ? 495 ASP   A C   1 
ATOM   1514 O  O   . ASP   A 1 199 ? -7.541  4.450   23.480 1.00 86.35  ? 495 ASP   A O   1 
ATOM   1515 C  CB  . ASP   A 1 199 ? -10.061 5.809   23.070 1.00 84.39  ? 495 ASP   A CB  1 
ATOM   1516 C  CG  . ASP   A 1 199 ? -11.072 5.113   23.960 1.00 93.92  ? 495 ASP   A CG  1 
ATOM   1517 O  OD1 . ASP   A 1 199 ? -10.700 4.676   25.084 1.00 86.39  ? 495 ASP   A OD1 1 
ATOM   1518 O  OD2 . ASP   A 1 199 ? -12.246 5.003   23.537 1.00 90.92  ? 495 ASP   A OD2 1 
ATOM   1519 N  N   . PRO   A 1 200 ? -7.534  5.267   25.583 1.00 102.99 ? 496 PRO   A N   1 
ATOM   1520 C  CA  . PRO   A 1 200 ? -6.564  4.245   26.013 1.00 103.61 ? 496 PRO   A CA  1 
ATOM   1521 C  C   . PRO   A 1 200 ? -7.050  2.818   25.817 1.00 95.86  ? 496 PRO   A C   1 
ATOM   1522 O  O   . PRO   A 1 200 ? -6.219  1.909   25.715 1.00 98.37  ? 496 PRO   A O   1 
ATOM   1523 C  CB  . PRO   A 1 200 ? -6.342  4.571   27.500 1.00 107.41 ? 496 PRO   A CB  1 
ATOM   1524 C  CG  . PRO   A 1 200 ? -6.810  5.992   27.668 1.00 107.30 ? 496 PRO   A CG  1 
ATOM   1525 C  CD  . PRO   A 1 200 ? -7.941  6.144   26.694 1.00 99.24  ? 496 PRO   A CD  1 
ATOM   1526 N  N   . ALA   A 1 201 ? -8.367  2.593   25.756 1.00 89.76  ? 497 ALA   A N   1 
ATOM   1527 C  CA  . ALA   A 1 201 ? -8.890  1.251   25.517 1.00 92.39  ? 497 ALA   A CA  1 
ATOM   1528 C  C   . ALA   A 1 201 ? -8.266  0.616   24.283 1.00 93.76  ? 497 ALA   A C   1 
ATOM   1529 O  O   . ALA   A 1 201 ? -7.882  -0.559  24.307 1.00 95.50  ? 497 ALA   A O   1 
ATOM   1530 C  CB  . ALA   A 1 201 ? -10.412 1.296   25.363 1.00 84.82  ? 497 ALA   A CB  1 
ATOM   1531 N  N   . ASN   A 1 202 ? -8.121  1.392   23.208 1.00 100.18 ? 498 ASN   A N   1 
ATOM   1532 C  CA  . ASN   A 1 202 ? -7.842  0.883   21.872 1.00 100.95 ? 498 ASN   A CA  1 
ATOM   1533 C  C   . ASN   A 1 202 ? -6.366  0.913   21.500 1.00 105.45 ? 498 ASN   A C   1 
ATOM   1534 O  O   . ASN   A 1 202 ? -6.032  0.609   20.352 1.00 106.07 ? 498 ASN   A O   1 
ATOM   1535 C  CB  . ASN   A 1 202 ? -8.633  1.689   20.838 1.00 99.26  ? 498 ASN   A CB  1 
ATOM   1536 C  CG  . ASN   A 1 202 ? -10.092 1.839   21.209 1.00 94.74  ? 498 ASN   A CG  1 
ATOM   1537 O  OD1 . ASN   A 1 202 ? -10.726 0.886   21.653 1.00 90.00  ? 498 ASN   A OD1 1 
ATOM   1538 N  ND2 . ASN   A 1 202 ? -10.633 3.038   21.025 1.00 98.82  ? 498 ASN   A ND2 1 
ATOM   1539 N  N   . VAL   A 1 203 ? -5.478  1.274   22.434 1.00 99.87  ? 499 VAL   A N   1 
ATOM   1540 C  CA  . VAL   A 1 203 ? -4.072  1.504   22.092 1.00 95.91  ? 499 VAL   A CA  1 
ATOM   1541 C  C   . VAL   A 1 203 ? -3.453  0.296   21.400 1.00 92.62  ? 499 VAL   A C   1 
ATOM   1542 O  O   . VAL   A 1 203 ? -2.616  0.450   20.503 1.00 103.23 ? 499 VAL   A O   1 
ATOM   1543 C  CB  . VAL   A 1 203 ? -3.278  1.900   23.356 1.00 99.39  ? 499 VAL   A CB  1 
ATOM   1544 C  CG1 . VAL   A 1 203 ? -1.797  2.039   23.043 1.00 104.52 ? 499 VAL   A CG1 1 
ATOM   1545 C  CG2 . VAL   A 1 203 ? -3.809  3.203   23.919 1.00 97.54  ? 499 VAL   A CG2 1 
ATOM   1546 N  N   . GLN   A 1 204 ? -3.862  -0.921  21.771 1.00 92.92  ? 500 GLN   A N   1 
ATOM   1547 C  CA  . GLN   A 1 204 ? -3.292  -2.084  21.099 1.00 98.91  ? 500 GLN   A CA  1 
ATOM   1548 C  C   . GLN   A 1 204 ? -3.895  -2.265  19.716 1.00 95.93  ? 500 GLN   A C   1 
ATOM   1549 O  O   . GLN   A 1 204 ? -3.188  -2.638  18.774 1.00 99.07  ? 500 GLN   A O   1 
ATOM   1550 C  CB  . GLN   A 1 204 ? -3.486  -3.356  21.923 1.00 107.13 ? 500 GLN   A CB  1 
ATOM   1551 C  CG  . GLN   A 1 204 ? -2.430  -4.419  21.600 1.00 118.06 ? 500 GLN   A CG  1 
ATOM   1552 C  CD  . GLN   A 1 204 ? -2.943  -5.846  21.699 1.00 119.60 ? 500 GLN   A CD  1 
ATOM   1553 O  OE1 . GLN   A 1 204 ? -4.095  -6.087  22.061 1.00 116.82 ? 500 GLN   A OE1 1 
ATOM   1554 N  NE2 . GLN   A 1 204 ? -2.080  -6.803  21.371 1.00 124.14 ? 500 GLN   A NE2 1 
ATOM   1555 N  N   . PHE   A 1 205 ? -5.203  -2.021  19.581 1.00 94.56  ? 501 PHE   A N   1 
ATOM   1556 C  CA  . PHE   A 1 205 ? -5.833  -2.079  18.262 1.00 94.53  ? 501 PHE   A CA  1 
ATOM   1557 C  C   . PHE   A 1 205 ? -5.339  -0.945  17.367 1.00 94.89  ? 501 PHE   A C   1 
ATOM   1558 O  O   . PHE   A 1 205 ? -5.037  -1.164  16.184 1.00 99.20  ? 501 PHE   A O   1 
ATOM   1559 C  CB  . PHE   A 1 205 ? -7.360  -2.042  18.387 1.00 92.25  ? 501 PHE   A CB  1 
ATOM   1560 C  CG  . PHE   A 1 205 ? -8.066  -2.073  17.057 1.00 94.15  ? 501 PHE   A CG  1 
ATOM   1561 C  CD1 . PHE   A 1 205 ? -8.112  -3.246  16.311 1.00 97.57  ? 501 PHE   A CD1 1 
ATOM   1562 C  CD2 . PHE   A 1 205 ? -8.663  -0.929  16.536 1.00 95.95  ? 501 PHE   A CD2 1 
ATOM   1563 C  CE1 . PHE   A 1 205 ? -8.741  -3.281  15.063 1.00 97.77  ? 501 PHE   A CE1 1 
ATOM   1564 C  CE2 . PHE   A 1 205 ? -9.298  -0.958  15.291 1.00 101.21 ? 501 PHE   A CE2 1 
ATOM   1565 C  CZ  . PHE   A 1 205 ? -9.332  -2.137  14.557 1.00 96.77  ? 501 PHE   A CZ  1 
ATOM   1566 N  N   . THR   A 1 206 ? -5.266  0.279   17.905 1.00 90.34  ? 502 THR   A N   1 
ATOM   1567 C  CA  . THR   A 1 206 ? -4.728  1.394   17.128 1.00 98.99  ? 502 THR   A CA  1 
ATOM   1568 C  C   . THR   A 1 206 ? -3.337  1.066   16.596 1.00 105.86 ? 502 THR   A C   1 
ATOM   1569 O  O   . THR   A 1 206 ? -2.988  1.454   15.472 1.00 99.11  ? 502 THR   A O   1 
ATOM   1570 C  CB  . THR   A 1 206 ? -4.700  2.677   17.976 1.00 96.74  ? 502 THR   A CB  1 
ATOM   1571 O  OG1 . THR   A 1 206 ? -6.037  3.032   18.364 1.00 87.82  ? 502 THR   A OG1 1 
ATOM   1572 C  CG2 . THR   A 1 206 ? -4.075  3.843   17.196 1.00 96.62  ? 502 THR   A CG2 1 
ATOM   1573 N  N   . GLU   A 1 207 ? -2.553  0.302   17.362 1.00 108.42 ? 503 GLU   A N   1 
ATOM   1574 C  CA  . GLU   A 1 207 ? -1.212  -0.059  16.917 1.00 122.30 ? 503 GLU   A CA  1 
ATOM   1575 C  C   . GLU   A 1 207 ? -1.249  -1.140  15.845 1.00 120.33 ? 503 GLU   A C   1 
ATOM   1576 O  O   . GLU   A 1 207 ? -0.433  -1.121  14.915 1.00 121.75 ? 503 GLU   A O   1 
ATOM   1577 C  CB  . GLU   A 1 207 ? -0.362  -0.498  18.105 1.00 131.06 ? 503 GLU   A CB  1 
ATOM   1578 C  CG  . GLU   A 1 207 ? 0.507   0.618   18.639 1.00 146.81 ? 503 GLU   A CG  1 
ATOM   1579 C  CD  . GLU   A 1 207 ? 0.817   0.456   20.107 1.00 158.46 ? 503 GLU   A CD  1 
ATOM   1580 O  OE1 . GLU   A 1 207 ? 0.887   -0.702  20.572 1.00 160.67 ? 503 GLU   A OE1 1 
ATOM   1581 O  OE2 . GLU   A 1 207 ? 0.977   1.484   20.799 1.00 165.57 ? 503 GLU   A OE2 1 
ATOM   1582 N  N   . ILE   A 1 208 ? -2.180  -2.093  15.957 1.00 115.27 ? 504 ILE   A N   1 
ATOM   1583 C  CA  . ILE   A 1 208 ? -2.321  -3.120  14.922 1.00 106.46 ? 504 ILE   A CA  1 
ATOM   1584 C  C   . ILE   A 1 208 ? -2.660  -2.480  13.580 1.00 102.63 ? 504 ILE   A C   1 
ATOM   1585 O  O   . ILE   A 1 208 ? -2.067  -2.814  12.547 1.00 102.90 ? 504 ILE   A O   1 
ATOM   1586 C  CB  . ILE   A 1 208 ? -3.380  -4.160  15.327 1.00 98.16  ? 504 ILE   A CB  1 
ATOM   1587 C  CG1 . ILE   A 1 208 ? -2.820  -5.092  16.394 1.00 95.48  ? 504 ILE   A CG1 1 
ATOM   1588 C  CG2 . ILE   A 1 208 ? -3.820  -4.963  14.107 1.00 86.48  ? 504 ILE   A CG2 1 
ATOM   1589 C  CD1 . ILE   A 1 208 ? -3.888  -5.767  17.216 1.00 100.28 ? 504 ILE   A CD1 1 
ATOM   1590 N  N   . CYS   A 1 209 ? -3.627  -1.556  13.581 1.00 101.37 ? 505 CYS   A N   1 
ATOM   1591 C  CA  . CYS   A 1 209 ? -3.952  -0.793  12.380 1.00 104.82 ? 505 CYS   A CA  1 
ATOM   1592 C  C   . CYS   A 1 209 ? -2.704  -0.169  11.769 1.00 113.45 ? 505 CYS   A C   1 
ATOM   1593 O  O   . CYS   A 1 209 ? -2.506  -0.215  10.548 1.00 107.26 ? 505 CYS   A O   1 
ATOM   1594 C  CB  . CYS   A 1 209 ? -4.979  0.295   12.708 1.00 99.79  ? 505 CYS   A CB  1 
ATOM   1595 S  SG  . CYS   A 1 209 ? -6.632  -0.306  13.085 1.00 96.79  ? 505 CYS   A SG  1 
ATOM   1596 N  N   . ILE   A 1 210 ? -1.847  0.424   12.606 1.00 110.41 ? 506 ILE   A N   1 
ATOM   1597 C  CA  . ILE   A 1 210 ? -0.637  1.057   12.087 1.00 116.52 ? 506 ILE   A CA  1 
ATOM   1598 C  C   . ILE   A 1 210 ? 0.347   0.001   11.592 1.00 118.89 ? 506 ILE   A C   1 
ATOM   1599 O  O   . ILE   A 1 210 ? 1.029   0.191   10.575 1.00 116.41 ? 506 ILE   A O   1 
ATOM   1600 C  CB  . ILE   A 1 210 ? -0.014  1.977   13.153 1.00 112.81 ? 506 ILE   A CB  1 
ATOM   1601 C  CG1 . ILE   A 1 210 ? -0.957  3.131   13.473 1.00 108.75 ? 506 ILE   A CG1 1 
ATOM   1602 C  CG2 . ILE   A 1 210 ? 1.294   2.558   12.668 1.00 124.90 ? 506 ILE   A CG2 1 
ATOM   1603 C  CD1 . ILE   A 1 210 ? -0.466  3.997   14.623 1.00 119.25 ? 506 ILE   A CD1 1 
ATOM   1604 N  N   . GLN   A 1 211 ? 0.423   -1.136  12.292 1.00 127.74 ? 507 GLN   A N   1 
ATOM   1605 C  CA  . GLN   A 1 211 ? 1.289   -2.225  11.851 1.00 133.22 ? 507 GLN   A CA  1 
ATOM   1606 C  C   . GLN   A 1 211 ? 0.851   -2.788  10.501 1.00 129.94 ? 507 GLN   A C   1 
ATOM   1607 O  O   . GLN   A 1 211 ? 1.689   -3.283  9.739  1.00 129.56 ? 507 GLN   A O   1 
ATOM   1608 C  CB  . GLN   A 1 211 ? 1.324   -3.326  12.916 1.00 136.16 ? 507 GLN   A CB  1 
ATOM   1609 C  CG  . GLN   A 1 211 ? 2.246   -3.021  14.101 1.00 145.86 ? 507 GLN   A CG  1 
ATOM   1610 C  CD  . GLN   A 1 211 ? 3.608   -3.689  13.969 1.00 153.37 ? 507 GLN   A CD  1 
ATOM   1611 O  OE1 . GLN   A 1 211 ? 3.729   -4.747  13.350 1.00 153.10 ? 507 GLN   A OE1 1 
ATOM   1612 N  NE2 . GLN   A 1 211 ? 4.638   -3.073  14.550 1.00 157.69 ? 507 GLN   A NE2 1 
ATOM   1613 N  N   . GLN   A 1 212 ? -0.443  -2.716  10.182 1.00 121.21 ? 508 GLN   A N   1 
ATOM   1614 C  CA  . GLN   A 1 212 ? -0.962  -3.176  8.896  1.00 118.86 ? 508 GLN   A CA  1 
ATOM   1615 C  C   . GLN   A 1 212 ? -1.037  -2.070  7.851  1.00 116.84 ? 508 GLN   A C   1 
ATOM   1616 O  O   . GLN   A 1 212 ? -1.507  -2.323  6.737  1.00 116.84 ? 508 GLN   A O   1 
ATOM   1617 C  CB  . GLN   A 1 212 ? -2.351  -3.796  9.068  1.00 117.52 ? 508 GLN   A CB  1 
ATOM   1618 C  CG  . GLN   A 1 212 ? -2.396  -4.971  10.029 1.00 127.17 ? 508 GLN   A CG  1 
ATOM   1619 C  CD  . GLN   A 1 212 ? -2.031  -6.285  9.372  1.00 138.11 ? 508 GLN   A CD  1 
ATOM   1620 O  OE1 . GLN   A 1 212 ? -2.828  -7.220  9.359  1.00 140.66 ? 508 GLN   A OE1 1 
ATOM   1621 N  NE2 . GLN   A 1 212 ? -0.820  -6.369  8.835  1.00 142.74 ? 508 GLN   A NE2 1 
ATOM   1622 N  N   . GLY   A 1 213 ? -0.608  -0.856  8.181  1.00 113.02 ? 509 GLY   A N   1 
ATOM   1623 C  CA  . GLY   A 1 213 ? -0.515  0.214   7.207  1.00 116.46 ? 509 GLY   A CA  1 
ATOM   1624 C  C   . GLY   A 1 213 ? -1.303  1.469   7.522  1.00 115.58 ? 509 GLY   A C   1 
ATOM   1625 O  O   . GLY   A 1 213 ? -1.243  2.419   6.727  1.00 113.61 ? 509 GLY   A O   1 
ATOM   1626 N  N   . TRP   A 1 214 ? -2.043  1.535   8.628  1.00 124.41 ? 510 TRP   A N   1 
ATOM   1627 C  CA  . TRP   A 1 214 ? -2.765  2.760   8.948  1.00 127.84 ? 510 TRP   A CA  1 
ATOM   1628 C  C   . TRP   A 1 214 ? -1.793  3.909   9.148  1.00 132.59 ? 510 TRP   A C   1 
ATOM   1629 O  O   . TRP   A 1 214 ? -0.755  3.772   9.807  1.00 128.65 ? 510 TRP   A O   1 
ATOM   1630 C  CB  . TRP   A 1 214 ? -3.631  2.618   10.209 1.00 121.62 ? 510 TRP   A CB  1 
ATOM   1631 C  CG  . TRP   A 1 214 ? -4.709  3.692   10.256 1.00 116.42 ? 510 TRP   A CG  1 
ATOM   1632 C  CD1 . TRP   A 1 214 ? -5.464  4.112   9.203  1.00 110.40 ? 510 TRP   A CD1 1 
ATOM   1633 C  CD2 . TRP   A 1 214 ? -5.105  4.507   11.380 1.00 111.93 ? 510 TRP   A CD2 1 
ATOM   1634 N  NE1 . TRP   A 1 214 ? -6.321  5.107   9.596  1.00 108.14 ? 510 TRP   A NE1 1 
ATOM   1635 C  CE2 . TRP   A 1 214 ? -6.125  5.372   10.924 1.00 108.87 ? 510 TRP   A CE2 1 
ATOM   1636 C  CE3 . TRP   A 1 214 ? -4.707  4.584   12.720 1.00 118.47 ? 510 TRP   A CE3 1 
ATOM   1637 C  CZ2 . TRP   A 1 214 ? -6.748  6.303   11.752 1.00 109.56 ? 510 TRP   A CZ2 1 
ATOM   1638 C  CZ3 . TRP   A 1 214 ? -5.339  5.512   13.552 1.00 117.18 ? 510 TRP   A CZ3 1 
ATOM   1639 C  CH2 . TRP   A 1 214 ? -6.348  6.355   13.063 1.00 117.20 ? 510 TRP   A CH2 1 
ATOM   1640 N  N   . LYS   A 1 215 ? -2.138  5.042   8.563  1.00 137.30 ? 511 LYS   A N   1 
ATOM   1641 C  CA  . LYS   A 1 215 ? -1.419  6.286   8.773  1.00 144.21 ? 511 LYS   A CA  1 
ATOM   1642 C  C   . LYS   A 1 215 ? -2.271  7.140   9.704  1.00 137.96 ? 511 LYS   A C   1 
ATOM   1643 O  O   . LYS   A 1 215 ? -3.335  7.633   9.315  1.00 139.30 ? 511 LYS   A O   1 
ATOM   1644 C  CB  . LYS   A 1 215 ? -1.121  6.960   7.438  1.00 149.46 ? 511 LYS   A CB  1 
ATOM   1645 C  CG  . LYS   A 1 215 ? -0.214  6.111   6.532  1.00 157.14 ? 511 LYS   A CG  1 
ATOM   1646 C  CD  . LYS   A 1 215 ? 1.273   6.477   6.673  1.00 169.60 ? 511 LYS   A CD  1 
ATOM   1647 C  CE  . LYS   A 1 215 ? 1.891   5.988   7.986  1.00 174.58 ? 511 LYS   A CE  1 
ATOM   1648 N  NZ  . LYS   A 1 215 ? 3.060   6.808   8.429  1.00 183.89 ? 511 LYS   A NZ  1 
ATOM   1649 N  N   . ALA   A 1 216 ? -1.813  7.284   10.927 1.00 127.31 ? 512 ALA   A N   1 
ATOM   1650 C  CA  . ALA   A 1 216 ? -2.620  7.802   12.026 1.00 112.32 ? 512 ALA   A CA  1 
ATOM   1651 C  C   . ALA   A 1 216 ? -2.530  9.321   12.089 1.00 118.00 ? 512 ALA   A C   1 
ATOM   1652 O  O   . ALA   A 1 216 ? -1.421  9.868   12.132 1.00 119.17 ? 512 ALA   A O   1 
ATOM   1653 C  CB  . ALA   A 1 216 ? -2.161  7.205   13.344 1.00 108.09 ? 512 ALA   A CB  1 
ATOM   1654 N  N   . PRO   A 1 217 ? -3.668  10.035  12.096 1.00 120.02 ? 513 PRO   A N   1 
ATOM   1655 C  CA  . PRO   A 1 217 ? -3.673  11.484  12.337 1.00 129.17 ? 513 PRO   A CA  1 
ATOM   1656 C  C   . PRO   A 1 217 ? -3.535  11.845  13.814 1.00 136.85 ? 513 PRO   A C   1 
ATOM   1657 O  O   . PRO   A 1 217 ? -4.297  12.657  14.339 1.00 137.51 ? 513 PRO   A O   1 
ATOM   1658 C  CB  . PRO   A 1 217 ? -5.038  11.912  11.791 1.00 123.59 ? 513 PRO   A CB  1 
ATOM   1659 C  CG  . PRO   A 1 217 ? -5.903  10.707  11.984 1.00 120.68 ? 513 PRO   A CG  1 
ATOM   1660 C  CD  . PRO   A 1 217 ? -5.002  9.529   11.721 1.00 119.97 ? 513 PRO   A CD  1 
ATOM   1661 N  N   . ARG   A 1 218 ? -2.541  11.239  14.479 1.00 143.50 ? 514 ARG   A N   1 
ATOM   1662 C  CA  . ARG   A 1 218 ? -2.370  11.188  15.935 1.00 138.71 ? 514 ARG   A CA  1 
ATOM   1663 C  C   . ARG   A 1 218 ? -2.963  12.366  16.701 1.00 134.63 ? 514 ARG   A C   1 
ATOM   1664 O  O   . ARG   A 1 218 ? -2.228  13.221  17.210 1.00 142.80 ? 514 ARG   A O   1 
ATOM   1665 C  CB  . ARG   A 1 218 ? -0.881  11.055  16.275 1.00 143.70 ? 514 ARG   A CB  1 
ATOM   1666 C  CG  . ARG   A 1 218 ? -0.304  9.694   15.927 1.00 143.04 ? 514 ARG   A CG  1 
ATOM   1667 C  CD  . ARG   A 1 218 ? 1.192   9.618   16.177 1.00 149.35 ? 514 ARG   A CD  1 
ATOM   1668 N  NE  . ARG   A 1 218 ? 1.548   8.456   16.989 1.00 151.12 ? 514 ARG   A NE  1 
ATOM   1669 C  CZ  . ARG   A 1 218 ? 1.569   7.203   16.543 1.00 151.07 ? 514 ARG   A CZ  1 
ATOM   1670 N  NH1 . ARG   A 1 218 ? 1.905   6.213   17.356 1.00 152.87 ? 514 ARG   A NH1 1 
ATOM   1671 N  NH2 . ARG   A 1 218 ? 1.246   6.934   15.289 1.00 157.70 ? 514 ARG   A NH2 1 
ATOM   1672 N  N   . GLY   A 1 219 ? -4.296  12.409  16.788 1.00 122.68 ? 515 GLY   A N   1 
ATOM   1673 C  CA  . GLY   A 1 219 ? -4.995  13.346  17.651 1.00 124.34 ? 515 GLY   A CA  1 
ATOM   1674 C  C   . GLY   A 1 219 ? -5.879  12.644  18.668 1.00 125.77 ? 515 GLY   A C   1 
ATOM   1675 O  O   . GLY   A 1 219 ? -5.562  11.536  19.110 1.00 117.60 ? 515 GLY   A O   1 
ATOM   1676 N  N   . ARG   A 1 220 ? -7.008  13.261  19.022 1.00 140.60 ? 516 ARG   A N   1 
ATOM   1677 C  CA  . ARG   A 1 220 ? -7.911  12.737  20.044 1.00 139.88 ? 516 ARG   A CA  1 
ATOM   1678 C  C   . ARG   A 1 220 ? -9.006  11.847  19.463 1.00 139.29 ? 516 ARG   A C   1 
ATOM   1679 O  O   . ARG   A 1 220 ? -8.893  10.616  19.477 1.00 141.58 ? 516 ARG   A O   1 
ATOM   1680 C  CB  . ARG   A 1 220 ? -8.547  13.898  20.809 1.00 142.65 ? 516 ARG   A CB  1 
ATOM   1681 C  CG  . ARG   A 1 220 ? -9.419  13.484  21.969 1.00 138.40 ? 516 ARG   A CG  1 
ATOM   1682 C  CD  . ARG   A 1 220 ? -8.714  13.730  23.287 1.00 140.37 ? 516 ARG   A CD  1 
ATOM   1683 N  NE  . ARG   A 1 220 ? -9.461  14.667  24.120 1.00 141.14 ? 516 ARG   A NE  1 
ATOM   1684 C  CZ  . ARG   A 1 220 ? -9.334  14.765  25.437 1.00 141.95 ? 516 ARG   A CZ  1 
ATOM   1685 N  NH1 . ARG   A 1 220 ? -8.483  13.980  26.087 1.00 141.19 ? 516 ARG   A NH1 1 
ATOM   1686 N  NH2 . ARG   A 1 220 ? -10.064 15.646  26.107 1.00 139.80 ? 516 ARG   A NH2 1 
ATOM   1687 N  N   . PHE   A 1 221 ? -10.074 12.470  18.958 1.00 133.41 ? 517 PHE   A N   1 
ATOM   1688 C  CA  . PHE   A 1 221 ? -11.239 11.754  18.433 1.00 120.75 ? 517 PHE   A CA  1 
ATOM   1689 C  C   . PHE   A 1 221 ? -11.036 11.396  16.954 1.00 122.46 ? 517 PHE   A C   1 
ATOM   1690 O  O   . PHE   A 1 221 ? -11.762 11.834  16.056 1.00 121.28 ? 517 PHE   A O   1 
ATOM   1691 C  CB  . PHE   A 1 221 ? -12.506 12.584  18.635 1.00 115.57 ? 517 PHE   A CB  1 
ATOM   1692 C  CG  . PHE   A 1 221 ? -12.742 13.037  20.065 1.00 109.65 ? 517 PHE   A CG  1 
ATOM   1693 C  CD1 . PHE   A 1 221 ? -12.477 14.343  20.441 1.00 115.17 ? 517 PHE   A CD1 1 
ATOM   1694 C  CD2 . PHE   A 1 221 ? -13.250 12.169  21.017 1.00 97.19  ? 517 PHE   A CD2 1 
ATOM   1695 C  CE1 . PHE   A 1 221 ? -12.701 14.775  21.743 1.00 114.95 ? 517 PHE   A CE1 1 
ATOM   1696 C  CE2 . PHE   A 1 221 ? -13.483 12.603  22.324 1.00 105.00 ? 517 PHE   A CE2 1 
ATOM   1697 C  CZ  . PHE   A 1 221 ? -13.199 13.898  22.687 1.00 105.49 ? 517 PHE   A CZ  1 
ATOM   1698 N  N   . ASP   A 1 222 ? -10.017 10.575  16.711 1.00 118.20 ? 518 ASP   A N   1 
ATOM   1699 C  CA  . ASP   A 1 222 ? -9.725  10.053  15.383 1.00 106.44 ? 518 ASP   A CA  1 
ATOM   1700 C  C   . ASP   A 1 222 ? -10.476 8.740   15.192 1.00 105.48 ? 518 ASP   A C   1 
ATOM   1701 O  O   . ASP   A 1 222 ? -10.186 7.751   15.876 1.00 101.49 ? 518 ASP   A O   1 
ATOM   1702 C  CB  . ASP   A 1 222 ? -8.224  9.831   15.205 1.00 101.14 ? 518 ASP   A CB  1 
ATOM   1703 C  CG  . ASP   A 1 222 ? -7.418  11.095  15.397 1.00 113.37 ? 518 ASP   A CG  1 
ATOM   1704 O  OD1 . ASP   A 1 222 ? -8.019  12.190  15.456 1.00 121.04 ? 518 ASP   A OD1 1 
ATOM   1705 O  OD2 . ASP   A 1 222 ? -6.176  10.992  15.493 1.00 117.95 ? 518 ASP   A OD2 1 
ATOM   1706 N  N   . VAL   A 1 223 ? -11.438 8.727   14.269 1.00 103.14 ? 519 VAL   A N   1 
ATOM   1707 C  CA  . VAL   A 1 223 ? -12.204 7.510   14.023 1.00 93.39  ? 519 VAL   A CA  1 
ATOM   1708 C  C   . VAL   A 1 223 ? -11.285 6.456   13.419 1.00 88.61  ? 519 VAL   A C   1 
ATOM   1709 O  O   . VAL   A 1 223 ? -10.512 6.738   12.495 1.00 92.44  ? 519 VAL   A O   1 
ATOM   1710 C  CB  . VAL   A 1 223 ? -13.409 7.801   13.116 1.00 91.43  ? 519 VAL   A CB  1 
ATOM   1711 C  CG1 . VAL   A 1 223 ? -14.264 6.568   12.965 1.00 89.67  ? 519 VAL   A CG1 1 
ATOM   1712 C  CG2 . VAL   A 1 223 ? -14.246 8.933   13.687 1.00 91.88  ? 519 VAL   A CG2 1 
ATOM   1713 N  N   . LEU   A 1 224 ? -11.351 5.241   13.953 1.00 88.38  ? 520 LEU   A N   1 
ATOM   1714 C  CA  . LEU   A 1 224 ? -10.487 4.159   13.517 1.00 82.97  ? 520 LEU   A CA  1 
ATOM   1715 C  C   . LEU   A 1 224 ? -10.977 3.541   12.211 1.00 87.73  ? 520 LEU   A C   1 
ATOM   1716 O  O   . LEU   A 1 224 ? -12.170 3.575   11.899 1.00 84.79  ? 520 LEU   A O   1 
ATOM   1717 C  CB  . LEU   A 1 224 ? -10.408 3.081   14.589 1.00 72.84  ? 520 LEU   A CB  1 
ATOM   1718 C  CG  . LEU   A 1 224 ? -9.510  3.414   15.771 1.00 79.51  ? 520 LEU   A CG  1 
ATOM   1719 C  CD1 . LEU   A 1 224 ? -10.182 2.844   17.008 1.00 69.75  ? 520 LEU   A CD1 1 
ATOM   1720 C  CD2 . LEU   A 1 224 ? -8.104  2.839   15.575 1.00 83.30  ? 520 LEU   A CD2 1 
ATOM   1721 N  N   . PRO   A 1 225 ? -10.076 2.964   11.427 1.00 89.51  ? 521 PRO   A N   1 
ATOM   1722 C  CA  . PRO   A 1 225 ? -10.502 2.261   10.217 1.00 88.06  ? 521 PRO   A CA  1 
ATOM   1723 C  C   . PRO   A 1 225 ? -10.984 0.865   10.574 1.00 83.65  ? 521 PRO   A C   1 
ATOM   1724 O  O   . PRO   A 1 225 ? -10.677 0.330   11.642 1.00 75.42  ? 521 PRO   A O   1 
ATOM   1725 C  CB  . PRO   A 1 225 ? -9.226  2.215   9.377  1.00 93.36  ? 521 PRO   A CB  1 
ATOM   1726 C  CG  . PRO   A 1 225 ? -8.135  2.104   10.422 1.00 95.59  ? 521 PRO   A CG  1 
ATOM   1727 C  CD  . PRO   A 1 225 ? -8.610  2.936   11.599 1.00 94.38  ? 521 PRO   A CD  1 
ATOM   1728 N  N   . LEU   A 1 226 ? -11.796 0.298   9.684  1.00 74.39  ? 522 LEU   A N   1 
ATOM   1729 C  CA  . LEU   A 1 226 ? -12.200 -1.092  9.843  1.00 77.12  ? 522 LEU   A CA  1 
ATOM   1730 C  C   . LEU   A 1 226 ? -11.034 -2.021  9.533  1.00 83.29  ? 522 LEU   A C   1 
ATOM   1731 O  O   . LEU   A 1 226 ? -10.215 -1.745  8.652  1.00 87.29  ? 522 LEU   A O   1 
ATOM   1732 C  CB  . LEU   A 1 226 ? -13.386 -1.411  8.927  1.00 75.88  ? 522 LEU   A CB  1 
ATOM   1733 C  CG  . LEU   A 1 226 ? -14.697 -0.694  9.260  1.00 75.12  ? 522 LEU   A CG  1 
ATOM   1734 C  CD1 . LEU   A 1 226 ? -15.689 -0.793  8.080  1.00 69.00  ? 522 LEU   A CD1 1 
ATOM   1735 C  CD2 . LEU   A 1 226 ? -15.306 -1.205  10.587 1.00 75.09  ? 522 LEU   A CD2 1 
ATOM   1736 N  N   . LEU   A 1 227 ? -10.953 -3.123  10.273 1.00 79.56  ? 523 LEU   A N   1 
ATOM   1737 C  CA  . LEU   A 1 227 ? -10.033 -4.214  9.958  1.00 83.83  ? 523 LEU   A CA  1 
ATOM   1738 C  C   . LEU   A 1 227 ? -10.866 -5.469  9.732  1.00 80.03  ? 523 LEU   A C   1 
ATOM   1739 O  O   . LEU   A 1 227 ? -11.356 -6.069  10.695 1.00 74.31  ? 523 LEU   A O   1 
ATOM   1740 C  CB  . LEU   A 1 227 ? -9.016  -4.442  11.077 1.00 79.81  ? 523 LEU   A CB  1 
ATOM   1741 C  CG  . LEU   A 1 227 ? -7.518  -4.414  10.762 1.00 89.41  ? 523 LEU   A CG  1 
ATOM   1742 C  CD1 . LEU   A 1 227 ? -6.740  -5.171  11.846 1.00 90.67  ? 523 LEU   A CD1 1 
ATOM   1743 C  CD2 . LEU   A 1 227 ? -7.170  -4.924  9.373  1.00 97.59  ? 523 LEU   A CD2 1 
ATOM   1744 N  N   . LEU   A 1 228 ? -11.002 -5.878  8.471  1.00 75.38  ? 524 LEU   A N   1 
ATOM   1745 C  CA  . LEU   A 1 228 ? -11.956 -6.910  8.077  1.00 76.09  ? 524 LEU   A CA  1 
ATOM   1746 C  C   . LEU   A 1 228 ? -11.237 -8.140  7.534  1.00 79.58  ? 524 LEU   A C   1 
ATOM   1747 O  O   . LEU   A 1 228 ? -10.489 -8.040  6.556  1.00 85.86  ? 524 LEU   A O   1 
ATOM   1748 C  CB  . LEU   A 1 228 ? -12.922 -6.370  7.016  1.00 68.59  ? 524 LEU   A CB  1 
ATOM   1749 C  CG  . LEU   A 1 228 ? -13.579 -5.038  7.393  1.00 65.86  ? 524 LEU   A CG  1 
ATOM   1750 C  CD1 . LEU   A 1 228 ? -14.473 -4.592  6.227  1.00 65.92  ? 524 LEU   A CD1 1 
ATOM   1751 C  CD2 . LEU   A 1 228 ? -14.341 -5.093  8.749  1.00 63.97  ? 524 LEU   A CD2 1 
ATOM   1752 N  N   . GLN   A 1 229 ? -11.505 -9.298  8.143  1.00 75.61  ? 525 GLN   A N   1 
ATOM   1753 C  CA  . GLN   A 1 229 ? -11.003 -10.591 7.690  1.00 75.92  ? 525 GLN   A CA  1 
ATOM   1754 C  C   . GLN   A 1 229 ? -12.146 -11.400 7.078  1.00 72.69  ? 525 GLN   A C   1 
ATOM   1755 O  O   . GLN   A 1 229 ? -13.197 -11.577 7.705  1.00 75.78  ? 525 GLN   A O   1 
ATOM   1756 C  CB  . GLN   A 1 229 ? -10.356 -11.348 8.856  1.00 64.42  ? 525 GLN   A CB  1 
ATOM   1757 C  CG  . GLN   A 1 229 ? -10.429 -12.871 8.825  1.00 66.59  ? 525 GLN   A CG  1 
ATOM   1758 C  CD  . GLN   A 1 229 ? -10.021 -13.465 10.162 1.00 80.39  ? 525 GLN   A CD  1 
ATOM   1759 O  OE1 . GLN   A 1 229 ? -9.814  -12.734 11.138 1.00 76.37  ? 525 GLN   A OE1 1 
ATOM   1760 N  NE2 . GLN   A 1 229 ? -9.920  -14.789 10.220 1.00 84.13  ? 525 GLN   A NE2 1 
ATOM   1761 N  N   . ALA   A 1 230 ? -11.948 -11.876 5.850  1.00 62.62  ? 526 ALA   A N   1 
ATOM   1762 C  CA  . ALA   A 1 230 ? -12.975 -12.614 5.123  1.00 63.70  ? 526 ALA   A CA  1 
ATOM   1763 C  C   . ALA   A 1 230 ? -12.484 -14.018 4.798  1.00 73.22  ? 526 ALA   A C   1 
ATOM   1764 O  O   . ALA   A 1 230 ? -11.354 -14.193 4.328  1.00 71.77  ? 526 ALA   A O   1 
ATOM   1765 C  CB  . ALA   A 1 230 ? -13.371 -11.888 3.829  1.00 73.24  ? 526 ALA   A CB  1 
ATOM   1766 N  N   . ASN   A 1 231 ? -13.347 -15.008 5.030  1.00 79.05  ? 527 ASN   A N   1 
ATOM   1767 C  CA  . ASN   A 1 231 ? -13.069 -16.414 4.733  1.00 86.09  ? 527 ASN   A CA  1 
ATOM   1768 C  C   . ASN   A 1 231 ? -11.682 -16.821 5.230  1.00 90.51  ? 527 ASN   A C   1 
ATOM   1769 O  O   . ASN   A 1 231 ? -10.892 -17.454 4.521  1.00 85.64  ? 527 ASN   A O   1 
ATOM   1770 C  CB  . ASN   A 1 231 ? -13.231 -16.698 3.239  1.00 94.53  ? 527 ASN   A CB  1 
ATOM   1771 C  CG  . ASN   A 1 231 ? -13.253 -18.182 2.925  1.00 95.01  ? 527 ASN   A CG  1 
ATOM   1772 O  OD1 . ASN   A 1 231 ? -14.071 -18.928 3.461  1.00 92.60  ? 527 ASN   A OD1 1 
ATOM   1773 N  ND2 . ASN   A 1 231 ? -12.359 -18.615 2.037  1.00 98.39  ? 527 ASN   A ND2 1 
ATOM   1774 N  N   . GLY   A 1 232 ? -11.386 -16.435 6.471  1.00 88.56  ? 528 GLY   A N   1 
ATOM   1775 C  CA  . GLY   A 1 232 ? -10.135 -16.801 7.105  1.00 96.29  ? 528 GLY   A CA  1 
ATOM   1776 C  C   . GLY   A 1 232 ? -8.893  -16.132 6.559  1.00 100.28 ? 528 GLY   A C   1 
ATOM   1777 O  O   . GLY   A 1 232 ? -7.786  -16.487 6.981  1.00 109.21 ? 528 GLY   A O   1 
ATOM   1778 N  N   . ASN   A 1 233 ? -9.029  -15.175 5.644  1.00 91.40  ? 529 ASN   A N   1 
ATOM   1779 C  CA  . ASN   A 1 233 ? -7.867  -14.513 5.070  1.00 93.57  ? 529 ASN   A CA  1 
ATOM   1780 C  C   . ASN   A 1 233 ? -7.373  -13.388 5.976  1.00 94.61  ? 529 ASN   A C   1 
ATOM   1781 O  O   . ASN   A 1 233 ? -8.097  -12.883 6.836  1.00 102.33 ? 529 ASN   A O   1 
ATOM   1782 C  CB  . ASN   A 1 233 ? -8.187  -13.948 3.684  1.00 85.55  ? 529 ASN   A CB  1 
ATOM   1783 C  CG  . ASN   A 1 233 ? -8.153  -15.004 2.603  1.00 92.66  ? 529 ASN   A CG  1 
ATOM   1784 O  OD1 . ASN   A 1 233 ? -7.112  -15.241 1.992  1.00 106.14 ? 529 ASN   A OD1 1 
ATOM   1785 N  ND2 . ASN   A 1 233 ? -9.295  -15.635 2.348  1.00 81.42  ? 529 ASN   A ND2 1 
ATOM   1786 N  N   . ASP   A 1 234 ? -6.122  -12.991 5.767  1.00 103.15 ? 530 ASP   A N   1 
ATOM   1787 C  CA  . ASP   A 1 234 ? -5.556  -11.921 6.574  1.00 109.65 ? 530 ASP   A CA  1 
ATOM   1788 C  C   . ASP   A 1 234 ? -6.389  -10.646 6.402  1.00 105.14 ? 530 ASP   A C   1 
ATOM   1789 O  O   . ASP   A 1 234 ? -6.842  -10.346 5.288  1.00 104.73 ? 530 ASP   A O   1 
ATOM   1790 C  CB  . ASP   A 1 234 ? -4.088  -11.676 6.192  1.00 117.47 ? 530 ASP   A CB  1 
ATOM   1791 C  CG  . ASP   A 1 234 ? -3.218  -12.945 6.284  1.00 118.17 ? 530 ASP   A CG  1 
ATOM   1792 O  OD1 . ASP   A 1 234 ? -2.253  -13.059 5.496  1.00 125.46 ? 530 ASP   A OD1 1 
ATOM   1793 O  OD2 . ASP   A 1 234 ? -3.489  -13.831 7.123  1.00 113.19 ? 530 ASP   A OD2 1 
ATOM   1794 N  N   . PRO   A 1 235 ? -6.629  -9.889  7.472  1.00 89.31  ? 531 PRO   A N   1 
ATOM   1795 C  CA  . PRO   A 1 235 ? -7.574  -8.768  7.399  1.00 83.20  ? 531 PRO   A CA  1 
ATOM   1796 C  C   . PRO   A 1 235 ? -6.995  -7.558  6.675  1.00 90.34  ? 531 PRO   A C   1 
ATOM   1797 O  O   . PRO   A 1 235 ? -5.781  -7.387  6.564  1.00 93.80  ? 531 PRO   A O   1 
ATOM   1798 C  CB  . PRO   A 1 235 ? -7.841  -8.443  8.874  1.00 88.24  ? 531 PRO   A CB  1 
ATOM   1799 C  CG  . PRO   A 1 235 ? -6.573  -8.810  9.550  1.00 88.44  ? 531 PRO   A CG  1 
ATOM   1800 C  CD  . PRO   A 1 235 ? -6.028  -10.014 8.812  1.00 85.85  ? 531 PRO   A CD  1 
ATOM   1801 N  N   . GLU   A 1 236 ? -7.902  -6.695  6.197  1.00 89.38  ? 532 GLU   A N   1 
ATOM   1802 C  CA  . GLU   A 1 236 ? -7.551  -5.542  5.371  1.00 87.61  ? 532 GLU   A CA  1 
ATOM   1803 C  C   . GLU   A 1 236 ? -8.209  -4.270  5.901  1.00 84.20  ? 532 GLU   A C   1 
ATOM   1804 O  O   . GLU   A 1 236 ? -9.304  -4.307  6.465  1.00 87.62  ? 532 GLU   A O   1 
ATOM   1805 C  CB  . GLU   A 1 236 ? -7.969  -5.767  3.902  1.00 91.75  ? 532 GLU   A CB  1 
ATOM   1806 C  CG  . GLU   A 1 236 ? -7.304  -6.973  3.255  1.00 98.42  ? 532 GLU   A CG  1 
ATOM   1807 C  CD  . GLU   A 1 236 ? -8.031  -7.469  2.013  1.00 110.18 ? 532 GLU   A CD  1 
ATOM   1808 O  OE1 . GLU   A 1 236 ? -8.538  -6.637  1.223  1.00 106.20 ? 532 GLU   A OE1 1 
ATOM   1809 O  OE2 . GLU   A 1 236 ? -8.096  -8.705  1.836  1.00 115.13 ? 532 GLU   A OE2 1 
ATOM   1810 N  N   . LEU   A 1 237 ? -7.547  -3.133  5.681  1.00 83.73  ? 533 LEU   A N   1 
ATOM   1811 C  CA  . LEU   A 1 237 ? -7.976  -1.853  6.237  1.00 85.09  ? 533 LEU   A CA  1 
ATOM   1812 C  C   . LEU   A 1 237 ? -8.913  -1.100  5.299  1.00 87.38  ? 533 LEU   A C   1 
ATOM   1813 O  O   . LEU   A 1 237 ? -8.665  -1.019  4.095  1.00 83.66  ? 533 LEU   A O   1 
ATOM   1814 C  CB  . LEU   A 1 237 ? -6.761  -0.978  6.538  1.00 92.66  ? 533 LEU   A CB  1 
ATOM   1815 C  CG  . LEU   A 1 237 ? -5.975  -1.359  7.796  1.00 94.53  ? 533 LEU   A CG  1 
ATOM   1816 C  CD1 . LEU   A 1 237 ? -4.619  -0.680  7.778  1.00 101.10 ? 533 LEU   A CD1 1 
ATOM   1817 C  CD2 . LEU   A 1 237 ? -6.756  -1.018  9.075  1.00 89.75  ? 533 LEU   A CD2 1 
ATOM   1818 N  N   . PHE   A 1 238 ? -9.984  -0.532  5.863  1.00 86.75  ? 534 PHE   A N   1 
ATOM   1819 C  CA  . PHE   A 1 238 ? -10.901 0.317   5.105  1.00 93.32  ? 534 PHE   A CA  1 
ATOM   1820 C  C   . PHE   A 1 238 ? -11.392 1.463   5.982  1.00 90.76  ? 534 PHE   A C   1 
ATOM   1821 O  O   . PHE   A 1 238 ? -11.739 1.256   7.147  1.00 90.92  ? 534 PHE   A O   1 
ATOM   1822 C  CB  . PHE   A 1 238 ? -12.127 -0.451  4.579  1.00 83.05  ? 534 PHE   A CB  1 
ATOM   1823 C  CG  . PHE   A 1 238 ? -11.804 -1.741  3.904  1.00 82.84  ? 534 PHE   A CG  1 
ATOM   1824 C  CD1 . PHE   A 1 238 ? -11.527 -2.882  4.645  1.00 81.10  ? 534 PHE   A CD1 1 
ATOM   1825 C  CD2 . PHE   A 1 238 ? -11.818 -1.833  2.512  1.00 79.86  ? 534 PHE   A CD2 1 
ATOM   1826 C  CE1 . PHE   A 1 238 ? -11.239 -4.082  4.007  1.00 84.91  ? 534 PHE   A CE1 1 
ATOM   1827 C  CE2 . PHE   A 1 238 ? -11.535 -3.023  1.886  1.00 78.99  ? 534 PHE   A CE2 1 
ATOM   1828 C  CZ  . PHE   A 1 238 ? -11.247 -4.146  2.618  1.00 78.80  ? 534 PHE   A CZ  1 
ATOM   1829 N  N   . GLN   A 1 239 ? -11.466 2.660   5.394  1.00 101.66 ? 535 GLN   A N   1 
ATOM   1830 C  CA  . GLN   A 1 239 ? -11.913 3.867   6.085  1.00 99.84  ? 535 GLN   A CA  1 
ATOM   1831 C  C   . GLN   A 1 239 ? -13.391 4.121   5.806  1.00 94.35  ? 535 GLN   A C   1 
ATOM   1832 O  O   . GLN   A 1 239 ? -13.786 4.295   4.650  1.00 91.36  ? 535 GLN   A O   1 
ATOM   1833 C  CB  . GLN   A 1 239 ? -11.103 5.083   5.640  1.00 107.96 ? 535 GLN   A CB  1 
ATOM   1834 C  CG  . GLN   A 1 239 ? -11.644 6.379   6.213  1.00 114.85 ? 535 GLN   A CG  1 
ATOM   1835 C  CD  . GLN   A 1 239 ? -11.326 7.589   5.361  1.00 121.23 ? 535 GLN   A CD  1 
ATOM   1836 O  OE1 . GLN   A 1 239 ? -12.228 8.303   4.922  1.00 121.93 ? 535 GLN   A OE1 1 
ATOM   1837 N  NE2 . GLN   A 1 239 ? -10.041 7.835   5.131  1.00 127.04 ? 535 GLN   A NE2 1 
ATOM   1838 N  N   . ILE   A 1 240 ? -14.196 4.164   6.862  1.00 84.08  ? 536 ILE   A N   1 
ATOM   1839 C  CA  . ILE   A 1 240 ? -15.608 4.528   6.741  1.00 85.58  ? 536 ILE   A CA  1 
ATOM   1840 C  C   . ILE   A 1 240 ? -15.691 5.957   6.221  1.00 89.72  ? 536 ILE   A C   1 
ATOM   1841 O  O   . ILE   A 1 240 ? -15.122 6.869   6.845  1.00 84.82  ? 536 ILE   A O   1 
ATOM   1842 C  CB  . ILE   A 1 240 ? -16.361 4.414   8.081  1.00 82.40  ? 536 ILE   A CB  1 
ATOM   1843 C  CG1 . ILE   A 1 240 ? -16.152 3.047   8.748  1.00 88.04  ? 536 ILE   A CG1 1 
ATOM   1844 C  CG2 . ILE   A 1 240 ? -17.849 4.693   7.858  1.00 79.62  ? 536 ILE   A CG2 1 
ATOM   1845 C  CD1 . ILE   A 1 240 ? -15.036 3.002   9.794  1.00 88.81  ? 536 ILE   A CD1 1 
ATOM   1846 N  N   . PRO   A 1 241 ? -16.373 6.198   5.098  1.00 95.25  ? 537 PRO   A N   1 
ATOM   1847 C  CA  . PRO   A 1 241 ? -16.567 7.575   4.617  1.00 99.14  ? 537 PRO   A CA  1 
ATOM   1848 C  C   . PRO   A 1 241 ? -16.998 8.482   5.754  1.00 98.68  ? 537 PRO   A C   1 
ATOM   1849 O  O   . PRO   A 1 241 ? -18.006 8.212   6.425  1.00 97.77  ? 537 PRO   A O   1 
ATOM   1850 C  CB  . PRO   A 1 241 ? -17.680 7.433   3.570  1.00 97.18  ? 537 PRO   A CB  1 
ATOM   1851 C  CG  . PRO   A 1 241 ? -17.610 6.007   3.134  1.00 96.03  ? 537 PRO   A CG  1 
ATOM   1852 C  CD  . PRO   A 1 241 ? -17.173 5.224   4.337  1.00 90.56  ? 537 PRO   A CD  1 
ATOM   1853 N  N   . PRO   A 1 242 ? -16.248 9.550   6.023  1.00 101.36 ? 538 PRO   A N   1 
ATOM   1854 C  CA  . PRO   A 1 242 ? -16.533 10.361  7.220  1.00 100.37 ? 538 PRO   A CA  1 
ATOM   1855 C  C   . PRO   A 1 242 ? -17.923 10.980  7.217  1.00 105.68 ? 538 PRO   A C   1 
ATOM   1856 O  O   . PRO   A 1 242 ? -18.451 11.290  8.293  1.00 111.46 ? 538 PRO   A O   1 
ATOM   1857 C  CB  . PRO   A 1 242 ? -15.435 11.431  7.192  1.00 102.89 ? 538 PRO   A CB  1 
ATOM   1858 C  CG  . PRO   A 1 242 ? -14.389 10.909  6.247  1.00 105.52 ? 538 PRO   A CG  1 
ATOM   1859 C  CD  . PRO   A 1 242 ? -15.117 10.077  5.246  1.00 99.88  ? 538 PRO   A CD  1 
ATOM   1860 N  N   . GLU   A 1 243 ? -18.542 11.154  6.044  1.00 100.61 ? 539 GLU   A N   1 
ATOM   1861 C  CA  . GLU   A 1 243 ? -19.926 11.614  5.991  1.00 97.94  ? 539 GLU   A CA  1 
ATOM   1862 C  C   . GLU   A 1 243 ? -20.904 10.586  6.567  1.00 96.59  ? 539 GLU   A C   1 
ATOM   1863 O  O   . GLU   A 1 243 ? -22.041 10.945  6.894  1.00 95.39  ? 539 GLU   A O   1 
ATOM   1864 C  CB  . GLU   A 1 243 ? -20.313 11.983  4.542  1.00 106.39 ? 539 GLU   A CB  1 
ATOM   1865 C  CG  . GLU   A 1 243 ? -20.332 10.832  3.520  1.00 100.34 ? 539 GLU   A CG  1 
ATOM   1866 C  CD  . GLU   A 1 243 ? -19.028 10.696  2.736  1.00 105.50 ? 539 GLU   A CD  1 
ATOM   1867 O  OE1 . GLU   A 1 243 ? -17.949 10.828  3.354  1.00 105.06 ? 539 GLU   A OE1 1 
ATOM   1868 O  OE2 . GLU   A 1 243 ? -19.084 10.463  1.500  1.00 98.37  ? 539 GLU   A OE2 1 
ATOM   1869 N  N   . LEU   A 1 244 ? -20.502 9.319   6.686  1.00 87.54  ? 540 LEU   A N   1 
ATOM   1870 C  CA  . LEU   A 1 244 ? -21.342 8.300   7.296  1.00 84.69  ? 540 LEU   A CA  1 
ATOM   1871 C  C   . LEU   A 1 244 ? -21.160 8.208   8.797  1.00 79.15  ? 540 LEU   A C   1 
ATOM   1872 O  O   . LEU   A 1 244 ? -21.907 7.461   9.454  1.00 74.60  ? 540 LEU   A O   1 
ATOM   1873 C  CB  . LEU   A 1 244 ? -21.048 6.924   6.695  1.00 88.70  ? 540 LEU   A CB  1 
ATOM   1874 C  CG  . LEU   A 1 244 ? -21.386 6.720   5.219  1.00 89.82  ? 540 LEU   A CG  1 
ATOM   1875 C  CD1 . LEU   A 1 244 ? -20.817 5.394   4.760  1.00 84.39  ? 540 LEU   A CD1 1 
ATOM   1876 C  CD2 . LEU   A 1 244 ? -22.886 6.760   5.022  1.00 93.77  ? 540 LEU   A CD2 1 
ATOM   1877 N  N   . VAL   A 1 245 ? -20.184 8.921   9.356  1.00 83.78  ? 541 VAL   A N   1 
ATOM   1878 C  CA  . VAL   A 1 245 ? -19.892 8.858   10.793 1.00 86.51  ? 541 VAL   A CA  1 
ATOM   1879 C  C   . VAL   A 1 245 ? -20.474 10.112  11.433 1.00 87.07  ? 541 VAL   A C   1 
ATOM   1880 O  O   . VAL   A 1 245 ? -19.866 11.181  11.393 1.00 91.01  ? 541 VAL   A O   1 
ATOM   1881 C  CB  . VAL   A 1 245 ? -18.394 8.734   11.071 1.00 87.10  ? 541 VAL   A CB  1 
ATOM   1882 C  CG1 . VAL   A 1 245 ? -18.154 8.653   12.562 1.00 83.74  ? 541 VAL   A CG1 1 
ATOM   1883 C  CG2 . VAL   A 1 245 ? -17.836 7.499   10.386 1.00 84.74  ? 541 VAL   A CG2 1 
ATOM   1884 N  N   . LEU   A 1 246 ? -21.655 9.975   12.032 1.00 83.49  ? 542 LEU   A N   1 
ATOM   1885 C  CA  . LEU   A 1 246 ? -22.331 11.074  12.706 1.00 83.93  ? 542 LEU   A CA  1 
ATOM   1886 C  C   . LEU   A 1 246 ? -21.772 11.272  14.108 1.00 86.26  ? 542 LEU   A C   1 
ATOM   1887 O  O   . LEU   A 1 246 ? -21.574 10.319  14.864 1.00 79.63  ? 542 LEU   A O   1 
ATOM   1888 C  CB  . LEU   A 1 246 ? -23.838 10.822  12.779 1.00 90.92  ? 542 LEU   A CB  1 
ATOM   1889 C  CG  . LEU   A 1 246 ? -24.704 11.784  13.599 1.00 97.59  ? 542 LEU   A CG  1 
ATOM   1890 C  CD1 . LEU   A 1 246 ? -24.815 13.159  12.939 1.00 102.68 ? 542 LEU   A CD1 1 
ATOM   1891 C  CD2 . LEU   A 1 246 ? -26.081 11.172  13.835 1.00 100.47 ? 542 LEU   A CD2 1 
ATOM   1892 N  N   . GLU   A 1 247 ? -21.512 12.520  14.446 1.00 93.52  ? 543 GLU   A N   1 
ATOM   1893 C  CA  . GLU   A 1 247 ? -20.903 12.833  15.723 1.00 93.56  ? 543 GLU   A CA  1 
ATOM   1894 C  C   . GLU   A 1 247 ? -21.646 14.000  16.354 1.00 99.07  ? 543 GLU   A C   1 
ATOM   1895 O  O   . GLU   A 1 247 ? -22.167 14.876  15.653 1.00 101.45 ? 543 GLU   A O   1 
ATOM   1896 C  CB  . GLU   A 1 247 ? -19.414 13.137  15.543 1.00 99.80  ? 543 GLU   A CB  1 
ATOM   1897 C  CG  . GLU   A 1 247 ? -18.597 11.918  15.130 1.00 97.63  ? 543 GLU   A CG  1 
ATOM   1898 C  CD  . GLU   A 1 247 ? -17.130 12.247  14.992 1.00 109.91 ? 543 GLU   A CD  1 
ATOM   1899 O  OE1 . GLU   A 1 247 ? -16.615 13.002  15.832 1.00 111.15 ? 543 GLU   A OE1 1 
ATOM   1900 O  OE2 . GLU   A 1 247 ? -16.496 11.787  14.021 1.00 118.10 ? 543 GLU   A OE2 1 
ATOM   1901 N  N   . VAL   A 1 248 ? -21.700 13.991  17.686 1.00 88.60  ? 544 VAL   A N   1 
ATOM   1902 C  CA  . VAL   A 1 248 ? -22.439 14.975  18.463 1.00 95.84  ? 544 VAL   A CA  1 
ATOM   1903 C  C   . VAL   A 1 248 ? -21.439 15.773  19.293 1.00 100.40 ? 544 VAL   A C   1 
ATOM   1904 O  O   . VAL   A 1 248 ? -20.691 15.190  20.081 1.00 97.44  ? 544 VAL   A O   1 
ATOM   1905 C  CB  . VAL   A 1 248 ? -23.489 14.325  19.384 1.00 94.31  ? 544 VAL   A CB  1 
ATOM   1906 C  CG1 . VAL   A 1 248 ? -24.176 15.399  20.244 1.00 97.09  ? 544 VAL   A CG1 1 
ATOM   1907 C  CG2 . VAL   A 1 248 ? -24.514 13.538  18.588 1.00 93.21  ? 544 VAL   A CG2 1 
ATOM   1908 N  N   . PRO   A 1 249 ? -21.397 17.098  19.154 1.00 105.12 ? 545 PRO   A N   1 
ATOM   1909 C  CA  . PRO   A 1 249 ? -20.517 17.912  19.996 1.00 107.82 ? 545 PRO   A CA  1 
ATOM   1910 C  C   . PRO   A 1 249 ? -21.192 18.197  21.326 1.00 110.51 ? 545 PRO   A C   1 
ATOM   1911 O  O   . PRO   A 1 249 ? -22.382 18.517  21.383 1.00 113.86 ? 545 PRO   A O   1 
ATOM   1912 C  CB  . PRO   A 1 249 ? -20.330 19.200  19.176 1.00 113.36 ? 545 PRO   A CB  1 
ATOM   1913 C  CG  . PRO   A 1 249 ? -21.247 19.080  17.982 1.00 113.54 ? 545 PRO   A CG  1 
ATOM   1914 C  CD  . PRO   A 1 249 ? -22.151 17.922  18.191 1.00 113.98 ? 545 PRO   A CD  1 
ATOM   1915 N  N   . ILE   A 1 250 ? -20.425 18.058  22.404 1.00 116.45 ? 546 ILE   A N   1 
ATOM   1916 C  CA  . ILE   A 1 250 ? -20.971 18.037  23.753 1.00 110.52 ? 546 ILE   A CA  1 
ATOM   1917 C  C   . ILE   A 1 250 ? -20.900 19.445  24.335 1.00 114.38 ? 546 ILE   A C   1 
ATOM   1918 O  O   . ILE   A 1 250 ? -19.814 19.947  24.645 1.00 124.82 ? 546 ILE   A O   1 
ATOM   1919 C  CB  . ILE   A 1 250 ? -20.224 17.035  24.642 1.00 108.98 ? 546 ILE   A CB  1 
ATOM   1920 C  CG1 . ILE   A 1 250 ? -20.068 15.696  23.912 1.00 97.92  ? 546 ILE   A CG1 1 
ATOM   1921 C  CG2 . ILE   A 1 250 ? -20.941 16.875  25.978 1.00 95.79  ? 546 ILE   A CG2 1 
ATOM   1922 C  CD1 . ILE   A 1 250 ? -21.370 15.035  23.584 1.00 94.66  ? 546 ILE   A CD1 1 
ATOM   1923 N  N   . ARG   A 1 251 ? -22.063 20.066  24.524 1.00 114.29 ? 547 ARG   A N   1 
ATOM   1924 C  CA  . ARG   A 1 251 ? -22.175 21.353  25.200 1.00 123.41 ? 547 ARG   A CA  1 
ATOM   1925 C  C   . ARG   A 1 251 ? -23.072 21.220  26.424 1.00 120.99 ? 547 ARG   A C   1 
ATOM   1926 O  O   . ARG   A 1 251 ? -23.940 20.342  26.493 1.00 110.81 ? 547 ARG   A O   1 
ATOM   1927 C  CB  . ARG   A 1 251 ? -22.730 22.443  24.260 1.00 131.90 ? 547 ARG   A CB  1 
ATOM   1928 C  CG  . ARG   A 1 251 ? -24.169 22.230  23.773 1.00 129.47 ? 547 ARG   A CG  1 
ATOM   1929 C  CD  . ARG   A 1 251 ? -24.227 21.349  22.515 1.00 127.84 ? 547 ARG   A CD  1 
ATOM   1930 N  NE  . ARG   A 1 251 ? -25.504 21.441  21.809 1.00 123.65 ? 547 ARG   A NE  1 
ATOM   1931 C  CZ  . ARG   A 1 251 ? -25.826 20.685  20.764 1.00 124.86 ? 547 ARG   A CZ  1 
ATOM   1932 N  NH1 . ARG   A 1 251 ? -26.997 20.838  20.162 1.00 125.78 ? 547 ARG   A NH1 1 
ATOM   1933 N  NH2 . ARG   A 1 251 ? -24.965 19.781  20.321 1.00 117.03 ? 547 ARG   A NH2 1 
ATOM   1934 N  N   . HIS   A 1 252 ? -22.840 22.123  27.437 1.00 127.71 ? 548 HIS   A N   1 
ATOM   1935 C  CA  . HIS   A 1 252 ? -23.763 22.142  28.562 1.00 123.93 ? 548 HIS   A CA  1 
ATOM   1936 C  C   . HIS   A 1 252 ? -24.811 23.233  28.377 1.00 125.94 ? 548 HIS   A C   1 
ATOM   1937 O  O   . HIS   A 1 252 ? -24.542 24.265  27.753 1.00 127.49 ? 548 HIS   A O   1 
ATOM   1938 C  CB  . HIS   A 1 252 ? -23.019 22.374  29.876 1.00 122.78 ? 548 HIS   A CB  1 
ATOM   1939 C  CG  . HIS   A 1 252 ? -23.723 21.805  31.068 1.00 136.73 ? 548 HIS   A CG  1 
ATOM   1940 N  ND1 . HIS   A 1 252 ? -24.721 22.478  31.742 1.00 140.71 ? 548 HIS   A ND1 1 
ATOM   1941 C  CD2 . HIS   A 1 252 ? -23.580 20.615  31.700 1.00 131.47 ? 548 HIS   A CD2 1 
ATOM   1942 C  CE1 . HIS   A 1 252 ? -25.162 21.727  32.736 1.00 134.08 ? 548 HIS   A CE1 1 
ATOM   1943 N  NE2 . HIS   A 1 252 ? -24.485 20.593  32.732 1.00 129.93 ? 548 HIS   A NE2 1 
ATOM   1944 N  N   . PRO   A 1 253 ? -26.024 23.024  28.891 1.00 130.11 ? 549 PRO   A N   1 
ATOM   1945 C  CA  . PRO   A 1 253 ? -27.049 24.074  28.862 1.00 138.12 ? 549 PRO   A CA  1 
ATOM   1946 C  C   . PRO   A 1 253 ? -26.872 25.166  29.908 1.00 150.43 ? 549 PRO   A C   1 
ATOM   1947 O  O   . PRO   A 1 253 ? -27.791 25.970  30.087 1.00 156.33 ? 549 PRO   A O   1 
ATOM   1948 C  CB  . PRO   A 1 253 ? -28.348 23.282  29.114 1.00 133.67 ? 549 PRO   A CB  1 
ATOM   1949 C  CG  . PRO   A 1 253 ? -27.927 22.073  29.866 1.00 121.56 ? 549 PRO   A CG  1 
ATOM   1950 C  CD  . PRO   A 1 253 ? -26.572 21.724  29.326 1.00 122.20 ? 549 PRO   A CD  1 
ATOM   1951 N  N   . LYS   A 1 254 ? -25.730 25.215  30.607 1.00 148.67 ? 550 LYS   A N   1 
ATOM   1952 C  CA  . LYS   A 1 254 ? -25.445 26.279  31.564 1.00 151.60 ? 550 LYS   A CA  1 
ATOM   1953 C  C   . LYS   A 1 254 ? -24.021 26.799  31.412 1.00 148.93 ? 550 LYS   A C   1 
ATOM   1954 O  O   . LYS   A 1 254 ? -23.789 28.012  31.423 1.00 157.05 ? 550 LYS   A O   1 
ATOM   1955 C  CB  . LYS   A 1 254 ? -25.646 25.795  33.001 1.00 151.97 ? 550 LYS   A CB  1 
ATOM   1956 C  CG  . LYS   A 1 254 ? -26.949 25.071  33.280 1.00 152.25 ? 550 LYS   A CG  1 
ATOM   1957 C  CD  . LYS   A 1 254 ? -28.139 26.012  33.257 1.00 161.97 ? 550 LYS   A CD  1 
ATOM   1958 C  CE  . LYS   A 1 254 ? -29.410 25.283  33.668 1.00 161.38 ? 550 LYS   A CE  1 
ATOM   1959 N  NZ  . LYS   A 1 254 ? -30.629 26.117  33.470 1.00 166.11 ? 550 LYS   A NZ  1 
ATOM   1960 N  N   . PHE   A 1 255 ? -23.071 25.888  31.250 1.00 138.12 ? 551 PHE   A N   1 
ATOM   1961 C  CA  . PHE   A 1 255 ? -21.648 26.180  31.398 1.00 145.90 ? 551 PHE   A CA  1 
ATOM   1962 C  C   . PHE   A 1 255 ? -20.995 26.317  30.023 1.00 150.13 ? 551 PHE   A C   1 
ATOM   1963 O  O   . PHE   A 1 255 ? -20.725 25.321  29.351 1.00 146.69 ? 551 PHE   A O   1 
ATOM   1964 C  CB  . PHE   A 1 255 ? -20.997 25.080  32.227 1.00 147.55 ? 551 PHE   A CB  1 
ATOM   1965 C  CG  . PHE   A 1 255 ? -21.663 24.849  33.573 1.00 151.98 ? 551 PHE   A CG  1 
ATOM   1966 C  CD1 . PHE   A 1 255 ? -22.494 23.754  33.779 1.00 147.83 ? 551 PHE   A CD1 1 
ATOM   1967 C  CD2 . PHE   A 1 255 ? -21.454 25.724  34.627 1.00 153.59 ? 551 PHE   A CD2 1 
ATOM   1968 C  CE1 . PHE   A 1 255 ? -23.103 23.536  35.016 1.00 140.66 ? 551 PHE   A CE1 1 
ATOM   1969 C  CE2 . PHE   A 1 255 ? -22.061 25.512  35.866 1.00 152.28 ? 551 PHE   A CE2 1 
ATOM   1970 C  CZ  . PHE   A 1 255 ? -22.885 24.419  36.057 1.00 145.61 ? 551 PHE   A CZ  1 
ATOM   1971 N  N   . ASP   A 1 256 ? -20.719 27.553  29.611 1.00 159.42 ? 552 ASP   A N   1 
ATOM   1972 C  CA  . ASP   A 1 256 ? -20.127 27.770  28.297 1.00 162.71 ? 552 ASP   A CA  1 
ATOM   1973 C  C   . ASP   A 1 256 ? -18.634 27.488  28.254 1.00 157.50 ? 552 ASP   A C   1 
ATOM   1974 O  O   . ASP   A 1 256 ? -18.059 27.472  27.163 1.00 159.79 ? 552 ASP   A O   1 
ATOM   1975 C  CB  . ASP   A 1 256 ? -20.395 29.194  27.822 1.00 179.28 ? 552 ASP   A CB  1 
ATOM   1976 C  CG  . ASP   A 1 256 ? -21.755 29.334  27.185 1.00 185.91 ? 552 ASP   A CG  1 
ATOM   1977 O  OD1 . ASP   A 1 256 ? -22.715 29.660  27.915 1.00 186.34 ? 552 ASP   A OD1 1 
ATOM   1978 O  OD2 . ASP   A 1 256 ? -21.866 29.088  25.961 1.00 184.92 ? 552 ASP   A OD2 1 
ATOM   1979 N  N   . TRP   A 1 257 ? -17.987 27.265  29.395 1.00 153.92 ? 553 TRP   A N   1 
ATOM   1980 C  CA  . TRP   A 1 257 ? -16.641 26.717  29.329 1.00 151.62 ? 553 TRP   A CA  1 
ATOM   1981 C  C   . TRP   A 1 257 ? -16.646 25.273  28.861 1.00 143.12 ? 553 TRP   A C   1 
ATOM   1982 O  O   . TRP   A 1 257 ? -15.572 24.717  28.602 1.00 138.86 ? 553 TRP   A O   1 
ATOM   1983 C  CB  . TRP   A 1 257 ? -15.964 26.822  30.690 1.00 153.45 ? 553 TRP   A CB  1 
ATOM   1984 C  CG  . TRP   A 1 257 ? -16.820 26.321  31.803 1.00 154.22 ? 553 TRP   A CG  1 
ATOM   1985 C  CD1 . TRP   A 1 257 ? -17.684 27.053  32.563 1.00 159.96 ? 553 TRP   A CD1 1 
ATOM   1986 C  CD2 . TRP   A 1 257 ? -16.906 24.974  32.284 1.00 147.57 ? 553 TRP   A CD2 1 
ATOM   1987 N  NE1 . TRP   A 1 257 ? -18.299 26.248  33.494 1.00 153.83 ? 553 TRP   A NE1 1 
ATOM   1988 C  CE2 . TRP   A 1 257 ? -17.839 24.966  33.341 1.00 147.78 ? 553 TRP   A CE2 1 
ATOM   1989 C  CE3 . TRP   A 1 257 ? -16.286 23.775  31.925 1.00 141.92 ? 553 TRP   A CE3 1 
ATOM   1990 C  CZ2 . TRP   A 1 257 ? -18.164 23.807  34.039 1.00 138.95 ? 553 TRP   A CZ2 1 
ATOM   1991 C  CZ3 . TRP   A 1 257 ? -16.609 22.628  32.619 1.00 134.73 ? 553 TRP   A CZ3 1 
ATOM   1992 C  CH2 . TRP   A 1 257 ? -17.538 22.652  33.664 1.00 134.18 ? 553 TRP   A CH2 1 
ATOM   1993 N  N   . PHE   A 1 258 ? -17.832 24.668  28.752 1.00 143.66 ? 554 PHE   A N   1 
ATOM   1994 C  CA  . PHE   A 1 258 ? -17.944 23.272  28.339 1.00 143.19 ? 554 PHE   A CA  1 
ATOM   1995 C  C   . PHE   A 1 258 ? -17.462 23.081  26.910 1.00 139.68 ? 554 PHE   A C   1 
ATOM   1996 O  O   . PHE   A 1 258 ? -16.739 22.125  26.613 1.00 138.98 ? 554 PHE   A O   1 
ATOM   1997 C  CB  . PHE   A 1 258 ? -19.391 22.803  28.475 1.00 143.93 ? 554 PHE   A CB  1 
ATOM   1998 C  CG  . PHE   A 1 258 ? -19.523 21.441  29.051 1.00 135.98 ? 554 PHE   A CG  1 
ATOM   1999 C  CD1 . PHE   A 1 258 ? -19.664 21.266  30.411 1.00 134.50 ? 554 PHE   A CD1 1 
ATOM   2000 C  CD2 . PHE   A 1 258 ? -19.494 20.325  28.233 1.00 135.27 ? 554 PHE   A CD2 1 
ATOM   2001 C  CE1 . PHE   A 1 258 ? -19.779 20.001  30.953 1.00 124.55 ? 554 PHE   A CE1 1 
ATOM   2002 C  CE2 . PHE   A 1 258 ? -19.610 19.056  28.762 1.00 132.01 ? 554 PHE   A CE2 1 
ATOM   2003 C  CZ  . PHE   A 1 258 ? -19.751 18.893  30.131 1.00 124.03 ? 554 PHE   A CZ  1 
ATOM   2004 N  N   . LYS   A 1 259 ? -17.869 23.971  26.004 1.00 137.08 ? 555 LYS   A N   1 
ATOM   2005 C  CA  . LYS   A 1 259 ? -17.395 23.874  24.627 1.00 145.91 ? 555 LYS   A CA  1 
ATOM   2006 C  C   . LYS   A 1 259 ? -15.874 23.897  24.579 1.00 148.95 ? 555 LYS   A C   1 
ATOM   2007 O  O   . LYS   A 1 259 ? -15.258 23.174  23.785 1.00 140.43 ? 555 LYS   A O   1 
ATOM   2008 C  CB  . LYS   A 1 259 ? -17.974 25.010  23.780 1.00 153.41 ? 555 LYS   A CB  1 
ATOM   2009 C  CG  . LYS   A 1 259 ? -19.296 25.555  24.295 1.00 158.75 ? 555 LYS   A CG  1 
ATOM   2010 C  CD  . LYS   A 1 259 ? -19.991 26.416  23.254 1.00 165.17 ? 555 LYS   A CD  1 
ATOM   2011 C  CE  . LYS   A 1 259 ? -21.338 26.876  23.774 1.00 167.48 ? 555 LYS   A CE  1 
ATOM   2012 N  NZ  . LYS   A 1 259 ? -21.919 25.859  24.697 1.00 159.10 ? 555 LYS   A NZ  1 
ATOM   2013 N  N   . ASP   A 1 260 ? -15.253 24.709  25.442 1.00 156.72 ? 556 ASP   A N   1 
ATOM   2014 C  CA  . ASP   A 1 260 ? -13.796 24.784  25.495 1.00 163.82 ? 556 ASP   A CA  1 
ATOM   2015 C  C   . ASP   A 1 260 ? -13.189 23.422  25.807 1.00 153.66 ? 556 ASP   A C   1 
ATOM   2016 O  O   . ASP   A 1 260 ? -12.099 23.097  25.321 1.00 149.84 ? 556 ASP   A O   1 
ATOM   2017 C  CB  . ASP   A 1 260 ? -13.356 25.827  26.531 1.00 175.29 ? 556 ASP   A CB  1 
ATOM   2018 C  CG  . ASP   A 1 260 ? -13.553 27.263  26.051 1.00 184.38 ? 556 ASP   A CG  1 
ATOM   2019 O  OD1 . ASP   A 1 260 ? -13.211 27.557  24.887 1.00 187.37 ? 556 ASP   A OD1 1 
ATOM   2020 O  OD2 . ASP   A 1 260 ? -14.045 28.100  26.840 1.00 189.41 ? 556 ASP   A OD2 1 
ATOM   2021 N  N   . LEU   A 1 261 ? -13.888 22.608  26.608 1.00 146.93 ? 557 LEU   A N   1 
ATOM   2022 C  CA  . LEU   A 1 261 ? -13.443 21.238  26.849 1.00 144.93 ? 557 LEU   A CA  1 
ATOM   2023 C  C   . LEU   A 1 261 ? -13.247 20.482  25.541 1.00 153.45 ? 557 LEU   A C   1 
ATOM   2024 O  O   . LEU   A 1 261 ? -12.348 19.641  25.435 1.00 153.56 ? 557 LEU   A O   1 
ATOM   2025 C  CB  . LEU   A 1 261 ? -14.448 20.499  27.741 1.00 132.83 ? 557 LEU   A CB  1 
ATOM   2026 C  CG  . LEU   A 1 261 ? -14.548 20.842  29.234 1.00 132.99 ? 557 LEU   A CG  1 
ATOM   2027 C  CD1 . LEU   A 1 261 ? -15.742 20.148  29.910 1.00 119.37 ? 557 LEU   A CD1 1 
ATOM   2028 C  CD2 . LEU   A 1 261 ? -13.256 20.483  29.958 1.00 136.18 ? 557 LEU   A CD2 1 
ATOM   2029 N  N   . GLY   A 1 262 ? -14.068 20.773  24.535 1.00 160.09 ? 558 GLY   A N   1 
ATOM   2030 C  CA  . GLY   A 1 262 ? -13.878 20.204  23.217 1.00 161.06 ? 558 GLY   A CA  1 
ATOM   2031 C  C   . GLY   A 1 262 ? -14.094 18.709  23.174 1.00 152.22 ? 558 GLY   A C   1 
ATOM   2032 O  O   . GLY   A 1 262 ? -13.201 17.956  22.775 1.00 155.14 ? 558 GLY   A O   1 
ATOM   2033 N  N   . LEU   A 1 263 ? -15.275 18.267  23.593 1.00 140.24 ? 559 LEU   A N   1 
ATOM   2034 C  CA  . LEU   A 1 263 ? -15.612 16.855  23.634 1.00 117.24 ? 559 LEU   A CA  1 
ATOM   2035 C  C   . LEU   A 1 263 ? -16.721 16.561  22.637 1.00 112.96 ? 559 LEU   A C   1 
ATOM   2036 O  O   . LEU   A 1 263 ? -17.569 17.417  22.359 1.00 107.57 ? 559 LEU   A O   1 
ATOM   2037 C  CB  . LEU   A 1 263 ? -16.038 16.426  25.044 1.00 110.08 ? 559 LEU   A CB  1 
ATOM   2038 C  CG  . LEU   A 1 263 ? -14.973 16.635  26.122 1.00 106.25 ? 559 LEU   A CG  1 
ATOM   2039 C  CD1 . LEU   A 1 263 ? -15.604 16.430  27.482 1.00 101.22 ? 559 LEU   A CD1 1 
ATOM   2040 C  CD2 . LEU   A 1 263 ? -13.779 15.704  25.905 1.00 99.06  ? 559 LEU   A CD2 1 
ATOM   2041 N  N   . LYS   A 1 264 ? -16.685 15.349  22.091 1.00 115.54 ? 560 LYS   A N   1 
ATOM   2042 C  CA  . LYS   A 1 264 ? -17.666 14.866  21.133 1.00 111.97 ? 560 LYS   A CA  1 
ATOM   2043 C  C   . LYS   A 1 264 ? -17.652 13.351  21.189 1.00 100.10 ? 560 LYS   A C   1 
ATOM   2044 O  O   . LYS   A 1 264 ? -16.669 12.736  21.607 1.00 93.53  ? 560 LYS   A O   1 
ATOM   2045 C  CB  . LYS   A 1 264 ? -17.380 15.346  19.700 1.00 115.33 ? 560 LYS   A CB  1 
ATOM   2046 C  CG  . LYS   A 1 264 ? -15.963 15.052  19.196 1.00 121.94 ? 560 LYS   A CG  1 
ATOM   2047 C  CD  . LYS   A 1 264 ? -15.820 15.386  17.694 1.00 130.00 ? 560 LYS   A CD  1 
ATOM   2048 C  CE  . LYS   A 1 264 ? -14.393 15.167  17.162 1.00 133.19 ? 560 LYS   A CE  1 
ATOM   2049 N  NZ  . LYS   A 1 264 ? -14.300 15.110  15.663 1.00 131.15 ? 560 LYS   A NZ  1 
ATOM   2050 N  N   . TRP   A 1 265 ? -18.761 12.752  20.784 1.00 93.80  ? 561 TRP   A N   1 
ATOM   2051 C  CA  . TRP   A 1 265 ? -18.832 11.306  20.707 1.00 89.69  ? 561 TRP   A CA  1 
ATOM   2052 C  C   . TRP   A 1 265 ? -19.594 10.950  19.437 1.00 89.46  ? 561 TRP   A C   1 
ATOM   2053 O  O   . TRP   A 1 265 ? -20.282 11.792  18.847 1.00 87.02  ? 561 TRP   A O   1 
ATOM   2054 C  CB  . TRP   A 1 265 ? -19.479 10.700  21.961 1.00 76.23  ? 561 TRP   A CB  1 
ATOM   2055 C  CG  . TRP   A 1 265 ? -19.069 9.241   22.199 1.00 71.99  ? 561 TRP   A CG  1 
ATOM   2056 C  CD1 . TRP   A 1 265 ? -19.839 8.133   21.997 1.00 78.73  ? 561 TRP   A CD1 1 
ATOM   2057 C  CD2 . TRP   A 1 265 ? -17.782 8.759   22.619 1.00 80.64  ? 561 TRP   A CD2 1 
ATOM   2058 N  NE1 . TRP   A 1 265 ? -19.125 6.988   22.295 1.00 77.75  ? 561 TRP   A NE1 1 
ATOM   2059 C  CE2 . TRP   A 1 265 ? -17.859 7.348   22.673 1.00 77.65  ? 561 TRP   A CE2 1 
ATOM   2060 C  CE3 . TRP   A 1 265 ? -16.584 9.382   22.994 1.00 89.72  ? 561 TRP   A CE3 1 
ATOM   2061 C  CZ2 . TRP   A 1 265 ? -16.784 6.554   23.071 1.00 82.60  ? 561 TRP   A CZ2 1 
ATOM   2062 C  CZ3 . TRP   A 1 265 ? -15.512 8.583   23.382 1.00 82.32  ? 561 TRP   A CZ3 1 
ATOM   2063 C  CH2 . TRP   A 1 265 ? -15.626 7.188   23.427 1.00 80.85  ? 561 TRP   A CH2 1 
ATOM   2064 N  N   . TYR   A 1 266 ? -19.430 9.704   19.004 1.00 79.97  ? 562 TYR   A N   1 
ATOM   2065 C  CA  . TYR   A 1 266 ? -20.125 9.221   17.820 1.00 85.72  ? 562 TYR   A CA  1 
ATOM   2066 C  C   . TYR   A 1 266 ? -21.522 8.736   18.186 1.00 84.12  ? 562 TYR   A C   1 
ATOM   2067 O  O   . TYR   A 1 266 ? -21.757 8.205   19.275 1.00 82.37  ? 562 TYR   A O   1 
ATOM   2068 C  CB  . TYR   A 1 266 ? -19.339 8.097   17.142 1.00 80.14  ? 562 TYR   A CB  1 
ATOM   2069 C  CG  . TYR   A 1 266 ? -18.808 7.041   18.098 1.00 75.79  ? 562 TYR   A CG  1 
ATOM   2070 C  CD1 . TYR   A 1 266 ? -19.575 5.938   18.435 1.00 71.58  ? 562 TYR   A CD1 1 
ATOM   2071 C  CD2 . TYR   A 1 266 ? -17.528 7.132   18.628 1.00 71.66  ? 562 TYR   A CD2 1 
ATOM   2072 C  CE1 . TYR   A 1 266 ? -19.096 4.964   19.279 1.00 78.15  ? 562 TYR   A CE1 1 
ATOM   2073 C  CE2 . TYR   A 1 266 ? -17.049 6.166   19.497 1.00 80.07  ? 562 TYR   A CE2 1 
ATOM   2074 C  CZ  . TYR   A 1 266 ? -17.835 5.082   19.812 1.00 79.97  ? 562 TYR   A CZ  1 
ATOM   2075 O  OH  . TYR   A 1 266 ? -17.375 4.094   20.656 1.00 84.33  ? 562 TYR   A OH  1 
ATOM   2076 N  N   . GLY   A 1 267 ? -22.458 8.921   17.256 1.00 81.37  ? 563 GLY   A N   1 
ATOM   2077 C  CA  . GLY   A 1 267 ? -23.845 8.667   17.581 1.00 78.82  ? 563 GLY   A CA  1 
ATOM   2078 C  C   . GLY   A 1 267 ? -24.218 7.203   17.663 1.00 74.28  ? 563 GLY   A C   1 
ATOM   2079 O  O   . GLY   A 1 267 ? -25.222 6.871   18.302 1.00 78.36  ? 563 GLY   A O   1 
ATOM   2080 N  N   . LEU   A 1 268 ? -23.424 6.319   17.052 1.00 69.43  ? 564 LEU   A N   1 
ATOM   2081 C  CA  . LEU   A 1 268 ? -23.877 4.958   16.789 1.00 64.53  ? 564 LEU   A CA  1 
ATOM   2082 C  C   . LEU   A 1 268 ? -23.076 3.937   17.580 1.00 68.08  ? 564 LEU   A C   1 
ATOM   2083 O  O   . LEU   A 1 268 ? -21.886 3.721   17.281 1.00 66.16  ? 564 LEU   A O   1 
ATOM   2084 C  CB  . LEU   A 1 268 ? -23.793 4.647   15.292 1.00 67.83  ? 564 LEU   A CB  1 
ATOM   2085 C  CG  . LEU   A 1 268 ? -24.514 3.372   14.831 1.00 68.19  ? 564 LEU   A CG  1 
ATOM   2086 C  CD1 . LEU   A 1 268 ? -26.022 3.590   14.662 1.00 74.29  ? 564 LEU   A CD1 1 
ATOM   2087 C  CD2 . LEU   A 1 268 ? -23.909 2.807   13.557 1.00 60.30  ? 564 LEU   A CD2 1 
ATOM   2088 N  N   . PRO   A 1 269 ? -23.691 3.278   18.590 1.00 64.89  ? 565 PRO   A N   1 
ATOM   2089 C  CA  . PRO   A 1 269 ? -23.014 2.174   19.278 1.00 57.66  ? 565 PRO   A CA  1 
ATOM   2090 C  C   . PRO   A 1 269 ? -23.221 0.870   18.531 1.00 58.88  ? 565 PRO   A C   1 
ATOM   2091 O  O   . PRO   A 1 269 ? -24.357 0.413   18.385 1.00 56.60  ? 565 PRO   A O   1 
ATOM   2092 C  CB  . PRO   A 1 269 ? -23.694 2.138   20.648 1.00 59.47  ? 565 PRO   A CB  1 
ATOM   2093 C  CG  . PRO   A 1 269 ? -25.072 2.788   20.442 1.00 55.62  ? 565 PRO   A CG  1 
ATOM   2094 C  CD  . PRO   A 1 269 ? -25.091 3.415   19.028 1.00 62.23  ? 565 PRO   A CD  1 
ATOM   2095 N  N   . ALA   A 1 270 ? -22.138 0.247   18.070 1.00 53.26  ? 566 ALA   A N   1 
ATOM   2096 C  CA  . ALA   A 1 270 ? -22.242 -0.886  17.152 1.00 55.39  ? 566 ALA   A CA  1 
ATOM   2097 C  C   . ALA   A 1 270 ? -21.172 -1.896  17.540 1.00 60.02  ? 566 ALA   A C   1 
ATOM   2098 O  O   . ALA   A 1 270 ? -19.999 -1.709  17.214 1.00 67.07  ? 566 ALA   A O   1 
ATOM   2099 C  CB  . ALA   A 1 270 ? -22.098 -0.432  15.691 1.00 46.26  ? 566 ALA   A CB  1 
ATOM   2100 N  N   . VAL   A 1 271 ? -21.581 -2.958  18.238 1.00 50.81  ? 567 VAL   A N   1 
ATOM   2101 C  CA  . VAL   A 1 271 ? -20.652 -3.988  18.683 1.00 55.87  ? 567 VAL   A CA  1 
ATOM   2102 C  C   . VAL   A 1 271 ? -20.338 -4.925  17.531 1.00 55.92  ? 567 VAL   A C   1 
ATOM   2103 O  O   . VAL   A 1 271 ? -21.245 -5.472  16.892 1.00 63.56  ? 567 VAL   A O   1 
ATOM   2104 C  CB  . VAL   A 1 271 ? -21.240 -4.770  19.863 1.00 51.78  ? 567 VAL   A CB  1 
ATOM   2105 C  CG1 . VAL   A 1 271 ? -20.565 -6.119  19.961 1.00 53.19  ? 567 VAL   A CG1 1 
ATOM   2106 C  CG2 . VAL   A 1 271 ? -21.117 -3.963  21.186 1.00 51.81  ? 567 VAL   A CG2 1 
ATOM   2107 N  N   . SER   A 1 272 ? -19.051 -5.176  17.306 1.00 57.98  ? 568 SER   A N   1 
ATOM   2108 C  CA  . SER   A 1 272 ? -18.650 -6.009  16.189 1.00 51.54  ? 568 SER   A CA  1 
ATOM   2109 C  C   . SER   A 1 272 ? -17.811 -7.233  16.531 1.00 55.73  ? 568 SER   A C   1 
ATOM   2110 O  O   . SER   A 1 272 ? -17.451 -7.976  15.611 1.00 65.76  ? 568 SER   A O   1 
ATOM   2111 C  CB  . SER   A 1 272 ? -17.885 -5.159  15.171 1.00 61.94  ? 568 SER   A CB  1 
ATOM   2112 O  OG  . SER   A 1 272 ? -16.936 -4.342  15.827 1.00 63.20  ? 568 SER   A OG  1 
ATOM   2113 N  N   . ASN   A 1 273 ? -17.486 -7.480  17.804 1.00 59.00  ? 569 ASN   A N   1 
ATOM   2114 C  CA  . ASN   A 1 273 ? -16.550 -8.547  18.155 1.00 63.61  ? 569 ASN   A CA  1 
ATOM   2115 C  C   . ASN   A 1 273 ? -17.232 -9.778  18.748 1.00 65.50  ? 569 ASN   A C   1 
ATOM   2116 O  O   . ASN   A 1 273 ? -16.537 -10.714 19.158 1.00 62.68  ? 569 ASN   A O   1 
ATOM   2117 C  CB  . ASN   A 1 273 ? -15.480 -8.030  19.128 1.00 69.34  ? 569 ASN   A CB  1 
ATOM   2118 C  CG  . ASN   A 1 273 ? -16.076 -7.467  20.403 1.00 71.11  ? 569 ASN   A CG  1 
ATOM   2119 O  OD1 . ASN   A 1 273 ? -17.291 -7.490  20.593 1.00 60.28  ? 569 ASN   A OD1 1 
ATOM   2120 N  ND2 . ASN   A 1 273 ? -15.217 -6.965  21.295 1.00 75.30  ? 569 ASN   A ND2 1 
ATOM   2121 N  N   . MET   A 1 274 ? -18.563 -9.811  18.796 1.00 57.20  ? 570 MET   A N   1 
ATOM   2122 C  CA  . MET   A 1 274 ? -19.275 -10.905 19.436 1.00 50.86  ? 570 MET   A CA  1 
ATOM   2123 C  C   . MET   A 1 274 ? -19.686 -11.975 18.434 1.00 57.79  ? 570 MET   A C   1 
ATOM   2124 O  O   . MET   A 1 274 ? -19.610 -11.796 17.219 1.00 57.77  ? 570 MET   A O   1 
ATOM   2125 C  CB  . MET   A 1 274 ? -20.483 -10.370 20.204 1.00 53.40  ? 570 MET   A CB  1 
ATOM   2126 C  CG  . MET   A 1 274 ? -20.030 -9.618  21.511 1.00 53.51  ? 570 MET   A CG  1 
ATOM   2127 S  SD  . MET   A 1 274 ? -21.411 -9.120  22.549 1.00 58.89  ? 570 MET   A SD  1 
ATOM   2128 C  CE  . MET   A 1 274 ? -21.676 -10.640 23.466 1.00 54.47  ? 570 MET   A CE  1 
ATOM   2129 N  N   . LEU   A 1 275 ? -20.113 -13.116 18.967 1.00 55.53  ? 571 LEU   A N   1 
ATOM   2130 C  CA  . LEU   A 1 275 ? -20.492 -14.276 18.173 1.00 53.91  ? 571 LEU   A CA  1 
ATOM   2131 C  C   . LEU   A 1 275 ? -21.987 -14.510 18.322 1.00 58.89  ? 571 LEU   A C   1 
ATOM   2132 O  O   . LEU   A 1 275 ? -22.496 -14.562 19.443 1.00 57.60  ? 571 LEU   A O   1 
ATOM   2133 C  CB  . LEU   A 1 275 ? -19.713 -15.519 18.612 1.00 49.60  ? 571 LEU   A CB  1 
ATOM   2134 C  CG  . LEU   A 1 275 ? -19.794 -16.804 17.781 1.00 67.62  ? 571 LEU   A CG  1 
ATOM   2135 C  CD1 . LEU   A 1 275 ? -18.455 -17.502 17.865 1.00 79.00  ? 571 LEU   A CD1 1 
ATOM   2136 C  CD2 . LEU   A 1 275 ? -20.899 -17.718 18.296 1.00 66.62  ? 571 LEU   A CD2 1 
ATOM   2137 N  N   . LEU   A 1 276 ? -22.689 -14.640 17.193 1.00 52.42  ? 572 LEU   A N   1 
ATOM   2138 C  CA  . LEU   A 1 276 ? -24.123 -14.930 17.192 1.00 58.64  ? 572 LEU   A CA  1 
ATOM   2139 C  C   . LEU   A 1 276 ? -24.320 -16.436 17.021 1.00 64.14  ? 572 LEU   A C   1 
ATOM   2140 O  O   . LEU   A 1 276 ? -23.830 -17.019 16.047 1.00 57.75  ? 572 LEU   A O   1 
ATOM   2141 C  CB  . LEU   A 1 276 ? -24.835 -14.155 16.068 1.00 51.68  ? 572 LEU   A CB  1 
ATOM   2142 C  CG  . LEU   A 1 276 ? -26.259 -14.565 15.655 1.00 55.32  ? 572 LEU   A CG  1 
ATOM   2143 C  CD1 . LEU   A 1 276 ? -27.233 -14.549 16.820 1.00 54.41  ? 572 LEU   A CD1 1 
ATOM   2144 C  CD2 . LEU   A 1 276 ? -26.785 -13.678 14.565 1.00 60.07  ? 572 LEU   A CD2 1 
ATOM   2145 N  N   . GLU   A 1 277 ? -25.028 -17.070 17.963 1.00 53.48  ? 573 GLU   A N   1 
ATOM   2146 C  CA  . GLU   A 1 277 ? -25.286 -18.504 17.903 1.00 60.60  ? 573 GLU   A CA  1 
ATOM   2147 C  C   . GLU   A 1 277 ? -26.766 -18.752 17.625 1.00 66.08  ? 573 GLU   A C   1 
ATOM   2148 O  O   . GLU   A 1 277 ? -27.627 -18.264 18.364 1.00 62.00  ? 573 GLU   A O   1 
ATOM   2149 C  CB  . GLU   A 1 277 ? -24.861 -19.186 19.202 1.00 62.51  ? 573 GLU   A CB  1 
ATOM   2150 C  CG  . GLU   A 1 277 ? -24.302 -20.566 19.002 1.00 75.45  ? 573 GLU   A CG  1 
ATOM   2151 C  CD  . GLU   A 1 277 ? -25.040 -21.614 19.804 1.00 92.12  ? 573 GLU   A CD  1 
ATOM   2152 O  OE1 . GLU   A 1 277 ? -26.221 -21.897 19.485 1.00 90.35  ? 573 GLU   A OE1 1 
ATOM   2153 O  OE2 . GLU   A 1 277 ? -24.437 -22.145 20.764 1.00 102.79 ? 573 GLU   A OE2 1 
ATOM   2154 N  N   . ILE   A 1 278 ? -27.059 -19.517 16.567 1.00 70.74  ? 574 ILE   A N   1 
ATOM   2155 C  CA  . ILE   A 1 278 ? -28.429 -19.847 16.168 1.00 64.08  ? 574 ILE   A CA  1 
ATOM   2156 C  C   . ILE   A 1 278 ? -28.483 -21.322 15.790 1.00 69.01  ? 574 ILE   A C   1 
ATOM   2157 O  O   . ILE   A 1 278 ? -27.763 -21.757 14.885 1.00 72.07  ? 574 ILE   A O   1 
ATOM   2158 C  CB  . ILE   A 1 278 ? -28.932 -18.996 14.989 1.00 60.68  ? 574 ILE   A CB  1 
ATOM   2159 C  CG1 . ILE   A 1 278 ? -29.051 -17.515 15.353 1.00 61.65  ? 574 ILE   A CG1 1 
ATOM   2160 C  CG2 . ILE   A 1 278 ? -30.282 -19.521 14.503 1.00 66.74  ? 574 ILE   A CG2 1 
ATOM   2161 C  CD1 . ILE   A 1 278 ? -29.046 -16.586 14.098 1.00 54.20  ? 574 ILE   A CD1 1 
ATOM   2162 N  N   . GLY   A 1 279 ? -29.336 -22.087 16.468 1.00 70.47  ? 575 GLY   A N   1 
ATOM   2163 C  CA  . GLY   A 1 279 ? -29.476 -23.506 16.146 1.00 72.65  ? 575 GLY   A CA  1 
ATOM   2164 C  C   . GLY   A 1 279 ? -28.163 -24.240 16.001 1.00 75.27  ? 575 GLY   A C   1 
ATOM   2165 O  O   . GLY   A 1 279 ? -28.022 -25.083 15.113 1.00 80.85  ? 575 GLY   A O   1 
ATOM   2166 N  N   . GLY   A 1 280 ? -27.183 -23.925 16.846 1.00 71.65  ? 576 GLY   A N   1 
ATOM   2167 C  CA  . GLY   A 1 280 ? -25.891 -24.575 16.731 1.00 78.36  ? 576 GLY   A CA  1 
ATOM   2168 C  C   . GLY   A 1 280 ? -24.969 -24.025 15.660 1.00 72.08  ? 576 GLY   A C   1 
ATOM   2169 O  O   . GLY   A 1 280 ? -23.828 -24.483 15.557 1.00 79.71  ? 576 GLY   A O   1 
ATOM   2170 N  N   . LEU   A 1 281 ? -25.409 -23.060 14.865 1.00 68.52  ? 577 LEU   A N   1 
ATOM   2171 C  CA  . LEU   A 1 281 ? -24.550 -22.418 13.875 1.00 74.97  ? 577 LEU   A CA  1 
ATOM   2172 C  C   . LEU   A 1 281 ? -23.901 -21.176 14.476 1.00 74.19  ? 577 LEU   A C   1 
ATOM   2173 O  O   . LEU   A 1 281 ? -24.543 -20.435 15.223 1.00 69.20  ? 577 LEU   A O   1 
ATOM   2174 C  CB  . LEU   A 1 281 ? -25.343 -22.027 12.630 1.00 72.46  ? 577 LEU   A CB  1 
ATOM   2175 C  CG  . LEU   A 1 281 ? -26.013 -23.132 11.811 1.00 71.42  ? 577 LEU   A CG  1 
ATOM   2176 C  CD1 . LEU   A 1 281 ? -26.649 -22.549 10.549 1.00 75.11  ? 577 LEU   A CD1 1 
ATOM   2177 C  CD2 . LEU   A 1 281 ? -25.020 -24.231 11.478 1.00 71.57  ? 577 LEU   A CD2 1 
ATOM   2178 N  N   . GLU   A 1 282 ? -22.639 -20.928 14.118 1.00 75.62  ? 578 GLU   A N   1 
ATOM   2179 C  CA  . GLU   A 1 282 ? -21.849 -19.861 14.727 1.00 76.73  ? 578 GLU   A CA  1 
ATOM   2180 C  C   . GLU   A 1 282 ? -21.528 -18.793 13.688 1.00 71.94  ? 578 GLU   A C   1 
ATOM   2181 O  O   . GLU   A 1 282 ? -20.784 -19.054 12.732 1.00 68.30  ? 578 GLU   A O   1 
ATOM   2182 C  CB  . GLU   A 1 282 ? -20.565 -20.424 15.346 1.00 77.11  ? 578 GLU   A CB  1 
ATOM   2183 C  CG  . GLU   A 1 282 ? -20.814 -21.272 16.596 1.00 84.88  ? 578 GLU   A CG  1 
ATOM   2184 C  CD  . GLU   A 1 282 ? -19.571 -21.974 17.118 1.00 89.01  ? 578 GLU   A CD  1 
ATOM   2185 O  OE1 . GLU   A 1 282 ? -18.545 -22.009 16.406 1.00 89.35  ? 578 GLU   A OE1 1 
ATOM   2186 O  OE2 . GLU   A 1 282 ? -19.627 -22.498 18.252 1.00 96.18  ? 578 GLU   A OE2 1 
ATOM   2187 N  N   . PHE   A 1 283 ? -22.072 -17.585 13.883 1.00 62.55  ? 579 PHE   A N   1 
ATOM   2188 C  CA  . PHE   A 1 283 ? -21.776 -16.434 13.026 1.00 55.13  ? 579 PHE   A CA  1 
ATOM   2189 C  C   . PHE   A 1 283 ? -20.749 -15.549 13.739 1.00 57.61  ? 579 PHE   A C   1 
ATOM   2190 O  O   . PHE   A 1 283 ? -21.099 -14.752 14.611 1.00 65.26  ? 579 PHE   A O   1 
ATOM   2191 C  CB  . PHE   A 1 283 ? -23.053 -15.669 12.686 1.00 52.80  ? 579 PHE   A CB  1 
ATOM   2192 C  CG  . PHE   A 1 283 ? -24.068 -16.493 11.939 1.00 54.76  ? 579 PHE   A CG  1 
ATOM   2193 C  CD1 . PHE   A 1 283 ? -25.045 -17.214 12.613 1.00 60.39  ? 579 PHE   A CD1 1 
ATOM   2194 C  CD2 . PHE   A 1 283 ? -24.008 -16.589 10.557 1.00 58.79  ? 579 PHE   A CD2 1 
ATOM   2195 C  CE1 . PHE   A 1 283 ? -25.973 -17.990 11.904 1.00 63.00  ? 579 PHE   A CE1 1 
ATOM   2196 C  CE2 . PHE   A 1 283 ? -24.941 -17.341 9.852  1.00 64.96  ? 579 PHE   A CE2 1 
ATOM   2197 C  CZ  . PHE   A 1 283 ? -25.915 -18.045 10.524 1.00 64.18  ? 579 PHE   A CZ  1 
ATOM   2198 N  N   . SER   A 1 284 ? -19.479 -15.684 13.345 1.00 63.01  ? 580 SER   A N   1 
ATOM   2199 C  CA  . SER   A 1 284 ? -18.350 -15.027 13.993 1.00 56.53  ? 580 SER   A CA  1 
ATOM   2200 C  C   . SER   A 1 284 ? -18.252 -13.543 13.685 1.00 59.41  ? 580 SER   A C   1 
ATOM   2201 O  O   . SER   A 1 284 ? -17.479 -12.836 14.345 1.00 58.11  ? 580 SER   A O   1 
ATOM   2202 C  CB  . SER   A 1 284 ? -17.060 -15.706 13.566 1.00 60.04  ? 580 SER   A CB  1 
ATOM   2203 O  OG  . SER   A 1 284 ? -17.156 -16.018 12.194 1.00 61.90  ? 580 SER   A OG  1 
ATOM   2204 N  N   . ALA   A 1 285 ? -18.974 -13.061 12.678 1.00 64.43  ? 581 ALA   A N   1 
ATOM   2205 C  CA  . ALA   A 1 285 ? -19.033 -11.640 12.367 1.00 55.09  ? 581 ALA   A CA  1 
ATOM   2206 C  C   . ALA   A 1 285 ? -20.506 -11.284 12.253 1.00 61.43  ? 581 ALA   A C   1 
ATOM   2207 O  O   . ALA   A 1 285 ? -21.182 -11.723 11.314 1.00 59.95  ? 581 ALA   A O   1 
ATOM   2208 C  CB  . ALA   A 1 285 ? -18.271 -11.324 11.070 1.00 46.77  ? 581 ALA   A CB  1 
ATOM   2209 N  N   . CYS   A 1 286 ? -21.001 -10.497 13.203 1.00 54.22  ? 582 CYS   A N   1 
ATOM   2210 C  CA  . CYS   A 1 286 ? -22.413 -10.138 13.260 1.00 53.73  ? 582 CYS   A CA  1 
ATOM   2211 C  C   . CYS   A 1 286 ? -22.612 -8.757  13.891 1.00 57.80  ? 582 CYS   A C   1 
ATOM   2212 O  O   . CYS   A 1 286 ? -23.335 -8.627  14.892 1.00 63.50  ? 582 CYS   A O   1 
ATOM   2213 C  CB  . CYS   A 1 286 ? -23.169 -11.206 14.043 1.00 58.37  ? 582 CYS   A CB  1 
ATOM   2214 S  SG  . CYS   A 1 286 ? -22.457 -11.461 15.719 1.00 57.02  ? 582 CYS   A SG  1 
ATOM   2215 N  N   . PRO   A 1 287 ? -22.027 -7.701  13.315 1.00 60.10  ? 583 PRO   A N   1 
ATOM   2216 C  CA  . PRO   A 1 287 ? -22.110 -6.371  13.937 1.00 53.47  ? 583 PRO   A CA  1 
ATOM   2217 C  C   . PRO   A 1 287 ? -23.553 -5.916  14.114 1.00 56.85  ? 583 PRO   A C   1 
ATOM   2218 O  O   . PRO   A 1 287 ? -24.357 -5.986  13.186 1.00 49.75  ? 583 PRO   A O   1 
ATOM   2219 C  CB  . PRO   A 1 287 ? -21.341 -5.479  12.954 1.00 59.49  ? 583 PRO   A CB  1 
ATOM   2220 C  CG  . PRO   A 1 287 ? -21.426 -6.182  11.655 1.00 64.27  ? 583 PRO   A CG  1 
ATOM   2221 C  CD  . PRO   A 1 287 ? -21.389 -7.649  11.987 1.00 61.97  ? 583 PRO   A CD  1 
ATOM   2222 N  N   . PHE   A 1 288 ? -23.873 -5.419  15.322 1.00 44.70  ? 584 PHE   A N   1 
ATOM   2223 C  CA  . PHE   A 1 288 ? -25.229 -4.998  15.675 1.00 49.83  ? 584 PHE   A CA  1 
ATOM   2224 C  C   . PHE   A 1 288 ? -25.199 -3.637  16.363 1.00 54.79  ? 584 PHE   A C   1 
ATOM   2225 O  O   . PHE   A 1 288 ? -24.277 -3.336  17.119 1.00 48.55  ? 584 PHE   A O   1 
ATOM   2226 C  CB  . PHE   A 1 288 ? -25.941 -6.053  16.583 1.00 49.67  ? 584 PHE   A CB  1 
ATOM   2227 C  CG  . PHE   A 1 288 ? -25.195 -6.403  17.854 1.00 57.65  ? 584 PHE   A CG  1 
ATOM   2228 C  CD1 . PHE   A 1 288 ? -25.363 -5.627  19.014 1.00 48.52  ? 584 PHE   A CD1 1 
ATOM   2229 C  CD2 . PHE   A 1 288 ? -24.401 -7.545  17.927 1.00 58.03  ? 584 PHE   A CD2 1 
ATOM   2230 C  CE1 . PHE   A 1 288 ? -24.706 -5.945  20.202 1.00 50.94  ? 584 PHE   A CE1 1 
ATOM   2231 C  CE2 . PHE   A 1 288 ? -23.753 -7.878  19.150 1.00 52.37  ? 584 PHE   A CE2 1 
ATOM   2232 C  CZ  . PHE   A 1 288 ? -23.911 -7.071  20.262 1.00 55.22  ? 584 PHE   A CZ  1 
ATOM   2233 N  N   . SER   A 1 289 ? -26.218 -2.818  16.114 1.00 58.41  ? 585 SER   A N   1 
ATOM   2234 C  CA  . SER   A 1 289 ? -26.208 -1.450  16.602 1.00 57.61  ? 585 SER   A CA  1 
ATOM   2235 C  C   . SER   A 1 289 ? -27.575 -1.036  17.138 1.00 56.82  ? 585 SER   A C   1 
ATOM   2236 O  O   . SER   A 1 289 ? -28.620 -1.466  16.645 1.00 55.92  ? 585 SER   A O   1 
ATOM   2237 C  CB  . SER   A 1 289 ? -25.752 -0.478  15.489 1.00 67.93  ? 585 SER   A CB  1 
ATOM   2238 O  OG  . SER   A 1 289 ? -26.661 -0.474  14.415 1.00 60.45  ? 585 SER   A OG  1 
ATOM   2239 N  N   . GLY   A 1 290 ? -27.552 -0.194  18.168 1.00 59.60  ? 586 GLY   A N   1 
ATOM   2240 C  CA  . GLY   A 1 290 ? -28.764 0.424   18.669 1.00 56.32  ? 586 GLY   A CA  1 
ATOM   2241 C  C   . GLY   A 1 290 ? -28.590 1.924   18.795 1.00 65.82  ? 586 GLY   A C   1 
ATOM   2242 O  O   . GLY   A 1 290 ? -28.140 2.585   17.850 1.00 66.95  ? 586 GLY   A O   1 
ATOM   2243 N  N   . TRP   A 1 291 ? -28.963 2.476   19.950 1.00 62.62  ? 587 TRP   A N   1 
ATOM   2244 C  CA  . TRP   A 1 291 ? -28.615 3.841   20.318 1.00 68.35  ? 587 TRP   A CA  1 
ATOM   2245 C  C   . TRP   A 1 291 ? -28.027 3.833   21.721 1.00 74.21  ? 587 TRP   A C   1 
ATOM   2246 O  O   . TRP   A 1 291 ? -28.168 2.860   22.465 1.00 70.88  ? 587 TRP   A O   1 
ATOM   2247 C  CB  . TRP   A 1 291 ? -29.812 4.800   20.250 1.00 76.54  ? 587 TRP   A CB  1 
ATOM   2248 C  CG  . TRP   A 1 291 ? -31.055 4.288   20.875 1.00 75.75  ? 587 TRP   A CG  1 
ATOM   2249 C  CD1 . TRP   A 1 291 ? -31.431 4.389   22.198 1.00 80.47  ? 587 TRP   A CD1 1 
ATOM   2250 C  CD2 . TRP   A 1 291 ? -32.109 3.598   20.210 1.00 80.30  ? 587 TRP   A CD2 1 
ATOM   2251 N  NE1 . TRP   A 1 291 ? -32.659 3.794   22.383 1.00 79.31  ? 587 TRP   A NE1 1 
ATOM   2252 C  CE2 . TRP   A 1 291 ? -33.096 3.301   21.177 1.00 84.66  ? 587 TRP   A CE2 1 
ATOM   2253 C  CE3 . TRP   A 1 291 ? -32.317 3.199   18.887 1.00 76.75  ? 587 TRP   A CE3 1 
ATOM   2254 C  CZ2 . TRP   A 1 291 ? -34.269 2.617   20.855 1.00 86.50  ? 587 TRP   A CZ2 1 
ATOM   2255 C  CZ3 . TRP   A 1 291 ? -33.478 2.529   18.571 1.00 80.96  ? 587 TRP   A CZ3 1 
ATOM   2256 C  CH2 . TRP   A 1 291 ? -34.436 2.237   19.552 1.00 83.83  ? 587 TRP   A CH2 1 
ATOM   2257 N  N   . TYR   A 1 292 ? -27.355 4.930   22.061 1.00 71.47  ? 588 TYR   A N   1 
ATOM   2258 C  CA  . TYR   A 1 292 ? -26.608 5.006   23.312 1.00 70.35  ? 588 TYR   A CA  1 
ATOM   2259 C  C   . TYR   A 1 292 ? -27.527 5.321   24.477 1.00 74.50  ? 588 TYR   A C   1 
ATOM   2260 O  O   . TYR   A 1 292 ? -28.461 6.121   24.350 1.00 70.29  ? 588 TYR   A O   1 
ATOM   2261 C  CB  . TYR   A 1 292 ? -25.534 6.094   23.223 1.00 76.35  ? 588 TYR   A CB  1 
ATOM   2262 C  CG  . TYR   A 1 292 ? -24.138 5.617   22.900 1.00 75.53  ? 588 TYR   A CG  1 
ATOM   2263 C  CD1 . TYR   A 1 292 ? -23.480 6.073   21.775 1.00 71.42  ? 588 TYR   A CD1 1 
ATOM   2264 C  CD2 . TYR   A 1 292 ? -23.472 4.724   23.735 1.00 75.91  ? 588 TYR   A CD2 1 
ATOM   2265 C  CE1 . TYR   A 1 292 ? -22.194 5.661   21.479 1.00 71.23  ? 588 TYR   A CE1 1 
ATOM   2266 C  CE2 . TYR   A 1 292 ? -22.178 4.307   23.450 1.00 77.52  ? 588 TYR   A CE2 1 
ATOM   2267 C  CZ  . TYR   A 1 292 ? -21.550 4.774   22.314 1.00 69.59  ? 588 TYR   A CZ  1 
ATOM   2268 O  OH  . TYR   A 1 292 ? -20.276 4.351   22.010 1.00 63.39  ? 588 TYR   A OH  1 
ATOM   2269 N  N   . MET   A 1 293 ? -27.245 4.699   25.627 1.00 65.33  ? 589 MET   A N   1 
ATOM   2270 C  CA  . MET   A 1 293 ? -27.711 5.210   26.898 1.00 73.31  ? 589 MET   A CA  1 
ATOM   2271 C  C   . MET   A 1 293 ? -26.684 6.212   27.405 1.00 73.03  ? 589 MET   A C   1 
ATOM   2272 O  O   . MET   A 1 293 ? -25.474 5.980   27.304 1.00 68.49  ? 589 MET   A O   1 
ATOM   2273 C  CB  . MET   A 1 293 ? -27.916 4.092   27.916 1.00 61.07  ? 589 MET   A CB  1 
ATOM   2274 C  CG  . MET   A 1 293 ? -28.518 4.601   29.222 1.00 72.81  ? 589 MET   A CG  1 
ATOM   2275 S  SD  . MET   A 1 293 ? -28.991 3.276   30.322 1.00 67.63  ? 589 MET   A SD  1 
ATOM   2276 C  CE  . MET   A 1 293 ? -27.418 2.632   30.917 1.00 71.58  ? 589 MET   A CE  1 
ATOM   2277 N  N   . GLY   A 1 294 ? -27.181 7.349   27.901 1.00 66.30  ? 590 GLY   A N   1 
ATOM   2278 C  CA  . GLY   A 1 294 ? -26.308 8.465   28.248 1.00 68.18  ? 590 GLY   A CA  1 
ATOM   2279 C  C   . GLY   A 1 294 ? -25.088 8.077   29.069 1.00 73.65  ? 590 GLY   A C   1 
ATOM   2280 O  O   . GLY   A 1 294 ? -23.984 8.579   28.829 1.00 73.40  ? 590 GLY   A O   1 
ATOM   2281 N  N   . THR   A 1 295 ? -25.267 7.193   30.049 1.00 73.60  ? 591 THR   A N   1 
ATOM   2282 C  CA  . THR   A 1 295 ? -24.192 6.922   31.001 1.00 73.49  ? 591 THR   A CA  1 
ATOM   2283 C  C   . THR   A 1 295 ? -23.017 6.177   30.371 1.00 72.32  ? 591 THR   A C   1 
ATOM   2284 O  O   . THR   A 1 295 ? -21.898 6.251   30.886 1.00 68.54  ? 591 THR   A O   1 
ATOM   2285 C  CB  . THR   A 1 295 ? -24.719 6.127   32.201 1.00 69.24  ? 591 THR   A CB  1 
ATOM   2286 O  OG1 . THR   A 1 295 ? -25.295 4.899   31.763 1.00 66.43  ? 591 THR   A OG1 1 
ATOM   2287 C  CG2 . THR   A 1 295 ? -25.760 6.945   32.988 1.00 68.45  ? 591 THR   A CG2 1 
ATOM   2288 N  N   . GLU   A 1 296 ? -23.228 5.443   29.279 1.00 64.43  ? 592 GLU   A N   1 
ATOM   2289 C  CA  . GLU   A 1 296 ? -22.090 4.775   28.652 1.00 68.54  ? 592 GLU   A CA  1 
ATOM   2290 C  C   . GLU   A 1 296 ? -21.056 5.785   28.171 1.00 69.26  ? 592 GLU   A C   1 
ATOM   2291 O  O   . GLU   A 1 296 ? -19.852 5.525   28.236 1.00 74.98  ? 592 GLU   A O   1 
ATOM   2292 C  CB  . GLU   A 1 296 ? -22.530 3.926   27.471 1.00 68.09  ? 592 GLU   A CB  1 
ATOM   2293 C  CG  . GLU   A 1 296 ? -23.531 2.842   27.729 1.00 63.12  ? 592 GLU   A CG  1 
ATOM   2294 C  CD  . GLU   A 1 296 ? -23.907 2.209   26.383 1.00 68.50  ? 592 GLU   A CD  1 
ATOM   2295 O  OE1 . GLU   A 1 296 ? -23.050 1.485   25.816 1.00 66.57  ? 592 GLU   A OE1 1 
ATOM   2296 O  OE2 . GLU   A 1 296 ? -25.005 2.523   25.852 1.00 65.26  ? 592 GLU   A OE2 1 
ATOM   2297 N  N   . ILE   A 1 297 ? -21.507 6.928   27.653 1.00 66.19  ? 593 ILE   A N   1 
ATOM   2298 C  CA  . ILE   A 1 297 ? -20.577 7.971   27.226 1.00 67.56  ? 593 ILE   A CA  1 
ATOM   2299 C  C   . ILE   A 1 297 ? -20.123 8.805   28.412 1.00 74.68  ? 593 ILE   A C   1 
ATOM   2300 O  O   . ILE   A 1 297 ? -18.921 8.985   28.653 1.00 74.93  ? 593 ILE   A O   1 
ATOM   2301 C  CB  . ILE   A 1 297 ? -21.225 8.869   26.158 1.00 69.24  ? 593 ILE   A CB  1 
ATOM   2302 C  CG1 . ILE   A 1 297 ? -21.639 8.050   24.952 1.00 69.09  ? 593 ILE   A CG1 1 
ATOM   2303 C  CG2 . ILE   A 1 297 ? -20.250 9.937   25.732 1.00 76.92  ? 593 ILE   A CG2 1 
ATOM   2304 C  CD1 . ILE   A 1 297 ? -22.637 8.764   24.082 1.00 68.65  ? 593 ILE   A CD1 1 
ATOM   2305 N  N   . GLY   A 1 298 ? -21.093 9.337   29.157 1.00 79.12  ? 594 GLY   A N   1 
ATOM   2306 C  CA  . GLY   A 1 298 ? -20.795 10.309  30.197 1.00 82.34  ? 594 GLY   A CA  1 
ATOM   2307 C  C   . GLY   A 1 298 ? -20.159 9.717   31.438 1.00 81.38  ? 594 GLY   A C   1 
ATOM   2308 O  O   . GLY   A 1 298 ? -19.408 10.403  32.138 1.00 82.67  ? 594 GLY   A O   1 
ATOM   2309 N  N   . VAL   A 1 299 ? -20.443 8.456   31.743 1.00 80.32  ? 595 VAL   A N   1 
ATOM   2310 C  CA  . VAL   A 1 299 ? -19.880 7.879   32.966 1.00 80.23  ? 595 VAL   A CA  1 
ATOM   2311 C  C   . VAL   A 1 299 ? -18.709 6.964   32.628 1.00 78.29  ? 595 VAL   A C   1 
ATOM   2312 O  O   . VAL   A 1 299 ? -17.591 7.167   33.108 1.00 78.21  ? 595 VAL   A O   1 
ATOM   2313 C  CB  . VAL   A 1 299 ? -20.936 7.123   33.794 1.00 73.21  ? 595 VAL   A CB  1 
ATOM   2314 C  CG1 . VAL   A 1 299 ? -20.298 6.648   35.080 1.00 71.07  ? 595 VAL   A CG1 1 
ATOM   2315 C  CG2 . VAL   A 1 299 ? -22.118 8.015   34.117 1.00 72.64  ? 595 VAL   A CG2 1 
ATOM   2316 N  N   . ARG   A 1 300 ? -18.945 5.969   31.774 1.00 70.93  ? 596 ARG   A N   1 
ATOM   2317 C  CA  . ARG   A 1 300 ? -17.897 5.005   31.461 1.00 64.77  ? 596 ARG   A CA  1 
ATOM   2318 C  C   . ARG   A 1 300 ? -16.874 5.577   30.479 1.00 72.76  ? 596 ARG   A C   1 
ATOM   2319 O  O   . ARG   A 1 300 ? -15.667 5.588   30.755 1.00 67.77  ? 596 ARG   A O   1 
ATOM   2320 C  CB  . ARG   A 1 300 ? -18.527 3.722   30.922 1.00 68.58  ? 596 ARG   A CB  1 
ATOM   2321 C  CG  . ARG   A 1 300 ? -19.636 3.157   31.838 1.00 70.31  ? 596 ARG   A CG  1 
ATOM   2322 C  CD  . ARG   A 1 300 ? -19.121 2.938   33.260 1.00 73.17  ? 596 ARG   A CD  1 
ATOM   2323 N  NE  . ARG   A 1 300 ? -17.847 2.216   33.301 1.00 66.14  ? 596 ARG   A NE  1 
ATOM   2324 C  CZ  . ARG   A 1 300 ? -17.699 0.925   33.004 1.00 65.73  ? 596 ARG   A CZ  1 
ATOM   2325 N  NH1 . ARG   A 1 300 ? -18.741 0.176   32.633 1.00 69.79  ? 596 ARG   A NH1 1 
ATOM   2326 N  NH2 . ARG   A 1 300 ? -16.494 0.379   33.059 1.00 62.99  ? 596 ARG   A NH2 1 
ATOM   2327 N  N   . ASP   A 1 301 ? -17.326 6.031   29.310 1.00 78.82  ? 597 ASP   A N   1 
ATOM   2328 C  CA  . ASP   A 1 301 ? -16.371 6.485   28.296 1.00 77.64  ? 597 ASP   A CA  1 
ATOM   2329 C  C   . ASP   A 1 301 ? -15.563 7.680   28.802 1.00 82.26  ? 597 ASP   A C   1 
ATOM   2330 O  O   . ASP   A 1 301 ? -14.341 7.733   28.631 1.00 88.00  ? 597 ASP   A O   1 
ATOM   2331 C  CB  . ASP   A 1 301 ? -17.098 6.809   26.972 1.00 75.21  ? 597 ASP   A CB  1 
ATOM   2332 C  CG  . ASP   A 1 301 ? -17.572 5.555   26.234 1.00 76.43  ? 597 ASP   A CG  1 
ATOM   2333 O  OD1 . ASP   A 1 301 ? -16.857 4.521   26.258 1.00 73.67  ? 597 ASP   A OD1 1 
ATOM   2334 O  OD2 . ASP   A 1 301 ? -18.662 5.603   25.613 1.00 80.12  ? 597 ASP   A OD2 1 
ATOM   2335 N  N   . TYR   A 1 302 ? -16.211 8.607   29.500 1.00 82.81  ? 598 TYR   A N   1 
ATOM   2336 C  CA  . TYR   A 1 302 ? -15.552 9.859   29.852 1.00 83.70  ? 598 TYR   A CA  1 
ATOM   2337 C  C   . TYR   A 1 302 ? -14.872 9.853   31.224 1.00 87.13  ? 598 TYR   A C   1 
ATOM   2338 O  O   . TYR   A 1 302 ? -13.861 10.552  31.392 1.00 84.13  ? 598 TYR   A O   1 
ATOM   2339 C  CB  . TYR   A 1 302 ? -16.562 11.009  29.797 1.00 94.33  ? 598 TYR   A CB  1 
ATOM   2340 C  CG  . TYR   A 1 302 ? -16.865 11.529  28.397 1.00 100.12 ? 598 TYR   A CG  1 
ATOM   2341 C  CD1 . TYR   A 1 302 ? -18.092 12.117  28.108 1.00 103.97 ? 598 TYR   A CD1 1 
ATOM   2342 C  CD2 . TYR   A 1 302 ? -15.924 11.455  27.374 1.00 93.67  ? 598 TYR   A CD2 1 
ATOM   2343 C  CE1 . TYR   A 1 302 ? -18.381 12.611  26.838 1.00 97.15  ? 598 TYR   A CE1 1 
ATOM   2344 C  CE2 . TYR   A 1 302 ? -16.204 11.945  26.103 1.00 101.11 ? 598 TYR   A CE2 1 
ATOM   2345 C  CZ  . TYR   A 1 302 ? -17.433 12.520  25.844 1.00 100.62 ? 598 TYR   A CZ  1 
ATOM   2346 O  OH  . TYR   A 1 302 ? -17.717 13.006  24.583 1.00 93.32  ? 598 TYR   A OH  1 
ATOM   2347 N  N   . CYS   A 1 303 ? -15.382 9.075   32.203 1.00 81.79  ? 599 CYS   A N   1 
ATOM   2348 C  CA  . CYS   A 1 303 ? -14.924 9.176   33.589 1.00 89.91  ? 599 CYS   A CA  1 
ATOM   2349 C  C   . CYS   A 1 303 ? -14.309 7.907   34.159 1.00 85.37  ? 599 CYS   A C   1 
ATOM   2350 O  O   . CYS   A 1 303 ? -13.777 7.953   35.285 1.00 80.83  ? 599 CYS   A O   1 
ATOM   2351 C  CB  . CYS   A 1 303 ? -16.080 9.591   34.510 1.00 87.25  ? 599 CYS   A CB  1 
ATOM   2352 S  SG  . CYS   A 1 303 ? -16.803 11.183  34.136 1.00 92.14  ? 599 CYS   A SG  1 
ATOM   2353 N  N   . ASP   A 1 304 ? -14.416 6.777   33.458 1.00 82.29  ? 600 ASP   A N   1 
ATOM   2354 C  CA  . ASP   A 1 304 ? -13.575 5.623   33.750 1.00 92.56  ? 600 ASP   A CA  1 
ATOM   2355 C  C   . ASP   A 1 304 ? -12.135 6.079   33.899 1.00 95.78  ? 600 ASP   A C   1 
ATOM   2356 O  O   . ASP   A 1 304 ? -11.659 6.936   33.148 1.00 98.62  ? 600 ASP   A O   1 
ATOM   2357 C  CB  . ASP   A 1 304 ? -13.646 4.588   32.624 1.00 94.14  ? 600 ASP   A CB  1 
ATOM   2358 C  CG  . ASP   A 1 304 ? -14.344 3.307   33.021 1.00 93.13  ? 600 ASP   A CG  1 
ATOM   2359 O  OD1 . ASP   A 1 304 ? -15.255 3.361   33.876 1.00 97.94  ? 600 ASP   A OD1 1 
ATOM   2360 O  OD2 . ASP   A 1 304 ? -13.961 2.241   32.476 1.00 87.44  ? 600 ASP   A OD2 1 
ATOM   2361 N  N   . ASN   A 1 305 ? -11.437 5.501   34.871 1.00 92.40  ? 601 ASN   A N   1 
ATOM   2362 C  CA  . ASN   A 1 305 ? -10.076 5.948   35.136 1.00 96.35  ? 601 ASN   A CA  1 
ATOM   2363 C  C   . ASN   A 1 305 ? -9.130  5.570   34.007 1.00 91.14  ? 601 ASN   A C   1 
ATOM   2364 O  O   . ASN   A 1 305 ? -8.171  6.301   33.737 1.00 96.93  ? 601 ASN   A O   1 
ATOM   2365 C  CB  . ASN   A 1 305 ? -9.583  5.378   36.466 1.00 98.57  ? 601 ASN   A CB  1 
ATOM   2366 C  CG  . ASN   A 1 305 ? -9.787  6.335   37.614 1.00 108.13 ? 601 ASN   A CG  1 
ATOM   2367 O  OD1 . ASN   A 1 305 ? -9.807  7.551   37.421 1.00 113.99 ? 601 ASN   A OD1 1 
ATOM   2368 N  ND2 . ASN   A 1 305 ? -9.927  5.795   38.825 1.00 106.06 ? 601 ASN   A ND2 1 
ATOM   2369 N  N   . SER   A 1 306 ? -9.379  4.444   33.342 1.00 98.88  ? 602 SER   A N   1 
ATOM   2370 C  CA  . SER   A 1 306 ? -8.567  4.012   32.213 1.00 105.23 ? 602 SER   A CA  1 
ATOM   2371 C  C   . SER   A 1 306 ? -9.168  4.389   30.861 1.00 99.22  ? 602 SER   A C   1 
ATOM   2372 O  O   . SER   A 1 306 ? -8.686  3.907   29.832 1.00 97.08  ? 602 SER   A O   1 
ATOM   2373 C  CB  . SER   A 1 306 ? -8.328  2.501   32.273 1.00 107.77 ? 602 SER   A CB  1 
ATOM   2374 O  OG  . SER   A 1 306 ? -9.188  1.879   33.206 1.00 112.21 ? 602 SER   A OG  1 
ATOM   2375 N  N   . ARG   A 1 307 ? -10.185 5.239   30.829 1.00 92.34  ? 603 ARG   A N   1 
ATOM   2376 C  CA  . ARG   A 1 307 ? -10.732 5.765   29.577 1.00 91.78  ? 603 ARG   A CA  1 
ATOM   2377 C  C   . ARG   A 1 307 ? -10.397 7.251   29.491 1.00 92.30  ? 603 ARG   A C   1 
ATOM   2378 O  O   . ARG   A 1 307 ? -9.235  7.603   29.717 1.00 99.34  ? 603 ARG   A O   1 
ATOM   2379 C  CB  . ARG   A 1 307 ? -12.208 5.416   29.471 1.00 84.12  ? 603 ARG   A CB  1 
ATOM   2380 C  CG  . ARG   A 1 307 ? -12.466 3.917   29.566 1.00 83.26  ? 603 ARG   A CG  1 
ATOM   2381 C  CD  . ARG   A 1 307 ? -11.968 3.146   28.346 1.00 82.66  ? 603 ARG   A CD  1 
ATOM   2382 N  NE  . ARG   A 1 307 ? -12.495 3.721   27.114 1.00 76.05  ? 603 ARG   A NE  1 
ATOM   2383 C  CZ  . ARG   A 1 307 ? -13.782 3.732   26.792 1.00 76.70  ? 603 ARG   A CZ  1 
ATOM   2384 N  NH1 . ARG   A 1 307 ? -14.677 3.207   27.612 1.00 68.68  ? 603 ARG   A NH1 1 
ATOM   2385 N  NH2 . ARG   A 1 307 ? -14.181 4.288   25.650 1.00 84.83  ? 603 ARG   A NH2 1 
ATOM   2386 N  N   . TYR   A 1 308 ? -11.346 8.145   29.173 1.00 93.47  ? 604 TYR   A N   1 
ATOM   2387 C  CA  . TYR   A 1 308 ? -10.971 9.530   28.869 1.00 96.78  ? 604 TYR   A CA  1 
ATOM   2388 C  C   . TYR   A 1 308 ? -10.600 10.327  30.115 1.00 104.37 ? 604 TYR   A C   1 
ATOM   2389 O  O   . TYR   A 1 308 ? -9.850  11.307  30.001 1.00 103.17 ? 604 TYR   A O   1 
ATOM   2390 C  CB  . TYR   A 1 308 ? -12.089 10.239  28.100 1.00 90.33  ? 604 TYR   A CB  1 
ATOM   2391 C  CG  . TYR   A 1 308 ? -11.957 10.068  26.600 1.00 100.13 ? 604 TYR   A CG  1 
ATOM   2392 C  CD1 . TYR   A 1 308 ? -11.979 8.808   26.030 1.00 95.59  ? 604 TYR   A CD1 1 
ATOM   2393 C  CD2 . TYR   A 1 308 ? -11.792 11.162  25.759 1.00 108.52 ? 604 TYR   A CD2 1 
ATOM   2394 C  CE1 . TYR   A 1 308 ? -11.849 8.631   24.667 1.00 98.22  ? 604 TYR   A CE1 1 
ATOM   2395 C  CE2 . TYR   A 1 308 ? -11.654 11.000  24.380 1.00 110.72 ? 604 TYR   A CE2 1 
ATOM   2396 C  CZ  . TYR   A 1 308 ? -11.689 9.726   23.844 1.00 107.54 ? 604 TYR   A CZ  1 
ATOM   2397 O  OH  . TYR   A 1 308 ? -11.560 9.520   22.493 1.00 106.59 ? 604 TYR   A OH  1 
ATOM   2398 N  N   . ASN   A 1 309 ? -11.121 9.939   31.280 1.00 103.62 ? 605 ASN   A N   1 
ATOM   2399 C  CA  . ASN   A 1 309 ? -10.664 10.420  32.584 1.00 108.64 ? 605 ASN   A CA  1 
ATOM   2400 C  C   . ASN   A 1 309 ? -10.680 11.952  32.644 1.00 115.40 ? 605 ASN   A C   1 
ATOM   2401 O  O   . ASN   A 1 309 ? -9.649  12.627  32.717 1.00 119.50 ? 605 ASN   A O   1 
ATOM   2402 C  CB  . ASN   A 1 309 ? -9.275  9.851   32.884 1.00 107.83 ? 605 ASN   A CB  1 
ATOM   2403 C  CG  . ASN   A 1 309 ? -8.879  10.002  34.324 1.00 104.11 ? 605 ASN   A CG  1 
ATOM   2404 O  OD1 . ASN   A 1 309 ? -9.730  10.072  35.223 1.00 101.22 ? 605 ASN   A OD1 1 
ATOM   2405 N  ND2 . ASN   A 1 309 ? -7.571  10.059  34.562 1.00 104.88 ? 605 ASN   A ND2 1 
ATOM   2406 N  N   . ILE   A 1 310 ? -11.904 12.479  32.597 1.00 113.43 ? 606 ILE   A N   1 
ATOM   2407 C  CA  . ILE   A 1 310 ? -12.124 13.921  32.569 1.00 110.11 ? 606 ILE   A CA  1 
ATOM   2408 C  C   . ILE   A 1 310 ? -12.626 14.486  33.895 1.00 103.84 ? 606 ILE   A C   1 
ATOM   2409 O  O   . ILE   A 1 310 ? -12.717 15.718  34.015 1.00 105.15 ? 606 ILE   A O   1 
ATOM   2410 C  CB  . ILE   A 1 310 ? -13.086 14.333  31.432 1.00 107.58 ? 606 ILE   A CB  1 
ATOM   2411 C  CG1 . ILE   A 1 310 ? -14.491 13.780  31.675 1.00 98.52  ? 606 ILE   A CG1 1 
ATOM   2412 C  CG2 . ILE   A 1 310 ? -12.578 13.878  30.045 1.00 93.40  ? 606 ILE   A CG2 1 
ATOM   2413 C  CD1 . ILE   A 1 310 ? -15.495 14.293  30.678 1.00 98.57  ? 606 ILE   A CD1 1 
ATOM   2414 N  N   . LEU   A 1 311 ? -12.949 13.653  34.899 1.00 103.81 ? 607 LEU   A N   1 
ATOM   2415 C  CA  . LEU   A 1 311 ? -13.338 14.218  36.197 1.00 103.56 ? 607 LEU   A CA  1 
ATOM   2416 C  C   . LEU   A 1 311 ? -12.296 15.201  36.708 1.00 118.55 ? 607 LEU   A C   1 
ATOM   2417 O  O   . LEU   A 1 311 ? -12.638 16.167  37.400 1.00 120.39 ? 607 LEU   A O   1 
ATOM   2418 C  CB  . LEU   A 1 311 ? -13.581 13.121  37.248 1.00 89.67  ? 607 LEU   A CB  1 
ATOM   2419 C  CG  . LEU   A 1 311 ? -14.939 12.403  37.151 1.00 84.76  ? 607 LEU   A CG  1 
ATOM   2420 C  CD1 . LEU   A 1 311 ? -15.036 11.230  38.109 1.00 95.51  ? 607 LEU   A CD1 1 
ATOM   2421 C  CD2 . LEU   A 1 311 ? -16.101 13.368  37.378 1.00 86.53  ? 607 LEU   A CD2 1 
ATOM   2422 N  N   . GLU   A 1 312 ? -11.025 14.973  36.371 1.00 139.73 ? 608 GLU   A N   1 
ATOM   2423 C  CA  . GLU   A 1 312 ? -9.964  15.921  36.692 1.00 157.11 ? 608 GLU   A CA  1 
ATOM   2424 C  C   . GLU   A 1 312 ? -10.326 17.343  36.275 1.00 156.86 ? 608 GLU   A C   1 
ATOM   2425 O  O   . GLU   A 1 312 ? -10.302 18.272  37.090 1.00 154.31 ? 608 GLU   A O   1 
ATOM   2426 C  CB  . GLU   A 1 312 ? -8.668  15.483  36.006 1.00 170.20 ? 608 GLU   A CB  1 
ATOM   2427 C  CG  . GLU   A 1 312 ? -7.962  14.311  36.669 1.00 171.35 ? 608 GLU   A CG  1 
ATOM   2428 C  CD  . GLU   A 1 312 ? -7.159  14.728  37.891 1.00 177.27 ? 608 GLU   A CD  1 
ATOM   2429 O  OE1 . GLU   A 1 312 ? -7.620  15.611  38.645 1.00 179.91 ? 608 GLU   A OE1 1 
ATOM   2430 O  OE2 . GLU   A 1 312 ? -6.055  14.177  38.093 1.00 179.43 ? 608 GLU   A OE2 1 
ATOM   2431 N  N   . GLU   A 1 313 ? -10.671 17.526  34.998 1.00 149.50 ? 609 GLU   A N   1 
ATOM   2432 C  CA  . GLU   A 1 313 ? -10.830 18.869  34.446 1.00 154.05 ? 609 GLU   A CA  1 
ATOM   2433 C  C   . GLU   A 1 313 ? -12.201 19.457  34.742 1.00 147.48 ? 609 GLU   A C   1 
ATOM   2434 O  O   . GLU   A 1 313 ? -12.306 20.613  35.166 1.00 154.48 ? 609 GLU   A O   1 
ATOM   2435 C  CB  . GLU   A 1 313 ? -10.578 18.856  32.941 1.00 159.62 ? 609 GLU   A CB  1 
ATOM   2436 C  CG  . GLU   A 1 313 ? -9.160  19.232  32.550 1.00 172.65 ? 609 GLU   A CG  1 
ATOM   2437 C  CD  . GLU   A 1 313 ? -8.750  20.613  33.051 1.00 185.34 ? 609 GLU   A CD  1 
ATOM   2438 O  OE1 . GLU   A 1 313 ? -8.436  20.753  34.253 1.00 187.17 ? 609 GLU   A OE1 1 
ATOM   2439 O  OE2 . GLU   A 1 313 ? -8.742  21.562  32.238 1.00 191.67 ? 609 GLU   A OE2 1 
ATOM   2440 N  N   . VAL   A 1 314 ? -13.265 18.691  34.498 1.00 136.62 ? 610 VAL   A N   1 
ATOM   2441 C  CA  . VAL   A 1 314 ? -14.611 19.197  34.749 1.00 126.46 ? 610 VAL   A CA  1 
ATOM   2442 C  C   . VAL   A 1 314 ? -14.756 19.678  36.190 1.00 124.53 ? 610 VAL   A C   1 
ATOM   2443 O  O   . VAL   A 1 314 ? -15.455 20.665  36.453 1.00 120.21 ? 610 VAL   A O   1 
ATOM   2444 C  CB  . VAL   A 1 314 ? -15.646 18.117  34.386 1.00 114.49 ? 610 VAL   A CB  1 
ATOM   2445 C  CG1 . VAL   A 1 314 ? -17.057 18.568  34.739 1.00 111.92 ? 610 VAL   A CG1 1 
ATOM   2446 C  CG2 . VAL   A 1 314 ? -15.536 17.784  32.885 1.00 105.24 ? 610 VAL   A CG2 1 
ATOM   2447 N  N   . ALA   A 1 315 ? -14.079 19.023  37.136 1.00 129.27 ? 611 ALA   A N   1 
ATOM   2448 C  CA  . ALA   A 1 315 ? -14.086 19.505  38.513 1.00 131.80 ? 611 ALA   A CA  1 
ATOM   2449 C  C   . ALA   A 1 315 ? -13.396 20.856  38.617 1.00 141.96 ? 611 ALA   A C   1 
ATOM   2450 O  O   . ALA   A 1 315 ? -13.911 21.780  39.255 1.00 143.42 ? 611 ALA   A O   1 
ATOM   2451 C  CB  . ALA   A 1 315 ? -13.409 18.492  39.430 1.00 130.49 ? 611 ALA   A CB  1 
ATOM   2452 N  N   . LYS   A 1 316 ? -12.215 20.978  38.007 1.00 148.86 ? 612 LYS   A N   1 
ATOM   2453 C  CA  . LYS   A 1 316 ? -11.470 22.230  38.050 1.00 153.39 ? 612 LYS   A CA  1 
ATOM   2454 C  C   . LYS   A 1 316 ? -12.328 23.390  37.561 1.00 152.02 ? 612 LYS   A C   1 
ATOM   2455 O  O   . LYS   A 1 316 ? -12.542 24.375  38.281 1.00 154.04 ? 612 LYS   A O   1 
ATOM   2456 C  CB  . LYS   A 1 316 ? -10.194 22.106  37.212 1.00 151.14 ? 612 LYS   A CB  1 
ATOM   2457 C  CG  . LYS   A 1 316 ? -9.095  21.284  37.869 1.00 150.64 ? 612 LYS   A CG  1 
ATOM   2458 C  CD  . LYS   A 1 316 ? -7.754  21.542  37.205 1.00 158.06 ? 612 LYS   A CD  1 
ATOM   2459 C  CE  . LYS   A 1 316 ? -7.453  23.039  37.133 1.00 171.66 ? 612 LYS   A CE  1 
ATOM   2460 N  NZ  . LYS   A 1 316 ? -6.294  23.367  36.242 1.00 179.41 ? 612 LYS   A NZ  1 
ATOM   2461 N  N   . LYS   A 1 317 ? -12.866 23.260  36.347 1.00 136.31 ? 613 LYS   A N   1 
ATOM   2462 C  CA  . LYS   A 1 317 ? -13.572 24.342  35.664 1.00 146.29 ? 613 LYS   A CA  1 
ATOM   2463 C  C   . LYS   A 1 317 ? -14.908 24.647  36.336 1.00 140.51 ? 613 LYS   A C   1 
ATOM   2464 O  O   . LYS   A 1 317 ? -15.616 25.575  35.929 1.00 148.77 ? 613 LYS   A O   1 
ATOM   2465 C  CB  . LYS   A 1 317 ? -13.778 23.995  34.181 1.00 137.17 ? 613 LYS   A CB  1 
ATOM   2466 C  CG  . LYS   A 1 317 ? -12.775 24.664  33.256 1.00 142.53 ? 613 LYS   A CG  1 
ATOM   2467 C  CD  . LYS   A 1 317 ? -12.414 23.779  32.083 1.00 138.42 ? 613 LYS   A CD  1 
ATOM   2468 C  CE  . LYS   A 1 317 ? -11.058 24.159  31.513 1.00 144.47 ? 613 LYS   A CE  1 
ATOM   2469 N  NZ  . LYS   A 1 317 ? -10.347 22.984  30.924 1.00 143.83 ? 613 LYS   A NZ  1 
ATOM   2470 N  N   . MET   A 1 318 ? -15.260 23.873  37.354 1.00 142.22 ? 614 MET   A N   1 
ATOM   2471 C  CA  . MET   A 1 318 ? -16.366 24.237  38.229 1.00 144.52 ? 614 MET   A CA  1 
ATOM   2472 C  C   . MET   A 1 318 ? -15.898 24.874  39.526 1.00 153.26 ? 614 MET   A C   1 
ATOM   2473 O  O   . MET   A 1 318 ? -16.732 25.375  40.285 1.00 157.38 ? 614 MET   A O   1 
ATOM   2474 C  CB  . MET   A 1 318 ? -17.233 23.014  38.538 1.00 132.24 ? 614 MET   A CB  1 
ATOM   2475 C  CG  . MET   A 1 318 ? -17.938 22.438  37.314 1.00 138.28 ? 614 MET   A CG  1 
ATOM   2476 S  SD  . MET   A 1 318 ? -18.823 20.904  37.688 1.00 131.60 ? 614 MET   A SD  1 
ATOM   2477 C  CE  . MET   A 1 318 ? -19.971 21.470  38.951 1.00 134.15 ? 614 MET   A CE  1 
ATOM   2478 N  N   . ASP   A 1 319 ? -14.583 24.891  39.772 1.00 167.95 ? 615 ASP   A N   1 
ATOM   2479 C  CA  . ASP   A 1 319 ? -13.987 25.286  41.049 1.00 177.62 ? 615 ASP   A CA  1 
ATOM   2480 C  C   . ASP   A 1 319 ? -14.618 24.513  42.199 1.00 172.58 ? 615 ASP   A C   1 
ATOM   2481 O  O   . ASP   A 1 319 ? -15.472 25.036  42.924 1.00 174.04 ? 615 ASP   A O   1 
ATOM   2482 C  CB  . ASP   A 1 319 ? -14.108 26.794  41.285 1.00 191.53 ? 615 ASP   A CB  1 
ATOM   2483 C  CG  . ASP   A 1 319 ? -12.770 27.438  41.610 1.00 201.43 ? 615 ASP   A CG  1 
ATOM   2484 O  OD1 . ASP   A 1 319 ? -11.727 26.820  41.309 1.00 200.33 ? 615 ASP   A OD1 1 
ATOM   2485 O  OD2 . ASP   A 1 319 ? -12.761 28.554  42.172 1.00 209.96 ? 615 ASP   A OD2 1 
ATOM   2486 N  N   . LEU   A 1 320 ? -14.200 23.265  42.368 1.00 165.90 ? 616 LEU   A N   1 
ATOM   2487 C  CA  . LEU   A 1 320 ? -14.710 22.394  43.411 1.00 153.53 ? 616 LEU   A CA  1 
ATOM   2488 C  C   . LEU   A 1 320 ? -13.608 22.092  44.414 1.00 154.20 ? 616 LEU   A C   1 
ATOM   2489 O  O   . LEU   A 1 320 ? -12.419 22.119  44.076 1.00 159.97 ? 616 LEU   A O   1 
ATOM   2490 C  CB  . LEU   A 1 320 ? -15.256 21.084  42.821 1.00 139.42 ? 616 LEU   A CB  1 
ATOM   2491 C  CG  . LEU   A 1 320 ? -16.531 21.224  41.992 1.00 136.25 ? 616 LEU   A CG  1 
ATOM   2492 C  CD1 . LEU   A 1 320 ? -17.085 19.854  41.617 1.00 132.74 ? 616 LEU   A CD1 1 
ATOM   2493 C  CD2 . LEU   A 1 320 ? -17.559 22.032  42.756 1.00 136.10 ? 616 LEU   A CD2 1 
ATOM   2494 N  N   . ASP   A 1 321 ? -14.020 21.816  45.655 1.00 141.50 ? 617 ASP   A N   1 
ATOM   2495 C  CA  . ASP   A 1 321 ? -13.109 21.387  46.708 1.00 144.56 ? 617 ASP   A CA  1 
ATOM   2496 C  C   . ASP   A 1 321 ? -12.486 20.046  46.339 1.00 133.88 ? 617 ASP   A C   1 
ATOM   2497 O  O   . ASP   A 1 321 ? -13.017 18.993  46.698 1.00 126.21 ? 617 ASP   A O   1 
ATOM   2498 C  CB  . ASP   A 1 321 ? -13.858 21.309  48.049 1.00 144.28 ? 617 ASP   A CB  1 
ATOM   2499 C  CG  . ASP   A 1 321 ? -12.935 21.068  49.234 1.00 154.55 ? 617 ASP   A CG  1 
ATOM   2500 O  OD1 . ASP   A 1 321 ? -13.332 20.339  50.172 1.00 153.13 ? 617 ASP   A OD1 1 
ATOM   2501 O  OD2 . ASP   A 1 321 ? -11.809 21.603  49.231 1.00 163.53 ? 617 ASP   A OD2 1 
ATOM   2502 N  N   . MET   A 1 322 ? -11.375 20.069  45.601 1.00 137.06 ? 618 MET   A N   1 
ATOM   2503 C  CA  . MET   A 1 322 ? -10.682 18.842  45.226 1.00 142.56 ? 618 MET   A CA  1 
ATOM   2504 C  C   . MET   A 1 322 ? -9.664  18.400  46.269 1.00 150.54 ? 618 MET   A C   1 
ATOM   2505 O  O   . MET   A 1 322 ? -9.115  17.298  46.154 1.00 146.98 ? 618 MET   A O   1 
ATOM   2506 C  CB  . MET   A 1 322 ? -9.999  19.006  43.854 1.00 146.81 ? 618 MET   A CB  1 
ATOM   2507 C  CG  . MET   A 1 322 ? -10.944 18.800  42.663 1.00 143.66 ? 618 MET   A CG  1 
ATOM   2508 S  SD  . MET   A 1 322 ? -10.226 18.962  41.008 1.00 149.58 ? 618 MET   A SD  1 
ATOM   2509 C  CE  . MET   A 1 322 ? -8.997  17.655  40.998 1.00 148.54 ? 618 MET   A CE  1 
ATOM   2510 N  N   . ARG   A 1 323 ? -9.418  19.219  47.292 1.00 160.22 ? 619 ARG   A N   1 
ATOM   2511 C  CA  . ARG   A 1 323 ? -8.477  18.838  48.338 1.00 169.01 ? 619 ARG   A CA  1 
ATOM   2512 C  C   . ARG   A 1 323 ? -8.992  17.647  49.140 1.00 166.08 ? 619 ARG   A C   1 
ATOM   2513 O  O   . ARG   A 1 323 ? -8.212  16.774  49.536 1.00 167.32 ? 619 ARG   A O   1 
ATOM   2514 C  CB  . ARG   A 1 323 ? -8.210  20.033  49.255 1.00 177.60 ? 619 ARG   A CB  1 
ATOM   2515 C  CG  . ARG   A 1 323 ? -7.574  21.225  48.557 1.00 187.27 ? 619 ARG   A CG  1 
ATOM   2516 C  CD  . ARG   A 1 323 ? -7.997  22.539  49.199 1.00 197.70 ? 619 ARG   A CD  1 
ATOM   2517 N  NE  . ARG   A 1 323 ? -9.409  22.829  48.964 1.00 199.65 ? 619 ARG   A NE  1 
ATOM   2518 C  CZ  . ARG   A 1 323 ? -10.000 23.981  49.268 1.00 206.89 ? 619 ARG   A CZ  1 
ATOM   2519 N  NH1 . ARG   A 1 323 ? -9.305  24.962  49.825 1.00 214.11 ? 619 ARG   A NH1 1 
ATOM   2520 N  NH2 . ARG   A 1 323 ? -11.290 24.151  49.012 1.00 206.44 ? 619 ARG   A NH2 1 
ATOM   2521 N  N   . LYS   A 1 324 ? -10.300 17.586  49.375 1.00 158.87 ? 620 LYS   A N   1 
ATOM   2522 C  CA  . LYS   A 1 324 ? -10.903 16.594  50.256 1.00 145.62 ? 620 LYS   A CA  1 
ATOM   2523 C  C   . LYS   A 1 324 ? -11.675 15.568  49.436 1.00 137.79 ? 620 LYS   A C   1 
ATOM   2524 O  O   . LYS   A 1 324 ? -12.480 15.933  48.574 1.00 140.33 ? 620 LYS   A O   1 
ATOM   2525 C  CB  . LYS   A 1 324 ? -11.826 17.266  51.279 1.00 142.50 ? 620 LYS   A CB  1 
ATOM   2526 C  CG  . LYS   A 1 324 ? -11.135 17.699  52.571 1.00 144.57 ? 620 LYS   A CG  1 
ATOM   2527 C  CD  . LYS   A 1 324 ? -10.036 18.725  52.334 1.00 152.03 ? 620 LYS   A CD  1 
ATOM   2528 C  CE  . LYS   A 1 324 ? -9.154  18.878  53.559 1.00 153.78 ? 620 LYS   A CE  1 
ATOM   2529 N  NZ  . LYS   A 1 324 ? -8.004  19.783  53.302 1.00 161.25 ? 620 LYS   A NZ  1 
ATOM   2530 N  N   . THR   A 1 325 ? -11.422 14.287  49.708 1.00 126.87 ? 621 THR   A N   1 
ATOM   2531 C  CA  . THR   A 1 325 ? -12.122 13.207  49.014 1.00 109.41 ? 621 THR   A CA  1 
ATOM   2532 C  C   . THR   A 1 325 ? -13.629 13.261  49.254 1.00 106.26 ? 621 THR   A C   1 
ATOM   2533 O  O   . THR   A 1 325 ? -14.424 12.963  48.353 1.00 94.48  ? 621 THR   A O   1 
ATOM   2534 C  CB  . THR   A 1 325 ? -11.562 11.855  49.471 1.00 112.04 ? 621 THR   A CB  1 
ATOM   2535 O  OG1 . THR   A 1 325 ? -12.476 10.807  49.125 1.00 106.67 ? 621 THR   A OG1 1 
ATOM   2536 C  CG2 . THR   A 1 325 ? -11.318 11.842  51.009 1.00 122.41 ? 621 THR   A CG2 1 
ATOM   2537 N  N   . SER   A 1 326 ? -14.036 13.639  50.468 1.00 117.61 ? 622 SER   A N   1 
ATOM   2538 C  CA  . SER   A 1 326 ? -15.417 13.617  50.934 1.00 107.68 ? 622 SER   A CA  1 
ATOM   2539 C  C   . SER   A 1 326 ? -16.189 14.885  50.592 1.00 109.58 ? 622 SER   A C   1 
ATOM   2540 O  O   . SER   A 1 326 ? -17.285 15.091  51.124 1.00 101.21 ? 622 SER   A O   1 
ATOM   2541 C  CB  . SER   A 1 326 ? -15.436 13.407  52.448 1.00 104.73 ? 622 SER   A CB  1 
ATOM   2542 O  OG  . SER   A 1 326 ? -14.421 14.189  53.028 1.00 105.62 ? 622 SER   A OG  1 
ATOM   2543 N  N   . SER   A 1 327 ? -15.639 15.751  49.744 1.00 114.69 ? 623 SER   A N   1 
ATOM   2544 C  CA  . SER   A 1 327 ? -16.436 16.838  49.198 1.00 114.80 ? 623 SER   A CA  1 
ATOM   2545 C  C   . SER   A 1 327 ? -17.349 16.370  48.074 1.00 113.18 ? 623 SER   A C   1 
ATOM   2546 O  O   . SER   A 1 327 ? -18.147 17.172  47.576 1.00 111.13 ? 623 SER   A O   1 
ATOM   2547 C  CB  . SER   A 1 327 ? -15.527 17.968  48.696 1.00 123.57 ? 623 SER   A CB  1 
ATOM   2548 O  OG  . SER   A 1 327 ? -14.712 17.552  47.612 1.00 118.60 ? 623 SER   A OG  1 
ATOM   2549 N  N   . LEU   A 1 328 ? -17.255 15.096  47.683 1.00 107.76 ? 624 LEU   A N   1 
ATOM   2550 C  CA  . LEU   A 1 328 ? -17.985 14.536  46.535 1.00 104.93 ? 624 LEU   A CA  1 
ATOM   2551 C  C   . LEU   A 1 328 ? -17.845 15.413  45.291 1.00 104.18 ? 624 LEU   A C   1 
ATOM   2552 O  O   . LEU   A 1 328 ? -18.766 15.520  44.475 1.00 109.37 ? 624 LEU   A O   1 
ATOM   2553 C  CB  . LEU   A 1 328 ? -19.459 14.298  46.875 1.00 103.45 ? 624 LEU   A CB  1 
ATOM   2554 C  CG  . LEU   A 1 328 ? -19.683 13.473  48.153 1.00 101.02 ? 624 LEU   A CG  1 
ATOM   2555 C  CD1 . LEU   A 1 328 ? -21.132 13.014  48.275 1.00 85.77  ? 624 LEU   A CD1 1 
ATOM   2556 C  CD2 . LEU   A 1 328 ? -18.747 12.284  48.151 1.00 98.10  ? 624 LEU   A CD2 1 
ATOM   2557 N  N   . TRP   A 1 329 ? -16.667 16.022  45.126 1.00 99.41  ? 625 TRP   A N   1 
ATOM   2558 C  CA  . TRP   A 1 329 ? -16.411 16.760  43.897 1.00 109.55 ? 625 TRP   A CA  1 
ATOM   2559 C  C   . TRP   A 1 329 ? -16.536 15.853  42.679 1.00 108.60 ? 625 TRP   A C   1 
ATOM   2560 O  O   . TRP   A 1 329 ? -17.053 16.278  41.641 1.00 104.24 ? 625 TRP   A O   1 
ATOM   2561 C  CB  . TRP   A 1 329 ? -15.032 17.419  43.935 1.00 117.39 ? 625 TRP   A CB  1 
ATOM   2562 C  CG  . TRP   A 1 329 ? -13.875 16.476  44.074 1.00 112.83 ? 625 TRP   A CG  1 
ATOM   2563 C  CD1 . TRP   A 1 329 ? -13.343 16.012  45.233 1.00 118.78 ? 625 TRP   A CD1 1 
ATOM   2564 C  CD2 . TRP   A 1 329 ? -13.084 15.909  43.015 1.00 114.95 ? 625 TRP   A CD2 1 
ATOM   2565 N  NE1 . TRP   A 1 329 ? -12.280 15.182  44.972 1.00 119.08 ? 625 TRP   A NE1 1 
ATOM   2566 C  CE2 . TRP   A 1 329 ? -12.099 15.100  43.619 1.00 113.42 ? 625 TRP   A CE2 1 
ATOM   2567 C  CE3 . TRP   A 1 329 ? -13.122 15.996  41.614 1.00 111.72 ? 625 TRP   A CE3 1 
ATOM   2568 C  CZ2 . TRP   A 1 329 ? -11.158 14.384  42.874 1.00 111.44 ? 625 TRP   A CZ2 1 
ATOM   2569 C  CZ3 . TRP   A 1 329 ? -12.183 15.294  40.878 1.00 101.72 ? 625 TRP   A CZ3 1 
ATOM   2570 C  CH2 . TRP   A 1 329 ? -11.217 14.495  41.505 1.00 107.83 ? 625 TRP   A CH2 1 
ATOM   2571 N  N   . LYS   A 1 330 ? -16.075 14.600  42.790 1.00 112.79 ? 626 LYS   A N   1 
ATOM   2572 C  CA  . LYS   A 1 330 ? -16.183 13.662  41.671 1.00 111.89 ? 626 LYS   A CA  1 
ATOM   2573 C  C   . LYS   A 1 330 ? -17.637 13.383  41.317 1.00 102.38 ? 626 LYS   A C   1 
ATOM   2574 O  O   . LYS   A 1 330 ? -17.995 13.330  40.136 1.00 103.50 ? 626 LYS   A O   1 
ATOM   2575 C  CB  . LYS   A 1 330 ? -15.474 12.344  41.998 1.00 114.28 ? 626 LYS   A CB  1 
ATOM   2576 C  CG  . LYS   A 1 330 ? -13.960 12.354  41.855 1.00 116.66 ? 626 LYS   A CG  1 
ATOM   2577 C  CD  . LYS   A 1 330 ? -13.382 10.952  42.007 1.00 108.93 ? 626 LYS   A CD  1 
ATOM   2578 C  CE  . LYS   A 1 330 ? -11.865 10.953  41.889 1.00 107.95 ? 626 LYS   A CE  1 
ATOM   2579 N  NZ  . LYS   A 1 330 ? -11.293 9.579   41.955 1.00 103.71 ? 626 LYS   A NZ  1 
ATOM   2580 N  N   . ASP   A 1 331 ? -18.483 13.178  42.326 1.00 104.55 ? 627 ASP   A N   1 
ATOM   2581 C  CA  . ASP   A 1 331 ? -19.899 12.940  42.068 1.00 100.57 ? 627 ASP   A CA  1 
ATOM   2582 C  C   . ASP   A 1 331 ? -20.526 14.139  41.388 1.00 101.07 ? 627 ASP   A C   1 
ATOM   2583 O  O   . ASP   A 1 331 ? -21.229 14.003  40.376 1.00 100.59 ? 627 ASP   A O   1 
ATOM   2584 C  CB  . ASP   A 1 331 ? -20.633 12.639  43.371 1.00 95.81  ? 627 ASP   A CB  1 
ATOM   2585 C  CG  . ASP   A 1 331 ? -20.073 11.428  44.079 1.00 98.08  ? 627 ASP   A CG  1 
ATOM   2586 O  OD1 . ASP   A 1 331 ? -18.872 11.448  44.402 1.00 96.85  ? 627 ASP   A OD1 1 
ATOM   2587 O  OD2 . ASP   A 1 331 ? -20.823 10.453  44.296 1.00 97.00  ? 627 ASP   A OD2 1 
ATOM   2588 N  N   . GLN   A 1 332 ? -20.273 15.330  41.933 1.00 97.78  ? 628 GLN   A N   1 
ATOM   2589 C  CA  . GLN   A 1 332 ? -20.879 16.541  41.388 1.00 111.51 ? 628 GLN   A CA  1 
ATOM   2590 C  C   . GLN   A 1 332 ? -20.466 16.777  39.938 1.00 103.79 ? 628 GLN   A C   1 
ATOM   2591 O  O   . GLN   A 1 332 ? -21.307 17.126  39.096 1.00 102.38 ? 628 GLN   A O   1 
ATOM   2592 C  CB  . GLN   A 1 332 ? -20.517 17.737  42.273 1.00 121.48 ? 628 GLN   A CB  1 
ATOM   2593 C  CG  . GLN   A 1 332 ? -21.687 18.642  42.567 1.00 124.71 ? 628 GLN   A CG  1 
ATOM   2594 C  CD  . GLN   A 1 332 ? -21.444 19.550  43.756 1.00 129.66 ? 628 GLN   A CD  1 
ATOM   2595 O  OE1 . GLN   A 1 332 ? -20.341 19.608  44.302 1.00 128.32 ? 628 GLN   A OE1 1 
ATOM   2596 N  NE2 . GLN   A 1 332 ? -22.483 20.259  44.169 1.00 139.86 ? 628 GLN   A NE2 1 
ATOM   2597 N  N   . ALA   A 1 333 ? -19.181 16.586  39.614 1.00 100.93 ? 629 ALA   A N   1 
ATOM   2598 C  CA  . ALA   A 1 333 ? -18.747 16.768  38.228 1.00 102.28 ? 629 ALA   A CA  1 
ATOM   2599 C  C   . ALA   A 1 333 ? -19.311 15.692  37.314 1.00 108.62 ? 629 ALA   A C   1 
ATOM   2600 O  O   . ALA   A 1 333 ? -19.401 15.903  36.089 1.00 110.87 ? 629 ALA   A O   1 
ATOM   2601 C  CB  . ALA   A 1 333 ? -17.224 16.777  38.125 1.00 104.22 ? 629 ALA   A CB  1 
ATOM   2602 N  N   . LEU   A 1 334 ? -19.695 14.548  37.883 1.00 92.31  ? 630 LEU   A N   1 
ATOM   2603 C  CA  . LEU   A 1 334 ? -20.243 13.464  37.076 1.00 89.36  ? 630 LEU   A CA  1 
ATOM   2604 C  C   . LEU   A 1 334 ? -21.646 13.794  36.580 1.00 93.47  ? 630 LEU   A C   1 
ATOM   2605 O  O   . LEU   A 1 334 ? -21.971 13.541  35.411 1.00 108.85 ? 630 LEU   A O   1 
ATOM   2606 C  CB  . LEU   A 1 334 ? -20.258 12.174  37.899 1.00 87.18  ? 630 LEU   A CB  1 
ATOM   2607 C  CG  . LEU   A 1 334 ? -20.638 10.937  37.087 1.00 90.36  ? 630 LEU   A CG  1 
ATOM   2608 C  CD1 . LEU   A 1 334 ? -19.434 10.434  36.338 1.00 88.77  ? 630 LEU   A CD1 1 
ATOM   2609 C  CD2 . LEU   A 1 334 ? -21.211 9.844   37.985 1.00 83.36  ? 630 LEU   A CD2 1 
ATOM   2610 N  N   . VAL   A 1 335 ? -22.486 14.371  37.448 1.00 94.72  ? 631 VAL   A N   1 
ATOM   2611 C  CA  . VAL   A 1 335 ? -23.861 14.691  37.069 1.00 103.50 ? 631 VAL   A CA  1 
ATOM   2612 C  C   . VAL   A 1 335 ? -23.897 15.755  35.970 1.00 107.58 ? 631 VAL   A C   1 
ATOM   2613 O  O   . VAL   A 1 335 ? -24.688 15.649  35.019 1.00 105.20 ? 631 VAL   A O   1 
ATOM   2614 C  CB  . VAL   A 1 335 ? -24.685 15.124  38.295 1.00 110.17 ? 631 VAL   A CB  1 
ATOM   2615 C  CG1 . VAL   A 1 335 ? -26.018 15.703  37.843 1.00 112.69 ? 631 VAL   A CG1 1 
ATOM   2616 C  CG2 . VAL   A 1 335 ? -24.909 13.940  39.244 1.00 106.94 ? 631 VAL   A CG2 1 
ATOM   2617 N  N   . GLU   A 1 336 ? -23.048 16.788  36.066 1.00 106.93 ? 632 GLU   A N   1 
ATOM   2618 C  CA  . GLU   A 1 336 ? -23.016 17.804  35.008 1.00 115.71 ? 632 GLU   A CA  1 
ATOM   2619 C  C   . GLU   A 1 336 ? -22.693 17.183  33.654 1.00 108.15 ? 632 GLU   A C   1 
ATOM   2620 O  O   . GLU   A 1 336 ? -23.327 17.508  32.641 1.00 103.20 ? 632 GLU   A O   1 
ATOM   2621 C  CB  . GLU   A 1 336 ? -21.994 18.899  35.318 1.00 129.90 ? 632 GLU   A CB  1 
ATOM   2622 C  CG  . GLU   A 1 336 ? -21.840 19.257  36.777 1.00 138.21 ? 632 GLU   A CG  1 
ATOM   2623 C  CD  . GLU   A 1 336 ? -23.061 19.936  37.351 1.00 150.04 ? 632 GLU   A CD  1 
ATOM   2624 O  OE1 . GLU   A 1 336 ? -23.867 20.473  36.556 1.00 157.31 ? 632 GLU   A OE1 1 
ATOM   2625 O  OE2 . GLU   A 1 336 ? -23.209 19.927  38.597 1.00 152.87 ? 632 GLU   A OE2 1 
ATOM   2626 N  N   . ILE   A 1 337 ? -21.700 16.289  33.617 1.00 107.15 ? 633 ILE   A N   1 
ATOM   2627 C  CA  . ILE   A 1 337 ? -21.243 15.715  32.351 1.00 104.18 ? 633 ILE   A CA  1 
ATOM   2628 C  C   . ILE   A 1 337 ? -22.368 14.948  31.666 1.00 105.91 ? 633 ILE   A C   1 
ATOM   2629 O  O   . ILE   A 1 337 ? -22.545 15.035  30.442 1.00 110.53 ? 633 ILE   A O   1 
ATOM   2630 C  CB  . ILE   A 1 337 ? -20.005 14.830  32.593 1.00 92.84  ? 633 ILE   A CB  1 
ATOM   2631 C  CG1 . ILE   A 1 337 ? -18.773 15.699  32.881 1.00 96.73  ? 633 ILE   A CG1 1 
ATOM   2632 C  CG2 . ILE   A 1 337 ? -19.719 13.917  31.428 1.00 101.87 ? 633 ILE   A CG2 1 
ATOM   2633 C  CD1 . ILE   A 1 337 ? -17.615 14.911  33.500 1.00 100.93 ? 633 ILE   A CD1 1 
ATOM   2634 N  N   . ASN   A 1 338 ? -23.154 14.200  32.439 1.00 101.15 ? 634 ASN   A N   1 
ATOM   2635 C  CA  . ASN   A 1 338 ? -24.245 13.415  31.871 1.00 91.79  ? 634 ASN   A CA  1 
ATOM   2636 C  C   . ASN   A 1 338 ? -25.457 14.274  31.511 1.00 98.11  ? 634 ASN   A C   1 
ATOM   2637 O  O   . ASN   A 1 338 ? -26.191 13.922  30.580 1.00 96.61  ? 634 ASN   A O   1 
ATOM   2638 C  CB  . ASN   A 1 338 ? -24.641 12.290  32.838 1.00 89.90  ? 634 ASN   A CB  1 
ATOM   2639 C  CG  . ASN   A 1 338 ? -23.607 11.178  32.882 1.00 84.75  ? 634 ASN   A CG  1 
ATOM   2640 O  OD1 . ASN   A 1 338 ? -23.681 10.197  32.135 1.00 83.80  ? 634 ASN   A OD1 1 
ATOM   2641 N  ND2 . ASN   A 1 338 ? -22.623 11.337  33.744 1.00 78.08  ? 634 ASN   A ND2 1 
ATOM   2642 N  N   . ILE   A 1 339 ? -25.693 15.393  32.215 1.00 98.62  ? 635 ILE   A N   1 
ATOM   2643 C  CA  . ILE   A 1 339 ? -26.710 16.334  31.743 1.00 96.83  ? 635 ILE   A CA  1 
ATOM   2644 C  C   . ILE   A 1 339 ? -26.300 16.896  30.391 1.00 98.39  ? 635 ILE   A C   1 
ATOM   2645 O  O   . ILE   A 1 339 ? -27.153 17.125  29.526 1.00 100.65 ? 635 ILE   A O   1 
ATOM   2646 C  CB  . ILE   A 1 339 ? -26.962 17.475  32.751 1.00 96.56  ? 635 ILE   A CB  1 
ATOM   2647 C  CG1 . ILE   A 1 339 ? -27.589 16.951  34.038 1.00 93.95  ? 635 ILE   A CG1 1 
ATOM   2648 C  CG2 . ILE   A 1 339 ? -27.908 18.529  32.160 1.00 101.94 ? 635 ILE   A CG2 1 
ATOM   2649 C  CD1 . ILE   A 1 339 ? -27.820 18.032  35.042 1.00 106.11 ? 635 ILE   A CD1 1 
ATOM   2650 N  N   . ALA   A 1 340 ? -24.989 17.064  30.172 1.00 98.34  ? 636 ALA   A N   1 
ATOM   2651 C  CA  . ALA   A 1 340 ? -24.447 17.662  28.954 1.00 107.11 ? 636 ALA   A CA  1 
ATOM   2652 C  C   . ALA   A 1 340 ? -24.434 16.687  27.772 1.00 109.19 ? 636 ALA   A C   1 
ATOM   2653 O  O   . ALA   A 1 340 ? -24.777 17.064  26.643 1.00 98.45  ? 636 ALA   A O   1 
ATOM   2654 C  CB  . ALA   A 1 340 ? -23.035 18.179  29.233 1.00 108.06 ? 636 ALA   A CB  1 
ATOM   2655 N  N   . VAL   A 1 341 ? -23.992 15.445  27.993 1.00 110.29 ? 637 VAL   A N   1 
ATOM   2656 C  CA  . VAL   A 1 341 ? -24.059 14.448  26.928 1.00 99.78  ? 637 VAL   A CA  1 
ATOM   2657 C  C   . VAL   A 1 341 ? -25.491 14.325  26.436 1.00 103.76 ? 637 VAL   A C   1 
ATOM   2658 O  O   . VAL   A 1 341 ? -25.768 14.398  25.231 1.00 113.66 ? 637 VAL   A O   1 
ATOM   2659 C  CB  . VAL   A 1 341 ? -23.520 13.088  27.406 1.00 95.12  ? 637 VAL   A CB  1 
ATOM   2660 C  CG1 . VAL   A 1 341 ? -23.972 11.985  26.434 1.00 94.26  ? 637 VAL   A CG1 1 
ATOM   2661 C  CG2 . VAL   A 1 341 ? -22.011 13.107  27.484 1.00 96.85  ? 637 VAL   A CG2 1 
ATOM   2662 N  N   . LEU   A 1 342 ? -26.426 14.142  27.373 1.00 94.71  ? 638 LEU   A N   1 
ATOM   2663 C  CA  . LEU   A 1 342 ? -27.836 14.070  27.016 1.00 93.02  ? 638 LEU   A CA  1 
ATOM   2664 C  C   . LEU   A 1 342 ? -28.265 15.317  26.258 1.00 99.38  ? 638 LEU   A C   1 
ATOM   2665 O  O   . LEU   A 1 342 ? -28.744 15.232  25.118 1.00 95.94  ? 638 LEU   A O   1 
ATOM   2666 C  CB  . LEU   A 1 342 ? -28.692 13.892  28.266 1.00 95.45  ? 638 LEU   A CB  1 
ATOM   2667 C  CG  . LEU   A 1 342 ? -28.549 12.586  29.041 1.00 87.47  ? 638 LEU   A CG  1 
ATOM   2668 C  CD1 . LEU   A 1 342 ? -29.547 12.559  30.185 1.00 84.73  ? 638 LEU   A CD1 1 
ATOM   2669 C  CD2 . LEU   A 1 342 ? -28.768 11.439  28.117 1.00 82.83  ? 638 LEU   A CD2 1 
ATOM   2670 N  N   . TYR   A 1 343 ? -28.077 16.493  26.878 1.00 98.52  ? 639 TYR   A N   1 
ATOM   2671 C  CA  . TYR   A 1 343 ? -28.524 17.742  26.261 1.00 114.70 ? 639 TYR   A CA  1 
ATOM   2672 C  C   . TYR   A 1 343 ? -28.026 17.880  24.826 1.00 109.88 ? 639 TYR   A C   1 
ATOM   2673 O  O   . TYR   A 1 343 ? -28.777 18.305  23.938 1.00 120.15 ? 639 TYR   A O   1 
ATOM   2674 C  CB  . TYR   A 1 343 ? -28.065 18.943  27.097 1.00 124.92 ? 639 TYR   A CB  1 
ATOM   2675 C  CG  . TYR   A 1 343 ? -28.371 20.263  26.416 1.00 126.20 ? 639 TYR   A CG  1 
ATOM   2676 C  CD1 . TYR   A 1 343 ? -29.678 20.727  26.323 1.00 127.77 ? 639 TYR   A CD1 1 
ATOM   2677 C  CD2 . TYR   A 1 343 ? -27.363 21.028  25.846 1.00 129.03 ? 639 TYR   A CD2 1 
ATOM   2678 C  CE1 . TYR   A 1 343 ? -29.972 21.914  25.697 1.00 136.70 ? 639 TYR   A CE1 1 
ATOM   2679 C  CE2 . TYR   A 1 343 ? -27.649 22.224  25.210 1.00 139.88 ? 639 TYR   A CE2 1 
ATOM   2680 C  CZ  . TYR   A 1 343 ? -28.956 22.661  25.137 1.00 145.59 ? 639 TYR   A CZ  1 
ATOM   2681 O  OH  . TYR   A 1 343 ? -29.254 23.849  24.505 1.00 155.48 ? 639 TYR   A OH  1 
ATOM   2682 N  N   . SER   A 1 344 ? -26.769 17.504  24.573 1.00 100.49 ? 640 SER   A N   1 
ATOM   2683 C  CA  . SER   A 1 344 ? -26.182 17.706  23.248 1.00 98.73  ? 640 SER   A CA  1 
ATOM   2684 C  C   . SER   A 1 344 ? -26.840 16.806  22.212 1.00 95.39  ? 640 SER   A C   1 
ATOM   2685 O  O   . SER   A 1 344 ? -27.170 17.249  21.095 1.00 94.33  ? 640 SER   A O   1 
ATOM   2686 C  CB  . SER   A 1 344 ? -24.678 17.441  23.305 1.00 100.13 ? 640 SER   A CB  1 
ATOM   2687 O  OG  . SER   A 1 344 ? -24.071 18.253  24.300 1.00 106.86 ? 640 SER   A OG  1 
ATOM   2688 N  N   . PHE   A 1 345 ? -27.010 15.528  22.559 1.00 97.81  ? 641 PHE   A N   1 
ATOM   2689 C  CA  . PHE   A 1 345 ? -27.622 14.559  21.655 1.00 100.81 ? 641 PHE   A CA  1 
ATOM   2690 C  C   . PHE   A 1 345 ? -29.065 14.945  21.319 1.00 109.78 ? 641 PHE   A C   1 
ATOM   2691 O  O   . PHE   A 1 345 ? -29.495 14.816  20.168 1.00 109.64 ? 641 PHE   A O   1 
ATOM   2692 C  CB  . PHE   A 1 345 ? -27.569 13.152  22.278 1.00 94.21  ? 641 PHE   A CB  1 
ATOM   2693 C  CG  . PHE   A 1 345 ? -26.283 12.371  22.000 1.00 83.06  ? 641 PHE   A CG  1 
ATOM   2694 C  CD1 . PHE   A 1 345 ? -25.069 12.755  22.560 1.00 83.50  ? 641 PHE   A CD1 1 
ATOM   2695 C  CD2 . PHE   A 1 345 ? -26.312 11.214  21.202 1.00 83.08  ? 641 PHE   A CD2 1 
ATOM   2696 C  CE1 . PHE   A 1 345 ? -23.899 12.016  22.321 1.00 83.67  ? 641 PHE   A CE1 1 
ATOM   2697 C  CE2 . PHE   A 1 345 ? -25.147 10.472  20.958 1.00 74.79  ? 641 PHE   A CE2 1 
ATOM   2698 C  CZ  . PHE   A 1 345 ? -23.940 10.878  21.514 1.00 80.97  ? 641 PHE   A CZ  1 
ATOM   2699 N  N   . GLN   A 1 346 ? -29.827 15.428  22.309 1.00 108.13 ? 642 GLN   A N   1 
ATOM   2700 C  CA  . GLN   A 1 346 ? -31.239 15.736  22.076 1.00 110.79 ? 642 GLN   A CA  1 
ATOM   2701 C  C   . GLN   A 1 346 ? -31.417 16.978  21.212 1.00 110.06 ? 642 GLN   A C   1 
ATOM   2702 O  O   . GLN   A 1 346 ? -32.337 17.039  20.391 1.00 106.00 ? 642 GLN   A O   1 
ATOM   2703 C  CB  . GLN   A 1 346 ? -31.970 15.942  23.395 1.00 112.14 ? 642 GLN   A CB  1 
ATOM   2704 C  CG  . GLN   A 1 346 ? -31.855 14.791  24.365 1.00 114.85 ? 642 GLN   A CG  1 
ATOM   2705 C  CD  . GLN   A 1 346 ? -32.194 15.220  25.772 1.00 120.74 ? 642 GLN   A CD  1 
ATOM   2706 O  OE1 . GLN   A 1 346 ? -31.326 15.658  26.520 1.00 128.24 ? 642 GLN   A OE1 1 
ATOM   2707 N  NE2 . GLN   A 1 346 ? -33.467 15.127  26.130 1.00 120.47 ? 642 GLN   A NE2 1 
ATOM   2708 N  N   . SER   A 1 347 ? -30.596 18.005  21.433 1.00 110.60 ? 643 SER   A N   1 
ATOM   2709 C  CA  . SER   A 1 347 ? -30.722 19.232  20.661 1.00 115.29 ? 643 SER   A CA  1 
ATOM   2710 C  C   . SER   A 1 347 ? -30.285 19.044  19.213 1.00 116.73 ? 643 SER   A C   1 
ATOM   2711 O  O   . SER   A 1 347 ? -30.388 19.985  18.417 1.00 114.38 ? 643 SER   A O   1 
ATOM   2712 C  CB  . SER   A 1 347 ? -29.917 20.361  21.322 1.00 114.96 ? 643 SER   A CB  1 
ATOM   2713 O  OG  . SER   A 1 347 ? -30.355 20.664  22.654 1.00 119.31 ? 643 SER   A OG  1 
ATOM   2714 N  N   . ASP   A 1 348 ? -29.799 17.850  18.870 1.00 117.47 ? 644 ASP   A N   1 
ATOM   2715 C  CA  . ASP   A 1 348 ? -29.374 17.495  17.524 1.00 122.15 ? 644 ASP   A CA  1 
ATOM   2716 C  C   . ASP   A 1 348 ? -30.268 16.440  16.888 1.00 121.33 ? 644 ASP   A C   1 
ATOM   2717 O  O   . ASP   A 1 348 ? -29.892 15.872  15.861 1.00 106.84 ? 644 ASP   A O   1 
ATOM   2718 C  CB  . ASP   A 1 348 ? -27.930 16.983  17.541 1.00 116.79 ? 644 ASP   A CB  1 
ATOM   2719 C  CG  . ASP   A 1 348 ? -26.908 18.084  17.765 1.00 115.74 ? 644 ASP   A CG  1 
ATOM   2720 O  OD1 . ASP   A 1 348 ? -27.301 19.267  17.918 1.00 115.93 ? 644 ASP   A OD1 1 
ATOM   2721 O  OD2 . ASP   A 1 348 ? -25.700 17.754  17.787 1.00 110.12 ? 644 ASP   A OD2 1 
ATOM   2722 N  N   . LYS   A 1 349 ? -31.419 16.140  17.495 1.00 132.45 ? 645 LYS   A N   1 
ATOM   2723 C  CA  . LYS   A 1 349 ? -32.331 15.099  17.010 1.00 135.99 ? 645 LYS   A CA  1 
ATOM   2724 C  C   . LYS   A 1 349 ? -31.625 13.750  16.869 1.00 121.40 ? 645 LYS   A C   1 
ATOM   2725 O  O   . LYS   A 1 349 ? -32.025 12.909  16.062 1.00 108.89 ? 645 LYS   A O   1 
ATOM   2726 C  CB  . LYS   A 1 349 ? -32.980 15.501  15.682 1.00 148.95 ? 645 LYS   A CB  1 
ATOM   2727 C  CG  . LYS   A 1 349 ? -34.440 15.081  15.539 1.00 156.03 ? 645 LYS   A CG  1 
ATOM   2728 C  CD  . LYS   A 1 349 ? -35.372 16.095  16.195 1.00 164.40 ? 645 LYS   A CD  1 
ATOM   2729 C  CE  . LYS   A 1 349 ? -36.821 15.617  16.211 1.00 165.20 ? 645 LYS   A CE  1 
ATOM   2730 N  NZ  . LYS   A 1 349 ? -37.053 14.549  17.227 1.00 159.61 ? 645 LYS   A NZ  1 
ATOM   2731 N  N   . VAL   A 1 350 ? -30.576 13.522  17.659 1.00 114.47 ? 646 VAL   A N   1 
ATOM   2732 C  CA  . VAL   A 1 350 ? -29.824 12.273  17.616 1.00 98.20  ? 646 VAL   A CA  1 
ATOM   2733 C  C   . VAL   A 1 350 ? -30.274 11.401  18.778 1.00 94.50  ? 646 VAL   A C   1 
ATOM   2734 O  O   . VAL   A 1 350 ? -30.133 11.784  19.949 1.00 99.86  ? 646 VAL   A O   1 
ATOM   2735 C  CB  . VAL   A 1 350 ? -28.309 12.515  17.653 1.00 85.15  ? 646 VAL   A CB  1 
ATOM   2736 C  CG1 . VAL   A 1 350 ? -27.578 11.168  17.618 1.00 78.11  ? 646 VAL   A CG1 1 
ATOM   2737 C  CG2 . VAL   A 1 350 ? -27.881 13.408  16.485 1.00 94.36  ? 646 VAL   A CG2 1 
ATOM   2738 N  N   . THR   A 1 351 ? -30.809 10.229  18.447 1.00 92.14  ? 647 THR   A N   1 
ATOM   2739 C  CA  . THR   A 1 351 ? -31.452 9.364   19.425 1.00 88.78  ? 647 THR   A CA  1 
ATOM   2740 C  C   . THR   A 1 351 ? -30.501 9.026   20.570 1.00 91.79  ? 647 THR   A C   1 
ATOM   2741 O  O   . THR   A 1 351 ? -29.342 8.663   20.348 1.00 94.43  ? 647 THR   A O   1 
ATOM   2742 C  CB  . THR   A 1 351 ? -31.941 8.078   18.737 1.00 82.01  ? 647 THR   A CB  1 
ATOM   2743 O  OG1 . THR   A 1 351 ? -32.794 8.405   17.634 1.00 87.53  ? 647 THR   A OG1 1 
ATOM   2744 C  CG2 . THR   A 1 351 ? -32.713 7.174   19.717 1.00 73.89  ? 647 THR   A CG2 1 
ATOM   2745 N  N   . ILE   A 1 352 ? -31.001 9.182   21.798 1.00 91.17  ? 648 ILE   A N   1 
ATOM   2746 C  CA  . ILE   A 1 352 ? -30.285 8.791   23.008 1.00 78.02  ? 648 ILE   A CA  1 
ATOM   2747 C  C   . ILE   A 1 352 ? -31.340 8.589   24.089 1.00 84.44  ? 648 ILE   A C   1 
ATOM   2748 O  O   . ILE   A 1 352 ? -32.448 9.124   24.000 1.00 85.72  ? 648 ILE   A O   1 
ATOM   2749 C  CB  . ILE   A 1 352 ? -29.239 9.855   23.433 1.00 83.35  ? 648 ILE   A CB  1 
ATOM   2750 C  CG1 . ILE   A 1 352 ? -28.297 9.313   24.529 1.00 75.16  ? 648 ILE   A CG1 1 
ATOM   2751 C  CG2 . ILE   A 1 352 ? -29.944 11.097  23.957 1.00 78.23  ? 648 ILE   A CG2 1 
ATOM   2752 C  CD1 . ILE   A 1 352 ? -26.996 10.102  24.650 1.00 82.07  ? 648 ILE   A CD1 1 
ATOM   2753 N  N   . VAL   A 1 353 ? -30.996 7.818   25.125 1.00 80.81  ? 649 VAL   A N   1 
ATOM   2754 C  CA  . VAL   A 1 353 ? -31.903 7.560   26.236 1.00 78.43  ? 649 VAL   A CA  1 
ATOM   2755 C  C   . VAL   A 1 353 ? -31.157 7.800   27.547 1.00 79.46  ? 649 VAL   A C   1 
ATOM   2756 O  O   . VAL   A 1 353 ? -29.987 7.422   27.689 1.00 71.74  ? 649 VAL   A O   1 
ATOM   2757 C  CB  . VAL   A 1 353 ? -32.489 6.129   26.173 1.00 77.77  ? 649 VAL   A CB  1 
ATOM   2758 C  CG1 . VAL   A 1 353 ? -31.389 5.071   26.273 1.00 72.30  ? 649 VAL   A CG1 1 
ATOM   2759 C  CG2 . VAL   A 1 353 ? -33.553 5.926   27.251 1.00 78.25  ? 649 VAL   A CG2 1 
ATOM   2760 N  N   . ASP   A 1 354 ? -31.824 8.471   28.485 1.00 81.01  ? 650 ASP   A N   1 
ATOM   2761 C  CA  . ASP   A 1 354 ? -31.272 8.694   29.806 1.00 83.94  ? 650 ASP   A CA  1 
ATOM   2762 C  C   . ASP   A 1 354 ? -31.458 7.428   30.637 1.00 79.92  ? 650 ASP   A C   1 
ATOM   2763 O  O   . ASP   A 1 354 ? -32.304 6.578   30.335 1.00 79.22  ? 650 ASP   A O   1 
ATOM   2764 C  CB  . ASP   A 1 354 ? -31.912 9.918   30.476 1.00 91.13  ? 650 ASP   A CB  1 
ATOM   2765 C  CG  . ASP   A 1 354 ? -33.354 9.680   30.932 1.00 98.00  ? 650 ASP   A CG  1 
ATOM   2766 O  OD1 . ASP   A 1 354 ? -34.272 10.364  30.439 1.00 100.40 ? 650 ASP   A OD1 1 
ATOM   2767 O  OD2 . ASP   A 1 354 ? -33.578 8.822   31.809 1.00 95.05  ? 650 ASP   A OD2 1 
ATOM   2768 N  N   . HIS   A 1 355 ? -30.650 7.293   31.689 1.00 75.21  ? 651 HIS   A N   1 
ATOM   2769 C  CA  . HIS   A 1 355 ? -30.631 6.024   32.411 1.00 67.48  ? 651 HIS   A CA  1 
ATOM   2770 C  C   . HIS   A 1 355 ? -31.886 5.808   33.255 1.00 82.04  ? 651 HIS   A C   1 
ATOM   2771 O  O   . HIS   A 1 355 ? -32.135 4.677   33.691 1.00 86.82  ? 651 HIS   A O   1 
ATOM   2772 C  CB  . HIS   A 1 355 ? -29.371 5.948   33.269 1.00 72.79  ? 651 HIS   A CB  1 
ATOM   2773 C  CG  . HIS   A 1 355 ? -29.149 7.162   34.127 1.00 74.54  ? 651 HIS   A CG  1 
ATOM   2774 N  ND1 . HIS   A 1 355 ? -28.652 8.347   33.623 1.00 78.84  ? 651 HIS   A ND1 1 
ATOM   2775 C  CD2 . HIS   A 1 355 ? -29.349 7.372   35.451 1.00 79.95  ? 651 HIS   A CD2 1 
ATOM   2776 C  CE1 . HIS   A 1 355 ? -28.552 9.231   34.602 1.00 88.43  ? 651 HIS   A CE1 1 
ATOM   2777 N  NE2 . HIS   A 1 355 ? -28.985 8.672   35.717 1.00 77.77  ? 651 HIS   A NE2 1 
ATOM   2778 N  N   . HIS   A 1 356 ? -32.678 6.863   33.498 1.00 80.66  ? 652 HIS   A N   1 
ATOM   2779 C  CA  . HIS   A 1 356 ? -33.965 6.703   34.174 1.00 77.63  ? 652 HIS   A CA  1 
ATOM   2780 C  C   . HIS   A 1 356 ? -35.036 6.165   33.236 1.00 80.68  ? 652 HIS   A C   1 
ATOM   2781 O  O   . HIS   A 1 356 ? -35.772 5.237   33.591 1.00 82.46  ? 652 HIS   A O   1 
ATOM   2782 C  CB  . HIS   A 1 356 ? -34.416 8.030   34.778 1.00 85.56  ? 652 HIS   A CB  1 
ATOM   2783 C  CG  . HIS   A 1 356 ? -33.392 8.652   35.668 1.00 85.97  ? 652 HIS   A CG  1 
ATOM   2784 N  ND1 . HIS   A 1 356 ? -33.207 8.260   36.978 1.00 84.24  ? 652 HIS   A ND1 1 
ATOM   2785 C  CD2 . HIS   A 1 356 ? -32.486 9.627   35.431 1.00 86.66  ? 652 HIS   A CD2 1 
ATOM   2786 C  CE1 . HIS   A 1 356 ? -32.232 8.976   37.509 1.00 86.96  ? 652 HIS   A CE1 1 
ATOM   2787 N  NE2 . HIS   A 1 356 ? -31.779 9.813   36.591 1.00 88.71  ? 652 HIS   A NE2 1 
ATOM   2788 N  N   . SER   A 1 357 ? -35.134 6.734   32.024 1.00 81.04  ? 653 SER   A N   1 
ATOM   2789 C  CA  . SER   A 1 357 ? -36.113 6.236   31.069 1.00 85.94  ? 653 SER   A CA  1 
ATOM   2790 C  C   . SER   A 1 357 ? -35.770 4.825   30.621 1.00 71.91  ? 653 SER   A C   1 
ATOM   2791 O  O   . SER   A 1 357 ? -36.666 3.986   30.476 1.00 77.96  ? 653 SER   A O   1 
ATOM   2792 C  CB  . SER   A 1 357 ? -36.228 7.154   29.855 1.00 82.32  ? 653 SER   A CB  1 
ATOM   2793 O  OG  . SER   A 1 357 ? -37.445 6.850   29.215 1.00 89.66  ? 653 SER   A OG  1 
ATOM   2794 N  N   . ALA   A 1 358 ? -34.482 4.540   30.404 1.00 67.38  ? 654 ALA   A N   1 
ATOM   2795 C  CA  . ALA   A 1 358 ? -34.090 3.202   29.959 1.00 71.09  ? 654 ALA   A CA  1 
ATOM   2796 C  C   . ALA   A 1 358 ? -34.392 2.154   31.028 1.00 69.83  ? 654 ALA   A C   1 
ATOM   2797 O  O   . ALA   A 1 358 ? -34.924 1.076   30.723 1.00 59.01  ? 654 ALA   A O   1 
ATOM   2798 C  CB  . ALA   A 1 358 ? -32.603 3.181   29.573 1.00 70.04  ? 654 ALA   A CB  1 
ATOM   2799 N  N   . THR   A 1 359 ? -34.076 2.446   32.293 1.00 68.78  ? 655 THR   A N   1 
ATOM   2800 C  CA  . THR   A 1 359 ? -34.302 1.435   33.313 1.00 67.77  ? 655 THR   A CA  1 
ATOM   2801 C  C   . THR   A 1 359 ? -35.782 1.265   33.617 1.00 67.68  ? 655 THR   A C   1 
ATOM   2802 O  O   . THR   A 1 359 ? -36.223 0.151   33.918 1.00 66.31  ? 655 THR   A O   1 
ATOM   2803 C  CB  . THR   A 1 359 ? -33.520 1.776   34.571 1.00 66.83  ? 655 THR   A CB  1 
ATOM   2804 O  OG1 . THR   A 1 359 ? -33.831 3.115   34.982 1.00 66.73  ? 655 THR   A OG1 1 
ATOM   2805 C  CG2 . THR   A 1 359 ? -32.052 1.652   34.268 1.00 53.29  ? 655 THR   A CG2 1 
ATOM   2806 N  N   . GLU   A 1 360 ? -36.568 2.338   33.534 1.00 76.04  ? 656 GLU   A N   1 
ATOM   2807 C  CA  . GLU   A 1 360 ? -38.011 2.174   33.672 1.00 84.57  ? 656 GLU   A CA  1 
ATOM   2808 C  C   . GLU   A 1 360 ? -38.572 1.282   32.568 1.00 82.42  ? 656 GLU   A C   1 
ATOM   2809 O  O   . GLU   A 1 360 ? -39.422 0.422   32.829 1.00 83.85  ? 656 GLU   A O   1 
ATOM   2810 C  CB  . GLU   A 1 360 ? -38.712 3.529   33.665 1.00 93.00  ? 656 GLU   A CB  1 
ATOM   2811 C  CG  . GLU   A 1 360 ? -40.169 3.439   34.088 1.00 109.54 ? 656 GLU   A CG  1 
ATOM   2812 C  CD  . GLU   A 1 360 ? -41.052 4.454   33.387 1.00 127.84 ? 656 GLU   A CD  1 
ATOM   2813 O  OE1 . GLU   A 1 360 ? -42.274 4.210   33.284 1.00 136.21 ? 656 GLU   A OE1 1 
ATOM   2814 O  OE2 . GLU   A 1 360 ? -40.525 5.492   32.933 1.00 133.82 ? 656 GLU   A OE2 1 
ATOM   2815 N  N   . SER   A 1 361 ? -38.109 1.465   31.325 1.00 80.75  ? 657 SER   A N   1 
ATOM   2816 C  CA  A SER   A 1 361 ? -38.632 0.650   30.234 0.44 75.96  ? 657 SER   A CA  1 
ATOM   2817 C  CA  B SER   A 1 361 ? -38.607 0.649   30.216 0.56 75.97  ? 657 SER   A CA  1 
ATOM   2818 C  C   . SER   A 1 361 ? -38.273 -0.820  30.416 1.00 73.73  ? 657 SER   A C   1 
ATOM   2819 O  O   . SER   A 1 361 ? -39.034 -1.703  29.996 1.00 77.14  ? 657 SER   A O   1 
ATOM   2820 C  CB  A SER   A 1 361 ? -38.116 1.174   28.893 0.44 72.64  ? 657 SER   A CB  1 
ATOM   2821 C  CB  B SER   A 1 361 ? -38.023 1.142   28.882 0.56 72.31  ? 657 SER   A CB  1 
ATOM   2822 O  OG  A SER   A 1 361 ? -38.484 2.530   28.705 0.44 67.36  ? 657 SER   A OG  1 
ATOM   2823 O  OG  B SER   A 1 361 ? -36.687 0.690   28.682 0.56 67.76  ? 657 SER   A OG  1 
ATOM   2824 N  N   . PHE   A 1 362 ? -37.140 -1.104  31.048 1.00 66.05  ? 658 PHE   A N   1 
ATOM   2825 C  CA  . PHE   A 1 362 ? -36.746 -2.491  31.210 1.00 64.77  ? 658 PHE   A CA  1 
ATOM   2826 C  C   . PHE   A 1 362 ? -37.574 -3.190  32.282 1.00 67.23  ? 658 PHE   A C   1 
ATOM   2827 O  O   . PHE   A 1 362 ? -37.888 -4.374  32.135 1.00 62.50  ? 658 PHE   A O   1 
ATOM   2828 C  CB  . PHE   A 1 362 ? -35.249 -2.564  31.499 1.00 67.33  ? 658 PHE   A CB  1 
ATOM   2829 C  CG  . PHE   A 1 362 ? -34.758 -3.953  31.711 1.00 66.55  ? 658 PHE   A CG  1 
ATOM   2830 C  CD1 . PHE   A 1 362 ? -34.448 -4.764  30.637 1.00 64.16  ? 658 PHE   A CD1 1 
ATOM   2831 C  CD2 . PHE   A 1 362 ? -34.636 -4.462  32.997 1.00 62.47  ? 658 PHE   A CD2 1 
ATOM   2832 C  CE1 . PHE   A 1 362 ? -34.008 -6.051  30.832 1.00 61.41  ? 658 PHE   A CE1 1 
ATOM   2833 C  CE2 . PHE   A 1 362 ? -34.195 -5.751  33.197 1.00 60.84  ? 658 PHE   A CE2 1 
ATOM   2834 C  CZ  . PHE   A 1 362 ? -33.879 -6.551  32.108 1.00 64.70  ? 658 PHE   A CZ  1 
ATOM   2835 N  N   . ILE   A 1 363 ? -37.962 -2.482  33.345 1.00 70.94  ? 659 ILE   A N   1 
ATOM   2836 C  CA  . ILE   A 1 363 ? -38.944 -3.037  34.271 1.00 78.13  ? 659 ILE   A CA  1 
ATOM   2837 C  C   . ILE   A 1 363 ? -40.220 -3.391  33.517 1.00 75.99  ? 659 ILE   A C   1 
ATOM   2838 O  O   . ILE   A 1 363 ? -40.755 -4.497  33.652 1.00 77.51  ? 659 ILE   A O   1 
ATOM   2839 C  CB  . ILE   A 1 363 ? -39.227 -2.055  35.427 1.00 78.78  ? 659 ILE   A CB  1 
ATOM   2840 C  CG1 . ILE   A 1 363 ? -37.992 -1.865  36.325 1.00 77.66  ? 659 ILE   A CG1 1 
ATOM   2841 C  CG2 . ILE   A 1 363 ? -40.415 -2.537  36.268 1.00 88.44  ? 659 ILE   A CG2 1 
ATOM   2842 C  CD1 . ILE   A 1 363 ? -37.765 -2.972  37.322 1.00 66.62  ? 659 ILE   A CD1 1 
ATOM   2843 N  N   . LYS   A 1 364 ? -40.721 -2.458  32.703 1.00 77.95  ? 660 LYS   A N   1 
ATOM   2844 C  CA  . LYS   A 1 364 ? -41.918 -2.744  31.915 1.00 84.58  ? 660 LYS   A CA  1 
ATOM   2845 C  C   . LYS   A 1 364 ? -41.688 -3.906  30.957 1.00 72.25  ? 660 LYS   A C   1 
ATOM   2846 O  O   . LYS   A 1 364 ? -42.570 -4.755  30.787 1.00 79.73  ? 660 LYS   A O   1 
ATOM   2847 C  CB  . LYS   A 1 364 ? -42.379 -1.504  31.150 1.00 84.42  ? 660 LYS   A CB  1 
ATOM   2848 C  CG  . LYS   A 1 364 ? -43.796 -1.643  30.597 1.00 93.53  ? 660 LYS   A CG  1 
ATOM   2849 C  CD  . LYS   A 1 364 ? -44.214 -0.407  29.811 1.00 100.81 ? 660 LYS   A CD  1 
ATOM   2850 C  CE  . LYS   A 1 364 ? -45.455 -0.656  28.957 1.00 108.04 ? 660 LYS   A CE  1 
ATOM   2851 N  NZ  . LYS   A 1 364 ? -45.129 -0.815  27.501 1.00 106.09 ? 660 LYS   A NZ  1 
ATOM   2852 N  N   . HIS   A 1 365 ? -40.504 -3.973  30.335 1.00 73.36  ? 661 HIS   A N   1 
ATOM   2853 C  CA  . HIS   A 1 365 ? -40.170 -5.115  29.480 1.00 76.33  ? 661 HIS   A CA  1 
ATOM   2854 C  C   . HIS   A 1 365 ? -40.148 -6.410  30.276 1.00 74.59  ? 661 HIS   A C   1 
ATOM   2855 O  O   . HIS   A 1 365 ? -40.674 -7.438  29.830 1.00 74.85  ? 661 HIS   A O   1 
ATOM   2856 C  CB  . HIS   A 1 365 ? -38.810 -4.898  28.811 1.00 73.89  ? 661 HIS   A CB  1 
ATOM   2857 C  CG  . HIS   A 1 365 ? -38.275 -6.111  28.102 1.00 73.19  ? 661 HIS   A CG  1 
ATOM   2858 N  ND1 . HIS   A 1 365 ? -38.910 -6.684  27.022 1.00 71.56  ? 661 HIS   A ND1 1 
ATOM   2859 C  CD2 . HIS   A 1 365 ? -37.157 -6.849  28.313 1.00 68.48  ? 661 HIS   A CD2 1 
ATOM   2860 C  CE1 . HIS   A 1 365 ? -38.207 -7.721  26.599 1.00 70.83  ? 661 HIS   A CE1 1 
ATOM   2861 N  NE2 . HIS   A 1 365 ? -37.140 -7.847  27.368 1.00 71.74  ? 661 HIS   A NE2 1 
ATOM   2862 N  N   . MET   A 1 366 ? -39.521 -6.384  31.452 1.00 70.71  ? 662 MET   A N   1 
ATOM   2863 C  CA  . MET   A 1 366 ? -39.506 -7.565  32.307 1.00 68.82  ? 662 MET   A CA  1 
ATOM   2864 C  C   . MET   A 1 366 ? -40.915 -8.056  32.605 1.00 64.88  ? 662 MET   A C   1 
ATOM   2865 O  O   . MET   A 1 366 ? -41.178 -9.262  32.552 1.00 63.90  ? 662 MET   A O   1 
ATOM   2866 C  CB  . MET   A 1 366 ? -38.768 -7.254  33.606 1.00 67.89  ? 662 MET   A CB  1 
ATOM   2867 C  CG  . MET   A 1 366 ? -37.592 -8.146  33.880 1.00 68.91  ? 662 MET   A CG  1 
ATOM   2868 S  SD  . MET   A 1 366 ? -36.798 -7.533  35.384 1.00 74.02  ? 662 MET   A SD  1 
ATOM   2869 C  CE  . MET   A 1 366 ? -36.289 -9.079  36.141 1.00 75.39  ? 662 MET   A CE  1 
ATOM   2870 N  N   . GLU   A 1 367 ? -41.836 -7.137  32.917 1.00 71.95  ? 663 GLU   A N   1 
ATOM   2871 C  CA  . GLU   A 1 367 ? -43.208 -7.533  33.229 1.00 85.80  ? 663 GLU   A CA  1 
ATOM   2872 C  C   . GLU   A 1 367 ? -43.838 -8.271  32.055 1.00 91.50  ? 663 GLU   A C   1 
ATOM   2873 O  O   . GLU   A 1 367 ? -44.496 -9.303  32.232 1.00 98.83  ? 663 GLU   A O   1 
ATOM   2874 C  CB  . GLU   A 1 367 ? -44.057 -6.310  33.583 1.00 96.94  ? 663 GLU   A CB  1 
ATOM   2875 C  CG  . GLU   A 1 367 ? -43.584 -5.475  34.756 1.00 109.35 ? 663 GLU   A CG  1 
ATOM   2876 C  CD  . GLU   A 1 367 ? -44.439 -4.231  34.949 1.00 120.10 ? 663 GLU   A CD  1 
ATOM   2877 O  OE1 . GLU   A 1 367 ? -45.422 -4.049  34.190 1.00 127.19 ? 663 GLU   A OE1 1 
ATOM   2878 O  OE2 . GLU   A 1 367 ? -44.123 -3.433  35.855 1.00 118.59 ? 663 GLU   A OE2 1 
ATOM   2879 N  N   . ASN   A 1 368 ? -43.641 -7.748  30.844 1.00 87.30  ? 664 ASN   A N   1 
ATOM   2880 C  CA  . ASN   A 1 368 ? -44.190 -8.387  29.652 1.00 85.96  ? 664 ASN   A CA  1 
ATOM   2881 C  C   . ASN   A 1 368 ? -43.619 -9.787  29.455 1.00 83.96  ? 664 ASN   A C   1 
ATOM   2882 O  O   . ASN   A 1 368 ? -44.353 -10.723 29.117 1.00 92.62  ? 664 ASN   A O   1 
ATOM   2883 C  CB  . ASN   A 1 368 ? -43.910 -7.521  28.424 1.00 86.10  ? 664 ASN   A CB  1 
ATOM   2884 C  CG  . ASN   A 1 368 ? -44.597 -6.174  28.486 1.00 91.81  ? 664 ASN   A CG  1 
ATOM   2885 O  OD1 . ASN   A 1 368 ? -45.594 -6.001  29.190 1.00 103.49 ? 664 ASN   A OD1 1 
ATOM   2886 N  ND2 . ASN   A 1 368 ? -44.072 -5.209  27.735 1.00 80.67  ? 664 ASN   A ND2 1 
ATOM   2887 N  N   . GLU   A 1 369 ? -42.303 -9.943  29.634 1.00 73.36  ? 665 GLU   A N   1 
ATOM   2888 C  CA  . GLU   A 1 369 ? -41.679 -11.249 29.440 1.00 65.53  ? 665 GLU   A CA  1 
ATOM   2889 C  C   . GLU   A 1 369 ? -42.219 -12.275 30.432 1.00 83.06  ? 665 GLU   A C   1 
ATOM   2890 O  O   . GLU   A 1 369 ? -42.512 -13.412 30.056 1.00 88.34  ? 665 GLU   A O   1 
ATOM   2891 C  CB  . GLU   A 1 369 ? -40.162 -11.134 29.580 1.00 68.97  ? 665 GLU   A CB  1 
ATOM   2892 C  CG  . GLU   A 1 369 ? -39.461 -10.333 28.522 1.00 76.56  ? 665 GLU   A CG  1 
ATOM   2893 C  CD  . GLU   A 1 369 ? -39.018 -11.198 27.364 1.00 78.02  ? 665 GLU   A CD  1 
ATOM   2894 O  OE1 . GLU   A 1 369 ? -37.909 -11.787 27.443 1.00 91.27  ? 665 GLU   A OE1 1 
ATOM   2895 O  OE2 . GLU   A 1 369 ? -39.812 -11.315 26.413 1.00 62.11  ? 665 GLU   A OE2 1 
ATOM   2896 N  N   . TYR   A 1 370 ? -42.335 -11.906 31.712 1.00 84.07  ? 666 TYR   A N   1 
ATOM   2897 C  CA  . TYR   A 1 370 ? -42.859 -12.858 32.689 1.00 88.04  ? 666 TYR   A CA  1 
ATOM   2898 C  C   . TYR   A 1 370 ? -44.289 -13.262 32.349 1.00 94.94  ? 666 TYR   A C   1 
ATOM   2899 O  O   . TYR   A 1 370 ? -44.664 -14.432 32.498 1.00 89.61  ? 666 TYR   A O   1 
ATOM   2900 C  CB  . TYR   A 1 370 ? -42.760 -12.276 34.100 1.00 85.92  ? 666 TYR   A CB  1 
ATOM   2901 C  CG  . TYR   A 1 370 ? -41.381 -12.468 34.677 1.00 81.05  ? 666 TYR   A CG  1 
ATOM   2902 C  CD1 . TYR   A 1 370 ? -40.361 -11.572 34.402 1.00 75.65  ? 666 TYR   A CD1 1 
ATOM   2903 C  CD2 . TYR   A 1 370 ? -41.083 -13.574 35.457 1.00 85.34  ? 666 TYR   A CD2 1 
ATOM   2904 C  CE1 . TYR   A 1 370 ? -39.088 -11.756 34.909 1.00 71.06  ? 666 TYR   A CE1 1 
ATOM   2905 C  CE2 . TYR   A 1 370 ? -39.812 -13.764 35.967 1.00 82.72  ? 666 TYR   A CE2 1 
ATOM   2906 C  CZ  . TYR   A 1 370 ? -38.819 -12.854 35.684 1.00 78.00  ? 666 TYR   A CZ  1 
ATOM   2907 O  OH  . TYR   A 1 370 ? -37.548 -13.035 36.183 1.00 81.54  ? 666 TYR   A OH  1 
ATOM   2908 N  N   . ARG   A 1 371 ? -45.086 -12.320 31.846 1.00 103.82 ? 667 ARG   A N   1 
ATOM   2909 C  CA  . ARG   A 1 371 ? -46.469 -12.590 31.471 1.00 112.90 ? 667 ARG   A CA  1 
ATOM   2910 C  C   . ARG   A 1 371 ? -46.550 -13.539 30.277 1.00 109.52 ? 667 ARG   A C   1 
ATOM   2911 O  O   . ARG   A 1 371 ? -46.988 -14.686 30.420 1.00 112.86 ? 667 ARG   A O   1 
ATOM   2912 C  CB  . ARG   A 1 371 ? -47.186 -11.272 31.168 1.00 121.43 ? 667 ARG   A CB  1 
ATOM   2913 C  CG  . ARG   A 1 371 ? -48.701 -11.349 31.134 1.00 134.84 ? 667 ARG   A CG  1 
ATOM   2914 C  CD  . ARG   A 1 371 ? -49.269 -10.082 30.521 1.00 142.83 ? 667 ARG   A CD  1 
ATOM   2915 N  NE  . ARG   A 1 371 ? -48.498 -9.685  29.343 1.00 147.54 ? 667 ARG   A NE  1 
ATOM   2916 C  CZ  . ARG   A 1 371 ? -48.682 -10.176 28.117 1.00 152.43 ? 667 ARG   A CZ  1 
ATOM   2917 N  NH1 . ARG   A 1 371 ? -49.621 -11.087 27.888 1.00 159.56 ? 667 ARG   A NH1 1 
ATOM   2918 N  NH2 . ARG   A 1 371 ? -47.925 -9.756  27.111 1.00 148.98 ? 667 ARG   A NH2 1 
ATOM   2919 N  N   . CYS   A 1 372 ? -46.110 -13.084 29.102 1.00 112.21 ? 668 CYS   A N   1 
ATOM   2920 C  CA  . CYS   A 1 372 ? -46.303 -13.825 27.860 1.00 107.61 ? 668 CYS   A CA  1 
ATOM   2921 C  C   . CYS   A 1 372 ? -45.149 -14.765 27.524 1.00 96.82  ? 668 CYS   A C   1 
ATOM   2922 O  O   . CYS   A 1 372 ? -45.193 -15.419 26.478 1.00 103.10 ? 668 CYS   A O   1 
ATOM   2923 C  CB  . CYS   A 1 372 ? -46.541 -12.849 26.694 1.00 118.90 ? 668 CYS   A CB  1 
ATOM   2924 S  SG  . CYS   A 1 372 ? -45.109 -11.863 26.127 1.00 122.31 ? 668 CYS   A SG  1 
ATOM   2925 N  N   . ARG   A 1 373 ? -44.124 -14.859 28.373 1.00 78.75  ? 669 ARG   A N   1 
ATOM   2926 C  CA  . ARG   A 1 373 ? -42.990 -15.748 28.115 1.00 73.34  ? 669 ARG   A CA  1 
ATOM   2927 C  C   . ARG   A 1 373 ? -42.551 -16.570 29.321 1.00 85.13  ? 669 ARG   A C   1 
ATOM   2928 O  O   . ARG   A 1 373 ? -41.808 -17.543 29.139 1.00 91.36  ? 669 ARG   A O   1 
ATOM   2929 C  CB  . ARG   A 1 373 ? -41.790 -14.939 27.604 1.00 76.99  ? 669 ARG   A CB  1 
ATOM   2930 C  CG  . ARG   A 1 373 ? -40.721 -15.768 26.927 1.00 75.35  ? 669 ARG   A CG  1 
ATOM   2931 C  CD  . ARG   A 1 373 ? -39.482 -14.964 26.583 1.00 73.03  ? 669 ARG   A CD  1 
ATOM   2932 N  NE  . ARG   A 1 373 ? -38.619 -15.745 25.699 1.00 75.83  ? 669 ARG   A NE  1 
ATOM   2933 C  CZ  . ARG   A 1 373 ? -37.331 -15.505 25.480 1.00 74.29  ? 669 ARG   A CZ  1 
ATOM   2934 N  NH1 . ARG   A 1 373 ? -36.723 -14.489 26.074 1.00 71.73  ? 669 ARG   A NH1 1 
ATOM   2935 N  NH2 . ARG   A 1 373 ? -36.652 -16.291 24.649 1.00 75.64  ? 669 ARG   A NH2 1 
ATOM   2936 N  N   . GLY   A 1 374 ? -42.971 -16.225 30.537 1.00 87.11  ? 670 GLY   A N   1 
ATOM   2937 C  CA  . GLY   A 1 374 ? -42.591 -16.957 31.728 1.00 92.71  ? 670 GLY   A CA  1 
ATOM   2938 C  C   . GLY   A 1 374 ? -41.260 -16.580 32.341 1.00 93.25  ? 670 GLY   A C   1 
ATOM   2939 O  O   . GLY   A 1 374 ? -40.764 -17.326 33.192 1.00 95.30  ? 670 GLY   A O   1 
ATOM   2940 N  N   . GLY   A 1 375 ? -40.658 -15.469 31.934 1.00 89.48  ? 671 GLY   A N   1 
ATOM   2941 C  CA  . GLY   A 1 375 ? -39.425 -15.025 32.552 1.00 87.67  ? 671 GLY   A CA  1 
ATOM   2942 C  C   . GLY   A 1 375 ? -38.646 -14.107 31.646 1.00 80.41  ? 671 GLY   A C   1 
ATOM   2943 O  O   . GLY   A 1 375 ? -38.986 -13.891 30.486 1.00 85.38  ? 671 GLY   A O   1 
ATOM   2944 N  N   . CYS   A 1 376 ? -37.565 -13.575 32.201 1.00 68.87  ? 672 CYS   A N   1 
ATOM   2945 C  CA  . CYS   A 1 376 ? -36.671 -12.681 31.464 1.00 73.05  ? 672 CYS   A CA  1 
ATOM   2946 C  C   . CYS   A 1 376 ? -35.288 -12.787 32.096 1.00 66.41  ? 672 CYS   A C   1 
ATOM   2947 O  O   . CYS   A 1 376 ? -35.031 -12.184 33.147 1.00 66.61  ? 672 CYS   A O   1 
ATOM   2948 C  CB  . CYS   A 1 376 ? -37.172 -11.239 31.483 1.00 68.58  ? 672 CYS   A CB  1 
ATOM   2949 S  SG  . CYS   A 1 376 ? -36.126 -10.023 30.609 1.00 63.91  ? 672 CYS   A SG  1 
ATOM   2950 N  N   . PRO   A 1 377 ? -34.370 -13.540 31.486 1.00 58.09  ? 673 PRO   A N   1 
ATOM   2951 C  CA  . PRO   A 1 377 ? -32.988 -13.582 31.990 1.00 52.73  ? 673 PRO   A CA  1 
ATOM   2952 C  C   . PRO   A 1 377 ? -32.413 -12.180 32.104 1.00 54.88  ? 673 PRO   A C   1 
ATOM   2953 O  O   . PRO   A 1 377 ? -32.605 -11.339 31.224 1.00 52.89  ? 673 PRO   A O   1 
ATOM   2954 C  CB  . PRO   A 1 377 ? -32.253 -14.402 30.931 1.00 54.75  ? 673 PRO   A CB  1 
ATOM   2955 C  CG  . PRO   A 1 377 ? -33.100 -14.195 29.657 1.00 47.34  ? 673 PRO   A CG  1 
ATOM   2956 C  CD  . PRO   A 1 377 ? -34.510 -14.077 30.116 1.00 55.04  ? 673 PRO   A CD  1 
ATOM   2957 N  N   . ALA   A 1 378 ? -31.724 -11.908 33.211 1.00 61.77  ? 674 ALA   A N   1 
ATOM   2958 C  CA  . ALA   A 1 378 ? -31.299 -10.541 33.486 1.00 52.02  ? 674 ALA   A CA  1 
ATOM   2959 C  C   . ALA   A 1 378 ? -30.096 -10.544 34.417 1.00 55.02  ? 674 ALA   A C   1 
ATOM   2960 O  O   . ALA   A 1 378 ? -30.070 -11.292 35.397 1.00 54.95  ? 674 ALA   A O   1 
ATOM   2961 C  CB  . ALA   A 1 378 ? -32.453 -9.730  34.075 1.00 45.92  ? 674 ALA   A CB  1 
ATOM   2962 N  N   . ASP   A 1 379 ? -29.101 -9.702  34.102 1.00 49.77  ? 675 ASP   A N   1 
ATOM   2963 C  CA  . ASP   A 1 379 ? -27.836 -9.648  34.833 1.00 45.36  ? 675 ASP   A CA  1 
ATOM   2964 C  C   . ASP   A 1 379 ? -27.838 -8.324  35.580 1.00 56.49  ? 675 ASP   A C   1 
ATOM   2965 O  O   . ASP   A 1 379 ? -27.565 -7.266  34.998 1.00 50.11  ? 675 ASP   A O   1 
ATOM   2966 C  CB  . ASP   A 1 379 ? -26.630 -9.776  33.903 1.00 55.03  ? 675 ASP   A CB  1 
ATOM   2967 C  CG  . ASP   A 1 379 ? -25.316 -9.920  34.653 1.00 61.86  ? 675 ASP   A CG  1 
ATOM   2968 O  OD1 . ASP   A 1 379 ? -24.398 -10.598 34.138 1.00 62.03  ? 675 ASP   A OD1 1 
ATOM   2969 O  OD2 . ASP   A 1 379 ? -25.194 -9.358  35.762 1.00 64.74  ? 675 ASP   A OD2 1 
ATOM   2970 N  N   . TRP   A 1 380 ? -28.157 -8.400  36.879 1.00 46.49  ? 676 TRP   A N   1 
ATOM   2971 C  CA  . TRP   A 1 380 ? -28.303 -7.196  37.690 1.00 46.62  ? 676 TRP   A CA  1 
ATOM   2972 C  C   . TRP   A 1 380 ? -27.031 -6.369  37.663 1.00 46.49  ? 676 TRP   A C   1 
ATOM   2973 O  O   . TRP   A 1 380 ? -27.079 -5.132  37.644 1.00 52.65  ? 676 TRP   A O   1 
ATOM   2974 C  CB  . TRP   A 1 380 ? -28.654 -7.603  39.128 1.00 46.32  ? 676 TRP   A CB  1 
ATOM   2975 C  CG  . TRP   A 1 380 ? -29.085 -6.507  40.060 1.00 51.72  ? 676 TRP   A CG  1 
ATOM   2976 C  CD1 . TRP   A 1 380 ? -30.366 -6.235  40.464 1.00 54.39  ? 676 TRP   A CD1 1 
ATOM   2977 C  CD2 . TRP   A 1 380 ? -28.240 -5.574  40.759 1.00 49.88  ? 676 TRP   A CD2 1 
ATOM   2978 N  NE1 . TRP   A 1 380 ? -30.370 -5.174  41.336 1.00 58.17  ? 676 TRP   A NE1 1 
ATOM   2979 C  CE2 . TRP   A 1 380 ? -29.080 -4.764  41.552 1.00 54.85  ? 676 TRP   A CE2 1 
ATOM   2980 C  CE3 . TRP   A 1 380 ? -26.859 -5.344  40.791 1.00 44.46  ? 676 TRP   A CE3 1 
ATOM   2981 C  CZ2 . TRP   A 1 380 ? -28.589 -3.727  42.347 1.00 47.91  ? 676 TRP   A CZ2 1 
ATOM   2982 C  CZ3 . TRP   A 1 380 ? -26.375 -4.313  41.612 1.00 45.75  ? 676 TRP   A CZ3 1 
ATOM   2983 C  CH2 . TRP   A 1 380 ? -27.242 -3.511  42.343 1.00 43.37  ? 676 TRP   A CH2 1 
ATOM   2984 N  N   . VAL   A 1 381 ? -25.880 -7.044  37.700 1.00 53.17  ? 677 VAL   A N   1 
ATOM   2985 C  CA  . VAL   A 1 381 ? -24.595 -6.355  37.757 1.00 46.03  ? 677 VAL   A CA  1 
ATOM   2986 C  C   . VAL   A 1 381 ? -24.433 -5.435  36.560 1.00 57.21  ? 677 VAL   A C   1 
ATOM   2987 O  O   . VAL   A 1 381 ? -23.851 -4.350  36.669 1.00 44.75  ? 677 VAL   A O   1 
ATOM   2988 C  CB  . VAL   A 1 381 ? -23.447 -7.383  37.848 1.00 49.29  ? 677 VAL   A CB  1 
ATOM   2989 C  CG1 . VAL   A 1 381 ? -22.129 -6.697  37.613 1.00 46.60  ? 677 VAL   A CG1 1 
ATOM   2990 C  CG2 . VAL   A 1 381 ? -23.425 -8.034  39.271 1.00 41.00  ? 677 VAL   A CG2 1 
ATOM   2991 N  N   . TRP   A 1 382 ? -24.979 -5.841  35.403 1.00 54.20  ? 678 TRP   A N   1 
ATOM   2992 C  CA  . TRP   A 1 382 ? -24.863 -5.072  34.174 1.00 55.44  ? 678 TRP   A CA  1 
ATOM   2993 C  C   . TRP   A 1 382 ? -26.075 -4.198  33.887 1.00 50.12  ? 678 TRP   A C   1 
ATOM   2994 O  O   . TRP   A 1 382 ? -25.906 -3.139  33.280 1.00 48.19  ? 678 TRP   A O   1 
ATOM   2995 C  CB  . TRP   A 1 382 ? -24.618 -6.001  32.985 1.00 52.93  ? 678 TRP   A CB  1 
ATOM   2996 C  CG  . TRP   A 1 382 ? -23.183 -6.338  32.752 1.00 53.18  ? 678 TRP   A CG  1 
ATOM   2997 C  CD1 . TRP   A 1 382 ? -22.341 -7.045  33.590 1.00 57.29  ? 678 TRP   A CD1 1 
ATOM   2998 C  CD2 . TRP   A 1 382 ? -22.402 -6.004  31.588 1.00 49.16  ? 678 TRP   A CD2 1 
ATOM   2999 N  NE1 . TRP   A 1 382 ? -21.086 -7.151  33.012 1.00 52.50  ? 678 TRP   A NE1 1 
ATOM   3000 C  CE2 . TRP   A 1 382 ? -21.106 -6.535  31.780 1.00 53.86  ? 678 TRP   A CE2 1 
ATOM   3001 C  CE3 . TRP   A 1 382 ? -22.680 -5.313  30.409 1.00 46.82  ? 678 TRP   A CE3 1 
ATOM   3002 C  CZ2 . TRP   A 1 382 ? -20.089 -6.374  30.842 1.00 61.24  ? 678 TRP   A CZ2 1 
ATOM   3003 C  CZ3 . TRP   A 1 382 ? -21.666 -5.177  29.463 1.00 64.44  ? 678 TRP   A CZ3 1 
ATOM   3004 C  CH2 . TRP   A 1 382 ? -20.394 -5.713  29.684 1.00 67.03  ? 678 TRP   A CH2 1 
ATOM   3005 N  N   . ILE   A 1 383 ? -27.278 -4.579  34.347 1.00 47.73  ? 679 ILE   A N   1 
ATOM   3006 C  CA  . ILE   A 1 383 ? -28.478 -3.778  34.082 1.00 45.71  ? 679 ILE   A CA  1 
ATOM   3007 C  C   . ILE   A 1 383 ? -28.469 -2.482  34.892 1.00 56.58  ? 679 ILE   A C   1 
ATOM   3008 O  O   . ILE   A 1 383 ? -28.935 -1.441  34.416 1.00 53.28  ? 679 ILE   A O   1 
ATOM   3009 C  CB  . ILE   A 1 383 ? -29.746 -4.604  34.383 1.00 53.66  ? 679 ILE   A CB  1 
ATOM   3010 C  CG1 . ILE   A 1 383 ? -29.861 -5.814  33.451 1.00 52.05  ? 679 ILE   A CG1 1 
ATOM   3011 C  CG2 . ILE   A 1 383 ? -31.009 -3.716  34.342 1.00 48.81  ? 679 ILE   A CG2 1 
ATOM   3012 C  CD1 . ILE   A 1 383 ? -30.261 -5.465  32.008 1.00 62.65  ? 679 ILE   A CD1 1 
ATOM   3013 N  N   . VAL   A 1 384 ? -28.024 -2.528  36.148 1.00 55.07  ? 680 VAL   A N   1 
ATOM   3014 C  CA  . VAL   A 1 384 ? -28.045 -1.307  36.975 1.00 49.49  ? 680 VAL   A CA  1 
ATOM   3015 C  C   . VAL   A 1 384 ? -27.065 -0.289  36.395 1.00 57.88  ? 680 VAL   A C   1 
ATOM   3016 O  O   . VAL   A 1 384 ? -25.901 -0.648  36.129 1.00 57.35  ? 680 VAL   A O   1 
ATOM   3017 C  CB  . VAL   A 1 384 ? -27.682 -1.647  38.428 1.00 56.40  ? 680 VAL   A CB  1 
ATOM   3018 C  CG1 . VAL   A 1 384 ? -27.513 -0.379  39.301 1.00 47.87  ? 680 VAL   A CG1 1 
ATOM   3019 C  CG2 . VAL   A 1 384 ? -28.743 -2.543  39.047 1.00 66.02  ? 680 VAL   A CG2 1 
ATOM   3020 N  N   . PRO   A 1 385 ? -27.467 0.977   36.192 1.00 60.96  ? 681 PRO   A N   1 
ATOM   3021 C  CA  . PRO   A 1 385 ? -26.567 1.933   35.549 1.00 62.57  ? 681 PRO   A CA  1 
ATOM   3022 C  C   . PRO   A 1 385 ? -25.401 2.308   36.446 1.00 68.79  ? 681 PRO   A C   1 
ATOM   3023 O  O   . PRO   A 1 385 ? -25.490 2.228   37.686 1.00 64.71  ? 681 PRO   A O   1 
ATOM   3024 C  CB  . PRO   A 1 385 ? -27.473 3.148   35.277 1.00 64.29  ? 681 PRO   A CB  1 
ATOM   3025 C  CG  . PRO   A 1 385 ? -28.836 2.575   35.227 1.00 66.43  ? 681 PRO   A CG  1 
ATOM   3026 C  CD  . PRO   A 1 385 ? -28.815 1.549   36.345 1.00 65.49  ? 681 PRO   A CD  1 
ATOM   3027 N  N   . PRO   A 1 386 ? -24.286 2.754   35.860 1.00 66.09  ? 682 PRO   A N   1 
ATOM   3028 C  CA  . PRO   A 1 386 ? -23.058 2.993   36.626 1.00 69.28  ? 682 PRO   A CA  1 
ATOM   3029 C  C   . PRO   A 1 386 ? -23.051 4.288   37.426 1.00 68.44  ? 682 PRO   A C   1 
ATOM   3030 O  O   . PRO   A 1 386 ? -21.982 4.712   37.877 1.00 66.71  ? 682 PRO   A O   1 
ATOM   3031 C  CB  . PRO   A 1 386 ? -22.000 3.034   35.511 1.00 69.11  ? 682 PRO   A CB  1 
ATOM   3032 C  CG  . PRO   A 1 386 ? -22.712 3.628   34.383 1.00 66.70  ? 682 PRO   A CG  1 
ATOM   3033 C  CD  . PRO   A 1 386 ? -24.074 2.993   34.415 1.00 67.74  ? 682 PRO   A CD  1 
ATOM   3034 N  N   . MET   A 1 387 ? -24.198 4.946   37.574 1.00 67.73  ? 683 MET   A N   1 
ATOM   3035 C  CA  . MET   A 1 387 ? -24.325 6.123   38.420 1.00 74.22  ? 683 MET   A CA  1 
ATOM   3036 C  C   . MET   A 1 387 ? -25.759 6.156   38.920 1.00 74.02  ? 683 MET   A C   1 
ATOM   3037 O  O   . MET   A 1 387 ? -26.666 5.638   38.263 1.00 68.72  ? 683 MET   A O   1 
ATOM   3038 C  CB  . MET   A 1 387 ? -24.001 7.427   37.678 1.00 80.51  ? 683 MET   A CB  1 
ATOM   3039 C  CG  . MET   A 1 387 ? -25.207 8.045   36.963 1.00 85.88  ? 683 MET   A CG  1 
ATOM   3040 S  SD  . MET   A 1 387 ? -24.862 9.573   36.066 1.00 96.22  ? 683 MET   A SD  1 
ATOM   3041 C  CE  . MET   A 1 387 ? -24.730 10.746  37.392 1.00 88.59  ? 683 MET   A CE  1 
ATOM   3042 N  N   . SER   A 1 388 ? -25.959 6.736   40.099 1.00 77.74  ? 684 SER   A N   1 
ATOM   3043 C  CA  . SER   A 1 388 ? -27.306 6.934   40.635 1.00 81.66  ? 684 SER   A CA  1 
ATOM   3044 C  C   . SER   A 1 388 ? -28.096 5.625   40.721 1.00 74.03  ? 684 SER   A C   1 
ATOM   3045 O  O   . SER   A 1 388 ? -29.324 5.618   40.614 1.00 83.95  ? 684 SER   A O   1 
ATOM   3046 C  CB  . SER   A 1 388 ? -28.064 7.961   39.784 1.00 81.07  ? 684 SER   A CB  1 
ATOM   3047 O  OG  . SER   A 1 388 ? -27.336 9.173   39.710 1.00 91.76  ? 684 SER   A OG  1 
ATOM   3048 N  N   . GLY   A 1 389 ? -27.401 4.509   40.897 1.00 64.29  ? 685 GLY   A N   1 
ATOM   3049 C  CA  . GLY   A 1 389 ? -28.015 3.191   40.881 1.00 58.02  ? 685 GLY   A CA  1 
ATOM   3050 C  C   . GLY   A 1 389 ? -29.345 3.039   41.608 1.00 66.34  ? 685 GLY   A C   1 
ATOM   3051 O  O   . GLY   A 1 389 ? -30.322 2.577   41.013 1.00 65.56  ? 685 GLY   A O   1 
ATOM   3052 N  N   . SER   A 1 390 ? -29.422 3.439   42.881 1.00 68.63  ? 686 SER   A N   1 
ATOM   3053 C  CA  . SER   A 1 390 ? -30.616 3.125   43.663 1.00 63.96  ? 686 SER   A CA  1 
ATOM   3054 C  C   . SER   A 1 390 ? -31.767 4.099   43.442 1.00 72.50  ? 686 SER   A C   1 
ATOM   3055 O  O   . SER   A 1 390 ? -32.863 3.849   43.961 1.00 72.92  ? 686 SER   A O   1 
ATOM   3056 C  CB  . SER   A 1 390 ? -30.288 3.045   45.163 1.00 63.38  ? 686 SER   A CB  1 
ATOM   3057 O  OG  . SER   A 1 390 ? -29.960 4.310   45.689 1.00 70.12  ? 686 SER   A OG  1 
ATOM   3058 N  N   . ILE   A 1 391 ? -31.569 5.194   42.692 1.00 76.65  ? 687 ILE   A N   1 
ATOM   3059 C  CA  . ILE   A 1 391 ? -32.708 6.027   42.311 1.00 76.96  ? 687 ILE   A CA  1 
ATOM   3060 C  C   . ILE   A 1 391 ? -33.314 5.572   40.995 1.00 80.50  ? 687 ILE   A C   1 
ATOM   3061 O  O   . ILE   A 1 391 ? -34.276 6.192   40.522 1.00 90.09  ? 687 ILE   A O   1 
ATOM   3062 C  CB  . ILE   A 1 391 ? -32.380 7.538   42.232 1.00 87.99  ? 687 ILE   A CB  1 
ATOM   3063 C  CG1 . ILE   A 1 391 ? -31.368 7.859   41.143 1.00 91.71  ? 687 ILE   A CG1 1 
ATOM   3064 C  CG2 . ILE   A 1 391 ? -31.944 8.110   43.612 1.00 80.71  ? 687 ILE   A CG2 1 
ATOM   3065 C  CD1 . ILE   A 1 391 ? -31.153 9.363   40.963 1.00 95.72  ? 687 ILE   A CD1 1 
ATOM   3066 N  N   . THR   A 1 392 ? -32.751 4.451   40.353 1.00 78.05  ? 688 THR   A N   1 
ATOM   3067 C  CA  . THR   A 1 392 ? -33.424 3.815   39.228 1.00 77.21  ? 688 THR   A CA  1 
ATOM   3068 C  C   . THR   A 1 392 ? -34.133 2.546   39.693 1.00 73.24  ? 688 THR   A C   1 
ATOM   3069 O  O   . THR   A 1 392 ? -33.674 1.869   40.625 1.00 68.47  ? 688 THR   A O   1 
ATOM   3070 C  CB  . THR   A 1 392 ? -32.450 3.468   38.083 1.00 80.72  ? 688 THR   A CB  1 
ATOM   3071 O  OG1 . THR   A 1 392 ? -31.637 2.342   38.437 1.00 72.74  ? 688 THR   A OG1 1 
ATOM   3072 C  CG2 . THR   A 1 392 ? -31.551 4.669   37.701 1.00 85.29  ? 688 THR   A CG2 1 
ATOM   3073 N  N   . PRO   A 1 393 ? -35.265 2.196   39.074 1.00 77.29  ? 689 PRO   A N   1 
ATOM   3074 C  CA  . PRO   A 1 393 ? -36.078 1.092   39.611 1.00 75.53  ? 689 PRO   A CA  1 
ATOM   3075 C  C   . PRO   A 1 393 ? -35.450 -0.285  39.459 1.00 70.58  ? 689 PRO   A C   1 
ATOM   3076 O  O   . PRO   A 1 393 ? -35.863 -1.204  40.185 1.00 72.92  ? 689 PRO   A O   1 
ATOM   3077 C  CB  . PRO   A 1 393 ? -37.380 1.194   38.805 1.00 80.13  ? 689 PRO   A CB  1 
ATOM   3078 C  CG  . PRO   A 1 393 ? -36.945 1.799   37.494 1.00 80.17  ? 689 PRO   A CG  1 
ATOM   3079 C  CD  . PRO   A 1 393 ? -35.892 2.811   37.888 1.00 80.97  ? 689 PRO   A CD  1 
ATOM   3080 N  N   . VAL   A 1 394 ? -34.482 -0.466  38.550 1.00 61.86  ? 690 VAL   A N   1 
ATOM   3081 C  CA  . VAL   A 1 394 ? -33.847 -1.778  38.413 1.00 61.32  ? 690 VAL   A CA  1 
ATOM   3082 C  C   . VAL   A 1 394 ? -32.942 -2.123  39.604 1.00 62.91  ? 690 VAL   A C   1 
ATOM   3083 O  O   . VAL   A 1 394 ? -32.664 -3.307  39.819 1.00 65.22  ? 690 VAL   A O   1 
ATOM   3084 C  CB  . VAL   A 1 394 ? -33.035 -1.906  37.103 1.00 54.23  ? 690 VAL   A CB  1 
ATOM   3085 C  CG1 . VAL   A 1 394 ? -33.970 -1.940  35.853 1.00 57.49  ? 690 VAL   A CG1 1 
ATOM   3086 C  CG2 . VAL   A 1 394 ? -31.992 -0.798  36.990 1.00 62.72  ? 690 VAL   A CG2 1 
ATOM   3087 N  N   . PHE   A 1 395 ? -32.463 -1.128  40.374 1.00 61.22  ? 691 PHE   A N   1 
ATOM   3088 C  CA  . PHE   A 1 395 ? -31.664 -1.433  41.563 1.00 62.11  ? 691 PHE   A CA  1 
ATOM   3089 C  C   . PHE   A 1 395 ? -32.462 -2.291  42.532 1.00 61.65  ? 691 PHE   A C   1 
ATOM   3090 O  O   . PHE   A 1 395 ? -31.924 -3.195  43.192 1.00 58.90  ? 691 PHE   A O   1 
ATOM   3091 C  CB  . PHE   A 1 395 ? -31.232 -0.123  42.242 1.00 63.03  ? 691 PHE   A CB  1 
ATOM   3092 C  CG  . PHE   A 1 395 ? -30.408 -0.305  43.489 1.00 60.90  ? 691 PHE   A CG  1 
ATOM   3093 C  CD1 . PHE   A 1 395 ? -29.022 -0.257  43.440 1.00 59.98  ? 691 PHE   A CD1 1 
ATOM   3094 C  CD2 . PHE   A 1 395 ? -31.022 -0.468  44.729 1.00 65.02  ? 691 PHE   A CD2 1 
ATOM   3095 C  CE1 . PHE   A 1 395 ? -28.261 -0.421  44.630 1.00 55.77  ? 691 PHE   A CE1 1 
ATOM   3096 C  CE2 . PHE   A 1 395 ? -30.277 -0.619  45.884 1.00 70.04  ? 691 PHE   A CE2 1 
ATOM   3097 C  CZ  . PHE   A 1 395 ? -28.900 -0.581  45.835 1.00 67.13  ? 691 PHE   A CZ  1 
ATOM   3098 N  N   . HIS   A 1 396 ? -33.757 -2.021  42.619 1.00 63.06  ? 692 HIS   A N   1 
ATOM   3099 C  CA  . HIS   A 1 396 ? -34.664 -2.594  43.596 1.00 56.09  ? 692 HIS   A CA  1 
ATOM   3100 C  C   . HIS   A 1 396 ? -35.352 -3.846  43.083 1.00 61.29  ? 692 HIS   A C   1 
ATOM   3101 O  O   . HIS   A 1 396 ? -36.266 -4.358  43.732 1.00 71.98  ? 692 HIS   A O   1 
ATOM   3102 C  CB  . HIS   A 1 396 ? -35.681 -1.526  43.970 1.00 65.12  ? 692 HIS   A CB  1 
ATOM   3103 C  CG  . HIS   A 1 396 ? -35.045 -0.266  44.473 1.00 70.92  ? 692 HIS   A CG  1 
ATOM   3104 N  ND1 . HIS   A 1 396 ? -34.553 -0.147  45.757 1.00 70.38  ? 692 HIS   A ND1 1 
ATOM   3105 C  CD2 . HIS   A 1 396 ? -34.795 0.917   43.861 1.00 71.93  ? 692 HIS   A CD2 1 
ATOM   3106 C  CE1 . HIS   A 1 396 ? -34.043 1.062   45.919 1.00 71.15  ? 692 HIS   A CE1 1 
ATOM   3107 N  NE2 . HIS   A 1 396 ? -34.175 1.726   44.783 1.00 71.04  ? 692 HIS   A NE2 1 
ATOM   3108 N  N   . GLN   A 1 397 ? -34.922 -4.343  41.935 1.00 64.77  ? 693 GLN   A N   1 
ATOM   3109 C  CA  . GLN   A 1 397 ? -35.592 -5.412  41.211 1.00 62.56  ? 693 GLN   A CA  1 
ATOM   3110 C  C   . GLN   A 1 397 ? -34.698 -6.637  41.216 1.00 59.75  ? 693 GLN   A C   1 
ATOM   3111 O  O   . GLN   A 1 397 ? -33.628 -6.625  40.598 1.00 58.78  ? 693 GLN   A O   1 
ATOM   3112 C  CB  . GLN   A 1 397 ? -35.884 -4.978  39.780 1.00 62.87  ? 693 GLN   A CB  1 
ATOM   3113 C  CG  . GLN   A 1 397 ? -36.496 -6.070  38.923 1.00 59.18  ? 693 GLN   A CG  1 
ATOM   3114 C  CD  . GLN   A 1 397 ? -37.874 -6.442  39.413 1.00 62.23  ? 693 GLN   A CD  1 
ATOM   3115 O  OE1 . GLN   A 1 397 ? -38.776 -5.599  39.465 1.00 63.12  ? 693 GLN   A OE1 1 
ATOM   3116 N  NE2 . GLN   A 1 397 ? -38.049 -7.708  39.786 1.00 67.76  ? 693 GLN   A NE2 1 
ATOM   3117 N  N   . GLU   A 1 398 ? -35.127 -7.679  41.929 1.00 55.66  ? 694 GLU   A N   1 
ATOM   3118 C  CA  . GLU   A 1 398 ? -34.474 -8.973  41.807 1.00 55.61  ? 694 GLU   A CA  1 
ATOM   3119 C  C   . GLU   A 1 398 ? -34.535 -9.456  40.361 1.00 57.42  ? 694 GLU   A C   1 
ATOM   3120 O  O   . GLU   A 1 398 ? -35.535 -9.257  39.667 1.00 65.20  ? 694 GLU   A O   1 
ATOM   3121 C  CB  . GLU   A 1 398 ? -35.133 -9.990  42.737 1.00 51.87  ? 694 GLU   A CB  1 
ATOM   3122 C  CG  . GLU   A 1 398 ? -34.962 -9.602  44.223 1.00 59.73  ? 694 GLU   A CG  1 
ATOM   3123 C  CD  . GLU   A 1 398 ? -35.700 -10.519 45.161 1.00 68.28  ? 694 GLU   A CD  1 
ATOM   3124 O  OE1 . GLU   A 1 398 ? -35.437 -10.431 46.386 1.00 74.50  ? 694 GLU   A OE1 1 
ATOM   3125 O  OE2 . GLU   A 1 398 ? -36.532 -11.324 44.679 1.00 74.45  ? 694 GLU   A OE2 1 
ATOM   3126 N  N   . MET   A 1 399 ? -33.450 -10.087 39.910 1.00 62.64  ? 695 MET   A N   1 
ATOM   3127 C  CA  . MET   A 1 399 ? -33.355 -10.636 38.563 1.00 61.03  ? 695 MET   A CA  1 
ATOM   3128 C  C   . MET   A 1 399 ? -32.702 -12.009 38.605 1.00 65.19  ? 695 MET   A C   1 
ATOM   3129 O  O   . MET   A 1 399 ? -31.697 -12.199 39.294 1.00 66.79  ? 695 MET   A O   1 
ATOM   3130 C  CB  . MET   A 1 399 ? -32.525 -9.723  37.628 1.00 52.56  ? 695 MET   A CB  1 
ATOM   3131 C  CG  . MET   A 1 399 ? -33.057 -8.305  37.452 1.00 53.78  ? 695 MET   A CG  1 
ATOM   3132 S  SD  . MET   A 1 399 ? -31.905 -7.142  36.678 1.00 57.73  ? 695 MET   A SD  1 
ATOM   3133 C  CE  . MET   A 1 399 ? -32.688 -5.590  37.113 1.00 60.55  ? 695 MET   A CE  1 
ATOM   3134 N  N   . LEU   A 1 400 ? -33.248 -12.956 37.840 1.00 57.83  ? 696 LEU   A N   1 
ATOM   3135 C  CA  . LEU   A 1 400 ? -32.623 -14.260 37.658 1.00 51.66  ? 696 LEU   A CA  1 
ATOM   3136 C  C   . LEU   A 1 400 ? -31.813 -14.243 36.371 1.00 63.66  ? 696 LEU   A C   1 
ATOM   3137 O  O   . LEU   A 1 400 ? -32.328 -13.866 35.307 1.00 58.28  ? 696 LEU   A O   1 
ATOM   3138 C  CB  . LEU   A 1 400 ? -33.658 -15.385 37.594 1.00 52.55  ? 696 LEU   A CB  1 
ATOM   3139 C  CG  . LEU   A 1 400 ? -34.555 -15.642 38.802 1.00 61.12  ? 696 LEU   A CG  1 
ATOM   3140 C  CD1 . LEU   A 1 400 ? -35.573 -16.732 38.488 1.00 61.04  ? 696 LEU   A CD1 1 
ATOM   3141 C  CD2 . LEU   A 1 400 ? -33.732 -15.990 40.028 1.00 64.08  ? 696 LEU   A CD2 1 
ATOM   3142 N  N   . ASN   A 1 401 ? -30.552 -14.644 36.463 1.00 62.16  ? 697 ASN   A N   1 
ATOM   3143 C  CA  . ASN   A 1 401 ? -29.707 -14.745 35.282 1.00 52.86  ? 697 ASN   A CA  1 
ATOM   3144 C  C   . ASN   A 1 401 ? -29.577 -16.198 34.864 1.00 55.76  ? 697 ASN   A C   1 
ATOM   3145 O  O   . ASN   A 1 401 ? -29.320 -17.070 35.700 1.00 56.86  ? 697 ASN   A O   1 
ATOM   3146 C  CB  . ASN   A 1 401 ? -28.322 -14.152 35.517 1.00 53.79  ? 697 ASN   A CB  1 
ATOM   3147 C  CG  . ASN   A 1 401 ? -27.623 -13.843 34.229 1.00 56.46  ? 697 ASN   A CG  1 
ATOM   3148 O  OD1 . ASN   A 1 401 ? -28.251 -13.849 33.173 1.00 56.58  ? 697 ASN   A OD1 1 
ATOM   3149 N  ND2 . ASN   A 1 401 ? -26.329 -13.556 34.297 1.00 51.54  ? 697 ASN   A ND2 1 
ATOM   3150 N  N   . TYR   A 1 402 ? -29.754 -16.446 33.565 1.00 64.36  ? 698 TYR   A N   1 
ATOM   3151 C  CA  . TYR   A 1 402 ? -29.579 -17.762 32.980 1.00 59.76  ? 698 TYR   A CA  1 
ATOM   3152 C  C   . TYR   A 1 402 ? -29.403 -17.590 31.467 1.00 60.30  ? 698 TYR   A C   1 
ATOM   3153 O  O   . TYR   A 1 402 ? -29.665 -16.517 30.897 1.00 49.71  ? 698 TYR   A O   1 
ATOM   3154 C  CB  . TYR   A 1 402 ? -30.752 -18.692 33.338 1.00 64.25  ? 698 TYR   A CB  1 
ATOM   3155 C  CG  . TYR   A 1 402 ? -32.143 -18.095 33.180 1.00 64.28  ? 698 TYR   A CG  1 
ATOM   3156 C  CD1 . TYR   A 1 402 ? -32.813 -18.168 31.962 1.00 65.81  ? 698 TYR   A CD1 1 
ATOM   3157 C  CD2 . TYR   A 1 402 ? -32.800 -17.475 34.263 1.00 62.65  ? 698 TYR   A CD2 1 
ATOM   3158 C  CE1 . TYR   A 1 402 ? -34.080 -17.638 31.794 1.00 62.45  ? 698 TYR   A CE1 1 
ATOM   3159 C  CE2 . TYR   A 1 402 ? -34.087 -16.938 34.109 1.00 62.43  ? 698 TYR   A CE2 1 
ATOM   3160 C  CZ  . TYR   A 1 402 ? -34.720 -17.033 32.857 1.00 68.77  ? 698 TYR   A CZ  1 
ATOM   3161 O  OH  . TYR   A 1 402 ? -35.987 -16.521 32.648 1.00 66.73  ? 698 TYR   A OH  1 
ATOM   3162 N  N   . ARG   A 1 403 ? -28.934 -18.658 30.818 1.00 58.12  ? 699 ARG   A N   1 
ATOM   3163 C  CA  . ARG   A 1 403 ? -28.467 -18.574 29.431 1.00 62.16  ? 699 ARG   A CA  1 
ATOM   3164 C  C   . ARG   A 1 403 ? -29.431 -19.322 28.520 1.00 60.51  ? 699 ARG   A C   1 
ATOM   3165 O  O   . ARG   A 1 403 ? -29.504 -20.556 28.549 1.00 59.67  ? 699 ARG   A O   1 
ATOM   3166 C  CB  . ARG   A 1 403 ? -27.047 -19.123 29.294 1.00 69.59  ? 699 ARG   A CB  1 
ATOM   3167 C  CG  . ARG   A 1 403 ? -26.075 -18.501 30.282 1.00 84.36  ? 699 ARG   A CG  1 
ATOM   3168 C  CD  . ARG   A 1 403 ? -25.085 -17.609 29.572 1.00 94.21  ? 699 ARG   A CD  1 
ATOM   3169 N  NE  . ARG   A 1 403 ? -23.873 -18.347 29.235 1.00 106.79 ? 699 ARG   A NE  1 
ATOM   3170 C  CZ  . ARG   A 1 403 ? -22.937 -17.910 28.399 1.00 110.53 ? 699 ARG   A CZ  1 
ATOM   3171 N  NH1 . ARG   A 1 403 ? -23.075 -16.732 27.795 1.00 108.06 ? 699 ARG   A NH1 1 
ATOM   3172 N  NH2 . ARG   A 1 403 ? -21.863 -18.657 28.163 1.00 112.98 ? 699 ARG   A NH2 1 
ATOM   3173 N  N   . LEU   A 1 404 ? -30.172 -18.573 27.724 1.00 64.00  ? 700 LEU   A N   1 
ATOM   3174 C  CA  . LEU   A 1 404 ? -31.026 -19.137 26.699 1.00 57.91  ? 700 LEU   A CA  1 
ATOM   3175 C  C   . LEU   A 1 404 ? -30.371 -18.970 25.329 1.00 62.66  ? 700 LEU   A C   1 
ATOM   3176 O  O   . LEU   A 1 404 ? -29.510 -18.112 25.116 1.00 57.31  ? 700 LEU   A O   1 
ATOM   3177 C  CB  . LEU   A 1 404 ? -32.402 -18.464 26.713 1.00 59.44  ? 700 LEU   A CB  1 
ATOM   3178 C  CG  . LEU   A 1 404 ? -33.220 -18.424 28.007 1.00 64.10  ? 700 LEU   A CG  1 
ATOM   3179 C  CD1 . LEU   A 1 404 ? -34.477 -17.602 27.772 1.00 64.29  ? 700 LEU   A CD1 1 
ATOM   3180 C  CD2 . LEU   A 1 404 ? -33.579 -19.824 28.502 1.00 73.90  ? 700 LEU   A CD2 1 
ATOM   3181 N  N   . THR   A 1 405 ? -30.802 -19.801 24.394 1.00 60.99  ? 701 THR   A N   1 
ATOM   3182 C  CA  . THR   A 1 405 ? -30.328 -19.733 23.022 1.00 61.25  ? 701 THR   A CA  1 
ATOM   3183 C  C   . THR   A 1 405 ? -31.516 -19.517 22.083 1.00 60.88  ? 701 THR   A C   1 
ATOM   3184 O  O   . THR   A 1 405 ? -32.641 -19.898 22.424 1.00 59.98  ? 701 THR   A O   1 
ATOM   3185 C  CB  . THR   A 1 405 ? -29.569 -21.022 22.664 1.00 68.82  ? 701 THR   A CB  1 
ATOM   3186 O  OG1 . THR   A 1 405 ? -28.646 -20.766 21.607 1.00 76.48  ? 701 THR   A OG1 1 
ATOM   3187 C  CG2 . THR   A 1 405 ? -30.515 -22.124 22.257 1.00 70.08  ? 701 THR   A CG2 1 
ATOM   3188 N  N   . PRO   A 1 406 ? -31.326 -18.846 20.918 1.00 57.48  ? 702 PRO   A N   1 
ATOM   3189 C  CA  . PRO   A 1 406 ? -30.171 -18.134 20.337 1.00 54.98  ? 702 PRO   A CA  1 
ATOM   3190 C  C   . PRO   A 1 406 ? -29.536 -17.116 21.289 1.00 59.06  ? 702 PRO   A C   1 
ATOM   3191 O  O   . PRO   A 1 406 ? -30.256 -16.595 22.144 1.00 55.68  ? 702 PRO   A O   1 
ATOM   3192 C  CB  . PRO   A 1 406 ? -30.776 -17.410 19.127 1.00 57.56  ? 702 PRO   A CB  1 
ATOM   3193 C  CG  . PRO   A 1 406 ? -31.933 -18.259 18.694 1.00 54.73  ? 702 PRO   A CG  1 
ATOM   3194 C  CD  . PRO   A 1 406 ? -32.480 -18.866 19.991 1.00 61.75  ? 702 PRO   A CD  1 
ATOM   3195 N  N   . SER   A 1 407 ? -28.241 -16.827 21.125 1.00 53.11  ? 703 SER   A N   1 
ATOM   3196 C  CA  . SER   A 1 407 ? -27.532 -15.954 22.046 1.00 56.78  ? 703 SER   A CA  1 
ATOM   3197 C  C   . SER   A 1 407 ? -26.348 -15.276 21.364 1.00 57.79  ? 703 SER   A C   1 
ATOM   3198 O  O   . SER   A 1 407 ? -25.834 -15.737 20.336 1.00 62.46  ? 703 SER   A O   1 
ATOM   3199 C  CB  . SER   A 1 407 ? -27.053 -16.737 23.277 1.00 64.28  ? 703 SER   A CB  1 
ATOM   3200 O  OG  . SER   A 1 407 ? -26.169 -17.766 22.873 1.00 73.54  ? 703 SER   A OG  1 
ATOM   3201 N  N   . PHE   A 1 408 ? -25.947 -14.143 21.939 1.00 55.93  ? 704 PHE   A N   1 
ATOM   3202 C  CA  . PHE   A 1 408 ? -24.680 -13.494 21.624 1.00 57.33  ? 704 PHE   A CA  1 
ATOM   3203 C  C   . PHE   A 1 408 ? -23.646 -13.926 22.656 1.00 61.20  ? 704 PHE   A C   1 
ATOM   3204 O  O   . PHE   A 1 408 ? -23.910 -13.853 23.859 1.00 59.99  ? 704 PHE   A O   1 
ATOM   3205 C  CB  . PHE   A 1 408 ? -24.817 -11.971 21.632 1.00 52.35  ? 704 PHE   A CB  1 
ATOM   3206 C  CG  . PHE   A 1 408 ? -25.644 -11.429 20.501 1.00 55.86  ? 704 PHE   A CG  1 
ATOM   3207 C  CD1 . PHE   A 1 408 ? -26.952 -11.011 20.719 1.00 56.66  ? 704 PHE   A CD1 1 
ATOM   3208 C  CD2 . PHE   A 1 408 ? -25.099 -11.315 19.215 1.00 54.64  ? 704 PHE   A CD2 1 
ATOM   3209 C  CE1 . PHE   A 1 408 ? -27.714 -10.502 19.662 1.00 57.52  ? 704 PHE   A CE1 1 
ATOM   3210 C  CE2 . PHE   A 1 408 ? -25.855 -10.805 18.153 1.00 52.76  ? 704 PHE   A CE2 1 
ATOM   3211 C  CZ  . PHE   A 1 408 ? -27.153 -10.401 18.372 1.00 54.04  ? 704 PHE   A CZ  1 
ATOM   3212 N  N   . GLU   A 1 409 ? -22.482 -14.379 22.187 1.00 54.60  ? 705 GLU   A N   1 
ATOM   3213 C  CA  . GLU   A 1 409 ? -21.417 -14.841 23.058 1.00 52.68  ? 705 GLU   A CA  1 
ATOM   3214 C  C   . GLU   A 1 409 ? -20.128 -14.069 22.809 1.00 62.04  ? 705 GLU   A C   1 
ATOM   3215 O  O   . GLU   A 1 409 ? -19.910 -13.483 21.742 1.00 61.89  ? 705 GLU   A O   1 
ATOM   3216 C  CB  . GLU   A 1 409 ? -21.149 -16.342 22.889 1.00 54.97  ? 705 GLU   A CB  1 
ATOM   3217 C  CG  . GLU   A 1 409 ? -22.375 -17.244 23.018 1.00 73.66  ? 705 GLU   A CG  1 
ATOM   3218 C  CD  . GLU   A 1 409 ? -22.990 -17.258 24.417 1.00 86.75  ? 705 GLU   A CD  1 
ATOM   3219 O  OE1 . GLU   A 1 409 ? -22.497 -16.536 25.317 1.00 89.48  ? 705 GLU   A OE1 1 
ATOM   3220 O  OE2 . GLU   A 1 409 ? -23.975 -18.002 24.610 1.00 91.69  ? 705 GLU   A OE2 1 
ATOM   3221 N  N   . TYR   A 1 410 ? -19.274 -14.063 23.833 1.00 53.81  ? 706 TYR   A N   1 
ATOM   3222 C  CA  . TYR   A 1 410 ? -17.942 -13.532 23.633 1.00 53.72  ? 706 TYR   A CA  1 
ATOM   3223 C  C   . TYR   A 1 410 ? -17.098 -14.522 22.846 1.00 58.49  ? 706 TYR   A C   1 
ATOM   3224 O  O   . TYR   A 1 410 ? -17.369 -15.729 22.804 1.00 64.17  ? 706 TYR   A O   1 
ATOM   3225 C  CB  . TYR   A 1 410 ? -17.261 -13.237 24.964 1.00 62.99  ? 706 TYR   A CB  1 
ATOM   3226 C  CG  . TYR   A 1 410 ? -17.956 -12.196 25.793 1.00 62.54  ? 706 TYR   A CG  1 
ATOM   3227 C  CD1 . TYR   A 1 410 ? -18.524 -12.533 27.019 1.00 69.84  ? 706 TYR   A CD1 1 
ATOM   3228 C  CD2 . TYR   A 1 410 ? -18.038 -10.874 25.366 1.00 64.83  ? 706 TYR   A CD2 1 
ATOM   3229 C  CE1 . TYR   A 1 410 ? -19.146 -11.592 27.797 1.00 75.05  ? 706 TYR   A CE1 1 
ATOM   3230 C  CE2 . TYR   A 1 410 ? -18.673 -9.920  26.138 1.00 70.58  ? 706 TYR   A CE2 1 
ATOM   3231 C  CZ  . TYR   A 1 410 ? -19.218 -10.290 27.361 1.00 77.81  ? 706 TYR   A CZ  1 
ATOM   3232 O  OH  . TYR   A 1 410 ? -19.849 -9.361  28.147 1.00 75.46  ? 706 TYR   A OH  1 
ATOM   3233 N  N   . GLN   A 1 411 ? -16.038 -14.001 22.246 1.00 53.36  ? 707 GLN   A N   1 
ATOM   3234 C  CA  . GLN   A 1 411 ? -15.098 -14.823 21.506 1.00 58.69  ? 707 GLN   A CA  1 
ATOM   3235 C  C   . GLN   A 1 411 ? -13.734 -14.165 21.607 1.00 61.99  ? 707 GLN   A C   1 
ATOM   3236 O  O   . GLN   A 1 411 ? -13.643 -12.968 21.901 1.00 61.73  ? 707 GLN   A O   1 
ATOM   3237 C  CB  . GLN   A 1 411 ? -15.542 -14.975 20.041 1.00 65.72  ? 707 GLN   A CB  1 
ATOM   3238 C  CG  . GLN   A 1 411 ? -15.503 -13.690 19.264 1.00 70.85  ? 707 GLN   A CG  1 
ATOM   3239 C  CD  . GLN   A 1 411 ? -15.977 -13.861 17.829 1.00 79.64  ? 707 GLN   A CD  1 
ATOM   3240 O  OE1 . GLN   A 1 411 ? -15.934 -14.960 17.272 1.00 82.29  ? 707 GLN   A OE1 1 
ATOM   3241 N  NE2 . GLN   A 1 411 ? -16.442 -12.774 17.229 1.00 79.88  ? 707 GLN   A NE2 1 
ATOM   3242 N  N   . PRO   A 1 412 ? -12.657 -14.924 21.412 1.00 75.67  ? 708 PRO   A N   1 
ATOM   3243 C  CA  . PRO   A 1 412 ? -11.313 -14.341 21.528 1.00 84.29  ? 708 PRO   A CA  1 
ATOM   3244 C  C   . PRO   A 1 412 ? -11.082 -13.245 20.503 1.00 88.17  ? 708 PRO   A C   1 
ATOM   3245 O  O   . PRO   A 1 412 ? -11.710 -13.211 19.443 1.00 87.45  ? 708 PRO   A O   1 
ATOM   3246 C  CB  . PRO   A 1 412 ? -10.380 -15.534 21.274 1.00 91.53  ? 708 PRO   A CB  1 
ATOM   3247 C  CG  . PRO   A 1 412 ? -11.197 -16.735 21.622 1.00 91.41  ? 708 PRO   A CG  1 
ATOM   3248 C  CD  . PRO   A 1 412 ? -12.623 -16.392 21.286 1.00 84.10  ? 708 PRO   A CD  1 
ATOM   3249 N  N   . ASP   A 1 413 ? -10.165 -12.343 20.829 1.00 86.53  ? 709 ASP   A N   1 
ATOM   3250 C  CA  . ASP   A 1 413 ? -9.723  -11.375 19.841 1.00 92.11  ? 709 ASP   A CA  1 
ATOM   3251 C  C   . ASP   A 1 413 ? -9.015  -12.104 18.703 1.00 98.14  ? 709 ASP   A C   1 
ATOM   3252 O  O   . ASP   A 1 413 ? -8.226  -13.023 18.949 1.00 97.80  ? 709 ASP   A O   1 
ATOM   3253 C  CB  . ASP   A 1 413 ? -8.797  -10.338 20.473 1.00 101.48 ? 709 ASP   A CB  1 
ATOM   3254 C  CG  . ASP   A 1 413 ? -9.559  -9.275  21.238 1.00 106.24 ? 709 ASP   A CG  1 
ATOM   3255 O  OD1 . ASP   A 1 413 ? -10.723 -9.008  20.868 1.00 106.07 ? 709 ASP   A OD1 1 
ATOM   3256 O  OD2 . ASP   A 1 413 ? -9.001  -8.706  22.201 1.00 105.97 ? 709 ASP   A OD2 1 
ATOM   3257 N  N   . PRO   A 1 414 ? -9.280  -11.733 17.451 1.00 103.76 ? 710 PRO   A N   1 
ATOM   3258 C  CA  . PRO   A 1 414 ? -8.778  -12.542 16.327 1.00 108.56 ? 710 PRO   A CA  1 
ATOM   3259 C  C   . PRO   A 1 414 ? -7.268  -12.511 16.163 1.00 113.95 ? 710 PRO   A C   1 
ATOM   3260 O  O   . PRO   A 1 414 ? -6.723  -13.417 15.521 1.00 122.59 ? 710 PRO   A O   1 
ATOM   3261 C  CB  . PRO   A 1 414 ? -9.485  -11.934 15.107 1.00 102.36 ? 710 PRO   A CB  1 
ATOM   3262 C  CG  . PRO   A 1 414 ? -9.852  -10.553 15.523 1.00 101.87 ? 710 PRO   A CG  1 
ATOM   3263 C  CD  . PRO   A 1 414 ? -10.108 -10.600 17.005 1.00 104.71 ? 710 PRO   A CD  1 
ATOM   3264 N  N   . TRP   A 1 415 ? -6.573  -11.514 16.707 1.00 104.81 ? 711 TRP   A N   1 
ATOM   3265 C  CA  . TRP   A 1 415 ? -5.122  -11.475 16.580 1.00 107.24 ? 711 TRP   A CA  1 
ATOM   3266 C  C   . TRP   A 1 415 ? -4.420  -12.385 17.581 1.00 106.60 ? 711 TRP   A C   1 
ATOM   3267 O  O   . TRP   A 1 415 ? -3.185  -12.430 17.593 1.00 109.91 ? 711 TRP   A O   1 
ATOM   3268 C  CB  . TRP   A 1 415 ? -4.604  -10.037 16.724 1.00 106.13 ? 711 TRP   A CB  1 
ATOM   3269 C  CG  . TRP   A 1 415 ? -5.025  -9.333  17.987 1.00 97.07  ? 711 TRP   A CG  1 
ATOM   3270 C  CD1 . TRP   A 1 415 ? -4.381  -9.353  19.191 1.00 100.47 ? 711 TRP   A CD1 1 
ATOM   3271 C  CD2 . TRP   A 1 415 ? -6.173  -8.488  18.161 1.00 93.22  ? 711 TRP   A CD2 1 
ATOM   3272 N  NE1 . TRP   A 1 415 ? -5.061  -8.583  20.104 1.00 92.60  ? 711 TRP   A NE1 1 
ATOM   3273 C  CE2 . TRP   A 1 415 ? -6.164  -8.042  19.497 1.00 93.74  ? 711 TRP   A CE2 1 
ATOM   3274 C  CE3 . TRP   A 1 415 ? -7.208  -8.070  17.318 1.00 95.45  ? 711 TRP   A CE3 1 
ATOM   3275 C  CZ2 . TRP   A 1 415 ? -7.149  -7.198  20.009 1.00 90.81  ? 711 TRP   A CZ2 1 
ATOM   3276 C  CZ3 . TRP   A 1 415 ? -8.187  -7.235  17.827 1.00 88.63  ? 711 TRP   A CZ3 1 
ATOM   3277 C  CH2 . TRP   A 1 415 ? -8.151  -6.810  19.160 1.00 91.92  ? 711 TRP   A CH2 1 
ATOM   3278 N  N   . ASN   A 1 416 ? -5.172  -13.107 18.411 1.00 99.52  ? 712 ASN   A N   1 
ATOM   3279 C  CA  . ASN   A 1 416 ? -4.616  -14.109 19.307 1.00 107.80 ? 712 ASN   A CA  1 
ATOM   3280 C  C   . ASN   A 1 416 ? -4.767  -15.521 18.764 1.00 107.20 ? 712 ASN   A C   1 
ATOM   3281 O  O   . ASN   A 1 416 ? -4.104  -16.437 19.262 1.00 107.92 ? 712 ASN   A O   1 
ATOM   3282 C  CB  . ASN   A 1 416 ? -5.284  -14.025 20.686 1.00 106.58 ? 712 ASN   A CB  1 
ATOM   3283 C  CG  . ASN   A 1 416 ? -5.195  -12.640 21.295 1.00 112.36 ? 712 ASN   A CG  1 
ATOM   3284 O  OD1 . ASN   A 1 416 ? -4.243  -11.899 21.039 1.00 121.16 ? 712 ASN   A OD1 1 
ATOM   3285 N  ND2 . ASN   A 1 416 ? -6.188  -12.282 22.106 1.00 109.54 ? 712 ASN   A ND2 1 
ATOM   3286 N  N   . THR   A 1 417 ? -5.606  -15.708 17.752 1.00 99.07  ? 713 THR   A N   1 
ATOM   3287 C  CA  . THR   A 1 417 ? -5.951  -17.013 17.209 1.00 102.06 ? 713 THR   A CA  1 
ATOM   3288 C  C   . THR   A 1 417 ? -5.510  -17.213 15.770 1.00 107.98 ? 713 THR   A C   1 
ATOM   3289 O  O   . THR   A 1 417 ? -5.156  -18.334 15.395 1.00 108.65 ? 713 THR   A O   1 
ATOM   3290 C  CB  . THR   A 1 417 ? -7.473  -17.213 17.285 1.00 106.90 ? 713 THR   A CB  1 
ATOM   3291 O  OG1 . THR   A 1 417 ? -8.113  -15.932 17.380 1.00 104.68 ? 713 THR   A OG1 1 
ATOM   3292 C  CG2 . THR   A 1 417 ? -7.849  -18.046 18.502 1.00 114.52 ? 713 THR   A CG2 1 
ATOM   3293 N  N   . HIS   A 1 418 ? -5.503  -16.152 14.970 1.00 107.80 ? 714 HIS   A N   1 
ATOM   3294 C  CA  . HIS   A 1 418 ? -5.377  -16.242 13.520 1.00 113.41 ? 714 HIS   A CA  1 
ATOM   3295 C  C   . HIS   A 1 418 ? -4.018  -16.817 13.133 1.00 125.95 ? 714 HIS   A C   1 
ATOM   3296 O  O   . HIS   A 1 418 ? -2.993  -16.138 13.253 1.00 132.71 ? 714 HIS   A O   1 
ATOM   3297 C  CB  . HIS   A 1 418 ? -5.585  -14.854 12.921 1.00 108.45 ? 714 HIS   A CB  1 
ATOM   3298 C  CG  . HIS   A 1 418 ? -5.607  -14.830 11.426 1.00 104.23 ? 714 HIS   A CG  1 
ATOM   3299 N  ND1 . HIS   A 1 418 ? -6.333  -15.731 10.678 1.00 106.08 ? 714 HIS   A ND1 1 
ATOM   3300 C  CD2 . HIS   A 1 418 ? -5.005  -14.002 10.538 1.00 110.50 ? 714 HIS   A CD2 1 
ATOM   3301 C  CE1 . HIS   A 1 418 ? -6.170  -15.465 9.392  1.00 107.55 ? 714 HIS   A CE1 1 
ATOM   3302 N  NE2 . HIS   A 1 418 ? -5.368  -14.420 9.280  1.00 106.15 ? 714 HIS   A NE2 1 
ATOM   3303 N  N   . VAL   A 1 419 ? -4.006  -18.068 12.667 1.00 125.25 ? 715 VAL   A N   1 
ATOM   3304 C  CA  . VAL   A 1 419 ? -2.821  -18.622 12.022 1.00 131.13 ? 715 VAL   A CA  1 
ATOM   3305 C  C   . VAL   A 1 419 ? -2.515  -17.723 10.831 1.00 133.53 ? 715 VAL   A C   1 
ATOM   3306 O  O   . VAL   A 1 419 ? -3.098  -17.872 9.749  1.00 123.05 ? 715 VAL   A O   1 
ATOM   3307 C  CB  . VAL   A 1 419 ? -3.014  -20.092 11.599 1.00 130.43 ? 715 VAL   A CB  1 
ATOM   3308 C  CG1 . VAL   A 1 419 ? -1.865  -20.559 10.710 1.00 135.38 ? 715 VAL   A CG1 1 
ATOM   3309 C  CG2 . VAL   A 1 419 ? -3.136  -20.998 12.826 1.00 124.07 ? 715 VAL   A CG2 1 
ATOM   3310 N  N   . TRP   A 1 420 ? -1.619  -16.766 11.040 1.00 149.40 ? 716 TRP   A N   1 
ATOM   3311 C  CA  . TRP   A 1 420 ? -1.388  -15.699 10.078 1.00 159.95 ? 716 TRP   A CA  1 
ATOM   3312 C  C   . TRP   A 1 420 ? -0.645  -16.254 8.863  1.00 178.08 ? 716 TRP   A C   1 
ATOM   3313 O  O   . TRP   A 1 420 ? -0.425  -17.461 8.725  1.00 181.40 ? 716 TRP   A O   1 
ATOM   3314 C  CB  . TRP   A 1 420 ? -0.632  -14.556 10.747 1.00 156.21 ? 716 TRP   A CB  1 
ATOM   3315 C  CG  . TRP   A 1 420 ? -1.073  -13.205 10.287 1.00 150.07 ? 716 TRP   A CG  1 
ATOM   3316 C  CD1 . TRP   A 1 420 ? -1.166  -12.768 8.999  1.00 151.55 ? 716 TRP   A CD1 1 
ATOM   3317 C  CD2 . TRP   A 1 420 ? -1.472  -12.105 11.111 1.00 144.14 ? 716 TRP   A CD2 1 
ATOM   3318 N  NE1 . TRP   A 1 420 ? -1.603  -11.469 8.968  1.00 147.12 ? 716 TRP   A NE1 1 
ATOM   3319 C  CE2 . TRP   A 1 420 ? -1.797  -11.037 10.252 1.00 142.91 ? 716 TRP   A CE2 1 
ATOM   3320 C  CE3 . TRP   A 1 420 ? -1.589  -11.920 12.489 1.00 141.82 ? 716 TRP   A CE3 1 
ATOM   3321 C  CZ2 . TRP   A 1 420 ? -2.228  -9.805  10.725 1.00 139.81 ? 716 TRP   A CZ2 1 
ATOM   3322 C  CZ3 . TRP   A 1 420 ? -2.016  -10.696 12.957 1.00 141.01 ? 716 TRP   A CZ3 1 
ATOM   3323 C  CH2 . TRP   A 1 420 ? -2.331  -9.654  12.076 1.00 137.81 ? 716 TRP   A CH2 1 
ATOM   3324 N  N   . LYS   A 1 421 ? -0.253  -15.360 7.958  1.00 92.41  ? 717 LYS   A N   1 
ATOM   3325 C  CA  . LYS   A 1 421 ? 0.497   -15.754 6.772  1.00 105.53 ? 717 LYS   A CA  1 
ATOM   3326 C  C   . LYS   A 1 421 ? 1.437   -14.637 6.329  1.00 113.28 ? 717 LYS   A C   1 
ATOM   3327 O  O   . LYS   A 1 421 ? 2.477   -14.410 6.965  1.00 118.98 ? 717 LYS   A O   1 
ATOM   3328 C  CB  . LYS   A 1 421 ? -0.460  -16.132 5.641  1.00 105.29 ? 717 LYS   A CB  1 
ATOM   3329 C  CG  . LYS   A 1 421 ? -0.173  -17.493 5.041  1.00 108.90 ? 717 LYS   A CG  1 
ATOM   3330 C  CD  . LYS   A 1 421 ? 1.279   -17.592 4.577  1.00 112.85 ? 717 LYS   A CD  1 
ATOM   3331 C  CE  . LYS   A 1 421 ? 1.532   -18.827 3.710  1.00 109.15 ? 717 LYS   A CE  1 
ATOM   3332 N  NZ  . LYS   A 1 421 ? 0.940   -18.730 2.348  1.00 107.63 ? 717 LYS   A NZ  1 
ATOM   3333 N  N   . GLY   A 1 422 ? 1.075   -13.935 5.259  1.00 113.68 ? 718 GLY   A N   1 
ATOM   3334 C  CA  . GLY   A 1 422 ? 1.894   -12.879 4.684  1.00 118.12 ? 718 GLY   A CA  1 
ATOM   3335 C  C   . GLY   A 1 422 ? 2.423   -11.811 5.625  1.00 129.20 ? 718 GLY   A C   1 
ATOM   3336 O  O   . GLY   A 1 422 ? 2.035   -11.712 6.791  1.00 132.18 ? 718 GLY   A O   1 
ATOM   3337 O  OXT . GLY   A 1 422 ? 3.275   -11.008 5.238  1.00 132.97 ? 718 GLY   A OXT 1 
HETATM 3338 C  CHA . HEM   B 2 .   ? -25.239 -4.394  26.208 1.00 51.33  ? 801 HEM   A CHA 1 
HETATM 3339 C  CHB . HEM   B 2 .   ? -28.380 -0.711  25.802 1.00 66.72  ? 801 HEM   A CHB 1 
HETATM 3340 C  CHC . HEM   B 2 .   ? -29.618 -2.349  21.373 1.00 58.93  ? 801 HEM   A CHC 1 
HETATM 3341 C  CHD . HEM   B 2 .   ? -27.392 -6.519  22.397 1.00 57.53  ? 801 HEM   A CHD 1 
HETATM 3342 C  C1A . HEM   B 2 .   ? -25.851 -3.172  26.408 1.00 59.37  ? 801 HEM   A C1A 1 
HETATM 3343 C  C2A . HEM   B 2 .   ? -25.454 -2.117  27.327 1.00 61.29  ? 801 HEM   A C2A 1 
HETATM 3344 C  C3A . HEM   B 2 .   ? -26.321 -1.097  27.207 1.00 53.82  ? 801 HEM   A C3A 1 
HETATM 3345 C  C4A . HEM   B 2 .   ? -27.312 -1.468  26.222 1.00 60.53  ? 801 HEM   A C4A 1 
HETATM 3346 C  CMA . HEM   B 2 .   ? -26.295 0.232   28.017 1.00 54.37  ? 801 HEM   A CMA 1 
HETATM 3347 C  CAA . HEM   B 2 .   ? -24.238 -2.148  28.276 1.00 62.82  ? 801 HEM   A CAA 1 
HETATM 3348 C  CBA . HEM   B 2 .   ? -23.015 -1.948  27.391 1.00 60.18  ? 801 HEM   A CBA 1 
HETATM 3349 C  CGA . HEM   B 2 .   ? -21.798 -1.975  28.266 1.00 67.49  ? 801 HEM   A CGA 1 
HETATM 3350 O  O1A . HEM   B 2 .   ? -21.853 -1.441  29.416 1.00 64.67  ? 801 HEM   A O1A 1 
HETATM 3351 O  O2A . HEM   B 2 .   ? -20.791 -2.548  27.776 1.00 61.39  ? 801 HEM   A O2A 1 
HETATM 3352 C  C1B . HEM   B 2 .   ? -28.965 -0.801  24.561 1.00 62.83  ? 801 HEM   A C1B 1 
HETATM 3353 C  C2B . HEM   B 2 .   ? -29.860 0.170   23.958 1.00 58.36  ? 801 HEM   A C2B 1 
HETATM 3354 C  C3B . HEM   B 2 .   ? -30.211 -0.305  22.757 1.00 65.74  ? 801 HEM   A C3B 1 
HETATM 3355 C  C4B . HEM   B 2 .   ? -29.533 -1.574  22.527 1.00 62.26  ? 801 HEM   A C4B 1 
HETATM 3356 C  CMB . HEM   B 2 .   ? -30.345 1.482   24.612 1.00 60.47  ? 801 HEM   A CMB 1 
HETATM 3357 C  CAB . HEM   B 2 .   ? -31.149 0.393   21.746 1.00 66.44  ? 801 HEM   A CAB 1 
HETATM 3358 C  CBB . HEM   B 2 .   ? -32.062 -0.346  21.107 1.00 72.72  ? 801 HEM   A CBB 1 
HETATM 3359 C  C1C . HEM   B 2 .   ? -29.100 -3.610  21.225 1.00 58.41  ? 801 HEM   A C1C 1 
HETATM 3360 C  C2C . HEM   B 2 .   ? -29.148 -4.459  20.038 1.00 54.73  ? 801 HEM   A C2C 1 
HETATM 3361 C  C3C . HEM   B 2 .   ? -28.519 -5.615  20.353 1.00 52.96  ? 801 HEM   A C3C 1 
HETATM 3362 C  C4C . HEM   B 2 .   ? -28.063 -5.525  21.729 1.00 53.83  ? 801 HEM   A C4C 1 
HETATM 3363 C  CMC . HEM   B 2 .   ? -29.812 -4.053  18.688 1.00 57.28  ? 801 HEM   A CMC 1 
HETATM 3364 C  CAC . HEM   B 2 .   ? -28.242 -6.903  19.567 1.00 48.15  ? 801 HEM   A CAC 1 
HETATM 3365 C  CBC . HEM   B 2 .   ? -28.869 -7.181  18.413 1.00 64.39  ? 801 HEM   A CBC 1 
HETATM 3366 C  C1D . HEM   B 2 .   ? -26.595 -6.311  23.497 1.00 61.49  ? 801 HEM   A C1D 1 
HETATM 3367 C  C2D . HEM   B 2 .   ? -25.663 -7.261  24.050 1.00 59.27  ? 801 HEM   A C2D 1 
HETATM 3368 C  C3D . HEM   B 2 .   ? -25.053 -6.690  25.103 1.00 52.93  ? 801 HEM   A C3D 1 
HETATM 3369 C  C4D . HEM   B 2 .   ? -25.590 -5.347  25.259 1.00 55.32  ? 801 HEM   A C4D 1 
HETATM 3370 C  CMD . HEM   B 2 .   ? -25.453 -8.675  23.481 1.00 60.92  ? 801 HEM   A CMD 1 
HETATM 3371 C  CAD . HEM   B 2 .   ? -23.979 -7.365  25.991 1.00 57.09  ? 801 HEM   A CAD 1 
HETATM 3372 C  CBD . HEM   B 2 .   ? -22.592 -6.824  25.627 1.00 57.44  ? 801 HEM   A CBD 1 
HETATM 3373 C  CGD . HEM   B 2 .   ? -21.560 -7.478  26.528 1.00 60.64  ? 801 HEM   A CGD 1 
HETATM 3374 O  O1D . HEM   B 2 .   ? -21.901 -8.470  27.246 1.00 63.27  ? 801 HEM   A O1D 1 
HETATM 3375 O  O2D . HEM   B 2 .   ? -20.383 -7.019  26.545 1.00 62.98  ? 801 HEM   A O2D 1 
HETATM 3376 N  NA  . HEM   B 2 .   ? -26.980 -2.719  25.751 1.00 59.84  ? 801 HEM   A NA  1 
HETATM 3377 N  NB  . HEM   B 2 .   ? -28.779 -1.852  23.653 1.00 53.95  ? 801 HEM   A NB  1 
HETATM 3378 N  NC  . HEM   B 2 .   ? -28.438 -4.300  22.218 1.00 60.20  ? 801 HEM   A NC  1 
HETATM 3379 N  ND  . HEM   B 2 .   ? -26.532 -5.149  24.244 1.00 57.00  ? 801 HEM   A ND  1 
HETATM 3380 FE FE  . HEM   B 2 .   ? -27.987 -3.723  24.265 1.00 53.96  ? 801 HEM   A FE  1 
HETATM 3381 N  N1  . H4B   C 3 .   ? -21.980 -3.185  33.855 1.00 69.98  ? 802 H4B   A N1  1 
HETATM 3382 C  C2  . H4B   C 3 .   ? -21.981 -2.655  32.619 1.00 57.22  ? 802 H4B   A C2  1 
HETATM 3383 N  N2  . H4B   C 3 .   ? -23.156 -2.233  32.107 1.00 54.28  ? 802 H4B   A N2  1 
HETATM 3384 N  N3  . H4B   C 3 .   ? -20.837 -2.545  31.905 1.00 52.40  ? 802 H4B   A N3  1 
HETATM 3385 C  C4  . H4B   C 3 .   ? -19.661 -2.963  32.416 1.00 55.33  ? 802 H4B   A C4  1 
HETATM 3386 O  O4  . H4B   C 3 .   ? -18.606 -2.847  31.751 1.00 57.44  ? 802 H4B   A O4  1 
HETATM 3387 C  C4A . H4B   C 3 .   ? -19.646 -3.523  33.689 1.00 63.26  ? 802 H4B   A C4A 1 
HETATM 3388 C  C8A . H4B   C 3 .   ? -20.830 -3.608  34.406 1.00 69.41  ? 802 H4B   A C8A 1 
HETATM 3389 N  N5  . H4B   C 3 .   ? -18.500 -3.966  34.244 1.00 57.50  ? 802 H4B   A N5  1 
HETATM 3390 N  N8  . H4B   C 3 .   ? -20.856 -4.146  35.645 1.00 61.12  ? 802 H4B   A N8  1 
HETATM 3391 C  C6  . H4B   C 3 .   ? -18.610 -4.979  35.304 1.00 60.80  ? 802 H4B   A C6  1 
HETATM 3392 C  C7  . H4B   C 3 .   ? -19.625 -4.506  36.339 1.00 62.74  ? 802 H4B   A C7  1 
HETATM 3393 C  C9  . H4B   C 3 .   ? -17.289 -5.226  36.029 1.00 58.65  ? 802 H4B   A C9  1 
HETATM 3394 O  O9  . H4B   C 3 .   ? -16.892 -3.931  36.482 1.00 60.97  ? 802 H4B   A O9  1 
HETATM 3395 C  C10 . H4B   C 3 .   ? -17.487 -6.149  37.245 1.00 60.91  ? 802 H4B   A C10 1 
HETATM 3396 C  C11 . H4B   C 3 .   ? -16.208 -6.479  38.037 1.00 51.83  ? 802 H4B   A C11 1 
HETATM 3397 O  O10 . H4B   C 3 .   ? -18.109 -7.392  36.865 1.00 57.95  ? 802 H4B   A O10 1 
HETATM 3398 C  C11 . A1A0B D 4 .   ? -22.314 -1.185  23.618 1.00 61.39  ? 803 A1A0B A C11 1 
HETATM 3399 C  C12 . A1A0B D 4 .   ? -21.342 -0.216  23.441 1.00 71.66  ? 803 A1A0B A C12 1 
HETATM 3400 C  C13 . A1A0B D 4 .   ? -20.022 -0.475  23.724 1.00 78.76  ? 803 A1A0B A C13 1 
HETATM 3401 C  C14 . A1A0B D 4 .   ? -19.655 -1.740  24.197 1.00 73.05  ? 803 A1A0B A C14 1 
HETATM 3402 C  C15 . A1A0B D 4 .   ? -20.630 -2.731  24.370 1.00 65.02  ? 803 A1A0B A C15 1 
HETATM 3403 C  C16 . A1A0B D 4 .   ? -21.962 -2.450  24.070 1.00 58.65  ? 803 A1A0B A C16 1 
HETATM 3404 C  C17 . A1A0B D 4 .   ? -20.298 -4.122  24.873 1.00 72.42  ? 803 A1A0B A C17 1 
HETATM 3405 C  C02 . A1A0B D 4 .   ? -25.706 0.356   23.435 1.00 57.23  ? 803 A1A0B A C02 1 
HETATM 3406 C  C03 . A1A0B D 4 .   ? -26.298 -0.386  22.404 1.00 52.74  ? 803 A1A0B A C03 1 
HETATM 3407 C  C04 . A1A0B D 4 .   ? -25.566 -1.384  21.789 1.00 59.47  ? 803 A1A0B A C04 1 
HETATM 3408 C  C05 . A1A0B D 4 .   ? -24.273 -1.612  22.231 1.00 64.00  ? 803 A1A0B A C05 1 
HETATM 3409 C  C06 . A1A0B D 4 .   ? -23.720 -0.863  23.261 1.00 60.88  ? 803 A1A0B A C06 1 
HETATM 3410 C  C07 . A1A0B D 4 .   ? -26.132 -2.204  20.651 1.00 56.40  ? 803 A1A0B A C07 1 
HETATM 3411 C  C19 . A1A0B D 4 .   ? -18.044 -4.730  25.430 1.00 84.60  ? 803 A1A0B A C19 1 
HETATM 3412 F  F12 . A1A0B D 4 .   ? -21.660 1.008   23.000 1.00 72.86  ? 803 A1A0B A F12 1 
HETATM 3413 F  F13 . A1A0B D 4 .   ? -19.137 0.532   23.528 1.00 83.44  ? 803 A1A0B A F13 1 
HETATM 3414 N  N01 . A1A0B D 4 .   ? -24.435 0.124   23.847 1.00 60.51  ? 803 A1A0B A N01 1 
HETATM 3415 N  N02 . A1A0B D 4 .   ? -26.428 1.321   24.037 1.00 57.68  ? 803 A1A0B A N02 1 
HETATM 3416 N  N18 . A1A0B D 4 .   ? -19.288 -4.135  25.945 1.00 77.51  ? 803 A1A0B A N18 1 
HETATM 3417 C  C   . ACT   E 5 .   ? -34.730 1.880   25.700 1.00 123.28 ? 804 ACT   A C   1 
HETATM 3418 O  O   . ACT   E 5 .   ? -34.244 2.957   25.288 1.00 124.09 ? 804 ACT   A O   1 
HETATM 3419 O  OXT . ACT   E 5 .   ? -35.029 1.701   26.903 1.00 124.76 ? 804 ACT   A OXT 1 
HETATM 3420 C  CH3 . ACT   E 5 .   ? -34.897 0.745   24.734 1.00 123.12 ? 804 ACT   A CH3 1 
HETATM 3421 ZN ZN  . ZN    F 6 .   ? -24.499 -16.633 41.101 0.50 49.70  ? 805 ZN    A ZN  1 
HETATM 3422 O  O   . HOH   G 7 .   ? -15.079 -21.196 9.516  1.00 70.43  ? 901 HOH   A O   1 
HETATM 3423 O  O   . HOH   G 7 .   ? -29.720 -12.944 40.443 1.00 72.80  ? 902 HOH   A O   1 
HETATM 3424 O  O   . HOH   G 7 .   ? -15.981 -30.032 19.336 1.00 83.82  ? 903 HOH   A O   1 
HETATM 3425 O  O   . HOH   G 7 .   ? -25.285 -4.298  5.939  1.00 69.78  ? 904 HOH   A O   1 
HETATM 3426 O  O   . HOH   G 7 .   ? -28.040 -13.363 23.909 1.00 58.61  ? 905 HOH   A O   1 
HETATM 3427 O  O   . HOH   G 7 .   ? -18.967 3.373   24.021 1.00 64.40  ? 906 HOH   A O   1 
HETATM 3428 O  O   . HOH   G 7 .   ? -35.137 -12.041 36.043 1.00 64.48  ? 907 HOH   A O   1 
HETATM 3429 O  O   . HOH   G 7 .   ? -24.831 -11.096 37.691 1.00 66.87  ? 908 HOH   A O   1 
HETATM 3430 O  O   . HOH   G 7 .   ? -19.703 -8.640  34.692 1.00 67.17  ? 909 HOH   A O   1 
HETATM 3431 O  O   . HOH   G 7 .   ? -27.160 -2.916  29.721 1.00 55.62  ? 910 HOH   A O   1 
HETATM 3432 O  O   . HOH   G 7 .   ? -21.901 1.168   30.170 1.00 67.65  ? 911 HOH   A O   1 
HETATM 3433 O  O   . HOH   G 7 .   ? -26.893 -12.254 1.132  1.00 59.24  ? 912 HOH   A O   1 
HETATM 3434 O  O   . HOH   G 7 .   ? -40.774 -7.899  40.272 1.00 90.25  ? 913 HOH   A O   1 
HETATM 3435 O  O   . HOH   G 7 .   ? -24.383 -2.073  38.199 1.00 56.29  ? 914 HOH   A O   1 
HETATM 3436 O  O   . HOH   G 7 .   ? -28.796 -10.877 38.008 1.00 66.99  ? 915 HOH   A O   1 
HETATM 3437 O  O   . HOH   G 7 .   ? -23.433 -0.860  34.627 1.00 65.09  ? 916 HOH   A O   1 
HETATM 3438 O  O   . HOH   G 7 .   ? -21.772 -10.212 35.508 1.00 65.69  ? 917 HOH   A O   1 
HETATM 3439 O  O   . HOH   G 7 .   ? -24.154 -18.577 6.574  1.00 57.15  ? 918 HOH   A O   1 
HETATM 3440 O  O   . HOH   G 7 .   ? -28.855 -15.071 1.318  1.00 86.92  ? 919 HOH   A O   1 
HETATM 3441 O  O   . HOH   G 7 .   ? -17.674 -18.326 21.251 1.00 81.65  ? 920 HOH   A O   1 
HETATM 3442 O  O   . HOH   G 7 .   ? -15.575 1.279   29.820 1.00 68.38  ? 921 HOH   A O   1 
HETATM 3443 O  O   . HOH   G 7 .   ? -20.715 -8.524  17.031 1.00 52.97  ? 922 HOH   A O   1 
HETATM 3444 O  O   . HOH   G 7 .   ? -9.195  -17.662 11.184 1.00 72.84  ? 923 HOH   A O   1 
HETATM 3445 O  O   . HOH   G 7 .   ? -22.072 -13.640 28.046 1.00 85.35  ? 924 HOH   A O   1 
HETATM 3446 O  O   . HOH   G 7 .   ? -25.795 0.101   32.327 1.00 69.41  ? 925 HOH   A O   1 
HETATM 3447 O  O   . HOH   G 7 .   ? -25.124 -10.683 27.423 1.00 58.00  ? 926 HOH   A O   1 
HETATM 3448 O  O   . HOH   G 7 .   ? -44.649 -12.091 23.230 1.00 97.30  ? 927 HOH   A O   1 
HETATM 3449 O  O   . HOH   G 7 .   ? -19.156 1.501   26.666 1.00 71.88  ? 928 HOH   A O   1 
HETATM 3450 O  O   . HOH   G 7 .   ? -17.669 0.940   28.761 1.00 72.79  ? 929 HOH   A O   1 
HETATM 3451 O  O   . HOH   G 7 .   ? -27.338 -16.764 1.797  1.00 72.22  ? 930 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   . PHE A 4   ? 1.2714 1.4788 1.0788 -0.5492 0.0248  0.0280  300 PHE A N   
2    C CA  . PHE A 4   ? 1.2640 1.6156 1.1457 -0.5299 0.0309  0.0202  300 PHE A CA  
3    C C   . PHE A 4   ? 1.2568 1.6591 1.1875 -0.4711 0.0368  0.0179  300 PHE A C   
4    O O   . PHE A 4   ? 1.2630 1.7682 1.2156 -0.4764 0.0477  0.0174  300 PHE A O   
5    C CB  . PHE A 4   ? 1.2887 1.7410 1.1612 -0.5875 0.0388  0.0209  300 PHE A CB  
6    C CG  . PHE A 4   ? 1.4635 1.8231 1.2481 -0.6406 0.0327  0.0256  300 PHE A CG  
7    C CD1 . PHE A 4   ? 1.5696 1.8741 1.2924 -0.6721 0.0356  0.0334  300 PHE A CD1 
8    C CD2 . PHE A 4   ? 1.5543 1.8786 1.3121 -0.6581 0.0237  0.0219  300 PHE A CD2 
9    C CE1 . PHE A 4   ? 1.6769 1.8902 1.3095 -0.7192 0.0290  0.0370  300 PHE A CE1 
10   C CE2 . PHE A 4   ? 1.6787 1.9127 1.3463 -0.7059 0.0180  0.0258  300 PHE A CE2 
11   C CZ  . PHE A 4   ? 1.7349 1.9122 1.3381 -0.7361 0.0203  0.0332  300 PHE A CZ  
12   N N   . LEU A 5   ? 1.1970 1.5303 1.1421 -0.4157 0.0293  0.0159  301 LEU A N   
13   C CA  . LEU A 5   ? 1.0753 1.4099 1.0411 -0.3683 0.0320  0.0158  301 LEU A CA  
14   C C   . LEU A 5   ? 0.9759 1.4218 0.9980 -0.3285 0.0382  0.0079  301 LEU A C   
15   O O   . LEU A 5   ? 0.9039 1.4162 0.9573 -0.3223 0.0375  0.0019  301 LEU A O   
16   C CB  . LEU A 5   ? 1.0175 1.2521 0.9798 -0.3268 0.0209  0.0159  301 LEU A CB  
17   C CG  . LEU A 5   ? 1.0940 1.2163 1.0014 -0.3503 0.0121  0.0213  301 LEU A CG  
18   C CD1 . LEU A 5   ? 1.1160 1.1929 1.0419 -0.3112 0.0018  0.0170  301 LEU A CD1 
19   C CD2 . LEU A 5   ? 1.1215 1.1686 0.9808 -0.3555 0.0114  0.0296  301 LEU A CD2 
20   N N   . LYS A 6   ? 0.9422 1.4000 0.9710 -0.2970 0.0431  0.0078  302 LYS A N   
21   C CA  . LYS A 6   ? 0.8964 1.4449 0.9626 -0.2534 0.0492  0.0003  302 LYS A CA  
22   C C   . LYS A 6   ? 0.8395 1.3291 0.9147 -0.1968 0.0423  -0.0031 302 LYS A C   
23   O O   . LYS A 6   ? 0.7646 1.1692 0.8172 -0.1935 0.0373  0.0015  302 LYS A O   
24   C CB  . LYS A 6   ? 0.9545 1.5787 1.0131 -0.2663 0.0628  0.0019  302 LYS A CB  
25   C CG  . LYS A 6   ? 1.0895 1.7619 1.1274 -0.3351 0.0701  0.0076  302 LYS A CG  
26   C CD  . LYS A 6   ? 1.0989 1.9147 1.1706 -0.3422 0.0771  0.0018  302 LYS A CD  
27   C CE  . LYS A 6   ? 1.1584 2.0217 1.2052 -0.4219 0.0831  0.0080  302 LYS A CE  
28   N NZ  . LYS A 6   ? 1.2192 2.0595 1.2244 -0.4593 0.0918  0.0165  302 LYS A NZ  
29   N N   . VAL A 7   ? 0.7750 1.3096 0.8780 -0.1535 0.0411  -0.0109 303 VAL A N   
30   C CA  . VAL A 7   ? 0.7751 1.2601 0.8787 -0.1030 0.0351  -0.0147 303 VAL A CA  
31   C C   . VAL A 7   ? 0.7787 1.3360 0.8868 -0.0623 0.0428  -0.0218 303 VAL A C   
32   O O   . VAL A 7   ? 0.7646 1.4156 0.8912 -0.0550 0.0482  -0.0264 303 VAL A O   
33   C CB  . VAL A 7   ? 0.7503 1.1922 0.8678 -0.0857 0.0241  -0.0172 303 VAL A CB  
34   C CG1 . VAL A 7   ? 0.7421 1.1227 0.8518 -0.1222 0.0177  -0.0113 303 VAL A CG1 
35   C CG2 . VAL A 7   ? 0.7984 1.3171 0.9397 -0.0674 0.0252  -0.0237 303 VAL A CG2 
36   N N   . LYS A 8   ? 0.6505 1.1660 0.7376 -0.0349 0.0430  -0.0228 304 LYS A N   
37   C CA  . LYS A 8   ? 0.6325 1.1994 0.7101 0.0083  0.0503  -0.0299 304 LYS A CA  
38   C C   . LYS A 8   ? 0.6858 1.1921 0.7478 0.0586  0.0411  -0.0359 304 LYS A C   
39   O O   . LYS A 8   ? 0.7751 1.1924 0.8293 0.0540  0.0304  -0.0330 304 LYS A O   
40   C CB  . LYS A 8   ? 0.7131 1.2745 0.7668 0.0000  0.0581  -0.0271 304 LYS A CB  
41   C CG  . LYS A 8   ? 0.8004 1.4190 0.8385 0.0461  0.0674  -0.0351 304 LYS A CG  
42   C CD  . LYS A 8   ? 0.7602 1.3881 0.7770 0.0296  0.0773  -0.0316 304 LYS A CD  
43   C CE  . LYS A 8   ? 0.8540 1.5225 0.8467 0.0830  0.0858  -0.0406 304 LYS A CE  
44   N NZ  . LYS A 8   ? 0.8942 1.5699 0.8643 0.0664  0.0957  -0.0372 304 LYS A NZ  
45   N N   . ASN A 9   ? 0.6978 1.2538 0.7504 0.1065  0.0452  -0.0441 305 ASN A N   
46   C CA  . ASN A 9   ? 0.7980 1.2851 0.8147 0.1567  0.0377  -0.0502 305 ASN A CA  
47   C C   . ASN A 9   ? 0.8264 1.3033 0.8059 0.1810  0.0441  -0.0537 305 ASN A C   
48   O O   . ASN A 9   ? 0.8741 1.4410 0.8564 0.1945  0.0563  -0.0572 305 ASN A O   
49   C CB  . ASN A 9   ? 0.8272 1.3595 0.8441 0.2014  0.0362  -0.0573 305 ASN A CB  
50   C CG  . ASN A 9   ? 0.8823 1.3245 0.8473 0.2515  0.0271  -0.0630 305 ASN A CG  
51   O OD1 . ASN A 9   ? 0.9785 1.3827 0.8989 0.2806  0.0289  -0.0673 305 ASN A OD1 
52   N ND2 . ASN A 9   ? 0.8348 1.2365 0.7984 0.2598  0.0172  -0.0630 305 ASN A ND2 
53   N N   . TRP A 10  ? 0.8427 1.2158 0.7870 0.1836  0.0359  -0.0529 306 TRP A N   
54   C CA  . TRP A 10  ? 0.9660 1.3146 0.8692 0.2028  0.0404  -0.0562 306 TRP A CA  
55   C C   . TRP A 10  ? 1.0884 1.3992 0.9360 0.2652  0.0378  -0.0666 306 TRP A C   
56   O O   . TRP A 10  ? 1.2423 1.4923 1.0407 0.2820  0.0366  -0.0700 306 TRP A O   
57   C CB  . TRP A 10  ? 0.9959 1.2559 0.8863 0.1684  0.0322  -0.0496 306 TRP A CB  
58   C CG  . TRP A 10  ? 0.9236 1.2114 0.8513 0.1157  0.0354  -0.0399 306 TRP A CG  
59   C CD1 . TRP A 10  ? 0.8455 1.1146 0.8036 0.0806  0.0284  -0.0330 306 TRP A CD1 
60   C CD2 . TRP A 10  ? 0.9011 1.2331 0.8303 0.0934  0.0464  -0.0361 306 TRP A CD2 
61   N NE1 . TRP A 10  ? 0.7558 1.0459 0.7285 0.0397  0.0334  -0.0253 306 TRP A NE1 
62   C CE2 . TRP A 10  ? 0.8987 1.2266 0.8539 0.0439  0.0444  -0.0264 306 TRP A CE2 
63   C CE3 . TRP A 10  ? 0.8879 1.2601 0.7940 0.1111  0.0579  -0.0399 306 TRP A CE3 
64   C CZ2 . TRP A 10  ? 0.8457 1.1997 0.7994 0.0089  0.0527  -0.0196 306 TRP A CZ2 
65   C CZ3 . TRP A 10  ? 0.9175 1.3267 0.8295 0.0743  0.0672  -0.0331 306 TRP A CZ3 
66   C CH2 . TRP A 10  ? 0.9086 1.3049 0.8421 0.0222  0.0642  -0.0226 306 TRP A CH2 
67   N N   . GLU A 11  ? 1.1681 1.5049 1.0150 0.3007  0.0359  -0.0717 307 GLU A N   
68   C CA  . GLU A 11  ? 1.2138 1.5244 1.0003 0.3686  0.0348  -0.0821 307 GLU A CA  
69   C C   . GLU A 11  ? 1.2491 1.6881 1.0513 0.4112  0.0467  -0.0886 307 GLU A C   
70   O O   . GLU A 11  ? 1.2711 1.7193 1.0243 0.4687  0.0519  -0.0976 307 GLU A O   
71   C CB  . GLU A 11  ? 1.1553 1.3705 0.9092 0.3837  0.0200  -0.0829 307 GLU A CB  
72   C CG  . GLU A 11  ? 1.2173 1.3563 0.8832 0.4510  0.0146  -0.0928 307 GLU A CG  
73   C CD  . GLU A 11  ? 1.3104 1.4028 0.9557 0.4721  0.0036  -0.0934 307 GLU A CD  
74   O OE1 . GLU A 11  ? 1.3425 1.4314 0.9361 0.5377  0.0029  -0.1016 307 GLU A OE1 
75   O OE2 . GLU A 11  ? 1.2626 1.3228 0.9401 0.4258  -0.0042 -0.0857 307 GLU A OE2 
76   N N   . THR A 12  ? 1.1082 1.6505 0.9750 0.3838  0.0511  -0.0844 308 THR A N   
77   C CA  . THR A 12  ? 1.0855 1.7725 0.9775 0.4143  0.0619  -0.0895 308 THR A CA  
78   C C   . THR A 12  ? 1.0485 1.8556 0.9920 0.3655  0.0761  -0.0845 308 THR A C   
79   O O   . THR A 12  ? 1.0452 1.9907 1.0127 0.3830  0.0862  -0.0882 308 THR A O   
80   C CB  . THR A 12  ? 1.0111 1.7318 0.9310 0.4201  0.0546  -0.0893 308 THR A CB  
81   O OG1 . THR A 12  ? 0.8888 1.6161 0.8640 0.3471  0.0523  -0.0796 308 THR A OG1 
82   C CG2 . THR A 12  ? 1.1441 1.7376 1.0085 0.4600  0.0402  -0.0925 308 THR A CG2 
83   N N   . ASP A 13  ? 1.0586 1.8192 1.0171 0.3034  0.0764  -0.0757 309 ASP A N   
84   C CA  . ASP A 13  ? 1.1191 1.9693 1.1153 0.2472  0.0883  -0.0689 309 ASP A CA  
85   C C   . ASP A 13  ? 1.0229 1.9640 1.0711 0.2068  0.0892  -0.0647 309 ASP A C   
86   O O   . ASP A 13  ? 1.0650 2.1044 1.1390 0.1638  0.1001  -0.0606 309 ASP A O   
87   C CB  . ASP A 13  ? 1.2462 2.1939 1.2280 0.2757  0.1043  -0.0744 309 ASP A CB  
88   C CG  . ASP A 13  ? 1.3642 2.2203 1.2947 0.2960  0.1049  -0.0766 309 ASP A CG  
89   O OD1 . ASP A 13  ? 1.3949 2.1912 1.3257 0.2455  0.1038  -0.0683 309 ASP A OD1 
90   O OD2 . ASP A 13  ? 1.4165 2.2559 1.3008 0.3642  0.1055  -0.0868 309 ASP A OD2 
91   N N   . VAL A 14  ? 0.9722 1.8798 1.0317 0.2155  0.0777  -0.0655 310 VAL A N   
92   C CA  . VAL A 14  ? 0.8898 1.8766 0.9937 0.1782  0.0770  -0.0623 310 VAL A CA  
93   C C   . VAL A 14  ? 0.9017 1.8300 1.0216 0.1030  0.0736  -0.0519 310 VAL A C   
94   O O   . VAL A 14  ? 0.9819 1.7875 1.0852 0.0937  0.0647  -0.0481 310 VAL A O   
95   C CB  . VAL A 14  ? 0.7857 1.7540 0.8912 0.2175  0.0656  -0.0671 310 VAL A CB  
96   C CG1 . VAL A 14  ? 0.7020 1.7150 0.8490 0.1679  0.0619  -0.0625 310 VAL A CG1 
97   C CG2 . VAL A 14  ? 0.7704 1.8255 0.8612 0.2908  0.0696  -0.0771 310 VAL A CG2 
98   N N   . VAL A 15  ? 0.8663 1.8821 1.0131 0.0493  0.0800  -0.0475 311 VAL A N   
99   C CA  . VAL A 15  ? 0.8509 1.8081 1.0025 -0.0198 0.0759  -0.0381 311 VAL A CA  
100  C C   . VAL A 15  ? 0.7939 1.7953 0.9723 -0.0456 0.0705  -0.0381 311 VAL A C   
101  O O   . VAL A 15  ? 0.8293 1.9541 1.0290 -0.0363 0.0751  -0.0428 311 VAL A O   
102  C CB  . VAL A 15  ? 0.8337 1.8259 0.9754 -0.0735 0.0872  -0.0313 311 VAL A CB  
103  C CG1 . VAL A 15  ? 0.8404 1.7528 0.9725 -0.1395 0.0813  -0.0218 311 VAL A CG1 
104  C CG2 . VAL A 15  ? 0.8839 1.8326 0.9978 -0.0455 0.0923  -0.0318 311 VAL A CG2 
105  N N   . LEU A 16  ? 0.6971 1.6010 0.8727 -0.0753 0.0602  -0.0333 312 LEU A N   
106  C CA  . LEU A 16  ? 0.7721 1.6997 0.9653 -0.1091 0.0546  -0.0325 312 LEU A CA  
107  C C   . LEU A 16  ? 0.7396 1.5899 0.9133 -0.1737 0.0520  -0.0240 312 LEU A C   
108  O O   . LEU A 16  ? 0.6973 1.4511 0.8476 -0.1771 0.0502  -0.0192 312 LEU A O   
109  C CB  . LEU A 16  ? 0.7138 1.5928 0.9162 -0.0678 0.0430  -0.0370 312 LEU A CB  
110  C CG  . LEU A 16  ? 0.7961 1.7344 1.0038 0.0008  0.0440  -0.0453 312 LEU A CG  
111  C CD1 . LEU A 16  ? 0.8291 1.6603 1.0212 0.0443  0.0335  -0.0472 312 LEU A CD1 
112  C CD2 . LEU A 16  ? 0.9020 1.9652 1.1360 0.0031  0.0446  -0.0497 312 LEU A CD2 
113  N N   . THR A 17  ? 0.6599 1.5508 0.8373 -0.2239 0.0510  -0.0223 313 THR A N   
114  C CA  . THR A 17  ? 0.6710 1.4887 0.8161 -0.2882 0.0487  -0.0146 313 THR A CA  
115  C C   . THR A 17  ? 0.7707 1.5130 0.9129 -0.2947 0.0366  -0.0153 313 THR A C   
116  O O   . THR A 17  ? 0.8507 1.6525 1.0157 -0.2918 0.0331  -0.0202 313 THR A O   
117  C CB  . THR A 17  ? 0.7354 1.6464 0.8710 -0.3525 0.0571  -0.0115 313 THR A CB  
118  O OG1 . THR A 17  ? 0.7006 1.6907 0.8394 -0.3451 0.0698  -0.0109 313 THR A OG1 
119  C CG2 . THR A 17  ? 0.8186 1.6300 0.9030 -0.4197 0.0535  -0.0031 313 THR A CG2 
120  N N   . ASP A 18  ? 0.7051 1.3212 0.8173 -0.3020 0.0302  -0.0104 314 ASP A N   
121  C CA  . ASP A 18  ? 0.8234 1.3593 0.9301 -0.2982 0.0191  -0.0114 314 ASP A CA  
122  C C   . ASP A 18  ? 0.8494 1.3303 0.9106 -0.3598 0.0162  -0.0067 314 ASP A C   
123  O O   . ASP A 18  ? 0.8585 1.2653 0.8770 -0.3833 0.0169  -0.0001 314 ASP A O   
124  C CB  . ASP A 18  ? 0.7749 1.2137 0.8777 -0.2563 0.0131  -0.0101 314 ASP A CB  
125  C CG  . ASP A 18  ? 0.7619 1.1415 0.8690 -0.2401 0.0031  -0.0125 314 ASP A CG  
126  O OD1 . ASP A 18  ? 0.7695 1.0898 0.8463 -0.2712 -0.0016 -0.0102 314 ASP A OD1 
127  O OD2 . ASP A 18  ? 0.7550 1.1431 0.8896 -0.1964 -0.0001 -0.0167 314 ASP A OD2 
128  N N   . THR A 19  ? 0.8357 1.3467 0.8988 -0.3860 0.0123  -0.0101 315 THR A N   
129  C CA  . THR A 19  ? 0.8461 1.2758 0.8551 -0.4379 0.0066  -0.0070 315 THR A CA  
130  C C   . THR A 19  ? 0.9134 1.2741 0.9206 -0.4163 -0.0038 -0.0111 315 THR A C   
131  O O   . THR A 19  ? 0.9047 1.1716 0.8581 -0.4462 -0.0097 -0.0091 315 THR A O   
132  C CB  . THR A 19  ? 0.9369 1.4464 0.9308 -0.5043 0.0100  -0.0068 315 THR A CB  
133  O OG1 . THR A 19  ? 0.8659 1.4949 0.9118 -0.4821 0.0107  -0.0138 315 THR A OG1 
134  C CG2 . THR A 19  ? 0.9431 1.4864 0.9132 -0.5340 0.0200  -0.0006 315 THR A CG2 
135  N N   . LEU A 20  ? 0.7887 1.1867 0.8460 -0.3640 -0.0061 -0.0166 316 LEU A N   
136  C CA  . LEU A 20  ? 0.8882 1.2282 0.9460 -0.3423 -0.0148 -0.0203 316 LEU A CA  
137  C C   . LEU A 20  ? 0.9338 1.1499 0.9544 -0.3288 -0.0196 -0.0165 316 LEU A C   
138  O O   . LEU A 20  ? 0.8858 1.0361 0.8827 -0.3282 -0.0265 -0.0186 316 LEU A O   
139  C CB  . LEU A 20  ? 0.7462 1.1419 0.8580 -0.2877 -0.0157 -0.0252 316 LEU A CB  
140  C CG  . LEU A 20  ? 0.7353 1.0931 0.8531 -0.2672 -0.0236 -0.0293 316 LEU A CG  
141  C CD1 . LEU A 20  ? 0.7316 1.1196 0.8369 -0.3074 -0.0271 -0.0329 316 LEU A CD1 
142  C CD2 . LEU A 20  ? 0.6428 1.0408 0.8027 -0.2143 -0.0242 -0.0324 316 LEU A CD2 
143  N N   . HIS A 21  ? 0.8459 1.0330 0.8588 -0.3158 -0.0163 -0.0114 317 HIS A N   
144  C CA  . HIS A 21  ? 0.8239 0.9057 0.8022 -0.2987 -0.0213 -0.0075 317 HIS A CA  
145  C C   . HIS A 21  ? 0.8843 0.8765 0.7914 -0.3373 -0.0258 -0.0049 317 HIS A C   
146  O O   . HIS A 21  ? 0.9391 0.8410 0.8123 -0.3163 -0.0320 -0.0037 317 HIS A O   
147  C CB  . HIS A 21  ? 0.8348 0.9128 0.8149 -0.2840 -0.0171 -0.0022 317 HIS A CB  
148  C CG  . HIS A 21  ? 0.8667 0.9437 0.8080 -0.3292 -0.0114 0.0033  317 HIS A CG  
149  N ND1 . HIS A 21  ? 0.8823 1.0553 0.8467 -0.3496 -0.0023 0.0030  317 HIS A ND1 
150  C CD2 . HIS A 21  ? 0.9769 0.9678 0.8528 -0.3571 -0.0133 0.0097  317 HIS A CD2 
151  C CE1 . HIS A 21  ? 0.9637 1.1148 0.8818 -0.3936 0.0018  0.0093  317 HIS A CE1 
152  N NE2 . HIS A 21  ? 0.9898 1.0243 0.8504 -0.3998 -0.0052 0.0138  317 HIS A NE2 
153  N N   . LEU A 22  ? 0.9080 0.9231 0.7864 -0.3929 -0.0231 -0.0043 318 LEU A N   
154  C CA  . LEU A 22  ? 1.1142 1.0317 0.9107 -0.4358 -0.0283 -0.0021 318 LEU A CA  
155  C C   . LEU A 22  ? 1.1470 1.0173 0.9296 -0.4239 -0.0364 -0.0085 318 LEU A C   
156  O O   . LEU A 22  ? 1.1481 0.9047 0.8576 -0.4315 -0.0430 -0.0078 318 LEU A O   
157  C CB  . LEU A 22  ? 1.2077 1.1721 0.9766 -0.5066 -0.0235 0.0002  318 LEU A CB  
158  C CG  . LEU A 22  ? 1.1866 1.2004 0.9627 -0.5227 -0.0142 0.0067  318 LEU A CG  
159  C CD1 . LEU A 22  ? 1.2427 1.3348 1.0041 -0.5892 -0.0079 0.0084  318 LEU A CD1 
160  C CD2 . LEU A 22  ? 1.2065 1.1014 0.9193 -0.5174 -0.0165 0.0144  318 LEU A CD2 
161  N N   . LYS A 23  ? 1.1890 1.1396 1.0344 -0.4022 -0.0363 -0.0149 319 LYS A N   
162  C CA  . LYS A 23  ? 1.2501 1.1600 1.0863 -0.3862 -0.0433 -0.0210 319 LYS A CA  
163  C C   . LYS A 23  ? 1.2888 1.1463 1.1367 -0.3258 -0.0465 -0.0213 319 LYS A C   
164  O O   . LYS A 23  ? 1.3882 1.2081 1.2256 -0.3069 -0.0515 -0.0261 319 LYS A O   
165  C CB  . LYS A 23  ? 1.0977 1.1115 0.9916 -0.3863 -0.0428 -0.0273 319 LYS A CB  
166  C CG  . LYS A 23  ? 1.0927 1.1936 0.9901 -0.4417 -0.0396 -0.0276 319 LYS A CG  
167  C CD  . LYS A 23  ? 1.3138 1.3451 1.1288 -0.5073 -0.0437 -0.0267 319 LYS A CD  
168  C CE  . LYS A 23  ? 1.4216 1.4550 1.2230 -0.5279 -0.0508 -0.0339 319 LYS A CE  
169  N NZ  . LYS A 23  ? 1.4276 1.6049 1.2880 -0.5384 -0.0480 -0.0368 319 LYS A NZ  
170  N N   . SER A 24  ? 1.1080 0.9679 0.9762 -0.2970 -0.0436 -0.0164 320 SER A N   
171  C CA  . SER A 24  ? 1.1220 0.9463 1.0028 -0.2442 -0.0468 -0.0161 320 SER A CA  
172  C C   . SER A 24  ? 1.3100 1.0228 1.1182 -0.2366 -0.0534 -0.0160 320 SER A C   
173  O O   . SER A 24  ? 1.3132 0.9543 1.0505 -0.2690 -0.0553 -0.0131 320 SER A O   
174  C CB  . SER A 24  ? 1.1399 0.9849 1.0467 -0.2227 -0.0436 -0.0107 320 SER A CB  
175  O OG  . SER A 24  ? 1.2294 1.0297 1.1312 -0.1806 -0.0483 -0.0093 320 SER A OG  
176  N N   . THR A 25  ? 1.5232 1.2202 1.3439 -0.1920 -0.0570 -0.0189 321 THR A N   
177  C CA  . THR A 25  ? 1.7212 1.3217 1.4738 -0.1757 -0.0633 -0.0212 321 THR A CA  
178  C C   . THR A 25  ? 1.6547 1.2333 1.4088 -0.1223 -0.0663 -0.0187 321 THR A C   
179  O O   . THR A 25  ? 1.6677 1.1637 1.3557 -0.1103 -0.0708 -0.0156 321 THR A O   
180  C CB  . THR A 25  ? 1.8130 1.4204 1.5698 -0.1752 -0.0650 -0.0292 321 THR A CB  
181  O OG1 . THR A 25  ? 1.9271 1.4547 1.6304 -0.1406 -0.0704 -0.0325 321 THR A OG1 
182  C CG2 . THR A 25  ? 1.7156 1.4256 1.5610 -0.1561 -0.0612 -0.0315 321 THR A CG2 
183  N N   . LEU A 26  ? 1.5623 1.2154 1.3869 -0.0915 -0.0643 -0.0197 322 LEU A N   
184  C CA  . LEU A 26  ? 1.5661 1.2205 1.4005 -0.0440 -0.0672 -0.0178 322 LEU A CA  
185  C C   . LEU A 26  ? 1.5193 1.1772 1.3570 -0.0409 -0.0675 -0.0105 322 LEU A C   
186  O O   . LEU A 26  ? 1.5106 1.1803 1.3530 -0.0735 -0.0640 -0.0072 322 LEU A O   
187  C CB  . LEU A 26  ? 1.5174 1.2519 1.4214 -0.0230 -0.0649 -0.0204 322 LEU A CB  
188  C CG  . LEU A 26  ? 1.5385 1.2688 1.4374 -0.0059 -0.0657 -0.0270 322 LEU A CG  
189  C CD1 . LEU A 26  ? 1.4322 1.2408 1.3964 -0.0118 -0.0617 -0.0290 322 LEU A CD1 
190  C CD2 . LEU A 26  ? 1.5651 1.2787 1.4444 0.0418  -0.0694 -0.0274 322 LEU A CD2 
191  N N   . GLU A 27  ? 1.4577 1.1125 1.2933 -0.0001 -0.0719 -0.0083 323 GLU A N   
192  C CA  . GLU A 27  ? 1.4187 1.0755 1.2538 0.0088  -0.0740 -0.0016 323 GLU A CA  
193  C C   . GLU A 27  ? 1.2994 1.0453 1.2085 0.0172  -0.0721 -0.0004 323 GLU A C   
194  O O   . GLU A 27  ? 1.2736 1.0696 1.2234 0.0302  -0.0712 -0.0038 323 GLU A O   
195  C CB  . GLU A 27  ? 1.5147 1.1101 1.2911 0.0494  -0.0817 0.0003  323 GLU A CB  
196  C CG  . GLU A 27  ? 1.7197 1.2074 1.4062 0.0442  -0.0849 -0.0017 323 GLU A CG  
197  C CD  . GLU A 27  ? 1.9391 1.3440 1.5473 0.0797  -0.0931 0.0023  323 GLU A CD  
198  O OE1 . GLU A 27  ? 1.9638 1.3976 1.5893 0.1002  -0.0961 0.0078  323 GLU A OE1 
199  O OE2 . GLU A 27  ? 2.0843 1.3900 1.6071 0.0879  -0.0974 -0.0002 323 GLU A OE2 
200  N N   . THR A 28  ? 1.1433 0.9027 1.0625 0.0069  -0.0716 0.0048  324 THR A N   
201  C CA  . THR A 28  ? 1.0482 0.8774 1.0248 0.0053  -0.0698 0.0058  324 THR A CA  
202  C C   . THR A 28  ? 0.9579 0.8121 0.9452 0.0343  -0.0762 0.0091  324 THR A C   
203  O O   . THR A 28  ? 0.9741 0.8851 1.0048 0.0342  -0.0763 0.0089  324 THR A O   
204  C CB  . THR A 28  ? 0.9880 0.8219 0.9676 -0.0231 -0.0650 0.0086  324 THR A CB  
205  O OG1 . THR A 28  ? 0.9529 0.7376 0.8871 -0.0218 -0.0682 0.0141  324 THR A OG1 
206  C CG2 . THR A 28  ? 1.0580 0.8912 1.0350 -0.0543 -0.0584 0.0054  324 THR A CG2 
207  N N   . GLY A 29  ? 0.9604 0.7736 0.9047 0.0585  -0.0825 0.0121  325 GLY A N   
208  C CA  . GLY A 29  ? 1.0154 0.8585 0.9667 0.0843  -0.0896 0.0159  325 GLY A CA  
209  C C   . GLY A 29  ? 1.0820 0.8961 1.0076 0.0774  -0.0922 0.0218  325 GLY A C   
210  O O   . GLY A 29  ? 1.1480 0.9647 1.0573 0.1041  -0.1003 0.0256  325 GLY A O   
211  N N   . CYS A 30  ? 1.0399 0.8318 0.9602 0.0435  -0.0857 0.0227  326 CYS A N   
212  C CA  . CYS A 30  ? 1.0124 0.7779 0.9068 0.0340  -0.0868 0.0284  326 CYS A CA  
213  C C   . CYS A 30  ? 1.1388 0.8164 0.9588 0.0371  -0.0894 0.0321  326 CYS A C   
214  O O   . CYS A 30  ? 1.1854 0.8172 0.9731 0.0323  -0.0878 0.0294  326 CYS A O   
215  C CB  . CYS A 30  ? 0.8703 0.6590 0.7896 -0.0018 -0.0778 0.0276  326 CYS A CB  
216  S SG  . CYS A 30  ? 0.9179 0.7863 0.9050 -0.0057 -0.0752 0.0231  326 CYS A SG  
217  N N   . THR A 31  ? 1.1960 0.8434 0.9813 0.0446  -0.0943 0.0384  327 THR A N   
218  C CA  . THR A 31  ? 1.2700 0.8219 0.9732 0.0407  -0.0966 0.0435  327 THR A CA  
219  C C   . THR A 31  ? 1.2850 0.8285 0.9785 0.0037  -0.0906 0.0486  327 THR A C   
220  O O   . THR A 31  ? 1.3098 0.9195 1.0590 -0.0151 -0.0841 0.0468  327 THR A O   
221  C CB  . THR A 31  ? 1.2664 0.7796 0.9219 0.0899  -0.1091 0.0473  327 THR A CB  
222  O OG1 . THR A 31  ? 1.2431 0.7984 0.9202 0.1007  -0.1140 0.0517  327 THR A OG1 
223  C CG2 . THR A 31  ? 1.1647 0.7138 0.8428 0.1299  -0.1137 0.0415  327 THR A CG2 
224  N N   . GLU A 32  ? 1.4442 0.9021 1.0599 -0.0058 -0.0926 0.0551  328 GLU A N   
225  C CA  . GLU A 32  ? 1.5251 0.9789 1.1281 -0.0391 -0.0867 0.0607  328 GLU A CA  
226  C C   . GLU A 32  ? 1.4679 0.9636 1.0979 -0.0166 -0.0920 0.0638  328 GLU A C   
227  O O   . GLU A 32  ? 1.4858 1.0028 1.1255 -0.0412 -0.0858 0.0664  328 GLU A O   
228  C CB  . GLU A 32  ? 1.7474 1.0918 1.2508 -0.0596 -0.0880 0.0681  328 GLU A CB  
229  C CG  . GLU A 32  ? 1.9493 1.2598 1.4233 -0.1069 -0.0799 0.0662  328 GLU A CG  
230  C CD  . GLU A 32  ? 2.1425 1.3815 1.5664 -0.0880 -0.0869 0.0627  328 GLU A CD  
231  O OE1 . GLU A 32  ? 2.3039 1.4333 1.6301 -0.1061 -0.0899 0.0672  328 GLU A OE1 
232  O OE2 . GLU A 32  ? 2.1311 1.4188 1.6071 -0.0560 -0.0893 0.0555  328 GLU A OE2 
233  N N   . HIS A 33  ? 1.4035 0.9186 1.0462 0.0287  -0.1031 0.0630  329 HIS A N   
234  C CA  . HIS A 33  ? 1.3971 0.9441 1.0515 0.0505  -0.1111 0.0667  329 HIS A CA  
235  C C   . HIS A 33  ? 1.2072 0.8487 0.9364 0.0675  -0.1146 0.0612  329 HIS A C   
236  O O   . HIS A 33  ? 1.1845 0.8604 0.9247 0.0849  -0.1232 0.0636  329 HIS A O   
237  C CB  . HIS A 33  ? 1.6570 1.1368 1.2395 0.0898  -0.1240 0.0731  329 HIS A CB  
238  C CG  . HIS A 33  ? 1.9259 1.2926 1.4177 0.0750  -0.1223 0.0783  329 HIS A CG  
239  N ND1 . HIS A 33  ? 2.0202 1.3342 1.4623 0.0454  -0.1189 0.0859  329 HIS A ND1 
240  C CD2 . HIS A 33  ? 2.0471 1.3384 1.4822 0.0816  -0.1236 0.0771  329 HIS A CD2 
241  C CE1 . HIS A 33  ? 2.1289 1.3387 1.4855 0.0308  -0.1184 0.0898  329 HIS A CE1 
242  N NE2 . HIS A 33  ? 2.1291 1.3192 1.4776 0.0527  -0.1217 0.0843  329 HIS A NE2 
243  N N   . ILE A 34  ? 1.0659 0.7493 0.8426 0.0598  -0.1089 0.0543  330 ILE A N   
244  C CA  . ILE A 34  ? 1.0029 0.7696 0.8437 0.0668  -0.1113 0.0497  330 ILE A CA  
245  C C   . ILE A 34  ? 0.9355 0.7304 0.8183 0.0431  -0.1010 0.0431  330 ILE A C   
246  O O   . ILE A 34  ? 0.9770 0.7404 0.8455 0.0377  -0.0960 0.0409  330 ILE A O   
247  C CB  . ILE A 34  ? 1.0700 0.8659 0.9136 0.1083  -0.1227 0.0496  330 ILE A CB  
248  C CG1 . ILE A 34  ? 1.0080 0.8936 0.9134 0.1048  -0.1252 0.0461  330 ILE A CG1 
249  C CG2 . ILE A 34  ? 1.2075 0.9713 1.0316 0.1252  -0.1210 0.0463  330 ILE A CG2 
250  C CD1 . ILE A 34  ? 1.0092 0.9464 0.9189 0.1382  -0.1381 0.0482  330 ILE A CD1 
251  N N   . CYS A 35  ? 0.8480 0.6966 0.7759 0.0289  -0.0985 0.0400  331 CYS A N   
252  C CA  . CYS A 35  ? 0.8086 0.6846 0.7730 0.0108  -0.0899 0.0340  331 CYS A CA  
253  C C   . CYS A 35  ? 0.8086 0.7382 0.8106 0.0208  -0.0953 0.0311  331 CYS A C   
254  O O   . CYS A 35  ? 0.7299 0.6898 0.7405 0.0242  -0.1026 0.0327  331 CYS A O   
255  C CB  . CYS A 35  ? 0.8718 0.7552 0.8443 -0.0131 -0.0819 0.0325  331 CYS A CB  
256  S SG  . CYS A 35  ? 0.7897 0.7115 0.8028 -0.0251 -0.0744 0.0252  331 CYS A SG  
257  N N   . MET A 36  ? 0.7980 0.7398 0.8183 0.0229  -0.0920 0.0271  332 MET A N   
258  C CA  . MET A 36  ? 0.8652 0.8581 0.9175 0.0293  -0.0959 0.0249  332 MET A CA  
259  C C   . MET A 36  ? 0.8405 0.8508 0.9194 0.0092  -0.0894 0.0204  332 MET A C   
260  O O   . MET A 36  ? 0.7825 0.8247 0.8829 0.0102  -0.0901 0.0183  332 MET A O   
261  C CB  . MET A 36  ? 1.0334 1.0278 1.0794 0.0545  -0.0985 0.0242  332 MET A CB  
262  C CG  . MET A 36  ? 1.1885 1.1565 1.1971 0.0818  -0.1059 0.0285  332 MET A CG  
263  S SD  . MET A 36  ? 1.3143 1.3229 1.3246 0.1227  -0.1130 0.0275  332 MET A SD  
264  C CE  . MET A 36  ? 1.3466 1.3505 1.3220 0.1536  -0.1251 0.0337  332 MET A CE  
265  N N   . GLY A 37  ? 0.7765 0.7682 0.8510 -0.0069 -0.0830 0.0190  333 GLY A N   
266  C CA  . GLY A 37  ? 0.7359 0.7394 0.8276 -0.0187 -0.0775 0.0146  333 GLY A CA  
267  C C   . GLY A 37  ? 0.7519 0.7781 0.8535 -0.0253 -0.0824 0.0139  333 GLY A C   
268  O O   . GLY A 37  ? 0.7251 0.7508 0.8316 -0.0320 -0.0788 0.0104  333 GLY A O   
269  N N   . SER A 38  ? 0.5818 0.6262 0.6809 -0.0253 -0.0911 0.0171  334 SER A N   
270  C CA  . SER A 38  ? 0.6756 0.7426 0.7790 -0.0398 -0.0964 0.0169  334 SER A CA  
271  C C   . SER A 38  ? 0.6316 0.7455 0.7535 -0.0359 -0.1013 0.0188  334 SER A C   
272  O O   . SER A 38  ? 0.6135 0.7546 0.7371 -0.0537 -0.1064 0.0197  334 SER A O   
273  C CB  . SER A 38  ? 0.7151 0.7763 0.7988 -0.0522 -0.1032 0.0184  334 SER A CB  
274  O OG  . SER A 38  ? 0.6764 0.7623 0.7598 -0.0444 -0.1112 0.0227  334 SER A OG  
275  N N   . ILE A 39  ? 0.5869 0.7101 0.7168 -0.0137 -0.1000 0.0193  335 ILE A N   
276  C CA  . ILE A 39  ? 0.6487 0.8216 0.7953 -0.0034 -0.1030 0.0200  335 ILE A CA  
277  C C   . ILE A 39  ? 0.6961 0.8700 0.8554 -0.0118 -0.0965 0.0167  335 ILE A C   
278  O O   . ILE A 39  ? 0.7509 0.8870 0.9072 -0.0091 -0.0895 0.0136  335 ILE A O   
279  C CB  . ILE A 39  ? 0.5807 0.7507 0.7188 0.0301  -0.1045 0.0208  335 ILE A CB  
280  C CG1 . ILE A 39  ? 0.5844 0.7425 0.7021 0.0406  -0.1113 0.0247  335 ILE A CG1 
281  C CG2 . ILE A 39  ? 0.5285 0.7583 0.6815 0.0486  -0.1073 0.0208  335 ILE A CG2 
282  C CD1 . ILE A 39  ? 0.7163 0.9264 0.8417 0.0282  -0.1207 0.0278  335 ILE A CD1 
283  N N   . MET A 40  ? 0.7466 0.9686 0.9188 -0.0238 -0.0990 0.0178  336 MET A N   
284  C CA  . MET A 40  ? 0.8145 1.0345 0.9933 -0.0364 -0.0936 0.0156  336 MET A CA  
285  C C   . MET A 40  ? 0.7948 1.0180 0.9841 -0.0132 -0.0879 0.0127  336 MET A C   
286  O O   . MET A 40  ? 0.7145 0.9066 0.9030 -0.0155 -0.0820 0.0095  336 MET A O   
287  C CB  . MET A 40  ? 0.8856 1.1548 1.0679 -0.0622 -0.0979 0.0187  336 MET A CB  
288  C CG  . MET A 40  ? 1.0024 1.2604 1.1816 -0.0798 -0.0932 0.0177  336 MET A CG  
289  S SD  . MET A 40  ? 1.0977 1.2955 1.2394 -0.1135 -0.0956 0.0183  336 MET A SD  
290  C CE  . MET A 40  ? 1.0626 1.3108 1.1925 -0.1534 -0.1046 0.0238  336 MET A CE  
291  N N   . LEU A 41  ? 0.9105 1.1706 1.1054 0.0113  -0.0902 0.0132  337 LEU A N   
292  C CA  . LEU A 41  ? 1.0801 1.3349 1.2747 0.0369  -0.0857 0.0096  337 LEU A CA  
293  C C   . LEU A 41  ? 1.1910 1.4346 1.3674 0.0720  -0.0893 0.0096  337 LEU A C   
294  O O   . LEU A 41  ? 1.2890 1.5845 1.4683 0.0960  -0.0933 0.0106  337 LEU A O   
295  C CB  . LEU A 41  ? 1.1335 1.4487 1.3454 0.0359  -0.0837 0.0093  337 LEU A CB  
296  C CG  . LEU A 41  ? 1.1427 1.5430 1.3694 0.0291  -0.0889 0.0133  337 LEU A CG  
297  C CD1 . LEU A 41  ? 1.2061 1.6621 1.4366 0.0695  -0.0897 0.0119  337 LEU A CD1 
298  C CD2 . LEU A 41  ? 1.0820 1.5123 1.3182 -0.0079 -0.0864 0.0152  337 LEU A CD2 
299  N N   . PRO A 42  ? 1.2053 1.3819 1.3578 0.0766  -0.0882 0.0087  338 PRO A N   
300  C CA  . PRO A 42  ? 1.2479 1.3906 1.3674 0.1103  -0.0912 0.0085  338 PRO A CA  
301  C C   . PRO A 42  ? 1.2883 1.3973 1.3893 0.1269  -0.0868 0.0033  338 PRO A C   
302  O O   . PRO A 42  ? 1.2712 1.3714 1.3845 0.1078  -0.0808 0.0000  338 PRO A O   
303  C CB  . PRO A 42  ? 1.2472 1.3296 1.3439 0.0969  -0.0916 0.0107  338 PRO A CB  
304  C CG  . PRO A 42  ? 1.1944 1.2752 1.3134 0.0605  -0.0861 0.0099  338 PRO A CG  
305  C CD  . PRO A 42  ? 1.1419 1.2712 1.2909 0.0509  -0.0840 0.0081  338 PRO A CD  
306  N N   . SER A 43  ? 1.3627 1.4509 1.4286 0.1657  -0.0906 0.0023  339 SER A N   
307  C CA  . SER A 43  ? 1.3965 1.4446 1.4327 0.1862  -0.0876 -0.0034 339 SER A CA  
308  C C   . SER A 43  ? 1.4584 1.4197 1.4628 0.1623  -0.0842 -0.0054 339 SER A C   
309  O O   . SER A 43  ? 1.4211 1.3843 1.4471 0.1332  -0.0785 -0.0080 339 SER A O   
310  C CB  . SER A 43  ? 1.3943 1.4315 1.3878 0.2398  -0.0936 -0.0043 339 SER A CB  
311  O OG  . SER A 43  ? 1.3670 1.3645 1.3273 0.2508  -0.1003 0.0004  339 SER A OG  
312  N N   . VAL A 52  ? 1.9674 1.8331 1.6604 0.5064  -0.0543 -0.0906 348 VAL A N   
313  C CA  . VAL A 52  ? 1.9746 1.7658 1.6314 0.4834  -0.0525 -0.0984 348 VAL A CA  
314  C C   . VAL A 52  ? 2.1148 1.7600 1.6984 0.4550  -0.0609 -0.0997 348 VAL A C   
315  O O   . VAL A 52  ? 2.2438 1.8218 1.7727 0.4780  -0.0679 -0.0979 348 VAL A O   
316  C CB  . VAL A 52  ? 1.9053 1.6932 1.5106 0.5442  -0.0484 -0.1096 348 VAL A CB  
317  C CG1 . VAL A 52  ? 1.9984 1.6816 1.4957 0.6099  -0.0557 -0.1162 348 VAL A CG1 
318  C CG2 . VAL A 52  ? 1.8306 1.5745 1.4202 0.5131  -0.0451 -0.1167 348 VAL A CG2 
319  N N   . ALA A 53  ? 2.0518 1.6528 1.6336 0.4023  -0.0605 -0.1023 349 ALA A N   
320  C CA  . ALA A 53  ? 2.0557 1.5311 1.5706 0.3635  -0.0679 -0.1036 349 ALA A CA  
321  C C   . ALA A 53  ? 2.2143 1.5680 1.6176 0.3892  -0.0719 -0.1154 349 ALA A C   
322  O O   . ALA A 53  ? 2.3578 1.7331 1.7486 0.4292  -0.0675 -0.1234 349 ALA A O   
323  C CB  . ALA A 53  ? 1.9044 1.4098 1.4786 0.2905  -0.0663 -0.0998 349 ALA A CB  
324  N N   . THR A 54  ? 2.1597 1.3809 1.4753 0.3639  -0.0802 -0.1167 350 THR A N   
325  C CA  . THR A 54  ? 2.1307 1.2103 1.3212 0.3791  -0.0861 -0.1277 350 THR A CA  
326  C C   . THR A 54  ? 2.0635 1.0763 1.2271 0.3007  -0.0903 -0.1295 350 THR A C   
327  O O   . THR A 54  ? 1.9075 0.9743 1.1396 0.2400  -0.0894 -0.1216 350 THR A O   
328  C CB  . THR A 54  ? 2.2193 1.1837 1.3007 0.4223  -0.0942 -0.1267 350 THR A CB  
329  O OG1 . THR A 54  ? 2.2420 1.1209 1.2822 0.3641  -0.1011 -0.1199 350 THR A OG1 
330  C CG2 . THR A 54  ? 2.1756 1.2348 1.3064 0.4832  -0.0916 -0.1202 350 THR A CG2 
331  N N   . LYS A 55  ? 2.1991 1.0953 1.2572 0.3038  -0.0952 -0.1405 351 LYS A N   
332  C CA  . LYS A 55  ? 2.2320 1.0695 1.2570 0.2295  -0.1001 -0.1438 351 LYS A CA  
333  C C   . LYS A 55  ? 2.3332 1.0742 1.2922 0.1751  -0.1082 -0.1366 351 LYS A C   
334  O O   . LYS A 55  ? 2.2062 0.9374 1.1678 0.1004  -0.1113 -0.1366 351 LYS A O   
335  C CB  . LYS A 55  ? 2.3549 1.1190 1.2965 0.2462  -0.1025 -0.1533 351 LYS A CB  
336  C CG  . LYS A 55  ? 2.4044 1.1433 1.2890 0.3264  -0.1022 -0.1503 351 LYS A CG  
337  C CD  . LYS A 55  ? 2.5029 1.1667 1.3003 0.3352  -0.1058 -0.1543 351 LYS A CD  
338  C CE  . LYS A 55  ? 2.5374 1.1713 1.2670 0.4154  -0.1076 -0.1504 351 LYS A CE  
339  N NZ  . LYS A 55  ? 2.6084 1.1135 1.2091 0.4143  -0.1164 -0.1486 351 LYS A NZ  
340  N N   . ASP A 56  ? 2.5632 1.2567 1.4721 0.2080  -0.1111 -0.1266 352 ASP A N   
341  C CA  . ASP A 56  ? 2.7082 1.3309 1.5634 0.1567  -0.1170 -0.1152 352 ASP A CA  
342  C C   . ASP A 56  ? 2.5457 1.2394 1.4900 0.1094  -0.1141 -0.1123 352 ASP A C   
343  O O   . ASP A 56  ? 2.5819 1.2616 1.5199 0.0343  -0.1163 -0.1077 352 ASP A O   
344  C CB  . ASP A 56  ? 2.9148 1.4758 1.6954 0.2114  -0.1213 -0.1066 352 ASP A CB  
345  C CG  . ASP A 56  ? 3.0916 1.6285 1.8171 0.2858  -0.1224 -0.1111 352 ASP A CG  
346  O OD1 . ASP A 56  ? 3.2432 1.6774 1.8613 0.2797  -0.1287 -0.1098 352 ASP A OD1 
347  O OD2 . ASP A 56  ? 3.0564 1.6830 1.8460 0.3489  -0.1168 -0.1155 352 ASP A OD2 
348  N N   . GLN A 57  ? 2.3219 1.1190 1.3608 0.1508  -0.1082 -0.1104 353 GLN A N   
349  C CA  . GLN A 57  ? 2.1205 1.0322 1.2701 0.1096  -0.1032 -0.0997 353 GLN A CA  
350  C C   . GLN A 57  ? 1.9668 0.9728 1.1998 0.0534  -0.0990 -0.1006 353 GLN A C   
351  O O   . GLN A 57  ? 1.8386 0.9152 1.1394 0.0074  -0.0964 -0.0929 353 GLN A O   
352  C CB  . GLN A 57  ? 2.0942 1.1160 1.3321 0.1659  -0.0974 -0.0943 353 GLN A CB  
353  C CG  . GLN A 57  ? 2.2915 1.2530 1.4596 0.2445  -0.1008 -0.0969 353 GLN A CG  
354  C CD  . GLN A 57  ? 2.2904 1.3763 1.5405 0.3040  -0.0940 -0.0980 353 GLN A CD  
355  O OE1 . GLN A 57  ? 2.2119 1.3956 1.5427 0.2902  -0.0872 -0.0999 353 GLN A OE1 
356  N NE2 . GLN A 57  ? 2.3664 1.4515 1.5928 0.3695  -0.0961 -0.0964 353 GLN A NE2 
357  N N   . LEU A 58  ? 1.8798 0.8877 1.1051 0.0591  -0.0984 -0.1099 354 LEU A N   
358  C CA  . LEU A 58  ? 1.7243 0.8449 1.0442 0.0258  -0.0938 -0.1103 354 LEU A CA  
359  C C   . LEU A 58  ? 1.7421 0.8446 1.0434 -0.0523 -0.0984 -0.1110 354 LEU A C   
360  O O   . LEU A 58  ? 1.6511 0.8610 1.0419 -0.0861 -0.0950 -0.1069 354 LEU A O   
361  C CB  . LEU A 58  ? 1.7507 0.8899 1.0734 0.0659  -0.0909 -0.1195 354 LEU A CB  
362  C CG  . LEU A 58  ? 1.5933 0.8755 1.0346 0.0720  -0.0830 -0.1168 354 LEU A CG  
363  C CD1 . LEU A 58  ? 1.4740 0.8382 0.9875 0.1083  -0.0771 -0.1081 354 LEU A CD1 
364  C CD2 . LEU A 58  ? 1.6681 0.9529 1.0945 0.1031  -0.0806 -0.1265 354 LEU A CD2 
365  N N   . PHE A 59  ? 1.8350 0.8053 1.0175 -0.0823 -0.1066 -0.1162 355 PHE A N   
366  C CA  . PHE A 59  ? 1.9439 0.9140 1.1122 -0.1626 -0.1112 -0.1170 355 PHE A CA  
367  C C   . PHE A 59  ? 1.9764 1.0003 1.1882 -0.2134 -0.1097 -0.1065 355 PHE A C   
368  O O   . PHE A 59  ? 1.9680 1.0867 1.2438 -0.2618 -0.1086 -0.1048 355 PHE A O   
369  C CB  . PHE A 59  ? 2.2663 1.0879 1.2949 -0.1914 -0.1203 -0.1230 355 PHE A CB  
370  C CG  . PHE A 59  ? 2.4146 1.2729 1.4455 -0.2726 -0.1229 -0.1192 355 PHE A CG  
371  C CD1 . PHE A 59  ? 2.4242 1.3472 1.4975 -0.2928 -0.1247 -0.1285 355 PHE A CD1 
372  C CD2 . PHE A 59  ? 2.5168 1.3554 1.5095 -0.3274 -0.1232 -0.1060 355 PHE A CD2 
373  C CE1 . PHE A 59  ? 2.4538 1.4268 1.5351 -0.3629 -0.1269 -0.1241 355 PHE A CE1 
374  C CE2 . PHE A 59  ? 2.5449 1.4334 1.5433 -0.3989 -0.1243 -0.1018 355 PHE A CE2 
375  C CZ  . PHE A 59  ? 2.5092 1.4682 1.5543 -0.4151 -0.1262 -0.1106 355 PHE A CZ  
376  N N   . PRO A 60  ? 2.0071 0.9758 1.1830 -0.2037 -0.1099 -0.0994 356 PRO A N   
377  C CA  . PRO A 60  ? 1.8529 0.8879 1.0803 -0.2477 -0.1067 -0.0893 356 PRO A CA  
378  C C   . PRO A 60  ? 1.6134 0.8124 0.9819 -0.2378 -0.0985 -0.0849 356 PRO A C   
379  O O   . PRO A 60  ? 1.6143 0.8932 1.0312 -0.2878 -0.0968 -0.0815 356 PRO A O   
380  C CB  . PRO A 60  ? 2.0033 0.9553 1.1762 -0.2153 -0.1075 -0.0830 356 PRO A CB  
381  C CG  . PRO A 60  ? 2.0439 0.9196 1.1631 -0.1416 -0.1099 -0.0897 356 PRO A CG  
382  C CD  . PRO A 60  ? 2.0995 0.9339 1.1721 -0.1570 -0.1140 -0.1005 356 PRO A CD  
383  N N   . LEU A 61  ? 1.4630 0.7134 0.8927 -0.1742 -0.0937 -0.0849 357 LEU A N   
384  C CA  . LEU A 61  ? 1.2984 0.6880 0.8480 -0.1636 -0.0870 -0.0812 357 LEU A CA  
385  C C   . LEU A 61  ? 1.3963 0.8508 0.9823 -0.1946 -0.0877 -0.0863 357 LEU A C   
386  O O   . LEU A 61  ? 1.3653 0.9187 1.0230 -0.2181 -0.0849 -0.0826 357 LEU A O   
387  C CB  . LEU A 61  ? 1.2909 0.7103 0.8810 -0.0961 -0.0828 -0.0811 357 LEU A CB  
388  C CG  . LEU A 61  ? 1.4358 0.8237 1.0112 -0.0570 -0.0821 -0.0754 357 LEU A CG  
389  C CD1 . LEU A 61  ? 1.4772 0.8677 1.0544 0.0083  -0.0804 -0.0790 357 LEU A CD1 
390  C CD2 . LEU A 61  ? 1.3588 0.8361 1.0157 -0.0660 -0.0774 -0.0665 357 LEU A CD2 
391  N N   . ALA A 62  ? 1.3840 0.7846 0.9186 -0.1907 -0.0918 -0.0952 358 ALA A N   
392  C CA  . ALA A 62  ? 1.3588 0.8166 0.9208 -0.2198 -0.0939 -0.1004 358 ALA A CA  
393  C C   . ALA A 62  ? 1.3923 0.8674 0.9387 -0.2914 -0.0983 -0.0992 358 ALA A C   
394  O O   . ALA A 62  ? 1.2359 0.8174 0.8497 -0.3139 -0.0975 -0.0981 358 ALA A O   
395  C CB  . ALA A 62  ? 1.4064 0.7881 0.9017 -0.2035 -0.0981 -0.1107 358 ALA A CB  
396  N N   . LYS A 63  ? 1.5556 0.9268 1.0076 -0.3275 -0.1034 -0.0994 359 LYS A N   
397  C CA  . LYS A 63  ? 1.6483 1.0319 1.0736 -0.4039 -0.1074 -0.0977 359 LYS A CA  
398  C C   . LYS A 63  ? 1.6005 1.1017 1.1124 -0.4171 -0.1010 -0.0888 359 LYS A C   
399  O O   . LYS A 63  ? 1.6747 1.2777 1.2335 -0.4561 -0.1013 -0.0885 359 LYS A O   
400  C CB  . LYS A 63  ? 1.7826 1.0182 1.0817 -0.4352 -0.1130 -0.0973 359 LYS A CB  
401  C CG  . LYS A 63  ? 1.8148 1.0871 1.0946 -0.5008 -0.1107 -0.0864 359 LYS A CG  
402  C CD  . LYS A 63  ? 1.9284 1.0789 1.0992 -0.5135 -0.1106 -0.0767 359 LYS A CD  
403  C CE  . LYS A 63  ? 1.9627 1.1174 1.0798 -0.5793 -0.1109 -0.0694 359 LYS A CE  
404  N NZ  . LYS A 63  ? 1.9068 1.2165 1.1116 -0.6215 -0.1060 -0.0661 359 LYS A NZ  
405  N N   . GLU A 64  ? 1.4362 0.9268 0.9670 -0.3827 -0.0955 -0.0818 360 GLU A N   
406  C CA  . GLU A 64  ? 1.4952 1.0885 1.1026 -0.3890 -0.0889 -0.0739 360 GLU A CA  
407  C C   . GLU A 64  ? 1.3494 1.0756 1.0575 -0.3698 -0.0856 -0.0749 360 GLU A C   
408  O O   . GLU A 64  ? 1.3434 1.1661 1.0942 -0.4019 -0.0843 -0.0732 360 GLU A O   
409  C CB  . GLU A 64  ? 1.5642 1.1208 1.1766 -0.3448 -0.0844 -0.0674 360 GLU A CB  
410  C CG  . GLU A 64  ? 1.6312 1.2863 1.3226 -0.3395 -0.0774 -0.0599 360 GLU A CG  
411  C CD  . GLU A 64  ? 1.7657 1.3930 1.4704 -0.2880 -0.0740 -0.0546 360 GLU A CD  
412  O OE1 . GLU A 64  ? 1.8680 1.4036 1.5188 -0.2567 -0.0773 -0.0564 360 GLU A OE1 
413  O OE2 . GLU A 64  ? 1.7140 1.4130 1.4801 -0.2771 -0.0687 -0.0491 360 GLU A OE2 
414  N N   . PHE A 65  ? 1.1979 0.9313 0.9399 -0.3168 -0.0844 -0.0778 361 PHE A N   
415  C CA  . PHE A 65  ? 1.0503 0.8939 0.8755 -0.2970 -0.0821 -0.0782 361 PHE A CA  
416  C C   . PHE A 65  ? 1.0801 0.9764 0.9055 -0.3375 -0.0875 -0.0835 361 PHE A C   
417  O O   . PHE A 65  ? 1.0455 1.0482 0.9305 -0.3421 -0.0865 -0.0819 361 PHE A O   
418  C CB  . PHE A 65  ? 1.0287 0.8606 0.8764 -0.2412 -0.0802 -0.0801 361 PHE A CB  
419  C CG  . PHE A 65  ? 0.9652 0.8889 0.8792 -0.2243 -0.0793 -0.0807 361 PHE A CG  
420  C CD1 . PHE A 65  ? 0.9317 0.9307 0.9097 -0.2055 -0.0749 -0.0748 361 PHE A CD1 
421  C CD2 . PHE A 65  ? 0.9614 0.8887 0.8659 -0.2263 -0.0836 -0.0873 361 PHE A CD2 
422  C CE1 . PHE A 65  ? 0.8925 0.9620 0.9184 -0.1874 -0.0751 -0.0751 361 PHE A CE1 
423  C CE2 . PHE A 65  ? 0.8847 0.8901 0.8431 -0.2092 -0.0835 -0.0871 361 PHE A CE2 
424  C CZ  . PHE A 65  ? 0.7432 0.8164 0.7597 -0.1890 -0.0795 -0.0808 361 PHE A CZ  
425  N N   . LEU A 66  ? 1.0724 0.8953 0.8275 -0.3647 -0.0941 -0.0901 362 LEU A N   
426  C CA  . LEU A 66  ? 1.1335 1.0069 0.8847 -0.4066 -0.1008 -0.0956 362 LEU A CA  
427  C C   . LEU A 66  ? 1.1948 1.1312 0.9462 -0.4673 -0.1020 -0.0926 362 LEU A C   
428  O O   . LEU A 66  ? 1.1295 1.1734 0.9220 -0.4887 -0.1048 -0.0941 362 LEU A O   
429  C CB  . LEU A 66  ? 1.2973 1.0646 0.9621 -0.4236 -0.1081 -0.1040 362 LEU A CB  
430  C CG  . LEU A 66  ? 1.2421 0.9808 0.9139 -0.3691 -0.1075 -0.1092 362 LEU A CG  
431  C CD1 . LEU A 66  ? 1.3709 1.0121 0.9530 -0.3906 -0.1152 -0.1185 362 LEU A CD1 
432  C CD2 . LEU A 66  ? 1.1694 1.0257 0.9271 -0.3459 -0.1060 -0.1085 362 LEU A CD2 
433  N N   . ASP A 67  ? 1.2878 1.1627 0.9910 -0.4954 -0.1001 -0.0880 363 ASP A N   
434  C CA  . ASP A 67  ? 1.3252 1.2632 1.0270 -0.5478 -0.0974 -0.0818 363 ASP A CA  
435  C C   . ASP A 67  ? 1.1783 1.2583 0.9748 -0.5311 -0.0918 -0.0783 363 ASP A C   
436  O O   . ASP A 67  ? 1.1669 1.3465 0.9874 -0.5520 -0.0875 -0.0738 363 ASP A O   
437  C CB  . ASP A 67  ? 1.5028 1.3380 1.1317 -0.5669 -0.0936 -0.0744 363 ASP A CB  
438  C CG  . ASP A 67  ? 1.7620 1.4846 1.2857 -0.5982 -0.0971 -0.0733 363 ASP A CG  
439  O OD1 . ASP A 67  ? 1.8771 1.6394 1.3768 -0.6439 -0.0954 -0.0683 363 ASP A OD1 
440  O OD2 . ASP A 67  ? 1.8846 1.4783 1.3446 -0.5750 -0.1015 -0.0773 363 ASP A OD2 
441  N N   . GLN A 68  ? 1.0705 1.1571 0.9180 -0.4722 -0.0866 -0.0759 364 GLN A N   
442  C CA  . GLN A 68  ? 1.0245 1.2318 0.9516 -0.4473 -0.0807 -0.0720 364 GLN A CA  
443  C C   . GLN A 68  ? 0.9456 1.2399 0.9274 -0.4169 -0.0837 -0.0761 364 GLN A C   
444  O O   . GLN A 68  ? 0.9192 1.3288 0.9522 -0.4105 -0.0820 -0.0751 364 GLN A O   
445  C CB  . GLN A 68  ? 1.0168 1.1917 0.9682 -0.3986 -0.0734 -0.0661 364 GLN A CB  
446  C CG  . GLN A 68  ? 1.0975 1.1948 1.0462 -0.3466 -0.0738 -0.0672 364 GLN A CG  
447  C CD  . GLN A 68  ? 1.0997 1.1617 1.0615 -0.3097 -0.0679 -0.0612 364 GLN A CD  
448  O OE1 . GLN A 68  ? 1.0752 1.1785 1.0890 -0.2670 -0.0646 -0.0591 364 GLN A OE1 
449  N NE2 . GLN A 68  ? 1.1434 1.1233 1.0512 -0.3269 -0.0675 -0.0582 364 GLN A NE2 
450  N N   . TYR A 69  ? 1.0710 1.3135 1.0373 -0.3977 -0.0886 -0.0811 365 TYR A N   
451  C CA  . TYR A 69  ? 0.9697 1.2884 0.9791 -0.3726 -0.0924 -0.0846 365 TYR A CA  
452  C C   . TYR A 69  ? 1.0128 1.4183 1.0196 -0.4214 -0.0994 -0.0887 365 TYR A C   
453  O O   . TYR A 69  ? 0.9222 1.4440 0.9795 -0.4070 -0.1003 -0.0886 365 TYR A O   
454  C CB  . TYR A 69  ? 0.9442 1.1869 0.9340 -0.3433 -0.0952 -0.0887 365 TYR A CB  
455  C CG  . TYR A 69  ? 0.9496 1.2619 0.9691 -0.3288 -0.1007 -0.0926 365 TYR A CG  
456  C CD1 . TYR A 69  ? 0.9050 1.3054 0.9830 -0.2909 -0.0990 -0.0893 365 TYR A CD1 
457  C CD2 . TYR A 69  ? 0.9644 1.2497 0.9463 -0.3523 -0.1085 -0.0996 365 TYR A CD2 
458  C CE1 . TYR A 69  ? 0.8998 1.3596 0.9984 -0.2746 -0.1050 -0.0923 365 TYR A CE1 
459  C CE2 . TYR A 69  ? 0.9640 1.3152 0.9716 -0.3388 -0.1143 -0.1028 365 TYR A CE2 
460  C CZ  . TYR A 69  ? 0.9321 1.3708 0.9984 -0.2988 -0.1126 -0.0987 365 TYR A CZ  
461  O OH  . TYR A 69  ? 0.9842 1.4841 1.0705 -0.2807 -0.1191 -0.1012 365 TYR A OH  
462  N N   . TYR A 70  ? 1.1306 1.4794 1.0732 -0.4773 -0.1046 -0.0922 366 TYR A N   
463  C CA  . TYR A 70  ? 1.1131 1.5275 1.0441 -0.5091 -0.1039 -0.0896 366 TYR A CA  
464  C C   . TYR A 70  ? 1.1297 1.6285 1.0803 -0.5227 -0.0941 -0.0813 366 TYR A C   
465  O O   . TYR A 70  ? 1.1865 1.7900 1.1592 -0.5276 -0.0921 -0.0795 366 TYR A O   
466  C CB  . TYR A 70  ? 1.2379 1.5494 1.0837 -0.5548 -0.1076 -0.0914 366 TYR A CB  
467  C CG  . TYR A 70  ? 1.2218 1.4837 1.0510 -0.5411 -0.1173 -0.1009 366 TYR A CG  
468  C CD1 . TYR A 70  ? 1.2304 1.3705 1.0199 -0.5246 -0.1214 -0.1077 366 TYR A CD1 
469  C CD2 . TYR A 70  ? 1.2070 1.5468 1.0586 -0.5406 -0.1221 -0.1037 366 TYR A CD2 
470  C CE1 . TYR A 70  ? 1.2236 1.3200 0.9949 -0.5062 -0.1283 -0.1165 366 TYR A CE1 
471  C CE2 . TYR A 70  ? 1.2091 1.5061 1.0443 -0.5277 -0.1311 -0.1127 366 TYR A CE2 
472  C CZ  . TYR A 70  ? 1.2095 1.3861 1.0039 -0.5130 -0.1345 -0.1200 366 TYR A CZ  
473  O OH  . TYR A 70  ? 1.1236 1.2587 0.8993 -0.4926 -0.1403 -0.1277 366 TYR A OH  
474  N N   . SER A 71  ? 1.0958 1.5529 1.0360 -0.5275 -0.0880 -0.0766 367 SER A N   
475  C CA  . SER A 71  ? 1.0511 1.5957 1.0161 -0.5323 -0.0785 -0.0698 367 SER A CA  
476  C C   . SER A 71  ? 1.0203 1.6820 1.0616 -0.4797 -0.0768 -0.0709 367 SER A C   
477  O O   . SER A 71  ? 1.1274 1.8920 1.1885 -0.4792 -0.0708 -0.0680 367 SER A O   
478  C CB  . SER A 71  ? 1.0294 1.5026 0.9719 -0.5402 -0.0731 -0.0650 367 SER A CB  
479  O OG  . SER A 71  ? 0.9733 1.5187 0.9211 -0.5576 -0.0639 -0.0585 367 SER A OG  
480  N N   . SER A 72  ? 0.9161 1.5616 0.9932 -0.4339 -0.0822 -0.0753 368 SER A N   
481  C CA  . SER A 72  ? 0.8548 1.5914 0.9925 -0.3780 -0.0811 -0.0755 368 SER A CA  
482  C C   . SER A 72  ? 0.9267 1.7480 1.0792 -0.3642 -0.0849 -0.0779 368 SER A C   
483  O O   . SER A 72  ? 0.9315 1.8467 1.1147 -0.3313 -0.0810 -0.0764 368 SER A O   
484  C CB  . SER A 72  ? 0.8368 1.5194 0.9979 -0.3342 -0.0848 -0.0778 368 SER A CB  
485  O OG  . SER A 72  ? 0.8717 1.5708 1.0487 -0.2989 -0.0910 -0.0811 368 SER A OG  
486  N N   . ILE A 73  ? 0.9002 1.6880 1.0270 -0.3860 -0.0928 -0.0821 369 ILE A N   
487  C CA  . ILE A 73  ? 0.9115 1.7783 1.0510 -0.3731 -0.0971 -0.0843 369 ILE A CA  
488  C C   . ILE A 73  ? 1.0131 1.9423 1.1277 -0.4187 -0.0920 -0.0815 369 ILE A C   
489  O O   . ILE A 73  ? 1.0459 2.0341 1.1583 -0.4243 -0.0955 -0.0833 369 ILE A O   
490  C CB  . ILE A 73  ? 0.9587 1.7696 1.0825 -0.3739 -0.1082 -0.0905 369 ILE A CB  
491  C CG1 . ILE A 73  ? 1.0287 1.7400 1.0916 -0.4314 -0.1105 -0.0926 369 ILE A CG1 
492  C CG2 . ILE A 73  ? 0.9120 1.6835 1.0631 -0.3250 -0.1131 -0.0933 369 ILE A CG2 
493  C CD1 . ILE A 73  ? 1.0409 1.6865 1.0807 -0.4308 -0.1210 -0.1002 369 ILE A CD1 
494  N N   . LYS A 74  ? 1.0765 1.9949 1.1696 -0.4528 -0.0837 -0.0767 370 LYS A N   
495  C CA  . LYS A 74  ? 1.2099 2.1906 1.2749 -0.5002 -0.0774 -0.0728 370 LYS A CA  
496  C C   . LYS A 74  ? 1.2660 2.2028 1.2767 -0.5563 -0.0825 -0.0737 370 LYS A C   
497  O O   . LYS A 74  ? 1.3459 2.3583 1.3398 -0.5891 -0.0801 -0.0719 370 LYS A O   
498  C CB  . LYS A 74  ? 1.2205 2.3437 1.3227 -0.4681 -0.0732 -0.0728 370 LYS A CB  
499  C CG  . LYS A 74  ? 1.1606 2.3152 1.3113 -0.4000 -0.0705 -0.0733 370 LYS A CG  
500  C CD  . LYS A 74  ? 1.1578 2.4382 1.3270 -0.3758 -0.0629 -0.0723 370 LYS A CD  
501  C CE  . LYS A 74  ? 1.0909 2.3830 1.2974 -0.3036 -0.0616 -0.0733 370 LYS A CE  
502  N NZ  . LYS A 74  ? 1.0630 2.4630 1.2788 -0.2769 -0.0536 -0.0729 370 LYS A NZ  
503  N N   . ARG A 75  ? 1.2196 2.0336 1.1975 -0.5677 -0.0895 -0.0768 371 ARG A N   
504  C CA  . ARG A 75  ? 1.2796 2.0191 1.1897 -0.6218 -0.0941 -0.0775 371 ARG A CA  
505  C C   . ARG A 75  ? 1.3832 1.9767 1.2340 -0.6464 -0.0942 -0.0761 371 ARG A C   
506  O O   . ARG A 75  ? 1.4336 1.9198 1.2437 -0.6506 -0.1015 -0.0809 371 ARG A O   
507  C CB  . ARG A 75  ? 1.2150 1.9447 1.1310 -0.6053 -0.1045 -0.0846 371 ARG A CB  
508  C CG  . ARG A 75  ? 1.2311 2.0962 1.1954 -0.5801 -0.1054 -0.0857 371 ARG A CG  
509  C CD  . ARG A 75  ? 1.2382 2.1163 1.2558 -0.5138 -0.1117 -0.0908 371 ARG A CD  
510  N NE  . ARG A 75  ? 1.2933 2.2047 1.3147 -0.5053 -0.1204 -0.0954 371 ARG A NE  
511  C CZ  . ARG A 75  ? 1.4322 2.2586 1.4183 -0.5207 -0.1294 -0.1010 371 ARG A CZ  
512  N NH1 . ARG A 75  ? 1.4216 2.2859 1.4130 -0.5113 -0.1373 -0.1050 371 ARG A NH1 
513  N NH2 . ARG A 75  ? 1.5194 2.2202 1.4602 -0.5431 -0.1304 -0.1030 371 ARG A NH2 
514  N N   . PHE A 76  ? 1.3993 1.9863 1.2408 -0.6592 -0.0861 -0.0698 372 PHE A N   
515  C CA  . PHE A 76  ? 1.4936 1.9450 1.2677 -0.6858 -0.0853 -0.0667 372 PHE A CA  
516  C C   . PHE A 76  ? 1.6391 2.0252 1.3238 -0.7468 -0.0876 -0.0639 372 PHE A C   
517  O O   . PHE A 76  ? 1.7178 2.1764 1.3843 -0.7891 -0.0831 -0.0585 372 PHE A O   
518  C CB  . PHE A 76  ? 1.5159 1.9933 1.3007 -0.6882 -0.0760 -0.0599 372 PHE A CB  
519  C CG  . PHE A 76  ? 1.5864 1.9243 1.3059 -0.7053 -0.0751 -0.0561 372 PHE A CG  
520  C CD1 . PHE A 76  ? 1.6757 1.8838 1.3033 -0.7397 -0.0801 -0.0554 372 PHE A CD1 
521  C CD2 . PHE A 76  ? 1.6409 1.9770 1.3861 -0.6840 -0.0694 -0.0527 372 PHE A CD2 
522  C CE1 . PHE A 76  ? 1.7513 1.8294 1.3124 -0.7477 -0.0797 -0.0515 372 PHE A CE1 
523  C CE2 . PHE A 76  ? 1.7121 1.9220 1.3952 -0.6961 -0.0690 -0.0488 372 PHE A CE2 
524  C CZ  . PHE A 76  ? 1.7805 1.8608 1.3703 -0.7259 -0.0743 -0.0481 372 PHE A CZ  
525  N N   . GLY A 77  ? 1.7342 1.9817 1.3571 -0.7510 -0.0944 -0.0674 373 GLY A N   
526  C CA  . GLY A 77  ? 1.8697 2.0266 1.3919 -0.8059 -0.0967 -0.0637 373 GLY A CA  
527  C C   . GLY A 77  ? 1.8852 2.0913 1.3958 -0.8336 -0.1013 -0.0660 373 GLY A C   
528  O O   . GLY A 77  ? 1.9860 2.1210 1.4081 -0.8844 -0.1032 -0.0621 373 GLY A O   
529  N N   . SER A 78  ? 1.8024 2.1236 1.3938 -0.8016 -0.1035 -0.0717 374 SER A N   
530  C CA  . SER A 78  ? 1.7768 2.1451 1.3605 -0.8226 -0.1088 -0.0746 374 SER A CA  
531  C C   . SER A 78  ? 1.7860 2.0133 1.3004 -0.8278 -0.1177 -0.0804 374 SER A C   
532  O O   . SER A 78  ? 1.8105 1.9109 1.2869 -0.8086 -0.1194 -0.0827 374 SER A O   
533  C CB  . SER A 78  ? 1.6675 2.1710 1.3484 -0.7747 -0.1106 -0.0800 374 SER A CB  
534  O OG  . SER A 78  ? 1.5962 2.0611 1.3214 -0.7155 -0.1148 -0.0869 374 SER A OG  
535  N N   . LYS A 79  ? 1.7060 1.9534 1.1991 -0.8519 -0.1233 -0.0830 375 LYS A N   
536  C CA  . LYS A 79  ? 1.7309 1.8518 1.1630 -0.8487 -0.1322 -0.0902 375 LYS A CA  
537  C C   . LYS A 79  ? 1.6066 1.6938 1.0865 -0.7818 -0.1370 -0.1007 375 LYS A C   
538  O O   . LYS A 79  ? 1.6447 1.5948 1.0683 -0.7654 -0.1405 -0.1058 375 LYS A O   
539  C CB  . LYS A 79  ? 1.7652 1.9359 1.1836 -0.8791 -0.1379 -0.0922 375 LYS A CB  
540  C CG  . LYS A 79  ? 1.8608 1.8931 1.1983 -0.8854 -0.1466 -0.0988 375 LYS A CG  
541  C CD  . LYS A 79  ? 1.9824 1.9162 1.2032 -0.9518 -0.1457 -0.0903 375 LYS A CD  
542  C CE  . LYS A 79  ? 1.9951 1.7693 1.1243 -0.9491 -0.1537 -0.0964 375 LYS A CE  
543  N NZ  . LYS A 79  ? 1.9969 1.6340 1.0903 -0.9043 -0.1534 -0.1000 375 LYS A NZ  
544  N N   . ALA A 80  ? 1.5501 1.7602 1.1283 -0.7407 -0.1367 -0.1036 376 ALA A N   
545  C CA  . ALA A 80  ? 1.5120 1.7012 1.1345 -0.6811 -0.1415 -0.1127 376 ALA A CA  
546  C C   . ALA A 80  ? 1.4987 1.5873 1.1017 -0.6594 -0.1378 -0.1129 376 ALA A C   
547  O O   . ALA A 80  ? 1.5504 1.5421 1.1273 -0.6295 -0.1422 -0.1212 376 ALA A O   
548  C CB  . ALA A 80  ? 1.3631 1.7020 1.0862 -0.6425 -0.1411 -0.1128 376 ALA A CB  
549  N N   . HIS A 81  ? 1.4631 1.5734 1.0744 -0.6731 -0.1295 -0.1039 377 HIS A N   
550  C CA  . HIS A 81  ? 1.4618 1.4788 1.0523 -0.6541 -0.1260 -0.1029 377 HIS A CA  
551  C C   . HIS A 81  ? 1.5250 1.3764 1.0055 -0.6722 -0.1284 -0.1037 377 HIS A C   
552  O O   . HIS A 81  ? 1.5151 1.2638 0.9683 -0.6368 -0.1301 -0.1093 377 HIS A O   
553  C CB  . HIS A 81  ? 1.4580 1.5387 1.0762 -0.6687 -0.1167 -0.0926 377 HIS A CB  
554  C CG  . HIS A 81  ? 1.5893 1.5724 1.1772 -0.6565 -0.1130 -0.0898 377 HIS A CG  
555  N ND1 . HIS A 81  ? 1.6288 1.6282 1.2092 -0.6792 -0.1051 -0.0801 377 HIS A ND1 
556  C CD2 . HIS A 81  ? 1.6177 1.4896 1.1794 -0.6218 -0.1159 -0.0956 377 HIS A CD2 
557  C CE1 . HIS A 81  ? 1.6515 1.5513 1.2029 -0.6595 -0.1040 -0.0794 377 HIS A CE1 
558  N NE2 . HIS A 81  ? 1.6602 1.4824 1.1998 -0.6233 -0.1103 -0.0887 377 HIS A NE2 
559  N N   . MET A 82  ? 1.5897 1.4118 1.0004 -0.7250 -0.1281 -0.0975 378 MET A N   
560  C CA  . MET A 82  ? 1.8212 1.4794 1.1160 -0.7404 -0.1306 -0.0965 378 MET A CA  
561  C C   . MET A 82  ? 1.8704 1.4457 1.1344 -0.7067 -0.1382 -0.1086 378 MET A C   
562  O O   . MET A 82  ? 1.9486 1.3871 1.1428 -0.6803 -0.1395 -0.1116 378 MET A O   
563  C CB  . MET A 82  ? 1.9858 1.6361 1.2084 -0.8088 -0.1295 -0.0867 378 MET A CB  
564  C CG  . MET A 82  ? 2.1106 1.8071 1.3332 -0.8435 -0.1213 -0.0747 378 MET A CG  
565  S SD  . MET A 82  ? 2.2099 1.7771 1.3838 -0.8168 -0.1181 -0.0705 378 MET A SD  
566  C CE  . MET A 82  ? 2.1022 1.8042 1.4086 -0.7754 -0.1117 -0.0720 378 MET A CE  
567  N N   . ASP A 83  ? 1.7704 1.4282 1.0829 -0.7027 -0.1431 -0.1156 379 ASP A N   
568  C CA  . ASP A 83  ? 1.7736 1.3590 1.0563 -0.6709 -0.1500 -0.1278 379 ASP A CA  
569  C C   . ASP A 83  ? 1.7175 1.2797 1.0393 -0.6072 -0.1497 -0.1369 379 ASP A C   
570  O O   . ASP A 83  ? 1.7484 1.1977 1.0125 -0.5733 -0.1517 -0.1452 379 ASP A O   
571  C CB  . ASP A 83  ? 1.8052 1.4892 1.1293 -0.6832 -0.1558 -0.1325 379 ASP A CB  
572  C CG  . ASP A 83  ? 1.9829 1.6409 1.2349 -0.7411 -0.1582 -0.1273 379 ASP A CG  
573  O OD1 . ASP A 83  ? 1.9769 1.7564 1.2720 -0.7737 -0.1584 -0.1229 379 ASP A OD1 
574  O OD2 . ASP A 83  ? 2.1399 1.6562 1.2883 -0.7525 -0.1598 -0.1269 379 ASP A OD2 
575  N N   . ARG A 84  ? 1.5206 1.1910 0.9370 -0.5885 -0.1467 -0.1354 380 ARG A N   
576  C CA  . ARG A 84  ? 1.5365 1.1918 0.9898 -0.5338 -0.1461 -0.1429 380 ARG A CA  
577  C C   . ARG A 84  ? 1.6279 1.1627 1.0241 -0.5144 -0.1415 -0.1409 380 ARG A C   
578  O O   . ARG A 84  ? 1.6592 1.1354 1.0493 -0.4588 -0.1387 -0.1458 380 ARG A O   
579  C CB  . ARG A 84  ? 1.3948 1.1947 0.9573 -0.5221 -0.1442 -0.1394 380 ARG A CB  
580  C CG  . ARG A 84  ? 1.3491 1.1526 0.9700 -0.4455 -0.1330 -0.1340 380 ARG A CG  
581  C CD  . ARG A 84  ? 1.3465 1.2173 1.0259 -0.4026 -0.1322 -0.1357 380 ARG A CD  
582  N NE  . ARG A 84  ? 1.3090 1.1655 1.0259 -0.3361 -0.1223 -0.1315 380 ARG A NE  
583  C CZ  . ARG A 84  ? 1.2619 1.0417 0.9429 -0.2996 -0.1196 -0.1363 380 ARG A CZ  
584  N NH1 . ARG A 84  ? 1.2698 0.9706 0.8728 -0.3194 -0.1263 -0.1459 380 ARG A NH1 
585  N NH2 . ARG A 84  ? 1.1672 0.9513 0.8865 -0.2445 -0.1104 -0.1317 380 ARG A NH2 
586  N N   . LEU A 85  ? 1.6243 1.1342 0.9863 -0.5485 -0.1372 -0.1293 381 LEU A N   
587  C CA  . LEU A 85  ? 1.6799 1.0640 0.9719 -0.5304 -0.1340 -0.1259 381 LEU A CA  
588  C C   . LEU A 85  ? 1.8566 1.1000 1.0471 -0.5089 -0.1376 -0.1320 381 LEU A C   
589  O O   . LEU A 85  ? 1.8991 1.0620 1.0619 -0.4539 -0.1367 -0.1384 381 LEU A O   
590  C CB  . LEU A 85  ? 1.8227 1.2058 1.0846 -0.5782 -0.1296 -0.1116 381 LEU A CB  
591  C CG  . LEU A 85  ? 1.8142 1.1465 1.0649 -0.5580 -0.1247 -0.1054 381 LEU A CG  
592  C CD1 . LEU A 85  ? 1.6851 1.1302 1.0458 -0.5357 -0.1213 -0.1068 381 LEU A CD1 
593  C CD2 . LEU A 85  ? 1.9503 1.2538 1.1413 -0.6087 -0.1214 -0.0917 381 LEU A CD2 
594  N N   . GLU A 86  ? 1.9954 1.2117 1.1279 -0.5492 -0.1411 -0.1297 382 GLU A N   
595  C CA  . GLU A 86  ? 2.1094 1.1924 1.1394 -0.5309 -0.1448 -0.1344 382 GLU A CA  
596  C C   . GLU A 86  ? 1.9429 1.0214 0.9964 -0.4729 -0.1465 -0.1497 382 GLU A C   
597  O O   . GLU A 86  ? 2.0207 0.9909 1.0087 -0.4232 -0.1458 -0.1548 382 GLU A O   
598  C CB  . GLU A 86  ? 2.3365 1.4114 1.3116 -0.5911 -0.1489 -0.1293 382 GLU A CB  
599  C CG  . GLU A 86  ? 2.6764 1.6024 1.5295 -0.5810 -0.1529 -0.1310 382 GLU A CG  
600  C CD  . GLU A 86  ? 2.9836 1.7765 1.7296 -0.5827 -0.1519 -0.1196 382 GLU A CD  
601  O OE1 . GLU A 86  ? 3.1729 1.8343 1.8120 -0.5639 -0.1555 -0.1199 382 GLU A OE1 
602  O OE2 . GLU A 86  ? 3.0364 1.8548 1.8004 -0.6012 -0.1478 -0.1100 382 GLU A OE2 
603  N N   . GLU A 87  ? 1.8123 1.0120 0.9566 -0.4751 -0.1484 -0.1565 383 GLU A N   
604  C CA  . GLU A 87  ? 1.7312 0.9370 0.8981 -0.4247 -0.1498 -0.1708 383 GLU A CA  
605  C C   . GLU A 87  ? 1.7339 0.9172 0.9248 -0.3556 -0.1417 -0.1714 383 GLU A C   
606  O O   . GLU A 87  ? 1.6314 0.7540 0.7886 -0.2986 -0.1380 -0.1775 383 GLU A O   
607  C CB  . GLU A 87  ? 1.6891 1.0396 0.9502 -0.4437 -0.1538 -0.1738 383 GLU A CB  
608  C CG  . GLU A 87  ? 1.7510 1.1525 1.0743 -0.3770 -0.1466 -0.1752 383 GLU A CG  
609  C CD  . GLU A 87  ? 1.6760 1.2213 1.0921 -0.3871 -0.1485 -0.1722 383 GLU A CD  
610  O OE1 . GLU A 87  ? 1.5780 1.2245 1.0673 -0.4030 -0.1469 -0.1634 383 GLU A OE1 
611  O OE2 . GLU A 87  ? 1.5507 1.1051 0.9613 -0.3761 -0.1517 -0.1789 383 GLU A OE2 
612  N N   . VAL A 88  ? 1.5753 0.8292 0.8391 -0.3516 -0.1353 -0.1602 384 VAL A N   
613  C CA  . VAL A 88  ? 1.5741 0.8328 0.8788 -0.2837 -0.1248 -0.1544 384 VAL A CA  
614  C C   . VAL A 88  ? 1.7485 0.8584 0.9449 -0.2613 -0.1262 -0.1575 384 VAL A C   
615  O O   . VAL A 88  ? 1.7076 0.7884 0.8990 -0.1939 -0.1201 -0.1588 384 VAL A O   
616  C CB  . VAL A 88  ? 1.5118 0.8792 0.9146 -0.2896 -0.1189 -0.1421 384 VAL A CB  
617  C CG1 . VAL A 88  ? 1.3873 0.7481 0.8189 -0.2287 -0.1099 -0.1360 384 VAL A CG1 
618  C CG2 . VAL A 88  ? 1.4946 1.0026 0.9997 -0.2934 -0.1172 -0.1393 384 VAL A CG2 
619  N N   . ASN A 89  ? 1.9819 0.9995 1.0880 -0.3166 -0.1341 -0.1578 385 ASN A N   
620  C CA  . ASN A 89  ? 2.2384 1.1250 1.2430 -0.2889 -0.1331 -0.1523 385 ASN A CA  
621  C C   . ASN A 89  ? 2.3353 1.1465 1.2764 -0.2384 -0.1337 -0.1617 385 ASN A C   
622  O O   . ASN A 89  ? 2.4802 1.2340 1.3884 -0.1705 -0.1302 -0.1641 385 ASN A O   
623  C CB  . ASN A 89  ? 2.4132 1.2563 1.3536 -0.3540 -0.1361 -0.1388 385 ASN A CB  
624  C CG  . ASN A 89  ? 2.6116 1.3215 1.4447 -0.3308 -0.1364 -0.1299 385 ASN A CG  
625  O OD1 . ASN A 89  ? 2.6327 1.3213 1.4711 -0.2861 -0.1333 -0.1277 385 ASN A OD1 
626  N ND2 . ASN A 89  ? 2.7044 1.3232 1.4345 -0.3611 -0.1410 -0.1239 385 ASN A ND2 
627  N N   . LYS A 90  ? 2.1696 0.9901 1.0962 -0.2682 -0.1379 -0.1667 386 LYS A N   
628  C CA  . LYS A 90  ? 2.2874 1.0370 1.1500 -0.2243 -0.1383 -0.1751 386 LYS A CA  
629  C C   . LYS A 90  ? 2.2492 1.0467 1.1659 -0.1546 -0.1324 -0.1882 386 LYS A C   
630  O O   . LYS A 90  ? 2.2429 0.9813 1.1088 -0.0932 -0.1290 -0.1931 386 LYS A O   
631  C CB  . LYS A 90  ? 2.3386 1.0957 1.1789 -0.2772 -0.1445 -0.1773 386 LYS A CB  
632  C CG  . LYS A 90  ? 2.4595 1.1575 1.2263 -0.3435 -0.1495 -0.1639 386 LYS A CG  
633  C CD  . LYS A 90  ? 2.4644 1.2259 1.2509 -0.4077 -0.1548 -0.1650 386 LYS A CD  
634  C CE  . LYS A 90  ? 2.5725 1.2493 1.2570 -0.4648 -0.1594 -0.1533 386 LYS A CE  
635  N NZ  . LYS A 90  ? 2.5128 1.2775 1.2309 -0.5340 -0.1636 -0.1519 386 LYS A NZ  
636  N N   . GLU A 91  ? 2.0884 1.0179 1.1225 -0.1584 -0.1281 -0.1867 387 GLU A N   
637  C CA  . GLU A 91  ? 1.9603 0.9784 1.0768 -0.0901 -0.1166 -0.1850 387 GLU A CA  
638  C C   . GLU A 91  ? 1.9330 0.9313 1.0498 -0.0290 -0.1093 -0.1802 387 GLU A C   
639  O O   . GLU A 91  ? 1.8734 0.8931 1.0038 0.0363  -0.1015 -0.1830 387 GLU A O   
640  C CB  . GLU A 91  ? 1.8110 0.9886 1.0619 -0.1089 -0.1119 -0.1760 387 GLU A CB  
641  C CG  . GLU A 91  ? 1.6990 0.9662 1.0297 -0.0486 -0.1004 -0.1731 387 GLU A CG  
642  C CD  . GLU A 91  ? 1.6419 1.0450 1.0851 -0.0671 -0.0974 -0.1649 387 GLU A CD  
643  O OE1 . GLU A 91  ? 1.6093 1.0808 1.1088 -0.0285 -0.0891 -0.1625 387 GLU A OE1 
644  O OE2 . GLU A 91  ? 1.6830 1.1246 1.1537 -0.1190 -0.1034 -0.1608 387 GLU A OE2 
645  N N   . ILE A 92  ? 1.9957 0.9609 1.0981 -0.0499 -0.1119 -0.1728 388 ILE A N   
646  C CA  . ILE A 92  ? 1.9402 0.8676 1.0223 0.0068  -0.1077 -0.1691 388 ILE A CA  
647  C C   . ILE A 92  ? 2.1094 0.8754 1.0463 0.0445  -0.1132 -0.1798 388 ILE A C   
648  O O   . ILE A 92  ? 2.1166 0.8658 1.0364 0.1143  -0.1086 -0.1786 388 ILE A O   
649  C CB  . ILE A 92  ? 1.8670 0.8071 0.9757 -0.0278 -0.1090 -0.1575 388 ILE A CB  
650  C CG1 . ILE A 92  ? 1.7089 0.8041 0.9537 -0.0591 -0.1037 -0.1479 388 ILE A CG1 
651  C CG2 . ILE A 92  ? 1.8947 0.8080 0.9900 0.0332  -0.1052 -0.1531 388 ILE A CG2 
652  C CD1 . ILE A 92  ? 1.5961 0.7113 0.8676 -0.0995 -0.1047 -0.1374 388 ILE A CD1 
653  N N   . GLU A 93  ? 2.2647 0.9565 1.1252 0.0024  -0.1201 -0.1780 389 GLU A N   
654  C CA  . GLU A 93  ? 2.4286 1.0189 1.1859 0.0454  -0.1218 -0.1759 389 GLU A CA  
655  C C   . GLU A 93  ? 2.3690 0.9949 1.1426 0.1084  -0.1155 -0.1878 389 GLU A C   
656  O O   . GLU A 93  ? 2.2724 0.8855 1.0224 0.1832  -0.1111 -0.1871 389 GLU A O   
657  C CB  . GLU A 93  ? 2.6005 1.1041 1.2703 -0.0179 -0.1306 -0.1701 389 GLU A CB  
658  C CG  . GLU A 93  ? 2.7393 1.2090 1.3823 -0.0825 -0.1354 -0.1564 389 GLU A CG  
659  C CD  . GLU A 93  ? 2.9053 1.2770 1.4622 -0.0464 -0.1375 -0.1451 389 GLU A CD  
660  O OE1 . GLU A 93  ? 2.9705 1.2897 1.4736 0.0261  -0.1371 -0.1471 389 GLU A OE1 
661  O OE2 . GLU A 93  ? 2.9449 1.2973 1.4865 -0.0894 -0.1397 -0.1339 389 GLU A OE2 
662  N N   . SER A 94  ? 2.4685 1.1528 1.2874 0.0794  -0.1150 -0.1981 390 SER A N   
663  C CA  . SER A 94  ? 2.5598 1.2709 1.3819 0.1284  -0.1093 -0.2089 390 SER A CA  
664  C C   . SER A 94  ? 2.5109 1.3117 1.4036 0.2009  -0.0973 -0.2130 390 SER A C   
665  O O   . SER A 94  ? 2.4954 1.2921 1.3615 0.2697  -0.0913 -0.2135 390 SER A O   
666  C CB  . SER A 94  ? 2.5368 1.2966 1.3941 0.0745  -0.1126 -0.2178 390 SER A CB  
667  O OG  . SER A 94  ? 2.4620 1.3559 1.4274 0.1038  -0.1022 -0.2180 390 SER A OG  
668  N N   . THR A 95  ? 2.4304 1.3592 1.4466 0.1800  -0.0920 -0.2019 391 THR A N   
669  C CA  . THR A 95  ? 2.3504 1.4087 1.4672 0.2311  -0.0793 -0.1949 391 THR A CA  
670  C C   . THR A 95  ? 2.2386 1.3112 1.3771 0.2589  -0.0772 -0.1858 391 THR A C   
671  O O   . THR A 95  ? 2.0799 1.2496 1.2850 0.3059  -0.0676 -0.1810 391 THR A O   
672  C CB  . THR A 95  ? 2.2999 1.4994 1.5429 0.1917  -0.0744 -0.1861 391 THR A CB  
673  O OG1 . THR A 95  ? 2.3937 1.5678 1.6187 0.1313  -0.0826 -0.1902 391 THR A OG1 
674  C CG2 . THR A 95  ? 2.2182 1.5168 1.5186 0.2386  -0.0625 -0.1865 391 THR A CG2 
675  N N   . SER A 96  ? 2.3569 1.3394 1.4401 0.2278  -0.0860 -0.1829 392 SER A N   
676  C CA  . SER A 96  ? 2.3569 1.3553 1.4665 0.2409  -0.0853 -0.1726 392 SER A CA  
677  C C   . SER A 96  ? 2.0994 1.2493 1.3502 0.2156  -0.0786 -0.1597 392 SER A C   
678  O O   . SER A 96  ? 2.1191 1.3212 1.4159 0.2419  -0.0748 -0.1515 392 SER A O   
679  C CB  . SER A 96  ? 2.5226 1.4943 1.5853 0.3273  -0.0819 -0.1760 392 SER A CB  
680  O OG  . SER A 96  ? 2.4987 1.5988 1.6427 0.3730  -0.0707 -0.1755 392 SER A OG  
681  N N   . THR A 97  ? 1.8518 1.0684 1.1648 0.1667  -0.0779 -0.1583 393 THR A N   
682  C CA  . THR A 97  ? 1.5285 0.8673 0.9582 0.1341  -0.0739 -0.1469 393 THR A CA  
683  C C   . THR A 97  ? 1.5163 0.8642 0.9579 0.0704  -0.0794 -0.1483 393 THR A C   
684  O O   . THR A 97  ? 1.6075 0.8668 0.9675 0.0467  -0.0868 -0.1571 393 THR A O   
685  C CB  . THR A 97  ? 1.3827 0.8378 0.8954 0.1727  -0.0633 -0.1431 393 THR A CB  
686  O OG1 . THR A 97  ? 1.3811 0.9339 0.9908 0.1449  -0.0605 -0.1315 393 THR A OG1 
687  C CG2 . THR A 97  ? 1.3748 0.8505 0.8865 0.1742  -0.0608 -0.1505 393 THR A CG2 
688  N N   . TYR A 98  ? 1.3416 0.7953 0.8788 0.0432  -0.0767 -0.1399 394 TYR A N   
689  C CA  . TYR A 98  ? 1.3513 0.8320 0.9046 -0.0064 -0.0819 -0.1419 394 TYR A CA  
690  C C   . TYR A 98  ? 1.1850 0.7881 0.8417 -0.0082 -0.0766 -0.1338 394 TYR A C   
691  O O   . TYR A 98  ? 1.1976 0.8570 0.9082 0.0221  -0.0691 -0.1267 394 TYR A O   
692  C CB  . TYR A 98  ? 1.3032 0.7379 0.8200 -0.0637 -0.0906 -0.1412 394 TYR A CB  
693  C CG  . TYR A 98  ? 1.2638 0.7574 0.8428 -0.0816 -0.0887 -0.1301 394 TYR A CG  
694  C CD1 . TYR A 98  ? 1.1873 0.7751 0.8385 -0.1148 -0.0893 -0.1248 394 TYR A CD1 
695  C CD2 . TYR A 98  ? 1.3256 0.7804 0.8873 -0.0616 -0.0866 -0.1253 394 TYR A CD2 
696  C CE1 . TYR A 98  ? 1.1540 0.7948 0.8580 -0.1271 -0.0871 -0.1155 394 TYR A CE1 
697  C CE2 . TYR A 98  ? 1.1426 0.6495 0.7584 -0.0780 -0.0847 -0.1156 394 TYR A CE2 
698  C CZ  . TYR A 98  ? 1.1163 0.7151 0.8025 -0.1108 -0.0845 -0.1110 394 TYR A CZ  
699  O OH  . TYR A 98  ? 1.1400 0.7889 0.8753 -0.1227 -0.0822 -0.1022 394 TYR A OH  
700  N N   . GLN A 99  ? 1.2658 0.9068 0.9429 -0.0438 -0.0813 -0.1351 395 GLN A N   
701  C CA  . GLN A 99  ? 1.1188 0.8605 0.8771 -0.0443 -0.0782 -0.1284 395 GLN A CA  
702  C C   . GLN A 99  ? 1.0754 0.8642 0.8680 -0.0877 -0.0842 -0.1238 395 GLN A C   
703  O O   . GLN A 99  ? 1.1312 0.8897 0.8839 -0.1272 -0.0923 -0.1288 395 GLN A O   
704  C CB  . GLN A 99  ? 1.1693 0.9260 0.9217 -0.0351 -0.0780 -0.1341 395 GLN A CB  
705  C CG  . GLN A 99  ? 1.0255 0.7557 0.7506 0.0115  -0.0702 -0.1386 395 GLN A CG  
706  C CD  . GLN A 99  ? 1.1155 0.9083 0.8987 0.0442  -0.0602 -0.1294 395 GLN A CD  
707  O OE1 . GLN A 99  ? 1.1464 1.0094 0.9915 0.0350  -0.0584 -0.1207 395 GLN A OE1 
708  N NE2 . GLN A 99  ? 1.1461 0.9126 0.9037 0.0826  -0.0544 -0.1314 395 GLN A NE2 
709  N N   . LEU A 100 ? 0.9011 0.7654 0.7633 -0.0807 -0.0805 -0.1146 396 LEU A N   
710  C CA  . LEU A 100 ? 0.8937 0.8143 0.7924 -0.1113 -0.0850 -0.1101 396 LEU A CA  
711  C C   . LEU A 100 ? 0.9275 0.9040 0.8468 -0.1215 -0.0903 -0.1118 396 LEU A C   
712  O O   . LEU A 100 ? 0.9542 0.9472 0.8868 -0.0971 -0.0875 -0.1114 396 LEU A O   
713  C CB  . LEU A 100 ? 0.7957 0.7627 0.7497 -0.0947 -0.0794 -0.1001 396 LEU A CB  
714  C CG  . LEU A 100 ? 0.9062 0.8336 0.8485 -0.0883 -0.0756 -0.0969 396 LEU A CG  
715  C CD1 . LEU A 100 ? 0.8585 0.8310 0.8534 -0.0657 -0.0698 -0.0878 396 LEU A CD1 
716  C CD2 . LEU A 100 ? 0.9227 0.8337 0.8426 -0.1269 -0.0804 -0.0975 396 LEU A CD2 
717  N N   . LYS A 101 ? 0.9046 0.9149 0.8247 -0.1583 -0.0980 -0.1134 397 LYS A N   
718  C CA  . LYS A 101 ? 0.9443 1.0273 0.8931 -0.1645 -0.1040 -0.1134 397 LYS A CA  
719  C C   . LYS A 101 ? 0.9830 1.1274 0.9895 -0.1347 -0.0999 -0.1043 397 LYS A C   
720  O O   . LYS A 101 ? 0.9979 1.1435 1.0263 -0.1242 -0.0943 -0.0982 397 LYS A O   
721  C CB  . LYS A 101 ? 0.9535 1.0751 0.8938 -0.2108 -0.1129 -0.1166 397 LYS A CB  
722  C CG  . LYS A 101 ? 1.1002 1.1575 0.9723 -0.2497 -0.1194 -0.1259 397 LYS A CG  
723  C CD  . LYS A 101 ? 1.0913 1.1282 0.9397 -0.2379 -0.1227 -0.1324 397 LYS A CD  
724  C CE  . LYS A 101 ? 1.2765 1.2339 1.0455 -0.2733 -0.1295 -0.1427 397 LYS A CE  
725  N NZ  . LYS A 101 ? 1.2628 1.2068 1.0119 -0.2579 -0.1324 -0.1492 397 LYS A NZ  
726  N N   . ASP A 102 ? 0.8242 1.0125 0.8478 -0.1207 -0.1035 -0.1034 398 ASP A N   
727  C CA  . ASP A 102 ? 0.7770 1.0135 0.8410 -0.0933 -0.1018 -0.0950 398 ASP A CA  
728  C C   . ASP A 102 ? 0.6920 0.9756 0.7819 -0.1016 -0.1029 -0.0916 398 ASP A C   
729  O O   . ASP A 102 ? 0.7233 1.0084 0.8347 -0.0820 -0.0974 -0.0849 398 ASP A O   
730  C CB  . ASP A 102 ? 0.9764 1.2536 1.0436 -0.0818 -0.1087 -0.0953 398 ASP A CB  
731  C CG  . ASP A 102 ? 1.0747 1.3133 1.1252 -0.0628 -0.1048 -0.0949 398 ASP A CG  
732  O OD1 . ASP A 102 ? 1.0957 1.2828 1.1319 -0.0588 -0.0969 -0.0958 398 ASP A OD1 
733  O OD2 . ASP A 102 ? 1.1388 1.4030 1.1888 -0.0500 -0.1098 -0.0935 398 ASP A OD2 
734  N N   . THR A 103 ? 0.6898 1.0161 0.7758 -0.1327 -0.1100 -0.0962 399 THR A N   
735  C CA  . THR A 103 ? 0.7124 1.0937 0.8221 -0.1429 -0.1100 -0.0935 399 THR A CA  
736  C C   . THR A 103 ? 0.7730 1.1042 0.8772 -0.1516 -0.1022 -0.0908 399 THR A C   
737  O O   . THR A 103 ? 0.6544 1.0125 0.7835 -0.1405 -0.0982 -0.0856 399 THR A O   
738  C CB  . THR A 103 ? 0.8246 1.2668 0.9270 -0.1832 -0.1187 -0.0992 399 THR A CB  
739  O OG1 . THR A 103 ? 0.8260 1.2047 0.8828 -0.2216 -0.1208 -0.1057 399 THR A OG1 
740  C CG2 . THR A 103 ? 0.7884 1.3002 0.9030 -0.1686 -0.1277 -0.1010 399 THR A CG2 
741  N N   . GLU A 104 ? 0.8701 1.1251 0.9369 -0.1681 -0.1003 -0.0945 400 GLU A N   
742  C CA  . GLU A 104 ? 0.7999 1.0021 0.8541 -0.1733 -0.0941 -0.0920 400 GLU A CA  
743  C C   . GLU A 104 ? 0.7656 0.9509 0.8444 -0.1335 -0.0865 -0.0853 400 GLU A C   
744  O O   . GLU A 104 ? 0.7226 0.9048 0.8139 -0.1301 -0.0820 -0.0805 400 GLU A O   
745  C CB  . GLU A 104 ? 0.8653 0.9823 0.8614 -0.1938 -0.0953 -0.0982 400 GLU A CB  
746  C CG  . GLU A 104 ? 0.8603 0.9803 0.8193 -0.2456 -0.1033 -0.1042 400 GLU A CG  
747  C CD  . GLU A 104 ? 1.0605 1.0841 0.9476 -0.2629 -0.1066 -0.1120 400 GLU A CD  
748  O OE1 . GLU A 104 ? 1.1656 1.1802 1.0114 -0.3109 -0.1141 -0.1172 400 GLU A OE1 
749  O OE2 . GLU A 104 ? 1.0857 1.0444 0.9533 -0.2292 -0.1021 -0.1131 400 GLU A OE2 
750  N N   . LEU A 105 ? 0.6534 0.8293 0.7367 -0.1065 -0.0851 -0.0847 401 LEU A N   
751  C CA  . LEU A 105 ? 0.7168 0.8833 0.8202 -0.0756 -0.0786 -0.0779 401 LEU A CA  
752  C C   . LEU A 105 ? 0.6976 0.9119 0.8331 -0.0632 -0.0787 -0.0717 401 LEU A C   
753  O O   . LEU A 105 ? 0.5759 0.7795 0.7234 -0.0513 -0.0740 -0.0662 401 LEU A O   
754  C CB  . LEU A 105 ? 0.7366 0.8898 0.8331 -0.0564 -0.0772 -0.0783 401 LEU A CB  
755  C CG  . LEU A 105 ? 0.6955 0.8350 0.8026 -0.0325 -0.0700 -0.0720 401 LEU A CG  
756  C CD1 . LEU A 105 ? 0.6716 0.7703 0.7641 -0.0280 -0.0646 -0.0732 401 LEU A CD1 
757  C CD2 . LEU A 105 ? 0.7915 0.9356 0.8929 -0.0203 -0.0696 -0.0715 401 LEU A CD2 
758  N N   . ILE A 106 ? 0.5776 0.8451 0.7231 -0.0641 -0.0846 -0.0728 402 ILE A N   
759  C CA  . ILE A 106 ? 0.4961 0.8047 0.6628 -0.0438 -0.0852 -0.0678 402 ILE A CA  
760  C C   . ILE A 106 ? 0.5753 0.9042 0.7534 -0.0567 -0.0827 -0.0670 402 ILE A C   
761  O O   . ILE A 106 ? 0.6159 0.9423 0.8045 -0.0398 -0.0791 -0.0621 402 ILE A O   
762  C CB  . ILE A 106 ? 0.6078 0.9712 0.7772 -0.0335 -0.0930 -0.0698 402 ILE A CB  
763  C CG1 . ILE A 106 ? 0.6045 0.9387 0.7596 -0.0151 -0.0943 -0.0681 402 ILE A CG1 
764  C CG2 . ILE A 106 ? 0.6305 1.0426 0.8138 -0.0099 -0.0949 -0.0666 402 ILE A CG2 
765  C CD1 . ILE A 106 ? 0.5911 0.9698 0.7409 -0.0085 -0.1033 -0.0712 402 ILE A CD1 
766  N N   . TYR A 107 ? 0.6811 1.0264 0.8518 -0.0900 -0.0847 -0.0718 403 TYR A N   
767  C CA  . TYR A 107 ? 0.6693 1.0293 0.8443 -0.1098 -0.0817 -0.0707 403 TYR A CA  
768  C C   . TYR A 107 ? 0.7109 1.0065 0.8791 -0.1045 -0.0752 -0.0667 403 TYR A C   
769  O O   . TYR A 107 ? 0.5473 0.8531 0.7290 -0.0959 -0.0714 -0.0626 403 TYR A O   
770  C CB  . TYR A 107 ? 0.7280 1.1006 0.8826 -0.1552 -0.0856 -0.0762 403 TYR A CB  
771  C CG  . TYR A 107 ? 0.8126 1.1878 0.9610 -0.1839 -0.0820 -0.0745 403 TYR A CG  
772  C CD1 . TYR A 107 ? 0.7875 1.2489 0.9562 -0.1965 -0.0822 -0.0741 403 TYR A CD1 
773  C CD2 . TYR A 107 ? 0.8671 1.1614 0.9865 -0.1962 -0.0783 -0.0732 403 TYR A CD2 
774  C CE1 . TYR A 107 ? 0.7593 1.2253 0.9201 -0.2260 -0.0780 -0.0720 403 TYR A CE1 
775  C CE2 . TYR A 107 ? 0.8214 1.1113 0.9292 -0.2230 -0.0752 -0.0708 403 TYR A CE2 
776  C CZ  . TYR A 107 ? 0.8385 1.2139 0.9673 -0.2405 -0.0747 -0.0700 403 TYR A CZ  
777  O OH  . TYR A 107 ? 0.8083 1.1815 0.9231 -0.2706 -0.0708 -0.0671 403 TYR A OH  
778  N N   . GLY A 108 ? 0.7130 0.9449 0.8580 -0.1068 -0.0742 -0.0683 404 GLY A N   
779  C CA  . GLY A 108 ? 0.6147 0.7933 0.7517 -0.0986 -0.0691 -0.0648 404 GLY A CA  
780  C C   . GLY A 108 ? 0.6706 0.8562 0.8316 -0.0693 -0.0656 -0.0586 404 GLY A C   
781  O O   . GLY A 108 ? 0.5809 0.7565 0.7475 -0.0661 -0.0624 -0.0546 404 GLY A O   
782  N N   . ALA A 109 ? 0.7394 0.9377 0.9090 -0.0502 -0.0667 -0.0575 405 ALA A N   
783  C CA  . ALA A 109 ? 0.6433 0.8387 0.8239 -0.0283 -0.0645 -0.0513 405 ALA A CA  
784  C C   . ALA A 109 ? 0.6501 0.8757 0.8423 -0.0221 -0.0649 -0.0489 405 ALA A C   
785  O O   . ALA A 109 ? 0.6497 0.8602 0.8447 -0.0153 -0.0621 -0.0447 405 ALA A O   
786  C CB  . ALA A 109 ? 0.6179 0.8140 0.7943 -0.0137 -0.0662 -0.0501 405 ALA A CB  
787  N N   . LYS A 110 ? 0.5645 0.8375 0.7619 -0.0227 -0.0685 -0.0520 406 LYS A N   
788  C CA  . LYS A 110 ? 0.6183 0.9276 0.8241 -0.0089 -0.0685 -0.0505 406 LYS A CA  
789  C C   . LYS A 110 ? 0.6000 0.9087 0.8112 -0.0244 -0.0640 -0.0496 406 LYS A C   
790  O O   . LYS A 110 ? 0.6356 0.9535 0.8498 -0.0097 -0.0620 -0.0471 406 LYS A O   
791  C CB  . LYS A 110 ? 0.6048 0.9814 0.8169 -0.0050 -0.0734 -0.0545 406 LYS A CB  
792  C CG  . LYS A 110 ? 0.6427 1.0236 0.8450 0.0255  -0.0785 -0.0537 406 LYS A CG  
793  C CD  . LYS A 110 ? 0.6276 1.0845 0.8369 0.0305  -0.0845 -0.0582 406 LYS A CD  
794  C CE  . LYS A 110 ? 0.6301 1.0829 0.8221 0.0653  -0.0907 -0.0568 406 LYS A CE  
795  N NZ  . LYS A 110 ? 0.6999 1.2378 0.8980 0.0823  -0.0974 -0.0607 406 LYS A NZ  
796  N N   . HIS A 111 ? 0.5434 0.8341 0.7483 -0.0530 -0.0627 -0.0515 407 HIS A N   
797  C CA  . HIS A 111 ? 0.6113 0.8947 0.8137 -0.0705 -0.0589 -0.0500 407 HIS A CA  
798  C C   . HIS A 111 ? 0.6973 0.9232 0.8928 -0.0632 -0.0560 -0.0458 407 HIS A C   
799  O O   . HIS A 111 ? 0.5860 0.8076 0.7820 -0.0658 -0.0530 -0.0429 407 HIS A O   
800  C CB  . HIS A 111 ? 0.6514 0.9370 0.8379 -0.1077 -0.0601 -0.0537 407 HIS A CB  
801  C CG  . HIS A 111 ? 0.6128 0.9759 0.8097 -0.1230 -0.0621 -0.0568 407 HIS A CG  
802  N ND1 . HIS A 111 ? 0.5963 1.0036 0.7972 -0.1424 -0.0589 -0.0560 407 HIS A ND1 
803  C CD2 . HIS A 111 ? 0.5806 0.9947 0.7858 -0.1199 -0.0671 -0.0606 407 HIS A CD2 
804  C CE1 . HIS A 111 ? 0.5965 1.0862 0.8097 -0.1516 -0.0616 -0.0593 407 HIS A CE1 
805  N NE2 . HIS A 111 ? 0.6137 1.1083 0.8296 -0.1371 -0.0671 -0.0622 407 HIS A NE2 
806  N N   . ALA A 112 ? 0.6502 0.8393 0.8394 -0.0536 -0.0568 -0.0454 408 ALA A N   
807  C CA  . ALA A 112 ? 0.6014 0.7561 0.7895 -0.0416 -0.0547 -0.0409 408 ALA A CA  
808  C C   . ALA A 112 ? 0.6461 0.8128 0.8441 -0.0269 -0.0540 -0.0368 408 ALA A C   
809  O O   . ALA A 112 ? 0.6111 0.7643 0.8084 -0.0269 -0.0523 -0.0336 408 ALA A O   
810  C CB  . ALA A 112 ? 0.5664 0.7014 0.7501 -0.0316 -0.0551 -0.0411 408 ALA A CB  
811  N N   . TRP A 113 ? 0.5053 0.6921 0.7055 -0.0130 -0.0560 -0.0370 409 TRP A N   
812  C CA  . TRP A 113 ? 0.4901 0.6773 0.6860 0.0035  -0.0562 -0.0341 409 TRP A CA  
813  C C   . TRP A 113 ? 0.5684 0.7834 0.7695 0.0015  -0.0539 -0.0354 409 TRP A C   
814  O O   . TRP A 113 ? 0.5170 0.7163 0.7136 0.0051  -0.0521 -0.0327 409 TRP A O   
815  C CB  . TRP A 113 ? 0.5320 0.7279 0.7176 0.0229  -0.0599 -0.0346 409 TRP A CB  
816  C CG  . TRP A 113 ? 0.5528 0.7321 0.7179 0.0445  -0.0614 -0.0322 409 TRP A CG  
817  C CD1 . TRP A 113 ? 0.6140 0.7700 0.7700 0.0460  -0.0598 -0.0297 409 TRP A CD1 
818  C CD2 . TRP A 113 ? 0.6166 0.7926 0.7581 0.0703  -0.0657 -0.0324 409 TRP A CD2 
819  N NE1 . TRP A 113 ? 0.6212 0.7546 0.7460 0.0699  -0.0628 -0.0288 409 TRP A NE1 
820  C CE2 . TRP A 113 ? 0.5967 0.7388 0.7096 0.0870  -0.0666 -0.0303 409 TRP A CE2 
821  C CE3 . TRP A 113 ? 0.6817 0.8747 0.8175 0.0823  -0.0698 -0.0342 409 TRP A CE3 
822  C CZ2 . TRP A 113 ? 0.6069 0.7246 0.6797 0.1179  -0.0714 -0.0300 409 TRP A CZ2 
823  C CZ3 . TRP A 113 ? 0.7004 0.8760 0.8013 0.1137  -0.0747 -0.0334 409 TRP A CZ3 
824  C CH2 . TRP A 113 ? 0.7190 0.8533 0.7856 0.1326  -0.0754 -0.0314 409 TRP A CH2 
825  N N   . ARG A 114 ? 0.5063 0.7678 0.7158 -0.0061 -0.0539 -0.0394 410 ARG A N   
826  C CA  . ARG A 114 ? 0.5292 0.8322 0.7446 -0.0117 -0.0507 -0.0406 410 ARG A CA  
827  C C   . ARG A 114 ? 0.6123 0.8863 0.8242 -0.0294 -0.0469 -0.0377 410 ARG A C   
828  O O   . ARG A 114 ? 0.4868 0.7775 0.6987 -0.0260 -0.0435 -0.0367 410 ARG A O   
829  C CB  . ARG A 114 ? 0.5608 0.9211 0.7849 -0.0310 -0.0515 -0.0449 410 ARG A CB  
830  C CG  . ARG A 114 ? 0.5608 0.9871 0.7931 -0.0352 -0.0479 -0.0463 410 ARG A CG  
831  C CD  . ARG A 114 ? 0.5886 1.0778 0.8278 -0.0645 -0.0492 -0.0501 410 ARG A CD  
832  N NE  . ARG A 114 ? 0.6628 1.2351 0.9126 -0.0672 -0.0452 -0.0514 410 ARG A NE  
833  C CZ  . ARG A 114 ? 0.6689 1.3232 0.9276 -0.0917 -0.0460 -0.0546 410 ARG A CZ  
834  N NH1 . ARG A 114 ? 0.5094 1.2506 0.7794 -0.0925 -0.0413 -0.0555 410 ARG A NH1 
835  N NH2 . ARG A 114 ? 0.7057 1.3598 0.9604 -0.1163 -0.0516 -0.0571 410 ARG A NH2 
836  N N   . ASN A 115 ? 0.6185 0.8481 0.8236 -0.0440 -0.0476 -0.0363 411 ASN A N   
837  C CA  . ASN A 115 ? 0.6562 0.8525 0.8511 -0.0585 -0.0455 -0.0334 411 ASN A CA  
838  C C   . ASN A 115 ? 0.6113 0.7716 0.8041 -0.0433 -0.0460 -0.0292 411 ASN A C   
839  O O   . ASN A 115 ? 0.4821 0.6153 0.6653 -0.0503 -0.0453 -0.0264 411 ASN A O   
840  C CB  . ASN A 115 ? 0.5794 0.7439 0.7580 -0.0776 -0.0471 -0.0350 411 ASN A CB  
841  C CG  . ASN A 115 ? 0.6647 0.8577 0.8361 -0.1049 -0.0470 -0.0385 411 ASN A CG  
842  O OD1 . ASN A 115 ? 0.6758 0.9200 0.8570 -0.1129 -0.0445 -0.0389 411 ASN A OD1 
843  N ND2 . ASN A 115 ? 0.6811 0.8443 0.8319 -0.1203 -0.0498 -0.0415 411 ASN A ND2 
844  N N   . ALA A 116 ? 0.5872 0.7449 0.7834 -0.0248 -0.0480 -0.0283 412 ALA A N   
845  C CA  . ALA A 116 ? 0.6434 0.7717 0.8347 -0.0173 -0.0496 -0.0242 412 ALA A CA  
846  C C   . ALA A 116 ? 0.6179 0.7443 0.8030 -0.0130 -0.0483 -0.0225 412 ALA A C   
847  O O   . ALA A 116 ? 0.5365 0.6688 0.7138 0.0009  -0.0487 -0.0234 412 ALA A O   
848  C CB  . ALA A 116 ? 0.5916 0.7132 0.7791 -0.0067 -0.0523 -0.0235 412 ALA A CB  
849  N N   . SER A 117 ? 0.6096 0.7229 0.7920 -0.0219 -0.0474 -0.0201 413 SER A N   
850  C CA  . SER A 117 ? 0.6313 0.7469 0.8069 -0.0198 -0.0453 -0.0191 413 SER A CA  
851  C C   . SER A 117 ? 0.6302 0.7236 0.7932 -0.0090 -0.0485 -0.0170 413 SER A C   
852  O O   . SER A 117 ? 0.5872 0.6797 0.7382 -0.0014 -0.0471 -0.0176 413 SER A O   
853  C CB  . SER A 117 ? 0.5979 0.7011 0.7682 -0.0338 -0.0438 -0.0166 413 SER A CB  
854  O OG  . SER A 117 ? 0.6099 0.6860 0.7765 -0.0333 -0.0477 -0.0134 413 SER A OG  
855  N N   . ARG A 118 ? 0.5020 0.5782 0.6632 -0.0103 -0.0526 -0.0147 414 ARG A N   
856  C CA  . ARG A 118 ? 0.5394 0.5909 0.6808 -0.0085 -0.0567 -0.0124 414 ARG A CA  
857  C C   . ARG A 118 ? 0.5843 0.6214 0.7048 0.0033  -0.0581 -0.0142 414 ARG A C   
858  O O   . ARG A 118 ? 0.5741 0.5772 0.6651 0.0017  -0.0622 -0.0122 414 ARG A O   
859  C CB  . ARG A 118 ? 0.6256 0.6744 0.7717 -0.0201 -0.0605 -0.0084 414 ARG A CB  
860  C CG  . ARG A 118 ? 0.5820 0.6384 0.7382 -0.0245 -0.0610 -0.0062 414 ARG A CG  
861  C CD  . ARG A 118 ? 0.5830 0.6513 0.7439 -0.0309 -0.0653 -0.0025 414 ARG A CD  
862  N NE  . ARG A 118 ? 0.6636 0.7357 0.8257 -0.0296 -0.0675 -0.0001 414 ARG A NE  
863  C CZ  . ARG A 118 ? 0.7243 0.8184 0.8925 -0.0287 -0.0715 0.0029  414 ARG A CZ  
864  N NH1 . ARG A 118 ? 0.7698 0.8901 0.9464 -0.0318 -0.0726 0.0038  414 ARG A NH1 
865  N NH2 . ARG A 118 ? 0.7125 0.8070 0.8771 -0.0231 -0.0744 0.0050  414 ARG A NH2 
866  N N   . CYS A 119 ? 0.5387 0.5969 0.6666 0.0147  -0.0559 -0.0177 415 CYS A N   
867  C CA  . CYS A 119 ? 0.5883 0.6294 0.6908 0.0310  -0.0585 -0.0190 415 CYS A CA  
868  C C   . CYS A 119 ? 0.6240 0.6700 0.7074 0.0560  -0.0571 -0.0229 415 CYS A C   
869  O O   . CYS A 119 ? 0.6735 0.7679 0.7787 0.0627  -0.0528 -0.0264 415 CYS A O   
870  C CB  . CYS A 119 ? 0.4989 0.5635 0.6179 0.0323  -0.0582 -0.0205 415 CYS A CB  
871  S SG  . CYS A 119 ? 0.5962 0.6426 0.6805 0.0583  -0.0622 -0.0221 415 CYS A SG  
872  N N   . VAL A 120 ? 0.7064 0.7026 0.7433 0.0700  -0.0610 -0.0226 416 VAL A N   
873  C CA  . VAL A 120 ? 0.6708 0.6653 0.6784 0.1032  -0.0601 -0.0272 416 VAL A CA  
874  C C   . VAL A 120 ? 0.7376 0.7462 0.7323 0.1328  -0.0618 -0.0303 416 VAL A C   
875  O O   . VAL A 120 ? 0.6878 0.7139 0.6634 0.1677  -0.0607 -0.0350 416 VAL A O   
876  C CB  . VAL A 120 ? 0.6961 0.6179 0.6457 0.1090  -0.0645 -0.0265 416 VAL A CB  
877  C CG1 . VAL A 120 ? 0.6572 0.5075 0.5485 0.1154  -0.0720 -0.0245 416 VAL A CG1 
878  C CG2 . VAL A 120 ? 0.7216 0.6515 0.6490 0.1415  -0.0612 -0.0319 416 VAL A CG2 
879  N N   . GLY A 121 ? 0.7567 0.7653 0.7614 0.1230  -0.0644 -0.0282 417 GLY A N   
880  C CA  . GLY A 121 ? 0.6034 0.6183 0.5882 0.1531  -0.0677 -0.0306 417 GLY A CA  
881  C C   . GLY A 121 ? 0.6988 0.7970 0.7315 0.1552  -0.0647 -0.0339 417 GLY A C   
882  O O   . GLY A 121 ? 0.7522 0.8610 0.7769 0.1719  -0.0684 -0.0349 417 GLY A O   
883  N N   . ARG A 122 ? 0.5750 0.7299 0.6520 0.1361  -0.0587 -0.0355 418 ARG A N   
884  C CA  . ARG A 122 ? 0.6160 0.8380 0.7341 0.1220  -0.0568 -0.0377 418 ARG A CA  
885  C C   . ARG A 122 ? 0.6082 0.9011 0.7301 0.1505  -0.0569 -0.0428 418 ARG A C   
886  O O   . ARG A 122 ? 0.5645 0.9178 0.7161 0.1367  -0.0566 -0.0450 418 ARG A O   
887  C CB  . ARG A 122 ? 0.5584 0.8044 0.7103 0.0870  -0.0514 -0.0369 418 ARG A CB  
888  C CG  . ARG A 122 ? 0.5343 0.7315 0.6908 0.0606  -0.0522 -0.0326 418 ARG A CG  
889  C CD  . ARG A 122 ? 0.5415 0.7541 0.7197 0.0335  -0.0479 -0.0320 418 ARG A CD  
890  N NE  . ARG A 122 ? 0.6026 0.8000 0.7716 0.0347  -0.0454 -0.0303 418 ARG A NE  
891  C CZ  . ARG A 122 ? 0.5889 0.8004 0.7679 0.0165  -0.0413 -0.0296 418 ARG A CZ  
892  N NH1 . ARG A 122 ? 0.4939 0.7294 0.6873 -0.0066 -0.0395 -0.0303 418 ARG A NH1 
893  N NH2 . ARG A 122 ? 0.6722 0.8672 0.8401 0.0194  -0.0394 -0.0279 418 ARG A NH2 
894  N N   . ILE A 123 ? 0.6049 0.8954 0.6943 0.1909  -0.0576 -0.0453 419 ILE A N   
895  C CA  . ILE A 123 ? 0.6149 0.9848 0.7073 0.2251  -0.0582 -0.0505 419 ILE A CA  
896  C C   . ILE A 123 ? 0.6720 1.0500 0.7618 0.2351  -0.0652 -0.0506 419 ILE A C   
897  O O   . ILE A 123 ? 0.5843 1.0460 0.6895 0.2528  -0.0667 -0.0547 419 ILE A O   
898  C CB  . ILE A 123 ? 0.7269 1.0802 0.7724 0.2773  -0.0586 -0.0536 419 ILE A CB  
899  C CG1 . ILE A 123 ? 0.8397 1.3075 0.9016 0.3099  -0.0561 -0.0596 419 ILE A CG1 
900  C CG2 . ILE A 123 ? 0.7526 1.0096 0.7341 0.3096  -0.0672 -0.0518 419 ILE A CG2 
901  C CD1 . ILE A 123 ? 0.9435 1.3971 0.9496 0.3769  -0.0584 -0.0640 419 ILE A CD1 
902  N N   . GLN A 124 ? 0.7478 1.0472 0.8192 0.2214  -0.0694 -0.0462 420 GLN A N   
903  C CA  . GLN A 124 ? 0.7930 1.0851 0.8543 0.2298  -0.0760 -0.0454 420 GLN A CA  
904  C C   . GLN A 124 ? 0.6978 1.0216 0.8034 0.1871  -0.0748 -0.0450 420 GLN A C   
905  O O   . GLN A 124 ? 0.6336 0.9505 0.7331 0.1889  -0.0798 -0.0444 420 GLN A O   
906  C CB  . GLN A 124 ? 0.9837 1.1677 0.9888 0.2390  -0.0810 -0.0403 420 GLN A CB  
907  C CG  . GLN A 124 ? 1.1833 1.3222 1.1216 0.2925  -0.0864 -0.0415 420 GLN A CG  
908  C CD  . GLN A 124 ? 1.2805 1.4345 1.1931 0.3306  -0.0942 -0.0427 420 GLN A CD  
909  O OE1 . GLN A 124 ? 1.3043 1.5359 1.2606 0.3223  -0.0947 -0.0449 420 GLN A OE1 
910  N NE2 . GLN A 124 ? 1.4167 1.4907 1.2515 0.3721  -0.1011 -0.0413 420 GLN A NE2 
911  N N   . TRP A 125 ? 0.6211 0.9749 0.7641 0.1505  -0.0687 -0.0457 421 TRP A N   
912  C CA  . TRP A 125 ? 0.5249 0.8723 0.6928 0.1101  -0.0676 -0.0447 421 TRP A CA  
913  C C   . TRP A 125 ? 0.5845 0.9834 0.7658 0.1063  -0.0719 -0.0481 421 TRP A C   
914  O O   . TRP A 125 ? 0.6160 0.9888 0.8005 0.0865  -0.0733 -0.0473 421 TRP A O   
915  C CB  . TRP A 125 ? 0.4793 0.8431 0.6720 0.0764  -0.0614 -0.0449 421 TRP A CB  
916  C CG  . TRP A 125 ? 0.5291 0.9783 0.7425 0.0679  -0.0595 -0.0491 421 TRP A CG  
917  C CD1 . TRP A 125 ? 0.6202 1.1199 0.8359 0.0831  -0.0559 -0.0508 421 TRP A CD1 
918  C CD2 . TRP A 125 ? 0.5993 1.0993 0.8305 0.0394  -0.0611 -0.0523 421 TRP A CD2 
919  N NE1 . TRP A 125 ? 0.5736 1.1617 0.8113 0.0634  -0.0547 -0.0543 421 TRP A NE1 
920  C CE2 . TRP A 125 ? 0.6173 1.2038 0.8628 0.0340  -0.0584 -0.0552 421 TRP A CE2 
921  C CE3 . TRP A 125 ? 0.5085 0.9897 0.7412 0.0169  -0.0645 -0.0532 421 TRP A CE3 
922  C CZ2 . TRP A 125 ? 0.6127 1.2670 0.8727 0.0008  -0.0599 -0.0585 421 TRP A CZ2 
923  C CZ3 . TRP A 125 ? 0.4716 1.0095 0.7150 -0.0129 -0.0663 -0.0571 421 TRP A CZ3 
924  C CH2 . TRP A 125 ? 0.4901 1.1140 0.7466 -0.0232 -0.0644 -0.0595 421 TRP A CH2 
925  N N   . SER A 126 ? 0.5751 1.0520 0.7633 0.1256  -0.0742 -0.0522 422 SER A N   
926  C CA  . SER A 126 ? 0.7038 1.2380 0.9043 0.1200  -0.0796 -0.0556 422 SER A CA  
927  C C   . SER A 126 ? 0.7429 1.2470 0.9152 0.1540  -0.0871 -0.0544 422 SER A C   
928  O O   . SER A 126 ? 0.7700 1.3033 0.9486 0.1468  -0.0923 -0.0564 422 SER A O   
929  C CB  . SER A 126 ? 0.6815 1.3278 0.9027 0.1241  -0.0795 -0.0604 422 SER A CB  
930  O OG  . SER A 126 ? 0.7056 1.3814 0.9084 0.1783  -0.0818 -0.0615 422 SER A OG  
931  N N   . LYS A 127 ? 0.7283 1.1684 0.8628 0.1885  -0.0884 -0.0508 423 LYS A N   
932  C CA  . LYS A 127 ? 0.7608 1.1476 0.8550 0.2158  -0.0954 -0.0479 423 LYS A CA  
933  C C   . LYS A 127 ? 0.8347 1.1345 0.9177 0.1868  -0.0927 -0.0424 423 LYS A C   
934  O O   . LYS A 127 ? 0.8112 1.0389 0.8629 0.1910  -0.0913 -0.0379 423 LYS A O   
935  C CB  . LYS A 127 ? 0.8233 1.1818 0.8681 0.2697  -0.0995 -0.0471 423 LYS A CB  
936  C CG  . LYS A 127 ? 0.9401 1.3877 0.9847 0.3135  -0.1048 -0.0523 423 LYS A CG  
937  C CD  . LYS A 127 ? 1.1447 1.5398 1.1252 0.3663  -0.1146 -0.0502 423 LYS A CD  
938  C CE  . LYS A 127 ? 1.1845 1.6729 1.1752 0.3953  -0.1226 -0.0543 423 LYS A CE  
939  N NZ  . LYS A 127 ? 1.3030 1.7237 1.2275 0.4393  -0.1329 -0.0508 423 LYS A NZ  
940  N N   . LEU A 128 ? 0.8021 1.1133 0.9092 0.1555  -0.0920 -0.0432 424 LEU A N   
941  C CA  . LEU A 128 ? 0.7305 0.9788 0.8323 0.1295  -0.0887 -0.0390 424 LEU A CA  
942  C C   . LEU A 128 ? 0.7200 0.9733 0.8195 0.1238  -0.0924 -0.0397 424 LEU A C   
943  O O   . LEU A 128 ? 0.6683 0.9798 0.7899 0.1171  -0.0950 -0.0450 424 LEU A O   
944  C CB  . LEU A 128 ? 0.6286 0.8798 0.7627 0.0948  -0.0814 -0.0399 424 LEU A CB  
945  C CG  . LEU A 128 ? 0.5757 0.7790 0.7085 0.0716  -0.0776 -0.0364 424 LEU A CG  
946  C CD1 . LEU A 128 ? 0.6128 0.7558 0.7141 0.0775  -0.0771 -0.0296 424 LEU A CD1 
947  C CD2 . LEU A 128 ? 0.5333 0.7453 0.6937 0.0447  -0.0721 -0.0386 424 LEU A CD2 
948  N N   . GLN A 129 ? 0.7184 0.9113 0.7866 0.1246  -0.0930 -0.0342 425 GLN A N   
949  C CA  . GLN A 129 ? 0.8295 1.0180 0.8881 0.1208  -0.0959 -0.0338 425 GLN A CA  
950  C C   . GLN A 129 ? 0.8099 0.9837 0.8876 0.0873  -0.0889 -0.0336 425 GLN A C   
951  O O   . GLN A 129 ? 0.7721 0.9065 0.8426 0.0751  -0.0838 -0.0288 425 GLN A O   
952  C CB  . GLN A 129 ? 0.9119 1.0420 0.9151 0.1434  -0.1009 -0.0272 425 GLN A CB  
953  C CG  . GLN A 129 ? 0.9419 1.0596 0.9295 0.1375  -0.1031 -0.0255 425 GLN A CG  
954  C CD  . GLN A 129 ? 0.9675 1.1488 0.9740 0.1481  -0.1093 -0.0320 425 GLN A CD  
955  O OE1 . GLN A 129 ? 0.9764 1.2081 0.9925 0.1705  -0.1145 -0.0361 425 GLN A OE1 
956  N NE2 . GLN A 129 ? 0.9987 1.1839 1.0098 0.1312  -0.1088 -0.0332 425 GLN A NE2 
957  N N   . VAL A 130 ? 0.6846 0.8924 0.7837 0.0732  -0.0890 -0.0393 426 VAL A N   
958  C CA  . VAL A 130 ? 0.6418 0.8390 0.7558 0.0480  -0.0825 -0.0411 426 VAL A CA  
959  C C   . VAL A 130 ? 0.6509 0.8328 0.7472 0.0466  -0.0828 -0.0402 426 VAL A C   
960  O O   . VAL A 130 ? 0.6248 0.8265 0.7129 0.0549  -0.0891 -0.0429 426 VAL A O   
961  C CB  . VAL A 130 ? 0.5919 0.8239 0.7307 0.0309  -0.0823 -0.0488 426 VAL A CB  
962  C CG1 . VAL A 130 ? 0.6570 0.8657 0.7989 0.0123  -0.0764 -0.0514 426 VAL A CG1 
963  C CG2 . VAL A 130 ? 0.5136 0.7657 0.6675 0.0316  -0.0815 -0.0489 426 VAL A CG2 
964  N N   . PHE A 131 ? 0.6569 0.8097 0.7463 0.0366  -0.0762 -0.0361 427 PHE A N   
965  C CA  . PHE A 131 ? 0.6386 0.7793 0.7095 0.0335  -0.0746 -0.0344 427 PHE A CA  
966  C C   . PHE A 131 ? 0.6413 0.7909 0.7279 0.0208  -0.0680 -0.0400 427 PHE A C   
967  O O   . PHE A 131 ? 0.5975 0.7427 0.6947 0.0141  -0.0615 -0.0384 427 PHE A O   
968  C CB  . PHE A 131 ? 0.5900 0.6947 0.6322 0.0310  -0.0719 -0.0245 427 PHE A CB  
969  C CG  . PHE A 131 ? 0.6364 0.7124 0.6419 0.0483  -0.0797 -0.0190 427 PHE A CG  
970  C CD1 . PHE A 131 ? 0.7243 0.8016 0.7082 0.0642  -0.0868 -0.0198 427 PHE A CD1 
971  C CD2 . PHE A 131 ? 0.7689 0.8117 0.7545 0.0511  -0.0807 -0.0133 427 PHE A CD2 
972  C CE1 . PHE A 131 ? 0.7015 0.7459 0.6422 0.0875  -0.0949 -0.0147 427 PHE A CE1 
973  C CE2 . PHE A 131 ? 0.8111 0.8155 0.7511 0.0723  -0.0884 -0.0089 427 PHE A CE2 
974  C CZ  . PHE A 131 ? 0.7626 0.7667 0.6787 0.0929  -0.0956 -0.0094 427 PHE A CZ  
975  N N   . ASP A 132 ? 0.6351 0.7962 0.7187 0.0198  -0.0705 -0.0469 428 ASP A N   
976  C CA  . ASP A 132 ? 0.6060 0.7654 0.6927 0.0124  -0.0658 -0.0542 428 ASP A CA  
977  C C   . ASP A 132 ? 0.6479 0.8006 0.7208 0.0143  -0.0587 -0.0514 428 ASP A C   
978  O O   . ASP A 132 ? 0.7167 0.8694 0.7722 0.0165  -0.0605 -0.0520 428 ASP A O   
979  C CB  . ASP A 132 ? 0.6474 0.8169 0.7286 0.0066  -0.0727 -0.0633 428 ASP A CB  
980  C CG  . ASP A 132 ? 0.7775 0.9278 0.8460 0.0002  -0.0692 -0.0718 428 ASP A CG  
981  O OD1 . ASP A 132 ? 0.8140 0.9633 0.8697 -0.0108 -0.0753 -0.0798 428 ASP A OD1 
982  O OD2 . ASP A 132 ? 0.8094 0.9456 0.8762 0.0067  -0.0611 -0.0708 428 ASP A OD2 
983  N N   . ALA A 133 ? 0.6012 0.7546 0.6815 0.0133  -0.0507 -0.0480 429 ALA A N   
984  C CA  . ALA A 133 ? 0.5995 0.7625 0.6700 0.0139  -0.0423 -0.0458 429 ALA A CA  
985  C C   . ALA A 133 ? 0.6054 0.7725 0.6751 0.0237  -0.0367 -0.0545 429 ALA A C   
986  O O   . ALA A 133 ? 0.6313 0.8195 0.7014 0.0291  -0.0281 -0.0529 429 ALA A O   
987  C CB  . ALA A 133 ? 0.6061 0.7783 0.6807 0.0049  -0.0373 -0.0354 429 ALA A CB  
988  N N   . ARG A 134 ? 0.6298 0.7771 0.6932 0.0263  -0.0417 -0.0637 430 ARG A N   
989  C CA  . ARG A 134 ? 0.6899 0.8229 0.7366 0.0389  -0.0378 -0.0727 430 ARG A CA  
990  C C   . ARG A 134 ? 0.7103 0.8456 0.7331 0.0486  -0.0334 -0.0776 430 ARG A C   
991  O O   . ARG A 134 ? 0.7554 0.8778 0.7576 0.0659  -0.0289 -0.0853 430 ARG A O   
992  C CB  . ARG A 134 ? 0.6837 0.7828 0.7180 0.0321  -0.0453 -0.0807 430 ARG A CB  
993  C CG  . ARG A 134 ? 0.7262 0.8233 0.7805 0.0265  -0.0469 -0.0766 430 ARG A CG  
994  C CD  . ARG A 134 ? 0.7463 0.8128 0.7847 0.0120  -0.0542 -0.0832 430 ARG A CD  
995  N NE  . ARG A 134 ? 0.7722 0.8519 0.8109 -0.0048 -0.0619 -0.0851 430 ARG A NE  
996  C CZ  . ARG A 134 ? 0.8044 0.8678 0.8230 -0.0242 -0.0691 -0.0921 430 ARG A CZ  
997  N NH1 . ARG A 134 ? 0.8943 0.9126 0.8830 -0.0311 -0.0696 -0.0977 430 ARG A NH1 
998  N NH2 . ARG A 134 ? 0.7895 0.8815 0.8129 -0.0378 -0.0765 -0.0933 430 ARG A NH2 
999  N N   . ASP A 135 ? 0.6880 0.8359 0.7075 0.0413  -0.0344 -0.0736 431 ASP A N   
1000 C CA  . ASP A 135 ? 0.7847 0.9403 0.7820 0.0500  -0.0285 -0.0769 431 ASP A CA  
1001 C C   . ASP A 135 ? 0.7800 0.9761 0.7859 0.0526  -0.0171 -0.0686 431 ASP A C   
1002 O O   . ASP A 135 ? 0.8239 1.0366 0.8131 0.0584  -0.0104 -0.0699 431 ASP A O   
1003 C CB  . ASP A 135 ? 0.8500 0.9981 0.8327 0.0403  -0.0358 -0.0769 431 ASP A CB  
1004 C CG  . ASP A 135 ? 0.9305 1.0902 0.9243 0.0289  -0.0390 -0.0644 431 ASP A CG  
1005 O OD1 . ASP A 135 ? 0.8808 1.0351 0.8597 0.0257  -0.0455 -0.0629 431 ASP A OD1 
1006 O OD2 . ASP A 135 ? 0.8747 1.0437 0.8858 0.0241  -0.0359 -0.0561 431 ASP A OD2 
1007 N N   . CYS A 136 ? 0.7451 0.9609 0.7746 0.0453  -0.0149 -0.0601 432 CYS A N   
1008 C CA  . CYS A 136 ? 0.7376 0.9992 0.7745 0.0394  -0.0050 -0.0514 432 CYS A CA  
1009 C C   . CYS A 136 ? 0.8025 1.1003 0.8383 0.0632  0.0050  -0.0579 432 CYS A C   
1010 O O   . CYS A 136 ? 0.9204 1.2019 0.9551 0.0843  0.0034  -0.0661 432 CYS A O   
1011 C CB  . CYS A 136 ? 0.6200 0.8882 0.6776 0.0229  -0.0072 -0.0417 432 CYS A CB  
1012 S SG  . CYS A 136 ? 0.7100 1.0242 0.7663 -0.0032 0.0011  -0.0278 432 CYS A SG  
1013 N N   . THR A 137 ? 0.6678 1.0160 0.6994 0.0609  0.0154  -0.0538 433 THR A N   
1014 C CA  . THR A 137 ? 0.5585 0.9568 0.5877 0.0888  0.0261  -0.0599 433 THR A CA  
1015 C C   . THR A 137 ? 0.5957 1.0779 0.6440 0.0760  0.0364  -0.0500 433 THR A C   
1016 O O   . THR A 137 ? 0.7130 1.2517 0.7662 0.1034  0.0446  -0.0546 433 THR A O   
1017 C CB  . THR A 137 ? 0.7165 1.1084 0.7147 0.1067  0.0309  -0.0687 433 THR A CB  
1018 O OG1 . THR A 137 ? 0.7427 1.1509 0.7339 0.0796  0.0341  -0.0600 433 THR A OG1 
1019 C CG2 . THR A 137 ? 0.7049 1.0183 0.6782 0.1178  0.0204  -0.0801 433 THR A CG2 
1020 N N   . THR A 138 ? 0.6841 1.1765 0.7378 0.0358  0.0357  -0.0368 434 THR A N   
1021 C CA  . THR A 138 ? 0.6670 1.2396 0.7304 0.0121  0.0452  -0.0266 434 THR A CA  
1022 C C   . THR A 138 ? 0.6365 1.1949 0.7086 -0.0255 0.0386  -0.0148 434 THR A C   
1023 O O   . THR A 138 ? 0.6799 1.1645 0.7444 -0.0349 0.0279  -0.0130 434 THR A O   
1024 C CB  . THR A 138 ? 0.7280 1.3260 0.7675 -0.0096 0.0536  -0.0209 434 THR A CB  
1025 O OG1 . THR A 138 ? 0.8348 1.3528 0.8492 -0.0275 0.0446  -0.0173 434 THR A OG1 
1026 C CG2 . THR A 138 ? 0.7393 1.3786 0.7701 0.0271  0.0639  -0.0317 434 THR A CG2 
1027 N N   . ALA A 139 ? 0.6960 1.3304 0.7807 -0.0475 0.0451  -0.0069 435 ALA A N   
1028 C CA  . ALA A 139 ? 0.6000 1.2213 0.6837 -0.0891 0.0392  0.0047  435 ALA A CA  
1029 C C   . ALA A 139 ? 0.7319 1.2860 0.7757 -0.1272 0.0346  0.0146  435 ALA A C   
1030 O O   . ALA A 139 ? 0.7737 1.2640 0.8037 -0.1460 0.0248  0.0202  435 ALA A O   
1031 C CB  . ALA A 139 ? 0.6473 1.3734 0.7465 -0.1119 0.0474  0.0115  435 ALA A CB  
1032 N N   . HIS A 140 ? 0.7000 1.2647 0.7191 -0.1367 0.0415  0.0170  436 HIS A N   
1033 C CA  . HIS A 140 ? 0.7989 1.2895 0.7709 -0.1658 0.0362  0.0259  436 HIS A CA  
1034 C C   . HIS A 140 ? 0.7731 1.1724 0.7382 -0.1392 0.0237  0.0198  436 HIS A C   
1035 O O   . HIS A 140 ? 0.8127 1.1400 0.7462 -0.1559 0.0141  0.0268  436 HIS A O   
1036 C CB  . HIS A 140 ? 0.8107 1.3312 0.7582 -0.1747 0.0462  0.0282  436 HIS A CB  
1037 C CG  . HIS A 140 ? 0.8455 1.4378 0.7782 -0.2219 0.0569  0.0399  436 HIS A CG  
1038 N ND1 . HIS A 140 ? 0.8530 1.5585 0.8222 -0.2212 0.0672  0.0381  436 HIS A ND1 
1039 C CD2 . HIS A 140 ? 0.8851 1.4549 0.7661 -0.2732 0.0586  0.0538  436 HIS A CD2 
1040 C CE1 . HIS A 140 ? 0.8919 1.6529 0.8380 -0.2732 0.0753  0.0503  436 HIS A CE1 
1041 N NE2 . HIS A 140 ? 0.8684 1.5426 0.7579 -0.3084 0.0703  0.0604  436 HIS A NE2 
1042 N N   . GLY A 141 ? 0.8148 1.2161 0.8030 -0.0979 0.0233  0.0066  437 GLY A N   
1043 C CA  . GLY A 141 ? 0.8221 1.1531 0.8083 -0.0764 0.0113  0.0004  437 GLY A CA  
1044 C C   . GLY A 141 ? 0.7743 1.0739 0.7741 -0.0788 0.0025  0.0021  437 GLY A C   
1045 O O   . GLY A 141 ? 0.7339 0.9732 0.7163 -0.0785 -0.0077 0.0041  437 GLY A O   
1046 N N   . MET A 142 ? 0.7684 1.1126 0.7978 -0.0782 0.0064  0.0012  438 MET A N   
1047 C CA  . MET A 142 ? 0.7137 1.0329 0.7539 -0.0840 -0.0010 0.0037  438 MET A CA  
1048 C C   . MET A 142 ? 0.7353 1.0123 0.7381 -0.1195 -0.0056 0.0162  438 MET A C   
1049 O O   . MET A 142 ? 0.8354 1.0523 0.8244 -0.1167 -0.0152 0.0175  438 MET A O   
1050 C CB  . MET A 142 ? 0.6672 1.0490 0.7406 -0.0795 0.0043  0.0019  438 MET A CB  
1051 C CG  . MET A 142 ? 0.5926 0.9997 0.6916 -0.0394 0.0072  -0.0106 438 MET A CG  
1052 S SD  . MET A 142 ? 0.5651 1.0470 0.6948 -0.0299 0.0119  -0.0110 438 MET A SD  
1053 C CE  . MET A 142 ? 0.6013 1.0326 0.7382 -0.0437 0.0010  -0.0069 438 MET A CE  
1054 N N   . PHE A 143 ? 0.7420 1.0479 0.7217 -0.1535 0.0010  0.0256  439 PHE A N   
1055 C CA  . PHE A 143 ? 0.7728 1.0223 0.6998 -0.1917 -0.0041 0.0380  439 PHE A CA  
1056 C C   . PHE A 143 ? 0.8753 1.0369 0.7612 -0.1780 -0.0135 0.0387  439 PHE A C   
1057 O O   . PHE A 143 ? 0.8306 0.9230 0.6845 -0.1808 -0.0231 0.0427  439 PHE A O   
1058 C CB  . PHE A 143 ? 0.7581 1.0522 0.6592 -0.2341 0.0052  0.0478  439 PHE A CB  
1059 C CG  . PHE A 143 ? 0.9188 1.1407 0.7492 -0.2794 -0.0003 0.0614  439 PHE A CG  
1060 C CD1 . PHE A 143 ? 0.9705 1.1510 0.7453 -0.2977 0.0007  0.0688  439 PHE A CD1 
1061 C CD2 . PHE A 143 ? 0.8908 1.0764 0.7019 -0.3031 -0.0073 0.0666  439 PHE A CD2 
1062 C CE1 . PHE A 143 ? 1.0491 1.1469 0.7445 -0.3393 -0.0054 0.0817  439 PHE A CE1 
1063 C CE2 . PHE A 143 ? 0.9887 1.0924 0.7211 -0.3448 -0.0133 0.0786  439 PHE A CE2 
1064 C CZ  . PHE A 143 ? 1.0517 1.1072 0.7229 -0.3629 -0.0126 0.0864  439 PHE A CZ  
1065 N N   . ASN A 144 ? 0.8288 0.9938 0.7127 -0.1595 -0.0114 0.0344  440 ASN A N   
1066 C CA  . ASN A 144 ? 0.7771 0.8703 0.6238 -0.1425 -0.0212 0.0347  440 ASN A CA  
1067 C C   . ASN A 144 ? 0.7259 0.7902 0.5945 -0.1101 -0.0314 0.0270  440 ASN A C   
1068 O O   . ASN A 144 ? 0.9519 0.9518 0.7828 -0.1035 -0.0413 0.0308  440 ASN A O   
1069 C CB  . ASN A 144 ? 0.8662 0.9801 0.7146 -0.1269 -0.0174 0.0297  440 ASN A CB  
1070 C CG  . ASN A 144 ? 0.8797 0.9256 0.6779 -0.1170 -0.0271 0.0332  440 ASN A CG  
1071 O OD1 . ASN A 144 ? 1.0477 1.0417 0.7853 -0.1408 -0.0294 0.0450  440 ASN A OD1 
1072 N ND2 . ASN A 144 ? 0.8317 0.8764 0.6491 -0.0829 -0.0335 0.0233  440 ASN A ND2 
1073 N N   . TYR A 145 ? 0.7066 0.8169 0.6305 -0.0884 -0.0290 0.0160  441 TYR A N   
1074 C CA  . TYR A 145 ? 0.7644 0.8558 0.7096 -0.0641 -0.0375 0.0093  441 TYR A CA  
1075 C C   . TYR A 145 ? 0.8126 0.8716 0.7447 -0.0751 -0.0419 0.0153  441 TYR A C   
1076 O O   . TYR A 145 ? 0.8128 0.8294 0.7289 -0.0589 -0.0509 0.0148  441 TYR A O   
1077 C CB  . TYR A 145 ? 0.6103 0.7483 0.6065 -0.0470 -0.0336 -0.0020 441 TYR A CB  
1078 C CG  . TYR A 145 ? 0.6261 0.7690 0.6292 -0.0265 -0.0359 -0.0115 441 TYR A CG  
1079 C CD1 . TYR A 145 ? 0.5709 0.7464 0.5818 -0.0223 -0.0282 -0.0172 441 TYR A CD1 
1080 C CD2 . TYR A 145 ? 0.7311 0.8499 0.7301 -0.0111 -0.0461 -0.0154 441 TYR A CD2 
1081 C CE1 . TYR A 145 ? 0.6908 0.8638 0.7009 -0.0068 -0.0312 -0.0264 441 TYR A CE1 
1082 C CE2 . TYR A 145 ? 0.7619 0.8897 0.7651 0.0016  -0.0493 -0.0241 441 TYR A CE2 
1083 C CZ  . TYR A 145 ? 0.7449 0.8942 0.7512 0.0020  -0.0421 -0.0297 441 TYR A CZ  
1084 O OH  . TYR A 145 ? 0.8248 0.9758 0.8277 0.0116  -0.0460 -0.0390 441 TYR A OH  
1085 N N   . ILE A 146 ? 0.8479 0.9311 0.7854 -0.1011 -0.0359 0.0204  442 ILE A N   
1086 C CA  . ILE A 146 ? 0.8363 0.8877 0.7588 -0.1143 -0.0404 0.0254  442 ILE A CA  
1087 C C   . ILE A 146 ? 0.9192 0.8900 0.7697 -0.1266 -0.0478 0.0346  442 ILE A C   
1088 O O   . ILE A 146 ? 0.9189 0.8373 0.7456 -0.1157 -0.0558 0.0351  442 ILE A O   
1089 C CB  . ILE A 146 ? 0.7363 0.8402 0.6786 -0.1428 -0.0331 0.0290  442 ILE A CB  
1090 C CG1 . ILE A 146 ? 0.6341 0.7982 0.6383 -0.1192 -0.0291 0.0192  442 ILE A CG1 
1091 C CG2 . ILE A 146 ? 0.7606 0.8224 0.6687 -0.1691 -0.0384 0.0366  442 ILE A CG2 
1092 C CD1 . ILE A 146 ? 0.6719 0.9044 0.7013 -0.1366 -0.0220 0.0212  442 ILE A CD1 
1093 N N   . CYS A 147 ? 0.8999 0.8544 0.7086 -0.1458 -0.0454 0.0416  443 CYS A N   
1094 C CA  . CYS A 147 ? 0.8721 0.7350 0.5972 -0.1569 -0.0532 0.0511  443 CYS A CA  
1095 C C   . CYS A 147 ? 0.9340 0.7466 0.6406 -0.1122 -0.0638 0.0464  443 CYS A C   
1096 O O   . CYS A 147 ? 1.1029 0.8399 0.7543 -0.1035 -0.0728 0.0501  443 CYS A O   
1097 C CB  . CYS A 147 ? 0.9558 0.8117 0.6380 -0.1853 -0.0483 0.0595  443 CYS A CB  
1098 S SG  . CYS A 147 ? 1.1277 1.0033 0.7805 -0.2520 -0.0401 0.0715  443 CYS A SG  
1099 N N   . ASN A 148 ? 0.7947 0.6497 0.5425 -0.0824 -0.0635 0.0380  444 ASN A N   
1100 C CA  . ASN A 148 ? 0.9494 0.7764 0.6855 -0.0405 -0.0739 0.0331  444 ASN A CA  
1101 C C   . ASN A 148 ? 0.8732 0.7063 0.6381 -0.0190 -0.0781 0.0270  444 ASN A C   
1102 O O   . ASN A 148 ? 0.9460 0.7402 0.6798 0.0121  -0.0876 0.0261  444 ASN A O   
1103 C CB  . ASN A 148 ? 1.0079 0.8866 0.7822 -0.0213 -0.0729 0.0252  444 ASN A CB  
1104 C CG  . ASN A 148 ? 1.0409 0.9038 0.7757 -0.0354 -0.0705 0.0314  444 ASN A CG  
1105 O OD1 . ASN A 148 ? 1.0548 0.8554 0.7221 -0.0548 -0.0721 0.0425  444 ASN A OD1 
1106 N ND2 . ASN A 148 ? 0.9719 0.8850 0.7413 -0.0276 -0.0670 0.0244  444 ASN A ND2 
1107 N N   . HIS A 149 ? 0.8045 0.6878 0.6255 -0.0320 -0.0713 0.0227  445 HIS A N   
1108 C CA  . HIS A 149 ? 0.8554 0.7402 0.6981 -0.0172 -0.0744 0.0183  445 HIS A CA  
1109 C C   . HIS A 149 ? 0.9086 0.7177 0.6874 -0.0244 -0.0798 0.0258  445 HIS A C   
1110 O O   . HIS A 149 ? 0.9133 0.6894 0.6702 0.0051  -0.0871 0.0235  445 HIS A O   
1111 C CB  . HIS A 149 ? 0.7621 0.7092 0.6692 -0.0312 -0.0663 0.0133  445 HIS A CB  
1112 C CG  . HIS A 149 ? 0.7955 0.7442 0.7232 -0.0232 -0.0681 0.0101  445 HIS A CG  
1113 N ND1 . HIS A 149 ? 0.7035 0.7025 0.6877 -0.0141 -0.0652 0.0021  445 HIS A ND1 
1114 C CD2 . HIS A 149 ? 0.8380 0.7400 0.7320 -0.0250 -0.0724 0.0140  445 HIS A CD2 
1115 C CE1 . HIS A 149 ? 0.7228 0.7117 0.7115 -0.0105 -0.0671 0.0015  445 HIS A CE1 
1116 N NE2 . HIS A 149 ? 0.7907 0.7227 0.7265 -0.0157 -0.0714 0.0082  445 HIS A NE2 
1117 N N   . VAL A 150 ? 0.9434 0.7254 0.6876 -0.0642 -0.0764 0.0346  446 VAL A N   
1118 C CA  . VAL A 150 ? 0.9922 0.6900 0.6629 -0.0790 -0.0823 0.0420  446 VAL A CA  
1119 C C   . VAL A 150 ? 1.1269 0.7387 0.7189 -0.0486 -0.0926 0.0447  446 VAL A C   
1120 O O   . VAL A 150 ? 1.2557 0.8072 0.8032 -0.0253 -0.1001 0.0440  446 VAL A O   
1121 C CB  . VAL A 150 ? 0.9964 0.6850 0.6364 -0.1353 -0.0772 0.0518  446 VAL A CB  
1122 C CG1 . VAL A 150 ? 1.0291 0.6127 0.5735 -0.1592 -0.0848 0.0604  446 VAL A CG1 
1123 C CG2 . VAL A 150 ? 0.8625 0.6427 0.5785 -0.1569 -0.0682 0.0486  446 VAL A CG2 
1124 N N   . LYS A 151 ? 1.0866 0.6903 0.6558 -0.0446 -0.0933 0.0477  447 LYS A N   
1125 C CA  . LYS A 151 ? 1.1936 0.7114 0.6791 -0.0128 -0.1042 0.0513  447 LYS A CA  
1126 C C   . LYS A 151 ? 1.2424 0.7821 0.7524 0.0466  -0.1111 0.0417  447 LYS A C   
1127 O O   . LYS A 151 ? 1.3078 0.7755 0.7516 0.0796  -0.1204 0.0424  447 LYS A O   
1128 C CB  . LYS A 151 ? 1.2153 0.7295 0.6772 -0.0201 -0.1034 0.0562  447 LYS A CB  
1129 C CG  . LYS A 151 ? 1.3890 0.7965 0.7445 0.0071  -0.1154 0.0627  447 LYS A CG  
1130 C CD  . LYS A 151 ? 1.3407 0.7356 0.6636 -0.0100 -0.1139 0.0696  447 LYS A CD  
1131 C CE  . LYS A 151 ? 1.5306 0.7912 0.7209 -0.0073 -0.1242 0.0810  447 LYS A CE  
1132 N NZ  . LYS A 151 ? 1.4861 0.7461 0.6528 -0.0212 -0.1222 0.0872  447 LYS A NZ  
1133 N N   . TYR A 152 ? 1.1072 0.7469 0.7079 0.0601  -0.1066 0.0323  448 TYR A N   
1134 C CA  . TYR A 152 ? 1.0811 0.7586 0.7090 0.1096  -0.1127 0.0234  448 TYR A CA  
1135 C C   . TYR A 152 ? 1.0850 0.7490 0.7125 0.1232  -0.1139 0.0203  448 TYR A C   
1136 O O   . TYR A 152 ? 1.2085 0.8433 0.7965 0.1674  -0.1221 0.0181  448 TYR A O   
1137 C CB  . TYR A 152 ? 1.0050 0.7870 0.7232 0.1100  -0.1077 0.0145  448 TYR A CB  
1138 C CG  . TYR A 152 ? 1.0423 0.8787 0.7966 0.1488  -0.1124 0.0053  448 TYR A CG  
1139 C CD1 . TYR A 152 ? 1.1483 1.0002 0.8845 0.1890  -0.1217 0.0025  448 TYR A CD1 
1140 C CD2 . TYR A 152 ? 1.0008 0.8796 0.8061 0.1440  -0.1078 -0.0002 448 TYR A CD2 
1141 C CE1 . TYR A 152 ? 1.1272 1.0443 0.8975 0.2219  -0.1258 -0.0056 448 TYR A CE1 
1142 C CE2 . TYR A 152 ? 1.0074 0.9424 0.8434 0.1745  -0.1112 -0.0078 448 TYR A CE2 
1143 C CZ  . TYR A 152 ? 1.0787 1.0377 0.8991 0.2120  -0.1199 -0.0106 448 TYR A CZ  
1144 O OH  . TYR A 152 ? 1.1617 1.1924 1.0155 0.2389  -0.1228 -0.0182 448 TYR A OH  
1145 N N   . ALA A 153 ? 1.0483 0.7360 0.7175 0.0887  -0.1060 0.0199  449 ALA A N   
1146 C CA  . ALA A 153 ? 1.0894 0.7719 0.7645 0.1002  -0.1066 0.0164  449 ALA A CA  
1147 C C   . ALA A 153 ? 1.1876 0.7594 0.7641 0.1067  -0.1137 0.0224  449 ALA A C   
1148 O O   . ALA A 153 ? 1.2308 0.7821 0.7887 0.1357  -0.1172 0.0185  449 ALA A O   
1149 C CB  . ALA A 153 ? 1.0249 0.7568 0.7633 0.0622  -0.0974 0.0151  449 ALA A CB  
1150 N N   . THR A 154 ? 1.1516 0.6477 0.6582 0.0780  -0.1157 0.0319  450 THR A N   
1151 C CA  . THR A 154 ? 1.3297 0.7034 0.7269 0.0792  -0.1235 0.0379  450 THR A CA  
1152 C C   . THR A 154 ? 1.4801 0.7931 0.8052 0.1411  -0.1345 0.0364  450 THR A C   
1153 O O   . THR A 154 ? 1.5372 0.7882 0.8045 0.1750  -0.1408 0.0340  450 THR A O   
1154 C CB  . THR A 154 ? 1.3793 0.6896 0.7174 0.0207  -0.1223 0.0493  450 THR A CB  
1155 O OG1 . THR A 154 ? 1.3325 0.7051 0.7339 -0.0303 -0.1131 0.0500  450 THR A OG1 
1156 C CG2 . THR A 154 ? 1.5330 0.6986 0.7399 0.0190  -0.1321 0.0559  450 THR A CG2 
1157 N N   . ASN A 155 ? 1.4606 0.7927 0.7855 0.1605  -0.1372 0.0374  451 ASN A N   
1158 C CA  . ASN A 155 ? 1.4358 0.7428 0.7119 0.2283  -0.1478 0.0343  451 ASN A CA  
1159 C C   . ASN A 155 ? 1.5776 0.7397 0.7197 0.2548  -0.1583 0.0389  451 ASN A C   
1160 O O   . ASN A 155 ? 1.7754 0.9226 0.8858 0.3162  -0.1652 0.0329  451 ASN A O   
1161 C CB  . ASN A 155 ? 1.4792 0.8994 0.8415 0.2717  -0.1465 0.0224  451 ASN A CB  
1162 C CG  . ASN A 155 ? 1.5243 0.9514 0.8513 0.3432  -0.1571 0.0184  451 ASN A CG  
1163 O OD1 . ASN A 155 ? 1.5643 0.9486 0.8364 0.3584  -0.1643 0.0234  451 ASN A OD1 
1164 N ND2 . ASN A 155 ? 1.4733 0.9597 0.8303 0.3886  -0.1583 0.0095  451 ASN A ND2 
1165 N N   . LYS A 156 ? 1.6238 0.6774 0.6813 0.2068  -0.1595 0.0496  452 LYS A N   
1166 C CA  . LYS A 156 ? 1.8746 0.7651 0.7821 0.2236  -0.1708 0.0555  452 LYS A CA  
1167 C C   . LYS A 156 ? 1.9659 0.8159 0.8474 0.2380  -0.1724 0.0500  452 LYS A C   
1168 O O   . LYS A 156 ? 2.1856 0.9408 0.9694 0.2796  -0.1796 0.0440  452 LYS A O   
1169 C CB  . LYS A 156 ? 2.0312 0.8697 0.8622 0.2977  -0.1831 0.0551  452 LYS A CB  
1170 C CG  . LYS A 156 ? 2.1533 0.9927 0.9719 0.2876  -0.1849 0.0623  452 LYS A CG  
1171 C CD  . LYS A 156 ? 2.3011 1.1031 1.0562 0.3540  -0.1914 0.0507  452 LYS A CD  
1172 C CE  . LYS A 156 ? 2.1831 1.1151 1.0235 0.4143  -0.1943 0.0447  452 LYS A CE  
1173 N NZ  . LYS A 156 ? 2.2449 1.2228 1.1194 0.3927  -0.1962 0.0558  452 LYS A NZ  
1174 N N   . GLY A 157 ? 1.7745 0.7151 0.7556 0.2021  -0.1622 0.0455  453 GLY A N   
1175 C CA  . GLY A 157 ? 1.8523 0.7750 0.8260 0.2153  -0.1623 0.0394  453 GLY A CA  
1176 C C   . GLY A 157 ? 1.7146 0.7364 0.7613 0.2807  -0.1607 0.0273  453 GLY A C   
1177 O O   . GLY A 157 ? 1.6055 0.6411 0.6709 0.2878  -0.1581 0.0214  453 GLY A O   
1178 N N   . ASN A 158 ? 1.6315 0.7259 0.7175 0.3269  -0.1625 0.0236  454 ASN A N   
1179 C CA  . ASN A 158 ? 1.5868 0.8025 0.7568 0.3775  -0.1596 0.0125  454 ASN A CA  
1180 C C   . ASN A 158 ? 1.4730 0.8277 0.7827 0.3320  -0.1478 0.0096  454 ASN A C   
1181 O O   . ASN A 158 ? 1.5210 0.9692 0.8980 0.3396  -0.1461 0.0069  454 ASN A O   
1182 C CB  . ASN A 158 ? 1.7024 0.9346 0.8420 0.4487  -0.1686 0.0095  454 ASN A CB  
1183 C CG  . ASN A 158 ? 1.7288 1.0910 0.9452 0.5006  -0.1664 -0.0018 454 ASN A CG  
1184 O OD1 . ASN A 158 ? 1.8043 1.2557 1.1112 0.4757  -0.1568 -0.0069 454 ASN A OD1 
1185 N ND2 . ASN A 158 ? 1.7370 1.1221 0.9216 0.5644  -0.1720 -0.0083 454 ASN A ND2 
1186 N N   . LEU A 159 ? 1.3679 0.7289 0.7131 0.2850  -0.1404 0.0100  455 LEU A N   
1187 C CA  . LEU A 159 ? 1.2792 0.7389 0.7329 0.2338  -0.1299 0.0096  455 LEU A CA  
1188 C C   . LEU A 159 ? 1.2270 0.8173 0.7786 0.2587  -0.1256 0.0008  455 LEU A C   
1189 O O   . LEU A 159 ? 1.2277 0.8520 0.7837 0.3050  -0.1275 -0.0061 455 LEU A O   
1190 C CB  . LEU A 159 ? 1.2977 0.7422 0.7648 0.1907  -0.1245 0.0107  455 LEU A CB  
1191 C CG  . LEU A 159 ? 1.3551 0.7262 0.7755 0.1299  -0.1242 0.0203  455 LEU A CG  
1192 C CD1 . LEU A 159 ? 1.5248 0.7792 0.8314 0.1332  -0.1330 0.0279  455 LEU A CD1 
1193 C CD2 . LEU A 159 ? 1.3743 0.7066 0.7743 0.1064  -0.1237 0.0202  455 LEU A CD2 
1194 N N   . ARG A 160 ? 1.0428 0.7063 0.6685 0.2254  -0.1196 0.0009  456 ARG A N   
1195 C CA  . ARG A 160 ? 0.9253 0.7055 0.6394 0.2337  -0.1157 -0.0066 456 ARG A CA  
1196 C C   . ARG A 160 ? 0.8621 0.6942 0.6510 0.1842  -0.1060 -0.0071 456 ARG A C   
1197 O O   . ARG A 160 ? 1.0446 0.8472 0.8286 0.1459  -0.1029 -0.0014 456 ARG A O   
1198 C CB  . ARG A 160 ? 0.8884 0.7001 0.6057 0.2494  -0.1203 -0.0068 456 ARG A CB  
1199 C CG  . ARG A 160 ? 1.0678 0.8289 0.7063 0.3031  -0.1313 -0.0056 456 ARG A CG  
1200 C CD  . ARG A 160 ? 1.1221 0.9228 0.7694 0.3159  -0.1363 -0.0059 456 ARG A CD  
1201 N NE  . ARG A 160 ? 1.1855 0.9184 0.7935 0.2843  -0.1364 0.0025  456 ARG A NE  
1202 C CZ  . ARG A 160 ? 1.2850 1.0051 0.8602 0.3006  -0.1431 0.0053  456 ARG A CZ  
1203 N NH1 . ARG A 160 ? 1.3037 1.0774 0.8821 0.3499  -0.1512 0.0000  456 ARG A NH1 
1204 N NH2 . ARG A 160 ? 1.2303 0.8891 0.7679 0.2674  -0.1417 0.0136  456 ARG A NH2 
1205 N N   . SER A 161 ? 0.8445 0.7566 0.6991 0.1859  -0.1015 -0.0139 457 SER A N   
1206 C CA  . SER A 161 ? 0.7817 0.7346 0.6980 0.1456  -0.0933 -0.0148 457 SER A CA  
1207 C C   . SER A 161 ? 0.7216 0.7178 0.6760 0.1274  -0.0912 -0.0161 457 SER A C   
1208 O O   . SER A 161 ? 0.8110 0.8429 0.7711 0.1465  -0.0952 -0.0195 457 SER A O   
1209 C CB  . SER A 161 ? 0.7258 0.7370 0.6875 0.1508  -0.0895 -0.0209 457 SER A CB  
1210 O OG  . SER A 161 ? 0.7789 0.7591 0.7016 0.1796  -0.0922 -0.0215 457 SER A OG  
1211 N N   . ALA A 162 ? 0.6748 0.6711 0.6534 0.0922  -0.0852 -0.0138 458 ALA A N   
1212 C CA  . ALA A 162 ? 0.6976 0.7233 0.7014 0.0769  -0.0827 -0.0151 458 ALA A CA  
1213 C C   . ALA A 162 ? 0.6885 0.7314 0.7281 0.0474  -0.0752 -0.0152 458 ALA A C   
1214 O O   . ALA A 162 ? 0.7413 0.7650 0.7776 0.0341  -0.0726 -0.0116 458 ALA A O   
1215 C CB  . ALA A 162 ? 0.7900 0.7724 0.7477 0.0766  -0.0858 -0.0092 458 ALA A CB  
1216 N N   . ILE A 163 ? 0.6303 0.7084 0.6990 0.0393  -0.0724 -0.0195 459 ILE A N   
1217 C CA  . ILE A 163 ? 0.6347 0.7273 0.7289 0.0197  -0.0658 -0.0203 459 ILE A CA  
1218 C C   . ILE A 163 ? 0.6293 0.7337 0.7240 0.0156  -0.0640 -0.0223 459 ILE A C   
1219 O O   . ILE A 163 ? 0.7172 0.8326 0.8087 0.0253  -0.0681 -0.0261 459 ILE A O   
1220 C CB  . ILE A 163 ? 0.6162 0.7351 0.7432 0.0178  -0.0640 -0.0261 459 ILE A CB  
1221 C CG1 . ILE A 163 ? 0.5077 0.6330 0.6508 0.0053  -0.0582 -0.0266 459 ILE A CG1 
1222 C CG2 . ILE A 163 ? 0.5622 0.7100 0.7006 0.0233  -0.0672 -0.0332 459 ILE A CG2 
1223 C CD1 . ILE A 163 ? 0.4798 0.6150 0.6427 0.0029  -0.0569 -0.0309 459 ILE A CD1 
1224 N N   . THR A 164 ? 0.5689 0.6754 0.6650 0.0021  -0.0581 -0.0195 460 THR A N   
1225 C CA  . THR A 164 ? 0.5539 0.6740 0.6490 -0.0003 -0.0547 -0.0218 460 THR A CA  
1226 C C   . THR A 164 ? 0.6474 0.7902 0.7662 -0.0017 -0.0489 -0.0270 460 THR A C   
1227 O O   . THR A 164 ? 0.6692 0.8204 0.7975 -0.0072 -0.0452 -0.0240 460 THR A O   
1228 C CB  . THR A 164 ? 0.5612 0.6684 0.6288 -0.0123 -0.0520 -0.0137 460 THR A CB  
1229 O OG1 . THR A 164 ? 0.6135 0.6833 0.6458 -0.0074 -0.0587 -0.0086 460 THR A OG1 
1230 C CG2 . THR A 164 ? 0.6231 0.7483 0.6878 -0.0128 -0.0477 -0.0163 460 THR A CG2 
1231 N N   . ILE A 165 ? 0.5580 0.7075 0.6808 0.0046  -0.0491 -0.0350 461 ILE A N   
1232 C CA  . ILE A 165 ? 0.5095 0.6635 0.6418 0.0086  -0.0458 -0.0413 461 ILE A CA  
1233 C C   . ILE A 165 ? 0.6195 0.7824 0.7411 0.0148  -0.0404 -0.0448 461 ILE A C   
1234 O O   . ILE A 165 ? 0.6344 0.7915 0.7428 0.0164  -0.0424 -0.0494 461 ILE A O   
1235 C CB  . ILE A 165 ? 0.5497 0.6931 0.6833 0.0077  -0.0509 -0.0485 461 ILE A CB  
1236 C CG1 . ILE A 165 ? 0.5194 0.6635 0.6655 0.0038  -0.0542 -0.0450 461 ILE A CG1 
1237 C CG2 . ILE A 165 ? 0.5295 0.6590 0.6558 0.0120  -0.0484 -0.0549 461 ILE A CG2 
1238 C CD1 . ILE A 165 ? 0.5209 0.6691 0.6691 -0.0024 -0.0594 -0.0505 461 ILE A CD1 
1239 N N   . PHE A 166 ? 0.6618 0.8439 0.7882 0.0200  -0.0339 -0.0430 462 PHE A N   
1240 C CA  . PHE A 166 ? 0.6217 0.8235 0.7384 0.0307  -0.0271 -0.0462 462 PHE A CA  
1241 C C   . PHE A 166 ? 0.6646 0.8474 0.7684 0.0500  -0.0268 -0.0564 462 PHE A C   
1242 O O   . PHE A 166 ? 0.7178 0.8720 0.8201 0.0497  -0.0316 -0.0595 462 PHE A O   
1243 C CB  . PHE A 166 ? 0.5668 0.8117 0.6938 0.0266  -0.0204 -0.0386 462 PHE A CB  
1244 C CG  . PHE A 166 ? 0.6517 0.9026 0.7731 0.0034  -0.0203 -0.0288 462 PHE A CG  
1245 C CD1 . PHE A 166 ? 0.6649 0.9157 0.7680 -0.0015 -0.0183 -0.0278 462 PHE A CD1 
1246 C CD2 . PHE A 166 ? 0.6069 0.8537 0.7325 -0.0140 -0.0232 -0.0206 462 PHE A CD2 
1247 C CE1 . PHE A 166 ? 0.7173 0.9603 0.8029 -0.0236 -0.0190 -0.0180 462 PHE A CE1 
1248 C CE2 . PHE A 166 ? 0.5941 0.8292 0.6990 -0.0366 -0.0242 -0.0115 462 PHE A CE2 
1249 C CZ  . PHE A 166 ? 0.6498 0.8803 0.7327 -0.0414 -0.0222 -0.0099 462 PHE A CZ  
1250 N N   . PRO A 167 ? 0.6477 0.8391 0.7338 0.0669  -0.0213 -0.0620 463 PRO A N   
1251 C CA  . PRO A 167 ? 0.7150 0.8693 0.7722 0.0877  -0.0224 -0.0728 463 PRO A CA  
1252 C C   . PRO A 167 ? 0.7735 0.9141 0.8304 0.1002  -0.0236 -0.0732 463 PRO A C   
1253 O O   . PRO A 167 ? 0.8162 0.9956 0.8966 0.1034  -0.0205 -0.0665 463 PRO A O   
1254 C CB  . PRO A 167 ? 0.6594 0.8389 0.6996 0.1102  -0.0142 -0.0771 463 PRO A CB  
1255 C CG  . PRO A 167 ? 0.6257 0.8348 0.6782 0.0909  -0.0120 -0.0709 463 PRO A CG  
1256 C CD  . PRO A 167 ? 0.5985 0.8230 0.6802 0.0665  -0.0149 -0.0598 463 PRO A CD  
1257 N N   . GLN A 168 ? 0.7946 0.8763 0.8194 0.1042  -0.0289 -0.0809 464 GLN A N   
1258 C CA  . GLN A 168 ? 0.7487 0.8039 0.7634 0.1148  -0.0312 -0.0810 464 GLN A CA  
1259 C C   . GLN A 168 ? 0.7980 0.8633 0.7918 0.1554  -0.0260 -0.0846 464 GLN A C   
1260 O O   . GLN A 168 ? 0.7312 0.8085 0.7068 0.1763  -0.0210 -0.0899 464 GLN A O   
1261 C CB  . GLN A 168 ? 0.6472 0.6296 0.6233 0.1012  -0.0388 -0.0875 464 GLN A CB  
1262 C CG  . GLN A 168 ? 0.7589 0.6848 0.6755 0.1165  -0.0399 -0.0989 464 GLN A CG  
1263 C CD  . GLN A 168 ? 0.8852 0.7533 0.7683 0.0845  -0.0482 -0.1044 464 GLN A CD  
1264 O OE1 . GLN A 168 ? 0.9767 0.8722 0.8908 0.0531  -0.0517 -0.1009 464 GLN A OE1 
1265 N NE2 . GLN A 168 ? 1.0300 0.8176 0.8441 0.0924  -0.0520 -0.1131 464 GLN A NE2 
1266 N N   . ARG A 169 ? 0.7729 0.8383 0.7684 0.1696  -0.0271 -0.0816 465 ARG A N   
1267 C CA  . ARG A 169 ? 0.8114 0.8853 0.7810 0.2154  -0.0238 -0.0856 465 ARG A CA  
1268 C C   . ARG A 169 ? 0.9432 0.9346 0.8422 0.2396  -0.0263 -0.0974 465 ARG A C   
1269 O O   . ARG A 169 ? 0.9884 0.9035 0.8543 0.2164  -0.0330 -0.1012 465 ARG A O   
1270 C CB  . ARG A 169 ? 0.9365 1.0131 0.9134 0.2254  -0.0270 -0.0804 465 ARG A CB  
1271 C CG  . ARG A 169 ? 1.0051 1.0899 0.9507 0.2791  -0.0255 -0.0843 465 ARG A CG  
1272 C CD  . ARG A 169 ? 1.0389 1.1271 0.9931 0.2854  -0.0301 -0.0783 465 ARG A CD  
1273 N NE  . ARG A 169 ? 0.9869 1.1796 1.0011 0.2781  -0.0266 -0.0693 465 ARG A NE  
1274 C CZ  . ARG A 169 ? 0.9256 1.1391 0.9808 0.2404  -0.0291 -0.0606 465 ARG A CZ  
1275 N NH1 . ARG A 169 ? 0.8996 1.0465 0.9483 0.2104  -0.0341 -0.0597 465 ARG A NH1 
1276 N NH2 . ARG A 169 ? 0.7538 1.0567 0.8532 0.2312  -0.0265 -0.0531 465 ARG A NH2 
1277 N N   . THR A 170 ? 1.0193 1.0279 0.8909 0.2846  -0.0208 -0.1037 466 THR A N   
1278 C CA  . THR A 170 ? 1.1192 1.0393 0.9101 0.3161  -0.0234 -0.1159 466 THR A CA  
1279 C C   . THR A 170 ? 1.2367 1.1494 0.9906 0.3736  -0.0233 -0.1185 466 THR A C   
1280 O O   . THR A 170 ? 1.2714 1.1278 0.9995 0.3757  -0.0302 -0.1166 466 THR A O   
1281 C CB  . THR A 170 ? 1.1873 1.1209 0.9640 0.3247  -0.0177 -0.1232 466 THR A CB  
1282 O OG1 . THR A 170 ? 1.0629 1.1099 0.8895 0.3414  -0.0075 -0.1185 466 THR A OG1 
1283 C CG2 . THR A 170 ? 1.1186 1.0309 0.9101 0.2718  -0.0214 -0.1225 466 THR A CG2 
1284 N N   . ASP A 171 ? 1.2322 1.2055 0.9814 0.4225  -0.0156 -0.1226 467 ASP A N   
1285 C CA  . ASP A 171 ? 1.4262 1.3952 1.1326 0.4872  -0.0162 -0.1264 467 ASP A CA  
1286 C C   . ASP A 171 ? 1.3938 1.4431 1.1565 0.4875  -0.0169 -0.1155 467 ASP A C   
1287 O O   . ASP A 171 ? 1.5182 1.5379 1.2426 0.5292  -0.0218 -0.1166 467 ASP A O   
1288 C CB  . ASP A 171 ? 1.5804 1.6090 1.2693 0.5423  -0.0069 -0.1343 467 ASP A CB  
1289 C CG  . ASP A 171 ? 1.6007 1.7860 1.3771 0.5281  0.0037  -0.1259 467 ASP A CG  
1290 O OD1 . ASP A 171 ? 1.5680 1.7873 1.4054 0.4665  0.0043  -0.1168 467 ASP A OD1 
1291 O OD2 . ASP A 171 ? 1.6489 1.9233 1.4285 0.5784  0.0111  -0.1282 467 ASP A OD2 
1292 N N   . GLY A 172 ? 1.2758 1.4205 1.1217 0.4422  -0.0127 -0.1052 468 GLY A N   
1293 C CA  . GLY A 172 ? 1.1934 1.4268 1.0933 0.4394  -0.0128 -0.0952 468 GLY A CA  
1294 C C   . GLY A 172 ? 1.2057 1.5821 1.1633 0.4393  -0.0032 -0.0903 468 GLY A C   
1295 O O   . GLY A 172 ? 1.1529 1.5993 1.1698 0.3980  -0.0025 -0.0798 468 GLY A O   
1296 N N   . LYS A 173 ? 1.2567 1.6771 1.1926 0.4835  0.0045  -0.0977 469 LYS A N   
1297 C CA  . LYS A 173 ? 1.2104 1.7749 1.1964 0.4813  0.0149  -0.0931 469 LYS A CA  
1298 C C   . LYS A 173 ? 1.1982 1.7787 1.2109 0.4307  0.0215  -0.0903 469 LYS A C   
1299 O O   . LYS A 173 ? 1.1858 1.8790 1.2351 0.4187  0.0307  -0.0855 469 LYS A O   
1300 C CB  . LYS A 173 ? 1.2778 1.8957 1.2275 0.5545  0.0207  -0.1017 469 LYS A CB  
1301 C CG  . LYS A 173 ? 1.3392 1.9565 1.2619 0.5885  0.0114  -0.0983 469 LYS A CG  
1302 C CD  . LYS A 173 ? 1.4265 2.0674 1.2944 0.6433  0.0113  -0.1023 469 LYS A CD  
1303 C CE  . LYS A 173 ? 1.4392 2.2344 1.3520 0.6300  0.0193  -0.0956 469 LYS A CE  
1304 N NZ  . LYS A 173 ? 1.5366 2.3616 1.3947 0.6882  0.0183  -0.0999 469 LYS A NZ  
1305 N N   . HIS A 174 ? 1.1728 1.6471 1.1654 0.3996  0.0167  -0.0927 470 HIS A N   
1306 C CA  . HIS A 174 ? 1.2019 1.6803 1.2170 0.3508  0.0205  -0.0891 470 HIS A CA  
1307 C C   . HIS A 174 ? 1.2470 1.6779 1.2888 0.2967  0.0123  -0.0808 470 HIS A C   
1308 O O   . HIS A 174 ? 1.3557 1.6922 1.3734 0.2818  0.0056  -0.0847 470 HIS A O   
1309 C CB  . HIS A 174 ? 1.1761 1.5820 1.1416 0.3664  0.0217  -0.1002 470 HIS A CB  
1310 C CG  . HIS A 174 ? 1.2490 1.6957 1.1809 0.4247  0.0302  -0.1096 470 HIS A CG  
1311 N ND1 . HIS A 174 ? 1.3493 1.7175 1.2116 0.4803  0.0268  -0.1221 470 HIS A ND1 
1312 C CD2 . HIS A 174 ? 1.2461 1.8054 1.1997 0.4377  0.0421  -0.1083 470 HIS A CD2 
1313 C CE1 . HIS A 174 ? 1.4058 1.8356 1.2482 0.5309  0.0363  -0.1291 470 HIS A CE1 
1314 N NE2 . HIS A 174 ? 1.3269 1.8804 1.2279 0.5052  0.0463  -0.1207 470 HIS A NE2 
1315 N N   . ASP A 175 ? 1.1046 1.6043 1.1930 0.2673  0.0126  -0.0698 471 ASP A N   
1316 C CA  . ASP A 175 ? 0.9088 1.3709 1.0203 0.2219  0.0053  -0.0619 471 ASP A CA  
1317 C C   . ASP A 175 ? 0.7816 1.2806 0.9209 0.1741  0.0087  -0.0530 471 ASP A C   
1318 O O   . ASP A 175 ? 0.8272 1.4125 0.9840 0.1660  0.0160  -0.0479 471 ASP A O   
1319 C CB  . ASP A 175 ? 0.9806 1.4723 1.1117 0.2250  0.0009  -0.0562 471 ASP A CB  
1320 C CG  . ASP A 175 ? 1.0133 1.4274 1.1112 0.2554  -0.0063 -0.0624 471 ASP A CG  
1321 O OD1 . ASP A 175 ? 1.1330 1.4706 1.1877 0.2745  -0.0078 -0.0714 471 ASP A OD1 
1322 O OD2 . ASP A 175 ? 1.0615 1.4869 1.1710 0.2577  -0.0111 -0.0579 471 ASP A OD2 
1323 N N   . PHE A 176 ? 0.7060 1.1403 0.8446 0.1425  0.0030  -0.0509 472 PHE A N   
1324 C CA  . PHE A 176 ? 0.6630 1.1132 0.8185 0.0986  0.0034  -0.0414 472 PHE A CA  
1325 C C   . PHE A 176 ? 0.6025 1.0603 0.7787 0.0750  -0.0017 -0.0330 472 PHE A C   
1326 O O   . PHE A 176 ? 0.6382 1.0457 0.8137 0.0787  -0.0086 -0.0347 472 PHE A O   
1327 C CB  . PHE A 176 ? 0.6038 0.9860 0.7444 0.0831  -0.0009 -0.0436 472 PHE A CB  
1328 C CG  . PHE A 176 ? 0.5952 0.9807 0.7165 0.0933  0.0045  -0.0490 472 PHE A CG  
1329 C CD1 . PHE A 176 ? 0.6654 1.0310 0.7621 0.1295  0.0063  -0.0603 472 PHE A CD1 
1330 C CD2 . PHE A 176 ? 0.5549 0.9560 0.6749 0.0672  0.0075  -0.0428 472 PHE A CD2 
1331 C CE1 . PHE A 176 ? 0.7418 1.1070 0.8162 0.1399  0.0112  -0.0662 472 PHE A CE1 
1332 C CE2 . PHE A 176 ? 0.6415 1.0462 0.7419 0.0768  0.0127  -0.0477 472 PHE A CE2 
1333 C CZ  . PHE A 176 ? 0.6890 1.0787 0.7688 0.1134  0.0148  -0.0598 472 PHE A CZ  
1334 N N   . ARG A 177 ? 0.5263 1.0458 0.7165 0.0479  0.0015  -0.0238 473 ARG A N   
1335 C CA  . ARG A 177 ? 0.6078 1.1336 0.8114 0.0235  -0.0038 -0.0162 473 ARG A CA  
1336 C C   . ARG A 177 ? 0.6125 1.1516 0.8104 -0.0240 -0.0031 -0.0058 473 ARG A C   
1337 O O   . ARG A 177 ? 0.6258 1.2213 0.8206 -0.0380 0.0039  -0.0022 473 ARG A O   
1338 C CB  . ARG A 177 ? 0.6893 1.2871 0.9098 0.0432  -0.0027 -0.0162 473 ARG A CB  
1339 C CG  . ARG A 177 ? 0.6934 1.2590 0.9082 0.0885  -0.0061 -0.0247 473 ARG A CG  
1340 C CD  . ARG A 177 ? 0.7578 1.2473 0.9705 0.0778  -0.0147 -0.0239 473 ARG A CD  
1341 N NE  . ARG A 177 ? 0.7713 1.2787 0.9983 0.0431  -0.0187 -0.0149 473 ARG A NE  
1342 C CZ  . ARG A 177 ? 0.7697 1.3182 1.0091 0.0471  -0.0219 -0.0120 473 ARG A CZ  
1343 N NH1 . ARG A 177 ? 0.6725 1.2510 0.9117 0.0890  -0.0215 -0.0169 473 ARG A NH1 
1344 N NH2 . ARG A 177 ? 0.7716 1.3272 1.0174 0.0111  -0.0261 -0.0043 473 ARG A NH2 
1345 N N   . VAL A 178 ? 0.5191 1.0028 0.7089 -0.0488 -0.0104 -0.0008 474 VAL A N   
1346 C CA  . VAL A 178 ? 0.5840 1.0708 0.7574 -0.0948 -0.0119 0.0097  474 VAL A CA  
1347 C C   . VAL A 178 ? 0.5866 1.1273 0.7755 -0.1074 -0.0140 0.0138  474 VAL A C   
1348 O O   . VAL A 178 ? 0.5987 1.1148 0.7981 -0.0933 -0.0198 0.0113  474 VAL A O   
1349 C CB  . VAL A 178 ? 0.4964 0.8913 0.6431 -0.1095 -0.0194 0.0123  474 VAL A CB  
1350 C CG1 . VAL A 178 ? 0.5569 0.9367 0.6697 -0.1564 -0.0217 0.0231  474 VAL A CG1 
1351 C CG2 . VAL A 178 ? 0.5594 0.9098 0.6937 -0.0926 -0.0187 0.0075  474 VAL A CG2 
1352 N N   . TRP A 179 ? 0.6077 1.2282 0.7978 -0.1355 -0.0094 0.0202  475 TRP A N   
1353 C CA  . TRP A 179 ? 0.5852 1.2749 0.7919 -0.1491 -0.0119 0.0240  475 TRP A CA  
1354 C C   . TRP A 179 ? 0.6238 1.2607 0.8062 -0.1919 -0.0206 0.0312  475 TRP A C   
1355 O O   . TRP A 179 ? 0.5516 1.2198 0.7469 -0.1966 -0.0257 0.0325  475 TRP A O   
1356 C CB  . TRP A 179 ? 0.5592 1.3677 0.7760 -0.1678 -0.0039 0.0283  475 TRP A CB  
1357 C CG  . TRP A 179 ? 0.5916 1.4725 0.8355 -0.1136 0.0036  0.0198  475 TRP A CG  
1358 C CD1 . TRP A 179 ? 0.6248 1.4563 0.8680 -0.0655 0.0061  0.0101  475 TRP A CD1 
1359 C CD2 . TRP A 179 ? 0.5412 1.5541 0.8100 -0.0995 0.0089  0.0195  475 TRP A CD2 
1360 N NE1 . TRP A 179 ? 0.6036 1.5151 0.8628 -0.0205 0.0125  0.0035  475 TRP A NE1 
1361 C CE2 . TRP A 179 ? 0.5676 1.5956 0.8450 -0.0366 0.0146  0.0090  475 TRP A CE2 
1362 C CE3 . TRP A 179 ? 0.5930 1.7052 0.8693 -0.1327 0.0087  0.0267  475 TRP A CE3 
1363 C CZ2 . TRP A 179 ? 0.6378 1.7827 0.9333 0.0003  0.0204  0.0054  475 TRP A CZ2 
1364 C CZ3 . TRP A 179 ? 0.6236 1.8207 0.9032 -0.0958 0.0134  0.0228  475 TRP A CZ3 
1365 C CH2 . TRP A 179 ? 0.6418 1.8534 0.9301 -0.0291 0.0190  0.0124  475 TRP A CH2 
1366 N N   . ASN A 180 ? 0.6131 1.1675 0.7552 -0.2201 -0.0232 0.0357  476 ASN A N   
1367 C CA  . ASN A 180 ? 0.7474 1.2283 0.8542 -0.2513 -0.0321 0.0408  476 ASN A CA  
1368 C C   . ASN A 180 ? 0.7260 1.1521 0.8472 -0.2155 -0.0380 0.0341  476 ASN A C   
1369 O O   . ASN A 180 ? 0.6272 1.0323 0.7680 -0.1741 -0.0360 0.0265  476 ASN A O   
1370 C CB  . ASN A 180 ? 0.8489 1.2420 0.9002 -0.2769 -0.0340 0.0459  476 ASN A CB  
1371 C CG  . ASN A 180 ? 0.9001 1.3355 0.9290 -0.3156 -0.0278 0.0533  476 ASN A CG  
1372 O OD1 . ASN A 180 ? 0.9449 1.4590 1.0059 -0.2999 -0.0190 0.0507  476 ASN A OD1 
1373 N ND2 . ASN A 180 ? 0.9700 1.3511 0.9374 -0.3676 -0.0323 0.0627  476 ASN A ND2 
1374 N N   . SER A 181 ? 0.6668 1.0686 0.7737 -0.2354 -0.0453 0.0371  477 SER A N   
1375 C CA  . SER A 181 ? 0.6222 0.9714 0.7379 -0.2060 -0.0504 0.0316  477 SER A CA  
1376 C C   . SER A 181 ? 0.6416 0.8895 0.7199 -0.2011 -0.0538 0.0307  477 SER A C   
1377 O O   . SER A 181 ? 0.5979 0.8112 0.6897 -0.1676 -0.0550 0.0245  477 SER A O   
1378 C CB  . SER A 181 ? 0.6143 0.9800 0.7285 -0.2258 -0.0568 0.0345  477 SER A CB  
1379 O OG  . SER A 181 ? 0.7960 1.1572 0.8683 -0.2802 -0.0602 0.0429  477 SER A OG  
1380 N N   . GLN A 182 ? 0.7341 0.9357 0.7611 -0.2339 -0.0558 0.0371  478 GLN A N   
1381 C CA  . GLN A 182 ? 0.7407 0.8519 0.7252 -0.2234 -0.0589 0.0366  478 GLN A CA  
1382 C C   . GLN A 182 ? 0.7310 0.8344 0.6825 -0.2461 -0.0558 0.0422  478 GLN A C   
1383 O O   . GLN A 182 ? 0.8056 0.9487 0.7440 -0.2871 -0.0537 0.0491  478 GLN A O   
1384 C CB  . GLN A 182 ? 0.8510 0.8775 0.7791 -0.2381 -0.0674 0.0393  478 GLN A CB  
1385 C CG  . GLN A 182 ? 0.9861 1.0141 0.9363 -0.2228 -0.0709 0.0350  478 GLN A CG  
1386 C CD  . GLN A 182 ? 1.1865 1.1349 1.0716 -0.2455 -0.0792 0.0383  478 GLN A CD  
1387 O OE1 . GLN A 182 ? 1.2573 1.2182 1.1488 -0.2559 -0.0827 0.0381  478 GLN A OE1 
1388 N NE2 . GLN A 182 ? 1.2223 1.0822 1.0376 -0.2507 -0.0832 0.0412  478 GLN A NE2 
1389 N N   . LEU A 183 ? 0.7478 0.8014 0.6823 -0.2216 -0.0560 0.0398  479 LEU A N   
1390 C CA  . LEU A 183 ? 0.8454 0.8848 0.7453 -0.2387 -0.0533 0.0451  479 LEU A CA  
1391 C C   . LEU A 183 ? 0.9377 0.9221 0.7625 -0.2898 -0.0578 0.0556  479 LEU A C   
1392 O O   . LEU A 183 ? 1.0012 1.0124 0.8065 -0.3263 -0.0535 0.0625  479 LEU A O   
1393 C CB  . LEU A 183 ? 0.8678 0.8531 0.7536 -0.2017 -0.0557 0.0408  479 LEU A CB  
1394 C CG  . LEU A 183 ? 0.8710 0.9016 0.8160 -0.1595 -0.0516 0.0312  479 LEU A CG  
1395 C CD1 . LEU A 183 ? 0.8133 0.7949 0.7325 -0.1339 -0.0552 0.0291  479 LEU A CD1 
1396 C CD2 . LEU A 183 ? 0.8983 1.0127 0.8859 -0.1642 -0.0425 0.0297  479 LEU A CD2 
1397 N N   . ILE A 184 ? 0.9237 0.8280 0.6992 -0.2953 -0.0664 0.0569  480 ILE A N   
1398 C CA  . ILE A 184 ? 0.9170 0.7454 0.6038 -0.3449 -0.0725 0.0664  480 ILE A CA  
1399 C C   . ILE A 184 ? 1.0399 0.8778 0.7251 -0.3719 -0.0770 0.0672  480 ILE A C   
1400 O O   . ILE A 184 ? 1.0552 0.8612 0.7476 -0.3423 -0.0816 0.0612  480 ILE A O   
1401 C CB  . ILE A 184 ? 1.1338 0.8332 0.7374 -0.3246 -0.0806 0.0675  480 ILE A CB  
1402 C CG1 . ILE A 184 ? 1.2381 0.9351 0.8441 -0.2979 -0.0772 0.0670  480 ILE A CG1 
1403 C CG2 . ILE A 184 ? 1.1580 0.7629 0.6545 -0.3786 -0.0876 0.0777  480 ILE A CG2 
1404 C CD1 . ILE A 184 ? 1.2932 0.8742 0.8221 -0.2665 -0.0859 0.0672  480 ILE A CD1 
1405 N N   . ARG A 185 ? 1.1426 1.0344 0.8213 -0.4288 -0.0753 0.0743  481 ARG A N   
1406 C CA  . ARG A 185 ? 1.1265 1.0350 0.7977 -0.4645 -0.0806 0.0763  481 ARG A CA  
1407 C C   . ARG A 185 ? 1.2644 1.1564 0.8633 -0.5422 -0.0834 0.0876  481 ARG A C   
1408 O O   . ARG A 185 ? 1.3993 1.3222 0.9879 -0.5688 -0.0775 0.0937  481 ARG A O   
1409 C CB  . ARG A 185 ? 1.1363 1.1803 0.9048 -0.4506 -0.0751 0.0715  481 ARG A CB  
1410 C CG  . ARG A 185 ? 1.1358 1.1975 0.9709 -0.3828 -0.0725 0.0611  481 ARG A CG  
1411 C CD  . ARG A 185 ? 1.0501 1.1819 0.9382 -0.3751 -0.0740 0.0574  481 ARG A CD  
1412 N NE  . ARG A 185 ? 1.1385 1.1980 0.9807 -0.3902 -0.0834 0.0578  481 ARG A NE  
1413 C CZ  . ARG A 185 ? 1.1293 1.2239 1.0040 -0.3814 -0.0866 0.0545  481 ARG A CZ  
1414 N NH1 . ARG A 185 ? 0.9402 1.1371 0.8901 -0.3558 -0.0817 0.0509  481 ARG A NH1 
1415 N NH2 . ARG A 185 ? 1.2647 1.2866 1.0905 -0.3958 -0.0952 0.0547  481 ARG A NH2 
1416 N N   . TYR A 186 ? 1.2620 1.1043 0.8070 -0.5813 -0.0926 0.0904  482 TYR A N   
1417 C CA  . TYR A 186 ? 1.3926 1.2277 0.8670 -0.6442 -0.0958 0.0985  482 TYR A CA  
1418 C C   . TYR A 186 ? 1.3434 1.3369 0.8871 -0.6626 -0.0901 0.0990  482 TYR A C   
1419 O O   . TYR A 186 ? 1.2415 1.3093 0.8583 -0.6381 -0.0895 0.0937  482 TYR A O   
1420 C CB  . TYR A 186 ? 1.5015 1.2102 0.8801 -0.6553 -0.1080 0.0980  482 TYR A CB  
1421 C CG  . TYR A 186 ? 1.6539 1.1989 0.9438 -0.6308 -0.1143 0.0974  482 TYR A CG  
1422 C CD1 . TYR A 186 ? 1.7417 1.1853 0.9954 -0.5960 -0.1222 0.0915  482 TYR A CD1 
1423 C CD2 . TYR A 186 ? 1.6004 1.0954 0.8412 -0.6365 -0.1124 0.1022  482 TYR A CD2 
1424 C CE1 . TYR A 186 ? 1.8422 1.1424 1.0119 -0.5618 -0.1280 0.0901  482 TYR A CE1 
1425 C CE2 . TYR A 186 ? 1.7032 1.0506 0.8590 -0.6050 -0.1189 0.1014  482 TYR A CE2 
1426 C CZ  . TYR A 186 ? 1.8488 1.1019 0.9698 -0.5645 -0.1266 0.0951  482 TYR A CZ  
1427 O OH  . TYR A 186 ? 1.9009 1.0168 0.9363 -0.5220 -0.1331 0.0932  482 TYR A OH  
1428 N N   . ALA A 187 ? 1.3225 1.3648 0.8367 -0.7036 -0.0868 0.1051  483 ALA A N   
1429 C CA  . ALA A 187 ? 1.2352 1.4297 0.8042 -0.7190 -0.0812 0.1062  483 ALA A CA  
1430 C C   . ALA A 187 ? 1.3802 1.5849 0.9323 -0.7376 -0.0887 0.1066  483 ALA A C   
1431 O O   . ALA A 187 ? 1.3269 1.4150 0.7971 -0.7580 -0.0987 0.1080  483 ALA A O   
1432 C CB  . ALA A 187 ? 1.3638 1.5950 0.8879 -0.7644 -0.0782 0.1125  483 ALA A CB  
1433 N N   . GLY A 188 ? 1.3658 1.7111 0.9911 -0.7280 -0.0837 0.1052  484 GLY A N   
1434 C CA  . GLY A 188 ? 1.4546 1.8339 1.0668 -0.7502 -0.0894 0.1070  484 GLY A CA  
1435 C C   . GLY A 188 ? 1.4808 1.9991 1.1084 -0.7780 -0.0846 0.1113  484 GLY A C   
1436 O O   . GLY A 188 ? 1.4476 2.0895 1.1548 -0.7447 -0.0757 0.1081  484 GLY A O   
1437 N N   . TYR A 189 ? 1.5430 2.0414 1.0889 -0.8381 -0.0910 0.1183  485 TYR A N   
1438 C CA  . TYR A 189 ? 1.5109 2.1412 1.0597 -0.8722 -0.0880 0.1229  485 TYR A CA  
1439 C C   . TYR A 189 ? 1.5195 2.1716 1.0448 -0.8992 -0.0947 0.1262  485 TYR A C   
1440 O O   . TYR A 189 ? 1.4947 2.0287 0.9420 -0.9296 -0.1044 0.1290  485 TYR A O   
1441 C CB  . TYR A 189 ? 1.5403 2.1466 1.0061 -0.9310 -0.0901 0.1290  485 TYR A CB  
1442 C CG  . TYR A 189 ? 1.5064 2.0244 0.9520 -0.9201 -0.0880 0.1274  485 TYR A CG  
1443 C CD1 . TYR A 189 ? 1.5850 1.9312 0.9497 -0.9297 -0.0965 0.1277  485 TYR A CD1 
1444 C CD2 . TYR A 189 ? 1.4104 2.0147 0.9106 -0.8992 -0.0779 0.1255  485 TYR A CD2 
1445 C CE1 . TYR A 189 ? 1.6293 1.8933 0.9703 -0.9186 -0.0949 0.1266  485 TYR A CE1 
1446 C CE2 . TYR A 189 ? 1.4939 2.0178 0.9733 -0.8915 -0.0758 0.1248  485 TYR A CE2 
1447 C CZ  . TYR A 189 ? 1.5526 1.9068 0.9524 -0.9019 -0.0844 0.1256  485 TYR A CZ  
1448 O OH  . TYR A 189 ? 1.5348 1.8067 0.9093 -0.8921 -0.0826 0.1252  485 TYR A OH  
1449 N N   . LYS A 190 ? 1.5826 2.3847 1.1701 -0.8864 -0.0896 0.1259  486 LYS A N   
1450 C CA  . LYS A 190 ? 1.7001 2.5483 1.2622 -0.9207 -0.0949 0.1307  486 LYS A CA  
1451 C C   . LYS A 190 ? 1.8844 2.7215 1.3454 -1.0018 -0.1001 0.1398  486 LYS A C   
1452 O O   . LYS A 190 ? 1.9536 2.7507 1.3674 -1.0284 -0.1001 0.1417  486 LYS A O   
1453 C CB  . LYS A 190 ? 1.6454 2.6614 1.2965 -0.8818 -0.0878 0.1277  486 LYS A CB  
1454 C CG  . LYS A 190 ? 1.5967 2.7080 1.3108 -0.8411 -0.0772 0.1232  486 LYS A CG  
1455 C CD  . LYS A 190 ? 1.5512 2.8244 1.3386 -0.7993 -0.0710 0.1198  486 LYS A CD  
1456 C CE  . LYS A 190 ? 1.4444 2.7099 1.3076 -0.7248 -0.0698 0.1111  486 LYS A CE  
1457 N NZ  . LYS A 190 ? 1.3935 2.8078 1.3226 -0.6726 -0.0630 0.1064  486 LYS A NZ  
1458 N N   . GLN A 191 ? 1.9277 2.7999 1.3509 -1.0438 -0.1053 0.1456  487 GLN A N   
1459 C CA  . GLN A 191 ? 1.9759 2.8211 1.2894 -1.1269 -0.1125 0.1546  487 GLN A CA  
1460 C C   . GLN A 191 ? 1.9444 2.9622 1.2712 -1.1602 -0.1093 0.1599  487 GLN A C   
1461 O O   . GLN A 191 ? 1.8329 2.9762 1.2470 -1.1169 -0.1030 0.1567  487 GLN A O   
1462 C CB  . GLN A 191 ? 2.0679 2.7676 1.2933 -1.1598 -0.1238 0.1582  487 GLN A CB  
1463 C CG  . GLN A 191 ? 2.1096 2.6215 1.2757 -1.1483 -0.1296 0.1550  487 GLN A CG  
1464 C CD  . GLN A 191 ? 2.2199 2.6741 1.3045 -1.1909 -0.1324 0.1577  487 GLN A CD  
1465 O OE1 . GLN A 191 ? 2.1642 2.6744 1.2983 -1.1688 -0.1251 0.1545  487 GLN A OE1 
1466 N NE2 . GLN A 191 ? 2.4063 2.7433 1.3599 -1.2524 -0.1437 0.1633  487 GLN A NE2 
1467 N N   . PRO A 192 ? 2.0503 3.0799 1.2876 -1.2366 -0.1142 0.1676  488 PRO A N   
1468 C CA  . PRO A 192 ? 2.0839 3.2718 1.3196 -1.2774 -0.1129 0.1737  488 PRO A CA  
1469 C C   . PRO A 192 ? 2.1309 3.3192 1.3566 -1.2901 -0.1171 0.1776  488 PRO A C   
1470 O O   . PRO A 192 ? 2.1372 3.4773 1.4130 -1.2838 -0.1126 0.1790  488 PRO A O   
1471 C CB  . PRO A 192 ? 2.2129 3.3750 1.3352 -1.3644 -0.1199 0.1810  488 PRO A CB  
1472 C CG  . PRO A 192 ? 2.2908 3.2437 1.3308 -1.3768 -0.1283 0.1801  488 PRO A CG  
1473 C CD  . PRO A 192 ? 2.1751 3.0814 1.3065 -1.2893 -0.1216 0.1706  488 PRO A CD  
1474 N N   . ASP A 193 ? 2.1530 3.1748 1.3130 -1.3051 -0.1258 0.1791  489 ASP A N   
1475 C CA  . ASP A 193 ? 2.1333 3.1369 1.2789 -1.3166 -0.1307 0.1825  489 ASP A CA  
1476 C C   . ASP A 193 ? 1.9877 2.9900 1.2350 -1.2346 -0.1272 0.1736  489 ASP A C   
1477 O O   . ASP A 193 ? 1.9894 2.9381 1.2229 -1.2358 -0.1327 0.1745  489 ASP A O   
1478 C CB  . ASP A 193 ? 2.2814 3.1017 1.2945 -1.3739 -0.1428 0.1883  489 ASP A CB  
1479 C CG  . ASP A 193 ? 2.3099 2.9567 1.2985 -1.3386 -0.1462 0.1818  489 ASP A CG  
1480 O OD1 . ASP A 193 ? 2.3073 2.9380 1.2880 -1.3363 -0.1440 0.1794  489 ASP A OD1 
1481 O OD2 . ASP A 193 ? 2.3373 2.8676 1.3147 -1.3117 -0.1511 0.1788  489 ASP A OD2 
1482 N N   . GLY A 194 ? 1.9188 2.9746 1.2629 -1.1649 -0.1188 0.1649  490 GLY A N   
1483 C CA  . GLY A 194 ? 1.8496 2.9216 1.2909 -1.0878 -0.1158 0.1560  490 GLY A CA  
1484 C C   . GLY A 194 ? 1.8806 2.7928 1.3232 -1.0480 -0.1196 0.1493  490 GLY A C   
1485 O O   . GLY A 194 ? 1.8167 2.7475 1.3463 -0.9789 -0.1158 0.1405  490 GLY A O   
1486 N N   . SER A 195 ? 1.9847 2.7400 1.3281 -1.0882 -0.1274 0.1528  491 SER A N   
1487 C CA  . SER A 195 ? 1.9864 2.5897 1.3234 -1.0492 -0.1315 0.1461  491 SER A CA  
1488 C C   . SER A 195 ? 1.9513 2.5304 1.3229 -1.0114 -0.1254 0.1405  491 SER A C   
1489 O O   . SER A 195 ? 1.8662 2.5641 1.2954 -0.9977 -0.1168 0.1397  491 SER A O   
1490 C CB  . SER A 195 ? 2.1077 2.5461 1.3169 -1.0992 -0.1425 0.1512  491 SER A CB  
1491 O OG  . SER A 195 ? 2.2276 2.6337 1.3450 -1.1583 -0.1447 0.1582  491 SER A OG  
1492 N N   . THR A 196 ? 1.9883 2.4156 1.3231 -0.9925 -0.1298 0.1365  492 THR A N   
1493 C CA  . THR A 196 ? 1.8956 2.2984 1.2737 -0.9485 -0.1239 0.1304  492 THR A CA  
1494 C C   . THR A 196 ? 2.0017 2.2329 1.2812 -0.9650 -0.1304 0.1309  492 THR A C   
1495 O O   . THR A 196 ? 2.1053 2.2091 1.3190 -0.9681 -0.1390 0.1302  492 THR A O   
1496 C CB  . THR A 196 ? 1.7016 2.1250 1.1806 -0.8760 -0.1206 0.1208  492 THR A CB  
1497 O OG1 . THR A 196 ? 1.5580 2.1442 1.1285 -0.8515 -0.1140 0.1192  492 THR A OG1 
1498 C CG2 . THR A 196 ? 1.6041 1.9763 1.1125 -0.8350 -0.1159 0.1151  492 THR A CG2 
1499 N N   . LEU A 197 ? 1.8467 2.0750 1.1137 -0.9717 -0.1263 0.1317  493 LEU A N   
1500 C CA  . LEU A 197 ? 1.8401 1.9159 1.0262 -0.9744 -0.1311 0.1308  493 LEU A CA  
1501 C C   . LEU A 197 ? 1.6866 1.7597 0.9510 -0.9126 -0.1236 0.1237  493 LEU A C   
1502 O O   . LEU A 197 ? 1.4488 1.6502 0.8130 -0.8845 -0.1137 0.1214  493 LEU A O   
1503 C CB  . LEU A 197 ? 1.9191 1.9858 1.0198 -1.0349 -0.1336 0.1371  493 LEU A CB  
1504 C CG  . LEU A 197 ? 1.9367 1.8624 0.9500 -1.0415 -0.1384 0.1361  493 LEU A CG  
1505 C CD1 . LEU A 197 ? 2.0090 1.7518 0.9250 -1.0328 -0.1495 0.1337  493 LEU A CD1 
1506 C CD2 . LEU A 197 ? 2.0156 1.9576 0.9486 -1.1094 -0.1419 0.1419  493 LEU A CD2 
1507 N N   . GLY A 198 ? 1.8132 1.7392 1.0268 -0.8896 -0.1286 0.1201  494 GLY A N   
1508 C CA  . GLY A 198 ? 1.8179 1.7258 1.0898 -0.8363 -0.1225 0.1143  494 GLY A CA  
1509 C C   . GLY A 198 ? 1.7233 1.6329 1.0692 -0.7814 -0.1219 0.1067  494 GLY A C   
1510 O O   . GLY A 198 ? 1.8915 1.7008 1.1882 -0.7734 -0.1300 0.1041  494 GLY A O   
1511 N N   . ASP A 199 ? 1.4426 1.4654 0.9013 -0.7437 -0.1129 0.1026  495 ASP A N   
1512 C CA  . ASP A 199 ? 1.3111 1.3501 0.8452 -0.6932 -0.1130 0.0944  495 ASP A CA  
1513 C C   . ASP A 199 ? 1.2220 1.4199 0.8495 -0.6816 -0.1078 0.0931  495 ASP A C   
1514 O O   . ASP A 199 ? 1.0945 1.3974 0.7890 -0.6639 -0.0986 0.0924  495 ASP A O   
1515 C CB  . ASP A 199 ? 1.2100 1.2143 0.7820 -0.6495 -0.1089 0.0891  495 ASP A CB  
1516 C CG  . ASP A 199 ? 1.3245 1.3018 0.9421 -0.6035 -0.1127 0.0802  495 ASP A CG  
1517 O OD1 . ASP A 199 ? 1.1995 1.2295 0.8535 -0.5975 -0.1157 0.0775  495 ASP A OD1 
1518 O OD2 . ASP A 199 ? 1.3124 1.2158 0.9263 -0.5737 -0.1133 0.0760  495 ASP A OD2 
1519 N N   . PRO A 200 ? 1.3542 1.5731 0.9858 -0.6863 -0.1132 0.0925  496 PRO A N   
1520 C CA  . PRO A 200 ? 1.2852 1.6539 0.9977 -0.6713 -0.1088 0.0915  496 PRO A CA  
1521 C C   . PRO A 200 ? 1.1317 1.5679 0.9426 -0.6106 -0.1034 0.0835  496 PRO A C   
1522 O O   . PRO A 200 ? 1.1004 1.6633 0.9738 -0.5905 -0.0975 0.0828  496 PRO A O   
1523 C CB  . PRO A 200 ? 1.3491 1.6953 1.0366 -0.6849 -0.1176 0.0918  496 PRO A CB  
1524 C CG  . PRO A 200 ? 1.4344 1.6321 1.0106 -0.7229 -0.1254 0.0955  496 PRO A CG  
1525 C CD  . PRO A 200 ? 1.3686 1.4747 0.9274 -0.7018 -0.1236 0.0924  496 PRO A CD  
1526 N N   . ALA A 201 ? 1.0789 1.4327 0.8989 -0.5794 -0.1057 0.0775  497 ALA A N   
1527 C CA  . ALA A 201 ? 1.0645 1.4761 0.9697 -0.5249 -0.1015 0.0703  497 ALA A CA  
1528 C C   . ALA A 201 ? 1.0341 1.5456 0.9828 -0.5129 -0.0904 0.0715  497 ALA A C   
1529 O O   . ALA A 201 ? 1.0002 1.6111 1.0171 -0.4727 -0.0859 0.0675  497 ALA A O   
1530 C CB  . ALA A 201 ? 1.0092 1.3113 0.9024 -0.5023 -0.1050 0.0650  497 ALA A CB  
1531 N N   . ASN A 202 ? 1.1406 1.6229 1.0429 -0.5457 -0.0862 0.0771  498 ASN A N   
1532 C CA  . ASN A 202 ? 1.1166 1.6675 1.0514 -0.5332 -0.0757 0.0775  498 ASN A CA  
1533 C C   . ASN A 202 ? 1.1363 1.7985 1.0717 -0.5556 -0.0696 0.0824  498 ASN A C   
1534 O O   . ASN A 202 ? 1.1196 1.8387 1.0718 -0.5497 -0.0608 0.0830  498 ASN A O   
1535 C CB  . ASN A 202 ? 1.1469 1.5969 1.0276 -0.5543 -0.0751 0.0806  498 ASN A CB  
1536 C CG  . ASN A 202 ? 1.1352 1.4654 0.9991 -0.5362 -0.0824 0.0762  498 ASN A CG  
1537 O OD1 . ASN A 202 ? 1.0551 1.3932 0.9714 -0.4785 -0.0811 0.0682  498 ASN A OD1 
1538 N ND2 . ASN A 202 ? 1.2584 1.4609 1.0353 -0.5653 -0.0877 0.0803  498 ASN A ND2 
1539 N N   . VAL A 203 ? 1.0609 1.7579 0.9759 -0.5815 -0.0742 0.0859  499 VAL A N   
1540 C CA  . VAL A 203 ? 0.9819 1.7794 0.8827 -0.6130 -0.0700 0.0916  499 VAL A CA  
1541 C C   . VAL A 203 ? 0.8742 1.8012 0.8436 -0.5682 -0.0597 0.0874  499 VAL A C   
1542 O O   . VAL A 203 ? 0.9892 1.9863 0.9466 -0.5881 -0.0537 0.0909  499 VAL A O   
1543 C CB  . VAL A 203 ? 1.0253 1.8489 0.9023 -0.6410 -0.0770 0.0951  499 VAL A CB  
1544 C CG1 . VAL A 203 ? 1.0537 1.9974 0.9200 -0.6719 -0.0728 0.1007  499 VAL A CG1 
1545 C CG2 . VAL A 203 ? 1.0750 1.7631 0.8680 -0.6878 -0.0868 0.0995  499 VAL A CG2 
1546 N N   . GLN A 204 ? 0.8463 1.8027 0.8816 -0.5061 -0.0583 0.0794  500 GLN A N   
1547 C CA  . GLN A 204 ? 0.8681 1.9338 0.9564 -0.4574 -0.0490 0.0746  500 GLN A CA  
1548 C C   . GLN A 204 ? 0.8352 1.8786 0.9311 -0.4442 -0.0413 0.0726  500 GLN A C   
1549 O O   . GLN A 204 ? 0.8437 1.9696 0.9510 -0.4334 -0.0329 0.0721  500 GLN A O   
1550 C CB  . GLN A 204 ? 0.9436 2.0397 1.0873 -0.3930 -0.0508 0.0667  500 GLN A CB  
1551 C CG  . GLN A 204 ? 1.0290 2.2500 1.2067 -0.3479 -0.0435 0.0630  500 GLN A CG  
1552 C CD  . GLN A 204 ? 1.0316 2.2563 1.2562 -0.2717 -0.0422 0.0536  500 GLN A CD  
1553 O OE1 . GLN A 204 ? 1.0198 2.1619 1.2570 -0.2537 -0.0470 0.0500  500 GLN A OE1 
1554 N NE2 . GLN A 204 ? 1.0517 2.3701 1.2951 -0.2258 -0.0362 0.0495  500 GLN A NE2 
1555 N N   . PHE A 205 ? 0.8564 1.7917 0.9448 -0.4436 -0.0443 0.0711  501 PHE A N   
1556 C CA  . PHE A 205 ? 0.8647 1.7725 0.9544 -0.4369 -0.0374 0.0702  501 PHE A CA  
1557 C C   . PHE A 205 ? 0.8929 1.7888 0.9237 -0.4954 -0.0349 0.0786  501 PHE A C   
1558 O O   . PHE A 205 ? 0.9290 1.8734 0.9665 -0.4907 -0.0262 0.0787  501 PHE A O   
1559 C CB  . PHE A 205 ? 0.8725 1.6695 0.9633 -0.4248 -0.0425 0.0670  501 PHE A CB  
1560 C CG  . PHE A 205 ? 0.9070 1.6736 0.9968 -0.4197 -0.0359 0.0665  501 PHE A CG  
1561 C CD1 . PHE A 205 ? 0.9131 1.7414 1.0529 -0.3672 -0.0272 0.0596  501 PHE A CD1 
1562 C CD2 . PHE A 205 ? 0.9839 1.6495 1.0124 -0.4629 -0.0385 0.0728  501 PHE A CD2 
1563 C CE1 . PHE A 205 ? 0.9358 1.7169 1.0621 -0.3527 -0.0203 0.0579  501 PHE A CE1 
1564 C CE2 . PHE A 205 ? 1.0702 1.6900 1.0855 -0.4452 -0.0319 0.0717  501 PHE A CE2 
1565 C CZ  . PHE A 205 ? 0.9761 1.6575 1.0432 -0.3918 -0.0228 0.0642  501 PHE A CZ  
1566 N N   . THR A 206 ? 0.8803 1.7058 0.8462 -0.5504 -0.0432 0.0855  502 THR A N   
1567 C CA  . THR A 206 ? 1.0186 1.8266 0.9161 -0.6090 -0.0430 0.0936  502 THR A CA  
1568 C C   . THR A 206 ? 1.0538 2.0010 0.9674 -0.6150 -0.0363 0.0948  502 THR A C   
1569 O O   . THR A 206 ? 0.9713 1.9370 0.8573 -0.6411 -0.0319 0.0983  502 THR A O   
1570 C CB  . THR A 206 ? 1.0472 1.7632 0.8655 -0.6632 -0.0544 0.0997  502 THR A CB  
1571 O OG1 . THR A 206 ? 0.9878 1.5671 0.7817 -0.6542 -0.0608 0.0980  502 THR A OG1 
1572 C CG2 . THR A 206 ? 1.0798 1.7747 0.8165 -0.7265 -0.0562 0.1077  502 THR A CG2 
1573 N N   . GLU A 207 ? 1.0381 2.0856 0.9957 -0.5873 -0.0356 0.0916  503 GLU A N   
1574 C CA  . GLU A 207 ? 1.1633 2.3495 1.1341 -0.5875 -0.0299 0.0922  503 GLU A CA  
1575 C C   . GLU A 207 ? 1.0998 2.3507 1.1215 -0.5331 -0.0192 0.0856  503 GLU A C   
1576 O O   . GLU A 207 ? 1.0935 2.4255 1.1069 -0.5448 -0.0139 0.0870  503 GLU A O   
1577 C CB  . GLU A 207 ? 1.2394 2.5077 1.2327 -0.5736 -0.0332 0.0911  503 GLU A CB  
1578 C CG  . GLU A 207 ? 1.4548 2.7362 1.3869 -0.6429 -0.0402 0.0997  503 GLU A CG  
1579 C CD  . GLU A 207 ? 1.5922 2.8930 1.5355 -0.6366 -0.0462 0.0995  503 GLU A CD  
1580 O OE1 . GLU A 207 ? 1.5804 2.9404 1.5840 -0.5753 -0.0434 0.0928  503 GLU A OE1 
1581 O OE2 . GLU A 207 ? 1.7178 2.9687 1.6044 -0.6921 -0.0542 0.1060  503 GLU A OE2 
1582 N N   . ILE A 208 ? 1.0309 2.2475 1.1014 -0.4739 -0.0167 0.0779  504 ILE A N   
1583 C CA  . ILE A 208 ? 0.8909 2.1528 1.0012 -0.4207 -0.0068 0.0710  504 ILE A CA  
1584 C C   . ILE A 208 ? 0.8649 2.0897 0.9448 -0.4530 -0.0017 0.0750  504 ILE A C   
1585 O O   . ILE A 208 ? 0.8410 2.1411 0.9274 -0.4422 0.0061  0.0735  504 ILE A O   
1586 C CB  . ILE A 208 ? 0.7863 2.0005 0.9429 -0.3582 -0.0070 0.0623  504 ILE A CB  
1587 C CG1 . ILE A 208 ? 0.7215 1.9964 0.9099 -0.3125 -0.0100 0.0571  504 ILE A CG1 
1588 C CG2 . ILE A 208 ? 0.6269 1.8512 0.8080 -0.3149 0.0026  0.0560  504 ILE A CG2 
1589 C CD1 . ILE A 208 ? 0.7960 2.0009 1.0132 -0.2713 -0.0154 0.0510  504 ILE A CD1 
1590 N N   . CYS A 209 ? 0.9015 2.0064 0.9436 -0.4909 -0.0066 0.0798  505 CYS A N   
1591 C CA  . CYS A 209 ? 0.9763 2.0306 0.9758 -0.5280 -0.0032 0.0851  505 CYS A CA  
1592 C C   . CYS A 209 ? 1.0736 2.2025 1.0345 -0.5745 -0.0024 0.0907  505 CYS A C   
1593 O O   . CYS A 209 ? 0.9854 2.1482 0.9419 -0.5775 0.0048  0.0911  505 CYS A O   
1594 C CB  . CYS A 209 ? 0.9800 1.8873 0.9241 -0.5676 -0.0118 0.0908  505 CYS A CB  
1595 S SG  . CYS A 209 ? 0.9610 1.7747 0.9419 -0.5205 -0.0134 0.0847  505 CYS A SG  
1596 N N   . ILE A 210 ? 1.0355 2.1934 0.9662 -0.6132 -0.0102 0.0950  506 ILE A N   
1597 C CA  . ILE A 210 ? 1.1011 2.3354 0.9907 -0.6636 -0.0114 0.1003  506 ILE A CA  
1598 C C   . ILE A 210 ? 1.0628 2.4506 1.0039 -0.6214 -0.0031 0.0949  506 ILE A C   
1599 O O   . ILE A 210 ? 1.0149 2.4688 0.9392 -0.6432 0.0001  0.0965  506 ILE A O   
1600 C CB  . ILE A 210 ? 1.0748 2.2982 0.9132 -0.7183 -0.0224 0.1063  506 ILE A CB  
1601 C CG1 . ILE A 210 ? 1.1008 2.1606 0.8705 -0.7608 -0.0315 0.1113  506 ILE A CG1 
1602 C CG2 . ILE A 210 ? 1.2106 2.5276 1.0076 -0.7718 -0.0245 0.1112  506 ILE A CG2 
1603 C CD1 . ILE A 210 ? 1.2610 2.2941 0.9759 -0.8094 -0.0425 0.1164  506 ILE A CD1 
1604 N N   . GLN A 211 ? 1.1373 2.5795 1.1367 -0.5583 -0.0004 0.0878  507 GLN A N   
1605 C CA  . GLN A 211 ? 1.1487 2.7236 1.1896 -0.5069 0.0067  0.0815  507 GLN A CA  
1606 C C   . GLN A 211 ? 1.1002 2.6761 1.1606 -0.4725 0.0164  0.0766  507 GLN A C   
1607 O O   . GLN A 211 ? 1.0569 2.7381 1.1278 -0.4522 0.0216  0.0737  507 GLN A O   
1608 C CB  . GLN A 211 ? 1.1594 2.7662 1.2478 -0.4427 0.0062  0.0745  507 GLN A CB  
1609 C CG  . GLN A 211 ? 1.2673 2.9321 1.3425 -0.4673 -0.0010 0.0784  507 GLN A CG  
1610 C CD  . GLN A 211 ? 1.3062 3.1260 1.3951 -0.4401 0.0019  0.0758  507 GLN A CD  
1611 O OE1 . GLN A 211 ? 1.2750 3.1474 1.3948 -0.3774 0.0085  0.0682  507 GLN A OE1 
1612 N NE2 . GLN A 211 ? 1.3460 3.2388 1.4068 -0.4864 -0.0034 0.0820  507 GLN A NE2 
1613 N N   . GLN A 212 ? 1.0266 2.4895 1.0894 -0.4653 0.0188  0.0758  508 GLN A N   
1614 C CA  . GLN A 212 ? 0.9953 2.4491 1.0717 -0.4371 0.0285  0.0718  508 GLN A CA  
1615 C C   . GLN A 212 ? 0.9998 2.4139 1.0256 -0.4998 0.0293  0.0797  508 GLN A C   
1616 O O   . GLN A 212 ? 1.0029 2.4023 1.0340 -0.4835 0.0377  0.0777  508 GLN A O   
1617 C CB  . GLN A 212 ? 0.9992 2.3602 1.1058 -0.3920 0.0312  0.0661  508 GLN A CB  
1618 C CG  . GLN A 212 ? 1.0979 2.4837 1.2501 -0.3263 0.0296  0.0572  508 GLN A CG  
1619 C CD  . GLN A 212 ? 1.2017 2.6614 1.3844 -0.2557 0.0378  0.0470  508 GLN A CD  
1620 O OE1 . GLN A 212 ? 1.2389 2.6579 1.4474 -0.2002 0.0405  0.0385  508 GLN A OE1 
1621 N NE2 . GLN A 212 ? 1.2276 2.7939 1.4020 -0.2567 0.0406  0.0475  508 GLN A NE2 
1622 N N   . GLY A 213 ? 0.9779 2.3674 0.9490 -0.5707 0.0202  0.0884  509 GLY A N   
1623 C CA  . GLY A 213 ? 1.0531 2.4067 0.9652 -0.6329 0.0188  0.0956  509 GLY A CA  
1624 C C   . GLY A 213 ? 1.1136 2.3190 0.9591 -0.6886 0.0097  0.1032  509 GLY A C   
1625 O O   . GLY A 213 ? 1.1241 2.2837 0.9087 -0.7416 0.0069  0.1090  509 GLY A O   
1626 N N   . TRP A 214 ? 1.2522 2.3747 1.1002 -0.6781 0.0041  0.1030  510 TRP A N   
1627 C CA  . TRP A 214 ? 1.3695 2.3445 1.1435 -0.7269 -0.0059 0.1097  510 TRP A CA  
1628 C C   . TRP A 214 ? 1.4526 2.4323 1.1528 -0.7990 -0.0165 0.1158  510 TRP A C   
1629 O O   . TRP A 214 ? 1.3658 2.4438 1.0785 -0.8088 -0.0194 0.1154  510 TRP A O   
1630 C CB  . TRP A 214 ? 1.3121 2.2076 1.1014 -0.7021 -0.0114 0.1077  510 TRP A CB  
1631 C CG  . TRP A 214 ? 1.3275 2.0534 1.0427 -0.7324 -0.0195 0.1130  510 TRP A CG  
1632 C CD1 . TRP A 214 ? 1.2929 1.9329 0.9688 -0.7407 -0.0170 0.1164  510 TRP A CD1 
1633 C CD2 . TRP A 214 ? 1.3239 1.9427 0.9861 -0.7557 -0.0320 0.1154  510 TRP A CD2 
1634 N NE1 . TRP A 214 ? 1.3416 1.8254 0.9420 -0.7628 -0.0276 0.1205  510 TRP A NE1 
1635 C CE2 . TRP A 214 ? 1.3597 1.8269 0.9498 -0.7717 -0.0370 0.1194  510 TRP A CE2 
1636 C CE3 . TRP A 214 ? 1.4010 2.0346 1.0658 -0.7615 -0.0393 0.1145  510 TRP A CE3 
1637 C CZ2 . TRP A 214 ? 1.4386 1.7676 0.9566 -0.7892 -0.0495 0.1213  510 TRP A CZ2 
1638 C CZ3 . TRP A 214 ? 1.4524 1.9507 1.0494 -0.7832 -0.0510 0.1169  510 TRP A CZ3 
1639 C CH2 . TRP A 214 ? 1.5274 1.8748 1.0509 -0.7948 -0.0561 0.1197  510 TRP A CH2 
1640 N N   . LYS A 215 ? 1.5762 2.4469 1.1937 -0.8492 -0.0228 0.1212  511 LYS A N   
1641 C CA  . LYS A 215 ? 1.7038 2.5434 1.2319 -0.9230 -0.0354 0.1264  511 LYS A CA  
1642 C C   . LYS A 215 ? 1.6996 2.3795 1.1627 -0.9386 -0.0468 0.1286  511 LYS A C   
1643 O O   . LYS A 215 ? 1.7777 2.3199 1.1952 -0.9356 -0.0492 0.1299  511 LYS A O   
1644 C CB  . LYS A 215 ? 1.7931 2.6209 1.2649 -0.9681 -0.0360 0.1294  511 LYS A CB  
1645 C CG  . LYS A 215 ? 1.8137 2.8079 1.3489 -0.9511 -0.0251 0.1267  511 LYS A CG  
1646 C CD  . LYS A 215 ? 1.9400 3.0535 1.4506 -1.0033 -0.0315 0.1284  511 LYS A CD  
1647 C CE  . LYS A 215 ? 1.9613 3.1603 1.5117 -0.9855 -0.0334 0.1270  511 LYS A CE  
1648 N NZ  . LYS A 215 ? 2.0814 3.3350 1.5707 -1.0555 -0.0443 0.1315  511 LYS A NZ  
1649 N N   . ALA A 216 ? 1.5603 2.2593 1.0176 -0.9509 -0.0535 0.1291  512 ALA A N   
1650 C CA  . ALA A 216 ? 1.4273 1.9960 0.8443 -0.9488 -0.0625 0.1295  512 ALA A CA  
1651 C C   . ALA A 216 ? 1.5835 2.0286 0.8713 -1.0161 -0.0770 0.1338  512 ALA A C   
1652 O O   . ALA A 216 ? 1.5941 2.0970 0.8369 -1.0721 -0.0826 0.1369  512 ALA A O   
1653 C CB  . ALA A 216 ? 1.3293 1.9771 0.8006 -0.9285 -0.0625 0.1277  512 ALA A CB  
1654 N N   . PRO A 217 ? 1.6890 1.9626 0.9087 -1.0117 -0.0841 0.1337  513 PRO A N   
1655 C CA  . PRO A 217 ? 1.8953 2.0313 0.9813 -1.0669 -0.0996 0.1359  513 PRO A CA  
1656 C C   . PRO A 217 ? 2.0139 2.1161 1.0697 -1.0778 -0.1082 0.1365  513 PRO A C   
1657 O O   . PRO A 217 ? 2.1008 2.0494 1.0745 -1.0785 -0.1184 0.1355  513 PRO A O   
1658 C CB  . PRO A 217 ? 1.8962 1.8681 0.9317 -1.0388 -0.1024 0.1340  513 PRO A CB  
1659 C CG  . PRO A 217 ? 1.8114 1.8183 0.9556 -0.9663 -0.0910 0.1316  513 PRO A CG  
1660 C CD  . PRO A 217 ? 1.7006 1.9005 0.9571 -0.9538 -0.0779 0.1312  513 PRO A CD  
1661 N N   . ARG A 218 ? 2.0285 2.2762 1.1477 -1.0838 -0.1039 0.1379  514 ARG A N   
1662 C CA  . ARG A 218 ? 1.9626 2.2177 1.0902 -1.0804 -0.1079 0.1386  514 ARG A CA  
1663 C C   . ARG A 218 ? 2.0070 2.0882 1.0200 -1.1035 -0.1219 0.1393  514 ARG A C   
1664 O O   . ARG A 218 ? 2.1439 2.2077 1.0741 -1.1611 -0.1313 0.1434  514 ARG A O   
1665 C CB  . ARG A 218 ? 1.9696 2.3770 1.1133 -1.1216 -0.1071 0.1425  514 ARG A CB  
1666 C CG  . ARG A 218 ? 1.8592 2.4481 1.1276 -1.0799 -0.0933 0.1400  514 ARG A CG  
1667 C CD  . ARG A 218 ? 1.8859 2.6279 1.1611 -1.1191 -0.0930 0.1438  514 ARG A CD  
1668 N NE  . ARG A 218 ? 1.8331 2.6991 1.2098 -1.0691 -0.0852 0.1411  514 ARG A NE  
1669 C CZ  . ARG A 218 ? 1.7628 2.7357 1.2414 -1.0084 -0.0735 0.1357  514 ARG A CZ  
1670 N NH1 . ARG A 218 ? 1.7266 2.7984 1.2833 -0.9633 -0.0685 0.1326  514 ARG A NH1 
1671 N NH2 . ARG A 218 ? 1.8394 2.8154 1.3370 -0.9912 -0.0672 0.1332  514 ARG A NH2 
1672 N N   . GLY A 219 ? 1.9015 1.8544 0.9053 -1.0572 -0.1234 0.1352  515 GLY A N   
1673 C CA  . GLY A 219 ? 2.0086 1.8000 0.9159 -1.0598 -0.1356 0.1341  515 GLY A CA  
1674 C C   . GLY A 219 ? 2.0097 1.7833 0.9857 -0.9984 -0.1328 0.1299  515 GLY A C   
1675 O O   . GLY A 219 ? 1.8255 1.7288 0.9138 -0.9716 -0.1239 0.1290  515 GLY A O   
1676 N N   . ARG A 220 ? 2.2740 1.8874 1.1808 -0.9725 -0.1407 0.1262  516 ARG A N   
1677 C CA  . ARG A 220 ? 2.2593 1.8405 1.2151 -0.9174 -0.1402 0.1214  516 ARG A CA  
1678 C C   . ARG A 220 ? 2.2257 1.8064 1.2604 -0.8544 -0.1320 0.1166  516 ARG A C   
1679 O O   . ARG A 220 ? 2.1732 1.8782 1.3280 -0.8265 -0.1218 0.1151  516 ARG A O   
1680 C CB  . ARG A 220 ? 2.3923 1.8030 1.2248 -0.9191 -0.1535 0.1193  516 ARG A CB  
1681 C CG  . ARG A 220 ? 2.3381 1.7120 1.2082 -0.8670 -0.1544 0.1139  516 ARG A CG  
1682 C CD  . ARG A 220 ? 2.3620 1.7582 1.2133 -0.8970 -0.1595 0.1165  516 ARG A CD  
1683 N NE  . ARG A 220 ? 2.4588 1.6987 1.2052 -0.8838 -0.1705 0.1133  516 ARG A NE  
1684 C CZ  . ARG A 220 ? 2.4756 1.7057 1.2122 -0.8864 -0.1748 0.1133  516 ARG A CZ  
1685 N NH1 . ARG A 220 ? 2.3900 1.7580 1.2166 -0.9020 -0.1696 0.1162  516 ARG A NH1 
1686 N NH2 . ARG A 220 ? 2.5316 1.6141 1.1659 -0.8699 -0.1844 0.1099  516 ARG A NH2 
1687 N N   . PHE A 221 ? 2.2225 1.6617 1.1846 -0.8302 -0.1371 0.1139  517 PHE A N   
1688 C CA  . PHE A 221 ? 2.0498 1.4689 1.0692 -0.7704 -0.1309 0.1103  517 PHE A CA  
1689 C C   . PHE A 221 ? 2.0419 1.5182 1.0930 -0.7779 -0.1222 0.1139  517 PHE A C   
1690 O O   . PHE A 221 ? 2.0762 1.4590 1.0729 -0.7623 -0.1240 0.1139  517 PHE A O   
1691 C CB  . PHE A 221 ? 2.0742 1.3185 0.9984 -0.7324 -0.1405 0.1055  517 PHE A CB  
1692 C CG  . PHE A 221 ? 2.0360 1.2139 0.9162 -0.7231 -0.1491 0.1014  517 PHE A CG  
1693 C CD1 . PHE A 221 ? 2.1853 1.2555 0.9350 -0.7559 -0.1609 0.1016  517 PHE A CD1 
1694 C CD2 . PHE A 221 ? 1.8372 1.0555 0.8001 -0.6821 -0.1460 0.0969  517 PHE A CD2 
1695 C CE1 . PHE A 221 ? 2.2189 1.2255 0.9230 -0.7466 -0.1684 0.0984  517 PHE A CE1 
1696 C CE2 . PHE A 221 ? 1.9713 1.1271 0.8910 -0.6728 -0.1536 0.0930  517 PHE A CE2 
1697 C CZ  . PHE A 221 ? 2.0547 1.1068 0.8466 -0.7043 -0.1643 0.0943  517 PHE A CZ  
1698 N N   . ASP A 222 ? 1.9052 1.5411 1.0446 -0.7985 -0.1126 0.1165  518 ASP A N   
1699 C CA  . ASP A 222 ? 1.7141 1.4304 0.8997 -0.8021 -0.1023 0.1193  518 ASP A CA  
1700 C C   . ASP A 222 ? 1.6451 1.4218 0.9408 -0.7458 -0.0916 0.1165  518 ASP A C   
1701 O O   . ASP A 222 ? 1.5273 1.4121 0.9167 -0.7267 -0.0865 0.1129  518 ASP A O   
1702 C CB  . ASP A 222 ? 1.5866 1.4497 0.8063 -0.8469 -0.0976 0.1224  518 ASP A CB  
1703 C CG  . ASP A 222 ? 1.7955 1.6079 0.9043 -0.9104 -0.1089 0.1256  518 ASP A CG  
1704 O OD1 . ASP A 222 ? 1.9816 1.6376 0.9796 -0.9202 -0.1202 0.1249  518 ASP A OD1 
1705 O OD2 . ASP A 222 ? 1.8082 1.7375 0.9360 -0.9492 -0.1071 0.1284  518 ASP A OD2 
1706 N N   . VAL A 223 ? 1.6445 1.3501 0.9244 -0.7187 -0.0891 0.1177  519 VAL A N   
1707 C CA  . VAL A 223 ? 1.4728 1.2285 0.8471 -0.6697 -0.0798 0.1155  519 VAL A CA  
1708 C C   . VAL A 223 ? 1.3223 1.2498 0.7946 -0.6749 -0.0665 0.1153  519 VAL A C   
1709 O O   . VAL A 223 ? 1.3631 1.3343 0.8147 -0.7066 -0.0620 0.1195  519 VAL A O   
1710 C CB  . VAL A 223 ? 1.5022 1.1439 0.8278 -0.6351 -0.0808 0.1176  519 VAL A CB  
1711 C CG1 . VAL A 223 ? 1.4248 1.1301 0.8522 -0.5534 -0.0750 0.1055  519 VAL A CG1 
1712 C CG2 . VAL A 223 ? 1.6025 1.0714 0.8173 -0.6258 -0.0946 0.1177  519 VAL A CG2 
1713 N N   . LEU A 224 ? 1.2524 1.2779 0.8277 -0.6355 -0.0614 0.1079  520 LEU A N   
1714 C CA  . LEU A 224 ? 1.0990 1.2879 0.7657 -0.6281 -0.0496 0.1055  520 LEU A CA  
1715 C C   . LEU A 224 ? 1.1433 1.3497 0.8404 -0.5847 -0.0403 0.1020  520 LEU A C   
1716 O O   . LEU A 224 ? 1.1434 1.2558 0.8223 -0.5403 -0.0436 0.0977  520 LEU A O   
1717 C CB  . LEU A 224 ? 0.9144 1.1856 0.6676 -0.5849 -0.0498 0.0959  520 LEU A CB  
1718 C CG  . LEU A 224 ? 0.9903 1.2970 0.7338 -0.6166 -0.0561 0.0974  520 LEU A CG  
1719 C CD1 . LEU A 224 ? 0.8587 1.1477 0.6438 -0.5810 -0.0625 0.0900  520 LEU A CD1 
1720 C CD2 . LEU A 224 ? 0.9709 1.4318 0.7624 -0.6213 -0.0484 0.0972  520 LEU A CD2 
1721 N N   . PRO A 225 ? 1.1093 1.4402 0.8515 -0.5954 -0.0289 0.1034  521 PRO A N   
1722 C CA  . PRO A 225 ? 1.0728 1.4261 0.8470 -0.5510 -0.0198 0.0986  521 PRO A CA  
1723 C C   . PRO A 225 ? 0.9715 1.3754 0.8314 -0.4766 -0.0174 0.0850  521 PRO A C   
1724 O O   . PRO A 225 ? 0.8355 1.2906 0.7394 -0.4633 -0.0198 0.0805  521 PRO A O   
1725 C CB  . PRO A 225 ? 1.0960 1.5705 0.8808 -0.5945 -0.0082 0.1053  521 PRO A CB  
1726 C CG  . PRO A 225 ? 1.0854 1.6501 0.8964 -0.6116 -0.0116 0.1038  521 PRO A CG  
1727 C CD  . PRO A 225 ? 1.1246 1.5774 0.8841 -0.6315 -0.0255 0.1059  521 PRO A CD  
1728 N N   . LEU A 226 ? 0.8572 1.2366 0.7326 -0.4295 -0.0136 0.0787  522 LEU A N   
1729 C CA  . LEU A 226 ? 0.8526 1.2781 0.7996 -0.3648 -0.0105 0.0661  522 LEU A CA  
1730 C C   . LEU A 226 ? 0.8659 1.4316 0.8674 -0.3574 0.0004  0.0634  522 LEU A C   
1731 O O   . LEU A 226 ? 0.9001 1.5270 0.8895 -0.3889 0.0087  0.0693  522 LEU A O   
1732 C CB  . LEU A 226 ? 0.8601 1.2211 0.8018 -0.3228 -0.0105 0.0602  522 LEU A CB  
1733 C CG  . LEU A 226 ? 0.9074 1.1424 0.8043 -0.3119 -0.0216 0.0604  522 LEU A CG  
1734 C CD1 . LEU A 226 ? 0.8514 1.0377 0.7327 -0.2824 -0.0215 0.0572  522 LEU A CD1 
1735 C CD2 . LEU A 226 ? 0.9015 1.1200 0.8318 -0.2799 -0.0281 0.0528  522 LEU A CD2 
1736 N N   . LEU A 227 ? 0.7831 1.3998 0.8401 -0.3139 0.0004  0.0544  523 LEU A N   
1737 C CA  . LEU A 227 ? 0.7801 1.5190 0.8863 -0.2855 0.0101  0.0488  523 LEU A CA  
1738 C C   . LEU A 227 ? 0.7321 1.4423 0.8666 -0.2187 0.0109  0.0362  523 LEU A C   
1739 O O   . LEU A 227 ? 0.6628 1.3435 0.8173 -0.1880 0.0047  0.0302  523 LEU A O   
1740 C CB  . LEU A 227 ? 0.6884 1.5186 0.8253 -0.2935 0.0083  0.0499  523 LEU A CB  
1741 C CG  . LEU A 227 ? 0.7559 1.7318 0.9094 -0.3206 0.0169  0.0549  523 LEU A CG  
1742 C CD1 . LEU A 227 ? 0.7322 1.7895 0.9235 -0.2910 0.0138  0.0503  523 LEU A CD1 
1743 C CD2 . LEU A 227 ? 0.8356 1.8743 0.9979 -0.3002 0.0298  0.0519  523 LEU A CD2 
1744 N N   . LEU A 228 ? 0.6713 1.3896 0.8031 -0.1993 0.0185  0.0323  524 LEU A N   
1745 C CA  . LEU A 228 ? 0.6932 1.3624 0.8356 -0.1462 0.0180  0.0209  524 LEU A CA  
1746 C C   . LEU A 228 ? 0.7013 1.4531 0.8694 -0.1035 0.0273  0.0123  524 LEU A C   
1747 O O   . LEU A 228 ? 0.7600 1.5786 0.9238 -0.1125 0.0371  0.0143  524 LEU A O   
1748 C CB  . LEU A 228 ? 0.6360 1.2262 0.7438 -0.1548 0.0169  0.0223  524 LEU A CB  
1749 C CG  . LEU A 228 ? 0.6431 1.1477 0.7114 -0.1931 0.0079  0.0314  524 LEU A CG  
1750 C CD1 . LEU A 228 ? 0.6791 1.1148 0.7110 -0.1930 0.0067  0.0324  524 LEU A CD1 
1751 C CD2 . LEU A 228 ? 0.6348 1.0833 0.7125 -0.1798 -0.0024 0.0285  524 LEU A CD2 
1752 N N   . GLN A 229 ? 0.6483 1.3886 0.8358 -0.0557 0.0242  0.0024  525 GLN A N   
1753 C CA  . GLN A 229 ? 0.6320 1.4225 0.8301 -0.0040 0.0309  -0.0079 525 GLN A CA  
1754 C C   . GLN A 229 ? 0.6262 1.3287 0.8069 0.0289  0.0285  -0.0181 525 GLN A C   
1755 O O   . GLN A 229 ? 0.6938 1.3147 0.8708 0.0329  0.0195  -0.0207 525 GLN A O   
1756 C CB  . GLN A 229 ? 0.4633 1.3008 0.6834 0.0265  0.0282  -0.0112 525 GLN A CB  
1757 C CG  . GLN A 229 ? 0.4978 1.3197 0.7125 0.0915  0.0286  -0.0240 525 GLN A CG  
1758 C CD  . GLN A 229 ? 0.6619 1.5028 0.8896 0.1174  0.0226  -0.0254 525 GLN A CD  
1759 O OE1 . GLN A 229 ? 0.5988 1.4596 0.8432 0.0849  0.0175  -0.0173 525 GLN A OE1 
1760 N NE2 . GLN A 229 ? 0.7190 1.5456 0.9319 0.1760  0.0224  -0.0357 525 GLN A NE2 
1761 N N   . ALA A 230 ? 0.4963 1.2190 0.6642 0.0495  0.0365  -0.0239 526 ALA A N   
1762 C CA  . ALA A 230 ? 0.5437 1.1872 0.6893 0.0749  0.0341  -0.0337 526 ALA A CA  
1763 C C   . ALA A 230 ? 0.6613 1.3250 0.7957 0.1308  0.0390  -0.0461 526 ALA A C   
1764 O O   . ALA A 230 ? 0.6122 1.3644 0.7503 0.1481  0.0490  -0.0470 526 ALA A O   
1765 C CB  . ALA A 230 ? 0.6767 1.3027 0.8035 0.0493  0.0375  -0.0303 526 ALA A CB  
1766 N N   . ASN A 231 ? 0.7696 1.3498 0.8842 0.1584  0.0319  -0.0558 527 ASN A N   
1767 C CA  . ASN A 231 ? 0.8733 1.4390 0.9585 0.2131  0.0341  -0.0687 527 ASN A CA  
1768 C C   . ASN A 231 ? 0.8953 1.5520 0.9915 0.2486  0.0401  -0.0692 527 ASN A C   
1769 O O   . ASN A 231 ? 0.8236 1.5279 0.9023 0.2893  0.0485  -0.0763 527 ASN A O   
1770 C CB  . ASN A 231 ? 0.9943 1.5467 1.0507 0.2243  0.0401  -0.0759 527 ASN A CB  
1771 C CG  . ASN A 231 ? 1.0333 1.5339 1.0429 0.2783  0.0395  -0.0909 527 ASN A CG  
1772 O OD1 . ASN A 231 ? 1.0412 1.4518 1.0255 0.2864  0.0300  -0.0967 527 ASN A OD1 
1773 N ND2 . ASN A 231 ? 1.0644 1.6184 1.0556 0.3146  0.0499  -0.0972 527 ASN A ND2 
1774 N N   . GLY A 232 ? 0.8518 1.5372 0.9759 0.2348  0.0355  -0.0617 528 GLY A N   
1775 C CA  . GLY A 232 ? 0.9152 1.6911 1.0522 0.2678  0.0387  -0.0615 528 GLY A CA  
1776 C C   . GLY A 232 ? 0.9119 1.8241 1.0741 0.2570  0.0500  -0.0556 528 GLY A C   
1777 O O   . GLY A 232 ? 0.9897 1.9964 1.1634 0.2892  0.0533  -0.0563 528 GLY A O   
1778 N N   . ASN A 233 ? 0.7917 1.7210 0.9599 0.2121  0.0558  -0.0494 529 ASN A N   
1779 C CA  . ASN A 233 ? 0.7694 1.8292 0.9565 0.1932  0.0673  -0.0428 529 ASN A CA  
1780 C C   . ASN A 233 ? 0.7515 1.8735 0.9699 0.1385  0.0643  -0.0292 529 ASN A C   
1781 O O   . ASN A 233 ? 0.8721 1.9214 1.0947 0.1074  0.0540  -0.0239 529 ASN A O   
1782 C CB  . ASN A 233 ? 0.6776 1.7240 0.8489 0.1648  0.0748  -0.0410 529 ASN A CB  
1783 C CG  . ASN A 233 ? 0.7810 1.8173 0.9223 0.2195  0.0820  -0.0543 529 ASN A CG  
1784 O OD1 . ASN A 233 ? 0.9163 2.0576 1.0589 0.2445  0.0939  -0.0569 529 ASN A OD1 
1785 N ND2 . ASN A 233 ? 0.6899 1.6026 0.8010 0.2372  0.0747  -0.0630 529 ASN A ND2 
1786 N N   . ASP A 234 ? 0.8122 2.0623 1.0447 0.1243  0.0721  -0.0234 530 ASP A N   
1787 C CA  . ASP A 234 ? 0.8770 2.1679 1.1214 0.0654  0.0662  -0.0103 530 ASP A CA  
1788 C C   . ASP A 234 ? 0.8373 2.0758 1.0815 -0.0035 0.0660  -0.0003 530 ASP A C   
1789 O O   . ASP A 234 ? 0.8532 2.0505 1.0755 -0.0176 0.0711  0.0001  530 ASP A O   
1790 C CB  . ASP A 234 ? 0.9439 2.3417 1.1776 0.0530  0.0688  -0.0055 530 ASP A CB  
1791 C CG  . ASP A 234 ? 0.9395 2.3870 1.1634 0.1247  0.0674  -0.0149 530 ASP A CG  
1792 O OD1 . ASP A 234 ? 1.0090 2.5377 1.2205 0.1341  0.0717  -0.0152 530 ASP A OD1 
1793 O OD2 . ASP A 234 ? 0.8911 2.2948 1.1147 0.1720  0.0613  -0.0218 530 ASP A OD2 
1794 N N   . PRO A 235 ? 0.6475 1.8499 0.8960 -0.0448 0.0560  0.0077  531 PRO A N   
1795 C CA  . PRO A 235 ? 0.6146 1.7100 0.8368 -0.0988 0.0497  0.0157  531 PRO A CA  
1796 C C   . PRO A 235 ? 0.6960 1.8381 0.8984 -0.1646 0.0562  0.0279  531 PRO A C   
1797 O O   . PRO A 235 ? 0.7029 1.9518 0.9091 -0.1817 0.0611  0.0320  531 PRO A O   
1798 C CB  . PRO A 235 ? 0.6896 1.7439 0.9194 -0.1147 0.0375  0.0193  531 PRO A CB  
1799 C CG  . PRO A 235 ? 0.6389 1.8226 0.8987 -0.1043 0.0396  0.0197  531 PRO A CG  
1800 C CD  . PRO A 235 ? 0.5872 1.8244 0.8503 -0.0404 0.0476  0.0093  531 PRO A CD  
1801 N N   . GLU A 236 ? 0.7317 1.7671 0.8973 -0.1992 0.0524  0.0334  532 GLU A N   
1802 C CA  . GLU A 236 ? 0.7174 1.7639 0.8474 -0.2614 0.0576  0.0452  532 GLU A CA  
1803 C C   . GLU A 236 ? 0.7252 1.6616 0.8123 -0.3146 0.0463  0.0553  532 GLU A C   
1804 O O   . GLU A 236 ? 0.8061 1.6361 0.8870 -0.2935 0.0360  0.0513  532 GLU A O   
1805 C CB  . GLU A 236 ? 0.7851 1.8050 0.8960 -0.2435 0.0656  0.0416  532 GLU A CB  
1806 C CG  . GLU A 236 ? 0.8258 1.9469 0.9669 -0.1897 0.0775  0.0311  532 GLU A CG  
1807 C CD  . GLU A 236 ? 0.9999 2.0638 1.1227 -0.1563 0.0818  0.0234  532 GLU A CD  
1808 O OE1 . GLU A 236 ? 0.9830 1.9837 1.0686 -0.1917 0.0814  0.0304  532 GLU A OE1 
1809 O OE2 . GLU A 236 ? 1.0524 2.1297 1.1922 -0.0937 0.0846  0.0101  532 GLU A OE2 
1810 N N   . LEU A 237 ? 0.7235 1.6836 0.7741 -0.3842 0.0485  0.0684  533 LEU A N   
1811 C CA  . LEU A 237 ? 0.7939 1.6496 0.7897 -0.4389 0.0374  0.0786  533 LEU A CA  
1812 C C   . LEU A 237 ? 0.8842 1.6169 0.8191 -0.4520 0.0349  0.0833  533 LEU A C   
1813 O O   . LEU A 237 ? 0.8338 1.5931 0.7518 -0.4627 0.0441  0.0863  533 LEU A O   
1814 C CB  . LEU A 237 ? 0.8783 1.7963 0.8462 -0.5055 0.0362  0.0887  533 LEU A CB  
1815 C CG  . LEU A 237 ? 0.8689 1.8536 0.8693 -0.4914 0.0290  0.0839  533 LEU A CG  
1816 C CD1 . LEU A 237 ? 0.9419 1.9920 0.9074 -0.5377 0.0251  0.0889  533 LEU A CD1 
1817 C CD2 . LEU A 237 ? 0.8411 1.7344 0.8344 -0.4976 0.0176  0.0849  533 LEU A CD2 
1818 N N   . PHE A 238 ? 0.9320 1.5326 0.8313 -0.4489 0.0222  0.0839  534 PHE A N   
1819 C CA  . PHE A 238 ? 1.0791 1.5556 0.9110 -0.4594 0.0171  0.0892  534 PHE A CA  
1820 C C   . PHE A 238 ? 1.1068 1.4657 0.8758 -0.4908 0.0037  0.0962  534 PHE A C   
1821 O O   . PHE A 238 ? 1.1080 1.4465 0.9001 -0.4703 -0.0039 0.0909  534 PHE A O   
1822 C CB  . PHE A 238 ? 0.9591 1.3836 0.8129 -0.3930 0.0152  0.0781  534 PHE A CB  
1823 C CG  . PHE A 238 ? 0.9046 1.4254 0.8174 -0.3509 0.0262  0.0681  534 PHE A CG  
1824 C CD1 . PHE A 238 ? 0.8376 1.4296 0.8144 -0.3115 0.0281  0.0579  534 PHE A CD1 
1825 C CD2 . PHE A 238 ? 0.8691 1.3996 0.7658 -0.3472 0.0340  0.0685  534 PHE A CD2 
1826 C CE1 . PHE A 238 ? 0.8473 1.5137 0.8651 -0.2681 0.0375  0.0479  534 PHE A CE1 
1827 C CE2 . PHE A 238 ? 0.8161 1.4264 0.7587 -0.3055 0.0438  0.0582  534 PHE A CE2 
1828 C CZ  . PHE A 238 ? 0.7731 1.4478 0.7730 -0.2650 0.0455  0.0477  534 PHE A CZ  
1829 N N   . GLN A 239 ? 1.3025 1.5754 0.9848 -0.5372 0.0005  0.1077  535 GLN A N   
1830 C CA  . GLN A 239 ? 1.3503 1.4926 0.9505 -0.5677 -0.0127 0.1149  535 GLN A CA  
1831 C C   . GLN A 239 ? 1.3363 1.3498 0.8988 -0.5186 -0.0220 0.1111  535 GLN A C   
1832 O O   . GLN A 239 ? 1.3213 1.2981 0.8517 -0.5099 -0.0200 0.1137  535 GLN A O   
1833 C CB  . GLN A 239 ? 1.4941 1.6041 1.0039 -0.6505 -0.0121 0.1307  535 GLN A CB  
1834 C CG  . GLN A 239 ? 1.6710 1.6186 1.0742 -0.6784 -0.0268 0.1380  535 GLN A CG  
1835 C CD  . GLN A 239 ? 1.8148 1.6803 1.1109 -0.7302 -0.0315 0.1467  535 GLN A CD  
1836 O OE1 . GLN A 239 ? 1.8980 1.6232 1.1114 -0.7174 -0.0391 0.1511  535 GLN A OE1 
1837 N NE2 . GLN A 239 ? 1.8585 1.8119 1.1565 -0.7773 -0.0309 0.1443  535 GLN A NE2 
1838 N N   . ILE A 240 ? 1.2266 1.1768 0.7912 -0.4865 -0.0322 0.1051  536 ILE A N   
1839 C CA  . ILE A 240 ? 1.2984 1.1317 0.8217 -0.4404 -0.0422 0.1018  536 ILE A CA  
1840 C C   . ILE A 240 ? 1.4337 1.1408 0.8344 -0.4791 -0.0493 0.1144  536 ILE A C   
1841 O O   . ILE A 240 ? 1.4115 1.0655 0.7457 -0.5317 -0.0543 0.1227  536 ILE A O   
1842 C CB  . ILE A 240 ? 1.2649 1.0597 0.8064 -0.4047 -0.0511 0.0939  536 ILE A CB  
1843 C CG1 . ILE A 240 ? 1.2613 1.1717 0.9122 -0.3750 -0.0448 0.0831  536 ILE A CG1 
1844 C CG2 . ILE A 240 ? 1.2732 0.9714 0.7804 -0.3504 -0.0602 0.0895  536 ILE A CG2 
1845 C CD1 . ILE A 240 ? 1.2426 1.2158 0.9161 -0.4143 -0.0432 0.0854  536 ILE A CD1 
1846 N N   . PRO A 241 ? 1.5359 1.1867 0.8965 -0.4565 -0.0509 0.1163  537 PRO A N   
1847 C CA  . PRO A 241 ? 1.6752 1.1860 0.9057 -0.4855 -0.0595 0.1284  537 PRO A CA  
1848 C C   . PRO A 241 ? 1.7333 1.1259 0.8903 -0.4856 -0.0728 0.1296  537 PRO A C   
1849 O O   . PRO A 241 ? 1.7203 1.0896 0.9048 -0.4260 -0.0794 0.1197  537 PRO A O   
1850 C CB  . PRO A 241 ? 1.6668 1.1376 0.8879 -0.4287 -0.0627 0.1249  537 PRO A CB  
1851 C CG  . PRO A 241 ? 1.5660 1.1758 0.9067 -0.3980 -0.0514 0.1144  537 PRO A CG  
1852 C CD  . PRO A 241 ? 1.4394 1.1368 0.8648 -0.3962 -0.0475 0.1064  537 PRO A CD  
1853 N N   . PRO A 242 ? 1.8244 1.1422 0.8845 -0.5535 -0.0768 0.1413  538 PRO A N   
1854 C CA  . PRO A 242 ? 1.8724 1.0800 0.8611 -0.5572 -0.0892 0.1413  538 PRO A CA  
1855 C C   . PRO A 242 ? 2.0117 1.0789 0.9246 -0.4924 -0.1022 0.1381  538 PRO A C   
1856 O O   . PRO A 242 ? 2.1144 1.1181 1.0024 -0.4658 -0.1110 0.1327  538 PRO A O   
1857 C CB  . PRO A 242 ? 1.9409 1.1163 0.8519 -0.6302 -0.0943 0.1414  538 PRO A CB  
1858 C CG  . PRO A 242 ? 1.9133 1.2165 0.8793 -0.6746 -0.0810 0.1462  538 PRO A CG  
1859 C CD  . PRO A 242 ? 1.8189 1.1496 0.8266 -0.6311 -0.0707 0.1537  538 PRO A CD  
1860 N N   . GLU A 243 ? 1.9747 0.9976 0.8505 -0.4625 -0.1038 0.1409  539 GLU A N   
1861 C CA  . GLU A 243 ? 1.9969 0.9107 0.8138 -0.3892 -0.1162 0.1365  539 GLU A CA  
1862 C C   . GLU A 243 ? 1.9123 0.9135 0.8441 -0.3135 -0.1153 0.1207  539 GLU A C   
1863 O O   . GLU A 243 ? 1.9344 0.8626 0.8273 -0.2519 -0.1256 0.1153  539 GLU A O   
1864 C CB  . GLU A 243 ? 2.1431 1.0017 0.8975 -0.3755 -0.1183 0.1435  539 GLU A CB  
1865 C CG  . GLU A 243 ? 1.9828 0.9799 0.8499 -0.3569 -0.1068 0.1387  539 GLU A CG  
1866 C CD  . GLU A 243 ? 2.0228 1.0864 0.8995 -0.4315 -0.0941 0.1484  539 GLU A CD  
1867 O OE1 . GLU A 243 ? 2.0064 1.1011 0.8844 -0.4957 -0.0889 0.1532  539 GLU A OE1 
1868 O OE2 . GLU A 243 ? 1.9218 1.0121 0.8038 -0.4261 -0.0893 0.1512  539 GLU A OE2 
1869 N N   . LEU A 244 ? 1.7018 0.8566 0.7678 -0.3159 -0.1034 0.1134  540 LEU A N   
1870 C CA  . LEU A 244 ? 1.6042 0.8398 0.7739 -0.2553 -0.1022 0.0993  540 LEU A CA  
1871 C C   . LEU A 244 ? 1.5217 0.7681 0.7175 -0.2608 -0.1035 0.0943  540 LEU A C   
1872 O O   . LEU A 244 ? 1.4217 0.7217 0.6911 -0.2126 -0.1033 0.0833  540 LEU A O   
1873 C CB  . LEU A 244 ? 1.5660 0.9475 0.8566 -0.2512 -0.0898 0.0932  540 LEU A CB  
1874 C CG  . LEU A 244 ? 1.5767 0.9708 0.8654 -0.2344 -0.0877 0.0946  540 LEU A CG  
1875 C CD1 . LEU A 244 ? 1.4257 0.9578 0.8230 -0.2412 -0.0746 0.0888  540 LEU A CD1 
1876 C CD2 . LEU A 244 ? 1.6436 0.9980 0.9213 -0.1644 -0.0976 0.0878  540 LEU A CD2 
1877 N N   . VAL A 245 ? 1.6153 0.8159 0.7521 -0.3215 -0.1048 0.1023  541 VAL A N   
1878 C CA  . VAL A 245 ? 1.6388 0.8512 0.7970 -0.3332 -0.1064 0.0982  541 VAL A CA  
1879 C C   . VAL A 245 ? 1.7398 0.7944 0.7740 -0.3207 -0.1198 0.1001  541 VAL A C   
1880 O O   . VAL A 245 ? 1.8613 0.8128 0.7839 -0.3732 -0.1255 0.1103  541 VAL A O   
1881 C CB  . VAL A 245 ? 1.6156 0.8972 0.7965 -0.4092 -0.0995 0.1045  541 VAL A CB  
1882 C CG1 . VAL A 245 ? 1.5617 0.8557 0.7643 -0.4173 -0.1025 0.0998  541 VAL A CG1 
1883 C CG2 . VAL A 245 ? 1.4968 0.9311 0.7918 -0.4117 -0.0861 0.1018  541 VAL A CG2 
1884 N N   . LEU A 246 ? 1.6960 0.7314 0.7448 -0.2516 -0.1249 0.0902  542 LEU A N   
1885 C CA  . LEU A 246 ? 1.7872 0.6795 0.7224 -0.2238 -0.1374 0.0896  542 LEU A CA  
1886 C C   . LEU A 246 ? 1.8252 0.7018 0.7507 -0.2559 -0.1393 0.0878  542 LEU A C   
1887 O O   . LEU A 246 ? 1.6677 0.6566 0.7011 -0.2545 -0.1324 0.0810  542 LEU A O   
1888 C CB  . LEU A 246 ? 1.8663 0.7628 0.8255 -0.1337 -0.1412 0.0791  542 LEU A CB  
1889 C CG  . LEU A 246 ? 2.0261 0.7977 0.8842 -0.0854 -0.1529 0.0751  542 LEU A CG  
1890 C CD1 . LEU A 246 ? 2.1923 0.8103 0.8989 -0.0845 -0.1632 0.0796  542 LEU A CD1 
1891 C CD2 . LEU A 246 ? 2.0174 0.8563 0.9438 -0.0014 -0.1527 0.0630  542 LEU A CD2 
1892 N N   . GLU A 247 ? 2.0070 0.7456 0.8007 -0.2840 -0.1490 0.0920  543 GLU A N   
1893 C CA  . GLU A 247 ? 2.0131 0.7471 0.7946 -0.3175 -0.1516 0.0862  543 GLU A CA  
1894 C C   . GLU A 247 ? 2.1604 0.7719 0.8320 -0.2752 -0.1628 0.0741  543 GLU A C   
1895 O O   . GLU A 247 ? 2.2506 0.7722 0.8319 -0.2485 -0.1692 0.0697  543 GLU A O   
1896 C CB  . GLU A 247 ? 2.0839 0.8553 0.8528 -0.4062 -0.1495 0.0910  543 GLU A CB  
1897 C CG  . GLU A 247 ? 1.9685 0.8847 0.8564 -0.4461 -0.1367 0.1003  543 GLU A CG  
1898 C CD  . GLU A 247 ? 2.1087 1.0807 0.9866 -0.5264 -0.1349 0.1035  543 GLU A CD  
1899 O OE1 . GLU A 247 ? 2.1564 1.0912 0.9755 -0.5563 -0.1426 0.0993  543 GLU A OE1 
1900 O OE2 . GLU A 247 ? 2.1700 1.2240 1.0930 -0.5583 -0.1263 0.1103  543 GLU A OE2 
1901 N N   . VAL A 248 ? 2.0256 0.6362 0.7046 -0.2673 -0.1648 0.0682  544 VAL A N   
1902 C CA  . VAL A 248 ? 2.1837 0.6913 0.7666 -0.2224 -0.1737 0.0565  544 VAL A CA  
1903 C C   . VAL A 248 ? 2.2791 0.7442 0.7913 -0.2843 -0.1795 0.0556  544 VAL A C   
1904 O O   . VAL A 248 ? 2.1943 0.7349 0.7731 -0.3246 -0.1756 0.0595  544 VAL A O   
1905 C CB  . VAL A 248 ? 2.1329 0.6738 0.7767 -0.1524 -0.1715 0.0499  544 VAL A CB  
1906 C CG1 . VAL A 248 ? 2.2362 0.6774 0.7754 -0.1084 -0.1795 0.0376  544 VAL A CG1 
1907 C CG2 . VAL A 248 ? 2.0802 0.6707 0.7905 -0.0893 -0.1674 0.0511  544 VAL A CG2 
1908 N N   . PRO A 249 ? 2.4246 0.7706 0.7988 -0.2932 -0.1894 0.0504  545 PRO A N   
1909 C CA  . PRO A 249 ? 2.5023 0.7990 0.7953 -0.3494 -0.1967 0.0503  545 PRO A CA  
1910 C C   . PRO A 249 ? 2.5636 0.8126 0.8226 -0.3027 -0.2007 0.0424  545 PRO A C   
1911 O O   . PRO A 249 ? 2.6399 0.8288 0.8575 -0.2272 -0.2031 0.0331  545 PRO A O   
1912 C CB  . PRO A 249 ? 2.6608 0.8372 0.8091 -0.3723 -0.2066 0.0472  545 PRO A CB  
1913 C CG  . PRO A 249 ? 2.6666 0.8255 0.8219 -0.3172 -0.2042 0.0440  545 PRO A CG  
1914 C CD  . PRO A 249 ? 2.6010 0.8491 0.8807 -0.2522 -0.1952 0.0441  545 PRO A CD  
1915 N N   . ILE A 250 ? 2.6200 0.9051 0.8996 -0.3461 -0.2009 0.0461  546 ILE A N   
1916 C CA  . ILE A 250 ? 2.5503 0.8197 0.8292 -0.3063 -0.2021 0.0404  546 ILE A CA  
1917 C C   . ILE A 250 ? 2.6980 0.8319 0.8160 -0.3152 -0.2142 0.0368  546 ILE A C   
1918 O O   . ILE A 250 ? 2.8541 0.9701 0.9184 -0.3865 -0.2195 0.0433  546 ILE A O   
1919 C CB  . ILE A 250 ? 2.4538 0.8393 0.8477 -0.3443 -0.1956 0.0460  546 ILE A CB  
1920 C CG1 . ILE A 250 ? 2.2229 0.7370 0.7607 -0.3497 -0.1847 0.0509  546 ILE A CG1 
1921 C CG2 . ILE A 250 ? 2.2861 0.6614 0.6919 -0.2947 -0.1957 0.0389  546 ILE A CG2 
1922 C CD1 . ILE A 250 ? 2.1570 0.6869 0.7528 -0.2703 -0.1795 0.0449  546 ILE A CD1 
1923 N N   . ARG A 251 ? 2.7534 0.7966 0.7924 -0.2414 -0.2185 0.0267  547 ARG A N   
1924 C CA  . ARG A 251 ? 2.9461 0.8749 0.8680 -0.2334 -0.2252 0.0245  547 ARG A CA  
1925 C C   . ARG A 251 ? 2.9139 0.8388 0.8443 -0.1685 -0.2241 0.0176  547 ARG A C   
1926 O O   . ARG A 251 ? 2.7384 0.7276 0.7442 -0.1097 -0.2187 0.0118  547 ARG A O   
1927 C CB  . ARG A 251 ? 3.1247 0.9453 0.9416 -0.2018 -0.2300 0.0198  547 ARG A CB  
1928 C CG  . ARG A 251 ? 3.0893 0.9096 0.9203 -0.1057 -0.2272 0.0097  547 ARG A CG  
1929 C CD  . ARG A 251 ? 3.0178 0.9126 0.9270 -0.1062 -0.2224 0.0104  547 ARG A CD  
1930 N NE  . ARG A 251 ? 2.9750 0.8519 0.8713 -0.0218 -0.2216 0.0014  547 ARG A NE  
1931 C CZ  . ARG A 251 ? 2.9488 0.8862 0.9090 -0.0036 -0.2177 0.0003  547 ARG A CZ  
1932 N NH1 . ARG A 251 ? 2.9700 0.8947 0.9143 0.0745  -0.2173 -0.0079 547 ARG A NH1 
1933 N NH2 . ARG A 251 ? 2.7837 0.8133 0.8496 -0.0630 -0.2112 0.0113  547 ARG A NH2 
1934 N N   . HIS A 252 ? 3.0522 0.9001 0.9001 -0.1811 -0.2294 0.0186  548 HIS A N   
1935 C CA  . HIS A 252 ? 3.0112 0.8445 0.8530 -0.1146 -0.2285 0.0117  548 HIS A CA  
1936 C C   . HIS A 252 ? 3.1070 0.8348 0.8435 -0.0446 -0.2325 0.0039  548 HIS A C   
1937 O O   . HIS A 252 ? 3.1912 0.8245 0.8282 -0.0657 -0.2388 0.0055  548 HIS A O   
1938 C CB  . HIS A 252 ? 3.0087 0.8272 0.8293 -0.1599 -0.2315 0.0169  548 HIS A CB  
1939 C CG  . HIS A 252 ? 3.1563 1.0142 1.0245 -0.1077 -0.2277 0.0117  548 HIS A CG  
1940 N ND1 . HIS A 252 ? 3.2518 1.0414 1.0531 -0.0382 -0.2293 0.0044  548 HIS A ND1 
1941 C CD2 . HIS A 252 ? 3.0202 0.9803 0.9947 -0.1144 -0.2223 0.0126  548 HIS A CD2 
1942 C CE1 . HIS A 252 ? 3.1253 0.9770 0.9921 -0.0051 -0.2245 0.0011  548 HIS A CE1 
1943 N NE2 . HIS A 252 ? 3.0051 0.9563 0.9753 -0.0507 -0.2205 0.0057  548 HIS A NE2 
1944 N N   . PRO A 253 ? 3.1477 0.8934 0.9025 0.0401  -0.2290 -0.0045 549 PRO A N   
1945 C CA  . PRO A 253 ? 3.3135 0.9674 0.9668 0.1115  -0.2329 -0.0117 549 PRO A CA  
1946 C C   . PRO A 253 ? 3.5420 1.0893 1.0845 0.1047  -0.2399 -0.0105 549 PRO A C   
1947 O O   . PRO A 253 ? 3.6676 1.1441 1.1280 0.1711  -0.2430 -0.0166 549 PRO A O   
1948 C CB  . PRO A 253 ? 3.2016 0.9439 0.9335 0.1999  -0.2254 -0.0203 549 PRO A CB  
1949 C CG  . PRO A 253 ? 2.9765 0.8218 0.8206 0.1713  -0.2195 -0.0175 549 PRO A CG  
1950 C CD  . PRO A 253 ? 2.9679 0.8315 0.8436 0.0775  -0.2209 -0.0082 549 PRO A CD  
1951 N N   . LYS A 254 ? 3.5255 1.0619 1.0615 0.0278  -0.2427 -0.0026 550 LYS A N   
1952 C CA  . LYS A 254 ? 3.6357 1.0646 1.0598 0.0123  -0.2502 -0.0004 550 LYS A CA  
1953 C C   . LYS A 254 ? 3.6352 1.0164 1.0070 -0.0887 -0.2566 0.0095  550 LYS A C   
1954 O O   . LYS A 254 ? 3.8227 1.0802 1.0642 -0.1061 -0.2652 0.0112  550 LYS A O   
1955 C CB  . LYS A 254 ? 3.6108 1.0832 1.0801 0.0316  -0.2469 -0.0014 550 LYS A CB  
1956 C CG  . LYS A 254 ? 3.5648 1.1132 1.1067 0.1226  -0.2392 -0.0102 550 LYS A CG  
1957 C CD  . LYS A 254 ? 3.7460 1.2152 1.1929 0.2076  -0.2422 -0.0177 550 LYS A CD  
1958 C CE  . LYS A 254 ? 3.6826 1.2438 1.2054 0.2952  -0.2341 -0.0258 550 LYS A CE  
1959 N NZ  . LYS A 254 ? 3.7878 1.2945 1.2292 0.3826  -0.2364 -0.0331 550 LYS A NZ  
1960 N N   . PHE A 255 ? 3.4323 0.9136 0.9022 -0.1552 -0.2525 0.0162  551 PHE A N   
1961 C CA  . PHE A 255 ? 3.5427 1.0144 0.9864 -0.2541 -0.2571 0.0265  551 PHE A CA  
1962 C C   . PHE A 255 ? 3.5978 1.0730 1.0334 -0.3055 -0.2582 0.0308  551 PHE A C   
1963 O O   . PHE A 255 ? 3.4830 1.0659 1.0247 -0.3237 -0.2518 0.0329  551 PHE A O   
1964 C CB  . PHE A 255 ? 3.4863 1.0761 1.0437 -0.2927 -0.2519 0.0315  551 PHE A CB  
1965 C CG  . PHE A 255 ? 3.5363 1.1293 1.1090 -0.2413 -0.2501 0.0268  551 PHE A CG  
1966 C CD1 . PHE A 255 ? 3.4187 1.1021 1.0960 -0.1820 -0.2421 0.0205  551 PHE A CD1 
1967 C CD2 . PHE A 255 ? 3.6173 1.1218 1.0965 -0.2536 -0.2567 0.0287  551 PHE A CD2 
1968 C CE1 . PHE A 255 ? 3.3215 1.0110 1.0120 -0.1358 -0.2402 0.0160  551 PHE A CE1 
1969 C CE2 . PHE A 255 ? 3.5954 1.1032 1.0875 -0.2065 -0.2549 0.0244  551 PHE A CE2 
1970 C CZ  . PHE A 255 ? 3.4440 1.0460 1.0426 -0.1476 -0.2464 0.0180  551 PHE A CZ  
1971 N N   . ASP A 256 ? 3.7991 1.1539 1.1043 -0.3308 -0.2666 0.0325  552 ASP A N   
1972 C CA  . ASP A 256 ? 3.8492 1.1980 1.1352 -0.3791 -0.2681 0.0362  552 ASP A CA  
1973 C C   . ASP A 256 ? 3.7466 1.1666 1.0710 -0.4824 -0.2679 0.0472  552 ASP A C   
1974 O O   . ASP A 256 ? 3.7659 1.2090 1.0964 -0.5273 -0.2675 0.0510  552 ASP A O   
1975 C CB  . ASP A 256 ? 4.1650 1.3553 1.2917 -0.3682 -0.2775 0.0335  552 ASP A CB  
1976 C CG  . ASP A 256 ? 4.2694 1.4184 1.3758 -0.2733 -0.2763 0.0232  552 ASP A CG  
1977 O OD1 . ASP A 256 ? 4.3052 1.4037 1.3712 -0.2010 -0.2776 0.0167  552 ASP A OD1 
1978 O OD2 . ASP A 256 ? 4.2394 1.4136 1.3732 -0.2700 -0.2739 0.0219  552 ASP A OD2 
1979 N N   . TRP A 257 ? 3.6790 1.1397 1.0296 -0.5208 -0.2681 0.0526  553 TRP A N   
1980 C CA  . TRP A 257 ? 3.5915 1.1593 1.0101 -0.6093 -0.2657 0.0628  553 TRP A CA  
1981 C C   . TRP A 257 ? 3.3819 1.1015 0.9545 -0.6004 -0.2556 0.0630  553 TRP A C   
1982 O O   . TRP A 257 ? 3.2709 1.0950 0.9101 -0.6676 -0.2525 0.0711  553 TRP A O   
1983 C CB  . TRP A 257 ? 3.6149 1.1921 1.0234 -0.6500 -0.2686 0.0686  553 TRP A CB  
1984 C CG  . TRP A 257 ? 3.6056 1.1953 1.0587 -0.5838 -0.2655 0.0626  553 TRP A CG  
1985 C CD1 . TRP A 257 ? 3.7447 1.2223 1.1109 -0.5269 -0.2701 0.0564  553 TRP A CD1 
1986 C CD2 . TRP A 257 ? 3.4311 1.1528 1.0233 -0.5669 -0.2574 0.0622  553 TRP A CD2 
1987 N NE1 . TRP A 257 ? 3.6213 1.1571 1.0665 -0.4764 -0.2648 0.0521  553 TRP A NE1 
1988 C CE2 . TRP A 257 ? 3.4503 1.1321 1.0326 -0.5008 -0.2573 0.0554  553 TRP A CE2 
1989 C CE3 . TRP A 257 ? 3.2677 1.1367 0.9879 -0.6005 -0.2503 0.0670  553 TRP A CE3 
1990 C CZ2 . TRP A 257 ? 3.2684 1.0486 0.9624 -0.4705 -0.2507 0.0530  553 TRP A CZ2 
1991 C CZ3 . TRP A 257 ? 3.1094 1.0719 0.9377 -0.5694 -0.2442 0.0648  553 TRP A CZ3 
1992 C CH2 . TRP A 257 ? 3.1228 1.0388 0.9366 -0.5064 -0.2446 0.0578  553 TRP A CH2 
1993 N N   . PHE A 258 ? 3.3654 1.1009 0.9922 -0.5184 -0.2507 0.0544  554 PHE A N   
1994 C CA  . PHE A 258 ? 3.2681 1.1379 1.0347 -0.5049 -0.2418 0.0541  554 PHE A CA  
1995 C C   . PHE A 258 ? 3.2016 1.1133 0.9924 -0.5413 -0.2395 0.0576  554 PHE A C   
1996 O O   . PHE A 258 ? 3.1185 1.1536 1.0087 -0.5828 -0.2339 0.0636  554 PHE A O   
1997 C CB  . PHE A 258 ? 3.2676 1.1318 1.0692 -0.4076 -0.2379 0.0436  554 PHE A CB  
1998 C CG  . PHE A 258 ? 3.0848 1.0684 1.0135 -0.3914 -0.2309 0.0432  554 PHE A CG  
1999 C CD1 . PHE A 258 ? 3.0600 1.0497 1.0008 -0.3763 -0.2311 0.0420  554 PHE A CD1 
2000 C CD2 . PHE A 258 ? 3.0069 1.0936 1.0391 -0.3928 -0.2246 0.0443  554 PHE A CD2 
2001 C CE1 . PHE A 258 ? 2.8613 0.9565 0.9143 -0.3629 -0.2254 0.0415  554 PHE A CE1 
2002 C CE2 . PHE A 258 ? 2.8838 1.0844 1.0475 -0.3773 -0.2167 0.0436  554 PHE A CE2 
2003 C CZ  . PHE A 258 ? 2.7761 0.9825 0.9540 -0.3624 -0.2168 0.0416  554 PHE A CZ  
2004 N N   . LYS A 259 ? 3.2327 1.0436 0.9321 -0.5242 -0.2437 0.0539  555 LYS A N   
2005 C CA  . LYS A 259 ? 3.3299 1.1716 1.0424 -0.5612 -0.2420 0.0572  555 LYS A CA  
2006 C C   . LYS A 259 ? 3.3432 1.2499 1.0663 -0.6603 -0.2425 0.0682  555 LYS A C   
2007 O O   . LYS A 259 ? 3.1746 1.1857 0.9755 -0.6975 -0.2370 0.0730  555 LYS A O   
2008 C CB  . LYS A 259 ? 3.5104 1.2164 1.1019 -0.5341 -0.2483 0.0520  555 LYS A CB  
2009 C CG  . LYS A 259 ? 3.6332 1.2385 1.1601 -0.4450 -0.2514 0.0421  555 LYS A CG  
2010 C CD  . LYS A 259 ? 3.7828 1.2793 1.2138 -0.4060 -0.2559 0.0361  555 LYS A CD  
2011 C CE  . LYS A 259 ? 3.8567 1.2735 1.2333 -0.3109 -0.2581 0.0262  555 LYS A CE  
2012 N NZ  . LYS A 259 ? 3.6843 1.1939 1.1669 -0.2629 -0.2513 0.0230  555 LYS A NZ  
2013 N N   . ASP A 260 ? 3.4858 1.3374 1.1313 -0.7029 -0.2489 0.0723  556 ASP A N   
2014 C CA  . ASP A 260 ? 3.5519 1.4700 1.2023 -0.7968 -0.2496 0.0828  556 ASP A CA  
2015 C C   . ASP A 260 ? 3.3167 1.4085 1.1132 -0.8185 -0.2410 0.0881  556 ASP A C   
2016 O O   . ASP A 260 ? 3.2200 1.4125 1.0607 -0.8833 -0.2379 0.0958  556 ASP A O   
2017 C CB  . ASP A 260 ? 3.7631 1.5906 1.3064 -0.8314 -0.2582 0.0860  556 ASP A CB  
2018 C CG  . ASP A 260 ? 3.9858 1.6486 1.3710 -0.8370 -0.2678 0.0836  556 ASP A CG  
2019 O OD1 . ASP A 260 ? 4.0373 1.6894 1.3925 -0.8692 -0.2687 0.0852  556 ASP A OD1 
2020 O OD2 . ASP A 260 ? 4.1223 1.6646 1.4096 -0.8094 -0.2746 0.0803  556 ASP A OD2 
2021 N N   . LEU A 261 ? 3.1935 1.3248 1.0642 -0.7634 -0.2370 0.0840  557 LEU A N   
2022 C CA  . LEU A 261 ? 3.0690 1.3600 1.0779 -0.7752 -0.2289 0.0882  557 LEU A CA  
2023 C C   . LEU A 261 ? 3.1209 1.5039 1.2054 -0.7847 -0.2223 0.0899  557 LEU A C   
2024 O O   . LEU A 261 ? 3.0460 1.5680 1.2204 -0.8268 -0.2165 0.0967  557 LEU A O   
2025 C CB  . LEU A 261 ? 2.8933 1.1935 0.9600 -0.7051 -0.2263 0.0817  557 LEU A CB  
2026 C CG  . LEU A 261 ? 2.9231 1.1767 0.9533 -0.6960 -0.2305 0.0808  557 LEU A CG  
2027 C CD1 . LEU A 261 ? 2.7341 0.9867 0.8146 -0.6167 -0.2277 0.0724  557 LEU A CD1 
2028 C CD2 . LEU A 261 ? 2.9140 1.2702 0.9902 -0.7655 -0.2296 0.0907  557 LEU A CD2 
2029 N N   . GLY A 262 ? 3.2417 1.5517 1.2892 -0.7446 -0.2230 0.0837  558 GLY A N   
2030 C CA  . GLY A 262 ? 3.2121 1.5928 1.3149 -0.7568 -0.2175 0.0854  558 GLY A CA  
2031 C C   . GLY A 262 ? 3.0053 1.5206 1.2578 -0.7278 -0.2072 0.0857  558 GLY A C   
2032 O O   . GLY A 262 ? 2.9656 1.6159 1.3133 -0.7681 -0.1991 0.0924  558 GLY A O   
2033 N N   . LEU A 263 ? 2.8475 1.3388 1.1420 -0.6524 -0.2043 0.0784  559 LEU A N   
2034 C CA  . LEU A 263 ? 2.4631 1.0766 0.9150 -0.6162 -0.1923 0.0778  559 LEU A CA  
2035 C C   . LEU A 263 ? 2.4110 0.9962 0.8846 -0.5553 -0.1884 0.0728  559 LEU A C   
2036 O O   . LEU A 263 ? 2.4181 0.8792 0.7899 -0.5156 -0.1954 0.0663  559 LEU A O   
2037 C CB  . LEU A 263 ? 2.3537 0.9802 0.8488 -0.5817 -0.1917 0.0735  559 LEU A CB  
2038 C CG  . LEU A 263 ? 2.2984 0.9590 0.7795 -0.6379 -0.1952 0.0791  559 LEU A CG  
2039 C CD1 . LEU A 263 ? 2.2370 0.8756 0.7334 -0.5956 -0.1965 0.0731  559 LEU A CD1 
2040 C CD2 . LEU A 263 ? 2.1149 0.9390 0.7098 -0.6893 -0.1870 0.0867  559 LEU A CD2 
2041 N N   . LYS A 264 ? 2.3612 1.0645 0.9644 -0.5478 -0.1775 0.0758  560 LYS A N   
2042 C CA  . LYS A 264 ? 2.3047 1.0032 0.9466 -0.4937 -0.1724 0.0736  560 LYS A CA  
2043 C C   . LYS A 264 ? 2.0582 0.8927 0.8524 -0.4823 -0.1611 0.0759  560 LYS A C   
2044 O O   . LYS A 264 ? 1.9147 0.8572 0.7817 -0.5263 -0.1565 0.0798  560 LYS A O   
2045 C CB  . LYS A 264 ? 2.3728 1.0444 0.9647 -0.5198 -0.1730 0.0777  560 LYS A CB  
2046 C CG  . LYS A 264 ? 2.4061 1.1849 1.0420 -0.5967 -0.1678 0.0866  560 LYS A CG  
2047 C CD  . LYS A 264 ? 2.5276 1.2861 1.1258 -0.6151 -0.1670 0.0898  560 LYS A CD  
2048 C CE  . LYS A 264 ? 2.5185 1.3888 1.1534 -0.6902 -0.1618 0.0977  560 LYS A CE  
2049 N NZ  . LYS A 264 ? 2.4870 1.3724 1.1236 -0.7016 -0.1571 0.1014  560 LYS A NZ  
2050 N N   . TRP A 265 ? 1.9653 0.7953 0.8033 -0.4204 -0.1573 0.0729  561 TRP A N   
2051 C CA  . TRP A 265 ? 1.8299 0.7765 0.8014 -0.4092 -0.1477 0.0745  561 TRP A CA  
2052 C C   . TRP A 265 ? 1.8176 0.7693 0.8122 -0.3675 -0.1431 0.0762  561 TRP A C   
2053 O O   . TRP A 265 ? 1.8549 0.6957 0.7559 -0.3391 -0.1492 0.0769  561 TRP A O   
2054 C CB  . TRP A 265 ? 1.6333 0.6033 0.6597 -0.3646 -0.1475 0.0653  561 TRP A CB  
2055 C CG  . TRP A 265 ? 1.4703 0.6152 0.6498 -0.3622 -0.1368 0.0617  561 TRP A CG  
2056 C CD1 . TRP A 265 ? 1.4907 0.7272 0.7736 -0.3041 -0.1285 0.0545  561 TRP A CD1 
2057 C CD2 . TRP A 265 ? 1.5289 0.7714 0.7637 -0.4204 -0.1343 0.0654  561 TRP A CD2 
2058 N NE1 . TRP A 265 ? 1.3973 0.7680 0.7890 -0.3200 -0.1212 0.0534  561 TRP A NE1 
2059 C CE2 . TRP A 265 ? 1.4005 0.7821 0.7676 -0.3872 -0.1245 0.0599  561 TRP A CE2 
2060 C CE3 . TRP A 265 ? 1.6650 0.8957 0.8481 -0.4952 -0.1398 0.0725  561 TRP A CE3 
2061 C CZ2 . TRP A 265 ? 1.3973 0.8990 0.8421 -0.4202 -0.1206 0.0613  561 TRP A CZ2 
2062 C CZ3 . TRP A 265 ? 1.4968 0.8641 0.7670 -0.5301 -0.1354 0.0740  561 TRP A CZ3 
2063 C CH2 . TRP A 265 ? 1.3925 0.8893 0.7901 -0.4903 -0.1263 0.0683  561 TRP A CH2 
2064 N N   . TYR A 266 ? 1.6043 0.7049 0.7294 -0.3568 -0.1321 0.0738  562 TYR A N   
2065 C CA  . TYR A 266 ? 1.6513 0.7880 0.8177 -0.3136 -0.1267 0.0724  562 TYR A CA  
2066 C C   . TYR A 266 ? 1.6125 0.7613 0.8222 -0.2323 -0.1264 0.0613  562 TYR A C   
2067 O O   . TYR A 266 ? 1.5577 0.7510 0.8210 -0.2122 -0.1249 0.0541  562 TYR A O   
2068 C CB  . TYR A 266 ? 1.4950 0.7783 0.7717 -0.3373 -0.1152 0.0741  562 TYR A CB  
2069 C CG  . TYR A 266 ? 1.3659 0.7676 0.7463 -0.3427 -0.1095 0.0688  562 TYR A CG  
2070 C CD1 . TYR A 266 ? 1.2573 0.7322 0.7302 -0.2870 -0.1045 0.0590  562 TYR A CD1 
2071 C CD2 . TYR A 266 ? 1.2994 0.7419 0.6814 -0.4052 -0.1096 0.0741  562 TYR A CD2 
2072 C CE1 . TYR A 266 ? 1.2800 0.8519 0.8375 -0.2899 -0.1000 0.0548  562 TYR A CE1 
2073 C CE2 . TYR A 266 ? 1.3403 0.8896 0.8124 -0.4043 -0.1055 0.0694  562 TYR A CE2 
2074 C CZ  . TYR A 266 ? 1.2912 0.8991 0.8481 -0.3451 -0.1007 0.0600  562 TYR A CZ  
2075 O OH  . TYR A 266 ? 1.2873 0.9914 0.9253 -0.3417 -0.0972 0.0559  562 TYR A OH  
2076 N N   . GLY A 267 ? 1.5976 0.7115 0.7825 -0.1866 -0.1281 0.0604  563 GLY A N   
2077 C CA  . GLY A 267 ? 1.5562 0.6751 0.7638 -0.1113 -0.1295 0.0506  563 GLY A CA  
2078 C C   . GLY A 267 ? 1.4053 0.6674 0.7496 -0.0852 -0.1199 0.0427  563 GLY A C   
2079 O O   . GLY A 267 ? 1.4390 0.7244 0.8140 -0.0351 -0.1199 0.0342  563 GLY A O   
2080 N N   . LEU A 268 ? 1.2869 0.6433 0.7080 -0.1185 -0.1118 0.0453  564 LEU A N   
2081 C CA  . LEU A 268 ? 1.1494 0.6215 0.6808 -0.0906 -0.1040 0.0383  564 LEU A CA  
2082 C C   . LEU A 268 ? 1.1362 0.6994 0.7512 -0.1158 -0.0971 0.0360  564 LEU A C   
2083 O O   . LEU A 268 ? 1.0925 0.6956 0.7256 -0.1609 -0.0930 0.0414  564 LEU A O   
2084 C CB  . LEU A 268 ? 1.1750 0.6791 0.7233 -0.0941 -0.1004 0.0413  564 LEU A CB  
2085 C CG  . LEU A 268 ? 1.1171 0.7169 0.7568 -0.0594 -0.0948 0.0333  564 LEU A CG  
2086 C CD1 . LEU A 268 ? 1.2079 0.7850 0.8296 -0.0021 -0.1005 0.0276  564 LEU A CD1 
2087 C CD2 . LEU A 268 ? 0.9890 0.6408 0.6614 -0.0802 -0.0887 0.0363  564 LEU A CD2 
2088 N N   . PRO A 269 ? 1.0662 0.6681 0.7312 -0.0867 -0.0956 0.0283  565 PRO A N   
2089 C CA  . PRO A 269 ? 0.9195 0.6076 0.6637 -0.1035 -0.0895 0.0260  565 PRO A CA  
2090 C C   . PRO A 269 ? 0.8798 0.6545 0.7030 -0.0877 -0.0824 0.0218  565 PRO A C   
2091 O O   . PRO A 269 ? 0.8374 0.6285 0.6848 -0.0503 -0.0819 0.0156  565 PRO A O   
2092 C CB  . PRO A 269 ? 0.9453 0.6212 0.6932 -0.0786 -0.0916 0.0202  565 PRO A CB  
2093 C CG  . PRO A 269 ? 0.9302 0.5509 0.6320 -0.0319 -0.0960 0.0164  565 PRO A CG  
2094 C CD  . PRO A 269 ? 1.0437 0.6228 0.6981 -0.0336 -0.0988 0.0213  565 PRO A CD  
2095 N N   . ALA A 270 ? 0.7765 0.6097 0.6375 -0.1158 -0.0771 0.0246  566 ALA A N   
2096 C CA  . ALA A 270 ? 0.7625 0.6616 0.6806 -0.1020 -0.0709 0.0207  566 ALA A CA  
2097 C C   . ALA A 270 ? 0.7784 0.7510 0.7510 -0.1177 -0.0654 0.0201  566 ALA A C   
2098 O O   . ALA A 270 ? 0.8607 0.8591 0.8284 -0.1489 -0.0631 0.0256  566 ALA A O   
2099 C CB  . ALA A 270 ? 0.6622 0.5454 0.5502 -0.1109 -0.0702 0.0250  566 ALA A CB  
2100 N N   . VAL A 271 ? 0.6344 0.6418 0.6544 -0.0957 -0.0635 0.0137  567 VAL A N   
2101 C CA  . VAL A 271 ? 0.6628 0.7322 0.7277 -0.1012 -0.0595 0.0126  567 VAL A CA  
2102 C C   . VAL A 271 ? 0.6380 0.7545 0.7321 -0.0928 -0.0536 0.0099  567 VAL A C   
2103 O O   . VAL A 271 ? 0.7331 0.8445 0.8375 -0.0713 -0.0526 0.0045  567 VAL A O   
2104 C CB  . VAL A 271 ? 0.6000 0.6752 0.6922 -0.0812 -0.0602 0.0073  567 VAL A CB  
2105 C CG1 . VAL A 271 ? 0.5850 0.7163 0.7195 -0.0736 -0.0561 0.0045  567 VAL A CG1 
2106 C CG2 . VAL A 271 ? 0.6195 0.6625 0.6866 -0.0935 -0.0652 0.0102  567 VAL A CG2 
2107 N N   . SER A 272 ? 0.6424 0.8105 0.7499 -0.1086 -0.0499 0.0129  568 SER A N   
2108 C CA  . SER A 272 ? 0.5389 0.7518 0.6675 -0.0980 -0.0437 0.0100  568 SER A CA  
2109 C C   . SER A 272 ? 0.5600 0.8335 0.7240 -0.0825 -0.0399 0.0063  568 SER A C   
2110 O O   . SER A 272 ? 0.6717 0.9795 0.8475 -0.0683 -0.0346 0.0029  568 SER A O   
2111 C CB  . SER A 272 ? 0.6746 0.9004 0.7783 -0.1259 -0.0408 0.0167  568 SER A CB  
2112 O OG  . SER A 272 ? 0.6918 0.9308 0.7787 -0.1605 -0.0429 0.0241  568 SER A OG  
2113 N N   . ASN A 273 ? 0.5934 0.8786 0.7696 -0.0810 -0.0429 0.0067  569 ASN A N   
2114 C CA  . ASN A 273 ? 0.6239 0.9674 0.8257 -0.0633 -0.0406 0.0043  569 ASN A CA  
2115 C C   . ASN A 273 ? 0.6526 0.9710 0.8652 -0.0314 -0.0419 -0.0026 569 ASN A C   
2116 O O   . ASN A 273 ? 0.6018 0.9538 0.8260 -0.0107 -0.0414 -0.0048 569 ASN A O   
2117 C CB  . ASN A 273 ? 0.6813 1.0672 0.8862 -0.0851 -0.0437 0.0104  569 ASN A CB  
2118 C CG  . ASN A 273 ? 0.7245 1.0602 0.9172 -0.0962 -0.0504 0.0122  569 ASN A CG  
2119 O OD1 . ASN A 273 ? 0.6099 0.8861 0.7946 -0.0847 -0.0520 0.0088  569 ASN A OD1 
2120 N ND2 . ASN A 273 ? 0.7684 1.1338 0.9588 -0.1186 -0.0545 0.0172  569 ASN A ND2 
2121 N N   . MET A 274 ? 0.5689 0.8309 0.7736 -0.0268 -0.0439 -0.0059 570 MET A N   
2122 C CA  . MET A 274 ? 0.4964 0.7315 0.7047 -0.0065 -0.0453 -0.0113 570 MET A CA  
2123 C C   . MET A 274 ? 0.5894 0.8132 0.7933 0.0124  -0.0425 -0.0183 570 MET A C   
2124 O O   . MET A 274 ? 0.5869 0.8208 0.7873 0.0114  -0.0395 -0.0195 570 MET A O   
2125 C CB  . MET A 274 ? 0.5451 0.7371 0.7469 -0.0151 -0.0489 -0.0109 570 MET A CB  
2126 C CG  . MET A 274 ? 0.5464 0.7404 0.7465 -0.0287 -0.0526 -0.0055 570 MET A CG  
2127 S SD  . MET A 274 ? 0.6335 0.7811 0.8230 -0.0308 -0.0557 -0.0063 570 MET A SD  
2128 C CE  . MET A 274 ? 0.5751 0.7196 0.7751 -0.0148 -0.0553 -0.0101 570 MET A CE  
2129 N N   . LEU A 275 ? 0.5716 0.7688 0.7692 0.0277  -0.0440 -0.0229 571 LEU A N   
2130 C CA  . LEU A 275 ? 0.5647 0.7376 0.7461 0.0434  -0.0427 -0.0302 571 LEU A CA  
2131 C C   . LEU A 275 ? 0.6445 0.7755 0.8174 0.0319  -0.0453 -0.0334 571 LEU A C   
2132 O O   . LEU A 275 ? 0.6334 0.7481 0.8069 0.0253  -0.0477 -0.0317 571 LEU A O   
2133 C CB  . LEU A 275 ? 0.5170 0.6847 0.6829 0.0699  -0.0430 -0.0331 571 LEU A CB  
2134 C CG  . LEU A 275 ? 0.7673 0.9008 0.9014 0.0915  -0.0421 -0.0411 571 LEU A CG  
2135 C CD1 . LEU A 275 ? 0.9070 1.0649 1.0296 0.1263  -0.0408 -0.0424 571 LEU A CD1 
2136 C CD2 . LEU A 275 ? 0.7863 0.8533 0.8918 0.0849  -0.0460 -0.0448 571 LEU A CD2 
2137 N N   . LEU A 276 ? 0.5688 0.6891 0.7338 0.0285  -0.0449 -0.0379 572 LEU A N   
2138 C CA  . LEU A 276 ? 0.6586 0.7537 0.8159 0.0155  -0.0478 -0.0415 572 LEU A CA  
2139 C C   . LEU A 276 ? 0.7519 0.8072 0.8779 0.0202  -0.0489 -0.0481 572 LEU A C   
2140 O O   . LEU A 276 ? 0.6801 0.7259 0.7881 0.0330  -0.0476 -0.0527 572 LEU A O   
2141 C CB  . LEU A 276 ? 0.5640 0.6727 0.7268 0.0077  -0.0484 -0.0424 572 LEU A CB  
2142 C CG  . LEU A 276 ? 0.6162 0.7151 0.7705 -0.0042 -0.0518 -0.0476 572 LEU A CG  
2143 C CD1 . LEU A 276 ? 0.6024 0.7024 0.7626 -0.0160 -0.0538 -0.0464 572 LEU A CD1 
2144 C CD2 . LEU A 276 ? 0.6681 0.7866 0.8277 -0.0054 -0.0532 -0.0475 572 LEU A CD2 
2145 N N   . GLU A 277 ? 0.6307 0.6579 0.7433 0.0090  -0.0513 -0.0486 573 GLU A N   
2146 C CA  . GLU A 277 ? 0.7534 0.7270 0.8222 0.0071  -0.0535 -0.0542 573 GLU A CA  
2147 C C   . GLU A 277 ? 0.8287 0.7942 0.8878 -0.0229 -0.0564 -0.0577 573 GLU A C   
2148 O O   . GLU A 277 ? 0.7626 0.7518 0.8411 -0.0406 -0.0568 -0.0545 573 GLU A O   
2149 C CB  . GLU A 277 ? 0.7950 0.7362 0.8437 0.0141  -0.0546 -0.0514 573 GLU A CB  
2150 C CG  . GLU A 277 ? 0.9980 0.8774 0.9913 0.0325  -0.0565 -0.0562 573 GLU A CG  
2151 C CD  . GLU A 277 ? 1.2467 1.0611 1.1924 0.0131  -0.0602 -0.0568 573 GLU A CD  
2152 O OE1 . GLU A 277 ? 1.2346 1.0330 1.1652 -0.0201 -0.0620 -0.0597 573 GLU A OE1 
2153 O OE2 . GLU A 277 ? 1.4008 1.1829 1.3221 0.0292  -0.0617 -0.0538 573 GLU A OE2 
2154 N N   . ILE A 278 ? 0.9080 0.8446 0.9351 -0.0284 -0.0585 -0.0645 574 ILE A N   
2155 C CA  . ILE A 278 ? 0.8286 0.7638 0.8424 -0.0610 -0.0623 -0.0686 574 ILE A CA  
2156 C C   . ILE A 278 ? 0.9379 0.7984 0.8856 -0.0710 -0.0659 -0.0753 574 ILE A C   
2157 O O   . ILE A 278 ? 0.9958 0.8256 0.9169 -0.0501 -0.0658 -0.0803 574 ILE A O   
2158 C CB  . ILE A 278 ? 0.7603 0.7439 0.8015 -0.0631 -0.0632 -0.0704 574 ILE A CB  
2159 C CG1 . ILE A 278 ? 0.7360 0.7791 0.8274 -0.0547 -0.0611 -0.0639 574 ILE A CG1 
2160 C CG2 . ILE A 278 ? 0.8424 0.8290 0.8646 -0.0969 -0.0685 -0.0756 574 ILE A CG2 
2161 C CD1 . ILE A 278 ? 0.6249 0.7007 0.7339 -0.0442 -0.0614 -0.0644 574 ILE A CD1 
2162 N N   . GLY A 279 ? 0.9781 0.8062 0.8931 -0.1038 -0.0691 -0.0755 575 GLY A N   
2163 C CA  . GLY A 279 ? 1.0608 0.8019 0.8976 -0.1202 -0.0738 -0.0817 575 GLY A CA  
2164 C C   . GLY A 279 ? 1.1331 0.8038 0.9231 -0.0797 -0.0733 -0.0845 575 GLY A C   
2165 O O   . GLY A 279 ? 1.2435 0.8528 0.9756 -0.0760 -0.0765 -0.0922 575 GLY A O   
2166 N N   . GLY A 280 ? 1.0764 0.7580 0.8880 -0.0467 -0.0698 -0.0790 576 GLY A N   
2167 C CA  . GLY A 280 ? 1.1916 0.8231 0.9626 -0.0013 -0.0693 -0.0816 576 GLY A CA  
2168 C C   . GLY A 280 ? 1.0869 0.7642 0.8877 0.0347  -0.0651 -0.0846 576 GLY A C   
2169 O O   . GLY A 280 ? 1.2000 0.8548 0.9738 0.0778  -0.0638 -0.0869 576 GLY A O   
2170 N N   . LEU A 281 ? 1.0027 0.7458 0.8549 0.0204  -0.0629 -0.0845 577 LEU A N   
2171 C CA  . LEU A 281 ? 1.0583 0.8502 0.9402 0.0490  -0.0581 -0.0858 577 LEU A CA  
2172 C C   . LEU A 281 ? 1.0008 0.8694 0.9487 0.0598  -0.0534 -0.0770 577 LEU A C   
2173 O O   . LEU A 281 ? 0.9155 0.8144 0.8996 0.0369  -0.0541 -0.0711 577 LEU A O   
2174 C CB  . LEU A 281 ? 1.0154 0.8294 0.9082 0.0278  -0.0591 -0.0899 577 LEU A CB  
2175 C CG  . LEU A 281 ? 1.0469 0.7921 0.8746 0.0112  -0.0645 -0.0995 577 LEU A CG  
2176 C CD1 . LEU A 281 ? 1.0733 0.8583 0.9223 -0.0047 -0.0654 -0.1026 577 LEU A CD1 
2177 C CD2 . LEU A 281 ? 1.0943 0.7692 0.8556 0.0484  -0.0640 -0.1064 577 LEU A CD2 
2178 N N   . GLU A 282 ? 1.0035 0.9060 0.9635 0.0932  -0.0487 -0.0765 578 GLU A N   
2179 C CA  . GLU A 282 ? 0.9779 0.9482 0.9894 0.1005  -0.0450 -0.0682 578 GLU A CA  
2180 C C   . GLU A 282 ? 0.8855 0.9157 0.9321 0.0980  -0.0403 -0.0663 578 GLU A C   
2181 O O   . GLU A 282 ? 0.8395 0.8823 0.8731 0.1200  -0.0364 -0.0704 578 GLU A O   
2182 C CB  . GLU A 282 ? 0.9868 0.9597 0.9832 0.1377  -0.0439 -0.0675 578 GLU A CB  
2183 C CG  . GLU A 282 ? 1.1158 1.0305 1.0789 0.1394  -0.0490 -0.0666 578 GLU A CG  
2184 C CD  . GLU A 282 ? 1.1785 1.0883 1.1151 0.1842  -0.0495 -0.0669 578 GLU A CD  
2185 O OE1 . GLU A 282 ? 1.1693 1.1188 1.1067 0.2175  -0.0456 -0.0697 578 GLU A OE1 
2186 O OE2 . GLU A 282 ? 1.2905 1.1603 1.2035 0.1877  -0.0538 -0.0642 578 GLU A OE2 
2187 N N   . PHE A 283 ? 0.7426 0.8065 0.8274 0.0730  -0.0407 -0.0600 579 PHE A N   
2188 C CA  . PHE A 283 ? 0.6243 0.7357 0.7348 0.0669  -0.0371 -0.0562 579 PHE A CA  
2189 C C   . PHE A 283 ? 0.6305 0.7898 0.7686 0.0677  -0.0344 -0.0480 579 PHE A C   
2190 O O   . PHE A 283 ? 0.7198 0.8839 0.8758 0.0510  -0.0368 -0.0421 579 PHE A O   
2191 C CB  . PHE A 283 ? 0.5924 0.7003 0.7134 0.0424  -0.0406 -0.0550 579 PHE A CB  
2192 C CG  . PHE A 283 ? 0.6374 0.7105 0.7326 0.0359  -0.0442 -0.0630 579 PHE A CG  
2193 C CD1 . PHE A 283 ? 0.7248 0.7645 0.8053 0.0219  -0.0490 -0.0660 579 PHE A CD1 
2194 C CD2 . PHE A 283 ? 0.6925 0.7671 0.7741 0.0405  -0.0429 -0.0676 579 PHE A CD2 
2195 C CE1 . PHE A 283 ? 0.7772 0.7873 0.8292 0.0086  -0.0532 -0.0734 579 PHE A CE1 
2196 C CE2 . PHE A 283 ? 0.7904 0.8330 0.8447 0.0309  -0.0474 -0.0753 579 PHE A CE2 
2197 C CZ  . PHE A 283 ? 0.7963 0.8073 0.8351 0.0133  -0.0529 -0.0783 579 PHE A CZ  
2198 N N   . SER A 284 ? 0.6856 0.8842 0.8243 0.0867  -0.0294 -0.0479 580 SER A N   
2199 C CA  . SER A 284 ? 0.5773 0.8319 0.7386 0.0862  -0.0271 -0.0407 580 SER A CA  
2200 C C   . SER A 284 ? 0.5969 0.8839 0.7766 0.0566  -0.0256 -0.0328 580 SER A C   
2201 O O   . SER A 284 ? 0.5625 0.8887 0.7569 0.0447  -0.0254 -0.0259 580 SER A O   
2202 C CB  . SER A 284 ? 0.6094 0.9080 0.7637 0.1177  -0.0220 -0.0438 580 SER A CB  
2203 O OG  . SER A 284 ? 0.6406 0.9334 0.7779 0.1269  -0.0178 -0.0497 580 SER A OG  
2204 N N   . ALA A 285 ? 0.6688 0.9377 0.8416 0.0441  -0.0253 -0.0334 581 ALA A N   
2205 C CA  . ALA A 285 ? 0.5461 0.8252 0.7220 0.0170  -0.0252 -0.0257 581 ALA A CA  
2206 C C   . ALA A 285 ? 0.6455 0.8754 0.8131 0.0089  -0.0308 -0.0270 581 ALA A C   
2207 O O   . ALA A 285 ? 0.6360 0.8485 0.7934 0.0155  -0.0313 -0.0326 581 ALA A O   
2208 C CB  . ALA A 285 ? 0.4303 0.7469 0.6000 0.0137  -0.0187 -0.0242 581 ALA A CB  
2209 N N   . CYS A 286 ? 0.5595 0.7712 0.7296 -0.0038 -0.0353 -0.0223 582 CYS A N   
2210 C CA  . CYS A 286 ? 0.5671 0.7439 0.7306 -0.0060 -0.0407 -0.0237 582 CYS A CA  
2211 C C   . CYS A 286 ? 0.6276 0.7876 0.7810 -0.0193 -0.0442 -0.0164 582 CYS A C   
2212 O O   . CYS A 286 ? 0.7046 0.8475 0.8605 -0.0171 -0.0479 -0.0168 582 CYS A O   
2213 C CB  . CYS A 286 ? 0.6283 0.7902 0.7993 0.0030  -0.0431 -0.0297 582 CYS A CB  
2214 S SG  . CYS A 286 ? 0.6055 0.7729 0.7882 0.0036  -0.0431 -0.0266 582 CYS A SG  
2215 N N   . PRO A 287 ? 0.6634 0.8223 0.7979 -0.0336 -0.0433 -0.0099 583 PRO A N   
2216 C CA  . PRO A 287 ? 0.5982 0.7256 0.7079 -0.0477 -0.0475 -0.0030 583 PRO A CA  
2217 C C   . PRO A 287 ? 0.6582 0.7482 0.7535 -0.0334 -0.0534 -0.0051 583 PRO A C   
2218 O O   . PRO A 287 ? 0.5718 0.6571 0.6613 -0.0219 -0.0551 -0.0082 583 PRO A O   
2219 C CB  . PRO A 287 ? 0.6844 0.8099 0.7660 -0.0679 -0.0454 0.0040  583 PRO A CB  
2220 C CG  . PRO A 287 ? 0.7348 0.8818 0.8254 -0.0569 -0.0415 -0.0005 583 PRO A CG  
2221 C CD  . PRO A 287 ? 0.6835 0.8615 0.8095 -0.0386 -0.0387 -0.0086 583 PRO A CD  
2222 N N   . PHE A 288 ? 0.5142 0.5823 0.6019 -0.0328 -0.0569 -0.0037 584 PHE A N   
2223 C CA  . PHE A 288 ? 0.5916 0.6351 0.6666 -0.0140 -0.0619 -0.0063 584 PHE A CA  
2224 C C   . PHE A 288 ? 0.6856 0.6793 0.7169 -0.0175 -0.0663 -0.0009 584 PHE A C   
2225 O O   . PHE A 288 ? 0.6118 0.5969 0.6359 -0.0369 -0.0658 0.0032  584 PHE A O   
2226 C CB  . PHE A 288 ? 0.5695 0.6390 0.6789 -0.0031 -0.0610 -0.0127 584 PHE A CB  
2227 C CG  . PHE A 288 ? 0.6637 0.7391 0.7875 -0.0129 -0.0590 -0.0113 584 PHE A CG  
2228 C CD1 . PHE A 288 ? 0.5620 0.6125 0.6688 -0.0126 -0.0617 -0.0090 584 PHE A CD1 
2229 C CD2 . PHE A 288 ? 0.6505 0.7540 0.8004 -0.0180 -0.0551 -0.0130 584 PHE A CD2 
2230 C CE1 . PHE A 288 ? 0.5865 0.6435 0.7054 -0.0216 -0.0608 -0.0077 584 PHE A CE1 
2231 C CE2 . PHE A 288 ? 0.5729 0.6831 0.7337 -0.0230 -0.0545 -0.0116 584 PHE A CE2 
2232 C CZ  . PHE A 288 ? 0.6206 0.7096 0.7679 -0.0266 -0.0574 -0.0087 584 PHE A CZ  
2233 N N   . SER A 289 ? 0.7543 0.7138 0.7512 0.0028  -0.0715 -0.0013 585 SER A N   
2234 C CA  . SER A 289 ? 0.7858 0.6799 0.7232 0.0034  -0.0767 0.0035  585 SER A CA  
2235 C C   . SER A 289 ? 0.7869 0.6653 0.7068 0.0398  -0.0813 -0.0010 585 SER A C   
2236 O O   . SER A 289 ? 0.7569 0.6706 0.6972 0.0641  -0.0821 -0.0060 585 SER A O   
2237 C CB  . SER A 289 ? 0.9509 0.7966 0.8335 -0.0089 -0.0795 0.0104  585 SER A CB  
2238 O OG  . SER A 289 ? 0.8572 0.7062 0.7334 0.0161  -0.0821 0.0080  585 SER A OG  
2239 N N   . GLY A 290 ? 0.8519 0.6811 0.7314 0.0432  -0.0845 0.0006  586 GLY A N   
2240 C CA  . GLY A 290 ? 0.8284 0.6350 0.6766 0.0828  -0.0889 -0.0034 586 GLY A CA  
2241 C C   . GLY A 290 ? 1.0124 0.7194 0.7691 0.0887  -0.0959 0.0013  586 GLY A C   
2242 O O   . GLY A 290 ? 1.0593 0.7162 0.7683 0.0767  -0.0993 0.0071  586 GLY A O   
2243 N N   . TRP A 291 ? 0.9947 0.6661 0.7185 0.1070  -0.0982 -0.0012 587 TRP A N   
2244 C CA  . TRP A 291 ? 1.1356 0.6980 0.7632 0.1054  -0.1051 0.0029  587 TRP A CA  
2245 C C   . TRP A 291 ? 1.2133 0.7637 0.8425 0.0836  -0.1037 0.0023  587 TRP A C   
2246 O O   . TRP A 291 ? 1.1234 0.7470 0.8227 0.0832  -0.0978 -0.0019 587 TRP A O   
2247 C CB  . TRP A 291 ? 1.2814 0.7884 0.8383 0.1628  -0.1120 -0.0007 587 TRP A CB  
2248 C CG  . TRP A 291 ? 1.2326 0.8117 0.8338 0.2082  -0.1091 -0.0094 587 TRP A CG  
2249 C CD1 . TRP A 291 ? 1.2940 0.8732 0.8902 0.2264  -0.1075 -0.0144 587 TRP A CD1 
2250 C CD2 . TRP A 291 ? 1.2425 0.9106 0.8980 0.2384  -0.1072 -0.0142 587 TRP A CD2 
2251 N NE1 . TRP A 291 ? 1.2329 0.9015 0.8790 0.2654  -0.1038 -0.0216 587 TRP A NE1 
2252 C CE2 . TRP A 291 ? 1.2694 0.9950 0.9524 0.2716  -0.1041 -0.0216 587 TRP A CE2 
2253 C CE3 . TRP A 291 ? 1.1756 0.8831 0.8573 0.2384  -0.1081 -0.0130 587 TRP A CE3 
2254 C CZ2 . TRP A 291 ? 1.2411 1.0678 0.9777 0.3001  -0.1020 -0.0274 587 TRP A CZ2 
2255 C CZ3 . TRP A 291 ? 1.1807 0.9817 0.9136 0.2681  -0.1069 -0.0192 587 TRP A CZ3 
2256 C CH2 . TRP A 291 ? 1.1873 1.0499 0.9478 0.2963  -0.1039 -0.0261 587 TRP A CH2 
2257 N N   . TYR A 292 ? 1.2394 0.6919 0.7843 0.0626  -0.1098 0.0070  588 TYR A N   
2258 C CA  . TYR A 292 ? 1.2329 0.6686 0.7717 0.0328  -0.1100 0.0075  588 TYR A CA  
2259 C C   . TYR A 292 ? 1.3020 0.7136 0.8150 0.0749  -0.1113 0.0003  588 TYR A C   
2260 O O   . TYR A 292 ? 1.2897 0.6434 0.7377 0.1214  -0.1159 -0.0030 588 TYR A O   
2261 C CB  . TYR A 292 ? 1.3711 0.7088 0.8210 -0.0129 -0.1170 0.0153  588 TYR A CB  
2262 C CG  . TYR A 292 ? 1.3305 0.7176 0.8218 -0.0747 -0.1139 0.0222  588 TYR A CG  
2263 C CD1 . TYR A 292 ? 1.3004 0.6586 0.7546 -0.1078 -0.1155 0.0300  588 TYR A CD1 
2264 C CD2 . TYR A 292 ? 1.2848 0.7505 0.8488 -0.0981 -0.1093 0.0212  588 TYR A CD2 
2265 C CE1 . TYR A 292 ? 1.2663 0.6820 0.7581 -0.1626 -0.1119 0.0361  588 TYR A CE1 
2266 C CE2 . TYR A 292 ? 1.2752 0.7954 0.8750 -0.1486 -0.1068 0.0271  588 TYR A CE2 
2267 C CZ  . TYR A 292 ? 1.1926 0.6931 0.7585 -0.1803 -0.1076 0.0343  588 TYR A CZ  
2268 O OH  . TYR A 292 ? 1.0786 0.6476 0.6822 -0.2279 -0.1042 0.0398  588 TYR A OH  
2269 N N   . MET A 293 ? 1.1552 0.6117 0.7156 0.0610  -0.1073 -0.0022 589 MET A N   
2270 C CA  . MET A 293 ? 1.2852 0.6980 0.8022 0.0851  -0.1093 -0.0074 589 MET A CA  
2271 C C   . MET A 293 ? 1.3438 0.6553 0.7757 0.0454  -0.1172 -0.0029 589 MET A C   
2272 O O   . MET A 293 ? 1.2740 0.6020 0.7263 -0.0100 -0.1177 0.0034  589 MET A O   
2273 C CB  . MET A 293 ? 1.0721 0.5756 0.6727 0.0873  -0.1017 -0.0117 589 MET A CB  
2274 C CG  . MET A 293 ? 1.2480 0.7136 0.8050 0.1172  -0.1026 -0.0178 589 MET A CG  
2275 S SD  . MET A 293 ? 1.1151 0.6891 0.7656 0.1243  -0.0927 -0.0225 589 MET A SD  
2276 C CE  . MET A 293 ? 1.1460 0.7382 0.8356 0.0615  -0.0933 -0.0163 589 MET A CE  
2277 N N   . GLY A 294 ? 1.3275 0.5338 0.6579 0.0746  -0.1239 -0.0062 590 GLY A N   
2278 C CA  . GLY A 294 ? 1.4266 0.5124 0.6514 0.0359  -0.1334 -0.0020 590 GLY A CA  
2279 C C   . GLY A 294 ? 1.4739 0.5917 0.7327 -0.0255 -0.1335 0.0015  590 GLY A C   
2280 O O   . GLY A 294 ? 1.5011 0.5729 0.7147 -0.0834 -0.1394 0.0087  590 GLY A O   
2281 N N   . THR A 295 ? 1.4207 0.6200 0.7558 -0.0151 -0.1273 -0.0032 591 THR A N   
2282 C CA  . THR A 295 ? 1.4053 0.6267 0.7605 -0.0647 -0.1291 -0.0007 591 THR A CA  
2283 C C   . THR A 295 ? 1.3393 0.6435 0.7652 -0.1172 -0.1270 0.0069  591 THR A C   
2284 O O   . THR A 295 ? 1.2915 0.6012 0.7115 -0.1680 -0.1314 0.0110  591 THR A O   
2285 C CB  . THR A 295 ? 1.3099 0.5955 0.7253 -0.0372 -0.1230 -0.0072 591 THR A CB  
2286 O OG1 . THR A 295 ? 1.2034 0.5990 0.7215 -0.0126 -0.1131 -0.0087 591 THR A OG1 
2287 C CG2 . THR A 295 ? 1.3523 0.5583 0.6903 0.0128  -0.1251 -0.0153 591 THR A CG2 
2288 N N   . GLU A 296 ? 1.1939 0.5683 0.6859 -0.1054 -0.1204 0.0085  592 GLU A N   
2289 C CA  . GLU A 296 ? 1.2006 0.6516 0.7521 -0.1501 -0.1180 0.0150  592 GLU A CA  
2290 C C   . GLU A 296 ? 1.2561 0.6436 0.7319 -0.2052 -0.1255 0.0228  592 GLU A C   
2291 O O   . GLU A 296 ? 1.3019 0.7427 0.8042 -0.2549 -0.1264 0.0281  592 GLU A O   
2292 C CB  . GLU A 296 ? 1.1489 0.6697 0.7683 -0.1269 -0.1103 0.0148  592 GLU A CB  
2293 C CG  . GLU A 296 ? 1.0384 0.6280 0.7319 -0.0821 -0.1028 0.0081  592 GLU A CG  
2294 C CD  . GLU A 296 ? 1.0745 0.7140 0.8141 -0.0671 -0.0975 0.0083  592 GLU A CD  
2295 O OE1 . GLU A 296 ? 1.0130 0.7137 0.8024 -0.0929 -0.0942 0.0119  592 GLU A OE1 
2296 O OE2 . GLU A 296 ? 1.0487 0.6636 0.7672 -0.0295 -0.0974 0.0049  592 GLU A OE2 
2297 N N   . ILE A 297 ? 1.2869 0.5633 0.6648 -0.1974 -0.1312 0.0238  593 ILE A N   
2298 C CA  . ILE A 297 ? 1.3601 0.5586 0.6482 -0.2554 -0.1391 0.0319  593 ILE A CA  
2299 C C   . ILE A 297 ? 1.5050 0.6213 0.7111 -0.2875 -0.1486 0.0315  593 ILE A C   
2300 O O   . ILE A 297 ? 1.5071 0.6392 0.7007 -0.3532 -0.1530 0.0374  593 ILE A O   
2301 C CB  . ILE A 297 ? 1.4435 0.5413 0.6459 -0.2346 -0.1424 0.0340  593 ILE A CB  
2302 C CG1 . ILE A 297 ? 1.3874 0.5685 0.6693 -0.2067 -0.1338 0.0343  593 ILE A CG1 
2303 C CG2 . ILE A 297 ? 1.6044 0.6135 0.7045 -0.3015 -0.1506 0.0433  593 ILE A CG2 
2304 C CD1 . ILE A 297 ? 1.4341 0.5288 0.6454 -0.1633 -0.1370 0.0337  593 ILE A CD1 
2305 N N   . GLY A 298 ? 1.6098 0.6404 0.7559 -0.2410 -0.1520 0.0241  594 GLY A N   
2306 C CA  . GLY A 298 ? 1.7213 0.6437 0.7637 -0.2663 -0.1623 0.0228  594 GLY A CA  
2307 C C   . GLY A 298 ? 1.6662 0.6606 0.7653 -0.2918 -0.1624 0.0209  594 GLY A C   
2308 O O   . GLY A 298 ? 1.7172 0.6697 0.7540 -0.3355 -0.1697 0.0240  594 GLY A O   
2309 N N   . VAL A 299 ? 1.5706 0.6897 0.7913 -0.2602 -0.1528 0.0172  595 VAL A N   
2310 C CA  . VAL A 299 ? 1.5323 0.7146 0.8015 -0.2791 -0.1536 0.0156  595 VAL A CA  
2311 C C   . VAL A 299 ? 1.4347 0.7445 0.7956 -0.3229 -0.1507 0.0223  595 VAL A C   
2312 O O   . VAL A 299 ? 1.4328 0.7596 0.7790 -0.3792 -0.1577 0.0266  595 VAL A O   
2313 C CB  . VAL A 299 ? 1.4103 0.6342 0.7372 -0.2168 -0.1461 0.0071  595 VAL A CB  
2314 C CG1 . VAL A 299 ? 1.3558 0.6282 0.7163 -0.2395 -0.1484 0.0063  595 VAL A CG1 
2315 C CG2 . VAL A 299 ? 1.4698 0.5822 0.7081 -0.1662 -0.1480 -0.0002 595 VAL A CG2 
2316 N N   . ARG A 300 ? 1.2808 0.6821 0.7322 -0.2968 -0.1409 0.0229  596 ARG A N   
2317 C CA  . ARG A 300 ? 1.1325 0.6576 0.6708 -0.3259 -0.1374 0.0279  596 ARG A CA  
2318 C C   . ARG A 300 ? 1.2443 0.7709 0.7495 -0.3831 -0.1407 0.0363  596 ARG A C   
2319 O O   . ARG A 300 ? 1.1611 0.7410 0.6728 -0.4359 -0.1453 0.0414  596 ARG A O   
2320 C CB  . ARG A 300 ? 1.1198 0.7307 0.7554 -0.2775 -0.1263 0.0248  596 ARG A CB  
2321 C CG  . ARG A 300 ? 1.1321 0.7431 0.7963 -0.2253 -0.1221 0.0171  596 ARG A CG  
2322 C CD  . ARG A 300 ? 1.1593 0.7898 0.8311 -0.2397 -0.1265 0.0162  596 ARG A CD  
2323 N NE  . ARG A 300 ? 1.0199 0.7456 0.7476 -0.2728 -0.1278 0.0213  596 ARG A NE  
2324 C CZ  . ARG A 300 ? 0.9552 0.7750 0.7672 -0.2532 -0.1210 0.0215  596 ARG A CZ  
2325 N NH1 . ARG A 300 ? 0.9897 0.8207 0.8413 -0.2082 -0.1124 0.0173  596 ARG A NH1 
2326 N NH2 . ARG A 300 ? 0.8795 0.7827 0.7312 -0.2787 -0.1232 0.0258  596 ARG A NH2 
2327 N N   . ASP A 301 ? 1.3493 0.8260 0.8196 -0.3744 -0.1383 0.0383  597 ASP A N   
2328 C CA  . ASP A 301 ? 1.3401 0.8267 0.7831 -0.4297 -0.1398 0.0470  597 ASP A CA  
2329 C C   . ASP A 301 ? 1.4591 0.8668 0.7996 -0.4971 -0.1515 0.0521  597 ASP A C   
2330 O O   . ASP A 301 ? 1.5013 0.9870 0.8554 -0.5432 -0.1499 0.0599  597 ASP A O   
2331 C CB  . ASP A 301 ? 1.3365 0.7705 0.7506 -0.4052 -0.1358 0.0483  597 ASP A CB  
2332 C CG  . ASP A 301 ? 1.2836 0.8172 0.8032 -0.3579 -0.1246 0.0450  597 ASP A CG  
2333 O OD1 . ASP A 301 ? 1.1801 0.8325 0.7867 -0.3658 -0.1193 0.0456  597 ASP A OD1 
2334 O OD2 . ASP A 301 ? 1.3474 0.8391 0.8577 -0.3119 -0.1217 0.0416  597 ASP A OD2 
2335 N N   . TYR A 302 ? 1.5375 0.8222 0.7867 -0.4794 -0.1576 0.0487  598 TYR A N   
2336 C CA  . TYR A 302 ? 1.6046 0.8237 0.7520 -0.5183 -0.1634 0.0553  598 TYR A CA  
2337 C C   . TYR A 302 ? 1.6355 0.8879 0.7870 -0.5423 -0.1678 0.0555  598 TYR A C   
2338 O O   . TYR A 302 ? 1.6136 0.8694 0.7138 -0.5928 -0.1711 0.0639  598 TYR A O   
2339 C CB  . TYR A 302 ? 1.8309 0.8930 0.8603 -0.4848 -0.1684 0.0522  598 TYR A CB  
2340 C CG  . TYR A 302 ? 1.9381 0.9469 0.9191 -0.4797 -0.1672 0.0559  598 TYR A CG  
2341 C CD1 . TYR A 302 ? 2.0480 0.9435 0.9590 -0.4241 -0.1695 0.0504  598 TYR A CD1 
2342 C CD2 . TYR A 302 ? 1.8274 0.9025 0.8292 -0.5271 -0.1637 0.0646  598 TYR A CD2 
2343 C CE1 . TYR A 302 ? 1.9947 0.8396 0.8571 -0.4168 -0.1694 0.0535  598 TYR A CE1 
2344 C CE2 . TYR A 302 ? 1.9555 0.9778 0.9085 -0.5235 -0.1630 0.0677  598 TYR A CE2 
2345 C CZ  . TYR A 302 ? 2.0119 0.9164 0.8948 -0.4688 -0.1664 0.0622  598 TYR A CZ  
2346 O OH  . TYR A 302 ? 1.9538 0.8059 0.7861 -0.4626 -0.1666 0.0648  598 TYR A OH  
2347 N N   . CYS A 303 ? 1.5405 0.8187 0.7486 -0.5094 -0.1682 0.0467  599 CYS A N   
2348 C CA  . CYS A 303 ? 1.6439 0.9308 0.8412 -0.5251 -0.1735 0.0460  599 CYS A CA  
2349 C C   . CYS A 303 ? 1.5023 0.9288 0.8126 -0.5309 -0.1720 0.0443  599 CYS A C   
2350 O O   . CYS A 303 ? 1.4396 0.8865 0.7451 -0.5482 -0.1766 0.0449  599 CYS A O   
2351 C CB  . CYS A 303 ? 1.6674 0.8420 0.8058 -0.4789 -0.1773 0.0364  599 CYS A CB  
2352 S SG  . CYS A 303 ? 1.8359 0.8404 0.8245 -0.4612 -0.1812 0.0378  599 CYS A SG  
2353 N N   . ASP A 304 ? 1.4006 0.9189 0.8070 -0.5133 -0.1665 0.0420  600 ASP A N   
2354 C CA  . ASP A 304 ? 1.4482 1.1130 0.9556 -0.5215 -0.1651 0.0433  600 ASP A CA  
2355 C C   . ASP A 304 ? 1.4740 1.2005 0.9647 -0.5720 -0.1656 0.0535  600 ASP A C   
2356 O O   . ASP A 304 ? 1.5385 1.2366 0.9719 -0.6051 -0.1637 0.0613  600 ASP A O   
2357 C CB  . ASP A 304 ? 1.4072 1.1659 1.0039 -0.4917 -0.1541 0.0442  600 ASP A CB  
2358 C CG  . ASP A 304 ? 1.3471 1.1619 1.0293 -0.4261 -0.1460 0.0383  600 ASP A CG  
2359 O OD1 . ASP A 304 ? 1.4349 1.1877 1.0987 -0.3921 -0.1464 0.0324  600 ASP A OD1 
2360 O OD2 . ASP A 304 ? 1.2132 1.1332 0.9759 -0.4097 -0.1393 0.0396  600 ASP A OD2 
2361 N N   . ASN A 305 ? 1.3874 1.1990 0.9244 -0.5779 -0.1684 0.0537  601 ASN A N   
2362 C CA  . ASN A 305 ? 1.4241 1.2955 0.9411 -0.6251 -0.1692 0.0632  601 ASN A CA  
2363 C C   . ASN A 305 ? 1.3048 1.2889 0.8692 -0.6417 -0.1611 0.0700  601 ASN A C   
2364 O O   . ASN A 305 ? 1.3876 1.3893 0.9061 -0.6878 -0.1601 0.0791  601 ASN A O   
2365 C CB  . ASN A 305 ? 1.4174 1.3550 0.9730 -0.6221 -0.1745 0.0614  601 ASN A CB  
2366 C CG  . ASN A 305 ? 1.6019 1.4350 1.0715 -0.6398 -0.1825 0.0610  601 ASN A CG  
2367 O OD1 . ASN A 305 ? 1.7410 1.4755 1.1146 -0.6689 -0.1840 0.0659  601 ASN A OD1 
2368 N ND2 . ASN A 305 ? 1.5603 1.4117 1.0580 -0.6214 -0.1882 0.0554  601 ASN A ND2 
2369 N N   . SER A 306 ? 1.3486 1.4091 0.9993 -0.6051 -0.1553 0.0659  602 SER A N   
2370 C CA  . SER A 306 ? 1.3787 1.5446 1.0749 -0.6119 -0.1465 0.0709  602 SER A CA  
2371 C C   . SER A 306 ? 1.3306 1.4379 1.0014 -0.6116 -0.1413 0.0717  602 SER A C   
2372 O O   . SER A 306 ? 1.2612 1.4520 0.9756 -0.6092 -0.1333 0.0743  602 SER A O   
2373 C CB  . SER A 306 ? 1.3335 1.6262 1.1352 -0.5688 -0.1430 0.0667  602 SER A CB  
2374 O OG  . SER A 306 ? 1.3903 1.6535 1.2195 -0.5330 -0.1493 0.0589  602 SER A OG  
2375 N N   . ARG A 307 ? 1.3149 1.2811 0.9125 -0.6110 -0.1455 0.0694  603 ARG A N   
2376 C CA  . ARG A 307 ? 1.3446 1.2413 0.9013 -0.6129 -0.1419 0.0711  603 ARG A CA  
2377 C C   . ARG A 307 ? 1.4224 1.2224 0.8623 -0.6584 -0.1462 0.0785  603 ARG A C   
2378 O O   . ARG A 307 ? 1.4993 1.3550 0.9201 -0.7011 -0.1468 0.0858  603 ARG A O   
2379 C CB  . ARG A 307 ? 1.2697 1.0888 0.8375 -0.5659 -0.1430 0.0621  603 ARG A CB  
2380 C CG  . ARG A 307 ? 1.1885 1.1083 0.8666 -0.5214 -0.1386 0.0560  603 ARG A CG  
2381 C CD  . ARG A 307 ? 1.1235 1.1493 0.8681 -0.5152 -0.1290 0.0589  603 ARG A CD  
2382 N NE  . ARG A 307 ? 1.0766 1.0339 0.7790 -0.5164 -0.1247 0.0611  603 ARG A NE  
2383 C CZ  . ARG A 307 ? 1.1163 0.9919 0.8060 -0.4670 -0.1212 0.0562  603 ARG A CZ  
2384 N NH1 . ARG A 307 ? 1.0125 0.8679 0.7292 -0.4164 -0.1205 0.0488  603 ARG A NH1 
2385 N NH2 . ARG A 307 ? 1.2528 1.0701 0.9003 -0.4694 -0.1186 0.0589  603 ARG A NH2 
2386 N N   . TYR A 308 ? 1.5130 1.1705 0.8678 -0.6500 -0.1499 0.0770  604 TYR A N   
2387 C CA  . TYR A 308 ? 1.6241 1.1919 0.8612 -0.6929 -0.1544 0.0846  604 TYR A CA  
2388 C C   . TYR A 308 ? 1.7628 1.2761 0.9266 -0.7197 -0.1628 0.0870  604 TYR A C   
2389 O O   . TYR A 308 ? 1.7866 1.2681 0.8653 -0.7700 -0.1667 0.0953  604 TYR A O   
2390 C CB  . TYR A 308 ? 1.6133 1.0440 0.7749 -0.6684 -0.1564 0.0821  604 TYR A CB  
2391 C CG  . TYR A 308 ? 1.7187 1.1856 0.9002 -0.6753 -0.1497 0.0859  604 TYR A CG  
2392 C CD1 . TYR A 308 ? 1.5849 1.1655 0.8815 -0.6523 -0.1409 0.0835  604 TYR A CD1 
2393 C CD2 . TYR A 308 ? 1.8853 1.2720 0.9661 -0.7055 -0.1529 0.0916  604 TYR A CD2 
2394 C CE1 . TYR A 308 ? 1.6005 1.2163 0.9152 -0.6581 -0.1342 0.0871  604 TYR A CE1 
2395 C CE2 . TYR A 308 ? 1.8957 1.3170 0.9940 -0.7131 -0.1468 0.0949  604 TYR A CE2 
2396 C CZ  . TYR A 308 ? 1.7772 1.3143 0.9946 -0.6888 -0.1369 0.0930  604 TYR A CZ  
2397 O OH  . TYR A 308 ? 1.7462 1.3208 0.9829 -0.6946 -0.1301 0.0963  604 TYR A OH  
2398 N N   . ASN A 309 ? 1.7494 1.2485 0.9392 -0.6892 -0.1661 0.0799  605 ASN A N   
2399 C CA  . ASN A 309 ? 1.8354 1.3125 0.9799 -0.7128 -0.1730 0.0819  605 ASN A CA  
2400 C C   . ASN A 309 ? 2.0166 1.3535 1.0147 -0.7438 -0.1805 0.0875  605 ASN A C   
2401 O O   . ASN A 309 ? 2.0835 1.4320 1.0248 -0.8005 -0.1835 0.0970  605 ASN A O   
2402 C CB  . ASN A 309 ? 1.7533 1.3806 0.9633 -0.7496 -0.1703 0.0882  605 ASN A CB  
2403 C CG  . ASN A 309 ? 1.7115 1.3401 0.9042 -0.7644 -0.1767 0.0888  605 ASN A CG  
2404 O OD1 . ASN A 309 ? 1.7082 1.2572 0.8804 -0.7339 -0.1816 0.0815  605 ASN A OD1 
2405 N ND2 . ASN A 309 ? 1.6881 1.4100 0.8868 -0.8112 -0.1764 0.0974  605 ASN A ND2 
2406 N N   . ILE A 310 ? 2.0578 1.2610 0.9911 -0.7027 -0.1838 0.0810  606 ILE A N   
2407 C CA  . ILE A 310 ? 2.1149 1.1689 0.9000 -0.7180 -0.1917 0.0845  606 ILE A CA  
2408 C C   . ILE A 310 ? 2.0916 1.0472 0.8065 -0.6998 -0.1989 0.0807  606 ILE A C   
2409 O O   . ILE A 310 ? 2.1945 1.0245 0.7764 -0.7145 -0.2065 0.0843  606 ILE A O   
2410 C CB  . ILE A 310 ? 2.1296 1.0917 0.8663 -0.6829 -0.1911 0.0808  606 ILE A CB  
2411 C CG1 . ILE A 310 ? 2.0134 0.9387 0.7911 -0.6065 -0.1885 0.0688  606 ILE A CG1 
2412 C CG2 . ILE A 310 ? 1.9020 0.9510 0.6958 -0.7043 -0.1842 0.0854  606 ILE A CG2 
2413 C CD1 . ILE A 310 ? 2.0667 0.8938 0.7846 -0.5659 -0.1889 0.0651  606 ILE A CD1 
2414 N N   . LEU A 311 ? 2.0492 1.0537 0.8414 -0.6687 -0.1972 0.0734  607 LEU A N   
2415 C CA  . LEU A 311 ? 2.0993 1.0142 0.8214 -0.6550 -0.2038 0.0703  607 LEU A CA  
2416 C C   . LEU A 311 ? 2.3322 1.2128 0.9595 -0.7198 -0.2109 0.0818  607 LEU A C   
2417 O O   . LEU A 311 ? 2.4339 1.1914 0.9490 -0.7162 -0.2180 0.0824  607 LEU A O   
2418 C CB  . LEU A 311 ? 1.8643 0.8557 0.6870 -0.6252 -0.2016 0.0616  607 LEU A CB  
2419 C CG  . LEU A 311 ? 1.7891 0.7659 0.6656 -0.5526 -0.1969 0.0482  607 LEU A CG  
2420 C CD1 . LEU A 311 ? 1.8625 0.9270 0.8396 -0.5324 -0.1954 0.0400  607 LEU A CD1 
2421 C CD2 . LEU A 311 ? 1.8985 0.7241 0.6653 -0.5053 -0.2001 0.0425  607 LEU A CD2 
2422 N N   . GLU A 312 ? 2.5510 1.5403 1.2179 -0.7783 -0.2089 0.0913  608 GLU A N   
2423 C CA  . GLU A 312 ? 2.8104 1.7754 1.3836 -0.8474 -0.2150 0.1036  608 GLU A CA  
2424 C C   . GLU A 312 ? 2.9161 1.7157 1.3281 -0.8591 -0.2226 0.1075  608 GLU A C   
2425 O O   . GLU A 312 ? 2.9559 1.6511 1.2561 -0.8768 -0.2308 0.1115  608 GLU A O   
2426 C CB  . GLU A 312 ? 2.9067 2.0165 1.5436 -0.9011 -0.2099 0.1123  608 GLU A CB  
2427 C CG  . GLU A 312 ? 2.8245 2.0958 1.5902 -0.9035 -0.2051 0.1114  608 GLU A CG  
2428 C CD  . GLU A 312 ? 2.9117 2.1895 1.6341 -0.9475 -0.2110 0.1183  608 GLU A CD  
2429 O OE1 . GLU A 312 ? 3.0242 2.1688 1.6429 -0.9479 -0.2186 0.1186  608 GLU A OE1 
2430 O OE2 . GLU A 312 ? 2.8702 2.2876 1.6597 -0.9802 -0.2080 0.1236  608 GLU A OE2 
2431 N N   . GLU A 313 ? 2.8385 1.6093 1.2323 -0.8483 -0.2207 0.1063  609 GLU A N   
2432 C CA  . GLU A 313 ? 2.9973 1.6221 1.2338 -0.8673 -0.2289 0.1103  609 GLU A CA  
2433 C C   . GLU A 313 ? 2.9885 1.4645 1.1505 -0.7987 -0.2331 0.1000  609 GLU A C   
2434 O O   . GLU A 313 ? 3.1549 1.5093 1.2052 -0.8042 -0.2401 0.0990  609 GLU A O   
2435 C CB  . GLU A 313 ? 3.0534 1.7113 1.3000 -0.8851 -0.2255 0.1121  609 GLU A CB  
2436 C CG  . GLU A 313 ? 3.2012 1.9267 1.4319 -0.9667 -0.2258 0.1220  609 GLU A CG  
2437 C CD  . GLU A 313 ? 3.4431 2.0547 1.5444 -1.0093 -0.2349 0.1249  609 GLU A CD  
2438 O OE1 . GLU A 313 ? 3.4733 2.0805 1.5580 -1.0256 -0.2383 0.1279  609 GLU A OE1 
2439 O OE2 . GLU A 313 ? 3.5822 2.1058 1.5946 -1.0276 -0.2390 0.1243  609 GLU A OE2 
2440 N N   . VAL A 314 ? 2.8206 1.3131 1.0573 -0.7292 -0.2274 0.0900  610 VAL A N   
2441 C CA  . VAL A 314 ? 2.7592 1.1226 0.9229 -0.6582 -0.2309 0.0807  610 VAL A CA  
2442 C C   . VAL A 314 ? 2.7774 1.0728 0.8815 -0.6499 -0.2362 0.0800  610 VAL A C   
2443 O O   . VAL A 314 ? 2.7986 0.9657 0.8031 -0.6146 -0.2408 0.0742  610 VAL A O   
2444 C CB  . VAL A 314 ? 2.5474 0.9720 0.8307 -0.5868 -0.2216 0.0690  610 VAL A CB  
2445 C CG1 . VAL A 314 ? 2.5746 0.8860 0.7917 -0.5075 -0.2239 0.0588  610 VAL A CG1 
2446 C CG2 . VAL A 314 ? 2.3981 0.8732 0.7272 -0.5945 -0.2167 0.0701  610 VAL A CG2 
2447 N N   . ALA A 315 ? 2.7825 1.1698 0.9594 -0.6792 -0.2344 0.0835  611 ALA A N   
2448 C CA  . ALA A 315 ? 2.8582 1.1801 0.9694 -0.6812 -0.2403 0.0850  611 ALA A CA  
2449 C C   . ALA A 315 ? 3.0573 1.2879 1.0486 -0.7336 -0.2478 0.0908  611 ALA A C   
2450 O O   . ALA A 315 ? 3.1498 1.2569 1.0427 -0.7093 -0.2533 0.0867  611 ALA A O   
2451 C CB  . ALA A 315 ? 2.7572 1.2120 0.9887 -0.7038 -0.2362 0.0851  611 ALA A CB  
2452 N N   . LYS A 316 ? 3.1221 1.4150 1.1189 -0.8060 -0.2480 0.1002  612 LYS A N   
2453 C CA  . LYS A 316 ? 3.2442 1.4570 1.1268 -0.8643 -0.2554 0.1063  612 LYS A CA  
2454 C C   . LYS A 316 ? 3.3207 1.3724 1.0829 -0.8270 -0.2606 0.0995  612 LYS A C   
2455 O O   . LYS A 316 ? 3.4227 1.3533 1.0769 -0.8227 -0.2677 0.0983  612 LYS A O   
2456 C CB  . LYS A 316 ? 3.1713 1.4861 1.0853 -0.9399 -0.2534 0.1161  612 LYS A CB  
2457 C CG  . LYS A 316 ? 3.0863 1.5497 1.0876 -0.9898 -0.2502 0.1250  612 LYS A CG  
2458 C CD  . LYS A 316 ? 3.1567 1.6972 1.1517 -1.0705 -0.2500 0.1350  612 LYS A CD  
2459 C CE  . LYS A 316 ? 3.4228 1.8291 1.2703 -1.1141 -0.2592 0.1376  612 LYS A CE  
2460 N NZ  . LYS A 316 ? 3.5060 1.9740 1.3368 -1.1888 -0.2590 0.1459  612 LYS A NZ  
2461 N N   . LYS A 317 ? 3.1173 1.1658 0.8960 -0.7959 -0.2571 0.0948  613 LYS A N   
2462 C CA  . LYS A 317 ? 3.3278 1.2360 0.9946 -0.7650 -0.2618 0.0891  613 LYS A CA  
2463 C C   . LYS A 317 ? 3.3041 1.1104 0.9244 -0.6801 -0.2633 0.0789  613 LYS A C   
2464 O O   . LYS A 317 ? 3.4826 1.1667 1.0034 -0.6428 -0.2675 0.0734  613 LYS A O   
2465 C CB  . LYS A 317 ? 3.1853 1.1323 0.8942 -0.7536 -0.2570 0.0869  613 LYS A CB  
2466 C CG  . LYS A 317 ? 3.2744 1.2133 0.9276 -0.8271 -0.2604 0.0943  613 LYS A CG  
2467 C CD  . LYS A 317 ? 3.1487 1.2091 0.9016 -0.8437 -0.2530 0.0966  613 LYS A CD  
2468 C CE  . LYS A 317 ? 3.2182 1.3241 0.9467 -0.9337 -0.2548 0.1065  613 LYS A CE  
2469 N NZ  . LYS A 317 ? 3.1092 1.3881 0.9677 -0.9620 -0.2460 0.1115  613 LYS A NZ  
2470 N N   . MET A 318 ? 3.2852 1.1437 0.9747 -0.6478 -0.2598 0.0761  614 MET A N   
2471 C CA  . MET A 318 ? 3.3621 1.1292 1.0000 -0.5761 -0.2615 0.0676  614 MET A CA  
2472 C C   . MET A 318 ? 3.5164 1.2241 1.0825 -0.6072 -0.2681 0.0719  614 MET A C   
2473 O O   . MET A 318 ? 3.6203 1.2369 1.1225 -0.5528 -0.2706 0.0657  614 MET A O   
2474 C CB  . MET A 318 ? 3.1411 0.9916 0.8918 -0.5113 -0.2535 0.0603  614 MET A CB  
2475 C CG  . MET A 318 ? 3.1841 1.0759 0.9942 -0.4668 -0.2475 0.0546  614 MET A CG  
2476 S SD  . MET A 318 ? 3.0188 1.0181 0.9631 -0.4025 -0.2386 0.0472  614 MET A SD  
2477 C CE  . MET A 318 ? 3.1063 1.0100 0.9810 -0.3263 -0.2402 0.0381  614 MET A CE  
2478 N N   . ASP A 319 ? 3.6833 1.4424 1.2555 -0.6927 -0.2708 0.0825  615 ASP A N   
2479 C CA  . ASP A 319 ? 3.8315 1.5614 1.3559 -0.7316 -0.2765 0.0879  615 ASP A CA  
2480 C C   . ASP A 319 ? 3.7344 1.5000 1.3230 -0.6806 -0.2729 0.0824  615 ASP A C   
2481 O O   . ASP A 319 ? 3.8084 1.4747 1.3294 -0.6268 -0.2755 0.0759  615 ASP A O   
2482 C CB  . ASP A 319 ? 4.1183 1.6803 1.4786 -0.7370 -0.2862 0.0880  615 ASP A CB  
2483 C CG  . ASP A 319 ? 4.2690 1.8195 1.5650 -0.8328 -0.2933 0.0996  615 ASP A CG  
2484 O OD1 . ASP A 319 ? 4.1871 1.8627 1.5617 -0.8960 -0.2901 0.1076  615 ASP A OD1 
2485 O OD2 . ASP A 319 ? 4.4643 1.8835 1.6296 -0.8444 -0.3019 0.1009  615 ASP A OD2 
2486 N N   . LEU A 320 ? 3.5597 1.4675 1.2760 -0.6966 -0.2669 0.0851  616 LEU A N   
2487 C CA  . LEU A 320 ? 3.3640 1.3189 1.1505 -0.6548 -0.2634 0.0804  616 LEU A CA  
2488 C C   . LEU A 320 ? 3.3407 1.3633 1.1551 -0.7192 -0.2660 0.0894  616 LEU A C   
2489 O O   . LEU A 320 ? 3.3878 1.4754 1.2149 -0.7935 -0.2674 0.0996  616 LEU A O   
2490 C CB  . LEU A 320 ? 3.1075 1.1702 1.0198 -0.6125 -0.2547 0.0753  616 LEU A CB  
2491 C CG  . LEU A 320 ? 3.0915 1.0975 0.9878 -0.5359 -0.2512 0.0649  616 LEU A CG  
2492 C CD1 . LEU A 320 ? 2.9697 1.0830 0.9910 -0.4952 -0.2431 0.0597  616 LEU A CD1 
2493 C CD2 . LEU A 320 ? 3.1614 1.0442 0.9658 -0.4726 -0.2540 0.0567  616 LEU A CD2 
2494 N N   . ASP A 321 ? 3.1814 1.1912 1.0037 -0.6889 -0.2666 0.0857  617 ASP A N   
2495 C CA  . ASP A 321 ? 3.1846 1.2647 1.0432 -0.7399 -0.2688 0.0932  617 ASP A CA  
2496 C C   . ASP A 321 ? 2.9434 1.1961 0.9474 -0.7638 -0.2624 0.0959  617 ASP A C   
2497 O O   . ASP A 321 ? 2.7815 1.1135 0.9003 -0.7164 -0.2566 0.0832  617 ASP A O   
2498 C CB  . ASP A 321 ? 3.2048 1.2317 1.0453 -0.6909 -0.2701 0.0863  617 ASP A CB  
2499 C CG  . ASP A 321 ? 3.3137 1.3895 1.1690 -0.7446 -0.2741 0.0941  617 ASP A CG  
2500 O OD1 . ASP A 321 ? 3.2587 1.3774 1.1823 -0.7093 -0.2716 0.0846  617 ASP A OD1 
2501 O OD2 . ASP A 321 ? 3.4373 1.5227 1.2533 -0.8193 -0.2790 0.1044  617 ASP A OD2 
2502 N N   . MET A 322 ? 2.9545 1.2797 0.9736 -0.8312 -0.2624 0.1068  618 MET A N   
2503 C CA  . MET A 322 ? 2.9114 1.4184 1.0867 -0.8496 -0.2554 0.1048  618 MET A CA  
2504 C C   . MET A 322 ? 2.9615 1.5677 1.1906 -0.8954 -0.2573 0.1091  618 MET A C   
2505 O O   . MET A 322 ? 2.8202 1.5825 1.1817 -0.9019 -0.2523 0.1064  618 MET A O   
2506 C CB  . MET A 322 ? 2.9505 1.5030 1.1246 -0.8932 -0.2530 0.1135  618 MET A CB  
2507 C CG  . MET A 322 ? 2.9104 1.4401 1.1079 -0.8392 -0.2479 0.1052  618 MET A CG  
2508 S SD  . MET A 322 ? 2.9689 1.5488 1.1657 -0.8854 -0.2450 0.1137  618 MET A SD  
2509 C CE  . MET A 322 ? 2.8262 1.6294 1.1881 -0.9240 -0.2376 0.1165  618 MET A CE  
2510 N N   . ARG A 323 ? 3.1470 1.6659 1.2746 -0.9242 -0.2648 0.1157  619 ARG A N   
2511 C CA  . ARG A 323 ? 3.2127 1.8223 1.3866 -0.9666 -0.2674 0.1194  619 ARG A CA  
2512 C C   . ARG A 323 ? 3.1082 1.7982 1.4039 -0.9119 -0.2645 0.1042  619 ARG A C   
2513 O O   . ARG A 323 ? 3.0427 1.8741 1.4406 -0.9327 -0.2637 0.1036  619 ARG A O   
2514 C CB  . ARG A 323 ? 3.4130 1.8944 1.4404 -1.0071 -0.2765 0.1295  619 ARG A CB  
2515 C CG  . ARG A 323 ? 3.5999 2.0079 1.5074 -1.0683 -0.2809 0.1420  619 ARG A CG  
2516 C CD  . ARG A 323 ? 3.8391 2.0695 1.6031 -1.0640 -0.2895 0.1390  619 ARG A CD  
2517 N NE  . ARG A 323 ? 3.9170 2.0281 1.6408 -0.9820 -0.2886 0.1266  619 ARG A NE  
2518 C CZ  . ARG A 323 ? 4.1051 2.0540 1.7020 -0.9602 -0.2948 0.1222  619 ARG A CZ  
2519 N NH1 . ARG A 323 ? 4.2552 2.1317 1.7482 -1.0177 -0.3032 0.1293  619 ARG A NH1 
2520 N NH2 . ARG A 323 ? 4.1372 1.9982 1.7085 -0.8800 -0.2926 0.1109  619 ARG A NH2 
2521 N N   . LYS A 324 ? 3.0493 1.6544 1.3327 -0.8404 -0.2631 0.0917  620 LYS A N   
2522 C CA  . LYS A 324 ? 2.8343 1.4909 1.2075 -0.7886 -0.2612 0.0769  620 LYS A CA  
2523 C C   . LYS A 324 ? 2.6774 1.4014 1.1567 -0.7320 -0.2531 0.0648  620 LYS A C   
2524 O O   . LYS A 324 ? 2.7464 1.3979 1.1874 -0.6974 -0.2496 0.0624  620 LYS A O   
2525 C CB  . LYS A 324 ? 2.8742 1.3893 1.1509 -0.7488 -0.2648 0.0711  620 LYS A CB  
2526 C CG  . LYS A 324 ? 2.9260 1.4178 1.1494 -0.7920 -0.2726 0.0772  620 LYS A CG  
2527 C CD  . LYS A 324 ? 3.0650 1.5195 1.1920 -0.8724 -0.2785 0.0958  620 LYS A CD  
2528 C CE  . LYS A 324 ? 3.0864 1.5627 1.1937 -0.9233 -0.2855 0.1017  620 LYS A CE  
2529 N NZ  . LYS A 324 ? 3.2158 1.6747 1.2364 -1.0083 -0.2904 0.1204  620 LYS A NZ  
2530 N N   . THR A 325 ? 2.4502 1.3118 1.0583 -0.7226 -0.2510 0.0577  621 THR A N   
2531 C CA  . THR A 325 ? 2.1721 1.1023 0.8826 -0.6721 -0.2440 0.0466  621 THR A CA  
2532 C C   . THR A 325 ? 2.1753 1.0075 0.8546 -0.6000 -0.2406 0.0331  621 THR A C   
2533 O O   . THR A 325 ? 2.0183 0.8455 0.7258 -0.5592 -0.2343 0.0268  621 THR A O   
2534 C CB  . THR A 325 ? 2.1119 1.1959 0.9492 -0.6743 -0.2447 0.0422  621 THR A CB  
2535 O OG1 . THR A 325 ? 2.0032 1.1272 0.9225 -0.6178 -0.2394 0.0296  621 THR A OG1 
2536 C CG2 . THR A 325 ? 2.2506 1.3297 1.0706 -0.6827 -0.2517 0.0398  621 THR A CG2 
2537 N N   . SER A 326 ? 2.3633 1.1212 0.9839 -0.5825 -0.2440 0.0284  622 SER A N   
2538 C CA  . SER A 326 ? 2.2714 0.9535 0.8666 -0.5111 -0.2398 0.0148  622 SER A CA  
2539 C C   . SER A 326 ? 2.3872 0.9197 0.8568 -0.4828 -0.2391 0.0175  622 SER A C   
2540 O O   . SER A 326 ? 2.3192 0.7791 0.7472 -0.4227 -0.2359 0.0079  622 SER A O   
2541 C CB  . SER A 326 ? 2.2362 0.9162 0.8270 -0.5048 -0.2436 0.0087  622 SER A CB  
2542 O OG  . SER A 326 ? 2.2792 0.9295 0.8044 -0.5644 -0.2518 0.0210  622 SER A OG  
2543 N N   . SER A 327 ? 2.4894 0.9757 0.8925 -0.5228 -0.2423 0.0306  623 SER A N   
2544 C CA  . SER A 327 ? 2.5736 0.9257 0.8626 -0.4889 -0.2423 0.0329  623 SER A CA  
2545 C C   . SER A 327 ? 2.5282 0.9031 0.8688 -0.4354 -0.2342 0.0244  623 SER A C   
2546 O O   . SER A 327 ? 2.5647 0.8386 0.8193 -0.3953 -0.2339 0.0245  623 SER A O   
2547 C CB  . SER A 327 ? 2.7417 1.0270 0.9265 -0.5533 -0.2496 0.0501  623 SER A CB  
2548 O OG  . SER A 327 ? 2.6245 1.0056 0.8762 -0.5984 -0.2476 0.0564  623 SER A OG  
2549 N N   . LEU A 328 ? 2.3718 0.8760 0.8465 -0.4327 -0.2285 0.0175  624 LEU A N   
2550 C CA  . LEU A 328 ? 2.3040 0.8441 0.8390 -0.3914 -0.2208 0.0106  624 LEU A CA  
2551 C C   . LEU A 328 ? 2.3377 0.8174 0.8032 -0.4077 -0.2225 0.0204  624 LEU A C   
2552 O O   . LEU A 328 ? 2.4189 0.8638 0.8728 -0.3582 -0.2180 0.0153  624 LEU A O   
2553 C CB  . LEU A 328 ? 2.2962 0.8017 0.8326 -0.3072 -0.2138 -0.0042 624 LEU A CB  
2554 C CG  . LEU A 328 ? 2.2298 0.7862 0.8223 -0.2884 -0.2117 -0.0150 624 LEU A CG  
2555 C CD1 . LEU A 328 ? 2.0296 0.5838 0.6454 -0.2060 -0.2016 -0.0303 624 LEU A CD1 
2556 C CD2 . LEU A 328 ? 2.1094 0.7991 0.8189 -0.3346 -0.2131 -0.0144 624 LEU A CD2 
2557 N N   . TRP A 329 ? 2.2952 0.7680 0.7138 -0.4787 -0.2290 0.0346  625 TRP A N   
2558 C CA  . TRP A 329 ? 2.4595 0.8869 0.8162 -0.5025 -0.2307 0.0438  625 TRP A CA  
2559 C C   . TRP A 329 ? 2.3801 0.9029 0.8431 -0.4907 -0.2233 0.0397  625 TRP A C   
2560 O O   . TRP A 329 ? 2.3556 0.8267 0.7783 -0.4680 -0.2219 0.0398  625 TRP A O   
2561 C CB  . TRP A 329 ? 2.5780 1.0043 0.8780 -0.5872 -0.2375 0.0596  625 TRP A CB  
2562 C CG  . TRP A 329 ? 2.4314 1.0100 0.8458 -0.6396 -0.2357 0.0634  625 TRP A CG  
2563 C CD1 . TRP A 329 ? 2.4719 1.1110 0.9303 -0.6594 -0.2379 0.0628  625 TRP A CD1 
2564 C CD2 . TRP A 329 ? 2.3937 1.0859 0.8879 -0.6761 -0.2316 0.0687  625 TRP A CD2 
2565 N NE1 . TRP A 329 ? 2.3923 1.1788 0.9535 -0.7026 -0.2357 0.0673  625 TRP A NE1 
2566 C CE2 . TRP A 329 ? 2.3004 1.1233 0.8859 -0.7128 -0.2313 0.0711  625 TRP A CE2 
2567 C CE3 . TRP A 329 ? 2.3499 1.0482 0.8469 -0.6784 -0.2280 0.0713  625 TRP A CE3 
2568 C CZ2 . TRP A 329 ? 2.1981 1.1600 0.8761 -0.7478 -0.2271 0.0764  625 TRP A CZ2 
2569 C CZ3 . TRP A 329 ? 2.1478 0.9804 0.7366 -0.7173 -0.2236 0.0766  625 TRP A CZ3 
2570 C CH2 . TRP A 329 ? 2.1515 1.1159 0.8297 -0.7494 -0.2229 0.0791  625 TRP A CH2 
2571 N N   . LYS A 330 ? 2.3433 1.0036 0.9385 -0.5042 -0.2191 0.0362  626 LYS A N   
2572 C CA  . LYS A 330 ? 2.2669 1.0195 0.9649 -0.4928 -0.2122 0.0329  626 LYS A CA  
2573 C C   . LYS A 330 ? 2.1554 0.8687 0.8659 -0.4160 -0.2063 0.0204  626 LYS A C   
2574 O O   . LYS A 330 ? 2.1651 0.8789 0.8884 -0.3999 -0.2024 0.0203  626 LYS A O   
2575 C CB  . LYS A 330 ? 2.2035 1.1061 1.0327 -0.5147 -0.2101 0.0313  626 LYS A CB  
2576 C CG  . LYS A 330 ? 2.1977 1.1863 1.0483 -0.5867 -0.2128 0.0443  626 LYS A CG  
2577 C CD  . LYS A 330 ? 2.0024 1.1481 0.9885 -0.5932 -0.2103 0.0418  626 LYS A CD  
2578 C CE  . LYS A 330 ? 1.9494 1.1939 0.9583 -0.6573 -0.2118 0.0545  626 LYS A CE  
2579 N NZ  . LYS A 330 ? 1.7999 1.2025 0.9380 -0.6548 -0.2094 0.0526  626 LYS A NZ  
2580 N N   . ASP A 331 ? 2.1926 0.8783 0.9014 -0.3674 -0.2049 0.0097  627 ASP A N   
2581 C CA  . ASP A 331 ? 2.1490 0.8055 0.8665 -0.2905 -0.1980 -0.0023 627 ASP A CA  
2582 C C   . ASP A 331 ? 2.2308 0.7729 0.8367 -0.2608 -0.1996 0.0008  627 ASP A C   
2583 O O   . ASP A 331 ? 2.2187 0.7619 0.8414 -0.2230 -0.1948 -0.0026 627 ASP A O   
2584 C CB  . ASP A 331 ? 2.0907 0.7373 0.8122 -0.2460 -0.1957 -0.0137 627 ASP A CB  
2585 C CG  . ASP A 331 ? 2.0489 0.8041 0.8736 -0.2717 -0.1956 -0.0179 627 ASP A CG  
2586 O OD1 . ASP A 331 ? 2.0173 0.8114 0.8511 -0.3336 -0.2021 -0.0088 627 ASP A OD1 
2587 O OD2 . ASP A 331 ? 1.9956 0.8007 0.8894 -0.2297 -0.1892 -0.0299 627 ASP A OD2 
2588 N N   . GLN A 332 ? 2.2631 0.7033 0.7487 -0.2773 -0.2073 0.0078  628 GLN A N   
2589 C CA  . GLN A 332 ? 2.5186 0.8381 0.8802 -0.2465 -0.2111 0.0108  628 GLN A CA  
2590 C C   . GLN A 332 ? 2.4231 0.7444 0.7760 -0.2764 -0.2122 0.0179  628 GLN A C   
2591 O O   . GLN A 332 ? 2.4328 0.7082 0.7490 -0.2289 -0.2107 0.0145  628 GLN A O   
2592 C CB  . GLN A 332 ? 2.7266 0.9343 0.9550 -0.2695 -0.2206 0.0189  628 GLN A CB  
2593 C CG  . GLN A 332 ? 2.8431 0.9348 0.9606 -0.1977 -0.2226 0.0147  628 GLN A CG  
2594 C CD  . GLN A 332 ? 2.9757 0.9695 0.9812 -0.2114 -0.2307 0.0208  628 GLN A CD  
2595 O OE1 . GLN A 332 ? 2.9564 0.9617 0.9576 -0.2807 -0.2356 0.0291  628 GLN A OE1 
2596 N NE2 . GLN A 332 ? 3.1633 1.0677 1.0829 -0.1432 -0.2317 0.0160  628 GLN A NE2 
2597 N N   . ALA A 333 ? 2.3557 0.7364 0.7426 -0.3530 -0.2144 0.0277  629 ALA A N   
2598 C CA  . ALA A 333 ? 2.3710 0.7620 0.7533 -0.3836 -0.2145 0.0344  629 ALA A CA  
2599 C C   . ALA A 333 ? 2.3837 0.8618 0.8817 -0.3480 -0.2054 0.0271  629 ALA A C   
2600 O O   . ALA A 333 ? 2.4212 0.8863 0.9049 -0.3475 -0.2045 0.0296  629 ALA A O   
2601 C CB  . ALA A 333 ? 2.3709 0.8218 0.7672 -0.4722 -0.2176 0.0468  629 ALA A CB  
2602 N N   . LEU A 334 ? 2.1129 0.6751 0.7194 -0.3192 -0.1990 0.0181  630 LEU A N   
2603 C CA  . LEU A 334 ? 2.0130 0.6557 0.7267 -0.2869 -0.1907 0.0117  630 LEU A CA  
2604 C C   . LEU A 334 ? 2.0999 0.6782 0.7732 -0.2094 -0.1874 0.0039  630 LEU A C   
2605 O O   . LEU A 334 ? 2.2779 0.8763 0.9815 -0.1935 -0.1836 0.0041  630 LEU A O   
2606 C CB  . LEU A 334 ? 1.9146 0.6565 0.7414 -0.2799 -0.1862 0.0040  630 LEU A CB  
2607 C CG  . LEU A 334 ? 1.8870 0.7192 0.8271 -0.2589 -0.1786 -0.0009 630 LEU A CG  
2608 C CD1 . LEU A 334 ? 1.8153 0.7377 0.8199 -0.3220 -0.1790 0.0088  630 LEU A CD1 
2609 C CD2 . LEU A 334 ? 1.7470 0.6488 0.7713 -0.2218 -0.1728 -0.0109 630 LEU A CD2 
2610 N N   . VAL A 335 ? 2.1628 0.6691 0.7668 -0.1584 -0.1886 -0.0025 631 VAL A N   
2611 C CA  . VAL A 335 ? 2.3009 0.7631 0.8684 -0.0773 -0.1852 -0.0100 631 VAL A CA  
2612 C C   . VAL A 335 ? 2.4137 0.7917 0.8823 -0.0780 -0.1910 -0.0039 631 VAL A C   
2613 O O   . VAL A 335 ? 2.3760 0.7626 0.8587 -0.0320 -0.1873 -0.0076 631 VAL A O   
2614 C CB  . VAL A 335 ? 2.4209 0.8331 0.9318 -0.0232 -0.1852 -0.0172 631 VAL A CB  
2615 C CG1 . VAL A 335 ? 2.4878 0.8534 0.9405 0.0588  -0.1834 -0.0227 631 VAL A CG1 
2616 C CG2 . VAL A 335 ? 2.3148 0.8177 0.9308 -0.0087 -0.1774 -0.0264 631 VAL A CG2 
2617 N N   . GLU A 336 ? 2.4675 0.7639 0.8316 -0.1305 -0.2005 0.0053  632 GLU A N   
2618 C CA  . GLU A 336 ? 2.6420 0.8521 0.9025 -0.1368 -0.2069 0.0102  632 GLU A CA  
2619 C C   . GLU A 336 ? 2.4972 0.7769 0.8351 -0.1607 -0.2024 0.0130  632 GLU A C   
2620 O O   . GLU A 336 ? 2.4570 0.7026 0.7614 -0.1246 -0.2025 0.0106  632 GLU A O   
2621 C CB  . GLU A 336 ? 2.8914 1.0122 1.0318 -0.2025 -0.2176 0.0206  632 GLU A CB  
2622 C CG  . GLU A 336 ? 3.0271 1.1059 1.1183 -0.2082 -0.2218 0.0219  632 GLU A CG  
2623 C CD  . GLU A 336 ? 3.2339 1.2255 1.2414 -0.1281 -0.2234 0.0143  632 GLU A CD  
2624 O OE1 . GLU A 336 ? 3.3566 1.3011 1.3194 -0.0780 -0.2231 0.0090  632 GLU A OE1 
2625 O OE2 . GLU A 336 ? 3.2763 1.2572 1.2749 -0.1141 -0.2236 0.0127  632 GLU A OE2 
2626 N N   . ILE A 337 ? 2.4171 0.7971 0.8570 -0.2202 -0.1987 0.0183  633 ILE A N   
2627 C CA  . ILE A 337 ? 2.3333 0.7821 0.8431 -0.2503 -0.1946 0.0231  633 ILE A CA  
2628 C C   . ILE A 337 ? 2.3162 0.8078 0.9001 -0.1834 -0.1868 0.0154  633 ILE A C   
2629 O O   . ILE A 337 ? 2.3785 0.8637 0.9573 -0.1767 -0.1858 0.0176  633 ILE A O   
2630 C CB  . ILE A 337 ? 2.1184 0.6808 0.7281 -0.3189 -0.1916 0.0296  633 ILE A CB  
2631 C CG1 . ILE A 337 ? 2.2059 0.7342 0.7351 -0.3928 -0.1993 0.0400  633 ILE A CG1 
2632 C CG2 . ILE A 337 ? 2.1681 0.8253 0.8772 -0.3350 -0.1849 0.0327  633 ILE A CG2 
2633 C CD1 . ILE A 337 ? 2.1902 0.8347 0.8098 -0.4503 -0.1972 0.0453  633 ILE A CD1 
2634 N N   . ASN A 338 ? 2.2191 0.7551 0.8689 -0.1331 -0.1812 0.0065  634 ASN A N   
2635 C CA  . ASN A 338 ? 2.0594 0.6463 0.7820 -0.0690 -0.1735 -0.0003 634 ASN A CA  
2636 C C   . ASN A 338 ? 2.1923 0.7056 0.8300 0.0042  -0.1752 -0.0059 634 ASN A C   
2637 O O   . ASN A 338 ? 2.1503 0.6957 0.8249 0.0463  -0.1711 -0.0080 634 ASN A O   
2638 C CB  . ASN A 338 ? 1.9765 0.6429 0.7965 -0.0435 -0.1668 -0.0084 634 ASN A CB  
2639 C CG  . ASN A 338 ? 1.8454 0.6058 0.7690 -0.1049 -0.1645 -0.0043 634 ASN A CG  
2640 O OD1 . ASN A 338 ? 1.7577 0.6352 0.7909 -0.0988 -0.1557 -0.0016 634 ASN A OD1 
2641 N ND2 . ASN A 338 ? 1.7637 0.5277 0.6754 -0.1591 -0.1690 -0.0010 634 ASN A ND2 
2642 N N   . ILE A 339 ? 2.2687 0.6873 0.7910 0.0219  -0.1818 -0.0081 635 ILE A N   
2643 C CA  . ILE A 339 ? 2.3032 0.6468 0.7290 0.0857  -0.1853 -0.0127 635 ILE A CA  
2644 C C   . ILE A 339 ? 2.3568 0.6526 0.7290 0.0567  -0.1903 -0.0070 635 ILE A C   
2645 O O   . ILE A 339 ? 2.3968 0.6802 0.7471 0.1089  -0.1899 -0.0112 635 ILE A O   
2646 C CB  . ILE A 339 ? 2.3767 0.6173 0.6750 0.1072  -0.1927 -0.0149 635 ILE A CB  
2647 C CG1 . ILE A 339 ? 2.3108 0.6004 0.6586 0.1496  -0.1867 -0.0218 635 ILE A CG1 
2648 C CG2 . ILE A 339 ? 2.5113 0.6670 0.6949 0.1693  -0.1980 -0.0192 635 ILE A CG2 
2649 C CD1 . ILE A 339 ? 2.5395 0.7290 0.7633 0.1711  -0.1939 -0.0222 635 ILE A CD1 
2650 N N   . ALA A 340 ? 2.3661 0.6470 0.7233 -0.0272 -0.1944 0.0025  636 ALA A N   
2651 C CA  . ALA A 340 ? 2.5131 0.7460 0.8106 -0.0657 -0.1993 0.0083  636 ALA A CA  
2652 C C   . ALA A 340 ? 2.4730 0.7964 0.8794 -0.0699 -0.1919 0.0112  636 ALA A C   
2653 O O   . ALA A 340 ? 2.3614 0.6505 0.7285 -0.0518 -0.1936 0.0108  636 ALA A O   
2654 C CB  . ALA A 340 ? 2.5538 0.7539 0.7980 -0.1557 -0.2058 0.0179  636 ALA A CB  
2655 N N   . VAL A 341 ? 2.4063 0.8411 0.9432 -0.0961 -0.1843 0.0145  637 VAL A N   
2656 C CA  . VAL A 341 ? 2.2112 0.7303 0.8497 -0.0945 -0.1773 0.0180  637 VAL A CA  
2657 C C   . VAL A 341 ? 2.2583 0.7787 0.9054 -0.0074 -0.1746 0.0106  637 VAL A C   
2658 O O   . VAL A 341 ? 2.3876 0.9030 1.0281 0.0066  -0.1745 0.0129  637 VAL A O   
2659 C CB  . VAL A 341 ? 2.0696 0.7038 0.8407 -0.1250 -0.1702 0.0204  637 VAL A CB  
2660 C CG1 . VAL A 341 ? 1.9991 0.7121 0.8700 -0.1000 -0.1631 0.0220  637 VAL A CG1 
2661 C CG2 . VAL A 341 ? 2.0786 0.7434 0.8577 -0.2143 -0.1719 0.0294  637 VAL A CG2 
2662 N N   . LEU A 342 ? 2.1334 0.6691 0.7961 0.0528  -0.1721 0.0014  638 LEU A N   
2663 C CA  . LEU A 342 ? 2.1021 0.6586 0.7737 0.1388  -0.1693 -0.0064 638 LEU A CA  
2664 C C   . LEU A 342 ? 2.2552 0.7159 0.8051 0.1661  -0.1764 -0.0089 638 LEU A C   
2665 O O   . LEU A 342 ? 2.2022 0.6798 0.7635 0.1929  -0.1758 -0.0085 638 LEU A O   
2666 C CB  . LEU A 342 ? 2.1178 0.7028 0.8061 0.1936  -0.1657 -0.0161 638 LEU A CB  
2667 C CG  . LEU A 342 ? 1.9438 0.6272 0.7526 0.1833  -0.1580 -0.0173 638 LEU A CG  
2668 C CD1 . LEU A 342 ? 1.8999 0.6084 0.7112 0.2448  -0.1540 -0.0279 638 LEU A CD1 
2669 C CD2 . LEU A 342 ? 1.8135 0.5996 0.7340 0.1904  -0.1518 -0.0143 638 LEU A CD2 
2670 N N   . TYR A 343 ? 2.3206 0.6757 0.7469 0.1587  -0.1841 -0.0114 639 TYR A N   
2671 C CA  . TYR A 343 ? 2.6052 0.8547 0.8982 0.1888  -0.1921 -0.0156 639 TYR A CA  
2672 C C   . TYR A 343 ? 2.5555 0.7845 0.8348 0.1529  -0.1943 -0.0101 639 TYR A C   
2673 O O   . TYR A 343 ? 2.7100 0.9106 0.9445 0.2003  -0.1964 -0.0152 639 TYR A O   
2674 C CB  . TYR A 343 ? 2.8209 0.9495 0.9760 0.1649  -0.2016 -0.0159 639 TYR A CB  
2675 C CG  . TYR A 343 ? 2.9248 0.9334 0.9368 0.1864  -0.2103 -0.0196 639 TYR A CG  
2676 C CD1 . TYR A 343 ? 2.9615 0.9559 0.9372 0.2740  -0.2097 -0.0285 639 TYR A CD1 
2677 C CD2 . TYR A 343 ? 3.0105 0.9401 0.9519 0.1182  -0.2162 -0.0128 639 TYR A CD2 
2678 C CE1 . TYR A 343 ? 3.1434 1.0389 1.0117 0.2950  -0.2155 -0.0307 639 TYR A CE1 
2679 C CE2 . TYR A 343 ? 3.2187 1.0454 1.0506 0.1371  -0.2219 -0.0151 639 TYR A CE2 
2680 C CZ  . TYR A 343 ? 3.3106 1.1164 1.1046 0.2267  -0.2219 -0.0242 639 TYR A CZ  
2681 O OH  . TYR A 343 ? 3.5096 1.2088 1.1892 0.2480  -0.2283 -0.0267 639 TYR A OH  
2682 N N   . SER A 344 ? 2.4158 0.6667 0.7356 0.0702  -0.1936 0.0003  640 SER A N   
2683 C CA  . SER A 344 ? 2.4077 0.6371 0.7063 0.0282  -0.1956 0.0064  640 SER A CA  
2684 C C   . SER A 344 ? 2.3053 0.6186 0.7005 0.0673  -0.1888 0.0077  640 SER A C   
2685 O O   . SER A 344 ? 2.3207 0.5951 0.6683 0.0859  -0.1916 0.0065  640 SER A O   
2686 C CB  . SER A 344 ? 2.4059 0.6633 0.7351 -0.0692 -0.1950 0.0176  640 SER A CB  
2687 O OG  . SER A 344 ? 2.5439 0.7314 0.7850 -0.1062 -0.2020 0.0175  640 SER A OG  
2688 N N   . PHE A 345 ? 2.2539 0.6808 0.7815 0.0782  -0.1805 0.0105  641 PHE A N   
2689 C CA  . PHE A 345 ? 2.2306 0.7453 0.8542 0.1136  -0.1748 0.0133  641 PHE A CA  
2690 C C   . PHE A 345 ? 2.3577 0.8654 0.9481 0.2033  -0.1764 0.0027  641 PHE A C   
2691 O O   . PHE A 345 ? 2.3449 0.8728 0.9481 0.2270  -0.1765 0.0043  641 PHE A O   
2692 C CB  . PHE A 345 ? 2.0644 0.6925 0.8224 0.1104  -0.1671 0.0164  641 PHE A CB  
2693 C CG  . PHE A 345 ? 1.8844 0.5608 0.7107 0.0302  -0.1634 0.0287  641 PHE A CG  
2694 C CD1 . PHE A 345 ? 1.9103 0.5580 0.7045 -0.0436 -0.1651 0.0323  641 PHE A CD1 
2695 C CD2 . PHE A 345 ? 1.7973 0.6104 0.7491 0.0283  -0.1542 0.0301  641 PHE A CD2 
2696 C CE1 . PHE A 345 ? 1.8646 0.5837 0.7306 -0.1152 -0.1603 0.0416  641 PHE A CE1 
2697 C CE2 . PHE A 345 ? 1.6367 0.5365 0.6686 -0.0399 -0.1474 0.0360  641 PHE A CE2 
2698 C CZ  . PHE A 345 ? 1.7424 0.6005 0.7334 -0.1094 -0.1502 0.0418  641 PHE A CZ  
2699 N N   . GLN A 346 ? 2.3588 0.8443 0.9053 0.2539  -0.1776 -0.0081 642 GLN A N   
2700 C CA  . GLN A 346 ? 2.3950 0.8967 0.9179 0.3410  -0.1778 -0.0188 642 GLN A CA  
2701 C C   . GLN A 346 ? 2.4658 0.8576 0.8583 0.3562  -0.1857 -0.0232 642 GLN A C   
2702 O O   . GLN A 346 ? 2.4059 0.8242 0.7973 0.4114  -0.1858 -0.0283 642 GLN A O   
2703 C CB  . GLN A 346 ? 2.4145 0.9258 0.9204 0.3890  -0.1763 -0.0283 642 GLN A CB  
2704 C CG  . GLN A 346 ? 2.3766 0.9874 0.9999 0.3778  -0.1686 -0.0264 642 GLN A CG  
2705 C CD  . GLN A 346 ? 2.4738 1.0603 1.0535 0.4032  -0.1685 -0.0337 642 GLN A CD  
2706 O OE1 . GLN A 346 ? 2.6108 1.1241 1.1378 0.3557  -0.1722 -0.0307 642 GLN A OE1 
2707 N NE2 . GLN A 346 ? 2.4424 1.0945 1.0404 0.4769  -0.1645 -0.0427 642 GLN A NE2 
2708 N N   . SER A 347 ? 2.5527 0.8211 0.8284 0.3098  -0.1930 -0.0224 643 SER A N   
2709 C CA  . SER A 347 ? 2.6978 0.8476 0.8352 0.3217  -0.2015 -0.0279 643 SER A CA  
2710 C C   . SER A 347 ? 2.7085 0.8613 0.8656 0.2886  -0.2016 -0.0211 643 SER A C   
2711 O O   . SER A 347 ? 2.7466 0.8042 0.7951 0.2972  -0.2082 -0.0259 643 SER A O   
2712 C CB  . SER A 347 ? 2.7833 0.7998 0.7850 0.2752  -0.2104 -0.0284 643 SER A CB  
2713 O OG  . SER A 347 ? 2.8490 0.8555 0.8287 0.3086  -0.2102 -0.0322 643 SER A OG  
2714 N N   . ASP A 348 ? 2.6397 0.8962 0.9275 0.2517  -0.1945 -0.0099 644 ASP A N   
2715 C CA  . ASP A 348 ? 2.6806 0.9578 1.0027 0.2199  -0.1933 -0.0009 644 ASP A CA  
2716 C C   . ASP A 348 ? 2.5926 0.9892 1.0283 0.2725  -0.1877 0.0009  644 ASP A C   
2717 O O   . ASP A 348 ? 2.3784 0.8149 0.8661 0.2450  -0.1857 0.0112  644 ASP A O   
2718 C CB  . ASP A 348 ? 2.5887 0.8890 0.9597 0.1253  -0.1903 0.0129  644 ASP A CB  
2719 C CG  . ASP A 348 ? 2.6522 0.8404 0.9048 0.0595  -0.1973 0.0127  644 ASP A CG  
2720 O OD1 . ASP A 348 ? 2.7352 0.8119 0.8577 0.0868  -0.2055 0.0022  644 ASP A OD1 
2721 O OD2 . ASP A 348 ? 2.5598 0.7768 0.8475 -0.0203 -0.1949 0.0230  644 ASP A OD2 
2722 N N   . LYS A 349 ? 2.6980 1.1604 1.1741 0.3443  -0.1852 -0.0083 645 LYS A N   
2723 C CA  . LYS A 349 ? 2.6621 1.2549 1.2501 0.3932  -0.1806 -0.0079 645 LYS A CA  
2724 C C   . LYS A 349 ? 2.4050 1.0906 1.1172 0.3452  -0.1756 0.0061  645 LYS A C   
2725 O O   . LYS A 349 ? 2.1904 0.9652 0.9817 0.3633  -0.1742 0.0107  645 LYS A O   
2726 C CB  . LYS A 349 ? 2.8436 1.4231 1.3927 0.4315  -0.1843 -0.0110 645 LYS A CB  
2727 C CG  . LYS A 349 ? 2.8776 1.5669 1.4838 0.5123  -0.1820 -0.0205 645 LYS A CG  
2728 C CD  . LYS A 349 ? 3.0307 1.6726 1.5430 0.5754  -0.1840 -0.0362 645 LYS A CD  
2729 C CE  . LYS A 349 ? 2.9752 1.7488 1.5527 0.6500  -0.1801 -0.0456 645 LYS A CE  
2730 N NZ  . LYS A 349 ? 2.8247 1.7218 1.5181 0.6498  -0.1728 -0.0447 645 LYS A NZ  
2731 N N   . VAL A 350 ? 2.3180 0.9860 1.0452 0.2841  -0.1734 0.0127  646 VAL A N   
2732 C CA  . VAL A 350 ? 2.0497 0.7974 0.8838 0.2367  -0.1687 0.0257  646 VAL A CA  
2733 C C   . VAL A 350 ? 1.9359 0.7874 0.8672 0.2590  -0.1619 0.0173  646 VAL A C   
2734 O O   . VAL A 350 ? 2.0343 0.8342 0.9258 0.2577  -0.1632 0.0139  646 VAL A O   
2735 C CB  . VAL A 350 ? 1.9145 0.6042 0.7166 0.1458  -0.1681 0.0360  646 VAL A CB  
2736 C CG1 . VAL A 350 ? 1.7276 0.5650 0.6753 0.0950  -0.1562 0.0378  646 VAL A CG1 
2737 C CG2 . VAL A 350 ? 2.0873 0.6967 0.8012 0.1172  -0.1720 0.0397  646 VAL A CG2 
2738 N N   . THR A 351 ? 1.8139 0.8153 0.8717 0.2745  -0.1538 0.0126  647 THR A N   
2739 C CA  . THR A 351 ? 1.7026 0.8162 0.8543 0.2997  -0.1464 0.0030  647 THR A CA  
2740 C C   . THR A 351 ? 1.7272 0.8483 0.9119 0.2461  -0.1409 0.0034  647 THR A C   
2741 O O   . THR A 351 ? 1.7457 0.8796 0.9626 0.1805  -0.1374 0.0100  647 THR A O   
2742 C CB  . THR A 351 ? 1.5248 0.7895 0.8017 0.3038  -0.1390 0.0000  647 THR A CB  
2743 O OG1 . THR A 351 ? 1.6060 0.8680 0.8516 0.3513  -0.1453 -0.0001 647 THR A OG1 
2744 C CG2 . THR A 351 ? 1.3538 0.7335 0.7201 0.3277  -0.1315 -0.0094 647 THR A CG2 
2745 N N   . ILE A 352 ? 1.7255 0.8407 0.8979 0.2771  -0.1404 -0.0037 648 ILE A N   
2746 C CA  . ILE A 352 ? 1.5403 0.6747 0.7496 0.2360  -0.1354 -0.0048 648 ILE A CA  
2747 C C   . ILE A 352 ? 1.5981 0.7803 0.8299 0.2901  -0.1320 -0.0148 648 ILE A C   
2748 O O   . ILE A 352 ? 1.6364 0.8003 0.8203 0.3575  -0.1357 -0.0203 648 ILE A O   
2749 C CB  . ILE A 352 ? 1.6907 0.6855 0.7906 0.1924  -0.1431 0.0011  648 ILE A CB  
2750 C CG1 . ILE A 352 ? 1.5565 0.5902 0.7089 0.1383  -0.1383 0.0015  648 ILE A CG1 
2751 C CG2 . ILE A 352 ? 1.7118 0.5787 0.6817 0.2471  -0.1521 -0.0036 648 ILE A CG2 
2752 C CD1 . ILE A 352 ? 1.7054 0.6368 0.7760 0.0717  -0.1451 0.0095  648 ILE A CD1 
2753 N N   . VAL A 353 ? 1.5069 0.7542 0.8093 0.2627  -0.1248 -0.0172 649 VAL A N   
2754 C CA  . VAL A 353 ? 1.4513 0.7500 0.7785 0.3052  -0.1200 -0.0260 649 VAL A CA  
2755 C C   . VAL A 353 ? 1.4916 0.7377 0.7900 0.2743  -0.1203 -0.0263 649 VAL A C   
2756 O O   . VAL A 353 ? 1.3823 0.6321 0.7114 0.2115  -0.1194 -0.0205 649 VAL A O   
2757 C CB  . VAL A 353 ? 1.3477 0.8033 0.8040 0.3067  -0.1097 -0.0292 649 VAL A CB  
2758 C CG1 . VAL A 353 ? 1.2329 0.7427 0.7714 0.2399  -0.1041 -0.0242 649 VAL A CG1 
2759 C CG2 . VAL A 353 ? 1.3277 0.8424 0.8032 0.3519  -0.1041 -0.0379 649 VAL A CG2 
2760 N N   . ASP A 354 ? 1.5490 0.7460 0.7831 0.3209  -0.1221 -0.0334 650 ASP A N   
2761 C CA  . ASP A 354 ? 1.6117 0.7618 0.8160 0.2984  -0.1225 -0.0352 650 ASP A CA  
2762 C C   . ASP A 354 ? 1.4787 0.7595 0.7982 0.2881  -0.1113 -0.0382 650 ASP A C   
2763 O O   . ASP A 354 ? 1.4054 0.7990 0.8056 0.3125  -0.1037 -0.0410 650 ASP A O   
2764 C CB  . ASP A 354 ? 1.7813 0.8192 0.8621 0.3552  -0.1287 -0.0422 650 ASP A CB  
2765 C CG  . ASP A 354 ? 1.8314 0.9518 0.9405 0.4308  -0.1217 -0.0522 650 ASP A CG  
2766 O OD1 . ASP A 354 ? 1.8870 0.9884 0.9395 0.4898  -0.1248 -0.0559 650 ASP A OD1 
2767 O OD2 . ASP A 354 ? 1.7339 0.9532 0.9242 0.4251  -0.1122 -0.0556 650 ASP A OD2 
2768 N N   . HIS A 355 ? 1.4239 0.6874 0.7464 0.2482  -0.1111 -0.0372 651 HIS A N   
2769 C CA  . HIS A 355 ? 1.2525 0.6306 0.6807 0.2294  -0.1015 -0.0380 651 HIS A CA  
2770 C C   . HIS A 355 ? 1.4124 0.8480 0.8568 0.2830  -0.0939 -0.0466 651 HIS A C   
2771 O O   . HIS A 355 ? 1.4086 0.9487 0.9416 0.2729  -0.0849 -0.0472 651 HIS A O   
2772 C CB  . HIS A 355 ? 1.3314 0.6781 0.7562 0.1729  -0.1045 -0.0339 651 HIS A CB  
2773 C CG  . HIS A 355 ? 1.4320 0.6561 0.7442 0.1780  -0.1126 -0.0370 651 HIS A CG  
2774 N ND1 . HIS A 355 ? 1.5637 0.6623 0.7694 0.1651  -0.1235 -0.0341 651 HIS A ND1 
2775 C CD2 . HIS A 355 ? 1.5183 0.7192 0.8002 0.1922  -0.1118 -0.0427 651 HIS A CD2 
2776 C CE1 . HIS A 355 ? 1.7502 0.7485 0.8614 0.1704  -0.1297 -0.0382 651 HIS A CE1 
2777 N NE2 . HIS A 355 ? 1.5794 0.6392 0.7361 0.1895  -0.1226 -0.0439 651 HIS A NE2 
2778 N N   . HIS A 356 ? 1.4467 0.8156 0.8024 0.3404  -0.0973 -0.0532 652 HIS A N   
2779 C CA  . HIS A 356 ? 1.3799 0.8188 0.7508 0.3983  -0.0892 -0.0619 652 HIS A CA  
2780 C C   . HIS A 356 ? 1.3625 0.9093 0.7936 0.4326  -0.0841 -0.0636 652 HIS A C   
2781 O O   . HIS A 356 ? 1.3182 0.9869 0.8281 0.4397  -0.0740 -0.0664 652 HIS A O   
2782 C CB  . HIS A 356 ? 1.5577 0.8877 0.8057 0.4542  -0.0948 -0.0693 652 HIS A CB  
2783 C CG  . HIS A 356 ? 1.6263 0.8391 0.8011 0.4184  -0.1015 -0.0683 652 HIS A CG  
2784 N ND1 . HIS A 356 ? 1.5881 0.8265 0.7864 0.4022  -0.0962 -0.0709 652 HIS A ND1 
2785 C CD2 . HIS A 356 ? 1.7154 0.7858 0.7913 0.3908  -0.1137 -0.0645 652 HIS A CD2 
2786 C CE1 . HIS A 356 ? 1.6886 0.8082 0.8075 0.3679  -0.1055 -0.0694 652 HIS A CE1 
2787 N NE2 . HIS A 356 ? 1.7705 0.7869 0.8131 0.3580  -0.1161 -0.0654 652 HIS A NE2 
2788 N N   . SER A 357 ? 1.3946 0.8984 0.7861 0.4508  -0.0914 -0.0615 653 SER A N   
2789 C CA  . SER A 357 ? 1.4034 1.0113 0.8508 0.4807  -0.0882 -0.0629 653 SER A CA  
2790 C C   . SER A 357 ? 1.1520 0.8648 0.7152 0.4243  -0.0818 -0.0576 653 SER A C   
2791 O O   . SER A 357 ? 1.1643 0.9989 0.7990 0.4357  -0.0747 -0.0604 653 SER A O   
2792 C CB  . SER A 357 ? 1.4070 0.9389 0.7818 0.5115  -0.0985 -0.0612 653 SER A CB  
2793 O OG  . SER A 357 ? 1.4514 1.0895 0.8659 0.5591  -0.0959 -0.0653 653 SER A OG  
2794 N N   . ALA A 358 ? 1.1047 0.7728 0.6829 0.3630  -0.0844 -0.0502 654 ALA A N   
2795 C CA  . ALA A 358 ? 1.0894 0.8449 0.7666 0.3145  -0.0790 -0.0457 654 ALA A CA  
2796 C C   . ALA A 358 ? 1.0222 0.8647 0.7664 0.3006  -0.0693 -0.0480 654 ALA A C   
2797 O O   . ALA A 358 ? 0.8275 0.7698 0.6447 0.2906  -0.0631 -0.0483 654 ALA A O   
2798 C CB  . ALA A 358 ? 1.0982 0.7916 0.7712 0.2579  -0.0837 -0.0378 654 ALA A CB  
2799 N N   . THR A 359 ? 1.0322 0.8342 0.7468 0.2977  -0.0682 -0.0495 655 THR A N   
2800 C CA  . THR A 359 ? 0.9745 0.8527 0.7480 0.2812  -0.0591 -0.0505 655 THR A CA  
2801 C C   . THR A 359 ? 0.9375 0.9055 0.7286 0.3249  -0.0513 -0.0573 655 THR A C   
2802 O O   . THR A 359 ? 0.8669 0.9286 0.7239 0.3057  -0.0430 -0.0570 655 THR A O   
2803 C CB  . THR A 359 ? 0.9964 0.8091 0.7336 0.2642  -0.0606 -0.0500 655 THR A CB  
2804 O OG1 . THR A 359 ? 1.0531 0.7837 0.6988 0.3071  -0.0653 -0.0553 655 THR A OG1 
2805 C CG2 . THR A 359 ? 0.8413 0.6016 0.5820 0.2122  -0.0670 -0.0426 655 THR A CG2 
2806 N N   . GLU A 360 ? 1.0724 1.0155 0.8014 0.3836  -0.0541 -0.0633 656 GLU A N   
2807 C CA  . GLU A 360 ? 1.1377 1.1872 0.8882 0.4287  -0.0468 -0.0698 656 GLU A CA  
2808 C C   . GLU A 360 ? 1.0529 1.2051 0.8736 0.4151  -0.0449 -0.0681 656 GLU A C   
2809 O O   . GLU A 360 ? 1.0131 1.2820 0.8908 0.4096  -0.0363 -0.0701 656 GLU A O   
2810 C CB  . GLU A 360 ? 1.2898 1.2906 0.9532 0.5030  -0.0515 -0.0769 656 GLU A CB  
2811 C CG  . GLU A 360 ? 1.4539 1.5737 1.1344 0.5556  -0.0429 -0.0847 656 GLU A CG  
2812 C CD  . GLU A 360 ? 1.7073 1.8223 1.3276 0.6323  -0.0491 -0.0906 656 GLU A CD  
2813 O OE1 . GLU A 360 ? 1.7622 2.0002 1.4130 0.6532  -0.0442 -0.0930 656 GLU A OE1 
2814 O OE2 . GLU A 360 ? 1.8549 1.8387 1.3910 0.6492  -0.0601 -0.0892 656 GLU A OE2 
2815 N N   . SER A 361 ? 1.0481 1.1583 0.8619 0.4058  -0.0529 -0.0643 657 SER A N   
2816 C CA  A SER A 361 ? 0.9369 1.1381 0.8110 0.3930  -0.0522 -0.0633 657 SER A CA  
2817 C CA  B SER A 361 ? 0.9377 1.1372 0.8117 0.3922  -0.0523 -0.0632 657 SER A CA  
2818 C C   . SER A 361 ? 0.8638 1.1236 0.8142 0.3304  -0.0456 -0.0592 657 SER A C   
2819 O O   . SER A 361 ? 0.8557 1.2164 0.8588 0.3180  -0.0417 -0.0603 657 SER A O   
2820 C CB  A SER A 361 ? 0.9268 1.0612 0.7719 0.3947  -0.0621 -0.0598 657 SER A CB  
2821 C CB  B SER A 361 ? 0.9238 1.0538 0.7700 0.3906  -0.0622 -0.0593 657 SER A CB  
2822 O OG  A SER A 361 ? 0.9097 0.9780 0.6718 0.4545  -0.0692 -0.0631 657 SER A OG  
2823 O OG  B SER A 361 ? 0.8797 0.9518 0.7429 0.3339  -0.0638 -0.0524 657 SER A OG  
2824 N N   . PHE A 362 ? 0.7870 0.9841 0.7385 0.2911  -0.0451 -0.0547 658 PHE A N   
2825 C CA  . PHE A 362 ? 0.7368 0.9754 0.7487 0.2376  -0.0401 -0.0507 658 PHE A CA  
2826 C C   . PHE A 362 ? 0.7316 1.0509 0.7719 0.2325  -0.0304 -0.0531 658 PHE A C   
2827 O O   . PHE A 362 ? 0.6337 1.0193 0.7216 0.1983  -0.0259 -0.0515 658 PHE A O   
2828 C CB  . PHE A 362 ? 0.8008 0.9544 0.8032 0.2022  -0.0436 -0.0450 658 PHE A CB  
2829 C CG  . PHE A 362 ? 0.7643 0.9473 0.8171 0.1553  -0.0397 -0.0410 658 PHE A CG  
2830 C CD1 . PHE A 362 ? 0.7178 0.9168 0.8033 0.1297  -0.0414 -0.0385 658 PHE A CD1 
2831 C CD2 . PHE A 362 ? 0.7077 0.8977 0.7682 0.1395  -0.0345 -0.0399 658 PHE A CD2 
2832 C CE1 . PHE A 362 ? 0.6666 0.8808 0.7859 0.0918  -0.0385 -0.0353 658 PHE A CE1 
2833 C CE2 . PHE A 362 ? 0.6699 0.8763 0.7655 0.1001  -0.0318 -0.0359 658 PHE A CE2 
2834 C CZ  . PHE A 362 ? 0.7068 0.9222 0.8293 0.0775  -0.0340 -0.0338 658 PHE A CZ  
2835 N N   . ILE A 363 ? 0.7922 1.1048 0.7984 0.2649  -0.0270 -0.0569 659 ILE A N   
2836 C CA  . ILE A 363 ? 0.8443 1.2494 0.8749 0.2659  -0.0167 -0.0598 659 ILE A CA  
2837 C C   . ILE A 363 ? 0.7674 1.2887 0.8310 0.2781  -0.0138 -0.0632 659 ILE A C   
2838 O O   . ILE A 363 ? 0.7435 1.3497 0.8516 0.2420  -0.0072 -0.0618 659 ILE A O   
2839 C CB  . ILE A 363 ? 0.8776 1.2575 0.8583 0.3094  -0.0137 -0.0647 659 ILE A CB  
2840 C CG1 . ILE A 363 ? 0.9074 1.1843 0.8592 0.2872  -0.0164 -0.0612 659 ILE A CG1 
2841 C CG2 . ILE A 363 ? 0.9533 1.4483 0.9589 0.3171  -0.0018 -0.0684 659 ILE A CG2 
2842 C CD1 . ILE A 363 ? 0.7455 1.0526 0.7330 0.2432  -0.0091 -0.0571 659 ILE A CD1 
2843 N N   . LYS A 364 ? 0.8001 1.3250 0.8368 0.3275  -0.0196 -0.0674 660 LYS A N   
2844 C CA  . LYS A 364 ? 0.8342 1.4772 0.9022 0.3415  -0.0186 -0.0708 660 LYS A CA  
2845 C C   . LYS A 364 ? 0.6527 1.3228 0.7699 0.2851  -0.0207 -0.0663 660 LYS A C   
2846 O O   . LYS A 364 ? 0.6972 1.4772 0.8550 0.2619  -0.0162 -0.0673 660 LYS A O   
2847 C CB  . LYS A 364 ? 0.8522 1.4804 0.8749 0.4089  -0.0265 -0.0755 660 LYS A CB  
2848 C CG  . LYS A 364 ? 0.9106 1.6821 0.9609 0.4372  -0.0250 -0.0805 660 LYS A CG  
2849 C CD  . LYS A 364 ? 1.0379 1.7667 1.0256 0.4967  -0.0342 -0.0833 660 LYS A CD  
2850 C CE  . LYS A 364 ? 1.0894 1.9236 1.0921 0.4966  -0.0352 -0.0847 660 LYS A CE  
2851 N NZ  . LYS A 364 ? 1.0673 1.8806 1.0829 0.4831  -0.0440 -0.0822 660 LYS A NZ  
2852 N N   . HIS A 365 ? 0.7016 1.2739 0.8120 0.2606  -0.0274 -0.0616 661 HIS A N   
2853 C CA  . HIS A 365 ? 0.7220 1.3067 0.8716 0.2091  -0.0291 -0.0579 661 HIS A CA  
2854 C C   . HIS A 365 ? 0.6788 1.2958 0.8595 0.1564  -0.0215 -0.0550 661 HIS A C   
2855 O O   . HIS A 365 ? 0.6502 1.3322 0.8614 0.1203  -0.0199 -0.0548 661 HIS A O   
2856 C CB  . HIS A 365 ? 0.7332 1.2082 0.8660 0.1965  -0.0364 -0.0534 661 HIS A CB  
2857 C CG  . HIS A 365 ? 0.7141 1.1868 0.8800 0.1462  -0.0373 -0.0500 661 HIS A CG  
2858 N ND1 . HIS A 365 ? 0.6654 1.1983 0.8551 0.1341  -0.0396 -0.0518 661 HIS A ND1 
2859 C CD2 . HIS A 365 ? 0.6712 1.0863 0.8445 0.1084  -0.0369 -0.0454 661 HIS A CD2 
2860 C CE1 . HIS A 365 ? 0.6604 1.1644 0.8665 0.0910  -0.0402 -0.0488 661 HIS A CE1 
2861 N NE2 . HIS A 365 ? 0.6981 1.1327 0.8949 0.0774  -0.0385 -0.0449 661 HIS A NE2 
2862 N N   . MET A 366 ? 0.6517 1.2167 0.8182 0.1491  -0.0176 -0.0526 662 MET A N   
2863 C CA  . MET A 366 ? 0.6142 1.2006 0.8001 0.1026  -0.0106 -0.0492 662 MET A CA  
2864 C C   . MET A 366 ? 0.5166 1.2250 0.7236 0.0937  -0.0028 -0.0520 662 MET A C   
2865 O O   . MET A 366 ? 0.4854 1.2304 0.7120 0.0436  0.0001  -0.0494 662 MET A O   
2866 C CB  . MET A 366 ? 0.6317 1.1535 0.7945 0.1064  -0.0080 -0.0470 662 MET A CB  
2867 C CG  . MET A 366 ? 0.6665 1.1191 0.8328 0.0647  -0.0098 -0.0407 662 MET A CG  
2868 S SD  . MET A 366 ? 0.7638 1.1491 0.8994 0.0772  -0.0085 -0.0390 662 MET A SD  
2869 C CE  . MET A 366 ? 0.7818 1.1531 0.9295 0.0245  -0.0052 -0.0322 662 MET A CE  
2870 N N   . GLU A 367 ? 0.5878 1.3604 0.7856 0.1416  0.0004  -0.0575 663 GLU A N   
2871 C CA  . GLU A 367 ? 0.7107 1.6190 0.9305 0.1356  0.0086  -0.0604 663 GLU A CA  
2872 C C   . GLU A 367 ? 0.7479 1.7313 0.9973 0.1052  0.0050  -0.0608 663 GLU A C   
2873 O O   . GLU A 367 ? 0.8077 1.8696 1.0779 0.0558  0.0105  -0.0592 663 GLU A O   
2874 C CB  . GLU A 367 ? 0.8384 1.8056 1.0395 0.2053  0.0113  -0.0673 663 GLU A CB  
2875 C CG  . GLU A 367 ? 1.0321 1.9281 1.1945 0.2404  0.0146  -0.0685 663 GLU A CG  
2876 C CD  . GLU A 367 ? 1.1625 2.1060 1.2948 0.3176  0.0159  -0.0766 663 GLU A CD  
2877 O OE1 . GLU A 367 ? 1.2203 2.2516 1.3609 0.3413  0.0135  -0.0800 663 GLU A OE1 
2878 O OE2 . GLU A 367 ? 1.1786 2.0584 1.2688 0.3529  0.0177  -0.0790 663 GLU A OE2 
2879 N N   . ASN A 368 ? 0.7048 1.6614 0.9510 0.1310  -0.0046 -0.0627 664 ASN A N   
2880 C CA  . ASN A 368 ? 0.6580 1.6795 0.9287 0.1043  -0.0095 -0.0636 664 ASN A CA  
2881 C C   . ASN A 368 ? 0.6441 1.6215 0.9245 0.0318  -0.0099 -0.0585 664 ASN A C   
2882 O O   . ASN A 368 ? 0.7225 1.7768 1.0198 -0.0136 -0.0089 -0.0587 664 ASN A O   
2883 C CB  . ASN A 368 ? 0.6778 1.6575 0.9360 0.1470  -0.0201 -0.0658 664 ASN A CB  
2884 C CG  . ASN A 368 ? 0.7458 1.7620 0.9805 0.2217  -0.0214 -0.0709 664 ASN A CG  
2885 O OD1 . ASN A 368 ? 0.8760 1.9577 1.0985 0.2351  -0.0144 -0.0731 664 ASN A OD1 
2886 N ND2 . ASN A 368 ? 0.6394 1.5799 0.8456 0.2651  -0.0304 -0.0716 664 ASN A ND2 
2887 N N   . GLU A 369 ? 0.5566 1.4098 0.8209 0.0207  -0.0120 -0.0543 665 GLU A N   
2888 C CA  . GLU A 369 ? 0.4757 1.2747 0.7393 -0.0381 -0.0131 -0.0499 665 GLU A CA  
2889 C C   . GLU A 369 ? 0.6837 1.5253 0.9467 -0.0871 -0.0050 -0.0471 665 GLU A C   
2890 O O   . GLU A 369 ? 0.7462 1.6030 1.0074 -0.1403 -0.0058 -0.0458 665 GLU A O   
2891 C CB  . GLU A 369 ? 0.5676 1.2390 0.8138 -0.0321 -0.0165 -0.0461 665 GLU A CB  
2892 C CG  . GLU A 369 ? 0.6832 1.3010 0.9247 0.0004  -0.0244 -0.0472 665 GLU A CG  
2893 C CD  . GLU A 369 ? 0.7110 1.2976 0.9559 -0.0303 -0.0299 -0.0466 665 GLU A CD  
2894 O OE1 . GLU A 369 ? 0.9089 1.4154 1.1435 -0.0492 -0.0311 -0.0431 665 GLU A OE1 
2895 O OE2 . GLU A 369 ? 0.4856 1.1327 0.7416 -0.0341 -0.0331 -0.0500 665 GLU A OE2 
2896 N N   . TYR A 370 ? 0.6946 1.5479 0.9518 -0.0727 0.0027  -0.0461 666 TYR A N   
2897 C CA  . TYR A 370 ? 0.7330 1.6266 0.9853 -0.1212 0.0112  -0.0425 666 TYR A CA  
2898 C C   . TYR A 370 ? 0.7686 1.7997 1.0388 -0.1491 0.0146  -0.0452 666 TYR A C   
2899 O O   . TYR A 370 ? 0.7004 1.7460 0.9584 -0.2122 0.0172  -0.0416 666 TYR A O   
2900 C CB  . TYR A 370 ? 0.7115 1.5990 0.9541 -0.0954 0.0191  -0.0415 666 TYR A CB  
2901 C CG  . TYR A 370 ? 0.7003 1.4584 0.9207 -0.0996 0.0165  -0.0364 666 TYR A CG  
2902 C CD1 . TYR A 370 ? 0.6609 1.3382 0.8752 -0.0576 0.0097  -0.0375 666 TYR A CD1 
2903 C CD2 . TYR A 370 ? 0.7746 1.4920 0.9760 -0.1477 0.0200  -0.0302 666 TYR A CD2 
2904 C CE1 . TYR A 370 ? 0.6430 1.2171 0.8398 -0.0628 0.0066  -0.0329 666 TYR A CE1 
2905 C CE2 . TYR A 370 ? 0.7850 1.3918 0.9660 -0.1469 0.0164  -0.0256 666 TYR A CE2 
2906 C CZ  . TYR A 370 ? 0.7463 1.2890 0.9286 -0.1045 0.0097  -0.0272 666 TYR A CZ  
2907 O OH  . TYR A 370 ? 0.8284 1.2765 0.9931 -0.1047 0.0056  -0.0228 666 TYR A OH  
2908 N N   . ARG A 371 ? 0.8486 1.9624 1.1338 -0.1019 0.0133  -0.0509 667 ARG A N   
2909 C CA  . ARG A 371 ? 0.9383 2.1387 1.2126 -0.1159 0.0143  -0.0524 667 ARG A CA  
2910 C C   . ARG A 371 ? 0.9039 2.0859 1.1716 -0.1631 0.0071  -0.0514 667 ARG A C   
2911 O O   . ARG A 371 ? 0.9512 2.1391 1.1978 -0.2242 0.0093  -0.0479 667 ARG A O   
2912 C CB  . ARG A 371 ? 1.0255 2.2875 1.3009 -0.0445 0.0125  -0.0584 667 ARG A CB  
2913 C CG  . ARG A 371 ? 1.1627 2.5350 1.4257 -0.0485 0.0149  -0.0604 667 ARG A CG  
2914 C CD  . ARG A 371 ? 1.2519 2.6659 1.5089 0.0237  0.0099  -0.0664 667 ARG A CD  
2915 N NE  . ARG A 371 ? 1.3319 2.6780 1.5959 0.0461  0.0008  -0.0676 667 ARG A NE  
2916 C CZ  . ARG A 371 ? 1.3902 2.7431 1.6583 0.0208  -0.0056 -0.0677 667 ARG A CZ  
2917 N NH1 . ARG A 371 ? 1.4591 2.8814 1.7223 -0.0286 -0.0039 -0.0669 667 ARG A NH1 
2918 N NH2 . ARG A 371 ? 1.3660 2.6554 1.6392 0.0438  -0.0140 -0.0687 667 ARG A NH2 
2919 N N   . CYS A 372 ? 0.9439 2.0965 1.2230 -0.1358 -0.0019 -0.0544 668 CYS A N   
2920 C CA  . CYS A 372 ? 0.8908 2.0356 1.1624 -0.1710 -0.0089 -0.0548 668 CYS A CA  
2921 C C   . CYS A 372 ? 0.7910 1.8328 1.0549 -0.2141 -0.0140 -0.0521 668 CYS A C   
2922 O O   . CYS A 372 ? 0.8812 1.9027 1.1335 -0.2430 -0.0202 -0.0530 668 CYS A O   
2923 C CB  . CYS A 372 ? 1.0210 2.1931 1.3036 -0.1187 -0.0162 -0.0597 668 CYS A CB  
2924 S SG  . CYS A 372 ? 1.0880 2.1728 1.3865 -0.0662 -0.0249 -0.0613 668 CYS A SG  
2925 N N   . ARG A 373 ? 0.5836 1.5593 0.8492 -0.2183 -0.0118 -0.0493 669 ARG A N   
2926 C CA  . ARG A 373 ? 0.5628 1.4189 0.8048 -0.2506 -0.0166 -0.0464 669 ARG A CA  
2927 C C   . ARG A 373 ? 0.7437 1.5348 0.9561 -0.2856 -0.0107 -0.0403 669 ARG A C   
2928 O O   . ARG A 373 ? 0.8672 1.5587 1.0455 -0.3171 -0.0145 -0.0375 669 ARG A O   
2929 C CB  . ARG A 373 ? 0.6383 1.4042 0.8829 -0.1981 -0.0219 -0.0469 669 ARG A CB  
2930 C CG  . ARG A 373 ? 0.6626 1.3179 0.8823 -0.2190 -0.0278 -0.0455 669 ARG A CG  
2931 C CD  . ARG A 373 ? 0.6581 1.2354 0.8812 -0.1717 -0.0314 -0.0451 669 ARG A CD  
2932 N NE  . ARG A 373 ? 0.7273 1.2238 0.9302 -0.1879 -0.0371 -0.0452 669 ARG A NE  
2933 C CZ  . ARG A 373 ? 0.7365 1.1529 0.9334 -0.1630 -0.0395 -0.0436 669 ARG A CZ  
2934 N NH1 . ARG A 373 ? 0.7058 1.1060 0.9136 -0.1260 -0.0376 -0.0414 669 ARG A NH1 
2935 N NH2 . ARG A 373 ? 0.7809 1.1356 0.9575 -0.1762 -0.0439 -0.0446 669 ARG A NH2 
2936 N N   . GLY A 374 ? 0.7504 1.5902 0.9691 -0.2786 -0.0018 -0.0382 670 GLY A N   
2937 C CA  . GLY A 374 ? 0.8513 1.6316 1.0395 -0.3102 0.0038  -0.0319 670 GLY A CA  
2938 C C   . GLY A 374 ? 0.8980 1.5692 1.0759 -0.2736 0.0028  -0.0289 670 GLY A C   
2939 O O   . GLY A 374 ? 0.9574 1.5601 1.1035 -0.2995 0.0049  -0.0233 670 GLY A O   
2940 N N   . GLY A 375 ? 0.8500 1.5014 1.0486 -0.2170 -0.0010 -0.0321 671 GLY A N   
2941 C CA  . GLY A 375 ? 0.8599 1.4215 1.0495 -0.1860 -0.0023 -0.0293 671 GLY A CA  
2942 C C   . GLY A 375 ? 0.7764 1.3000 0.9788 -0.1420 -0.0093 -0.0323 671 GLY A C   
2943 O O   . GLY A 375 ? 0.8246 1.3793 1.0403 -0.1347 -0.0137 -0.0361 671 GLY A O   
2944 N N   . CYS A 376 ? 0.6555 1.1106 0.8505 -0.1159 -0.0108 -0.0299 672 CYS A N   
2945 C CA  . CYS A 376 ? 0.7217 1.1322 0.9218 -0.0802 -0.0173 -0.0314 672 CYS A CA  
2946 C C   . CYS A 376 ? 0.6706 0.9971 0.8557 -0.0774 -0.0198 -0.0268 672 CYS A C   
2947 O O   . CYS A 376 ? 0.6795 0.9934 0.8579 -0.0617 -0.0176 -0.0254 672 CYS A O   
2948 C CB  . CYS A 376 ? 0.6491 1.0999 0.8565 -0.0360 -0.0166 -0.0353 672 CYS A CB  
2949 S SG  . CYS A 376 ? 0.6137 1.0010 0.8137 0.0022  -0.0247 -0.0360 672 CYS A SG  
2950 N N   . PRO A 377 ? 0.5862 0.8575 0.7636 -0.0904 -0.0246 -0.0249 673 PRO A N   
2951 C CA  . PRO A 377 ? 0.5443 0.7492 0.7102 -0.0822 -0.0280 -0.0209 673 PRO A CA  
2952 C C   . PRO A 377 ? 0.5724 0.7685 0.7443 -0.0505 -0.0304 -0.0214 673 PRO A C   
2953 O O   . PRO A 377 ? 0.5393 0.7510 0.7193 -0.0329 -0.0325 -0.0245 673 PRO A O   
2954 C CB  . PRO A 377 ? 0.5849 0.7509 0.7445 -0.0906 -0.0330 -0.0209 673 PRO A CB  
2955 C CG  . PRO A 377 ? 0.4719 0.6810 0.6459 -0.0917 -0.0335 -0.0258 673 PRO A CG  
2956 C CD  . PRO A 377 ? 0.5452 0.8199 0.7260 -0.1023 -0.0283 -0.0276 673 PRO A CD  
2957 N N   . ALA A 378 ? 0.6731 0.8396 0.8344 -0.0449 -0.0309 -0.0183 674 ALA A N   
2958 C CA  . ALA A 378 ? 0.5558 0.7089 0.7117 -0.0208 -0.0334 -0.0189 674 ALA A CA  
2959 C C   . ALA A 378 ? 0.6119 0.7228 0.7560 -0.0230 -0.0370 -0.0146 674 ALA A C   
2960 O O   . ALA A 378 ? 0.6157 0.7197 0.7525 -0.0348 -0.0350 -0.0118 674 ALA A O   
2961 C CB  . ALA A 378 ? 0.4681 0.6582 0.6186 -0.0043 -0.0284 -0.0225 674 ALA A CB  
2962 N N   . ASP A 379 ? 0.5559 0.6404 0.6949 -0.0139 -0.0428 -0.0138 675 ASP A N   
2963 C CA  . ASP A 379 ? 0.5127 0.5679 0.6427 -0.0181 -0.0480 -0.0097 675 ASP A CA  
2964 C C   . ASP A 379 ? 0.6672 0.7045 0.7745 -0.0083 -0.0497 -0.0109 675 ASP A C   
2965 O O   . ASP A 379 ? 0.5968 0.6166 0.6907 -0.0018 -0.0535 -0.0120 675 ASP A O   
2966 C CB  . ASP A 379 ? 0.6351 0.6821 0.7736 -0.0215 -0.0534 -0.0076 675 ASP A CB  
2967 C CG  . ASP A 379 ? 0.7275 0.7623 0.8608 -0.0262 -0.0591 -0.0033 675 ASP A CG  
2968 O OD1 . ASP A 379 ? 0.7245 0.7652 0.8673 -0.0270 -0.0621 -0.0012 675 ASP A OD1 
2969 O OD2 . ASP A 379 ? 0.7730 0.7957 0.8911 -0.0272 -0.0609 -0.0022 675 ASP A OD2 
2970 N N   . TRP A 380 ? 0.5453 0.5803 0.6407 -0.0080 -0.0472 -0.0106 676 TRP A N   
2971 C CA  . TRP A 380 ? 0.5643 0.5771 0.6300 0.0038  -0.0483 -0.0129 676 TRP A CA  
2972 C C   . TRP A 380 ? 0.5819 0.5566 0.6280 -0.0032 -0.0574 -0.0108 676 TRP A C   
2973 O O   . TRP A 380 ? 0.6820 0.6240 0.6945 0.0053  -0.0605 -0.0133 676 TRP A O   
2974 C CB  . TRP A 380 ? 0.5618 0.5791 0.6189 0.0018  -0.0441 -0.0121 676 TRP A CB  
2975 C CG  . TRP A 380 ? 0.6478 0.6463 0.6708 0.0181  -0.0430 -0.0160 676 TRP A CG  
2976 C CD1 . TRP A 380 ? 0.6759 0.7007 0.6901 0.0368  -0.0348 -0.0207 676 TRP A CD1 
2977 C CD2 . TRP A 380 ? 0.6522 0.6029 0.6402 0.0173  -0.0505 -0.0159 676 TRP A CD2 
2978 N NE1 . TRP A 380 ? 0.7491 0.7390 0.7222 0.0531  -0.0364 -0.0241 676 TRP A NE1 
2979 C CE2 . TRP A 380 ? 0.7303 0.6695 0.6844 0.0387  -0.0464 -0.0212 676 TRP A CE2 
2980 C CE3 . TRP A 380 ? 0.5960 0.5174 0.5758 -0.0006 -0.0605 -0.0121 676 TRP A CE3 
2981 C CZ2 . TRP A 380 ? 0.6764 0.5616 0.5823 0.0421  -0.0525 -0.0232 676 TRP A CZ2 
2982 C CZ3 . TRP A 380 ? 0.6422 0.5183 0.5777 -0.0027 -0.0669 -0.0135 676 TRP A CZ3 
2983 C CH2 . TRP A 380 ? 0.6333 0.4849 0.5296 0.0183  -0.0631 -0.0192 676 TRP A CH2 
2984 N N   . VAL A 381 ? 0.6602 0.6386 0.7213 -0.0191 -0.0623 -0.0060 677 VAL A N   
2985 C CA  . VAL A 381 ? 0.5814 0.5404 0.6272 -0.0323 -0.0712 -0.0033 677 VAL A CA  
2986 C C   . VAL A 381 ? 0.7316 0.6760 0.7660 -0.0343 -0.0737 -0.0043 677 VAL A C   
2987 O O   . VAL A 381 ? 0.5964 0.5075 0.5965 -0.0453 -0.0800 -0.0037 677 VAL A O   
2988 C CB  . VAL A 381 ? 0.6065 0.5903 0.6759 -0.0427 -0.0754 0.0017  677 VAL A CB  
2989 C CG1 . VAL A 381 ? 0.5748 0.5600 0.6358 -0.0593 -0.0841 0.0045  677 VAL A CG1 
2990 C CG2 . VAL A 381 ? 0.5038 0.4862 0.5679 -0.0419 -0.0758 0.0037  677 VAL A CG2 
2991 N N   . TRP A 382 ? 0.6794 0.6439 0.7361 -0.0261 -0.0691 -0.0057 678 TRP A N   
2992 C CA  . TRP A 382 ? 0.7031 0.6544 0.7488 -0.0271 -0.0711 -0.0061 678 TRP A CA  
2993 C C   . TRP A 382 ? 0.6524 0.5806 0.6712 -0.0056 -0.0685 -0.0107 678 TRP A C   
2994 O O   . TRP A 382 ? 0.6520 0.5428 0.6361 -0.0058 -0.0727 -0.0107 678 TRP A O   
2995 C CB  . TRP A 382 ? 0.6475 0.6339 0.7298 -0.0296 -0.0689 -0.0049 678 TRP A CB  
2996 C CG  . TRP A 382 ? 0.6402 0.6449 0.7355 -0.0464 -0.0733 -0.0005 678 TRP A CG  
2997 C CD1 . TRP A 382 ? 0.6820 0.7057 0.7891 -0.0521 -0.0761 0.0023  678 TRP A CD1 
2998 C CD2 . TRP A 382 ? 0.5855 0.5998 0.6827 -0.0575 -0.0754 0.0016  678 TRP A CD2 
2999 N NE1 . TRP A 382 ? 0.6082 0.6603 0.7265 -0.0633 -0.0799 0.0057  678 TRP A NE1 
3000 C CE2 . TRP A 382 ? 0.6281 0.6767 0.7417 -0.0688 -0.0788 0.0053  678 TRP A CE2 
3001 C CE3 . TRP A 382 ? 0.5648 0.5648 0.6493 -0.0578 -0.0747 0.0010  678 TRP A CE3 
3002 C CZ2 . TRP A 382 ? 0.7100 0.7866 0.8302 -0.0820 -0.0805 0.0082  678 TRP A CZ2 
3003 C CZ3 . TRP A 382 ? 0.7803 0.7991 0.8690 -0.0736 -0.0763 0.0043  678 TRP A CZ3 
3004 C CH2 . TRP A 382 ? 0.7927 0.8534 0.9008 -0.0862 -0.0786 0.0077  678 TRP A CH2 
3005 N N   . ILE A 383 ? 0.6119 0.5616 0.6399 0.0131  -0.0621 -0.0146 679 ILE A N   
3006 C CA  . ILE A 383 ? 0.5970 0.5390 0.6006 0.0409  -0.0596 -0.0196 679 ILE A CA  
3007 C C   . ILE A 383 ? 0.7739 0.6576 0.7185 0.0532  -0.0636 -0.0217 679 ILE A C   
3008 O O   . ILE A 383 ? 0.7585 0.6053 0.6606 0.0748  -0.0660 -0.0246 679 ILE A O   
3009 C CB  . ILE A 383 ? 0.6694 0.6676 0.7019 0.0540  -0.0512 -0.0229 679 ILE A CB  
3010 C CG1 . ILE A 383 ? 0.6192 0.6620 0.6963 0.0403  -0.0484 -0.0216 679 ILE A CG1 
3011 C CG2 . ILE A 383 ? 0.6151 0.6190 0.6205 0.0896  -0.0486 -0.0288 679 ILE A CG2 
3012 C CD1 . ILE A 383 ? 0.7499 0.8014 0.8291 0.0513  -0.0498 -0.0235 679 ILE A CD1 
3013 N N   . VAL A 384 ? 0.7631 0.6325 0.6969 0.0429  -0.0647 -0.0209 680 VAL A N   
3014 C CA  . VAL A 384 ? 0.7349 0.5411 0.6043 0.0542  -0.0689 -0.0239 680 VAL A CA  
3015 C C   . VAL A 384 ? 0.8787 0.6195 0.7010 0.0354  -0.0786 -0.0212 680 VAL A C   
3016 O O   . VAL A 384 ? 0.8610 0.6129 0.7049 0.0015  -0.0830 -0.0156 680 VAL A O   
3017 C CB  . VAL A 384 ? 0.8224 0.6293 0.6914 0.0425  -0.0688 -0.0232 680 VAL A CB  
3018 C CG1 . VAL A 384 ? 0.7643 0.4956 0.5589 0.0485  -0.0747 -0.0265 680 VAL A CG1 
3019 C CG2 . VAL A 384 ? 0.9135 0.7781 0.8168 0.0587  -0.0585 -0.0256 680 VAL A CG2 
3020 N N   . PRO A 385 ? 0.9637 0.6359 0.7165 0.0558  -0.0826 -0.0246 681 PRO A N   
3021 C CA  . PRO A 385 ? 1.0249 0.6281 0.7243 0.0315  -0.0919 -0.0210 681 PRO A CA  
3022 C C   . PRO A 385 ? 1.1281 0.6913 0.7945 -0.0069 -0.0998 -0.0180 681 PRO A C   
3023 O O   . PRO A 385 ? 1.0802 0.6400 0.7386 -0.0029 -0.0993 -0.0208 681 PRO A O   
3024 C CB  . PRO A 385 ? 1.0978 0.6266 0.7183 0.0708  -0.0942 -0.0262 681 PRO A CB  
3025 C CG  . PRO A 385 ? 1.0888 0.6841 0.7510 0.1155  -0.0848 -0.0315 681 PRO A CG  
3026 C CD  . PRO A 385 ? 1.0372 0.6958 0.7553 0.1046  -0.0785 -0.0317 681 PRO A CD  
3027 N N   . PRO A 386 ? 1.1107 0.6461 0.7542 -0.0470 -0.1074 -0.0124 682 PRO A N   
3028 C CA  . PRO A 386 ? 1.1638 0.6828 0.7857 -0.0919 -0.1156 -0.0087 682 PRO A CA  
3029 C C   . PRO A 386 ? 1.2229 0.6352 0.7423 -0.0971 -0.1240 -0.0120 682 PRO A C   
3030 O O   . PRO A 386 ? 1.2212 0.6073 0.7062 -0.1427 -0.1331 -0.0086 682 PRO A O   
3031 C CB  . PRO A 386 ? 1.1517 0.6895 0.7848 -0.1324 -0.1195 -0.0016 682 PRO A CB  
3032 C CG  . PRO A 386 ? 1.1476 0.6401 0.7465 -0.1105 -0.1179 -0.0026 682 PRO A CG  
3033 C CD  . PRO A 386 ? 1.1345 0.6641 0.7753 -0.0565 -0.1084 -0.0086 682 PRO A CD  
3034 N N   . MET A 387 ? 1.2528 0.6032 0.7173 -0.0515 -0.1219 -0.0188 683 MET A N   
3035 C CA  . MET A 387 ? 1.4071 0.6475 0.7657 -0.0460 -0.1293 -0.0237 683 MET A CA  
3036 C C   . MET A 387 ? 1.4091 0.6458 0.7575 0.0196  -0.1213 -0.0325 683 MET A C   
3037 O O   . MET A 387 ? 1.3053 0.6010 0.7046 0.0570  -0.1126 -0.0341 683 MET A O   
3038 C CB  . MET A 387 ? 1.5603 0.6851 0.8135 -0.0641 -0.1392 -0.0218 683 MET A CB  
3039 C CG  . MET A 387 ? 1.6642 0.7327 0.8664 -0.0057 -0.1366 -0.0267 683 MET A CG  
3040 S SD  . MET A 387 ? 1.8930 0.8074 0.9556 -0.0244 -0.1492 -0.0235 683 MET A SD  
3041 C CE  . MET A 387 ? 1.8887 0.6616 0.8159 -0.0288 -0.1598 -0.0297 683 MET A CE  
3042 N N   . SER A 388 ? 1.4982 0.6735 0.7820 0.0327  -0.1242 -0.0385 684 SER A N   
3043 C CA  . SER A 388 ? 1.5584 0.7261 0.8180 0.0981  -0.1167 -0.0477 684 SER A CA  
3044 C C   . SER A 388 ? 1.3806 0.6807 0.7515 0.1231  -0.1028 -0.0483 684 SER A C   
3045 O O   . SER A 388 ? 1.4952 0.8244 0.8702 0.1767  -0.0946 -0.0541 684 SER A O   
3046 C CB  . SER A 388 ? 1.6051 0.6919 0.7831 0.1423  -0.1193 -0.0517 684 SER A CB  
3047 O OG  . SER A 388 ? 1.8252 0.7747 0.8867 0.1147  -0.1328 -0.0506 684 SER A OG  
3048 N N   . GLY A 389 ? 1.2016 0.5829 0.6580 0.0841  -0.1004 -0.0421 685 GLY A N   
3049 C CA  . GLY A 389 ? 1.0518 0.5469 0.6059 0.0968  -0.0886 -0.0411 685 GLY A CA  
3050 C C   . GLY A 389 ? 1.1441 0.6752 0.7012 0.1452  -0.0780 -0.0484 685 GLY A C   
3051 O O   . GLY A 389 ? 1.0982 0.6952 0.6976 0.1736  -0.0695 -0.0501 685 GLY A O   
3052 N N   . SER A 390 ? 1.2012 0.6948 0.7116 0.1547  -0.0783 -0.0530 686 SER A N   
3053 C CA  . SER A 390 ? 1.1195 0.6672 0.6435 0.1956  -0.0663 -0.0590 686 SER A CA  
3054 C C   . SER A 390 ? 1.2591 0.7756 0.7201 0.2575  -0.0634 -0.0681 686 SER A C   
3055 O O   . SER A 390 ? 1.2383 0.8178 0.7146 0.2960  -0.0523 -0.0735 686 SER A O   
3056 C CB  . SER A 390 ? 1.1241 0.6555 0.6285 0.1835  -0.0663 -0.0604 686 SER A CB  
3057 O OG  . SER A 390 ? 1.2808 0.6999 0.6835 0.1913  -0.0756 -0.0658 686 SER A OG  
3058 N N   . ILE A 391 ? 1.3673 0.7909 0.7542 0.2699  -0.0731 -0.0697 687 ILE A N   
3059 C CA  . ILE A 391 ? 1.3983 0.7985 0.7273 0.3365  -0.0709 -0.0778 687 ILE A CA  
3060 C C   . ILE A 391 ? 1.3981 0.8744 0.7862 0.3512  -0.0669 -0.0753 687 ILE A C   
3061 O O   . ILE A 391 ? 1.5345 1.0060 0.8826 0.4089  -0.0659 -0.0813 687 ILE A O   
3062 C CB  . ILE A 391 ? 1.6342 0.8787 0.8304 0.3539  -0.0837 -0.0819 687 ILE A CB  
3063 C CG1 . ILE A 391 ? 1.7091 0.8886 0.8869 0.3084  -0.0953 -0.0740 687 ILE A CG1 
3064 C CG2 . ILE A 391 ? 1.5952 0.7555 0.7159 0.3464  -0.0881 -0.0867 687 ILE A CG2 
3065 C CD1 . ILE A 391 ? 1.8619 0.8788 0.8962 0.3242  -0.1082 -0.0774 687 ILE A CD1 
3066 N N   . THR A 392 ? 1.3113 0.8604 0.7939 0.3011  -0.0653 -0.0666 688 THR A N   
3067 C CA  . THR A 392 ? 1.2496 0.8865 0.7975 0.3122  -0.0600 -0.0649 688 THR A CA  
3068 C C   . THR A 392 ? 1.1278 0.8920 0.7631 0.3079  -0.0472 -0.0648 688 THR A C   
3069 O O   . THR A 392 ? 1.0512 0.8342 0.7163 0.2757  -0.0440 -0.0620 688 THR A O   
3070 C CB  . THR A 392 ? 1.2861 0.9128 0.8680 0.2658  -0.0666 -0.0565 688 THR A CB  
3071 O OG1 . THR A 392 ? 1.1455 0.8206 0.7976 0.2141  -0.0643 -0.0502 688 THR A OG1 
3072 C CG2 . THR A 392 ? 1.4165 0.9147 0.9093 0.2532  -0.0795 -0.0546 688 THR A CG2 
3073 N N   . PRO A 393 ? 1.1368 0.9900 0.8101 0.3379  -0.0402 -0.0676 689 PRO A N   
3074 C CA  . PRO A 393 ? 1.0519 1.0242 0.7937 0.3325  -0.0276 -0.0680 689 PRO A CA  
3075 C C   . PRO A 393 ? 0.9486 0.9666 0.7665 0.2725  -0.0255 -0.0598 689 PRO A C   
3076 O O   . PRO A 393 ? 0.9412 1.0295 0.7999 0.2565  -0.0164 -0.0587 689 PRO A O   
3077 C CB  . PRO A 393 ? 1.0784 1.1322 0.8340 0.3770  -0.0233 -0.0729 689 PRO A CB  
3078 C CG  . PRO A 393 ? 1.1088 1.0990 0.8382 0.3821  -0.0341 -0.0709 689 PRO A CG  
3079 C CD  . PRO A 393 ? 1.1916 1.0431 0.8417 0.3772  -0.0439 -0.0703 689 PRO A CD  
3080 N N   . VAL A 394 ? 0.8463 0.8253 0.6787 0.2402  -0.0335 -0.0539 690 VAL A N   
3081 C CA  . VAL A 394 ? 0.8064 0.8217 0.7019 0.1903  -0.0321 -0.0468 690 VAL A CA  
3082 C C   . VAL A 394 ? 0.8387 0.8212 0.7306 0.1609  -0.0331 -0.0432 690 VAL A C   
3083 O O   . VAL A 394 ? 0.8401 0.8603 0.7777 0.1287  -0.0299 -0.0382 690 VAL A O   
3084 C CB  . VAL A 394 ? 0.7195 0.7096 0.6313 0.1677  -0.0396 -0.0421 690 VAL A CB  
3085 C CG1 . VAL A 394 ? 0.7372 0.7788 0.6684 0.1891  -0.0379 -0.0446 690 VAL A CG1 
3086 C CG2 . VAL A 394 ? 0.8792 0.7704 0.7335 0.1644  -0.0500 -0.0408 690 VAL A CG2 
3087 N N   . PHE A 395 ? 0.8617 0.7699 0.6945 0.1709  -0.0384 -0.0454 691 PHE A N   
3088 C CA  . PHE A 395 ? 0.8826 0.7664 0.7107 0.1447  -0.0401 -0.0424 691 PHE A CA  
3089 C C   . PHE A 395 ? 0.8447 0.7958 0.7017 0.1463  -0.0288 -0.0429 691 PHE A C   
3090 O O   . PHE A 395 ? 0.7975 0.7605 0.6800 0.1158  -0.0281 -0.0376 691 PHE A O   
3091 C CB  . PHE A 395 ? 0.9508 0.7436 0.7003 0.1579  -0.0476 -0.0464 691 PHE A CB  
3092 C CG  . PHE A 395 ? 0.9367 0.7025 0.6747 0.1319  -0.0509 -0.0439 691 PHE A CG  
3093 C CD1 . PHE A 395 ? 0.9409 0.6645 0.6736 0.0936  -0.0619 -0.0383 691 PHE A CD1 
3094 C CD2 . PHE A 395 ? 0.9850 0.7717 0.7138 0.1467  -0.0433 -0.0472 691 PHE A CD2 
3095 C CE1 . PHE A 395 ? 0.8974 0.6028 0.6186 0.0710  -0.0662 -0.0361 691 PHE A CE1 
3096 C CE2 . PHE A 395 ? 1.0620 0.8224 0.7768 0.1241  -0.0470 -0.0449 691 PHE A CE2 
3097 C CZ  . PHE A 395 ? 1.0405 0.7594 0.7509 0.0871  -0.0592 -0.0395 691 PHE A CZ  
3098 N N   . HIS A 396 ? 0.8491 0.8475 0.6992 0.1825  -0.0201 -0.0491 692 HIS A N   
3099 C CA  . HIS A 396 ? 0.7331 0.7993 0.5988 0.1880  -0.0081 -0.0507 692 HIS A CA  
3100 C C   . HIS A 396 ? 0.7474 0.9064 0.6748 0.1663  0.0001  -0.0471 692 HIS A C   
3101 O O   . HIS A 396 ? 0.8544 1.0842 0.7964 0.1668  0.0111  -0.0481 692 HIS A O   
3102 C CB  . HIS A 396 ? 0.8609 0.9340 0.6793 0.2428  -0.0031 -0.0602 692 HIS A CB  
3103 C CG  . HIS A 396 ? 0.9956 0.9614 0.7378 0.2634  -0.0120 -0.0645 692 HIS A CG  
3104 N ND1 . HIS A 396 ? 1.0133 0.9364 0.7245 0.2533  -0.0126 -0.0647 692 HIS A ND1 
3105 C CD2 . HIS A 396 ? 1.0549 0.9398 0.7383 0.2893  -0.0215 -0.0684 692 HIS A CD2 
3106 C CE1 . HIS A 396 ? 1.0817 0.9035 0.7180 0.2707  -0.0223 -0.0692 692 HIS A CE1 
3107 N NE2 . HIS A 396 ? 1.0971 0.8900 0.7123 0.2918  -0.0278 -0.0712 692 HIS A NE2 
3108 N N   . GLN A 397 ? 0.7810 0.9398 0.7402 0.1447  -0.0052 -0.0430 693 GLN A N   
3109 C CA  . GLN A 397 ? 0.7113 0.9467 0.7190 0.1247  0.0004  -0.0407 693 GLN A CA  
3110 C C   . GLN A 397 ? 0.6737 0.8894 0.7073 0.0783  -0.0025 -0.0326 693 GLN A C   
3111 O O   . GLN A 397 ? 0.6780 0.8417 0.7136 0.0671  -0.0117 -0.0295 693 GLN A O   
3112 C CB  . GLN A 397 ? 0.7086 0.9558 0.7244 0.1427  -0.0039 -0.0435 693 GLN A CB  
3113 C CG  . GLN A 397 ? 0.6221 0.9422 0.6842 0.1180  -0.0002 -0.0414 693 GLN A CG  
3114 C CD  . GLN A 397 ? 0.6228 1.0425 0.6992 0.1219  0.0113  -0.0443 693 GLN A CD  
3115 O OE1 . GLN A 397 ? 0.6241 1.0883 0.6859 0.1644  0.0149  -0.0508 693 GLN A OE1 
3116 N NE2 . GLN A 397 ? 0.6729 1.1289 0.7727 0.0781  0.0170  -0.0393 693 GLN A NE2 
3117 N N   . GLU A 398 ? 0.6037 0.8596 0.6514 0.0528  0.0052  -0.0291 694 GLU A N   
3118 C CA  . GLU A 398 ? 0.6035 0.8411 0.6682 0.0127  0.0026  -0.0217 694 GLU A CA  
3119 C C   . GLU A 398 ? 0.6127 0.8660 0.7029 0.0016  -0.0006 -0.0215 694 GLU A C   
3120 O O   . GLU A 398 ? 0.6874 0.9989 0.7912 0.0119  0.0034  -0.0257 694 GLU A O   
3121 C CB  . GLU A 398 ? 0.5434 0.8194 0.6080 -0.0142 0.0120  -0.0179 694 GLU A CB  
3122 C CG  . GLU A 398 ? 0.6590 0.9141 0.6963 -0.0054 0.0149  -0.0175 694 GLU A CG  
3123 C CD  . GLU A 398 ? 0.7551 1.0516 0.7878 -0.0322 0.0255  -0.0135 694 GLU A CD  
3124 O OE1 . GLU A 398 ? 0.8497 1.1222 0.8589 -0.0313 0.0273  -0.0116 694 GLU A OE1 
3125 O OE2 . GLU A 398 ? 0.8095 1.1611 0.8582 -0.0573 0.0316  -0.0120 694 GLU A OE2 
3126 N N   . MET A 399 ? 0.6935 0.8980 0.7885 -0.0168 -0.0081 -0.0168 695 MET A N   
3127 C CA  . MET A 399 ? 0.6652 0.8742 0.7794 -0.0281 -0.0115 -0.0166 695 MET A CA  
3128 C C   . MET A 399 ? 0.7300 0.9058 0.8412 -0.0581 -0.0141 -0.0106 695 MET A C   
3129 O O   . MET A 399 ? 0.7702 0.8997 0.8679 -0.0596 -0.0186 -0.0065 695 MET A O   
3130 C CB  . MET A 399 ? 0.5691 0.7434 0.6845 -0.0082 -0.0199 -0.0184 695 MET A CB  
3131 C CG  . MET A 399 ? 0.5851 0.7697 0.6884 0.0253  -0.0197 -0.0241 695 MET A CG  
3132 S SD  . MET A 399 ? 0.6620 0.7839 0.7477 0.0405  -0.0301 -0.0244 695 MET A SD  
3133 C CE  . MET A 399 ? 0.7133 0.8275 0.7598 0.0810  -0.0289 -0.0307 695 MET A CE  
3134 N N   . LEU A 400 ? 0.6277 0.8237 0.7458 -0.0804 -0.0122 -0.0103 696 LEU A N   
3135 C CA  . LEU A 400 ? 0.5698 0.7198 0.6734 -0.1042 -0.0160 -0.0057 696 LEU A CA  
3136 C C   . LEU A 400 ? 0.7265 0.8517 0.8407 -0.0940 -0.0232 -0.0073 696 LEU A C   
3137 O O   . LEU A 400 ? 0.6417 0.7992 0.7736 -0.0891 -0.0229 -0.0116 696 LEU A O   
3138 C CB  . LEU A 400 ? 0.5774 0.7506 0.6687 -0.1405 -0.0104 -0.0044 696 LEU A CB  
3139 C CG  . LEU A 400 ? 0.6798 0.8854 0.7570 -0.1608 -0.0017 -0.0018 696 LEU A CG  
3140 C CD1 . LEU A 400 ? 0.6746 0.9074 0.7374 -0.2051 0.0028  -0.0006 696 LEU A CD1 
3141 C CD2 . LEU A 400 ? 0.7460 0.8934 0.7954 -0.1614 -0.0036 0.0042  696 LEU A CD2 
3142 N N   . ASN A 401 ? 0.7285 0.8020 0.8314 -0.0889 -0.0297 -0.0038 697 ASN A N   
3143 C CA  . ASN A 401 ? 0.6143 0.6689 0.7252 -0.0793 -0.0356 -0.0050 697 ASN A CA  
3144 C C   . ASN A 401 ? 0.6715 0.6893 0.7578 -0.0954 -0.0374 -0.0035 697 ASN A C   
3145 O O   . ASN A 401 ? 0.7084 0.6876 0.7643 -0.1041 -0.0384 0.0009  697 ASN A O   
3146 C CB  . ASN A 401 ? 0.6320 0.6655 0.7464 -0.0597 -0.0420 -0.0030 697 ASN A CB  
3147 C CG  . ASN A 401 ? 0.6602 0.6957 0.7894 -0.0488 -0.0461 -0.0051 697 ASN A CG  
3148 O OD1 . ASN A 401 ? 0.6529 0.7051 0.7918 -0.0520 -0.0441 -0.0086 697 ASN A OD1 
3149 N ND2 . ASN A 401 ? 0.6008 0.6257 0.7319 -0.0374 -0.0518 -0.0028 697 ASN A ND2 
3150 N N   . TYR A 402 ? 0.7767 0.7994 0.8692 -0.0983 -0.0384 -0.0072 698 TYR A N   
3151 C CA  . TYR A 402 ? 0.7440 0.7215 0.8050 -0.1106 -0.0411 -0.0072 698 TYR A CA  
3152 C C   . TYR A 402 ? 0.7421 0.7301 0.8190 -0.1016 -0.0434 -0.0121 698 TYR A C   
3153 O O   . TYR A 402 ? 0.5819 0.6148 0.6921 -0.0918 -0.0422 -0.0149 698 TYR A O   
3154 C CB  . TYR A 402 ? 0.8129 0.7844 0.8440 -0.1476 -0.0371 -0.0062 698 TYR A CB  
3155 C CG  . TYR A 402 ? 0.7800 0.8247 0.8377 -0.1649 -0.0309 -0.0093 698 TYR A CG  
3156 C CD1 . TYR A 402 ? 0.7861 0.8605 0.8539 -0.1763 -0.0312 -0.0142 698 TYR A CD1 
3157 C CD2 . TYR A 402 ? 0.7404 0.8293 0.8108 -0.1673 -0.0249 -0.0077 698 TYR A CD2 
3158 C CE1 . TYR A 402 ? 0.7095 0.8616 0.8017 -0.1878 -0.0265 -0.0173 698 TYR A CE1 
3159 C CE2 . TYR A 402 ? 0.7039 0.8706 0.7974 -0.1765 -0.0191 -0.0112 698 TYR A CE2 
3160 C CZ  . TYR A 402 ? 0.7689 0.9698 0.8741 -0.1863 -0.0203 -0.0158 698 TYR A CZ  
3161 O OH  . TYR A 402 ? 0.7062 0.9944 0.8347 -0.1917 -0.0157 -0.0195 698 TYR A OH  
3162 N N   . ARG A 403 ? 0.7409 0.6806 0.7868 -0.1025 -0.0470 -0.0131 699 ARG A N   
3163 C CA  . ARG A 403 ? 0.7880 0.7297 0.8441 -0.0884 -0.0495 -0.0175 699 ARG A CA  
3164 C C   . ARG A 403 ? 0.7767 0.7100 0.8123 -0.1143 -0.0492 -0.0218 699 ARG A C   
3165 O O   . ARG A 403 ? 0.8023 0.6772 0.7876 -0.1301 -0.0513 -0.0219 699 ARG A O   
3166 C CB  . ARG A 403 ? 0.9030 0.8024 0.9387 -0.0615 -0.0542 -0.0165 699 ARG A CB  
3167 C CG  . ARG A 403 ? 1.0802 0.9929 1.1322 -0.0411 -0.0558 -0.0118 699 ARG A CG  
3168 C CD  . ARG A 403 ? 1.1818 1.1310 1.2667 -0.0192 -0.0573 -0.0127 699 ARG A CD  
3169 N NE  . ARG A 403 ? 1.3548 1.2827 1.4200 0.0061  -0.0612 -0.0129 699 ARG A NE  
3170 C CZ  . ARG A 403 ? 1.3850 1.3445 1.4703 0.0242  -0.0620 -0.0143 699 ARG A CZ  
3171 N NH1 . ARG A 403 ? 1.3275 1.3301 1.4482 0.0162  -0.0597 -0.0149 699 ARG A NH1 
3172 N NH2 . ARG A 403 ? 1.4267 1.3745 1.4916 0.0518  -0.0651 -0.0148 699 ARG A NH2 
3173 N N   . LEU A 404 ? 0.7922 0.7794 0.8602 -0.1191 -0.0474 -0.0255 700 LEU A N   
3174 C CA  . LEU A 404 ? 0.7182 0.7096 0.7726 -0.1425 -0.0484 -0.0303 700 LEU A CA  
3175 C C   . LEU A 404 ? 0.7777 0.7631 0.8399 -0.1221 -0.0513 -0.0344 700 LEU A C   
3176 O O   . LEU A 404 ? 0.6958 0.6965 0.7853 -0.0936 -0.0513 -0.0334 700 LEU A O   
3177 C CB  . LEU A 404 ? 0.7027 0.7695 0.7863 -0.1603 -0.0451 -0.0317 700 LEU A CB  
3178 C CG  . LEU A 404 ? 0.7516 0.8484 0.8357 -0.1795 -0.0403 -0.0282 700 LEU A CG  
3179 C CD1 . LEU A 404 ? 0.7127 0.8993 0.8307 -0.1841 -0.0374 -0.0311 700 LEU A CD1 
3180 C CD2 . LEU A 404 ? 0.9089 0.9579 0.9412 -0.2193 -0.0405 -0.0261 700 LEU A CD2 
3181 N N   . THR A 405 ? 0.7736 0.7364 0.8074 -0.1407 -0.0538 -0.0391 701 THR A N   
3182 C CA  . THR A 405 ? 0.7776 0.7354 0.8141 -0.1246 -0.0561 -0.0438 701 THR A CA  
3183 C C   . THR A 405 ? 0.7531 0.7576 0.8023 -0.1467 -0.0572 -0.0483 701 THR A C   
3184 O O   . THR A 405 ? 0.7384 0.7630 0.7774 -0.1808 -0.0572 -0.0487 701 THR A O   
3185 C CB  . THR A 405 ? 0.9199 0.7958 0.8993 -0.1194 -0.0594 -0.0464 701 THR A CB  
3186 O OG1 . THR A 405 ? 1.0136 0.8896 1.0025 -0.0891 -0.0599 -0.0496 701 THR A OG1 
3187 C CG2 . THR A 405 ? 0.9658 0.8024 0.8944 -0.1582 -0.0626 -0.0506 701 THR A CG2 
3188 N N   . PRO A 406 ? 0.6933 0.7248 0.7659 -0.1289 -0.0583 -0.0513 702 PRO A N   
3189 C CA  . PRO A 406 ? 0.6553 0.6862 0.7473 -0.0943 -0.0575 -0.0506 702 PRO A CA  
3190 C C   . PRO A 406 ? 0.6907 0.7413 0.8120 -0.0740 -0.0547 -0.0446 702 PRO A C   
3191 O O   . PRO A 406 ? 0.6324 0.7134 0.7696 -0.0816 -0.0533 -0.0421 702 PRO A O   
3192 C CB  . PRO A 406 ? 0.6659 0.7416 0.7793 -0.0933 -0.0591 -0.0538 702 PRO A CB  
3193 C CG  . PRO A 406 ? 0.6365 0.7158 0.7273 -0.1262 -0.0624 -0.0587 702 PRO A CG  
3194 C CD  . PRO A 406 ? 0.7333 0.8041 0.8088 -0.1513 -0.0611 -0.0561 702 PRO A CD  
3195 N N   . SER A 407 ? 0.6178 0.6561 0.7442 -0.0500 -0.0541 -0.0426 703 SER A N   
3196 C CA  . SER A 407 ? 0.6529 0.7050 0.7995 -0.0364 -0.0526 -0.0370 703 SER A CA  
3197 C C   . SER A 407 ? 0.6576 0.7214 0.8167 -0.0177 -0.0521 -0.0354 703 SER A C   
3198 O O   . SER A 407 ? 0.7229 0.7785 0.8720 -0.0096 -0.0520 -0.0386 703 SER A O   
3199 C CB  . SER A 407 ? 0.7649 0.7848 0.8926 -0.0358 -0.0528 -0.0342 703 SER A CB  
3200 O OG  . SER A 407 ? 0.9045 0.8861 1.0036 -0.0227 -0.0542 -0.0363 703 SER A OG  
3201 N N   . PHE A 408 ? 0.6215 0.7051 0.7986 -0.0132 -0.0518 -0.0306 704 PHE A N   
3202 C CA  . PHE A 408 ? 0.6319 0.7293 0.8170 -0.0032 -0.0514 -0.0273 704 PHE A CA  
3203 C C   . PHE A 408 ? 0.6831 0.7768 0.8654 0.0044  -0.0521 -0.0242 704 PHE A C   
3204 O O   . PHE A 408 ? 0.6705 0.7565 0.8524 -0.0002 -0.0532 -0.0217 704 PHE A O   
3205 C CB  . PHE A 408 ? 0.5610 0.6728 0.7551 -0.0075 -0.0520 -0.0235 704 PHE A CB  
3206 C CG  . PHE A 408 ? 0.6041 0.7213 0.7969 -0.0083 -0.0524 -0.0258 704 PHE A CG  
3207 C CD1 . PHE A 408 ? 0.6130 0.7342 0.8055 -0.0092 -0.0537 -0.0274 704 PHE A CD1 
3208 C CD2 . PHE A 408 ? 0.5872 0.7110 0.7778 -0.0058 -0.0515 -0.0263 704 PHE A CD2 
3209 C CE1 . PHE A 408 ? 0.6217 0.7527 0.8111 -0.0053 -0.0552 -0.0295 704 PHE A CE1 
3210 C CE2 . PHE A 408 ? 0.5639 0.6907 0.7499 -0.0052 -0.0527 -0.0281 704 PHE A CE2 
3211 C CZ  . PHE A 408 ? 0.5794 0.7094 0.7645 -0.0038 -0.0552 -0.0296 704 PHE A CZ  
3212 N N   . GLU A 409 ? 0.5970 0.7011 0.7764 0.0186  -0.0516 -0.0244 705 GLU A N   
3213 C CA  . GLU A 409 ? 0.5717 0.6822 0.7475 0.0320  -0.0532 -0.0218 705 GLU A CA  
3214 C C   . GLU A 409 ? 0.6684 0.8282 0.8606 0.0349  -0.0528 -0.0179 705 GLU A C   
3215 O O   . GLU A 409 ? 0.6566 0.8388 0.8562 0.0298  -0.0503 -0.0180 705 GLU A O   
3216 C CB  . GLU A 409 ? 0.6205 0.7003 0.7677 0.0529  -0.0538 -0.0261 705 GLU A CB  
3217 C CG  . GLU A 409 ? 0.8844 0.9100 1.0043 0.0424  -0.0546 -0.0298 705 GLU A CG  
3218 C CD  . GLU A 409 ? 1.0573 1.0650 1.1738 0.0287  -0.0562 -0.0262 705 GLU A CD  
3219 O OE1 . GLU A 409 ? 1.0775 1.1100 1.2123 0.0294  -0.0571 -0.0213 705 GLU A OE1 
3220 O OE2 . GLU A 409 ? 1.1409 1.1100 1.2329 0.0144  -0.0565 -0.0283 705 GLU A OE2 
3221 N N   . TYR A 410 ? 0.5563 0.7360 0.7521 0.0403  -0.0556 -0.0140 706 TYR A N   
3222 C CA  . TYR A 410 ? 0.5310 0.7697 0.7406 0.0412  -0.0557 -0.0105 706 TYR A CA  
3223 C C   . TYR A 410 ? 0.5849 0.8489 0.7884 0.0710  -0.0535 -0.0142 706 TYR A C   
3224 O O   . TYR A 410 ? 0.6776 0.9023 0.8581 0.0949  -0.0538 -0.0190 706 TYR A O   
3225 C CB  . TYR A 410 ? 0.6391 0.9003 0.8540 0.0374  -0.0605 -0.0055 706 TYR A CB  
3226 C CG  . TYR A 410 ? 0.6418 0.8780 0.8566 0.0109  -0.0628 -0.0023 706 TYR A CG  
3227 C CD1 . TYR A 410 ? 0.7483 0.9506 0.9546 0.0131  -0.0655 -0.0020 706 TYR A CD1 
3228 C CD2 . TYR A 410 ? 0.6690 0.9098 0.8846 -0.0148 -0.0623 0.0003  706 TYR A CD2 
3229 C CE1 . TYR A 410 ? 0.8227 1.0034 1.0253 -0.0062 -0.0671 0.0001  706 TYR A CE1 
3230 C CE2 . TYR A 410 ? 0.7559 0.9647 0.9610 -0.0329 -0.0649 0.0024  706 TYR A CE2 
3231 C CZ  . TYR A 410 ? 0.8578 1.0402 1.0584 -0.0269 -0.0670 0.0018  706 TYR A CZ  
3232 O OH  . TYR A 410 ? 0.8428 0.9947 1.0297 -0.0403 -0.0689 0.0030  706 TYR A OH  
3233 N N   . GLN A 411 ? 0.4934 0.8224 0.7117 0.0691  -0.0512 -0.0120 707 GLN A N   
3234 C CA  . GLN A 411 ? 0.5487 0.9184 0.7626 0.1015  -0.0483 -0.0155 707 GLN A CA  
3235 C C   . GLN A 411 ? 0.5521 1.0155 0.7878 0.0947  -0.0481 -0.0103 707 GLN A C   
3236 O O   . GLN A 411 ? 0.5375 1.0216 0.7862 0.0567  -0.0495 -0.0043 707 GLN A O   
3237 C CB  . GLN A 411 ? 0.6461 0.9990 0.8521 0.1038  -0.0426 -0.0206 707 GLN A CB  
3238 C CG  . GLN A 411 ? 0.6951 1.0794 0.9174 0.0704  -0.0392 -0.0164 707 GLN A CG  
3239 C CD  . GLN A 411 ? 0.8157 1.1818 1.0283 0.0739  -0.0342 -0.0213 707 GLN A CD  
3240 O OE1 . GLN A 411 ? 0.8600 1.2113 1.0554 0.1045  -0.0322 -0.0282 707 GLN A OE1 
3241 N NE2 . GLN A 411 ? 0.8196 1.1796 1.0360 0.0438  -0.0329 -0.0179 707 GLN A NE2 
3242 N N   . PRO A 412 ? 0.7062 1.2280 0.9410 0.1309  -0.0471 -0.0125 708 PRO A N   
3243 C CA  . PRO A 412 ? 0.7713 1.4019 1.0294 0.1229  -0.0470 -0.0075 708 PRO A CA  
3244 C C   . PRO A 412 ? 0.8012 1.4760 1.0731 0.0841  -0.0410 -0.0039 708 PRO A C   
3245 O O   . PRO A 412 ? 0.8078 1.4439 1.0710 0.0805  -0.0357 -0.0070 708 PRO A O   
3246 C CB  . PRO A 412 ? 0.8494 1.5303 1.0982 0.1807  -0.0457 -0.0127 708 PRO A CB  
3247 C CG  . PRO A 412 ? 0.8938 1.4729 1.1065 0.2162  -0.0490 -0.0186 708 PRO A CG  
3248 C CD  . PRO A 412 ? 0.8340 1.3218 1.0396 0.1827  -0.0474 -0.0197 708 PRO A CD  
3249 N N   . ASP A 413 ? 0.7481 1.5030 1.0368 0.0519  -0.0425 0.0030  709 ASP A N   
3250 C CA  . ASP A 413 ? 0.7997 1.6060 1.0940 0.0137  -0.0367 0.0074  709 ASP A CA  
3251 C C   . ASP A 413 ? 0.8514 1.7267 1.1510 0.0488  -0.0282 0.0026  709 ASP A C   
3252 O O   . ASP A 413 ? 0.8243 1.7615 1.1303 0.0942  -0.0285 -0.0010 709 ASP A O   
3253 C CB  . ASP A 413 ? 0.8900 1.7717 1.1940 -0.0328 -0.0408 0.0159  709 ASP A CB  
3254 C CG  . ASP A 413 ? 0.9829 1.7841 1.2696 -0.0783 -0.0474 0.0208  709 ASP A CG  
3255 O OD1 . ASP A 413 ? 1.0185 1.7240 1.2877 -0.0836 -0.0462 0.0190  709 ASP A OD1 
3256 O OD2 . ASP A 413 ? 0.9680 1.8030 1.2555 -0.1069 -0.0542 0.0260  709 ASP A OD2 
3257 N N   . PRO A 414 ? 0.9281 1.7930 1.2211 0.0333  -0.0208 0.0022  710 PRO A N   
3258 C CA  . PRO A 414 ? 0.9726 1.8872 1.2649 0.0731  -0.0122 -0.0040 710 PRO A CA  
3259 C C   . PRO A 414 ? 0.9854 2.0464 1.2977 0.0785  -0.0076 -0.0014 710 PRO A C   
3260 O O   . PRO A 414 ? 1.0878 2.1811 1.3889 0.1263  -0.0014 -0.0080 710 PRO A O   
3261 C CB  . PRO A 414 ? 0.9148 1.7803 1.1940 0.0450  -0.0064 -0.0035 710 PRO A CB  
3262 C CG  . PRO A 414 ? 0.9210 1.7536 1.1962 -0.0162 -0.0109 0.0057  710 PRO A CG  
3263 C CD  . PRO A 414 ? 0.9670 1.7656 1.2461 -0.0158 -0.0205 0.0069  710 PRO A CD  
3264 N N   . TRP A 415 ? 0.8539 1.9604 1.1681 0.0284  -0.0100 0.0075  711 TRP A N   
3265 C CA  . TRP A 415 ? 0.8560 2.0579 1.1610 0.0275  -0.0055 0.0100  711 TRP A CA  
3266 C C   . TRP A 415 ? 0.8382 2.0717 1.1404 0.0742  -0.0104 0.0066  711 TRP A C   
3267 O O   . TRP A 415 ? 0.8539 2.1747 1.1477 0.0785  -0.0079 0.0082  711 TRP A O   
3268 C CB  . TRP A 415 ? 0.8342 2.0675 1.1307 -0.0475 -0.0064 0.0209  711 TRP A CB  
3269 C CG  . TRP A 415 ? 0.7357 1.9202 1.0323 -0.0846 -0.0168 0.0262  711 TRP A CG  
3270 C CD1 . TRP A 415 ? 0.7688 1.9837 1.0649 -0.0853 -0.0234 0.0283  711 TRP A CD1 
3271 C CD2 . TRP A 415 ? 0.7178 1.8142 1.0100 -0.1256 -0.0221 0.0298  711 TRP A CD2 
3272 N NE1 . TRP A 415 ? 0.6926 1.8415 0.9844 -0.1241 -0.0324 0.0327  711 TRP A NE1 
3273 C CE2 . TRP A 415 ? 0.7333 1.8074 1.0208 -0.1484 -0.0320 0.0335  711 TRP A CE2 
3274 C CE3 . TRP A 415 ? 0.7679 1.8023 1.0563 -0.1437 -0.0199 0.0300  711 TRP A CE3 
3275 C CZ2 . TRP A 415 ? 0.7289 1.7172 1.0044 -0.1870 -0.0398 0.0370  711 TRP A CZ2 
3276 C CZ3 . TRP A 415 ? 0.7248 1.6527 0.9899 -0.1772 -0.0271 0.0333  711 TRP A CZ3 
3277 C CH2 . TRP A 415 ? 0.7739 1.6842 1.0344 -0.1985 -0.0369 0.0366  711 TRP A CH2 
3278 N N   . ASN A 416 ? 0.7700 1.9363 1.0752 0.1089  -0.0178 0.0023  712 ASN A N   
3279 C CA  . ASN A 416 ? 0.8739 2.0540 1.1681 0.1605  -0.0227 -0.0015 712 ASN A CA  
3280 C C   . ASN A 416 ? 0.8858 2.0310 1.1564 0.2332  -0.0200 -0.0117 712 ASN A C   
3281 O O   . ASN A 416 ? 0.8966 2.0586 1.1452 0.2824  -0.0226 -0.0154 712 ASN A O   
3282 C CB  . ASN A 416 ? 0.8751 1.9972 1.1773 0.1519  -0.0340 0.0011  712 ASN A CB  
3283 C CG  . ASN A 416 ? 0.9383 2.0778 1.2531 0.0808  -0.0380 0.0104  712 ASN A CG  
3284 O OD1 . ASN A 416 ? 1.0268 2.2383 1.3383 0.0446  -0.0339 0.0155  712 ASN A OD1 
3285 N ND2 . ASN A 416 ? 0.9233 1.9931 1.2457 0.0600  -0.0466 0.0125  712 ASN A ND2 
3286 N N   . THR A 417 ? 0.8010 1.8943 1.0689 0.2409  -0.0152 -0.0165 713 THR A N   
3287 C CA  . THR A 417 ? 0.8692 1.9039 1.1048 0.3051  -0.0135 -0.0269 713 THR A CA  
3288 C C   . THR A 417 ? 0.9362 2.0085 1.1581 0.3210  -0.0031 -0.0316 713 THR A C   
3289 O O   . THR A 417 ? 0.9625 2.0198 1.1460 0.3797  -0.0017 -0.0397 713 THR A O   
3290 C CB  . THR A 417 ? 0.9664 1.8930 1.2023 0.3060  -0.0180 -0.0304 713 THR A CB  
3291 O OG1 . THR A 417 ? 0.9367 1.8434 1.1974 0.2355  -0.0187 -0.0227 713 THR A OG1 
3292 C CG2 . THR A 417 ? 1.0955 1.9480 1.3076 0.3383  -0.0283 -0.0323 713 THR A CG2 
3293 N N   . HIS A 418 ? 0.9112 2.0276 1.1570 0.2698  0.0037  -0.0265 714 HIS A N   
3294 C CA  . HIS A 418 ? 0.9787 2.1163 1.2142 0.2784  0.0137  -0.0307 714 HIS A CA  
3295 C C   . HIS A 418 ? 1.1179 2.3382 1.3296 0.3160  0.0175  -0.0332 714 HIS A C   
3296 O O   . HIS A 418 ? 1.1676 2.4842 1.3906 0.2856  0.0188  -0.0261 714 HIS A O   
3297 C CB  . HIS A 418 ? 0.8969 2.0651 1.1588 0.2080  0.0188  -0.0222 714 HIS A CB  
3298 C CG  . HIS A 418 ? 0.8410 2.0250 1.0942 0.2101  0.0293  -0.0256 714 HIS A CG  
3299 N ND1 . HIS A 418 ? 0.8925 2.0117 1.1263 0.2555  0.0326  -0.0364 714 HIS A ND1 
3300 C CD2 . HIS A 418 ? 0.8964 2.1493 1.1528 0.1704  0.0369  -0.0196 714 HIS A CD2 
3301 C CE1 . HIS A 418 ? 0.9019 2.0538 1.1308 0.2458  0.0425  -0.0372 714 HIS A CE1 
3302 N NE2 . HIS A 418 ? 0.8521 2.0859 1.0952 0.1943  0.0452  -0.0267 714 HIS A NE2 
3303 N N   . VAL A 419 ? 1.1353 2.3159 1.3076 0.3818  0.0182  -0.0435 715 VAL A N   
3304 C CA  . VAL A 419 ? 1.1938 2.4502 1.3383 0.4213  0.0219  -0.0469 715 VAL A CA  
3305 C C   . VAL A 419 ? 1.1936 2.5222 1.3578 0.3793  0.0314  -0.0427 715 VAL A C   
3306 O O   . VAL A 419 ? 1.0773 2.3660 1.2323 0.3861  0.0376  -0.0479 715 VAL A O   
3307 C CB  . VAL A 419 ? 1.2296 2.4088 1.3173 0.4967  0.0203  -0.0589 715 VAL A CB  
3308 C CG1 . VAL A 419 ? 1.2750 2.5353 1.3336 0.5354  0.0242  -0.0621 715 VAL A CG1 
3309 C CG2 . VAL A 419 ? 1.1820 2.2931 1.2389 0.5374  0.0100  -0.0617 715 VAL A CG2 
3310 N N   . TRP A 420 ? 1.3531 2.7838 1.5398 0.3326  0.0322  -0.0332 716 TRP A N   
3311 C CA  . TRP A 420 ? 1.4611 2.9520 1.6644 0.2770  0.0397  -0.0266 716 TRP A CA  
3312 C C   . TRP A 420 ? 1.6785 3.2300 1.8576 0.3150  0.0457  -0.0319 716 TRP A C   
3313 O O   . TRP A 420 ? 1.7371 3.2712 1.8840 0.3851  0.0440  -0.0411 716 TRP A O   
3314 C CB  . TRP A 420 ? 1.3808 2.9515 1.6029 0.2142  0.0369  -0.0150 716 TRP A CB  
3315 C CG  . TRP A 420 ? 1.3008 2.8627 1.5384 0.1366  0.0405  -0.0061 716 TRP A CG  
3316 C CD1 . TRP A 420 ? 1.3164 2.8920 1.5498 0.1135  0.0485  -0.0048 716 TRP A CD1 
3317 C CD2 . TRP A 420 ? 1.2314 2.7621 1.4831 0.0720  0.0355  0.0032  716 TRP A CD2 
3318 N NE1 . TRP A 420 ? 1.2662 2.8170 1.5066 0.0385  0.0487  0.0050  716 TRP A NE1 
3319 C CE2 . TRP A 420 ? 1.2200 2.7404 1.4695 0.0124  0.0404  0.0099  716 TRP A CE2 
3320 C CE3 . TRP A 420 ? 1.2074 2.7128 1.4681 0.0596  0.0268  0.0065  716 TRP A CE3 
3321 C CZ2 . TRP A 420 ? 1.1946 2.6734 1.4440 -0.0574 0.0362  0.0197  716 TRP A CZ2 
3322 C CZ3 . TRP A 420 ? 1.2077 2.6771 1.4731 -0.0096 0.0230  0.0157  716 TRP A CZ3 
3323 C CH2 . TRP A 420 ? 1.1756 2.6284 1.4322 -0.0667 0.0273  0.0222  716 TRP A CH2 
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